data_9MFQ
# 
_entry.id   9MFQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MFQ         pdb_00009mfq 10.2210/pdb9mfq/pdb 
WWPDB D_1000284693 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-07 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MFQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              sgrigoriu@accenttx.com 
_pdbx_contact_author.name_first         Simina 
_pdbx_contact_author.name_last          Grigoriu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5525-7300 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lockbaum, G.J.'       1 0000-0003-2720-6984 
'Lee, Y.-T.'           2 0000-0002-3522-9361 
'Sickmier, E.A.'       3 0000-0002-5595-9257 
'Boriack-Sjodin, P.A.' 4 0000-0003-0179-5936 
'Grigoriu, S.'         5 0000-0002-5525-7300 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                9537 
_citation.page_last                 9554 
_citation.title                     'Discovery of ATX968: An Orally Available Allosteric Inhibitor of DHX9.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.5c00252 
_citation.pdbx_database_id_PubMed   40298172 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Daniels, M.H.'        1  ? 
primary 'Castro, J.'           2  ? 
primary 'Lee, Y.T.'            3  ? 
primary 'Gotur, D.'            4  ? 
primary 'Knockenhauer, K.E.'   5  ? 
primary 'Grigoriu, S.'         6  ? 
primary 'Lockbaum, G.J.'       7  ? 
primary 'Cheong, J.E.'         8  ? 
primary 'Lu, C.'               9  ? 
primary 'Brennan, D.'          10 ? 
primary 'Buker, S.M.'          11 ? 
primary 'Liu, J.'              12 ? 
primary 'Yao, S.'              13 ? 
primary 'Sparling, B.A.'       14 ? 
primary 'Sickmier, E.A.'       15 ? 
primary 'Ribich, S.'           16 ? 
primary 'Blakemore, S.J.'      17 ? 
primary 'Silver, S.J.'         18 ? 
primary 'Boriack-Sjodin, P.A.' 19 ? 
primary 'Duncan, K.W.'         20 ? 
primary 'Copeland, R.A.'       21 ? 
# 
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 'RNA helicase'                                                     114605.445 1   3.6.4.13 ? 'residues 151-1151' 
? 
2 non-polymer syn 'N-[3-(methanesulfonamido)phenyl]-4-phenylthiophene-2-carboxamide' 372.461    1   ?        ? ?                   
? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                                         427.201    1   ?        ? ?                   
? 
4 non-polymer syn 'MAGNESIUM ION'                                                    24.305     1   ?        ? ?                   
? 
5 non-polymer syn 'SULFATE ION'                                                      96.063     5   ?        ? ?                   
? 
6 non-polymer syn 1,2-ETHANEDIOL                                                     62.068     5   ?        ? ?                   
? 
7 water       nat water                                                              18.015     114 ?        ? ?                   
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DEAH box protein 9,Nuclear DNA helicase II' 
# 
_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       
;MSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFA
REHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGETVEPYKVNLSQDLEHQLQNVIQELNLEIVPPPEDPFLPV
VLNLGKLAHFEPSQRQNQIGVVPWSPPQSNWNPWTSSNIDEGPLAYATPEQISMDLKNELMYQLEQDHDLQAILQERELL
PVKKFESEILEAISQNSVIIIRGATGCGKTTQVPQFILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAYERGEEPGKS
CGYSVRFESVLPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPEVRIVLMSATIDT
SMFCEYFFNCPIIEVYGRTYPVQEYFLEDCIQMTHFVPPPKDKKKKEKDDDGFEDDDANCNLICGDEYGPETRMSMAQLN
EKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLEMNPHFGSHRYQILPLHSQIPREEQRKVFDPVPSGVTK
VILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFERLETH
MTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAVIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMM
IMGCIFYVGDAVCTISAATCFPEPFISEGKRLGYVHRNFAGNRFSDHVALLSVFQAWDDARMGGEEAEIRFCEHKRLNMA
TLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVN
CPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVLVDDWIRLQISHEAAACITALRAAME
ALVVEVTKQPNIISQLDPVNEHMLNMIRQISRPSAAGINLMIDYKDDDDK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFA
REHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGETVEPYKVNLSQDLEHQLQNVIQELNLEIVPPPEDPFLPV
VLNLGKLAHFEPSQRQNQIGVVPWSPPQSNWNPWTSSNIDEGPLAYATPEQISMDLKNELMYQLEQDHDLQAILQERELL
PVKKFESEILEAISQNSVIIIRGATGCGKTTQVPQFILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAYERGEEPGKS
CGYSVRFESVLPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPEVRIVLMSATIDT
SMFCEYFFNCPIIEVYGRTYPVQEYFLEDCIQMTHFVPPPKDKKKKEKDDDGFEDDDANCNLICGDEYGPETRMSMAQLN
EKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLEMNPHFGSHRYQILPLHSQIPREEQRKVFDPVPSGVTK
VILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFERLETH
MTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAVIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMM
IMGCIFYVGDAVCTISAATCFPEPFISEGKRLGYVHRNFAGNRFSDHVALLSVFQAWDDARMGGEEAEIRFCEHKRLNMA
TLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVN
CPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVLVDDWIRLQISHEAAACITALRAAME
ALVVEVTKQPNIISQLDPVNEHMLNMIRQISRPSAAGINLMIDYKDDDDK
;
_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 'N-[3-(methanesulfonamido)phenyl]-4-phenylthiophene-2-carboxamide' A1BKZ 
3 "ADENOSINE-5'-DIPHOSPHATE"                                         ADP   
4 'MAGNESIUM ION'                                                    MG    
5 'SULFATE ION'                                                      SO4   
6 1,2-ETHANEDIOL                                                     EDO   
7 water                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    ARG n 
1 4    LYS n 
1 5    GLU n 
1 6    GLU n 
1 7    GLN n 
1 8    GLU n 
1 9    VAL n 
1 10   GLN n 
1 11   ALA n 
1 12   THR n 
1 13   LEU n 
1 14   GLU n 
1 15   SER n 
1 16   GLU n 
1 17   GLU n 
1 18   VAL n 
1 19   ASP n 
1 20   LEU n 
1 21   ASN n 
1 22   ALA n 
1 23   GLY n 
1 24   LEU n 
1 25   HIS n 
1 26   GLY n 
1 27   ASN n 
1 28   TRP n 
1 29   THR n 
1 30   LEU n 
1 31   GLU n 
1 32   ASN n 
1 33   ALA n 
1 34   LYS n 
1 35   ALA n 
1 36   ARG n 
1 37   LEU n 
1 38   ASN n 
1 39   GLN n 
1 40   TYR n 
1 41   PHE n 
1 42   GLN n 
1 43   LYS n 
1 44   GLU n 
1 45   LYS n 
1 46   ILE n 
1 47   GLN n 
1 48   GLY n 
1 49   GLU n 
1 50   TYR n 
1 51   LYS n 
1 52   TYR n 
1 53   THR n 
1 54   GLN n 
1 55   VAL n 
1 56   GLY n 
1 57   PRO n 
1 58   ASP n 
1 59   HIS n 
1 60   ASN n 
1 61   ARG n 
1 62   SER n 
1 63   PHE n 
1 64   ILE n 
1 65   ALA n 
1 66   GLU n 
1 67   MET n 
1 68   THR n 
1 69   ILE n 
1 70   TYR n 
1 71   ILE n 
1 72   LYS n 
1 73   GLN n 
1 74   LEU n 
1 75   GLY n 
1 76   ARG n 
1 77   ARG n 
1 78   ILE n 
1 79   PHE n 
1 80   ALA n 
1 81   ARG n 
1 82   GLU n 
1 83   HIS n 
1 84   GLY n 
1 85   SER n 
1 86   ASN n 
1 87   LYS n 
1 88   LYS n 
1 89   LEU n 
1 90   ALA n 
1 91   ALA n 
1 92   GLN n 
1 93   SER n 
1 94   CYS n 
1 95   ALA n 
1 96   LEU n 
1 97   SER n 
1 98   LEU n 
1 99   VAL n 
1 100  ARG n 
1 101  GLN n 
1 102  LEU n 
1 103  TYR n 
1 104  HIS n 
1 105  LEU n 
1 106  GLY n 
1 107  VAL n 
1 108  ILE n 
1 109  GLU n 
1 110  ALA n 
1 111  TYR n 
1 112  SER n 
1 113  GLY n 
1 114  LEU n 
1 115  THR n 
1 116  LYS n 
1 117  LYS n 
1 118  LYS n 
1 119  GLU n 
1 120  GLY n 
1 121  GLU n 
1 122  THR n 
1 123  VAL n 
1 124  GLU n 
1 125  PRO n 
1 126  TYR n 
1 127  LYS n 
1 128  VAL n 
1 129  ASN n 
1 130  LEU n 
1 131  SER n 
1 132  GLN n 
1 133  ASP n 
1 134  LEU n 
1 135  GLU n 
1 136  HIS n 
1 137  GLN n 
1 138  LEU n 
1 139  GLN n 
1 140  ASN n 
1 141  VAL n 
1 142  ILE n 
1 143  GLN n 
1 144  GLU n 
1 145  LEU n 
1 146  ASN n 
1 147  LEU n 
1 148  GLU n 
1 149  ILE n 
1 150  VAL n 
1 151  PRO n 
1 152  PRO n 
1 153  PRO n 
1 154  GLU n 
1 155  ASP n 
1 156  PRO n 
1 157  PHE n 
1 158  LEU n 
1 159  PRO n 
1 160  VAL n 
1 161  VAL n 
1 162  LEU n 
1 163  ASN n 
1 164  LEU n 
1 165  GLY n 
1 166  LYS n 
1 167  LEU n 
1 168  ALA n 
1 169  HIS n 
1 170  PHE n 
1 171  GLU n 
1 172  PRO n 
1 173  SER n 
1 174  GLN n 
1 175  ARG n 
1 176  GLN n 
1 177  ASN n 
1 178  GLN n 
1 179  ILE n 
1 180  GLY n 
1 181  VAL n 
1 182  VAL n 
1 183  PRO n 
1 184  TRP n 
1 185  SER n 
1 186  PRO n 
1 187  PRO n 
1 188  GLN n 
1 189  SER n 
1 190  ASN n 
1 191  TRP n 
1 192  ASN n 
1 193  PRO n 
1 194  TRP n 
1 195  THR n 
1 196  SER n 
1 197  SER n 
1 198  ASN n 
1 199  ILE n 
1 200  ASP n 
1 201  GLU n 
1 202  GLY n 
1 203  PRO n 
1 204  LEU n 
1 205  ALA n 
1 206  TYR n 
1 207  ALA n 
1 208  THR n 
1 209  PRO n 
1 210  GLU n 
1 211  GLN n 
1 212  ILE n 
1 213  SER n 
1 214  MET n 
1 215  ASP n 
1 216  LEU n 
1 217  LYS n 
1 218  ASN n 
1 219  GLU n 
1 220  LEU n 
1 221  MET n 
1 222  TYR n 
1 223  GLN n 
1 224  LEU n 
1 225  GLU n 
1 226  GLN n 
1 227  ASP n 
1 228  HIS n 
1 229  ASP n 
1 230  LEU n 
1 231  GLN n 
1 232  ALA n 
1 233  ILE n 
1 234  LEU n 
1 235  GLN n 
1 236  GLU n 
1 237  ARG n 
1 238  GLU n 
1 239  LEU n 
1 240  LEU n 
1 241  PRO n 
1 242  VAL n 
1 243  LYS n 
1 244  LYS n 
1 245  PHE n 
1 246  GLU n 
1 247  SER n 
1 248  GLU n 
1 249  ILE n 
1 250  LEU n 
1 251  GLU n 
1 252  ALA n 
1 253  ILE n 
1 254  SER n 
1 255  GLN n 
1 256  ASN n 
1 257  SER n 
1 258  VAL n 
1 259  ILE n 
1 260  ILE n 
1 261  ILE n 
1 262  ARG n 
1 263  GLY n 
1 264  ALA n 
1 265  THR n 
1 266  GLY n 
1 267  CYS n 
1 268  GLY n 
1 269  LYS n 
1 270  THR n 
1 271  THR n 
1 272  GLN n 
1 273  VAL n 
1 274  PRO n 
1 275  GLN n 
1 276  PHE n 
1 277  ILE n 
1 278  LEU n 
1 279  ASP n 
1 280  ASP n 
1 281  PHE n 
1 282  ILE n 
1 283  GLN n 
1 284  ASN n 
1 285  ASP n 
1 286  ARG n 
1 287  ALA n 
1 288  ALA n 
1 289  GLU n 
1 290  CYS n 
1 291  ASN n 
1 292  ILE n 
1 293  VAL n 
1 294  VAL n 
1 295  THR n 
1 296  GLN n 
1 297  PRO n 
1 298  ARG n 
1 299  ARG n 
1 300  ILE n 
1 301  SER n 
1 302  ALA n 
1 303  VAL n 
1 304  SER n 
1 305  VAL n 
1 306  ALA n 
1 307  GLU n 
1 308  ARG n 
1 309  VAL n 
1 310  ALA n 
1 311  TYR n 
1 312  GLU n 
1 313  ARG n 
1 314  GLY n 
1 315  GLU n 
1 316  GLU n 
1 317  PRO n 
1 318  GLY n 
1 319  LYS n 
1 320  SER n 
1 321  CYS n 
1 322  GLY n 
1 323  TYR n 
1 324  SER n 
1 325  VAL n 
1 326  ARG n 
1 327  PHE n 
1 328  GLU n 
1 329  SER n 
1 330  VAL n 
1 331  LEU n 
1 332  PRO n 
1 333  ARG n 
1 334  PRO n 
1 335  HIS n 
1 336  ALA n 
1 337  SER n 
1 338  ILE n 
1 339  MET n 
1 340  PHE n 
1 341  CYS n 
1 342  THR n 
1 343  VAL n 
1 344  GLY n 
1 345  VAL n 
1 346  LEU n 
1 347  LEU n 
1 348  ARG n 
1 349  LYS n 
1 350  LEU n 
1 351  GLU n 
1 352  ALA n 
1 353  GLY n 
1 354  ILE n 
1 355  ARG n 
1 356  GLY n 
1 357  ILE n 
1 358  SER n 
1 359  HIS n 
1 360  VAL n 
1 361  ILE n 
1 362  VAL n 
1 363  ASP n 
1 364  GLU n 
1 365  ILE n 
1 366  HIS n 
1 367  GLU n 
1 368  ARG n 
1 369  ASP n 
1 370  ILE n 
1 371  ASN n 
1 372  THR n 
1 373  ASP n 
1 374  PHE n 
1 375  LEU n 
1 376  LEU n 
1 377  VAL n 
1 378  VAL n 
1 379  LEU n 
1 380  ARG n 
1 381  ASP n 
1 382  VAL n 
1 383  VAL n 
1 384  GLN n 
1 385  ALA n 
1 386  TYR n 
1 387  PRO n 
1 388  GLU n 
1 389  VAL n 
1 390  ARG n 
1 391  ILE n 
1 392  VAL n 
1 393  LEU n 
1 394  MET n 
1 395  SER n 
1 396  ALA n 
1 397  THR n 
1 398  ILE n 
1 399  ASP n 
1 400  THR n 
1 401  SER n 
1 402  MET n 
1 403  PHE n 
1 404  CYS n 
1 405  GLU n 
1 406  TYR n 
1 407  PHE n 
1 408  PHE n 
1 409  ASN n 
1 410  CYS n 
1 411  PRO n 
1 412  ILE n 
1 413  ILE n 
1 414  GLU n 
1 415  VAL n 
1 416  TYR n 
1 417  GLY n 
1 418  ARG n 
1 419  THR n 
1 420  TYR n 
1 421  PRO n 
1 422  VAL n 
1 423  GLN n 
1 424  GLU n 
1 425  TYR n 
1 426  PHE n 
1 427  LEU n 
1 428  GLU n 
1 429  ASP n 
1 430  CYS n 
1 431  ILE n 
1 432  GLN n 
1 433  MET n 
1 434  THR n 
1 435  HIS n 
1 436  PHE n 
1 437  VAL n 
1 438  PRO n 
1 439  PRO n 
1 440  PRO n 
1 441  LYS n 
1 442  ASP n 
1 443  LYS n 
1 444  LYS n 
1 445  LYS n 
1 446  LYS n 
1 447  GLU n 
1 448  LYS n 
1 449  ASP n 
1 450  ASP n 
1 451  ASP n 
1 452  GLY n 
1 453  PHE n 
1 454  GLU n 
1 455  ASP n 
1 456  ASP n 
1 457  ASP n 
1 458  ALA n 
1 459  ASN n 
1 460  CYS n 
1 461  ASN n 
1 462  LEU n 
1 463  ILE n 
1 464  CYS n 
1 465  GLY n 
1 466  ASP n 
1 467  GLU n 
1 468  TYR n 
1 469  GLY n 
1 470  PRO n 
1 471  GLU n 
1 472  THR n 
1 473  ARG n 
1 474  MET n 
1 475  SER n 
1 476  MET n 
1 477  ALA n 
1 478  GLN n 
1 479  LEU n 
1 480  ASN n 
1 481  GLU n 
1 482  LYS n 
1 483  GLU n 
1 484  THR n 
1 485  PRO n 
1 486  PHE n 
1 487  GLU n 
1 488  LEU n 
1 489  ILE n 
1 490  GLU n 
1 491  ALA n 
1 492  LEU n 
1 493  LEU n 
1 494  LYS n 
1 495  TYR n 
1 496  ILE n 
1 497  GLU n 
1 498  THR n 
1 499  LEU n 
1 500  ASN n 
1 501  VAL n 
1 502  PRO n 
1 503  GLY n 
1 504  ALA n 
1 505  VAL n 
1 506  LEU n 
1 507  VAL n 
1 508  PHE n 
1 509  LEU n 
1 510  PRO n 
1 511  GLY n 
1 512  TRP n 
1 513  ASN n 
1 514  LEU n 
1 515  ILE n 
1 516  TYR n 
1 517  THR n 
1 518  MET n 
1 519  GLN n 
1 520  LYS n 
1 521  HIS n 
1 522  LEU n 
1 523  GLU n 
1 524  MET n 
1 525  ASN n 
1 526  PRO n 
1 527  HIS n 
1 528  PHE n 
1 529  GLY n 
1 530  SER n 
1 531  HIS n 
1 532  ARG n 
1 533  TYR n 
1 534  GLN n 
1 535  ILE n 
1 536  LEU n 
1 537  PRO n 
1 538  LEU n 
1 539  HIS n 
1 540  SER n 
1 541  GLN n 
1 542  ILE n 
1 543  PRO n 
1 544  ARG n 
1 545  GLU n 
1 546  GLU n 
1 547  GLN n 
1 548  ARG n 
1 549  LYS n 
1 550  VAL n 
1 551  PHE n 
1 552  ASP n 
1 553  PRO n 
1 554  VAL n 
1 555  PRO n 
1 556  SER n 
1 557  GLY n 
1 558  VAL n 
1 559  THR n 
1 560  LYS n 
1 561  VAL n 
1 562  ILE n 
1 563  LEU n 
1 564  SER n 
1 565  THR n 
1 566  ASN n 
1 567  ILE n 
1 568  ALA n 
1 569  GLU n 
1 570  THR n 
1 571  SER n 
1 572  ILE n 
1 573  THR n 
1 574  ILE n 
1 575  ASN n 
1 576  ASP n 
1 577  VAL n 
1 578  VAL n 
1 579  TYR n 
1 580  VAL n 
1 581  ILE n 
1 582  ASP n 
1 583  SER n 
1 584  CYS n 
1 585  LYS n 
1 586  GLN n 
1 587  LYS n 
1 588  VAL n 
1 589  LYS n 
1 590  LEU n 
1 591  PHE n 
1 592  THR n 
1 593  ALA n 
1 594  HIS n 
1 595  ASN n 
1 596  ASN n 
1 597  MET n 
1 598  THR n 
1 599  ASN n 
1 600  TYR n 
1 601  ALA n 
1 602  THR n 
1 603  VAL n 
1 604  TRP n 
1 605  ALA n 
1 606  SER n 
1 607  LYS n 
1 608  THR n 
1 609  ASN n 
1 610  LEU n 
1 611  GLU n 
1 612  GLN n 
1 613  ARG n 
1 614  LYS n 
1 615  GLY n 
1 616  ARG n 
1 617  ALA n 
1 618  GLY n 
1 619  ARG n 
1 620  VAL n 
1 621  ARG n 
1 622  PRO n 
1 623  GLY n 
1 624  PHE n 
1 625  CYS n 
1 626  PHE n 
1 627  HIS n 
1 628  LEU n 
1 629  CYS n 
1 630  SER n 
1 631  ARG n 
1 632  ALA n 
1 633  ARG n 
1 634  PHE n 
1 635  GLU n 
1 636  ARG n 
1 637  LEU n 
1 638  GLU n 
1 639  THR n 
1 640  HIS n 
1 641  MET n 
1 642  THR n 
1 643  PRO n 
1 644  GLU n 
1 645  MET n 
1 646  PHE n 
1 647  ARG n 
1 648  THR n 
1 649  PRO n 
1 650  LEU n 
1 651  HIS n 
1 652  GLU n 
1 653  ILE n 
1 654  ALA n 
1 655  LEU n 
1 656  SER n 
1 657  ILE n 
1 658  LYS n 
1 659  LEU n 
1 660  LEU n 
1 661  ARG n 
1 662  LEU n 
1 663  GLY n 
1 664  GLY n 
1 665  ILE n 
1 666  GLY n 
1 667  GLN n 
1 668  PHE n 
1 669  LEU n 
1 670  ALA n 
1 671  LYS n 
1 672  ALA n 
1 673  ILE n 
1 674  GLU n 
1 675  PRO n 
1 676  PRO n 
1 677  PRO n 
1 678  LEU n 
1 679  ASP n 
1 680  ALA n 
1 681  VAL n 
1 682  ILE n 
1 683  GLU n 
1 684  ALA n 
1 685  GLU n 
1 686  HIS n 
1 687  THR n 
1 688  LEU n 
1 689  ARG n 
1 690  GLU n 
1 691  LEU n 
1 692  ASP n 
1 693  ALA n 
1 694  LEU n 
1 695  ASP n 
1 696  ALA n 
1 697  ASN n 
1 698  ASP n 
1 699  GLU n 
1 700  LEU n 
1 701  THR n 
1 702  PRO n 
1 703  LEU n 
1 704  GLY n 
1 705  ARG n 
1 706  ILE n 
1 707  LEU n 
1 708  ALA n 
1 709  LYS n 
1 710  LEU n 
1 711  PRO n 
1 712  ILE n 
1 713  GLU n 
1 714  PRO n 
1 715  ARG n 
1 716  PHE n 
1 717  GLY n 
1 718  LYS n 
1 719  MET n 
1 720  MET n 
1 721  ILE n 
1 722  MET n 
1 723  GLY n 
1 724  CYS n 
1 725  ILE n 
1 726  PHE n 
1 727  TYR n 
1 728  VAL n 
1 729  GLY n 
1 730  ASP n 
1 731  ALA n 
1 732  VAL n 
1 733  CYS n 
1 734  THR n 
1 735  ILE n 
1 736  SER n 
1 737  ALA n 
1 738  ALA n 
1 739  THR n 
1 740  CYS n 
1 741  PHE n 
1 742  PRO n 
1 743  GLU n 
1 744  PRO n 
1 745  PHE n 
1 746  ILE n 
1 747  SER n 
1 748  GLU n 
1 749  GLY n 
1 750  LYS n 
1 751  ARG n 
1 752  LEU n 
1 753  GLY n 
1 754  TYR n 
1 755  VAL n 
1 756  HIS n 
1 757  ARG n 
1 758  ASN n 
1 759  PHE n 
1 760  ALA n 
1 761  GLY n 
1 762  ASN n 
1 763  ARG n 
1 764  PHE n 
1 765  SER n 
1 766  ASP n 
1 767  HIS n 
1 768  VAL n 
1 769  ALA n 
1 770  LEU n 
1 771  LEU n 
1 772  SER n 
1 773  VAL n 
1 774  PHE n 
1 775  GLN n 
1 776  ALA n 
1 777  TRP n 
1 778  ASP n 
1 779  ASP n 
1 780  ALA n 
1 781  ARG n 
1 782  MET n 
1 783  GLY n 
1 784  GLY n 
1 785  GLU n 
1 786  GLU n 
1 787  ALA n 
1 788  GLU n 
1 789  ILE n 
1 790  ARG n 
1 791  PHE n 
1 792  CYS n 
1 793  GLU n 
1 794  HIS n 
1 795  LYS n 
1 796  ARG n 
1 797  LEU n 
1 798  ASN n 
1 799  MET n 
1 800  ALA n 
1 801  THR n 
1 802  LEU n 
1 803  ARG n 
1 804  MET n 
1 805  THR n 
1 806  TRP n 
1 807  GLU n 
1 808  ALA n 
1 809  LYS n 
1 810  VAL n 
1 811  GLN n 
1 812  LEU n 
1 813  LYS n 
1 814  GLU n 
1 815  ILE n 
1 816  LEU n 
1 817  ILE n 
1 818  ASN n 
1 819  SER n 
1 820  GLY n 
1 821  PHE n 
1 822  PRO n 
1 823  GLU n 
1 824  ASP n 
1 825  CYS n 
1 826  LEU n 
1 827  LEU n 
1 828  THR n 
1 829  GLN n 
1 830  VAL n 
1 831  PHE n 
1 832  THR n 
1 833  ASN n 
1 834  THR n 
1 835  GLY n 
1 836  PRO n 
1 837  ASP n 
1 838  ASN n 
1 839  ASN n 
1 840  LEU n 
1 841  ASP n 
1 842  VAL n 
1 843  VAL n 
1 844  ILE n 
1 845  SER n 
1 846  LEU n 
1 847  LEU n 
1 848  ALA n 
1 849  PHE n 
1 850  GLY n 
1 851  VAL n 
1 852  TYR n 
1 853  PRO n 
1 854  ASN n 
1 855  VAL n 
1 856  CYS n 
1 857  TYR n 
1 858  HIS n 
1 859  LYS n 
1 860  GLU n 
1 861  LYS n 
1 862  ARG n 
1 863  LYS n 
1 864  ILE n 
1 865  LEU n 
1 866  THR n 
1 867  THR n 
1 868  GLU n 
1 869  GLY n 
1 870  ARG n 
1 871  ASN n 
1 872  ALA n 
1 873  LEU n 
1 874  ILE n 
1 875  HIS n 
1 876  LYS n 
1 877  SER n 
1 878  SER n 
1 879  VAL n 
1 880  ASN n 
1 881  CYS n 
1 882  PRO n 
1 883  PHE n 
1 884  SER n 
1 885  SER n 
1 886  GLN n 
1 887  ASP n 
1 888  MET n 
1 889  LYS n 
1 890  TYR n 
1 891  PRO n 
1 892  SER n 
1 893  PRO n 
1 894  PHE n 
1 895  PHE n 
1 896  VAL n 
1 897  PHE n 
1 898  GLY n 
1 899  GLU n 
1 900  LYS n 
1 901  ILE n 
1 902  ARG n 
1 903  THR n 
1 904  ARG n 
1 905  ALA n 
1 906  ILE n 
1 907  SER n 
1 908  ALA n 
1 909  LYS n 
1 910  GLY n 
1 911  MET n 
1 912  THR n 
1 913  LEU n 
1 914  VAL n 
1 915  THR n 
1 916  PRO n 
1 917  LEU n 
1 918  GLN n 
1 919  LEU n 
1 920  LEU n 
1 921  LEU n 
1 922  PHE n 
1 923  ALA n 
1 924  SER n 
1 925  LYS n 
1 926  LYS n 
1 927  VAL n 
1 928  GLN n 
1 929  SER n 
1 930  ASP n 
1 931  GLY n 
1 932  GLN n 
1 933  ILE n 
1 934  VAL n 
1 935  LEU n 
1 936  VAL n 
1 937  ASP n 
1 938  ASP n 
1 939  TRP n 
1 940  ILE n 
1 941  ARG n 
1 942  LEU n 
1 943  GLN n 
1 944  ILE n 
1 945  SER n 
1 946  HIS n 
1 947  GLU n 
1 948  ALA n 
1 949  ALA n 
1 950  ALA n 
1 951  CYS n 
1 952  ILE n 
1 953  THR n 
1 954  ALA n 
1 955  LEU n 
1 956  ARG n 
1 957  ALA n 
1 958  ALA n 
1 959  MET n 
1 960  GLU n 
1 961  ALA n 
1 962  LEU n 
1 963  VAL n 
1 964  VAL n 
1 965  GLU n 
1 966  VAL n 
1 967  THR n 
1 968  LYS n 
1 969  GLN n 
1 970  PRO n 
1 971  ASN n 
1 972  ILE n 
1 973  ILE n 
1 974  SER n 
1 975  GLN n 
1 976  LEU n 
1 977  ASP n 
1 978  PRO n 
1 979  VAL n 
1 980  ASN n 
1 981  GLU n 
1 982  HIS n 
1 983  MET n 
1 984  LEU n 
1 985  ASN n 
1 986  MET n 
1 987  ILE n 
1 988  ARG n 
1 989  GLN n 
1 990  ILE n 
1 991  SER n 
1 992  ARG n 
1 993  PRO n 
1 994  SER n 
1 995  ALA n 
1 996  ALA n 
1 997  GLY n 
1 998  ILE n 
1 999  ASN n 
1 1000 LEU n 
1 1001 MET n 
1 1002 ILE n 
1 1003 ASP n 
1 1004 TYR n 
1 1005 LYS n 
1 1006 ASP n 
1 1007 ASP n 
1 1008 ASP n 
1 1009 ASP n 
1 1010 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                   1010 
_entity_src_gen.gene_src_common_name               'domestic cat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 DHX9 
_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      'Felis catus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9685 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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 
A1BKZ non-polymer         . 'N-[3-(methanesulfonamido)phenyl]-4-phenylthiophene-2-carboxamide' ?                 
'C18 H16 N2 O3 S2'  372.461 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                     'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 
GLN   'L-peptide linking' y GLUTAMINE                                                          ?                 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                    ?                 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                            ?                 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                          ?                 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                              ?                 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                         ?                 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                            ?                 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                             ?                 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                         ?                 'C5 H11 N O2 S' 
149.211 
MG    non-polymer         . 'MAGNESIUM ION'                                                    ?                 'Mg 2' 24.305  
PHE   'L-peptide linking' y PHENYLALANINE                                                      ?                 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                            ?                 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                             ?                 'C3 H7 N O3' 
105.093 
SO4   non-polymer         . 'SULFATE ION'                                                      ?                 'O4 S -2' 96.063  
THR   'L-peptide linking' y THREONINE                                                          ?                 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                         ?                 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                           ?                 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                             ?                 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    150  ?    ?   ?   A . n 
A 1 2    SER 2    151  ?    ?   ?   A . n 
A 1 3    ARG 3    152  ?    ?   ?   A . n 
A 1 4    LYS 4    153  ?    ?   ?   A . n 
A 1 5    GLU 5    154  ?    ?   ?   A . n 
A 1 6    GLU 6    155  ?    ?   ?   A . n 
A 1 7    GLN 7    156  ?    ?   ?   A . n 
A 1 8    GLU 8    157  ?    ?   ?   A . n 
A 1 9    VAL 9    158  ?    ?   ?   A . n 
A 1 10   GLN 10   159  ?    ?   ?   A . n 
A 1 11   ALA 11   160  ?    ?   ?   A . n 
A 1 12   THR 12   161  ?    ?   ?   A . n 
A 1 13   LEU 13   162  ?    ?   ?   A . n 
A 1 14   GLU 14   163  ?    ?   ?   A . n 
A 1 15   SER 15   164  ?    ?   ?   A . n 
A 1 16   GLU 16   165  ?    ?   ?   A . n 
A 1 17   GLU 17   166  ?    ?   ?   A . n 
A 1 18   VAL 18   167  ?    ?   ?   A . n 
A 1 19   ASP 19   168  ?    ?   ?   A . n 
A 1 20   LEU 20   169  ?    ?   ?   A . n 
A 1 21   ASN 21   170  ?    ?   ?   A . n 
A 1 22   ALA 22   171  ?    ?   ?   A . n 
A 1 23   GLY 23   172  ?    ?   ?   A . n 
A 1 24   LEU 24   173  ?    ?   ?   A . n 
A 1 25   HIS 25   174  ?    ?   ?   A . n 
A 1 26   GLY 26   175  ?    ?   ?   A . n 
A 1 27   ASN 27   176  ?    ?   ?   A . n 
A 1 28   TRP 28   177  ?    ?   ?   A . n 
A 1 29   THR 29   178  ?    ?   ?   A . n 
A 1 30   LEU 30   179  ?    ?   ?   A . n 
A 1 31   GLU 31   180  ?    ?   ?   A . n 
A 1 32   ASN 32   181  ?    ?   ?   A . n 
A 1 33   ALA 33   182  ?    ?   ?   A . n 
A 1 34   LYS 34   183  ?    ?   ?   A . n 
A 1 35   ALA 35   184  ?    ?   ?   A . n 
A 1 36   ARG 36   185  ?    ?   ?   A . n 
A 1 37   LEU 37   186  ?    ?   ?   A . n 
A 1 38   ASN 38   187  ?    ?   ?   A . n 
A 1 39   GLN 39   188  ?    ?   ?   A . n 
A 1 40   TYR 40   189  ?    ?   ?   A . n 
A 1 41   PHE 41   190  ?    ?   ?   A . n 
A 1 42   GLN 42   191  ?    ?   ?   A . n 
A 1 43   LYS 43   192  ?    ?   ?   A . n 
A 1 44   GLU 44   193  ?    ?   ?   A . n 
A 1 45   LYS 45   194  ?    ?   ?   A . n 
A 1 46   ILE 46   195  ?    ?   ?   A . n 
A 1 47   GLN 47   196  ?    ?   ?   A . n 
A 1 48   GLY 48   197  ?    ?   ?   A . n 
A 1 49   GLU 49   198  ?    ?   ?   A . n 
A 1 50   TYR 50   199  ?    ?   ?   A . n 
A 1 51   LYS 51   200  ?    ?   ?   A . n 
A 1 52   TYR 52   201  ?    ?   ?   A . n 
A 1 53   THR 53   202  ?    ?   ?   A . n 
A 1 54   GLN 54   203  ?    ?   ?   A . n 
A 1 55   VAL 55   204  ?    ?   ?   A . n 
A 1 56   GLY 56   205  ?    ?   ?   A . n 
A 1 57   PRO 57   206  ?    ?   ?   A . n 
A 1 58   ASP 58   207  ?    ?   ?   A . n 
A 1 59   HIS 59   208  ?    ?   ?   A . n 
A 1 60   ASN 60   209  ?    ?   ?   A . n 
A 1 61   ARG 61   210  ?    ?   ?   A . n 
A 1 62   SER 62   211  ?    ?   ?   A . n 
A 1 63   PHE 63   212  ?    ?   ?   A . n 
A 1 64   ILE 64   213  ?    ?   ?   A . n 
A 1 65   ALA 65   214  ?    ?   ?   A . n 
A 1 66   GLU 66   215  ?    ?   ?   A . n 
A 1 67   MET 67   216  ?    ?   ?   A . n 
A 1 68   THR 68   217  ?    ?   ?   A . n 
A 1 69   ILE 69   218  ?    ?   ?   A . n 
A 1 70   TYR 70   219  ?    ?   ?   A . n 
A 1 71   ILE 71   220  ?    ?   ?   A . n 
A 1 72   LYS 72   221  ?    ?   ?   A . n 
A 1 73   GLN 73   222  ?    ?   ?   A . n 
A 1 74   LEU 74   223  ?    ?   ?   A . n 
A 1 75   GLY 75   224  ?    ?   ?   A . n 
A 1 76   ARG 76   225  ?    ?   ?   A . n 
A 1 77   ARG 77   226  ?    ?   ?   A . n 
A 1 78   ILE 78   227  ?    ?   ?   A . n 
A 1 79   PHE 79   228  ?    ?   ?   A . n 
A 1 80   ALA 80   229  ?    ?   ?   A . n 
A 1 81   ARG 81   230  ?    ?   ?   A . n 
A 1 82   GLU 82   231  ?    ?   ?   A . n 
A 1 83   HIS 83   232  ?    ?   ?   A . n 
A 1 84   GLY 84   233  ?    ?   ?   A . n 
A 1 85   SER 85   234  ?    ?   ?   A . n 
A 1 86   ASN 86   235  ?    ?   ?   A . n 
A 1 87   LYS 87   236  ?    ?   ?   A . n 
A 1 88   LYS 88   237  ?    ?   ?   A . n 
A 1 89   LEU 89   238  ?    ?   ?   A . n 
A 1 90   ALA 90   239  ?    ?   ?   A . n 
A 1 91   ALA 91   240  ?    ?   ?   A . n 
A 1 92   GLN 92   241  ?    ?   ?   A . n 
A 1 93   SER 93   242  ?    ?   ?   A . n 
A 1 94   CYS 94   243  ?    ?   ?   A . n 
A 1 95   ALA 95   244  ?    ?   ?   A . n 
A 1 96   LEU 96   245  ?    ?   ?   A . n 
A 1 97   SER 97   246  ?    ?   ?   A . n 
A 1 98   LEU 98   247  ?    ?   ?   A . n 
A 1 99   VAL 99   248  ?    ?   ?   A . n 
A 1 100  ARG 100  249  ?    ?   ?   A . n 
A 1 101  GLN 101  250  ?    ?   ?   A . n 
A 1 102  LEU 102  251  ?    ?   ?   A . n 
A 1 103  TYR 103  252  ?    ?   ?   A . n 
A 1 104  HIS 104  253  ?    ?   ?   A . n 
A 1 105  LEU 105  254  ?    ?   ?   A . n 
A 1 106  GLY 106  255  ?    ?   ?   A . n 
A 1 107  VAL 107  256  ?    ?   ?   A . n 
A 1 108  ILE 108  257  ?    ?   ?   A . n 
A 1 109  GLU 109  258  ?    ?   ?   A . n 
A 1 110  ALA 110  259  ?    ?   ?   A . n 
A 1 111  TYR 111  260  ?    ?   ?   A . n 
A 1 112  SER 112  261  ?    ?   ?   A . n 
A 1 113  GLY 113  262  ?    ?   ?   A . n 
A 1 114  LEU 114  263  ?    ?   ?   A . n 
A 1 115  THR 115  264  ?    ?   ?   A . n 
A 1 116  LYS 116  265  ?    ?   ?   A . n 
A 1 117  LYS 117  266  ?    ?   ?   A . n 
A 1 118  LYS 118  267  ?    ?   ?   A . n 
A 1 119  GLU 119  268  ?    ?   ?   A . n 
A 1 120  GLY 120  269  ?    ?   ?   A . n 
A 1 121  GLU 121  270  ?    ?   ?   A . n 
A 1 122  THR 122  271  271  THR THR A . n 
A 1 123  VAL 123  272  272  VAL VAL A . n 
A 1 124  GLU 124  273  273  GLU GLU A . n 
A 1 125  PRO 125  274  274  PRO PRO A . n 
A 1 126  TYR 126  275  275  TYR TYR A . n 
A 1 127  LYS 127  276  276  LYS LYS A . n 
A 1 128  VAL 128  277  277  VAL VAL A . n 
A 1 129  ASN 129  278  278  ASN ASN A . n 
A 1 130  LEU 130  279  279  LEU LEU A . n 
A 1 131  SER 131  280  280  SER SER A . n 
A 1 132  GLN 132  281  281  GLN GLN A . n 
A 1 133  ASP 133  282  282  ASP ASP A . n 
A 1 134  LEU 134  283  283  LEU LEU A . n 
A 1 135  GLU 135  284  284  GLU GLU A . n 
A 1 136  HIS 136  285  285  HIS HIS A . n 
A 1 137  GLN 137  286  286  GLN GLN A . n 
A 1 138  LEU 138  287  287  LEU LEU A . n 
A 1 139  GLN 139  288  288  GLN GLN A . n 
A 1 140  ASN 140  289  289  ASN ASN A . n 
A 1 141  VAL 141  290  290  VAL VAL A . n 
A 1 142  ILE 142  291  291  ILE ILE A . n 
A 1 143  GLN 143  292  292  GLN GLN A . n 
A 1 144  GLU 144  293  293  GLU GLU A . n 
A 1 145  LEU 145  294  294  LEU LEU A . n 
A 1 146  ASN 146  295  295  ASN ASN A . n 
A 1 147  LEU 147  296  296  LEU LEU A . n 
A 1 148  GLU 148  297  297  GLU GLU A . n 
A 1 149  ILE 149  298  298  ILE ILE A . n 
A 1 150  VAL 150  299  299  VAL VAL A . n 
A 1 151  PRO 151  300  300  PRO PRO A . n 
A 1 152  PRO 152  301  301  PRO PRO A . n 
A 1 153  PRO 153  302  302  PRO PRO A . n 
A 1 154  GLU 154  303  303  GLU GLU A . n 
A 1 155  ASP 155  304  304  ASP ASP A . n 
A 1 156  PRO 156  305  305  PRO PRO A . n 
A 1 157  PHE 157  306  306  PHE PHE A . n 
A 1 158  LEU 158  307  307  LEU LEU A . n 
A 1 159  PRO 159  308  308  PRO PRO A . n 
A 1 160  VAL 160  309  309  VAL VAL A . n 
A 1 161  VAL 161  310  310  VAL VAL A . n 
A 1 162  LEU 162  311  311  LEU LEU A . n 
A 1 163  ASN 163  312  312  ASN ASN A . n 
A 1 164  LEU 164  313  313  LEU LEU A . n 
A 1 165  GLY 165  314  314  GLY GLY A . n 
A 1 166  LYS 166  315  315  LYS LYS A . n 
A 1 167  LEU 167  316  ?    ?   ?   A . n 
A 1 168  ALA 168  317  ?    ?   ?   A . n 
A 1 169  HIS 169  318  ?    ?   ?   A . n 
A 1 170  PHE 170  319  ?    ?   ?   A . n 
A 1 171  GLU 171  320  ?    ?   ?   A . n 
A 1 172  PRO 172  321  321  PRO PRO A . n 
A 1 173  SER 173  322  322  SER SER A . n 
A 1 174  GLN 174  323  323  GLN GLN A . n 
A 1 175  ARG 175  324  324  ARG ARG A . n 
A 1 176  GLN 176  325  325  GLN GLN A . n 
A 1 177  ASN 177  326  ?    ?   ?   A . n 
A 1 178  GLN 178  327  ?    ?   ?   A . n 
A 1 179  ILE 179  328  328  ILE ILE A . n 
A 1 180  GLY 180  329  329  GLY GLY A . n 
A 1 181  VAL 181  330  330  VAL VAL A . n 
A 1 182  VAL 182  331  331  VAL VAL A . n 
A 1 183  PRO 183  332  332  PRO PRO A . n 
A 1 184  TRP 184  333  333  TRP TRP A . n 
A 1 185  SER 185  334  334  SER SER A . n 
A 1 186  PRO 186  335  335  PRO PRO A . n 
A 1 187  PRO 187  336  336  PRO PRO A . n 
A 1 188  GLN 188  337  337  GLN GLN A . n 
A 1 189  SER 189  338  338  SER SER A . n 
A 1 190  ASN 190  339  339  ASN ASN A . n 
A 1 191  TRP 191  340  340  TRP TRP A . n 
A 1 192  ASN 192  341  341  ASN ASN A . n 
A 1 193  PRO 193  342  342  PRO PRO A . n 
A 1 194  TRP 194  343  343  TRP TRP A . n 
A 1 195  THR 195  344  344  THR THR A . n 
A 1 196  SER 196  345  345  SER SER A . n 
A 1 197  SER 197  346  346  SER SER A . n 
A 1 198  ASN 198  347  347  ASN ASN A . n 
A 1 199  ILE 199  348  348  ILE ILE A . n 
A 1 200  ASP 200  349  349  ASP ASP A . n 
A 1 201  GLU 201  350  350  GLU GLU A . n 
A 1 202  GLY 202  351  351  GLY GLY A . n 
A 1 203  PRO 203  352  352  PRO PRO A . n 
A 1 204  LEU 204  353  353  LEU LEU A . n 
A 1 205  ALA 205  354  354  ALA ALA A . n 
A 1 206  TYR 206  355  355  TYR TYR A . n 
A 1 207  ALA 207  356  356  ALA ALA A . n 
A 1 208  THR 208  357  357  THR THR A . n 
A 1 209  PRO 209  358  358  PRO PRO A . n 
A 1 210  GLU 210  359  359  GLU GLU A . n 
A 1 211  GLN 211  360  360  GLN GLN A . n 
A 1 212  ILE 212  361  361  ILE ILE A . n 
A 1 213  SER 213  362  362  SER SER A . n 
A 1 214  MET 214  363  363  MET MET A . n 
A 1 215  ASP 215  364  364  ASP ASP A . n 
A 1 216  LEU 216  365  365  LEU LEU A . n 
A 1 217  LYS 217  366  366  LYS LYS A . n 
A 1 218  ASN 218  367  367  ASN ASN A . n 
A 1 219  GLU 219  368  368  GLU GLU A . n 
A 1 220  LEU 220  369  369  LEU LEU A . n 
A 1 221  MET 221  370  370  MET MET A . n 
A 1 222  TYR 222  371  371  TYR TYR A . n 
A 1 223  GLN 223  372  372  GLN GLN A . n 
A 1 224  LEU 224  373  373  LEU LEU A . n 
A 1 225  GLU 225  374  374  GLU GLU A . n 
A 1 226  GLN 226  375  375  GLN GLN A . n 
A 1 227  ASP 227  376  376  ASP ASP A . n 
A 1 228  HIS 228  377  377  HIS HIS A . n 
A 1 229  ASP 229  378  378  ASP ASP A . n 
A 1 230  LEU 230  379  379  LEU LEU A . n 
A 1 231  GLN 231  380  380  GLN GLN A . n 
A 1 232  ALA 232  381  381  ALA ALA A . n 
A 1 233  ILE 233  382  382  ILE ILE A . n 
A 1 234  LEU 234  383  383  LEU LEU A . n 
A 1 235  GLN 235  384  384  GLN GLN A . n 
A 1 236  GLU 236  385  385  GLU GLU A . n 
A 1 237  ARG 237  386  386  ARG ARG A . n 
A 1 238  GLU 238  387  387  GLU GLU A . n 
A 1 239  LEU 239  388  388  LEU LEU A . n 
A 1 240  LEU 240  389  389  LEU LEU A . n 
A 1 241  PRO 241  390  390  PRO PRO A . n 
A 1 242  VAL 242  391  391  VAL VAL A . n 
A 1 243  LYS 243  392  392  LYS LYS A . n 
A 1 244  LYS 244  393  393  LYS LYS A . n 
A 1 245  PHE 245  394  394  PHE PHE A . n 
A 1 246  GLU 246  395  395  GLU GLU A . n 
A 1 247  SER 247  396  396  SER SER A . n 
A 1 248  GLU 248  397  397  GLU GLU A . n 
A 1 249  ILE 249  398  398  ILE ILE A . n 
A 1 250  LEU 250  399  399  LEU LEU A . n 
A 1 251  GLU 251  400  400  GLU GLU A . n 
A 1 252  ALA 252  401  401  ALA ALA A . n 
A 1 253  ILE 253  402  402  ILE ILE A . n 
A 1 254  SER 254  403  403  SER SER A . n 
A 1 255  GLN 255  404  404  GLN GLN A . n 
A 1 256  ASN 256  405  405  ASN ASN A . n 
A 1 257  SER 257  406  406  SER SER A . n 
A 1 258  VAL 258  407  407  VAL VAL A . n 
A 1 259  ILE 259  408  408  ILE ILE A . n 
A 1 260  ILE 260  409  409  ILE ILE A . n 
A 1 261  ILE 261  410  410  ILE ILE A . n 
A 1 262  ARG 262  411  411  ARG ARG A . n 
A 1 263  GLY 263  412  412  GLY GLY A . n 
A 1 264  ALA 264  413  413  ALA ALA A . n 
A 1 265  THR 265  414  414  THR THR A . n 
A 1 266  GLY 266  415  415  GLY GLY A . n 
A 1 267  CYS 267  416  416  CYS CYS A . n 
A 1 268  GLY 268  417  417  GLY GLY A . n 
A 1 269  LYS 269  418  418  LYS LYS A . n 
A 1 270  THR 270  419  419  THR THR A . n 
A 1 271  THR 271  420  420  THR THR A . n 
A 1 272  GLN 272  421  421  GLN GLN A . n 
A 1 273  VAL 273  422  422  VAL VAL A . n 
A 1 274  PRO 274  423  423  PRO PRO A . n 
A 1 275  GLN 275  424  424  GLN GLN A . n 
A 1 276  PHE 276  425  425  PHE PHE A . n 
A 1 277  ILE 277  426  426  ILE ILE A . n 
A 1 278  LEU 278  427  427  LEU LEU A . n 
A 1 279  ASP 279  428  428  ASP ASP A . n 
A 1 280  ASP 280  429  429  ASP ASP A . n 
A 1 281  PHE 281  430  430  PHE PHE A . n 
A 1 282  ILE 282  431  431  ILE ILE A . n 
A 1 283  GLN 283  432  432  GLN GLN A . n 
A 1 284  ASN 284  433  433  ASN ASN A . n 
A 1 285  ASP 285  434  434  ASP ASP A . n 
A 1 286  ARG 286  435  435  ARG ARG A . n 
A 1 287  ALA 287  436  436  ALA ALA A . n 
A 1 288  ALA 288  437  437  ALA ALA A . n 
A 1 289  GLU 289  438  438  GLU GLU A . n 
A 1 290  CYS 290  439  439  CYS CYS A . n 
A 1 291  ASN 291  440  440  ASN ASN A . n 
A 1 292  ILE 292  441  441  ILE ILE A . n 
A 1 293  VAL 293  442  442  VAL VAL A . n 
A 1 294  VAL 294  443  443  VAL VAL A . n 
A 1 295  THR 295  444  444  THR THR A . n 
A 1 296  GLN 296  445  445  GLN GLN A . n 
A 1 297  PRO 297  446  446  PRO PRO A . n 
A 1 298  ARG 298  447  447  ARG ARG A . n 
A 1 299  ARG 299  448  448  ARG ARG A . n 
A 1 300  ILE 300  449  449  ILE ILE A . n 
A 1 301  SER 301  450  450  SER SER A . n 
A 1 302  ALA 302  451  451  ALA ALA A . n 
A 1 303  VAL 303  452  452  VAL VAL A . n 
A 1 304  SER 304  453  453  SER SER A . n 
A 1 305  VAL 305  454  454  VAL VAL A . n 
A 1 306  ALA 306  455  455  ALA ALA A . n 
A 1 307  GLU 307  456  456  GLU GLU A . n 
A 1 308  ARG 308  457  457  ARG ARG A . n 
A 1 309  VAL 309  458  458  VAL VAL A . n 
A 1 310  ALA 310  459  459  ALA ALA A . n 
A 1 311  TYR 311  460  460  TYR TYR A . n 
A 1 312  GLU 312  461  461  GLU GLU A . n 
A 1 313  ARG 313  462  462  ARG ARG A . n 
A 1 314  GLY 314  463  463  GLY GLY A . n 
A 1 315  GLU 315  464  464  GLU GLU A . n 
A 1 316  GLU 316  465  465  GLU GLU A . n 
A 1 317  PRO 317  466  466  PRO PRO A . n 
A 1 318  GLY 318  467  467  GLY GLY A . n 
A 1 319  LYS 319  468  468  LYS LYS A . n 
A 1 320  SER 320  469  469  SER SER A . n 
A 1 321  CYS 321  470  470  CYS CYS A . n 
A 1 322  GLY 322  471  471  GLY GLY A . n 
A 1 323  TYR 323  472  472  TYR TYR A . n 
A 1 324  SER 324  473  473  SER SER A . n 
A 1 325  VAL 325  474  474  VAL VAL A . n 
A 1 326  ARG 326  475  475  ARG ARG A . n 
A 1 327  PHE 327  476  476  PHE PHE A . n 
A 1 328  GLU 328  477  477  GLU GLU A . n 
A 1 329  SER 329  478  478  SER SER A . n 
A 1 330  VAL 330  479  479  VAL VAL A . n 
A 1 331  LEU 331  480  480  LEU LEU A . n 
A 1 332  PRO 332  481  481  PRO PRO A . n 
A 1 333  ARG 333  482  482  ARG ARG A . n 
A 1 334  PRO 334  483  483  PRO PRO A . n 
A 1 335  HIS 335  484  484  HIS HIS A . n 
A 1 336  ALA 336  485  485  ALA ALA A . n 
A 1 337  SER 337  486  486  SER SER A . n 
A 1 338  ILE 338  487  487  ILE ILE A . n 
A 1 339  MET 339  488  488  MET MET A . n 
A 1 340  PHE 340  489  489  PHE PHE A . n 
A 1 341  CYS 341  490  490  CYS CYS A . n 
A 1 342  THR 342  491  491  THR THR A . n 
A 1 343  VAL 343  492  492  VAL VAL A . n 
A 1 344  GLY 344  493  493  GLY GLY A . n 
A 1 345  VAL 345  494  494  VAL VAL A . n 
A 1 346  LEU 346  495  495  LEU LEU A . n 
A 1 347  LEU 347  496  496  LEU LEU A . n 
A 1 348  ARG 348  497  497  ARG ARG A . n 
A 1 349  LYS 349  498  498  LYS LYS A . n 
A 1 350  LEU 350  499  499  LEU LEU A . n 
A 1 351  GLU 351  500  500  GLU GLU A . n 
A 1 352  ALA 352  501  501  ALA ALA A . n 
A 1 353  GLY 353  502  502  GLY GLY A . n 
A 1 354  ILE 354  503  503  ILE ILE A . n 
A 1 355  ARG 355  504  504  ARG ARG A . n 
A 1 356  GLY 356  505  505  GLY GLY A . n 
A 1 357  ILE 357  506  506  ILE ILE A . n 
A 1 358  SER 358  507  507  SER SER A . n 
A 1 359  HIS 359  508  508  HIS HIS A . n 
A 1 360  VAL 360  509  509  VAL VAL A . n 
A 1 361  ILE 361  510  510  ILE ILE A . n 
A 1 362  VAL 362  511  511  VAL VAL A . n 
A 1 363  ASP 363  512  512  ASP ASP A . n 
A 1 364  GLU 364  513  513  GLU GLU A . n 
A 1 365  ILE 365  514  514  ILE ILE A . n 
A 1 366  HIS 366  515  515  HIS HIS A . n 
A 1 367  GLU 367  516  516  GLU GLU A . n 
A 1 368  ARG 368  517  517  ARG ARG A . n 
A 1 369  ASP 369  518  518  ASP ASP A . n 
A 1 370  ILE 370  519  519  ILE ILE A . n 
A 1 371  ASN 371  520  520  ASN ASN A . n 
A 1 372  THR 372  521  521  THR THR A . n 
A 1 373  ASP 373  522  522  ASP ASP A . n 
A 1 374  PHE 374  523  523  PHE PHE A . n 
A 1 375  LEU 375  524  524  LEU LEU A . n 
A 1 376  LEU 376  525  525  LEU LEU A . n 
A 1 377  VAL 377  526  526  VAL VAL A . n 
A 1 378  VAL 378  527  527  VAL VAL A . n 
A 1 379  LEU 379  528  528  LEU LEU A . n 
A 1 380  ARG 380  529  529  ARG ARG A . n 
A 1 381  ASP 381  530  530  ASP ASP A . n 
A 1 382  VAL 382  531  531  VAL VAL A . n 
A 1 383  VAL 383  532  532  VAL VAL A . n 
A 1 384  GLN 384  533  533  GLN GLN A . n 
A 1 385  ALA 385  534  534  ALA ALA A . n 
A 1 386  TYR 386  535  535  TYR TYR A . n 
A 1 387  PRO 387  536  536  PRO PRO A . n 
A 1 388  GLU 388  537  537  GLU GLU A . n 
A 1 389  VAL 389  538  538  VAL VAL A . n 
A 1 390  ARG 390  539  539  ARG ARG A . n 
A 1 391  ILE 391  540  540  ILE ILE A . n 
A 1 392  VAL 392  541  541  VAL VAL A . n 
A 1 393  LEU 393  542  542  LEU LEU A . n 
A 1 394  MET 394  543  543  MET MET A . n 
A 1 395  SER 395  544  544  SER SER A . n 
A 1 396  ALA 396  545  545  ALA ALA A . n 
A 1 397  THR 397  546  546  THR THR A . n 
A 1 398  ILE 398  547  547  ILE ILE A . n 
A 1 399  ASP 399  548  548  ASP ASP A . n 
A 1 400  THR 400  549  549  THR THR A . n 
A 1 401  SER 401  550  550  SER SER A . n 
A 1 402  MET 402  551  551  MET MET A . n 
A 1 403  PHE 403  552  552  PHE PHE A . n 
A 1 404  CYS 404  553  553  CYS CYS A . n 
A 1 405  GLU 405  554  554  GLU GLU A . n 
A 1 406  TYR 406  555  555  TYR TYR A . n 
A 1 407  PHE 407  556  556  PHE PHE A . n 
A 1 408  PHE 408  557  557  PHE PHE A . n 
A 1 409  ASN 409  558  558  ASN ASN A . n 
A 1 410  CYS 410  559  559  CYS CYS A . n 
A 1 411  PRO 411  560  560  PRO PRO A . n 
A 1 412  ILE 412  561  561  ILE ILE A . n 
A 1 413  ILE 413  562  562  ILE ILE A . n 
A 1 414  GLU 414  563  563  GLU GLU A . n 
A 1 415  VAL 415  564  564  VAL VAL A . n 
A 1 416  TYR 416  565  565  TYR TYR A . n 
A 1 417  GLY 417  566  566  GLY GLY A . n 
A 1 418  ARG 418  567  567  ARG ARG A . n 
A 1 419  THR 419  568  568  THR THR A . n 
A 1 420  TYR 420  569  569  TYR TYR A . n 
A 1 421  PRO 421  570  570  PRO PRO A . n 
A 1 422  VAL 422  571  571  VAL VAL A . n 
A 1 423  GLN 423  572  572  GLN GLN A . n 
A 1 424  GLU 424  573  573  GLU GLU A . n 
A 1 425  TYR 425  574  574  TYR TYR A . n 
A 1 426  PHE 426  575  575  PHE PHE A . n 
A 1 427  LEU 427  576  576  LEU LEU A . n 
A 1 428  GLU 428  577  577  GLU GLU A . n 
A 1 429  ASP 429  578  578  ASP ASP A . n 
A 1 430  CYS 430  579  579  CYS CYS A . n 
A 1 431  ILE 431  580  580  ILE ILE A . n 
A 1 432  GLN 432  581  581  GLN GLN A . n 
A 1 433  MET 433  582  582  MET MET A . n 
A 1 434  THR 434  583  583  THR THR A . n 
A 1 435  HIS 435  584  584  HIS HIS A . n 
A 1 436  PHE 436  585  585  PHE PHE A . n 
A 1 437  VAL 437  586  586  VAL VAL A . n 
A 1 438  PRO 438  587  587  PRO PRO A . n 
A 1 439  PRO 439  588  588  PRO PRO A . n 
A 1 440  PRO 440  589  589  PRO PRO A . n 
A 1 441  LYS 441  590  ?    ?   ?   A . n 
A 1 442  ASP 442  591  ?    ?   ?   A . n 
A 1 443  LYS 443  592  ?    ?   ?   A . n 
A 1 444  LYS 444  593  ?    ?   ?   A . n 
A 1 445  LYS 445  594  ?    ?   ?   A . n 
A 1 446  LYS 446  595  ?    ?   ?   A . n 
A 1 447  GLU 447  596  ?    ?   ?   A . n 
A 1 448  LYS 448  597  ?    ?   ?   A . n 
A 1 449  ASP 449  598  ?    ?   ?   A . n 
A 1 450  ASP 450  599  ?    ?   ?   A . n 
A 1 451  ASP 451  600  ?    ?   ?   A . n 
A 1 452  GLY 452  601  ?    ?   ?   A . n 
A 1 453  PHE 453  602  ?    ?   ?   A . n 
A 1 454  GLU 454  603  ?    ?   ?   A . n 
A 1 455  ASP 455  604  ?    ?   ?   A . n 
A 1 456  ASP 456  605  ?    ?   ?   A . n 
A 1 457  ASP 457  606  ?    ?   ?   A . n 
A 1 458  ALA 458  607  607  ALA ALA A . n 
A 1 459  ASN 459  608  608  ASN ASN A . n 
A 1 460  CYS 460  609  609  CYS CYS A . n 
A 1 461  ASN 461  610  610  ASN ASN A . n 
A 1 462  LEU 462  611  611  LEU LEU A . n 
A 1 463  ILE 463  612  612  ILE ILE A . n 
A 1 464  CYS 464  613  613  CYS CYS A . n 
A 1 465  GLY 465  614  614  GLY GLY A . n 
A 1 466  ASP 466  615  615  ASP ASP A . n 
A 1 467  GLU 467  616  616  GLU GLU A . n 
A 1 468  TYR 468  617  617  TYR TYR A . n 
A 1 469  GLY 469  618  618  GLY GLY A . n 
A 1 470  PRO 470  619  619  PRO PRO A . n 
A 1 471  GLU 471  620  620  GLU GLU A . n 
A 1 472  THR 472  621  621  THR THR A . n 
A 1 473  ARG 473  622  622  ARG ARG A . n 
A 1 474  MET 474  623  623  MET MET A . n 
A 1 475  SER 475  624  624  SER SER A . n 
A 1 476  MET 476  625  625  MET MET A . n 
A 1 477  ALA 477  626  626  ALA ALA A . n 
A 1 478  GLN 478  627  627  GLN GLN A . n 
A 1 479  LEU 479  628  628  LEU LEU A . n 
A 1 480  ASN 480  629  629  ASN ASN A . n 
A 1 481  GLU 481  630  630  GLU GLU A . n 
A 1 482  LYS 482  631  631  LYS LYS A . n 
A 1 483  GLU 483  632  632  GLU GLU A . n 
A 1 484  THR 484  633  633  THR THR A . n 
A 1 485  PRO 485  634  634  PRO PRO A . n 
A 1 486  PHE 486  635  635  PHE PHE A . n 
A 1 487  GLU 487  636  636  GLU GLU A . n 
A 1 488  LEU 488  637  637  LEU LEU A . n 
A 1 489  ILE 489  638  638  ILE ILE A . n 
A 1 490  GLU 490  639  639  GLU GLU A . n 
A 1 491  ALA 491  640  640  ALA ALA A . n 
A 1 492  LEU 492  641  641  LEU LEU A . n 
A 1 493  LEU 493  642  642  LEU LEU A . n 
A 1 494  LYS 494  643  643  LYS LYS A . n 
A 1 495  TYR 495  644  644  TYR TYR A . n 
A 1 496  ILE 496  645  645  ILE ILE A . n 
A 1 497  GLU 497  646  646  GLU GLU A . n 
A 1 498  THR 498  647  647  THR THR A . n 
A 1 499  LEU 499  648  648  LEU LEU A . n 
A 1 500  ASN 500  649  649  ASN ASN A . n 
A 1 501  VAL 501  650  650  VAL VAL A . n 
A 1 502  PRO 502  651  651  PRO PRO A . n 
A 1 503  GLY 503  652  652  GLY GLY A . n 
A 1 504  ALA 504  653  653  ALA ALA A . n 
A 1 505  VAL 505  654  654  VAL VAL A . n 
A 1 506  LEU 506  655  655  LEU LEU A . n 
A 1 507  VAL 507  656  656  VAL VAL A . n 
A 1 508  PHE 508  657  657  PHE PHE A . n 
A 1 509  LEU 509  658  658  LEU LEU A . n 
A 1 510  PRO 510  659  659  PRO PRO A . n 
A 1 511  GLY 511  660  660  GLY GLY A . n 
A 1 512  TRP 512  661  661  TRP TRP A . n 
A 1 513  ASN 513  662  662  ASN ASN A . n 
A 1 514  LEU 514  663  663  LEU LEU A . n 
A 1 515  ILE 515  664  664  ILE ILE A . n 
A 1 516  TYR 516  665  665  TYR TYR A . n 
A 1 517  THR 517  666  666  THR THR A . n 
A 1 518  MET 518  667  667  MET MET A . n 
A 1 519  GLN 519  668  668  GLN GLN A . n 
A 1 520  LYS 520  669  669  LYS LYS A . n 
A 1 521  HIS 521  670  670  HIS HIS A . n 
A 1 522  LEU 522  671  671  LEU LEU A . n 
A 1 523  GLU 523  672  672  GLU GLU A . n 
A 1 524  MET 524  673  673  MET MET A . n 
A 1 525  ASN 525  674  674  ASN ASN A . n 
A 1 526  PRO 526  675  675  PRO PRO A . n 
A 1 527  HIS 527  676  676  HIS HIS A . n 
A 1 528  PHE 528  677  677  PHE PHE A . n 
A 1 529  GLY 529  678  678  GLY GLY A . n 
A 1 530  SER 530  679  679  SER SER A . n 
A 1 531  HIS 531  680  680  HIS HIS A . n 
A 1 532  ARG 532  681  681  ARG ARG A . n 
A 1 533  TYR 533  682  682  TYR TYR A . n 
A 1 534  GLN 534  683  683  GLN GLN A . n 
A 1 535  ILE 535  684  684  ILE ILE A . n 
A 1 536  LEU 536  685  685  LEU LEU A . n 
A 1 537  PRO 537  686  686  PRO PRO A . n 
A 1 538  LEU 538  687  687  LEU LEU A . n 
A 1 539  HIS 539  688  688  HIS HIS A . n 
A 1 540  SER 540  689  689  SER SER A . n 
A 1 541  GLN 541  690  690  GLN GLN A . n 
A 1 542  ILE 542  691  691  ILE ILE A . n 
A 1 543  PRO 543  692  692  PRO PRO A . n 
A 1 544  ARG 544  693  693  ARG ARG A . n 
A 1 545  GLU 545  694  694  GLU GLU A . n 
A 1 546  GLU 546  695  695  GLU GLU A . n 
A 1 547  GLN 547  696  696  GLN GLN A . n 
A 1 548  ARG 548  697  697  ARG ARG A . n 
A 1 549  LYS 549  698  698  LYS LYS A . n 
A 1 550  VAL 550  699  699  VAL VAL A . n 
A 1 551  PHE 551  700  700  PHE PHE A . n 
A 1 552  ASP 552  701  701  ASP ASP A . n 
A 1 553  PRO 553  702  702  PRO PRO A . n 
A 1 554  VAL 554  703  703  VAL VAL A . n 
A 1 555  PRO 555  704  704  PRO PRO A . n 
A 1 556  SER 556  705  705  SER SER A . n 
A 1 557  GLY 557  706  706  GLY GLY A . n 
A 1 558  VAL 558  707  707  VAL VAL A . n 
A 1 559  THR 559  708  708  THR THR A . n 
A 1 560  LYS 560  709  709  LYS LYS A . n 
A 1 561  VAL 561  710  710  VAL VAL A . n 
A 1 562  ILE 562  711  711  ILE ILE A . n 
A 1 563  LEU 563  712  712  LEU LEU A . n 
A 1 564  SER 564  713  713  SER SER A . n 
A 1 565  THR 565  714  714  THR THR A . n 
A 1 566  ASN 566  715  715  ASN ASN A . n 
A 1 567  ILE 567  716  716  ILE ILE A . n 
A 1 568  ALA 568  717  717  ALA ALA A . n 
A 1 569  GLU 569  718  718  GLU GLU A . n 
A 1 570  THR 570  719  719  THR THR A . n 
A 1 571  SER 571  720  720  SER SER A . n 
A 1 572  ILE 572  721  721  ILE ILE A . n 
A 1 573  THR 573  722  722  THR THR A . n 
A 1 574  ILE 574  723  723  ILE ILE A . n 
A 1 575  ASN 575  724  724  ASN ASN A . n 
A 1 576  ASP 576  725  725  ASP ASP A . n 
A 1 577  VAL 577  726  726  VAL VAL A . n 
A 1 578  VAL 578  727  727  VAL VAL A . n 
A 1 579  TYR 579  728  728  TYR TYR A . n 
A 1 580  VAL 580  729  729  VAL VAL A . n 
A 1 581  ILE 581  730  730  ILE ILE A . n 
A 1 582  ASP 582  731  731  ASP ASP A . n 
A 1 583  SER 583  732  732  SER SER A . n 
A 1 584  CYS 584  733  733  CYS CYS A . n 
A 1 585  LYS 585  734  734  LYS LYS A . n 
A 1 586  GLN 586  735  735  GLN GLN A . n 
A 1 587  LYS 587  736  736  LYS LYS A . n 
A 1 588  VAL 588  737  737  VAL VAL A . n 
A 1 589  LYS 589  738  738  LYS LYS A . n 
A 1 590  LEU 590  739  739  LEU LEU A . n 
A 1 591  PHE 591  740  740  PHE PHE A . n 
A 1 592  THR 592  741  741  THR THR A . n 
A 1 593  ALA 593  742  742  ALA ALA A . n 
A 1 594  HIS 594  743  743  HIS HIS A . n 
A 1 595  ASN 595  744  744  ASN ASN A . n 
A 1 596  ASN 596  745  745  ASN ASN A . n 
A 1 597  MET 597  746  746  MET MET A . n 
A 1 598  THR 598  747  747  THR THR A . n 
A 1 599  ASN 599  748  748  ASN ASN A . n 
A 1 600  TYR 600  749  749  TYR TYR A . n 
A 1 601  ALA 601  750  750  ALA ALA A . n 
A 1 602  THR 602  751  751  THR THR A . n 
A 1 603  VAL 603  752  752  VAL VAL A . n 
A 1 604  TRP 604  753  753  TRP TRP A . n 
A 1 605  ALA 605  754  754  ALA ALA A . n 
A 1 606  SER 606  755  755  SER SER A . n 
A 1 607  LYS 607  756  756  LYS LYS A . n 
A 1 608  THR 608  757  757  THR THR A . n 
A 1 609  ASN 609  758  758  ASN ASN A . n 
A 1 610  LEU 610  759  759  LEU LEU A . n 
A 1 611  GLU 611  760  760  GLU GLU A . n 
A 1 612  GLN 612  761  761  GLN GLN A . n 
A 1 613  ARG 613  762  762  ARG ARG A . n 
A 1 614  LYS 614  763  763  LYS LYS A . n 
A 1 615  GLY 615  764  764  GLY GLY A . n 
A 1 616  ARG 616  765  765  ARG ARG A . n 
A 1 617  ALA 617  766  766  ALA ALA A . n 
A 1 618  GLY 618  767  767  GLY GLY A . n 
A 1 619  ARG 619  768  768  ARG ARG A . n 
A 1 620  VAL 620  769  769  VAL VAL A . n 
A 1 621  ARG 621  770  770  ARG ARG A . n 
A 1 622  PRO 622  771  771  PRO PRO A . n 
A 1 623  GLY 623  772  772  GLY GLY A . n 
A 1 624  PHE 624  773  773  PHE PHE A . n 
A 1 625  CYS 625  774  774  CYS CYS A . n 
A 1 626  PHE 626  775  775  PHE PHE A . n 
A 1 627  HIS 627  776  776  HIS HIS A . n 
A 1 628  LEU 628  777  777  LEU LEU A . n 
A 1 629  CYS 629  778  778  CYS CYS A . n 
A 1 630  SER 630  779  779  SER SER A . n 
A 1 631  ARG 631  780  780  ARG ARG A . n 
A 1 632  ALA 632  781  781  ALA ALA A . n 
A 1 633  ARG 633  782  782  ARG ARG A . n 
A 1 634  PHE 634  783  783  PHE PHE A . n 
A 1 635  GLU 635  784  784  GLU GLU A . n 
A 1 636  ARG 636  785  785  ARG ARG A . n 
A 1 637  LEU 637  786  786  LEU LEU A . n 
A 1 638  GLU 638  787  787  GLU GLU A . n 
A 1 639  THR 639  788  788  THR THR A . n 
A 1 640  HIS 640  789  789  HIS HIS A . n 
A 1 641  MET 641  790  790  MET MET A . n 
A 1 642  THR 642  791  791  THR THR A . n 
A 1 643  PRO 643  792  792  PRO PRO A . n 
A 1 644  GLU 644  793  793  GLU GLU A . n 
A 1 645  MET 645  794  794  MET MET A . n 
A 1 646  PHE 646  795  795  PHE PHE A . n 
A 1 647  ARG 647  796  796  ARG ARG A . n 
A 1 648  THR 648  797  797  THR THR A . n 
A 1 649  PRO 649  798  798  PRO PRO A . n 
A 1 650  LEU 650  799  799  LEU LEU A . n 
A 1 651  HIS 651  800  800  HIS HIS A . n 
A 1 652  GLU 652  801  801  GLU GLU A . n 
A 1 653  ILE 653  802  802  ILE ILE A . n 
A 1 654  ALA 654  803  803  ALA ALA A . n 
A 1 655  LEU 655  804  804  LEU LEU A . n 
A 1 656  SER 656  805  805  SER SER A . n 
A 1 657  ILE 657  806  806  ILE ILE A . n 
A 1 658  LYS 658  807  807  LYS LYS A . n 
A 1 659  LEU 659  808  808  LEU LEU A . n 
A 1 660  LEU 660  809  809  LEU LEU A . n 
A 1 661  ARG 661  810  810  ARG ARG A . n 
A 1 662  LEU 662  811  811  LEU LEU A . n 
A 1 663  GLY 663  812  812  GLY GLY A . n 
A 1 664  GLY 664  813  813  GLY GLY A . n 
A 1 665  ILE 665  814  814  ILE ILE A . n 
A 1 666  GLY 666  815  815  GLY GLY A . n 
A 1 667  GLN 667  816  816  GLN GLN A . n 
A 1 668  PHE 668  817  817  PHE PHE A . n 
A 1 669  LEU 669  818  818  LEU LEU A . n 
A 1 670  ALA 670  819  819  ALA ALA A . n 
A 1 671  LYS 671  820  820  LYS LYS A . n 
A 1 672  ALA 672  821  821  ALA ALA A . n 
A 1 673  ILE 673  822  822  ILE ILE A . n 
A 1 674  GLU 674  823  823  GLU GLU A . n 
A 1 675  PRO 675  824  824  PRO PRO A . n 
A 1 676  PRO 676  825  825  PRO PRO A . n 
A 1 677  PRO 677  826  826  PRO PRO A . n 
A 1 678  LEU 678  827  827  LEU LEU A . n 
A 1 679  ASP 679  828  828  ASP ASP A . n 
A 1 680  ALA 680  829  829  ALA ALA A . n 
A 1 681  VAL 681  830  830  VAL VAL A . n 
A 1 682  ILE 682  831  831  ILE ILE A . n 
A 1 683  GLU 683  832  832  GLU GLU A . n 
A 1 684  ALA 684  833  833  ALA ALA A . n 
A 1 685  GLU 685  834  834  GLU GLU A . n 
A 1 686  HIS 686  835  835  HIS HIS A . n 
A 1 687  THR 687  836  836  THR THR A . n 
A 1 688  LEU 688  837  837  LEU LEU A . n 
A 1 689  ARG 689  838  838  ARG ARG A . n 
A 1 690  GLU 690  839  839  GLU GLU A . n 
A 1 691  LEU 691  840  840  LEU LEU A . n 
A 1 692  ASP 692  841  841  ASP ASP A . n 
A 1 693  ALA 693  842  842  ALA ALA A . n 
A 1 694  LEU 694  843  843  LEU LEU A . n 
A 1 695  ASP 695  844  844  ASP ASP A . n 
A 1 696  ALA 696  845  845  ALA ALA A . n 
A 1 697  ASN 697  846  846  ASN ASN A . n 
A 1 698  ASP 698  847  847  ASP ASP A . n 
A 1 699  GLU 699  848  848  GLU GLU A . n 
A 1 700  LEU 700  849  849  LEU LEU A . n 
A 1 701  THR 701  850  850  THR THR A . n 
A 1 702  PRO 702  851  851  PRO PRO A . n 
A 1 703  LEU 703  852  852  LEU LEU A . n 
A 1 704  GLY 704  853  853  GLY GLY A . n 
A 1 705  ARG 705  854  854  ARG ARG A . n 
A 1 706  ILE 706  855  855  ILE ILE A . n 
A 1 707  LEU 707  856  856  LEU LEU A . n 
A 1 708  ALA 708  857  857  ALA ALA A . n 
A 1 709  LYS 709  858  858  LYS LYS A . n 
A 1 710  LEU 710  859  859  LEU LEU A . n 
A 1 711  PRO 711  860  860  PRO PRO A . n 
A 1 712  ILE 712  861  861  ILE ILE A . n 
A 1 713  GLU 713  862  862  GLU GLU A . n 
A 1 714  PRO 714  863  863  PRO PRO A . n 
A 1 715  ARG 715  864  864  ARG ARG A . n 
A 1 716  PHE 716  865  865  PHE PHE A . n 
A 1 717  GLY 717  866  866  GLY GLY A . n 
A 1 718  LYS 718  867  867  LYS LYS A . n 
A 1 719  MET 719  868  868  MET MET A . n 
A 1 720  MET 720  869  869  MET MET A . n 
A 1 721  ILE 721  870  870  ILE ILE A . n 
A 1 722  MET 722  871  871  MET MET A . n 
A 1 723  GLY 723  872  872  GLY GLY A . n 
A 1 724  CYS 724  873  873  CYS CYS A . n 
A 1 725  ILE 725  874  874  ILE ILE A . n 
A 1 726  PHE 726  875  875  PHE PHE A . n 
A 1 727  TYR 727  876  876  TYR TYR A . n 
A 1 728  VAL 728  877  877  VAL VAL A . n 
A 1 729  GLY 729  878  878  GLY GLY A . n 
A 1 730  ASP 730  879  879  ASP ASP A . n 
A 1 731  ALA 731  880  880  ALA ALA A . n 
A 1 732  VAL 732  881  881  VAL VAL A . n 
A 1 733  CYS 733  882  882  CYS CYS A . n 
A 1 734  THR 734  883  883  THR THR A . n 
A 1 735  ILE 735  884  884  ILE ILE A . n 
A 1 736  SER 736  885  885  SER SER A . n 
A 1 737  ALA 737  886  886  ALA ALA A . n 
A 1 738  ALA 738  887  887  ALA ALA A . n 
A 1 739  THR 739  888  888  THR THR A . n 
A 1 740  CYS 740  889  889  CYS CYS A . n 
A 1 741  PHE 741  890  890  PHE PHE A . n 
A 1 742  PRO 742  891  891  PRO PRO A . n 
A 1 743  GLU 743  892  892  GLU GLU A . n 
A 1 744  PRO 744  893  893  PRO PRO A . n 
A 1 745  PHE 745  894  894  PHE PHE A . n 
A 1 746  ILE 746  895  895  ILE ILE A . n 
A 1 747  SER 747  896  896  SER SER A . n 
A 1 748  GLU 748  897  897  GLU GLU A . n 
A 1 749  GLY 749  898  898  GLY GLY A . n 
A 1 750  LYS 750  899  899  LYS LYS A . n 
A 1 751  ARG 751  900  900  ARG ARG A . n 
A 1 752  LEU 752  901  901  LEU LEU A . n 
A 1 753  GLY 753  902  902  GLY GLY A . n 
A 1 754  TYR 754  903  903  TYR TYR A . n 
A 1 755  VAL 755  904  904  VAL VAL A . n 
A 1 756  HIS 756  905  905  HIS HIS A . n 
A 1 757  ARG 757  906  906  ARG ARG A . n 
A 1 758  ASN 758  907  907  ASN ASN A . n 
A 1 759  PHE 759  908  908  PHE PHE A . n 
A 1 760  ALA 760  909  909  ALA ALA A . n 
A 1 761  GLY 761  910  910  GLY GLY A . n 
A 1 762  ASN 762  911  911  ASN ASN A . n 
A 1 763  ARG 763  912  912  ARG ARG A . n 
A 1 764  PHE 764  913  913  PHE PHE A . n 
A 1 765  SER 765  914  914  SER SER A . n 
A 1 766  ASP 766  915  915  ASP ASP A . n 
A 1 767  HIS 767  916  916  HIS HIS A . n 
A 1 768  VAL 768  917  917  VAL VAL A . n 
A 1 769  ALA 769  918  918  ALA ALA A . n 
A 1 770  LEU 770  919  919  LEU LEU A . n 
A 1 771  LEU 771  920  920  LEU LEU A . n 
A 1 772  SER 772  921  921  SER SER A . n 
A 1 773  VAL 773  922  922  VAL VAL A . n 
A 1 774  PHE 774  923  923  PHE PHE A . n 
A 1 775  GLN 775  924  924  GLN GLN A . n 
A 1 776  ALA 776  925  925  ALA ALA A . n 
A 1 777  TRP 777  926  926  TRP TRP A . n 
A 1 778  ASP 778  927  927  ASP ASP A . n 
A 1 779  ASP 779  928  928  ASP ASP A . n 
A 1 780  ALA 780  929  929  ALA ALA A . n 
A 1 781  ARG 781  930  930  ARG ARG A . n 
A 1 782  MET 782  931  931  MET MET A . n 
A 1 783  GLY 783  932  932  GLY GLY A . n 
A 1 784  GLY 784  933  933  GLY GLY A . n 
A 1 785  GLU 785  934  934  GLU GLU A . n 
A 1 786  GLU 786  935  935  GLU GLU A . n 
A 1 787  ALA 787  936  936  ALA ALA A . n 
A 1 788  GLU 788  937  937  GLU GLU A . n 
A 1 789  ILE 789  938  938  ILE ILE A . n 
A 1 790  ARG 790  939  939  ARG ARG A . n 
A 1 791  PHE 791  940  940  PHE PHE A . n 
A 1 792  CYS 792  941  941  CYS CYS A . n 
A 1 793  GLU 793  942  942  GLU GLU A . n 
A 1 794  HIS 794  943  943  HIS HIS A . n 
A 1 795  LYS 795  944  944  LYS LYS A . n 
A 1 796  ARG 796  945  945  ARG ARG A . n 
A 1 797  LEU 797  946  946  LEU LEU A . n 
A 1 798  ASN 798  947  947  ASN ASN A . n 
A 1 799  MET 799  948  948  MET MET A . n 
A 1 800  ALA 800  949  949  ALA ALA A . n 
A 1 801  THR 801  950  950  THR THR A . n 
A 1 802  LEU 802  951  951  LEU LEU A . n 
A 1 803  ARG 803  952  952  ARG ARG A . n 
A 1 804  MET 804  953  953  MET MET A . n 
A 1 805  THR 805  954  954  THR THR A . n 
A 1 806  TRP 806  955  955  TRP TRP A . n 
A 1 807  GLU 807  956  956  GLU GLU A . n 
A 1 808  ALA 808  957  957  ALA ALA A . n 
A 1 809  LYS 809  958  958  LYS LYS A . n 
A 1 810  VAL 810  959  959  VAL VAL A . n 
A 1 811  GLN 811  960  960  GLN GLN A . n 
A 1 812  LEU 812  961  961  LEU LEU A . n 
A 1 813  LYS 813  962  962  LYS LYS A . n 
A 1 814  GLU 814  963  963  GLU GLU A . n 
A 1 815  ILE 815  964  964  ILE ILE A . n 
A 1 816  LEU 816  965  965  LEU LEU A . n 
A 1 817  ILE 817  966  966  ILE ILE A . n 
A 1 818  ASN 818  967  967  ASN ASN A . n 
A 1 819  SER 819  968  968  SER SER A . n 
A 1 820  GLY 820  969  969  GLY GLY A . n 
A 1 821  PHE 821  970  970  PHE PHE A . n 
A 1 822  PRO 822  971  971  PRO PRO A . n 
A 1 823  GLU 823  972  972  GLU GLU A . n 
A 1 824  ASP 824  973  973  ASP ASP A . n 
A 1 825  CYS 825  974  974  CYS CYS A . n 
A 1 826  LEU 826  975  975  LEU LEU A . n 
A 1 827  LEU 827  976  976  LEU LEU A . n 
A 1 828  THR 828  977  977  THR THR A . n 
A 1 829  GLN 829  978  978  GLN GLN A . n 
A 1 830  VAL 830  979  979  VAL VAL A . n 
A 1 831  PHE 831  980  980  PHE PHE A . n 
A 1 832  THR 832  981  981  THR THR A . n 
A 1 833  ASN 833  982  982  ASN ASN A . n 
A 1 834  THR 834  983  983  THR THR A . n 
A 1 835  GLY 835  984  984  GLY GLY A . n 
A 1 836  PRO 836  985  985  PRO PRO A . n 
A 1 837  ASP 837  986  986  ASP ASP A . n 
A 1 838  ASN 838  987  987  ASN ASN A . n 
A 1 839  ASN 839  988  988  ASN ASN A . n 
A 1 840  LEU 840  989  989  LEU LEU A . n 
A 1 841  ASP 841  990  990  ASP ASP A . n 
A 1 842  VAL 842  991  991  VAL VAL A . n 
A 1 843  VAL 843  992  992  VAL VAL A . n 
A 1 844  ILE 844  993  993  ILE ILE A . n 
A 1 845  SER 845  994  994  SER SER A . n 
A 1 846  LEU 846  995  995  LEU LEU A . n 
A 1 847  LEU 847  996  996  LEU LEU A . n 
A 1 848  ALA 848  997  997  ALA ALA A . n 
A 1 849  PHE 849  998  998  PHE PHE A . n 
A 1 850  GLY 850  999  999  GLY GLY A . n 
A 1 851  VAL 851  1000 1000 VAL VAL A . n 
A 1 852  TYR 852  1001 1001 TYR TYR A . n 
A 1 853  PRO 853  1002 1002 PRO PRO A . n 
A 1 854  ASN 854  1003 1003 ASN ASN A . n 
A 1 855  VAL 855  1004 1004 VAL VAL A . n 
A 1 856  CYS 856  1005 1005 CYS CYS A . n 
A 1 857  TYR 857  1006 1006 TYR TYR A . n 
A 1 858  HIS 858  1007 1007 HIS HIS A . n 
A 1 859  LYS 859  1008 1008 LYS LYS A . n 
A 1 860  GLU 860  1009 1009 GLU GLU A . n 
A 1 861  LYS 861  1010 1010 LYS LYS A . n 
A 1 862  ARG 862  1011 1011 ARG ARG A . n 
A 1 863  LYS 863  1012 1012 LYS LYS A . n 
A 1 864  ILE 864  1013 1013 ILE ILE A . n 
A 1 865  LEU 865  1014 1014 LEU LEU A . n 
A 1 866  THR 866  1015 1015 THR THR A . n 
A 1 867  THR 867  1016 1016 THR THR A . n 
A 1 868  GLU 868  1017 1017 GLU GLU A . n 
A 1 869  GLY 869  1018 1018 GLY GLY A . n 
A 1 870  ARG 870  1019 1019 ARG ARG A . n 
A 1 871  ASN 871  1020 1020 ASN ASN A . n 
A 1 872  ALA 872  1021 1021 ALA ALA A . n 
A 1 873  LEU 873  1022 1022 LEU LEU A . n 
A 1 874  ILE 874  1023 1023 ILE ILE A . n 
A 1 875  HIS 875  1024 1024 HIS HIS A . n 
A 1 876  LYS 876  1025 1025 LYS LYS A . n 
A 1 877  SER 877  1026 1026 SER SER A . n 
A 1 878  SER 878  1027 1027 SER SER A . n 
A 1 879  VAL 879  1028 1028 VAL VAL A . n 
A 1 880  ASN 880  1029 1029 ASN ASN A . n 
A 1 881  CYS 881  1030 1030 CYS CYS A . n 
A 1 882  PRO 882  1031 1031 PRO PRO A . n 
A 1 883  PHE 883  1032 1032 PHE PHE A . n 
A 1 884  SER 884  1033 1033 SER SER A . n 
A 1 885  SER 885  1034 1034 SER SER A . n 
A 1 886  GLN 886  1035 1035 GLN GLN A . n 
A 1 887  ASP 887  1036 1036 ASP ASP A . n 
A 1 888  MET 888  1037 1037 MET MET A . n 
A 1 889  LYS 889  1038 1038 LYS LYS A . n 
A 1 890  TYR 890  1039 1039 TYR TYR A . n 
A 1 891  PRO 891  1040 1040 PRO PRO A . n 
A 1 892  SER 892  1041 1041 SER SER A . n 
A 1 893  PRO 893  1042 1042 PRO PRO A . n 
A 1 894  PHE 894  1043 1043 PHE PHE A . n 
A 1 895  PHE 895  1044 1044 PHE PHE A . n 
A 1 896  VAL 896  1045 1045 VAL VAL A . n 
A 1 897  PHE 897  1046 1046 PHE PHE A . n 
A 1 898  GLY 898  1047 1047 GLY GLY A . n 
A 1 899  GLU 899  1048 1048 GLU GLU A . n 
A 1 900  LYS 900  1049 1049 LYS LYS A . n 
A 1 901  ILE 901  1050 1050 ILE ILE A . n 
A 1 902  ARG 902  1051 1051 ARG ARG A . n 
A 1 903  THR 903  1052 1052 THR THR A . n 
A 1 904  ARG 904  1053 1053 ARG ARG A . n 
A 1 905  ALA 905  1054 1054 ALA ALA A . n 
A 1 906  ILE 906  1055 1055 ILE ILE A . n 
A 1 907  SER 907  1056 1056 SER SER A . n 
A 1 908  ALA 908  1057 1057 ALA ALA A . n 
A 1 909  LYS 909  1058 1058 LYS LYS A . n 
A 1 910  GLY 910  1059 1059 GLY GLY A . n 
A 1 911  MET 911  1060 1060 MET MET A . n 
A 1 912  THR 912  1061 1061 THR THR A . n 
A 1 913  LEU 913  1062 1062 LEU LEU A . n 
A 1 914  VAL 914  1063 1063 VAL VAL A . n 
A 1 915  THR 915  1064 1064 THR THR A . n 
A 1 916  PRO 916  1065 1065 PRO PRO A . n 
A 1 917  LEU 917  1066 1066 LEU LEU A . n 
A 1 918  GLN 918  1067 1067 GLN GLN A . n 
A 1 919  LEU 919  1068 1068 LEU LEU A . n 
A 1 920  LEU 920  1069 1069 LEU LEU A . n 
A 1 921  LEU 921  1070 1070 LEU LEU A . n 
A 1 922  PHE 922  1071 1071 PHE PHE A . n 
A 1 923  ALA 923  1072 1072 ALA ALA A . n 
A 1 924  SER 924  1073 1073 SER SER A . n 
A 1 925  LYS 925  1074 1074 LYS LYS A . n 
A 1 926  LYS 926  1075 1075 LYS LYS A . n 
A 1 927  VAL 927  1076 1076 VAL VAL A . n 
A 1 928  GLN 928  1077 1077 GLN GLN A . n 
A 1 929  SER 929  1078 1078 SER SER A . n 
A 1 930  ASP 930  1079 1079 ASP ASP A . n 
A 1 931  GLY 931  1080 1080 GLY GLY A . n 
A 1 932  GLN 932  1081 1081 GLN GLN A . n 
A 1 933  ILE 933  1082 1082 ILE ILE A . n 
A 1 934  VAL 934  1083 1083 VAL VAL A . n 
A 1 935  LEU 935  1084 1084 LEU LEU A . n 
A 1 936  VAL 936  1085 1085 VAL VAL A . n 
A 1 937  ASP 937  1086 1086 ASP ASP A . n 
A 1 938  ASP 938  1087 1087 ASP ASP A . n 
A 1 939  TRP 939  1088 1088 TRP TRP A . n 
A 1 940  ILE 940  1089 1089 ILE ILE A . n 
A 1 941  ARG 941  1090 1090 ARG ARG A . n 
A 1 942  LEU 942  1091 1091 LEU LEU A . n 
A 1 943  GLN 943  1092 1092 GLN GLN A . n 
A 1 944  ILE 944  1093 1093 ILE ILE A . n 
A 1 945  SER 945  1094 1094 SER SER A . n 
A 1 946  HIS 946  1095 1095 HIS HIS A . n 
A 1 947  GLU 947  1096 1096 GLU GLU A . n 
A 1 948  ALA 948  1097 1097 ALA ALA A . n 
A 1 949  ALA 949  1098 1098 ALA ALA A . n 
A 1 950  ALA 950  1099 1099 ALA ALA A . n 
A 1 951  CYS 951  1100 1100 CYS CYS A . n 
A 1 952  ILE 952  1101 1101 ILE ILE A . n 
A 1 953  THR 953  1102 1102 THR THR A . n 
A 1 954  ALA 954  1103 1103 ALA ALA A . n 
A 1 955  LEU 955  1104 1104 LEU LEU A . n 
A 1 956  ARG 956  1105 1105 ARG ARG A . n 
A 1 957  ALA 957  1106 1106 ALA ALA A . n 
A 1 958  ALA 958  1107 1107 ALA ALA A . n 
A 1 959  MET 959  1108 1108 MET MET A . n 
A 1 960  GLU 960  1109 1109 GLU GLU A . n 
A 1 961  ALA 961  1110 1110 ALA ALA A . n 
A 1 962  LEU 962  1111 1111 LEU LEU A . n 
A 1 963  VAL 963  1112 1112 VAL VAL A . n 
A 1 964  VAL 964  1113 1113 VAL VAL A . n 
A 1 965  GLU 965  1114 1114 GLU GLU A . n 
A 1 966  VAL 966  1115 1115 VAL VAL A . n 
A 1 967  THR 967  1116 1116 THR THR A . n 
A 1 968  LYS 968  1117 1117 LYS LYS A . n 
A 1 969  GLN 969  1118 1118 GLN GLN A . n 
A 1 970  PRO 970  1119 1119 PRO PRO A . n 
A 1 971  ASN 971  1120 1120 ASN ASN A . n 
A 1 972  ILE 972  1121 1121 ILE ILE A . n 
A 1 973  ILE 973  1122 1122 ILE ILE A . n 
A 1 974  SER 974  1123 1123 SER SER A . n 
A 1 975  GLN 975  1124 1124 GLN GLN A . n 
A 1 976  LEU 976  1125 1125 LEU LEU A . n 
A 1 977  ASP 977  1126 1126 ASP ASP A . n 
A 1 978  PRO 978  1127 1127 PRO PRO A . n 
A 1 979  VAL 979  1128 1128 VAL VAL A . n 
A 1 980  ASN 980  1129 1129 ASN ASN A . n 
A 1 981  GLU 981  1130 1130 GLU GLU A . n 
A 1 982  HIS 982  1131 1131 HIS HIS A . n 
A 1 983  MET 983  1132 1132 MET MET A . n 
A 1 984  LEU 984  1133 1133 LEU LEU A . n 
A 1 985  ASN 985  1134 1134 ASN ASN A . n 
A 1 986  MET 986  1135 1135 MET MET A . n 
A 1 987  ILE 987  1136 1136 ILE ILE A . n 
A 1 988  ARG 988  1137 1137 ARG ARG A . n 
A 1 989  GLN 989  1138 1138 GLN GLN A . n 
A 1 990  ILE 990  1139 1139 ILE ILE A . n 
A 1 991  SER 991  1140 1140 SER SER A . n 
A 1 992  ARG 992  1141 1141 ARG ARG A . n 
A 1 993  PRO 993  1142 1142 PRO PRO A . n 
A 1 994  SER 994  1143 1143 SER SER A . n 
A 1 995  ALA 995  1144 1144 ALA ALA A . n 
A 1 996  ALA 996  1145 1145 ALA ALA A . n 
A 1 997  GLY 997  1146 1146 GLY GLY A . n 
A 1 998  ILE 998  1147 1147 ILE ILE A . n 
A 1 999  ASN 999  1148 1148 ASN ASN A . n 
A 1 1000 LEU 1000 1149 1149 LEU LEU A . n 
A 1 1001 MET 1001 1150 1150 MET MET A . n 
A 1 1002 ILE 1002 1151 1151 ILE ILE A . n 
A 1 1003 ASP 1003 1152 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1153 ?    ?   ?   A . n 
A 1 1005 LYS 1005 1154 ?    ?   ?   A . n 
A 1 1006 ASP 1006 1155 ?    ?   ?   A . n 
A 1 1007 ASP 1007 1156 ?    ?   ?   A . n 
A 1 1008 ASP 1008 1157 ?    ?   ?   A . n 
A 1 1009 ASP 1009 1158 ?    ?   ?   A . n 
A 1 1010 LYS 1010 1159 ?    ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BKZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BKZ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BKZ 1   1201 1201 A1BKZ LIG A . 
C 3 ADP   1   1202 1202 ADP   ADP A . 
D 4 MG    1   1203 1203 MG    MG  A . 
E 5 SO4   1   1204 1204 SO4   SO4 A . 
F 5 SO4   1   1205 1205 SO4   SO4 A . 
G 5 SO4   1   1206 1206 SO4   SO4 A . 
H 5 SO4   1   1207 1207 SO4   SO4 A . 
I 5 SO4   1   1208 1208 SO4   SO4 A . 
J 6 EDO   1   1209 1209 EDO   EDO A . 
K 6 EDO   1   1210 1210 EDO   EDO A . 
L 6 EDO   1   1211 1211 EDO   EDO A . 
M 6 EDO   1   1212 1212 EDO   EDO A . 
N 6 EDO   1   1213 1213 EDO   EDO A . 
O 7 HOH   1   1301 1216 HOH   HOH A . 
O 7 HOH   2   1302 1214 HOH   HOH A . 
O 7 HOH   3   1303 1290 HOH   HOH A . 
O 7 HOH   4   1304 1301 HOH   HOH A . 
O 7 HOH   5   1305 1234 HOH   HOH A . 
O 7 HOH   6   1306 1293 HOH   HOH A . 
O 7 HOH   7   1307 1318 HOH   HOH A . 
O 7 HOH   8   1308 1319 HOH   HOH A . 
O 7 HOH   9   1309 1235 HOH   HOH A . 
O 7 HOH   10  1310 1227 HOH   HOH A . 
O 7 HOH   11  1311 1303 HOH   HOH A . 
O 7 HOH   12  1312 1275 HOH   HOH A . 
O 7 HOH   13  1313 1267 HOH   HOH A . 
O 7 HOH   14  1314 1226 HOH   HOH A . 
O 7 HOH   15  1315 1278 HOH   HOH A . 
O 7 HOH   16  1316 1308 HOH   HOH A . 
O 7 HOH   17  1317 1295 HOH   HOH A . 
O 7 HOH   18  1318 1276 HOH   HOH A . 
O 7 HOH   19  1319 1277 HOH   HOH A . 
O 7 HOH   20  1320 1260 HOH   HOH A . 
O 7 HOH   21  1321 1215 HOH   HOH A . 
O 7 HOH   22  1322 1298 HOH   HOH A . 
O 7 HOH   23  1323 1263 HOH   HOH A . 
O 7 HOH   24  1324 1257 HOH   HOH A . 
O 7 HOH   25  1325 1312 HOH   HOH A . 
O 7 HOH   26  1326 1317 HOH   HOH A . 
O 7 HOH   27  1327 1259 HOH   HOH A . 
O 7 HOH   28  1328 1281 HOH   HOH A . 
O 7 HOH   29  1329 1279 HOH   HOH A . 
O 7 HOH   30  1330 1264 HOH   HOH A . 
O 7 HOH   31  1331 1254 HOH   HOH A . 
O 7 HOH   32  1332 1261 HOH   HOH A . 
O 7 HOH   33  1333 1304 HOH   HOH A . 
O 7 HOH   34  1334 1329 HOH   HOH A . 
O 7 HOH   35  1335 1291 HOH   HOH A . 
O 7 HOH   36  1336 1272 HOH   HOH A . 
O 7 HOH   37  1337 1232 HOH   HOH A . 
O 7 HOH   38  1338 1307 HOH   HOH A . 
O 7 HOH   39  1339 1326 HOH   HOH A . 
O 7 HOH   40  1340 1327 HOH   HOH A . 
O 7 HOH   41  1341 1225 HOH   HOH A . 
O 7 HOH   42  1342 1271 HOH   HOH A . 
O 7 HOH   43  1343 1248 HOH   HOH A . 
O 7 HOH   44  1344 1220 HOH   HOH A . 
O 7 HOH   45  1345 1262 HOH   HOH A . 
O 7 HOH   46  1346 1325 HOH   HOH A . 
O 7 HOH   47  1347 1228 HOH   HOH A . 
O 7 HOH   48  1348 1306 HOH   HOH A . 
O 7 HOH   49  1349 1324 HOH   HOH A . 
O 7 HOH   50  1350 1253 HOH   HOH A . 
O 7 HOH   51  1351 1222 HOH   HOH A . 
O 7 HOH   52  1352 1269 HOH   HOH A . 
O 7 HOH   53  1353 1273 HOH   HOH A . 
O 7 HOH   54  1354 1239 HOH   HOH A . 
O 7 HOH   55  1355 1255 HOH   HOH A . 
O 7 HOH   56  1356 1289 HOH   HOH A . 
O 7 HOH   57  1357 1274 HOH   HOH A . 
O 7 HOH   58  1358 1243 HOH   HOH A . 
O 7 HOH   59  1359 1233 HOH   HOH A . 
O 7 HOH   60  1360 1299 HOH   HOH A . 
O 7 HOH   61  1361 1251 HOH   HOH A . 
O 7 HOH   62  1362 1240 HOH   HOH A . 
O 7 HOH   63  1363 1322 HOH   HOH A . 
O 7 HOH   64  1364 1288 HOH   HOH A . 
O 7 HOH   65  1365 1231 HOH   HOH A . 
O 7 HOH   66  1366 1244 HOH   HOH A . 
O 7 HOH   67  1367 1237 HOH   HOH A . 
O 7 HOH   68  1368 1241 HOH   HOH A . 
O 7 HOH   69  1369 1285 HOH   HOH A . 
O 7 HOH   70  1370 1250 HOH   HOH A . 
O 7 HOH   71  1371 1247 HOH   HOH A . 
O 7 HOH   72  1372 1321 HOH   HOH A . 
O 7 HOH   73  1373 1270 HOH   HOH A . 
O 7 HOH   74  1374 1265 HOH   HOH A . 
O 7 HOH   75  1375 1256 HOH   HOH A . 
O 7 HOH   76  1376 1315 HOH   HOH A . 
O 7 HOH   77  1377 1330 HOH   HOH A . 
O 7 HOH   78  1378 1230 HOH   HOH A . 
O 7 HOH   79  1379 1218 HOH   HOH A . 
O 7 HOH   80  1380 1314 HOH   HOH A . 
O 7 HOH   81  1381 1266 HOH   HOH A . 
O 7 HOH   82  1382 1302 HOH   HOH A . 
O 7 HOH   83  1383 1238 HOH   HOH A . 
O 7 HOH   84  1384 1221 HOH   HOH A . 
O 7 HOH   85  1385 1229 HOH   HOH A . 
O 7 HOH   86  1386 1242 HOH   HOH A . 
O 7 HOH   87  1387 1252 HOH   HOH A . 
O 7 HOH   88  1388 1236 HOH   HOH A . 
O 7 HOH   89  1389 1286 HOH   HOH A . 
O 7 HOH   90  1390 1320 HOH   HOH A . 
O 7 HOH   91  1391 1282 HOH   HOH A . 
O 7 HOH   92  1392 1217 HOH   HOH A . 
O 7 HOH   93  1393 1297 HOH   HOH A . 
O 7 HOH   94  1394 1223 HOH   HOH A . 
O 7 HOH   95  1395 1224 HOH   HOH A . 
O 7 HOH   96  1396 1292 HOH   HOH A . 
O 7 HOH   97  1397 1249 HOH   HOH A . 
O 7 HOH   98  1398 1268 HOH   HOH A . 
O 7 HOH   99  1399 1219 HOH   HOH A . 
O 7 HOH   100 1400 1294 HOH   HOH A . 
O 7 HOH   101 1401 1323 HOH   HOH A . 
O 7 HOH   102 1402 1331 HOH   HOH A . 
O 7 HOH   103 1403 1283 HOH   HOH A . 
O 7 HOH   104 1404 1328 HOH   HOH A . 
O 7 HOH   105 1405 1296 HOH   HOH A . 
O 7 HOH   106 1406 1284 HOH   HOH A . 
O 7 HOH   107 1407 1258 HOH   HOH A . 
O 7 HOH   108 1408 1310 HOH   HOH A . 
O 7 HOH   109 1409 1280 HOH   HOH A . 
O 7 HOH   110 1410 1245 HOH   HOH A . 
O 7 HOH   111 1411 1332 HOH   HOH A . 
O 7 HOH   112 1412 1313 HOH   HOH A . 
O 7 HOH   113 1413 1316 HOH   HOH A . 
O 7 HOH   114 1414 1311 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 4 
# 
_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                     9MFQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.730 
_cell.length_a_esd                 ? 
_cell.length_b                     85.730 
_cell.length_b_esd                 ? 
_cell.length_c                     348.480 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9MFQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   9MFQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.79 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.15 M Ammonium sulfate, 0.1 M TRIS pH 8, 20% w/v PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MFQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.99 
_reflns.d_resolution_low                               43.05 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     27613 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                24.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.168 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.99 
_reflns_shell.d_res_low                                     3.17 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4318 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               19.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.186 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            1.70 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            1.70 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -3.41 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               74.333 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.925 
_refine.correlation_coeff_Fo_to_Fc_free          0.880 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MFQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.99 
_refine.ls_d_res_low                             42.90 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     26157 
_refine.ls_number_reflns_R_free                  1357 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.22872 
_refine.ls_R_factor_R_free                       0.27682 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22620 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.435 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             18.194 
_refine.overall_SU_ML                            0.322 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.99 
_refine_hist.d_res_low                        42.90 
_refine_hist.number_atoms_solvent             114 
_refine_hist.number_atoms_total               7005 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6793 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         98 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  0.013  7042  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  6743  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.159  1.649  9554  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.012  1.573  15532 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.063  5.000  855   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 28.963 22.369 363   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.689 15.000 1212  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.561 15.000 47    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.034  0.200  931   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  7840  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1576  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.841  7.877  3426  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.837  7.876  3425  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.193  11.810 4276  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.193  11.811 4277  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.526  8.106  3616  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.526  8.107  3617  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.742  12.091 5278  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.339  91.546 7459  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.307  91.559 7445  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.99 
_refine_ls_shell.d_res_low                        3.063 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             104 
_refine_ls_shell.number_reflns_R_work             1868 
_refine_ls_shell.percent_reflns_obs               98.65 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.335 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.367 
# 
_struct.entry_id                     9MFQ 
_struct.title                        'Cat DHX9 in Complex with Compound 10 and ADP' 
_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        9MFQ 
_struct_keywords.text            'Helicase, DHX9, Inhibitor, Complex, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    M3WPI7_FELCA 
_struct_ref.pdbx_db_accession          M3WPI7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAR
EHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGETVEPYKVNLSQDLEHQLQNVIQELNLEIVPPPEDPFLPVV
LNLGKLAHFEPSQRQNQIGVVPWSPPQSNWNPWTSSNIDEGPLAYATPEQISMDLKNELMYQLEQDHDLQAILQERELLP
VKKFESEILEAISQNSVIIIRGATGCGKTTQVPQFILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAYERGEEPGKSC
GYSVRFESVLPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPEVRIVLMSATIDTS
MFCEYFFNCPIIEVYGRTYPVQEYFLEDCIQMTHFVPPPKDKKKKEKDDDGFEDDDANCNLICGDEYGPETRMSMAQLNE
KETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLEMNPHFGSHRYQILPLHSQIPREEQRKVFDPVPSGVTKV
ILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFERLETHM
TPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAVIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMI
MGCIFYVGDAVCTISAATCFPEPFISEGKRLGYVHRNFAGNRFSDHVALLSVFQAWDDARMGGEEAEIRFCEHKRLNMAT
LRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNC
PFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVLVDDWIRLQISHEAAACITALRAAMEA
LVVEVTKQPNIISQLDPVNEHMLNMIRQISRPSAAGINLMI
;
_struct_ref.pdbx_align_begin           151 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MFQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1002 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             M3WPI7 
_struct_ref_seq.db_align_beg                  151 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1151 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       151 
_struct_ref_seq.pdbx_auth_seq_align_end       1151 
# 
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 9MFQ MET A 1    ? UNP M3WPI7 ? ? 'initiating methionine' 150  1 
1 9MFQ ASP A 1003 ? UNP M3WPI7 ? ? 'expression tag'        1152 2 
1 9MFQ TYR A 1004 ? UNP M3WPI7 ? ? 'expression tag'        1153 3 
1 9MFQ LYS A 1005 ? UNP M3WPI7 ? ? 'expression tag'        1154 4 
1 9MFQ ASP A 1006 ? UNP M3WPI7 ? ? 'expression tag'        1155 5 
1 9MFQ ASP A 1007 ? UNP M3WPI7 ? ? 'expression tag'        1156 6 
1 9MFQ ASP A 1008 ? UNP M3WPI7 ? ? 'expression tag'        1157 7 
1 9MFQ ASP A 1009 ? UNP M3WPI7 ? ? 'expression tag'        1158 8 
1 9MFQ LYS A 1010 ? UNP M3WPI7 ? ? 'expression tag'        1159 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 131 ? LEU A 145 ? SER A 280  LEU A 294  1 ? 15 
HELX_P HELX_P2  AA2 GLY A 202 ? TYR A 206 ? GLY A 351  TYR A 355  5 ? 5  
HELX_P HELX_P3  AA3 THR A 208 ? ASP A 227 ? THR A 357  ASP A 376  1 ? 20 
HELX_P HELX_P4  AA4 ASP A 227 ? GLU A 238 ? ASP A 376  GLU A 387  1 ? 12 
HELX_P HELX_P5  AA5 LEU A 239 ? LYS A 244 ? LEU A 388  LYS A 393  5 ? 6  
HELX_P HELX_P6  AA6 PHE A 245 ? ASN A 256 ? PHE A 394  ASN A 405  1 ? 12 
HELX_P HELX_P7  AA7 GLY A 268 ? ASN A 284 ? GLY A 417  ASN A 433  1 ? 17 
HELX_P HELX_P8  AA8 ARG A 286 ? GLU A 289 ? ARG A 435  GLU A 438  5 ? 4  
HELX_P HELX_P9  AA9 ARG A 298 ? ARG A 313 ? ARG A 447  ARG A 462  1 ? 16 
HELX_P HELX_P10 AB1 VAL A 343 ? LEU A 350 ? VAL A 492  LEU A 499  1 ? 8  
HELX_P HELX_P11 AB2 GLU A 364 ? ARG A 368 ? GLU A 513  ARG A 517  5 ? 5  
HELX_P HELX_P12 AB3 ASP A 369 ? TYR A 386 ? ASP A 518  TYR A 535  1 ? 18 
HELX_P HELX_P13 AB4 THR A 400 ? PHE A 407 ? THR A 549  PHE A 556  1 ? 8  
HELX_P HELX_P14 AB5 PHE A 426 ? HIS A 435 ? PHE A 575  HIS A 584  1 ? 10 
HELX_P HELX_P15 AB6 GLY A 469 ? ALA A 477 ? GLY A 618  ALA A 626  1 ? 9  
HELX_P HELX_P16 AB7 PRO A 485 ? LEU A 499 ? PRO A 634  LEU A 648  1 ? 15 
HELX_P HELX_P17 AB8 GLY A 511 ? ASN A 525 ? GLY A 660  ASN A 674  1 ? 15 
HELX_P HELX_P18 AB9 PRO A 543 ? LYS A 549 ? PRO A 692  LYS A 698  1 ? 7  
HELX_P HELX_P19 AC1 ASN A 566 ? SER A 571 ? ASN A 715  SER A 720  1 ? 6  
HELX_P HELX_P20 AC2 SER A 606 ? GLY A 615 ? SER A 755  GLY A 764  1 ? 10 
HELX_P HELX_P21 AC3 SER A 630 ? LEU A 637 ? SER A 779  LEU A 786  1 ? 8  
HELX_P HELX_P22 AC4 PRO A 643 ? ARG A 647 ? PRO A 792  ARG A 796  5 ? 5  
HELX_P HELX_P23 AC5 LEU A 650 ? LEU A 660 ? LEU A 799  LEU A 809  1 ? 11 
HELX_P HELX_P24 AC6 GLY A 664 ? ALA A 670 ? GLY A 813  ALA A 819  1 ? 7  
HELX_P HELX_P25 AC7 PRO A 677 ? LEU A 691 ? PRO A 826  LEU A 840  1 ? 15 
HELX_P HELX_P26 AC8 THR A 701 ? LEU A 710 ? THR A 850  LEU A 859  1 ? 10 
HELX_P HELX_P27 AC9 GLU A 713 ? PHE A 726 ? GLU A 862  PHE A 875  1 ? 14 
HELX_P HELX_P28 AD1 VAL A 728 ? THR A 739 ? VAL A 877  THR A 888  1 ? 12 
HELX_P HELX_P29 AD2 GLY A 753 ? PHE A 759 ? GLY A 902  PHE A 908  1 ? 7  
HELX_P HELX_P30 AD3 SER A 765 ? ARG A 781 ? SER A 914  ARG A 930  1 ? 17 
HELX_P HELX_P31 AD4 GLY A 783 ? LYS A 795 ? GLY A 932  LYS A 944  1 ? 13 
HELX_P HELX_P32 AD5 ASN A 798 ? SER A 819 ? ASN A 947  SER A 968  1 ? 22 
HELX_P HELX_P33 AD6 PRO A 822 ? LEU A 826 ? PRO A 971  LEU A 975  5 ? 5  
HELX_P HELX_P34 AD7 ASP A 837 ? TYR A 852 ? ASP A 986  TYR A 1001 1 ? 16 
HELX_P HELX_P35 AD8 THR A 915 ? PHE A 922 ? THR A 1064 PHE A 1071 1 ? 8  
HELX_P HELX_P36 AD9 SER A 945 ? GLN A 969 ? SER A 1094 GLN A 1118 1 ? 25 
HELX_P HELX_P37 AE1 PRO A 970 ? SER A 974 ? PRO A 1119 SER A 1123 5 ? 5  
HELX_P HELX_P38 AE2 ASP A 977 ? SER A 991 ? ASP A 1126 SER A 1140 1 ? 15 
HELX_P HELX_P39 AE3 PRO A 993 ? GLY A 997 ? PRO A 1142 GLY A 1146 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 270 OG1 ? ? ? 1_555 D MG  . MG ? ? A THR 419  A MG  1203 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc2 metalc ? ? A GLU 364 OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 513  A MG  1203 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc3 metalc ? ? C ADP .   O3B ? ? ? 1_555 D MG  . MG ? ? A ADP 1202 A MG  1203 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc4 metalc ? ? D MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  1203 A HOH 1301 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc5 metalc ? ? D MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  1203 A HOH 1302 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc6 metalc ? ? D MG  .   MG  ? ? ? 1_555 O HOH . O  ? ? A MG  1203 A HOH 1321 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
# 
_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 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 OE2 ? A GLU 364 ? A GLU 513  ? 1_555 88.6  ? 
2  OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O3B ? C ADP .   ? A ADP 1202 ? 1_555 77.9  ? 
3  OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O3B ? C ADP .   ? A ADP 1202 ? 1_555 165.1 ? 
4  OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1301 ? 1_555 87.2  ? 
5  OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1301 ? 1_555 108.3 ? 
6  O3B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1301 ? 1_555 65.1  ? 
7  OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1302 ? 1_555 83.8  ? 
8  OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1302 ? 1_555 84.6  ? 
9  O3B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1302 ? 1_555 100.1 ? 
10 O   ? O HOH .   ? A HOH 1301 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1302 ? 1_555 164.1 ? 
11 OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1321 ? 1_555 164.0 ? 
12 OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1321 ? 1_555 97.5  ? 
13 O3B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1321 ? 1_555 97.2  ? 
14 O   ? O HOH .   ? A HOH 1301 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1321 ? 1_555 104.7 ? 
15 O   ? O HOH .   ? A HOH 1302 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? O HOH .   ? A HOH 1321 ? 1_555 82.0  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           852 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            1001 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    853 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     1002 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       7.27 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 8 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? parallel      
AA4 7 8 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA7 5 6 ? 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 TYR A 126 ? LYS A 127 ? TYR A 275  LYS A 276  
AA1 2 ILE A 940 ? GLN A 943 ? ILE A 1089 GLN A 1092 
AA1 3 ILE A 933 ? VAL A 936 ? ILE A 1082 VAL A 1085 
AA1 4 VAL A 927 ? SER A 929 ? VAL A 1076 SER A 1078 
AA1 5 VAL A 160 ? VAL A 161 ? VAL A 309  VAL A 310  
AA2 1 TRP A 184 ? SER A 185 ? TRP A 333  SER A 334  
AA2 2 ILE A 354 ? ARG A 355 ? ILE A 503  ARG A 504  
AA3 1 TRP A 191 ? ASN A 192 ? TRP A 340  ASN A 341  
AA3 2 SER A 197 ? ASN A 198 ? SER A 346  ASN A 347  
AA4 1 GLU A 328 ? VAL A 330 ? GLU A 477  VAL A 479  
AA4 2 CYS A 321 ? VAL A 325 ? CYS A 470  VAL A 474  
AA4 3 SER A 337 ? THR A 342 ? SER A 486  THR A 491  
AA4 4 ASN A 291 ? GLN A 296 ? ASN A 440  GLN A 445  
AA4 5 HIS A 359 ? VAL A 362 ? HIS A 508  VAL A 511  
AA4 6 ARG A 390 ? SER A 395 ? ARG A 539  SER A 544  
AA4 7 VAL A 258 ? GLY A 263 ? VAL A 407  GLY A 412  
AA4 8 ILE A 412 ? VAL A 415 ? ILE A 561  VAL A 564  
AA5 1 GLN A 423 ? TYR A 425 ? GLN A 572  TYR A 574  
AA5 2 PHE A 624 ? HIS A 627 ? PHE A 773  HIS A 776  
AA5 3 VAL A 577 ? ASP A 582 ? VAL A 726  ASP A 731  
AA5 4 ALA A 504 ? PHE A 508 ? ALA A 653  PHE A 657  
AA5 5 THR A 559 ? SER A 564 ? THR A 708  SER A 713  
AA5 6 TYR A 533 ? LEU A 538 ? TYR A 682  LEU A 687  
AA6 1 LYS A 585 ? THR A 592 ? LYS A 734  THR A 741  
AA6 2 MET A 597 ? TRP A 604 ? MET A 746  TRP A 753  
AA7 1 VAL A 855 ? GLU A 860 ? VAL A 1004 GLU A 1009 
AA7 2 LYS A 863 ? LEU A 865 ? LYS A 1012 LEU A 1014 
AA7 3 ASN A 871 ? ILE A 874 ? ASN A 1020 ILE A 1023 
AA7 4 ILE A 906 ? LEU A 913 ? ILE A 1055 LEU A 1062 
AA7 5 PHE A 894 ? ARG A 902 ? PHE A 1043 ARG A 1051 
AA7 6 VAL A 855 ? GLU A 860 ? VAL A 1004 GLU A 1009 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 126 ? N TYR A 275  O GLN A 943 ? O GLN A 1092 
AA1 2 3 O LEU A 942 ? O LEU A 1091 N VAL A 934 ? N VAL A 1083 
AA1 3 4 O LEU A 935 ? O LEU A 1084 N GLN A 928 ? N GLN A 1077 
AA1 4 5 O SER A 929 ? O SER A 1078 N VAL A 160 ? N VAL A 309  
AA2 1 2 N SER A 185 ? N SER A 334  O ILE A 354 ? O ILE A 503  
AA3 1 2 N ASN A 192 ? N ASN A 341  O SER A 197 ? O SER A 346  
AA4 1 2 O VAL A 330 ? O VAL A 479  N TYR A 323 ? N TYR A 472  
AA4 2 3 N GLY A 322 ? N GLY A 471  O PHE A 340 ? O PHE A 489  
AA4 3 4 O MET A 339 ? O MET A 488  N VAL A 294 ? N VAL A 443  
AA4 4 5 N VAL A 293 ? N VAL A 442  O ILE A 361 ? O ILE A 510  
AA4 5 6 N VAL A 360 ? N VAL A 509  O VAL A 392 ? O VAL A 541  
AA4 6 7 O LEU A 393 ? O LEU A 542  N ILE A 261 ? N ILE A 410  
AA4 7 8 N ILE A 260 ? N ILE A 409  O ILE A 413 ? O ILE A 562  
AA5 1 2 N TYR A 425 ? N TYR A 574  O HIS A 627 ? O HIS A 776  
AA5 2 3 O PHE A 626 ? O PHE A 775  N VAL A 580 ? N VAL A 729  
AA5 3 4 O ILE A 581 ? O ILE A 730  N PHE A 508 ? N PHE A 657  
AA5 4 5 N VAL A 507 ? N VAL A 656  O ILE A 562 ? O ILE A 711  
AA5 5 6 O THR A 559 ? O THR A 708  N GLN A 534 ? N GLN A 683  
AA6 1 2 N LEU A 590 ? N LEU A 739  O ASN A 599 ? O ASN A 748  
AA7 1 2 N TYR A 857 ? N TYR A 1006 O LEU A 865 ? O LEU A 1014 
AA7 2 3 N ILE A 864 ? N ILE A 1013 O ALA A 872 ? O ALA A 1021 
AA7 3 4 N LEU A 873 ? N LEU A 1022 O ILE A 906 ? O ILE A 1055 
AA7 4 5 O SER A 907 ? O SER A 1056 N ILE A 901 ? N ILE A 1050 
AA7 5 6 O PHE A 895 ? O PHE A 1044 N CYS A 856 ? N CYS A 1005 
# 
_pdbx_entry_details.entry_id                   9MFQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 PRO A 305  ? ? -61.31  -179.43 
2  1 PHE A 306  ? ? 81.75   -37.57  
3  1 GLN A 375  ? ? -92.89  -69.65  
4  1 PRO A 390  ? ? -39.04  -39.32  
5  1 ARG A 435  ? ? -140.66 34.35   
6  1 LYS A 468  ? ? -111.50 -104.55 
7  1 GLU A 477  ? ? -170.73 124.98  
8  1 PHE A 556  ? ? -96.41  44.81   
9  1 GLN A 690  ? ? -96.26  59.81   
10 1 THR A 719  ? ? -141.34 -11.51  
11 1 CYS A 733  ? ? 70.06   30.42   
12 1 LEU A 777  ? ? -97.57  37.24   
13 1 ASP A 844  ? ? -105.08 -162.94 
14 1 THR A 983  ? ? -120.12 -55.47  
15 1 PRO A 1002 ? ? -93.37  35.46   
16 1 LYS A 1008 ? ? -104.77 -74.11  
17 1 LYS A 1010 ? ? 53.00   -120.05 
18 1 SER A 1033 ? ? 61.36   -140.61 
19 1 SER A 1033 ? ? 60.86   -140.31 
20 1 THR A 1052 ? ? -125.27 -111.51 
21 1 ALA A 1072 ? ? -96.85  40.98   
22 1 TRP A 1088 ? ? -145.50 -34.18  
23 1 GLN A 1118 ? ? -153.85 84.47   
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1414 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.49 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 150  ? A MET 1    
2   1 Y 1 A SER 151  ? A SER 2    
3   1 Y 1 A ARG 152  ? A ARG 3    
4   1 Y 1 A LYS 153  ? A LYS 4    
5   1 Y 1 A GLU 154  ? A GLU 5    
6   1 Y 1 A GLU 155  ? A GLU 6    
7   1 Y 1 A GLN 156  ? A GLN 7    
8   1 Y 1 A GLU 157  ? A GLU 8    
9   1 Y 1 A VAL 158  ? A VAL 9    
10  1 Y 1 A GLN 159  ? A GLN 10   
11  1 Y 1 A ALA 160  ? A ALA 11   
12  1 Y 1 A THR 161  ? A THR 12   
13  1 Y 1 A LEU 162  ? A LEU 13   
14  1 Y 1 A GLU 163  ? A GLU 14   
15  1 Y 1 A SER 164  ? A SER 15   
16  1 Y 1 A GLU 165  ? A GLU 16   
17  1 Y 1 A GLU 166  ? A GLU 17   
18  1 Y 1 A VAL 167  ? A VAL 18   
19  1 Y 1 A ASP 168  ? A ASP 19   
20  1 Y 1 A LEU 169  ? A LEU 20   
21  1 Y 1 A ASN 170  ? A ASN 21   
22  1 Y 1 A ALA 171  ? A ALA 22   
23  1 Y 1 A GLY 172  ? A GLY 23   
24  1 Y 1 A LEU 173  ? A LEU 24   
25  1 Y 1 A HIS 174  ? A HIS 25   
26  1 Y 1 A GLY 175  ? A GLY 26   
27  1 Y 1 A ASN 176  ? A ASN 27   
28  1 Y 1 A TRP 177  ? A TRP 28   
29  1 Y 1 A THR 178  ? A THR 29   
30  1 Y 1 A LEU 179  ? A LEU 30   
31  1 Y 1 A GLU 180  ? A GLU 31   
32  1 Y 1 A ASN 181  ? A ASN 32   
33  1 Y 1 A ALA 182  ? A ALA 33   
34  1 Y 1 A LYS 183  ? A LYS 34   
35  1 Y 1 A ALA 184  ? A ALA 35   
36  1 Y 1 A ARG 185  ? A ARG 36   
37  1 Y 1 A LEU 186  ? A LEU 37   
38  1 Y 1 A ASN 187  ? A ASN 38   
39  1 Y 1 A GLN 188  ? A GLN 39   
40  1 Y 1 A TYR 189  ? A TYR 40   
41  1 Y 1 A PHE 190  ? A PHE 41   
42  1 Y 1 A GLN 191  ? A GLN 42   
43  1 Y 1 A LYS 192  ? A LYS 43   
44  1 Y 1 A GLU 193  ? A GLU 44   
45  1 Y 1 A LYS 194  ? A LYS 45   
46  1 Y 1 A ILE 195  ? A ILE 46   
47  1 Y 1 A GLN 196  ? A GLN 47   
48  1 Y 1 A GLY 197  ? A GLY 48   
49  1 Y 1 A GLU 198  ? A GLU 49   
50  1 Y 1 A TYR 199  ? A TYR 50   
51  1 Y 1 A LYS 200  ? A LYS 51   
52  1 Y 1 A TYR 201  ? A TYR 52   
53  1 Y 1 A THR 202  ? A THR 53   
54  1 Y 1 A GLN 203  ? A GLN 54   
55  1 Y 1 A VAL 204  ? A VAL 55   
56  1 Y 1 A GLY 205  ? A GLY 56   
57  1 Y 1 A PRO 206  ? A PRO 57   
58  1 Y 1 A ASP 207  ? A ASP 58   
59  1 Y 1 A HIS 208  ? A HIS 59   
60  1 Y 1 A ASN 209  ? A ASN 60   
61  1 Y 1 A ARG 210  ? A ARG 61   
62  1 Y 1 A SER 211  ? A SER 62   
63  1 Y 1 A PHE 212  ? A PHE 63   
64  1 Y 1 A ILE 213  ? A ILE 64   
65  1 Y 1 A ALA 214  ? A ALA 65   
66  1 Y 1 A GLU 215  ? A GLU 66   
67  1 Y 1 A MET 216  ? A MET 67   
68  1 Y 1 A THR 217  ? A THR 68   
69  1 Y 1 A ILE 218  ? A ILE 69   
70  1 Y 1 A TYR 219  ? A TYR 70   
71  1 Y 1 A ILE 220  ? A ILE 71   
72  1 Y 1 A LYS 221  ? A LYS 72   
73  1 Y 1 A GLN 222  ? A GLN 73   
74  1 Y 1 A LEU 223  ? A LEU 74   
75  1 Y 1 A GLY 224  ? A GLY 75   
76  1 Y 1 A ARG 225  ? A ARG 76   
77  1 Y 1 A ARG 226  ? A ARG 77   
78  1 Y 1 A ILE 227  ? A ILE 78   
79  1 Y 1 A PHE 228  ? A PHE 79   
80  1 Y 1 A ALA 229  ? A ALA 80   
81  1 Y 1 A ARG 230  ? A ARG 81   
82  1 Y 1 A GLU 231  ? A GLU 82   
83  1 Y 1 A HIS 232  ? A HIS 83   
84  1 Y 1 A GLY 233  ? A GLY 84   
85  1 Y 1 A SER 234  ? A SER 85   
86  1 Y 1 A ASN 235  ? A ASN 86   
87  1 Y 1 A LYS 236  ? A LYS 87   
88  1 Y 1 A LYS 237  ? A LYS 88   
89  1 Y 1 A LEU 238  ? A LEU 89   
90  1 Y 1 A ALA 239  ? A ALA 90   
91  1 Y 1 A ALA 240  ? A ALA 91   
92  1 Y 1 A GLN 241  ? A GLN 92   
93  1 Y 1 A SER 242  ? A SER 93   
94  1 Y 1 A CYS 243  ? A CYS 94   
95  1 Y 1 A ALA 244  ? A ALA 95   
96  1 Y 1 A LEU 245  ? A LEU 96   
97  1 Y 1 A SER 246  ? A SER 97   
98  1 Y 1 A LEU 247  ? A LEU 98   
99  1 Y 1 A VAL 248  ? A VAL 99   
100 1 Y 1 A ARG 249  ? A ARG 100  
101 1 Y 1 A GLN 250  ? A GLN 101  
102 1 Y 1 A LEU 251  ? A LEU 102  
103 1 Y 1 A TYR 252  ? A TYR 103  
104 1 Y 1 A HIS 253  ? A HIS 104  
105 1 Y 1 A LEU 254  ? A LEU 105  
106 1 Y 1 A GLY 255  ? A GLY 106  
107 1 Y 1 A VAL 256  ? A VAL 107  
108 1 Y 1 A ILE 257  ? A ILE 108  
109 1 Y 1 A GLU 258  ? A GLU 109  
110 1 Y 1 A ALA 259  ? A ALA 110  
111 1 Y 1 A TYR 260  ? A TYR 111  
112 1 Y 1 A SER 261  ? A SER 112  
113 1 Y 1 A GLY 262  ? A GLY 113  
114 1 Y 1 A LEU 263  ? A LEU 114  
115 1 Y 1 A THR 264  ? A THR 115  
116 1 Y 1 A LYS 265  ? A LYS 116  
117 1 Y 1 A LYS 266  ? A LYS 117  
118 1 Y 1 A LYS 267  ? A LYS 118  
119 1 Y 1 A GLU 268  ? A GLU 119  
120 1 Y 1 A GLY 269  ? A GLY 120  
121 1 Y 1 A GLU 270  ? A GLU 121  
122 1 Y 1 A LEU 316  ? A LEU 167  
123 1 Y 1 A ALA 317  ? A ALA 168  
124 1 Y 1 A HIS 318  ? A HIS 169  
125 1 Y 1 A PHE 319  ? A PHE 170  
126 1 Y 1 A GLU 320  ? A GLU 171  
127 1 Y 1 A ASN 326  ? A ASN 177  
128 1 Y 1 A GLN 327  ? A GLN 178  
129 1 Y 1 A LYS 590  ? A LYS 441  
130 1 Y 1 A ASP 591  ? A ASP 442  
131 1 Y 1 A LYS 592  ? A LYS 443  
132 1 Y 1 A LYS 593  ? A LYS 444  
133 1 Y 1 A LYS 594  ? A LYS 445  
134 1 Y 1 A LYS 595  ? A LYS 446  
135 1 Y 1 A GLU 596  ? A GLU 447  
136 1 Y 1 A LYS 597  ? A LYS 448  
137 1 Y 1 A ASP 598  ? A ASP 449  
138 1 Y 1 A ASP 599  ? A ASP 450  
139 1 Y 1 A ASP 600  ? A ASP 451  
140 1 Y 1 A GLY 601  ? A GLY 452  
141 1 Y 1 A PHE 602  ? A PHE 453  
142 1 Y 1 A GLU 603  ? A GLU 454  
143 1 Y 1 A ASP 604  ? A ASP 455  
144 1 Y 1 A ASP 605  ? A ASP 456  
145 1 Y 1 A ASP 606  ? A ASP 457  
146 1 Y 1 A ASP 1152 ? A ASP 1003 
147 1 Y 1 A TYR 1153 ? A TYR 1004 
148 1 Y 1 A LYS 1154 ? A LYS 1005 
149 1 Y 1 A ASP 1155 ? A ASP 1006 
150 1 Y 1 A ASP 1156 ? A ASP 1007 
151 1 Y 1 A ASP 1157 ? A ASP 1008 
152 1 Y 1 A ASP 1158 ? A ASP 1009 
153 1 Y 1 A LYS 1159 ? A LYS 1010 
# 
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 
A1BKZ C6     C  Y N 1   
A1BKZ C7     C  Y N 2   
A1BKZ C8     C  Y N 3   
A1BKZ C10    C  Y N 4   
A1BKZ C15    C  Y N 5   
A1BKZ C17    C  Y N 6   
A1BKZ C20    C  Y N 7   
A1BKZ C21    C  Y N 8   
A1BKZ C22    C  Y N 9   
A1BKZ C24    C  Y N 10  
A1BKZ C1     C  N N 11  
A1BKZ S2     S  N N 12  
A1BKZ O3     O  N N 13  
A1BKZ O4     O  N N 14  
A1BKZ N5     N  N N 15  
A1BKZ C9     C  Y N 16  
A1BKZ N11    N  N N 17  
A1BKZ C12    C  N N 18  
A1BKZ O13    O  N N 19  
A1BKZ C14    C  Y N 20  
A1BKZ C16    C  Y N 21  
A1BKZ S18    S  Y N 22  
A1BKZ C19    C  Y N 23  
A1BKZ C23    C  Y N 24  
A1BKZ C25    C  Y N 25  
A1BKZ H1     H  N N 26  
A1BKZ H2     H  N N 27  
A1BKZ H3     H  N N 28  
A1BKZ H4     H  N N 29  
A1BKZ H5     H  N N 30  
A1BKZ H6     H  N N 31  
A1BKZ H7     H  N N 32  
A1BKZ H8     H  N N 33  
A1BKZ H9     H  N N 34  
A1BKZ H10    H  N N 35  
A1BKZ H11    H  N N 36  
A1BKZ H12    H  N N 37  
A1BKZ H13    H  N N 38  
A1BKZ H14    H  N N 39  
A1BKZ H15    H  N N 40  
A1BKZ H16    H  N N 41  
ADP   PB     P  N N 42  
ADP   O1B    O  N N 43  
ADP   O2B    O  N N 44  
ADP   O3B    O  N N 45  
ADP   PA     P  N S 46  
ADP   O1A    O  N N 47  
ADP   O2A    O  N N 48  
ADP   O3A    O  N N 49  
ADP   "O5'"  O  N N 50  
ADP   "C5'"  C  N N 51  
ADP   "C4'"  C  N R 52  
ADP   "O4'"  O  N N 53  
ADP   "C3'"  C  N S 54  
ADP   "O3'"  O  N N 55  
ADP   "C2'"  C  N R 56  
ADP   "O2'"  O  N N 57  
ADP   "C1'"  C  N R 58  
ADP   N9     N  Y N 59  
ADP   C8     C  Y N 60  
ADP   N7     N  Y N 61  
ADP   C5     C  Y N 62  
ADP   C6     C  Y N 63  
ADP   N6     N  N N 64  
ADP   N1     N  Y N 65  
ADP   C2     C  Y N 66  
ADP   N3     N  Y N 67  
ADP   C4     C  Y N 68  
ADP   HOB2   H  N N 69  
ADP   HOB3   H  N N 70  
ADP   HOA2   H  N N 71  
ADP   "H5'1" H  N N 72  
ADP   "H5'2" H  N N 73  
ADP   "H4'"  H  N N 74  
ADP   "H3'"  H  N N 75  
ADP   "HO3'" H  N N 76  
ADP   "H2'"  H  N N 77  
ADP   "HO2'" H  N N 78  
ADP   "H1'"  H  N N 79  
ADP   H8     H  N N 80  
ADP   HN61   H  N N 81  
ADP   HN62   H  N N 82  
ADP   H2     H  N N 83  
ALA   N      N  N N 84  
ALA   CA     C  N S 85  
ALA   C      C  N N 86  
ALA   O      O  N N 87  
ALA   CB     C  N N 88  
ALA   OXT    O  N N 89  
ALA   H      H  N N 90  
ALA   H2     H  N N 91  
ALA   HA     H  N N 92  
ALA   HB1    H  N N 93  
ALA   HB2    H  N N 94  
ALA   HB3    H  N N 95  
ALA   HXT    H  N N 96  
ARG   N      N  N N 97  
ARG   CA     C  N S 98  
ARG   C      C  N N 99  
ARG   O      O  N N 100 
ARG   CB     C  N N 101 
ARG   CG     C  N N 102 
ARG   CD     C  N N 103 
ARG   NE     N  N N 104 
ARG   CZ     C  N N 105 
ARG   NH1    N  N N 106 
ARG   NH2    N  N N 107 
ARG   OXT    O  N N 108 
ARG   H      H  N N 109 
ARG   H2     H  N N 110 
ARG   HA     H  N N 111 
ARG   HB2    H  N N 112 
ARG   HB3    H  N N 113 
ARG   HG2    H  N N 114 
ARG   HG3    H  N N 115 
ARG   HD2    H  N N 116 
ARG   HD3    H  N N 117 
ARG   HE     H  N N 118 
ARG   HH11   H  N N 119 
ARG   HH12   H  N N 120 
ARG   HH21   H  N N 121 
ARG   HH22   H  N N 122 
ARG   HXT    H  N N 123 
ASN   N      N  N N 124 
ASN   CA     C  N S 125 
ASN   C      C  N N 126 
ASN   O      O  N N 127 
ASN   CB     C  N N 128 
ASN   CG     C  N N 129 
ASN   OD1    O  N N 130 
ASN   ND2    N  N N 131 
ASN   OXT    O  N N 132 
ASN   H      H  N N 133 
ASN   H2     H  N N 134 
ASN   HA     H  N N 135 
ASN   HB2    H  N N 136 
ASN   HB3    H  N N 137 
ASN   HD21   H  N N 138 
ASN   HD22   H  N N 139 
ASN   HXT    H  N N 140 
ASP   N      N  N N 141 
ASP   CA     C  N S 142 
ASP   C      C  N N 143 
ASP   O      O  N N 144 
ASP   CB     C  N N 145 
ASP   CG     C  N N 146 
ASP   OD1    O  N N 147 
ASP   OD2    O  N N 148 
ASP   OXT    O  N N 149 
ASP   H      H  N N 150 
ASP   H2     H  N N 151 
ASP   HA     H  N N 152 
ASP   HB2    H  N N 153 
ASP   HB3    H  N N 154 
ASP   HD2    H  N N 155 
ASP   HXT    H  N N 156 
CYS   N      N  N N 157 
CYS   CA     C  N R 158 
CYS   C      C  N N 159 
CYS   O      O  N N 160 
CYS   CB     C  N N 161 
CYS   SG     S  N N 162 
CYS   OXT    O  N N 163 
CYS   H      H  N N 164 
CYS   H2     H  N N 165 
CYS   HA     H  N N 166 
CYS   HB2    H  N N 167 
CYS   HB3    H  N N 168 
CYS   HG     H  N N 169 
CYS   HXT    H  N N 170 
EDO   C1     C  N N 171 
EDO   O1     O  N N 172 
EDO   C2     C  N N 173 
EDO   O2     O  N N 174 
EDO   H11    H  N N 175 
EDO   H12    H  N N 176 
EDO   HO1    H  N N 177 
EDO   H21    H  N N 178 
EDO   H22    H  N N 179 
EDO   HO2    H  N N 180 
GLN   N      N  N N 181 
GLN   CA     C  N S 182 
GLN   C      C  N N 183 
GLN   O      O  N N 184 
GLN   CB     C  N N 185 
GLN   CG     C  N N 186 
GLN   CD     C  N N 187 
GLN   OE1    O  N N 188 
GLN   NE2    N  N N 189 
GLN   OXT    O  N N 190 
GLN   H      H  N N 191 
GLN   H2     H  N N 192 
GLN   HA     H  N N 193 
GLN   HB2    H  N N 194 
GLN   HB3    H  N N 195 
GLN   HG2    H  N N 196 
GLN   HG3    H  N N 197 
GLN   HE21   H  N N 198 
GLN   HE22   H  N N 199 
GLN   HXT    H  N N 200 
GLU   N      N  N N 201 
GLU   CA     C  N S 202 
GLU   C      C  N N 203 
GLU   O      O  N N 204 
GLU   CB     C  N N 205 
GLU   CG     C  N N 206 
GLU   CD     C  N N 207 
GLU   OE1    O  N N 208 
GLU   OE2    O  N N 209 
GLU   OXT    O  N N 210 
GLU   H      H  N N 211 
GLU   H2     H  N N 212 
GLU   HA     H  N N 213 
GLU   HB2    H  N N 214 
GLU   HB3    H  N N 215 
GLU   HG2    H  N N 216 
GLU   HG3    H  N N 217 
GLU   HE2    H  N N 218 
GLU   HXT    H  N N 219 
GLY   N      N  N N 220 
GLY   CA     C  N N 221 
GLY   C      C  N N 222 
GLY   O      O  N N 223 
GLY   OXT    O  N N 224 
GLY   H      H  N N 225 
GLY   H2     H  N N 226 
GLY   HA2    H  N N 227 
GLY   HA3    H  N N 228 
GLY   HXT    H  N N 229 
HIS   N      N  N N 230 
HIS   CA     C  N S 231 
HIS   C      C  N N 232 
HIS   O      O  N N 233 
HIS   CB     C  N N 234 
HIS   CG     C  Y N 235 
HIS   ND1    N  Y N 236 
HIS   CD2    C  Y N 237 
HIS   CE1    C  Y N 238 
HIS   NE2    N  Y N 239 
HIS   OXT    O  N N 240 
HIS   H      H  N N 241 
HIS   H2     H  N N 242 
HIS   HA     H  N N 243 
HIS   HB2    H  N N 244 
HIS   HB3    H  N N 245 
HIS   HD1    H  N N 246 
HIS   HD2    H  N N 247 
HIS   HE1    H  N N 248 
HIS   HE2    H  N N 249 
HIS   HXT    H  N N 250 
HOH   O      O  N N 251 
HOH   H1     H  N N 252 
HOH   H2     H  N N 253 
ILE   N      N  N N 254 
ILE   CA     C  N S 255 
ILE   C      C  N N 256 
ILE   O      O  N N 257 
ILE   CB     C  N S 258 
ILE   CG1    C  N N 259 
ILE   CG2    C  N N 260 
ILE   CD1    C  N N 261 
ILE   OXT    O  N N 262 
ILE   H      H  N N 263 
ILE   H2     H  N N 264 
ILE   HA     H  N N 265 
ILE   HB     H  N N 266 
ILE   HG12   H  N N 267 
ILE   HG13   H  N N 268 
ILE   HG21   H  N N 269 
ILE   HG22   H  N N 270 
ILE   HG23   H  N N 271 
ILE   HD11   H  N N 272 
ILE   HD12   H  N N 273 
ILE   HD13   H  N N 274 
ILE   HXT    H  N N 275 
LEU   N      N  N N 276 
LEU   CA     C  N S 277 
LEU   C      C  N N 278 
LEU   O      O  N N 279 
LEU   CB     C  N N 280 
LEU   CG     C  N N 281 
LEU   CD1    C  N N 282 
LEU   CD2    C  N N 283 
LEU   OXT    O  N N 284 
LEU   H      H  N N 285 
LEU   H2     H  N N 286 
LEU   HA     H  N N 287 
LEU   HB2    H  N N 288 
LEU   HB3    H  N N 289 
LEU   HG     H  N N 290 
LEU   HD11   H  N N 291 
LEU   HD12   H  N N 292 
LEU   HD13   H  N N 293 
LEU   HD21   H  N N 294 
LEU   HD22   H  N N 295 
LEU   HD23   H  N N 296 
LEU   HXT    H  N N 297 
LYS   N      N  N N 298 
LYS   CA     C  N S 299 
LYS   C      C  N N 300 
LYS   O      O  N N 301 
LYS   CB     C  N N 302 
LYS   CG     C  N N 303 
LYS   CD     C  N N 304 
LYS   CE     C  N N 305 
LYS   NZ     N  N N 306 
LYS   OXT    O  N N 307 
LYS   H      H  N N 308 
LYS   H2     H  N N 309 
LYS   HA     H  N N 310 
LYS   HB2    H  N N 311 
LYS   HB3    H  N N 312 
LYS   HG2    H  N N 313 
LYS   HG3    H  N N 314 
LYS   HD2    H  N N 315 
LYS   HD3    H  N N 316 
LYS   HE2    H  N N 317 
LYS   HE3    H  N N 318 
LYS   HZ1    H  N N 319 
LYS   HZ2    H  N N 320 
LYS   HZ3    H  N N 321 
LYS   HXT    H  N N 322 
MET   N      N  N N 323 
MET   CA     C  N S 324 
MET   C      C  N N 325 
MET   O      O  N N 326 
MET   CB     C  N N 327 
MET   CG     C  N N 328 
MET   SD     S  N N 329 
MET   CE     C  N N 330 
MET   OXT    O  N N 331 
MET   H      H  N N 332 
MET   H2     H  N N 333 
MET   HA     H  N N 334 
MET   HB2    H  N N 335 
MET   HB3    H  N N 336 
MET   HG2    H  N N 337 
MET   HG3    H  N N 338 
MET   HE1    H  N N 339 
MET   HE2    H  N N 340 
MET   HE3    H  N N 341 
MET   HXT    H  N N 342 
MG    MG     MG N N 343 
PHE   N      N  N N 344 
PHE   CA     C  N S 345 
PHE   C      C  N N 346 
PHE   O      O  N N 347 
PHE   CB     C  N N 348 
PHE   CG     C  Y N 349 
PHE   CD1    C  Y N 350 
PHE   CD2    C  Y N 351 
PHE   CE1    C  Y N 352 
PHE   CE2    C  Y N 353 
PHE   CZ     C  Y N 354 
PHE   OXT    O  N N 355 
PHE   H      H  N N 356 
PHE   H2     H  N N 357 
PHE   HA     H  N N 358 
PHE   HB2    H  N N 359 
PHE   HB3    H  N N 360 
PHE   HD1    H  N N 361 
PHE   HD2    H  N N 362 
PHE   HE1    H  N N 363 
PHE   HE2    H  N N 364 
PHE   HZ     H  N N 365 
PHE   HXT    H  N N 366 
PRO   N      N  N N 367 
PRO   CA     C  N S 368 
PRO   C      C  N N 369 
PRO   O      O  N N 370 
PRO   CB     C  N N 371 
PRO   CG     C  N N 372 
PRO   CD     C  N N 373 
PRO   OXT    O  N N 374 
PRO   H      H  N N 375 
PRO   HA     H  N N 376 
PRO   HB2    H  N N 377 
PRO   HB3    H  N N 378 
PRO   HG2    H  N N 379 
PRO   HG3    H  N N 380 
PRO   HD2    H  N N 381 
PRO   HD3    H  N N 382 
PRO   HXT    H  N N 383 
SER   N      N  N N 384 
SER   CA     C  N S 385 
SER   C      C  N N 386 
SER   O      O  N N 387 
SER   CB     C  N N 388 
SER   OG     O  N N 389 
SER   OXT    O  N N 390 
SER   H      H  N N 391 
SER   H2     H  N N 392 
SER   HA     H  N N 393 
SER   HB2    H  N N 394 
SER   HB3    H  N N 395 
SER   HG     H  N N 396 
SER   HXT    H  N N 397 
SO4   S      S  N N 398 
SO4   O1     O  N N 399 
SO4   O2     O  N N 400 
SO4   O3     O  N N 401 
SO4   O4     O  N N 402 
THR   N      N  N N 403 
THR   CA     C  N S 404 
THR   C      C  N N 405 
THR   O      O  N N 406 
THR   CB     C  N R 407 
THR   OG1    O  N N 408 
THR   CG2    C  N N 409 
THR   OXT    O  N N 410 
THR   H      H  N N 411 
THR   H2     H  N N 412 
THR   HA     H  N N 413 
THR   HB     H  N N 414 
THR   HG1    H  N N 415 
THR   HG21   H  N N 416 
THR   HG22   H  N N 417 
THR   HG23   H  N N 418 
THR   HXT    H  N N 419 
TRP   N      N  N N 420 
TRP   CA     C  N S 421 
TRP   C      C  N N 422 
TRP   O      O  N N 423 
TRP   CB     C  N N 424 
TRP   CG     C  Y N 425 
TRP   CD1    C  Y N 426 
TRP   CD2    C  Y N 427 
TRP   NE1    N  Y N 428 
TRP   CE2    C  Y N 429 
TRP   CE3    C  Y N 430 
TRP   CZ2    C  Y N 431 
TRP   CZ3    C  Y N 432 
TRP   CH2    C  Y N 433 
TRP   OXT    O  N N 434 
TRP   H      H  N N 435 
TRP   H2     H  N N 436 
TRP   HA     H  N N 437 
TRP   HB2    H  N N 438 
TRP   HB3    H  N N 439 
TRP   HD1    H  N N 440 
TRP   HE1    H  N N 441 
TRP   HE3    H  N N 442 
TRP   HZ2    H  N N 443 
TRP   HZ3    H  N N 444 
TRP   HH2    H  N N 445 
TRP   HXT    H  N N 446 
TYR   N      N  N N 447 
TYR   CA     C  N S 448 
TYR   C      C  N N 449 
TYR   O      O  N N 450 
TYR   CB     C  N N 451 
TYR   CG     C  Y N 452 
TYR   CD1    C  Y N 453 
TYR   CD2    C  Y N 454 
TYR   CE1    C  Y N 455 
TYR   CE2    C  Y N 456 
TYR   CZ     C  Y N 457 
TYR   OH     O  N N 458 
TYR   OXT    O  N N 459 
TYR   H      H  N N 460 
TYR   H2     H  N N 461 
TYR   HA     H  N N 462 
TYR   HB2    H  N N 463 
TYR   HB3    H  N N 464 
TYR   HD1    H  N N 465 
TYR   HD2    H  N N 466 
TYR   HE1    H  N N 467 
TYR   HE2    H  N N 468 
TYR   HH     H  N N 469 
TYR   HXT    H  N N 470 
VAL   N      N  N N 471 
VAL   CA     C  N S 472 
VAL   C      C  N N 473 
VAL   O      O  N N 474 
VAL   CB     C  N N 475 
VAL   CG1    C  N N 476 
VAL   CG2    C  N N 477 
VAL   OXT    O  N N 478 
VAL   H      H  N N 479 
VAL   H2     H  N N 480 
VAL   HA     H  N N 481 
VAL   HB     H  N N 482 
VAL   HG11   H  N N 483 
VAL   HG12   H  N N 484 
VAL   HG13   H  N N 485 
VAL   HG21   H  N N 486 
VAL   HG22   H  N N 487 
VAL   HG23   H  N N 488 
VAL   HXT    H  N N 489 
# 
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 
A1BKZ O4    S2     doub N N 1   
A1BKZ O3    S2     doub N N 2   
A1BKZ S2    C1     sing N N 3   
A1BKZ S2    N5     sing N N 4   
A1BKZ N5    C6     sing N N 5   
A1BKZ C7    C6     doub Y N 6   
A1BKZ C7    C8     sing Y N 7   
A1BKZ C6    C25    sing Y N 8   
A1BKZ C8    C9     doub Y N 9   
A1BKZ C25   C10    doub Y N 10  
A1BKZ C9    C10    sing Y N 11  
A1BKZ C10   N11    sing N N 12  
A1BKZ N11   C12    sing N N 13  
A1BKZ O13   C12    doub N N 14  
A1BKZ C12   C14    sing N N 15  
A1BKZ C14   C15    doub Y N 16  
A1BKZ C14   S18    sing Y N 17  
A1BKZ C15   C16    sing Y N 18  
A1BKZ S18   C17    sing Y N 19  
A1BKZ C24   C23    doub Y N 20  
A1BKZ C24   C19    sing Y N 21  
A1BKZ C16   C19    sing N N 22  
A1BKZ C16   C17    doub Y N 23  
A1BKZ C23   C22    sing Y N 24  
A1BKZ C19   C20    doub Y N 25  
A1BKZ C22   C21    doub Y N 26  
A1BKZ C20   C21    sing Y N 27  
A1BKZ C7    H1     sing N N 28  
A1BKZ C8    H2     sing N N 29  
A1BKZ C15   H3     sing N N 30  
A1BKZ C17   H4     sing N N 31  
A1BKZ C20   H5     sing N N 32  
A1BKZ C21   H6     sing N N 33  
A1BKZ C22   H7     sing N N 34  
A1BKZ C24   H8     sing N N 35  
A1BKZ C1    H9     sing N N 36  
A1BKZ C1    H10    sing N N 37  
A1BKZ C1    H11    sing N N 38  
A1BKZ N5    H12    sing N N 39  
A1BKZ C9    H13    sing N N 40  
A1BKZ N11   H14    sing N N 41  
A1BKZ C23   H15    sing N N 42  
A1BKZ C25   H16    sing N N 43  
ADP   PB    O1B    doub N N 44  
ADP   PB    O2B    sing N N 45  
ADP   PB    O3B    sing N N 46  
ADP   PB    O3A    sing N N 47  
ADP   O2B   HOB2   sing N N 48  
ADP   O3B   HOB3   sing N N 49  
ADP   PA    O1A    doub N N 50  
ADP   PA    O2A    sing N N 51  
ADP   PA    O3A    sing N N 52  
ADP   PA    "O5'"  sing N N 53  
ADP   O2A   HOA2   sing N N 54  
ADP   "O5'" "C5'"  sing N N 55  
ADP   "C5'" "C4'"  sing N N 56  
ADP   "C5'" "H5'1" sing N N 57  
ADP   "C5'" "H5'2" sing N N 58  
ADP   "C4'" "O4'"  sing N N 59  
ADP   "C4'" "C3'"  sing N N 60  
ADP   "C4'" "H4'"  sing N N 61  
ADP   "O4'" "C1'"  sing N N 62  
ADP   "C3'" "O3'"  sing N N 63  
ADP   "C3'" "C2'"  sing N N 64  
ADP   "C3'" "H3'"  sing N N 65  
ADP   "O3'" "HO3'" sing N N 66  
ADP   "C2'" "O2'"  sing N N 67  
ADP   "C2'" "C1'"  sing N N 68  
ADP   "C2'" "H2'"  sing N N 69  
ADP   "O2'" "HO2'" sing N N 70  
ADP   "C1'" N9     sing N N 71  
ADP   "C1'" "H1'"  sing N N 72  
ADP   N9    C8     sing Y N 73  
ADP   N9    C4     sing Y N 74  
ADP   C8    N7     doub Y N 75  
ADP   C8    H8     sing N N 76  
ADP   N7    C5     sing Y N 77  
ADP   C5    C6     sing Y N 78  
ADP   C5    C4     doub Y N 79  
ADP   C6    N6     sing N N 80  
ADP   C6    N1     doub Y N 81  
ADP   N6    HN61   sing N N 82  
ADP   N6    HN62   sing N N 83  
ADP   N1    C2     sing Y N 84  
ADP   C2    N3     doub Y N 85  
ADP   C2    H2     sing N N 86  
ADP   N3    C4     sing Y N 87  
ALA   N     CA     sing N N 88  
ALA   N     H      sing N N 89  
ALA   N     H2     sing N N 90  
ALA   CA    C      sing N N 91  
ALA   CA    CB     sing N N 92  
ALA   CA    HA     sing N N 93  
ALA   C     O      doub N N 94  
ALA   C     OXT    sing N N 95  
ALA   CB    HB1    sing N N 96  
ALA   CB    HB2    sing N N 97  
ALA   CB    HB3    sing N N 98  
ALA   OXT   HXT    sing N N 99  
ARG   N     CA     sing N N 100 
ARG   N     H      sing N N 101 
ARG   N     H2     sing N N 102 
ARG   CA    C      sing N N 103 
ARG   CA    CB     sing N N 104 
ARG   CA    HA     sing N N 105 
ARG   C     O      doub N N 106 
ARG   C     OXT    sing N N 107 
ARG   CB    CG     sing N N 108 
ARG   CB    HB2    sing N N 109 
ARG   CB    HB3    sing N N 110 
ARG   CG    CD     sing N N 111 
ARG   CG    HG2    sing N N 112 
ARG   CG    HG3    sing N N 113 
ARG   CD    NE     sing N N 114 
ARG   CD    HD2    sing N N 115 
ARG   CD    HD3    sing N N 116 
ARG   NE    CZ     sing N N 117 
ARG   NE    HE     sing N N 118 
ARG   CZ    NH1    sing N N 119 
ARG   CZ    NH2    doub N N 120 
ARG   NH1   HH11   sing N N 121 
ARG   NH1   HH12   sing N N 122 
ARG   NH2   HH21   sing N N 123 
ARG   NH2   HH22   sing N N 124 
ARG   OXT   HXT    sing N N 125 
ASN   N     CA     sing N N 126 
ASN   N     H      sing N N 127 
ASN   N     H2     sing N N 128 
ASN   CA    C      sing N N 129 
ASN   CA    CB     sing N N 130 
ASN   CA    HA     sing N N 131 
ASN   C     O      doub N N 132 
ASN   C     OXT    sing N N 133 
ASN   CB    CG     sing N N 134 
ASN   CB    HB2    sing N N 135 
ASN   CB    HB3    sing N N 136 
ASN   CG    OD1    doub N N 137 
ASN   CG    ND2    sing N N 138 
ASN   ND2   HD21   sing N N 139 
ASN   ND2   HD22   sing N N 140 
ASN   OXT   HXT    sing N N 141 
ASP   N     CA     sing N N 142 
ASP   N     H      sing N N 143 
ASP   N     H2     sing N N 144 
ASP   CA    C      sing N N 145 
ASP   CA    CB     sing N N 146 
ASP   CA    HA     sing N N 147 
ASP   C     O      doub N N 148 
ASP   C     OXT    sing N N 149 
ASP   CB    CG     sing N N 150 
ASP   CB    HB2    sing N N 151 
ASP   CB    HB3    sing N N 152 
ASP   CG    OD1    doub N N 153 
ASP   CG    OD2    sing N N 154 
ASP   OD2   HD2    sing N N 155 
ASP   OXT   HXT    sing N N 156 
CYS   N     CA     sing N N 157 
CYS   N     H      sing N N 158 
CYS   N     H2     sing N N 159 
CYS   CA    C      sing N N 160 
CYS   CA    CB     sing N N 161 
CYS   CA    HA     sing N N 162 
CYS   C     O      doub N N 163 
CYS   C     OXT    sing N N 164 
CYS   CB    SG     sing N N 165 
CYS   CB    HB2    sing N N 166 
CYS   CB    HB3    sing N N 167 
CYS   SG    HG     sing N N 168 
CYS   OXT   HXT    sing N N 169 
EDO   C1    O1     sing N N 170 
EDO   C1    C2     sing N N 171 
EDO   C1    H11    sing N N 172 
EDO   C1    H12    sing N N 173 
EDO   O1    HO1    sing N N 174 
EDO   C2    O2     sing N N 175 
EDO   C2    H21    sing N N 176 
EDO   C2    H22    sing N N 177 
EDO   O2    HO2    sing N N 178 
GLN   N     CA     sing N N 179 
GLN   N     H      sing N N 180 
GLN   N     H2     sing N N 181 
GLN   CA    C      sing N N 182 
GLN   CA    CB     sing N N 183 
GLN   CA    HA     sing N N 184 
GLN   C     O      doub N N 185 
GLN   C     OXT    sing N N 186 
GLN   CB    CG     sing N N 187 
GLN   CB    HB2    sing N N 188 
GLN   CB    HB3    sing N N 189 
GLN   CG    CD     sing N N 190 
GLN   CG    HG2    sing N N 191 
GLN   CG    HG3    sing N N 192 
GLN   CD    OE1    doub N N 193 
GLN   CD    NE2    sing N N 194 
GLN   NE2   HE21   sing N N 195 
GLN   NE2   HE22   sing N N 196 
GLN   OXT   HXT    sing N N 197 
GLU   N     CA     sing N N 198 
GLU   N     H      sing N N 199 
GLU   N     H2     sing N N 200 
GLU   CA    C      sing N N 201 
GLU   CA    CB     sing N N 202 
GLU   CA    HA     sing N N 203 
GLU   C     O      doub N N 204 
GLU   C     OXT    sing N N 205 
GLU   CB    CG     sing N N 206 
GLU   CB    HB2    sing N N 207 
GLU   CB    HB3    sing N N 208 
GLU   CG    CD     sing N N 209 
GLU   CG    HG2    sing N N 210 
GLU   CG    HG3    sing N N 211 
GLU   CD    OE1    doub N N 212 
GLU   CD    OE2    sing N N 213 
GLU   OE2   HE2    sing N N 214 
GLU   OXT   HXT    sing N N 215 
GLY   N     CA     sing N N 216 
GLY   N     H      sing N N 217 
GLY   N     H2     sing N N 218 
GLY   CA    C      sing N N 219 
GLY   CA    HA2    sing N N 220 
GLY   CA    HA3    sing N N 221 
GLY   C     O      doub N N 222 
GLY   C     OXT    sing N N 223 
GLY   OXT   HXT    sing N N 224 
HIS   N     CA     sing N N 225 
HIS   N     H      sing N N 226 
HIS   N     H2     sing N N 227 
HIS   CA    C      sing N N 228 
HIS   CA    CB     sing N N 229 
HIS   CA    HA     sing N N 230 
HIS   C     O      doub N N 231 
HIS   C     OXT    sing N N 232 
HIS   CB    CG     sing N N 233 
HIS   CB    HB2    sing N N 234 
HIS   CB    HB3    sing N N 235 
HIS   CG    ND1    sing Y N 236 
HIS   CG    CD2    doub Y N 237 
HIS   ND1   CE1    doub Y N 238 
HIS   ND1   HD1    sing N N 239 
HIS   CD2   NE2    sing Y N 240 
HIS   CD2   HD2    sing N N 241 
HIS   CE1   NE2    sing Y N 242 
HIS   CE1   HE1    sing N N 243 
HIS   NE2   HE2    sing N N 244 
HIS   OXT   HXT    sing N N 245 
HOH   O     H1     sing N N 246 
HOH   O     H2     sing N N 247 
ILE   N     CA     sing N N 248 
ILE   N     H      sing N N 249 
ILE   N     H2     sing N N 250 
ILE   CA    C      sing N N 251 
ILE   CA    CB     sing N N 252 
ILE   CA    HA     sing N N 253 
ILE   C     O      doub N N 254 
ILE   C     OXT    sing N N 255 
ILE   CB    CG1    sing N N 256 
ILE   CB    CG2    sing N N 257 
ILE   CB    HB     sing N N 258 
ILE   CG1   CD1    sing N N 259 
ILE   CG1   HG12   sing N N 260 
ILE   CG1   HG13   sing N N 261 
ILE   CG2   HG21   sing N N 262 
ILE   CG2   HG22   sing N N 263 
ILE   CG2   HG23   sing N N 264 
ILE   CD1   HD11   sing N N 265 
ILE   CD1   HD12   sing N N 266 
ILE   CD1   HD13   sing N N 267 
ILE   OXT   HXT    sing N N 268 
LEU   N     CA     sing N N 269 
LEU   N     H      sing N N 270 
LEU   N     H2     sing N N 271 
LEU   CA    C      sing N N 272 
LEU   CA    CB     sing N N 273 
LEU   CA    HA     sing N N 274 
LEU   C     O      doub N N 275 
LEU   C     OXT    sing N N 276 
LEU   CB    CG     sing N N 277 
LEU   CB    HB2    sing N N 278 
LEU   CB    HB3    sing N N 279 
LEU   CG    CD1    sing N N 280 
LEU   CG    CD2    sing N N 281 
LEU   CG    HG     sing N N 282 
LEU   CD1   HD11   sing N N 283 
LEU   CD1   HD12   sing N N 284 
LEU   CD1   HD13   sing N N 285 
LEU   CD2   HD21   sing N N 286 
LEU   CD2   HD22   sing N N 287 
LEU   CD2   HD23   sing N N 288 
LEU   OXT   HXT    sing N N 289 
LYS   N     CA     sing N N 290 
LYS   N     H      sing N N 291 
LYS   N     H2     sing N N 292 
LYS   CA    C      sing N N 293 
LYS   CA    CB     sing N N 294 
LYS   CA    HA     sing N N 295 
LYS   C     O      doub N N 296 
LYS   C     OXT    sing N N 297 
LYS   CB    CG     sing N N 298 
LYS   CB    HB2    sing N N 299 
LYS   CB    HB3    sing N N 300 
LYS   CG    CD     sing N N 301 
LYS   CG    HG2    sing N N 302 
LYS   CG    HG3    sing N N 303 
LYS   CD    CE     sing N N 304 
LYS   CD    HD2    sing N N 305 
LYS   CD    HD3    sing N N 306 
LYS   CE    NZ     sing N N 307 
LYS   CE    HE2    sing N N 308 
LYS   CE    HE3    sing N N 309 
LYS   NZ    HZ1    sing N N 310 
LYS   NZ    HZ2    sing N N 311 
LYS   NZ    HZ3    sing N N 312 
LYS   OXT   HXT    sing N N 313 
MET   N     CA     sing N N 314 
MET   N     H      sing N N 315 
MET   N     H2     sing N N 316 
MET   CA    C      sing N N 317 
MET   CA    CB     sing N N 318 
MET   CA    HA     sing N N 319 
MET   C     O      doub N N 320 
MET   C     OXT    sing N N 321 
MET   CB    CG     sing N N 322 
MET   CB    HB2    sing N N 323 
MET   CB    HB3    sing N N 324 
MET   CG    SD     sing N N 325 
MET   CG    HG2    sing N N 326 
MET   CG    HG3    sing N N 327 
MET   SD    CE     sing N N 328 
MET   CE    HE1    sing N N 329 
MET   CE    HE2    sing N N 330 
MET   CE    HE3    sing N N 331 
MET   OXT   HXT    sing N N 332 
PHE   N     CA     sing N N 333 
PHE   N     H      sing N N 334 
PHE   N     H2     sing N N 335 
PHE   CA    C      sing N N 336 
PHE   CA    CB     sing N N 337 
PHE   CA    HA     sing N N 338 
PHE   C     O      doub N N 339 
PHE   C     OXT    sing N N 340 
PHE   CB    CG     sing N N 341 
PHE   CB    HB2    sing N N 342 
PHE   CB    HB3    sing N N 343 
PHE   CG    CD1    doub Y N 344 
PHE   CG    CD2    sing Y N 345 
PHE   CD1   CE1    sing Y N 346 
PHE   CD1   HD1    sing N N 347 
PHE   CD2   CE2    doub Y N 348 
PHE   CD2   HD2    sing N N 349 
PHE   CE1   CZ     doub Y N 350 
PHE   CE1   HE1    sing N N 351 
PHE   CE2   CZ     sing Y N 352 
PHE   CE2   HE2    sing N N 353 
PHE   CZ    HZ     sing N N 354 
PHE   OXT   HXT    sing N N 355 
PRO   N     CA     sing N N 356 
PRO   N     CD     sing N N 357 
PRO   N     H      sing N N 358 
PRO   CA    C      sing N N 359 
PRO   CA    CB     sing N N 360 
PRO   CA    HA     sing N N 361 
PRO   C     O      doub N N 362 
PRO   C     OXT    sing N N 363 
PRO   CB    CG     sing N N 364 
PRO   CB    HB2    sing N N 365 
PRO   CB    HB3    sing N N 366 
PRO   CG    CD     sing N N 367 
PRO   CG    HG2    sing N N 368 
PRO   CG    HG3    sing N N 369 
PRO   CD    HD2    sing N N 370 
PRO   CD    HD3    sing N N 371 
PRO   OXT   HXT    sing N N 372 
SER   N     CA     sing N N 373 
SER   N     H      sing N N 374 
SER   N     H2     sing N N 375 
SER   CA    C      sing N N 376 
SER   CA    CB     sing N N 377 
SER   CA    HA     sing N N 378 
SER   C     O      doub N N 379 
SER   C     OXT    sing N N 380 
SER   CB    OG     sing N N 381 
SER   CB    HB2    sing N N 382 
SER   CB    HB3    sing N N 383 
SER   OG    HG     sing N N 384 
SER   OXT   HXT    sing N N 385 
SO4   S     O1     doub N N 386 
SO4   S     O2     doub N N 387 
SO4   S     O3     sing N N 388 
SO4   S     O4     sing N N 389 
THR   N     CA     sing N N 390 
THR   N     H      sing N N 391 
THR   N     H2     sing N N 392 
THR   CA    C      sing N N 393 
THR   CA    CB     sing N N 394 
THR   CA    HA     sing N N 395 
THR   C     O      doub N N 396 
THR   C     OXT    sing N N 397 
THR   CB    OG1    sing N N 398 
THR   CB    CG2    sing N N 399 
THR   CB    HB     sing N N 400 
THR   OG1   HG1    sing N N 401 
THR   CG2   HG21   sing N N 402 
THR   CG2   HG22   sing N N 403 
THR   CG2   HG23   sing N N 404 
THR   OXT   HXT    sing N N 405 
TRP   N     CA     sing N N 406 
TRP   N     H      sing N N 407 
TRP   N     H2     sing N N 408 
TRP   CA    C      sing N N 409 
TRP   CA    CB     sing N N 410 
TRP   CA    HA     sing N N 411 
TRP   C     O      doub N N 412 
TRP   C     OXT    sing N N 413 
TRP   CB    CG     sing N N 414 
TRP   CB    HB2    sing N N 415 
TRP   CB    HB3    sing N N 416 
TRP   CG    CD1    doub Y N 417 
TRP   CG    CD2    sing Y N 418 
TRP   CD1   NE1    sing Y N 419 
TRP   CD1   HD1    sing N N 420 
TRP   CD2   CE2    doub Y N 421 
TRP   CD2   CE3    sing Y N 422 
TRP   NE1   CE2    sing Y N 423 
TRP   NE1   HE1    sing N N 424 
TRP   CE2   CZ2    sing Y N 425 
TRP   CE3   CZ3    doub Y N 426 
TRP   CE3   HE3    sing N N 427 
TRP   CZ2   CH2    doub Y N 428 
TRP   CZ2   HZ2    sing N N 429 
TRP   CZ3   CH2    sing Y N 430 
TRP   CZ3   HZ3    sing N N 431 
TRP   CH2   HH2    sing N N 432 
TRP   OXT   HXT    sing N N 433 
TYR   N     CA     sing N N 434 
TYR   N     H      sing N N 435 
TYR   N     H2     sing N N 436 
TYR   CA    C      sing N N 437 
TYR   CA    CB     sing N N 438 
TYR   CA    HA     sing N N 439 
TYR   C     O      doub N N 440 
TYR   C     OXT    sing N N 441 
TYR   CB    CG     sing N N 442 
TYR   CB    HB2    sing N N 443 
TYR   CB    HB3    sing N N 444 
TYR   CG    CD1    doub Y N 445 
TYR   CG    CD2    sing Y N 446 
TYR   CD1   CE1    sing Y N 447 
TYR   CD1   HD1    sing N N 448 
TYR   CD2   CE2    doub Y N 449 
TYR   CD2   HD2    sing N N 450 
TYR   CE1   CZ     doub Y N 451 
TYR   CE1   HE1    sing N N 452 
TYR   CE2   CZ     sing Y N 453 
TYR   CE2   HE2    sing N N 454 
TYR   CZ    OH     sing N N 455 
TYR   OH    HH     sing N N 456 
TYR   OXT   HXT    sing N N 457 
VAL   N     CA     sing N N 458 
VAL   N     H      sing N N 459 
VAL   N     H2     sing N N 460 
VAL   CA    C      sing N N 461 
VAL   CA    CB     sing N N 462 
VAL   CA    HA     sing N N 463 
VAL   C     O      doub N N 464 
VAL   C     OXT    sing N N 465 
VAL   CB    CG1    sing N N 466 
VAL   CB    CG2    sing N N 467 
VAL   CB    HB     sing N N 468 
VAL   CG1   HG11   sing N N 469 
VAL   CG1   HG12   sing N N 470 
VAL   CG1   HG13   sing N N 471 
VAL   CG2   HG21   sing N N 472 
VAL   CG2   HG22   sing N N 473 
VAL   CG2   HG23   sing N N 474 
VAL   OXT   HXT    sing N N 475 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8SZQ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MFQ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011665 
_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]   0.011665 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.002870 
_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     . THR   A 1 122  ? -15.457 -31.610 -65.739 1.00 117.95 ? 271  THR   A N     1 
ATOM   2    C  CA    . THR   A 1 122  ? -16.180 -30.301 -65.798 1.00 117.25 ? 271  THR   A CA    1 
ATOM   3    C  C     . THR   A 1 122  ? -16.486 -29.830 -64.370 1.00 118.43 ? 271  THR   A C     1 
ATOM   4    O  O     . THR   A 1 122  ? -16.099 -30.541 -63.421 1.00 119.31 ? 271  THR   A O     1 
ATOM   5    C  CB    . THR   A 1 122  ? -17.461 -30.407 -66.638 1.00 115.92 ? 271  THR   A CB    1 
ATOM   6    O  OG1   . THR   A 1 122  ? -18.486 -30.998 -65.837 1.00 114.65 ? 271  THR   A OG1   1 
ATOM   7    C  CG2   . THR   A 1 122  ? -17.284 -31.219 -67.903 1.00 114.91 ? 271  THR   A CG2   1 
ATOM   8    N  N     . VAL   A 1 123  ? -17.151 -28.677 -64.233 1.00 119.72 ? 272  VAL   A N     1 
ATOM   9    C  CA    . VAL   A 1 123  ? -17.602 -28.100 -62.928 1.00 119.00 ? 272  VAL   A CA    1 
ATOM   10   C  C     . VAL   A 1 123  ? -18.994 -27.481 -63.113 1.00 116.60 ? 272  VAL   A C     1 
ATOM   11   O  O     . VAL   A 1 123  ? -19.205 -26.789 -64.128 1.00 114.74 ? 272  VAL   A O     1 
ATOM   12   C  CB    . VAL   A 1 123  ? -16.593 -27.072 -62.376 1.00 120.69 ? 272  VAL   A CB    1 
ATOM   13   C  CG1   . VAL   A 1 123  ? -15.354 -27.749 -61.809 1.00 121.04 ? 272  VAL   A CG1   1 
ATOM   14   C  CG2   . VAL   A 1 123  ? -16.206 -26.025 -63.412 1.00 120.75 ? 272  VAL   A CG2   1 
ATOM   15   N  N     . GLU   A 1 124  ? -19.900 -27.728 -62.160 1.00 116.02 ? 273  GLU   A N     1 
ATOM   16   C  CA    . GLU   A 1 124  ? -21.297 -27.209 -62.156 1.00 116.12 ? 273  GLU   A CA    1 
ATOM   17   C  C     . GLU   A 1 124  ? -21.275 -25.684 -62.086 1.00 111.22 ? 273  GLU   A C     1 
ATOM   18   O  O     . GLU   A 1 124  ? -20.331 -25.100 -61.557 1.00 113.22 ? 273  GLU   A O     1 
ATOM   19   C  CB    . GLU   A 1 124  ? -22.086 -27.790 -60.977 1.00 119.31 ? 273  GLU   A CB    1 
ATOM   20   C  CG    . GLU   A 1 124  ? -22.750 -29.122 -61.283 1.00 121.78 ? 273  GLU   A CG    1 
ATOM   21   C  CD    . GLU   A 1 124  ? -24.158 -29.009 -61.846 1.00 123.96 ? 273  GLU   A CD    1 
ATOM   22   O  OE1   . GLU   A 1 124  ? -25.088 -28.736 -61.059 1.00 122.53 ? 273  GLU   A OE1   1 
ATOM   23   O  OE2   . GLU   A 1 124  ? -24.320 -29.181 -63.071 1.00 127.30 ? 273  GLU   A OE2   1 
ATOM   24   N  N     . PRO   A 1 125  ? -22.313 -24.989 -62.607 1.00 104.94 ? 274  PRO   A N     1 
ATOM   25   C  CA    . PRO   A 1 125  ? -22.390 -23.533 -62.496 1.00 101.75 ? 274  PRO   A CA    1 
ATOM   26   C  C     . PRO   A 1 125  ? -22.575 -23.119 -61.029 1.00 98.60  ? 274  PRO   A C     1 
ATOM   27   O  O     . PRO   A 1 125  ? -23.488 -23.621 -60.398 1.00 98.67  ? 274  PRO   A O     1 
ATOM   28   C  CB    . PRO   A 1 125  ? -23.609 -23.162 -63.355 1.00 101.29 ? 274  PRO   A CB    1 
ATOM   29   C  CG    . PRO   A 1 125  ? -24.464 -24.411 -63.342 1.00 102.41 ? 274  PRO   A CG    1 
ATOM   30   C  CD    . PRO   A 1 125  ? -23.476 -25.559 -63.304 1.00 104.21 ? 274  PRO   A CD    1 
ATOM   31   N  N     . TYR   A 1 126  ? -21.698 -22.243 -60.528 1.00 94.23  ? 275  TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 126  ? -21.684 -21.748 -59.125 1.00 91.89  ? 275  TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 126  ? -22.893 -20.833 -58.901 1.00 91.22  ? 275  TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 126  ? -23.064 -19.874 -59.677 1.00 90.73  ? 275  TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 126  ? -20.370 -21.019 -58.829 1.00 88.60  ? 275  TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 126  ? -20.195 -20.581 -57.396 1.00 85.40  ? 275  TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 126  ? -19.647 -21.432 -56.450 1.00 82.99  ? 275  TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 126  ? -20.571 -19.311 -56.985 1.00 84.19  ? 275  TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 126  ? -19.481 -21.038 -55.132 1.00 81.33  ? 275  TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 126  ? -20.414 -18.901 -55.670 1.00 83.22  ? 275  TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 126  ? -19.866 -19.767 -54.741 1.00 82.27  ? 275  TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 126  ? -19.703 -19.371 -53.445 1.00 82.68  ? 275  TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 127  ? -23.703 -21.122 -57.876 1.00 92.21  ? 276  LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 127  ? -24.908 -20.324 -57.523 1.00 96.33  ? 276  LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 127  ? -24.475 -19.090 -56.724 1.00 94.85  ? 276  LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 127  ? -23.715 -19.251 -55.749 1.00 94.50  ? 276  LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 127  ? -25.921 -21.163 -56.737 1.00 100.97 ? 276  LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 127  ? -27.343 -20.616 -56.756 1.00 105.20 ? 276  LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 127  ? -28.246 -21.198 -55.692 1.00 107.99 ? 276  LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 127  ? -29.592 -20.508 -55.626 1.00 109.23 ? 276  LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 127  ? -30.366 -20.933 -54.435 1.00 110.38 ? 276  LYS   A NZ    1 
ATOM   52   N  N     . VAL   A 1 128  ? -24.949 -17.909 -57.133 1.00 93.92  ? 277  VAL   A N     1 
ATOM   53   C  CA    . VAL   A 1 128  ? -24.640 -16.593 -56.500 1.00 95.14  ? 277  VAL   A CA    1 
ATOM   54   C  C     . VAL   A 1 128  ? -25.900 -16.107 -55.773 1.00 95.93  ? 277  VAL   A C     1 
ATOM   55   O  O     . VAL   A 1 128  ? -26.803 -15.573 -56.446 1.00 95.19  ? 277  VAL   A O     1 
ATOM   56   C  CB    . VAL   A 1 128  ? -24.148 -15.574 -57.548 1.00 94.91  ? 277  VAL   A CB    1 
ATOM   57   C  CG1   . VAL   A 1 128  ? -23.658 -14.287 -56.900 1.00 94.81  ? 277  VAL   A CG1   1 
ATOM   58   C  CG2   . VAL   A 1 128  ? -23.071 -16.165 -58.447 1.00 93.91  ? 277  VAL   A CG2   1 
ATOM   59   N  N     . ASN   A 1 129  ? -25.959 -16.303 -54.452 1.00 99.36  ? 278  ASN   A N     1 
ATOM   60   C  CA    . ASN   A 1 129  ? -27.121 -15.928 -53.600 1.00 102.96 ? 278  ASN   A CA    1 
ATOM   61   C  C     . ASN   A 1 129  ? -27.114 -14.408 -53.396 1.00 103.29 ? 278  ASN   A C     1 
ATOM   62   O  O     . ASN   A 1 129  ? -26.558 -13.943 -52.379 1.00 103.04 ? 278  ASN   A O     1 
ATOM   63   C  CB    . ASN   A 1 129  ? -27.131 -16.702 -52.277 1.00 103.69 ? 278  ASN   A CB    1 
ATOM   64   C  CG    . ASN   A 1 129  ? -27.511 -18.159 -52.446 1.00 105.13 ? 278  ASN   A CG    1 
ATOM   65   O  OD1   . ASN   A 1 129  ? -28.155 -18.534 -53.425 1.00 103.35 ? 278  ASN   A OD1   1 
ATOM   66   N  ND2   . ASN   A 1 129  ? -27.125 -18.990 -51.492 1.00 105.96 ? 278  ASN   A ND2   1 
ATOM   67   N  N     . LEU   A 1 130  ? -27.720 -13.682 -54.341 1.00 102.93 ? 279  LEU   A N     1 
ATOM   68   C  CA    . LEU   A 1 130  ? -27.817 -12.198 -54.376 1.00 102.39 ? 279  LEU   A CA    1 
ATOM   69   C  C     . LEU   A 1 130  ? -29.216 -11.778 -53.906 1.00 102.74 ? 279  LEU   A C     1 
ATOM   70   O  O     . LEU   A 1 130  ? -30.201 -12.308 -54.458 1.00 102.16 ? 279  LEU   A O     1 
ATOM   71   C  CB    . LEU   A 1 130  ? -27.545 -11.740 -55.813 1.00 101.86 ? 279  LEU   A CB    1 
ATOM   72   C  CG    . LEU   A 1 130  ? -27.400 -10.234 -56.026 1.00 101.81 ? 279  LEU   A CG    1 
ATOM   73   C  CD1   . LEU   A 1 130  ? -26.163 -9.703  -55.323 1.00 101.89 ? 279  LEU   A CD1   1 
ATOM   74   C  CD2   . LEU   A 1 130  ? -27.353 -9.903  -57.510 1.00 102.05 ? 279  LEU   A CD2   1 
ATOM   75   N  N     . SER   A 1 131  ? -29.296 -10.861 -52.932 1.00 102.78 ? 280  SER   A N     1 
ATOM   76   C  CA    . SER   A 1 131  ? -30.554 -10.408 -52.277 1.00 102.92 ? 280  SER   A CA    1 
ATOM   77   C  C     . SER   A 1 131  ? -31.419 -9.617  -53.267 1.00 106.67 ? 280  SER   A C     1 
ATOM   78   O  O     . SER   A 1 131  ? -30.860 -9.057  -54.231 1.00 107.94 ? 280  SER   A O     1 
ATOM   79   C  CB    . SER   A 1 131  ? -30.267 -9.598  -51.037 1.00 100.41 ? 280  SER   A CB    1 
ATOM   80   O  OG    . SER   A 1 131  ? -29.708 -8.336  -51.369 1.00 98.33  ? 280  SER   A OG    1 
ATOM   81   N  N     . GLN   A 1 132  ? -32.734 -9.576  -53.022 1.00 112.41 ? 281  GLN   A N     1 
ATOM   82   C  CA    . GLN   A 1 132  ? -33.739 -8.862  -53.859 1.00 116.65 ? 281  GLN   A CA    1 
ATOM   83   C  C     . GLN   A 1 132  ? -33.522 -7.347  -53.752 1.00 114.59 ? 281  GLN   A C     1 
ATOM   84   O  O     . GLN   A 1 132  ? -33.687 -6.661  -54.780 1.00 116.07 ? 281  GLN   A O     1 
ATOM   85   C  CB    . GLN   A 1 132  ? -35.165 -9.236  -53.440 1.00 122.90 ? 281  GLN   A CB    1 
ATOM   86   C  CG    . GLN   A 1 132  ? -35.706 -10.481 -54.136 1.00 125.91 ? 281  GLN   A CG    1 
ATOM   87   C  CD    . GLN   A 1 132  ? -36.367 -10.180 -55.461 1.00 128.00 ? 281  GLN   A CD    1 
ATOM   88   O  OE1   . GLN   A 1 132  ? -37.140 -9.233  -55.593 1.00 129.72 ? 281  GLN   A OE1   1 
ATOM   89   N  NE2   . GLN   A 1 132  ? -36.081 -11.002 -56.459 1.00 127.68 ? 281  GLN   A NE2   1 
ATOM   90   N  N     . ASP   A 1 133  ? -33.179 -6.853  -52.555 1.00 112.04 ? 282  ASP   A N     1 
ATOM   91   C  CA    . ASP   A 1 133  ? -32.911 -5.415  -52.275 1.00 109.01 ? 282  ASP   A CA    1 
ATOM   92   C  C     . ASP   A 1 133  ? -31.794 -4.912  -53.198 1.00 103.19 ? 282  ASP   A C     1 
ATOM   93   O  O     . ASP   A 1 133  ? -31.983 -3.851  -53.823 1.00 100.83 ? 282  ASP   A O     1 
ATOM   94   C  CB    . ASP   A 1 133  ? -32.533 -5.184  -50.808 1.00 111.80 ? 282  ASP   A CB    1 
ATOM   95   C  CG    . ASP   A 1 133  ? -33.695 -5.296  -49.836 1.00 114.11 ? 282  ASP   A CG    1 
ATOM   96   O  OD1   . ASP   A 1 133  ? -34.759 -4.710  -50.121 1.00 114.94 ? 282  ASP   A OD1   1 
ATOM   97   O  OD2   . ASP   A 1 133  ? -33.525 -5.966  -48.797 1.00 116.46 ? 282  ASP   A OD2   1 
ATOM   98   N  N     . LEU   A 1 134  ? -30.684 -5.654  -53.274 1.00 98.76  ? 283  LEU   A N     1 
ATOM   99   C  CA    . LEU   A 1 134  ? -29.463 -5.276  -54.038 1.00 96.55  ? 283  LEU   A CA    1 
ATOM   100  C  C     . LEU   A 1 134  ? -29.752 -5.335  -55.544 1.00 94.09  ? 283  LEU   A C     1 
ATOM   101  O  O     . LEU   A 1 134  ? -29.341 -4.398  -56.259 1.00 91.20  ? 283  LEU   A O     1 
ATOM   102  C  CB    . LEU   A 1 134  ? -28.319 -6.218  -53.647 1.00 96.49  ? 283  LEU   A CB    1 
ATOM   103  C  CG    . LEU   A 1 134  ? -26.942 -5.881  -54.224 1.00 96.93  ? 283  LEU   A CG    1 
ATOM   104  C  CD1   . LEU   A 1 134  ? -26.601 -4.410  -54.024 1.00 97.17  ? 283  LEU   A CD1   1 
ATOM   105  C  CD2   . LEU   A 1 134  ? -25.867 -6.762  -53.606 1.00 95.98  ? 283  LEU   A CD2   1 
ATOM   106  N  N     . GLU   A 1 135  ? -30.442 -6.385  -55.999 1.00 93.76  ? 284  GLU   A N     1 
ATOM   107  C  CA    . GLU   A 1 135  ? -30.780 -6.613  -57.432 1.00 94.99  ? 284  GLU   A CA    1 
ATOM   108  C  C     . GLU   A 1 135  ? -31.607 -5.435  -57.967 1.00 94.65  ? 284  GLU   A C     1 
ATOM   109  O  O     . GLU   A 1 135  ? -31.415 -5.078  -59.145 1.00 91.28  ? 284  GLU   A O     1 
ATOM   110  C  CB    . GLU   A 1 135  ? -31.526 -7.937  -57.608 1.00 95.70  ? 284  GLU   A CB    1 
ATOM   111  C  CG    . GLU   A 1 135  ? -31.649 -8.367  -59.060 1.00 96.42  ? 284  GLU   A CG    1 
ATOM   112  C  CD    . GLU   A 1 135  ? -31.989 -9.832  -59.275 1.00 96.62  ? 284  GLU   A CD    1 
ATOM   113  O  OE1   . GLU   A 1 135  ? -32.659 -10.136 -60.284 1.00 98.06  ? 284  GLU   A OE1   1 
ATOM   114  O  OE2   . GLU   A 1 135  ? -31.571 -10.668 -58.446 1.00 93.76  ? 284  GLU   A OE2   1 
ATOM   115  N  N     . HIS   A 1 136  ? -32.489 -4.862  -57.139 1.00 96.07  ? 285  HIS   A N     1 
ATOM   116  C  CA    . HIS   A 1 136  ? -33.277 -3.636  -57.450 1.00 97.25  ? 285  HIS   A CA    1 
ATOM   117  C  C     . HIS   A 1 136  ? -32.337 -2.427  -57.523 1.00 95.07  ? 285  HIS   A C     1 
ATOM   118  O  O     . HIS   A 1 136  ? -32.417 -1.677  -58.516 1.00 95.20  ? 285  HIS   A O     1 
ATOM   119  C  CB    . HIS   A 1 136  ? -34.391 -3.401  -56.416 1.00 100.35 ? 285  HIS   A CB    1 
ATOM   120  C  CG    . HIS   A 1 136  ? -35.535 -4.355  -56.508 1.00 101.88 ? 285  HIS   A CG    1 
ATOM   121  N  ND1   . HIS   A 1 136  ? -36.254 -4.750  -55.395 1.00 101.87 ? 285  HIS   A ND1   1 
ATOM   122  C  CD2   . HIS   A 1 136  ? -36.088 -4.991  -57.563 1.00 102.86 ? 285  HIS   A CD2   1 
ATOM   123  C  CE1   . HIS   A 1 136  ? -37.202 -5.588  -55.763 1.00 103.37 ? 285  HIS   A CE1   1 
ATOM   124  N  NE2   . HIS   A 1 136  ? -37.121 -5.754  -57.089 1.00 103.50 ? 285  HIS   A NE2   1 
ATOM   125  N  N     . GLN   A 1 137  ? -31.487 -2.252  -56.505 1.00 91.69  ? 286  GLN   A N     1 
ATOM   126  C  CA    . GLN   A 1 137  ? -30.532 -1.116  -56.376 1.00 89.19  ? 286  GLN   A CA    1 
ATOM   127  C  C     . GLN   A 1 137  ? -29.641 -1.042  -57.623 1.00 84.53  ? 286  GLN   A C     1 
ATOM   128  O  O     . GLN   A 1 137  ? -29.418 0.082   -58.115 1.00 82.06  ? 286  GLN   A O     1 
ATOM   129  C  CB    . GLN   A 1 137  ? -29.696 -1.260  -55.103 1.00 90.19  ? 286  GLN   A CB    1 
ATOM   130  C  CG    . GLN   A 1 137  ? -30.481 -0.997  -53.826 1.00 91.17  ? 286  GLN   A CG    1 
ATOM   131  C  CD    . GLN   A 1 137  ? -29.835 -1.615  -52.610 1.00 91.31  ? 286  GLN   A CD    1 
ATOM   132  O  OE1   . GLN   A 1 137  ? -28.612 -1.668  -52.490 1.00 92.26  ? 286  GLN   A OE1   1 
ATOM   133  N  NE2   . GLN   A 1 137  ? -30.659 -2.091  -51.690 1.00 91.35  ? 286  GLN   A NE2   1 
ATOM   134  N  N     . LEU   A 1 138  ? -29.155 -2.192  -58.107 1.00 79.62  ? 287  LEU   A N     1 
ATOM   135  C  CA    . LEU   A 1 138  ? -28.338 -2.300  -59.348 1.00 78.65  ? 287  LEU   A CA    1 
ATOM   136  C  C     . LEU   A 1 138  ? -29.151 -1.783  -60.540 1.00 78.79  ? 287  LEU   A C     1 
ATOM   137  O  O     . LEU   A 1 138  ? -28.625 -0.932  -61.286 1.00 78.20  ? 287  LEU   A O     1 
ATOM   138  C  CB    . LEU   A 1 138  ? -27.917 -3.757  -59.568 1.00 77.81  ? 287  LEU   A CB    1 
ATOM   139  C  CG    . LEU   A 1 138  ? -26.762 -4.251  -58.699 1.00 77.07  ? 287  LEU   A CG    1 
ATOM   140  C  CD1   . LEU   A 1 138  ? -26.642 -5.766  -58.769 1.00 76.49  ? 287  LEU   A CD1   1 
ATOM   141  C  CD2   . LEU   A 1 138  ? -25.453 -3.591  -59.105 1.00 76.69  ? 287  LEU   A CD2   1 
ATOM   142  N  N     . GLN   A 1 139  ? -30.383 -2.281  -60.702 1.00 78.76  ? 288  GLN   A N     1 
ATOM   143  C  CA    . GLN   A 1 139  ? -31.316 -1.884  -61.793 1.00 78.23  ? 288  GLN   A CA    1 
ATOM   144  C  C     . GLN   A 1 139  ? -31.604 -0.381  -61.698 1.00 76.32  ? 288  GLN   A C     1 
ATOM   145  O  O     . GLN   A 1 139  ? -31.612 0.281   -62.755 1.00 75.32  ? 288  GLN   A O     1 
ATOM   146  C  CB    . GLN   A 1 139  ? -32.619 -2.682  -61.723 1.00 79.04  ? 288  GLN   A CB    1 
ATOM   147  C  CG    . GLN   A 1 139  ? -32.469 -4.148  -62.105 1.00 80.68  ? 288  GLN   A CG    1 
ATOM   148  C  CD    . GLN   A 1 139  ? -33.727 -4.935  -61.828 1.00 81.97  ? 288  GLN   A CD    1 
ATOM   149  O  OE1   . GLN   A 1 139  ? -34.359 -4.794  -60.783 1.00 83.79  ? 288  GLN   A OE1   1 
ATOM   150  N  NE2   . GLN   A 1 139  ? -34.105 -5.783  -62.769 1.00 82.28  ? 288  GLN   A NE2   1 
ATOM   151  N  N     . ASN   A 1 140  ? -31.824 0.129   -60.480 1.00 75.21  ? 289  ASN   A N     1 
ATOM   152  C  CA    . ASN   A 1 140  ? -32.131 1.560   -60.208 1.00 77.07  ? 289  ASN   A CA    1 
ATOM   153  C  C     . ASN   A 1 140  ? -30.978 2.437   -60.712 1.00 76.96  ? 289  ASN   A C     1 
ATOM   154  O  O     . ASN   A 1 140  ? -31.247 3.356   -61.509 1.00 77.91  ? 289  ASN   A O     1 
ATOM   155  C  CB    . ASN   A 1 140  ? -32.406 1.817   -58.723 1.00 78.72  ? 289  ASN   A CB    1 
ATOM   156  C  CG    . ASN   A 1 140  ? -33.729 1.249   -58.253 1.00 80.31  ? 289  ASN   A CG    1 
ATOM   157  O  OD1   . ASN   A 1 140  ? -33.783 0.551   -57.243 1.00 83.43  ? 289  ASN   A OD1   1 
ATOM   158  N  ND2   . ASN   A 1 140  ? -34.799 1.542   -58.974 1.00 79.18  ? 289  ASN   A ND2   1 
ATOM   159  N  N     . VAL   A 1 141  ? -29.747 2.152   -60.272 1.00 75.67  ? 290  VAL   A N     1 
ATOM   160  C  CA    . VAL   A 1 141  ? -28.519 2.931   -60.621 1.00 74.24  ? 290  VAL   A CA    1 
ATOM   161  C  C     . VAL   A 1 141  ? -28.347 2.932   -62.145 1.00 73.45  ? 290  VAL   A C     1 
ATOM   162  O  O     . VAL   A 1 141  ? -28.159 4.024   -62.715 1.00 71.39  ? 290  VAL   A O     1 
ATOM   163  C  CB    . VAL   A 1 141  ? -27.274 2.376   -59.900 1.00 74.06  ? 290  VAL   A CB    1 
ATOM   164  C  CG1   . VAL   A 1 141  ? -25.978 2.928   -60.477 1.00 73.40  ? 290  VAL   A CG1   1 
ATOM   165  C  CG2   . VAL   A 1 141  ? -27.336 2.638   -58.403 1.00 75.26  ? 290  VAL   A CG2   1 
ATOM   166  N  N     . ILE   A 1 142  ? -28.420 1.755   -62.773 1.00 73.69  ? 291  ILE   A N     1 
ATOM   167  C  CA    . ILE   A 1 142  ? -28.317 1.568   -64.254 1.00 75.81  ? 291  ILE   A CA    1 
ATOM   168  C  C     . ILE   A 1 142  ? -29.370 2.442   -64.955 1.00 77.71  ? 291  ILE   A C     1 
ATOM   169  O  O     . ILE   A 1 142  ? -29.048 3.011   -66.018 1.00 77.31  ? 291  ILE   A O     1 
ATOM   170  C  CB    . ILE   A 1 142  ? -28.439 0.073   -64.624 1.00 76.03  ? 291  ILE   A CB    1 
ATOM   171  C  CG1   . ILE   A 1 142  ? -27.069 -0.607  -64.698 1.00 76.53  ? 291  ILE   A CG1   1 
ATOM   172  C  CG2   . ILE   A 1 142  ? -29.214 -0.125  -65.920 1.00 76.22  ? 291  ILE   A CG2   1 
ATOM   173  C  CD1   . ILE   A 1 142  ? -26.212 -0.440  -63.461 1.00 76.57  ? 291  ILE   A CD1   1 
ATOM   174  N  N     . GLN   A 1 143  ? -30.575 2.539   -64.384 1.00 79.46  ? 292  GLN   A N     1 
ATOM   175  C  CA    . GLN   A 1 143  ? -31.705 3.337   -64.936 1.00 81.35  ? 292  GLN   A CA    1 
ATOM   176  C  C     . GLN   A 1 143  ? -31.422 4.830   -64.716 1.00 83.87  ? 292  GLN   A C     1 
ATOM   177  O  O     . GLN   A 1 143  ? -31.677 5.617   -65.648 1.00 84.32  ? 292  GLN   A O     1 
ATOM   178  C  CB    . GLN   A 1 143  ? -33.025 2.890   -64.299 1.00 80.53  ? 292  GLN   A CB    1 
ATOM   179  C  CG    . GLN   A 1 143  ? -34.264 3.293   -65.090 1.00 78.84  ? 292  GLN   A CG    1 
ATOM   180  C  CD    . GLN   A 1 143  ? -34.703 4.709   -64.810 1.00 78.14  ? 292  GLN   A CD    1 
ATOM   181  O  OE1   . GLN   A 1 143  ? -34.616 5.197   -63.684 1.00 77.35  ? 292  GLN   A OE1   1 
ATOM   182  N  NE2   . GLN   A 1 143  ? -35.187 5.384   -65.840 1.00 76.40  ? 292  GLN   A NE2   1 
ATOM   183  N  N     . GLU   A 1 144  ? -30.898 5.197   -63.541 1.00 88.13  ? 293  GLU   A N     1 
ATOM   184  C  CA    . GLU   A 1 144  ? -30.559 6.596   -63.155 1.00 92.64  ? 293  GLU   A CA    1 
ATOM   185  C  C     . GLU   A 1 144  ? -29.430 7.137   -64.045 1.00 93.98  ? 293  GLU   A C     1 
ATOM   186  O  O     . GLU   A 1 144  ? -29.398 8.363   -64.264 1.00 93.76  ? 293  GLU   A O     1 
ATOM   187  C  CB    . GLU   A 1 144  ? -30.159 6.664   -61.679 1.00 96.23  ? 293  GLU   A CB    1 
ATOM   188  C  CG    . GLU   A 1 144  ? -31.326 6.472   -60.723 1.00 100.40 ? 293  GLU   A CG    1 
ATOM   189  C  CD    . GLU   A 1 144  ? -30.967 5.936   -59.344 1.00 103.50 ? 293  GLU   A CD    1 
ATOM   190  O  OE1   . GLU   A 1 144  ? -29.793 6.079   -58.933 1.00 104.90 ? 293  GLU   A OE1   1 
ATOM   191  O  OE2   . GLU   A 1 144  ? -31.866 5.374   -58.682 1.00 101.88 ? 293  GLU   A OE2   1 
ATOM   192  N  N     . LEU   A 1 145  ? -28.541 6.262   -64.530 1.00 95.67  ? 294  LEU   A N     1 
ATOM   193  C  CA    . LEU   A 1 145  ? -27.385 6.623   -65.399 1.00 97.00  ? 294  LEU   A CA    1 
ATOM   194  C  C     . LEU   A 1 145  ? -27.787 6.546   -66.878 1.00 97.05  ? 294  LEU   A C     1 
ATOM   195  O  O     . LEU   A 1 145  ? -26.986 6.997   -67.721 1.00 96.53  ? 294  LEU   A O     1 
ATOM   196  C  CB    . LEU   A 1 145  ? -26.208 5.684   -65.103 1.00 99.24  ? 294  LEU   A CB    1 
ATOM   197  C  CG    . LEU   A 1 145  ? -25.225 6.159   -64.032 1.00 100.87 ? 294  LEU   A CG    1 
ATOM   198  C  CD1   . LEU   A 1 145  ? -25.887 6.242   -62.664 1.00 102.08 ? 294  LEU   A CD1   1 
ATOM   199  C  CD2   . LEU   A 1 145  ? -24.008 5.247   -63.977 1.00 99.05  ? 294  LEU   A CD2   1 
ATOM   200  N  N     . ASN   A 1 146  ? -28.969 5.992   -67.177 1.00 98.97  ? 295  ASN   A N     1 
ATOM   201  C  CA    . ASN   A 1 146  ? -29.520 5.831   -68.550 1.00 100.80 ? 295  ASN   A CA    1 
ATOM   202  C  C     . ASN   A 1 146  ? -28.577 4.934   -69.364 1.00 102.47 ? 295  ASN   A C     1 
ATOM   203  O  O     . ASN   A 1 146  ? -28.228 5.314   -70.499 1.00 101.45 ? 295  ASN   A O     1 
ATOM   204  C  CB    . ASN   A 1 146  ? -29.758 7.188   -69.223 1.00 100.73 ? 295  ASN   A CB    1 
ATOM   205  C  CG    . ASN   A 1 146  ? -30.418 7.080   -70.583 1.00 101.57 ? 295  ASN   A CG    1 
ATOM   206  O  OD1   . ASN   A 1 146  ? -31.143 6.126   -70.858 1.00 100.98 ? 295  ASN   A OD1   1 
ATOM   207  N  ND2   . ASN   A 1 146  ? -30.169 8.053   -71.444 1.00 101.86 ? 295  ASN   A ND2   1 
ATOM   208  N  N     . LEU   A 1 147  ? -28.189 3.784   -68.801 1.00 107.22 ? 296  LEU   A N     1 
ATOM   209  C  CA    . LEU   A 1 147  ? -27.229 2.830   -69.420 1.00 111.85 ? 296  LEU   A CA    1 
ATOM   210  C  C     . LEU   A 1 147  ? -28.001 1.806   -70.258 1.00 113.25 ? 296  LEU   A C     1 
ATOM   211  O  O     . LEU   A 1 147  ? -28.996 1.249   -69.748 1.00 106.55 ? 296  LEU   A O     1 
ATOM   212  C  CB    . LEU   A 1 147  ? -26.405 2.145   -68.324 1.00 115.24 ? 296  LEU   A CB    1 
ATOM   213  C  CG    . LEU   A 1 147  ? -25.663 3.085   -67.373 1.00 118.06 ? 296  LEU   A CG    1 
ATOM   214  C  CD1   . LEU   A 1 147  ? -24.856 2.299   -66.350 1.00 119.24 ? 296  LEU   A CD1   1 
ATOM   215  C  CD2   . LEU   A 1 147  ? -24.763 4.045   -68.137 1.00 118.21 ? 296  LEU   A CD2   1 
ATOM   216  N  N     . GLU   A 1 148  ? -27.544 1.580   -71.494 1.00 120.37 ? 297  GLU   A N     1 
ATOM   217  C  CA    . GLU   A 1 148  ? -28.175 0.673   -72.491 1.00 125.45 ? 297  GLU   A CA    1 
ATOM   218  C  C     . GLU   A 1 148  ? -27.852 -0.778  -72.114 1.00 126.42 ? 297  GLU   A C     1 
ATOM   219  O  O     . GLU   A 1 148  ? -26.873 -1.332  -72.657 1.00 125.34 ? 297  GLU   A O     1 
ATOM   220  C  CB    . GLU   A 1 148  ? -27.691 1.031   -73.900 1.00 128.20 ? 297  GLU   A CB    1 
ATOM   221  C  CG    . GLU   A 1 148  ? -28.424 0.296   -75.011 1.00 129.34 ? 297  GLU   A CG    1 
ATOM   222  C  CD    . GLU   A 1 148  ? -28.106 0.780   -76.417 1.00 128.21 ? 297  GLU   A CD    1 
ATOM   223  O  OE1   . GLU   A 1 148  ? -27.035 1.392   -76.606 1.00 128.76 ? 297  GLU   A OE1   1 
ATOM   224  O  OE2   . GLU   A 1 148  ? -28.933 0.547   -77.321 1.00 125.96 ? 297  GLU   A OE2   1 
ATOM   225  N  N     . ILE   A 1 149  ? -28.645 -1.358  -71.205 1.00 126.22 ? 298  ILE   A N     1 
ATOM   226  C  CA    . ILE   A 1 149  ? -28.516 -2.779  -70.757 1.00 125.98 ? 298  ILE   A CA    1 
ATOM   227  C  C     . ILE   A 1 149  ? -29.008 -3.698  -71.882 1.00 124.79 ? 298  ILE   A C     1 
ATOM   228  O  O     . ILE   A 1 149  ? -30.047 -3.381  -72.497 1.00 126.67 ? 298  ILE   A O     1 
ATOM   229  C  CB    . ILE   A 1 149  ? -29.263 -3.048  -69.431 1.00 126.31 ? 298  ILE   A CB    1 
ATOM   230  C  CG1   . ILE   A 1 149  ? -30.683 -2.472  -69.413 1.00 122.98 ? 298  ILE   A CG1   1 
ATOM   231  C  CG2   . ILE   A 1 149  ? -28.444 -2.554  -68.250 1.00 128.98 ? 298  ILE   A CG2   1 
ATOM   232  C  CD1   . ILE   A 1 149  ? -31.569 -3.066  -68.343 1.00 121.02 ? 298  ILE   A CD1   1 
ATOM   233  N  N     . VAL   A 1 150  ? -28.280 -4.790  -72.134 1.00 121.12 ? 299  VAL   A N     1 
ATOM   234  C  CA    . VAL   A 1 150  ? -28.637 -5.824  -73.150 1.00 117.46 ? 299  VAL   A CA    1 
ATOM   235  C  C     . VAL   A 1 150  ? -29.772 -6.667  -72.576 1.00 116.42 ? 299  VAL   A C     1 
ATOM   236  O  O     . VAL   A 1 150  ? -29.615 -7.270  -71.516 1.00 109.07 ? 299  VAL   A O     1 
ATOM   237  C  CB    . VAL   A 1 150  ? -27.422 -6.691  -73.537 1.00 114.48 ? 299  VAL   A CB    1 
ATOM   238  C  CG1   . VAL   A 1 150  ? -27.799 -7.779  -74.533 1.00 113.68 ? 299  VAL   A CG1   1 
ATOM   239  C  CG2   . VAL   A 1 150  ? -26.275 -5.848  -74.077 1.00 112.88 ? 299  VAL   A CG2   1 
ATOM   240  N  N     . PRO   A 1 151  ? -30.949 -6.728  -73.245 1.00 120.44 ? 300  PRO   A N     1 
ATOM   241  C  CA    . PRO   A 1 151  ? -32.086 -7.489  -72.730 1.00 122.77 ? 300  PRO   A CA    1 
ATOM   242  C  C     . PRO   A 1 151  ? -31.871 -8.996  -72.862 1.00 124.82 ? 300  PRO   A C     1 
ATOM   243  O  O     . PRO   A 1 151  ? -30.951 -9.435  -73.550 1.00 127.07 ? 300  PRO   A O     1 
ATOM   244  C  CB    . PRO   A 1 151  ? -33.259 -7.007  -73.597 1.00 122.12 ? 300  PRO   A CB    1 
ATOM   245  C  CG    . PRO   A 1 151  ? -32.612 -6.619  -74.910 1.00 122.50 ? 300  PRO   A CG    1 
ATOM   246  C  CD    . PRO   A 1 151  ? -31.246 -6.080  -74.533 1.00 122.16 ? 300  PRO   A CD    1 
ATOM   247  N  N     . PRO   A 1 152  ? -32.709 -9.833  -72.207 1.00 125.86 ? 301  PRO   A N     1 
ATOM   248  C  CA    . PRO   A 1 152  ? -32.515 -11.284 -72.217 1.00 125.50 ? 301  PRO   A CA    1 
ATOM   249  C  C     . PRO   A 1 152  ? -32.661 -11.895 -73.608 1.00 127.22 ? 301  PRO   A C     1 
ATOM   250  O  O     . PRO   A 1 152  ? -33.166 -11.249 -74.523 1.00 124.65 ? 301  PRO   A O     1 
ATOM   251  C  CB    . PRO   A 1 152  ? -33.621 -11.824 -71.296 1.00 124.66 ? 301  PRO   A CB    1 
ATOM   252  C  CG    . PRO   A 1 152  ? -34.100 -10.618 -70.508 1.00 125.00 ? 301  PRO   A CG    1 
ATOM   253  C  CD    . PRO   A 1 152  ? -33.881 -9.429  -71.417 1.00 125.65 ? 301  PRO   A CD    1 
ATOM   254  N  N     . PRO   A 1 153  ? -32.224 -13.160 -73.809 1.00 133.41 ? 302  PRO   A N     1 
ATOM   255  C  CA    . PRO   A 1 153  ? -32.392 -13.838 -75.094 1.00 137.16 ? 302  PRO   A CA    1 
ATOM   256  C  C     . PRO   A 1 153  ? -33.829 -14.349 -75.284 1.00 140.47 ? 302  PRO   A C     1 
ATOM   257  O  O     . PRO   A 1 153  ? -34.493 -14.608 -74.293 1.00 137.72 ? 302  PRO   A O     1 
ATOM   258  C  CB    . PRO   A 1 153  ? -31.385 -14.994 -75.000 1.00 136.04 ? 302  PRO   A CB    1 
ATOM   259  C  CG    . PRO   A 1 153  ? -31.356 -15.331 -73.524 1.00 135.30 ? 302  PRO   A CG    1 
ATOM   260  C  CD    . PRO   A 1 153  ? -31.548 -14.007 -72.812 1.00 134.49 ? 302  PRO   A CD    1 
ATOM   261  N  N     . GLU   A 1 154  ? -34.264 -14.477 -76.543 1.00 144.44 ? 303  GLU   A N     1 
ATOM   262  C  CA    . GLU   A 1 154  ? -35.618 -14.963 -76.928 1.00 145.05 ? 303  GLU   A CA    1 
ATOM   263  C  C     . GLU   A 1 154  ? -35.753 -16.432 -76.511 1.00 145.75 ? 303  GLU   A C     1 
ATOM   264  O  O     . GLU   A 1 154  ? -36.828 -16.805 -76.000 1.00 143.75 ? 303  GLU   A O     1 
ATOM   265  C  CB    . GLU   A 1 154  ? -35.854 -14.800 -78.433 1.00 145.17 ? 303  GLU   A CB    1 
ATOM   266  C  CG    . GLU   A 1 154  ? -35.755 -13.365 -78.928 1.00 145.34 ? 303  GLU   A CG    1 
ATOM   267  C  CD    . GLU   A 1 154  ? -36.730 -12.383 -78.297 1.00 144.91 ? 303  GLU   A CD    1 
ATOM   268  O  OE1   . GLU   A 1 154  ? -37.809 -12.821 -77.852 1.00 146.91 ? 303  GLU   A OE1   1 
ATOM   269  O  OE2   . GLU   A 1 154  ? -36.406 -11.180 -78.254 1.00 141.42 ? 303  GLU   A OE2   1 
ATOM   270  N  N     . ASP   A 1 155  ? -34.695 -17.222 -76.727 1.00 148.06 ? 304  ASP   A N     1 
ATOM   271  C  CA    . ASP   A 1 155  ? -34.589 -18.647 -76.311 1.00 148.22 ? 304  ASP   A CA    1 
ATOM   272  C  C     . ASP   A 1 155  ? -33.166 -18.922 -75.829 1.00 147.67 ? 304  ASP   A C     1 
ATOM   273  O  O     . ASP   A 1 155  ? -32.241 -18.194 -76.186 1.00 146.92 ? 304  ASP   A O     1 
ATOM   274  C  CB    . ASP   A 1 155  ? -34.967 -19.589 -77.460 1.00 147.62 ? 304  ASP   A CB    1 
ATOM   275  C  CG    . ASP   A 1 155  ? -34.015 -19.542 -78.646 1.00 145.87 ? 304  ASP   A CG    1 
ATOM   276  O  OD1   . ASP   A 1 155  ? -33.486 -18.448 -78.936 1.00 143.36 ? 304  ASP   A OD1   1 
ATOM   277  O  OD2   . ASP   A 1 155  ? -33.805 -20.602 -79.269 1.00 141.27 ? 304  ASP   A OD2   1 
ATOM   278  N  N     . PRO   A 1 156  ? -32.942 -19.970 -75.000 1.00 144.23 ? 305  PRO   A N     1 
ATOM   279  C  CA    . PRO   A 1 156  ? -31.589 -20.463 -74.733 1.00 142.52 ? 305  PRO   A CA    1 
ATOM   280  C  C     . PRO   A 1 156  ? -30.903 -20.961 -76.016 1.00 141.83 ? 305  PRO   A C     1 
ATOM   281  O  O     . PRO   A 1 156  ? -31.510 -20.879 -77.071 1.00 144.35 ? 305  PRO   A O     1 
ATOM   282  C  CB    . PRO   A 1 156  ? -31.798 -21.619 -73.739 1.00 141.10 ? 305  PRO   A CB    1 
ATOM   283  C  CG    . PRO   A 1 156  ? -33.166 -21.365 -73.137 1.00 140.07 ? 305  PRO   A CG    1 
ATOM   284  C  CD    . PRO   A 1 156  ? -33.966 -20.706 -74.241 1.00 141.49 ? 305  PRO   A CD    1 
ATOM   285  N  N     . PHE   A 1 157  ? -29.662 -21.448 -75.896 1.00 139.21 ? 306  PHE   A N     1 
ATOM   286  C  CA    . PHE   A 1 157  ? -28.809 -21.984 -76.995 1.00 137.99 ? 306  PHE   A CA    1 
ATOM   287  C  C     . PHE   A 1 157  ? -28.122 -20.834 -77.746 1.00 135.58 ? 306  PHE   A C     1 
ATOM   288  O  O     . PHE   A 1 157  ? -26.960 -21.021 -78.159 1.00 137.31 ? 306  PHE   A O     1 
ATOM   289  C  CB    . PHE   A 1 157  ? -29.605 -22.868 -77.962 1.00 138.61 ? 306  PHE   A CB    1 
ATOM   290  C  CG    . PHE   A 1 157  ? -30.380 -23.989 -77.314 1.00 138.66 ? 306  PHE   A CG    1 
ATOM   291  C  CD1   . PHE   A 1 157  ? -29.730 -24.969 -76.579 1.00 136.76 ? 306  PHE   A CD1   1 
ATOM   292  C  CD2   . PHE   A 1 157  ? -31.759 -24.073 -77.450 1.00 138.56 ? 306  PHE   A CD2   1 
ATOM   293  C  CE1   . PHE   A 1 157  ? -30.442 -26.001 -75.986 1.00 136.14 ? 306  PHE   A CE1   1 
ATOM   294  C  CE2   . PHE   A 1 157  ? -32.469 -25.107 -76.858 1.00 138.01 ? 306  PHE   A CE2   1 
ATOM   295  C  CZ    . PHE   A 1 157  ? -31.809 -26.069 -76.127 1.00 137.47 ? 306  PHE   A CZ    1 
ATOM   296  N  N     . LEU   A 1 158  ? -28.820 -19.706 -77.938 1.00 131.76 ? 307  LEU   A N     1 
ATOM   297  C  CA    . LEU   A 1 158  ? -28.267 -18.442 -78.500 1.00 127.63 ? 307  LEU   A CA    1 
ATOM   298  C  C     . LEU   A 1 158  ? -28.087 -17.428 -77.372 1.00 123.15 ? 307  LEU   A C     1 
ATOM   299  O  O     . LEU   A 1 158  ? -28.980 -16.621 -77.118 1.00 117.60 ? 307  LEU   A O     1 
ATOM   300  C  CB    . LEU   A 1 158  ? -29.216 -17.904 -79.578 1.00 127.09 ? 307  LEU   A CB    1 
ATOM   301  C  CG    . LEU   A 1 158  ? -29.266 -18.700 -80.882 1.00 125.88 ? 307  LEU   A CG    1 
ATOM   302  C  CD1   . LEU   A 1 158  ? -30.343 -18.152 -81.808 1.00 125.05 ? 307  LEU   A CD1   1 
ATOM   303  C  CD2   . LEU   A 1 158  ? -27.913 -18.697 -81.579 1.00 123.99 ? 307  LEU   A CD2   1 
ATOM   304  N  N     . PRO   A 1 159  ? -26.937 -17.442 -76.655 1.00 120.70 ? 308  PRO   A N     1 
ATOM   305  C  CA    . PRO   A 1 159  ? -26.682 -16.474 -75.588 1.00 117.81 ? 308  PRO   A CA    1 
ATOM   306  C  C     . PRO   A 1 159  ? -26.177 -15.132 -76.139 1.00 115.75 ? 308  PRO   A C     1 
ATOM   307  O  O     . PRO   A 1 159  ? -25.546 -15.131 -77.181 1.00 115.14 ? 308  PRO   A O     1 
ATOM   308  C  CB    . PRO   A 1 159  ? -25.605 -17.183 -74.755 1.00 117.23 ? 308  PRO   A CB    1 
ATOM   309  C  CG    . PRO   A 1 159  ? -24.804 -17.951 -75.785 1.00 117.71 ? 308  PRO   A CG    1 
ATOM   310  C  CD    . PRO   A 1 159  ? -25.823 -18.391 -76.818 1.00 118.80 ? 308  PRO   A CD    1 
ATOM   311  N  N     . VAL   A 1 160  ? -26.457 -14.038 -75.423 1.00 114.41 ? 309  VAL   A N     1 
ATOM   312  C  CA    . VAL   A 1 160  ? -26.115 -12.640 -75.829 1.00 115.73 ? 309  VAL   A CA    1 
ATOM   313  C  C     . VAL   A 1 160  ? -24.972 -12.127 -74.943 1.00 115.77 ? 309  VAL   A C     1 
ATOM   314  O  O     . VAL   A 1 160  ? -25.003 -12.395 -73.725 1.00 118.43 ? 309  VAL   A O     1 
ATOM   315  C  CB    . VAL   A 1 160  ? -27.343 -11.709 -75.764 1.00 116.67 ? 309  VAL   A CB    1 
ATOM   316  C  CG1   . VAL   A 1 160  ? -28.403 -12.112 -76.777 1.00 118.15 ? 309  VAL   A CG1   1 
ATOM   317  C  CG2   . VAL   A 1 160  ? -27.947 -11.623 -74.368 1.00 116.35 ? 309  VAL   A CG2   1 
ATOM   318  N  N     . VAL   A 1 161  ? -24.004 -11.421 -75.538 1.00 112.78 ? 310  VAL   A N     1 
ATOM   319  C  CA    . VAL   A 1 161  ? -22.879 -10.755 -74.812 1.00 110.60 ? 310  VAL   A CA    1 
ATOM   320  C  C     . VAL   A 1 161  ? -23.442 -9.535  -74.069 1.00 107.77 ? 310  VAL   A C     1 
ATOM   321  O  O     . VAL   A 1 161  ? -24.148 -8.727  -74.708 1.00 106.13 ? 310  VAL   A O     1 
ATOM   322  C  CB    . VAL   A 1 161  ? -21.714 -10.373 -75.749 1.00 111.24 ? 310  VAL   A CB    1 
ATOM   323  C  CG1   . VAL   A 1 161  ? -21.111 -11.596 -76.426 1.00 110.63 ? 310  VAL   A CG1   1 
ATOM   324  C  CG2   . VAL   A 1 161  ? -22.105 -9.325  -76.785 1.00 112.09 ? 310  VAL   A CG2   1 
ATOM   325  N  N     . LEU   A 1 162  ? -23.148 -9.421  -72.768 1.00 104.63 ? 311  LEU   A N     1 
ATOM   326  C  CA    . LEU   A 1 162  ? -23.625 -8.325  -71.879 1.00 101.21 ? 311  LEU   A CA    1 
ATOM   327  C  C     . LEU   A 1 162  ? -22.672 -7.126  -71.968 1.00 100.39 ? 311  LEU   A C     1 
ATOM   328  O  O     . LEU   A 1 162  ? -23.051 -6.039  -71.484 1.00 102.03 ? 311  LEU   A O     1 
ATOM   329  C  CB    . LEU   A 1 162  ? -23.703 -8.842  -70.439 1.00 99.20  ? 311  LEU   A CB    1 
ATOM   330  C  CG    . LEU   A 1 162  ? -24.583 -10.072 -70.221 1.00 98.21  ? 311  LEU   A CG    1 
ATOM   331  C  CD1   . LEU   A 1 162  ? -24.542 -10.513 -68.766 1.00 98.25  ? 311  LEU   A CD1   1 
ATOM   332  C  CD2   . LEU   A 1 162  ? -26.016 -9.802  -70.653 1.00 97.36  ? 311  LEU   A CD2   1 
ATOM   333  N  N     . ASN   A 1 163  ? -21.492 -7.322  -72.567 1.00 99.85  ? 312  ASN   A N     1 
ATOM   334  C  CA    . ASN   A 1 163  ? -20.372 -6.343  -72.592 1.00 100.85 ? 312  ASN   A CA    1 
ATOM   335  C  C     . ASN   A 1 163  ? -20.790 -5.109  -73.398 1.00 104.01 ? 312  ASN   A C     1 
ATOM   336  O  O     . ASN   A 1 163  ? -21.135 -5.267  -74.587 1.00 104.74 ? 312  ASN   A O     1 
ATOM   337  C  CB    . ASN   A 1 163  ? -19.093 -6.954  -73.171 1.00 99.62  ? 312  ASN   A CB    1 
ATOM   338  C  CG    . ASN   A 1 163  ? -18.820 -8.352  -72.658 1.00 99.67  ? 312  ASN   A CG    1 
ATOM   339  O  OD1   . ASN   A 1 163  ? -18.772 -9.301  -73.437 1.00 102.49 ? 312  ASN   A OD1   1 
ATOM   340  N  ND2   . ASN   A 1 163  ? -18.665 -8.490  -71.352 1.00 99.69  ? 312  ASN   A ND2   1 
ATOM   341  N  N     . LEU   A 1 164  ? -20.757 -3.932  -72.765 1.00 106.45 ? 313  LEU   A N     1 
ATOM   342  C  CA    . LEU   A 1 164  ? -21.037 -2.619  -73.403 1.00 107.89 ? 313  LEU   A CA    1 
ATOM   343  C  C     . LEU   A 1 164  ? -19.707 -1.999  -73.850 1.00 107.49 ? 313  LEU   A C     1 
ATOM   344  O  O     . LEU   A 1 164  ? -18.870 -1.712  -72.972 1.00 109.03 ? 313  LEU   A O     1 
ATOM   345  C  CB    . LEU   A 1 164  ? -21.770 -1.718  -72.403 1.00 108.97 ? 313  LEU   A CB    1 
ATOM   346  C  CG    . LEU   A 1 164  ? -23.002 -2.331  -71.735 1.00 111.09 ? 313  LEU   A CG    1 
ATOM   347  C  CD1   . LEU   A 1 164  ? -23.651 -1.339  -70.781 1.00 111.69 ? 313  LEU   A CD1   1 
ATOM   348  C  CD2   . LEU   A 1 164  ? -24.010 -2.808  -72.770 1.00 112.52 ? 313  LEU   A CD2   1 
ATOM   349  N  N     . GLY   A 1 165  ? -19.518 -1.831  -75.164 1.00 106.42 ? 314  GLY   A N     1 
ATOM   350  C  CA    . GLY   A 1 165  ? -18.318 -1.215  -75.766 1.00 106.23 ? 314  GLY   A CA    1 
ATOM   351  C  C     . GLY   A 1 165  ? -18.080 0.190   -75.235 1.00 107.33 ? 314  GLY   A C     1 
ATOM   352  O  O     . GLY   A 1 165  ? -16.913 0.512   -74.931 1.00 107.69 ? 314  GLY   A O     1 
ATOM   353  N  N     . LYS   A 1 166  ? -19.150 0.986   -75.125 1.00 106.89 ? 315  LYS   A N     1 
ATOM   354  C  CA    . LYS   A 1 166  ? -19.148 2.389   -74.621 1.00 106.16 ? 315  LYS   A CA    1 
ATOM   355  C  C     . LYS   A 1 166  ? -18.226 3.244   -75.501 1.00 106.31 ? 315  LYS   A C     1 
ATOM   356  O  O     . LYS   A 1 166  ? -17.032 3.350   -75.154 1.00 105.31 ? 315  LYS   A O     1 
ATOM   357  C  CB    . LYS   A 1 166  ? -18.743 2.429   -73.142 1.00 104.66 ? 315  LYS   A CB    1 
ATOM   358  C  CG    . LYS   A 1 166  ? -18.776 3.806   -72.490 1.00 103.06 ? 315  LYS   A CG    1 
ATOM   359  C  CD    . LYS   A 1 166  ? -20.155 4.433   -72.443 1.00 102.06 ? 315  LYS   A CD    1 
ATOM   360  C  CE    . LYS   A 1 166  ? -20.143 5.859   -71.935 1.00 102.88 ? 315  LYS   A CE    1 
ATOM   361  N  NZ    . LYS   A 1 166  ? -19.387 6.761   -72.836 1.00 101.62 ? 315  LYS   A NZ    1 
ATOM   362  N  N     . PRO   A 1 172  ? -11.041 12.363  -80.489 1.00 129.17 ? 321  PRO   A N     1 
ATOM   363  C  CA    . PRO   A 1 172  ? -9.605  12.050  -80.544 1.00 128.45 ? 321  PRO   A CA    1 
ATOM   364  C  C     . PRO   A 1 172  ? -8.743  13.251  -80.965 1.00 125.63 ? 321  PRO   A C     1 
ATOM   365  O  O     . PRO   A 1 172  ? -9.298  14.271  -81.335 1.00 122.82 ? 321  PRO   A O     1 
ATOM   366  C  CB    . PRO   A 1 172  ? -9.518  10.926  -81.585 1.00 128.76 ? 321  PRO   A CB    1 
ATOM   367  C  CG    . PRO   A 1 172  ? -10.814 10.181  -81.401 1.00 128.71 ? 321  PRO   A CG    1 
ATOM   368  C  CD    . PRO   A 1 172  ? -11.824 11.261  -81.068 1.00 128.72 ? 321  PRO   A CD    1 
ATOM   369  N  N     . SER   A 1 173  ? -7.416  13.095  -80.897 1.00 125.39 ? 322  SER   A N     1 
ATOM   370  C  CA    . SER   A 1 173  ? -6.404  14.133  -81.227 1.00 126.66 ? 322  SER   A CA    1 
ATOM   371  C  C     . SER   A 1 173  ? -5.849  13.895  -82.637 1.00 129.13 ? 322  SER   A C     1 
ATOM   372  O  O     . SER   A 1 173  ? -5.951  12.753  -83.133 1.00 128.68 ? 322  SER   A O     1 
ATOM   373  C  CB    . SER   A 1 173  ? -5.300  14.154  -80.200 1.00 124.78 ? 322  SER   A CB    1 
ATOM   374  O  OG    . SER   A 1 173  ? -4.458  15.283  -80.384 1.00 123.15 ? 322  SER   A OG    1 
ATOM   375  N  N     . GLN   A 1 174  ? -5.281  14.941  -83.247 1.00 131.91 ? 323  GLN   A N     1 
ATOM   376  C  CA    . GLN   A 1 174  ? -4.694  14.917  -84.615 1.00 133.74 ? 323  GLN   A CA    1 
ATOM   377  C  C     . GLN   A 1 174  ? -3.371  14.141  -84.579 1.00 131.53 ? 323  GLN   A C     1 
ATOM   378  O  O     . GLN   A 1 174  ? -2.639  14.267  -83.576 1.00 129.08 ? 323  GLN   A O     1 
ATOM   379  C  CB    . GLN   A 1 174  ? -4.500  16.346  -85.129 1.00 136.44 ? 323  GLN   A CB    1 
ATOM   380  C  CG    . GLN   A 1 174  ? -4.260  16.434  -86.630 1.00 137.52 ? 323  GLN   A CG    1 
ATOM   381  C  CD    . GLN   A 1 174  ? -4.306  17.854  -87.142 1.00 137.24 ? 323  GLN   A CD    1 
ATOM   382  O  OE1   . GLN   A 1 174  ? -4.270  18.816  -86.377 1.00 137.86 ? 323  GLN   A OE1   1 
ATOM   383  N  NE2   . GLN   A 1 174  ? -4.388  17.998  -88.455 1.00 135.88 ? 323  GLN   A NE2   1 
ATOM   384  N  N     . ARG   A 1 175  ? -3.080  13.374  -85.636 1.00 129.52 ? 324  ARG   A N     1 
ATOM   385  C  CA    . ARG   A 1 175  ? -1.896  12.476  -85.729 1.00 127.67 ? 324  ARG   A CA    1 
ATOM   386  C  C     . ARG   A 1 175  ? -0.635  13.317  -85.969 1.00 130.69 ? 324  ARG   A C     1 
ATOM   387  O  O     . ARG   A 1 175  ? -0.567  13.981  -87.023 1.00 133.15 ? 324  ARG   A O     1 
ATOM   388  C  CB    . ARG   A 1 175  ? -2.074  11.453  -86.855 1.00 123.38 ? 324  ARG   A CB    1 
ATOM   389  C  CG    . ARG   A 1 175  ? -3.339  10.613  -86.750 1.00 122.06 ? 324  ARG   A CG    1 
ATOM   390  C  CD    . ARG   A 1 175  ? -3.339  9.482   -87.761 1.00 121.58 ? 324  ARG   A CD    1 
ATOM   391  N  NE    . ARG   A 1 175  ? -2.687  8.281   -87.249 1.00 121.43 ? 324  ARG   A NE    1 
ATOM   392  C  CZ    . ARG   A 1 175  ? -3.292  7.125   -86.971 1.00 121.32 ? 324  ARG   A CZ    1 
ATOM   393  N  NH1   . ARG   A 1 175  ? -2.581  6.110   -86.506 1.00 120.25 ? 324  ARG   A NH1   1 
ATOM   394  N  NH2   . ARG   A 1 175  ? -4.593  6.972   -87.157 1.00 120.85 ? 324  ARG   A NH2   1 
ATOM   395  N  N     . GLN   A 1 176  ? 0.317   13.271  -85.027 1.00 132.10 ? 325  GLN   A N     1 
ATOM   396  C  CA    . GLN   A 1 176  ? 1.627   13.984  -85.067 1.00 131.86 ? 325  GLN   A CA    1 
ATOM   397  C  C     . GLN   A 1 176  ? 1.506   15.259  -85.913 1.00 131.47 ? 325  GLN   A C     1 
ATOM   398  O  O     . GLN   A 1 176  ? 2.556   15.884  -86.165 1.00 129.40 ? 325  GLN   A O     1 
ATOM   399  C  CB    . GLN   A 1 176  ? 2.725   13.056  -85.597 1.00 130.79 ? 325  GLN   A CB    1 
ATOM   400  C  CG    . GLN   A 1 176  ? 2.458   12.506  -86.992 1.00 131.00 ? 325  GLN   A CG    1 
ATOM   401  C  CD    . GLN   A 1 176  ? 3.602   11.670  -87.514 1.00 130.54 ? 325  GLN   A CD    1 
ATOM   402  O  OE1   . GLN   A 1 176  ? 4.772   12.001  -87.337 1.00 129.06 ? 325  GLN   A OE1   1 
ATOM   403  N  NE2   . GLN   A 1 176  ? 3.268   10.573  -88.175 1.00 129.36 ? 325  GLN   A NE2   1 
ATOM   404  N  N     . ILE   A 1 179  ? 7.336   11.745  -86.808 1.00 90.38  ? 328  ILE   A N     1 
ATOM   405  C  CA    . ILE   A 1 179  ? 8.696   11.450  -86.260 1.00 93.00  ? 328  ILE   A CA    1 
ATOM   406  C  C     . ILE   A 1 179  ? 9.233   12.700  -85.547 1.00 93.59  ? 328  ILE   A C     1 
ATOM   407  O  O     . ILE   A 1 179  ? 8.919   13.823  -85.997 1.00 98.59  ? 328  ILE   A O     1 
ATOM   408  C  CB    . ILE   A 1 179  ? 9.647   10.957  -87.374 1.00 95.11  ? 328  ILE   A CB    1 
ATOM   409  C  CG1   . ILE   A 1 179  ? 10.811  10.134  -86.812 1.00 95.88  ? 328  ILE   A CG1   1 
ATOM   410  C  CG2   . ILE   A 1 179  ? 10.136  12.109  -88.243 1.00 95.61  ? 328  ILE   A CG2   1 
ATOM   411  C  CD1   . ILE   A 1 179  ? 10.457  8.695   -86.505 1.00 95.65  ? 328  ILE   A CD1   1 
ATOM   412  N  N     . GLY   A 1 180  ? 10.005  12.507  -84.473 1.00 89.85  ? 329  GLY   A N     1 
ATOM   413  C  CA    . GLY   A 1 180  ? 10.598  13.591  -83.664 1.00 86.16  ? 329  GLY   A CA    1 
ATOM   414  C  C     . GLY   A 1 180  ? 11.879  13.148  -82.978 1.00 82.35  ? 329  GLY   A C     1 
ATOM   415  O  O     . GLY   A 1 180  ? 11.936  11.986  -82.527 1.00 81.13  ? 329  GLY   A O     1 
ATOM   416  N  N     . VAL   A 1 181  ? 12.870  14.041  -82.903 1.00 79.00  ? 330  VAL   A N     1 
ATOM   417  C  CA    . VAL   A 1 181  ? 14.196  13.793  -82.261 1.00 77.95  ? 330  VAL   A CA    1 
ATOM   418  C  C     . VAL   A 1 181  ? 14.207  14.486  -80.895 1.00 74.34  ? 330  VAL   A C     1 
ATOM   419  O  O     . VAL   A 1 181  ? 13.794  15.659  -80.827 1.00 72.76  ? 330  VAL   A O     1 
ATOM   420  C  CB    . VAL   A 1 181  ? 15.353  14.285  -83.153 1.00 79.17  ? 330  VAL   A CB    1 
ATOM   421  C  CG1   . VAL   A 1 181  ? 16.711  13.965  -82.547 1.00 79.19  ? 330  VAL   A CG1   1 
ATOM   422  C  CG2   . VAL   A 1 181  ? 15.251  13.726  -84.566 1.00 80.07  ? 330  VAL   A CG2   1 
ATOM   423  N  N     . VAL   A 1 182  ? 14.666  13.783  -79.855 1.00 72.52  ? 331  VAL   A N     1 
ATOM   424  C  CA    . VAL   A 1 182  ? 14.774  14.311  -78.461 1.00 72.38  ? 331  VAL   A CA    1 
ATOM   425  C  C     . VAL   A 1 182  ? 15.816  15.426  -78.469 1.00 71.57  ? 331  VAL   A C     1 
ATOM   426  O  O     . VAL   A 1 182  ? 16.953  15.199  -78.876 1.00 72.98  ? 331  VAL   A O     1 
ATOM   427  C  CB    . VAL   A 1 182  ? 15.142  13.202  -77.455 1.00 73.20  ? 331  VAL   A CB    1 
ATOM   428  C  CG1   . VAL   A 1 182  ? 15.291  13.746  -76.041 1.00 73.86  ? 331  VAL   A CG1   1 
ATOM   429  C  CG2   . VAL   A 1 182  ? 14.139  12.059  -77.481 1.00 73.46  ? 331  VAL   A CG2   1 
ATOM   430  N  N     . PRO   A 1 183  ? 15.470  16.658  -78.030 1.00 69.76  ? 332  PRO   A N     1 
ATOM   431  C  CA    . PRO   A 1 183  ? 16.387  17.794  -78.132 1.00 69.41  ? 332  PRO   A CA    1 
ATOM   432  C  C     . PRO   A 1 183  ? 17.583  17.673  -77.175 1.00 69.39  ? 332  PRO   A C     1 
ATOM   433  O  O     . PRO   A 1 183  ? 17.474  16.962  -76.193 1.00 68.42  ? 332  PRO   A O     1 
ATOM   434  C  CB    . PRO   A 1 183  ? 15.507  19.002  -77.780 1.00 69.89  ? 332  PRO   A CB    1 
ATOM   435  C  CG    . PRO   A 1 183  ? 14.421  18.427  -76.894 1.00 70.35  ? 332  PRO   A CG    1 
ATOM   436  C  CD    . PRO   A 1 183  ? 14.189  17.021  -77.405 1.00 69.79  ? 332  PRO   A CD    1 
ATOM   437  N  N     . TRP   A 1 184  ? 18.685  18.361  -77.492 1.00 71.86  ? 333  TRP   A N     1 
ATOM   438  C  CA    . TRP   A 1 184  ? 19.962  18.321  -76.728 1.00 73.70  ? 333  TRP   A CA    1 
ATOM   439  C  C     . TRP   A 1 184  ? 20.572  19.724  -76.612 1.00 75.53  ? 333  TRP   A C     1 
ATOM   440  O  O     . TRP   A 1 184  ? 20.460  20.506  -77.578 1.00 77.74  ? 333  TRP   A O     1 
ATOM   441  C  CB    . TRP   A 1 184  ? 20.947  17.349  -77.384 1.00 74.20  ? 333  TRP   A CB    1 
ATOM   442  C  CG    . TRP   A 1 184  ? 22.307  17.357  -76.756 1.00 74.96  ? 333  TRP   A CG    1 
ATOM   443  C  CD1   . TRP   A 1 184  ? 22.741  16.567  -75.733 1.00 76.01  ? 333  TRP   A CD1   1 
ATOM   444  C  CD2   . TRP   A 1 184  ? 23.416  18.204  -77.104 1.00 75.40  ? 333  TRP   A CD2   1 
ATOM   445  N  NE1   . TRP   A 1 184  ? 24.040  16.859  -75.423 1.00 75.79  ? 333  TRP   A NE1   1 
ATOM   446  C  CE2   . TRP   A 1 184  ? 24.483  17.860  -76.246 1.00 75.32  ? 333  TRP   A CE2   1 
ATOM   447  C  CE3   . TRP   A 1 184  ? 23.613  19.216  -78.050 1.00 76.74  ? 333  TRP   A CE3   1 
ATOM   448  C  CZ2   . TRP   A 1 184  ? 25.725  18.489  -76.312 1.00 75.74  ? 333  TRP   A CZ2   1 
ATOM   449  C  CZ3   . TRP   A 1 184  ? 24.841  19.839  -78.114 1.00 77.15  ? 333  TRP   A CZ3   1 
ATOM   450  C  CH2   . TRP   A 1 184  ? 25.882  19.478  -77.256 1.00 75.69  ? 333  TRP   A CH2   1 
ATOM   451  N  N     . SER   A 1 185  ? 21.210  20.007  -75.471 1.00 76.01  ? 334  SER   A N     1 
ATOM   452  C  CA    . SER   A 1 185  ? 22.035  21.217  -75.212 1.00 75.63  ? 334  SER   A CA    1 
ATOM   453  C  C     . SER   A 1 185  ? 23.184  20.852  -74.274 1.00 75.41  ? 334  SER   A C     1 
ATOM   454  O  O     . SER   A 1 185  ? 23.018  20.011  -73.393 1.00 76.53  ? 334  SER   A O     1 
ATOM   455  C  CB    . SER   A 1 185  ? 21.200  22.342  -74.655 1.00 75.28  ? 334  SER   A CB    1 
ATOM   456  O  OG    . SER   A 1 185  ? 20.516  21.935  -73.481 1.00 74.32  ? 334  SER   A OG    1 
ATOM   457  N  N     . PRO   A 1 186  ? 24.380  21.464  -74.435 1.00 75.27  ? 335  PRO   A N     1 
ATOM   458  C  CA    . PRO   A 1 186  ? 25.541  21.123  -73.609 1.00 76.02  ? 335  PRO   A CA    1 
ATOM   459  C  C     . PRO   A 1 186  ? 25.451  21.685  -72.191 1.00 75.64  ? 335  PRO   A C     1 
ATOM   460  O  O     . PRO   A 1 186  ? 24.544  22.458  -71.885 1.00 74.42  ? 335  PRO   A O     1 
ATOM   461  C  CB    . PRO   A 1 186  ? 26.712  21.745  -74.387 1.00 75.40  ? 335  PRO   A CB    1 
ATOM   462  C  CG    . PRO   A 1 186  ? 26.096  22.938  -75.085 1.00 75.67  ? 335  PRO   A CG    1 
ATOM   463  C  CD    . PRO   A 1 186  ? 24.682  22.510  -75.424 1.00 75.55  ? 335  PRO   A CD    1 
ATOM   464  N  N     . PRO   A 1 187  ? 26.381  21.308  -71.281 1.00 76.46  ? 336  PRO   A N     1 
ATOM   465  C  CA    . PRO   A 1 187  ? 26.374  21.808  -69.903 1.00 78.72  ? 336  PRO   A CA    1 
ATOM   466  C  C     . PRO   A 1 187  ? 26.389  23.339  -69.787 1.00 79.59  ? 336  PRO   A C     1 
ATOM   467  O  O     . PRO   A 1 187  ? 27.023  23.983  -70.602 1.00 78.23  ? 336  PRO   A O     1 
ATOM   468  C  CB    . PRO   A 1 187  ? 27.670  21.235  -69.309 1.00 78.95  ? 336  PRO   A CB    1 
ATOM   469  C  CG    . PRO   A 1 187  ? 27.921  19.987  -70.119 1.00 78.18  ? 336  PRO   A CG    1 
ATOM   470  C  CD    . PRO   A 1 187  ? 27.477  20.354  -71.519 1.00 77.28  ? 336  PRO   A CD    1 
ATOM   471  N  N     . GLN   A 1 188  ? 25.697  23.868  -68.773 1.00 83.80  ? 337  GLN   A N     1 
ATOM   472  C  CA    . GLN   A 1 188  ? 25.619  25.319  -68.453 1.00 86.83  ? 337  GLN   A CA    1 
ATOM   473  C  C     . GLN   A 1 188  ? 25.820  25.506  -66.943 1.00 87.29  ? 337  GLN   A C     1 
ATOM   474  O  O     . GLN   A 1 188  ? 25.316  24.665  -66.168 1.00 87.25  ? 337  GLN   A O     1 
ATOM   475  C  CB    . GLN   A 1 188  ? 24.282  25.890  -68.927 1.00 89.19  ? 337  GLN   A CB    1 
ATOM   476  C  CG    . GLN   A 1 188  ? 24.338  27.374  -69.256 1.00 92.61  ? 337  GLN   A CG    1 
ATOM   477  C  CD    . GLN   A 1 188  ? 23.043  27.876  -69.847 1.00 95.65  ? 337  GLN   A CD    1 
ATOM   478  O  OE1   . GLN   A 1 188  ? 21.976  27.306  -69.629 1.00 97.48  ? 337  GLN   A OE1   1 
ATOM   479  N  NE2   . GLN   A 1 188  ? 23.127  28.959  -70.603 1.00 96.57  ? 337  GLN   A NE2   1 
ATOM   480  N  N     . SER   A 1 189  ? 26.523  26.574  -66.555 1.00 86.01  ? 338  SER   A N     1 
ATOM   481  C  CA    . SER   A 1 189  ? 27.028  26.832  -65.179 1.00 83.58  ? 338  SER   A CA    1 
ATOM   482  C  C     . SER   A 1 189  ? 25.877  27.120  -64.204 1.00 80.85  ? 338  SER   A C     1 
ATOM   483  O  O     . SER   A 1 189  ? 26.034  26.807  -63.008 1.00 78.42  ? 338  SER   A O     1 
ATOM   484  C  CB    . SER   A 1 189  ? 28.031  27.958  -65.185 1.00 83.88  ? 338  SER   A CB    1 
ATOM   485  O  OG    . SER   A 1 189  ? 27.500  29.103  -65.835 1.00 84.33  ? 338  SER   A OG    1 
ATOM   486  N  N     . ASN   A 1 190  ? 24.772  27.700  -64.684 1.00 78.01  ? 339  ASN   A N     1 
ATOM   487  C  CA    . ASN   A 1 190  ? 23.626  28.129  -63.834 1.00 78.82  ? 339  ASN   A CA    1 
ATOM   488  C  C     . ASN   A 1 190  ? 22.471  27.126  -63.963 1.00 78.22  ? 339  ASN   A C     1 
ATOM   489  O  O     . ASN   A 1 190  ? 21.344  27.472  -63.550 1.00 78.46  ? 339  ASN   A O     1 
ATOM   490  C  CB    . ASN   A 1 190  ? 23.179  29.553  -64.178 1.00 79.33  ? 339  ASN   A CB    1 
ATOM   491  C  CG    . ASN   A 1 190  ? 22.579  29.670  -65.563 1.00 79.04  ? 339  ASN   A CG    1 
ATOM   492  O  OD1   . ASN   A 1 190  ? 23.066  29.056  -66.511 1.00 78.03  ? 339  ASN   A OD1   1 
ATOM   493  N  ND2   . ASN   A 1 190  ? 21.523  30.456  -65.689 1.00 79.33  ? 339  ASN   A ND2   1 
ATOM   494  N  N     . TRP   A 1 191  ? 22.743  25.930  -64.497 1.00 77.62  ? 340  TRP   A N     1 
ATOM   495  C  CA    . TRP   A 1 191  ? 21.741  24.860  -64.758 1.00 74.87  ? 340  TRP   A CA    1 
ATOM   496  C  C     . TRP   A 1 191  ? 22.159  23.579  -64.031 1.00 71.88  ? 340  TRP   A C     1 
ATOM   497  O  O     . TRP   A 1 191  ? 23.351  23.222  -64.110 1.00 69.82  ? 340  TRP   A O     1 
ATOM   498  C  CB    . TRP   A 1 191  ? 21.590  24.629  -66.267 1.00 76.15  ? 340  TRP   A CB    1 
ATOM   499  C  CG    . TRP   A 1 191  ? 20.629  23.539  -66.632 1.00 76.78  ? 340  TRP   A CG    1 
ATOM   500  C  CD1   . TRP   A 1 191  ? 20.936  22.264  -67.009 1.00 77.15  ? 340  TRP   A CD1   1 
ATOM   501  C  CD2   . TRP   A 1 191  ? 19.194  23.628  -66.657 1.00 77.00  ? 340  TRP   A CD2   1 
ATOM   502  N  NE1   . TRP   A 1 191  ? 19.795  21.556  -67.268 1.00 76.90  ? 340  TRP   A NE1   1 
ATOM   503  C  CE2   . TRP   A 1 191  ? 18.710  22.365  -67.061 1.00 76.87  ? 340  TRP   A CE2   1 
ATOM   504  C  CE3   . TRP   A 1 191  ? 18.273  24.645  -66.380 1.00 77.71  ? 340  TRP   A CE3   1 
ATOM   505  C  CZ2   . TRP   A 1 191  ? 17.348  22.096  -67.194 1.00 76.80  ? 340  TRP   A CZ2   1 
ATOM   506  C  CZ3   . TRP   A 1 191  ? 16.928  24.380  -66.513 1.00 78.57  ? 340  TRP   A CZ3   1 
ATOM   507  C  CH2   . TRP   A 1 191  ? 16.474  23.122  -66.914 1.00 78.58  ? 340  TRP   A CH2   1 
ATOM   508  N  N     . ASN   A 1 192  ? 21.210  22.932  -63.346 1.00 71.01  ? 341  ASN   A N     1 
ATOM   509  C  CA    . ASN   A 1 192  ? 21.382  21.598  -62.710 1.00 69.63  ? 341  ASN   A CA    1 
ATOM   510  C  C     . ASN   A 1 192  ? 20.745  20.552  -63.621 1.00 68.05  ? 341  ASN   A C     1 
ATOM   511  O  O     . ASN   A 1 192  ? 19.522  20.449  -63.687 1.00 66.47  ? 341  ASN   A O     1 
ATOM   512  C  CB    . ASN   A 1 192  ? 20.794  21.557  -61.297 1.00 68.74  ? 341  ASN   A CB    1 
ATOM   513  C  CG    . ASN   A 1 192  ? 21.138  20.290  -60.541 1.00 68.17  ? 341  ASN   A CG    1 
ATOM   514  O  OD1   . ASN   A 1 192  ? 21.353  19.238  -61.137 1.00 69.29  ? 341  ASN   A OD1   1 
ATOM   515  N  ND2   . ASN   A 1 192  ? 21.191  20.378  -59.222 1.00 68.31  ? 341  ASN   A ND2   1 
ATOM   516  N  N     . PRO   A 1 193  ? 21.551  19.736  -64.338 1.00 67.60  ? 342  PRO   A N     1 
ATOM   517  C  CA    . PRO   A 1 193  ? 21.015  18.804  -65.331 1.00 67.82  ? 342  PRO   A CA    1 
ATOM   518  C  C     . PRO   A 1 193  ? 20.255  17.624  -64.706 1.00 66.47  ? 342  PRO   A C     1 
ATOM   519  O  O     . PRO   A 1 193  ? 19.425  17.045  -65.386 1.00 66.59  ? 342  PRO   A O     1 
ATOM   520  C  CB    . PRO   A 1 193  ? 22.272  18.315  -66.068 1.00 68.55  ? 342  PRO   A CB    1 
ATOM   521  C  CG    . PRO   A 1 193  ? 23.370  18.416  -65.030 1.00 68.79  ? 342  PRO   A CG    1 
ATOM   522  C  CD    . PRO   A 1 193  ? 23.013  19.633  -64.202 1.00 68.07  ? 342  PRO   A CD    1 
ATOM   523  N  N     . TRP   A 1 194  ? 20.544  17.313  -63.438 1.00 63.80  ? 343  TRP   A N     1 
ATOM   524  C  CA    . TRP   A 1 194  ? 19.974  16.156  -62.697 1.00 62.60  ? 343  TRP   A CA    1 
ATOM   525  C  C     . TRP   A 1 194  ? 18.568  16.496  -62.187 1.00 62.75  ? 343  TRP   A C     1 
ATOM   526  O  O     . TRP   A 1 194  ? 17.689  15.625  -62.292 1.00 61.53  ? 343  TRP   A O     1 
ATOM   527  C  CB    . TRP   A 1 194  ? 20.910  15.729  -61.561 1.00 61.58  ? 343  TRP   A CB    1 
ATOM   528  C  CG    . TRP   A 1 194  ? 22.350  15.646  -61.969 1.00 60.70  ? 343  TRP   A CG    1 
ATOM   529  C  CD1   . TRP   A 1 194  ? 23.412  16.223  -61.340 1.00 60.83  ? 343  TRP   A CD1   1 
ATOM   530  C  CD2   . TRP   A 1 194  ? 22.889  14.967  -63.118 1.00 60.41  ? 343  TRP   A CD2   1 
ATOM   531  N  NE1   . TRP   A 1 194  ? 24.572  15.942  -62.007 1.00 59.94  ? 343  TRP   A NE1   1 
ATOM   532  C  CE2   . TRP   A 1 194  ? 24.285  15.172  -63.101 1.00 59.65  ? 343  TRP   A CE2   1 
ATOM   533  C  CE3   . TRP   A 1 194  ? 22.337  14.200  -64.151 1.00 60.59  ? 343  TRP   A CE3   1 
ATOM   534  C  CZ2   . TRP   A 1 194  ? 25.129  14.639  -64.076 1.00 59.14  ? 343  TRP   A CZ2   1 
ATOM   535  C  CZ3   . TRP   A 1 194  ? 23.171  13.678  -65.115 1.00 59.82  ? 343  TRP   A CZ3   1 
ATOM   536  C  CH2   . TRP   A 1 194  ? 24.549  13.893  -65.075 1.00 58.34  ? 343  TRP   A CH2   1 
ATOM   537  N  N     . THR   A 1 195  ? 18.366  17.713  -61.668 1.00 64.07  ? 344  THR   A N     1 
ATOM   538  C  CA    . THR   A 1 195  ? 17.061  18.215  -61.154 1.00 64.40  ? 344  THR   A CA    1 
ATOM   539  C  C     . THR   A 1 195  ? 16.285  18.912  -62.281 1.00 65.84  ? 344  THR   A C     1 
ATOM   540  O  O     . THR   A 1 195  ? 15.103  19.239  -62.057 1.00 65.39  ? 344  THR   A O     1 
ATOM   541  C  CB    . THR   A 1 195  ? 17.254  19.148  -59.951 1.00 63.95  ? 344  THR   A CB    1 
ATOM   542  O  OG1   . THR   A 1 195  ? 18.027  20.271  -60.371 1.00 64.42  ? 344  THR   A OG1   1 
ATOM   543  C  CG2   . THR   A 1 195  ? 17.939  18.478  -58.780 1.00 63.81  ? 344  THR   A CG2   1 
ATOM   544  N  N     . SER   A 1 196  ? 16.924  19.133  -63.437 1.00 68.09  ? 345  SER   A N     1 
ATOM   545  C  CA    . SER   A 1 196  ? 16.322  19.746  -64.653 1.00 69.98  ? 345  SER   A CA    1 
ATOM   546  C  C     . SER   A 1 196  ? 15.702  21.104  -64.303 1.00 72.17  ? 345  SER   A C     1 
ATOM   547  O  O     . SER   A 1 196  ? 14.596  21.400  -64.802 1.00 72.49  ? 345  SER   A O     1 
ATOM   548  C  CB    . SER   A 1 196  ? 15.308  18.821  -65.278 1.00 69.26  ? 345  SER   A CB    1 
ATOM   549  O  OG    . SER   A 1 196  ? 15.904  17.580  -65.621 1.00 69.84  ? 345  SER   A OG    1 
ATOM   550  N  N     . SER   A 1 197  ? 16.399  21.895  -63.481 1.00 75.48  ? 346  SER   A N     1 
ATOM   551  C  CA    . SER   A 1 197  ? 15.939  23.209  -62.958 1.00 77.59  ? 346  SER   A CA    1 
ATOM   552  C  C     . SER   A 1 197  ? 17.096  24.215  -62.956 1.00 79.50  ? 346  SER   A C     1 
ATOM   553  O  O     . SER   A 1 197  ? 18.267  23.780  -63.015 1.00 78.54  ? 346  SER   A O     1 
ATOM   554  C  CB    . SER   A 1 197  ? 15.352  23.056  -61.581 1.00 78.36  ? 346  SER   A CB    1 
ATOM   555  O  OG    . SER   A 1 197  ? 16.312  22.523  -60.682 1.00 78.91  ? 346  SER   A OG    1 
ATOM   556  N  N     . ASN   A 1 198  ? 16.765  25.508  -62.889 1.00 82.09  ? 347  ASN   A N     1 
ATOM   557  C  CA    . ASN   A 1 198  ? 17.740  26.628  -62.789 1.00 82.76  ? 347  ASN   A CA    1 
ATOM   558  C  C     . ASN   A 1 198  ? 18.320  26.660  -61.372 1.00 84.84  ? 347  ASN   A C     1 
ATOM   559  O  O     . ASN   A 1 198  ? 17.627  26.210  -60.436 1.00 82.17  ? 347  ASN   A O     1 
ATOM   560  C  CB    . ASN   A 1 198  ? 17.104  27.977  -63.136 1.00 82.65  ? 347  ASN   A CB    1 
ATOM   561  C  CG    . ASN   A 1 198  ? 16.791  28.127  -64.610 1.00 83.50  ? 347  ASN   A CG    1 
ATOM   562  O  OD1   . ASN   A 1 198  ? 15.637  28.321  -64.987 1.00 83.87  ? 347  ASN   A OD1   1 
ATOM   563  N  ND2   . ASN   A 1 198  ? 17.810  28.039  -65.450 1.00 83.02  ? 347  ASN   A ND2   1 
ATOM   564  N  N     . ILE   A 1 199  ? 19.551  27.163  -61.237 1.00 88.99  ? 348  ILE   A N     1 
ATOM   565  C  CA    . ILE   A 1 199  ? 20.210  27.478  -59.935 1.00 91.02  ? 348  ILE   A CA    1 
ATOM   566  C  C     . ILE   A 1 199  ? 20.100  28.994  -59.724 1.00 95.55  ? 348  ILE   A C     1 
ATOM   567  O  O     . ILE   A 1 199  ? 20.898  29.734  -60.333 1.00 97.18  ? 348  ILE   A O     1 
ATOM   568  C  CB    . ILE   A 1 199  ? 21.671  26.979  -59.916 1.00 89.60  ? 348  ILE   A CB    1 
ATOM   569  C  CG1   . ILE   A 1 199  ? 21.787  25.536  -60.418 1.00 89.07  ? 348  ILE   A CG1   1 
ATOM   570  C  CG2   . ILE   A 1 199  ? 22.280  27.143  -58.530 1.00 88.96  ? 348  ILE   A CG2   1 
ATOM   571  C  CD1   . ILE   A 1 199  ? 23.207  25.073  -60.649 1.00 88.63  ? 348  ILE   A CD1   1 
ATOM   572  N  N     . ASP   A 1 200  ? 19.120  29.430  -58.923 1.00 100.32 ? 349  ASP   A N     1 
ATOM   573  C  CA    . ASP   A 1 200  ? 18.800  30.862  -58.667 1.00 102.12 ? 349  ASP   A CA    1 
ATOM   574  C  C     . ASP   A 1 200  ? 19.079  31.197  -57.196 1.00 104.23 ? 349  ASP   A C     1 
ATOM   575  O  O     . ASP   A 1 200  ? 18.515  32.194  -56.702 1.00 106.49 ? 349  ASP   A O     1 
ATOM   576  C  CB    . ASP   A 1 200  ? 17.351  31.172  -59.056 1.00 101.43 ? 349  ASP   A CB    1 
ATOM   577  C  CG    . ASP   A 1 200  ? 17.033  30.916  -60.521 1.00 101.67 ? 349  ASP   A CG    1 
ATOM   578  O  OD1   . ASP   A 1 200  ? 17.979  30.892  -61.335 1.00 100.94 ? 349  ASP   A OD1   1 
ATOM   579  O  OD2   . ASP   A 1 200  ? 15.840  30.742  -60.837 1.00 101.38 ? 349  ASP   A OD2   1 
ATOM   580  N  N     . GLU   A 1 201  ? 19.918  30.396  -56.529 1.00 105.98 ? 350  GLU   A N     1 
ATOM   581  C  CA    . GLU   A 1 201  ? 20.357  30.590  -55.120 1.00 106.71 ? 350  GLU   A CA    1 
ATOM   582  C  C     . GLU   A 1 201  ? 21.774  30.025  -54.961 1.00 107.34 ? 350  GLU   A C     1 
ATOM   583  O  O     . GLU   A 1 201  ? 22.177  29.196  -55.800 1.00 107.24 ? 350  GLU   A O     1 
ATOM   584  C  CB    . GLU   A 1 201  ? 19.390  29.908  -54.149 1.00 107.78 ? 350  GLU   A CB    1 
ATOM   585  C  CG    . GLU   A 1 201  ? 18.000  30.523  -54.135 1.00 109.65 ? 350  GLU   A CG    1 
ATOM   586  C  CD    . GLU   A 1 201  ? 17.083  30.025  -53.030 1.00 110.63 ? 350  GLU   A CD    1 
ATOM   587  O  OE1   . GLU   A 1 201  ? 17.261  28.873  -52.585 1.00 111.97 ? 350  GLU   A OE1   1 
ATOM   588  O  OE2   . GLU   A 1 201  ? 16.190  30.793  -52.617 1.00 109.23 ? 350  GLU   A OE2   1 
ATOM   589  N  N     . GLY   A 1 202  ? 22.495  30.463  -53.925 1.00 109.95 ? 351  GLY   A N     1 
ATOM   590  C  CA    . GLY   A 1 202  ? 23.866  30.011  -53.619 1.00 111.45 ? 351  GLY   A CA    1 
ATOM   591  C  C     . GLY   A 1 202  ? 24.903  30.679  -54.519 1.00 112.35 ? 351  GLY   A C     1 
ATOM   592  O  O     . GLY   A 1 202  ? 24.561  31.512  -55.358 1.00 109.51 ? 351  GLY   A O     1 
ATOM   593  N  N     . PRO   A 1 203  ? 26.201  30.325  -54.376 1.00 114.25 ? 352  PRO   A N     1 
ATOM   594  C  CA    . PRO   A 1 203  ? 27.274  30.990  -55.119 1.00 115.73 ? 352  PRO   A CA    1 
ATOM   595  C  C     . PRO   A 1 203  ? 27.317  30.657  -56.620 1.00 116.18 ? 352  PRO   A C     1 
ATOM   596  O  O     . PRO   A 1 203  ? 27.797  31.480  -57.380 1.00 115.06 ? 352  PRO   A O     1 
ATOM   597  C  CB    . PRO   A 1 203  ? 28.548  30.477  -54.427 1.00 114.76 ? 352  PRO   A CB    1 
ATOM   598  C  CG    . PRO   A 1 203  ? 28.157  29.119  -53.885 1.00 114.13 ? 352  PRO   A CG    1 
ATOM   599  C  CD    . PRO   A 1 203  ? 26.702  29.263  -53.488 1.00 113.29 ? 352  PRO   A CD    1 
ATOM   600  N  N     . LEU   A 1 204  ? 26.806  29.484  -57.009 1.00 117.10 ? 353  LEU   A N     1 
ATOM   601  C  CA    . LEU   A 1 204  ? 26.924  28.924  -58.384 1.00 117.08 ? 353  LEU   A CA    1 
ATOM   602  C  C     . LEU   A 1 204  ? 25.831  29.498  -59.298 1.00 117.50 ? 353  LEU   A C     1 
ATOM   603  O  O     . LEU   A 1 204  ? 25.820  29.130  -60.491 1.00 118.46 ? 353  LEU   A O     1 
ATOM   604  C  CB    . LEU   A 1 204  ? 26.832  27.396  -58.307 1.00 117.46 ? 353  LEU   A CB    1 
ATOM   605  C  CG    . LEU   A 1 204  ? 27.861  26.714  -57.404 1.00 118.27 ? 353  LEU   A CG    1 
ATOM   606  C  CD1   . LEU   A 1 204  ? 27.582  25.223  -57.293 1.00 118.53 ? 353  LEU   A CD1   1 
ATOM   607  C  CD2   . LEU   A 1 204  ? 29.276  26.955  -57.907 1.00 118.53 ? 353  LEU   A CD2   1 
ATOM   608  N  N     . ALA   A 1 205  ? 24.955  30.363  -58.771 1.00 116.10 ? 354  ALA   A N     1 
ATOM   609  C  CA    . ALA   A 1 205  ? 23.846  31.013  -59.513 1.00 113.96 ? 354  ALA   A CA    1 
ATOM   610  C  C     . ALA   A 1 205  ? 24.403  32.035  -60.513 1.00 112.64 ? 354  ALA   A C     1 
ATOM   611  O  O     . ALA   A 1 205  ? 23.870  32.109  -61.637 1.00 113.61 ? 354  ALA   A O     1 
ATOM   612  C  CB    . ALA   A 1 205  ? 22.888  31.662  -58.543 1.00 113.35 ? 354  ALA   A CB    1 
ATOM   613  N  N     . TYR   A 1 206  ? 25.434  32.786  -60.111 1.00 110.94 ? 355  TYR   A N     1 
ATOM   614  C  CA    . TYR   A 1 206  ? 26.049  33.902  -60.882 1.00 107.19 ? 355  TYR   A CA    1 
ATOM   615  C  C     . TYR   A 1 206  ? 27.460  33.523  -61.357 1.00 103.13 ? 355  TYR   A C     1 
ATOM   616  O  O     . TYR   A 1 206  ? 27.842  33.959  -62.461 1.00 100.16 ? 355  TYR   A O     1 
ATOM   617  C  CB    . TYR   A 1 206  ? 26.074  35.182  -60.041 1.00 106.58 ? 355  TYR   A CB    1 
ATOM   618  C  CG    . TYR   A 1 206  ? 26.533  34.995  -58.616 1.00 105.94 ? 355  TYR   A CG    1 
ATOM   619  C  CD1   . TYR   A 1 206  ? 27.879  34.877  -58.307 1.00 105.26 ? 355  TYR   A CD1   1 
ATOM   620  C  CD2   . TYR   A 1 206  ? 25.621  34.922  -57.574 1.00 105.30 ? 355  TYR   A CD2   1 
ATOM   621  C  CE1   . TYR   A 1 206  ? 28.309  34.695  -57.003 1.00 106.51 ? 355  TYR   A CE1   1 
ATOM   622  C  CE2   . TYR   A 1 206  ? 26.034  34.743  -56.263 1.00 106.80 ? 355  TYR   A CE2   1 
ATOM   623  C  CZ    . TYR   A 1 206  ? 27.384  34.628  -55.976 1.00 106.41 ? 355  TYR   A CZ    1 
ATOM   624  O  OH    . TYR   A 1 206  ? 27.804  34.450  -54.689 1.00 101.15 ? 355  TYR   A OH    1 
ATOM   625  N  N     . ALA   A 1 207  ? 28.204  32.749  -60.556 1.00 101.05 ? 356  ALA   A N     1 
ATOM   626  C  CA    . ALA   A 1 207  ? 29.622  32.375  -60.788 1.00 101.72 ? 356  ALA   A CA    1 
ATOM   627  C  C     . ALA   A 1 207  ? 29.822  31.912  -62.237 1.00 102.06 ? 356  ALA   A C     1 
ATOM   628  O  O     . ALA   A 1 207  ? 28.943  31.199  -62.761 1.00 102.53 ? 356  ALA   A O     1 
ATOM   629  C  CB    . ALA   A 1 207  ? 30.040  31.304  -59.811 1.00 101.38 ? 356  ALA   A CB    1 
ATOM   630  N  N     . THR   A 1 208  ? 30.944  32.305  -62.850 1.00 102.73 ? 357  THR   A N     1 
ATOM   631  C  CA    . THR   A 1 208  ? 31.305  31.997  -64.260 1.00 100.95 ? 357  THR   A CA    1 
ATOM   632  C  C     . THR   A 1 208  ? 31.895  30.590  -64.339 1.00 100.39 ? 357  THR   A C     1 
ATOM   633  O  O     . THR   A 1 208  ? 32.372  30.062  -63.335 1.00 100.86 ? 357  THR   A O     1 
ATOM   634  C  CB    . THR   A 1 208  ? 32.280  33.042  -64.819 1.00 99.17  ? 357  THR   A CB    1 
ATOM   635  O  OG1   . THR   A 1 208  ? 33.458  33.022  -64.012 1.00 97.40  ? 357  THR   A OG1   1 
ATOM   636  C  CG2   . THR   A 1 208  ? 31.698  34.438  -64.846 1.00 97.75  ? 357  THR   A CG2   1 
ATOM   637  N  N     . PRO   A 1 209  ? 31.877  29.939  -65.528 1.00 97.78  ? 358  PRO   A N     1 
ATOM   638  C  CA    . PRO   A 1 209  ? 32.499  28.625  -65.705 1.00 96.83  ? 358  PRO   A CA    1 
ATOM   639  C  C     . PRO   A 1 209  ? 33.975  28.564  -65.275 1.00 96.20  ? 358  PRO   A C     1 
ATOM   640  O  O     . PRO   A 1 209  ? 34.375  27.558  -64.714 1.00 94.35  ? 358  PRO   A O     1 
ATOM   641  C  CB    . PRO   A 1 209  ? 32.395  28.375  -67.219 1.00 97.05  ? 358  PRO   A CB    1 
ATOM   642  C  CG    . PRO   A 1 209  ? 31.205  29.201  -67.655 1.00 97.28  ? 358  PRO   A CG    1 
ATOM   643  C  CD    . PRO   A 1 209  ? 31.232  30.423  -66.760 1.00 97.84  ? 358  PRO   A CD    1 
ATOM   644  N  N     . GLU   A 1 210  ? 34.731  29.636  -65.542 1.00 95.79  ? 359  GLU   A N     1 
ATOM   645  C  CA    . GLU   A 1 210  ? 36.196  29.733  -65.293 1.00 94.10  ? 359  GLU   A CA    1 
ATOM   646  C  C     . GLU   A 1 210  ? 36.475  29.571  -63.794 1.00 92.50  ? 359  GLU   A C     1 
ATOM   647  O  O     . GLU   A 1 210  ? 37.416  28.830  -63.450 1.00 90.21  ? 359  GLU   A O     1 
ATOM   648  C  CB    . GLU   A 1 210  ? 36.751  31.065  -65.807 1.00 95.32  ? 359  GLU   A CB    1 
ATOM   649  C  CG    . GLU   A 1 210  ? 36.784  31.178  -67.324 1.00 95.63  ? 359  GLU   A CG    1 
ATOM   650  C  CD    . GLU   A 1 210  ? 35.477  31.577  -67.994 1.00 94.70  ? 359  GLU   A CD    1 
ATOM   651  O  OE1   . GLU   A 1 210  ? 34.456  31.696  -67.286 1.00 93.41  ? 359  GLU   A OE1   1 
ATOM   652  O  OE2   . GLU   A 1 210  ? 35.484  31.768  -69.226 1.00 92.32  ? 359  GLU   A OE2   1 
ATOM   653  N  N     . GLN   A 1 211  ? 35.691  30.244  -62.944 1.00 94.48  ? 360  GLN   A N     1 
ATOM   654  C  CA    . GLN   A 1 211  ? 35.798  30.171  -61.460 1.00 98.75  ? 360  GLN   A CA    1 
ATOM   655  C  C     . GLN   A 1 211  ? 35.547  28.731  -61.002 1.00 97.69  ? 360  GLN   A C     1 
ATOM   656  O  O     . GLN   A 1 211  ? 36.398  28.184  -60.271 1.00 96.69  ? 360  GLN   A O     1 
ATOM   657  C  CB    . GLN   A 1 211  ? 34.798  31.116  -60.789 1.00 103.39 ? 360  GLN   A CB    1 
ATOM   658  C  CG    . GLN   A 1 211  ? 35.234  32.574  -60.791 1.00 106.55 ? 360  GLN   A CG    1 
ATOM   659  C  CD    . GLN   A 1 211  ? 34.347  33.430  -59.920 1.00 109.39 ? 360  GLN   A CD    1 
ATOM   660  O  OE1   . GLN   A 1 211  ? 33.137  33.224  -59.840 1.00 110.48 ? 360  GLN   A OE1   1 
ATOM   661  N  NE2   . GLN   A 1 211  ? 34.946  34.405  -59.257 1.00 111.52 ? 360  GLN   A NE2   1 
ATOM   662  N  N     . ILE   A 1 212  ? 34.420  28.151  -61.431 1.00 94.82  ? 361  ILE   A N     1 
ATOM   663  C  CA    . ILE   A 1 212  ? 33.966  26.777  -61.060 1.00 91.44  ? 361  ILE   A CA    1 
ATOM   664  C  C     . ILE   A 1 212  ? 35.046  25.771  -61.477 1.00 89.12  ? 361  ILE   A C     1 
ATOM   665  O  O     . ILE   A 1 212  ? 35.367  24.883  -60.661 1.00 87.96  ? 361  ILE   A O     1 
ATOM   666  C  CB    . ILE   A 1 212  ? 32.593  26.462  -61.693 1.00 91.88  ? 361  ILE   A CB    1 
ATOM   667  C  CG1   . ILE   A 1 212  ? 31.489  27.363  -61.131 1.00 92.13  ? 361  ILE   A CG1   1 
ATOM   668  C  CG2   . ILE   A 1 212  ? 32.244  24.988  -61.534 1.00 92.35  ? 361  ILE   A CG2   1 
ATOM   669  C  CD1   . ILE   A 1 212  ? 30.257  27.449  -62.004 1.00 91.65  ? 361  ILE   A CD1   1 
ATOM   670  N  N     . SER   A 1 213  ? 35.590  25.919  -62.690 1.00 87.19  ? 362  SER   A N     1 
ATOM   671  C  CA    . SER   A 1 213  ? 36.626  25.029  -63.283 1.00 87.60  ? 362  SER   A CA    1 
ATOM   672  C  C     . SER   A 1 213  ? 37.900  25.038  -62.426 1.00 89.27  ? 362  SER   A C     1 
ATOM   673  O  O     . SER   A 1 213  ? 38.490  23.953  -62.235 1.00 87.30  ? 362  SER   A O     1 
ATOM   674  C  CB    . SER   A 1 213  ? 36.922  25.415  -64.711 1.00 86.06  ? 362  SER   A CB    1 
ATOM   675  O  OG    . SER   A 1 213  ? 35.785  25.219  -65.538 1.00 83.45  ? 362  SER   A OG    1 
ATOM   676  N  N     . MET   A 1 214  ? 38.304  26.214  -61.930 1.00 92.09  ? 363  MET   A N     1 
ATOM   677  C  CA    . MET   A 1 214  ? 39.528  26.401  -61.101 1.00 92.63  ? 363  MET   A CA    1 
ATOM   678  C  C     . MET   A 1 214  ? 39.255  25.898  -59.678 1.00 88.24  ? 363  MET   A C     1 
ATOM   679  O  O     . MET   A 1 214  ? 40.122  25.188  -59.132 1.00 86.35  ? 363  MET   A O     1 
ATOM   680  C  CB    . MET   A 1 214  ? 39.953  27.873  -61.055 1.00 96.72  ? 363  MET   A CB    1 
ATOM   681  C  CG    . MET   A 1 214  ? 41.458  28.065  -60.935 1.00 99.31  ? 363  MET   A CG    1 
ATOM   682  S  SD    . MET   A 1 214  ? 41.923  29.673  -60.227 1.00 104.75 ? 363  MET   A SD    1 
ATOM   683  C  CE    . MET   A 1 214  ? 40.916  30.787  -61.206 1.00 101.90 ? 363  MET   A CE    1 
ATOM   684  N  N     . ASP   A 1 215  ? 38.097  26.256  -59.111 1.00 85.72  ? 364  ASP   A N     1 
ATOM   685  C  CA    . ASP   A 1 215  ? 37.646  25.841  -57.752 1.00 86.14  ? 364  ASP   A CA    1 
ATOM   686  C  C     . ASP   A 1 215  ? 37.657  24.310  -57.644 1.00 85.13  ? 364  ASP   A C     1 
ATOM   687  O  O     . ASP   A 1 215  ? 38.131  23.798  -56.610 1.00 83.01  ? 364  ASP   A O     1 
ATOM   688  C  CB    . ASP   A 1 215  ? 36.251  26.383  -57.428 1.00 86.56  ? 364  ASP   A CB    1 
ATOM   689  C  CG    . ASP   A 1 215  ? 36.229  27.835  -56.978 1.00 85.87  ? 364  ASP   A CG    1 
ATOM   690  O  OD1   . ASP   A 1 215  ? 37.034  28.629  -57.504 1.00 86.23  ? 364  ASP   A OD1   1 
ATOM   691  O  OD2   . ASP   A 1 215  ? 35.404  28.159  -56.102 1.00 83.93  ? 364  ASP   A OD2   1 
ATOM   692  N  N     . LEU   A 1 216  ? 37.144  23.617  -58.667 1.00 85.79  ? 365  LEU   A N     1 
ATOM   693  C  CA    . LEU   A 1 216  ? 37.027  22.131  -58.708 1.00 84.66  ? 365  LEU   A CA    1 
ATOM   694  C  C     . LEU   A 1 216  ? 38.408  21.504  -58.934 1.00 83.58  ? 365  LEU   A C     1 
ATOM   695  O  O     . LEU   A 1 216  ? 38.665  20.433  -58.350 1.00 81.20  ? 365  LEU   A O     1 
ATOM   696  C  CB    . LEU   A 1 216  ? 36.045  21.724  -59.812 1.00 83.65  ? 365  LEU   A CB    1 
ATOM   697  C  CG    . LEU   A 1 216  ? 34.570  21.992  -59.512 1.00 82.26  ? 365  LEU   A CG    1 
ATOM   698  C  CD1   . LEU   A 1 216  ? 33.731  21.881  -60.776 1.00 81.46  ? 365  LEU   A CD1   1 
ATOM   699  C  CD2   . LEU   A 1 216  ? 34.049  21.048  -58.439 1.00 81.50  ? 365  LEU   A CD2   1 
ATOM   700  N  N     . LYS   A 1 217  ? 39.258  22.142  -59.748 1.00 84.48  ? 366  LYS   A N     1 
ATOM   701  C  CA    . LYS   A 1 217  ? 40.639  21.672  -60.047 1.00 85.91  ? 366  LYS   A CA    1 
ATOM   702  C  C     . LYS   A 1 217  ? 41.487  21.734  -58.770 1.00 84.87  ? 366  LYS   A C     1 
ATOM   703  O  O     . LYS   A 1 217  ? 42.054  20.690  -58.392 1.00 84.24  ? 366  LYS   A O     1 
ATOM   704  C  CB    . LYS   A 1 217  ? 41.278  22.512  -61.157 1.00 86.05  ? 366  LYS   A CB    1 
ATOM   705  C  CG    . LYS   A 1 217  ? 42.651  22.034  -61.612 1.00 85.69  ? 366  LYS   A CG    1 
ATOM   706  C  CD    . LYS   A 1 217  ? 43.251  22.878  -62.712 1.00 87.14  ? 366  LYS   A CD    1 
ATOM   707  C  CE    . LYS   A 1 217  ? 44.569  22.334  -63.216 1.00 88.49  ? 366  LYS   A CE    1 
ATOM   708  N  NZ    . LYS   A 1 217  ? 45.138  23.185  -64.288 1.00 89.78  ? 366  LYS   A NZ    1 
ATOM   709  N  N     . ASN   A 1 218  ? 41.563  22.913  -58.143 1.00 84.93  ? 367  ASN   A N     1 
ATOM   710  C  CA    . ASN   A 1 218  ? 42.378  23.189  -56.927 1.00 85.15  ? 367  ASN   A CA    1 
ATOM   711  C  C     . ASN   A 1 218  ? 41.996  22.207  -55.813 1.00 84.39  ? 367  ASN   A C     1 
ATOM   712  O  O     . ASN   A 1 218  ? 42.910  21.715  -55.118 1.00 83.86  ? 367  ASN   A O     1 
ATOM   713  C  CB    . ASN   A 1 218  ? 42.214  24.635  -56.451 1.00 85.22  ? 367  ASN   A CB    1 
ATOM   714  C  CG    . ASN   A 1 218  ? 42.817  25.653  -57.398 1.00 85.85  ? 367  ASN   A CG    1 
ATOM   715  O  OD1   . ASN   A 1 218  ? 43.837  25.394  -58.034 1.00 86.90  ? 367  ASN   A OD1   1 
ATOM   716  N  ND2   . ASN   A 1 218  ? 42.200  26.820  -57.492 1.00 84.70  ? 367  ASN   A ND2   1 
ATOM   717  N  N     . GLU   A 1 219  ? 40.693  21.947  -55.661 1.00 85.09  ? 368  GLU   A N     1 
ATOM   718  C  CA    . GLU   A 1 219  ? 40.105  21.017  -54.658 1.00 86.10  ? 368  GLU   A CA    1 
ATOM   719  C  C     . GLU   A 1 219  ? 40.656  19.600  -54.875 1.00 85.00  ? 368  GLU   A C     1 
ATOM   720  O  O     . GLU   A 1 219  ? 40.991  18.943  -53.869 1.00 80.88  ? 368  GLU   A O     1 
ATOM   721  C  CB    . GLU   A 1 219  ? 38.579  21.057  -54.776 1.00 87.91  ? 368  GLU   A CB    1 
ATOM   722  C  CG    . GLU   A 1 219  ? 37.848  20.196  -53.763 1.00 89.39  ? 368  GLU   A CG    1 
ATOM   723  C  CD    . GLU   A 1 219  ? 36.397  19.933  -54.127 1.00 90.98  ? 368  GLU   A CD    1 
ATOM   724  O  OE1   . GLU   A 1 219  ? 35.949  18.785  -53.954 1.00 91.87  ? 368  GLU   A OE1   1 
ATOM   725  O  OE2   . GLU   A 1 219  ? 35.722  20.875  -54.593 1.00 92.64  ? 368  GLU   A OE2   1 
ATOM   726  N  N     . LEU   A 1 220  ? 40.742  19.157  -56.137 1.00 86.07  ? 369  LEU   A N     1 
ATOM   727  C  CA    . LEU   A 1 220  ? 41.184  17.789  -56.533 1.00 86.67  ? 369  LEU   A CA    1 
ATOM   728  C  C     . LEU   A 1 220  ? 42.708  17.672  -56.393 1.00 89.67  ? 369  LEU   A C     1 
ATOM   729  O  O     . LEU   A 1 220  ? 43.169  16.622  -55.903 1.00 90.15  ? 369  LEU   A O     1 
ATOM   730  C  CB    . LEU   A 1 220  ? 40.737  17.505  -57.973 1.00 84.63  ? 369  LEU   A CB    1 
ATOM   731  C  CG    . LEU   A 1 220  ? 41.052  16.106  -58.505 1.00 82.08  ? 369  LEU   A CG    1 
ATOM   732  C  CD1   . LEU   A 1 220  ? 40.278  15.042  -57.741 1.00 81.13  ? 369  LEU   A CD1   1 
ATOM   733  C  CD2   . LEU   A 1 220  ? 40.756  16.011  -59.994 1.00 81.02  ? 369  LEU   A CD2   1 
ATOM   734  N  N     . MET   A 1 221  ? 43.454  18.696  -56.824 1.00 92.98  ? 370  MET   A N     1 
ATOM   735  C  CA    . MET   A 1 221  ? 44.938  18.757  -56.713 1.00 95.33  ? 370  MET   A CA    1 
ATOM   736  C  C     . MET   A 1 221  ? 45.340  18.651  -55.236 1.00 92.79  ? 370  MET   A C     1 
ATOM   737  O  O     . MET   A 1 221  ? 46.308  17.920  -54.944 1.00 91.03  ? 370  MET   A O     1 
ATOM   738  C  CB    . MET   A 1 221  ? 45.493  20.061  -57.298 1.00 101.09 ? 370  MET   A CB    1 
ATOM   739  C  CG    . MET   A 1 221  ? 45.467  20.103  -58.816 1.00 106.44 ? 370  MET   A CG    1 
ATOM   740  S  SD    . MET   A 1 221  ? 46.444  21.468  -59.508 1.00 114.20 ? 370  MET   A SD    1 
ATOM   741  C  CE    . MET   A 1 221  ? 45.569  22.887  -58.849 1.00 110.88 ? 370  MET   A CE    1 
ATOM   742  N  N     . TYR   A 1 222  ? 44.614  19.343  -54.350 1.00 90.57  ? 371  TYR   A N     1 
ATOM   743  C  CA    . TYR   A 1 222  ? 44.875  19.389  -52.885 1.00 91.80  ? 371  TYR   A CA    1 
ATOM   744  C  C     . TYR   A 1 222  ? 44.531  18.040  -52.237 1.00 92.24  ? 371  TYR   A C     1 
ATOM   745  O  O     . TYR   A 1 222  ? 45.229  17.640  -51.282 1.00 91.75  ? 371  TYR   A O     1 
ATOM   746  C  CB    . TYR   A 1 222  ? 44.090  20.521  -52.218 1.00 91.83  ? 371  TYR   A CB    1 
ATOM   747  C  CG    . TYR   A 1 222  ? 44.331  20.621  -50.733 1.00 93.44  ? 371  TYR   A CG    1 
ATOM   748  C  CD1   . TYR   A 1 222  ? 45.568  21.006  -50.239 1.00 93.58  ? 371  TYR   A CD1   1 
ATOM   749  C  CD2   . TYR   A 1 222  ? 43.342  20.296  -49.818 1.00 94.34  ? 371  TYR   A CD2   1 
ATOM   750  C  CE1   . TYR   A 1 222  ? 45.811  21.083  -48.878 1.00 93.49  ? 371  TYR   A CE1   1 
ATOM   751  C  CE2   . TYR   A 1 222  ? 43.568  20.368  -48.453 1.00 94.80  ? 371  TYR   A CE2   1 
ATOM   752  C  CZ    . TYR   A 1 222  ? 44.808  20.764  -47.981 1.00 94.88  ? 371  TYR   A CZ    1 
ATOM   753  O  OH    . TYR   A 1 222  ? 45.046  20.835  -46.640 1.00 96.67  ? 371  TYR   A OH    1 
ATOM   754  N  N     . GLN   A 1 223  ? 43.482  17.372  -52.727 1.00 92.30  ? 372  GLN   A N     1 
ATOM   755  C  CA    . GLN   A 1 223  ? 43.002  16.061  -52.208 1.00 92.43  ? 372  GLN   A CA    1 
ATOM   756  C  C     . GLN   A 1 223  ? 44.068  14.991  -52.481 1.00 91.77  ? 372  GLN   A C     1 
ATOM   757  O  O     . GLN   A 1 223  ? 44.430  14.269  -51.531 1.00 89.29  ? 372  GLN   A O     1 
ATOM   758  C  CB    . GLN   A 1 223  ? 41.660  15.699  -52.850 1.00 93.94  ? 372  GLN   A CB    1 
ATOM   759  C  CG    . GLN   A 1 223  ? 40.877  14.638  -52.090 1.00 93.51  ? 372  GLN   A CG    1 
ATOM   760  C  CD    . GLN   A 1 223  ? 39.638  14.194  -52.830 1.00 92.46  ? 372  GLN   A CD    1 
ATOM   761  O  OE1   . GLN   A 1 223  ? 39.352  14.647  -53.937 1.00 89.38  ? 372  GLN   A OE1   1 
ATOM   762  N  NE2   . GLN   A 1 223  ? 38.885  13.295  -52.217 1.00 93.01  ? 372  GLN   A NE2   1 
ATOM   763  N  N     . LEU   A 1 224  ? 44.544  14.905  -53.731 1.00 94.02  ? 373  LEU   A N     1 
ATOM   764  C  CA    . LEU   A 1 224  ? 45.609  13.965  -54.189 1.00 96.32  ? 373  LEU   A CA    1 
ATOM   765  C  C     . LEU   A 1 224  ? 46.918  14.257  -53.444 1.00 95.30  ? 373  LEU   A C     1 
ATOM   766  O  O     . LEU   A 1 224  ? 47.649  13.293  -53.135 1.00 91.19  ? 373  LEU   A O     1 
ATOM   767  C  CB    . LEU   A 1 224  ? 45.806  14.108  -55.704 1.00 98.68  ? 373  LEU   A CB    1 
ATOM   768  C  CG    . LEU   A 1 224  ? 45.004  13.144  -56.580 1.00 99.88  ? 373  LEU   A CG    1 
ATOM   769  C  CD1   . LEU   A 1 224  ? 43.507  13.362  -56.421 1.00 100.70 ? 373  LEU   A CD1   1 
ATOM   770  C  CD2   . LEU   A 1 224  ? 45.407  13.282  -58.041 1.00 99.69  ? 373  LEU   A CD2   1 
ATOM   771  N  N     . GLU   A 1 225  ? 47.198  15.541  -53.194 1.00 96.82  ? 374  GLU   A N     1 
ATOM   772  C  CA    . GLU   A 1 225  ? 48.404  16.046  -52.480 1.00 97.47  ? 374  GLU   A CA    1 
ATOM   773  C  C     . GLU   A 1 225  ? 48.430  15.499  -51.045 1.00 95.68  ? 374  GLU   A C     1 
ATOM   774  O  O     . GLU   A 1 225  ? 49.521  15.094  -50.595 1.00 93.18  ? 374  GLU   A O     1 
ATOM   775  C  CB    . GLU   A 1 225  ? 48.406  17.578  -52.507 1.00 99.96  ? 374  GLU   A CB    1 
ATOM   776  C  CG    . GLU   A 1 225  ? 49.479  18.227  -51.648 1.00 102.75 ? 374  GLU   A CG    1 
ATOM   777  C  CD    . GLU   A 1 225  ? 49.228  19.697  -51.351 1.00 104.68 ? 374  GLU   A CD    1 
ATOM   778  O  OE1   . GLU   A 1 225  ? 49.002  20.464  -52.312 1.00 105.73 ? 374  GLU   A OE1   1 
ATOM   779  O  OE2   . GLU   A 1 225  ? 49.243  20.070  -50.158 1.00 101.41 ? 374  GLU   A OE2   1 
ATOM   780  N  N     . GLN   A 1 226  ? 47.278  15.484  -50.363 1.00 94.94  ? 375  GLN   A N     1 
ATOM   781  C  CA    . GLN   A 1 226  ? 47.160  15.169  -48.912 1.00 94.97  ? 375  GLN   A CA    1 
ATOM   782  C  C     . GLN   A 1 226  ? 46.877  13.675  -48.705 1.00 94.01  ? 375  GLN   A C     1 
ATOM   783  O  O     . GLN   A 1 226  ? 47.776  12.975  -48.202 1.00 97.26  ? 375  GLN   A O     1 
ATOM   784  C  CB    . GLN   A 1 226  ? 46.068  16.032  -48.273 1.00 96.09  ? 375  GLN   A CB    1 
ATOM   785  C  CG    . GLN   A 1 226  ? 46.441  17.504  -48.166 1.00 97.77  ? 375  GLN   A CG    1 
ATOM   786  C  CD    . GLN   A 1 226  ? 47.576  17.739  -47.197 1.00 99.51  ? 375  GLN   A CD    1 
ATOM   787  O  OE1   . GLN   A 1 226  ? 47.462  17.473  -46.002 1.00 100.19 ? 375  GLN   A OE1   1 
ATOM   788  N  NE2   . GLN   A 1 226  ? 48.688  18.246  -47.707 1.00 98.79  ? 375  GLN   A NE2   1 
ATOM   789  N  N     . ASP   A 1 227  ? 45.678  13.213  -49.074 1.00 92.04  ? 376  ASP   A N     1 
ATOM   790  C  CA    . ASP   A 1 227  ? 45.144  11.863  -48.741 1.00 91.08  ? 376  ASP   A CA    1 
ATOM   791  C  C     . ASP   A 1 227  ? 46.096  10.782  -49.274 1.00 88.92  ? 376  ASP   A C     1 
ATOM   792  O  O     . ASP   A 1 227  ? 46.207  10.656  -50.505 1.00 89.45  ? 376  ASP   A O     1 
ATOM   793  C  CB    . ASP   A 1 227  ? 43.718  11.703  -49.280 1.00 91.41  ? 376  ASP   A CB    1 
ATOM   794  C  CG    . ASP   A 1 227  ? 42.939  10.544  -48.679 1.00 92.92  ? 376  ASP   A CG    1 
ATOM   795  O  OD1   . ASP   A 1 227  ? 43.578  9.595   -48.180 1.00 93.88  ? 376  ASP   A OD1   1 
ATOM   796  O  OD2   . ASP   A 1 227  ? 41.693  10.603  -48.714 1.00 93.68  ? 376  ASP   A OD2   1 
ATOM   797  N  N     . HIS   A 1 228  ? 46.753  10.039  -48.372 1.00 89.61  ? 377  HIS   A N     1 
ATOM   798  C  CA    . HIS   A 1 228  ? 47.708  8.941   -48.695 1.00 91.14  ? 377  HIS   A CA    1 
ATOM   799  C  C     . HIS   A 1 228  ? 46.943  7.661   -49.054 1.00 89.00  ? 377  HIS   A C     1 
ATOM   800  O  O     . HIS   A 1 228  ? 47.493  6.852   -49.828 1.00 87.99  ? 377  HIS   A O     1 
ATOM   801  C  CB    . HIS   A 1 228  ? 48.702  8.693   -47.546 1.00 94.04  ? 377  HIS   A CB    1 
ATOM   802  C  CG    . HIS   A 1 228  ? 49.863  9.633   -47.526 1.00 98.16  ? 377  HIS   A CG    1 
ATOM   803  N  ND1   . HIS   A 1 228  ? 50.771  9.708   -48.567 1.00 101.24 ? 377  HIS   A ND1   1 
ATOM   804  C  CD2   . HIS   A 1 228  ? 50.282  10.518  -46.595 1.00 100.57 ? 377  HIS   A CD2   1 
ATOM   805  C  CE1   . HIS   A 1 228  ? 51.690  10.608  -48.283 1.00 100.59 ? 377  HIS   A CE1   1 
ATOM   806  N  NE2   . HIS   A 1 228  ? 51.413  11.119  -47.078 1.00 101.23 ? 377  HIS   A NE2   1 
ATOM   807  N  N     . ASP   A 1 229  ? 45.737  7.476   -48.504 1.00 87.15  ? 378  ASP   A N     1 
ATOM   808  C  CA    . ASP   A 1 229  ? 44.839  6.333   -48.831 1.00 85.94  ? 378  ASP   A CA    1 
ATOM   809  C  C     . ASP   A 1 229  ? 44.302  6.503   -50.259 1.00 82.98  ? 378  ASP   A C     1 
ATOM   810  O  O     . ASP   A 1 229  ? 44.096  5.473   -50.930 1.00 81.68  ? 378  ASP   A O     1 
ATOM   811  C  CB    . ASP   A 1 229  ? 43.705  6.186   -47.810 1.00 87.02  ? 378  ASP   A CB    1 
ATOM   812  C  CG    . ASP   A 1 229  ? 44.102  5.446   -46.543 1.00 87.66  ? 378  ASP   A CG    1 
ATOM   813  O  OD1   . ASP   A 1 229  ? 45.315  5.357   -46.266 1.00 88.84  ? 378  ASP   A OD1   1 
ATOM   814  O  OD2   . ASP   A 1 229  ? 43.193  4.957   -45.843 1.00 88.54  ? 378  ASP   A OD2   1 
ATOM   815  N  N     . LEU   A 1 230  ? 44.090  7.748   -50.701 1.00 81.13  ? 379  LEU   A N     1 
ATOM   816  C  CA    . LEU   A 1 230  ? 43.616  8.087   -52.072 1.00 80.36  ? 379  LEU   A CA    1 
ATOM   817  C  C     . LEU   A 1 230  ? 44.751  7.846   -53.074 1.00 80.94  ? 379  LEU   A C     1 
ATOM   818  O  O     . LEU   A 1 230  ? 44.472  7.294   -54.156 1.00 82.89  ? 379  LEU   A O     1 
ATOM   819  C  CB    . LEU   A 1 230  ? 43.146  9.546   -52.103 1.00 79.38  ? 379  LEU   A CB    1 
ATOM   820  C  CG    . LEU   A 1 230  ? 42.493  10.011  -53.406 1.00 79.13  ? 379  LEU   A CG    1 
ATOM   821  C  CD1   . LEU   A 1 230  ? 41.301  9.138   -53.768 1.00 78.90  ? 379  LEU   A CD1   1 
ATOM   822  C  CD2   . LEU   A 1 230  ? 42.070  11.469  -53.312 1.00 77.98  ? 379  LEU   A CD2   1 
ATOM   823  N  N     . GLN   A 1 231  ? 45.977  8.251   -52.722 1.00 81.27  ? 380  GLN   A N     1 
ATOM   824  C  CA    . GLN   A 1 231  ? 47.205  8.045   -53.539 1.00 81.83  ? 380  GLN   A CA    1 
ATOM   825  C  C     . GLN   A 1 231  ? 47.375  6.550   -53.839 1.00 79.41  ? 380  GLN   A C     1 
ATOM   826  O  O     . GLN   A 1 231  ? 47.715  6.222   -54.992 1.00 81.07  ? 380  GLN   A O     1 
ATOM   827  C  CB    . GLN   A 1 231  ? 48.436  8.602   -52.818 1.00 85.62  ? 380  GLN   A CB    1 
ATOM   828  C  CG    . GLN   A 1 231  ? 48.568  10.117  -52.916 1.00 88.05  ? 380  GLN   A CG    1 
ATOM   829  C  CD    . GLN   A 1 231  ? 49.677  10.667  -52.050 1.00 89.01  ? 380  GLN   A CD    1 
ATOM   830  O  OE1   . GLN   A 1 231  ? 50.568  9.945   -51.608 1.00 90.69  ? 380  GLN   A OE1   1 
ATOM   831  N  NE2   . GLN   A 1 231  ? 49.630  11.966  -51.800 1.00 88.70  ? 380  GLN   A NE2   1 
ATOM   832  N  N     . ALA   A 1 232  ? 47.140  5.689   -52.841 1.00 76.75  ? 381  ALA   A N     1 
ATOM   833  C  CA    . ALA   A 1 232  ? 47.266  4.212   -52.929 1.00 77.07  ? 381  ALA   A CA    1 
ATOM   834  C  C     . ALA   A 1 232  ? 46.203  3.641   -53.878 1.00 76.75  ? 381  ALA   A C     1 
ATOM   835  O  O     . ALA   A 1 232  ? 46.527  2.699   -54.630 1.00 75.69  ? 381  ALA   A O     1 
ATOM   836  C  CB    . ALA   A 1 232  ? 47.155  3.601   -51.553 1.00 76.76  ? 381  ALA   A CB    1 
ATOM   837  N  N     . ILE   A 1 233  ? 44.981  4.185   -53.828 1.00 75.81  ? 382  ILE   A N     1 
ATOM   838  C  CA    . ILE   A 1 233  ? 43.829  3.789   -54.694 1.00 74.81  ? 382  ILE   A CA    1 
ATOM   839  C  C     . ILE   A 1 233  ? 44.136  4.185   -56.146 1.00 74.61  ? 382  ILE   A C     1 
ATOM   840  O  O     . ILE   A 1 233  ? 43.915  3.345   -57.039 1.00 74.13  ? 382  ILE   A O     1 
ATOM   841  C  CB    . ILE   A 1 233  ? 42.514  4.409   -54.171 1.00 75.67  ? 382  ILE   A CB    1 
ATOM   842  C  CG1   . ILE   A 1 233  ? 42.049  3.722   -52.883 1.00 75.39  ? 382  ILE   A CG1   1 
ATOM   843  C  CG2   . ILE   A 1 233  ? 41.430  4.388   -55.240 1.00 76.24  ? 382  ILE   A CG2   1 
ATOM   844  C  CD1   . ILE   A 1 233  ? 41.013  4.498   -52.103 1.00 75.24  ? 382  ILE   A CD1   1 
ATOM   845  N  N     . LEU   A 1 234  ? 44.625  5.410   -56.372 1.00 73.60  ? 383  LEU   A N     1 
ATOM   846  C  CA    . LEU   A 1 234  ? 45.048  5.901   -57.714 1.00 74.59  ? 383  LEU   A CA    1 
ATOM   847  C  C     . LEU   A 1 234  ? 46.141  4.984   -58.277 1.00 76.15  ? 383  LEU   A C     1 
ATOM   848  O  O     . LEU   A 1 234  ? 46.140  4.757   -59.501 1.00 78.24  ? 383  LEU   A O     1 
ATOM   849  C  CB    . LEU   A 1 234  ? 45.544  7.348   -57.617 1.00 75.49  ? 383  LEU   A CB    1 
ATOM   850  C  CG    . LEU   A 1 234  ? 44.509  8.421   -57.956 1.00 76.12  ? 383  LEU   A CG    1 
ATOM   851  C  CD1   . LEU   A 1 234  ? 43.482  8.563   -56.844 1.00 76.41  ? 383  LEU   A CD1   1 
ATOM   852  C  CD2   . LEU   A 1 234  ? 45.183  9.756   -58.229 1.00 76.81  ? 383  LEU   A CD2   1 
ATOM   853  N  N     . GLN   A 1 235  ? 47.034  4.481   -57.419 1.00 77.10  ? 384  GLN   A N     1 
ATOM   854  C  CA    . GLN   A 1 235  ? 48.146  3.572   -57.809 1.00 77.95  ? 384  GLN   A CA    1 
ATOM   855  C  C     . GLN   A 1 235  ? 47.578  2.223   -58.269 1.00 78.69  ? 384  GLN   A C     1 
ATOM   856  O  O     . GLN   A 1 235  ? 48.212  1.598   -59.138 1.00 79.64  ? 384  GLN   A O     1 
ATOM   857  C  CB    . GLN   A 1 235  ? 49.149  3.412   -56.664 1.00 78.89  ? 384  GLN   A CB    1 
ATOM   858  C  CG    . GLN   A 1 235  ? 50.164  4.546   -56.601 1.00 79.65  ? 384  GLN   A CG    1 
ATOM   859  C  CD    . GLN   A 1 235  ? 51.111  4.417   -55.433 1.00 80.49  ? 384  GLN   A CD    1 
ATOM   860  O  OE1   . GLN   A 1 235  ? 50.712  4.099   -54.315 1.00 80.69  ? 384  GLN   A OE1   1 
ATOM   861  N  NE2   . GLN   A 1 235  ? 52.383  4.676   -55.687 1.00 81.51  ? 384  GLN   A NE2   1 
ATOM   862  N  N     . GLU   A 1 236  ? 46.437  1.796   -57.714 1.00 77.82  ? 385  GLU   A N     1 
ATOM   863  C  CA    . GLU   A 1 236  ? 45.698  0.579   -58.157 1.00 76.37  ? 385  GLU   A CA    1 
ATOM   864  C  C     . GLU   A 1 236  ? 44.991  0.866   -59.487 1.00 73.99  ? 385  GLU   A C     1 
ATOM   865  O  O     . GLU   A 1 236  ? 44.975  -0.035  -60.350 1.00 73.36  ? 385  GLU   A O     1 
ATOM   866  C  CB    . GLU   A 1 236  ? 44.678  0.126   -57.110 1.00 77.96  ? 385  GLU   A CB    1 
ATOM   867  C  CG    . GLU   A 1 236  ? 45.192  -0.959  -56.182 1.00 80.63  ? 385  GLU   A CG    1 
ATOM   868  C  CD    . GLU   A 1 236  ? 44.097  -1.720  -55.454 1.00 83.53  ? 385  GLU   A CD    1 
ATOM   869  O  OE1   . GLU   A 1 236  ? 43.227  -2.300  -56.138 1.00 83.52  ? 385  GLU   A OE1   1 
ATOM   870  O  OE2   . GLU   A 1 236  ? 44.110  -1.723  -54.206 1.00 86.27  ? 385  GLU   A OE2   1 
ATOM   871  N  N     . ARG   A 1 237  ? 44.418  2.066   -59.629 1.00 71.94  ? 386  ARG   A N     1 
ATOM   872  C  CA    . ARG   A 1 237  ? 43.694  2.524   -60.847 1.00 71.03  ? 386  ARG   A CA    1 
ATOM   873  C  C     . ARG   A 1 237  ? 44.635  2.507   -62.057 1.00 71.41  ? 386  ARG   A C     1 
ATOM   874  O  O     . ARG   A 1 237  ? 44.172  2.150   -63.160 1.00 73.29  ? 386  ARG   A O     1 
ATOM   875  C  CB    . ARG   A 1 237  ? 43.144  3.941   -60.661 1.00 69.35  ? 386  ARG   A CB    1 
ATOM   876  C  CG    . ARG   A 1 237  ? 41.818  4.018   -59.917 1.00 67.27  ? 386  ARG   A CG    1 
ATOM   877  C  CD    . ARG   A 1 237  ? 41.277  5.434   -59.934 1.00 66.04  ? 386  ARG   A CD    1 
ATOM   878  N  NE    . ARG   A 1 237  ? 41.046  5.916   -61.292 1.00 64.76  ? 386  ARG   A NE    1 
ATOM   879  C  CZ    . ARG   A 1 237  ? 40.888  7.191   -61.637 1.00 63.72  ? 386  ARG   A CZ    1 
ATOM   880  N  NH1   . ARG   A 1 237  ? 40.938  8.146   -60.722 1.00 64.18  ? 386  ARG   A NH1   1 
ATOM   881  N  NH2   . ARG   A 1 237  ? 40.683  7.509   -62.905 1.00 63.13  ? 386  ARG   A NH2   1 
ATOM   882  N  N     . GLU   A 1 238  ? 45.900  2.882   -61.851 1.00 70.80  ? 387  GLU   A N     1 
ATOM   883  C  CA    . GLU   A 1 238  ? 46.900  3.092   -62.931 1.00 71.56  ? 387  GLU   A CA    1 
ATOM   884  C  C     . GLU   A 1 238  ? 47.484  1.748   -63.394 1.00 70.07  ? 387  GLU   A C     1 
ATOM   885  O  O     . GLU   A 1 238  ? 48.273  1.769   -64.359 1.00 71.98  ? 387  GLU   A O     1 
ATOM   886  C  CB    . GLU   A 1 238  ? 47.984  4.059   -62.448 1.00 74.42  ? 387  GLU   A CB    1 
ATOM   887  C  CG    . GLU   A 1 238  ? 47.473  5.481   -62.260 1.00 77.40  ? 387  GLU   A CG    1 
ATOM   888  C  CD    . GLU   A 1 238  ? 48.265  6.364   -61.305 1.00 78.61  ? 387  GLU   A CD    1 
ATOM   889  O  OE1   . GLU   A 1 238  ? 48.795  5.841   -60.302 1.00 77.80  ? 387  GLU   A OE1   1 
ATOM   890  O  OE2   . GLU   A 1 238  ? 48.340  7.581   -61.563 1.00 79.03  ? 387  GLU   A OE2   1 
ATOM   891  N  N     . LEU   A 1 239  ? 47.109  0.630   -62.755 1.00 68.80  ? 388  LEU   A N     1 
ATOM   892  C  CA    . LEU   A 1 239  ? 47.563  -0.745  -63.117 1.00 69.18  ? 388  LEU   A CA    1 
ATOM   893  C  C     . LEU   A 1 239  ? 46.494  -1.479  -63.939 1.00 68.18  ? 388  LEU   A C     1 
ATOM   894  O  O     . LEU   A 1 239  ? 46.793  -2.597  -64.408 1.00 65.74  ? 388  LEU   A O     1 
ATOM   895  C  CB    . LEU   A 1 239  ? 47.877  -1.532  -61.840 1.00 70.21  ? 388  LEU   A CB    1 
ATOM   896  C  CG    . LEU   A 1 239  ? 49.023  -0.988  -60.990 1.00 71.31  ? 388  LEU   A CG    1 
ATOM   897  C  CD1   . LEU   A 1 239  ? 49.333  -1.930  -59.837 1.00 71.59  ? 388  LEU   A CD1   1 
ATOM   898  C  CD2   . LEU   A 1 239  ? 50.264  -0.746  -61.834 1.00 71.54  ? 388  LEU   A CD2   1 
ATOM   899  N  N     . LEU   A 1 240  ? 45.301  -0.894  -64.100 1.00 66.67  ? 389  LEU   A N     1 
ATOM   900  C  CA    . LEU   A 1 240  ? 44.160  -1.530  -64.815 1.00 65.79  ? 389  LEU   A CA    1 
ATOM   901  C  C     . LEU   A 1 240  ? 44.414  -1.486  -66.320 1.00 65.23  ? 389  LEU   A C     1 
ATOM   902  O  O     . LEU   A 1 240  ? 44.765  -0.436  -66.858 1.00 65.82  ? 389  LEU   A O     1 
ATOM   903  C  CB    . LEU   A 1 240  ? 42.854  -0.816  -64.447 1.00 65.21  ? 389  LEU   A CB    1 
ATOM   904  C  CG    . LEU   A 1 240  ? 42.342  -1.072  -63.030 1.00 64.06  ? 389  LEU   A CG    1 
ATOM   905  C  CD1   . LEU   A 1 240  ? 41.176  -0.154  -62.700 1.00 63.61  ? 389  LEU   A CD1   1 
ATOM   906  C  CD2   . LEU   A 1 240  ? 41.943  -2.529  -62.847 1.00 63.04  ? 389  LEU   A CD2   1 
ATOM   907  N  N     . PRO   A 1 241  ? 44.238  -2.622  -67.038 1.00 63.32  ? 390  PRO   A N     1 
ATOM   908  C  CA    . PRO   A 1 241  ? 44.498  -2.698  -68.478 1.00 63.27  ? 390  PRO   A CA    1 
ATOM   909  C  C     . PRO   A 1 241  ? 44.088  -1.478  -69.320 1.00 64.15  ? 390  PRO   A C     1 
ATOM   910  O  O     . PRO   A 1 241  ? 44.826  -1.129  -70.218 1.00 67.77  ? 390  PRO   A O     1 
ATOM   911  C  CB    . PRO   A 1 241  ? 43.654  -3.910  -68.888 1.00 62.25  ? 390  PRO   A CB    1 
ATOM   912  C  CG    . PRO   A 1 241  ? 43.745  -4.836  -67.693 1.00 62.03  ? 390  PRO   A CG    1 
ATOM   913  C  CD    . PRO   A 1 241  ? 43.796  -3.916  -66.490 1.00 62.29  ? 390  PRO   A CD    1 
ATOM   914  N  N     . VAL   A 1 242  ? 42.940  -0.864  -69.016 1.00 64.92  ? 391  VAL   A N     1 
ATOM   915  C  CA    . VAL   A 1 242  ? 42.366  0.285   -69.785 1.00 65.87  ? 391  VAL   A CA    1 
ATOM   916  C  C     . VAL   A 1 242  ? 43.305  1.499   -69.704 1.00 66.72  ? 391  VAL   A C     1 
ATOM   917  O  O     . VAL   A 1 242  ? 43.267  2.323   -70.640 1.00 65.37  ? 391  VAL   A O     1 
ATOM   918  C  CB    . VAL   A 1 242  ? 40.943  0.638   -69.301 1.00 65.71  ? 391  VAL   A CB    1 
ATOM   919  C  CG1   . VAL   A 1 242  ? 40.933  1.219   -67.894 1.00 64.72  ? 391  VAL   A CG1   1 
ATOM   920  C  CG2   . VAL   A 1 242  ? 40.235  1.576   -70.270 1.00 65.57  ? 391  VAL   A CG2   1 
ATOM   921  N  N     . LYS   A 1 243  ? 44.113  1.606   -68.641 1.00 68.97  ? 392  LYS   A N     1 
ATOM   922  C  CA    . LYS   A 1 243  ? 44.926  2.813   -68.320 1.00 71.07  ? 392  LYS   A CA    1 
ATOM   923  C  C     . LYS   A 1 243  ? 45.795  3.225   -69.515 1.00 72.80  ? 392  LYS   A C     1 
ATOM   924  O  O     . LYS   A 1 243  ? 45.831  4.432   -69.821 1.00 74.48  ? 392  LYS   A O     1 
ATOM   925  C  CB    . LYS   A 1 243  ? 45.825  2.577   -67.103 1.00 71.35  ? 392  LYS   A CB    1 
ATOM   926  C  CG    . LYS   A 1 243  ? 46.703  3.764   -66.723 1.00 72.23  ? 392  LYS   A CG    1 
ATOM   927  C  CD    . LYS   A 1 243  ? 45.947  5.077   -66.646 1.00 72.32  ? 392  LYS   A CD    1 
ATOM   928  C  CE    . LYS   A 1 243  ? 46.754  6.203   -66.041 1.00 73.44  ? 392  LYS   A CE    1 
ATOM   929  N  NZ    . LYS   A 1 243  ? 45.883  7.322   -65.612 1.00 74.22  ? 392  LYS   A NZ    1 
ATOM   930  N  N     . LYS   A 1 244  ? 46.478  2.267   -70.151 1.00 73.76  ? 393  LYS   A N     1 
ATOM   931  C  CA    . LYS   A 1 244  ? 47.456  2.534   -71.243 1.00 74.11  ? 393  LYS   A CA    1 
ATOM   932  C  C     . LYS   A 1 244  ? 46.740  3.007   -72.518 1.00 72.37  ? 393  LYS   A C     1 
ATOM   933  O  O     . LYS   A 1 244  ? 47.447  3.480   -73.427 1.00 74.23  ? 393  LYS   A O     1 
ATOM   934  C  CB    . LYS   A 1 244  ? 48.334  1.306   -71.517 1.00 76.98  ? 393  LYS   A CB    1 
ATOM   935  C  CG    . LYS   A 1 244  ? 47.603  0.004   -71.822 1.00 79.90  ? 393  LYS   A CG    1 
ATOM   936  C  CD    . LYS   A 1 244  ? 48.537  -1.139  -72.183 1.00 82.37  ? 393  LYS   A CD    1 
ATOM   937  C  CE    . LYS   A 1 244  ? 47.930  -2.512  -71.971 1.00 83.23  ? 393  LYS   A CE    1 
ATOM   938  N  NZ    . LYS   A 1 244  ? 47.847  -2.870  -70.533 1.00 82.49  ? 393  LYS   A NZ    1 
ATOM   939  N  N     . PHE   A 1 245  ? 45.405  2.903   -72.585 1.00 69.54  ? 394  PHE   A N     1 
ATOM   940  C  CA    . PHE   A 1 245  ? 44.573  3.336   -73.742 1.00 66.94  ? 394  PHE   A CA    1 
ATOM   941  C  C     . PHE   A 1 245  ? 43.913  4.695   -73.464 1.00 67.33  ? 394  PHE   A C     1 
ATOM   942  O  O     . PHE   A 1 245  ? 43.164  5.173   -74.339 1.00 66.05  ? 394  PHE   A O     1 
ATOM   943  C  CB    . PHE   A 1 245  ? 43.513  2.278   -74.064 1.00 64.22  ? 394  PHE   A CB    1 
ATOM   944  C  CG    . PHE   A 1 245  ? 44.054  0.888   -74.288 1.00 62.97  ? 394  PHE   A CG    1 
ATOM   945  C  CD1   . PHE   A 1 245  ? 44.188  -0.000  -73.231 1.00 62.50  ? 394  PHE   A CD1   1 
ATOM   946  C  CD2   . PHE   A 1 245  ? 44.425  0.464   -75.555 1.00 62.27  ? 394  PHE   A CD2   1 
ATOM   947  C  CE1   . PHE   A 1 245  ? 44.681  -1.280  -73.436 1.00 61.14  ? 394  PHE   A CE1   1 
ATOM   948  C  CE2   . PHE   A 1 245  ? 44.918  -0.817  -75.758 1.00 62.30  ? 394  PHE   A CE2   1 
ATOM   949  C  CZ    . PHE   A 1 245  ? 45.045  -1.687  -74.698 1.00 61.31  ? 394  PHE   A CZ    1 
ATOM   950  N  N     . GLU   A 1 246  ? 44.186  5.302   -72.302 1.00 69.44  ? 395  GLU   A N     1 
ATOM   951  C  CA    . GLU   A 1 246  ? 43.605  6.601   -71.857 1.00 71.30  ? 395  GLU   A CA    1 
ATOM   952  C  C     . GLU   A 1 246  ? 43.769  7.654   -72.962 1.00 72.45  ? 395  GLU   A C     1 
ATOM   953  O  O     . GLU   A 1 246  ? 42.765  8.305   -73.312 1.00 72.61  ? 395  GLU   A O     1 
ATOM   954  C  CB    . GLU   A 1 246  ? 44.267  7.059   -70.555 1.00 72.14  ? 395  GLU   A CB    1 
ATOM   955  C  CG    . GLU   A 1 246  ? 43.772  8.403   -70.047 1.00 72.69  ? 395  GLU   A CG    1 
ATOM   956  C  CD    . GLU   A 1 246  ? 44.204  8.754   -68.631 1.00 73.98  ? 395  GLU   A CD    1 
ATOM   957  O  OE1   . GLU   A 1 246  ? 45.188  8.156   -68.143 1.00 73.50  ? 395  GLU   A OE1   1 
ATOM   958  O  OE2   . GLU   A 1 246  ? 43.553  9.624   -68.017 1.00 74.52  ? 395  GLU   A OE2   1 
ATOM   959  N  N     . SER   A 1 247  ? 44.989  7.810   -73.484 1.00 75.03  ? 396  SER   A N     1 
ATOM   960  C  CA    . SER   A 1 247  ? 45.354  8.811   -74.523 1.00 77.00  ? 396  SER   A CA    1 
ATOM   961  C  C     . SER   A 1 247  ? 44.465  8.635   -75.761 1.00 77.71  ? 396  SER   A C     1 
ATOM   962  O  O     . SER   A 1 247  ? 43.881  9.640   -76.212 1.00 78.54  ? 396  SER   A O     1 
ATOM   963  C  CB    . SER   A 1 247  ? 46.815  8.710   -74.880 1.00 78.30  ? 396  SER   A CB    1 
ATOM   964  O  OG    . SER   A 1 247  ? 47.628  8.871   -73.727 1.00 79.63  ? 396  SER   A OG    1 
ATOM   965  N  N     . GLU   A 1 248  ? 44.362  7.400   -76.267 1.00 76.71  ? 397  GLU   A N     1 
ATOM   966  C  CA    . GLU   A 1 248  ? 43.628  7.040   -77.513 1.00 75.83  ? 397  GLU   A CA    1 
ATOM   967  C  C     . GLU   A 1 248  ? 42.123  7.263   -77.313 1.00 75.90  ? 397  GLU   A C     1 
ATOM   968  O  O     . GLU   A 1 248  ? 41.499  7.881   -78.201 1.00 76.12  ? 397  GLU   A O     1 
ATOM   969  C  CB    . GLU   A 1 248  ? 43.914  5.585   -77.894 1.00 76.22  ? 397  GLU   A CB    1 
ATOM   970  C  CG    . GLU   A 1 248  ? 43.438  5.210   -79.287 1.00 77.16  ? 397  GLU   A CG    1 
ATOM   971  C  CD    . GLU   A 1 248  ? 43.473  3.720   -79.595 1.00 79.54  ? 397  GLU   A CD    1 
ATOM   972  O  OE1   . GLU   A 1 248  ? 44.039  2.957   -78.780 1.00 78.16  ? 397  GLU   A OE1   1 
ATOM   973  O  OE2   . GLU   A 1 248  ? 42.927  3.323   -80.649 1.00 79.83  ? 397  GLU   A OE2   1 
ATOM   974  N  N     . ILE   A 1 249  ? 41.570  6.768   -76.197 1.00 73.72  ? 398  ILE   A N     1 
ATOM   975  C  CA    . ILE   A 1 249  ? 40.116  6.845   -75.855 1.00 71.50  ? 398  ILE   A CA    1 
ATOM   976  C  C     . ILE   A 1 249  ? 39.686  8.317   -75.850 1.00 72.38  ? 398  ILE   A C     1 
ATOM   977  O  O     . ILE   A 1 249  ? 38.725  8.650   -76.566 1.00 71.42  ? 398  ILE   A O     1 
ATOM   978  C  CB    . ILE   A 1 249  ? 39.818  6.144   -74.512 1.00 69.31  ? 398  ILE   A CB    1 
ATOM   979  C  CG1   . ILE   A 1 249  ? 39.985  4.625   -74.619 1.00 70.22  ? 398  ILE   A CG1   1 
ATOM   980  C  CG2   . ILE   A 1 249  ? 38.434  6.513   -73.998 1.00 68.45  ? 398  ILE   A CG2   1 
ATOM   981  C  CD1   . ILE   A 1 249  ? 40.148  3.922   -73.290 1.00 70.62  ? 398  ILE   A CD1   1 
ATOM   982  N  N     . LEU   A 1 250  ? 40.382  9.159   -75.079 1.00 73.65  ? 399  LEU   A N     1 
ATOM   983  C  CA    . LEU   A 1 250  ? 40.100  10.616  -74.953 1.00 75.63  ? 399  LEU   A CA    1 
ATOM   984  C  C     . LEU   A 1 250  ? 40.228  11.282  -76.330 1.00 76.55  ? 399  LEU   A C     1 
ATOM   985  O  O     . LEU   A 1 250  ? 39.359  12.114  -76.668 1.00 71.87  ? 399  LEU   A O     1 
ATOM   986  C  CB    . LEU   A 1 250  ? 41.072  11.233  -73.942 1.00 77.00  ? 399  LEU   A CB    1 
ATOM   987  C  CG    . LEU   A 1 250  ? 40.883  10.788  -72.491 1.00 77.74  ? 399  LEU   A CG    1 
ATOM   988  C  CD1   . LEU   A 1 250  ? 42.100  11.140  -71.649 1.00 77.36  ? 399  LEU   A CD1   1 
ATOM   989  C  CD2   . LEU   A 1 250  ? 39.623  11.397  -71.892 1.00 77.82  ? 399  LEU   A CD2   1 
ATOM   990  N  N     . GLU   A 1 251  ? 41.269  10.915  -77.086 1.00 80.53  ? 400  GLU   A N     1 
ATOM   991  C  CA    . GLU   A 1 251  ? 41.560  11.419  -78.457 1.00 82.51  ? 400  GLU   A CA    1 
ATOM   992  C  C     . GLU   A 1 251  ? 40.390  11.073  -79.386 1.00 80.02  ? 400  GLU   A C     1 
ATOM   993  O  O     . GLU   A 1 251  ? 39.952  11.966  -80.138 1.00 79.11  ? 400  GLU   A O     1 
ATOM   994  C  CB    . GLU   A 1 251  ? 42.880  10.826  -78.960 1.00 87.00  ? 400  GLU   A CB    1 
ATOM   995  C  CG    . GLU   A 1 251  ? 43.270  11.259  -80.363 1.00 90.61  ? 400  GLU   A CG    1 
ATOM   996  C  CD    . GLU   A 1 251  ? 44.607  10.713  -80.841 1.00 93.42  ? 400  GLU   A CD    1 
ATOM   997  O  OE1   . GLU   A 1 251  ? 45.024  9.642   -80.346 1.00 93.39  ? 400  GLU   A OE1   1 
ATOM   998  O  OE2   . GLU   A 1 251  ? 45.231  11.358  -81.709 1.00 95.59  ? 400  GLU   A OE2   1 
ATOM   999  N  N     . ALA   A 1 252  ? 39.903  9.829   -79.325 1.00 77.57  ? 401  ALA   A N     1 
ATOM   1000 C  CA    . ALA   A 1 252  ? 38.791  9.305   -80.154 1.00 75.49  ? 401  ALA   A CA    1 
ATOM   1001 C  C     . ALA   A 1 252  ? 37.494  10.065  -79.843 1.00 73.41  ? 401  ALA   A C     1 
ATOM   1002 O  O     . ALA   A 1 252  ? 36.845  10.530  -80.799 1.00 73.07  ? 401  ALA   A O     1 
ATOM   1003 C  CB    . ALA   A 1 252  ? 38.629  7.822   -79.924 1.00 75.08  ? 401  ALA   A CB    1 
ATOM   1004 N  N     . ILE   A 1 253  ? 37.145  10.191  -78.557 1.00 71.62  ? 402  ILE   A N     1 
ATOM   1005 C  CA    . ILE   A 1 253  ? 35.881  10.828  -78.073 1.00 71.48  ? 402  ILE   A CA    1 
ATOM   1006 C  C     . ILE   A 1 253  ? 35.824  12.276  -78.576 1.00 74.13  ? 402  ILE   A C     1 
ATOM   1007 O  O     . ILE   A 1 253  ? 34.748  12.695  -79.037 1.00 75.07  ? 402  ILE   A O     1 
ATOM   1008 C  CB    . ILE   A 1 253  ? 35.764  10.762  -76.535 1.00 69.63  ? 402  ILE   A CB    1 
ATOM   1009 C  CG1   . ILE   A 1 253  ? 35.658  9.323   -76.021 1.00 68.90  ? 402  ILE   A CG1   1 
ATOM   1010 C  CG2   . ILE   A 1 253  ? 34.598  11.611  -76.045 1.00 69.10  ? 402  ILE   A CG2   1 
ATOM   1011 C  CD1   . ILE   A 1 253  ? 36.096  9.151   -74.584 1.00 68.08  ? 402  ILE   A CD1   1 
ATOM   1012 N  N     . SER   A 1 254  ? 36.937  13.008  -78.477 1.00 77.39  ? 403  SER   A N     1 
ATOM   1013 C  CA    . SER   A 1 254  ? 37.042  14.450  -78.828 1.00 77.96  ? 403  SER   A CA    1 
ATOM   1014 C  C     . SER   A 1 254  ? 36.783  14.659  -80.326 1.00 76.70  ? 403  SER   A C     1 
ATOM   1015 O  O     . SER   A 1 254  ? 36.171  15.687  -80.677 1.00 73.95  ? 403  SER   A O     1 
ATOM   1016 C  CB    . SER   A 1 254  ? 38.382  15.006  -78.416 1.00 78.05  ? 403  SER   A CB    1 
ATOM   1017 O  OG    . SER   A 1 254  ? 39.431  14.142  -78.825 1.00 79.72  ? 403  SER   A OG    1 
ATOM   1018 N  N     . GLN   A 1 255  ? 37.216  13.711  -81.165 1.00 77.60  ? 404  GLN   A N     1 
ATOM   1019 C  CA    . GLN   A 1 255  ? 37.196  13.825  -82.650 1.00 80.32  ? 404  GLN   A CA    1 
ATOM   1020 C  C     . GLN   A 1 255  ? 35.829  13.411  -83.216 1.00 78.70  ? 404  GLN   A C     1 
ATOM   1021 O  O     . GLN   A 1 255  ? 35.350  14.108  -84.132 1.00 78.84  ? 404  GLN   A O     1 
ATOM   1022 C  CB    . GLN   A 1 255  ? 38.319  12.984  -83.261 1.00 82.66  ? 404  GLN   A CB    1 
ATOM   1023 C  CG    . GLN   A 1 255  ? 39.704  13.582  -83.058 1.00 84.69  ? 404  GLN   A CG    1 
ATOM   1024 C  CD    . GLN   A 1 255  ? 40.798  12.683  -83.583 1.00 87.36  ? 404  GLN   A CD    1 
ATOM   1025 O  OE1   . GLN   A 1 255  ? 40.618  11.963  -84.563 1.00 89.87  ? 404  GLN   A OE1   1 
ATOM   1026 N  NE2   . GLN   A 1 255  ? 41.951  12.721  -82.933 1.00 87.61  ? 404  GLN   A NE2   1 
ATOM   1027 N  N     . ASN   A 1 256  ? 35.231  12.327  -82.704 1.00 76.86  ? 405  ASN   A N     1 
ATOM   1028 C  CA    . ASN   A 1 256  ? 34.017  11.686  -83.283 1.00 74.89  ? 405  ASN   A CA    1 
ATOM   1029 C  C     . ASN   A 1 256  ? 32.814  11.848  -82.344 1.00 72.72  ? 405  ASN   A C     1 
ATOM   1030 O  O     . ASN   A 1 256  ? 33.004  11.744  -81.117 1.00 71.88  ? 405  ASN   A O     1 
ATOM   1031 C  CB    . ASN   A 1 256  ? 34.257  10.204  -83.577 1.00 76.07  ? 405  ASN   A CB    1 
ATOM   1032 C  CG    . ASN   A 1 256  ? 35.492  9.971   -84.420 1.00 77.24  ? 405  ASN   A CG    1 
ATOM   1033 O  OD1   . ASN   A 1 256  ? 36.590  10.368  -84.038 1.00 78.79  ? 405  ASN   A OD1   1 
ATOM   1034 N  ND2   . ASN   A 1 256  ? 35.323  9.328   -85.565 1.00 77.54  ? 405  ASN   A ND2   1 
ATOM   1035 N  N     . SER   A 1 257  ? 31.623  12.064  -82.920 1.00 69.62  ? 406  SER   A N     1 
ATOM   1036 C  CA    . SER   A 1 257  ? 30.317  12.177  -82.214 1.00 67.81  ? 406  SER   A CA    1 
ATOM   1037 C  C     . SER   A 1 257  ? 30.034  10.898  -81.418 1.00 67.00  ? 406  SER   A C     1 
ATOM   1038 O  O     . SER   A 1 257  ? 29.537  11.007  -80.282 1.00 69.56  ? 406  SER   A O     1 
ATOM   1039 C  CB    . SER   A 1 257  ? 29.190  12.460  -83.180 1.00 67.65  ? 406  SER   A CB    1 
ATOM   1040 O  OG    . SER   A 1 257  ? 29.244  13.797  -83.656 1.00 68.86  ? 406  SER   A OG    1 
ATOM   1041 N  N     . VAL   A 1 258  ? 30.320  9.735   -82.010 1.00 64.87  ? 407  VAL   A N     1 
ATOM   1042 C  CA    . VAL   A 1 258  ? 30.084  8.389   -81.408 1.00 63.37  ? 407  VAL   A CA    1 
ATOM   1043 C  C     . VAL   A 1 258  ? 31.371  7.569   -81.531 1.00 63.39  ? 407  VAL   A C     1 
ATOM   1044 O  O     . VAL   A 1 258  ? 32.067  7.720   -82.550 1.00 64.52  ? 407  VAL   A O     1 
ATOM   1045 C  CB    . VAL   A 1 258  ? 28.904  7.669   -82.089 1.00 63.33  ? 407  VAL   A CB    1 
ATOM   1046 C  CG1   . VAL   A 1 258  ? 28.600  6.329   -81.433 1.00 63.33  ? 407  VAL   A CG1   1 
ATOM   1047 C  CG2   . VAL   A 1 258  ? 27.662  8.545   -82.130 1.00 63.56  ? 407  VAL   A CG2   1 
ATOM   1048 N  N     . ILE   A 1 259  ? 31.670  6.747   -80.522 1.00 63.05  ? 408  ILE   A N     1 
ATOM   1049 C  CA    . ILE   A 1 259  ? 32.731  5.696   -80.580 1.00 65.14  ? 408  ILE   A CA    1 
ATOM   1050 C  C     . ILE   A 1 259  ? 32.217  4.441   -79.870 1.00 65.35  ? 408  ILE   A C     1 
ATOM   1051 O  O     . ILE   A 1 259  ? 31.202  4.530   -79.150 1.00 65.65  ? 408  ILE   A O     1 
ATOM   1052 C  CB    . ILE   A 1 259  ? 34.067  6.176   -79.972 1.00 66.95  ? 408  ILE   A CB    1 
ATOM   1053 C  CG1   . ILE   A 1 259  ? 33.965  6.440   -78.466 1.00 68.34  ? 408  ILE   A CG1   1 
ATOM   1054 C  CG2   . ILE   A 1 259  ? 34.600  7.388   -80.719 1.00 67.60  ? 408  ILE   A CG2   1 
ATOM   1055 C  CD1   . ILE   A 1 259  ? 35.286  6.337   -77.739 1.00 68.41  ? 408  ILE   A CD1   1 
ATOM   1056 N  N     . ILE   A 1 260  ? 32.907  3.321   -80.088 1.00 64.77  ? 409  ILE   A N     1 
ATOM   1057 C  CA    . ILE   A 1 260  ? 32.711  2.034   -79.363 1.00 64.17  ? 409  ILE   A CA    1 
ATOM   1058 C  C     . ILE   A 1 260  ? 34.030  1.711   -78.657 1.00 64.41  ? 409  ILE   A C     1 
ATOM   1059 O  O     . ILE   A 1 260  ? 35.077  1.745   -79.331 1.00 65.23  ? 409  ILE   A O     1 
ATOM   1060 C  CB    . ILE   A 1 260  ? 32.273  0.910   -80.327 1.00 64.25  ? 409  ILE   A CB    1 
ATOM   1061 C  CG1   . ILE   A 1 260  ? 30.966  1.257   -81.047 1.00 65.58  ? 409  ILE   A CG1   1 
ATOM   1062 C  CG2   . ILE   A 1 260  ? 32.171  -0.423  -79.600 1.00 63.22  ? 409  ILE   A CG2   1 
ATOM   1063 C  CD1   . ILE   A 1 260  ? 30.731  0.467   -82.317 1.00 66.23  ? 409  ILE   A CD1   1 
ATOM   1064 N  N     . ILE   A 1 261  ? 33.982  1.454   -77.348 1.00 63.38  ? 410  ILE   A N     1 
ATOM   1065 C  CA    . ILE   A 1 261  ? 35.136  0.934   -76.560 1.00 63.27  ? 410  ILE   A CA    1 
ATOM   1066 C  C     . ILE   A 1 261  ? 34.892  -0.560  -76.325 1.00 64.34  ? 410  ILE   A C     1 
ATOM   1067 O  O     . ILE   A 1 261  ? 34.254  -0.917  -75.315 1.00 66.08  ? 410  ILE   A O     1 
ATOM   1068 C  CB    . ILE   A 1 261  ? 35.341  1.740   -75.260 1.00 63.06  ? 410  ILE   A CB    1 
ATOM   1069 C  CG1   . ILE   A 1 261  ? 35.514  3.233   -75.556 1.00 63.21  ? 410  ILE   A CG1   1 
ATOM   1070 C  CG2   . ILE   A 1 261  ? 36.512  1.188   -74.457 1.00 62.39  ? 410  ILE   A CG2   1 
ATOM   1071 C  CD1   . ILE   A 1 261  ? 35.679  4.100   -74.328 1.00 63.60  ? 410  ILE   A CD1   1 
ATOM   1072 N  N     . ARG   A 1 262  ? 35.338  -1.387  -77.273 1.00 64.27  ? 411  ARG   A N     1 
ATOM   1073 C  CA    . ARG   A 1 262  ? 35.361  -2.869  -77.171 1.00 63.98  ? 411  ARG   A CA    1 
ATOM   1074 C  C     . ARG   A 1 262  ? 36.555  -3.257  -76.295 1.00 62.36  ? 411  ARG   A C     1 
ATOM   1075 O  O     . ARG   A 1 262  ? 37.563  -2.531  -76.331 1.00 61.17  ? 411  ARG   A O     1 
ATOM   1076 C  CB    . ARG   A 1 262  ? 35.448  -3.487  -78.571 1.00 66.45  ? 411  ARG   A CB    1 
ATOM   1077 C  CG    . ARG   A 1 262  ? 35.445  -5.010  -78.597 1.00 68.37  ? 411  ARG   A CG    1 
ATOM   1078 C  CD    . ARG   A 1 262  ? 35.374  -5.556  -80.012 1.00 69.78  ? 411  ARG   A CD    1 
ATOM   1079 N  NE    . ARG   A 1 262  ? 35.332  -7.014  -80.040 1.00 71.69  ? 411  ARG   A NE    1 
ATOM   1080 C  CZ    . ARG   A 1 262  ? 36.393  -7.823  -80.050 1.00 72.55  ? 411  ARG   A CZ    1 
ATOM   1081 N  NH1   . ARG   A 1 262  ? 36.216  -9.134  -80.074 1.00 72.24  ? 411  ARG   A NH1   1 
ATOM   1082 N  NH2   . ARG   A 1 262  ? 37.622  -7.333  -80.035 1.00 73.08  ? 411  ARG   A NH2   1 
ATOM   1083 N  N     . GLY   A 1 263  ? 36.438  -4.346  -75.530 1.00 62.85  ? 412  GLY   A N     1 
ATOM   1084 C  CA    . GLY   A 1 263  ? 37.525  -4.866  -74.680 1.00 63.96  ? 412  GLY   A CA    1 
ATOM   1085 C  C     . GLY   A 1 263  ? 37.030  -5.874  -73.660 1.00 65.24  ? 412  GLY   A C     1 
ATOM   1086 O  O     . GLY   A 1 263  ? 35.881  -5.737  -73.202 1.00 64.91  ? 412  GLY   A O     1 
ATOM   1087 N  N     . ALA   A 1 264  ? 37.883  -6.839  -73.302 1.00 67.94  ? 413  ALA   A N     1 
ATOM   1088 C  CA    . ALA   A 1 264  ? 37.597  -7.938  -72.348 1.00 71.11  ? 413  ALA   A CA    1 
ATOM   1089 C  C     . ALA   A 1 264  ? 37.036  -7.374  -71.036 1.00 71.79  ? 413  ALA   A C     1 
ATOM   1090 O  O     . ALA   A 1 264  ? 37.353  -6.213  -70.695 1.00 69.25  ? 413  ALA   A O     1 
ATOM   1091 C  CB    . ALA   A 1 264  ? 38.852  -8.745  -72.107 1.00 71.23  ? 413  ALA   A CB    1 
ATOM   1092 N  N     . THR   A 1 265  ? 36.231  -8.176  -70.331 1.00 72.44  ? 414  THR   A N     1 
ATOM   1093 C  CA    . THR   A 1 265  ? 35.631  -7.840  -69.013 1.00 73.01  ? 414  THR   A CA    1 
ATOM   1094 C  C     . THR   A 1 265  ? 36.724  -7.889  -67.937 1.00 74.41  ? 414  THR   A C     1 
ATOM   1095 O  O     . THR   A 1 265  ? 37.289  -8.981  -67.728 1.00 73.50  ? 414  THR   A O     1 
ATOM   1096 C  CB    . THR   A 1 265  ? 34.468  -8.781  -68.678 1.00 72.06  ? 414  THR   A CB    1 
ATOM   1097 O  OG1   . THR   A 1 265  ? 33.452  -8.583  -69.662 1.00 71.20  ? 414  THR   A OG1   1 
ATOM   1098 C  CG2   . THR   A 1 265  ? 33.902  -8.548  -67.294 1.00 72.50  ? 414  THR   A CG2   1 
ATOM   1099 N  N     . GLY   A 1 266  ? 36.992  -6.752  -67.283 1.00 76.24  ? 415  GLY   A N     1 
ATOM   1100 C  CA    . GLY   A 1 266  ? 37.983  -6.614  -66.195 1.00 75.22  ? 415  GLY   A CA    1 
ATOM   1101 C  C     . GLY   A 1 266  ? 39.072  -5.597  -66.505 1.00 73.26  ? 415  GLY   A C     1 
ATOM   1102 O  O     . GLY   A 1 266  ? 39.981  -5.448  -65.667 1.00 74.30  ? 415  GLY   A O     1 
ATOM   1103 N  N     . CYS   A 1 267  ? 38.991  -4.913  -67.651 1.00 71.59  ? 416  CYS   A N     1 
ATOM   1104 C  CA    . CYS   A 1 267  ? 40.003  -3.930  -68.127 1.00 71.35  ? 416  CYS   A CA    1 
ATOM   1105 C  C     . CYS   A 1 267  ? 39.789  -2.573  -67.447 1.00 69.46  ? 416  CYS   A C     1 
ATOM   1106 O  O     . CYS   A 1 267  ? 40.786  -1.849  -67.267 1.00 70.34  ? 416  CYS   A O     1 
ATOM   1107 C  CB    . CYS   A 1 267  ? 39.954  -3.775  -69.642 1.00 72.97  ? 416  CYS   A CB    1 
ATOM   1108 S  SG    . CYS   A 1 267  ? 40.570  -5.230  -70.530 1.00 75.21  ? 416  CYS   A SG    1 
ATOM   1109 N  N     . GLY   A 1 268  ? 38.542  -2.248  -67.091 1.00 67.98  ? 417  GLY   A N     1 
ATOM   1110 C  CA    . GLY   A 1 268  ? 38.167  -1.005  -66.386 1.00 64.99  ? 417  GLY   A CA    1 
ATOM   1111 C  C     . GLY   A 1 268  ? 37.335  -0.066  -67.245 1.00 63.34  ? 417  GLY   A C     1 
ATOM   1112 O  O     . GLY   A 1 268  ? 37.389  1.148   -66.995 1.00 61.55  ? 417  GLY   A O     1 
ATOM   1113 N  N     . LYS   A 1 269  ? 36.577  -0.599  -68.208 1.00 63.97  ? 418  LYS   A N     1 
ATOM   1114 C  CA    . LYS   A 1 269  ? 35.707  0.191   -69.120 1.00 63.93  ? 418  LYS   A CA    1 
ATOM   1115 C  C     . LYS   A 1 269  ? 34.701  0.991   -68.284 1.00 63.30  ? 418  LYS   A C     1 
ATOM   1116 O  O     . LYS   A 1 269  ? 34.639  2.219   -68.453 1.00 63.45  ? 418  LYS   A O     1 
ATOM   1117 C  CB    . LYS   A 1 269  ? 34.972  -0.723  -70.105 1.00 64.33  ? 418  LYS   A CB    1 
ATOM   1118 C  CG    . LYS   A 1 269  ? 35.860  -1.501  -71.068 1.00 65.71  ? 418  LYS   A CG    1 
ATOM   1119 C  CD    . LYS   A 1 269  ? 35.089  -2.324  -72.083 1.00 66.65  ? 418  LYS   A CD    1 
ATOM   1120 C  CE    . LYS   A 1 269  ? 34.303  -3.470  -71.474 1.00 68.16  ? 418  LYS   A CE    1 
ATOM   1121 N  NZ    . LYS   A 1 269  ? 35.184  -4.501  -70.874 1.00 69.70  ? 418  LYS   A NZ    1 
ATOM   1122 N  N     . THR   A 1 270  ? 33.970  0.308   -67.398 1.00 62.18  ? 419  THR   A N     1 
ATOM   1123 C  CA    . THR   A 1 270  ? 32.826  0.853   -66.615 1.00 61.54  ? 419  THR   A CA    1 
ATOM   1124 C  C     . THR   A 1 270  ? 33.307  1.917   -65.619 1.00 61.02  ? 419  THR   A C     1 
ATOM   1125 O  O     . THR   A 1 270  ? 32.703  3.014   -65.591 1.00 59.91  ? 419  THR   A O     1 
ATOM   1126 C  CB    . THR   A 1 270  ? 32.084  -0.273  -65.880 1.00 61.27  ? 419  THR   A CB    1 
ATOM   1127 O  OG1   . THR   A 1 270  ? 31.619  -1.217  -66.845 1.00 60.02  ? 419  THR   A OG1   1 
ATOM   1128 C  CG2   . THR   A 1 270  ? 30.923  0.232   -65.051 1.00 61.65  ? 419  THR   A CG2   1 
ATOM   1129 N  N     . THR   A 1 271  ? 34.340  1.598   -64.831 1.00 58.86  ? 420  THR   A N     1 
ATOM   1130 C  CA    . THR   A 1 271  ? 34.764  2.366   -63.628 1.00 57.45  ? 420  THR   A CA    1 
ATOM   1131 C  C     . THR   A 1 271  ? 35.740  3.490   -63.993 1.00 56.46  ? 420  THR   A C     1 
ATOM   1132 O  O     . THR   A 1 271  ? 35.734  4.502   -63.272 1.00 57.82  ? 420  THR   A O     1 
ATOM   1133 C  CB    . THR   A 1 271  ? 35.388  1.444   -62.573 1.00 58.05  ? 420  THR   A CB    1 
ATOM   1134 O  OG1   . THR   A 1 271  ? 36.403  0.668   -63.208 1.00 58.22  ? 420  THR   A OG1   1 
ATOM   1135 C  CG2   . THR   A 1 271  ? 34.376  0.531   -61.917 1.00 58.85  ? 420  THR   A CG2   1 
ATOM   1136 N  N     . GLN   A 1 272  ? 36.543  3.328   -65.052 1.00 56.54  ? 421  GLN   A N     1 
ATOM   1137 C  CA    . GLN   A 1 272  ? 37.681  4.237   -65.372 1.00 56.67  ? 421  GLN   A CA    1 
ATOM   1138 C  C     . GLN   A 1 272  ? 37.302  5.244   -66.467 1.00 55.84  ? 421  GLN   A C     1 
ATOM   1139 O  O     . GLN   A 1 272  ? 37.686  6.419   -66.324 1.00 56.14  ? 421  GLN   A O     1 
ATOM   1140 C  CB    . GLN   A 1 272  ? 38.911  3.435   -65.797 1.00 57.24  ? 421  GLN   A CB    1 
ATOM   1141 C  CG    . GLN   A 1 272  ? 39.287  2.331   -64.819 1.00 57.78  ? 421  GLN   A CG    1 
ATOM   1142 C  CD    . GLN   A 1 272  ? 39.812  2.886   -63.518 1.00 58.57  ? 421  GLN   A CD    1 
ATOM   1143 O  OE1   . GLN   A 1 272  ? 40.887  3.480   -63.469 1.00 60.02  ? 421  GLN   A OE1   1 
ATOM   1144 N  NE2   . GLN   A 1 272  ? 39.056  2.694   -62.449 1.00 59.78  ? 421  GLN   A NE2   1 
ATOM   1145 N  N     . VAL   A 1 273  ? 36.603  4.813   -67.523 1.00 55.46  ? 422  VAL   A N     1 
ATOM   1146 C  CA    . VAL   A 1 273  ? 36.364  5.637   -68.750 1.00 55.39  ? 422  VAL   A CA    1 
ATOM   1147 C  C     . VAL   A 1 273  ? 35.643  6.931   -68.376 1.00 55.12  ? 422  VAL   A C     1 
ATOM   1148 O  O     . VAL   A 1 273  ? 36.032  7.998   -68.840 1.00 55.22  ? 422  VAL   A O     1 
ATOM   1149 C  CB    . VAL   A 1 273  ? 35.604  4.864   -69.844 1.00 56.06  ? 422  VAL   A CB    1 
ATOM   1150 C  CG1   . VAL   A 1 273  ? 35.123  5.784   -70.958 1.00 56.55  ? 422  VAL   A CG1   1 
ATOM   1151 C  CG2   . VAL   A 1 273  ? 36.446  3.731   -70.413 1.00 56.17  ? 422  VAL   A CG2   1 
ATOM   1152 N  N     . PRO   A 1 274  ? 34.568  6.899   -67.553 1.00 56.71  ? 423  PRO   A N     1 
ATOM   1153 C  CA    . PRO   A 1 274  ? 33.888  8.132   -67.150 1.00 57.21  ? 423  PRO   A CA    1 
ATOM   1154 C  C     . PRO   A 1 274  ? 34.824  9.084   -66.387 1.00 57.53  ? 423  PRO   A C     1 
ATOM   1155 O  O     . PRO   A 1 274  ? 34.734  10.279  -66.604 1.00 56.30  ? 423  PRO   A O     1 
ATOM   1156 C  CB    . PRO   A 1 274  ? 32.735  7.651   -66.253 1.00 57.17  ? 423  PRO   A CB    1 
ATOM   1157 C  CG    . PRO   A 1 274  ? 32.547  6.194   -66.628 1.00 57.25  ? 423  PRO   A CG    1 
ATOM   1158 C  CD    . PRO   A 1 274  ? 33.934  5.701   -66.980 1.00 56.90  ? 423  PRO   A CD    1 
ATOM   1159 N  N     . GLN   A 1 275  ? 35.694  8.532   -65.530 1.00 59.28  ? 424  GLN   A N     1 
ATOM   1160 C  CA    . GLN   A 1 275  ? 36.683  9.291   -64.714 1.00 59.08  ? 424  GLN   A CA    1 
ATOM   1161 C  C     . GLN   A 1 275  ? 37.703  9.954   -65.646 1.00 59.59  ? 424  GLN   A C     1 
ATOM   1162 O  O     . GLN   A 1 275  ? 37.901  11.178  -65.514 1.00 62.28  ? 424  GLN   A O     1 
ATOM   1163 C  CB    . GLN   A 1 275  ? 37.391  8.383   -63.705 1.00 58.18  ? 424  GLN   A CB    1 
ATOM   1164 C  CG    . GLN   A 1 275  ? 36.470  7.801   -62.643 1.00 57.10  ? 424  GLN   A CG    1 
ATOM   1165 C  CD    . GLN   A 1 275  ? 37.230  7.356   -61.416 1.00 57.05  ? 424  GLN   A CD    1 
ATOM   1166 O  OE1   . GLN   A 1 275  ? 37.651  8.169   -60.598 1.00 56.82  ? 424  GLN   A OE1   1 
ATOM   1167 N  NE2   . GLN   A 1 275  ? 37.405  6.052   -61.270 1.00 57.06  ? 424  GLN   A NE2   1 
ATOM   1168 N  N     . PHE   A 1 276  ? 38.315  9.178   -66.550 1.00 58.78  ? 425  PHE   A N     1 
ATOM   1169 C  CA    . PHE   A 1 276  ? 39.268  9.669   -67.583 1.00 59.54  ? 425  PHE   A CA    1 
ATOM   1170 C  C     . PHE   A 1 276  ? 38.688  10.919  -68.253 1.00 60.48  ? 425  PHE   A C     1 
ATOM   1171 O  O     . PHE   A 1 276  ? 39.374  11.956  -68.277 1.00 62.06  ? 425  PHE   A O     1 
ATOM   1172 C  CB    . PHE   A 1 276  ? 39.562  8.600   -68.642 1.00 59.14  ? 425  PHE   A CB    1 
ATOM   1173 C  CG    . PHE   A 1 276  ? 40.364  7.406   -68.184 1.00 59.42  ? 425  PHE   A CG    1 
ATOM   1174 C  CD1   . PHE   A 1 276  ? 41.122  7.436   -67.021 1.00 60.33  ? 425  PHE   A CD1   1 
ATOM   1175 C  CD2   . PHE   A 1 276  ? 40.389  6.250   -68.950 1.00 60.64  ? 425  PHE   A CD2   1 
ATOM   1176 C  CE1   . PHE   A 1 276  ? 41.857  6.330   -66.623 1.00 60.57  ? 425  PHE   A CE1   1 
ATOM   1177 C  CE2   . PHE   A 1 276  ? 41.129  5.146   -68.553 1.00 61.24  ? 425  PHE   A CE2   1 
ATOM   1178 C  CZ    . PHE   A 1 276  ? 41.861  5.188   -67.389 1.00 60.91  ? 425  PHE   A CZ    1 
ATOM   1179 N  N     . ILE   A 1 277  ? 37.453  10.814  -68.754 1.00 62.31  ? 426  ILE   A N     1 
ATOM   1180 C  CA    . ILE   A 1 277  ? 36.721  11.898  -69.480 1.00 63.00  ? 426  ILE   A CA    1 
ATOM   1181 C  C     . ILE   A 1 277  ? 36.568  13.110  -68.550 1.00 63.31  ? 426  ILE   A C     1 
ATOM   1182 O  O     . ILE   A 1 277  ? 36.868  14.226  -69.002 1.00 62.88  ? 426  ILE   A O     1 
ATOM   1183 C  CB    . ILE   A 1 277  ? 35.358  11.392  -70.002 1.00 63.39  ? 426  ILE   A CB    1 
ATOM   1184 C  CG1   . ILE   A 1 277  ? 35.524  10.284  -71.046 1.00 64.14  ? 426  ILE   A CG1   1 
ATOM   1185 C  CG2   . ILE   A 1 277  ? 34.520  12.542  -70.548 1.00 63.15  ? 426  ILE   A CG2   1 
ATOM   1186 C  CD1   . ILE   A 1 277  ? 34.298  9.421   -71.229 1.00 64.74  ? 426  ILE   A CD1   1 
ATOM   1187 N  N     . LEU   A 1 278  ? 36.116  12.894  -67.309 1.00 64.77  ? 427  LEU   A N     1 
ATOM   1188 C  CA    . LEU   A 1 278  ? 35.836  13.969  -66.315 1.00 65.48  ? 427  LEU   A CA    1 
ATOM   1189 C  C     . LEU   A 1 278  ? 37.144  14.666  -65.925 1.00 68.45  ? 427  LEU   A C     1 
ATOM   1190 O  O     . LEU   A 1 278  ? 37.189  15.912  -65.997 1.00 67.57  ? 427  LEU   A O     1 
ATOM   1191 C  CB    . LEU   A 1 278  ? 35.149  13.366  -65.084 1.00 64.09  ? 427  LEU   A CB    1 
ATOM   1192 C  CG    . LEU   A 1 278  ? 34.958  14.316  -63.900 1.00 62.23  ? 427  LEU   A CG    1 
ATOM   1193 C  CD1   . LEU   A 1 278  ? 34.061  15.484  -64.272 1.00 60.74  ? 427  LEU   A CD1   1 
ATOM   1194 C  CD2   . LEU   A 1 278  ? 34.396  13.578  -62.696 1.00 62.80  ? 427  LEU   A CD2   1 
ATOM   1195 N  N     . ASP   A 1 279  ? 38.153  13.886  -65.515 1.00 71.55  ? 428  ASP   A N     1 
ATOM   1196 C  CA    . ASP   A 1 279  ? 39.500  14.375  -65.109 1.00 73.24  ? 428  ASP   A CA    1 
ATOM   1197 C  C     . ASP   A 1 279  ? 40.114  15.203  -66.247 1.00 75.22  ? 428  ASP   A C     1 
ATOM   1198 O  O     . ASP   A 1 279  ? 40.731  16.240  -65.943 1.00 79.43  ? 428  ASP   A O     1 
ATOM   1199 C  CB    . ASP   A 1 279  ? 40.425  13.217  -64.716 1.00 73.30  ? 428  ASP   A CB    1 
ATOM   1200 C  CG    . ASP   A 1 279  ? 40.169  12.653  -63.327 1.00 73.89  ? 428  ASP   A CG    1 
ATOM   1201 O  OD1   . ASP   A 1 279  ? 39.865  13.448  -62.415 1.00 74.22  ? 428  ASP   A OD1   1 
ATOM   1202 O  OD2   . ASP   A 1 279  ? 40.287  11.421  -63.166 1.00 74.45  ? 428  ASP   A OD2   1 
ATOM   1203 N  N     . ASP   A 1 280  ? 39.941  14.766  -67.500 1.00 74.24  ? 429  ASP   A N     1 
ATOM   1204 C  CA    . ASP   A 1 280  ? 40.492  15.435  -68.711 1.00 74.51  ? 429  ASP   A CA    1 
ATOM   1205 C  C     . ASP   A 1 280  ? 39.917  16.853  -68.832 1.00 75.12  ? 429  ASP   A C     1 
ATOM   1206 O  O     . ASP   A 1 280  ? 40.638  17.733  -69.333 1.00 78.23  ? 429  ASP   A O     1 
ATOM   1207 C  CB    . ASP   A 1 280  ? 40.218  14.618  -69.976 1.00 74.89  ? 429  ASP   A CB    1 
ATOM   1208 C  CG    . ASP   A 1 280  ? 40.960  15.125  -71.201 1.00 76.70  ? 429  ASP   A CG    1 
ATOM   1209 O  OD1   . ASP   A 1 280  ? 42.208  15.124  -71.172 1.00 77.43  ? 429  ASP   A OD1   1 
ATOM   1210 O  OD2   . ASP   A 1 280  ? 40.284  15.525  -72.171 1.00 77.34  ? 429  ASP   A OD2   1 
ATOM   1211 N  N     . PHE   A 1 281  ? 38.669  17.063  -68.400 1.00 74.92  ? 430  PHE   A N     1 
ATOM   1212 C  CA    . PHE   A 1 281  ? 37.976  18.380  -68.417 1.00 75.48  ? 430  PHE   A CA    1 
ATOM   1213 C  C     . PHE   A 1 281  ? 38.394  19.196  -67.185 1.00 79.51  ? 430  PHE   A C     1 
ATOM   1214 O  O     . PHE   A 1 281  ? 38.583  20.422  -67.318 1.00 79.38  ? 430  PHE   A O     1 
ATOM   1215 C  CB    . PHE   A 1 281  ? 36.457  18.197  -68.508 1.00 71.98  ? 430  PHE   A CB    1 
ATOM   1216 C  CG    . PHE   A 1 281  ? 35.917  18.080  -69.912 1.00 70.21  ? 430  PHE   A CG    1 
ATOM   1217 C  CD1   . PHE   A 1 281  ? 36.030  16.894  -70.624 1.00 69.13  ? 430  PHE   A CD1   1 
ATOM   1218 C  CD2   . PHE   A 1 281  ? 35.287  19.155  -70.524 1.00 68.55  ? 430  PHE   A CD2   1 
ATOM   1219 C  CE1   . PHE   A 1 281  ? 35.532  16.788  -71.914 1.00 67.79  ? 430  PHE   A CE1   1 
ATOM   1220 C  CE2   . PHE   A 1 281  ? 34.788  19.047  -71.814 1.00 67.72  ? 430  PHE   A CE2   1 
ATOM   1221 C  CZ    . PHE   A 1 281  ? 34.911  17.864  -72.506 1.00 68.11  ? 430  PHE   A CZ    1 
ATOM   1222 N  N     . ILE   A 1 282  ? 38.534  18.539  -66.027 1.00 83.63  ? 431  ILE   A N     1 
ATOM   1223 C  CA    . ILE   A 1 282  ? 38.988  19.165  -64.746 1.00 86.68  ? 431  ILE   A CA    1 
ATOM   1224 C  C     . ILE   A 1 282  ? 40.424  19.672  -64.929 1.00 88.50  ? 431  ILE   A C     1 
ATOM   1225 O  O     . ILE   A 1 282  ? 40.644  20.890  -64.759 1.00 89.72  ? 431  ILE   A O     1 
ATOM   1226 C  CB    . ILE   A 1 282  ? 38.867  18.175  -63.565 1.00 86.23  ? 431  ILE   A CB    1 
ATOM   1227 C  CG1   . ILE   A 1 282  ? 37.403  17.925  -63.190 1.00 84.51  ? 431  ILE   A CG1   1 
ATOM   1228 C  CG2   . ILE   A 1 282  ? 39.681  18.648  -62.367 1.00 85.89  ? 431  ILE   A CG2   1 
ATOM   1229 C  CD1   . ILE   A 1 282  ? 37.194  16.776  -62.229 1.00 83.38  ? 431  ILE   A CD1   1 
ATOM   1230 N  N     . GLN   A 1 283  ? 41.344  18.765  -65.280 1.00 89.20  ? 432  GLN   A N     1 
ATOM   1231 C  CA    . GLN   A 1 283  ? 42.809  19.013  -65.397 1.00 89.79  ? 432  GLN   A CA    1 
ATOM   1232 C  C     . GLN   A 1 283  ? 43.090  20.096  -66.447 1.00 87.67  ? 432  GLN   A C     1 
ATOM   1233 O  O     . GLN   A 1 283  ? 44.059  20.852  -66.248 1.00 88.90  ? 432  GLN   A O     1 
ATOM   1234 C  CB    . GLN   A 1 283  ? 43.545  17.720  -65.759 1.00 92.38  ? 432  GLN   A CB    1 
ATOM   1235 C  CG    . GLN   A 1 283  ? 43.553  16.684  -64.641 1.00 94.59  ? 432  GLN   A CG    1 
ATOM   1236 C  CD    . GLN   A 1 283  ? 44.591  16.979  -63.586 1.00 96.05  ? 432  GLN   A CD    1 
ATOM   1237 O  OE1   . GLN   A 1 283  ? 45.793  16.936  -63.841 1.00 95.69  ? 432  GLN   A OE1   1 
ATOM   1238 N  NE2   . GLN   A 1 283  ? 44.130  17.274  -62.380 1.00 95.10  ? 432  GLN   A NE2   1 
ATOM   1239 N  N     . ASN   A 1 284  ? 42.283  20.166  -67.513 1.00 85.71  ? 433  ASN   A N     1 
ATOM   1240 C  CA    . ASN   A 1 284  ? 42.459  21.126  -68.639 1.00 85.82  ? 433  ASN   A CA    1 
ATOM   1241 C  C     . ASN   A 1 284  ? 41.545  22.346  -68.449 1.00 85.52  ? 433  ASN   A C     1 
ATOM   1242 O  O     . ASN   A 1 284  ? 41.243  23.014  -69.459 1.00 84.62  ? 433  ASN   A O     1 
ATOM   1243 C  CB    . ASN   A 1 284  ? 42.229  20.450  -69.996 1.00 86.88  ? 433  ASN   A CB    1 
ATOM   1244 C  CG    . ASN   A 1 284  ? 43.217  19.337  -70.284 1.00 87.87  ? 433  ASN   A CG    1 
ATOM   1245 O  OD1   . ASN   A 1 284  ? 44.377  19.403  -69.879 1.00 87.69  ? 433  ASN   A OD1   1 
ATOM   1246 N  ND2   . ASN   A 1 284  ? 42.774  18.312  -70.994 1.00 88.33  ? 433  ASN   A ND2   1 
ATOM   1247 N  N     . ASP   A 1 285  ? 41.126  22.626  -67.207 1.00 87.17  ? 434  ASP   A N     1 
ATOM   1248 C  CA    . ASP   A 1 285  ? 40.506  23.911  -66.776 1.00 88.90  ? 434  ASP   A CA    1 
ATOM   1249 C  C     . ASP   A 1 285  ? 39.144  24.114  -67.456 1.00 90.00  ? 434  ASP   A C     1 
ATOM   1250 O  O     . ASP   A 1 285  ? 38.824  25.273  -67.794 1.00 88.92  ? 434  ASP   A O     1 
ATOM   1251 C  CB    . ASP   A 1 285  ? 41.441  25.091  -67.066 1.00 88.59  ? 434  ASP   A CB    1 
ATOM   1252 C  CG    . ASP   A 1 285  ? 42.867  24.888  -66.580 1.00 88.79  ? 434  ASP   A CG    1 
ATOM   1253 O  OD1   . ASP   A 1 285  ? 43.057  24.768  -65.352 1.00 86.22  ? 434  ASP   A OD1   1 
ATOM   1254 O  OD2   . ASP   A 1 285  ? 43.778  24.843  -67.435 1.00 88.10  ? 434  ASP   A OD2   1 
ATOM   1255 N  N     . ARG   A 1 286  ? 38.364  23.040  -67.629 1.00 91.84  ? 435  ARG   A N     1 
ATOM   1256 C  CA    . ARG   A 1 286  ? 37.033  23.061  -68.299 1.00 90.96  ? 435  ARG   A CA    1 
ATOM   1257 C  C     . ARG   A 1 286  ? 36.059  22.132  -67.558 1.00 87.18  ? 435  ARG   A C     1 
ATOM   1258 O  O     . ARG   A 1 286  ? 35.188  21.539  -68.222 1.00 85.03  ? 435  ARG   A O     1 
ATOM   1259 C  CB    . ARG   A 1 286  ? 37.186  22.663  -69.772 1.00 94.52  ? 435  ARG   A CB    1 
ATOM   1260 C  CG    . ARG   A 1 286  ? 37.725  23.769  -70.667 1.00 99.23  ? 435  ARG   A CG    1 
ATOM   1261 C  CD    . ARG   A 1 286  ? 38.172  23.244  -72.019 1.00 104.51 ? 435  ARG   A CD    1 
ATOM   1262 N  NE    . ARG   A 1 286  ? 38.394  24.309  -72.992 1.00 109.35 ? 435  ARG   A NE    1 
ATOM   1263 C  CZ    . ARG   A 1 286  ? 38.840  24.129  -74.235 1.00 111.26 ? 435  ARG   A CZ    1 
ATOM   1264 N  NH1   . ARG   A 1 286  ? 39.002  25.173  -75.032 1.00 112.06 ? 435  ARG   A NH1   1 
ATOM   1265 N  NH2   . ARG   A 1 286  ? 39.122  22.916  -74.681 1.00 110.40 ? 435  ARG   A NH2   1 
ATOM   1266 N  N     . ALA   A 1 287  ? 36.182  22.037  -66.229 1.00 84.77  ? 436  ALA   A N     1 
ATOM   1267 C  CA    . ALA   A 1 287  ? 35.364  21.159  -65.357 1.00 81.26  ? 436  ALA   A CA    1 
ATOM   1268 C  C     . ALA   A 1 287  ? 33.873  21.492  -65.515 1.00 78.13  ? 436  ALA   A C     1 
ATOM   1269 O  O     . ALA   A 1 287  ? 33.055  20.555  -65.468 1.00 77.93  ? 436  ALA   A O     1 
ATOM   1270 C  CB    . ALA   A 1 287  ? 35.806  21.290  -63.919 1.00 80.42  ? 436  ALA   A CB    1 
ATOM   1271 N  N     . ALA   A 1 288  ? 33.540  22.772  -65.706 1.00 75.75  ? 437  ALA   A N     1 
ATOM   1272 C  CA    . ALA   A 1 288  ? 32.156  23.291  -65.829 1.00 76.36  ? 437  ALA   A CA    1 
ATOM   1273 C  C     . ALA   A 1 288  ? 31.484  22.787  -67.116 1.00 76.70  ? 437  ALA   A C     1 
ATOM   1274 O  O     . ALA   A 1 288  ? 30.239  22.777  -67.155 1.00 76.46  ? 437  ALA   A O     1 
ATOM   1275 C  CB    . ALA   A 1 288  ? 32.175  24.798  -65.783 1.00 76.19  ? 437  ALA   A CB    1 
ATOM   1276 N  N     . GLU   A 1 289  ? 32.270  22.389  -68.123 1.00 78.13  ? 438  GLU   A N     1 
ATOM   1277 C  CA    . GLU   A 1 289  ? 31.781  21.958  -69.463 1.00 79.37  ? 438  GLU   A CA    1 
ATOM   1278 C  C     . GLU   A 1 289  ? 31.582  20.434  -69.514 1.00 77.68  ? 438  GLU   A C     1 
ATOM   1279 O  O     . GLU   A 1 289  ? 31.370  19.913  -70.631 1.00 77.33  ? 438  GLU   A O     1 
ATOM   1280 C  CB    . GLU   A 1 289  ? 32.774  22.388  -70.546 1.00 81.98  ? 438  GLU   A CB    1 
ATOM   1281 C  CG    . GLU   A 1 289  ? 33.046  23.880  -70.572 1.00 84.30  ? 438  GLU   A CG    1 
ATOM   1282 C  CD    . GLU   A 1 289  ? 33.882  24.341  -71.753 1.00 87.04  ? 438  GLU   A CD    1 
ATOM   1283 O  OE1   . GLU   A 1 289  ? 34.809  23.602  -72.148 1.00 86.71  ? 438  GLU   A OE1   1 
ATOM   1284 O  OE2   . GLU   A 1 289  ? 33.598  25.436  -72.282 1.00 90.16  ? 438  GLU   A OE2   1 
ATOM   1285 N  N     . CYS   A 1 290  ? 31.637  19.745  -68.368 1.00 75.17  ? 439  CYS   A N     1 
ATOM   1286 C  CA    . CYS   A 1 290  ? 31.536  18.263  -68.266 1.00 73.55  ? 439  CYS   A CA    1 
ATOM   1287 C  C     . CYS   A 1 290  ? 30.350  17.862  -67.379 1.00 73.36  ? 439  CYS   A C     1 
ATOM   1288 O  O     . CYS   A 1 290  ? 30.308  18.288  -66.206 1.00 72.49  ? 439  CYS   A O     1 
ATOM   1289 C  CB    . CYS   A 1 290  ? 32.818  17.659  -67.708 1.00 73.77  ? 439  CYS   A CB    1 
ATOM   1290 S  SG    . CYS   A 1 290  ? 32.802  15.847  -67.692 1.00 75.48  ? 439  CYS   A SG    1 
ATOM   1291 N  N     . ASN   A 1 291  ? 29.429  17.072  -67.940 1.00 72.33  ? 440  ASN   A N     1 
ATOM   1292 C  CA    . ASN   A 1 291  ? 28.313  16.392  -67.229 1.00 69.04  ? 440  ASN   A CA    1 
ATOM   1293 C  C     . ASN   A 1 291  ? 28.042  15.062  -67.943 1.00 65.77  ? 440  ASN   A C     1 
ATOM   1294 O  O     . ASN   A 1 291  ? 27.501  15.101  -69.063 1.00 65.70  ? 440  ASN   A O     1 
ATOM   1295 C  CB    . ASN   A 1 291  ? 27.058  17.267  -67.172 1.00 70.40  ? 440  ASN   A CB    1 
ATOM   1296 C  CG    . ASN   A 1 291  ? 27.107  18.319  -66.083 1.00 73.08  ? 440  ASN   A CG    1 
ATOM   1297 O  OD1   . ASN   A 1 291  ? 26.927  19.505  -66.351 1.00 75.77  ? 440  ASN   A OD1   1 
ATOM   1298 N  ND2   . ASN   A 1 291  ? 27.342  17.896  -64.851 1.00 73.66  ? 440  ASN   A ND2   1 
ATOM   1299 N  N     . ILE   A 1 292  ? 28.425  13.940  -67.326 1.00 63.33  ? 441  ILE   A N     1 
ATOM   1300 C  CA    . ILE   A 1 292  ? 28.374  12.576  -67.935 1.00 62.38  ? 441  ILE   A CA    1 
ATOM   1301 C  C     . ILE   A 1 292  ? 27.148  11.824  -67.398 1.00 61.53  ? 441  ILE   A C     1 
ATOM   1302 O  O     . ILE   A 1 292  ? 26.965  11.786  -66.165 1.00 63.12  ? 441  ILE   A O     1 
ATOM   1303 C  CB    . ILE   A 1 292  ? 29.684  11.803  -67.665 1.00 63.04  ? 441  ILE   A CB    1 
ATOM   1304 C  CG1   . ILE   A 1 292  ? 30.919  12.598  -68.102 1.00 63.16  ? 441  ILE   A CG1   1 
ATOM   1305 C  CG2   . ILE   A 1 292  ? 29.644  10.426  -68.315 1.00 63.38  ? 441  ILE   A CG2   1 
ATOM   1306 C  CD1   . ILE   A 1 292  ? 32.239  11.900  -67.844 1.00 61.96  ? 441  ILE   A CD1   1 
ATOM   1307 N  N     . VAL   A 1 293  ? 26.341  11.259  -68.301 1.00 59.84  ? 442  VAL   A N     1 
ATOM   1308 C  CA    . VAL   A 1 293  ? 25.293  10.238  -67.999 1.00 58.38  ? 442  VAL   A CA    1 
ATOM   1309 C  C     . VAL   A 1 293  ? 25.870  8.865   -68.362 1.00 55.88  ? 442  VAL   A C     1 
ATOM   1310 O  O     . VAL   A 1 293  ? 26.390  8.730   -69.483 1.00 56.12  ? 442  VAL   A O     1 
ATOM   1311 C  CB    . VAL   A 1 293  ? 23.984  10.512  -68.767 1.00 58.99  ? 442  VAL   A CB    1 
ATOM   1312 C  CG1   . VAL   A 1 293  ? 22.975  9.387   -68.582 1.00 59.83  ? 442  VAL   A CG1   1 
ATOM   1313 C  CG2   . VAL   A 1 293  ? 23.368  11.847  -68.383 1.00 58.41  ? 442  VAL   A CG2   1 
ATOM   1314 N  N     . VAL   A 1 294  ? 25.794  7.898   -67.445 1.00 54.33  ? 443  VAL   A N     1 
ATOM   1315 C  CA    . VAL   A 1 294  ? 26.246  6.491   -67.660 1.00 55.24  ? 443  VAL   A CA    1 
ATOM   1316 C  C     . VAL   A 1 294  ? 25.051  5.568   -67.398 1.00 55.02  ? 443  VAL   A C     1 
ATOM   1317 O  O     . VAL   A 1 294  ? 24.554  5.553   -66.257 1.00 53.83  ? 443  VAL   A O     1 
ATOM   1318 C  CB    . VAL   A 1 294  ? 27.452  6.132   -66.768 1.00 55.89  ? 443  VAL   A CB    1 
ATOM   1319 C  CG1   . VAL   A 1 294  ? 28.005  4.748   -67.082 1.00 54.97  ? 443  VAL   A CG1   1 
ATOM   1320 C  CG2   . VAL   A 1 294  ? 28.555  7.176   -66.861 1.00 56.46  ? 443  VAL   A CG2   1 
ATOM   1321 N  N     . THR   A 1 295  ? 24.602  4.841   -68.423 1.00 55.91  ? 444  THR   A N     1 
ATOM   1322 C  CA    . THR   A 1 295  ? 23.440  3.917   -68.355 1.00 56.88  ? 444  THR   A CA    1 
ATOM   1323 C  C     . THR   A 1 295  ? 23.957  2.501   -68.082 1.00 58.26  ? 444  THR   A C     1 
ATOM   1324 O  O     . THR   A 1 295  ? 24.915  2.087   -68.763 1.00 60.48  ? 444  THR   A O     1 
ATOM   1325 C  CB    . THR   A 1 295  ? 22.590  3.984   -69.632 1.00 56.45  ? 444  THR   A CB    1 
ATOM   1326 O  OG1   . THR   A 1 295  ? 23.226  3.215   -70.654 1.00 55.80  ? 444  THR   A OG1   1 
ATOM   1327 C  CG2   . THR   A 1 295  ? 22.363  5.399   -70.119 1.00 55.80  ? 444  THR   A CG2   1 
ATOM   1328 N  N     . GLN   A 1 296  ? 23.356  1.808   -67.112 1.00 59.23  ? 445  GLN   A N     1 
ATOM   1329 C  CA    . GLN   A 1 296  ? 23.647  0.388   -66.778 1.00 60.71  ? 445  GLN   A CA    1 
ATOM   1330 C  C     . GLN   A 1 296  ? 22.364  -0.421  -66.960 1.00 61.78  ? 445  GLN   A C     1 
ATOM   1331 O  O     . GLN   A 1 296  ? 21.291  0.032   -66.566 1.00 61.10  ? 445  GLN   A O     1 
ATOM   1332 C  CB    . GLN   A 1 296  ? 24.181  0.272   -65.348 1.00 62.07  ? 445  GLN   A CB    1 
ATOM   1333 C  CG    . GLN   A 1 296  ? 25.492  1.012   -65.109 1.00 61.68  ? 445  GLN   A CG    1 
ATOM   1334 C  CD    . GLN   A 1 296  ? 26.696  0.286   -65.661 1.00 61.10  ? 445  GLN   A CD    1 
ATOM   1335 O  OE1   . GLN   A 1 296  ? 26.759  -0.941  -65.677 1.00 61.78  ? 445  GLN   A OE1   1 
ATOM   1336 N  NE2   . GLN   A 1 296  ? 27.679  1.049   -66.107 1.00 61.18  ? 445  GLN   A NE2   1 
ATOM   1337 N  N     . PRO   A 1 297  ? 22.420  -1.621  -67.584 1.00 63.74  ? 446  PRO   A N     1 
ATOM   1338 C  CA    . PRO   A 1 297  ? 21.233  -2.461  -67.756 1.00 64.75  ? 446  PRO   A CA    1 
ATOM   1339 C  C     . PRO   A 1 297  ? 20.513  -2.846  -66.454 1.00 66.35  ? 446  PRO   A C     1 
ATOM   1340 O  O     . PRO   A 1 297  ? 19.294  -2.832  -66.443 1.00 69.46  ? 446  PRO   A O     1 
ATOM   1341 C  CB    . PRO   A 1 297  ? 21.785  -3.733  -68.415 1.00 64.75  ? 446  PRO   A CB    1 
ATOM   1342 C  CG    . PRO   A 1 297  ? 23.034  -3.270  -69.123 1.00 65.20  ? 446  PRO   A CG    1 
ATOM   1343 C  CD    . PRO   A 1 297  ? 23.614  -2.210  -68.211 1.00 65.09  ? 446  PRO   A CD    1 
ATOM   1344 N  N     . ARG   A 1 298  ? 21.272  -3.190  -65.408 1.00 66.65  ? 447  ARG   A N     1 
ATOM   1345 C  CA    . ARG   A 1 298  ? 20.742  -3.708  -64.116 1.00 68.60  ? 447  ARG   A CA    1 
ATOM   1346 C  C     . ARG   A 1 298  ? 20.656  -2.568  -63.095 1.00 67.55  ? 447  ARG   A C     1 
ATOM   1347 O  O     . ARG   A 1 298  ? 21.414  -1.590  -63.231 1.00 64.93  ? 447  ARG   A O     1 
ATOM   1348 C  CB    . ARG   A 1 298  ? 21.636  -4.831  -63.582 1.00 71.60  ? 447  ARG   A CB    1 
ATOM   1349 C  CG    . ARG   A 1 298  ? 21.920  -5.942  -64.584 1.00 75.00  ? 447  ARG   A CG    1 
ATOM   1350 C  CD    . ARG   A 1 298  ? 23.205  -6.677  -64.253 1.00 77.99  ? 447  ARG   A CD    1 
ATOM   1351 N  NE    . ARG   A 1 298  ? 23.607  -7.622  -65.287 1.00 80.78  ? 447  ARG   A NE    1 
ATOM   1352 C  CZ    . ARG   A 1 298  ? 23.200  -8.889  -65.374 1.00 84.63  ? 447  ARG   A CZ    1 
ATOM   1353 N  NH1   . ARG   A 1 298  ? 23.640  -9.653  -66.361 1.00 85.09  ? 447  ARG   A NH1   1 
ATOM   1354 N  NH2   . ARG   A 1 298  ? 22.358  -9.394  -64.487 1.00 85.46  ? 447  ARG   A NH2   1 
ATOM   1355 N  N     . ARG   A 1 299  ? 19.761  -2.706  -62.112 1.00 68.97  ? 448  ARG   A N     1 
ATOM   1356 C  CA    . ARG   A 1 299  ? 19.623  -1.795  -60.944 1.00 69.61  ? 448  ARG   A CA    1 
ATOM   1357 C  C     . ARG   A 1 299  ? 20.919  -1.847  -60.123 1.00 68.08  ? 448  ARG   A C     1 
ATOM   1358 O  O     . ARG   A 1 299  ? 21.511  -0.781  -59.886 1.00 67.91  ? 448  ARG   A O     1 
ATOM   1359 C  CB    . ARG   A 1 299  ? 18.413  -2.213  -60.100 1.00 72.07  ? 448  ARG   A CB    1 
ATOM   1360 C  CG    . ARG   A 1 299  ? 18.129  -1.321  -58.900 1.00 75.33  ? 448  ARG   A CG    1 
ATOM   1361 C  CD    . ARG   A 1 299  ? 17.301  -2.036  -57.846 1.00 79.32  ? 448  ARG   A CD    1 
ATOM   1362 N  NE    . ARG   A 1 299  ? 16.808  -1.132  -56.812 1.00 83.11  ? 448  ARG   A NE    1 
ATOM   1363 C  CZ    . ARG   A 1 299  ? 17.526  -0.657  -55.793 1.00 86.35  ? 448  ARG   A CZ    1 
ATOM   1364 N  NH1   . ARG   A 1 299  ? 18.799  -0.988  -55.647 1.00 86.99  ? 448  ARG   A NH1   1 
ATOM   1365 N  NH2   . ARG   A 1 299  ? 16.962  0.161   -54.919 1.00 87.50  ? 448  ARG   A NH2   1 
ATOM   1366 N  N     . ILE   A 1 300  ? 21.337  -3.054  -59.730 1.00 66.97  ? 449  ILE   A N     1 
ATOM   1367 C  CA    . ILE   A 1 300  ? 22.501  -3.318  -58.829 1.00 66.61  ? 449  ILE   A CA    1 
ATOM   1368 C  C     . ILE   A 1 300  ? 23.770  -2.670  -59.400 1.00 64.80  ? 449  ILE   A C     1 
ATOM   1369 O  O     . ILE   A 1 300  ? 24.571  -2.159  -58.597 1.00 66.11  ? 449  ILE   A O     1 
ATOM   1370 C  CB    . ILE   A 1 300  ? 22.685  -4.833  -58.586 1.00 67.70  ? 449  ILE   A CB    1 
ATOM   1371 C  CG1   . ILE   A 1 300  ? 23.741  -5.119  -57.514 1.00 68.58  ? 449  ILE   A CG1   1 
ATOM   1372 C  CG2   . ILE   A 1 300  ? 23.005  -5.570  -59.879 1.00 68.79  ? 449  ILE   A CG2   1 
ATOM   1373 C  CD1   . ILE   A 1 300  ? 23.431  -4.524  -56.157 1.00 70.24  ? 449  ILE   A CD1   1 
ATOM   1374 N  N     . SER   A 1 301  ? 23.956  -2.696  -60.723 1.00 62.68  ? 450  SER   A N     1 
ATOM   1375 C  CA    . SER   A 1 301  ? 25.159  -2.162  -61.415 1.00 61.73  ? 450  SER   A CA    1 
ATOM   1376 C  C     . SER   A 1 301  ? 25.207  -0.635  -61.281 1.00 61.35  ? 450  SER   A C     1 
ATOM   1377 O  O     . SER   A 1 301  ? 26.267  -0.114  -60.899 1.00 63.00  ? 450  SER   A O     1 
ATOM   1378 C  CB    . SER   A 1 301  ? 25.195  -2.588  -62.859 1.00 61.88  ? 450  SER   A CB    1 
ATOM   1379 O  OG    . SER   A 1 301  ? 25.211  -4.005  -62.965 1.00 63.09  ? 450  SER   A OG    1 
ATOM   1380 N  N     . ALA   A 1 302  ? 24.096  0.047   -61.572 1.00 60.52  ? 451  ALA   A N     1 
ATOM   1381 C  CA    . ALA   A 1 302  ? 23.953  1.522   -61.499 1.00 59.79  ? 451  ALA   A CA    1 
ATOM   1382 C  C     . ALA   A 1 302  ? 24.364  2.029   -60.110 1.00 59.27  ? 451  ALA   A C     1 
ATOM   1383 O  O     . ALA   A 1 302  ? 25.086  3.043   -60.039 1.00 60.11  ? 451  ALA   A O     1 
ATOM   1384 C  CB    . ALA   A 1 302  ? 22.532  1.916   -61.822 1.00 59.42  ? 451  ALA   A CB    1 
ATOM   1385 N  N     . VAL   A 1 303  ? 23.921  1.345   -59.051 1.00 57.48  ? 452  VAL   A N     1 
ATOM   1386 C  CA    . VAL   A 1 303  ? 24.133  1.752   -57.630 1.00 56.89  ? 452  VAL   A CA    1 
ATOM   1387 C  C     . VAL   A 1 303  ? 25.556  1.374   -57.200 1.00 57.29  ? 452  VAL   A C     1 
ATOM   1388 O  O     . VAL   A 1 303  ? 26.221  2.224   -56.579 1.00 58.62  ? 452  VAL   A O     1 
ATOM   1389 C  CB    . VAL   A 1 303  ? 23.077  1.118   -56.704 1.00 56.30  ? 452  VAL   A CB    1 
ATOM   1390 C  CG1   . VAL   A 1 303  ? 23.316  1.480   -55.245 1.00 57.99  ? 452  VAL   A CG1   1 
ATOM   1391 C  CG2   . VAL   A 1 303  ? 21.665  1.494   -57.123 1.00 55.72  ? 452  VAL   A CG2   1 
ATOM   1392 N  N     . SER   A 1 304  ? 25.994  0.148   -57.506 1.00 57.58  ? 453  SER   A N     1 
ATOM   1393 C  CA    . SER   A 1 304  ? 27.308  -0.422  -57.102 1.00 58.42  ? 453  SER   A CA    1 
ATOM   1394 C  C     . SER   A 1 304  ? 28.456  0.355   -57.757 1.00 57.74  ? 453  SER   A C     1 
ATOM   1395 O  O     . SER   A 1 304  ? 29.420  0.693   -57.042 1.00 57.45  ? 453  SER   A O     1 
ATOM   1396 C  CB    . SER   A 1 304  ? 27.390  -1.888  -57.437 1.00 58.91  ? 453  SER   A CB    1 
ATOM   1397 O  OG    . SER   A 1 304  ? 26.412  -2.620  -56.713 1.00 61.53  ? 453  SER   A OG    1 
ATOM   1398 N  N     . VAL   A 1 305  ? 28.356  0.609   -59.065 1.00 57.53  ? 454  VAL   A N     1 
ATOM   1399 C  CA    . VAL   A 1 305  ? 29.391  1.322   -59.873 1.00 58.09  ? 454  VAL   A CA    1 
ATOM   1400 C  C     . VAL   A 1 305  ? 29.529  2.755   -59.344 1.00 59.15  ? 454  VAL   A C     1 
ATOM   1401 O  O     . VAL   A 1 305  ? 30.674  3.229   -59.242 1.00 63.13  ? 454  VAL   A O     1 
ATOM   1402 C  CB    . VAL   A 1 305  ? 29.059  1.293   -61.379 1.00 57.78  ? 454  VAL   A CB    1 
ATOM   1403 C  CG1   . VAL   A 1 305  ? 29.877  2.305   -62.170 1.00 57.67  ? 454  VAL   A CG1   1 
ATOM   1404 C  CG2   . VAL   A 1 305  ? 29.230  -0.105  -61.960 1.00 56.63  ? 454  VAL   A CG2   1 
ATOM   1405 N  N     . ALA   A 1 306  ? 28.412  3.414   -59.019 1.00 58.44  ? 455  ALA   A N     1 
ATOM   1406 C  CA    . ALA   A 1 306  ? 28.387  4.771   -58.424 1.00 59.35  ? 455  ALA   A CA    1 
ATOM   1407 C  C     . ALA   A 1 306  ? 29.161  4.756   -57.101 1.00 59.46  ? 455  ALA   A C     1 
ATOM   1408 O  O     . ALA   A 1 306  ? 29.994  5.655   -56.894 1.00 60.00  ? 455  ALA   A O     1 
ATOM   1409 C  CB    . ALA   A 1 306  ? 26.966  5.236   -58.226 1.00 60.10  ? 455  ALA   A CB    1 
ATOM   1410 N  N     . GLU   A 1 307  ? 28.897  3.759   -56.253 1.00 61.12  ? 456  GLU   A N     1 
ATOM   1411 C  CA    . GLU   A 1 307  ? 29.559  3.581   -54.932 1.00 64.15  ? 456  GLU   A CA    1 
ATOM   1412 C  C     . GLU   A 1 307  ? 31.045  3.263   -55.135 1.00 64.13  ? 456  GLU   A C     1 
ATOM   1413 O  O     . GLU   A 1 307  ? 31.857  3.698   -54.296 1.00 62.87  ? 456  GLU   A O     1 
ATOM   1414 C  CB    . GLU   A 1 307  ? 28.871  2.479   -54.123 1.00 65.49  ? 456  GLU   A CB    1 
ATOM   1415 C  CG    . GLU   A 1 307  ? 27.568  2.928   -53.487 1.00 67.65  ? 456  GLU   A CG    1 
ATOM   1416 C  CD    . GLU   A 1 307  ? 26.887  1.879   -52.628 1.00 70.42  ? 456  GLU   A CD    1 
ATOM   1417 O  OE1   . GLU   A 1 307  ? 27.176  0.680   -52.818 1.00 71.40  ? 456  GLU   A OE1   1 
ATOM   1418 O  OE2   . GLU   A 1 307  ? 26.067  2.264   -51.769 1.00 73.54  ? 456  GLU   A OE2   1 
ATOM   1419 N  N     . ARG   A 1 308  ? 31.379  2.535   -56.204 1.00 65.12  ? 457  ARG   A N     1 
ATOM   1420 C  CA    . ARG   A 1 308  ? 32.766  2.094   -56.511 1.00 65.02  ? 457  ARG   A CA    1 
ATOM   1421 C  C     . ARG   A 1 308  ? 33.584  3.284   -57.023 1.00 63.80  ? 457  ARG   A C     1 
ATOM   1422 O  O     . ARG   A 1 308  ? 34.715  3.466   -56.537 1.00 67.18  ? 457  ARG   A O     1 
ATOM   1423 C  CB    . ARG   A 1 308  ? 32.764  0.948   -57.529 1.00 66.03  ? 457  ARG   A CB    1 
ATOM   1424 C  CG    . ARG   A 1 308  ? 34.148  0.533   -58.010 1.00 66.64  ? 457  ARG   A CG    1 
ATOM   1425 C  CD    . ARG   A 1 308  ? 35.087  0.159   -56.877 1.00 67.63  ? 457  ARG   A CD    1 
ATOM   1426 N  NE    . ARG   A 1 308  ? 36.463  0.021   -57.329 1.00 69.32  ? 457  ARG   A NE    1 
ATOM   1427 C  CZ    . ARG   A 1 308  ? 37.489  -0.322  -56.555 1.00 69.72  ? 457  ARG   A CZ    1 
ATOM   1428 N  NH1   . ARG   A 1 308  ? 37.308  -0.576  -55.268 1.00 69.68  ? 457  ARG   A NH1   1 
ATOM   1429 N  NH2   . ARG   A 1 308  ? 38.699  -0.413  -57.077 1.00 70.44  ? 457  ARG   A NH2   1 
ATOM   1430 N  N     . VAL   A 1 309  ? 33.043  4.052   -57.972 1.00 61.61  ? 458  VAL   A N     1 
ATOM   1431 C  CA    . VAL   A 1 309  ? 33.747  5.209   -58.603 1.00 62.00  ? 458  VAL   A CA    1 
ATOM   1432 C  C     . VAL   A 1 309  ? 33.905  6.315   -57.550 1.00 62.76  ? 458  VAL   A C     1 
ATOM   1433 O  O     . VAL   A 1 309  ? 34.959  6.976   -57.552 1.00 66.71  ? 458  VAL   A O     1 
ATOM   1434 C  CB    . VAL   A 1 309  ? 33.024  5.699   -59.877 1.00 60.90  ? 458  VAL   A CB    1 
ATOM   1435 C  CG1   . VAL   A 1 309  ? 33.647  6.963   -60.449 1.00 60.19  ? 458  VAL   A CG1   1 
ATOM   1436 C  CG2   . VAL   A 1 309  ? 32.986  4.619   -60.948 1.00 60.79  ? 458  VAL   A CG2   1 
ATOM   1437 N  N     . ALA   A 1 310  ? 32.914  6.493   -56.671 1.00 61.74  ? 459  ALA   A N     1 
ATOM   1438 C  CA    . ALA   A 1 310  ? 32.939  7.472   -55.557 1.00 61.44  ? 459  ALA   A CA    1 
ATOM   1439 C  C     . ALA   A 1 310  ? 34.126  7.169   -54.632 1.00 61.69  ? 459  ALA   A C     1 
ATOM   1440 O  O     . ALA   A 1 310  ? 34.916  8.094   -54.363 1.00 61.24  ? 459  ALA   A O     1 
ATOM   1441 C  CB    . ALA   A 1 310  ? 31.629  7.442   -54.811 1.00 62.07  ? 459  ALA   A CB    1 
ATOM   1442 N  N     . TYR   A 1 311  ? 34.245  5.917   -54.176 1.00 63.59  ? 460  TYR   A N     1 
ATOM   1443 C  CA    . TYR   A 1 311  ? 35.363  5.403   -53.338 1.00 65.82  ? 460  TYR   A CA    1 
ATOM   1444 C  C     . TYR   A 1 311  ? 36.705  5.668   -54.035 1.00 67.14  ? 460  TYR   A C     1 
ATOM   1445 O  O     . TYR   A 1 311  ? 37.675  6.038   -53.341 1.00 68.84  ? 460  TYR   A O     1 
ATOM   1446 C  CB    . TYR   A 1 311  ? 35.185  3.908   -53.049 1.00 67.13  ? 460  TYR   A CB    1 
ATOM   1447 C  CG    . TYR   A 1 311  ? 36.433  3.196   -52.587 1.00 68.99  ? 460  TYR   A CG    1 
ATOM   1448 C  CD1   . TYR   A 1 311  ? 37.364  2.725   -53.499 1.00 71.16  ? 460  TYR   A CD1   1 
ATOM   1449 C  CD2   . TYR   A 1 311  ? 36.686  2.989   -51.240 1.00 69.31  ? 460  TYR   A CD2   1 
ATOM   1450 C  CE1   . TYR   A 1 311  ? 38.516  2.073   -53.089 1.00 72.29  ? 460  TYR   A CE1   1 
ATOM   1451 C  CE2   . TYR   A 1 311  ? 37.832  2.337   -50.812 1.00 70.75  ? 460  TYR   A CE2   1 
ATOM   1452 C  CZ    . TYR   A 1 311  ? 38.752  1.878   -51.740 1.00 72.60  ? 460  TYR   A CZ    1 
ATOM   1453 O  OH    . TYR   A 1 311  ? 39.886  1.236   -51.337 1.00 74.97  ? 460  TYR   A OH    1 
ATOM   1454 N  N     . GLU   A 1 312  ? 36.755  5.473   -55.359 1.00 66.83  ? 461  GLU   A N     1 
ATOM   1455 C  CA    . GLU   A 1 312  ? 37.974  5.642   -56.200 1.00 65.12  ? 461  GLU   A CA    1 
ATOM   1456 C  C     . GLU   A 1 312  ? 38.356  7.126   -56.293 1.00 64.45  ? 461  GLU   A C     1 
ATOM   1457 O  O     . GLU   A 1 312  ? 39.511  7.402   -56.674 1.00 67.92  ? 461  GLU   A O     1 
ATOM   1458 C  CB    . GLU   A 1 312  ? 37.769  5.047   -57.598 1.00 63.72  ? 461  GLU   A CB    1 
ATOM   1459 C  CG    . GLU   A 1 312  ? 37.963  3.539   -57.660 1.00 61.91  ? 461  GLU   A CG    1 
ATOM   1460 C  CD    . GLU   A 1 312  ? 38.048  2.950   -59.061 1.00 60.22  ? 461  GLU   A CD    1 
ATOM   1461 O  OE1   . GLU   A 1 312  ? 38.309  3.713   -60.015 1.00 56.70  ? 461  GLU   A OE1   1 
ATOM   1462 O  OE2   . GLU   A 1 312  ? 37.856  1.724   -59.195 1.00 58.57  ? 461  GLU   A OE2   1 
ATOM   1463 N  N     . ARG   A 1 313  ? 37.429  8.040   -55.981 1.00 62.03  ? 462  ARG   A N     1 
ATOM   1464 C  CA    . ARG   A 1 313  ? 37.677  9.507   -55.918 1.00 63.10  ? 462  ARG   A CA    1 
ATOM   1465 C  C     . ARG   A 1 313  ? 37.666  9.982   -54.458 1.00 64.01  ? 462  ARG   A C     1 
ATOM   1466 O  O     . ARG   A 1 313  ? 37.609  11.213  -54.245 1.00 62.99  ? 462  ARG   A O     1 
ATOM   1467 C  CB    . ARG   A 1 313  ? 36.629  10.256  -56.744 1.00 62.99  ? 462  ARG   A CB    1 
ATOM   1468 C  CG    . ARG   A 1 313  ? 36.574  9.822   -58.200 1.00 62.89  ? 462  ARG   A CG    1 
ATOM   1469 C  CD    . ARG   A 1 313  ? 35.628  10.682  -59.009 1.00 63.22  ? 462  ARG   A CD    1 
ATOM   1470 N  NE    . ARG   A 1 313  ? 36.240  11.944  -59.400 1.00 63.64  ? 462  ARG   A NE    1 
ATOM   1471 C  CZ    . ARG   A 1 313  ? 37.129  12.091  -60.381 1.00 63.89  ? 462  ARG   A CZ    1 
ATOM   1472 N  NH1   . ARG   A 1 313  ? 37.537  11.047  -61.086 1.00 62.51  ? 462  ARG   A NH1   1 
ATOM   1473 N  NH2   . ARG   A 1 313  ? 37.613  13.291  -60.654 1.00 64.85  ? 462  ARG   A NH2   1 
ATOM   1474 N  N     . GLY   A 1 314  ? 37.738  9.047   -53.502 1.00 64.08  ? 463  GLY   A N     1 
ATOM   1475 C  CA    . GLY   A 1 314  ? 37.768  9.318   -52.051 1.00 64.69  ? 463  GLY   A CA    1 
ATOM   1476 C  C     . GLY   A 1 314  ? 36.530  10.065  -51.587 1.00 66.39  ? 463  GLY   A C     1 
ATOM   1477 O  O     . GLY   A 1 314  ? 36.672  10.975  -50.746 1.00 70.50  ? 463  GLY   A O     1 
ATOM   1478 N  N     . GLU   A 1 315  ? 35.358  9.691   -52.109 1.00 66.96  ? 464  GLU   A N     1 
ATOM   1479 C  CA    . GLU   A 1 315  ? 34.054  10.346  -51.822 1.00 66.91  ? 464  GLU   A CA    1 
ATOM   1480 C  C     . GLU   A 1 315  ? 33.010  9.288   -51.455 1.00 67.16  ? 464  GLU   A C     1 
ATOM   1481 O  O     . GLU   A 1 315  ? 33.314  8.082   -51.560 1.00 65.25  ? 464  GLU   A O     1 
ATOM   1482 C  CB    . GLU   A 1 315  ? 33.565  11.125  -53.044 1.00 67.04  ? 464  GLU   A CB    1 
ATOM   1483 C  CG    . GLU   A 1 315  ? 34.404  12.343  -53.380 1.00 68.67  ? 464  GLU   A CG    1 
ATOM   1484 C  CD    . GLU   A 1 315  ? 34.115  12.949  -54.744 1.00 71.02  ? 464  GLU   A CD    1 
ATOM   1485 O  OE1   . GLU   A 1 315  ? 33.152  12.497  -55.400 1.00 73.50  ? 464  GLU   A OE1   1 
ATOM   1486 O  OE2   . GLU   A 1 315  ? 34.853  13.870  -55.151 1.00 71.95  ? 464  GLU   A OE2   1 
ATOM   1487 N  N     . GLU   A 1 316  ? 31.834  9.747   -51.021 1.00 69.16  ? 465  GLU   A N     1 
ATOM   1488 C  CA    . GLU   A 1 316  ? 30.562  8.979   -51.031 1.00 70.18  ? 465  GLU   A CA    1 
ATOM   1489 C  C     . GLU   A 1 316  ? 29.743  9.482   -52.218 1.00 67.56  ? 465  GLU   A C     1 
ATOM   1490 O  O     . GLU   A 1 316  ? 30.000  10.574  -52.723 1.00 68.09  ? 465  GLU   A O     1 
ATOM   1491 C  CB    . GLU   A 1 316  ? 29.813  9.156   -49.707 1.00 73.53  ? 465  GLU   A CB    1 
ATOM   1492 C  CG    . GLU   A 1 316  ? 30.593  8.700   -48.482 1.00 76.05  ? 465  GLU   A CG    1 
ATOM   1493 C  CD    . GLU   A 1 316  ? 30.591  7.201   -48.221 1.00 79.49  ? 465  GLU   A CD    1 
ATOM   1494 O  OE1   . GLU   A 1 316  ? 30.616  6.426   -49.199 1.00 81.75  ? 465  GLU   A OE1   1 
ATOM   1495 O  OE2   . GLU   A 1 316  ? 30.563  6.807   -47.037 1.00 81.08  ? 465  GLU   A OE2   1 
ATOM   1496 N  N     . PRO   A 1 317  ? 28.761  8.708   -52.734 1.00 64.11  ? 466  PRO   A N     1 
ATOM   1497 C  CA    . PRO   A 1 317  ? 27.861  9.219   -53.767 1.00 62.95  ? 466  PRO   A CA    1 
ATOM   1498 C  C     . PRO   A 1 317  ? 27.111  10.460  -53.257 1.00 61.73  ? 466  PRO   A C     1 
ATOM   1499 O  O     . PRO   A 1 317  ? 26.673  10.444  -52.121 1.00 62.41  ? 466  PRO   A O     1 
ATOM   1500 C  CB    . PRO   A 1 317  ? 26.906  8.049   -54.049 1.00 62.93  ? 466  PRO   A CB    1 
ATOM   1501 C  CG    . PRO   A 1 317  ? 27.653  6.825   -53.561 1.00 63.69  ? 466  PRO   A CG    1 
ATOM   1502 C  CD    . PRO   A 1 317  ? 28.481  7.307   -52.387 1.00 64.03  ? 466  PRO   A CD    1 
ATOM   1503 N  N     . GLY   A 1 318  ? 26.992  11.490  -54.101 1.00 61.59  ? 467  GLY   A N     1 
ATOM   1504 C  CA    . GLY   A 1 318  ? 26.404  12.799  -53.751 1.00 63.23  ? 467  GLY   A CA    1 
ATOM   1505 C  C     . GLY   A 1 318  ? 27.336  13.961  -54.061 1.00 63.87  ? 467  GLY   A C     1 
ATOM   1506 O  O     . GLY   A 1 318  ? 26.904  15.117  -53.891 1.00 63.25  ? 467  GLY   A O     1 
ATOM   1507 N  N     . LYS   A 1 319  ? 28.565  13.677  -54.503 1.00 66.48  ? 468  LYS   A N     1 
ATOM   1508 C  CA    . LYS   A 1 319  ? 29.601  14.697  -54.813 1.00 69.83  ? 468  LYS   A CA    1 
ATOM   1509 C  C     . LYS   A 1 319  ? 29.829  14.700  -56.333 1.00 69.64  ? 468  LYS   A C     1 
ATOM   1510 O  O     . LYS   A 1 319  ? 28.952  15.230  -57.040 1.00 70.85  ? 468  LYS   A O     1 
ATOM   1511 C  CB    . LYS   A 1 319  ? 30.840  14.421  -53.952 1.00 74.62  ? 468  LYS   A CB    1 
ATOM   1512 C  CG    . LYS   A 1 319  ? 31.339  15.605  -53.134 1.00 77.68  ? 468  LYS   A CG    1 
ATOM   1513 C  CD    . LYS   A 1 319  ? 32.298  16.510  -53.883 1.00 79.51  ? 468  LYS   A CD    1 
ATOM   1514 C  CE    . LYS   A 1 319  ? 32.152  17.972  -53.512 1.00 80.65  ? 468  LYS   A CE    1 
ATOM   1515 N  NZ    . LYS   A 1 319  ? 33.468  18.626  -53.323 1.00 81.60  ? 468  LYS   A NZ    1 
ATOM   1516 N  N     . SER   A 1 320  ? 30.936  14.128  -56.823 1.00 68.75  ? 469  SER   A N     1 
ATOM   1517 C  CA    . SER   A 1 320  ? 31.269  14.023  -58.269 1.00 68.35  ? 469  SER   A CA    1 
ATOM   1518 C  C     . SER   A 1 320  ? 30.450  12.892  -58.901 1.00 68.30  ? 469  SER   A C     1 
ATOM   1519 O  O     . SER   A 1 320  ? 30.141  12.990  -60.102 1.00 69.00  ? 469  SER   A O     1 
ATOM   1520 C  CB    . SER   A 1 320  ? 32.749  13.810  -58.481 1.00 68.52  ? 469  SER   A CB    1 
ATOM   1521 O  OG    . SER   A 1 320  ? 33.165  12.556  -57.959 1.00 66.51  ? 469  SER   A OG    1 
ATOM   1522 N  N     . CYS   A 1 321  ? 30.128  11.860  -58.115 1.00 67.40  ? 470  CYS   A N     1 
ATOM   1523 C  CA    . CYS   A 1 321  ? 29.366  10.658  -58.543 1.00 65.61  ? 470  CYS   A CA    1 
ATOM   1524 C  C     . CYS   A 1 321  ? 28.001  10.623  -57.852 1.00 65.63  ? 470  CYS   A C     1 
ATOM   1525 O  O     . CYS   A 1 321  ? 27.898  11.085  -56.701 1.00 67.13  ? 470  CYS   A O     1 
ATOM   1526 C  CB    . CYS   A 1 321  ? 30.139  9.386   -58.228 1.00 65.42  ? 470  CYS   A CB    1 
ATOM   1527 S  SG    . CYS   A 1 321  ? 31.703  9.282   -59.132 1.00 69.67  ? 470  CYS   A SG    1 
ATOM   1528 N  N     . GLY   A 1 322  ? 26.997  10.104  -58.560 1.00 65.04  ? 471  GLY   A N     1 
ATOM   1529 C  CA    . GLY   A 1 322  ? 25.632  9.871   -58.056 1.00 64.12  ? 471  GLY   A CA    1 
ATOM   1530 C  C     . GLY   A 1 322  ? 24.935  8.816   -58.892 1.00 64.21  ? 471  GLY   A C     1 
ATOM   1531 O  O     . GLY   A 1 322  ? 25.400  8.562   -60.020 1.00 65.17  ? 471  GLY   A O     1 
ATOM   1532 N  N     . TYR   A 1 323  ? 23.874  8.207   -58.360 1.00 63.24  ? 472  TYR   A N     1 
ATOM   1533 C  CA    . TYR   A 1 323  ? 23.049  7.193   -59.066 1.00 61.35  ? 472  TYR   A CA    1 
ATOM   1534 C  C     . TYR   A 1 323  ? 21.575  7.600   -59.000 1.00 60.27  ? 472  TYR   A C     1 
ATOM   1535 O  O     . TYR   A 1 323  ? 21.183  8.319   -58.065 1.00 59.85  ? 472  TYR   A O     1 
ATOM   1536 C  CB    . TYR   A 1 323  ? 23.292  5.797   -58.485 1.00 60.15  ? 472  TYR   A CB    1 
ATOM   1537 C  CG    . TYR   A 1 323  ? 22.793  5.591   -57.078 1.00 58.92  ? 472  TYR   A CG    1 
ATOM   1538 C  CD1   . TYR   A 1 323  ? 23.606  5.839   -55.985 1.00 58.30  ? 472  TYR   A CD1   1 
ATOM   1539 C  CD2   . TYR   A 1 323  ? 21.509  5.135   -56.838 1.00 58.54  ? 472  TYR   A CD2   1 
ATOM   1540 C  CE1   . TYR   A 1 323  ? 23.154  5.646   -54.689 1.00 56.52  ? 472  TYR   A CE1   1 
ATOM   1541 C  CE2   . TYR   A 1 323  ? 21.043  4.934   -55.550 1.00 58.23  ? 472  TYR   A CE2   1 
ATOM   1542 C  CZ    . TYR   A 1 323  ? 21.868  5.191   -54.471 1.00 56.19  ? 472  TYR   A CZ    1 
ATOM   1543 O  OH    . TYR   A 1 323  ? 21.413  4.997   -53.200 1.00 57.12  ? 472  TYR   A OH    1 
ATOM   1544 N  N     . SER   A 1 324  ? 20.797  7.160   -59.991 1.00 60.33  ? 473  SER   A N     1 
ATOM   1545 C  CA    . SER   A 1 324  ? 19.325  7.338   -60.073 1.00 59.89  ? 473  SER   A CA    1 
ATOM   1546 C  C     . SER   A 1 324  ? 18.696  6.085   -60.690 1.00 61.77  ? 473  SER   A C     1 
ATOM   1547 O  O     . SER   A 1 324  ? 18.486  6.063   -61.918 1.00 62.72  ? 473  SER   A O     1 
ATOM   1548 C  CB    . SER   A 1 324  ? 18.965  8.576   -60.848 1.00 58.30  ? 473  SER   A CB    1 
ATOM   1549 O  OG    . SER   A 1 324  ? 17.557  8.723   -60.925 1.00 56.53  ? 473  SER   A OG    1 
ATOM   1550 N  N     . VAL   A 1 325  ? 18.438  5.073   -59.860 1.00 62.54  ? 474  VAL   A N     1 
ATOM   1551 C  CA    . VAL   A 1 325  ? 17.657  3.855   -60.229 1.00 62.50  ? 474  VAL   A CA    1 
ATOM   1552 C  C     . VAL   A 1 325  ? 16.183  4.133   -59.914 1.00 63.93  ? 474  VAL   A C     1 
ATOM   1553 O  O     . VAL   A 1 325  ? 15.859  5.289   -59.574 1.00 64.65  ? 474  VAL   A O     1 
ATOM   1554 C  CB    . VAL   A 1 325  ? 18.184  2.600   -59.506 1.00 62.26  ? 474  VAL   A CB    1 
ATOM   1555 C  CG1   . VAL   A 1 325  ? 19.672  2.407   -59.753 1.00 62.51  ? 474  VAL   A CG1   1 
ATOM   1556 C  CG2   . VAL   A 1 325  ? 17.887  2.614   -58.014 1.00 61.94  ? 474  VAL   A CG2   1 
ATOM   1557 N  N     . ARG   A 1 326  ? 15.324  3.121   -60.036 1.00 65.69  ? 475  ARG   A N     1 
ATOM   1558 C  CA    . ARG   A 1 326  ? 13.863  3.263   -59.805 1.00 67.12  ? 475  ARG   A CA    1 
ATOM   1559 C  C     . ARG   A 1 326  ? 13.599  3.310   -58.295 1.00 68.12  ? 475  ARG   A C     1 
ATOM   1560 O  O     . ARG   A 1 326  ? 14.075  2.403   -57.581 1.00 71.28  ? 475  ARG   A O     1 
ATOM   1561 C  CB    . ARG   A 1 326  ? 13.090  2.119   -60.465 1.00 68.78  ? 475  ARG   A CB    1 
ATOM   1562 C  CG    . ARG   A 1 326  ? 11.905  2.590   -61.297 1.00 70.53  ? 475  ARG   A CG    1 
ATOM   1563 C  CD    . ARG   A 1 326  ? 10.586  1.963   -60.900 1.00 71.67  ? 475  ARG   A CD    1 
ATOM   1564 N  NE    . ARG   A 1 326  ? 10.055  1.098   -61.945 1.00 73.86  ? 475  ARG   A NE    1 
ATOM   1565 C  CZ    . ARG   A 1 326  ? 10.374  -0.180  -62.128 1.00 76.11  ? 475  ARG   A CZ    1 
ATOM   1566 N  NH1   . ARG   A 1 326  ? 11.240  -0.786  -61.332 1.00 77.78  ? 475  ARG   A NH1   1 
ATOM   1567 N  NH2   . ARG   A 1 326  ? 9.819   -0.850  -63.123 1.00 77.16  ? 475  ARG   A NH2   1 
ATOM   1568 N  N     . PHE   A 1 327  ? 12.882  4.344   -57.843 1.00 67.19  ? 476  PHE   A N     1 
ATOM   1569 C  CA    . PHE   A 1 327  ? 12.426  4.553   -56.442 1.00 65.34  ? 476  PHE   A CA    1 
ATOM   1570 C  C     . PHE   A 1 327  ? 13.622  4.700   -55.492 1.00 65.15  ? 476  PHE   A C     1 
ATOM   1571 O  O     . PHE   A 1 327  ? 13.471  4.364   -54.298 1.00 65.24  ? 476  PHE   A O     1 
ATOM   1572 C  CB    . PHE   A 1 327  ? 11.524  3.402   -55.987 1.00 64.45  ? 476  PHE   A CB    1 
ATOM   1573 C  CG    . PHE   A 1 327  ? 10.342  3.122   -56.880 1.00 62.76  ? 476  PHE   A CG    1 
ATOM   1574 C  CD1   . PHE   A 1 327  ? 9.465   4.135   -57.237 1.00 62.56  ? 476  PHE   A CD1   1 
ATOM   1575 C  CD2   . PHE   A 1 327  ? 10.087  1.837   -57.333 1.00 61.25  ? 476  PHE   A CD2   1 
ATOM   1576 C  CE1   . PHE   A 1 327  ? 8.370   3.873   -58.045 1.00 61.72  ? 476  PHE   A CE1   1 
ATOM   1577 C  CE2   . PHE   A 1 327  ? 8.988   1.576   -58.135 1.00 61.92  ? 476  PHE   A CE2   1 
ATOM   1578 C  CZ    . PHE   A 1 327  ? 8.135   2.594   -58.493 1.00 62.45  ? 476  PHE   A CZ    1 
ATOM   1579 N  N     . GLU   A 1 328  ? 14.761  5.194   -55.993 1.00 65.28  ? 477  GLU   A N     1 
ATOM   1580 C  CA    . GLU   A 1 328  ? 15.980  5.478   -55.184 1.00 65.38  ? 477  GLU   A CA    1 
ATOM   1581 C  C     . GLU   A 1 328  ? 16.996  6.243   -56.038 1.00 62.90  ? 477  GLU   A C     1 
ATOM   1582 O  O     . GLU   A 1 328  ? 17.358  5.744   -57.120 1.00 60.98  ? 477  GLU   A O     1 
ATOM   1583 C  CB    . GLU   A 1 328  ? 16.605  4.191   -54.640 1.00 66.31  ? 477  GLU   A CB    1 
ATOM   1584 C  CG    . GLU   A 1 328  ? 17.688  4.442   -53.605 1.00 67.33  ? 477  GLU   A CG    1 
ATOM   1585 C  CD    . GLU   A 1 328  ? 18.200  3.197   -52.903 1.00 69.20  ? 477  GLU   A CD    1 
ATOM   1586 O  OE1   . GLU   A 1 328  ? 17.372  2.471   -52.316 1.00 71.36  ? 477  GLU   A OE1   1 
ATOM   1587 O  OE2   . GLU   A 1 328  ? 19.425  2.954   -52.948 1.00 68.74  ? 477  GLU   A OE2   1 
ATOM   1588 N  N     . SER   A 1 329  ? 17.439  7.406   -55.557 1.00 61.78  ? 478  SER   A N     1 
ATOM   1589 C  CA    . SER   A 1 329  ? 18.444  8.271   -56.227 1.00 59.89  ? 478  SER   A CA    1 
ATOM   1590 C  C     . SER   A 1 329  ? 19.250  9.046   -55.181 1.00 58.23  ? 478  SER   A C     1 
ATOM   1591 O  O     . SER   A 1 329  ? 18.650  9.500   -54.192 1.00 58.25  ? 478  SER   A O     1 
ATOM   1592 C  CB    . SER   A 1 329  ? 17.784  9.207   -57.208 1.00 58.70  ? 478  SER   A CB    1 
ATOM   1593 O  OG    . SER   A 1 329  ? 17.157  10.290  -56.538 1.00 57.49  ? 478  SER   A OG    1 
ATOM   1594 N  N     . VAL   A 1 330  ? 20.562  9.165   -55.401 1.00 58.50  ? 479  VAL   A N     1 
ATOM   1595 C  CA    . VAL   A 1 330  ? 21.472  10.110  -54.689 1.00 59.38  ? 479  VAL   A CA    1 
ATOM   1596 C  C     . VAL   A 1 330  ? 22.082  11.038  -55.746 1.00 60.60  ? 479  VAL   A C     1 
ATOM   1597 O  O     . VAL   A 1 330  ? 23.072  10.632  -56.387 1.00 60.02  ? 479  VAL   A O     1 
ATOM   1598 C  CB    . VAL   A 1 330  ? 22.556  9.363   -53.888 1.00 58.45  ? 479  VAL   A CB    1 
ATOM   1599 C  CG1   . VAL   A 1 330  ? 23.529  10.329  -53.228 1.00 58.26  ? 479  VAL   A CG1   1 
ATOM   1600 C  CG2   . VAL   A 1 330  ? 21.948  8.422   -52.858 1.00 57.84  ? 479  VAL   A CG2   1 
ATOM   1601 N  N     . LEU   A 1 331  ? 21.493  12.225  -55.930 1.00 62.78  ? 480  LEU   A N     1 
ATOM   1602 C  CA    . LEU   A 1 331  ? 21.871  13.193  -56.996 1.00 64.14  ? 480  LEU   A CA    1 
ATOM   1603 C  C     . LEU   A 1 331  ? 23.305  13.659  -56.767 1.00 64.64  ? 480  LEU   A C     1 
ATOM   1604 O  O     . LEU   A 1 331  ? 23.678  13.987  -55.643 1.00 65.47  ? 480  LEU   A O     1 
ATOM   1605 C  CB    . LEU   A 1 331  ? 20.909  14.386  -56.979 1.00 64.85  ? 480  LEU   A CB    1 
ATOM   1606 C  CG    . LEU   A 1 331  ? 19.443  14.068  -57.268 1.00 67.10  ? 480  LEU   A CG    1 
ATOM   1607 C  CD1   . LEU   A 1 331  ? 18.609  15.339  -57.279 1.00 68.56  ? 480  LEU   A CD1   1 
ATOM   1608 C  CD2   . LEU   A 1 331  ? 19.289  13.320  -58.583 1.00 68.30  ? 480  LEU   A CD2   1 
ATOM   1609 N  N     . PRO   A 1 332  ? 24.155  13.692  -57.818 1.00 65.28  ? 481  PRO   A N     1 
ATOM   1610 C  CA    . PRO   A 1 332  ? 25.479  14.303  -57.712 1.00 65.86  ? 481  PRO   A CA    1 
ATOM   1611 C  C     . PRO   A 1 332  ? 25.382  15.829  -57.849 1.00 65.55  ? 481  PRO   A C     1 
ATOM   1612 O  O     . PRO   A 1 332  ? 24.304  16.326  -58.122 1.00 64.00  ? 481  PRO   A O     1 
ATOM   1613 C  CB    . PRO   A 1 332  ? 26.252  13.666  -58.875 1.00 65.67  ? 481  PRO   A CB    1 
ATOM   1614 C  CG    . PRO   A 1 332  ? 25.191  13.372  -59.918 1.00 65.33  ? 481  PRO   A CG    1 
ATOM   1615 C  CD    . PRO   A 1 332  ? 23.898  13.146  -59.158 1.00 65.32  ? 481  PRO   A CD    1 
ATOM   1616 N  N     . ARG   A 1 333  ? 26.505  16.526  -57.654 1.00 67.11  ? 482  ARG   A N     1 
ATOM   1617 C  CA    . ARG   A 1 333  ? 26.597  18.010  -57.721 1.00 67.22  ? 482  ARG   A CA    1 
ATOM   1618 C  C     . ARG   A 1 333  ? 26.299  18.460  -59.151 1.00 66.81  ? 482  ARG   A C     1 
ATOM   1619 O  O     . ARG   A 1 333  ? 26.475  17.686  -60.088 1.00 65.70  ? 482  ARG   A O     1 
ATOM   1620 C  CB    . ARG   A 1 333  ? 27.980  18.479  -57.257 1.00 67.02  ? 482  ARG   A CB    1 
ATOM   1621 C  CG    . ARG   A 1 333  ? 29.095  18.205  -58.255 1.00 66.78  ? 482  ARG   A CG    1 
ATOM   1622 C  CD    . ARG   A 1 333  ? 30.475  18.234  -57.630 1.00 66.97  ? 482  ARG   A CD    1 
ATOM   1623 N  NE    . ARG   A 1 333  ? 31.507  17.851  -58.584 1.00 66.56  ? 482  ARG   A NE    1 
ATOM   1624 C  CZ    . ARG   A 1 333  ? 32.795  17.700  -58.292 1.00 66.56  ? 482  ARG   A CZ    1 
ATOM   1625 N  NH1   . ARG   A 1 333  ? 33.233  17.906  -57.059 1.00 67.73  ? 482  ARG   A NH1   1 
ATOM   1626 N  NH2   . ARG   A 1 333  ? 33.646  17.343  -59.237 1.00 66.27  ? 482  ARG   A NH2   1 
ATOM   1627 N  N     . PRO   A 1 334  ? 25.842  19.716  -59.364 1.00 67.12  ? 483  PRO   A N     1 
ATOM   1628 C  CA    . PRO   A 1 334  ? 25.440  20.182  -60.695 1.00 68.11  ? 483  PRO   A CA    1 
ATOM   1629 C  C     . PRO   A 1 334  ? 26.549  20.283  -61.760 1.00 68.26  ? 483  PRO   A C     1 
ATOM   1630 O  O     . PRO   A 1 334  ? 26.200  20.332  -62.927 1.00 67.20  ? 483  PRO   A O     1 
ATOM   1631 C  CB    . PRO   A 1 334  ? 24.885  21.595  -60.439 1.00 69.13  ? 483  PRO   A CB    1 
ATOM   1632 C  CG    . PRO   A 1 334  ? 24.585  21.631  -58.953 1.00 68.97  ? 483  PRO   A CG    1 
ATOM   1633 C  CD    . PRO   A 1 334  ? 25.638  20.742  -58.330 1.00 68.07  ? 483  PRO   A CD    1 
ATOM   1634 N  N     . HIS   A 1 335  ? 27.826  20.324  -61.356 1.00 69.12  ? 484  HIS   A N     1 
ATOM   1635 C  CA    . HIS   A 1 335  ? 28.996  20.562  -62.249 1.00 69.57  ? 484  HIS   A CA    1 
ATOM   1636 C  C     . HIS   A 1 335  ? 30.037  19.447  -62.102 1.00 67.04  ? 484  HIS   A C     1 
ATOM   1637 O  O     . HIS   A 1 335  ? 30.230  18.960  -60.973 1.00 65.97  ? 484  HIS   A O     1 
ATOM   1638 C  CB    . HIS   A 1 335  ? 29.630  21.928  -61.947 1.00 72.11  ? 484  HIS   A CB    1 
ATOM   1639 C  CG    . HIS   A 1 335  ? 28.657  23.057  -61.948 1.00 73.55  ? 484  HIS   A CG    1 
ATOM   1640 N  ND1   . HIS   A 1 335  ? 28.133  23.580  -60.780 1.00 74.50  ? 484  HIS   A ND1   1 
ATOM   1641 C  CD2   . HIS   A 1 335  ? 28.102  23.755  -62.962 1.00 74.40  ? 484  HIS   A CD2   1 
ATOM   1642 C  CE1   . HIS   A 1 335  ? 27.300  24.557  -61.076 1.00 74.81  ? 484  HIS   A CE1   1 
ATOM   1643 N  NE2   . HIS   A 1 335  ? 27.263  24.682  -62.408 1.00 75.15  ? 484  HIS   A NE2   1 
ATOM   1644 N  N     . ALA   A 1 336  ? 30.702  19.089  -63.207 1.00 65.74  ? 485  ALA   A N     1 
ATOM   1645 C  CA    . ALA   A 1 336  ? 31.822  18.119  -63.259 1.00 65.60  ? 485  ALA   A CA    1 
ATOM   1646 C  C     . ALA   A 1 336  ? 31.410  16.816  -62.565 1.00 63.75  ? 485  ALA   A C     1 
ATOM   1647 O  O     . ALA   A 1 336  ? 32.167  16.336  -61.699 1.00 62.96  ? 485  ALA   A O     1 
ATOM   1648 C  CB    . ALA   A 1 336  ? 33.046  18.727  -62.619 1.00 65.99  ? 485  ALA   A CB    1 
ATOM   1649 N  N     . SER   A 1 337  ? 30.255  16.266  -62.949 1.00 62.62  ? 486  SER   A N     1 
ATOM   1650 C  CA    . SER   A 1 337  ? 29.564  15.155  -62.243 1.00 61.95  ? 486  SER   A CA    1 
ATOM   1651 C  C     . SER   A 1 337  ? 29.270  13.994  -63.198 1.00 61.96  ? 486  SER   A C     1 
ATOM   1652 O  O     . SER   A 1 337  ? 29.153  14.234  -64.415 1.00 63.47  ? 486  SER   A O     1 
ATOM   1653 C  CB    . SER   A 1 337  ? 28.301  15.654  -61.607 1.00 62.57  ? 486  SER   A CB    1 
ATOM   1654 O  OG    . SER   A 1 337  ? 27.539  16.401  -62.542 1.00 64.07  ? 486  SER   A OG    1 
ATOM   1655 N  N     . ILE   A 1 338  ? 29.145  12.786  -62.640 1.00 61.70  ? 487  ILE   A N     1 
ATOM   1656 C  CA    . ILE   A 1 338  ? 28.761  11.533  -63.358 1.00 60.97  ? 487  ILE   A CA    1 
ATOM   1657 C  C     . ILE   A 1 338  ? 27.484  10.983  -62.709 1.00 60.86  ? 487  ILE   A C     1 
ATOM   1658 O  O     . ILE   A 1 338  ? 27.480  10.804  -61.474 1.00 61.13  ? 487  ILE   A O     1 
ATOM   1659 C  CB    . ILE   A 1 338  ? 29.910  10.502  -63.327 1.00 60.69  ? 487  ILE   A CB    1 
ATOM   1660 C  CG1   . ILE   A 1 338  ? 31.228  11.097  -63.831 1.00 62.00  ? 487  ILE   A CG1   1 
ATOM   1661 C  CG2   . ILE   A 1 338  ? 29.528  9.250   -64.102 1.00 60.11  ? 487  ILE   A CG2   1 
ATOM   1662 C  CD1   . ILE   A 1 338  ? 32.455  10.295  -63.451 1.00 62.37  ? 487  ILE   A CD1   1 
ATOM   1663 N  N     . MET   A 1 339  ? 26.442  10.738  -63.510 1.00 59.61  ? 488  MET   A N     1 
ATOM   1664 C  CA    . MET   A 1 339  ? 25.168  10.107  -63.069 1.00 58.12  ? 488  MET   A CA    1 
ATOM   1665 C  C     . MET   A 1 339  ? 25.122  8.671   -63.598 1.00 56.36  ? 488  MET   A C     1 
ATOM   1666 O  O     . MET   A 1 339  ? 25.010  8.505   -64.823 1.00 57.57  ? 488  MET   A O     1 
ATOM   1667 C  CB    . MET   A 1 339  ? 23.958  10.890  -63.592 1.00 59.18  ? 488  MET   A CB    1 
ATOM   1668 C  CG    . MET   A 1 339  ? 22.619  10.218  -63.322 1.00 59.41  ? 488  MET   A CG    1 
ATOM   1669 S  SD    . MET   A 1 339  ? 22.209  10.127  -61.560 1.00 59.36  ? 488  MET   A SD    1 
ATOM   1670 C  CE    . MET   A 1 339  ? 21.316  11.667  -61.356 1.00 58.14  ? 488  MET   A CE    1 
ATOM   1671 N  N     . PHE   A 1 340  ? 25.216  7.682   -62.704 1.00 55.97  ? 489  PHE   A N     1 
ATOM   1672 C  CA    . PHE   A 1 340  ? 25.060  6.235   -63.005 1.00 55.85  ? 489  PHE   A CA    1 
ATOM   1673 C  C     . PHE   A 1 340  ? 23.600  5.827   -62.761 1.00 56.06  ? 489  PHE   A C     1 
ATOM   1674 O  O     . PHE   A 1 340  ? 23.267  5.402   -61.640 1.00 55.57  ? 489  PHE   A O     1 
ATOM   1675 C  CB    . PHE   A 1 340  ? 26.026  5.400   -62.161 1.00 55.50  ? 489  PHE   A CB    1 
ATOM   1676 C  CG    . PHE   A 1 340  ? 27.486  5.664   -62.426 1.00 56.52  ? 489  PHE   A CG    1 
ATOM   1677 C  CD1   . PHE   A 1 340  ? 28.128  5.081   -63.508 1.00 57.18  ? 489  PHE   A CD1   1 
ATOM   1678 C  CD2   . PHE   A 1 340  ? 28.224  6.487   -61.589 1.00 58.13  ? 489  PHE   A CD2   1 
ATOM   1679 C  CE1   . PHE   A 1 340  ? 29.472  5.323   -63.750 1.00 58.07  ? 489  PHE   A CE1   1 
ATOM   1680 C  CE2   . PHE   A 1 340  ? 29.570  6.723   -61.830 1.00 57.84  ? 489  PHE   A CE2   1 
ATOM   1681 C  CZ    . PHE   A 1 340  ? 30.191  6.142   -62.911 1.00 57.71  ? 489  PHE   A CZ    1 
ATOM   1682 N  N     . CYS   A 1 341  ? 22.755  5.957   -63.788 1.00 57.04  ? 490  CYS   A N     1 
ATOM   1683 C  CA    . CYS   A 1 341  ? 21.301  5.640   -63.751 1.00 57.12  ? 490  CYS   A CA    1 
ATOM   1684 C  C     . CYS   A 1 341  ? 21.012  4.379   -64.573 1.00 57.13  ? 490  CYS   A C     1 
ATOM   1685 O  O     . CYS   A 1 341  ? 21.930  3.893   -65.261 1.00 58.99  ? 490  CYS   A O     1 
ATOM   1686 C  CB    . CYS   A 1 341  ? 20.481  6.797   -64.309 1.00 56.67  ? 490  CYS   A CB    1 
ATOM   1687 S  SG    . CYS   A 1 341  ? 20.801  7.117   -66.062 1.00 56.16  ? 490  CYS   A SG    1 
ATOM   1688 N  N     . THR   A 1 342  ? 19.776  3.876   -64.493 1.00 56.90  ? 491  THR   A N     1 
ATOM   1689 C  CA    . THR   A 1 342  ? 19.215  2.827   -65.387 1.00 56.01  ? 491  THR   A CA    1 
ATOM   1690 C  C     . THR   A 1 342  ? 18.509  3.509   -66.565 1.00 55.14  ? 491  THR   A C     1 
ATOM   1691 O  O     . THR   A 1 342  ? 18.059  4.661   -66.401 1.00 52.88  ? 491  THR   A O     1 
ATOM   1692 C  CB    . THR   A 1 342  ? 18.269  1.894   -64.623 1.00 55.82  ? 491  THR   A CB    1 
ATOM   1693 O  OG1   . THR   A 1 342  ? 17.335  2.704   -63.909 1.00 56.03  ? 491  THR   A OG1   1 
ATOM   1694 C  CG2   . THR   A 1 342  ? 18.995  0.981   -63.660 1.00 56.32  ? 491  THR   A CG2   1 
ATOM   1695 N  N     . VAL   A 1 343  ? 18.413  2.820   -67.704 1.00 55.83  ? 492  VAL   A N     1 
ATOM   1696 C  CA    . VAL   A 1 343  ? 17.880  3.389   -68.979 1.00 56.74  ? 492  VAL   A CA    1 
ATOM   1697 C  C     . VAL   A 1 343  ? 16.413  3.787   -68.767 1.00 57.29  ? 492  VAL   A C     1 
ATOM   1698 O  O     . VAL   A 1 343  ? 16.023  4.867   -69.251 1.00 57.89  ? 492  VAL   A O     1 
ATOM   1699 C  CB    . VAL   A 1 343  ? 18.032  2.414   -70.162 1.00 57.51  ? 492  VAL   A CB    1 
ATOM   1700 C  CG1   . VAL   A 1 343  ? 17.464  3.009   -71.441 1.00 58.75  ? 492  VAL   A CG1   1 
ATOM   1701 C  CG2   . VAL   A 1 343  ? 19.477  1.987   -70.376 1.00 57.48  ? 492  VAL   A CG2   1 
ATOM   1702 N  N     . GLY   A 1 344  ? 15.641  2.951   -68.063 1.00 57.10  ? 493  GLY   A N     1 
ATOM   1703 C  CA    . GLY   A 1 344  ? 14.230  3.211   -67.716 1.00 56.61  ? 493  GLY   A CA    1 
ATOM   1704 C  C     . GLY   A 1 344  ? 14.043  4.576   -67.073 1.00 56.42  ? 493  GLY   A C     1 
ATOM   1705 O  O     . GLY   A 1 344  ? 13.078  5.272   -67.441 1.00 57.36  ? 493  GLY   A O     1 
ATOM   1706 N  N     . VAL   A 1 345  ? 14.937  4.945   -66.150 1.00 57.40  ? 494  VAL   A N     1 
ATOM   1707 C  CA    . VAL   A 1 345  ? 14.916  6.245   -65.413 1.00 57.76  ? 494  VAL   A CA    1 
ATOM   1708 C  C     . VAL   A 1 345  ? 15.244  7.377   -66.392 1.00 57.94  ? 494  VAL   A C     1 
ATOM   1709 O  O     . VAL   A 1 345  ? 14.501  8.375   -66.401 1.00 59.00  ? 494  VAL   A O     1 
ATOM   1710 C  CB    . VAL   A 1 345  ? 15.893  6.241   -64.221 1.00 57.38  ? 494  VAL   A CB    1 
ATOM   1711 C  CG1   . VAL   A 1 345  ? 16.051  7.626   -63.613 1.00 57.89  ? 494  VAL   A CG1   1 
ATOM   1712 C  CG2   . VAL   A 1 345  ? 15.480  5.236   -63.159 1.00 57.62  ? 494  VAL   A CG2   1 
ATOM   1713 N  N     . LEU   A 1 346  ? 16.323  7.226   -67.168 1.00 58.43  ? 495  LEU   A N     1 
ATOM   1714 C  CA    . LEU   A 1 346  ? 16.792  8.234   -68.157 1.00 59.22  ? 495  LEU   A CA    1 
ATOM   1715 C  C     . LEU   A 1 346  ? 15.642  8.583   -69.110 1.00 60.29  ? 495  LEU   A C     1 
ATOM   1716 O  O     . LEU   A 1 346  ? 15.330  9.782   -69.234 1.00 61.94  ? 495  LEU   A O     1 
ATOM   1717 C  CB    . LEU   A 1 346  ? 18.003  7.678   -68.914 1.00 58.94  ? 495  LEU   A CB    1 
ATOM   1718 C  CG    . LEU   A 1 346  ? 18.539  8.549   -70.049 1.00 59.37  ? 495  LEU   A CG    1 
ATOM   1719 C  CD1   . LEU   A 1 346  ? 18.775  9.978   -69.585 1.00 59.31  ? 495  LEU   A CD1   1 
ATOM   1720 C  CD2   . LEU   A 1 346  ? 19.819  7.958   -70.623 1.00 60.17  ? 495  LEU   A CD2   1 
ATOM   1721 N  N     . LEU   A 1 347  ? 15.017  7.569   -69.719 1.00 60.77  ? 496  LEU   A N     1 
ATOM   1722 C  CA    . LEU   A 1 347  ? 13.894  7.721   -70.687 1.00 61.20  ? 496  LEU   A CA    1 
ATOM   1723 C  C     . LEU   A 1 347  ? 12.744  8.506   -70.040 1.00 64.07  ? 496  LEU   A C     1 
ATOM   1724 O  O     . LEU   A 1 347  ? 12.141  9.341   -70.741 1.00 66.49  ? 496  LEU   A O     1 
ATOM   1725 C  CB    . LEU   A 1 347  ? 13.424  6.336   -71.145 1.00 59.18  ? 496  LEU   A CB    1 
ATOM   1726 C  CG    . LEU   A 1 347  ? 14.398  5.571   -72.041 1.00 57.39  ? 496  LEU   A CG    1 
ATOM   1727 C  CD1   . LEU   A 1 347  ? 14.018  4.100   -72.125 1.00 56.27  ? 496  LEU   A CD1   1 
ATOM   1728 C  CD2   . LEU   A 1 347  ? 14.466  6.188   -73.429 1.00 56.54  ? 496  LEU   A CD2   1 
ATOM   1729 N  N     . ARG   A 1 348  ? 12.456  8.254   -68.758 1.00 65.91  ? 497  ARG   A N     1 
ATOM   1730 C  CA    . ARG   A 1 348  ? 11.364  8.925   -67.997 1.00 68.49  ? 497  ARG   A CA    1 
ATOM   1731 C  C     . ARG   A 1 348  ? 11.727  10.392  -67.723 1.00 69.14  ? 497  ARG   A C     1 
ATOM   1732 O  O     . ARG   A 1 348  ? 10.799  11.172  -67.428 1.00 67.31  ? 497  ARG   A O     1 
ATOM   1733 C  CB    . ARG   A 1 348  ? 11.062  8.177   -66.692 1.00 71.30  ? 497  ARG   A CB    1 
ATOM   1734 C  CG    . ARG   A 1 348  ? 9.900   7.198   -66.800 1.00 74.95  ? 497  ARG   A CG    1 
ATOM   1735 C  CD    . ARG   A 1 348  ? 9.597   6.455   -65.510 1.00 77.08  ? 497  ARG   A CD    1 
ATOM   1736 N  NE    . ARG   A 1 348  ? 10.376  5.224   -65.384 1.00 79.53  ? 497  ARG   A NE    1 
ATOM   1737 C  CZ    . ARG   A 1 348  ? 11.353  5.001   -64.500 1.00 80.49  ? 497  ARG   A CZ    1 
ATOM   1738 N  NH1   . ARG   A 1 348  ? 11.975  3.833   -64.497 1.00 78.97  ? 497  ARG   A NH1   1 
ATOM   1739 N  NH2   . ARG   A 1 348  ? 11.707  5.925   -63.620 1.00 81.81  ? 497  ARG   A NH2   1 
ATOM   1740 N  N     . LYS   A 1 349  ? 13.014  10.753  -67.820 1.00 71.52  ? 498  LYS   A N     1 
ATOM   1741 C  CA    . LYS   A 1 349  ? 13.534  12.125  -67.558 1.00 72.69  ? 498  LYS   A CA    1 
ATOM   1742 C  C     . LYS   A 1 349  ? 13.829  12.867  -68.872 1.00 73.38  ? 498  LYS   A C     1 
ATOM   1743 O  O     . LYS   A 1 349  ? 14.161  14.068  -68.794 1.00 73.79  ? 498  LYS   A O     1 
ATOM   1744 C  CB    . LYS   A 1 349  ? 14.783  12.050  -66.673 1.00 72.00  ? 498  LYS   A CB    1 
ATOM   1745 C  CG    . LYS   A 1 349  ? 14.528  11.683  -65.216 1.00 72.23  ? 498  LYS   A CG    1 
ATOM   1746 C  CD    . LYS   A 1 349  ? 13.466  12.540  -64.553 1.00 74.21  ? 498  LYS   A CD    1 
ATOM   1747 C  CE    . LYS   A 1 349  ? 13.528  12.526  -63.040 1.00 75.25  ? 498  LYS   A CE    1 
ATOM   1748 N  NZ    . LYS   A 1 349  ? 13.174  11.198  -62.484 1.00 75.75  ? 498  LYS   A NZ    1 
ATOM   1749 N  N     . LEU   A 1 350  ? 13.688  12.204  -70.029 1.00 73.33  ? 499  LEU   A N     1 
ATOM   1750 C  CA    . LEU   A 1 350  ? 13.957  12.795  -71.372 1.00 72.93  ? 499  LEU   A CA    1 
ATOM   1751 C  C     . LEU   A 1 350  ? 12.771  13.649  -71.838 1.00 73.27  ? 499  LEU   A C     1 
ATOM   1752 O  O     . LEU   A 1 350  ? 12.921  14.322  -72.874 1.00 72.04  ? 499  LEU   A O     1 
ATOM   1753 C  CB    . LEU   A 1 350  ? 14.238  11.679  -72.386 1.00 72.66  ? 499  LEU   A CB    1 
ATOM   1754 C  CG    . LEU   A 1 350  ? 15.594  10.985  -72.265 1.00 72.19  ? 499  LEU   A CG    1 
ATOM   1755 C  CD1   . LEU   A 1 350  ? 15.739  9.898   -73.319 1.00 72.84  ? 499  LEU   A CD1   1 
ATOM   1756 C  CD2   . LEU   A 1 350  ? 16.734  11.982  -72.377 1.00 71.16  ? 499  LEU   A CD2   1 
ATOM   1757 N  N     . GLU   A 1 351  ? 11.645  13.623  -71.114 1.00 77.69  ? 500  GLU   A N     1 
ATOM   1758 C  CA    . GLU   A 1 351  ? 10.402  14.378  -71.446 1.00 81.34  ? 500  GLU   A CA    1 
ATOM   1759 C  C     . GLU   A 1 351  ? 10.747  15.846  -71.736 1.00 82.48  ? 500  GLU   A C     1 
ATOM   1760 O  O     . GLU   A 1 351  ? 10.100  16.436  -72.623 1.00 80.98  ? 500  GLU   A O     1 
ATOM   1761 C  CB    . GLU   A 1 351  ? 9.385   14.261  -70.307 1.00 82.56  ? 500  GLU   A CB    1 
ATOM   1762 C  CG    . GLU   A 1 351  ? 7.981   14.694  -70.694 1.00 83.33  ? 500  GLU   A CG    1 
ATOM   1763 C  CD    . GLU   A 1 351  ? 6.900   14.369  -69.674 1.00 85.67  ? 500  GLU   A CD    1 
ATOM   1764 O  OE1   . GLU   A 1 351  ? 5.718   14.645  -69.963 1.00 88.47  ? 500  GLU   A OE1   1 
ATOM   1765 O  OE2   . GLU   A 1 351  ? 7.238   13.841  -68.594 1.00 84.66  ? 500  GLU   A OE2   1 
ATOM   1766 N  N     . ALA   A 1 352  ? 11.723  16.403  -71.009 1.00 85.89  ? 501  ALA   A N     1 
ATOM   1767 C  CA    . ALA   A 1 352  ? 12.283  17.762  -71.209 1.00 86.34  ? 501  ALA   A CA    1 
ATOM   1768 C  C     . ALA   A 1 352  ? 13.362  17.720  -72.297 1.00 85.57  ? 501  ALA   A C     1 
ATOM   1769 O  O     . ALA   A 1 352  ? 13.387  18.636  -73.142 1.00 86.63  ? 501  ALA   A O     1 
ATOM   1770 C  CB    . ALA   A 1 352  ? 12.840  18.286  -69.907 1.00 87.56  ? 501  ALA   A CB    1 
ATOM   1771 N  N     . GLY   A 1 353  ? 14.222  16.696  -72.257 1.00 82.91  ? 502  GLY   A N     1 
ATOM   1772 C  CA    . GLY   A 1 353  ? 15.310  16.460  -73.226 1.00 80.27  ? 502  GLY   A CA    1 
ATOM   1773 C  C     . GLY   A 1 353  ? 16.626  16.175  -72.523 1.00 78.63  ? 502  GLY   A C     1 
ATOM   1774 O  O     . GLY   A 1 353  ? 16.640  16.181  -71.274 1.00 78.76  ? 502  GLY   A O     1 
ATOM   1775 N  N     . ILE   A 1 354  ? 17.691  15.924  -73.290 1.00 76.58  ? 503  ILE   A N     1 
ATOM   1776 C  CA    . ILE   A 1 354  ? 19.081  15.770  -72.767 1.00 76.38  ? 503  ILE   A CA    1 
ATOM   1777 C  C     . ILE   A 1 354  ? 19.691  17.174  -72.680 1.00 77.18  ? 503  ILE   A C     1 
ATOM   1778 O  O     . ILE   A 1 354  ? 20.499  17.532  -73.560 1.00 77.00  ? 503  ILE   A O     1 
ATOM   1779 C  CB    . ILE   A 1 354  ? 19.923  14.810  -73.636 1.00 75.38  ? 503  ILE   A CB    1 
ATOM   1780 C  CG1   . ILE   A 1 354  ? 19.203  13.484  -73.894 1.00 74.12  ? 503  ILE   A CG1   1 
ATOM   1781 C  CG2   . ILE   A 1 354  ? 21.291  14.583  -73.007 1.00 75.84  ? 503  ILE   A CG2   1 
ATOM   1782 C  CD1   . ILE   A 1 354  ? 19.843  12.629  -74.963 1.00 74.06  ? 503  ILE   A CD1   1 
ATOM   1783 N  N     . ARG   A 1 355  ? 19.289  17.942  -71.663 1.00 77.99  ? 504  ARG   A N     1 
ATOM   1784 C  CA    . ARG   A 1 355  ? 19.712  19.351  -71.449 1.00 78.61  ? 504  ARG   A CA    1 
ATOM   1785 C  C     . ARG   A 1 355  ? 20.791  19.401  -70.361 1.00 72.76  ? 504  ARG   A C     1 
ATOM   1786 O  O     . ARG   A 1 355  ? 20.509  18.960  -69.232 1.00 72.10  ? 504  ARG   A O     1 
ATOM   1787 C  CB    . ARG   A 1 355  ? 18.504  20.215  -71.074 1.00 84.55  ? 504  ARG   A CB    1 
ATOM   1788 C  CG    . ARG   A 1 355  ? 17.402  20.221  -72.124 1.00 90.26  ? 504  ARG   A CG    1 
ATOM   1789 C  CD    . ARG   A 1 355  ? 16.507  21.444  -72.034 1.00 94.44  ? 504  ARG   A CD    1 
ATOM   1790 N  NE    . ARG   A 1 355  ? 15.566  21.519  -73.146 1.00 98.15  ? 504  ARG   A NE    1 
ATOM   1791 C  CZ    . ARG   A 1 355  ? 15.866  21.907  -74.387 1.00 99.21  ? 504  ARG   A CZ    1 
ATOM   1792 N  NH1   . ARG   A 1 355  ? 17.100  22.263  -74.708 1.00 99.48  ? 504  ARG   A NH1   1 
ATOM   1793 N  NH2   . ARG   A 1 355  ? 14.920  21.932  -75.311 1.00 99.53  ? 504  ARG   A NH2   1 
ATOM   1794 N  N     . GLY   A 1 356  ? 21.979  19.906  -70.707 1.00 67.36  ? 505  GLY   A N     1 
ATOM   1795 C  CA    . GLY   A 1 356  ? 23.088  20.165  -69.769 1.00 66.67  ? 505  GLY   A CA    1 
ATOM   1796 C  C     . GLY   A 1 356  ? 23.995  18.960  -69.584 1.00 64.84  ? 505  GLY   A C     1 
ATOM   1797 O  O     . GLY   A 1 356  ? 24.591  18.842  -68.494 1.00 65.39  ? 505  GLY   A O     1 
ATOM   1798 N  N     . ILE   A 1 357  ? 24.113  18.109  -70.611 1.00 63.03  ? 506  ILE   A N     1 
ATOM   1799 C  CA    . ILE   A 1 357  ? 24.920  16.850  -70.601 1.00 60.90  ? 506  ILE   A CA    1 
ATOM   1800 C  C     . ILE   A 1 357  ? 25.914  16.910  -71.766 1.00 58.97  ? 506  ILE   A C     1 
ATOM   1801 O  O     . ILE   A 1 357  ? 25.485  17.259  -72.880 1.00 58.05  ? 506  ILE   A O     1 
ATOM   1802 C  CB    . ILE   A 1 357  ? 23.998  15.615  -70.688 1.00 61.01  ? 506  ILE   A CB    1 
ATOM   1803 C  CG1   . ILE   A 1 357  ? 22.967  15.589  -69.555 1.00 61.97  ? 506  ILE   A CG1   1 
ATOM   1804 C  CG2   . ILE   A 1 357  ? 24.800  14.324  -70.743 1.00 61.80  ? 506  ILE   A CG2   1 
ATOM   1805 C  CD1   . ILE   A 1 357  ? 23.563  15.524  -68.165 1.00 61.90  ? 506  ILE   A CD1   1 
ATOM   1806 N  N     . SER   A 1 358  ? 27.188  16.596  -71.508 1.00 57.14  ? 507  SER   A N     1 
ATOM   1807 C  CA    . SER   A 1 358  ? 28.303  16.659  -72.491 1.00 57.81  ? 507  SER   A CA    1 
ATOM   1808 C  C     . SER   A 1 358  ? 28.527  15.285  -73.130 1.00 58.37  ? 507  SER   A C     1 
ATOM   1809 O  O     . SER   A 1 358  ? 28.784  15.236  -74.349 1.00 57.77  ? 507  SER   A O     1 
ATOM   1810 C  CB    . SER   A 1 358  ? 29.569  17.169  -71.850 1.00 57.69  ? 507  SER   A CB    1 
ATOM   1811 O  OG    . SER   A 1 358  ? 29.959  16.347  -70.761 1.00 57.55  ? 507  SER   A OG    1 
ATOM   1812 N  N     . HIS   A 1 359  ? 28.449  14.220  -72.326 1.00 60.01  ? 508  HIS   A N     1 
ATOM   1813 C  CA    . HIS   A 1 359  ? 28.731  12.815  -72.726 1.00 61.26  ? 508  HIS   A CA    1 
ATOM   1814 C  C     . HIS   A 1 359  ? 27.578  11.905  -72.285 1.00 59.94  ? 508  HIS   A C     1 
ATOM   1815 O  O     . HIS   A 1 359  ? 27.019  12.144  -71.198 1.00 60.33  ? 508  HIS   A O     1 
ATOM   1816 C  CB    . HIS   A 1 359  ? 30.071  12.350  -72.135 1.00 62.61  ? 508  HIS   A CB    1 
ATOM   1817 C  CG    . HIS   A 1 359  ? 31.249  13.156  -72.574 1.00 63.97  ? 508  HIS   A CG    1 
ATOM   1818 N  ND1   . HIS   A 1 359  ? 31.428  14.473  -72.198 1.00 63.83  ? 508  HIS   A ND1   1 
ATOM   1819 C  CD2   . HIS   A 1 359  ? 32.318  12.834  -73.336 1.00 65.44  ? 508  HIS   A CD2   1 
ATOM   1820 C  CE1   . HIS   A 1 359  ? 32.547  14.931  -72.720 1.00 64.93  ? 508  HIS   A CE1   1 
ATOM   1821 N  NE2   . HIS   A 1 359  ? 33.114  13.944  -73.422 1.00 64.78  ? 508  HIS   A NE2   1 
ATOM   1822 N  N     . VAL   A 1 360  ? 27.241  10.907  -73.107 1.00 58.33  ? 509  VAL   A N     1 
ATOM   1823 C  CA    . VAL   A 1 360  ? 26.301  9.797   -72.767 1.00 57.09  ? 509  VAL   A CA    1 
ATOM   1824 C  C     . VAL   A 1 360  ? 27.053  8.478   -72.963 1.00 55.51  ? 509  VAL   A C     1 
ATOM   1825 O  O     . VAL   A 1 360  ? 27.383  8.155   -74.118 1.00 56.28  ? 509  VAL   A O     1 
ATOM   1826 C  CB    . VAL   A 1 360  ? 25.015  9.844   -73.618 1.00 56.51  ? 509  VAL   A CB    1 
ATOM   1827 C  CG1   . VAL   A 1 360  ? 24.035  8.752   -73.211 1.00 55.58  ? 509  VAL   A CG1   1 
ATOM   1828 C  CG2   . VAL   A 1 360  ? 24.348  11.211  -73.565 1.00 56.84  ? 509  VAL   A CG2   1 
ATOM   1829 N  N     . ILE   A 1 361  ? 27.332  7.763   -71.872 1.00 55.05  ? 510  ILE   A N     1 
ATOM   1830 C  CA    . ILE   A 1 361  ? 28.053  6.457   -71.890 1.00 56.05  ? 510  ILE   A CA    1 
ATOM   1831 C  C     . ILE   A 1 361  ? 27.014  5.342   -71.736 1.00 55.51  ? 510  ILE   A C     1 
ATOM   1832 O  O     . ILE   A 1 361  ? 26.517  5.141   -70.613 1.00 55.36  ? 510  ILE   A O     1 
ATOM   1833 C  CB    . ILE   A 1 361  ? 29.146  6.402   -70.800 1.00 57.23  ? 510  ILE   A CB    1 
ATOM   1834 C  CG1   . ILE   A 1 361  ? 30.175  7.524   -70.979 1.00 58.16  ? 510  ILE   A CG1   1 
ATOM   1835 C  CG2   . ILE   A 1 361  ? 29.811  5.032   -70.763 1.00 57.38  ? 510  ILE   A CG2   1 
ATOM   1836 C  CD1   . ILE   A 1 361  ? 31.200  7.611   -69.871 1.00 58.94  ? 510  ILE   A CD1   1 
ATOM   1837 N  N     . VAL   A 1 362  ? 26.690  4.659   -72.835 1.00 55.56  ? 511  VAL   A N     1 
ATOM   1838 C  CA    . VAL   A 1 362  ? 25.804  3.459   -72.838 1.00 56.59  ? 511  VAL   A CA    1 
ATOM   1839 C  C     . VAL   A 1 362  ? 26.695  2.234   -72.611 1.00 56.88  ? 511  VAL   A C     1 
ATOM   1840 O  O     . VAL   A 1 362  ? 27.486  1.905   -73.510 1.00 58.94  ? 511  VAL   A O     1 
ATOM   1841 C  CB    . VAL   A 1 362  ? 24.991  3.354   -74.141 1.00 57.11  ? 511  VAL   A CB    1 
ATOM   1842 C  CG1   . VAL   A 1 362  ? 23.991  2.209   -74.087 1.00 58.04  ? 511  VAL   A CG1   1 
ATOM   1843 C  CG2   . VAL   A 1 362  ? 24.286  4.663   -74.469 1.00 56.80  ? 511  VAL   A CG2   1 
ATOM   1844 N  N     . ASP   A 1 363  ? 26.587  1.609   -71.438 1.00 57.66  ? 512  ASP   A N     1 
ATOM   1845 C  CA    . ASP   A 1 363  ? 27.510  0.537   -70.983 1.00 60.38  ? 512  ASP   A CA    1 
ATOM   1846 C  C     . ASP   A 1 363  ? 26.830  -0.824  -71.159 1.00 61.21  ? 512  ASP   A C     1 
ATOM   1847 O  O     . ASP   A 1 363  ? 25.583  -0.876  -71.131 1.00 61.94  ? 512  ASP   A O     1 
ATOM   1848 C  CB    . ASP   A 1 363  ? 27.944  0.775   -69.534 1.00 62.51  ? 512  ASP   A CB    1 
ATOM   1849 C  CG    . ASP   A 1 363  ? 29.209  0.037   -69.125 1.00 64.04  ? 512  ASP   A CG    1 
ATOM   1850 O  OD1   . ASP   A 1 363  ? 29.907  -0.481  -70.017 1.00 65.31  ? 512  ASP   A OD1   1 
ATOM   1851 O  OD2   . ASP   A 1 363  ? 29.489  -0.012  -67.910 1.00 65.41  ? 512  ASP   A OD2   1 
ATOM   1852 N  N     . GLU   A 1 364  ? 27.638  -1.875  -71.337 1.00 63.37  ? 513  GLU   A N     1 
ATOM   1853 C  CA    . GLU   A 1 364  ? 27.208  -3.299  -71.378 1.00 65.11  ? 513  GLU   A CA    1 
ATOM   1854 C  C     . GLU   A 1 364  ? 26.190  -3.500  -72.511 1.00 62.88  ? 513  GLU   A C     1 
ATOM   1855 O  O     . GLU   A 1 364  ? 25.195  -4.216  -72.289 1.00 64.33  ? 513  GLU   A O     1 
ATOM   1856 C  CB    . GLU   A 1 364  ? 26.620  -3.718  -70.024 1.00 68.35  ? 513  GLU   A CB    1 
ATOM   1857 C  CG    . GLU   A 1 364  ? 27.383  -3.202  -68.809 1.00 70.62  ? 513  GLU   A CG    1 
ATOM   1858 C  CD    . GLU   A 1 364  ? 28.833  -3.642  -68.681 1.00 73.32  ? 513  GLU   A CD    1 
ATOM   1859 O  OE1   . GLU   A 1 364  ? 29.217  -4.625  -69.346 1.00 75.14  ? 513  GLU   A OE1   1 
ATOM   1860 O  OE2   . GLU   A 1 364  ? 29.577  -3.002  -67.903 1.00 72.69  ? 513  GLU   A OE2   1 
ATOM   1861 N  N     . ILE   A 1 365  ? 26.436  -2.902  -73.682 1.00 61.44  ? 514  ILE   A N     1 
ATOM   1862 C  CA    . ILE   A 1 365  ? 25.511  -2.947  -74.857 1.00 61.44  ? 514  ILE   A CA    1 
ATOM   1863 C  C     . ILE   A 1 365  ? 25.375  -4.395  -75.349 1.00 61.42  ? 514  ILE   A C     1 
ATOM   1864 O  O     . ILE   A 1 365  ? 24.299  -4.734  -75.874 1.00 65.67  ? 514  ILE   A O     1 
ATOM   1865 C  CB    . ILE   A 1 365  ? 25.963  -1.999  -75.990 1.00 60.55  ? 514  ILE   A CB    1 
ATOM   1866 C  CG1   . ILE   A 1 365  ? 27.371  -2.313  -76.502 1.00 61.19  ? 514  ILE   A CG1   1 
ATOM   1867 C  CG2   . ILE   A 1 365  ? 25.836  -0.549  -75.553 1.00 60.11  ? 514  ILE   A CG2   1 
ATOM   1868 C  CD1   . ILE   A 1 365  ? 27.651  -1.773  -77.885 1.00 62.01  ? 514  ILE   A CD1   1 
ATOM   1869 N  N     . HIS   A 1 366  ? 26.425  -5.205  -75.180 1.00 60.55  ? 515  HIS   A N     1 
ATOM   1870 C  CA    . HIS   A 1 366  ? 26.510  -6.622  -75.631 1.00 60.34  ? 515  HIS   A CA    1 
ATOM   1871 C  C     . HIS   A 1 366  ? 25.449  -7.488  -74.940 1.00 62.05  ? 515  HIS   A C     1 
ATOM   1872 O  O     . HIS   A 1 366  ? 25.062  -8.508  -75.538 1.00 65.73  ? 515  HIS   A O     1 
ATOM   1873 C  CB    . HIS   A 1 366  ? 27.916  -7.185  -75.383 1.00 58.46  ? 515  HIS   A CB    1 
ATOM   1874 C  CG    . HIS   A 1 366  ? 28.301  -7.193  -73.944 1.00 57.14  ? 515  HIS   A CG    1 
ATOM   1875 N  ND1   . HIS   A 1 366  ? 28.963  -6.137  -73.355 1.00 55.70  ? 515  HIS   A ND1   1 
ATOM   1876 C  CD2   . HIS   A 1 366  ? 28.099  -8.106  -72.970 1.00 56.31  ? 515  HIS   A CD2   1 
ATOM   1877 C  CE1   . HIS   A 1 366  ? 29.166  -6.405  -72.083 1.00 55.45  ? 515  HIS   A CE1   1 
ATOM   1878 N  NE2   . HIS   A 1 366  ? 28.643  -7.606  -71.822 1.00 54.73  ? 515  HIS   A NE2   1 
ATOM   1879 N  N     . GLU   A 1 367  ? 25.018  -7.125  -73.728 1.00 64.73  ? 516  GLU   A N     1 
ATOM   1880 C  CA    . GLU   A 1 367  ? 23.994  -7.887  -72.958 1.00 68.63  ? 516  GLU   A CA    1 
ATOM   1881 C  C     . GLU   A 1 367  ? 22.646  -7.837  -73.692 1.00 67.46  ? 516  GLU   A C     1 
ATOM   1882 O  O     . GLU   A 1 367  ? 21.846  -8.775  -73.507 1.00 69.06  ? 516  GLU   A O     1 
ATOM   1883 C  CB    . GLU   A 1 367  ? 23.872  -7.362  -71.524 1.00 71.61  ? 516  GLU   A CB    1 
ATOM   1884 C  CG    . GLU   A 1 367  ? 24.937  -7.914  -70.589 1.00 74.39  ? 516  GLU   A CG    1 
ATOM   1885 C  CD    . GLU   A 1 367  ? 24.750  -7.589  -69.116 1.00 77.68  ? 516  GLU   A CD    1 
ATOM   1886 O  OE1   . GLU   A 1 367  ? 23.647  -7.139  -68.739 1.00 79.78  ? 516  GLU   A OE1   1 
ATOM   1887 O  OE2   . GLU   A 1 367  ? 25.712  -7.790  -68.345 1.00 81.51  ? 516  GLU   A OE2   1 
ATOM   1888 N  N     . ARG   A 1 368  ? 22.412  -6.789  -74.491 1.00 65.83  ? 517  ARG   A N     1 
ATOM   1889 C  CA    . ARG   A 1 368  ? 21.192  -6.596  -75.321 1.00 65.03  ? 517  ARG   A CA    1 
ATOM   1890 C  C     . ARG   A 1 368  ? 19.969  -6.462  -74.404 1.00 65.65  ? 517  ARG   A C     1 
ATOM   1891 O  O     . ARG   A 1 368  ? 18.945  -7.128  -74.669 1.00 67.13  ? 517  ARG   A O     1 
ATOM   1892 C  CB    . ARG   A 1 368  ? 21.025  -7.740  -76.328 1.00 63.84  ? 517  ARG   A CB    1 
ATOM   1893 C  CG    . ARG   A 1 368  ? 22.204  -7.927  -77.274 1.00 64.51  ? 517  ARG   A CG    1 
ATOM   1894 C  CD    . ARG   A 1 368  ? 22.490  -6.709  -78.132 1.00 64.68  ? 517  ARG   A CD    1 
ATOM   1895 N  NE    . ARG   A 1 368  ? 21.316  -6.289  -78.885 1.00 65.46  ? 517  ARG   A NE    1 
ATOM   1896 C  CZ    . ARG   A 1 368  ? 20.900  -6.834  -80.026 1.00 65.31  ? 517  ARG   A CZ    1 
ATOM   1897 N  NH1   . ARG   A 1 368  ? 21.561  -7.836  -80.581 1.00 64.98  ? 517  ARG   A NH1   1 
ATOM   1898 N  NH2   . ARG   A 1 368  ? 19.811  -6.370  -80.614 1.00 66.02  ? 517  ARG   A NH2   1 
ATOM   1899 N  N     . ASP   A 1 369  ? 20.081  -5.625  -73.367 1.00 64.54  ? 518  ASP   A N     1 
ATOM   1900 C  CA    . ASP   A 1 369  ? 18.942  -5.165  -72.530 1.00 63.16  ? 518  ASP   A CA    1 
ATOM   1901 C  C     . ASP   A 1 369  ? 17.973  -4.397  -73.437 1.00 62.87  ? 518  ASP   A C     1 
ATOM   1902 O  O     . ASP   A 1 369  ? 18.449  -3.536  -74.203 1.00 61.08  ? 518  ASP   A O     1 
ATOM   1903 C  CB    . ASP   A 1 369  ? 19.428  -4.300  -71.366 1.00 63.03  ? 518  ASP   A CB    1 
ATOM   1904 C  CG    . ASP   A 1 369  ? 18.309  -3.728  -70.516 1.00 64.00  ? 518  ASP   A CG    1 
ATOM   1905 O  OD1   . ASP   A 1 369  ? 17.481  -4.525  -70.025 1.00 65.98  ? 518  ASP   A OD1   1 
ATOM   1906 O  OD2   . ASP   A 1 369  ? 18.269  -2.491  -70.359 1.00 63.82  ? 518  ASP   A OD2   1 
ATOM   1907 N  N     . ILE   A 1 370  ? 16.674  -4.706  -73.361 1.00 62.23  ? 519  ILE   A N     1 
ATOM   1908 C  CA    . ILE   A 1 370  ? 15.635  -4.175  -74.296 1.00 62.24  ? 519  ILE   A CA    1 
ATOM   1909 C  C     . ILE   A 1 370  ? 15.604  -2.642  -74.229 1.00 60.91  ? 519  ILE   A C     1 
ATOM   1910 O  O     . ILE   A 1 370  ? 15.439  -2.019  -75.297 1.00 62.69  ? 519  ILE   A O     1 
ATOM   1911 C  CB    . ILE   A 1 370  ? 14.245  -4.784  -74.023 1.00 63.46  ? 519  ILE   A CB    1 
ATOM   1912 C  CG1   . ILE   A 1 370  ? 13.273  -4.431  -75.152 1.00 64.37  ? 519  ILE   A CG1   1 
ATOM   1913 C  CG2   . ILE   A 1 370  ? 13.703  -4.376  -72.660 1.00 63.75  ? 519  ILE   A CG2   1 
ATOM   1914 C  CD1   . ILE   A 1 370  ? 11.973  -5.190  -75.109 1.00 65.57  ? 519  ILE   A CD1   1 
ATOM   1915 N  N     . ASN   A 1 371  ? 15.741  -2.060  -73.033 1.00 57.90  ? 520  ASN   A N     1 
ATOM   1916 C  CA    . ASN   A 1 371  ? 15.688  -0.590  -72.812 1.00 55.36  ? 520  ASN   A CA    1 
ATOM   1917 C  C     . ASN   A 1 371  ? 16.940  0.057   -73.415 1.00 53.62  ? 520  ASN   A C     1 
ATOM   1918 O  O     . ASN   A 1 371  ? 16.816  1.162   -73.965 1.00 53.56  ? 520  ASN   A O     1 
ATOM   1919 C  CB    . ASN   A 1 371  ? 15.515  -0.240  -71.331 1.00 56.32  ? 520  ASN   A CB    1 
ATOM   1920 C  CG    . ASN   A 1 371  ? 14.109  -0.477  -70.815 1.00 56.43  ? 520  ASN   A CG    1 
ATOM   1921 O  OD1   . ASN   A 1 371  ? 13.213  -0.850  -71.568 1.00 56.80  ? 520  ASN   A OD1   1 
ATOM   1922 N  ND2   . ASN   A 1 371  ? 13.901  -0.254  -69.529 1.00 57.27  ? 520  ASN   A ND2   1 
ATOM   1923 N  N     . THR   A 1 372  ? 18.095  -0.610  -73.330 1.00 53.63  ? 521  THR   A N     1 
ATOM   1924 C  CA    . THR   A 1 372  ? 19.375  -0.155  -73.937 1.00 53.80  ? 521  THR   A CA    1 
ATOM   1925 C  C     . THR   A 1 372  ? 19.212  -0.101  -75.462 1.00 53.60  ? 521  THR   A C     1 
ATOM   1926 O  O     . THR   A 1 372  ? 19.432  0.982   -76.031 1.00 54.43  ? 521  THR   A O     1 
ATOM   1927 C  CB    . THR   A 1 372  ? 20.549  -1.037  -73.487 1.00 54.33  ? 521  THR   A CB    1 
ATOM   1928 O  OG1   . THR   A 1 372  ? 20.601  -0.998  -72.060 1.00 54.74  ? 521  THR   A OG1   1 
ATOM   1929 C  CG2   . THR   A 1 372  ? 21.881  -0.592  -74.050 1.00 54.06  ? 521  THR   A CG2   1 
ATOM   1930 N  N     . ASP   A 1 373  ? 18.821  -1.218  -76.089 1.00 53.75  ? 522  ASP   A N     1 
ATOM   1931 C  CA    . ASP   A 1 373  ? 18.547  -1.325  -77.551 1.00 53.57  ? 522  ASP   A CA    1 
ATOM   1932 C  C     . ASP   A 1 373  ? 17.644  -0.164  -77.992 1.00 52.77  ? 522  ASP   A C     1 
ATOM   1933 O  O     . ASP   A 1 373  ? 17.933  0.443   -79.040 1.00 53.80  ? 522  ASP   A O     1 
ATOM   1934 C  CB    . ASP   A 1 373  ? 17.902  -2.669  -77.913 1.00 54.36  ? 522  ASP   A CB    1 
ATOM   1935 C  CG    . ASP   A 1 373  ? 18.865  -3.841  -78.045 1.00 54.34  ? 522  ASP   A CG    1 
ATOM   1936 O  OD1   . ASP   A 1 373  ? 20.074  -3.656  -77.788 1.00 53.39  ? 522  ASP   A OD1   1 
ATOM   1937 O  OD2   . ASP   A 1 373  ? 18.395  -4.941  -78.408 1.00 54.86  ? 522  ASP   A OD2   1 
ATOM   1938 N  N     . PHE   A 1 374  ? 16.595  0.126   -77.216 1.00 50.99  ? 523  PHE   A N     1 
ATOM   1939 C  CA    . PHE   A 1 374  ? 15.604  1.206   -77.467 1.00 51.69  ? 523  PHE   A CA    1 
ATOM   1940 C  C     . PHE   A 1 374  ? 16.294  2.575   -77.403 1.00 53.32  ? 523  PHE   A C     1 
ATOM   1941 O  O     . PHE   A 1 374  ? 16.024  3.419   -78.280 1.00 53.42  ? 523  PHE   A O     1 
ATOM   1942 C  CB    . PHE   A 1 374  ? 14.447  1.093   -76.471 1.00 51.28  ? 523  PHE   A CB    1 
ATOM   1943 C  CG    . PHE   A 1 374  ? 13.469  2.241   -76.474 1.00 51.17  ? 523  PHE   A CG    1 
ATOM   1944 C  CD1   . PHE   A 1 374  ? 12.844  2.645   -77.642 1.00 52.36  ? 523  PHE   A CD1   1 
ATOM   1945 C  CD2   . PHE   A 1 374  ? 13.150  2.900   -75.298 1.00 51.39  ? 523  PHE   A CD2   1 
ATOM   1946 C  CE1   . PHE   A 1 374  ? 11.938  3.696   -77.635 1.00 52.45  ? 523  PHE   A CE1   1 
ATOM   1947 C  CE2   . PHE   A 1 374  ? 12.242  3.947   -75.292 1.00 51.83  ? 523  PHE   A CE2   1 
ATOM   1948 C  CZ    . PHE   A 1 374  ? 11.639  4.345   -76.461 1.00 51.72  ? 523  PHE   A CZ    1 
ATOM   1949 N  N     . LEU   A 1 375  ? 17.153  2.790   -76.401 1.00 55.41  ? 524  LEU   A N     1 
ATOM   1950 C  CA    . LEU   A 1 375  ? 17.857  4.084   -76.167 1.00 57.06  ? 524  LEU   A CA    1 
ATOM   1951 C  C     . LEU   A 1 375  ? 18.801  4.382   -77.339 1.00 57.58  ? 524  LEU   A C     1 
ATOM   1952 O  O     . LEU   A 1 375  ? 18.889  5.561   -77.733 1.00 59.38  ? 524  LEU   A O     1 
ATOM   1953 C  CB    . LEU   A 1 375  ? 18.625  4.024   -74.842 1.00 56.79  ? 524  LEU   A CB    1 
ATOM   1954 C  CG    . LEU   A 1 375  ? 19.450  5.265   -74.503 1.00 56.53  ? 524  LEU   A CG    1 
ATOM   1955 C  CD1   . LEU   A 1 375  ? 18.550  6.463   -74.242 1.00 56.77  ? 524  LEU   A CD1   1 
ATOM   1956 C  CD2   . LEU   A 1 375  ? 20.353  5.004   -73.309 1.00 57.18  ? 524  LEU   A CD2   1 
ATOM   1957 N  N     . LEU   A 1 376  ? 19.478  3.358   -77.867 1.00 57.02  ? 525  LEU   A N     1 
ATOM   1958 C  CA    . LEU   A 1 376  ? 20.418  3.485   -79.014 1.00 57.82  ? 525  LEU   A CA    1 
ATOM   1959 C  C     . LEU   A 1 376  ? 19.667  4.061   -80.223 1.00 58.00  ? 525  LEU   A C     1 
ATOM   1960 O  O     . LEU   A 1 376  ? 20.286  4.832   -80.984 1.00 58.20  ? 525  LEU   A O     1 
ATOM   1961 C  CB    . LEU   A 1 376  ? 21.027  2.116   -79.339 1.00 57.83  ? 525  LEU   A CB    1 
ATOM   1962 C  CG    . LEU   A 1 376  ? 21.874  1.482   -78.235 1.00 58.09  ? 525  LEU   A CG    1 
ATOM   1963 C  CD1   . LEU   A 1 376  ? 22.270  0.064   -78.611 1.00 58.84  ? 525  LEU   A CD1   1 
ATOM   1964 C  CD2   . LEU   A 1 376  ? 23.108  2.319   -77.931 1.00 57.09  ? 525  LEU   A CD2   1 
ATOM   1965 N  N     . VAL   A 1 377  ? 18.385  3.707   -80.380 1.00 57.47  ? 526  VAL   A N     1 
ATOM   1966 C  CA    . VAL   A 1 377  ? 17.490  4.225   -81.460 1.00 57.62  ? 526  VAL   A CA    1 
ATOM   1967 C  C     . VAL   A 1 377  ? 17.299  5.727   -81.235 1.00 57.65  ? 526  VAL   A C     1 
ATOM   1968 O  O     . VAL   A 1 377  ? 17.453  6.496   -82.203 1.00 57.89  ? 526  VAL   A O     1 
ATOM   1969 C  CB    . VAL   A 1 377  ? 16.129  3.501   -81.503 1.00 57.78  ? 526  VAL   A CB    1 
ATOM   1970 C  CG1   . VAL   A 1 377  ? 15.348  3.855   -82.760 1.00 57.55  ? 526  VAL   A CG1   1 
ATOM   1971 C  CG2   . VAL   A 1 377  ? 16.270  1.994   -81.371 1.00 58.50  ? 526  VAL   A CG2   1 
ATOM   1972 N  N     . VAL   A 1 378  ? 16.970  6.114   -79.999 1.00 58.44  ? 527  VAL   A N     1 
ATOM   1973 C  CA    . VAL   A 1 378  ? 16.771  7.534   -79.585 1.00 57.81  ? 527  VAL   A CA    1 
ATOM   1974 C  C     . VAL   A 1 378  ? 18.082  8.285   -79.828 1.00 58.36  ? 527  VAL   A C     1 
ATOM   1975 O  O     . VAL   A 1 378  ? 18.046  9.305   -80.537 1.00 59.53  ? 527  VAL   A O     1 
ATOM   1976 C  CB    . VAL   A 1 378  ? 16.322  7.648   -78.115 1.00 56.89  ? 527  VAL   A CB    1 
ATOM   1977 C  CG1   . VAL   A 1 378  ? 16.273  9.096   -77.653 1.00 57.30  ? 527  VAL   A CG1   1 
ATOM   1978 C  CG2   . VAL   A 1 378  ? 14.984  6.964   -77.882 1.00 57.03  ? 527  VAL   A CG2   1 
ATOM   1979 N  N     . LEU   A 1 379  ? 19.187  7.769   -79.282 1.00 58.89  ? 528  LEU   A N     1 
ATOM   1980 C  CA    . LEU   A 1 379  ? 20.520  8.432   -79.281 1.00 61.09  ? 528  LEU   A CA    1 
ATOM   1981 C  C     . LEU   A 1 379  ? 21.030  8.616   -80.716 1.00 64.35  ? 528  LEU   A C     1 
ATOM   1982 O  O     . LEU   A 1 379  ? 21.674  9.650   -80.966 1.00 66.65  ? 528  LEU   A O     1 
ATOM   1983 C  CB    . LEU   A 1 379  ? 21.508  7.615   -78.439 1.00 60.04  ? 528  LEU   A CB    1 
ATOM   1984 C  CG    . LEU   A 1 379  ? 21.341  7.726   -76.922 1.00 58.81  ? 528  LEU   A CG    1 
ATOM   1985 C  CD1   . LEU   A 1 379  ? 22.371  6.870   -76.203 1.00 58.43  ? 528  LEU   A CD1   1 
ATOM   1986 C  CD2   . LEU   A 1 379  ? 21.439  9.171   -76.457 1.00 58.05  ? 528  LEU   A CD2   1 
ATOM   1987 N  N     . ARG   A 1 380  ? 20.762  7.671   -81.624 1.00 68.60  ? 529  ARG   A N     1 
ATOM   1988 C  CA    . ARG   A 1 380  ? 21.216  7.768   -83.039 1.00 71.65  ? 529  ARG   A CA    1 
ATOM   1989 C  C     . ARG   A 1 380  ? 20.563  8.988   -83.701 1.00 73.01  ? 529  ARG   A C     1 
ATOM   1990 O  O     . ARG   A 1 380  ? 21.276  9.710   -84.424 1.00 75.88  ? 529  ARG   A O     1 
ATOM   1991 C  CB    . ARG   A 1 380  ? 20.904  6.505   -83.847 1.00 73.32  ? 529  ARG   A CB    1 
ATOM   1992 C  CG    . ARG   A 1 380  ? 21.516  6.533   -85.241 1.00 76.12  ? 529  ARG   A CG    1 
ATOM   1993 C  CD    . ARG   A 1 380  ? 21.289  5.276   -86.054 1.00 79.57  ? 529  ARG   A CD    1 
ATOM   1994 N  NE    . ARG   A 1 380  ? 19.898  5.110   -86.451 1.00 81.85  ? 529  ARG   A NE    1 
ATOM   1995 C  CZ    . ARG   A 1 380  ? 19.462  4.236   -87.355 1.00 84.42  ? 529  ARG   A CZ    1 
ATOM   1996 N  NH1   . ARG   A 1 380  ? 20.309  3.431   -87.977 1.00 85.08  ? 529  ARG   A NH1   1 
ATOM   1997 N  NH2   . ARG   A 1 380  ? 18.171  4.173   -87.637 1.00 85.77  ? 529  ARG   A NH2   1 
ATOM   1998 N  N     . ASP   A 1 381  ? 19.262  9.199   -83.470 1.00 73.03  ? 530  ASP   A N     1 
ATOM   1999 C  CA    . ASP   A 1 381  ? 18.509  10.385  -83.962 1.00 73.44  ? 530  ASP   A CA    1 
ATOM   2000 C  C     . ASP   A 1 381  ? 19.118  11.653  -83.353 1.00 74.10  ? 530  ASP   A C     1 
ATOM   2001 O  O     . ASP   A 1 381  ? 19.233  12.656  -84.083 1.00 76.37  ? 530  ASP   A O     1 
ATOM   2002 C  CB    . ASP   A 1 381  ? 17.018  10.296  -83.627 1.00 74.49  ? 530  ASP   A CB    1 
ATOM   2003 C  CG    . ASP   A 1 381  ? 16.280  9.168   -84.327 1.00 75.02  ? 530  ASP   A CG    1 
ATOM   2004 O  OD1   . ASP   A 1 381  ? 16.801  8.660   -85.341 1.00 73.89  ? 530  ASP   A OD1   1 
ATOM   2005 O  OD2   . ASP   A 1 381  ? 15.184  8.807   -83.849 1.00 76.75  ? 530  ASP   A OD2   1 
ATOM   2006 N  N     . VAL   A 1 382  ? 19.492  11.596  -82.069 1.00 72.88  ? 531  VAL   A N     1 
ATOM   2007 C  CA    . VAL   A 1 382  ? 20.087  12.731  -81.300 1.00 72.18  ? 531  VAL   A CA    1 
ATOM   2008 C  C     . VAL   A 1 382  ? 21.455  13.081  -81.903 1.00 72.05  ? 531  VAL   A C     1 
ATOM   2009 O  O     . VAL   A 1 382  ? 21.695  14.280  -82.138 1.00 73.90  ? 531  VAL   A O     1 
ATOM   2010 C  CB    . VAL   A 1 382  ? 20.188  12.408  -79.796 1.00 71.66  ? 531  VAL   A CB    1 
ATOM   2011 C  CG1   . VAL   A 1 382  ? 21.003  13.448  -79.040 1.00 72.81  ? 531  VAL   A CG1   1 
ATOM   2012 C  CG2   . VAL   A 1 382  ? 18.814  12.251  -79.163 1.00 71.39  ? 531  VAL   A CG2   1 
ATOM   2013 N  N     . VAL   A 1 383  ? 22.308  12.078  -82.141 1.00 71.71  ? 532  VAL   A N     1 
ATOM   2014 C  CA    . VAL   A 1 383  ? 23.666  12.240  -82.747 1.00 72.91  ? 532  VAL   A CA    1 
ATOM   2015 C  C     . VAL   A 1 383  ? 23.530  12.941  -84.104 1.00 75.39  ? 532  VAL   A C     1 
ATOM   2016 O  O     . VAL   A 1 383  ? 24.357  13.825  -84.395 1.00 77.88  ? 532  VAL   A O     1 
ATOM   2017 C  CB    . VAL   A 1 383  ? 24.388  10.887  -82.904 1.00 72.65  ? 532  VAL   A CB    1 
ATOM   2018 C  CG1   . VAL   A 1 383  ? 25.571  10.976  -83.857 1.00 73.41  ? 532  VAL   A CG1   1 
ATOM   2019 C  CG2   . VAL   A 1 383  ? 24.830  10.324  -81.565 1.00 73.16  ? 532  VAL   A CG2   1 
ATOM   2020 N  N     . GLN   A 1 384  ? 22.536  12.541  -84.901 1.00 77.52  ? 533  GLN   A N     1 
ATOM   2021 C  CA    . GLN   A 1 384  ? 22.338  13.005  -86.300 1.00 78.83  ? 533  GLN   A CA    1 
ATOM   2022 C  C     . GLN   A 1 384  ? 21.983  14.497  -86.296 1.00 76.04  ? 533  GLN   A C     1 
ATOM   2023 O  O     . GLN   A 1 384  ? 22.588  15.245  -87.083 1.00 77.98  ? 533  GLN   A O     1 
ATOM   2024 C  CB    . GLN   A 1 384  ? 21.255  12.166  -86.984 1.00 82.31  ? 533  GLN   A CB    1 
ATOM   2025 C  CG    . GLN   A 1 384  ? 21.376  12.121  -88.501 1.00 85.04  ? 533  GLN   A CG    1 
ATOM   2026 C  CD    . GLN   A 1 384  ? 20.611  10.963  -89.096 1.00 86.91  ? 533  GLN   A CD    1 
ATOM   2027 O  OE1   . GLN   A 1 384  ? 21.132  10.206  -89.913 1.00 89.16  ? 533  GLN   A OE1   1 
ATOM   2028 N  NE2   . GLN   A 1 384  ? 19.365  10.807  -88.678 1.00 86.96  ? 533  GLN   A NE2   1 
ATOM   2029 N  N     . ALA   A 1 385  ? 21.051  14.905  -85.429 1.00 74.02  ? 534  ALA   A N     1 
ATOM   2030 C  CA    . ALA   A 1 385  ? 20.518  16.285  -85.335 1.00 73.31  ? 534  ALA   A CA    1 
ATOM   2031 C  C     . ALA   A 1 385  ? 21.475  17.176  -84.532 1.00 72.21  ? 534  ALA   A C     1 
ATOM   2032 O  O     . ALA   A 1 385  ? 21.646  18.345  -84.919 1.00 76.13  ? 534  ALA   A O     1 
ATOM   2033 C  CB    . ALA   A 1 385  ? 19.142  16.264  -84.714 1.00 73.56  ? 534  ALA   A CB    1 
ATOM   2034 N  N     . TYR   A 1 386  ? 22.062  16.644  -83.455 1.00 69.27  ? 535  TYR   A N     1 
ATOM   2035 C  CA    . TYR   A 1 386  ? 22.922  17.382  -82.493 1.00 66.60  ? 535  TYR   A CA    1 
ATOM   2036 C  C     . TYR   A 1 386  ? 24.294  16.717  -82.413 1.00 67.26  ? 535  TYR   A C     1 
ATOM   2037 O  O     . TYR   A 1 386  ? 24.617  16.083  -81.412 1.00 66.52  ? 535  TYR   A O     1 
ATOM   2038 C  CB    . TYR   A 1 386  ? 22.244  17.424  -81.121 1.00 65.58  ? 535  TYR   A CB    1 
ATOM   2039 C  CG    . TYR   A 1 386  ? 20.861  18.021  -81.120 1.00 65.11  ? 535  TYR   A CG    1 
ATOM   2040 C  CD1   . TYR   A 1 386  ? 20.670  19.381  -80.937 1.00 65.51  ? 535  TYR   A CD1   1 
ATOM   2041 C  CD2   . TYR   A 1 386  ? 19.738  17.228  -81.296 1.00 65.39  ? 535  TYR   A CD2   1 
ATOM   2042 C  CE1   . TYR   A 1 386  ? 19.402  19.939  -80.934 1.00 65.56  ? 535  TYR   A CE1   1 
ATOM   2043 C  CE2   . TYR   A 1 386  ? 18.463  17.770  -81.296 1.00 65.53  ? 535  TYR   A CE2   1 
ATOM   2044 C  CZ    . TYR   A 1 386  ? 18.294  19.131  -81.113 1.00 65.33  ? 535  TYR   A CZ    1 
ATOM   2045 O  OH    . TYR   A 1 386  ? 17.044  19.677  -81.105 1.00 65.23  ? 535  TYR   A OH    1 
ATOM   2046 N  N     . PRO   A 1 387  ? 25.157  16.854  -83.447 1.00 68.75  ? 536  PRO   A N     1 
ATOM   2047 C  CA    . PRO   A 1 387  ? 26.430  16.129  -83.491 1.00 70.07  ? 536  PRO   A CA    1 
ATOM   2048 C  C     . PRO   A 1 387  ? 27.484  16.589  -82.467 1.00 72.23  ? 536  PRO   A C     1 
ATOM   2049 O  O     . PRO   A 1 387  ? 28.483  15.904  -82.326 1.00 68.58  ? 536  PRO   A O     1 
ATOM   2050 C  CB    . PRO   A 1 387  ? 26.930  16.385  -84.922 1.00 68.62  ? 536  PRO   A CB    1 
ATOM   2051 C  CG    . PRO   A 1 387  ? 26.314  17.715  -85.296 1.00 68.14  ? 536  PRO   A CG    1 
ATOM   2052 C  CD    . PRO   A 1 387  ? 24.957  17.714  -84.625 1.00 67.92  ? 536  PRO   A CD    1 
ATOM   2053 N  N     . GLU   A 1 388  ? 27.244  17.715  -81.783 1.00 76.64  ? 537  GLU   A N     1 
ATOM   2054 C  CA    . GLU   A 1 388  ? 28.158  18.278  -80.751 1.00 79.18  ? 537  GLU   A CA    1 
ATOM   2055 C  C     . GLU   A 1 388  ? 28.147  17.376  -79.509 1.00 76.46  ? 537  GLU   A C     1 
ATOM   2056 O  O     . GLU   A 1 388  ? 29.180  17.335  -78.815 1.00 77.60  ? 537  GLU   A O     1 
ATOM   2057 C  CB    . GLU   A 1 388  ? 27.772  19.714  -80.388 1.00 83.46  ? 537  GLU   A CB    1 
ATOM   2058 C  CG    . GLU   A 1 388  ? 28.090  20.727  -81.476 1.00 87.01  ? 537  GLU   A CG    1 
ATOM   2059 C  CD    . GLU   A 1 388  ? 27.152  20.710  -82.672 1.00 92.18  ? 537  GLU   A CD    1 
ATOM   2060 O  OE1   . GLU   A 1 388  ? 27.512  21.300  -83.711 1.00 95.38  ? 537  GLU   A OE1   1 
ATOM   2061 O  OE2   . GLU   A 1 388  ? 26.061  20.106  -82.563 1.00 93.99  ? 537  GLU   A OE2   1 
ATOM   2062 N  N     . VAL   A 1 389  ? 27.033  16.681  -79.243 1.00 73.40  ? 538  VAL   A N     1 
ATOM   2063 C  CA    . VAL   A 1 389  ? 26.918  15.670  -78.147 1.00 70.90  ? 538  VAL   A CA    1 
ATOM   2064 C  C     . VAL   A 1 389  ? 27.993  14.605  -78.370 1.00 68.24  ? 538  VAL   A C     1 
ATOM   2065 O  O     . VAL   A 1 389  ? 28.463  14.471  -79.515 1.00 67.94  ? 538  VAL   A O     1 
ATOM   2066 C  CB    . VAL   A 1 389  ? 25.521  15.021  -78.080 1.00 70.68  ? 538  VAL   A CB    1 
ATOM   2067 C  CG1   . VAL   A 1 389  ? 25.292  14.041  -79.223 1.00 71.40  ? 538  VAL   A CG1   1 
ATOM   2068 C  CG2   . VAL   A 1 389  ? 25.284  14.334  -76.742 1.00 69.62  ? 538  VAL   A CG2   1 
ATOM   2069 N  N     . ARG   A 1 390  ? 28.352  13.874  -77.316 1.00 66.99  ? 539  ARG   A N     1 
ATOM   2070 C  CA    . ARG   A 1 390  ? 29.307  12.741  -77.387 1.00 66.36  ? 539  ARG   A CA    1 
ATOM   2071 C  C     . ARG   A 1 390  ? 28.635  11.493  -76.807 1.00 63.59  ? 539  ARG   A C     1 
ATOM   2072 O  O     . ARG   A 1 390  ? 28.125  11.565  -75.673 1.00 62.76  ? 539  ARG   A O     1 
ATOM   2073 C  CB    . ARG   A 1 390  ? 30.617  13.120  -76.690 1.00 68.20  ? 539  ARG   A CB    1 
ATOM   2074 C  CG    . ARG   A 1 390  ? 31.447  14.131  -77.472 1.00 69.60  ? 539  ARG   A CG    1 
ATOM   2075 C  CD    . ARG   A 1 390  ? 31.868  13.578  -78.821 1.00 72.62  ? 539  ARG   A CD    1 
ATOM   2076 N  NE    . ARG   A 1 390  ? 32.716  14.479  -79.592 1.00 73.98  ? 539  ARG   A NE    1 
ATOM   2077 C  CZ    . ARG   A 1 390  ? 32.289  15.343  -80.513 1.00 76.27  ? 539  ARG   A CZ    1 
ATOM   2078 N  NH1   . ARG   A 1 390  ? 33.164  16.103  -81.150 1.00 79.17  ? 539  ARG   A NH1   1 
ATOM   2079 N  NH2   . ARG   A 1 390  ? 31.002  15.457  -80.799 1.00 76.03  ? 539  ARG   A NH2   1 
ATOM   2080 N  N     . ILE   A 1 391  ? 28.603  10.415  -77.596 1.00 60.11  ? 540  ILE   A N     1 
ATOM   2081 C  CA    . ILE   A 1 391  ? 28.026  9.092   -77.222 1.00 58.79  ? 540  ILE   A CA    1 
ATOM   2082 C  C     . ILE   A 1 391  ? 29.176  8.086   -77.164 1.00 56.68  ? 540  ILE   A C     1 
ATOM   2083 O  O     . ILE   A 1 391  ? 29.886  7.958   -78.172 1.00 57.86  ? 540  ILE   A O     1 
ATOM   2084 C  CB    . ILE   A 1 391  ? 26.942  8.652   -78.229 1.00 59.28  ? 540  ILE   A CB    1 
ATOM   2085 C  CG1   . ILE   A 1 391  ? 25.925  9.759   -78.523 1.00 58.70  ? 540  ILE   A CG1   1 
ATOM   2086 C  CG2   . ILE   A 1 391  ? 26.260  7.375   -77.763 1.00 60.27  ? 540  ILE   A CG2   1 
ATOM   2087 C  CD1   . ILE   A 1 391  ? 25.176  10.265  -77.311 1.00 58.45  ? 540  ILE   A CD1   1 
ATOM   2088 N  N     . VAL   A 1 392  ? 29.354  7.407   -76.031 1.00 56.02  ? 541  VAL   A N     1 
ATOM   2089 C  CA    . VAL   A 1 392  ? 30.382  6.339   -75.860 1.00 56.75  ? 541  VAL   A CA    1 
ATOM   2090 C  C     . VAL   A 1 392  ? 29.662  5.023   -75.556 1.00 56.93  ? 541  VAL   A C     1 
ATOM   2091 O  O     . VAL   A 1 392  ? 29.113  4.891   -74.449 1.00 58.77  ? 541  VAL   A O     1 
ATOM   2092 C  CB    . VAL   A 1 392  ? 31.402  6.700   -74.764 1.00 57.29  ? 541  VAL   A CB    1 
ATOM   2093 C  CG1   . VAL   A 1 392  ? 32.384  5.564   -74.509 1.00 57.40  ? 541  VAL   A CG1   1 
ATOM   2094 C  CG2   . VAL   A 1 392  ? 32.143  7.988   -75.092 1.00 57.31  ? 541  VAL   A CG2   1 
ATOM   2095 N  N     . LEU   A 1 393  ? 29.661  4.099   -76.518 1.00 57.00  ? 542  LEU   A N     1 
ATOM   2096 C  CA    . LEU   A 1 393  ? 29.126  2.722   -76.353 1.00 57.54  ? 542  LEU   A CA    1 
ATOM   2097 C  C     . LEU   A 1 393  ? 30.283  1.827   -75.905 1.00 58.59  ? 542  LEU   A C     1 
ATOM   2098 O  O     . LEU   A 1 393  ? 31.340  1.878   -76.552 1.00 60.08  ? 542  LEU   A O     1 
ATOM   2099 C  CB    . LEU   A 1 393  ? 28.527  2.237   -77.676 1.00 57.62  ? 542  LEU   A CB    1 
ATOM   2100 C  CG    . LEU   A 1 393  ? 27.680  3.255   -78.439 1.00 57.05  ? 542  LEU   A CG    1 
ATOM   2101 C  CD1   . LEU   A 1 393  ? 27.101  2.628   -79.696 1.00 57.43  ? 542  LEU   A CD1   1 
ATOM   2102 C  CD2   . LEU   A 1 393  ? 26.572  3.820   -77.562 1.00 55.97  ? 542  LEU   A CD2   1 
ATOM   2103 N  N     . MET   A 1 394  ? 30.100  1.064   -74.827 1.00 60.69  ? 543  MET   A N     1 
ATOM   2104 C  CA    . MET   A 1 394  ? 31.159  0.198   -74.246 1.00 63.11  ? 543  MET   A CA    1 
ATOM   2105 C  C     . MET   A 1 394  ? 30.660  -1.250  -74.235 1.00 61.85  ? 543  MET   A C     1 
ATOM   2106 O  O     . MET   A 1 394  ? 29.512  -1.475  -73.809 1.00 60.67  ? 543  MET   A O     1 
ATOM   2107 C  CB    . MET   A 1 394  ? 31.529  0.668   -72.835 1.00 65.57  ? 543  MET   A CB    1 
ATOM   2108 C  CG    . MET   A 1 394  ? 31.971  2.127   -72.802 1.00 67.78  ? 543  MET   A CG    1 
ATOM   2109 S  SD    . MET   A 1 394  ? 33.010  2.549   -71.380 1.00 69.85  ? 543  MET   A SD    1 
ATOM   2110 C  CE    . MET   A 1 394  ? 31.891  2.159   -70.036 1.00 71.35  ? 543  MET   A CE    1 
ATOM   2111 N  N     . SER   A 1 395  ? 31.492  -2.179  -74.715 1.00 62.30  ? 544  SER   A N     1 
ATOM   2112 C  CA    . SER   A 1 395  ? 31.119  -3.583  -75.031 1.00 62.86  ? 544  SER   A CA    1 
ATOM   2113 C  C     . SER   A 1 395  ? 32.254  -4.542  -74.663 1.00 61.87  ? 544  SER   A C     1 
ATOM   2114 O  O     . SER   A 1 395  ? 33.421  -4.117  -74.685 1.00 60.72  ? 544  SER   A O     1 
ATOM   2115 C  CB    . SER   A 1 395  ? 30.766  -3.715  -76.489 1.00 63.79  ? 544  SER   A CB    1 
ATOM   2116 O  OG    . SER   A 1 395  ? 30.575  -5.076  -76.846 1.00 64.46  ? 544  SER   A OG    1 
ATOM   2117 N  N     . ALA   A 1 396  ? 31.905  -5.798  -74.373 1.00 63.33  ? 545  ALA   A N     1 
ATOM   2118 C  CA    . ALA   A 1 396  ? 32.842  -6.928  -74.177 1.00 65.44  ? 545  ALA   A CA    1 
ATOM   2119 C  C     . ALA   A 1 396  ? 33.370  -7.374  -75.546 1.00 68.09  ? 545  ALA   A C     1 
ATOM   2120 O  O     . ALA   A 1 396  ? 32.957  -6.779  -76.560 1.00 68.36  ? 545  ALA   A O     1 
ATOM   2121 C  CB    . ALA   A 1 396  ? 32.149  -8.054  -73.451 1.00 64.68  ? 545  ALA   A CB    1 
ATOM   2122 N  N     . THR   A 1 397  ? 34.253  -8.376  -75.573 1.00 71.83  ? 546  THR   A N     1 
ATOM   2123 C  CA    . THR   A 1 397  ? 34.833  -8.951  -76.818 1.00 73.74  ? 546  THR   A CA    1 
ATOM   2124 C  C     . THR   A 1 397  ? 33.745  -9.753  -77.545 1.00 73.62  ? 546  THR   A C     1 
ATOM   2125 O  O     . THR   A 1 397  ? 33.685  -10.983 -77.361 1.00 72.84  ? 546  THR   A O     1 
ATOM   2126 C  CB    . THR   A 1 397  ? 36.100  -9.766  -76.521 1.00 75.37  ? 546  THR   A CB    1 
ATOM   2127 O  OG1   . THR   A 1 397  ? 35.907  -10.502 -75.312 1.00 78.20  ? 546  THR   A OG1   1 
ATOM   2128 C  CG2   . THR   A 1 397  ? 37.332  -8.898  -76.389 1.00 75.39  ? 546  THR   A CG2   1 
ATOM   2129 N  N     . ILE   A 1 398  ? 32.905  -9.054  -78.315 1.00 74.12  ? 547  ILE   A N     1 
ATOM   2130 C  CA    . ILE   A 1 398  ? 31.865  -9.629  -79.220 1.00 73.74  ? 547  ILE   A CA    1 
ATOM   2131 C  C     . ILE   A 1 398  ? 31.973  -8.919  -80.574 1.00 75.15  ? 547  ILE   A C     1 
ATOM   2132 O  O     . ILE   A 1 398  ? 32.729  -7.931  -80.660 1.00 75.16  ? 547  ILE   A O     1 
ATOM   2133 C  CB    . ILE   A 1 398  ? 30.453  -9.490  -78.614 1.00 72.15  ? 547  ILE   A CB    1 
ATOM   2134 C  CG1   . ILE   A 1 398  ? 30.021  -8.025  -78.479 1.00 71.22  ? 547  ILE   A CG1   1 
ATOM   2135 C  CG2   . ILE   A 1 398  ? 30.368  -10.225 -77.285 1.00 71.80  ? 547  ILE   A CG2   1 
ATOM   2136 C  CD1   . ILE   A 1 398  ? 28.547  -7.793  -78.720 1.00 70.18  ? 547  ILE   A CD1   1 
ATOM   2137 N  N     . ASP   A 1 399  ? 31.233  -9.389  -81.580 1.00 76.39  ? 548  ASP   A N     1 
ATOM   2138 C  CA    . ASP   A 1 399  ? 31.200  -8.771  -82.932 1.00 77.29  ? 548  ASP   A CA    1 
ATOM   2139 C  C     . ASP   A 1 399  ? 30.363  -7.487  -82.851 1.00 76.92  ? 548  ASP   A C     1 
ATOM   2140 O  O     . ASP   A 1 399  ? 29.122  -7.573  -82.949 1.00 78.97  ? 548  ASP   A O     1 
ATOM   2141 C  CB    . ASP   A 1 399  ? 30.694  -9.760  -83.986 1.00 78.51  ? 548  ASP   A CB    1 
ATOM   2142 C  CG    . ASP   A 1 399  ? 31.180  -9.449  -85.391 1.00 79.42  ? 548  ASP   A CG    1 
ATOM   2143 O  OD1   . ASP   A 1 399  ? 31.452  -8.262  -85.671 1.00 78.67  ? 548  ASP   A OD1   1 
ATOM   2144 O  OD2   . ASP   A 1 399  ? 31.293  -10.400 -86.191 1.00 81.71  ? 548  ASP   A OD2   1 
ATOM   2145 N  N     . THR   A 1 400  ? 31.032  -6.343  -82.673 1.00 75.46  ? 549  THR   A N     1 
ATOM   2146 C  CA    . THR   A 1 400  ? 30.415  -5.004  -82.470 1.00 73.96  ? 549  THR   A CA    1 
ATOM   2147 C  C     . THR   A 1 400  ? 30.148  -4.328  -83.822 1.00 74.45  ? 549  THR   A C     1 
ATOM   2148 O  O     . THR   A 1 400  ? 29.770  -3.141  -83.813 1.00 74.58  ? 549  THR   A O     1 
ATOM   2149 C  CB    . THR   A 1 400  ? 31.304  -4.129  -81.576 1.00 72.91  ? 549  THR   A CB    1 
ATOM   2150 O  OG1   . THR   A 1 400  ? 32.619  -4.108  -82.133 1.00 72.96  ? 549  THR   A OG1   1 
ATOM   2151 C  CG2   . THR   A 1 400  ? 31.369  -4.624  -80.149 1.00 72.86  ? 549  THR   A CG2   1 
ATOM   2152 N  N     . SER   A 1 401  ? 30.329  -5.049  -84.935 1.00 75.57  ? 550  SER   A N     1 
ATOM   2153 C  CA    . SER   A 1 401  ? 30.123  -4.548  -86.322 1.00 76.18  ? 550  SER   A CA    1 
ATOM   2154 C  C     . SER   A 1 401  ? 28.676  -4.072  -86.500 1.00 75.57  ? 550  SER   A C     1 
ATOM   2155 O  O     . SER   A 1 401  ? 28.468  -3.060  -87.203 1.00 74.53  ? 550  SER   A O     1 
ATOM   2156 C  CB    . SER   A 1 401  ? 30.483  -5.603  -87.337 1.00 75.45  ? 550  SER   A CB    1 
ATOM   2157 O  OG    . SER   A 1 401  ? 29.752  -6.796  -87.105 1.00 74.96  ? 550  SER   A OG    1 
ATOM   2158 N  N     . MET   A 1 402  ? 27.724  -4.778  -85.882 1.00 75.24  ? 551  MET   A N     1 
ATOM   2159 C  CA    . MET   A 1 402  ? 26.269  -4.464  -85.908 1.00 74.25  ? 551  MET   A CA    1 
ATOM   2160 C  C     . MET   A 1 402  ? 26.038  -3.034  -85.398 1.00 70.98  ? 551  MET   A C     1 
ATOM   2161 O  O     . MET   A 1 402  ? 25.310  -2.279  -86.072 1.00 69.01  ? 551  MET   A O     1 
ATOM   2162 C  CB    . MET   A 1 402  ? 25.493  -5.461  -85.041 1.00 75.88  ? 551  MET   A CB    1 
ATOM   2163 C  CG    . MET   A 1 402  ? 23.994  -5.224  -85.024 1.00 77.86  ? 551  MET   A CG    1 
ATOM   2164 S  SD    . MET   A 1 402  ? 23.061  -6.630  -84.366 1.00 81.30  ? 551  MET   A SD    1 
ATOM   2165 C  CE    . MET   A 1 402  ? 23.871  -6.870  -82.785 1.00 81.25  ? 551  MET   A CE    1 
ATOM   2166 N  N     . PHE   A 1 403  ? 26.646  -2.679  -84.261 1.00 68.30  ? 552  PHE   A N     1 
ATOM   2167 C  CA    . PHE   A 1 403  ? 26.504  -1.361  -83.585 1.00 67.23  ? 552  PHE   A CA    1 
ATOM   2168 C  C     . PHE   A 1 403  ? 27.298  -0.291  -84.343 1.00 68.65  ? 552  PHE   A C     1 
ATOM   2169 O  O     . PHE   A 1 403  ? 26.820  0.858   -84.433 1.00 68.53  ? 552  PHE   A O     1 
ATOM   2170 C  CB    . PHE   A 1 403  ? 26.965  -1.450  -82.130 1.00 66.13  ? 552  PHE   A CB    1 
ATOM   2171 C  CG    . PHE   A 1 403  ? 26.156  -2.390  -81.274 1.00 65.52  ? 552  PHE   A CG    1 
ATOM   2172 C  CD1   . PHE   A 1 403  ? 25.004  -1.954  -80.638 1.00 65.06  ? 552  PHE   A CD1   1 
ATOM   2173 C  CD2   . PHE   A 1 403  ? 26.549  -3.708  -81.102 1.00 64.62  ? 552  PHE   A CD2   1 
ATOM   2174 C  CE1   . PHE   A 1 403  ? 24.261  -2.818  -79.848 1.00 65.16  ? 552  PHE   A CE1   1 
ATOM   2175 C  CE2   . PHE   A 1 403  ? 25.806  -4.570  -80.311 1.00 65.20  ? 552  PHE   A CE2   1 
ATOM   2176 C  CZ    . PHE   A 1 403  ? 24.664  -4.124  -79.685 1.00 65.69  ? 552  PHE   A CZ    1 
ATOM   2177 N  N     . CYS   A 1 404  ? 28.479  -0.656  -84.851 1.00 69.56  ? 553  CYS   A N     1 
ATOM   2178 C  CA    . CYS   A 1 404  ? 29.363  0.214   -85.672 1.00 69.13  ? 553  CYS   A CA    1 
ATOM   2179 C  C     . CYS   A 1 404  ? 28.600  0.672   -86.920 1.00 69.28  ? 553  CYS   A C     1 
ATOM   2180 O  O     . CYS   A 1 404  ? 28.484  1.898   -87.121 1.00 68.78  ? 553  CYS   A O     1 
ATOM   2181 C  CB    . CYS   A 1 404  ? 30.642  -0.517  -86.066 1.00 70.64  ? 553  CYS   A CB    1 
ATOM   2182 S  SG    . CYS   A 1 404  ? 31.830  0.528   -86.948 1.00 70.42  ? 553  CYS   A SG    1 
ATOM   2183 N  N     . GLU   A 1 405  ? 28.085  -0.285  -87.702 1.00 70.20  ? 554  GLU   A N     1 
ATOM   2184 C  CA    . GLU   A 1 405  ? 27.278  -0.045  -88.933 1.00 70.83  ? 554  GLU   A CA    1 
ATOM   2185 C  C     . GLU   A 1 405  ? 26.090  0.864   -88.595 1.00 69.52  ? 554  GLU   A C     1 
ATOM   2186 O  O     . GLU   A 1 405  ? 25.771  1.748   -89.415 1.00 68.00  ? 554  GLU   A O     1 
ATOM   2187 C  CB    . GLU   A 1 405  ? 26.788  -1.368  -89.529 1.00 73.20  ? 554  GLU   A CB    1 
ATOM   2188 C  CG    . GLU   A 1 405  ? 27.869  -2.150  -90.258 1.00 75.85  ? 554  GLU   A CG    1 
ATOM   2189 C  CD    . GLU   A 1 405  ? 27.491  -3.570  -90.653 1.00 76.69  ? 554  GLU   A CD    1 
ATOM   2190 O  OE1   . GLU   A 1 405  ? 28.377  -4.299  -91.147 1.00 75.58  ? 554  GLU   A OE1   1 
ATOM   2191 O  OE2   . GLU   A 1 405  ? 26.315  -3.947  -90.465 1.00 77.48  ? 554  GLU   A OE2   1 
ATOM   2192 N  N     . TYR   A 1 406  ? 25.472  0.653   -87.429 1.00 68.98  ? 555  TYR   A N     1 
ATOM   2193 C  CA    . TYR   A 1 406  ? 24.273  1.390   -86.950 1.00 67.86  ? 555  TYR   A CA    1 
ATOM   2194 C  C     . TYR   A 1 406  ? 24.629  2.865   -86.721 1.00 67.93  ? 555  TYR   A C     1 
ATOM   2195 O  O     . TYR   A 1 406  ? 23.868  3.736   -87.185 1.00 67.36  ? 555  TYR   A O     1 
ATOM   2196 C  CB    . TYR   A 1 406  ? 23.706  0.738   -85.686 1.00 67.12  ? 555  TYR   A CB    1 
ATOM   2197 C  CG    . TYR   A 1 406  ? 22.323  1.209   -85.316 1.00 66.31  ? 555  TYR   A CG    1 
ATOM   2198 C  CD1   . TYR   A 1 406  ? 21.227  0.871   -86.093 1.00 64.99  ? 555  TYR   A CD1   1 
ATOM   2199 C  CD2   . TYR   A 1 406  ? 22.106  1.998   -84.198 1.00 66.24  ? 555  TYR   A CD2   1 
ATOM   2200 C  CE1   . TYR   A 1 406  ? 19.951  1.302   -85.770 1.00 65.00  ? 555  TYR   A CE1   1 
ATOM   2201 C  CE2   . TYR   A 1 406  ? 20.836  2.437   -83.859 1.00 66.68  ? 555  TYR   A CE2   1 
ATOM   2202 C  CZ    . TYR   A 1 406  ? 19.754  2.090   -84.651 1.00 65.61  ? 555  TYR   A CZ    1 
ATOM   2203 O  OH    . TYR   A 1 406  ? 18.498  2.514   -84.331 1.00 65.58  ? 555  TYR   A OH    1 
ATOM   2204 N  N     . PHE   A 1 407  ? 25.753  3.133   -86.045 1.00 68.58  ? 556  PHE   A N     1 
ATOM   2205 C  CA    . PHE   A 1 407  ? 26.218  4.498   -85.672 1.00 68.50  ? 556  PHE   A CA    1 
ATOM   2206 C  C     . PHE   A 1 407  ? 27.234  5.007   -86.707 1.00 71.98  ? 556  PHE   A C     1 
ATOM   2207 O  O     . PHE   A 1 407  ? 28.274  5.574   -86.312 1.00 73.08  ? 556  PHE   A O     1 
ATOM   2208 C  CB    . PHE   A 1 407  ? 26.766  4.502   -84.241 1.00 65.95  ? 556  PHE   A CB    1 
ATOM   2209 C  CG    . PHE   A 1 407  ? 25.705  4.519   -83.168 1.00 63.03  ? 556  PHE   A CG    1 
ATOM   2210 C  CD1   . PHE   A 1 407  ? 25.053  5.695   -82.836 1.00 61.36  ? 556  PHE   A CD1   1 
ATOM   2211 C  CD2   . PHE   A 1 407  ? 25.351  3.359   -82.496 1.00 63.49  ? 556  PHE   A CD2   1 
ATOM   2212 C  CE1   . PHE   A 1 407  ? 24.072  5.713   -81.857 1.00 60.98  ? 556  PHE   A CE1   1 
ATOM   2213 C  CE2   . PHE   A 1 407  ? 24.373  3.379   -81.514 1.00 63.04  ? 556  PHE   A CE2   1 
ATOM   2214 C  CZ    . PHE   A 1 407  ? 23.734  4.555   -81.196 1.00 61.66  ? 556  PHE   A CZ    1 
ATOM   2215 N  N     . PHE   A 1 408  ? 26.928  4.819   -87.997 1.00 74.43  ? 557  PHE   A N     1 
ATOM   2216 C  CA    . PHE   A 1 408  ? 27.615  5.452   -89.156 1.00 74.21  ? 557  PHE   A CA    1 
ATOM   2217 C  C     . PHE   A 1 408  ? 29.095  5.045   -89.182 1.00 74.96  ? 557  PHE   A C     1 
ATOM   2218 O  O     . PHE   A 1 408  ? 29.967  5.930   -89.319 1.00 75.50  ? 557  PHE   A O     1 
ATOM   2219 C  CB    . PHE   A 1 408  ? 27.424  6.969   -89.096 1.00 74.39  ? 557  PHE   A CB    1 
ATOM   2220 C  CG    . PHE   A 1 408  ? 26.026  7.399   -88.729 1.00 75.04  ? 557  PHE   A CG    1 
ATOM   2221 C  CD1   . PHE   A 1 408  ? 24.939  6.997   -89.491 1.00 75.11  ? 557  PHE   A CD1   1 
ATOM   2222 C  CD2   . PHE   A 1 408  ? 25.794  8.194   -87.617 1.00 75.95  ? 557  PHE   A CD2   1 
ATOM   2223 C  CE1   . PHE   A 1 408  ? 23.651  7.386   -89.154 1.00 75.05  ? 557  PHE   A CE1   1 
ATOM   2224 C  CE2   . PHE   A 1 408  ? 24.506  8.584   -87.282 1.00 77.16  ? 557  PHE   A CE2   1 
ATOM   2225 C  CZ    . PHE   A 1 408  ? 23.438  8.180   -88.051 1.00 76.72  ? 557  PHE   A CZ    1 
ATOM   2226 N  N     . ASN   A 1 409  ? 29.358  3.738   -89.070 1.00 75.65  ? 558  ASN   A N     1 
ATOM   2227 C  CA    . ASN   A 1 409  ? 30.717  3.128   -89.054 1.00 76.51  ? 558  ASN   A CA    1 
ATOM   2228 C  C     . ASN   A 1 409  ? 31.638  3.978   -88.170 1.00 74.91  ? 558  ASN   A C     1 
ATOM   2229 O  O     . ASN   A 1 409  ? 32.664  4.474   -88.675 1.00 74.69  ? 558  ASN   A O     1 
ATOM   2230 C  CB    . ASN   A 1 409  ? 31.262  2.931   -90.473 1.00 77.63  ? 558  ASN   A CB    1 
ATOM   2231 C  CG    . ASN   A 1 409  ? 30.649  1.734   -91.169 1.00 78.78  ? 558  ASN   A CG    1 
ATOM   2232 O  OD1   . ASN   A 1 409  ? 30.892  0.592   -90.781 1.00 78.60  ? 558  ASN   A OD1   1 
ATOM   2233 N  ND2   . ASN   A 1 409  ? 29.851  1.982   -92.196 1.00 79.18  ? 558  ASN   A ND2   1 
ATOM   2234 N  N     . CYS   A 1 410  ? 31.265  4.143   -86.898 1.00 73.18  ? 559  CYS   A N     1 
ATOM   2235 C  CA    . CYS   A 1 410  ? 32.046  4.880   -85.870 1.00 71.93  ? 559  CYS   A CA    1 
ATOM   2236 C  C     . CYS   A 1 410  ? 33.319  4.099   -85.554 1.00 72.67  ? 559  CYS   A C     1 
ATOM   2237 O  O     . CYS   A 1 410  ? 33.410  2.912   -85.859 1.00 75.35  ? 559  CYS   A O     1 
ATOM   2238 C  CB    . CYS   A 1 410  ? 31.226  5.092   -84.603 1.00 71.19  ? 559  CYS   A CB    1 
ATOM   2239 S  SG    . CYS   A 1 410  ? 30.854  3.556   -83.718 1.00 69.74  ? 559  CYS   A SG    1 
ATOM   2240 N  N     . PRO   A 1 411  ? 34.349  4.735   -84.951 1.00 72.02  ? 560  PRO   A N     1 
ATOM   2241 C  CA    . PRO   A 1 411  ? 35.557  4.017   -84.544 1.00 71.50  ? 560  PRO   A CA    1 
ATOM   2242 C  C     . PRO   A 1 411  ? 35.273  2.950   -83.477 1.00 70.91  ? 560  PRO   A C     1 
ATOM   2243 O  O     . PRO   A 1 411  ? 34.319  3.101   -82.742 1.00 71.56  ? 560  PRO   A O     1 
ATOM   2244 C  CB    . PRO   A 1 411  ? 36.468  5.109   -83.960 1.00 72.38  ? 560  PRO   A CB    1 
ATOM   2245 C  CG    . PRO   A 1 411  ? 35.919  6.405   -84.524 1.00 72.58  ? 560  PRO   A CG    1 
ATOM   2246 C  CD    . PRO   A 1 411  ? 34.430  6.175   -84.662 1.00 72.15  ? 560  PRO   A CD    1 
ATOM   2247 N  N     . ILE   A 1 412  ? 36.105  1.906   -83.431 1.00 71.62  ? 561  ILE   A N     1 
ATOM   2248 C  CA    . ILE   A 1 412  ? 36.097  0.849   -82.377 1.00 73.06  ? 561  ILE   A CA    1 
ATOM   2249 C  C     . ILE   A 1 412  ? 37.466  0.863   -81.687 1.00 74.16  ? 561  ILE   A C     1 
ATOM   2250 O  O     . ILE   A 1 412  ? 38.432  0.344   -82.281 1.00 76.10  ? 561  ILE   A O     1 
ATOM   2251 C  CB    . ILE   A 1 412  ? 35.757  -0.534  -82.973 1.00 74.09  ? 561  ILE   A CB    1 
ATOM   2252 C  CG1   . ILE   A 1 412  ? 34.402  -0.523  -83.687 1.00 75.27  ? 561  ILE   A CG1   1 
ATOM   2253 C  CG2   . ILE   A 1 412  ? 35.823  -1.617  -81.902 1.00 73.24  ? 561  ILE   A CG2   1 
ATOM   2254 C  CD1   . ILE   A 1 412  ? 34.118  -1.764  -84.506 1.00 75.96  ? 561  ILE   A CD1   1 
ATOM   2255 N  N     . ILE   A 1 413  ? 37.542  1.444   -80.485 1.00 73.83  ? 562  ILE   A N     1 
ATOM   2256 C  CA    . ILE   A 1 413  ? 38.786  1.509   -79.661 1.00 73.01  ? 562  ILE   A CA    1 
ATOM   2257 C  C     . ILE   A 1 413  ? 38.936  0.167   -78.935 1.00 73.03  ? 562  ILE   A C     1 
ATOM   2258 O  O     . ILE   A 1 413  ? 38.070  -0.152  -78.098 1.00 71.45  ? 562  ILE   A O     1 
ATOM   2259 C  CB    . ILE   A 1 413  ? 38.764  2.702   -78.681 1.00 72.57  ? 562  ILE   A CB    1 
ATOM   2260 C  CG1   . ILE   A 1 413  ? 38.308  4.003   -79.351 1.00 72.86  ? 562  ILE   A CG1   1 
ATOM   2261 C  CG2   . ILE   A 1 413  ? 40.118  2.865   -78.007 1.00 72.31  ? 562  ILE   A CG2   1 
ATOM   2262 C  CD1   . ILE   A 1 413  ? 39.022  4.324   -80.646 1.00 73.27  ? 562  ILE   A CD1   1 
ATOM   2263 N  N     . GLU   A 1 414  ? 39.988  -0.588  -79.266 1.00 73.71  ? 563  GLU   A N     1 
ATOM   2264 C  CA    . GLU   A 1 414  ? 40.258  -1.945  -78.722 1.00 75.24  ? 563  GLU   A CA    1 
ATOM   2265 C  C     . GLU   A 1 414  ? 41.053  -1.820  -77.416 1.00 75.77  ? 563  GLU   A C     1 
ATOM   2266 O  O     . GLU   A 1 414  ? 42.097  -1.141  -77.423 1.00 77.44  ? 563  GLU   A O     1 
ATOM   2267 C  CB    . GLU   A 1 414  ? 41.019  -2.785  -79.751 1.00 76.58  ? 563  GLU   A CB    1 
ATOM   2268 C  CG    . GLU   A 1 414  ? 40.205  -3.111  -80.991 1.00 76.56  ? 563  GLU   A CG    1 
ATOM   2269 C  CD    . GLU   A 1 414  ? 39.088  -4.120  -80.783 1.00 76.37  ? 563  GLU   A CD    1 
ATOM   2270 O  OE1   . GLU   A 1 414  ? 39.041  -4.743  -79.702 1.00 74.57  ? 563  GLU   A OE1   1 
ATOM   2271 O  OE2   . GLU   A 1 414  ? 38.266  -4.283  -81.707 1.00 76.96  ? 563  GLU   A OE2   1 
ATOM   2272 N  N     . VAL   A 1 415  ? 40.569  -2.463  -76.348 1.00 75.54  ? 564  VAL   A N     1 
ATOM   2273 C  CA    . VAL   A 1 415  ? 41.189  -2.471  -74.989 1.00 74.76  ? 564  VAL   A CA    1 
ATOM   2274 C  C     . VAL   A 1 415  ? 41.450  -3.929  -74.584 1.00 77.20  ? 564  VAL   A C     1 
ATOM   2275 O  O     . VAL   A 1 415  ? 40.589  -4.786  -74.867 1.00 75.44  ? 564  VAL   A O     1 
ATOM   2276 C  CB    . VAL   A 1 415  ? 40.293  -1.740  -73.972 1.00 73.00  ? 564  VAL   A CB    1 
ATOM   2277 C  CG1   . VAL   A 1 415  ? 40.828  -1.857  -72.553 1.00 73.32  ? 564  VAL   A CG1   1 
ATOM   2278 C  CG2   . VAL   A 1 415  ? 40.097  -0.281  -74.352 1.00 72.79  ? 564  VAL   A CG2   1 
ATOM   2279 N  N     . TYR   A 1 416  ? 42.597  -4.192  -73.949 1.00 79.65  ? 565  TYR   A N     1 
ATOM   2280 C  CA    . TYR   A 1 416  ? 43.081  -5.554  -73.600 1.00 80.39  ? 565  TYR   A CA    1 
ATOM   2281 C  C     . TYR   A 1 416  ? 44.186  -5.471  -72.541 1.00 80.37  ? 565  TYR   A C     1 
ATOM   2282 O  O     . TYR   A 1 416  ? 44.813  -4.403  -72.385 1.00 78.36  ? 565  TYR   A O     1 
ATOM   2283 C  CB    . TYR   A 1 416  ? 43.588  -6.275  -74.853 1.00 81.37  ? 565  TYR   A CB    1 
ATOM   2284 C  CG    . TYR   A 1 416  ? 44.610  -5.503  -75.649 1.00 81.57  ? 565  TYR   A CG    1 
ATOM   2285 C  CD1   . TYR   A 1 416  ? 44.222  -4.560  -76.587 1.00 83.14  ? 565  TYR   A CD1   1 
ATOM   2286 C  CD2   . TYR   A 1 416  ? 45.968  -5.711  -75.465 1.00 82.76  ? 565  TYR   A CD2   1 
ATOM   2287 C  CE1   . TYR   A 1 416  ? 45.152  -3.844  -77.323 1.00 84.85  ? 565  TYR   A CE1   1 
ATOM   2288 C  CE2   . TYR   A 1 416  ? 46.913  -5.003  -76.191 1.00 83.84  ? 565  TYR   A CE2   1 
ATOM   2289 C  CZ    . TYR   A 1 416  ? 46.504  -4.065  -77.124 1.00 84.85  ? 565  TYR   A CZ    1 
ATOM   2290 O  OH    . TYR   A 1 416  ? 47.424  -3.361  -77.844 1.00 84.43  ? 565  TYR   A OH    1 
ATOM   2291 N  N     . GLY   A 1 417  ? 44.406  -6.587  -71.840 1.00 82.04  ? 566  GLY   A N     1 
ATOM   2292 C  CA    . GLY   A 1 417  ? 45.477  -6.769  -70.841 1.00 83.35  ? 566  GLY   A CA    1 
ATOM   2293 C  C     . GLY   A 1 417  ? 45.870  -8.230  -70.723 1.00 84.32  ? 566  GLY   A C     1 
ATOM   2294 O  O     . GLY   A 1 417  ? 45.491  -9.015  -71.614 1.00 81.35  ? 566  GLY   A O     1 
ATOM   2295 N  N     . ARG   A 1 418  ? 46.595  -8.589  -69.661 1.00 89.25  ? 567  ARG   A N     1 
ATOM   2296 C  CA    . ARG   A 1 418  ? 47.076  -9.975  -69.415 1.00 94.46  ? 567  ARG   A CA    1 
ATOM   2297 C  C     . ARG   A 1 418  ? 45.869  -10.908 -69.259 1.00 92.70  ? 567  ARG   A C     1 
ATOM   2298 O  O     . ARG   A 1 418  ? 44.947  -10.566 -68.495 1.00 93.06  ? 567  ARG   A O     1 
ATOM   2299 C  CB    . ARG   A 1 418  ? 47.980  -10.026 -68.178 1.00 100.85 ? 567  ARG   A CB    1 
ATOM   2300 C  CG    . ARG   A 1 418  ? 48.485  -11.420 -67.826 1.00 106.32 ? 567  ARG   A CG    1 
ATOM   2301 C  CD    . ARG   A 1 418  ? 49.935  -11.413 -67.363 1.00 109.79 ? 567  ARG   A CD    1 
ATOM   2302 N  NE    . ARG   A 1 418  ? 50.502  -12.730 -67.079 1.00 111.60 ? 567  ARG   A NE    1 
ATOM   2303 C  CZ    . ARG   A 1 418  ? 50.764  -13.676 -67.982 1.00 112.88 ? 567  ARG   A CZ    1 
ATOM   2304 N  NH1   . ARG   A 1 418  ? 50.488  -13.492 -69.263 1.00 112.31 ? 567  ARG   A NH1   1 
ATOM   2305 N  NH2   . ARG   A 1 418  ? 51.293  -14.825 -67.595 1.00 114.00 ? 567  ARG   A NH2   1 
ATOM   2306 N  N     . THR   A 1 419  ? 45.876  -12.025 -69.991 1.00 92.46  ? 568  THR   A N     1 
ATOM   2307 C  CA    . THR   A 1 419  ? 44.965  -13.185 -69.803 1.00 94.48  ? 568  THR   A CA    1 
ATOM   2308 C  C     . THR   A 1 419  ? 45.801  -14.467 -69.876 1.00 94.06  ? 568  THR   A C     1 
ATOM   2309 O  O     . THR   A 1 419  ? 46.815  -14.470 -70.600 1.00 93.30  ? 568  THR   A O     1 
ATOM   2310 C  CB    . THR   A 1 419  ? 43.823  -13.186 -70.828 1.00 96.38  ? 568  THR   A CB    1 
ATOM   2311 O  OG1   . THR   A 1 419  ? 44.381  -13.265 -72.141 1.00 96.90  ? 568  THR   A OG1   1 
ATOM   2312 C  CG2   . THR   A 1 419  ? 42.938  -11.964 -70.720 1.00 97.31  ? 568  THR   A CG2   1 
ATOM   2313 N  N     . TYR   A 1 420  ? 45.384  -15.503 -69.146 1.00 94.54  ? 569  TYR   A N     1 
ATOM   2314 C  CA    . TYR   A 1 420  ? 46.082  -16.809 -69.034 1.00 95.29  ? 569  TYR   A CA    1 
ATOM   2315 C  C     . TYR   A 1 420  ? 45.259  -17.874 -69.753 1.00 95.89  ? 569  TYR   A C     1 
ATOM   2316 O  O     . TYR   A 1 420  ? 44.036  -17.768 -69.820 1.00 94.96  ? 569  TYR   A O     1 
ATOM   2317 C  CB    . TYR   A 1 420  ? 46.302  -17.165 -67.561 1.00 95.75  ? 569  TYR   A CB    1 
ATOM   2318 C  CG    . TYR   A 1 420  ? 46.941  -16.076 -66.737 1.00 96.42  ? 569  TYR   A CG    1 
ATOM   2319 C  CD1   . TYR   A 1 420  ? 46.202  -14.991 -66.290 1.00 97.61  ? 569  TYR   A CD1   1 
ATOM   2320 C  CD2   . TYR   A 1 420  ? 48.283  -16.128 -66.395 1.00 96.67  ? 569  TYR   A CD2   1 
ATOM   2321 C  CE1   . TYR   A 1 420  ? 46.778  -13.986 -65.530 1.00 97.48  ? 569  TYR   A CE1   1 
ATOM   2322 C  CE2   . TYR   A 1 420  ? 48.873  -15.134 -65.630 1.00 96.14  ? 569  TYR   A CE2   1 
ATOM   2323 C  CZ    . TYR   A 1 420  ? 48.119  -14.057 -65.198 1.00 96.60  ? 569  TYR   A CZ    1 
ATOM   2324 O  OH    . TYR   A 1 420  ? 48.691  -13.071 -64.447 1.00 95.56  ? 569  TYR   A OH    1 
ATOM   2325 N  N     . PRO   A 1 421  ? 45.897  -18.930 -70.310 1.00 97.04  ? 570  PRO   A N     1 
ATOM   2326 C  CA    . PRO   A 1 421  ? 45.161  -20.005 -70.975 1.00 97.75  ? 570  PRO   A CA    1 
ATOM   2327 C  C     . PRO   A 1 421  ? 44.379  -20.842 -69.952 1.00 98.26  ? 570  PRO   A C     1 
ATOM   2328 O  O     . PRO   A 1 421  ? 45.003  -21.463 -69.108 1.00 100.30 ? 570  PRO   A O     1 
ATOM   2329 C  CB    . PRO   A 1 421  ? 46.263  -20.822 -71.667 1.00 98.16  ? 570  PRO   A CB    1 
ATOM   2330 C  CG    . PRO   A 1 421  ? 47.495  -20.578 -70.819 1.00 97.84  ? 570  PRO   A CG    1 
ATOM   2331 C  CD    . PRO   A 1 421  ? 47.351  -19.157 -70.315 1.00 97.64  ? 570  PRO   A CD    1 
ATOM   2332 N  N     . VAL   A 1 422  ? 43.045  -20.814 -70.037 1.00 95.85  ? 571  VAL   A N     1 
ATOM   2333 C  CA    . VAL   A 1 422  ? 42.124  -21.554 -69.124 1.00 96.30  ? 571  VAL   A CA    1 
ATOM   2334 C  C     . VAL   A 1 422  ? 41.817  -22.921 -69.742 1.00 97.18  ? 571  VAL   A C     1 
ATOM   2335 O  O     . VAL   A 1 422  ? 41.463  -22.965 -70.937 1.00 97.09  ? 571  VAL   A O     1 
ATOM   2336 C  CB    . VAL   A 1 422  ? 40.831  -20.761 -68.855 1.00 96.55  ? 571  VAL   A CB    1 
ATOM   2337 C  CG1   . VAL   A 1 422  ? 39.842  -21.558 -68.014 1.00 96.24  ? 571  VAL   A CG1   1 
ATOM   2338 C  CG2   . VAL   A 1 422  ? 41.122  -19.415 -68.212 1.00 97.23  ? 571  VAL   A CG2   1 
ATOM   2339 N  N     . GLN   A 1 423  ? 41.944  -23.985 -68.945 1.00 99.34  ? 572  GLN   A N     1 
ATOM   2340 C  CA    . GLN   A 1 423  ? 41.618  -25.380 -69.339 1.00 100.61 ? 572  GLN   A CA    1 
ATOM   2341 C  C     . GLN   A 1 423  ? 40.096  -25.553 -69.285 1.00 101.09 ? 572  GLN   A C     1 
ATOM   2342 O  O     . GLN   A 1 423  ? 39.518  -25.328 -68.204 1.00 101.58 ? 572  GLN   A O     1 
ATOM   2343 C  CB    . GLN   A 1 423  ? 42.341  -26.367 -68.418 1.00 100.69 ? 572  GLN   A CB    1 
ATOM   2344 C  CG    . GLN   A 1 423  ? 42.102  -27.834 -68.757 1.00 101.56 ? 572  GLN   A CG    1 
ATOM   2345 C  CD    . GLN   A 1 423  ? 42.523  -28.197 -70.161 1.00 103.40 ? 572  GLN   A CD    1 
ATOM   2346 O  OE1   . GLN   A 1 423  ? 41.810  -28.894 -70.880 1.00 102.75 ? 572  GLN   A OE1   1 
ATOM   2347 N  NE2   . GLN   A 1 423  ? 43.691  -27.724 -70.564 1.00 104.71 ? 572  GLN   A NE2   1 
ATOM   2348 N  N     . GLU   A 1 424  ? 39.479  -25.917 -70.414 1.00 100.93 ? 573  GLU   A N     1 
ATOM   2349 C  CA    . GLU   A 1 424  ? 38.018  -26.177 -70.528 1.00 100.51 ? 573  GLU   A CA    1 
ATOM   2350 C  C     . GLU   A 1 424  ? 37.744  -27.649 -70.203 1.00 96.98  ? 573  GLU   A C     1 
ATOM   2351 O  O     . GLU   A 1 424  ? 38.451  -28.514 -70.754 1.00 95.02  ? 573  GLU   A O     1 
ATOM   2352 C  CB    . GLU   A 1 424  ? 37.510  -25.832 -71.930 1.00 105.27 ? 573  GLU   A CB    1 
ATOM   2353 C  CG    . GLU   A 1 424  ? 37.630  -24.356 -72.274 1.00 107.79 ? 573  GLU   A CG    1 
ATOM   2354 C  CD    . GLU   A 1 424  ? 36.715  -23.861 -73.385 1.00 108.53 ? 573  GLU   A CD    1 
ATOM   2355 O  OE1   . GLU   A 1 424  ? 35.721  -24.553 -73.691 1.00 109.85 ? 573  GLU   A OE1   1 
ATOM   2356 O  OE2   . GLU   A 1 424  ? 36.997  -22.779 -73.942 1.00 105.84 ? 573  GLU   A OE2   1 
ATOM   2357 N  N     . TYR   A 1 425  ? 36.764  -27.907 -69.332 1.00 96.37  ? 574  TYR   A N     1 
ATOM   2358 C  CA    . TYR   A 1 425  ? 36.249  -29.259 -68.983 1.00 96.50  ? 574  TYR   A CA    1 
ATOM   2359 C  C     . TYR   A 1 425  ? 34.722  -29.265 -69.124 1.00 93.22  ? 574  TYR   A C     1 
ATOM   2360 O  O     . TYR   A 1 425  ? 34.084  -28.263 -68.746 1.00 93.65  ? 574  TYR   A O     1 
ATOM   2361 C  CB    . TYR   A 1 425  ? 36.646  -29.654 -67.557 1.00 98.28  ? 574  TYR   A CB    1 
ATOM   2362 C  CG    . TYR   A 1 425  ? 38.119  -29.898 -67.333 1.00 97.38  ? 574  TYR   A CG    1 
ATOM   2363 C  CD1   . TYR   A 1 425  ? 38.824  -30.805 -68.110 1.00 96.10  ? 574  TYR   A CD1   1 
ATOM   2364 C  CD2   . TYR   A 1 425  ? 38.803  -29.246 -66.319 1.00 97.04  ? 574  TYR   A CD2   1 
ATOM   2365 C  CE1   . TYR   A 1 425  ? 40.173  -31.040 -67.900 1.00 97.02  ? 574  TYR   A CE1   1 
ATOM   2366 C  CE2   . TYR   A 1 425  ? 40.151  -29.472 -66.095 1.00 96.80  ? 574  TYR   A CE2   1 
ATOM   2367 C  CZ    . TYR   A 1 425  ? 40.839  -30.372 -66.887 1.00 97.69  ? 574  TYR   A CZ    1 
ATOM   2368 O  OH    . TYR   A 1 425  ? 42.168  -30.596 -66.670 1.00 100.05 ? 574  TYR   A OH    1 
ATOM   2369 N  N     . PHE   A 1 426  ? 34.166  -30.363 -69.647 1.00 89.19  ? 575  PHE   A N     1 
ATOM   2370 C  CA    . PHE   A 1 426  ? 32.706  -30.589 -69.818 1.00 87.73  ? 575  PHE   A CA    1 
ATOM   2371 C  C     . PHE   A 1 426  ? 32.277  -31.764 -68.930 1.00 88.37  ? 575  PHE   A C     1 
ATOM   2372 O  O     . PHE   A 1 426  ? 33.160  -32.431 -68.357 1.00 90.79  ? 575  PHE   A O     1 
ATOM   2373 C  CB    . PHE   A 1 426  ? 32.378  -30.783 -71.301 1.00 86.41  ? 575  PHE   A CB    1 
ATOM   2374 C  CG    . PHE   A 1 426  ? 32.531  -29.528 -72.126 1.00 84.89  ? 575  PHE   A CG    1 
ATOM   2375 C  CD1   . PHE   A 1 426  ? 31.509  -28.594 -72.195 1.00 83.30  ? 575  PHE   A CD1   1 
ATOM   2376 C  CD2   . PHE   A 1 426  ? 33.707  -29.268 -72.813 1.00 84.04  ? 575  PHE   A CD2   1 
ATOM   2377 C  CE1   . PHE   A 1 426  ? 31.656  -27.434 -72.941 1.00 82.70  ? 575  PHE   A CE1   1 
ATOM   2378 C  CE2   . PHE   A 1 426  ? 33.852  -28.107 -73.560 1.00 83.26  ? 575  PHE   A CE2   1 
ATOM   2379 C  CZ    . PHE   A 1 426  ? 32.827  -27.192 -73.622 1.00 81.97  ? 575  PHE   A CZ    1 
ATOM   2380 N  N     . LEU   A 1 427  ? 30.964  -32.003 -68.831 1.00 88.01  ? 576  LEU   A N     1 
ATOM   2381 C  CA    . LEU   A 1 427  ? 30.317  -32.918 -67.845 1.00 88.89  ? 576  LEU   A CA    1 
ATOM   2382 C  C     . LEU   A 1 427  ? 31.043  -34.271 -67.776 1.00 91.56  ? 576  LEU   A C     1 
ATOM   2383 O  O     . LEU   A 1 427  ? 31.127  -34.826 -66.662 1.00 89.95  ? 576  LEU   A O     1 
ATOM   2384 C  CB    . LEU   A 1 427  ? 28.844  -33.098 -68.230 1.00 88.23  ? 576  LEU   A CB    1 
ATOM   2385 C  CG    . LEU   A 1 427  ? 27.993  -33.916 -67.259 1.00 87.68  ? 576  LEU   A CG    1 
ATOM   2386 C  CD1   . LEU   A 1 427  ? 28.105  -33.378 -65.840 1.00 87.79  ? 576  LEU   A CD1   1 
ATOM   2387 C  CD2   . LEU   A 1 427  ? 26.539  -33.936 -67.703 1.00 88.32  ? 576  LEU   A CD2   1 
ATOM   2388 N  N     . GLU   A 1 428  ? 31.534  -34.787 -68.910 1.00 97.01  ? 577  GLU   A N     1 
ATOM   2389 C  CA    . GLU   A 1 428  ? 32.301  -36.063 -68.992 1.00 98.76  ? 577  GLU   A CA    1 
ATOM   2390 C  C     . GLU   A 1 428  ? 33.606  -35.929 -68.200 1.00 99.18  ? 577  GLU   A C     1 
ATOM   2391 O  O     . GLU   A 1 428  ? 33.863  -36.795 -67.340 1.00 101.82 ? 577  GLU   A O     1 
ATOM   2392 C  CB    . GLU   A 1 428  ? 32.634  -36.435 -70.438 1.00 100.43 ? 577  GLU   A CB    1 
ATOM   2393 C  CG    . GLU   A 1 428  ? 31.421  -36.757 -71.291 1.00 100.12 ? 577  GLU   A CG    1 
ATOM   2394 C  CD    . GLU   A 1 428  ? 30.949  -35.619 -72.178 1.00 98.88  ? 577  GLU   A CD    1 
ATOM   2395 O  OE1   . GLU   A 1 428  ? 29.827  -35.127 -71.959 1.00 98.57  ? 577  GLU   A OE1   1 
ATOM   2396 O  OE2   . GLU   A 1 428  ? 31.704  -35.234 -73.091 1.00 95.57  ? 577  GLU   A OE2   1 
ATOM   2397 N  N     . ASP   A 1 429  ? 34.393  -34.888 -68.495 1.00 97.27  ? 578  ASP   A N     1 
ATOM   2398 C  CA    . ASP   A 1 429  ? 35.718  -34.615 -67.873 1.00 97.86  ? 578  ASP   A CA    1 
ATOM   2399 C  C     . ASP   A 1 429  ? 35.563  -34.502 -66.350 1.00 99.09  ? 578  ASP   A C     1 
ATOM   2400 O  O     . ASP   A 1 429  ? 36.431  -35.038 -65.634 1.00 100.77 ? 578  ASP   A O     1 
ATOM   2401 C  CB    . ASP   A 1 429  ? 36.360  -33.351 -68.453 1.00 98.02  ? 578  ASP   A CB    1 
ATOM   2402 C  CG    . ASP   A 1 429  ? 36.697  -33.438 -69.934 1.00 98.87  ? 578  ASP   A CG    1 
ATOM   2403 O  OD1   . ASP   A 1 429  ? 36.998  -34.551 -70.404 1.00 101.06 ? 578  ASP   A OD1   1 
ATOM   2404 O  OD2   . ASP   A 1 429  ? 36.657  -32.389 -70.605 1.00 98.99  ? 578  ASP   A OD2   1 
ATOM   2405 N  N     . CYS   A 1 430  ? 34.497  -33.844 -65.880 1.00 99.32  ? 579  CYS   A N     1 
ATOM   2406 C  CA    . CYS   A 1 430  ? 34.211  -33.583 -64.441 1.00 100.87 ? 579  CYS   A CA    1 
ATOM   2407 C  C     . CYS   A 1 430  ? 33.869  -34.889 -63.715 1.00 101.72 ? 579  CYS   A C     1 
ATOM   2408 O  O     . CYS   A 1 430  ? 34.518  -35.178 -62.690 1.00 103.92 ? 579  CYS   A O     1 
ATOM   2409 C  CB    . CYS   A 1 430  ? 33.060  -32.598 -64.274 1.00 101.59 ? 579  CYS   A CB    1 
ATOM   2410 S  SG    . CYS   A 1 430  ? 33.414  -30.951 -64.942 1.00 101.99 ? 579  CYS   A SG    1 
ATOM   2411 N  N     . ILE   A 1 431  ? 32.883  -35.634 -64.224 1.00 101.89 ? 580  ILE   A N     1 
ATOM   2412 C  CA    . ILE   A 1 431  ? 32.389  -36.919 -63.637 1.00 102.45 ? 580  ILE   A CA    1 
ATOM   2413 C  C     . ILE   A 1 431  ? 33.555  -37.914 -63.539 1.00 101.19 ? 580  ILE   A C     1 
ATOM   2414 O  O     . ILE   A 1 431  ? 33.610  -38.656 -62.536 1.00 100.04 ? 580  ILE   A O     1 
ATOM   2415 C  CB    . ILE   A 1 431  ? 31.204  -37.476 -64.457 1.00 102.19 ? 580  ILE   A CB    1 
ATOM   2416 C  CG1   . ILE   A 1 431  ? 29.947  -36.621 -64.269 1.00 102.30 ? 580  ILE   A CG1   1 
ATOM   2417 C  CG2   . ILE   A 1 431  ? 30.938  -38.939 -64.124 1.00 102.76 ? 580  ILE   A CG2   1 
ATOM   2418 C  CD1   . ILE   A 1 431  ? 28.874  -36.858 -65.306 1.00 103.16 ? 580  ILE   A CD1   1 
ATOM   2419 N  N     . GLN   A 1 432  ? 34.451  -37.918 -64.532 1.00 99.20  ? 581  GLN   A N     1 
ATOM   2420 C  CA    . GLN   A 1 432  ? 35.603  -38.856 -64.633 1.00 100.08 ? 581  GLN   A CA    1 
ATOM   2421 C  C     . GLN   A 1 432  ? 36.695  -38.466 -63.626 1.00 102.14 ? 581  GLN   A C     1 
ATOM   2422 O  O     . GLN   A 1 432  ? 37.221  -39.379 -62.955 1.00 103.08 ? 581  GLN   A O     1 
ATOM   2423 C  CB    . GLN   A 1 432  ? 36.145  -38.871 -66.064 1.00 98.53  ? 581  GLN   A CB    1 
ATOM   2424 C  CG    . GLN   A 1 432  ? 37.252  -39.893 -66.285 1.00 96.94  ? 581  GLN   A CG    1 
ATOM   2425 C  CD    . GLN   A 1 432  ? 37.255  -40.441 -67.691 1.00 95.29  ? 581  GLN   A CD    1 
ATOM   2426 O  OE1   . GLN   A 1 432  ? 36.307  -41.093 -68.123 1.00 93.33  ? 581  GLN   A OE1   1 
ATOM   2427 N  NE2   . GLN   A 1 432  ? 38.333  -40.191 -68.418 1.00 95.14  ? 581  GLN   A NE2   1 
ATOM   2428 N  N     . MET   A 1 433  ? 37.027  -37.173 -63.532 1.00 101.43 ? 582  MET   A N     1 
ATOM   2429 C  CA    . MET   A 1 433  ? 38.098  -36.636 -62.644 1.00 101.86 ? 582  MET   A CA    1 
ATOM   2430 C  C     . MET   A 1 433  ? 37.743  -36.879 -61.170 1.00 100.63 ? 582  MET   A C     1 
ATOM   2431 O  O     . MET   A 1 433  ? 38.660  -37.205 -60.389 1.00 101.23 ? 582  MET   A O     1 
ATOM   2432 C  CB    . MET   A 1 433  ? 38.307  -35.133 -62.866 1.00 102.94 ? 582  MET   A CB    1 
ATOM   2433 C  CG    . MET   A 1 433  ? 39.247  -34.814 -64.014 1.00 104.00 ? 582  MET   A CG    1 
ATOM   2434 S  SD    . MET   A 1 433  ? 39.695  -33.058 -64.080 1.00 106.48 ? 582  MET   A SD    1 
ATOM   2435 C  CE    . MET   A 1 433  ? 38.076  -32.301 -64.212 1.00 104.89 ? 582  MET   A CE    1 
ATOM   2436 N  N     . THR   A 1 434  ? 36.466  -36.722 -60.808 1.00 98.71  ? 583  THR   A N     1 
ATOM   2437 C  CA    . THR   A 1 434  ? 35.959  -36.795 -59.411 1.00 99.84  ? 583  THR   A CA    1 
ATOM   2438 C  C     . THR   A 1 434  ? 35.515  -38.223 -59.066 1.00 99.08  ? 583  THR   A C     1 
ATOM   2439 O  O     . THR   A 1 434  ? 35.293  -38.483 -57.867 1.00 101.06 ? 583  THR   A O     1 
ATOM   2440 C  CB    . THR   A 1 434  ? 34.807  -35.805 -59.199 1.00 102.34 ? 583  THR   A CB    1 
ATOM   2441 O  OG1   . THR   A 1 434  ? 33.726  -36.190 -60.050 1.00 102.73 ? 583  THR   A OG1   1 
ATOM   2442 C  CG2   . THR   A 1 434  ? 35.203  -34.374 -59.488 1.00 103.61 ? 583  THR   A CG2   1 
ATOM   2443 N  N     . HIS   A 1 435  ? 35.384  -39.103 -60.067 1.00 98.25  ? 584  HIS   A N     1 
ATOM   2444 C  CA    . HIS   A 1 435  ? 34.867  -40.493 -59.930 1.00 96.94  ? 584  HIS   A CA    1 
ATOM   2445 C  C     . HIS   A 1 435  ? 33.455  -40.446 -59.328 1.00 97.05  ? 584  HIS   A C     1 
ATOM   2446 O  O     . HIS   A 1 435  ? 33.157  -41.265 -58.435 1.00 97.91  ? 584  HIS   A O     1 
ATOM   2447 C  CB    . HIS   A 1 435  ? 35.843  -41.356 -59.112 1.00 96.11  ? 584  HIS   A CB    1 
ATOM   2448 C  CG    . HIS   A 1 435  ? 37.247  -41.340 -59.621 1.00 98.83  ? 584  HIS   A CG    1 
ATOM   2449 N  ND1   . HIS   A 1 435  ? 37.657  -42.114 -60.692 1.00 100.73 ? 584  HIS   A ND1   1 
ATOM   2450 C  CD2   . HIS   A 1 435  ? 38.339  -40.657 -59.210 1.00 99.67  ? 584  HIS   A CD2   1 
ATOM   2451 C  CE1   . HIS   A 1 435  ? 38.939  -41.904 -60.921 1.00 99.49  ? 584  HIS   A CE1   1 
ATOM   2452 N  NE2   . HIS   A 1 435  ? 39.381  -41.014 -60.025 1.00 99.78  ? 584  HIS   A NE2   1 
ATOM   2453 N  N     . PHE   A 1 436  ? 32.623  -39.517 -59.814 1.00 95.65  ? 585  PHE   A N     1 
ATOM   2454 C  CA    . PHE   A 1 436  ? 31.259  -39.218 -59.300 1.00 94.46  ? 585  PHE   A CA    1 
ATOM   2455 C  C     . PHE   A 1 436  ? 30.297  -40.345 -59.696 1.00 93.93  ? 585  PHE   A C     1 
ATOM   2456 O  O     . PHE   A 1 436  ? 30.550  -41.027 -60.709 1.00 96.49  ? 585  PHE   A O     1 
ATOM   2457 C  CB    . PHE   A 1 436  ? 30.786  -37.857 -59.820 1.00 92.93  ? 585  PHE   A CB    1 
ATOM   2458 C  CG    . PHE   A 1 436  ? 29.389  -37.461 -59.411 1.00 91.99  ? 585  PHE   A CG    1 
ATOM   2459 C  CD1   . PHE   A 1 436  ? 29.095  -37.161 -58.090 1.00 92.72  ? 585  PHE   A CD1   1 
ATOM   2460 C  CD2   . PHE   A 1 436  ? 28.369  -37.379 -60.347 1.00 92.64  ? 585  PHE   A CD2   1 
ATOM   2461 C  CE1   . PHE   A 1 436  ? 27.811  -36.796 -57.714 1.00 92.64  ? 585  PHE   A CE1   1 
ATOM   2462 C  CE2   . PHE   A 1 436  ? 27.085  -37.011 -59.969 1.00 91.33  ? 585  PHE   A CE2   1 
ATOM   2463 C  CZ    . PHE   A 1 436  ? 26.808  -36.721 -58.653 1.00 90.76  ? 585  PHE   A CZ    1 
ATOM   2464 N  N     . VAL   A 1 437  ? 29.236  -40.535 -58.905 1.00 92.97  ? 586  VAL   A N     1 
ATOM   2465 C  CA    . VAL   A 1 437  ? 28.141  -41.522 -59.152 1.00 96.44  ? 586  VAL   A CA    1 
ATOM   2466 C  C     . VAL   A 1 437  ? 26.820  -40.882 -58.730 1.00 98.02  ? 586  VAL   A C     1 
ATOM   2467 O  O     . VAL   A 1 437  ? 26.610  -40.635 -57.545 1.00 101.47 ? 586  VAL   A O     1 
ATOM   2468 C  CB    . VAL   A 1 437  ? 28.393  -42.846 -58.401 1.00 97.62  ? 586  VAL   A CB    1 
ATOM   2469 C  CG1   . VAL   A 1 437  ? 27.238  -43.824 -58.569 1.00 95.77  ? 586  VAL   A CG1   1 
ATOM   2470 C  CG2   . VAL   A 1 437  ? 29.706  -43.493 -58.819 1.00 97.73  ? 586  VAL   A CG2   1 
ATOM   2471 N  N     . PRO   A 1 438  ? 25.898  -40.573 -59.673 1.00 99.38  ? 587  PRO   A N     1 
ATOM   2472 C  CA    . PRO   A 1 438  ? 24.616  -39.959 -59.325 1.00 99.46  ? 587  PRO   A CA    1 
ATOM   2473 C  C     . PRO   A 1 438  ? 23.707  -40.852 -58.483 1.00 101.56 ? 587  PRO   A C     1 
ATOM   2474 O  O     . PRO   A 1 438  ? 23.859  -42.071 -58.483 1.00 102.46 ? 587  PRO   A O     1 
ATOM   2475 C  CB    . PRO   A 1 438  ? 23.936  -39.697 -60.678 1.00 100.35 ? 587  PRO   A CB    1 
ATOM   2476 C  CG    . PRO   A 1 438  ? 25.061  -39.754 -61.691 1.00 101.12 ? 587  PRO   A CG    1 
ATOM   2477 C  CD    . PRO   A 1 438  ? 26.055  -40.745 -61.125 1.00 100.62 ? 587  PRO   A CD    1 
ATOM   2478 N  N     . PRO   A 1 439  ? 22.724  -40.267 -57.760 1.00 106.59 ? 588  PRO   A N     1 
ATOM   2479 C  CA    . PRO   A 1 439  ? 21.766  -41.046 -56.970 1.00 109.85 ? 588  PRO   A CA    1 
ATOM   2480 C  C     . PRO   A 1 439  ? 20.764  -41.790 -57.854 1.00 115.77 ? 588  PRO   A C     1 
ATOM   2481 O  O     . PRO   A 1 439  ? 20.864  -41.738 -59.079 1.00 115.99 ? 588  PRO   A O     1 
ATOM   2482 C  CB    . PRO   A 1 439  ? 21.088  -39.975 -56.096 1.00 107.86 ? 588  PRO   A CB    1 
ATOM   2483 C  CG    . PRO   A 1 439  ? 21.183  -38.702 -56.908 1.00 107.76 ? 588  PRO   A CG    1 
ATOM   2484 C  CD    . PRO   A 1 439  ? 22.487  -38.817 -57.668 1.00 107.58 ? 588  PRO   A CD    1 
ATOM   2485 N  N     . PRO   A 1 440  ? 19.796  -42.541 -57.271 1.00 121.66 ? 589  PRO   A N     1 
ATOM   2486 C  CA    . PRO   A 1 440  ? 18.686  -43.118 -58.032 1.00 121.22 ? 589  PRO   A CA    1 
ATOM   2487 C  C     . PRO   A 1 440  ? 18.239  -42.273 -59.237 1.00 119.65 ? 589  PRO   A C     1 
ATOM   2488 O  O     . PRO   A 1 440  ? 17.181  -42.567 -59.766 1.00 118.65 ? 589  PRO   A O     1 
ATOM   2489 C  CB    . PRO   A 1 440  ? 17.573  -43.173 -56.973 1.00 121.46 ? 589  PRO   A CB    1 
ATOM   2490 C  CG    . PRO   A 1 440  ? 18.297  -43.371 -55.646 1.00 120.65 ? 589  PRO   A CG    1 
ATOM   2491 C  CD    . PRO   A 1 440  ? 19.734  -42.932 -55.853 1.00 120.96 ? 589  PRO   A CD    1 
ATOM   2492 N  N     . ALA   A 1 458  ? 16.193  -33.713 -76.990 1.00 96.75  ? 607  ALA   A N     1 
ATOM   2493 C  CA    . ALA   A 1 458  ? 16.928  -34.994 -76.855 1.00 97.82  ? 607  ALA   A CA    1 
ATOM   2494 C  C     . ALA   A 1 458  ? 17.947  -34.890 -75.714 1.00 99.85  ? 607  ALA   A C     1 
ATOM   2495 O  O     . ALA   A 1 458  ? 18.611  -33.840 -75.603 1.00 99.34  ? 607  ALA   A O     1 
ATOM   2496 C  CB    . ALA   A 1 458  ? 17.603  -35.347 -78.158 1.00 96.47  ? 607  ALA   A CB    1 
ATOM   2497 N  N     . ASN   A 1 459  ? 18.064  -35.952 -74.911 1.00 102.00 ? 608  ASN   A N     1 
ATOM   2498 C  CA    . ASN   A 1 459  ? 18.987  -36.043 -73.748 1.00 103.66 ? 608  ASN   A CA    1 
ATOM   2499 C  C     . ASN   A 1 459  ? 20.415  -36.270 -74.263 1.00 103.34 ? 608  ASN   A C     1 
ATOM   2500 O  O     . ASN   A 1 459  ? 20.686  -37.367 -74.786 1.00 102.60 ? 608  ASN   A O     1 
ATOM   2501 C  CB    . ASN   A 1 459  ? 18.539  -37.138 -72.777 1.00 105.42 ? 608  ASN   A CB    1 
ATOM   2502 C  CG    . ASN   A 1 459  ? 19.300  -37.112 -71.470 1.00 108.08 ? 608  ASN   A CG    1 
ATOM   2503 O  OD1   . ASN   A 1 459  ? 20.488  -37.422 -71.438 1.00 109.84 ? 608  ASN   A OD1   1 
ATOM   2504 N  ND2   . ASN   A 1 459  ? 18.628  -36.749 -70.389 1.00 108.71 ? 608  ASN   A ND2   1 
ATOM   2505 N  N     . CYS   A 1 460  ? 21.288  -35.266 -74.110 1.00 105.68 ? 609  CYS   A N     1 
ATOM   2506 C  CA    . CYS   A 1 460  ? 22.691  -35.257 -74.612 1.00 105.88 ? 609  CYS   A CA    1 
ATOM   2507 C  C     . CYS   A 1 460  ? 23.639  -35.905 -73.593 1.00 104.23 ? 609  CYS   A C     1 
ATOM   2508 O  O     . CYS   A 1 460  ? 24.833  -36.061 -73.924 1.00 102.51 ? 609  CYS   A O     1 
ATOM   2509 C  CB    . CYS   A 1 460  ? 23.156  -33.840 -74.931 1.00 106.27 ? 609  CYS   A CB    1 
ATOM   2510 S  SG    . CYS   A 1 460  ? 22.481  -33.196 -76.484 1.00 105.09 ? 609  CYS   A SG    1 
ATOM   2511 N  N     . ASN   A 1 461  ? 23.135  -36.260 -72.406 1.00 103.51 ? 610  ASN   A N     1 
ATOM   2512 C  CA    . ASN   A 1 461  ? 23.894  -37.012 -71.369 1.00 104.10 ? 610  ASN   A CA    1 
ATOM   2513 C  C     . ASN   A 1 461  ? 24.023  -38.480 -71.802 1.00 105.15 ? 610  ASN   A C     1 
ATOM   2514 O  O     . ASN   A 1 461  ? 24.959  -39.151 -71.323 1.00 107.54 ? 610  ASN   A O     1 
ATOM   2515 C  CB    . ASN   A 1 461  ? 23.249  -36.878 -69.985 1.00 102.01 ? 610  ASN   A CB    1 
ATOM   2516 C  CG    . ASN   A 1 461  ? 23.273  -35.463 -69.444 1.00 100.21 ? 610  ASN   A CG    1 
ATOM   2517 O  OD1   . ASN   A 1 461  ? 23.993  -34.605 -69.951 1.00 96.33  ? 610  ASN   A OD1   1 
ATOM   2518 N  ND2   . ASN   A 1 461  ? 22.489  -35.207 -68.409 1.00 99.98  ? 610  ASN   A ND2   1 
ATOM   2519 N  N     . LEU   A 1 462  ? 23.122  -38.954 -72.673 1.00 104.03 ? 611  LEU   A N     1 
ATOM   2520 C  CA    . LEU   A 1 462  ? 23.147  -40.325 -73.254 1.00 100.98 ? 611  LEU   A CA    1 
ATOM   2521 C  C     . LEU   A 1 462  ? 24.266  -40.419 -74.299 1.00 99.36  ? 611  LEU   A C     1 
ATOM   2522 O  O     . LEU   A 1 462  ? 24.939  -41.468 -74.345 1.00 101.02 ? 611  LEU   A O     1 
ATOM   2523 C  CB    . LEU   A 1 462  ? 21.782  -40.643 -73.875 1.00 100.64 ? 611  LEU   A CB    1 
ATOM   2524 C  CG    . LEU   A 1 462  ? 20.603  -40.681 -72.904 1.00 102.30 ? 611  LEU   A CG    1 
ATOM   2525 C  CD1   . LEU   A 1 462  ? 19.297  -40.933 -73.644 1.00 102.17 ? 611  LEU   A CD1   1 
ATOM   2526 C  CD2   . LEU   A 1 462  ? 20.814  -41.733 -71.824 1.00 103.35 ? 611  LEU   A CD2   1 
ATOM   2527 N  N     . ILE   A 1 463  ? 24.452  -39.367 -75.103 1.00 97.41  ? 612  ILE   A N     1 
ATOM   2528 C  CA    . ILE   A 1 463  ? 25.529  -39.273 -76.135 1.00 97.88  ? 612  ILE   A CA    1 
ATOM   2529 C  C     . ILE   A 1 463  ? 26.852  -38.981 -75.415 1.00 99.32  ? 612  ILE   A C     1 
ATOM   2530 O  O     . ILE   A 1 463  ? 26.899  -38.004 -74.643 1.00 99.65  ? 612  ILE   A O     1 
ATOM   2531 C  CB    . ILE   A 1 463  ? 25.199  -38.209 -77.207 1.00 96.55  ? 612  ILE   A CB    1 
ATOM   2532 C  CG1   . ILE   A 1 463  ? 24.019  -38.628 -78.092 1.00 96.16  ? 612  ILE   A CG1   1 
ATOM   2533 C  CG2   . ILE   A 1 463  ? 26.428  -37.879 -78.044 1.00 95.49  ? 612  ILE   A CG2   1 
ATOM   2534 C  CD1   . ILE   A 1 463  ? 22.655  -38.370 -77.490 1.00 96.11  ? 612  ILE   A CD1   1 
ATOM   2535 N  N     . CYS   A 1 464  ? 27.877  -39.801 -75.661 1.00 102.89 ? 613  CYS   A N     1 
ATOM   2536 C  CA    . CYS   A 1 464  ? 29.226  -39.696 -75.041 1.00 107.42 ? 613  CYS   A CA    1 
ATOM   2537 C  C     . CYS   A 1 464  ? 30.244  -40.471 -75.888 1.00 107.53 ? 613  CYS   A C     1 
ATOM   2538 O  O     . CYS   A 1 464  ? 29.954  -41.632 -76.235 1.00 107.29 ? 613  CYS   A O     1 
ATOM   2539 C  CB    . CYS   A 1 464  ? 29.204  -40.227 -73.612 1.00 111.24 ? 613  CYS   A CB    1 
ATOM   2540 S  SG    . CYS   A 1 464  ? 30.766  -40.001 -72.720 1.00 117.57 ? 613  CYS   A SG    1 
ATOM   2541 N  N     . GLY   A 1 465  ? 31.385  -39.846 -76.201 1.00 110.75 ? 614  GLY   A N     1 
ATOM   2542 C  CA    . GLY   A 1 465  ? 32.456  -40.422 -77.040 1.00 115.94 ? 614  GLY   A CA    1 
ATOM   2543 C  C     . GLY   A 1 465  ? 33.072  -41.664 -76.414 1.00 121.29 ? 614  GLY   A C     1 
ATOM   2544 O  O     . GLY   A 1 465  ? 32.955  -41.828 -75.183 1.00 120.96 ? 614  GLY   A O     1 
ATOM   2545 N  N     . ASP   A 1 466  ? 33.716  -42.503 -77.235 1.00 126.91 ? 615  ASP   A N     1 
ATOM   2546 C  CA    . ASP   A 1 466  ? 34.352  -43.786 -76.821 1.00 128.66 ? 615  ASP   A CA    1 
ATOM   2547 C  C     . ASP   A 1 466  ? 35.634  -43.504 -76.024 1.00 129.48 ? 615  ASP   A C     1 
ATOM   2548 O  O     . ASP   A 1 466  ? 36.047  -44.392 -75.250 1.00 129.60 ? 615  ASP   A O     1 
ATOM   2549 C  CB    . ASP   A 1 466  ? 34.664  -44.675 -78.029 1.00 128.41 ? 615  ASP   A CB    1 
ATOM   2550 C  CG    . ASP   A 1 466  ? 33.443  -45.120 -78.818 1.00 128.19 ? 615  ASP   A CG    1 
ATOM   2551 O  OD1   . ASP   A 1 466  ? 32.347  -45.182 -78.225 1.00 130.53 ? 615  ASP   A OD1   1 
ATOM   2552 O  OD2   . ASP   A 1 466  ? 33.600  -45.403 -80.023 1.00 125.49 ? 615  ASP   A OD2   1 
ATOM   2553 N  N     . GLU   A 1 467  ? 36.230  -42.318 -76.201 1.00 127.59 ? 616  GLU   A N     1 
ATOM   2554 C  CA    . GLU   A 1 467  ? 37.493  -41.887 -75.535 1.00 125.73 ? 616  GLU   A CA    1 
ATOM   2555 C  C     . GLU   A 1 467  ? 37.265  -41.643 -74.033 1.00 124.96 ? 616  GLU   A C     1 
ATOM   2556 O  O     . GLU   A 1 467  ? 38.202  -41.138 -73.383 1.00 122.91 ? 616  GLU   A O     1 
ATOM   2557 C  CB    . GLU   A 1 467  ? 38.070  -40.643 -76.223 1.00 124.72 ? 616  GLU   A CB    1 
ATOM   2558 C  CG    . GLU   A 1 467  ? 37.252  -39.370 -76.035 1.00 124.96 ? 616  GLU   A CG    1 
ATOM   2559 C  CD    . GLU   A 1 467  ? 36.099  -39.169 -77.006 1.00 124.09 ? 616  GLU   A CD    1 
ATOM   2560 O  OE1   . GLU   A 1 467  ? 35.689  -40.153 -77.655 1.00 122.20 ? 616  GLU   A OE1   1 
ATOM   2561 O  OE2   . GLU   A 1 467  ? 35.610  -38.027 -77.109 1.00 121.92 ? 616  GLU   A OE2   1 
ATOM   2562 N  N     . TYR   A 1 468  ? 36.080  -41.977 -73.505 1.00 126.01 ? 617  TYR   A N     1 
ATOM   2563 C  CA    . TYR   A 1 468  ? 35.721  -41.897 -72.062 1.00 127.04 ? 617  TYR   A CA    1 
ATOM   2564 C  C     . TYR   A 1 468  ? 35.444  -43.306 -71.521 1.00 125.88 ? 617  TYR   A C     1 
ATOM   2565 O  O     . TYR   A 1 468  ? 35.357  -44.258 -72.323 1.00 127.68 ? 617  TYR   A O     1 
ATOM   2566 C  CB    . TYR   A 1 468  ? 34.519  -40.967 -71.863 1.00 129.89 ? 617  TYR   A CB    1 
ATOM   2567 C  CG    . TYR   A 1 468  ? 34.814  -39.509 -72.113 1.00 131.25 ? 617  TYR   A CG    1 
ATOM   2568 C  CD1   . TYR   A 1 468  ? 35.626  -38.790 -71.251 1.00 130.80 ? 617  TYR   A CD1   1 
ATOM   2569 C  CD2   . TYR   A 1 468  ? 34.288  -38.845 -73.211 1.00 131.70 ? 617  TYR   A CD2   1 
ATOM   2570 C  CE1   . TYR   A 1 468  ? 35.910  -37.452 -71.471 1.00 130.05 ? 617  TYR   A CE1   1 
ATOM   2571 C  CE2   . TYR   A 1 468  ? 34.562  -37.506 -73.445 1.00 131.45 ? 617  TYR   A CE2   1 
ATOM   2572 C  CZ    . TYR   A 1 468  ? 35.377  -36.806 -72.572 1.00 130.06 ? 617  TYR   A CZ    1 
ATOM   2573 O  OH    . TYR   A 1 468  ? 35.653  -35.488 -72.793 1.00 127.47 ? 617  TYR   A OH    1 
ATOM   2574 N  N     . GLY   A 1 469  ? 35.309  -43.426 -70.196 1.00 124.24 ? 618  GLY   A N     1 
ATOM   2575 C  CA    . GLY   A 1 469  ? 35.111  -44.706 -69.488 1.00 123.89 ? 618  GLY   A CA    1 
ATOM   2576 C  C     . GLY   A 1 469  ? 33.664  -45.191 -69.568 1.00 124.07 ? 618  GLY   A C     1 
ATOM   2577 O  O     . GLY   A 1 469  ? 32.751  -44.386 -69.743 1.00 125.24 ? 618  GLY   A O     1 
ATOM   2578 N  N     . PRO   A 1 470  ? 33.413  -46.518 -69.456 1.00 124.79 ? 619  PRO   A N     1 
ATOM   2579 C  CA    . PRO   A 1 470  ? 32.051  -47.057 -69.405 1.00 123.92 ? 619  PRO   A CA    1 
ATOM   2580 C  C     . PRO   A 1 470  ? 31.188  -46.518 -68.252 1.00 121.87 ? 619  PRO   A C     1 
ATOM   2581 O  O     . PRO   A 1 470  ? 30.017  -46.271 -68.476 1.00 119.66 ? 619  PRO   A O     1 
ATOM   2582 C  CB    . PRO   A 1 470  ? 32.253  -48.567 -69.197 1.00 124.37 ? 619  PRO   A CB    1 
ATOM   2583 C  CG    . PRO   A 1 470  ? 33.647  -48.841 -69.718 1.00 125.01 ? 619  PRO   A CG    1 
ATOM   2584 C  CD    . PRO   A 1 470  ? 34.432  -47.579 -69.427 1.00 124.52 ? 619  PRO   A CD    1 
ATOM   2585 N  N     . GLU   A 1 471  ? 31.774  -46.374 -67.058 1.00 120.64 ? 620  GLU   A N     1 
ATOM   2586 C  CA    . GLU   A 1 471  ? 31.075  -45.900 -65.831 1.00 120.06 ? 620  GLU   A CA    1 
ATOM   2587 C  C     . GLU   A 1 471  ? 30.764  -44.403 -65.963 1.00 119.06 ? 620  GLU   A C     1 
ATOM   2588 O  O     . GLU   A 1 471  ? 29.668  -43.998 -65.534 1.00 119.59 ? 620  GLU   A O     1 
ATOM   2589 C  CB    . GLU   A 1 471  ? 31.909  -46.179 -64.578 1.00 119.53 ? 620  GLU   A CB    1 
ATOM   2590 C  CG    . GLU   A 1 471  ? 31.127  -46.006 -63.284 1.00 118.19 ? 620  GLU   A CG    1 
ATOM   2591 C  CD    . GLU   A 1 471  ? 31.962  -45.989 -62.014 1.00 116.13 ? 620  GLU   A CD    1 
ATOM   2592 O  OE1   . GLU   A 1 471  ? 31.516  -46.576 -61.007 1.00 114.15 ? 620  GLU   A OE1   1 
ATOM   2593 O  OE2   . GLU   A 1 471  ? 33.048  -45.375 -62.029 1.00 114.44 ? 620  GLU   A OE2   1 
ATOM   2594 N  N     . THR   A 1 472  ? 31.695  -43.619 -66.520 1.00 115.80 ? 621  THR   A N     1 
ATOM   2595 C  CA    . THR   A 1 472  ? 31.525  -42.169 -66.818 1.00 113.20 ? 621  THR   A CA    1 
ATOM   2596 C  C     . THR   A 1 472  ? 30.293  -41.989 -67.714 1.00 110.53 ? 621  THR   A C     1 
ATOM   2597 O  O     . THR   A 1 472  ? 29.401  -41.199 -67.343 1.00 107.87 ? 621  THR   A O     1 
ATOM   2598 C  CB    . THR   A 1 472  ? 32.786  -41.586 -67.474 1.00 113.54 ? 621  THR   A CB    1 
ATOM   2599 O  OG1   . THR   A 1 472  ? 33.904  -41.868 -66.631 1.00 113.75 ? 621  THR   A OG1   1 
ATOM   2600 C  CG2   . THR   A 1 472  ? 32.698  -40.094 -67.711 1.00 113.47 ? 621  THR   A CG2   1 
ATOM   2601 N  N     . ARG   A 1 473  ? 30.262  -42.710 -68.839 1.00 109.45 ? 622  ARG   A N     1 
ATOM   2602 C  CA    . ARG   A 1 473  ? 29.148  -42.730 -69.826 1.00 109.94 ? 622  ARG   A CA    1 
ATOM   2603 C  C     . ARG   A 1 473  ? 27.864  -43.213 -69.135 1.00 109.81 ? 622  ARG   A C     1 
ATOM   2604 O  O     . ARG   A 1 473  ? 26.810  -42.580 -69.346 1.00 110.58 ? 622  ARG   A O     1 
ATOM   2605 C  CB    . ARG   A 1 473  ? 29.546  -43.610 -71.018 1.00 111.53 ? 622  ARG   A CB    1 
ATOM   2606 C  CG    . ARG   A 1 473  ? 28.487  -43.740 -72.105 1.00 113.93 ? 622  ARG   A CG    1 
ATOM   2607 C  CD    . ARG   A 1 473  ? 29.049  -44.178 -73.451 1.00 115.55 ? 622  ARG   A CD    1 
ATOM   2608 N  NE    . ARG   A 1 473  ? 30.142  -45.144 -73.350 1.00 118.03 ? 622  ARG   A NE    1 
ATOM   2609 C  CZ    . ARG   A 1 473  ? 31.444  -44.867 -73.461 1.00 118.22 ? 622  ARG   A CZ    1 
ATOM   2610 N  NH1   . ARG   A 1 473  ? 31.865  -43.631 -73.680 1.00 118.12 ? 622  ARG   A NH1   1 
ATOM   2611 N  NH2   . ARG   A 1 473  ? 32.333  -45.840 -73.346 1.00 117.49 ? 622  ARG   A NH2   1 
ATOM   2612 N  N     . MET   A 1 474  ? 27.959  -44.278 -68.330 1.00 110.24 ? 623  MET   A N     1 
ATOM   2613 C  CA    . MET   A 1 474  ? 26.821  -44.892 -67.588 1.00 110.50 ? 623  MET   A CA    1 
ATOM   2614 C  C     . MET   A 1 474  ? 26.331  -43.929 -66.497 1.00 108.88 ? 623  MET   A C     1 
ATOM   2615 O  O     . MET   A 1 474  ? 25.106  -43.878 -66.267 1.00 102.77 ? 623  MET   A O     1 
ATOM   2616 C  CB    . MET   A 1 474  ? 27.237  -46.226 -66.955 1.00 110.85 ? 623  MET   A CB    1 
ATOM   2617 C  CG    . MET   A 1 474  ? 26.159  -46.888 -66.104 1.00 112.31 ? 623  MET   A CG    1 
ATOM   2618 S  SD    . MET   A 1 474  ? 24.595  -47.162 -66.982 1.00 114.55 ? 623  MET   A SD    1 
ATOM   2619 C  CE    . MET   A 1 474  ? 23.684  -48.098 -65.756 1.00 113.63 ? 623  MET   A CE    1 
ATOM   2620 N  N     . SER   A 1 475  ? 27.254  -43.205 -65.851 1.00 110.21 ? 624  SER   A N     1 
ATOM   2621 C  CA    . SER   A 1 475  ? 26.973  -42.221 -64.771 1.00 108.57 ? 624  SER   A CA    1 
ATOM   2622 C  C     . SER   A 1 475  ? 26.231  -41.015 -65.357 1.00 105.38 ? 624  SER   A C     1 
ATOM   2623 O  O     . SER   A 1 475  ? 25.096  -40.750 -64.914 1.00 102.62 ? 624  SER   A O     1 
ATOM   2624 C  CB    . SER   A 1 475  ? 28.238  -41.791 -64.067 1.00 109.43 ? 624  SER   A CB    1 
ATOM   2625 O  OG    . SER   A 1 475  ? 28.782  -42.856 -63.301 1.00 109.89 ? 624  SER   A OG    1 
ATOM   2626 N  N     . MET   A 1 476  ? 26.852  -40.328 -66.322 1.00 101.33 ? 625  MET   A N     1 
ATOM   2627 C  CA    . MET   A 1 476  ? 26.299  -39.117 -66.988 1.00 98.52  ? 625  MET   A CA    1 
ATOM   2628 C  C     . MET   A 1 476  ? 24.850  -39.386 -67.411 1.00 95.95  ? 625  MET   A C     1 
ATOM   2629 O  O     . MET   A 1 476  ? 23.982  -38.550 -67.101 1.00 94.13  ? 625  MET   A O     1 
ATOM   2630 C  CB    . MET   A 1 476  ? 27.128  -38.726 -68.218 1.00 96.49  ? 625  MET   A CB    1 
ATOM   2631 C  CG    . MET   A 1 476  ? 26.720  -37.391 -68.818 1.00 94.99  ? 625  MET   A CG    1 
ATOM   2632 S  SD    . MET   A 1 476  ? 28.015  -36.636 -69.832 1.00 93.30  ? 625  MET   A SD    1 
ATOM   2633 C  CE    . MET   A 1 476  ? 27.955  -37.695 -71.275 1.00 95.17  ? 625  MET   A CE    1 
ATOM   2634 N  N     . ALA   A 1 477  ? 24.605  -40.534 -68.053 1.00 95.45  ? 626  ALA   A N     1 
ATOM   2635 C  CA    . ALA   A 1 477  ? 23.292  -40.967 -68.593 1.00 95.14  ? 626  ALA   A CA    1 
ATOM   2636 C  C     . ALA   A 1 477  ? 22.196  -40.890 -67.519 1.00 93.81  ? 626  ALA   A C     1 
ATOM   2637 O  O     . ALA   A 1 477  ? 21.026  -40.689 -67.899 1.00 93.47  ? 626  ALA   A O     1 
ATOM   2638 C  CB    . ALA   A 1 477  ? 23.410  -42.363 -69.155 1.00 95.40  ? 626  ALA   A CB    1 
ATOM   2639 N  N     . GLN   A 1 478  ? 22.549  -41.046 -66.236 1.00 93.22  ? 627  GLN   A N     1 
ATOM   2640 C  CA    . GLN   A 1 478  ? 21.591  -41.057 -65.095 1.00 92.64  ? 627  GLN   A CA    1 
ATOM   2641 C  C     . GLN   A 1 478  ? 21.190  -39.625 -64.708 1.00 89.98  ? 627  GLN   A C     1 
ATOM   2642 O  O     . GLN   A 1 478  ? 20.178  -39.486 -63.993 1.00 87.14  ? 627  GLN   A O     1 
ATOM   2643 C  CB    . GLN   A 1 478  ? 22.191  -41.772 -63.880 1.00 94.83  ? 627  GLN   A CB    1 
ATOM   2644 C  CG    . GLN   A 1 478  ? 22.609  -43.213 -64.148 1.00 95.62  ? 627  GLN   A CG    1 
ATOM   2645 C  CD    . GLN   A 1 478  ? 21.443  -44.157 -64.320 1.00 95.24  ? 627  GLN   A CD    1 
ATOM   2646 O  OE1   . GLN   A 1 478  ? 20.324  -43.888 -63.886 1.00 93.70  ? 627  GLN   A OE1   1 
ATOM   2647 N  NE2   . GLN   A 1 478  ? 21.704  -45.288 -64.956 1.00 95.83  ? 627  GLN   A NE2   1 
ATOM   2648 N  N     . LEU   A 1 479  ? 21.947  -38.609 -65.146 1.00 89.54  ? 628  LEU   A N     1 
ATOM   2649 C  CA    . LEU   A 1 479  ? 21.715  -37.177 -64.798 1.00 88.63  ? 628  LEU   A CA    1 
ATOM   2650 C  C     . LEU   A 1 479  ? 20.652  -36.574 -65.724 1.00 88.30  ? 628  LEU   A C     1 
ATOM   2651 O  O     . LEU   A 1 479  ? 20.804  -36.685 -66.956 1.00 88.37  ? 628  LEU   A O     1 
ATOM   2652 C  CB    . LEU   A 1 479  ? 23.027  -36.391 -64.912 1.00 87.57  ? 628  LEU   A CB    1 
ATOM   2653 C  CG    . LEU   A 1 479  ? 24.075  -36.692 -63.843 1.00 87.17  ? 628  LEU   A CG    1 
ATOM   2654 C  CD1   . LEU   A 1 479  ? 25.429  -36.118 -64.236 1.00 86.37  ? 628  LEU   A CD1   1 
ATOM   2655 C  CD2   . LEU   A 1 479  ? 23.637  -36.158 -62.486 1.00 86.29  ? 628  LEU   A CD2   1 
ATOM   2656 N  N     . ASN   A 1 480  ? 19.631  -35.946 -65.136 1.00 88.52  ? 629  ASN   A N     1 
ATOM   2657 C  CA    . ASN   A 1 480  ? 18.608  -35.128 -65.840 1.00 89.88  ? 629  ASN   A CA    1 
ATOM   2658 C  C     . ASN   A 1 480  ? 19.244  -33.783 -66.217 1.00 90.13  ? 629  ASN   A C     1 
ATOM   2659 O  O     . ASN   A 1 480  ? 19.829  -33.141 -65.322 1.00 94.38  ? 629  ASN   A O     1 
ATOM   2660 C  CB    . ASN   A 1 480  ? 17.361  -34.949 -64.967 1.00 90.55  ? 629  ASN   A CB    1 
ATOM   2661 C  CG    . ASN   A 1 480  ? 16.154  -34.425 -65.716 1.00 91.87  ? 629  ASN   A CG    1 
ATOM   2662 O  OD1   . ASN   A 1 480  ? 16.169  -34.311 -66.940 1.00 94.50  ? 629  ASN   A OD1   1 
ATOM   2663 N  ND2   . ASN   A 1 480  ? 15.096  -34.111 -64.986 1.00 91.85  ? 629  ASN   A ND2   1 
ATOM   2664 N  N     . GLU   A 1 481  ? 19.145  -33.379 -67.488 1.00 88.03  ? 630  GLU   A N     1 
ATOM   2665 C  CA    . GLU   A 1 481  ? 19.734  -32.114 -68.011 1.00 86.41  ? 630  GLU   A CA    1 
ATOM   2666 C  C     . GLU   A 1 481  ? 18.953  -30.902 -67.487 1.00 85.67  ? 630  GLU   A C     1 
ATOM   2667 O  O     . GLU   A 1 481  ? 19.564  -29.824 -67.361 1.00 83.41  ? 630  GLU   A O     1 
ATOM   2668 C  CB    . GLU   A 1 481  ? 19.749  -32.106 -69.541 1.00 86.07  ? 630  GLU   A CB    1 
ATOM   2669 C  CG    . GLU   A 1 481  ? 20.958  -32.799 -70.138 1.00 86.31  ? 630  GLU   A CG    1 
ATOM   2670 C  CD    . GLU   A 1 481  ? 21.180  -32.507 -71.611 1.00 86.16  ? 630  GLU   A CD    1 
ATOM   2671 O  OE1   . GLU   A 1 481  ? 20.255  -32.765 -72.408 1.00 85.45  ? 630  GLU   A OE1   1 
ATOM   2672 O  OE2   . GLU   A 1 481  ? 22.275  -32.017 -71.956 1.00 85.32  ? 630  GLU   A OE2   1 
ATOM   2673 N  N     . LYS   A 1 482  ? 17.660  -31.072 -67.193 1.00 88.15  ? 631  LYS   A N     1 
ATOM   2674 C  CA    . LYS   A 1 482  ? 16.740  -29.976 -66.778 1.00 91.83  ? 631  LYS   A CA    1 
ATOM   2675 C  C     . LYS   A 1 482  ? 17.058  -29.531 -65.343 1.00 93.20  ? 631  LYS   A C     1 
ATOM   2676 O  O     . LYS   A 1 482  ? 16.563  -28.459 -64.945 1.00 93.35  ? 631  LYS   A O     1 
ATOM   2677 C  CB    . LYS   A 1 482  ? 15.281  -30.424 -66.919 1.00 92.95  ? 631  LYS   A CB    1 
ATOM   2678 C  CG    . LYS   A 1 482  ? 14.881  -30.850 -68.325 1.00 95.09  ? 631  LYS   A CG    1 
ATOM   2679 C  CD    . LYS   A 1 482  ? 13.391  -31.012 -68.524 1.00 96.54  ? 631  LYS   A CD    1 
ATOM   2680 C  CE    . LYS   A 1 482  ? 13.040  -31.495 -69.916 1.00 97.64  ? 631  LYS   A CE    1 
ATOM   2681 N  NZ    . LYS   A 1 482  ? 11.583  -31.418 -70.174 1.00 98.89  ? 631  LYS   A NZ    1 
ATOM   2682 N  N     . GLU   A 1 483  ? 17.841  -30.322 -64.601 1.00 96.84  ? 632  GLU   A N     1 
ATOM   2683 C  CA    . GLU   A 1 483  ? 18.334  -29.997 -63.234 1.00 98.27  ? 632  GLU   A CA    1 
ATOM   2684 C  C     . GLU   A 1 483  ? 19.857  -29.826 -63.266 1.00 96.10  ? 632  GLU   A C     1 
ATOM   2685 O  O     . GLU   A 1 483  ? 20.501  -30.418 -64.156 1.00 92.88  ? 632  GLU   A O     1 
ATOM   2686 C  CB    . GLU   A 1 483  ? 17.950  -31.104 -62.251 1.00 100.88 ? 632  GLU   A CB    1 
ATOM   2687 C  CG    . GLU   A 1 483  ? 16.454  -31.229 -62.026 1.00 102.70 ? 632  GLU   A CG    1 
ATOM   2688 C  CD    . GLU   A 1 483  ? 16.041  -32.419 -61.175 1.00 104.50 ? 632  GLU   A CD    1 
ATOM   2689 O  OE1   . GLU   A 1 483  ? 14.981  -32.337 -60.524 1.00 107.34 ? 632  GLU   A OE1   1 
ATOM   2690 O  OE2   . GLU   A 1 483  ? 16.778  -33.426 -61.168 1.00 104.23 ? 632  GLU   A OE2   1 
ATOM   2691 N  N     . THR   A 1 484  ? 20.402  -29.050 -62.325 1.00 96.05  ? 633  THR   A N     1 
ATOM   2692 C  CA    . THR   A 1 484  ? 21.863  -28.861 -62.115 1.00 95.76  ? 633  THR   A CA    1 
ATOM   2693 C  C     . THR   A 1 484  ? 22.339  -29.871 -61.073 1.00 93.96  ? 633  THR   A C     1 
ATOM   2694 O  O     . THR   A 1 484  ? 21.749  -29.977 -60.000 1.00 92.04  ? 633  THR   A O     1 
ATOM   2695 C  CB    . THR   A 1 484  ? 22.189  -27.421 -61.697 1.00 96.09  ? 633  THR   A CB    1 
ATOM   2696 O  OG1   . THR   A 1 484  ? 21.572  -26.531 -62.627 1.00 96.82  ? 633  THR   A OG1   1 
ATOM   2697 C  CG2   . THR   A 1 484  ? 23.677  -27.149 -61.648 1.00 96.14  ? 633  THR   A CG2   1 
ATOM   2698 N  N     . PRO   A 1 485  ? 23.411  -30.647 -61.357 1.00 92.97  ? 634  PRO   A N     1 
ATOM   2699 C  CA    . PRO   A 1 485  ? 23.916  -31.638 -60.406 1.00 94.13  ? 634  PRO   A CA    1 
ATOM   2700 C  C     . PRO   A 1 485  ? 24.707  -30.976 -59.266 1.00 94.82  ? 634  PRO   A C     1 
ATOM   2701 O  O     . PRO   A 1 485  ? 25.883  -30.709 -59.438 1.00 95.37  ? 634  PRO   A O     1 
ATOM   2702 C  CB    . PRO   A 1 485  ? 24.795  -32.538 -61.288 1.00 94.71  ? 634  PRO   A CB    1 
ATOM   2703 C  CG    . PRO   A 1 485  ? 25.314  -31.607 -62.364 1.00 94.20  ? 634  PRO   A CG    1 
ATOM   2704 C  CD    . PRO   A 1 485  ? 24.194  -30.615 -62.603 1.00 93.25  ? 634  PRO   A CD    1 
ATOM   2705 N  N     . PHE   A 1 486  ? 24.036  -30.730 -58.136 1.00 94.90  ? 635  PHE   A N     1 
ATOM   2706 C  CA    . PHE   A 1 486  ? 24.589  -30.050 -56.933 1.00 95.07  ? 635  PHE   A CA    1 
ATOM   2707 C  C     . PHE   A 1 486  ? 25.692  -30.917 -56.310 1.00 95.73  ? 635  PHE   A C     1 
ATOM   2708 O  O     . PHE   A 1 486  ? 26.720  -30.362 -55.872 1.00 94.64  ? 635  PHE   A O     1 
ATOM   2709 C  CB    . PHE   A 1 486  ? 23.484  -29.771 -55.911 1.00 95.40  ? 635  PHE   A CB    1 
ATOM   2710 C  CG    . PHE   A 1 486  ? 22.350  -28.917 -56.419 1.00 97.87  ? 635  PHE   A CG    1 
ATOM   2711 C  CD1   . PHE   A 1 486  ? 22.410  -27.534 -56.341 1.00 98.01  ? 635  PHE   A CD1   1 
ATOM   2712 C  CD2   . PHE   A 1 486  ? 21.215  -29.497 -56.969 1.00 100.22 ? 635  PHE   A CD2   1 
ATOM   2713 C  CE1   . PHE   A 1 486  ? 21.365  -26.751 -56.806 1.00 98.74  ? 635  PHE   A CE1   1 
ATOM   2714 C  CE2   . PHE   A 1 486  ? 20.170  -28.713 -57.435 1.00 100.18 ? 635  PHE   A CE2   1 
ATOM   2715 C  CZ    . PHE   A 1 486  ? 20.247  -27.341 -57.352 1.00 99.77  ? 635  PHE   A CZ    1 
ATOM   2716 N  N     . GLU   A 1 487  ? 25.476  -32.237 -56.282 1.00 95.90  ? 636  GLU   A N     1 
ATOM   2717 C  CA    . GLU   A 1 487  ? 26.396  -33.241 -55.679 1.00 93.86  ? 636  GLU   A CA    1 
ATOM   2718 C  C     . GLU   A 1 487  ? 27.698  -33.295 -56.490 1.00 90.81  ? 636  GLU   A C     1 
ATOM   2719 O  O     . GLU   A 1 487  ? 28.753  -33.575 -55.887 1.00 91.40  ? 636  GLU   A O     1 
ATOM   2720 C  CB    . GLU   A 1 487  ? 25.729  -34.618 -55.608 1.00 95.61  ? 636  GLU   A CB    1 
ATOM   2721 C  CG    . GLU   A 1 487  ? 24.637  -34.722 -54.553 1.00 96.61  ? 636  GLU   A CG    1 
ATOM   2722 C  CD    . GLU   A 1 487  ? 23.274  -34.164 -54.936 1.00 97.61  ? 636  GLU   A CD    1 
ATOM   2723 O  OE1   . GLU   A 1 487  ? 22.337  -34.292 -54.124 1.00 99.16  ? 636  GLU   A OE1   1 
ATOM   2724 O  OE2   . GLU   A 1 487  ? 23.149  -33.603 -56.043 1.00 98.90  ? 636  GLU   A OE2   1 
ATOM   2725 N  N     . LEU   A 1 488  ? 27.627  -33.037 -57.801 1.00 87.73  ? 637  LEU   A N     1 
ATOM   2726 C  CA    . LEU   A 1 488  ? 28.811  -32.975 -58.701 1.00 86.56  ? 637  LEU   A CA    1 
ATOM   2727 C  C     . LEU   A 1 488  ? 29.622  -31.710 -58.391 1.00 85.32  ? 637  LEU   A C     1 
ATOM   2728 O  O     . LEU   A 1 488  ? 30.863  -31.799 -58.404 1.00 84.31  ? 637  LEU   A O     1 
ATOM   2729 C  CB    . LEU   A 1 488  ? 28.351  -32.993 -60.163 1.00 86.63  ? 637  LEU   A CB    1 
ATOM   2730 C  CG    . LEU   A 1 488  ? 29.460  -32.880 -61.210 1.00 88.29  ? 637  LEU   A CG    1 
ATOM   2731 C  CD1   . LEU   A 1 488  ? 30.538  -33.932 -60.994 1.00 88.83  ? 637  LEU   A CD1   1 
ATOM   2732 C  CD2   . LEU   A 1 488  ? 28.887  -32.986 -62.615 1.00 89.28  ? 637  LEU   A CD2   1 
ATOM   2733 N  N     . ILE   A 1 489  ? 28.948  -30.585 -58.127 1.00 85.00  ? 638  ILE   A N     1 
ATOM   2734 C  CA    . ILE   A 1 489  ? 29.595  -29.280 -57.786 1.00 86.75  ? 638  ILE   A CA    1 
ATOM   2735 C  C     . ILE   A 1 489  ? 30.338  -29.446 -56.454 1.00 86.10  ? 638  ILE   A C     1 
ATOM   2736 O  O     . ILE   A 1 489  ? 31.464  -28.926 -56.344 1.00 84.44  ? 638  ILE   A O     1 
ATOM   2737 C  CB    . ILE   A 1 489  ? 28.569  -28.125 -57.744 1.00 88.22  ? 638  ILE   A CB    1 
ATOM   2738 C  CG1   . ILE   A 1 489  ? 27.879  -27.922 -59.095 1.00 89.70  ? 638  ILE   A CG1   1 
ATOM   2739 C  CG2   . ILE   A 1 489  ? 29.222  -26.834 -57.265 1.00 87.85  ? 638  ILE   A CG2   1 
ATOM   2740 C  CD1   . ILE   A 1 489  ? 26.635  -27.066 -59.029 1.00 90.56  ? 638  ILE   A CD1   1 
ATOM   2741 N  N     . GLU   A 1 490  ? 29.728  -30.150 -55.493 1.00 86.46  ? 639  GLU   A N     1 
ATOM   2742 C  CA    . GLU   A 1 490  ? 30.339  -30.512 -54.184 1.00 86.32  ? 639  GLU   A CA    1 
ATOM   2743 C  C     . GLU   A 1 490  ? 31.595  -31.361 -54.424 1.00 85.15  ? 639  GLU   A C     1 
ATOM   2744 O  O     . GLU   A 1 490  ? 32.608  -31.115 -53.740 1.00 85.02  ? 639  GLU   A O     1 
ATOM   2745 C  CB    . GLU   A 1 490  ? 29.326  -31.258 -53.313 1.00 87.94  ? 639  GLU   A CB    1 
ATOM   2746 C  CG    . GLU   A 1 490  ? 29.841  -31.595 -51.923 1.00 89.49  ? 639  GLU   A CG    1 
ATOM   2747 C  CD    . GLU   A 1 490  ? 28.828  -32.274 -51.016 1.00 91.01  ? 639  GLU   A CD    1 
ATOM   2748 O  OE1   . GLU   A 1 490  ? 27.616  -32.118 -51.261 1.00 89.84  ? 639  GLU   A OE1   1 
ATOM   2749 O  OE2   . GLU   A 1 490  ? 29.255  -32.961 -50.066 1.00 92.06  ? 639  GLU   A OE2   1 
ATOM   2750 N  N     . ALA   A 1 491  ? 31.525  -32.316 -55.358 1.00 82.87  ? 640  ALA   A N     1 
ATOM   2751 C  CA    . ALA   A 1 491  ? 32.638  -33.214 -55.753 1.00 81.57  ? 640  ALA   A CA    1 
ATOM   2752 C  C     . ALA   A 1 491  ? 33.728  -32.423 -56.492 1.00 80.33  ? 640  ALA   A C     1 
ATOM   2753 O  O     . ALA   A 1 491  ? 34.911  -32.792 -56.362 1.00 80.42  ? 640  ALA   A O     1 
ATOM   2754 C  CB    . ALA   A 1 491  ? 32.112  -34.347 -56.600 1.00 81.47  ? 640  ALA   A CB    1 
ATOM   2755 N  N     . LEU   A 1 492  ? 33.345  -31.388 -57.248 1.00 79.67  ? 641  LEU   A N     1 
ATOM   2756 C  CA    . LEU   A 1 492  ? 34.281  -30.525 -58.022 1.00 78.55  ? 641  LEU   A CA    1 
ATOM   2757 C  C     . LEU   A 1 492  ? 35.069  -29.622 -57.067 1.00 76.71  ? 641  LEU   A C     1 
ATOM   2758 O  O     . LEU   A 1 492  ? 36.254  -29.370 -57.348 1.00 75.56  ? 641  LEU   A O     1 
ATOM   2759 C  CB    . LEU   A 1 492  ? 33.494  -29.695 -59.043 1.00 79.11  ? 641  LEU   A CB    1 
ATOM   2760 C  CG    . LEU   A 1 492  ? 33.110  -30.425 -60.329 1.00 79.66  ? 641  LEU   A CG    1 
ATOM   2761 C  CD1   . LEU   A 1 492  ? 32.118  -29.604 -61.140 1.00 79.43  ? 641  LEU   A CD1   1 
ATOM   2762 C  CD2   . LEU   A 1 492  ? 34.343  -30.750 -61.159 1.00 79.65  ? 641  LEU   A CD2   1 
ATOM   2763 N  N     . LEU   A 1 493  ? 34.431  -29.147 -55.992 1.00 76.24  ? 642  LEU   A N     1 
ATOM   2764 C  CA    . LEU   A 1 493  ? 35.068  -28.297 -54.949 1.00 77.89  ? 642  LEU   A CA    1 
ATOM   2765 C  C     . LEU   A 1 493  ? 36.146  -29.106 -54.217 1.00 80.11  ? 642  LEU   A C     1 
ATOM   2766 O  O     . LEU   A 1 493  ? 37.226  -28.542 -53.953 1.00 81.08  ? 642  LEU   A O     1 
ATOM   2767 C  CB    . LEU   A 1 493  ? 33.998  -27.786 -53.978 1.00 77.19  ? 642  LEU   A CB    1 
ATOM   2768 C  CG    . LEU   A 1 493  ? 33.081  -26.691 -54.522 1.00 76.70  ? 642  LEU   A CG    1 
ATOM   2769 C  CD1   . LEU   A 1 493  ? 31.949  -26.396 -53.548 1.00 76.30  ? 642  LEU   A CD1   1 
ATOM   2770 C  CD2   . LEU   A 1 493  ? 33.865  -25.423 -54.830 1.00 76.79  ? 642  LEU   A CD2   1 
ATOM   2771 N  N     . LYS   A 1 494  ? 35.862  -30.377 -53.912 1.00 82.00  ? 643  LYS   A N     1 
ATOM   2772 C  CA    . LYS   A 1 494  ? 36.786  -31.303 -53.201 1.00 82.05  ? 643  LYS   A CA    1 
ATOM   2773 C  C     . LYS   A 1 494  ? 37.950  -31.697 -54.121 1.00 83.32  ? 643  LYS   A C     1 
ATOM   2774 O  O     . LYS   A 1 494  ? 39.034  -31.995 -53.581 1.00 88.29  ? 643  LYS   A O     1 
ATOM   2775 C  CB    . LYS   A 1 494  ? 36.026  -32.533 -52.693 1.00 83.04  ? 643  LYS   A CB    1 
ATOM   2776 C  CG    . LYS   A 1 494  ? 35.098  -32.266 -51.515 1.00 85.41  ? 643  LYS   A CG    1 
ATOM   2777 C  CD    . LYS   A 1 494  ? 34.164  -33.412 -51.193 1.00 87.85  ? 643  LYS   A CD    1 
ATOM   2778 C  CE    . LYS   A 1 494  ? 33.140  -33.050 -50.137 1.00 90.92  ? 643  LYS   A CE    1 
ATOM   2779 N  NZ    . LYS   A 1 494  ? 32.081  -34.080 -50.017 1.00 92.47  ? 643  LYS   A NZ    1 
ATOM   2780 N  N     . TYR   A 1 495  ? 37.746  -31.705 -55.444 1.00 82.18  ? 644  TYR   A N     1 
ATOM   2781 C  CA    . TYR   A 1 495  ? 38.810  -31.966 -56.453 1.00 82.23  ? 644  TYR   A CA    1 
ATOM   2782 C  C     . TYR   A 1 495  ? 39.720  -30.738 -56.576 1.00 83.86  ? 644  TYR   A C     1 
ATOM   2783 O  O     . TYR   A 1 495  ? 40.935  -30.914 -56.778 1.00 85.08  ? 644  TYR   A O     1 
ATOM   2784 C  CB    . TYR   A 1 495  ? 38.230  -32.326 -57.824 1.00 82.07  ? 644  TYR   A CB    1 
ATOM   2785 C  CG    . TYR   A 1 495  ? 39.277  -32.469 -58.903 1.00 82.25  ? 644  TYR   A CG    1 
ATOM   2786 C  CD1   . TYR   A 1 495  ? 39.953  -33.665 -59.089 1.00 82.25  ? 644  TYR   A CD1   1 
ATOM   2787 C  CD2   . TYR   A 1 495  ? 39.624  -31.399 -59.714 1.00 82.52  ? 644  TYR   A CD2   1 
ATOM   2788 C  CE1   . TYR   A 1 495  ? 40.929  -33.800 -60.064 1.00 82.20  ? 644  TYR   A CE1   1 
ATOM   2789 C  CE2   . TYR   A 1 495  ? 40.600  -31.516 -60.691 1.00 81.71  ? 644  TYR   A CE2   1 
ATOM   2790 C  CZ    . TYR   A 1 495  ? 41.256  -32.722 -60.868 1.00 81.92  ? 644  TYR   A CZ    1 
ATOM   2791 O  OH    . TYR   A 1 495  ? 42.215  -32.851 -61.830 1.00 82.15  ? 644  TYR   A OH    1 
ATOM   2792 N  N     . ILE   A 1 496  ? 39.144  -29.535 -56.483 1.00 87.13  ? 645  ILE   A N     1 
ATOM   2793 C  CA    . ILE   A 1 496  ? 39.874  -28.236 -56.598 1.00 90.98  ? 645  ILE   A CA    1 
ATOM   2794 C  C     . ILE   A 1 496  ? 40.927  -28.152 -55.483 1.00 93.19  ? 645  ILE   A C     1 
ATOM   2795 O  O     . ILE   A 1 496  ? 42.004  -27.572 -55.733 1.00 92.77  ? 645  ILE   A O     1 
ATOM   2796 C  CB    . ILE   A 1 496  ? 38.881  -27.052 -56.589 1.00 91.70  ? 645  ILE   A CB    1 
ATOM   2797 C  CG1   . ILE   A 1 496  ? 38.157  -26.935 -57.935 1.00 91.93  ? 645  ILE   A CG1   1 
ATOM   2798 C  CG2   . ILE   A 1 496  ? 39.568  -25.747 -56.210 1.00 91.63  ? 645  ILE   A CG2   1 
ATOM   2799 C  CD1   . ILE   A 1 496  ? 36.829  -26.214 -57.869 1.00 92.41  ? 645  ILE   A CD1   1 
ATOM   2800 N  N     . GLU   A 1 497  ? 40.636  -28.734 -54.314 1.00 94.83  ? 646  GLU   A N     1 
ATOM   2801 C  CA    . GLU   A 1 497  ? 41.554  -28.788 -53.143 1.00 96.27  ? 646  GLU   A CA    1 
ATOM   2802 C  C     . GLU   A 1 497  ? 42.825  -29.567 -53.510 1.00 98.82  ? 646  GLU   A C     1 
ATOM   2803 O  O     . GLU   A 1 497  ? 43.925  -29.039 -53.262 1.00 102.96 ? 646  GLU   A O     1 
ATOM   2804 C  CB    . GLU   A 1 497  ? 40.860  -29.433 -51.942 1.00 95.62  ? 646  GLU   A CB    1 
ATOM   2805 C  CG    . GLU   A 1 497  ? 39.720  -28.603 -51.380 1.00 95.34  ? 646  GLU   A CG    1 
ATOM   2806 C  CD    . GLU   A 1 497  ? 39.083  -29.167 -50.122 1.00 96.99  ? 646  GLU   A CD    1 
ATOM   2807 O  OE1   . GLU   A 1 497  ? 38.636  -28.364 -49.281 1.00 99.68  ? 646  GLU   A OE1   1 
ATOM   2808 O  OE2   . GLU   A 1 497  ? 39.031  -30.406 -49.986 1.00 97.50  ? 646  GLU   A OE2   1 
ATOM   2809 N  N     . THR   A 1 498  ? 42.672  -30.761 -54.097 1.00 100.52 ? 647  THR   A N     1 
ATOM   2810 C  CA    . THR   A 1 498  ? 43.763  -31.746 -54.350 1.00 101.71 ? 647  THR   A CA    1 
ATOM   2811 C  C     . THR   A 1 498  ? 44.811  -31.169 -55.314 1.00 102.99 ? 647  THR   A C     1 
ATOM   2812 O  O     . THR   A 1 498  ? 45.960  -31.652 -55.279 1.00 105.51 ? 647  THR   A O     1 
ATOM   2813 C  CB    . THR   A 1 498  ? 43.214  -33.077 -54.885 1.00 101.24 ? 647  THR   A CB    1 
ATOM   2814 O  OG1   . THR   A 1 498  ? 42.536  -32.832 -56.117 1.00 100.06 ? 647  THR   A OG1   1 
ATOM   2815 C  CG2   . THR   A 1 498  ? 42.277  -33.766 -53.917 1.00 100.92 ? 647  THR   A CG2   1 
ATOM   2816 N  N     . LEU   A 1 499  ? 44.433  -30.186 -56.140 1.00 103.36 ? 648  LEU   A N     1 
ATOM   2817 C  CA    . LEU   A 1 499  ? 45.331  -29.514 -57.121 1.00 104.51 ? 648  LEU   A CA    1 
ATOM   2818 C  C     . LEU   A 1 499  ? 46.397  -28.687 -56.390 1.00 103.56 ? 648  LEU   A C     1 
ATOM   2819 O  O     . LEU   A 1 499  ? 47.448  -28.425 -57.006 1.00 102.39 ? 648  LEU   A O     1 
ATOM   2820 C  CB    . LEU   A 1 499  ? 44.491  -28.630 -58.050 1.00 107.54 ? 648  LEU   A CB    1 
ATOM   2821 C  CG    . LEU   A 1 499  ? 43.572  -29.377 -59.016 1.00 108.63 ? 648  LEU   A CG    1 
ATOM   2822 C  CD1   . LEU   A 1 499  ? 42.511  -28.451 -59.589 1.00 108.94 ? 648  LEU   A CD1   1 
ATOM   2823 C  CD2   . LEU   A 1 499  ? 44.373  -30.025 -60.137 1.00 108.58 ? 648  LEU   A CD2   1 
ATOM   2824 N  N     . ASN   A 1 500  ? 46.129  -28.285 -55.140 1.00 104.52 ? 649  ASN   A N     1 
ATOM   2825 C  CA    . ASN   A 1 500  ? 47.059  -27.519 -54.264 1.00 105.25 ? 649  ASN   A CA    1 
ATOM   2826 C  C     . ASN   A 1 500  ? 47.523  -26.259 -55.005 1.00 103.55 ? 649  ASN   A C     1 
ATOM   2827 O  O     . ASN   A 1 500  ? 48.742  -26.108 -55.224 1.00 102.32 ? 649  ASN   A O     1 
ATOM   2828 C  CB    . ASN   A 1 500  ? 48.239  -28.376 -53.789 1.00 107.14 ? 649  ASN   A CB    1 
ATOM   2829 C  CG    . ASN   A 1 500  ? 47.897  -29.265 -52.612 1.00 109.05 ? 649  ASN   A CG    1 
ATOM   2830 O  OD1   . ASN   A 1 500  ? 46.744  -29.649 -52.426 1.00 110.38 ? 649  ASN   A OD1   1 
ATOM   2831 N  ND2   . ASN   A 1 500  ? 48.894  -29.599 -51.809 1.00 110.06 ? 649  ASN   A ND2   1 
ATOM   2832 N  N     . VAL   A 1 501  ? 46.569  -25.409 -55.393 1.00 102.54 ? 650  VAL   A N     1 
ATOM   2833 C  CA    . VAL   A 1 501  ? 46.810  -24.065 -55.999 1.00 102.02 ? 650  VAL   A CA    1 
ATOM   2834 C  C     . VAL   A 1 501  ? 45.776  -23.102 -55.421 1.00 100.64 ? 650  VAL   A C     1 
ATOM   2835 O  O     . VAL   A 1 501  ? 44.620  -23.118 -55.839 1.00 98.58  ? 650  VAL   A O     1 
ATOM   2836 C  CB    . VAL   A 1 501  ? 46.751  -24.117 -57.538 1.00 102.05 ? 650  VAL   A CB    1 
ATOM   2837 C  CG1   . VAL   A 1 501  ? 46.820  -22.729 -58.158 1.00 101.57 ? 650  VAL   A CG1   1 
ATOM   2838 C  CG2   . VAL   A 1 501  ? 47.839  -25.013 -58.112 1.00 102.09 ? 650  VAL   A CG2   1 
ATOM   2839 N  N     . PRO   A 1 502  ? 46.146  -22.263 -54.424 1.00 100.25 ? 651  PRO   A N     1 
ATOM   2840 C  CA    . PRO   A 1 502  ? 45.210  -21.311 -53.825 1.00 98.68  ? 651  PRO   A CA    1 
ATOM   2841 C  C     . PRO   A 1 502  ? 44.551  -20.389 -54.864 1.00 95.79  ? 651  PRO   A C     1 
ATOM   2842 O  O     . PRO   A 1 502  ? 45.248  -19.857 -55.714 1.00 92.94  ? 651  PRO   A O     1 
ATOM   2843 C  CB    . PRO   A 1 502  ? 46.080  -20.501 -52.852 1.00 100.00 ? 651  PRO   A CB    1 
ATOM   2844 C  CG    . PRO   A 1 502  ? 47.221  -21.435 -52.514 1.00 101.31 ? 651  PRO   A CG    1 
ATOM   2845 C  CD    . PRO   A 1 502  ? 47.474  -22.211 -53.790 1.00 101.37 ? 651  PRO   A CD    1 
ATOM   2846 N  N     . GLY   A 1 503  ? 43.227  -20.236 -54.764 1.00 92.38  ? 652  GLY   A N     1 
ATOM   2847 C  CA    . GLY   A 1 503  ? 42.394  -19.448 -55.693 1.00 88.86  ? 652  GLY   A CA    1 
ATOM   2848 C  C     . GLY   A 1 503  ? 40.917  -19.580 -55.365 1.00 85.40  ? 652  GLY   A C     1 
ATOM   2849 O  O     . GLY   A 1 503  ? 40.534  -20.606 -54.766 1.00 85.03  ? 652  GLY   A O     1 
ATOM   2850 N  N     . ALA   A 1 504  ? 40.120  -18.577 -55.745 1.00 82.06  ? 653  ALA   A N     1 
ATOM   2851 C  CA    . ALA   A 1 504  ? 38.658  -18.505 -55.514 1.00 78.39  ? 653  ALA   A CA    1 
ATOM   2852 C  C     . ALA   A 1 504  ? 37.921  -19.285 -56.610 1.00 75.38  ? 653  ALA   A C     1 
ATOM   2853 O  O     . ALA   A 1 504  ? 38.450  -19.377 -57.738 1.00 72.95  ? 653  ALA   A O     1 
ATOM   2854 C  CB    . ALA   A 1 504  ? 38.213  -17.063 -55.471 1.00 77.82  ? 653  ALA   A CB    1 
ATOM   2855 N  N     . VAL   A 1 505  ? 36.744  -19.821 -56.276 1.00 74.22  ? 654  VAL   A N     1 
ATOM   2856 C  CA    . VAL   A 1 505  ? 35.862  -20.596 -57.199 1.00 75.21  ? 654  VAL   A CA    1 
ATOM   2857 C  C     . VAL   A 1 505  ? 34.602  -19.767 -57.468 1.00 74.58  ? 654  VAL   A C     1 
ATOM   2858 O  O     . VAL   A 1 505  ? 33.911  -19.414 -56.493 1.00 74.33  ? 654  VAL   A O     1 
ATOM   2859 C  CB    . VAL   A 1 505  ? 35.505  -21.979 -56.617 1.00 76.28  ? 654  VAL   A CB    1 
ATOM   2860 C  CG1   . VAL   A 1 505  ? 34.814  -22.860 -57.649 1.00 75.39  ? 654  VAL   A CG1   1 
ATOM   2861 C  CG2   . VAL   A 1 505  ? 36.725  -22.684 -56.041 1.00 76.35  ? 654  VAL   A CG2   1 
ATOM   2862 N  N     . LEU   A 1 506  ? 34.326  -19.469 -58.742 1.00 74.57  ? 655  LEU   A N     1 
ATOM   2863 C  CA    . LEU   A 1 506  ? 33.096  -18.766 -59.198 1.00 74.09  ? 655  LEU   A CA    1 
ATOM   2864 C  C     . LEU   A 1 506  ? 32.120  -19.802 -59.767 1.00 73.88  ? 655  LEU   A C     1 
ATOM   2865 O  O     . LEU   A 1 506  ? 32.380  -20.313 -60.874 1.00 75.65  ? 655  LEU   A O     1 
ATOM   2866 C  CB    . LEU   A 1 506  ? 33.479  -17.714 -60.246 1.00 72.92  ? 655  LEU   A CB    1 
ATOM   2867 C  CG    . LEU   A 1 506  ? 32.330  -16.875 -60.805 1.00 71.11  ? 655  LEU   A CG    1 
ATOM   2868 C  CD1   . LEU   A 1 506  ? 31.575  -16.165 -59.691 1.00 69.37  ? 655  LEU   A CD1   1 
ATOM   2869 C  CD2   . LEU   A 1 506  ? 32.847  -15.871 -61.824 1.00 70.78  ? 655  LEU   A CD2   1 
ATOM   2870 N  N     . VAL   A 1 507  ? 31.052  -20.111 -59.027 1.00 72.39  ? 656  VAL   A N     1 
ATOM   2871 C  CA    . VAL   A 1 507  ? 29.986  -21.068 -59.448 1.00 73.41  ? 656  VAL   A CA    1 
ATOM   2872 C  C     . VAL   A 1 507  ? 28.851  -20.263 -60.092 1.00 73.24  ? 656  VAL   A C     1 
ATOM   2873 O  O     . VAL   A 1 507  ? 28.195  -19.486 -59.366 1.00 72.88  ? 656  VAL   A O     1 
ATOM   2874 C  CB    . VAL   A 1 507  ? 29.476  -21.917 -58.266 1.00 75.94  ? 656  VAL   A CB    1 
ATOM   2875 C  CG1   . VAL   A 1 507  ? 28.529  -23.017 -58.728 1.00 76.63  ? 656  VAL   A CG1   1 
ATOM   2876 C  CG2   . VAL   A 1 507  ? 30.620  -22.507 -57.454 1.00 75.90  ? 656  VAL   A CG2   1 
ATOM   2877 N  N     . PHE   A 1 508  ? 28.644  -20.435 -61.403 1.00 72.11  ? 657  PHE   A N     1 
ATOM   2878 C  CA    . PHE   A 1 508  ? 27.550  -19.801 -62.188 1.00 70.40  ? 657  PHE   A CA    1 
ATOM   2879 C  C     . PHE   A 1 508  ? 26.286  -20.662 -62.091 1.00 71.15  ? 657  PHE   A C     1 
ATOM   2880 O  O     . PHE   A 1 508  ? 26.337  -21.852 -62.454 1.00 71.27  ? 657  PHE   A O     1 
ATOM   2881 C  CB    . PHE   A 1 508  ? 27.956  -19.612 -63.650 1.00 68.81  ? 657  PHE   A CB    1 
ATOM   2882 C  CG    . PHE   A 1 508  ? 28.849  -18.426 -63.904 1.00 67.95  ? 657  PHE   A CG    1 
ATOM   2883 C  CD1   . PHE   A 1 508  ? 28.337  -17.137 -63.891 1.00 66.94  ? 657  PHE   A CD1   1 
ATOM   2884 C  CD2   . PHE   A 1 508  ? 30.200  -18.598 -64.163 1.00 67.68  ? 657  PHE   A CD2   1 
ATOM   2885 C  CE1   . PHE   A 1 508  ? 29.158  -16.046 -64.126 1.00 66.35  ? 657  PHE   A CE1   1 
ATOM   2886 C  CE2   . PHE   A 1 508  ? 31.018  -17.505 -64.402 1.00 67.96  ? 657  PHE   A CE2   1 
ATOM   2887 C  CZ    . PHE   A 1 508  ? 30.496  -16.233 -64.383 1.00 67.15  ? 657  PHE   A CZ    1 
ATOM   2888 N  N     . LEU   A 1 509  ? 25.192  -20.066 -61.611 1.00 73.22  ? 658  LEU   A N     1 
ATOM   2889 C  CA    . LEU   A 1 509  ? 23.858  -20.711 -61.478 1.00 74.83  ? 658  LEU   A CA    1 
ATOM   2890 C  C     . LEU   A 1 509  ? 22.799  -19.763 -62.037 1.00 77.72  ? 658  LEU   A C     1 
ATOM   2891 O  O     . LEU   A 1 509  ? 23.062  -18.575 -62.211 1.00 79.27  ? 658  LEU   A O     1 
ATOM   2892 C  CB    . LEU   A 1 509  ? 23.609  -21.037 -60.001 1.00 73.54  ? 658  LEU   A CB    1 
ATOM   2893 C  CG    . LEU   A 1 509  ? 24.553  -22.068 -59.382 1.00 72.52  ? 658  LEU   A CG    1 
ATOM   2894 C  CD1   . LEU   A 1 509  ? 24.475  -22.032 -57.864 1.00 72.11  ? 658  LEU   A CD1   1 
ATOM   2895 C  CD2   . LEU   A 1 509  ? 24.249  -23.468 -59.895 1.00 72.08  ? 658  LEU   A CD2   1 
ATOM   2896 N  N     . PRO   A 1 510  ? 21.580  -20.254 -62.360 1.00 80.03  ? 659  PRO   A N     1 
ATOM   2897 C  CA    . PRO   A 1 510  ? 20.528  -19.401 -62.913 1.00 80.34  ? 659  PRO   A CA    1 
ATOM   2898 C  C     . PRO   A 1 510  ? 20.130  -18.237 -61.992 1.00 82.49  ? 659  PRO   A C     1 
ATOM   2899 O  O     . PRO   A 1 510  ? 20.373  -17.106 -62.372 1.00 86.38  ? 659  PRO   A O     1 
ATOM   2900 C  CB    . PRO   A 1 510  ? 19.340  -20.355 -63.118 1.00 80.43  ? 659  PRO   A CB    1 
ATOM   2901 C  CG    . PRO   A 1 510  ? 19.970  -21.729 -63.185 1.00 80.57  ? 659  PRO   A CG    1 
ATOM   2902 C  CD    . PRO   A 1 510  ? 21.160  -21.658 -62.252 1.00 80.52  ? 659  PRO   A CD    1 
ATOM   2903 N  N     . GLY   A 1 511  ? 19.555  -18.533 -60.820 1.00 84.61  ? 660  GLY   A N     1 
ATOM   2904 C  CA    . GLY   A 1 511  ? 18.883  -17.534 -59.963 1.00 87.84  ? 660  GLY   A CA    1 
ATOM   2905 C  C     . GLY   A 1 511  ? 19.095  -17.771 -58.477 1.00 91.36  ? 660  GLY   A C     1 
ATOM   2906 O  O     . GLY   A 1 511  ? 19.870  -18.679 -58.117 1.00 90.60  ? 660  GLY   A O     1 
ATOM   2907 N  N     . TRP   A 1 512  ? 18.406  -16.976 -57.650 1.00 98.07  ? 661  TRP   A N     1 
ATOM   2908 C  CA    . TRP   A 1 512  ? 18.522  -16.940 -56.165 1.00 102.80 ? 661  TRP   A CA    1 
ATOM   2909 C  C     . TRP   A 1 512  ? 18.094  -18.276 -55.543 1.00 102.03 ? 661  TRP   A C     1 
ATOM   2910 O  O     . TRP   A 1 512  ? 18.485  -18.524 -54.389 1.00 103.19 ? 661  TRP   A O     1 
ATOM   2911 C  CB    . TRP   A 1 512  ? 17.729  -15.756 -55.583 1.00 107.90 ? 661  TRP   A CB    1 
ATOM   2912 C  CG    . TRP   A 1 512  ? 16.235  -15.873 -55.649 1.00 113.58 ? 661  TRP   A CG    1 
ATOM   2913 C  CD1   . TRP   A 1 512  ? 15.456  -15.897 -56.770 1.00 116.85 ? 661  TRP   A CD1   1 
ATOM   2914 C  CD2   . TRP   A 1 512  ? 15.325  -15.931 -54.533 1.00 119.83 ? 661  TRP   A CD2   1 
ATOM   2915 N  NE1   . TRP   A 1 512  ? 14.132  -15.989 -56.432 1.00 118.84 ? 661  TRP   A NE1   1 
ATOM   2916 C  CE2   . TRP   A 1 512  ? 14.020  -16.009 -55.068 1.00 120.08 ? 661  TRP   A CE2   1 
ATOM   2917 C  CE3   . TRP   A 1 512  ? 15.483  -15.934 -53.141 1.00 120.31 ? 661  TRP   A CE3   1 
ATOM   2918 C  CZ2   . TRP   A 1 512  ? 12.887  -16.093 -54.258 1.00 118.97 ? 661  TRP   A CZ2   1 
ATOM   2919 C  CZ3   . TRP   A 1 512  ? 14.362  -16.015 -52.342 1.00 118.94 ? 661  TRP   A CZ3   1 
ATOM   2920 C  CH2   . TRP   A 1 512  ? 13.083  -16.094 -52.895 1.00 118.66 ? 661  TRP   A CH2   1 
ATOM   2921 N  N     . ASN   A 1 513  ? 17.330  -19.097 -56.271 1.00 102.10 ? 662  ASN   A N     1 
ATOM   2922 C  CA    . ASN   A 1 513  ? 16.827  -20.416 -55.797 1.00 102.46 ? 662  ASN   A CA    1 
ATOM   2923 C  C     . ASN   A 1 513  ? 17.963  -21.445 -55.801 1.00 100.53 ? 662  ASN   A C     1 
ATOM   2924 O  O     . ASN   A 1 513  ? 18.228  -22.025 -54.731 1.00 103.53 ? 662  ASN   A O     1 
ATOM   2925 C  CB    . ASN   A 1 513  ? 15.639  -20.908 -56.629 1.00 104.02 ? 662  ASN   A CB    1 
ATOM   2926 C  CG    . ASN   A 1 513  ? 14.309  -20.363 -56.151 1.00 105.21 ? 662  ASN   A CG    1 
ATOM   2927 O  OD1   . ASN   A 1 513  ? 13.272  -20.989 -56.358 1.00 106.78 ? 662  ASN   A OD1   1 
ATOM   2928 N  ND2   . ASN   A 1 513  ? 14.325  -19.206 -55.509 1.00 104.10 ? 662  ASN   A ND2   1 
ATOM   2929 N  N     . LEU   A 1 514  ? 18.599  -21.672 -56.954 1.00 97.33  ? 663  LEU   A N     1 
ATOM   2930 C  CA    . LEU   A 1 514  ? 19.663  -22.702 -57.114 1.00 96.76  ? 663  LEU   A CA    1 
ATOM   2931 C  C     . LEU   A 1 514  ? 20.930  -22.267 -56.366 1.00 95.75  ? 663  LEU   A C     1 
ATOM   2932 O  O     . LEU   A 1 514  ? 21.762  -23.144 -56.077 1.00 97.75  ? 663  LEU   A O     1 
ATOM   2933 C  CB    . LEU   A 1 514  ? 19.949  -22.942 -58.602 1.00 98.36  ? 663  LEU   A CB    1 
ATOM   2934 C  CG    . LEU   A 1 514  ? 18.810  -23.533 -59.440 1.00 98.95  ? 663  LEU   A CG    1 
ATOM   2935 C  CD1   . LEU   A 1 514  ? 19.363  -24.450 -60.522 1.00 99.05  ? 663  LEU   A CD1   1 
ATOM   2936 C  CD2   . LEU   A 1 514  ? 17.796  -24.291 -58.592 1.00 99.02  ? 663  LEU   A CD2   1 
ATOM   2937 N  N     . ILE   A 1 515  ? 21.071  -20.971 -56.065 1.00 94.72  ? 664  ILE   A N     1 
ATOM   2938 C  CA    . ILE   A 1 515  ? 22.145  -20.424 -55.181 1.00 93.69  ? 664  ILE   A CA    1 
ATOM   2939 C  C     . ILE   A 1 515  ? 21.800  -20.768 -53.725 1.00 97.03  ? 664  ILE   A C     1 
ATOM   2940 O  O     . ILE   A 1 515  ? 22.700  -21.241 -53.005 1.00 99.52  ? 664  ILE   A O     1 
ATOM   2941 C  CB    . ILE   A 1 515  ? 22.329  -18.908 -55.402 1.00 90.57  ? 664  ILE   A CB    1 
ATOM   2942 C  CG1   . ILE   A 1 515  ? 22.922  -18.618 -56.784 1.00 88.58  ? 664  ILE   A CG1   1 
ATOM   2943 C  CG2   . ILE   A 1 515  ? 23.167  -18.291 -54.290 1.00 90.46  ? 664  ILE   A CG2   1 
ATOM   2944 C  CD1   . ILE   A 1 515  ? 22.841  -17.169 -57.202 1.00 88.55  ? 664  ILE   A CD1   1 
ATOM   2945 N  N     . TYR   A 1 516  ? 20.546  -20.538 -53.317 1.00 99.45  ? 665  TYR   A N     1 
ATOM   2946 C  CA    . TYR   A 1 516  ? 20.004  -20.872 -51.971 1.00 101.55 ? 665  TYR   A CA    1 
ATOM   2947 C  C     . TYR   A 1 516  ? 20.116  -22.383 -51.738 1.00 100.10 ? 665  TYR   A C     1 
ATOM   2948 O  O     . TYR   A 1 516  ? 20.541  -22.785 -50.639 1.00 102.43 ? 665  TYR   A O     1 
ATOM   2949 C  CB    . TYR   A 1 516  ? 18.552  -20.399 -51.842 1.00 107.09 ? 665  TYR   A CB    1 
ATOM   2950 C  CG    . TYR   A 1 516  ? 17.945  -20.534 -50.468 1.00 113.16 ? 665  TYR   A CG    1 
ATOM   2951 C  CD1   . TYR   A 1 516  ? 17.346  -21.716 -50.058 1.00 115.40 ? 665  TYR   A CD1   1 
ATOM   2952 C  CD2   . TYR   A 1 516  ? 17.943  -19.467 -49.583 1.00 116.97 ? 665  TYR   A CD2   1 
ATOM   2953 C  CE1   . TYR   A 1 516  ? 16.777  -21.840 -48.800 1.00 117.64 ? 665  TYR   A CE1   1 
ATOM   2954 C  CE2   . TYR   A 1 516  ? 17.378  -19.574 -48.322 1.00 118.05 ? 665  TYR   A CE2   1 
ATOM   2955 C  CZ    . TYR   A 1 516  ? 16.793  -20.764 -47.928 1.00 118.79 ? 665  TYR   A CZ    1 
ATOM   2956 O  OH    . TYR   A 1 516  ? 16.238  -20.873 -46.686 1.00 117.15 ? 665  TYR   A OH    1 
ATOM   2957 N  N     . THR   A 1 517  ? 19.750  -23.181 -52.747 1.00 99.10  ? 666  THR   A N     1 
ATOM   2958 C  CA    . THR   A 1 517  ? 19.734  -24.671 -52.713 1.00 98.72  ? 666  THR   A CA    1 
ATOM   2959 C  C     . THR   A 1 517  ? 21.170  -25.199 -52.599 1.00 100.00 ? 666  THR   A C     1 
ATOM   2960 O  O     . THR   A 1 517  ? 21.400  -26.074 -51.743 1.00 106.71 ? 666  THR   A O     1 
ATOM   2961 C  CB    . THR   A 1 517  ? 19.007  -25.245 -53.937 1.00 96.47  ? 666  THR   A CB    1 
ATOM   2962 O  OG1   . THR   A 1 517  ? 17.644  -24.823 -53.870 1.00 94.49  ? 666  THR   A OG1   1 
ATOM   2963 C  CG2   . THR   A 1 517  ? 19.064  -26.755 -54.021 1.00 94.55  ? 666  THR   A CG2   1 
ATOM   2964 N  N     . MET   A 1 518  ? 22.087  -24.696 -53.433 1.00 98.54  ? 667  MET   A N     1 
ATOM   2965 C  CA    . MET   A 1 518  ? 23.521  -25.099 -53.450 1.00 97.99  ? 667  MET   A CA    1 
ATOM   2966 C  C     . MET   A 1 518  ? 24.167  -24.742 -52.105 1.00 99.79  ? 667  MET   A C     1 
ATOM   2967 O  O     . MET   A 1 518  ? 24.958  -25.560 -51.596 1.00 98.90  ? 667  MET   A O     1 
ATOM   2968 C  CB    . MET   A 1 518  ? 24.280  -24.399 -54.583 1.00 96.77  ? 667  MET   A CB    1 
ATOM   2969 C  CG    . MET   A 1 518  ? 25.737  -24.817 -54.700 1.00 96.11  ? 667  MET   A CG    1 
ATOM   2970 S  SD    . MET   A 1 518  ? 25.928  -26.537 -55.227 1.00 96.80  ? 667  MET   A SD    1 
ATOM   2971 C  CE    . MET   A 1 518  ? 27.505  -26.940 -54.478 1.00 97.50  ? 667  MET   A CE    1 
ATOM   2972 N  N     . GLN   A 1 519  ? 23.836  -23.567 -51.557 1.00 101.33 ? 668  GLN   A N     1 
ATOM   2973 C  CA    . GLN   A 1 519  ? 24.404  -23.036 -50.288 1.00 102.76 ? 668  GLN   A CA    1 
ATOM   2974 C  C     . GLN   A 1 519  ? 23.951  -23.923 -49.121 1.00 104.88 ? 668  GLN   A C     1 
ATOM   2975 O  O     . GLN   A 1 519  ? 24.830  -24.411 -48.381 1.00 108.10 ? 668  GLN   A O     1 
ATOM   2976 C  CB    . GLN   A 1 519  ? 23.988  -21.577 -50.095 1.00 102.62 ? 668  GLN   A CB    1 
ATOM   2977 C  CG    . GLN   A 1 519  ? 24.733  -20.872 -48.971 1.00 103.41 ? 668  GLN   A CG    1 
ATOM   2978 C  CD    . GLN   A 1 519  ? 24.564  -19.373 -49.019 1.00 103.47 ? 668  GLN   A CD    1 
ATOM   2979 O  OE1   . GLN   A 1 519  ? 23.749  -18.842 -49.772 1.00 100.64 ? 668  GLN   A OE1   1 
ATOM   2980 N  NE2   . GLN   A 1 519  ? 25.339  -18.674 -48.206 1.00 103.74 ? 668  GLN   A NE2   1 
ATOM   2981 N  N     . LYS   A 1 520  ? 22.634  -24.121 -48.974 1.00 105.05 ? 669  LYS   A N     1 
ATOM   2982 C  CA    . LYS   A 1 520  ? 22.010  -25.015 -47.956 1.00 104.05 ? 669  LYS   A CA    1 
ATOM   2983 C  C     . LYS   A 1 520  ? 22.662  -26.402 -48.016 1.00 102.41 ? 669  LYS   A C     1 
ATOM   2984 O  O     . LYS   A 1 520  ? 23.002  -26.940 -46.947 1.00 104.89 ? 669  LYS   A O     1 
ATOM   2985 C  CB    . LYS   A 1 520  ? 20.497  -25.135 -48.175 1.00 105.48 ? 669  LYS   A CB    1 
ATOM   2986 C  CG    . LYS   A 1 520  ? 19.632  -24.297 -47.242 1.00 107.47 ? 669  LYS   A CG    1 
ATOM   2987 C  CD    . LYS   A 1 520  ? 19.538  -24.864 -45.837 1.00 109.37 ? 669  LYS   A CD    1 
ATOM   2988 C  CE    . LYS   A 1 520  ? 18.402  -24.275 -45.027 1.00 109.38 ? 669  LYS   A CE    1 
ATOM   2989 N  NZ    . LYS   A 1 520  ? 18.592  -22.825 -44.785 1.00 110.87 ? 669  LYS   A NZ    1 
ATOM   2990 N  N     . HIS   A 1 521  ? 22.824  -26.948 -49.225 1.00 99.48  ? 670  HIS   A N     1 
ATOM   2991 C  CA    . HIS   A 1 521  ? 23.411  -28.289 -49.491 1.00 99.57  ? 670  HIS   A CA    1 
ATOM   2992 C  C     . HIS   A 1 521  ? 24.837  -28.367 -48.929 1.00 100.85 ? 670  HIS   A C     1 
ATOM   2993 O  O     . HIS   A 1 521  ? 25.180  -29.417 -48.354 1.00 103.21 ? 670  HIS   A O     1 
ATOM   2994 C  CB    . HIS   A 1 521  ? 23.368  -28.598 -50.995 1.00 99.00  ? 670  HIS   A CB    1 
ATOM   2995 C  CG    . HIS   A 1 521  ? 23.797  -29.984 -51.337 1.00 98.44  ? 670  HIS   A CG    1 
ATOM   2996 N  ND1   . HIS   A 1 521  ? 22.909  -31.041 -51.377 1.00 99.58  ? 670  HIS   A ND1   1 
ATOM   2997 C  CD2   . HIS   A 1 521  ? 25.008  -30.490 -51.653 1.00 97.74  ? 670  HIS   A CD2   1 
ATOM   2998 C  CE1   . HIS   A 1 521  ? 23.556  -32.141 -51.703 1.00 100.54 ? 670  HIS   A CE1   1 
ATOM   2999 N  NE2   . HIS   A 1 521  ? 24.846  -31.829 -51.878 1.00 99.64  ? 670  HIS   A NE2   1 
ATOM   3000 N  N     . LEU   A 1 522  ? 25.629  -27.300 -49.085 1.00 100.80 ? 671  LEU   A N     1 
ATOM   3001 C  CA    . LEU   A 1 522  ? 27.064  -27.259 -48.684 1.00 101.43 ? 671  LEU   A CA    1 
ATOM   3002 C  C     . LEU   A 1 522  ? 27.189  -27.181 -47.158 1.00 104.37 ? 671  LEU   A C     1 
ATOM   3003 O  O     . LEU   A 1 522  ? 28.013  -27.933 -46.604 1.00 106.81 ? 671  LEU   A O     1 
ATOM   3004 C  CB    . LEU   A 1 522  ? 27.754  -26.063 -49.349 1.00 99.10  ? 671  LEU   A CB    1 
ATOM   3005 C  CG    . LEU   A 1 522  ? 28.102  -26.236 -50.826 1.00 97.93  ? 671  LEU   A CG    1 
ATOM   3006 C  CD1   . LEU   A 1 522  ? 28.621  -24.932 -51.414 1.00 98.54  ? 671  LEU   A CD1   1 
ATOM   3007 C  CD2   . LEU   A 1 522  ? 29.117  -27.352 -51.025 1.00 96.24  ? 671  LEU   A CD2   1 
ATOM   3008 N  N     . GLU   A 1 523  ? 26.414  -26.304 -46.509 1.00 107.38 ? 672  GLU   A N     1 
ATOM   3009 C  CA    . GLU   A 1 523  ? 26.523  -26.018 -45.050 1.00 110.45 ? 672  GLU   A CA    1 
ATOM   3010 C  C     . GLU   A 1 523  ? 26.095  -27.247 -44.231 1.00 113.52 ? 672  GLU   A C     1 
ATOM   3011 O  O     . GLU   A 1 523  ? 26.525  -27.337 -43.064 1.00 114.74 ? 672  GLU   A O     1 
ATOM   3012 C  CB    . GLU   A 1 523  ? 25.727  -24.763 -44.674 1.00 109.85 ? 672  GLU   A CB    1 
ATOM   3013 C  CG    . GLU   A 1 523  ? 24.220  -24.915 -44.788 1.00 110.93 ? 672  GLU   A CG    1 
ATOM   3014 C  CD    . GLU   A 1 523  ? 23.427  -23.696 -44.349 1.00 112.18 ? 672  GLU   A CD    1 
ATOM   3015 O  OE1   . GLU   A 1 523  ? 23.871  -22.565 -44.637 1.00 110.39 ? 672  GLU   A OE1   1 
ATOM   3016 O  OE2   . GLU   A 1 523  ? 22.366  -23.879 -43.718 1.00 114.52 ? 672  GLU   A OE2   1 
ATOM   3017 N  N     . MET   A 1 524  ? 25.291  -28.152 -44.808 1.00 114.90 ? 673  MET   A N     1 
ATOM   3018 C  CA    . MET   A 1 524  ? 24.921  -29.460 -44.193 1.00 114.53 ? 673  MET   A CA    1 
ATOM   3019 C  C     . MET   A 1 524  ? 26.195  -30.264 -43.905 1.00 113.61 ? 673  MET   A C     1 
ATOM   3020 O  O     . MET   A 1 524  ? 26.325  -30.779 -42.776 1.00 114.60 ? 673  MET   A O     1 
ATOM   3021 C  CB    . MET   A 1 524  ? 24.010  -30.283 -45.111 1.00 114.43 ? 673  MET   A CB    1 
ATOM   3022 C  CG    . MET   A 1 524  ? 22.593  -29.749 -45.225 1.00 115.85 ? 673  MET   A CG    1 
ATOM   3023 S  SD    . MET   A 1 524  ? 21.721  -29.660 -43.638 1.00 118.96 ? 673  MET   A SD    1 
ATOM   3024 C  CE    . MET   A 1 524  ? 21.923  -27.924 -43.240 1.00 117.50 ? 673  MET   A CE    1 
ATOM   3025 N  N     . ASN   A 1 525  ? 27.089  -30.367 -44.894 1.00 110.34 ? 674  ASN   A N     1 
ATOM   3026 C  CA    . ASN   A 1 525  ? 28.417  -31.029 -44.774 1.00 109.72 ? 674  ASN   A CA    1 
ATOM   3027 C  C     . ASN   A 1 525  ? 29.331  -30.131 -43.939 1.00 111.75 ? 674  ASN   A C     1 
ATOM   3028 O  O     . ASN   A 1 525  ? 29.606  -28.999 -44.334 1.00 111.75 ? 674  ASN   A O     1 
ATOM   3029 C  CB    . ASN   A 1 525  ? 29.008  -31.335 -46.153 1.00 108.40 ? 674  ASN   A CB    1 
ATOM   3030 C  CG    . ASN   A 1 525  ? 30.178  -32.295 -46.111 1.00 108.24 ? 674  ASN   A CG    1 
ATOM   3031 O  OD1   . ASN   A 1 525  ? 31.027  -32.215 -45.225 1.00 109.22 ? 674  ASN   A OD1   1 
ATOM   3032 N  ND2   . ASN   A 1 525  ? 30.242  -33.203 -47.072 1.00 107.76 ? 674  ASN   A ND2   1 
ATOM   3033 N  N     . PRO   A 1 526  ? 29.824  -30.592 -42.762 1.00 111.50 ? 675  PRO   A N     1 
ATOM   3034 C  CA    . PRO   A 1 526  ? 30.673  -29.764 -41.899 1.00 109.33 ? 675  PRO   A CA    1 
ATOM   3035 C  C     . PRO   A 1 526  ? 32.021  -29.341 -42.510 1.00 107.83 ? 675  PRO   A C     1 
ATOM   3036 O  O     . PRO   A 1 526  ? 32.618  -28.414 -41.989 1.00 109.40 ? 675  PRO   A O     1 
ATOM   3037 C  CB    . PRO   A 1 526  ? 30.941  -30.649 -40.669 1.00 109.30 ? 675  PRO   A CB    1 
ATOM   3038 C  CG    . PRO   A 1 526  ? 29.852  -31.699 -40.705 1.00 109.76 ? 675  PRO   A CG    1 
ATOM   3039 C  CD    . PRO   A 1 526  ? 29.567  -31.917 -42.175 1.00 109.91 ? 675  PRO   A CD    1 
ATOM   3040 N  N     . HIS   A 1 527  ? 32.472  -30.025 -43.569 1.00 103.43 ? 676  HIS   A N     1 
ATOM   3041 C  CA    . HIS   A 1 527  ? 33.738  -29.734 -44.298 1.00 100.69 ? 676  HIS   A CA    1 
ATOM   3042 C  C     . HIS   A 1 527  ? 33.711  -28.305 -44.855 1.00 100.52 ? 676  HIS   A C     1 
ATOM   3043 O  O     . HIS   A 1 527  ? 34.754  -27.628 -44.772 1.00 101.73 ? 676  HIS   A O     1 
ATOM   3044 C  CB    . HIS   A 1 527  ? 33.979  -30.776 -45.400 1.00 98.88  ? 676  HIS   A CB    1 
ATOM   3045 C  CG    . HIS   A 1 527  ? 35.188  -30.504 -46.232 1.00 97.94  ? 676  HIS   A CG    1 
ATOM   3046 N  ND1   . HIS   A 1 527  ? 35.121  -30.353 -47.603 1.00 98.33  ? 676  HIS   A ND1   1 
ATOM   3047 C  CD2   . HIS   A 1 527  ? 36.486  -30.342 -45.896 1.00 96.90  ? 676  HIS   A CD2   1 
ATOM   3048 C  CE1   . HIS   A 1 527  ? 36.327  -30.119 -48.077 1.00 96.19  ? 676  HIS   A CE1   1 
ATOM   3049 N  NE2   . HIS   A 1 527  ? 37.183  -30.106 -47.050 1.00 96.17  ? 676  HIS   A NE2   1 
ATOM   3050 N  N     . PHE   A 1 528  ? 32.564  -27.869 -45.391 1.00 99.49  ? 677  PHE   A N     1 
ATOM   3051 C  CA    . PHE   A 1 528  ? 32.359  -26.535 -46.019 1.00 98.70  ? 677  PHE   A CA    1 
ATOM   3052 C  C     . PHE   A 1 528  ? 31.917  -25.522 -44.953 1.00 100.77 ? 677  PHE   A C     1 
ATOM   3053 O  O     . PHE   A 1 528  ? 30.846  -24.896 -45.111 1.00 99.20  ? 677  PHE   A O     1 
ATOM   3054 C  CB    . PHE   A 1 528  ? 31.349  -26.635 -47.168 1.00 95.19  ? 677  PHE   A CB    1 
ATOM   3055 C  CG    . PHE   A 1 528  ? 31.759  -27.563 -48.284 1.00 91.01  ? 677  PHE   A CG    1 
ATOM   3056 C  CD1   . PHE   A 1 528  ? 32.639  -27.144 -49.271 1.00 88.91  ? 677  PHE   A CD1   1 
ATOM   3057 C  CD2   . PHE   A 1 528  ? 31.268  -28.858 -48.347 1.00 89.02  ? 677  PHE   A CD2   1 
ATOM   3058 C  CE1   . PHE   A 1 528  ? 33.019  -28.000 -50.294 1.00 87.80  ? 677  PHE   A CE1   1 
ATOM   3059 C  CE2   . PHE   A 1 528  ? 31.648  -29.712 -49.371 1.00 88.26  ? 677  PHE   A CE2   1 
ATOM   3060 C  CZ    . PHE   A 1 528  ? 32.522  -29.282 -50.343 1.00 87.57  ? 677  PHE   A CZ    1 
ATOM   3061 N  N     . GLY   A 1 529  ? 32.738  -25.361 -43.907 1.00 102.04 ? 678  GLY   A N     1 
ATOM   3062 C  CA    . GLY   A 1 529  ? 32.484  -24.469 -42.758 1.00 101.82 ? 678  GLY   A CA    1 
ATOM   3063 C  C     . GLY   A 1 529  ? 33.426  -23.278 -42.752 1.00 100.77 ? 678  GLY   A C     1 
ATOM   3064 O  O     . GLY   A 1 529  ? 34.313  -23.223 -43.626 1.00 99.74  ? 678  GLY   A O     1 
ATOM   3065 N  N     . SER   A 1 530  ? 33.248  -22.372 -41.784 1.00 99.66  ? 679  SER   A N     1 
ATOM   3066 C  CA    . SER   A 1 530  ? 33.975  -21.080 -41.648 1.00 100.60 ? 679  SER   A CA    1 
ATOM   3067 C  C     . SER   A 1 530  ? 35.493  -21.297 -41.699 1.00 102.29 ? 679  SER   A C     1 
ATOM   3068 O  O     . SER   A 1 530  ? 36.187  -20.473 -42.329 1.00 100.85 ? 679  SER   A O     1 
ATOM   3069 C  CB    . SER   A 1 530  ? 33.573  -20.376 -40.378 1.00 100.52 ? 679  SER   A CB    1 
ATOM   3070 O  OG    . SER   A 1 530  ? 32.161  -20.360 -40.232 1.00 100.74 ? 679  SER   A OG    1 
ATOM   3071 N  N     . HIS   A 1 531  ? 35.981  -22.361 -41.053 1.00 104.62 ? 680  HIS   A N     1 
ATOM   3072 C  CA    . HIS   A 1 531  ? 37.426  -22.689 -40.898 1.00 105.40 ? 680  HIS   A CA    1 
ATOM   3073 C  C     . HIS   A 1 531  ? 38.089  -22.932 -42.262 1.00 103.22 ? 680  HIS   A C     1 
ATOM   3074 O  O     . HIS   A 1 531  ? 39.265  -22.540 -42.408 1.00 100.43 ? 680  HIS   A O     1 
ATOM   3075 C  CB    . HIS   A 1 531  ? 37.614  -23.883 -39.946 1.00 107.31 ? 680  HIS   A CB    1 
ATOM   3076 C  CG    . HIS   A 1 531  ? 36.897  -25.123 -40.365 1.00 109.99 ? 680  HIS   A CG    1 
ATOM   3077 N  ND1   . HIS   A 1 531  ? 37.456  -26.045 -41.229 1.00 111.14 ? 680  HIS   A ND1   1 
ATOM   3078 C  CD2   . HIS   A 1 531  ? 35.676  -25.601 -40.038 1.00 111.46 ? 680  HIS   A CD2   1 
ATOM   3079 C  CE1   . HIS   A 1 531  ? 36.608  -27.035 -41.421 1.00 112.29 ? 680  HIS   A CE1   1 
ATOM   3080 N  NE2   . HIS   A 1 531  ? 35.507  -26.786 -40.701 1.00 113.01 ? 680  HIS   A NE2   1 
ATOM   3081 N  N     . ARG   A 1 532  ? 37.376  -23.548 -43.216 1.00 101.58 ? 681  ARG   A N     1 
ATOM   3082 C  CA    . ARG   A 1 532  ? 37.943  -24.032 -44.509 1.00 99.41  ? 681  ARG   A CA    1 
ATOM   3083 C  C     . ARG   A 1 532  ? 37.368  -23.258 -45.707 1.00 95.60  ? 681  ARG   A C     1 
ATOM   3084 O  O     . ARG   A 1 532  ? 38.131  -23.042 -46.670 1.00 93.10  ? 681  ARG   A O     1 
ATOM   3085 C  CB    . ARG   A 1 532  ? 37.684  -25.535 -44.666 1.00 101.15 ? 681  ARG   A CB    1 
ATOM   3086 C  CG    . ARG   A 1 532  ? 38.286  -26.160 -45.920 1.00 102.06 ? 681  ARG   A CG    1 
ATOM   3087 C  CD    . ARG   A 1 532  ? 39.803  -26.224 -45.895 1.00 103.10 ? 681  ARG   A CD    1 
ATOM   3088 N  NE    . ARG   A 1 532  ? 40.370  -26.486 -47.213 1.00 102.81 ? 681  ARG   A NE    1 
ATOM   3089 C  CZ    . ARG   A 1 532  ? 40.557  -25.574 -48.167 1.00 102.02 ? 681  ARG   A CZ    1 
ATOM   3090 N  NH1   . ARG   A 1 532  ? 40.216  -24.310 -47.974 1.00 101.16 ? 681  ARG   A NH1   1 
ATOM   3091 N  NH2   . ARG   A 1 532  ? 41.086  -25.936 -49.323 1.00 102.04 ? 681  ARG   A NH2   1 
ATOM   3092 N  N     . TYR   A 1 533  ? 36.083  -22.883 -45.677 1.00 91.49  ? 682  TYR   A N     1 
ATOM   3093 C  CA    . TYR   A 1 533  ? 35.345  -22.326 -46.845 1.00 87.08  ? 682  TYR   A CA    1 
ATOM   3094 C  C     . TYR   A 1 533  ? 34.566  -21.064 -46.456 1.00 84.38  ? 682  TYR   A C     1 
ATOM   3095 O  O     . TYR   A 1 533  ? 33.874  -21.074 -45.420 1.00 81.42  ? 682  TYR   A O     1 
ATOM   3096 C  CB    . TYR   A 1 533  ? 34.390  -23.376 -47.418 1.00 86.00  ? 682  TYR   A CB    1 
ATOM   3097 C  CG    . TYR   A 1 533  ? 34.998  -24.289 -48.452 1.00 85.02  ? 682  TYR   A CG    1 
ATOM   3098 C  CD1   . TYR   A 1 533  ? 35.150  -23.875 -49.765 1.00 84.75  ? 682  TYR   A CD1   1 
ATOM   3099 C  CD2   . TYR   A 1 533  ? 35.414  -25.570 -48.126 1.00 84.00  ? 682  TYR   A CD2   1 
ATOM   3100 C  CE1   . TYR   A 1 533  ? 35.703  -24.705 -50.726 1.00 85.61  ? 682  TYR   A CE1   1 
ATOM   3101 C  CE2   . TYR   A 1 533  ? 35.967  -26.415 -49.076 1.00 84.71  ? 682  TYR   A CE2   1 
ATOM   3102 C  CZ    . TYR   A 1 533  ? 36.113  -25.980 -50.382 1.00 85.86  ? 682  TYR   A CZ    1 
ATOM   3103 O  OH    . TYR   A 1 533  ? 36.657  -26.800 -51.328 1.00 87.21  ? 682  TYR   A OH    1 
ATOM   3104 N  N     . GLN   A 1 534  ? 34.669  -20.021 -47.289 1.00 84.32  ? 683  GLN   A N     1 
ATOM   3105 C  CA    . GLN   A 1 534  ? 33.804  -18.810 -47.254 1.00 84.02  ? 683  GLN   A CA    1 
ATOM   3106 C  C     . GLN   A 1 534  ? 32.883  -18.842 -48.482 1.00 81.77  ? 683  GLN   A C     1 
ATOM   3107 O  O     . GLN   A 1 534  ? 33.368  -18.555 -49.594 1.00 80.49  ? 683  GLN   A O     1 
ATOM   3108 C  CB    . GLN   A 1 534  ? 34.661  -17.541 -47.199 1.00 84.94  ? 683  GLN   A CB    1 
ATOM   3109 C  CG    . GLN   A 1 534  ? 33.860  -16.246 -47.112 1.00 85.77  ? 683  GLN   A CG    1 
ATOM   3110 C  CD    . GLN   A 1 534  ? 33.024  -16.129 -45.858 1.00 88.05  ? 683  GLN   A CD    1 
ATOM   3111 O  OE1   . GLN   A 1 534  ? 33.083  -16.966 -44.959 1.00 89.07  ? 683  GLN   A OE1   1 
ATOM   3112 N  NE2   . GLN   A 1 534  ? 32.231  -15.072 -45.785 1.00 88.81  ? 683  GLN   A NE2   1 
ATOM   3113 N  N     . ILE   A 1 535  ? 31.611  -19.200 -48.273 1.00 81.36  ? 684  ILE   A N     1 
ATOM   3114 C  CA    . ILE   A 1 535  ? 30.578  -19.396 -49.334 1.00 81.56  ? 684  ILE   A CA    1 
ATOM   3115 C  C     . ILE   A 1 535  ? 29.670  -18.162 -49.360 1.00 80.59  ? 684  ILE   A C     1 
ATOM   3116 O  O     . ILE   A 1 535  ? 28.819  -18.039 -48.458 1.00 80.00  ? 684  ILE   A O     1 
ATOM   3117 C  CB    . ILE   A 1 535  ? 29.786  -20.697 -49.089 1.00 83.43  ? 684  ILE   A CB    1 
ATOM   3118 C  CG1   . ILE   A 1 535  ? 30.673  -21.933 -49.270 1.00 84.78  ? 684  ILE   A CG1   1 
ATOM   3119 C  CG2   . ILE   A 1 535  ? 28.547  -20.761 -49.973 1.00 84.38  ? 684  ILE   A CG2   1 
ATOM   3120 C  CD1   . ILE   A 1 535  ? 30.138  -23.181 -48.607 1.00 85.51  ? 684  ILE   A CD1   1 
ATOM   3121 N  N     . LEU   A 1 536  ? 29.846  -17.299 -50.367 1.00 81.48  ? 685  LEU   A N     1 
ATOM   3122 C  CA    . LEU   A 1 536  ? 29.156  -15.987 -50.496 1.00 81.86  ? 685  LEU   A CA    1 
ATOM   3123 C  C     . LEU   A 1 536  ? 28.159  -16.037 -51.649 1.00 79.39  ? 685  LEU   A C     1 
ATOM   3124 O  O     . LEU   A 1 536  ? 28.548  -16.281 -52.789 1.00 79.05  ? 685  LEU   A O     1 
ATOM   3125 C  CB    . LEU   A 1 536  ? 30.206  -14.897 -50.732 1.00 83.93  ? 685  LEU   A CB    1 
ATOM   3126 C  CG    . LEU   A 1 536  ? 31.076  -14.556 -49.523 1.00 85.62  ? 685  LEU   A CG    1 
ATOM   3127 C  CD1   . LEU   A 1 536  ? 32.283  -13.728 -49.940 1.00 86.92  ? 685  LEU   A CD1   1 
ATOM   3128 C  CD2   . LEU   A 1 536  ? 30.267  -13.829 -48.458 1.00 85.25  ? 685  LEU   A CD2   1 
ATOM   3129 N  N     . PRO   A 1 537  ? 26.852  -15.794 -51.394 1.00 77.95  ? 686  PRO   A N     1 
ATOM   3130 C  CA    . PRO   A 1 537  ? 25.859  -15.698 -52.463 1.00 78.24  ? 686  PRO   A CA    1 
ATOM   3131 C  C     . PRO   A 1 537  ? 25.915  -14.317 -53.129 1.00 78.54  ? 686  PRO   A C     1 
ATOM   3132 O  O     . PRO   A 1 537  ? 26.245  -13.357 -52.448 1.00 78.92  ? 686  PRO   A O     1 
ATOM   3133 C  CB    . PRO   A 1 537  ? 24.534  -15.910 -51.720 1.00 78.76  ? 686  PRO   A CB    1 
ATOM   3134 C  CG    . PRO   A 1 537  ? 24.789  -15.310 -50.353 1.00 78.76  ? 686  PRO   A CG    1 
ATOM   3135 C  CD    . PRO   A 1 537  ? 26.254  -15.578 -50.067 1.00 79.16  ? 686  PRO   A CD    1 
ATOM   3136 N  N     . LEU   A 1 538  ? 25.595  -14.253 -54.425 1.00 78.06  ? 687  LEU   A N     1 
ATOM   3137 C  CA    . LEU   A 1 538  ? 25.651  -13.012 -55.243 1.00 77.75  ? 687  LEU   A CA    1 
ATOM   3138 C  C     . LEU   A 1 538  ? 24.485  -12.996 -56.240 1.00 80.87  ? 687  LEU   A C     1 
ATOM   3139 O  O     . LEU   A 1 538  ? 24.626  -13.585 -57.327 1.00 82.91  ? 687  LEU   A O     1 
ATOM   3140 C  CB    . LEU   A 1 538  ? 27.008  -12.959 -55.953 1.00 74.10  ? 687  LEU   A CB    1 
ATOM   3141 C  CG    . LEU   A 1 538  ? 27.222  -11.790 -56.913 1.00 72.97  ? 687  LEU   A CG    1 
ATOM   3142 C  CD1   . LEU   A 1 538  ? 26.833  -10.468 -56.269 1.00 72.60  ? 687  LEU   A CD1   1 
ATOM   3143 C  CD2   . LEU   A 1 538  ? 28.665  -11.747 -57.390 1.00 73.18  ? 687  LEU   A CD2   1 
ATOM   3144 N  N     . HIS   A 1 539  ? 23.373  -12.355 -55.868 1.00 83.63  ? 688  HIS   A N     1 
ATOM   3145 C  CA    . HIS   A 1 539  ? 22.207  -12.084 -56.752 1.00 88.02  ? 688  HIS   A CA    1 
ATOM   3146 C  C     . HIS   A 1 539  ? 21.622  -10.709 -56.408 1.00 91.13  ? 688  HIS   A C     1 
ATOM   3147 O  O     . HIS   A 1 539  ? 22.115  -10.081 -55.454 1.00 88.30  ? 688  HIS   A O     1 
ATOM   3148 C  CB    . HIS   A 1 539  ? 21.187  -13.232 -56.680 1.00 88.54  ? 688  HIS   A CB    1 
ATOM   3149 C  CG    . HIS   A 1 539  ? 20.635  -13.498 -55.320 1.00 90.20  ? 688  HIS   A CG    1 
ATOM   3150 N  ND1   . HIS   A 1 539  ? 21.219  -14.397 -54.446 1.00 92.28  ? 688  HIS   A ND1   1 
ATOM   3151 C  CD2   . HIS   A 1 539  ? 19.543  -13.015 -54.690 1.00 91.38  ? 688  HIS   A CD2   1 
ATOM   3152 C  CE1   . HIS   A 1 539  ? 20.516  -14.445 -53.332 1.00 91.53  ? 688  HIS   A CE1   1 
ATOM   3153 N  NE2   . HIS   A 1 539  ? 19.480  -13.608 -53.458 1.00 92.16  ? 688  HIS   A NE2   1 
ATOM   3154 N  N     . SER   A 1 540  ? 20.623  -10.260 -57.174 1.00 98.53  ? 689  SER   A N     1 
ATOM   3155 C  CA    . SER   A 1 540  ? 20.073  -8.878  -57.148 1.00 104.13 ? 689  SER   A CA    1 
ATOM   3156 C  C     . SER   A 1 540  ? 19.518  -8.535  -55.759 1.00 106.36 ? 689  SER   A C     1 
ATOM   3157 O  O     . SER   A 1 540  ? 19.874  -7.459  -55.239 1.00 109.15 ? 689  SER   A O     1 
ATOM   3158 C  CB    . SER   A 1 540  ? 19.020  -8.696  -58.214 1.00 106.92 ? 689  SER   A CB    1 
ATOM   3159 O  OG    . SER   A 1 540  ? 17.862  -9.465  -57.921 1.00 109.92 ? 689  SER   A OG    1 
ATOM   3160 N  N     . GLN   A 1 541  ? 18.692  -9.417  -55.184 1.00 107.07 ? 690  GLN   A N     1 
ATOM   3161 C  CA    . GLN   A 1 541  ? 17.861  -9.128  -53.980 1.00 108.92 ? 690  GLN   A CA    1 
ATOM   3162 C  C     . GLN   A 1 541  ? 18.564  -9.616  -52.702 1.00 106.57 ? 690  GLN   A C     1 
ATOM   3163 O  O     . GLN   A 1 541  ? 17.980  -10.450 -51.980 1.00 106.51 ? 690  GLN   A O     1 
ATOM   3164 C  CB    . GLN   A 1 541  ? 16.455  -9.721  -54.141 1.00 111.14 ? 690  GLN   A CB    1 
ATOM   3165 C  CG    . GLN   A 1 541  ? 16.419  -11.217 -54.431 1.00 112.63 ? 690  GLN   A CG    1 
ATOM   3166 C  CD    . GLN   A 1 541  ? 15.033  -11.794 -54.275 1.00 113.49 ? 690  GLN   A CD    1 
ATOM   3167 O  OE1   . GLN   A 1 541  ? 14.749  -12.535 -53.335 1.00 112.81 ? 690  GLN   A OE1   1 
ATOM   3168 N  NE2   . GLN   A 1 541  ? 14.151  -11.449 -55.199 1.00 114.16 ? 690  GLN   A NE2   1 
ATOM   3169 N  N     . ILE   A 1 542  ? 19.763  -9.092  -52.423 1.00 104.70 ? 691  ILE   A N     1 
ATOM   3170 C  CA    . ILE   A 1 542  ? 20.447  -9.186  -51.096 1.00 105.34 ? 691  ILE   A CA    1 
ATOM   3171 C  C     . ILE   A 1 542  ? 21.108  -7.842  -50.801 1.00 106.81 ? 691  ILE   A C     1 
ATOM   3172 O  O     . ILE   A 1 542  ? 21.366  -7.069  -51.722 1.00 109.03 ? 691  ILE   A O     1 
ATOM   3173 C  CB    . ILE   A 1 542  ? 21.459  -10.351 -51.047 1.00 104.26 ? 691  ILE   A CB    1 
ATOM   3174 C  CG1   . ILE   A 1 542  ? 22.544  -10.226 -52.119 1.00 101.83 ? 691  ILE   A CG1   1 
ATOM   3175 C  CG2   . ILE   A 1 542  ? 20.745  -11.690 -51.127 1.00 104.96 ? 691  ILE   A CG2   1 
ATOM   3176 C  CD1   . ILE   A 1 542  ? 23.748  -11.105 -51.871 1.00 101.14 ? 691  ILE   A CD1   1 
ATOM   3177 N  N     . PRO   A 1 543  ? 21.407  -7.520  -49.520 1.00 107.33 ? 692  PRO   A N     1 
ATOM   3178 C  CA    . PRO   A 1 543  ? 22.021  -6.237  -49.172 1.00 106.62 ? 692  PRO   A CA    1 
ATOM   3179 C  C     . PRO   A 1 543  ? 23.378  -6.039  -49.865 1.00 104.03 ? 692  PRO   A C     1 
ATOM   3180 O  O     . PRO   A 1 543  ? 24.084  -7.015  -50.057 1.00 101.41 ? 692  PRO   A O     1 
ATOM   3181 C  CB    . PRO   A 1 543  ? 22.202  -6.303  -47.647 1.00 109.42 ? 692  PRO   A CB    1 
ATOM   3182 C  CG    . PRO   A 1 543  ? 21.226  -7.370  -47.193 1.00 109.55 ? 692  PRO   A CG    1 
ATOM   3183 C  CD    . PRO   A 1 543  ? 21.171  -8.362  -48.336 1.00 108.18 ? 692  PRO   A CD    1 
ATOM   3184 N  N     . ARG   A 1 544  ? 23.703  -4.791  -50.216 1.00 102.82 ? 693  ARG   A N     1 
ATOM   3185 C  CA    . ARG   A 1 544  ? 24.955  -4.425  -50.935 1.00 104.32 ? 693  ARG   A CA    1 
ATOM   3186 C  C     . ARG   A 1 544  ? 26.165  -4.722  -50.040 1.00 106.32 ? 693  ARG   A C     1 
ATOM   3187 O  O     . ARG   A 1 544  ? 27.246  -5.004  -50.596 1.00 107.23 ? 693  ARG   A O     1 
ATOM   3188 C  CB    . ARG   A 1 544  ? 24.912  -2.963  -51.393 1.00 102.66 ? 693  ARG   A CB    1 
ATOM   3189 C  CG    . ARG   A 1 544  ? 24.001  -2.725  -52.589 1.00 101.75 ? 693  ARG   A CG    1 
ATOM   3190 C  CD    . ARG   A 1 544  ? 24.266  -1.403  -53.280 1.00 101.42 ? 693  ARG   A CD    1 
ATOM   3191 N  NE    . ARG   A 1 544  ? 23.992  -0.257  -52.420 1.00 102.26 ? 693  ARG   A NE    1 
ATOM   3192 C  CZ    . ARG   A 1 544  ? 22.782  0.220   -52.131 1.00 101.28 ? 693  ARG   A CZ    1 
ATOM   3193 N  NH1   . ARG   A 1 544  ? 22.665  1.274   -51.340 1.00 100.96 ? 693  ARG   A NH1   1 
ATOM   3194 N  NH2   . ARG   A 1 544  ? 21.692  -0.345  -52.624 1.00 101.00 ? 693  ARG   A NH2   1 
ATOM   3195 N  N     . GLU   A 1 545  ? 25.984  -4.679  -48.715 1.00 108.29 ? 694  GLU   A N     1 
ATOM   3196 C  CA    . GLU   A 1 545  ? 27.013  -5.070  -47.713 1.00 108.74 ? 694  GLU   A CA    1 
ATOM   3197 C  C     . GLU   A 1 545  ? 27.460  -6.510  -47.989 1.00 108.16 ? 694  GLU   A C     1 
ATOM   3198 O  O     . GLU   A 1 545  ? 28.682  -6.750  -48.018 1.00 111.02 ? 694  GLU   A O     1 
ATOM   3199 C  CB    . GLU   A 1 545  ? 26.465  -4.938  -46.290 1.00 111.31 ? 694  GLU   A CB    1 
ATOM   3200 C  CG    . GLU   A 1 545  ? 27.532  -5.075  -45.216 1.00 113.42 ? 694  GLU   A CG    1 
ATOM   3201 C  CD    . GLU   A 1 545  ? 27.002  -5.257  -43.804 1.00 114.86 ? 694  GLU   A CD    1 
ATOM   3202 O  OE1   . GLU   A 1 545  ? 25.830  -4.905  -43.561 1.00 115.85 ? 694  GLU   A OE1   1 
ATOM   3203 O  OE2   . GLU   A 1 545  ? 27.764  -5.755  -42.952 1.00 116.26 ? 694  GLU   A OE2   1 
ATOM   3204 N  N     . GLU   A 1 546  ? 26.502  -7.423  -48.186 1.00 105.91 ? 695  GLU   A N     1 
ATOM   3205 C  CA    . GLU   A 1 546  ? 26.750  -8.866  -48.459 1.00 103.76 ? 695  GLU   A CA    1 
ATOM   3206 C  C     . GLU   A 1 546  ? 27.350  -9.041  -49.861 1.00 100.13 ? 695  GLU   A C     1 
ATOM   3207 O  O     . GLU   A 1 546  ? 28.135  -9.991  -50.045 1.00 98.83  ? 695  GLU   A O     1 
ATOM   3208 C  CB    . GLU   A 1 546  ? 25.461  -9.681  -48.307 1.00 104.91 ? 695  GLU   A CB    1 
ATOM   3209 C  CG    . GLU   A 1 546  ? 25.265  -10.252 -46.913 1.00 105.48 ? 695  GLU   A CG    1 
ATOM   3210 C  CD    . GLU   A 1 546  ? 26.211  -11.389 -46.560 1.00 107.60 ? 695  GLU   A CD    1 
ATOM   3211 O  OE1   . GLU   A 1 546  ? 26.262  -12.375 -47.325 1.00 109.79 ? 695  GLU   A OE1   1 
ATOM   3212 O  OE2   . GLU   A 1 546  ? 26.905  -11.282 -45.528 1.00 105.00 ? 695  GLU   A OE2   1 
ATOM   3213 N  N     . GLN   A 1 547  ? 26.987  -8.169  -50.809 1.00 97.11  ? 696  GLN   A N     1 
ATOM   3214 C  CA    . GLN   A 1 547  ? 27.463  -8.219  -52.219 1.00 96.38  ? 696  GLN   A CA    1 
ATOM   3215 C  C     . GLN   A 1 547  ? 28.903  -7.697  -52.301 1.00 93.97  ? 696  GLN   A C     1 
ATOM   3216 O  O     . GLN   A 1 547  ? 29.678  -8.250  -53.104 1.00 90.69  ? 696  GLN   A O     1 
ATOM   3217 C  CB    . GLN   A 1 547  ? 26.522  -7.432  -53.134 1.00 98.38  ? 696  GLN   A CB    1 
ATOM   3218 C  CG    . GLN   A 1 547  ? 25.234  -8.179  -53.444 1.00 101.05 ? 696  GLN   A CG    1 
ATOM   3219 C  CD    . GLN   A 1 547  ? 24.189  -7.309  -54.101 1.00 104.10 ? 696  GLN   A CD    1 
ATOM   3220 O  OE1   . GLN   A 1 547  ? 23.709  -6.336  -53.523 1.00 104.70 ? 696  GLN   A OE1   1 
ATOM   3221 N  NE2   . GLN   A 1 547  ? 23.810  -7.668  -55.316 1.00 106.55 ? 696  GLN   A NE2   1 
ATOM   3222 N  N     . ARG   A 1 548  ? 29.247  -6.684  -51.499 1.00 94.52  ? 697  ARG   A N     1 
ATOM   3223 C  CA    . ARG   A 1 548  ? 30.608  -6.078  -51.445 1.00 94.38  ? 697  ARG   A CA    1 
ATOM   3224 C  C     . ARG   A 1 548  ? 31.630  -7.116  -50.954 1.00 92.06  ? 697  ARG   A C     1 
ATOM   3225 O  O     . ARG   A 1 548  ? 32.807  -6.999  -51.341 1.00 93.02  ? 697  ARG   A O     1 
ATOM   3226 C  CB    . ARG   A 1 548  ? 30.618  -4.831  -50.552 1.00 95.29  ? 697  ARG   A CB    1 
ATOM   3227 C  CG    . ARG   A 1 548  ? 30.232  -3.543  -51.269 1.00 95.83  ? 697  ARG   A CG    1 
ATOM   3228 C  CD    . ARG   A 1 548  ? 30.427  -2.302  -50.414 1.00 96.04  ? 697  ARG   A CD    1 
ATOM   3229 N  NE    . ARG   A 1 548  ? 29.335  -2.078  -49.471 1.00 97.64  ? 697  ARG   A NE    1 
ATOM   3230 C  CZ    . ARG   A 1 548  ? 28.200  -1.427  -49.738 1.00 97.66  ? 697  ARG   A CZ    1 
ATOM   3231 N  NH1   . ARG   A 1 548  ? 27.282  -1.288  -48.795 1.00 96.02  ? 697  ARG   A NH1   1 
ATOM   3232 N  NH2   . ARG   A 1 548  ? 27.975  -0.919  -50.938 1.00 98.87  ? 697  ARG   A NH2   1 
ATOM   3233 N  N     . LYS   A 1 549  ? 31.195  -8.098  -50.155 1.00 90.86  ? 698  LYS   A N     1 
ATOM   3234 C  CA    . LYS   A 1 549  ? 32.072  -9.098  -49.481 1.00 90.83  ? 698  LYS   A CA    1 
ATOM   3235 C  C     . LYS   A 1 549  ? 32.739  -10.040 -50.495 1.00 89.31  ? 698  LYS   A C     1 
ATOM   3236 O  O     . LYS   A 1 549  ? 33.732  -10.686 -50.109 1.00 92.51  ? 698  LYS   A O     1 
ATOM   3237 C  CB    . LYS   A 1 549  ? 31.276  -9.914  -48.456 1.00 92.53  ? 698  LYS   A CB    1 
ATOM   3238 C  CG    . LYS   A 1 549  ? 30.978  -9.197  -47.146 1.00 93.82  ? 698  LYS   A CG    1 
ATOM   3239 C  CD    . LYS   A 1 549  ? 30.077  -9.985  -46.220 1.00 94.49  ? 698  LYS   A CD    1 
ATOM   3240 C  CE    . LYS   A 1 549  ? 29.736  -9.237  -44.950 1.00 95.23  ? 698  LYS   A CE    1 
ATOM   3241 N  NZ    . LYS   A 1 549  ? 28.782  -9.998  -44.111 1.00 95.65  ? 698  LYS   A NZ    1 
ATOM   3242 N  N     . VAL   A 1 550  ? 32.226  -10.131 -51.728 1.00 87.17  ? 699  VAL   A N     1 
ATOM   3243 C  CA    . VAL   A 1 550  ? 32.760  -11.049 -52.783 1.00 84.75  ? 699  VAL   A CA    1 
ATOM   3244 C  C     . VAL   A 1 550  ? 34.145  -10.559 -53.235 1.00 84.34  ? 699  VAL   A C     1 
ATOM   3245 O  O     . VAL   A 1 550  ? 34.937  -11.403 -53.701 1.00 85.31  ? 699  VAL   A O     1 
ATOM   3246 C  CB    . VAL   A 1 550  ? 31.797  -11.192 -53.981 1.00 83.22  ? 699  VAL   A CB    1 
ATOM   3247 C  CG1   . VAL   A 1 550  ? 30.410  -11.639 -53.544 1.00 83.00  ? 699  VAL   A CG1   1 
ATOM   3248 C  CG2   . VAL   A 1 550  ? 31.717  -9.921  -54.813 1.00 83.21  ? 699  VAL   A CG2   1 
ATOM   3249 N  N     . PHE   A 1 551  ? 34.423  -9.256  -53.103 1.00 83.53  ? 700  PHE   A N     1 
ATOM   3250 C  CA    . PHE   A 1 551  ? 35.691  -8.600  -53.523 1.00 83.62  ? 700  PHE   A CA    1 
ATOM   3251 C  C     . PHE   A 1 551  ? 36.725  -8.645  -52.388 1.00 86.90  ? 700  PHE   A C     1 
ATOM   3252 O  O     . PHE   A 1 551  ? 37.933  -8.543  -52.688 1.00 89.06  ? 700  PHE   A O     1 
ATOM   3253 C  CB    . PHE   A 1 551  ? 35.422  -7.160  -53.966 1.00 81.25  ? 700  PHE   A CB    1 
ATOM   3254 C  CG    . PHE   A 1 551  ? 34.434  -7.030  -55.098 1.00 79.62  ? 700  PHE   A CG    1 
ATOM   3255 C  CD1   . PHE   A 1 551  ? 34.835  -7.199  -56.414 1.00 78.26  ? 700  PHE   A CD1   1 
ATOM   3256 C  CD2   . PHE   A 1 551  ? 33.101  -6.740  -54.847 1.00 78.99  ? 700  PHE   A CD2   1 
ATOM   3257 C  CE1   . PHE   A 1 551  ? 33.925  -7.079  -57.453 1.00 77.49  ? 700  PHE   A CE1   1 
ATOM   3258 C  CE2   . PHE   A 1 551  ? 32.192  -6.623  -55.887 1.00 77.60  ? 700  PHE   A CE2   1 
ATOM   3259 C  CZ    . PHE   A 1 551  ? 32.605  -6.792  -57.188 1.00 76.93  ? 700  PHE   A CZ    1 
ATOM   3260 N  N     . ASP   A 1 552  ? 36.271  -8.781  -51.136 1.00 86.66  ? 701  ASP   A N     1 
ATOM   3261 C  CA    . ASP   A 1 552  ? 37.137  -8.875  -49.929 1.00 87.22  ? 701  ASP   A CA    1 
ATOM   3262 C  C     . ASP   A 1 552  ? 38.048  -10.094 -50.052 1.00 90.67  ? 701  ASP   A C     1 
ATOM   3263 O  O     . ASP   A 1 552  ? 37.580  -11.179 -50.392 1.00 88.75  ? 701  ASP   A O     1 
ATOM   3264 C  CB    . ASP   A 1 552  ? 36.311  -8.979  -48.643 1.00 85.84  ? 701  ASP   A CB    1 
ATOM   3265 C  CG    . ASP   A 1 552  ? 35.562  -7.710  -48.271 1.00 85.24  ? 701  ASP   A CG    1 
ATOM   3266 O  OD1   . ASP   A 1 552  ? 35.851  -6.656  -48.873 1.00 86.33  ? 701  ASP   A OD1   1 
ATOM   3267 O  OD2   . ASP   A 1 552  ? 34.696  -7.785  -47.378 1.00 82.95  ? 701  ASP   A OD2   1 
ATOM   3268 N  N     . PRO   A 1 553  ? 39.373  -9.960  -49.798 1.00 96.42  ? 702  PRO   A N     1 
ATOM   3269 C  CA    . PRO   A 1 553  ? 40.249  -11.124 -49.651 1.00 96.87  ? 702  PRO   A CA    1 
ATOM   3270 C  C     . PRO   A 1 553  ? 39.899  -11.937 -48.394 1.00 94.88  ? 702  PRO   A C     1 
ATOM   3271 O  O     . PRO   A 1 553  ? 39.307  -11.381 -47.484 1.00 92.26  ? 702  PRO   A O     1 
ATOM   3272 C  CB    . PRO   A 1 553  ? 41.667  -10.535 -49.536 1.00 97.48  ? 702  PRO   A CB    1 
ATOM   3273 C  CG    . PRO   A 1 553  ? 41.535  -9.098  -50.011 1.00 97.66  ? 702  PRO   A CG    1 
ATOM   3274 C  CD    . PRO   A 1 553  ? 40.112  -8.693  -49.687 1.00 97.05  ? 702  PRO   A CD    1 
ATOM   3275 N  N     . VAL   A 1 554  ? 40.278  -13.219 -48.376 1.00 94.01  ? 703  VAL   A N     1 
ATOM   3276 C  CA    . VAL   A 1 554  ? 40.017  -14.171 -47.253 1.00 96.33  ? 703  VAL   A CA    1 
ATOM   3277 C  C     . VAL   A 1 554  ? 41.356  -14.582 -46.644 1.00 97.27  ? 703  VAL   A C     1 
ATOM   3278 O  O     . VAL   A 1 554  ? 42.390  -14.492 -47.304 1.00 97.17  ? 703  VAL   A O     1 
ATOM   3279 C  CB    . VAL   A 1 554  ? 39.206  -15.399 -47.716 1.00 98.47  ? 703  VAL   A CB    1 
ATOM   3280 C  CG1   . VAL   A 1 554  ? 37.752  -15.043 -47.989 1.00 99.57  ? 703  VAL   A CG1   1 
ATOM   3281 C  CG2   . VAL   A 1 554  ? 39.824  -16.086 -48.927 1.00 97.46  ? 703  VAL   A CG2   1 
ATOM   3282 N  N     . PRO   A 1 555  ? 41.383  -15.038 -45.369 1.00 97.05  ? 704  PRO   A N     1 
ATOM   3283 C  CA    . PRO   A 1 555  ? 42.612  -15.553 -44.764 1.00 96.47  ? 704  PRO   A CA    1 
ATOM   3284 C  C     . PRO   A 1 555  ? 43.063  -16.861 -45.434 1.00 96.88  ? 704  PRO   A C     1 
ATOM   3285 O  O     . PRO   A 1 555  ? 42.227  -17.727 -45.628 1.00 94.62  ? 704  PRO   A O     1 
ATOM   3286 C  CB    . PRO   A 1 555  ? 42.235  -15.777 -43.291 1.00 96.67  ? 704  PRO   A CB    1 
ATOM   3287 C  CG    . PRO   A 1 555  ? 40.730  -15.961 -43.311 1.00 95.73  ? 704  PRO   A CG    1 
ATOM   3288 C  CD    . PRO   A 1 555  ? 40.241  -15.075 -44.439 1.00 96.22  ? 704  PRO   A CD    1 
ATOM   3289 N  N     . SER   A 1 556  ? 44.355  -16.959 -45.773 1.00 98.33  ? 705  SER   A N     1 
ATOM   3290 C  CA    . SER   A 1 556  ? 44.991  -18.139 -46.422 1.00 95.97  ? 705  SER   A CA    1 
ATOM   3291 C  C     . SER   A 1 556  ? 44.647  -19.409 -45.634 1.00 94.04  ? 705  SER   A C     1 
ATOM   3292 O  O     . SER   A 1 556  ? 44.738  -19.376 -44.388 1.00 92.03  ? 705  SER   A O     1 
ATOM   3293 C  CB    . SER   A 1 556  ? 46.484  -17.953 -46.556 1.00 95.35  ? 705  SER   A CB    1 
ATOM   3294 O  OG    . SER   A 1 556  ? 47.099  -17.825 -45.283 1.00 95.40  ? 705  SER   A OG    1 
ATOM   3295 N  N     . GLY   A 1 557  ? 44.256  -20.476 -46.340 1.00 92.00  ? 706  GLY   A N     1 
ATOM   3296 C  CA    . GLY   A 1 557  ? 43.707  -21.716 -45.757 1.00 90.89  ? 706  GLY   A CA    1 
ATOM   3297 C  C     . GLY   A 1 557  ? 42.207  -21.823 -45.986 1.00 90.71  ? 706  GLY   A C     1 
ATOM   3298 O  O     . GLY   A 1 557  ? 41.699  -22.962 -46.032 1.00 90.02  ? 706  GLY   A O     1 
ATOM   3299 N  N     . VAL   A 1 558  ? 41.524  -20.679 -46.113 1.00 90.73  ? 707  VAL   A N     1 
ATOM   3300 C  CA    . VAL   A 1 558  ? 40.073  -20.576 -46.457 1.00 90.76  ? 707  VAL   A CA    1 
ATOM   3301 C  C     . VAL   A 1 558  ? 39.943  -20.350 -47.969 1.00 89.46  ? 707  VAL   A C     1 
ATOM   3302 O  O     . VAL   A 1 558  ? 40.751  -19.572 -48.521 1.00 88.77  ? 707  VAL   A O     1 
ATOM   3303 C  CB    . VAL   A 1 558  ? 39.378  -19.451 -45.664 1.00 92.37  ? 707  VAL   A CB    1 
ATOM   3304 C  CG1   . VAL   A 1 558  ? 37.873  -19.443 -45.893 1.00 92.02  ? 707  VAL   A CG1   1 
ATOM   3305 C  CG2   . VAL   A 1 558  ? 39.691  -19.529 -44.177 1.00 93.64  ? 707  VAL   A CG2   1 
ATOM   3306 N  N     . THR   A 1 559  ? 38.962  -21.002 -48.603 1.00 88.57  ? 708  THR   A N     1 
ATOM   3307 C  CA    . THR   A 1 559  ? 38.630  -20.862 -50.048 1.00 87.59  ? 708  THR   A CA    1 
ATOM   3308 C  C     . THR   A 1 559  ? 37.409  -19.945 -50.195 1.00 84.91  ? 708  THR   A C     1 
ATOM   3309 O  O     . THR   A 1 559  ? 36.430  -20.146 -49.447 1.00 82.08  ? 708  THR   A O     1 
ATOM   3310 C  CB    . THR   A 1 559  ? 38.376  -22.228 -50.700 1.00 88.35  ? 708  THR   A CB    1 
ATOM   3311 O  OG1   . THR   A 1 559  ? 39.417  -23.123 -50.308 1.00 90.72  ? 708  THR   A OG1   1 
ATOM   3312 C  CG2   . THR   A 1 559  ? 38.318  -22.161 -52.211 1.00 87.93  ? 708  THR   A CG2   1 
ATOM   3313 N  N     . LYS   A 1 560  ? 37.477  -18.981 -51.120 1.00 83.40  ? 709  LYS   A N     1 
ATOM   3314 C  CA    . LYS   A 1 560  ? 36.374  -18.037 -51.450 1.00 82.96  ? 709  LYS   A CA    1 
ATOM   3315 C  C     . LYS   A 1 560  ? 35.540  -18.631 -52.593 1.00 81.95  ? 709  LYS   A C     1 
ATOM   3316 O  O     . LYS   A 1 560  ? 36.009  -18.586 -53.744 1.00 85.46  ? 709  LYS   A O     1 
ATOM   3317 C  CB    . LYS   A 1 560  ? 36.945  -16.667 -51.833 1.00 83.25  ? 709  LYS   A CB    1 
ATOM   3318 C  CG    . LYS   A 1 560  ? 35.908  -15.604 -52.173 1.00 83.65  ? 709  LYS   A CG    1 
ATOM   3319 C  CD    . LYS   A 1 560  ? 36.494  -14.228 -52.417 1.00 84.00  ? 709  LYS   A CD    1 
ATOM   3320 C  CE    . LYS   A 1 560  ? 37.322  -14.150 -53.682 1.00 84.94  ? 709  LYS   A CE    1 
ATOM   3321 N  NZ    . LYS   A 1 560  ? 37.645  -12.749 -54.042 1.00 84.80  ? 709  LYS   A NZ    1 
ATOM   3322 N  N     . VAL   A 1 561  ? 34.357  -19.171 -52.282 1.00 79.22  ? 710  VAL   A N     1 
ATOM   3323 C  CA    . VAL   A 1 561  ? 33.420  -19.778 -53.274 1.00 79.04  ? 710  VAL   A CA    1 
ATOM   3324 C  C     . VAL   A 1 561  ? 32.256  -18.806 -53.506 1.00 77.86  ? 710  VAL   A C     1 
ATOM   3325 O  O     . VAL   A 1 561  ? 31.502  -18.550 -52.547 1.00 76.81  ? 710  VAL   A O     1 
ATOM   3326 C  CB    . VAL   A 1 561  ? 32.923  -21.161 -52.811 1.00 80.67  ? 710  VAL   A CB    1 
ATOM   3327 C  CG1   . VAL   A 1 561  ? 31.875  -21.736 -53.754 1.00 80.88  ? 710  VAL   A CG1   1 
ATOM   3328 C  CG2   . VAL   A 1 561  ? 34.075  -22.139 -52.639 1.00 81.27  ? 710  VAL   A CG2   1 
ATOM   3329 N  N     . ILE   A 1 562  ? 32.121  -18.295 -54.735 1.00 77.04  ? 711  ILE   A N     1 
ATOM   3330 C  CA    . ILE   A 1 562  ? 31.055  -17.330 -55.141 1.00 76.14  ? 711  ILE   A CA    1 
ATOM   3331 C  C     . ILE   A 1 562  ? 29.965  -18.090 -55.906 1.00 73.21  ? 711  ILE   A C     1 
ATOM   3332 O  O     . ILE   A 1 562  ? 30.240  -18.527 -57.041 1.00 73.95  ? 711  ILE   A O     1 
ATOM   3333 C  CB    . ILE   A 1 562  ? 31.636  -16.176 -55.984 1.00 77.82  ? 711  ILE   A CB    1 
ATOM   3334 C  CG1   . ILE   A 1 562  ? 32.935  -15.618 -55.394 1.00 80.09  ? 711  ILE   A CG1   1 
ATOM   3335 C  CG2   . ILE   A 1 562  ? 30.593  -15.086 -56.182 1.00 76.87  ? 711  ILE   A CG2   1 
ATOM   3336 C  CD1   . ILE   A 1 562  ? 32.805  -15.102 -53.977 1.00 82.10  ? 711  ILE   A CD1   1 
ATOM   3337 N  N     . LEU   A 1 563  ? 28.785  -18.241 -55.295 1.00 70.52  ? 712  LEU   A N     1 
ATOM   3338 C  CA    . LEU   A 1 563  ? 27.552  -18.772 -55.937 1.00 69.81  ? 712  LEU   A CA    1 
ATOM   3339 C  C     . LEU   A 1 563  ? 26.766  -17.587 -56.510 1.00 69.55  ? 712  LEU   A C     1 
ATOM   3340 O  O     . LEU   A 1 563  ? 26.025  -16.949 -55.735 1.00 71.21  ? 712  LEU   A O     1 
ATOM   3341 C  CB    . LEU   A 1 563  ? 26.720  -19.533 -54.899 1.00 69.91  ? 712  LEU   A CB    1 
ATOM   3342 C  CG    . LEU   A 1 563  ? 27.460  -20.601 -54.095 1.00 70.39  ? 712  LEU   A CG    1 
ATOM   3343 C  CD1   . LEU   A 1 563  ? 26.532  -21.238 -53.073 1.00 71.11  ? 712  LEU   A CD1   1 
ATOM   3344 C  CD2   . LEU   A 1 563  ? 28.061  -21.659 -55.008 1.00 70.94  ? 712  LEU   A CD2   1 
ATOM   3345 N  N     . SER   A 1 564  ? 26.933  -17.298 -57.805 1.00 69.24  ? 713  SER   A N     1 
ATOM   3346 C  CA    . SER   A 1 564  ? 26.458  -16.048 -58.458 1.00 69.43  ? 713  SER   A CA    1 
ATOM   3347 C  C     . SER   A 1 564  ? 25.551  -16.349 -59.656 1.00 69.01  ? 713  SER   A C     1 
ATOM   3348 O  O     . SER   A 1 564  ? 25.616  -17.472 -60.194 1.00 67.08  ? 713  SER   A O     1 
ATOM   3349 C  CB    . SER   A 1 564  ? 27.621  -15.187 -58.880 1.00 68.41  ? 713  SER   A CB    1 
ATOM   3350 O  OG    . SER   A 1 564  ? 28.399  -15.840 -59.870 1.00 68.45  ? 713  SER   A OG    1 
ATOM   3351 N  N     . THR   A 1 565  ? 24.746  -15.353 -60.047 1.00 69.48  ? 714  THR   A N     1 
ATOM   3352 C  CA    . THR   A 1 565  ? 24.010  -15.280 -61.338 1.00 69.65  ? 714  THR   A CA    1 
ATOM   3353 C  C     . THR   A 1 565  ? 24.981  -14.752 -62.403 1.00 69.93  ? 714  THR   A C     1 
ATOM   3354 O  O     . THR   A 1 565  ? 26.183  -14.631 -62.088 1.00 71.28  ? 714  THR   A O     1 
ATOM   3355 C  CB    . THR   A 1 565  ? 22.746  -14.420 -61.202 1.00 68.76  ? 714  THR   A CB    1 
ATOM   3356 O  OG1   . THR   A 1 565  ? 23.139  -13.083 -60.889 1.00 70.37  ? 714  THR   A OG1   1 
ATOM   3357 C  CG2   . THR   A 1 565  ? 21.799  -14.921 -60.135 1.00 67.94  ? 714  THR   A CG2   1 
ATOM   3358 N  N     . ASN   A 1 566  ? 24.484  -14.433 -63.602 1.00 70.12  ? 715  ASN   A N     1 
ATOM   3359 C  CA    . ASN   A 1 566  ? 25.307  -13.953 -64.748 1.00 68.97  ? 715  ASN   A CA    1 
ATOM   3360 C  C     . ASN   A 1 566  ? 25.692  -12.478 -64.552 1.00 69.09  ? 715  ASN   A C     1 
ATOM   3361 O  O     . ASN   A 1 566  ? 26.221  -11.885 -65.510 1.00 70.25  ? 715  ASN   A O     1 
ATOM   3362 C  CB    . ASN   A 1 566  ? 24.600  -14.176 -66.089 1.00 67.62  ? 715  ASN   A CB    1 
ATOM   3363 C  CG    . ASN   A 1 566  ? 23.341  -13.350 -66.255 1.00 66.03  ? 715  ASN   A CG    1 
ATOM   3364 O  OD1   . ASN   A 1 566  ? 22.723  -12.940 -65.276 1.00 64.02  ? 715  ASN   A OD1   1 
ATOM   3365 N  ND2   . ASN   A 1 566  ? 22.949  -13.107 -67.494 1.00 67.22  ? 715  ASN   A ND2   1 
ATOM   3366 N  N     . ILE   A 1 567  ? 25.421  -11.899 -63.375 1.00 70.20  ? 716  ILE   A N     1 
ATOM   3367 C  CA    . ILE   A 1 567  ? 25.976  -10.581 -62.937 1.00 71.38  ? 716  ILE   A CA    1 
ATOM   3368 C  C     . ILE   A 1 567  ? 27.504  -10.626 -63.077 1.00 72.11  ? 716  ILE   A C     1 
ATOM   3369 O  O     . ILE   A 1 567  ? 28.078  -9.637  -63.571 1.00 75.17  ? 716  ILE   A O     1 
ATOM   3370 C  CB    . ILE   A 1 567  ? 25.531  -10.229 -61.499 1.00 73.45  ? 716  ILE   A CB    1 
ATOM   3371 C  CG1   . ILE   A 1 567  ? 25.983  -8.826  -61.080 1.00 74.94  ? 716  ILE   A CG1   1 
ATOM   3372 C  CG2   . ILE   A 1 567  ? 25.995  -11.276 -60.495 1.00 74.93  ? 716  ILE   A CG2   1 
ATOM   3373 C  CD1   . ILE   A 1 567  ? 25.196  -7.707  -61.716 1.00 76.49  ? 716  ILE   A CD1   1 
ATOM   3374 N  N     . ALA   A 1 568  ? 28.128  -11.748 -62.695 1.00 70.31  ? 717  ALA   A N     1 
ATOM   3375 C  CA    . ALA   A 1 568  ? 29.597  -11.946 -62.663 1.00 68.35  ? 717  ALA   A CA    1 
ATOM   3376 C  C     . ALA   A 1 568  ? 30.092  -12.537 -63.989 1.00 67.89  ? 717  ALA   A C     1 
ATOM   3377 O  O     . ALA   A 1 568  ? 31.163  -13.164 -63.976 1.00 69.33  ? 717  ALA   A O     1 
ATOM   3378 C  CB    . ALA   A 1 568  ? 29.961  -12.836 -61.497 1.00 67.70  ? 717  ALA   A CB    1 
ATOM   3379 N  N     . GLU   A 1 569  ? 29.358  -12.323 -65.087 1.00 68.84  ? 718  GLU   A N     1 
ATOM   3380 C  CA    . GLU   A 1 569  ? 29.677  -12.854 -66.441 1.00 69.68  ? 718  GLU   A CA    1 
ATOM   3381 C  C     . GLU   A 1 569  ? 30.423  -11.783 -67.247 1.00 69.50  ? 718  GLU   A C     1 
ATOM   3382 O  O     . GLU   A 1 569  ? 31.473  -12.118 -67.830 1.00 68.38  ? 718  GLU   A O     1 
ATOM   3383 C  CB    . GLU   A 1 569  ? 28.394  -13.279 -67.157 1.00 71.91  ? 718  GLU   A CB    1 
ATOM   3384 C  CG    . GLU   A 1 569  ? 28.628  -14.151 -68.377 1.00 73.95  ? 718  GLU   A CG    1 
ATOM   3385 C  CD    . GLU   A 1 569  ? 27.355  -14.580 -69.087 1.00 76.30  ? 718  GLU   A CD    1 
ATOM   3386 O  OE1   . GLU   A 1 569  ? 27.116  -15.801 -69.190 1.00 76.74  ? 718  GLU   A OE1   1 
ATOM   3387 O  OE2   . GLU   A 1 569  ? 26.604  -13.691 -69.538 1.00 80.29  ? 718  GLU   A OE2   1 
ATOM   3388 N  N     . THR   A 1 570  ? 29.882  -10.559 -67.298 1.00 71.12  ? 719  THR   A N     1 
ATOM   3389 C  CA    . THR   A 1 570  ? 30.464  -9.400  -68.035 1.00 71.15  ? 719  THR   A CA    1 
ATOM   3390 C  C     . THR   A 1 570  ? 30.304  -8.074  -67.273 1.00 72.05  ? 719  THR   A C     1 
ATOM   3391 O  O     . THR   A 1 570  ? 30.939  -7.093  -67.703 1.00 71.43  ? 719  THR   A O     1 
ATOM   3392 C  CB    . THR   A 1 570  ? 29.823  -9.253  -69.419 1.00 71.83  ? 719  THR   A CB    1 
ATOM   3393 O  OG1   . THR   A 1 570  ? 28.438  -8.958  -69.228 1.00 73.02  ? 719  THR   A OG1   1 
ATOM   3394 C  CG2   . THR   A 1 570  ? 29.987  -10.486 -70.281 1.00 71.82  ? 719  THR   A CG2   1 
ATOM   3395 N  N     . SER   A 1 571  ? 29.498  -8.025  -66.205 1.00 75.75  ? 720  SER   A N     1 
ATOM   3396 C  CA    . SER   A 1 571  ? 29.070  -6.766  -65.534 1.00 78.86  ? 720  SER   A CA    1 
ATOM   3397 C  C     . SER   A 1 571  ? 30.050  -6.388  -64.413 1.00 79.52  ? 720  SER   A C     1 
ATOM   3398 O  O     . SER   A 1 571  ? 30.299  -5.180  -64.242 1.00 81.37  ? 720  SER   A O     1 
ATOM   3399 C  CB    . SER   A 1 571  ? 27.648  -6.865  -65.027 1.00 79.62  ? 720  SER   A CB    1 
ATOM   3400 O  OG    . SER   A 1 571  ? 27.612  -7.177  -63.642 1.00 80.62  ? 720  SER   A OG    1 
ATOM   3401 N  N     . ILE   A 1 572  ? 30.566  -7.374  -63.670 1.00 80.03  ? 721  ILE   A N     1 
ATOM   3402 C  CA    . ILE   A 1 572  ? 31.572  -7.174  -62.580 1.00 80.82  ? 721  ILE   A CA    1 
ATOM   3403 C  C     . ILE   A 1 572  ? 32.627  -8.282  -62.655 1.00 80.62  ? 721  ILE   A C     1 
ATOM   3404 O  O     . ILE   A 1 572  ? 32.296  -9.390  -63.123 1.00 80.87  ? 721  ILE   A O     1 
ATOM   3405 C  CB    . ILE   A 1 572  ? 30.894  -7.132  -61.196 1.00 81.23  ? 721  ILE   A CB    1 
ATOM   3406 C  CG1   . ILE   A 1 572  ? 30.122  -8.420  -60.900 1.00 81.57  ? 721  ILE   A CG1   1 
ATOM   3407 C  CG2   . ILE   A 1 572  ? 30.011  -5.899  -61.068 1.00 82.18  ? 721  ILE   A CG2   1 
ATOM   3408 C  CD1   . ILE   A 1 572  ? 29.681  -8.557  -59.465 1.00 82.89  ? 721  ILE   A CD1   1 
ATOM   3409 N  N     . THR   A 1 573  ? 33.845  -7.985  -62.195 1.00 80.33  ? 722  THR   A N     1 
ATOM   3410 C  CA    . THR   A 1 573  ? 34.999  -8.921  -62.163 1.00 81.26  ? 722  THR   A CA    1 
ATOM   3411 C  C     . THR   A 1 573  ? 35.460  -9.104  -60.714 1.00 82.87  ? 722  THR   A C     1 
ATOM   3412 O  O     . THR   A 1 573  ? 35.775  -8.090  -60.066 1.00 85.05  ? 722  THR   A O     1 
ATOM   3413 C  CB    . THR   A 1 573  ? 36.150  -8.419  -63.043 1.00 80.69  ? 722  THR   A CB    1 
ATOM   3414 O  OG1   . THR   A 1 573  ? 35.603  -7.952  -64.276 1.00 81.52  ? 722  THR   A OG1   1 
ATOM   3415 C  CG2   . THR   A 1 573  ? 37.186  -9.488  -63.312 1.00 79.75  ? 722  THR   A CG2   1 
ATOM   3416 N  N     . ILE   A 1 574  ? 35.488  -10.352 -60.239 1.00 84.98  ? 723  ILE   A N     1 
ATOM   3417 C  CA    . ILE   A 1 574  ? 36.001  -10.743 -58.893 1.00 86.65  ? 723  ILE   A CA    1 
ATOM   3418 C  C     . ILE   A 1 574  ? 37.454  -11.204 -59.056 1.00 89.10  ? 723  ILE   A C     1 
ATOM   3419 O  O     . ILE   A 1 574  ? 37.720  -11.990 -59.988 1.00 89.13  ? 723  ILE   A O     1 
ATOM   3420 C  CB    . ILE   A 1 574  ? 35.108  -11.831 -58.265 1.00 87.08  ? 723  ILE   A CB    1 
ATOM   3421 C  CG1   . ILE   A 1 574  ? 33.637  -11.407 -58.246 1.00 86.53  ? 723  ILE   A CG1   1 
ATOM   3422 C  CG2   . ILE   A 1 574  ? 35.608  -12.206 -56.876 1.00 88.40  ? 723  ILE   A CG2   1 
ATOM   3423 C  CD1   . ILE   A 1 574  ? 32.674  -12.534 -57.965 1.00 87.64  ? 723  ILE   A CD1   1 
ATOM   3424 N  N     . ASN   A 1 575  ? 38.351  -10.725 -58.189 1.00 93.18  ? 724  ASN   A N     1 
ATOM   3425 C  CA    . ASN   A 1 575  ? 39.813  -10.995 -58.259 1.00 96.53  ? 724  ASN   A CA    1 
ATOM   3426 C  C     . ASN   A 1 575  ? 40.138  -12.267 -57.468 1.00 97.19  ? 724  ASN   A C     1 
ATOM   3427 O  O     . ASN   A 1 575  ? 39.356  -12.627 -56.562 1.00 95.88  ? 724  ASN   A O     1 
ATOM   3428 C  CB    . ASN   A 1 575  ? 40.633  -9.799  -57.768 1.00 97.45  ? 724  ASN   A CB    1 
ATOM   3429 C  CG    . ASN   A 1 575  ? 40.517  -8.590  -58.673 1.00 100.16 ? 724  ASN   A CG    1 
ATOM   3430 O  OD1   . ASN   A 1 575  ? 40.000  -8.682  -59.785 1.00 100.49 ? 724  ASN   A OD1   1 
ATOM   3431 N  ND2   . ASN   A 1 575  ? 40.997  -7.448  -58.207 1.00 101.19 ? 724  ASN   A ND2   1 
ATOM   3432 N  N     . ASP   A 1 576  ? 41.252  -12.916 -57.823 1.00 98.30  ? 725  ASP   A N     1 
ATOM   3433 C  CA    . ASP   A 1 576  ? 41.766  -14.165 -57.197 1.00 101.42 ? 725  ASP   A CA    1 
ATOM   3434 C  C     . ASP   A 1 576  ? 40.897  -15.356 -57.630 1.00 99.10  ? 725  ASP   A C     1 
ATOM   3435 O  O     . ASP   A 1 576  ? 40.955  -16.398 -56.949 1.00 100.37 ? 725  ASP   A O     1 
ATOM   3436 C  CB    . ASP   A 1 576  ? 41.843  -14.029 -55.671 1.00 105.21 ? 725  ASP   A CB    1 
ATOM   3437 C  CG    . ASP   A 1 576  ? 42.864  -14.941 -55.005 1.00 109.10 ? 725  ASP   A CG    1 
ATOM   3438 O  OD1   . ASP   A 1 576  ? 43.672  -15.560 -55.732 1.00 108.71 ? 725  ASP   A OD1   1 
ATOM   3439 O  OD2   . ASP   A 1 576  ? 42.843  -15.025 -53.760 1.00 112.65 ? 725  ASP   A OD2   1 
ATOM   3440 N  N     . VAL   A 1 577  ? 40.144  -15.222 -58.729 1.00 95.17  ? 726  VAL   A N     1 
ATOM   3441 C  CA    . VAL   A 1 577  ? 39.296  -16.310 -59.304 1.00 92.65  ? 726  VAL   A CA    1 
ATOM   3442 C  C     . VAL   A 1 577  ? 40.160  -17.136 -60.265 1.00 91.69  ? 726  VAL   A C     1 
ATOM   3443 O  O     . VAL   A 1 577  ? 40.559  -16.598 -61.318 1.00 88.84  ? 726  VAL   A O     1 
ATOM   3444 C  CB    . VAL   A 1 577  ? 38.040  -15.754 -60.005 1.00 91.54  ? 726  VAL   A CB    1 
ATOM   3445 C  CG1   . VAL   A 1 577  ? 37.230  -16.857 -60.671 1.00 90.21  ? 726  VAL   A CG1   1 
ATOM   3446 C  CG2   . VAL   A 1 577  ? 37.167  -14.959 -59.046 1.00 90.77  ? 726  VAL   A CG2   1 
ATOM   3447 N  N     . VAL   A 1 578  ? 40.445  -18.387 -59.892 1.00 92.20  ? 727  VAL   A N     1 
ATOM   3448 C  CA    . VAL   A 1 578  ? 41.266  -19.357 -60.677 1.00 92.88  ? 727  VAL   A CA    1 
ATOM   3449 C  C     . VAL   A 1 578  ? 40.345  -20.430 -61.271 1.00 91.62  ? 727  VAL   A C     1 
ATOM   3450 O  O     . VAL   A 1 578  ? 40.632  -20.891 -62.392 1.00 93.41  ? 727  VAL   A O     1 
ATOM   3451 C  CB    . VAL   A 1 578  ? 42.365  -19.989 -59.800 1.00 93.46  ? 727  VAL   A CB    1 
ATOM   3452 C  CG1   . VAL   A 1 578  ? 43.210  -20.989 -60.576 1.00 92.62  ? 727  VAL   A CG1   1 
ATOM   3453 C  CG2   . VAL   A 1 578  ? 43.245  -18.929 -59.155 1.00 94.31  ? 727  VAL   A CG2   1 
ATOM   3454 N  N     . TYR   A 1 579  ? 39.295  -20.816 -60.539 1.00 89.11  ? 728  TYR   A N     1 
ATOM   3455 C  CA    . TYR   A 1 579  ? 38.360  -21.915 -60.896 1.00 89.32  ? 728  TYR   A CA    1 
ATOM   3456 C  C     . TYR   A 1 579  ? 36.975  -21.332 -61.199 1.00 86.53  ? 728  TYR   A C     1 
ATOM   3457 O  O     . TYR   A 1 579  ? 36.557  -20.379 -60.513 1.00 86.64  ? 728  TYR   A O     1 
ATOM   3458 C  CB    . TYR   A 1 579  ? 38.299  -22.944 -59.764 1.00 91.56  ? 728  TYR   A CB    1 
ATOM   3459 C  CG    . TYR   A 1 579  ? 39.648  -23.396 -59.264 1.00 93.98  ? 728  TYR   A CG    1 
ATOM   3460 C  CD1   . TYR   A 1 579  ? 40.299  -24.476 -59.838 1.00 94.99  ? 728  TYR   A CD1   1 
ATOM   3461 C  CD2   . TYR   A 1 579  ? 40.283  -22.735 -58.225 1.00 95.71  ? 728  TYR   A CD2   1 
ATOM   3462 C  CE1   . TYR   A 1 579  ? 41.541  -24.894 -59.388 1.00 96.35  ? 728  TYR   A CE1   1 
ATOM   3463 C  CE2   . TYR   A 1 579  ? 41.525  -23.140 -57.762 1.00 96.14  ? 728  TYR   A CE2   1 
ATOM   3464 C  CZ    . TYR   A 1 579  ? 42.157  -24.223 -58.346 1.00 96.93  ? 728  TYR   A CZ    1 
ATOM   3465 O  OH    . TYR   A 1 579  ? 43.379  -24.628 -57.893 1.00 99.34  ? 728  TYR   A OH    1 
ATOM   3466 N  N     . VAL   A 1 580  ? 36.298  -21.889 -62.208 1.00 84.08  ? 729  VAL   A N     1 
ATOM   3467 C  CA    . VAL   A 1 580  ? 34.906  -21.520 -62.607 1.00 82.14  ? 729  VAL   A CA    1 
ATOM   3468 C  C     . VAL   A 1 580  ? 34.110  -22.809 -62.842 1.00 79.45  ? 729  VAL   A C     1 
ATOM   3469 O  O     . VAL   A 1 580  ? 34.465  -23.553 -63.772 1.00 79.88  ? 729  VAL   A O     1 
ATOM   3470 C  CB    . VAL   A 1 580  ? 34.891  -20.614 -63.855 1.00 81.19  ? 729  VAL   A CB    1 
ATOM   3471 C  CG1   . VAL   A 1 580  ? 33.472  -20.323 -64.321 1.00 81.66  ? 729  VAL   A CG1   1 
ATOM   3472 C  CG2   . VAL   A 1 580  ? 35.652  -19.316 -63.626 1.00 80.71  ? 729  VAL   A CG2   1 
ATOM   3473 N  N     . ILE   A 1 581  ? 33.089  -23.060 -62.018 1.00 78.25  ? 730  ILE   A N     1 
ATOM   3474 C  CA    . ILE   A 1 581  ? 32.105  -24.170 -62.200 1.00 81.20  ? 730  ILE   A CA    1 
ATOM   3475 C  C     . ILE   A 1 581  ? 30.861  -23.579 -62.873 1.00 81.64  ? 730  ILE   A C     1 
ATOM   3476 O  O     . ILE   A 1 581  ? 30.131  -22.821 -62.205 1.00 84.64  ? 730  ILE   A O     1 
ATOM   3477 C  CB    . ILE   A 1 581  ? 31.785  -24.863 -60.857 1.00 83.53  ? 730  ILE   A CB    1 
ATOM   3478 C  CG1   . ILE   A 1 581  ? 32.999  -25.629 -60.321 1.00 83.99  ? 730  ILE   A CG1   1 
ATOM   3479 C  CG2   . ILE   A 1 581  ? 30.564  -25.765 -60.981 1.00 82.88  ? 730  ILE   A CG2   1 
ATOM   3480 C  CD1   . ILE   A 1 581  ? 32.848  -26.112 -58.895 1.00 84.15  ? 730  ILE   A CD1   1 
ATOM   3481 N  N     . ASP   A 1 582  ? 30.646  -23.911 -64.151 1.00 79.45  ? 731  ASP   A N     1 
ATOM   3482 C  CA    . ASP   A 1 582  ? 29.585  -23.331 -65.017 1.00 76.82  ? 731  ASP   A CA    1 
ATOM   3483 C  C     . ASP   A 1 582  ? 28.445  -24.342 -65.169 1.00 75.13  ? 731  ASP   A C     1 
ATOM   3484 O  O     . ASP   A 1 582  ? 28.703  -25.450 -65.678 1.00 74.26  ? 731  ASP   A O     1 
ATOM   3485 C  CB    . ASP   A 1 582  ? 30.162  -22.936 -66.379 1.00 77.86  ? 731  ASP   A CB    1 
ATOM   3486 C  CG    . ASP   A 1 582  ? 29.209  -22.156 -67.269 1.00 78.31  ? 731  ASP   A CG    1 
ATOM   3487 O  OD1   . ASP   A 1 582  ? 28.054  -21.933 -66.853 1.00 77.22  ? 731  ASP   A OD1   1 
ATOM   3488 O  OD2   . ASP   A 1 582  ? 29.635  -21.772 -68.375 1.00 81.77  ? 731  ASP   A OD2   1 
ATOM   3489 N  N     . SER   A 1 583  ? 27.233  -23.960 -64.753 1.00 74.14  ? 732  SER   A N     1 
ATOM   3490 C  CA    . SER   A 1 583  ? 25.981  -24.744 -64.922 1.00 74.67  ? 732  SER   A CA    1 
ATOM   3491 C  C     . SER   A 1 583  ? 25.573  -24.767 -66.400 1.00 75.72  ? 732  SER   A C     1 
ATOM   3492 O  O     . SER   A 1 583  ? 24.905  -25.737 -66.804 1.00 76.55  ? 732  SER   A O     1 
ATOM   3493 C  CB    . SER   A 1 583  ? 24.875  -24.191 -64.060 1.00 74.31  ? 732  SER   A CB    1 
ATOM   3494 O  OG    . SER   A 1 583  ? 24.614  -22.833 -64.381 1.00 74.48  ? 732  SER   A OG    1 
ATOM   3495 N  N     . CYS   A 1 584  ? 25.963  -23.735 -67.160 1.00 77.42  ? 733  CYS   A N     1 
ATOM   3496 C  CA    . CYS   A 1 584  ? 25.654  -23.533 -68.604 1.00 78.85  ? 733  CYS   A CA    1 
ATOM   3497 C  C     . CYS   A 1 584  ? 24.164  -23.210 -68.783 1.00 78.81  ? 733  CYS   A C     1 
ATOM   3498 O  O     . CYS   A 1 584  ? 23.611  -23.552 -69.848 1.00 79.39  ? 733  CYS   A O     1 
ATOM   3499 C  CB    . CYS   A 1 584  ? 26.031  -24.753 -69.440 1.00 79.90  ? 733  CYS   A CB    1 
ATOM   3500 S  SG    . CYS   A 1 584  ? 27.756  -25.266 -69.242 1.00 80.95  ? 733  CYS   A SG    1 
ATOM   3501 N  N     . LYS   A 1 585  ? 23.551  -22.563 -67.785 1.00 77.69  ? 734  LYS   A N     1 
ATOM   3502 C  CA    . LYS   A 1 585  ? 22.108  -22.198 -67.767 1.00 76.97  ? 734  LYS   A CA    1 
ATOM   3503 C  C     . LYS   A 1 585  ? 21.962  -20.676 -67.648 1.00 76.59  ? 734  LYS   A C     1 
ATOM   3504 O  O     . LYS   A 1 585  ? 22.950  -20.010 -67.275 1.00 75.65  ? 734  LYS   A O     1 
ATOM   3505 C  CB    . LYS   A 1 585  ? 21.398  -22.894 -66.601 1.00 77.28  ? 734  LYS   A CB    1 
ATOM   3506 C  CG    . LYS   A 1 585  ? 21.552  -24.409 -66.550 1.00 78.09  ? 734  LYS   A CG    1 
ATOM   3507 C  CD    . LYS   A 1 585  ? 21.109  -25.114 -67.817 1.00 78.62  ? 734  LYS   A CD    1 
ATOM   3508 C  CE    . LYS   A 1 585  ? 20.626  -26.529 -67.578 1.00 79.29  ? 734  LYS   A CE    1 
ATOM   3509 N  NZ    . LYS   A 1 585  ? 19.269  -26.555 -66.978 1.00 79.06  ? 734  LYS   A NZ    1 
ATOM   3510 N  N     . GLN   A 1 586  ? 20.769  -20.162 -67.964 1.00 77.76  ? 735  GLN   A N     1 
ATOM   3511 C  CA    . GLN   A 1 586  ? 20.378  -18.732 -67.826 1.00 79.08  ? 735  GLN   A CA    1 
ATOM   3512 C  C     . GLN   A 1 586  ? 18.946  -18.661 -67.283 1.00 77.82  ? 735  GLN   A C     1 
ATOM   3513 O  O     . GLN   A 1 586  ? 18.129  -19.514 -67.682 1.00 77.02  ? 735  GLN   A O     1 
ATOM   3514 C  CB    . GLN   A 1 586  ? 20.455  -18.016 -69.177 1.00 81.34  ? 735  GLN   A CB    1 
ATOM   3515 C  CG    . GLN   A 1 586  ? 21.872  -17.768 -69.675 1.00 83.68  ? 735  GLN   A CG    1 
ATOM   3516 C  CD    . GLN   A 1 586  ? 22.491  -16.518 -69.095 1.00 86.79  ? 735  GLN   A CD    1 
ATOM   3517 O  OE1   . GLN   A 1 586  ? 22.146  -16.080 -68.000 1.00 89.80  ? 735  GLN   A OE1   1 
ATOM   3518 N  NE2   . GLN   A 1 586  ? 23.423  -15.932 -69.831 1.00 87.28  ? 735  GLN   A NE2   1 
ATOM   3519 N  N     . LYS   A 1 587  ? 18.657  -17.692 -66.410 1.00 78.40  ? 736  LYS   A N     1 
ATOM   3520 C  CA    . LYS   A 1 587  ? 17.275  -17.380 -65.955 1.00 80.67  ? 736  LYS   A CA    1 
ATOM   3521 C  C     . LYS   A 1 587  ? 16.764  -16.175 -66.750 1.00 81.62  ? 736  LYS   A C     1 
ATOM   3522 O  O     . LYS   A 1 587  ? 17.316  -15.070 -66.571 1.00 81.69  ? 736  LYS   A O     1 
ATOM   3523 C  CB    . LYS   A 1 587  ? 17.210  -17.113 -64.448 1.00 82.50  ? 736  LYS   A CB    1 
ATOM   3524 C  CG    . LYS   A 1 587  ? 15.806  -17.188 -63.859 1.00 84.26  ? 736  LYS   A CG    1 
ATOM   3525 C  CD    . LYS   A 1 587  ? 15.734  -16.920 -62.373 1.00 86.51  ? 736  LYS   A CD    1 
ATOM   3526 C  CE    . LYS   A 1 587  ? 15.716  -15.444 -62.034 1.00 88.47  ? 736  LYS   A CE    1 
ATOM   3527 N  NZ    . LYS   A 1 587  ? 15.552  -15.216 -60.578 1.00 89.00  ? 736  LYS   A NZ    1 
ATOM   3528 N  N     . VAL   A 1 588  ? 15.759  -16.401 -67.601 1.00 82.89  ? 737  VAL   A N     1 
ATOM   3529 C  CA    . VAL   A 1 588  ? 15.076  -15.361 -68.427 1.00 82.16  ? 737  VAL   A CA    1 
ATOM   3530 C  C     . VAL   A 1 588  ? 13.576  -15.430 -68.130 1.00 80.38  ? 737  VAL   A C     1 
ATOM   3531 O  O     . VAL   A 1 588  ? 13.058  -16.554 -67.976 1.00 78.47  ? 737  VAL   A O     1 
ATOM   3532 C  CB    . VAL   A 1 588  ? 15.367  -15.542 -69.931 1.00 84.46  ? 737  VAL   A CB    1 
ATOM   3533 C  CG1   . VAL   A 1 588  ? 16.853  -15.422 -70.234 1.00 85.78  ? 737  VAL   A CG1   1 
ATOM   3534 C  CG2   . VAL   A 1 588  ? 14.816  -16.853 -70.480 1.00 84.50  ? 737  VAL   A CG2   1 
ATOM   3535 N  N     . LYS   A 1 589  ? 12.916  -14.272 -68.036 1.00 81.52  ? 738  LYS   A N     1 
ATOM   3536 C  CA    . LYS   A 1 589  ? 11.448  -14.169 -67.826 1.00 82.82  ? 738  LYS   A CA    1 
ATOM   3537 C  C     . LYS   A 1 589  ? 10.753  -14.208 -69.191 1.00 81.80  ? 738  LYS   A C     1 
ATOM   3538 O  O     . LYS   A 1 589  ? 10.681  -13.153 -69.848 1.00 83.54  ? 738  LYS   A O     1 
ATOM   3539 C  CB    . LYS   A 1 589  ? 11.087  -12.896 -67.052 1.00 84.86  ? 738  LYS   A CB    1 
ATOM   3540 C  CG    . LYS   A 1 589  ? 9.627   -12.812 -66.624 1.00 87.69  ? 738  LYS   A CG    1 
ATOM   3541 C  CD    . LYS   A 1 589  ? 9.261   -11.554 -65.865 1.00 88.20  ? 738  LYS   A CD    1 
ATOM   3542 C  CE    . LYS   A 1 589  ? 7.855   -11.611 -65.305 1.00 89.21  ? 738  LYS   A CE    1 
ATOM   3543 N  NZ    . LYS   A 1 589  ? 7.424   -10.304 -64.758 1.00 91.15  ? 738  LYS   A NZ    1 
ATOM   3544 N  N     . LEU   A 1 590  ? 10.287  -15.390 -69.605 1.00 82.37  ? 739  LEU   A N     1 
ATOM   3545 C  CA    . LEU   A 1 590  ? 9.420   -15.575 -70.800 1.00 84.22  ? 739  LEU   A CA    1 
ATOM   3546 C  C     . LEU   A 1 590  ? 7.971   -15.300 -70.389 1.00 83.07  ? 739  LEU   A C     1 
ATOM   3547 O  O     . LEU   A 1 590  ? 7.545   -15.825 -69.344 1.00 83.15  ? 739  LEU   A O     1 
ATOM   3548 C  CB    . LEU   A 1 590  ? 9.579   -16.999 -71.343 1.00 86.83  ? 739  LEU   A CB    1 
ATOM   3549 C  CG    . LEU   A 1 590  ? 10.981  -17.378 -71.822 1.00 88.70  ? 739  LEU   A CG    1 
ATOM   3550 C  CD1   . LEU   A 1 590  ? 11.011  -18.818 -72.314 1.00 87.99  ? 739  LEU   A CD1   1 
ATOM   3551 C  CD2   . LEU   A 1 590  ? 11.466  -16.432 -72.912 1.00 89.75  ? 739  LEU   A CD2   1 
ATOM   3552 N  N     . PHE   A 1 591  ? 7.258   -14.487 -71.172 1.00 83.67  ? 740  PHE   A N     1 
ATOM   3553 C  CA    . PHE   A 1 591  ? 5.834   -14.127 -70.955 1.00 85.88  ? 740  PHE   A CA    1 
ATOM   3554 C  C     . PHE   A 1 591  ? 5.063   -14.359 -72.257 1.00 86.19  ? 740  PHE   A C     1 
ATOM   3555 O  O     . PHE   A 1 591  ? 5.350   -13.663 -73.250 1.00 88.89  ? 740  PHE   A O     1 
ATOM   3556 C  CB    . PHE   A 1 591  ? 5.709   -12.676 -70.481 1.00 88.53  ? 740  PHE   A CB    1 
ATOM   3557 C  CG    . PHE   A 1 591  ? 4.292   -12.171 -70.350 1.00 91.09  ? 740  PHE   A CG    1 
ATOM   3558 C  CD1   . PHE   A 1 591  ? 3.542   -12.434 -69.212 1.00 90.56  ? 740  PHE   A CD1   1 
ATOM   3559 C  CD2   . PHE   A 1 591  ? 3.705   -11.432 -71.367 1.00 92.86  ? 740  PHE   A CD2   1 
ATOM   3560 C  CE1   . PHE   A 1 591  ? 2.240   -11.968 -69.097 1.00 90.00  ? 740  PHE   A CE1   1 
ATOM   3561 C  CE2   . PHE   A 1 591  ? 2.403   -10.968 -71.250 1.00 91.49  ? 740  PHE   A CE2   1 
ATOM   3562 C  CZ    . PHE   A 1 591  ? 1.674   -11.236 -70.116 1.00 90.12  ? 740  PHE   A CZ    1 
ATOM   3563 N  N     . THR   A 1 592  ? 4.131   -15.317 -72.248 1.00 85.38  ? 741  THR   A N     1 
ATOM   3564 C  CA    . THR   A 1 592  ? 3.171   -15.579 -73.353 1.00 87.17  ? 741  THR   A CA    1 
ATOM   3565 C  C     . THR   A 1 592  ? 1.848   -14.885 -73.011 1.00 85.86  ? 741  THR   A C     1 
ATOM   3566 O  O     . THR   A 1 592  ? 1.232   -15.264 -71.997 1.00 83.19  ? 741  THR   A O     1 
ATOM   3567 C  CB    . THR   A 1 592  ? 3.009   -17.083 -73.606 1.00 88.36  ? 741  THR   A CB    1 
ATOM   3568 O  OG1   . THR   A 1 592  ? 2.664   -17.709 -72.370 1.00 87.67  ? 741  THR   A OG1   1 
ATOM   3569 C  CG2   . THR   A 1 592  ? 4.258   -17.719 -74.177 1.00 87.87  ? 741  THR   A CG2   1 
ATOM   3570 N  N     . ALA   A 1 593  ? 1.448   -13.903 -73.827 1.00 87.32  ? 742  ALA   A N     1 
ATOM   3571 C  CA    . ALA   A 1 593  ? 0.318   -12.978 -73.572 1.00 90.12  ? 742  ALA   A CA    1 
ATOM   3572 C  C     . ALA   A 1 593  ? -1.025  -13.707 -73.710 1.00 91.37  ? 742  ALA   A C     1 
ATOM   3573 O  O     . ALA   A 1 593  ? -1.970  -13.321 -72.992 1.00 90.85  ? 742  ALA   A O     1 
ATOM   3574 C  CB    . ALA   A 1 593  ? 0.400   -11.796 -74.509 1.00 89.47  ? 742  ALA   A CB    1 
ATOM   3575 N  N     . HIS   A 1 594  ? -1.103  -14.720 -74.583 1.00 94.34  ? 743  HIS   A N     1 
ATOM   3576 C  CA    . HIS   A 1 594  ? -2.359  -15.435 -74.949 1.00 96.94  ? 743  HIS   A CA    1 
ATOM   3577 C  C     . HIS   A 1 594  ? -2.989  -16.076 -73.703 1.00 100.46 ? 743  HIS   A C     1 
ATOM   3578 O  O     . HIS   A 1 594  ? -4.225  -15.980 -73.561 1.00 104.25 ? 743  HIS   A O     1 
ATOM   3579 C  CB    . HIS   A 1 594  ? -2.112  -16.442 -76.088 1.00 94.75  ? 743  HIS   A CB    1 
ATOM   3580 C  CG    . HIS   A 1 594  ? -1.517  -17.745 -75.663 1.00 93.91  ? 743  HIS   A CG    1 
ATOM   3581 N  ND1   . HIS   A 1 594  ? -0.151  -17.953 -75.605 1.00 92.33  ? 743  HIS   A ND1   1 
ATOM   3582 C  CD2   . HIS   A 1 594  ? -2.095  -18.911 -75.295 1.00 91.23  ? 743  HIS   A CD2   1 
ATOM   3583 C  CE1   . HIS   A 1 594  ? 0.087   -19.188 -75.211 1.00 90.71  ? 743  HIS   A CE1   1 
ATOM   3584 N  NE2   . HIS   A 1 594  ? -1.090  -19.796 -75.013 1.00 90.92  ? 743  HIS   A NE2   1 
ATOM   3585 N  N     . ASN   A 1 595  ? -2.174  -16.691 -72.836 1.00 102.50 ? 744  ASN   A N     1 
ATOM   3586 C  CA    . ASN   A 1 595  ? -2.618  -17.389 -71.596 1.00 102.46 ? 744  ASN   A CA    1 
ATOM   3587 C  C     . ASN   A 1 595  ? -2.095  -16.651 -70.353 1.00 103.65 ? 744  ASN   A C     1 
ATOM   3588 O  O     . ASN   A 1 595  ? -2.359  -17.138 -69.233 1.00 104.83 ? 744  ASN   A O     1 
ATOM   3589 C  CB    . ASN   A 1 595  ? -2.195  -18.863 -71.596 1.00 101.97 ? 744  ASN   A CB    1 
ATOM   3590 C  CG    . ASN   A 1 595  ? -0.705  -19.069 -71.780 1.00 101.88 ? 744  ASN   A CG    1 
ATOM   3591 O  OD1   . ASN   A 1 595  ? 0.010   -18.165 -72.208 1.00 102.58 ? 744  ASN   A OD1   1 
ATOM   3592 N  ND2   . ASN   A 1 595  ? -0.227  -20.263 -71.469 1.00 101.22 ? 744  ASN   A ND2   1 
ATOM   3593 N  N     . ASN   A 1 596  ? -1.391  -15.526 -70.542 1.00 102.07 ? 745  ASN   A N     1 
ATOM   3594 C  CA    . ASN   A 1 596  ? -0.855  -14.650 -69.465 1.00 100.11 ? 745  ASN   A CA    1 
ATOM   3595 C  C     . ASN   A 1 596  ? 0.057   -15.474 -68.543 1.00 99.51  ? 745  ASN   A C     1 
ATOM   3596 O  O     . ASN   A 1 596  ? -0.078  -15.356 -67.305 1.00 99.03  ? 745  ASN   A O     1 
ATOM   3597 C  CB    . ASN   A 1 596  ? -1.988  -13.953 -68.704 1.00 98.26  ? 745  ASN   A CB    1 
ATOM   3598 C  CG    . ASN   A 1 596  ? -1.529  -12.708 -67.973 1.00 97.00  ? 745  ASN   A CG    1 
ATOM   3599 O  OD1   . ASN   A 1 596  ? -1.126  -11.730 -68.596 1.00 94.78  ? 745  ASN   A OD1   1 
ATOM   3600 N  ND2   . ASN   A 1 596  ? -1.594  -12.731 -66.652 1.00 97.72  ? 745  ASN   A ND2   1 
ATOM   3601 N  N     . MET   A 1 597  ? 0.963   -16.261 -69.133 1.00 98.67  ? 746  MET   A N     1 
ATOM   3602 C  CA    . MET   A 1 597  ? 1.867   -17.203 -68.417 1.00 98.30  ? 746  MET   A CA    1 
ATOM   3603 C  C     . MET   A 1 597  ? 3.259   -16.573 -68.277 1.00 96.56  ? 746  MET   A C     1 
ATOM   3604 O  O     . MET   A 1 597  ? 3.930   -16.382 -69.311 1.00 96.20  ? 746  MET   A O     1 
ATOM   3605 C  CB    . MET   A 1 597  ? 1.979   -18.530 -69.178 1.00 99.38  ? 746  MET   A CB    1 
ATOM   3606 C  CG    . MET   A 1 597  ? 2.554   -19.666 -68.353 1.00 99.27  ? 746  MET   A CG    1 
ATOM   3607 S  SD    . MET   A 1 597  ? 1.360   -20.334 -67.169 1.00 101.89 ? 746  MET   A SD    1 
ATOM   3608 C  CE    . MET   A 1 597  ? 0.244   -21.202 -68.269 1.00 101.65 ? 746  MET   A CE    1 
ATOM   3609 N  N     . THR   A 1 598  ? 3.661   -16.253 -67.042 1.00 94.12  ? 747  THR   A N     1 
ATOM   3610 C  CA    . THR   A 1 598  ? 5.054   -15.895 -66.663 1.00 91.85  ? 747  THR   A CA    1 
ATOM   3611 C  C     . THR   A 1 598  ? 5.829   -17.195 -66.423 1.00 91.00  ? 747  THR   A C     1 
ATOM   3612 O  O     . THR   A 1 598  ? 5.372   -18.002 -65.595 1.00 90.62  ? 747  THR   A O     1 
ATOM   3613 C  CB    . THR   A 1 598  ? 5.091   -14.979 -65.432 1.00 89.70  ? 747  THR   A CB    1 
ATOM   3614 O  OG1   . THR   A 1 598  ? 4.565   -13.707 -65.809 1.00 88.52  ? 747  THR   A OG1   1 
ATOM   3615 C  CG2   . THR   A 1 598  ? 6.482   -14.795 -64.865 1.00 89.25  ? 747  THR   A CG2   1 
ATOM   3616 N  N     . ASN   A 1 599  ? 6.940   -17.392 -67.138 1.00 92.82  ? 748  ASN   A N     1 
ATOM   3617 C  CA    . ASN   A 1 599  ? 7.844   -18.563 -66.984 1.00 93.99  ? 748  ASN   A CA    1 
ATOM   3618 C  C     . ASN   A 1 599  ? 9.258   -18.045 -66.696 1.00 94.01  ? 748  ASN   A C     1 
ATOM   3619 O  O     . ASN   A 1 599  ? 9.913   -17.561 -67.640 1.00 97.37  ? 748  ASN   A O     1 
ATOM   3620 C  CB    . ASN   A 1 599  ? 7.799   -19.481 -68.211 1.00 93.89  ? 748  ASN   A CB    1 
ATOM   3621 C  CG    . ASN   A 1 599  ? 8.577   -20.772 -68.041 1.00 94.35  ? 748  ASN   A CG    1 
ATOM   3622 O  OD1   . ASN   A 1 599  ? 9.221   -20.997 -67.018 1.00 93.04  ? 748  ASN   A OD1   1 
ATOM   3623 N  ND2   . ASN   A 1 599  ? 8.530   -21.632 -69.047 1.00 95.51  ? 748  ASN   A ND2   1 
ATOM   3624 N  N     . TYR   A 1 600  ? 9.693   -18.126 -65.435 1.00 91.57  ? 749  TYR   A N     1 
ATOM   3625 C  CA    . TYR   A 1 600  ? 11.100  -17.911 -65.010 1.00 91.80  ? 749  TYR   A CA    1 
ATOM   3626 C  C     . TYR   A 1 600  ? 11.890  -19.174 -65.370 1.00 90.23  ? 749  TYR   A C     1 
ATOM   3627 O  O     . TYR   A 1 600  ? 12.333  -19.906 -64.463 1.00 92.54  ? 749  TYR   A O     1 
ATOM   3628 C  CB    . TYR   A 1 600  ? 11.168  -17.556 -63.523 1.00 93.53  ? 749  TYR   A CB    1 
ATOM   3629 C  CG    . TYR   A 1 600  ? 10.558  -16.222 -63.176 1.00 94.56  ? 749  TYR   A CG    1 
ATOM   3630 C  CD1   . TYR   A 1 600  ? 11.274  -15.045 -63.336 1.00 94.65  ? 749  TYR   A CD1   1 
ATOM   3631 C  CD2   . TYR   A 1 600  ? 9.262   -16.131 -62.692 1.00 94.45  ? 749  TYR   A CD2   1 
ATOM   3632 C  CE1   . TYR   A 1 600  ? 10.723  -13.814 -63.021 1.00 94.15  ? 749  TYR   A CE1   1 
ATOM   3633 C  CE2   . TYR   A 1 600  ? 8.696   -14.908 -62.371 1.00 94.63  ? 749  TYR   A CE2   1 
ATOM   3634 C  CZ    . TYR   A 1 600  ? 9.428   -13.745 -62.537 1.00 94.58  ? 749  TYR   A CZ    1 
ATOM   3635 O  OH    . TYR   A 1 600  ? 8.878   -12.535 -62.223 1.00 96.02  ? 749  TYR   A OH    1 
ATOM   3636 N  N     . ALA   A 1 601  ? 12.040  -19.412 -66.676 1.00 86.83  ? 750  ALA   A N     1 
ATOM   3637 C  CA    . ALA   A 1 601  ? 12.551  -20.669 -67.268 1.00 85.55  ? 750  ALA   A CA    1 
ATOM   3638 C  C     . ALA   A 1 601  ? 14.065  -20.764 -67.060 1.00 81.89  ? 750  ALA   A C     1 
ATOM   3639 O  O     . ALA   A 1 601  ? 14.737  -19.716 -67.088 1.00 79.51  ? 750  ALA   A O     1 
ATOM   3640 C  CB    . ALA   A 1 601  ? 12.198  -20.732 -68.735 1.00 86.47  ? 750  ALA   A CB    1 
ATOM   3641 N  N     . THR   A 1 602  ? 14.559  -21.986 -66.849 1.00 80.29  ? 751  THR   A N     1 
ATOM   3642 C  CA    . THR   A 1 602  ? 16.002  -22.338 -66.804 1.00 81.05  ? 751  THR   A CA    1 
ATOM   3643 C  C     . THR   A 1 602  ? 16.393  -22.861 -68.190 1.00 81.16  ? 751  THR   A C     1 
ATOM   3644 O  O     . THR   A 1 602  ? 16.409  -24.097 -68.386 1.00 84.18  ? 751  THR   A O     1 
ATOM   3645 C  CB    . THR   A 1 602  ? 16.286  -23.327 -65.664 1.00 80.65  ? 751  THR   A CB    1 
ATOM   3646 O  OG1   . THR   A 1 602  ? 15.824  -22.734 -64.450 1.00 77.53  ? 751  THR   A OG1   1 
ATOM   3647 C  CG2   . THR   A 1 602  ? 17.751  -23.683 -65.534 1.00 80.90  ? 751  THR   A CG2   1 
ATOM   3648 N  N     . VAL   A 1 603  ? 16.662  -21.943 -69.120 1.00 78.43  ? 752  VAL   A N     1 
ATOM   3649 C  CA    . VAL   A 1 603  ? 17.011  -22.254 -70.537 1.00 78.62  ? 752  VAL   A CA    1 
ATOM   3650 C  C     . VAL   A 1 603  ? 18.535  -22.362 -70.657 1.00 76.81  ? 752  VAL   A C     1 
ATOM   3651 O  O     . VAL   A 1 603  ? 19.241  -21.846 -69.768 1.00 74.18  ? 752  VAL   A O     1 
ATOM   3652 C  CB    . VAL   A 1 603  ? 16.432  -21.210 -71.514 1.00 80.73  ? 752  VAL   A CB    1 
ATOM   3653 C  CG1   . VAL   A 1 603  ? 14.919  -21.107 -71.385 1.00 81.57  ? 752  VAL   A CG1   1 
ATOM   3654 C  CG2   . VAL   A 1 603  ? 17.079  -19.840 -71.359 1.00 80.88  ? 752  VAL   A CG2   1 
ATOM   3655 N  N     . TRP   A 1 604  ? 19.005  -23.017 -71.721 1.00 76.83  ? 753  TRP   A N     1 
ATOM   3656 C  CA    . TRP   A 1 604  ? 20.444  -23.199 -72.046 1.00 76.46  ? 753  TRP   A CA    1 
ATOM   3657 C  C     . TRP   A 1 604  ? 21.089  -21.839 -72.325 1.00 74.95  ? 753  TRP   A C     1 
ATOM   3658 O  O     . TRP   A 1 604  ? 20.420  -20.970 -72.920 1.00 75.43  ? 753  TRP   A O     1 
ATOM   3659 C  CB    . TRP   A 1 604  ? 20.614  -24.145 -73.239 1.00 79.92  ? 753  TRP   A CB    1 
ATOM   3660 C  CG    . TRP   A 1 604  ? 20.273  -25.565 -72.921 1.00 82.23  ? 753  TRP   A CG    1 
ATOM   3661 C  CD1   . TRP   A 1 604  ? 19.189  -26.272 -73.351 1.00 84.54  ? 753  TRP   A CD1   1 
ATOM   3662 C  CD2   . TRP   A 1 604  ? 21.023  -26.453 -72.077 1.00 84.73  ? 753  TRP   A CD2   1 
ATOM   3663 N  NE1   . TRP   A 1 604  ? 19.218  -27.542 -72.842 1.00 86.09  ? 753  TRP   A NE1   1 
ATOM   3664 C  CE2   . TRP   A 1 604  ? 20.329  -27.681 -72.053 1.00 86.85  ? 753  TRP   A CE2   1 
ATOM   3665 C  CE3   . TRP   A 1 604  ? 22.209  -26.330 -71.344 1.00 86.56  ? 753  TRP   A CE3   1 
ATOM   3666 C  CZ2   . TRP   A 1 604  ? 20.789  -28.777 -71.325 1.00 88.06  ? 753  TRP   A CZ2   1 
ATOM   3667 C  CZ3   . TRP   A 1 604  ? 22.661  -27.414 -70.624 1.00 87.46  ? 753  TRP   A CZ3   1 
ATOM   3668 C  CH2   . TRP   A 1 604  ? 21.958  -28.620 -70.615 1.00 88.54  ? 753  TRP   A CH2   1 
ATOM   3669 N  N     . ALA   A 1 605  ? 22.347  -21.678 -71.910 1.00 72.65  ? 754  ALA   A N     1 
ATOM   3670 C  CA    . ALA   A 1 605  ? 23.196  -20.506 -72.214 1.00 71.39  ? 754  ALA   A CA    1 
ATOM   3671 C  C     . ALA   A 1 605  ? 23.702  -20.629 -73.654 1.00 69.23  ? 754  ALA   A C     1 
ATOM   3672 O  O     . ALA   A 1 605  ? 23.600  -21.733 -74.220 1.00 67.23  ? 754  ALA   A O     1 
ATOM   3673 C  CB    . ALA   A 1 605  ? 24.333  -20.421 -71.226 1.00 72.64  ? 754  ALA   A CB    1 
ATOM   3674 N  N     . SER   A 1 606  ? 24.211  -19.531 -74.217 1.00 69.32  ? 755  SER   A N     1 
ATOM   3675 C  CA    . SER   A 1 606  ? 24.807  -19.468 -75.577 1.00 70.75  ? 755  SER   A CA    1 
ATOM   3676 C  C     . SER   A 1 606  ? 26.253  -19.975 -75.525 1.00 73.83  ? 755  SER   A C     1 
ATOM   3677 O  O     . SER   A 1 606  ? 26.773  -20.158 -74.410 1.00 75.26  ? 755  SER   A O     1 
ATOM   3678 C  CB    . SER   A 1 606  ? 24.728  -18.069 -76.135 1.00 70.39  ? 755  SER   A CB    1 
ATOM   3679 O  OG    . SER   A 1 606  ? 25.698  -17.221 -75.538 1.00 69.84  ? 755  SER   A OG    1 
ATOM   3680 N  N     . LYS   A 1 607  ? 26.869  -20.202 -76.690 1.00 77.82  ? 756  LYS   A N     1 
ATOM   3681 C  CA    . LYS   A 1 607  ? 28.320  -20.511 -76.817 1.00 78.63  ? 756  LYS   A CA    1 
ATOM   3682 C  C     . LYS   A 1 607  ? 29.119  -19.299 -76.327 1.00 77.29  ? 756  LYS   A C     1 
ATOM   3683 O  O     . LYS   A 1 607  ? 30.134  -19.506 -75.634 1.00 76.93  ? 756  LYS   A O     1 
ATOM   3684 C  CB    . LYS   A 1 607  ? 28.698  -20.856 -78.262 1.00 80.42  ? 756  LYS   A CB    1 
ATOM   3685 C  CG    . LYS   A 1 607  ? 28.391  -22.282 -78.701 1.00 80.92  ? 756  LYS   A CG    1 
ATOM   3686 C  CD    . LYS   A 1 607  ? 29.068  -22.659 -80.004 1.00 83.32  ? 756  LYS   A CD    1 
ATOM   3687 C  CE    . LYS   A 1 607  ? 28.918  -24.122 -80.365 1.00 84.69  ? 756  LYS   A CE    1 
ATOM   3688 N  NZ    . LYS   A 1 607  ? 27.529  -24.454 -80.760 1.00 86.30  ? 756  LYS   A NZ    1 
ATOM   3689 N  N     . THR   A 1 608  ? 28.665  -18.089 -76.678 1.00 75.95  ? 757  THR   A N     1 
ATOM   3690 C  CA    . THR   A 1 608  ? 29.286  -16.793 -76.289 1.00 77.29  ? 757  THR   A CA    1 
ATOM   3691 C  C     . THR   A 1 608  ? 29.312  -16.678 -74.759 1.00 76.41  ? 757  THR   A C     1 
ATOM   3692 O  O     . THR   A 1 608  ? 30.342  -16.219 -74.228 1.00 77.44  ? 757  THR   A O     1 
ATOM   3693 C  CB    . THR   A 1 608  ? 28.556  -15.604 -76.930 1.00 77.11  ? 757  THR   A CB    1 
ATOM   3694 O  OG1   . THR   A 1 608  ? 28.369  -15.881 -78.318 1.00 76.99  ? 757  THR   A OG1   1 
ATOM   3695 C  CG2   . THR   A 1 608  ? 29.307  -14.299 -76.780 1.00 76.15  ? 757  THR   A CG2   1 
ATOM   3696 N  N     . ASN   A 1 609  ? 28.230  -17.085 -74.086 1.00 74.52  ? 758  ASN   A N     1 
ATOM   3697 C  CA    . ASN   A 1 609  ? 28.115  -17.080 -72.601 1.00 74.76  ? 758  ASN   A CA    1 
ATOM   3698 C  C     . ASN   A 1 609  ? 29.215  -17.968 -72.007 1.00 76.10  ? 758  ASN   A C     1 
ATOM   3699 O  O     . ASN   A 1 609  ? 30.000  -17.463 -71.182 1.00 80.28  ? 758  ASN   A O     1 
ATOM   3700 C  CB    . ASN   A 1 609  ? 26.741  -17.554 -72.120 1.00 74.44  ? 758  ASN   A CB    1 
ATOM   3701 C  CG    . ASN   A 1 609  ? 25.604  -16.631 -72.507 1.00 74.91  ? 758  ASN   A CG    1 
ATOM   3702 O  OD1   . ASN   A 1 609  ? 24.592  -17.082 -73.036 1.00 74.37  ? 758  ASN   A OD1   1 
ATOM   3703 N  ND2   . ASN   A 1 609  ? 25.754  -15.342 -72.246 1.00 75.98  ? 758  ASN   A ND2   1 
ATOM   3704 N  N     . LEU   A 1 610  ? 29.266  -19.238 -72.425 1.00 75.86  ? 759  LEU   A N     1 
ATOM   3705 C  CA    . LEU   A 1 610  ? 30.214  -20.267 -71.910 1.00 74.97  ? 759  LEU   A CA    1 
ATOM   3706 C  C     . LEU   A 1 610  ? 31.664  -19.835 -72.168 1.00 76.95  ? 759  LEU   A C     1 
ATOM   3707 O  O     . LEU   A 1 610  ? 32.529  -20.194 -71.350 1.00 77.87  ? 759  LEU   A O     1 
ATOM   3708 C  CB    . LEU   A 1 610  ? 29.913  -21.618 -72.569 1.00 74.09  ? 759  LEU   A CB    1 
ATOM   3709 C  CG    . LEU   A 1 610  ? 28.941  -22.519 -71.807 1.00 74.09  ? 759  LEU   A CG    1 
ATOM   3710 C  CD1   . LEU   A 1 610  ? 27.585  -21.853 -71.631 1.00 73.25  ? 759  LEU   A CD1   1 
ATOM   3711 C  CD2   . LEU   A 1 610  ? 28.783  -23.859 -72.507 1.00 75.30  ? 759  LEU   A CD2   1 
ATOM   3712 N  N     . GLU   A 1 611  ? 31.919  -19.100 -73.256 1.00 80.15  ? 760  GLU   A N     1 
ATOM   3713 C  CA    . GLU   A 1 611  ? 33.271  -18.595 -73.624 1.00 82.90  ? 760  GLU   A CA    1 
ATOM   3714 C  C     . GLU   A 1 611  ? 33.646  -17.421 -72.708 1.00 82.20  ? 760  GLU   A C     1 
ATOM   3715 O  O     . GLU   A 1 611  ? 34.832  -17.324 -72.338 1.00 83.42  ? 760  GLU   A O     1 
ATOM   3716 C  CB    . GLU   A 1 611  ? 33.312  -18.191 -75.101 1.00 85.25  ? 760  GLU   A CB    1 
ATOM   3717 C  CG    . GLU   A 1 611  ? 34.697  -17.798 -75.597 1.00 87.59  ? 760  GLU   A CG    1 
ATOM   3718 C  CD    . GLU   A 1 611  ? 35.766  -18.875 -75.486 1.00 91.39  ? 760  GLU   A CD    1 
ATOM   3719 O  OE1   . GLU   A 1 611  ? 35.411  -20.072 -75.499 1.00 95.80  ? 760  GLU   A OE1   1 
ATOM   3720 O  OE2   . GLU   A 1 611  ? 36.956  -18.514 -75.386 1.00 93.42  ? 760  GLU   A OE2   1 
ATOM   3721 N  N     . GLN   A 1 612  ? 32.678  -16.564 -72.367 1.00 81.20  ? 761  GLN   A N     1 
ATOM   3722 C  CA    . GLN   A 1 612  ? 32.867  -15.405 -71.450 1.00 81.48  ? 761  GLN   A CA    1 
ATOM   3723 C  C     . GLN   A 1 612  ? 33.084  -15.920 -70.021 1.00 80.08  ? 761  GLN   A C     1 
ATOM   3724 O  O     . GLN   A 1 612  ? 34.029  -15.440 -69.364 1.00 80.06  ? 761  GLN   A O     1 
ATOM   3725 C  CB    . GLN   A 1 612  ? 31.665  -14.460 -71.510 1.00 82.89  ? 761  GLN   A CB    1 
ATOM   3726 C  CG    . GLN   A 1 612  ? 31.591  -13.644 -72.794 1.00 83.96  ? 761  GLN   A CG    1 
ATOM   3727 C  CD    . GLN   A 1 612  ? 30.238  -13.007 -73.010 1.00 85.87  ? 761  GLN   A CD    1 
ATOM   3728 O  OE1   . GLN   A 1 612  ? 29.250  -13.349 -72.361 1.00 85.12  ? 761  GLN   A OE1   1 
ATOM   3729 N  NE2   . GLN   A 1 612  ? 30.180  -12.068 -73.940 1.00 86.84  ? 761  GLN   A NE2   1 
ATOM   3730 N  N     . ARG   A 1 613  ? 32.237  -16.855 -69.571 1.00 77.10  ? 762  ARG   A N     1 
ATOM   3731 C  CA    . ARG   A 1 613  ? 32.305  -17.507 -68.232 1.00 75.90  ? 762  ARG   A CA    1 
ATOM   3732 C  C     . ARG   A 1 613  ? 33.642  -18.246 -68.075 1.00 78.05  ? 762  ARG   A C     1 
ATOM   3733 O  O     . ARG   A 1 613  ? 34.213  -18.204 -66.967 1.00 77.86  ? 762  ARG   A O     1 
ATOM   3734 C  CB    . ARG   A 1 613  ? 31.128  -18.471 -68.043 1.00 72.10  ? 762  ARG   A CB    1 
ATOM   3735 C  CG    . ARG   A 1 613  ? 29.785  -17.782 -67.848 1.00 69.50  ? 762  ARG   A CG    1 
ATOM   3736 C  CD    . ARG   A 1 613  ? 28.631  -18.761 -67.752 1.00 66.86  ? 762  ARG   A CD    1 
ATOM   3737 N  NE    . ARG   A 1 613  ? 27.341  -18.089 -67.677 1.00 65.05  ? 762  ARG   A NE    1 
ATOM   3738 C  CZ    . ARG   A 1 613  ? 26.160  -18.702 -67.638 1.00 65.18  ? 762  ARG   A CZ    1 
ATOM   3739 N  NH1   . ARG   A 1 613  ? 26.084  -20.023 -67.665 1.00 64.89  ? 762  ARG   A NH1   1 
ATOM   3740 N  NH2   . ARG   A 1 613  ? 25.050  -17.985 -67.572 1.00 64.96  ? 762  ARG   A NH2   1 
ATOM   3741 N  N     . LYS   A 1 614  ? 34.114  -18.899 -69.142 1.00 80.64  ? 763  LYS   A N     1 
ATOM   3742 C  CA    . LYS   A 1 614  ? 35.416  -19.619 -69.194 1.00 81.95  ? 763  LYS   A CA    1 
ATOM   3743 C  C     . LYS   A 1 614  ? 36.562  -18.621 -68.986 1.00 83.17  ? 763  LYS   A C     1 
ATOM   3744 O  O     . LYS   A 1 614  ? 37.549  -18.996 -68.326 1.00 86.53  ? 763  LYS   A O     1 
ATOM   3745 C  CB    . LYS   A 1 614  ? 35.539  -20.376 -70.522 1.00 83.66  ? 763  LYS   A CB    1 
ATOM   3746 C  CG    . LYS   A 1 614  ? 36.915  -20.942 -70.851 1.00 85.53  ? 763  LYS   A CG    1 
ATOM   3747 C  CD    . LYS   A 1 614  ? 37.695  -20.104 -71.849 1.00 88.05  ? 763  LYS   A CD    1 
ATOM   3748 C  CE    . LYS   A 1 614  ? 38.939  -20.792 -72.371 1.00 88.70  ? 763  LYS   A CE    1 
ATOM   3749 N  NZ    . LYS   A 1 614  ? 39.275  -20.345 -73.743 1.00 89.64  ? 763  LYS   A NZ    1 
ATOM   3750 N  N     . GLY   A 1 615  ? 36.424  -17.399 -69.512 1.00 82.83  ? 764  GLY   A N     1 
ATOM   3751 C  CA    . GLY   A 1 615  ? 37.448  -16.336 -69.448 1.00 82.01  ? 764  GLY   A CA    1 
ATOM   3752 C  C     . GLY   A 1 615  ? 37.599  -15.740 -68.055 1.00 82.28  ? 764  GLY   A C     1 
ATOM   3753 O  O     . GLY   A 1 615  ? 38.601  -15.030 -67.833 1.00 83.02  ? 764  GLY   A O     1 
ATOM   3754 N  N     . ARG   A 1 616  ? 36.661  -16.021 -67.143 1.00 81.80  ? 765  ARG   A N     1 
ATOM   3755 C  CA    . ARG   A 1 616  ? 36.620  -15.446 -65.769 1.00 81.22  ? 765  ARG   A CA    1 
ATOM   3756 C  C     . ARG   A 1 616  ? 37.650  -16.145 -64.870 1.00 81.98  ? 765  ARG   A C     1 
ATOM   3757 O  O     . ARG   A 1 616  ? 37.876  -15.647 -63.750 1.00 82.31  ? 765  ARG   A O     1 
ATOM   3758 C  CB    . ARG   A 1 616  ? 35.219  -15.581 -65.162 1.00 81.26  ? 765  ARG   A CB    1 
ATOM   3759 C  CG    . ARG   A 1 616  ? 34.091  -15.051 -66.037 1.00 82.08  ? 765  ARG   A CG    1 
ATOM   3760 C  CD    . ARG   A 1 616  ? 33.720  -13.605 -65.767 1.00 81.32  ? 765  ARG   A CD    1 
ATOM   3761 N  NE    . ARG   A 1 616  ? 34.850  -12.690 -65.826 1.00 80.43  ? 765  ARG   A NE    1 
ATOM   3762 C  CZ    . ARG   A 1 616  ? 35.443  -12.272 -66.940 1.00 81.76  ? 765  ARG   A CZ    1 
ATOM   3763 N  NH1   . ARG   A 1 616  ? 35.035  -12.691 -68.128 1.00 82.46  ? 765  ARG   A NH1   1 
ATOM   3764 N  NH2   . ARG   A 1 616  ? 36.462  -11.434 -66.857 1.00 82.43  ? 765  ARG   A NH2   1 
ATOM   3765 N  N     . ALA   A 1 617  ? 38.240  -17.253 -65.338 1.00 83.56  ? 766  ALA   A N     1 
ATOM   3766 C  CA    . ALA   A 1 617  ? 39.244  -18.072 -64.615 1.00 82.65  ? 766  ALA   A CA    1 
ATOM   3767 C  C     . ALA   A 1 617  ? 40.661  -17.548 -64.884 1.00 82.68  ? 766  ALA   A C     1 
ATOM   3768 O  O     . ALA   A 1 617  ? 41.494  -17.602 -63.954 1.00 84.71  ? 766  ALA   A O     1 
ATOM   3769 C  CB    . ALA   A 1 617  ? 39.114  -19.517 -65.030 1.00 81.38  ? 766  ALA   A CB    1 
ATOM   3770 N  N     . GLY   A 1 618  ? 40.920  -17.071 -66.107 1.00 82.65  ? 767  GLY   A N     1 
ATOM   3771 C  CA    . GLY   A 1 618  ? 42.255  -16.658 -66.584 1.00 84.56  ? 767  GLY   A CA    1 
ATOM   3772 C  C     . GLY   A 1 618  ? 42.458  -15.156 -66.488 1.00 86.56  ? 767  GLY   A C     1 
ATOM   3773 O  O     . GLY   A 1 618  ? 42.657  -14.521 -67.543 1.00 86.78  ? 767  GLY   A O     1 
ATOM   3774 N  N     . ARG   A 1 619  ? 42.402  -14.610 -65.270 1.00 90.90  ? 768  ARG   A N     1 
ATOM   3775 C  CA    . ARG   A 1 619  ? 42.694  -13.181 -64.969 1.00 93.93  ? 768  ARG   A CA    1 
ATOM   3776 C  C     . ARG   A 1 619  ? 43.776  -13.059 -63.886 1.00 95.29  ? 768  ARG   A C     1 
ATOM   3777 O  O     . ARG   A 1 619  ? 44.296  -11.938 -63.710 1.00 91.15  ? 768  ARG   A O     1 
ATOM   3778 C  CB    . ARG   A 1 619  ? 41.413  -12.468 -64.531 1.00 95.01  ? 768  ARG   A CB    1 
ATOM   3779 C  CG    . ARG   A 1 619  ? 40.500  -12.079 -65.684 1.00 96.30  ? 768  ARG   A CG    1 
ATOM   3780 C  CD    . ARG   A 1 619  ? 39.611  -10.894 -65.356 1.00 97.56  ? 768  ARG   A CD    1 
ATOM   3781 N  NE    . ARG   A 1 619  ? 40.353  -9.643  -65.222 1.00 97.64  ? 768  ARG   A NE    1 
ATOM   3782 C  CZ    . ARG   A 1 619  ? 40.736  -9.081  -64.073 1.00 97.83  ? 768  ARG   A CZ    1 
ATOM   3783 N  NH1   . ARG   A 1 619  ? 40.462  -9.647  -62.908 1.00 97.27  ? 768  ARG   A NH1   1 
ATOM   3784 N  NH2   . ARG   A 1 619  ? 41.400  -7.938  -64.095 1.00 98.90  ? 768  ARG   A NH2   1 
ATOM   3785 N  N     . VAL   A 1 620  ? 44.099  -14.156 -63.191 1.00 98.91  ? 769  VAL   A N     1 
ATOM   3786 C  CA    . VAL   A 1 620  ? 45.083  -14.194 -62.066 1.00 101.07 ? 769  VAL   A CA    1 
ATOM   3787 C  C     . VAL   A 1 620  ? 46.252  -15.113 -62.450 1.00 101.40 ? 769  VAL   A C     1 
ATOM   3788 O  O     . VAL   A 1 620  ? 47.412  -14.701 -62.258 1.00 101.37 ? 769  VAL   A O     1 
ATOM   3789 C  CB    . VAL   A 1 620  ? 44.415  -14.659 -60.757 1.00 100.72 ? 769  VAL   A CB    1 
ATOM   3790 C  CG1   . VAL   A 1 620  ? 45.214  -14.229 -59.536 1.00 99.49  ? 769  VAL   A CG1   1 
ATOM   3791 C  CG2   . VAL   A 1 620  ? 42.976  -14.175 -60.653 1.00 100.66 ? 769  VAL   A CG2   1 
ATOM   3792 N  N     . ARG   A 1 621  ? 45.948  -16.309 -62.963 1.00 101.26 ? 770  ARG   A N     1 
ATOM   3793 C  CA    . ARG   A 1 621  ? 46.938  -17.368 -63.297 1.00 102.21 ? 770  ARG   A CA    1 
ATOM   3794 C  C     . ARG   A 1 621  ? 46.277  -18.386 -64.224 1.00 100.41 ? 770  ARG   A C     1 
ATOM   3795 O  O     . ARG   A 1 621  ? 45.066  -18.332 -64.426 1.00 98.36  ? 770  ARG   A O     1 
ATOM   3796 C  CB    . ARG   A 1 621  ? 47.445  -18.014 -62.002 1.00 104.01 ? 770  ARG   A CB    1 
ATOM   3797 C  CG    . ARG   A 1 621  ? 46.351  -18.303 -60.984 1.00 105.41 ? 770  ARG   A CG    1 
ATOM   3798 C  CD    . ARG   A 1 621  ? 46.752  -19.333 -59.944 1.00 108.14 ? 770  ARG   A CD    1 
ATOM   3799 N  NE    . ARG   A 1 621  ? 47.262  -20.558 -60.552 1.00 111.77 ? 770  ARG   A NE    1 
ATOM   3800 C  CZ    . ARG   A 1 621  ? 48.530  -20.971 -60.529 1.00 113.72 ? 770  ARG   A CZ    1 
ATOM   3801 N  NH1   . ARG   A 1 621  ? 49.466  -20.270 -59.908 1.00 114.48 ? 770  ARG   A NH1   1 
ATOM   3802 N  NH2   . ARG   A 1 621  ? 48.859  -22.103 -61.129 1.00 115.23 ? 770  ARG   A NH2   1 
ATOM   3803 N  N     . PRO   A 1 622  ? 47.037  -19.329 -64.833 1.00 100.98 ? 771  PRO   A N     1 
ATOM   3804 C  CA    . PRO   A 1 622  ? 46.434  -20.418 -65.603 1.00 101.08 ? 771  PRO   A CA    1 
ATOM   3805 C  C     . PRO   A 1 622  ? 45.308  -21.089 -64.801 1.00 100.55 ? 771  PRO   A C     1 
ATOM   3806 O  O     . PRO   A 1 622  ? 45.588  -21.628 -63.744 1.00 101.57 ? 771  PRO   A O     1 
ATOM   3807 C  CB    . PRO   A 1 622  ? 47.615  -21.367 -65.863 1.00 101.04 ? 771  PRO   A CB    1 
ATOM   3808 C  CG    . PRO   A 1 622  ? 48.816  -20.447 -65.886 1.00 101.11 ? 771  PRO   A CG    1 
ATOM   3809 C  CD    . PRO   A 1 622  ? 48.508  -19.390 -64.844 1.00 102.11 ? 771  PRO   A CD    1 
ATOM   3810 N  N     . GLY   A 1 623  ? 44.075  -21.010 -65.312 1.00 99.36  ? 772  GLY   A N     1 
ATOM   3811 C  CA    . GLY   A 1 623  ? 42.846  -21.404 -64.595 1.00 96.84  ? 772  GLY   A CA    1 
ATOM   3812 C  C     . GLY   A 1 623  ? 42.200  -22.646 -65.185 1.00 92.71  ? 772  GLY   A C     1 
ATOM   3813 O  O     . GLY   A 1 623  ? 42.765  -23.219 -66.139 1.00 90.06  ? 772  GLY   A O     1 
ATOM   3814 N  N     . PHE   A 1 624  ? 41.055  -23.044 -64.621 1.00 90.66  ? 773  PHE   A N     1 
ATOM   3815 C  CA    . PHE   A 1 624  ? 40.229  -24.203 -65.048 1.00 92.21  ? 773  PHE   A CA    1 
ATOM   3816 C  C     . PHE   A 1 624  ? 38.757  -23.774 -65.080 1.00 90.56  ? 773  PHE   A C     1 
ATOM   3817 O  O     . PHE   A 1 624  ? 38.325  -23.082 -64.138 1.00 90.84  ? 773  PHE   A O     1 
ATOM   3818 C  CB    . PHE   A 1 624  ? 40.427  -25.390 -64.099 1.00 94.25  ? 773  PHE   A CB    1 
ATOM   3819 C  CG    . PHE   A 1 624  ? 41.858  -25.835 -63.915 1.00 96.83  ? 773  PHE   A CG    1 
ATOM   3820 C  CD1   . PHE   A 1 624  ? 42.413  -26.805 -64.737 1.00 98.45  ? 773  PHE   A CD1   1 
ATOM   3821 C  CD2   . PHE   A 1 624  ? 42.649  -25.290 -62.914 1.00 98.67  ? 773  PHE   A CD2   1 
ATOM   3822 C  CE1   . PHE   A 1 624  ? 43.728  -27.213 -64.568 1.00 99.15  ? 773  PHE   A CE1   1 
ATOM   3823 C  CE2   . PHE   A 1 624  ? 43.964  -25.700 -62.746 1.00 99.31  ? 773  PHE   A CE2   1 
ATOM   3824 C  CZ    . PHE   A 1 624  ? 44.501  -26.660 -63.573 1.00 100.11 ? 773  PHE   A CZ    1 
ATOM   3825 N  N     . CYS   A 1 625  ? 38.023  -24.159 -66.131 1.00 88.25  ? 774  CYS   A N     1 
ATOM   3826 C  CA    . CYS   A 1 625  ? 36.553  -23.959 -66.261 1.00 85.73  ? 774  CYS   A CA    1 
ATOM   3827 C  C     . CYS   A 1 625  ? 35.850  -25.319 -66.329 1.00 83.94  ? 774  CYS   A C     1 
ATOM   3828 O  O     . CYS   A 1 625  ? 36.215  -26.129 -67.203 1.00 83.70  ? 774  CYS   A O     1 
ATOM   3829 C  CB    . CYS   A 1 625  ? 36.192  -23.137 -67.492 1.00 84.41  ? 774  CYS   A CB    1 
ATOM   3830 S  SG    . CYS   A 1 625  ? 34.413  -22.824 -67.628 1.00 83.61  ? 774  CYS   A SG    1 
ATOM   3831 N  N     . PHE   A 1 626  ? 34.875  -25.545 -65.443 1.00 82.40  ? 775  PHE   A N     1 
ATOM   3832 C  CA    . PHE   A 1 626  ? 34.105  -26.810 -65.317 1.00 84.33  ? 775  PHE   A CA    1 
ATOM   3833 C  C     . PHE   A 1 626  ? 32.672  -26.585 -65.818 1.00 83.30  ? 775  PHE   A C     1 
ATOM   3834 O  O     . PHE   A 1 626  ? 31.800  -26.201 -65.010 1.00 83.73  ? 775  PHE   A O     1 
ATOM   3835 C  CB    . PHE   A 1 626  ? 34.135  -27.309 -63.868 1.00 86.62  ? 775  PHE   A CB    1 
ATOM   3836 C  CG    . PHE   A 1 626  ? 35.517  -27.489 -63.291 1.00 87.62  ? 775  PHE   A CG    1 
ATOM   3837 C  CD1   . PHE   A 1 626  ? 36.175  -26.431 -62.680 1.00 89.22  ? 775  PHE   A CD1   1 
ATOM   3838 C  CD2   . PHE   A 1 626  ? 36.162  -28.715 -63.356 1.00 86.86  ? 775  PHE   A CD2   1 
ATOM   3839 C  CE1   . PHE   A 1 626  ? 37.446  -26.595 -62.151 1.00 89.19  ? 775  PHE   A CE1   1 
ATOM   3840 C  CE2   . PHE   A 1 626  ? 37.434  -28.877 -62.826 1.00 86.83  ? 775  PHE   A CE2   1 
ATOM   3841 C  CZ    . PHE   A 1 626  ? 38.074  -27.817 -62.225 1.00 88.02  ? 775  PHE   A CZ    1 
ATOM   3842 N  N     . HIS   A 1 627  ? 32.444  -26.811 -67.117 1.00 80.82  ? 776  HIS   A N     1 
ATOM   3843 C  CA    . HIS   A 1 627  ? 31.106  -26.775 -67.768 1.00 78.08  ? 776  HIS   A CA    1 
ATOM   3844 C  C     . HIS   A 1 627  ? 30.329  -28.037 -67.376 1.00 76.65  ? 776  HIS   A C     1 
ATOM   3845 O  O     . HIS   A 1 627  ? 30.872  -29.141 -67.569 1.00 77.52  ? 776  HIS   A O     1 
ATOM   3846 C  CB    . HIS   A 1 627  ? 31.237  -26.646 -69.293 1.00 76.48  ? 776  HIS   A CB    1 
ATOM   3847 C  CG    . HIS   A 1 627  ? 31.884  -25.382 -69.750 1.00 74.65  ? 776  HIS   A CG    1 
ATOM   3848 N  ND1   . HIS   A 1 627  ? 33.042  -25.374 -70.505 1.00 74.31  ? 776  HIS   A ND1   1 
ATOM   3849 C  CD2   . HIS   A 1 627  ? 31.542  -24.089 -69.568 1.00 73.52  ? 776  HIS   A CD2   1 
ATOM   3850 C  CE1   . HIS   A 1 627  ? 33.385  -24.129 -70.768 1.00 73.46  ? 776  HIS   A CE1   1 
ATOM   3851 N  NE2   . HIS   A 1 627  ? 32.480  -23.321 -70.202 1.00 74.33  ? 776  HIS   A NE2   1 
ATOM   3852 N  N     . LEU   A 1 628  ? 29.108  -27.878 -66.853 1.00 74.87  ? 777  LEU   A N     1 
ATOM   3853 C  CA    . LEU   A 1 628  ? 28.233  -28.999 -66.412 1.00 75.99  ? 777  LEU   A CA    1 
ATOM   3854 C  C     . LEU   A 1 628  ? 27.225  -29.332 -67.520 1.00 76.84  ? 777  LEU   A C     1 
ATOM   3855 O  O     . LEU   A 1 628  ? 26.070  -29.665 -67.190 1.00 77.38  ? 777  LEU   A O     1 
ATOM   3856 C  CB    . LEU   A 1 628  ? 27.531  -28.602 -65.110 1.00 77.02  ? 777  LEU   A CB    1 
ATOM   3857 C  CG    . LEU   A 1 628  ? 28.455  -28.277 -63.937 1.00 77.43  ? 777  LEU   A CG    1 
ATOM   3858 C  CD1   . LEU   A 1 628  ? 27.655  -27.809 -62.731 1.00 77.81  ? 777  LEU   A CD1   1 
ATOM   3859 C  CD2   . LEU   A 1 628  ? 29.318  -29.476 -63.571 1.00 76.74  ? 777  LEU   A CD2   1 
ATOM   3860 N  N     . CYS   A 1 629  ? 27.660  -29.253 -68.781 1.00 79.28  ? 778  CYS   A N     1 
ATOM   3861 C  CA    . CYS   A 1 629  ? 26.882  -29.623 -69.993 1.00 81.53  ? 778  CYS   A CA    1 
ATOM   3862 C  C     . CYS   A 1 629  ? 27.700  -30.620 -70.822 1.00 83.26  ? 778  CYS   A C     1 
ATOM   3863 O  O     . CYS   A 1 629  ? 28.934  -30.446 -70.901 1.00 83.59  ? 778  CYS   A O     1 
ATOM   3864 C  CB    . CYS   A 1 629  ? 26.542  -28.393 -70.828 1.00 82.58  ? 778  CYS   A CB    1 
ATOM   3865 S  SG    . CYS   A 1 629  ? 27.944  -27.738 -71.773 1.00 82.43  ? 778  CYS   A SG    1 
ATOM   3866 N  N     . SER   A 1 630  ? 27.037  -31.620 -71.410 1.00 85.18  ? 779  SER   A N     1 
ATOM   3867 C  CA    . SER   A 1 630  ? 27.657  -32.676 -72.256 1.00 86.24  ? 779  SER   A CA    1 
ATOM   3868 C  C     . SER   A 1 630  ? 28.372  -32.030 -73.451 1.00 86.57  ? 779  SER   A C     1 
ATOM   3869 O  O     . SER   A 1 630  ? 27.930  -30.948 -73.885 1.00 90.37  ? 779  SER   A O     1 
ATOM   3870 C  CB    . SER   A 1 630  ? 26.624  -33.678 -72.708 1.00 86.95  ? 779  SER   A CB    1 
ATOM   3871 O  OG    . SER   A 1 630  ? 25.735  -34.002 -71.648 1.00 86.72  ? 779  SER   A OG    1 
ATOM   3872 N  N     . ARG   A 1 631  ? 29.434  -32.665 -73.959 1.00 85.99  ? 780  ARG   A N     1 
ATOM   3873 C  CA    . ARG   A 1 631  ? 30.196  -32.189 -75.149 1.00 87.91  ? 780  ARG   A CA    1 
ATOM   3874 C  C     . ARG   A 1 631  ? 29.285  -32.222 -76.382 1.00 88.36  ? 780  ARG   A C     1 
ATOM   3875 O  O     . ARG   A 1 631  ? 29.550  -31.457 -77.329 1.00 87.96  ? 780  ARG   A O     1 
ATOM   3876 C  CB    . ARG   A 1 631  ? 31.463  -33.023 -75.369 1.00 88.20  ? 780  ARG   A CB    1 
ATOM   3877 C  CG    . ARG   A 1 631  ? 32.631  -32.612 -74.484 1.00 89.24  ? 780  ARG   A CG    1 
ATOM   3878 C  CD    . ARG   A 1 631  ? 33.890  -33.410 -74.766 1.00 90.44  ? 780  ARG   A CD    1 
ATOM   3879 N  NE    . ARG   A 1 631  ? 35.084  -32.785 -74.208 1.00 91.20  ? 780  ARG   A NE    1 
ATOM   3880 C  CZ    . ARG   A 1 631  ? 35.748  -31.767 -74.756 1.00 91.50  ? 780  ARG   A CZ    1 
ATOM   3881 N  NH1   . ARG   A 1 631  ? 35.341  -31.228 -75.895 1.00 92.46  ? 780  ARG   A NH1   1 
ATOM   3882 N  NH2   . ARG   A 1 631  ? 36.823  -31.285 -74.157 1.00 90.65  ? 780  ARG   A NH2   1 
ATOM   3883 N  N     . ALA   A 1 632  ? 28.258  -33.079 -76.364 1.00 90.10  ? 781  ALA   A N     1 
ATOM   3884 C  CA    . ALA   A 1 632  ? 27.177  -33.145 -77.375 1.00 91.39  ? 781  ALA   A CA    1 
ATOM   3885 C  C     . ALA   A 1 632  ? 26.287  -31.902 -77.258 1.00 92.93  ? 781  ALA   A C     1 
ATOM   3886 O  O     . ALA   A 1 632  ? 26.024  -31.266 -78.298 1.00 98.62  ? 781  ALA   A O     1 
ATOM   3887 C  CB    . ALA   A 1 632  ? 26.378  -34.413 -77.194 1.00 90.67  ? 781  ALA   A CB    1 
ATOM   3888 N  N     . ARG   A 1 633  ? 25.853  -31.572 -76.036 1.00 91.31  ? 782  ARG   A N     1 
ATOM   3889 C  CA    . ARG   A 1 633  ? 24.944  -30.430 -75.737 1.00 90.57  ? 782  ARG   A CA    1 
ATOM   3890 C  C     . ARG   A 1 633  ? 25.592  -29.113 -76.186 1.00 89.13  ? 782  ARG   A C     1 
ATOM   3891 O  O     . ARG   A 1 633  ? 24.858  -28.266 -76.729 1.00 90.15  ? 782  ARG   A O     1 
ATOM   3892 C  CB    . ARG   A 1 633  ? 24.591  -30.394 -74.245 1.00 89.74  ? 782  ARG   A CB    1 
ATOM   3893 C  CG    . ARG   A 1 633  ? 23.719  -29.217 -73.825 1.00 89.88  ? 782  ARG   A CG    1 
ATOM   3894 C  CD    . ARG   A 1 633  ? 22.431  -29.070 -74.617 1.00 90.70  ? 782  ARG   A CD    1 
ATOM   3895 N  NE    . ARG   A 1 633  ? 21.566  -30.238 -74.514 1.00 93.47  ? 782  ARG   A NE    1 
ATOM   3896 C  CZ    . ARG   A 1 633  ? 20.344  -30.332 -75.032 1.00 94.77  ? 782  ARG   A CZ    1 
ATOM   3897 N  NH1   . ARG   A 1 633  ? 19.816  -29.319 -75.699 1.00 95.40  ? 782  ARG   A NH1   1 
ATOM   3898 N  NH2   . ARG   A 1 633  ? 19.648  -31.446 -74.876 1.00 95.35  ? 782  ARG   A NH2   1 
ATOM   3899 N  N     . PHE   A 1 634  ? 26.905  -28.949 -75.978 1.00 86.32  ? 783  PHE   A N     1 
ATOM   3900 C  CA    . PHE   A 1 634  ? 27.673  -27.731 -76.356 1.00 86.16  ? 783  PHE   A CA    1 
ATOM   3901 C  C     . PHE   A 1 634  ? 27.536  -27.463 -77.860 1.00 87.46  ? 783  PHE   A C     1 
ATOM   3902 O  O     . PHE   A 1 634  ? 27.464  -26.281 -78.247 1.00 88.26  ? 783  PHE   A O     1 
ATOM   3903 C  CB    . PHE   A 1 634  ? 29.153  -27.849 -75.987 1.00 84.89  ? 783  PHE   A CB    1 
ATOM   3904 C  CG    . PHE   A 1 634  ? 29.977  -26.656 -76.407 1.00 83.48  ? 783  PHE   A CG    1 
ATOM   3905 C  CD1   . PHE   A 1 634  ? 29.837  -25.438 -75.759 1.00 82.96  ? 783  PHE   A CD1   1 
ATOM   3906 C  CD2   . PHE   A 1 634  ? 30.872  -26.741 -77.463 1.00 82.67  ? 783  PHE   A CD2   1 
ATOM   3907 C  CE1   . PHE   A 1 634  ? 30.585  -24.336 -76.148 1.00 83.35  ? 783  PHE   A CE1   1 
ATOM   3908 C  CE2   . PHE   A 1 634  ? 31.620  -25.639 -77.850 1.00 82.87  ? 783  PHE   A CE2   1 
ATOM   3909 C  CZ    . PHE   A 1 634  ? 31.474  -24.438 -77.193 1.00 83.05  ? 783  PHE   A CZ    1 
ATOM   3910 N  N     . GLU   A 1 635  ? 27.518  -28.524 -78.675 1.00 88.00  ? 784  GLU   A N     1 
ATOM   3911 C  CA    . GLU   A 1 635  ? 27.377  -28.437 -80.154 1.00 89.57  ? 784  GLU   A CA    1 
ATOM   3912 C  C     . GLU   A 1 635  ? 25.974  -27.918 -80.499 1.00 89.46  ? 784  GLU   A C     1 
ATOM   3913 O  O     . GLU   A 1 635  ? 25.851  -27.168 -81.488 1.00 88.68  ? 784  GLU   A O     1 
ATOM   3914 C  CB    . GLU   A 1 635  ? 27.640  -29.796 -80.809 1.00 90.84  ? 784  GLU   A CB    1 
ATOM   3915 C  CG    . GLU   A 1 635  ? 29.048  -30.331 -80.585 1.00 92.34  ? 784  GLU   A CG    1 
ATOM   3916 C  CD    . GLU   A 1 635  ? 30.174  -29.547 -81.242 1.00 92.56  ? 784  GLU   A CD    1 
ATOM   3917 O  OE1   . GLU   A 1 635  ? 29.888  -28.705 -82.117 1.00 93.84  ? 784  GLU   A OE1   1 
ATOM   3918 O  OE2   . GLU   A 1 635  ? 31.342  -29.783 -80.875 1.00 91.41  ? 784  GLU   A OE2   1 
ATOM   3919 N  N     . ARG   A 1 636  ? 24.967  -28.290 -79.699 1.00 88.60  ? 785  ARG   A N     1 
ATOM   3920 C  CA    . ARG   A 1 636  ? 23.534  -27.955 -79.922 1.00 88.40  ? 785  ARG   A CA    1 
ATOM   3921 C  C     . ARG   A 1 636  ? 23.202  -26.552 -79.393 1.00 86.73  ? 785  ARG   A C     1 
ATOM   3922 O  O     . ARG   A 1 636  ? 22.095  -26.068 -79.700 1.00 87.61  ? 785  ARG   A O     1 
ATOM   3923 C  CB    . ARG   A 1 636  ? 22.627  -28.981 -79.237 1.00 90.91  ? 785  ARG   A CB    1 
ATOM   3924 C  CG    . ARG   A 1 636  ? 22.739  -30.393 -79.793 1.00 93.05  ? 785  ARG   A CG    1 
ATOM   3925 C  CD    . ARG   A 1 636  ? 21.394  -31.094 -79.747 1.00 95.73  ? 785  ARG   A CD    1 
ATOM   3926 N  NE    . ARG   A 1 636  ? 21.486  -32.546 -79.786 1.00 97.38  ? 785  ARG   A NE    1 
ATOM   3927 C  CZ    . ARG   A 1 636  ? 20.442  -33.366 -79.887 1.00 98.78  ? 785  ARG   A CZ    1 
ATOM   3928 N  NH1   . ARG   A 1 636  ? 20.629  -34.675 -79.908 1.00 99.62  ? 785  ARG   A NH1   1 
ATOM   3929 N  NH2   . ARG   A 1 636  ? 19.215  -32.878 -79.972 1.00 99.60  ? 785  ARG   A NH2   1 
ATOM   3930 N  N     . LEU   A 1 637  ? 24.097  -25.931 -78.616 1.00 84.65  ? 786  LEU   A N     1 
ATOM   3931 C  CA    . LEU   A 1 637  ? 23.899  -24.561 -78.065 1.00 82.98  ? 786  LEU   A CA    1 
ATOM   3932 C  C     . LEU   A 1 637  ? 23.887  -23.550 -79.216 1.00 81.36  ? 786  LEU   A C     1 
ATOM   3933 O  O     . LEU   A 1 637  ? 24.683  -23.722 -80.160 1.00 80.51  ? 786  LEU   A O     1 
ATOM   3934 C  CB    . LEU   A 1 637  ? 25.017  -24.221 -77.071 1.00 81.73  ? 786  LEU   A CB    1 
ATOM   3935 C  CG    . LEU   A 1 637  ? 25.061  -25.051 -75.789 1.00 79.75  ? 786  LEU   A CG    1 
ATOM   3936 C  CD1   . LEU   A 1 637  ? 26.169  -24.555 -74.873 1.00 79.55  ? 786  LEU   A CD1   1 
ATOM   3937 C  CD2   . LEU   A 1 637  ? 23.721  -25.034 -75.066 1.00 78.48  ? 786  LEU   A CD2   1 
ATOM   3938 N  N     . GLU   A 1 638  ? 23.018  -22.538 -79.131 1.00 80.16  ? 787  GLU   A N     1 
ATOM   3939 C  CA    . GLU   A 1 638  ? 22.997  -21.375 -80.057 1.00 79.55  ? 787  GLU   A CA    1 
ATOM   3940 C  C     . GLU   A 1 638  ? 24.249  -20.530 -79.800 1.00 75.61  ? 787  GLU   A C     1 
ATOM   3941 O  O     . GLU   A 1 638  ? 24.755  -20.559 -78.665 1.00 76.69  ? 787  GLU   A O     1 
ATOM   3942 C  CB    . GLU   A 1 638  ? 21.718  -20.553 -79.873 1.00 81.81  ? 787  GLU   A CB    1 
ATOM   3943 C  CG    . GLU   A 1 638  ? 20.470  -21.241 -80.403 1.00 84.48  ? 787  GLU   A CG    1 
ATOM   3944 C  CD    . GLU   A 1 638  ? 20.455  -21.499 -81.903 1.00 86.50  ? 787  GLU   A CD    1 
ATOM   3945 O  OE1   . GLU   A 1 638  ? 21.164  -20.779 -82.640 1.00 87.43  ? 787  GLU   A OE1   1 
ATOM   3946 O  OE2   . GLU   A 1 638  ? 19.736  -22.425 -82.332 1.00 87.04  ? 787  GLU   A OE2   1 
ATOM   3947 N  N     . THR   A 1 639  ? 24.733  -19.823 -80.823 1.00 72.01  ? 788  THR   A N     1 
ATOM   3948 C  CA    . THR   A 1 639  ? 25.950  -18.971 -80.766 1.00 70.65  ? 788  THR   A CA    1 
ATOM   3949 C  C     . THR   A 1 639  ? 25.692  -17.781 -79.833 1.00 71.60  ? 788  THR   A C     1 
ATOM   3950 O  O     . THR   A 1 639  ? 26.586  -17.474 -79.020 1.00 72.79  ? 788  THR   A O     1 
ATOM   3951 C  CB    . THR   A 1 639  ? 26.376  -18.542 -82.176 1.00 69.83  ? 788  THR   A CB    1 
ATOM   3952 O  OG1   . THR   A 1 639  ? 26.596  -19.738 -82.922 1.00 69.95  ? 788  THR   A OG1   1 
ATOM   3953 C  CG2   . THR   A 1 639  ? 27.625  -17.688 -82.198 1.00 69.65  ? 788  THR   A CG2   1 
ATOM   3954 N  N     . HIS   A 1 640  ? 24.517  -17.151 -79.944 1.00 72.26  ? 789  HIS   A N     1 
ATOM   3955 C  CA    . HIS   A 1 640  ? 24.108  -15.948 -79.168 1.00 71.85  ? 789  HIS   A CA    1 
ATOM   3956 C  C     . HIS   A 1 640  ? 22.736  -16.169 -78.520 1.00 70.10  ? 789  HIS   A C     1 
ATOM   3957 O  O     . HIS   A 1 640  ? 21.898  -16.868 -79.123 1.00 68.90  ? 789  HIS   A O     1 
ATOM   3958 C  CB    . HIS   A 1 640  ? 24.085  -14.706 -80.070 1.00 74.30  ? 789  HIS   A CB    1 
ATOM   3959 C  CG    . HIS   A 1 640  ? 25.402  -14.367 -80.682 1.00 77.03  ? 789  HIS   A CG    1 
ATOM   3960 N  ND1   . HIS   A 1 640  ? 26.404  -13.730 -79.974 1.00 79.27  ? 789  HIS   A ND1   1 
ATOM   3961 C  CD2   . HIS   A 1 640  ? 25.879  -14.553 -81.932 1.00 78.94  ? 789  HIS   A CD2   1 
ATOM   3962 C  CE1   . HIS   A 1 640  ? 27.445  -13.547 -80.761 1.00 81.12  ? 789  HIS   A CE1   1 
ATOM   3963 N  NE2   . HIS   A 1 640  ? 27.149  -14.046 -81.968 1.00 81.09  ? 789  HIS   A NE2   1 
ATOM   3964 N  N     . MET   A 1 641  ? 22.524  -15.581 -77.338 1.00 69.70  ? 790  MET   A N     1 
ATOM   3965 C  CA    . MET   A 1 641  ? 21.202  -15.497 -76.660 1.00 67.56  ? 790  MET   A CA    1 
ATOM   3966 C  C     . MET   A 1 641  ? 20.270  -14.636 -77.517 1.00 64.87  ? 790  MET   A C     1 
ATOM   3967 O  O     . MET   A 1 641  ? 20.741  -13.606 -78.040 1.00 64.78  ? 790  MET   A O     1 
ATOM   3968 C  CB    . MET   A 1 641  ? 21.319  -14.853 -75.273 1.00 68.86  ? 790  MET   A CB    1 
ATOM   3969 C  CG    . MET   A 1 641  ? 22.011  -15.723 -74.240 1.00 69.76  ? 790  MET   A CG    1 
ATOM   3970 S  SD    . MET   A 1 641  ? 21.035  -17.167 -73.744 1.00 71.96  ? 790  MET   A SD    1 
ATOM   3971 C  CE    . MET   A 1 641  ? 19.571  -16.378 -73.076 1.00 72.21  ? 790  MET   A CE    1 
ATOM   3972 N  N     . THR   A 1 642  ? 19.006  -15.046 -77.648 1.00 62.15  ? 791  THR   A N     1 
ATOM   3973 C  CA    . THR   A 1 642  ? 17.907  -14.236 -78.237 1.00 60.22  ? 791  THR   A CA    1 
ATOM   3974 C  C     . THR   A 1 642  ? 17.853  -12.894 -77.511 1.00 59.59  ? 791  THR   A C     1 
ATOM   3975 O  O     . THR   A 1 642  ? 17.642  -12.864 -76.300 1.00 60.32  ? 791  THR   A O     1 
ATOM   3976 C  CB    . THR   A 1 642  ? 16.570  -14.980 -78.136 1.00 60.23  ? 791  THR   A CB    1 
ATOM   3977 O  OG1   . THR   A 1 642  ? 16.707  -16.215 -78.838 1.00 61.66  ? 791  THR   A OG1   1 
ATOM   3978 C  CG2   . THR   A 1 642  ? 15.403  -14.200 -78.701 1.00 60.26  ? 791  THR   A CG2   1 
ATOM   3979 N  N     . PRO   A 1 643  ? 18.058  -11.747 -78.203 1.00 57.03  ? 792  PRO   A N     1 
ATOM   3980 C  CA    . PRO   A 1 643  ? 18.002  -10.440 -77.549 1.00 57.21  ? 792  PRO   A CA    1 
ATOM   3981 C  C     . PRO   A 1 643  ? 16.607  -10.162 -76.968 1.00 57.57  ? 792  PRO   A C     1 
ATOM   3982 O  O     . PRO   A 1 643  ? 15.640  -10.619 -77.544 1.00 57.43  ? 792  PRO   A O     1 
ATOM   3983 C  CB    . PRO   A 1 643  ? 18.364  -9.442  -78.660 1.00 57.52  ? 792  PRO   A CB    1 
ATOM   3984 C  CG    . PRO   A 1 643  ? 18.081  -10.183 -79.948 1.00 57.30  ? 792  PRO   A CG    1 
ATOM   3985 C  CD    . PRO   A 1 643  ? 18.350  -11.641 -79.641 1.00 57.21  ? 792  PRO   A CD    1 
ATOM   3986 N  N     . GLU   A 1 644  ? 16.547  -9.430  -75.848 1.00 58.88  ? 793  GLU   A N     1 
ATOM   3987 C  CA    . GLU   A 1 644  ? 15.309  -9.184  -75.055 1.00 58.63  ? 793  GLU   A CA    1 
ATOM   3988 C  C     . GLU   A 1 644  ? 14.219  -8.581  -75.951 1.00 57.63  ? 793  GLU   A C     1 
ATOM   3989 O  O     . GLU   A 1 644  ? 13.038  -8.919  -75.735 1.00 57.70  ? 793  GLU   A O     1 
ATOM   3990 C  CB    . GLU   A 1 644  ? 15.588  -8.260  -73.868 1.00 59.57  ? 793  GLU   A CB    1 
ATOM   3991 C  CG    . GLU   A 1 644  ? 16.392  -8.912  -72.757 1.00 60.28  ? 793  GLU   A CG    1 
ATOM   3992 C  CD    . GLU   A 1 644  ? 16.439  -8.126  -71.455 1.00 61.64  ? 793  GLU   A CD    1 
ATOM   3993 O  OE1   . GLU   A 1 644  ? 17.060  -8.621  -70.493 1.00 62.08  ? 793  GLU   A OE1   1 
ATOM   3994 O  OE2   . GLU   A 1 644  ? 15.857  -7.021  -71.403 1.00 62.59  ? 793  GLU   A OE2   1 
ATOM   3995 N  N     . MET   A 1 645  ? 14.606  -7.731  -76.911 1.00 56.12  ? 794  MET   A N     1 
ATOM   3996 C  CA    . MET   A 1 645  ? 13.696  -7.056  -77.881 1.00 55.06  ? 794  MET   A CA    1 
ATOM   3997 C  C     . MET   A 1 645  ? 12.774  -8.089  -78.548 1.00 54.03  ? 794  MET   A C     1 
ATOM   3998 O  O     . MET   A 1 645  ? 11.598  -7.757  -78.791 1.00 54.02  ? 794  MET   A O     1 
ATOM   3999 C  CB    . MET   A 1 645  ? 14.504  -6.315  -78.955 1.00 55.07  ? 794  MET   A CB    1 
ATOM   4000 C  CG    . MET   A 1 645  ? 13.661  -5.494  -79.921 1.00 55.00  ? 794  MET   A CG    1 
ATOM   4001 S  SD    . MET   A 1 645  ? 12.760  -4.135  -79.128 1.00 55.18  ? 794  MET   A SD    1 
ATOM   4002 C  CE    . MET   A 1 645  ? 14.097  -2.984  -78.815 1.00 54.84  ? 794  MET   A CE    1 
ATOM   4003 N  N     . PHE   A 1 646  ? 13.286  -9.293  -78.820 1.00 53.23  ? 795  PHE   A N     1 
ATOM   4004 C  CA    . PHE   A 1 646  ? 12.578  -10.377 -79.549 1.00 53.18  ? 795  PHE   A CA    1 
ATOM   4005 C  C     . PHE   A 1 646  ? 11.532  -11.053 -78.649 1.00 54.47  ? 795  PHE   A C     1 
ATOM   4006 O  O     . PHE   A 1 646  ? 10.551  -11.585 -79.202 1.00 56.54  ? 795  PHE   A O     1 
ATOM   4007 C  CB    . PHE   A 1 646  ? 13.575  -11.415 -80.075 1.00 52.26  ? 795  PHE   A CB    1 
ATOM   4008 C  CG    . PHE   A 1 646  ? 14.463  -10.971 -81.214 1.00 52.58  ? 795  PHE   A CG    1 
ATOM   4009 C  CD1   . PHE   A 1 646  ? 14.513  -9.647  -81.632 1.00 52.63  ? 795  PHE   A CD1   1 
ATOM   4010 C  CD2   . PHE   A 1 646  ? 15.281  -11.890 -81.859 1.00 52.38  ? 795  PHE   A CD2   1 
ATOM   4011 C  CE1   . PHE   A 1 646  ? 15.343  -9.260  -82.675 1.00 52.07  ? 795  PHE   A CE1   1 
ATOM   4012 C  CE2   . PHE   A 1 646  ? 16.112  -11.500 -82.898 1.00 52.02  ? 795  PHE   A CE2   1 
ATOM   4013 C  CZ    . PHE   A 1 646  ? 16.142  -10.186 -83.304 1.00 51.65  ? 795  PHE   A CZ    1 
ATOM   4014 N  N     . ARG   A 1 647  ? 11.717  -11.033 -77.323 1.00 54.74  ? 796  ARG   A N     1 
ATOM   4015 C  CA    . ARG   A 1 647  ? 10.977  -11.921 -76.382 1.00 55.64  ? 796  ARG   A CA    1 
ATOM   4016 C  C     . ARG   A 1 647  ? 10.529  -11.166 -75.122 1.00 53.69  ? 796  ARG   A C     1 
ATOM   4017 O  O     . ARG   A 1 647  ? 10.600  -11.763 -74.036 1.00 53.02  ? 796  ARG   A O     1 
ATOM   4018 C  CB    . ARG   A 1 647  ? 11.868  -13.112 -76.010 1.00 58.37  ? 796  ARG   A CB    1 
ATOM   4019 C  CG    . ARG   A 1 647  ? 13.249  -12.731 -75.492 1.00 60.07  ? 796  ARG   A CG    1 
ATOM   4020 C  CD    . ARG   A 1 647  ? 13.915  -13.886 -74.765 1.00 62.03  ? 796  ARG   A CD    1 
ATOM   4021 N  NE    . ARG   A 1 647  ? 15.354  -13.711 -74.594 1.00 62.82  ? 796  ARG   A NE    1 
ATOM   4022 C  CZ    . ARG   A 1 647  ? 15.944  -13.063 -73.589 1.00 62.01  ? 796  ARG   A CZ    1 
ATOM   4023 N  NH1   . ARG   A 1 647  ? 15.228  -12.492 -72.634 1.00 60.71  ? 796  ARG   A NH1   1 
ATOM   4024 N  NH2   . ARG   A 1 647  ? 17.264  -12.985 -73.549 1.00 62.08  ? 796  ARG   A NH2   1 
ATOM   4025 N  N     . THR   A 1 648  ? 10.056  -9.923  -75.255 1.00 53.90  ? 797  THR   A N     1 
ATOM   4026 C  CA    . THR   A 1 648  ? 9.593   -9.078  -74.118 1.00 53.74  ? 797  THR   A CA    1 
ATOM   4027 C  C     . THR   A 1 648  ? 8.413   -8.210  -74.550 1.00 53.55  ? 797  THR   A C     1 
ATOM   4028 O  O     . THR   A 1 648  ? 8.433   -7.636  -75.638 1.00 53.64  ? 797  THR   A O     1 
ATOM   4029 C  CB    . THR   A 1 648  ? 10.727  -8.194  -73.580 1.00 54.43  ? 797  THR   A CB    1 
ATOM   4030 O  OG1   . THR   A 1 648  ? 11.888  -8.999  -73.367 1.00 53.83  ? 797  THR   A OG1   1 
ATOM   4031 C  CG2   . THR   A 1 648  ? 10.364  -7.485  -72.293 1.00 54.55  ? 797  THR   A CG2   1 
ATOM   4032 N  N     . PRO   A 1 649  ? 7.359   -8.073  -73.708 1.00 52.93  ? 798  PRO   A N     1 
ATOM   4033 C  CA    . PRO   A 1 649  ? 6.272   -7.127  -73.967 1.00 52.52  ? 798  PRO   A CA    1 
ATOM   4034 C  C     . PRO   A 1 649  ? 6.802   -5.709  -74.227 1.00 51.98  ? 798  PRO   A C     1 
ATOM   4035 O  O     . PRO   A 1 649  ? 7.773   -5.336  -73.592 1.00 52.70  ? 798  PRO   A O     1 
ATOM   4036 C  CB    . PRO   A 1 649  ? 5.441   -7.147  -72.676 1.00 52.84  ? 798  PRO   A CB    1 
ATOM   4037 C  CG    . PRO   A 1 649  ? 5.729   -8.500  -72.063 1.00 52.77  ? 798  PRO   A CG    1 
ATOM   4038 C  CD    . PRO   A 1 649  ? 7.152   -8.830  -72.464 1.00 52.75  ? 798  PRO   A CD    1 
ATOM   4039 N  N     . LEU   A 1 650  ? 6.151   -4.962  -75.124 1.00 51.67  ? 799  LEU   A N     1 
ATOM   4040 C  CA    . LEU   A 1 650  ? 6.659   -3.670  -75.663 1.00 51.62  ? 799  LEU   A CA    1 
ATOM   4041 C  C     . LEU   A 1 650  ? 5.754   -2.500  -75.257 1.00 52.87  ? 799  LEU   A C     1 
ATOM   4042 O  O     . LEU   A 1 650  ? 5.985   -1.391  -75.774 1.00 53.67  ? 799  LEU   A O     1 
ATOM   4043 C  CB    . LEU   A 1 650  ? 6.745   -3.776  -77.190 1.00 50.15  ? 799  LEU   A CB    1 
ATOM   4044 C  CG    . LEU   A 1 650  ? 7.686   -4.850  -77.732 1.00 49.66  ? 799  LEU   A CG    1 
ATOM   4045 C  CD1   . LEU   A 1 650  ? 7.511   -5.016  -79.232 1.00 49.39  ? 799  LEU   A CD1   1 
ATOM   4046 C  CD2   . LEU   A 1 650  ? 9.134   -4.522  -77.402 1.00 49.86  ? 799  LEU   A CD2   1 
ATOM   4047 N  N     . HIS   A 1 651  ? 4.775   -2.711  -74.370 1.00 54.78  ? 800  HIS   A N     1 
ATOM   4048 C  CA    . HIS   A 1 651  ? 3.747   -1.685  -74.037 1.00 56.62  ? 800  HIS   A CA    1 
ATOM   4049 C  C     . HIS   A 1 651  ? 4.370   -0.560  -73.197 1.00 58.30  ? 800  HIS   A C     1 
ATOM   4050 O  O     . HIS   A 1 651  ? 3.962   0.603   -73.390 1.00 59.22  ? 800  HIS   A O     1 
ATOM   4051 C  CB    . HIS   A 1 651  ? 2.495   -2.312  -73.400 1.00 57.44  ? 800  HIS   A CB    1 
ATOM   4052 C  CG    . HIS   A 1 651  ? 2.747   -3.168  -72.207 1.00 58.68  ? 800  HIS   A CG    1 
ATOM   4053 N  ND1   . HIS   A 1 651  ? 2.837   -4.541  -72.295 1.00 59.75  ? 800  HIS   A ND1   1 
ATOM   4054 C  CD2   . HIS   A 1 651  ? 2.892   -2.860  -70.900 1.00 60.53  ? 800  HIS   A CD2   1 
ATOM   4055 C  CE1   . HIS   A 1 651  ? 3.043   -5.044  -71.095 1.00 61.03  ? 800  HIS   A CE1   1 
ATOM   4056 N  NE2   . HIS   A 1 651  ? 3.081   -4.033  -70.221 1.00 61.73  ? 800  HIS   A NE2   1 
ATOM   4057 N  N     . GLU   A 1 652  ? 5.331   -0.874  -72.322 1.00 59.51  ? 801  GLU   A N     1 
ATOM   4058 C  CA    . GLU   A 1 652  ? 6.055   0.138   -71.503 1.00 59.25  ? 801  GLU   A CA    1 
ATOM   4059 C  C     . GLU   A 1 652  ? 6.941   0.988   -72.423 1.00 58.34  ? 801  GLU   A C     1 
ATOM   4060 O  O     . GLU   A 1 652  ? 6.988   2.216   -72.218 1.00 61.32  ? 801  GLU   A O     1 
ATOM   4061 C  CB    . GLU   A 1 652  ? 6.854   -0.536  -70.386 1.00 62.04  ? 801  GLU   A CB    1 
ATOM   4062 C  CG    . GLU   A 1 652  ? 5.985   -0.988  -69.223 1.00 65.18  ? 801  GLU   A CG    1 
ATOM   4063 C  CD    . GLU   A 1 652  ? 6.683   -1.812  -68.153 1.00 67.88  ? 801  GLU   A CD    1 
ATOM   4064 O  OE1   . GLU   A 1 652  ? 7.644   -2.537  -68.489 1.00 69.70  ? 801  GLU   A OE1   1 
ATOM   4065 O  OE2   . GLU   A 1 652  ? 6.258   -1.733  -66.980 1.00 69.73  ? 801  GLU   A OE2   1 
ATOM   4066 N  N     . ILE   A 1 653  ? 7.599   0.363   -73.405 1.00 55.64  ? 802  ILE   A N     1 
ATOM   4067 C  CA    . ILE   A 1 653  ? 8.425   1.051   -74.445 1.00 54.06  ? 802  ILE   A CA    1 
ATOM   4068 C  C     . ILE   A 1 653  ? 7.499   1.832   -75.387 1.00 53.58  ? 802  ILE   A C     1 
ATOM   4069 O  O     . ILE   A 1 653  ? 7.876   2.951   -75.783 1.00 54.19  ? 802  ILE   A O     1 
ATOM   4070 C  CB    . ILE   A 1 653  ? 9.324   0.045   -75.197 1.00 53.81  ? 802  ILE   A CB    1 
ATOM   4071 C  CG1   . ILE   A 1 653  ? 10.566  -0.295  -74.370 1.00 53.91  ? 802  ILE   A CG1   1 
ATOM   4072 C  CG2   . ILE   A 1 653  ? 9.696   0.551   -76.585 1.00 53.15  ? 802  ILE   A CG2   1 
ATOM   4073 C  CD1   . ILE   A 1 653  ? 11.400  -1.415  -74.935 1.00 54.10  ? 802  ILE   A CD1   1 
ATOM   4074 N  N     . ALA   A 1 654  ? 6.341   1.265   -75.738 1.00 53.29  ? 803  ALA   A N     1 
ATOM   4075 C  CA    . ALA   A 1 654  ? 5.312   1.906   -76.593 1.00 53.44  ? 803  ALA   A CA    1 
ATOM   4076 C  C     . ALA   A 1 654  ? 4.885   3.247   -75.976 1.00 53.12  ? 803  ALA   A C     1 
ATOM   4077 O  O     . ALA   A 1 654  ? 4.841   4.248   -76.716 1.00 52.21  ? 803  ALA   A O     1 
ATOM   4078 C  CB    . ALA   A 1 654  ? 4.135   0.981   -76.780 1.00 53.37  ? 803  ALA   A CB    1 
ATOM   4079 N  N     . LEU   A 1 655  ? 4.595   3.266   -74.670 1.00 53.16  ? 804  LEU   A N     1 
ATOM   4080 C  CA    . LEU   A 1 655  ? 4.199   4.493   -73.925 1.00 52.50  ? 804  LEU   A CA    1 
ATOM   4081 C  C     . LEU   A 1 655  ? 5.337   5.521   -73.981 1.00 53.41  ? 804  LEU   A C     1 
ATOM   4082 O  O     . LEU   A 1 655  ? 5.046   6.692   -74.288 1.00 55.29  ? 804  LEU   A O     1 
ATOM   4083 C  CB    . LEU   A 1 655  ? 3.844   4.131   -72.480 1.00 51.61  ? 804  LEU   A CB    1 
ATOM   4084 C  CG    . LEU   A 1 655  ? 2.473   3.489   -72.277 1.00 52.03  ? 804  LEU   A CG    1 
ATOM   4085 C  CD1   . LEU   A 1 655  ? 2.217   3.219   -70.802 1.00 52.57  ? 804  LEU   A CD1   1 
ATOM   4086 C  CD2   . LEU   A 1 655  ? 1.364   4.359   -72.853 1.00 52.33  ? 804  LEU   A CD2   1 
ATOM   4087 N  N     . SER   A 1 656  ? 6.577   5.101   -73.706 1.00 53.49  ? 805  SER   A N     1 
ATOM   4088 C  CA    . SER   A 1 656  ? 7.790   5.963   -73.736 1.00 55.21  ? 805  SER   A CA    1 
ATOM   4089 C  C     . SER   A 1 656  ? 7.870   6.701   -75.079 1.00 55.76  ? 805  SER   A C     1 
ATOM   4090 O  O     . SER   A 1 656  ? 8.049   7.936   -75.067 1.00 55.33  ? 805  SER   A O     1 
ATOM   4091 C  CB    . SER   A 1 656  ? 9.043   5.162   -73.477 1.00 56.21  ? 805  SER   A CB    1 
ATOM   4092 O  OG    . SER   A 1 656  ? 10.184  6.008   -73.417 1.00 56.94  ? 805  SER   A OG    1 
ATOM   4093 N  N     . ILE   A 1 657  ? 7.725   5.962   -76.185 1.00 56.92  ? 806  ILE   A N     1 
ATOM   4094 C  CA    . ILE   A 1 657  ? 7.741   6.487   -77.586 1.00 55.57  ? 806  ILE   A CA    1 
ATOM   4095 C  C     . ILE   A 1 657  ? 6.724   7.628   -77.708 1.00 56.08  ? 806  ILE   A C     1 
ATOM   4096 O  O     . ILE   A 1 657  ? 7.071   8.661   -78.312 1.00 57.27  ? 806  ILE   A O     1 
ATOM   4097 C  CB    . ILE   A 1 657  ? 7.457   5.359   -78.599 1.00 53.95  ? 806  ILE   A CB    1 
ATOM   4098 C  CG1   . ILE   A 1 657  ? 8.634   4.386   -78.704 1.00 54.48  ? 806  ILE   A CG1   1 
ATOM   4099 C  CG2   . ILE   A 1 657  ? 7.080   5.931   -79.957 1.00 53.73  ? 806  ILE   A CG2   1 
ATOM   4100 C  CD1   . ILE   A 1 657  ? 8.271   3.041   -79.294 1.00 54.67  ? 806  ILE   A CD1   1 
ATOM   4101 N  N     . LYS   A 1 658  ? 5.520   7.441   -77.160 1.00 56.38  ? 807  LYS   A N     1 
ATOM   4102 C  CA    . LYS   A 1 658  ? 4.387   8.396   -77.293 1.00 57.76  ? 807  LYS   A CA    1 
ATOM   4103 C  C     . LYS   A 1 658  ? 4.618   9.610   -76.385 1.00 58.67  ? 807  LYS   A C     1 
ATOM   4104 O  O     . LYS   A 1 658  ? 4.367   10.742  -76.851 1.00 58.48  ? 807  LYS   A O     1 
ATOM   4105 C  CB    . LYS   A 1 658  ? 3.059   7.693   -76.995 1.00 57.99  ? 807  LYS   A CB    1 
ATOM   4106 C  CG    . LYS   A 1 658  ? 2.544   6.822   -78.132 1.00 59.42  ? 807  LYS   A CG    1 
ATOM   4107 C  CD    . LYS   A 1 658  ? 2.003   7.621   -79.300 1.00 61.08  ? 807  LYS   A CD    1 
ATOM   4108 C  CE    . LYS   A 1 658  ? 2.184   6.934   -80.636 1.00 62.87  ? 807  LYS   A CE    1 
ATOM   4109 N  NZ    . LYS   A 1 658  ? 1.805   7.822   -81.761 1.00 63.32  ? 807  LYS   A NZ    1 
ATOM   4110 N  N     . LEU   A 1 659  ? 5.085   9.385   -75.151 1.00 59.45  ? 808  LEU   A N     1 
ATOM   4111 C  CA    . LEU   A 1 659  ? 5.380   10.460  -74.165 1.00 60.28  ? 808  LEU   A CA    1 
ATOM   4112 C  C     . LEU   A 1 659  ? 6.436   11.402  -74.751 1.00 61.33  ? 808  LEU   A C     1 
ATOM   4113 O  O     . LEU   A 1 659  ? 6.210   12.627  -74.718 1.00 62.82  ? 808  LEU   A O     1 
ATOM   4114 C  CB    . LEU   A 1 659  ? 5.872   9.842   -72.852 1.00 61.38  ? 808  LEU   A CB    1 
ATOM   4115 C  CG    . LEU   A 1 659  ? 6.066   10.827  -71.698 1.00 61.64  ? 808  LEU   A CG    1 
ATOM   4116 C  CD1   . LEU   A 1 659  ? 4.727   11.335  -71.189 1.00 62.27  ? 808  LEU   A CD1   1 
ATOM   4117 C  CD2   . LEU   A 1 659  ? 6.860   10.195  -70.565 1.00 62.03  ? 808  LEU   A CD2   1 
ATOM   4118 N  N     . LEU   A 1 660  ? 7.531   10.841  -75.277 1.00 62.20  ? 809  LEU   A N     1 
ATOM   4119 C  CA    . LEU   A 1 660  ? 8.690   11.598  -75.826 1.00 63.90  ? 809  LEU   A CA    1 
ATOM   4120 C  C     . LEU   A 1 660  ? 8.375   12.133  -77.230 1.00 65.89  ? 809  LEU   A C     1 
ATOM   4121 O  O     . LEU   A 1 660  ? 9.219   12.880  -77.767 1.00 64.01  ? 809  LEU   A O     1 
ATOM   4122 C  CB    . LEU   A 1 660  ? 9.921   10.685  -75.848 1.00 62.78  ? 809  LEU   A CB    1 
ATOM   4123 C  CG    . LEU   A 1 660  ? 10.418  10.215  -74.482 1.00 62.63  ? 809  LEU   A CG    1 
ATOM   4124 C  CD1   . LEU   A 1 660  ? 11.740  9.477   -74.616 1.00 62.68  ? 809  LEU   A CD1   1 
ATOM   4125 C  CD2   . LEU   A 1 660  ? 10.556  11.381  -73.514 1.00 62.95  ? 809  LEU   A CD2   1 
ATOM   4126 N  N     . ARG   A 1 661  ? 7.218   11.765  -77.797 1.00 69.83  ? 810  ARG   A N     1 
ATOM   4127 C  CA    . ARG   A 1 661  ? 6.701   12.266  -79.100 1.00 73.93  ? 810  ARG   A CA    1 
ATOM   4128 C  C     . ARG   A 1 661  ? 7.698   11.905  -80.208 1.00 71.72  ? 810  ARG   A C     1 
ATOM   4129 O  O     . ARG   A 1 661  ? 8.117   12.815  -80.948 1.00 73.19  ? 810  ARG   A O     1 
ATOM   4130 C  CB    . ARG   A 1 661  ? 6.440   13.776  -79.029 1.00 79.39  ? 810  ARG   A CB    1 
ATOM   4131 C  CG    . ARG   A 1 661  ? 5.443   14.185  -77.953 1.00 86.14  ? 810  ARG   A CG    1 
ATOM   4132 C  CD    . ARG   A 1 661  ? 5.158   15.678  -77.931 1.00 92.50  ? 810  ARG   A CD    1 
ATOM   4133 N  NE    . ARG   A 1 661  ? 4.544   16.155  -79.168 1.00 99.05  ? 810  ARG   A NE    1 
ATOM   4134 C  CZ    . ARG   A 1 661  ? 5.154   16.862  -80.124 1.00 102.09 ? 810  ARG   A CZ    1 
ATOM   4135 N  NH1   . ARG   A 1 661  ? 6.427   17.208  -80.012 1.00 103.92 ? 810  ARG   A NH1   1 
ATOM   4136 N  NH2   . ARG   A 1 661  ? 4.476   17.227  -81.200 1.00 101.49 ? 810  ARG   A NH2   1 
ATOM   4137 N  N     . LEU   A 1 662  ? 8.051   10.619  -80.311 1.00 68.67  ? 811  LEU   A N     1 
ATOM   4138 C  CA    . LEU   A 1 662  ? 9.014   10.078  -81.310 1.00 67.64  ? 811  LEU   A CA    1 
ATOM   4139 C  C     . LEU   A 1 662  ? 8.259   9.525   -82.527 1.00 65.56  ? 811  LEU   A C     1 
ATOM   4140 O  O     . LEU   A 1 662  ? 8.927   8.983   -83.430 1.00 65.68  ? 811  LEU   A O     1 
ATOM   4141 C  CB    . LEU   A 1 662  ? 9.860   8.987   -80.645 1.00 68.67  ? 811  LEU   A CB    1 
ATOM   4142 C  CG    . LEU   A 1 662  ? 10.589  9.403   -79.369 1.00 70.05  ? 811  LEU   A CG    1 
ATOM   4143 C  CD1   . LEU   A 1 662  ? 11.326  8.223   -78.755 1.00 70.56  ? 811  LEU   A CD1   1 
ATOM   4144 C  CD2   . LEU   A 1 662  ? 11.553  10.549  -79.639 1.00 70.16  ? 811  LEU   A CD2   1 
ATOM   4145 N  N     . GLY   A 1 663  ? 6.927   9.653   -82.548 1.00 63.73  ? 812  GLY   A N     1 
ATOM   4146 C  CA    . GLY   A 1 663  ? 6.066   9.250   -83.677 1.00 62.61  ? 812  GLY   A CA    1 
ATOM   4147 C  C     . GLY   A 1 663  ? 5.359   7.931   -83.413 1.00 60.70  ? 812  GLY   A C     1 
ATOM   4148 O  O     . GLY   A 1 663  ? 4.984   7.681   -82.251 1.00 59.60  ? 812  GLY   A O     1 
ATOM   4149 N  N     . GLY   A 1 664  ? 5.175   7.121   -84.459 1.00 59.31  ? 813  GLY   A N     1 
ATOM   4150 C  CA    . GLY   A 1 664  ? 4.436   5.846   -84.400 1.00 59.21  ? 813  GLY   A CA    1 
ATOM   4151 C  C     . GLY   A 1 664  ? 5.229   4.767   -83.684 1.00 58.31  ? 813  GLY   A C     1 
ATOM   4152 O  O     . GLY   A 1 664  ? 6.456   4.701   -83.897 1.00 58.40  ? 813  GLY   A O     1 
ATOM   4153 N  N     . ILE   A 1 665  ? 4.549   3.947   -82.876 1.00 56.58  ? 814  ILE   A N     1 
ATOM   4154 C  CA    . ILE   A 1 665  ? 5.155   2.829   -82.092 1.00 56.30  ? 814  ILE   A CA    1 
ATOM   4155 C  C     . ILE   A 1 665  ? 5.874   1.889   -83.065 1.00 56.18  ? 814  ILE   A C     1 
ATOM   4156 O  O     . ILE   A 1 665  ? 7.095   1.691   -82.904 1.00 57.46  ? 814  ILE   A O     1 
ATOM   4157 C  CB    . ILE   A 1 665  ? 4.084   2.101   -81.252 1.00 57.33  ? 814  ILE   A CB    1 
ATOM   4158 C  CG1   . ILE   A 1 665  ? 3.562   2.987   -80.117 1.00 57.60  ? 814  ILE   A CG1   1 
ATOM   4159 C  CG2   . ILE   A 1 665  ? 4.610   0.772   -80.729 1.00 57.49  ? 814  ILE   A CG2   1 
ATOM   4160 C  CD1   . ILE   A 1 665  ? 2.218   2.563   -79.567 1.00 57.79  ? 814  ILE   A CD1   1 
ATOM   4161 N  N     . GLY   A 1 666  ? 5.141   1.347   -84.042 1.00 55.73  ? 815  GLY   A N     1 
ATOM   4162 C  CA    . GLY   A 1 666  ? 5.673   0.431   -85.069 1.00 55.65  ? 815  GLY   A CA    1 
ATOM   4163 C  C     . GLY   A 1 666  ? 6.706   1.110   -85.950 1.00 55.63  ? 815  GLY   A C     1 
ATOM   4164 O  O     . GLY   A 1 666  ? 7.710   0.455   -86.286 1.00 54.09  ? 815  GLY   A O     1 
ATOM   4165 N  N     . GLN   A 1 667  ? 6.468   2.376   -86.307 1.00 58.01  ? 816  GLN   A N     1 
ATOM   4166 C  CA    . GLN   A 1 667  ? 7.350   3.192   -87.188 1.00 60.94  ? 816  GLN   A CA    1 
ATOM   4167 C  C     . GLN   A 1 667  ? 8.722   3.350   -86.526 1.00 59.70  ? 816  GLN   A C     1 
ATOM   4168 O  O     . GLN   A 1 667  ? 9.739   3.219   -87.234 1.00 57.25  ? 816  GLN   A O     1 
ATOM   4169 C  CB    . GLN   A 1 667  ? 6.736   4.568   -87.468 1.00 65.19  ? 816  GLN   A CB    1 
ATOM   4170 C  CG    . GLN   A 1 667  ? 5.609   4.552   -88.496 1.00 70.23  ? 816  GLN   A CG    1 
ATOM   4171 C  CD    . GLN   A 1 667  ? 4.249   4.253   -87.907 1.00 74.17  ? 816  GLN   A CD    1 
ATOM   4172 O  OE1   . GLN   A 1 667  ? 4.093   3.394   -87.038 1.00 75.41  ? 816  GLN   A OE1   1 
ATOM   4173 N  NE2   . GLN   A 1 667  ? 3.238   4.961   -88.389 1.00 75.69  ? 816  GLN   A NE2   1 
ATOM   4174 N  N     . PHE   A 1 668  ? 8.741   3.615   -85.216 1.00 60.24  ? 817  PHE   A N     1 
ATOM   4175 C  CA    . PHE   A 1 668  ? 9.969   3.891   -84.428 1.00 60.00  ? 817  PHE   A CA    1 
ATOM   4176 C  C     . PHE   A 1 668  ? 10.723  2.584   -84.155 1.00 58.34  ? 817  PHE   A C     1 
ATOM   4177 O  O     . PHE   A 1 668  ? 11.955  2.560   -84.335 1.00 56.53  ? 817  PHE   A O     1 
ATOM   4178 C  CB    . PHE   A 1 668  ? 9.639   4.615   -83.121 1.00 60.82  ? 817  PHE   A CB    1 
ATOM   4179 C  CG    . PHE   A 1 668  ? 10.861  5.124   -82.403 1.00 62.54  ? 817  PHE   A CG    1 
ATOM   4180 C  CD1   . PHE   A 1 668  ? 11.413  6.352   -82.734 1.00 63.10  ? 817  PHE   A CD1   1 
ATOM   4181 C  CD2   . PHE   A 1 668  ? 11.490  4.355   -81.435 1.00 62.96  ? 817  PHE   A CD2   1 
ATOM   4182 C  CE1   . PHE   A 1 668  ? 12.552  6.812   -82.091 1.00 64.34  ? 817  PHE   A CE1   1 
ATOM   4183 C  CE2   . PHE   A 1 668  ? 12.629  4.817   -80.794 1.00 63.32  ? 817  PHE   A CE2   1 
ATOM   4184 C  CZ    . PHE   A 1 668  ? 13.158  6.044   -81.122 1.00 63.89  ? 817  PHE   A CZ    1 
ATOM   4185 N  N     . LEU   A 1 669  ? 10.008  1.536   -83.733 1.00 58.40  ? 818  LEU   A N     1 
ATOM   4186 C  CA    . LEU   A 1 669  ? 10.594  0.210   -83.390 1.00 58.56  ? 818  LEU   A CA    1 
ATOM   4187 C  C     . LEU   A 1 669  ? 11.151  -0.468  -84.651 1.00 59.05  ? 818  LEU   A C     1 
ATOM   4188 O  O     . LEU   A 1 669  ? 11.980  -1.386  -84.499 1.00 60.37  ? 818  LEU   A O     1 
ATOM   4189 C  CB    . LEU   A 1 669  ? 9.529   -0.657  -82.710 1.00 57.84  ? 818  LEU   A CB    1 
ATOM   4190 C  CG    . LEU   A 1 669  ? 9.144   -0.224  -81.295 1.00 57.54  ? 818  LEU   A CG    1 
ATOM   4191 C  CD1   . LEU   A 1 669  ? 7.871   -0.919  -80.838 1.00 57.30  ? 818  LEU   A CD1   1 
ATOM   4192 C  CD2   . LEU   A 1 669  ? 10.277  -0.489  -80.317 1.00 57.37  ? 818  LEU   A CD2   1 
ATOM   4193 N  N     . ALA   A 1 670  ? 10.722  -0.034  -85.842 1.00 58.83  ? 819  ALA   A N     1 
ATOM   4194 C  CA    . ALA   A 1 670  ? 11.238  -0.499  -87.153 1.00 59.05  ? 819  ALA   A CA    1 
ATOM   4195 C  C     . ALA   A 1 670  ? 12.675  -0.005  -87.369 1.00 58.87  ? 819  ALA   A C     1 
ATOM   4196 O  O     . ALA   A 1 670  ? 13.405  -0.664  -88.131 1.00 59.75  ? 819  ALA   A O     1 
ATOM   4197 C  CB    . ALA   A 1 670  ? 10.331  -0.033  -88.265 1.00 59.29  ? 819  ALA   A CB    1 
ATOM   4198 N  N     . LYS   A 1 671  ? 13.057  1.110   -86.731 1.00 58.30  ? 820  LYS   A N     1 
ATOM   4199 C  CA    . LYS   A 1 671  ? 14.402  1.738   -86.856 1.00 57.83  ? 820  LYS   A CA    1 
ATOM   4200 C  C     . LYS   A 1 671  ? 15.391  1.096   -85.873 1.00 57.60  ? 820  LYS   A C     1 
ATOM   4201 O  O     . LYS   A 1 671  ? 16.581  1.460   -85.932 1.00 56.91  ? 820  LYS   A O     1 
ATOM   4202 C  CB    . LYS   A 1 671  ? 14.337  3.243   -86.582 1.00 57.91  ? 820  LYS   A CB    1 
ATOM   4203 C  CG    . LYS   A 1 671  ? 13.384  4.032   -87.467 1.00 59.33  ? 820  LYS   A CG    1 
ATOM   4204 C  CD    . LYS   A 1 671  ? 13.658  5.522   -87.468 1.00 60.78  ? 820  LYS   A CD    1 
ATOM   4205 C  CE    . LYS   A 1 671  ? 13.604  6.148   -86.090 1.00 61.43  ? 820  LYS   A CE    1 
ATOM   4206 N  NZ    . LYS   A 1 671  ? 13.825  7.613   -86.148 1.00 62.50  ? 820  LYS   A NZ    1 
ATOM   4207 N  N     . ALA   A 1 672  ? 14.925  0.195   -85.000 1.00 57.58  ? 821  ALA   A N     1 
ATOM   4208 C  CA    . ALA   A 1 672  ? 15.760  -0.511  -83.997 1.00 59.18  ? 821  ALA   A CA    1 
ATOM   4209 C  C     . ALA   A 1 672  ? 16.893  -1.265  -84.702 1.00 60.02  ? 821  ALA   A C     1 
ATOM   4210 O  O     . ALA   A 1 672  ? 16.737  -1.602  -85.891 1.00 61.35  ? 821  ALA   A O     1 
ATOM   4211 C  CB    . ALA   A 1 672  ? 14.913  -1.443  -83.166 1.00 58.61  ? 821  ALA   A CB    1 
ATOM   4212 N  N     . ILE   A 1 673  ? 17.995  -1.499  -83.987 1.00 61.93  ? 822  ILE   A N     1 
ATOM   4213 C  CA    . ILE   A 1 673  ? 19.208  -2.207  -84.499 1.00 63.21  ? 822  ILE   A CA    1 
ATOM   4214 C  C     . ILE   A 1 673  ? 18.821  -3.640  -84.898 1.00 61.43  ? 822  ILE   A C     1 
ATOM   4215 O  O     . ILE   A 1 673  ? 19.369  -4.138  -85.898 1.00 61.47  ? 822  ILE   A O     1 
ATOM   4216 C  CB    . ILE   A 1 673  ? 20.351  -2.151  -83.461 1.00 65.58  ? 822  ILE   A CB    1 
ATOM   4217 C  CG1   . ILE   A 1 673  ? 21.695  -2.543  -84.078 1.00 66.85  ? 822  ILE   A CG1   1 
ATOM   4218 C  CG2   . ILE   A 1 673  ? 20.038  -2.985  -82.225 1.00 66.46  ? 822  ILE   A CG2   1 
ATOM   4219 C  CD1   . ILE   A 1 673  ? 22.879  -2.231  -83.197 1.00 68.17  ? 822  ILE   A CD1   1 
ATOM   4220 N  N     . GLU   A 1 674  ? 17.912  -4.266  -84.141 1.00 60.60  ? 823  GLU   A N     1 
ATOM   4221 C  CA    . GLU   A 1 674  ? 17.238  -5.552  -84.471 1.00 59.18  ? 823  GLU   A CA    1 
ATOM   4222 C  C     . GLU   A 1 674  ? 15.774  -5.430  -84.057 1.00 58.08  ? 823  GLU   A C     1 
ATOM   4223 O  O     . GLU   A 1 674  ? 15.432  -5.720  -82.911 1.00 57.78  ? 823  GLU   A O     1 
ATOM   4224 C  CB    . GLU   A 1 674  ? 17.906  -6.735  -83.766 1.00 59.90  ? 823  GLU   A CB    1 
ATOM   4225 C  CG    . GLU   A 1 674  ? 19.313  -7.029  -84.260 1.00 61.97  ? 823  GLU   A CG    1 
ATOM   4226 C  CD    . GLU   A 1 674  ? 19.812  -8.442  -83.996 1.00 63.59  ? 823  GLU   A CD    1 
ATOM   4227 O  OE1   . GLU   A 1 674  ? 19.459  -9.012  -82.945 1.00 65.53  ? 823  GLU   A OE1   1 
ATOM   4228 O  OE2   . GLU   A 1 674  ? 20.554  -8.973  -84.848 1.00 63.93  ? 823  GLU   A OE2   1 
ATOM   4229 N  N     . PRO   A 1 675  ? 14.878  -4.967  -84.962 1.00 55.55  ? 824  PRO   A N     1 
ATOM   4230 C  CA    . PRO   A 1 675  ? 13.486  -4.680  -84.606 1.00 53.60  ? 824  PRO   A CA    1 
ATOM   4231 C  C     . PRO   A 1 675  ? 12.752  -5.850  -83.961 1.00 51.30  ? 824  PRO   A C     1 
ATOM   4232 O  O     . PRO   A 1 675  ? 13.088  -7.006  -84.201 1.00 51.08  ? 824  PRO   A O     1 
ATOM   4233 C  CB    . PRO   A 1 675  ? 12.834  -4.334  -85.954 1.00 54.54  ? 824  PRO   A CB    1 
ATOM   4234 C  CG    . PRO   A 1 675  ? 13.979  -3.814  -86.791 1.00 54.71  ? 824  PRO   A CG    1 
ATOM   4235 C  CD    . PRO   A 1 675  ? 15.165  -4.658  -86.372 1.00 55.36  ? 824  PRO   A CD    1 
ATOM   4236 N  N     . PRO   A 1 676  ? 11.728  -5.581  -83.118 1.00 50.25  ? 825  PRO   A N     1 
ATOM   4237 C  CA    . PRO   A 1 676  ? 10.952  -6.647  -82.487 1.00 49.17  ? 825  PRO   A CA    1 
ATOM   4238 C  C     . PRO   A 1 676  ? 10.030  -7.347  -83.482 1.00 49.13  ? 825  PRO   A C     1 
ATOM   4239 O  O     . PRO   A 1 676  ? 9.750   -6.816  -84.554 1.00 48.92  ? 825  PRO   A O     1 
ATOM   4240 C  CB    . PRO   A 1 676  ? 10.153  -5.911  -81.400 1.00 48.75  ? 825  PRO   A CB    1 
ATOM   4241 C  CG    . PRO   A 1 676  ? 10.007  -4.498  -81.925 1.00 48.79  ? 825  PRO   A CG    1 
ATOM   4242 C  CD    . PRO   A 1 676  ? 11.268  -4.239  -82.724 1.00 49.68  ? 825  PRO   A CD    1 
ATOM   4243 N  N     . PRO   A 1 677  ? 9.535   -8.566  -83.167 1.00 50.97  ? 826  PRO   A N     1 
ATOM   4244 C  CA    . PRO   A 1 677  ? 8.579   -9.251  -84.033 1.00 51.28  ? 826  PRO   A CA    1 
ATOM   4245 C  C     . PRO   A 1 677  ? 7.251   -8.482  -84.090 1.00 52.45  ? 826  PRO   A C     1 
ATOM   4246 O  O     . PRO   A 1 677  ? 6.945   -7.771  -83.150 1.00 52.78  ? 826  PRO   A O     1 
ATOM   4247 C  CB    . PRO   A 1 677  ? 8.418   -10.632 -83.380 1.00 51.38  ? 826  PRO   A CB    1 
ATOM   4248 C  CG    . PRO   A 1 677  ? 8.774   -10.402 -81.927 1.00 50.86  ? 826  PRO   A CG    1 
ATOM   4249 C  CD    . PRO   A 1 677  ? 9.859   -9.347  -81.963 1.00 51.57  ? 826  PRO   A CD    1 
ATOM   4250 N  N     . LEU   A 1 678  ? 6.512   -8.648  -85.189 1.00 53.89  ? 827  LEU   A N     1 
ATOM   4251 C  CA    . LEU   A 1 678  ? 5.272   -7.892  -85.511 1.00 54.69  ? 827  LEU   A CA    1 
ATOM   4252 C  C     . LEU   A 1 678  ? 4.246   -8.056  -84.384 1.00 55.38  ? 827  LEU   A C     1 
ATOM   4253 O  O     . LEU   A 1 678  ? 3.742   -7.029  -83.906 1.00 55.66  ? 827  LEU   A O     1 
ATOM   4254 C  CB    . LEU   A 1 678  ? 4.719   -8.403  -86.845 1.00 55.08  ? 827  LEU   A CB    1 
ATOM   4255 C  CG    . LEU   A 1 678  ? 3.374   -7.822  -87.274 1.00 55.42  ? 827  LEU   A CG    1 
ATOM   4256 C  CD1   . LEU   A 1 678  ? 3.473   -6.319  -87.483 1.00 55.39  ? 827  LEU   A CD1   1 
ATOM   4257 C  CD2   . LEU   A 1 678  ? 2.877   -8.510  -88.534 1.00 56.99  ? 827  LEU   A CD2   1 
ATOM   4258 N  N     . ASP   A 1 679  ? 3.954   -9.296  -83.980 1.00 58.21  ? 828  ASP   A N     1 
ATOM   4259 C  CA    . ASP   A 1 679  ? 2.858   -9.630  -83.027 1.00 60.17  ? 828  ASP   A CA    1 
ATOM   4260 C  C     . ASP   A 1 679  ? 3.084   -8.911  -81.689 1.00 59.86  ? 828  ASP   A C     1 
ATOM   4261 O  O     . ASP   A 1 679  ? 2.081   -8.536  -81.056 1.00 62.80  ? 828  ASP   A O     1 
ATOM   4262 C  CB    . ASP   A 1 679  ? 2.701   -11.143 -82.845 1.00 62.84  ? 828  ASP   A CB    1 
ATOM   4263 C  CG    . ASP   A 1 679  ? 3.942   -11.869 -82.353 1.00 65.60  ? 828  ASP   A CG    1 
ATOM   4264 O  OD1   . ASP   A 1 679  ? 4.979   -11.204 -82.158 1.00 68.51  ? 828  ASP   A OD1   1 
ATOM   4265 O  OD2   . ASP   A 1 679  ? 3.861   -13.101 -82.175 1.00 68.25  ? 828  ASP   A OD2   1 
ATOM   4266 N  N     . ALA   A 1 680  ? 4.344   -8.722  -81.284 1.00 58.51  ? 829  ALA   A N     1 
ATOM   4267 C  CA    . ALA   A 1 680  ? 4.746   -8.033  -80.034 1.00 57.10  ? 829  ALA   A CA    1 
ATOM   4268 C  C     . ALA   A 1 680  ? 4.346   -6.552  -80.091 1.00 56.39  ? 829  ALA   A C     1 
ATOM   4269 O  O     . ALA   A 1 680  ? 3.958   -6.004  -79.039 1.00 56.45  ? 829  ALA   A O     1 
ATOM   4270 C  CB    . ALA   A 1 680  ? 6.230   -8.193  -79.816 1.00 57.66  ? 829  ALA   A CB    1 
ATOM   4271 N  N     . VAL   A 1 681  ? 4.449   -5.929  -81.270 1.00 54.88  ? 830  VAL   A N     1 
ATOM   4272 C  CA    . VAL   A 1 681  ? 4.053   -4.509  -81.520 1.00 54.27  ? 830  VAL   A CA    1 
ATOM   4273 C  C     . VAL   A 1 681  ? 2.520   -4.431  -81.566 1.00 55.96  ? 830  VAL   A C     1 
ATOM   4274 O  O     . VAL   A 1 681  ? 1.960   -3.450  -81.036 1.00 55.77  ? 830  VAL   A O     1 
ATOM   4275 C  CB    . VAL   A 1 681  ? 4.688   -3.966  -82.816 1.00 52.02  ? 830  VAL   A CB    1 
ATOM   4276 C  CG1   . VAL   A 1 681  ? 4.279   -2.527  -83.088 1.00 51.93  ? 830  VAL   A CG1   1 
ATOM   4277 C  CG2   . VAL   A 1 681  ? 6.203   -4.091  -82.796 1.00 52.06  ? 830  VAL   A CG2   1 
ATOM   4278 N  N     . ILE   A 1 682  ? 1.876   -5.427  -82.184 1.00 57.18  ? 831  ILE   A N     1 
ATOM   4279 C  CA    . ILE   A 1 682  ? 0.391   -5.546  -82.300 1.00 58.18  ? 831  ILE   A CA    1 
ATOM   4280 C  C     . ILE   A 1 682  ? -0.190  -5.767  -80.899 1.00 59.27  ? 831  ILE   A C     1 
ATOM   4281 O  O     . ILE   A 1 682  ? -1.213  -5.129  -80.580 1.00 58.13  ? 831  ILE   A O     1 
ATOM   4282 C  CB    . ILE   A 1 682  ? -0.000  -6.679  -83.275 1.00 58.44  ? 831  ILE   A CB    1 
ATOM   4283 C  CG1   . ILE   A 1 682  ? 0.460   -6.391  -84.708 1.00 58.42  ? 831  ILE   A CG1   1 
ATOM   4284 C  CG2   . ILE   A 1 682  ? -1.494  -6.968  -83.213 1.00 57.81  ? 831  ILE   A CG2   1 
ATOM   4285 C  CD1   . ILE   A 1 682  ? -0.195  -5.185  -85.349 1.00 58.46  ? 831  ILE   A CD1   1 
ATOM   4286 N  N     . GLU   A 1 683  ? 0.445   -6.639  -80.107 1.00 61.30  ? 832  GLU   A N     1 
ATOM   4287 C  CA    . GLU   A 1 683  ? 0.030   -6.985  -78.721 1.00 63.44  ? 832  GLU   A CA    1 
ATOM   4288 C  C     . GLU   A 1 683  ? 0.149   -5.741  -77.830 1.00 61.14  ? 832  GLU   A C     1 
ATOM   4289 O  O     . GLU   A 1 683  ? -0.757  -5.520  -77.008 1.00 63.38  ? 832  GLU   A O     1 
ATOM   4290 C  CB    . GLU   A 1 683  ? 0.876   -8.140  -78.180 1.00 67.39  ? 832  GLU   A CB    1 
ATOM   4291 C  CG    . GLU   A 1 683  ? 0.370   -8.701  -76.863 1.00 72.79  ? 832  GLU   A CG    1 
ATOM   4292 C  CD    . GLU   A 1 683  ? -0.975  -9.404  -76.953 1.00 78.20  ? 832  GLU   A CD    1 
ATOM   4293 O  OE1   . GLU   A 1 683  ? -1.911  -8.982  -76.240 1.00 81.31  ? 832  GLU   A OE1   1 
ATOM   4294 O  OE2   . GLU   A 1 683  ? -1.083  -10.374 -77.733 1.00 82.89  ? 832  GLU   A OE2   1 
ATOM   4295 N  N     . ALA   A 1 684  ? 1.224   -4.965  -77.990 1.00 58.83  ? 833  ALA   A N     1 
ATOM   4296 C  CA    . ALA   A 1 684  ? 1.481   -3.714  -77.238 1.00 58.08  ? 833  ALA   A CA    1 
ATOM   4297 C  C     . ALA   A 1 684  ? 0.411   -2.675  -77.593 1.00 58.34  ? 833  ALA   A C     1 
ATOM   4298 O  O     . ALA   A 1 684  ? -0.166  -2.089  -76.661 1.00 60.71  ? 833  ALA   A O     1 
ATOM   4299 C  CB    . ALA   A 1 684  ? 2.870   -3.204  -77.532 1.00 57.79  ? 833  ALA   A CB    1 
ATOM   4300 N  N     . GLU   A 1 685  ? 0.154   -2.470  -78.889 1.00 58.34  ? 834  GLU   A N     1 
ATOM   4301 C  CA    . GLU   A 1 685  ? -0.841  -1.488  -79.404 1.00 59.58  ? 834  GLU   A CA    1 
ATOM   4302 C  C     . GLU   A 1 685  ? -2.246  -1.877  -78.924 1.00 60.10  ? 834  GLU   A C     1 
ATOM   4303 O  O     . GLU   A 1 685  ? -3.023  -0.964  -78.586 1.00 58.67  ? 834  GLU   A O     1 
ATOM   4304 C  CB    . GLU   A 1 685  ? -0.761  -1.394  -80.930 1.00 61.38  ? 834  GLU   A CB    1 
ATOM   4305 C  CG    . GLU   A 1 685  ? 0.436   -0.589  -81.416 1.00 63.38  ? 834  GLU   A CG    1 
ATOM   4306 C  CD    . GLU   A 1 685  ? 0.694   -0.607  -82.915 1.00 63.71  ? 834  GLU   A CD    1 
ATOM   4307 O  OE1   . GLU   A 1 685  ? 0.182   -1.519  -83.598 1.00 63.82  ? 834  GLU   A OE1   1 
ATOM   4308 O  OE2   . GLU   A 1 685  ? 1.414   0.294   -83.397 1.00 62.19  ? 834  GLU   A OE2   1 
ATOM   4309 N  N     . HIS   A 1 686  ? -2.552  -3.178  -78.881 1.00 62.91  ? 835  HIS   A N     1 
ATOM   4310 C  CA    . HIS   A 1 686  ? -3.845  -3.732  -78.392 1.00 65.63  ? 835  HIS   A CA    1 
ATOM   4311 C  C     . HIS   A 1 686  ? -3.993  -3.468  -76.887 1.00 63.27  ? 835  HIS   A C     1 
ATOM   4312 O  O     . HIS   A 1 686  ? -5.070  -2.991  -76.478 1.00 62.08  ? 835  HIS   A O     1 
ATOM   4313 C  CB    . HIS   A 1 686  ? -3.954  -5.229  -78.724 1.00 69.88  ? 835  HIS   A CB    1 
ATOM   4314 C  CG    . HIS   A 1 686  ? -5.239  -5.850  -78.284 1.00 74.03  ? 835  HIS   A CG    1 
ATOM   4315 N  ND1   . HIS   A 1 686  ? -6.395  -5.771  -79.040 1.00 76.64  ? 835  HIS   A ND1   1 
ATOM   4316 C  CD2   . HIS   A 1 686  ? -5.557  -6.550  -77.174 1.00 75.56  ? 835  HIS   A CD2   1 
ATOM   4317 C  CE1   . HIS   A 1 686  ? -7.370  -6.398  -78.413 1.00 77.80  ? 835  HIS   A CE1   1 
ATOM   4318 N  NE2   . HIS   A 1 686  ? -6.881  -6.887  -77.264 1.00 77.55  ? 835  HIS   A NE2   1 
ATOM   4319 N  N     . THR   A 1 687  ? -2.952  -3.776  -76.105 1.00 61.53  ? 836  THR   A N     1 
ATOM   4320 C  CA    . THR   A 1 687  ? -2.898  -3.606  -74.627 1.00 61.88  ? 836  THR   A CA    1 
ATOM   4321 C  C     . THR   A 1 687  ? -3.246  -2.157  -74.261 1.00 62.00  ? 836  THR   A C     1 
ATOM   4322 O  O     . THR   A 1 687  ? -4.090  -1.962  -73.363 1.00 61.69  ? 836  THR   A O     1 
ATOM   4323 C  CB    . THR   A 1 687  ? -1.522  -4.012  -74.081 1.00 61.87  ? 836  THR   A CB    1 
ATOM   4324 O  OG1   . THR   A 1 687  ? -1.321  -5.390  -74.395 1.00 62.78  ? 836  THR   A OG1   1 
ATOM   4325 C  CG2   . THR   A 1 687  ? -1.379  -3.816  -72.588 1.00 61.89  ? 836  THR   A CG2   1 
ATOM   4326 N  N     . LEU   A 1 688  ? -2.625  -1.188  -74.938 1.00 61.93  ? 837  LEU   A N     1 
ATOM   4327 C  CA    . LEU   A 1 688  ? -2.749  0.263   -74.629 1.00 62.34  ? 837  LEU   A CA    1 
ATOM   4328 C  C     . LEU   A 1 688  ? -4.103  0.799   -75.112 1.00 65.08  ? 837  LEU   A C     1 
ATOM   4329 O  O     . LEU   A 1 688  ? -4.610  1.742   -74.479 1.00 67.81  ? 837  LEU   A O     1 
ATOM   4330 C  CB    . LEU   A 1 688  ? -1.587  1.016   -75.281 1.00 60.23  ? 837  LEU   A CB    1 
ATOM   4331 C  CG    . LEU   A 1 688  ? -0.199  0.649   -74.761 1.00 59.33  ? 837  LEU   A CG    1 
ATOM   4332 C  CD1   . LEU   A 1 688  ? 0.880   1.289   -75.619 1.00 59.71  ? 837  LEU   A CD1   1 
ATOM   4333 C  CD2   . LEU   A 1 688  ? -0.036  1.053   -73.303 1.00 59.28  ? 837  LEU   A CD2   1 
ATOM   4334 N  N     . ARG   A 1 689  ? -4.662  0.235   -76.188 1.00 68.58  ? 838  ARG   A N     1 
ATOM   4335 C  CA    . ARG   A 1 689  ? -6.016  0.599   -76.690 1.00 70.41  ? 838  ARG   A CA    1 
ATOM   4336 C  C     . ARG   A 1 689  ? -7.065  0.137   -75.670 1.00 70.50  ? 838  ARG   A C     1 
ATOM   4337 O  O     . ARG   A 1 689  ? -7.944  0.950   -75.333 1.00 69.39  ? 838  ARG   A O     1 
ATOM   4338 C  CB    . ARG   A 1 689  ? -6.268  0.015   -78.085 1.00 72.05  ? 838  ARG   A CB    1 
ATOM   4339 C  CG    . ARG   A 1 689  ? -5.792  0.908   -79.225 1.00 74.20  ? 838  ARG   A CG    1 
ATOM   4340 C  CD    . ARG   A 1 689  ? -6.431  0.564   -80.558 1.00 76.03  ? 838  ARG   A CD    1 
ATOM   4341 N  NE    . ARG   A 1 689  ? -5.832  -0.609  -81.186 1.00 76.75  ? 838  ARG   A NE    1 
ATOM   4342 C  CZ    . ARG   A 1 689  ? -4.706  -0.608  -81.899 1.00 77.10  ? 838  ARG   A CZ    1 
ATOM   4343 N  NH1   . ARG   A 1 689  ? -4.260  -1.738  -82.422 1.00 77.36  ? 838  ARG   A NH1   1 
ATOM   4344 N  NH2   . ARG   A 1 689  ? -4.026  0.511   -82.089 1.00 76.22  ? 838  ARG   A NH2   1 
ATOM   4345 N  N     . GLU   A 1 690  ? -6.952  -1.104  -75.183 1.00 73.56  ? 839  GLU   A N     1 
ATOM   4346 C  CA    . GLU   A 1 690  ? -7.841  -1.710  -74.150 1.00 75.20  ? 839  GLU   A CA    1 
ATOM   4347 C  C     . GLU   A 1 690  ? -7.892  -0.818  -72.902 1.00 72.77  ? 839  GLU   A C     1 
ATOM   4348 O  O     . GLU   A 1 690  ? -8.995  -0.634  -72.359 1.00 75.28  ? 839  GLU   A O     1 
ATOM   4349 C  CB    . GLU   A 1 690  ? -7.351  -3.110  -73.769 1.00 80.12  ? 839  GLU   A CB    1 
ATOM   4350 C  CG    . GLU   A 1 690  ? -7.669  -4.175  -74.804 1.00 83.49  ? 839  GLU   A CG    1 
ATOM   4351 C  CD    . GLU   A 1 690  ? -8.962  -4.936  -74.558 1.00 87.79  ? 839  GLU   A CD    1 
ATOM   4352 O  OE1   . GLU   A 1 690  ? -9.134  -5.461  -73.436 1.00 87.80  ? 839  GLU   A OE1   1 
ATOM   4353 O  OE2   . GLU   A 1 690  ? -9.793  -5.003  -75.488 1.00 91.83  ? 839  GLU   A OE2   1 
ATOM   4354 N  N     . LEU   A 1 691  ? -6.742  -0.289  -72.470 1.00 68.73  ? 840  LEU   A N     1 
ATOM   4355 C  CA    . LEU   A 1 691  ? -6.604  0.560   -71.254 1.00 65.79  ? 840  LEU   A CA    1 
ATOM   4356 C  C     . LEU   A 1 691  ? -7.069  1.996   -71.528 1.00 65.57  ? 840  LEU   A C     1 
ATOM   4357 O  O     . LEU   A 1 691  ? -7.109  2.774   -70.560 1.00 66.03  ? 840  LEU   A O     1 
ATOM   4358 C  CB    . LEU   A 1 691  ? -5.138  0.567   -70.808 1.00 65.41  ? 840  LEU   A CB    1 
ATOM   4359 C  CG    . LEU   A 1 691  ? -4.624  -0.725  -70.180 1.00 65.25  ? 840  LEU   A CG    1 
ATOM   4360 C  CD1   . LEU   A 1 691  ? -3.106  -0.704  -70.081 1.00 65.19  ? 840  LEU   A CD1   1 
ATOM   4361 C  CD2   . LEU   A 1 691  ? -5.246  -0.948  -68.810 1.00 64.73  ? 840  LEU   A CD2   1 
ATOM   4362 N  N     . ASP   A 1 692  ? -7.377  2.341   -72.784 1.00 65.57  ? 841  ASP   A N     1 
ATOM   4363 C  CA    . ASP   A 1 692  ? -7.678  3.728   -73.237 1.00 66.80  ? 841  ASP   A CA    1 
ATOM   4364 C  C     . ASP   A 1 692  ? -6.459  4.622   -72.972 1.00 65.53  ? 841  ASP   A C     1 
ATOM   4365 O  O     . ASP   A 1 692  ? -6.651  5.825   -72.709 1.00 63.90  ? 841  ASP   A O     1 
ATOM   4366 C  CB    . ASP   A 1 692  ? -8.941  4.286   -72.568 1.00 71.24  ? 841  ASP   A CB    1 
ATOM   4367 C  CG    . ASP   A 1 692  ? -10.248 3.852   -73.212 1.00 74.00  ? 841  ASP   A CG    1 
ATOM   4368 O  OD1   . ASP   A 1 692  ? -10.290 3.756   -74.456 1.00 75.51  ? 841  ASP   A OD1   1 
ATOM   4369 O  OD2   . ASP   A 1 692  ? -11.221 3.632   -72.461 1.00 77.21  ? 841  ASP   A OD2   1 
ATOM   4370 N  N     . ALA   A 1 693  ? -5.250  4.055   -73.040 1.00 65.96  ? 842  ALA   A N     1 
ATOM   4371 C  CA    . ALA   A 1 693  ? -3.967  4.793   -72.990 1.00 65.80  ? 842  ALA   A CA    1 
ATOM   4372 C  C     . ALA   A 1 693  ? -3.736  5.450   -74.355 1.00 66.70  ? 842  ALA   A C     1 
ATOM   4373 O  O     . ALA   A 1 693  ? -3.280  6.606   -74.387 1.00 68.23  ? 842  ALA   A O     1 
ATOM   4374 C  CB    . ALA   A 1 693  ? -2.840  3.862   -72.613 1.00 64.87  ? 842  ALA   A CB    1 
ATOM   4375 N  N     . LEU   A 1 694  ? -4.050  4.724   -75.434 1.00 69.65  ? 843  LEU   A N     1 
ATOM   4376 C  CA    . LEU   A 1 694  ? -4.132  5.245   -76.825 1.00 72.79  ? 843  LEU   A CA    1 
ATOM   4377 C  C     . LEU   A 1 694  ? -5.608  5.375   -77.220 1.00 77.68  ? 843  LEU   A C     1 
ATOM   4378 O  O     . LEU   A 1 694  ? -6.457  4.755   -76.549 1.00 80.91  ? 843  LEU   A O     1 
ATOM   4379 C  CB    . LEU   A 1 694  ? -3.402  4.286   -77.770 1.00 71.54  ? 843  LEU   A CB    1 
ATOM   4380 C  CG    . LEU   A 1 694  ? -1.906  4.107   -77.514 1.00 72.02  ? 843  LEU   A CG    1 
ATOM   4381 C  CD1   . LEU   A 1 694  ? -1.313  3.089   -78.476 1.00 71.59  ? 843  LEU   A CD1   1 
ATOM   4382 C  CD2   . LEU   A 1 694  ? -1.169  5.433   -77.621 1.00 72.50  ? 843  LEU   A CD2   1 
ATOM   4383 N  N     . ASP   A 1 695  ? -5.888  6.148   -78.275 1.00 81.30  ? 844  ASP   A N     1 
ATOM   4384 C  CA    . ASP   A 1 695  ? -7.236  6.296   -78.890 1.00 84.12  ? 844  ASP   A CA    1 
ATOM   4385 C  C     . ASP   A 1 695  ? -7.251  5.505   -80.209 1.00 89.40  ? 844  ASP   A C     1 
ATOM   4386 O  O     . ASP   A 1 695  ? -6.372  4.636   -80.382 1.00 90.77  ? 844  ASP   A O     1 
ATOM   4387 C  CB    . ASP   A 1 695  ? -7.605  7.778   -79.031 1.00 83.27  ? 844  ASP   A CB    1 
ATOM   4388 C  CG    . ASP   A 1 695  ? -6.584  8.626   -79.772 1.00 82.50  ? 844  ASP   A CG    1 
ATOM   4389 O  OD1   . ASP   A 1 695  ? -5.888  8.079   -80.651 1.00 82.40  ? 844  ASP   A OD1   1 
ATOM   4390 O  OD2   . ASP   A 1 695  ? -6.491  9.831   -79.460 1.00 80.22  ? 844  ASP   A OD2   1 
ATOM   4391 N  N     . ALA   A 1 696  ? -8.220  5.771   -81.092 1.00 95.44  ? 845  ALA   A N     1 
ATOM   4392 C  CA    . ALA   A 1 696  ? -8.341  5.147   -82.433 1.00 97.91  ? 845  ALA   A CA    1 
ATOM   4393 C  C     . ALA   A 1 696  ? -7.214  5.644   -83.349 1.00 99.13  ? 845  ALA   A C     1 
ATOM   4394 O  O     . ALA   A 1 696  ? -6.806  4.879   -84.246 1.00 98.34  ? 845  ALA   A O     1 
ATOM   4395 C  CB    . ALA   A 1 696  ? -9.698  5.444   -83.023 1.00 99.04  ? 845  ALA   A CB    1 
ATOM   4396 N  N     . ASN   A 1 697  ? -6.729  6.872   -83.121 1.00 99.64  ? 846  ASN   A N     1 
ATOM   4397 C  CA    . ASN   A 1 697  ? -5.627  7.512   -83.893 1.00 99.13  ? 846  ASN   A CA    1 
ATOM   4398 C  C     . ASN   A 1 697  ? -4.261  7.079   -83.332 1.00 96.65  ? 846  ASN   A C     1 
ATOM   4399 O  O     . ASN   A 1 697  ? -3.238  7.620   -83.805 1.00 96.53  ? 846  ASN   A O     1 
ATOM   4400 C  CB    . ASN   A 1 697  ? -5.760  9.040   -83.898 1.00 100.31 ? 846  ASN   A CB    1 
ATOM   4401 C  CG    . ASN   A 1 697  ? -6.993  9.535   -84.626 1.00 100.37 ? 846  ASN   A CG    1 
ATOM   4402 O  OD1   . ASN   A 1 697  ? -7.839  8.744   -85.040 1.00 101.07 ? 846  ASN   A OD1   1 
ATOM   4403 N  ND2   . ASN   A 1 697  ? -7.105  10.844  -84.789 1.00 97.70  ? 846  ASN   A ND2   1 
ATOM   4404 N  N     . ASP   A 1 698  ? -4.243  6.147   -82.368 1.00 91.72  ? 847  ASP   A N     1 
ATOM   4405 C  CA    . ASP   A 1 698  ? -3.023  5.628   -81.688 1.00 87.30  ? 847  ASP   A CA    1 
ATOM   4406 C  C     . ASP   A 1 698  ? -2.229  6.798   -81.085 1.00 83.00  ? 847  ASP   A C     1 
ATOM   4407 O  O     . ASP   A 1 698  ? -0.991  6.684   -80.983 1.00 80.99  ? 847  ASP   A O     1 
ATOM   4408 C  CB    . ASP   A 1 698  ? -2.179  4.772   -82.641 1.00 86.86  ? 847  ASP   A CB    1 
ATOM   4409 C  CG    . ASP   A 1 698  ? -2.690  3.351   -82.815 1.00 86.41  ? 847  ASP   A CG    1 
ATOM   4410 O  OD1   . ASP   A 1 698  ? -3.884  3.114   -82.535 1.00 86.31  ? 847  ASP   A OD1   1 
ATOM   4411 O  OD2   . ASP   A 1 698  ? -1.887  2.487   -83.222 1.00 84.46  ? 847  ASP   A OD2   1 
ATOM   4412 N  N     . GLU   A 1 699  ? -2.921  7.868   -80.679 1.00 79.07  ? 848  GLU   A N     1 
ATOM   4413 C  CA    . GLU   A 1 699  ? -2.312  9.073   -80.054 1.00 79.11  ? 848  GLU   A CA    1 
ATOM   4414 C  C     . GLU   A 1 699  ? -2.566  9.026   -78.544 1.00 77.18  ? 848  GLU   A C     1 
ATOM   4415 O  O     . GLU   A 1 699  ? -3.628  8.516   -78.131 1.00 76.49  ? 848  GLU   A O     1 
ATOM   4416 C  CB    . GLU   A 1 699  ? -2.856  10.355  -80.689 1.00 80.58  ? 848  GLU   A CB    1 
ATOM   4417 C  CG    . GLU   A 1 699  ? -2.101  10.780  -81.938 1.00 82.70  ? 848  GLU   A CG    1 
ATOM   4418 C  CD    . GLU   A 1 699  ? -0.608  11.007  -81.751 1.00 84.57  ? 848  GLU   A CD    1 
ATOM   4419 O  OE1   . GLU   A 1 699  ? -0.199  11.399  -80.635 1.00 86.36  ? 848  GLU   A OE1   1 
ATOM   4420 O  OE2   . GLU   A 1 699  ? 0.147   10.781  -82.719 1.00 83.36  ? 848  GLU   A OE2   1 
ATOM   4421 N  N     . LEU   A 1 700  ? -1.614  9.541   -77.763 1.00 74.21  ? 849  LEU   A N     1 
ATOM   4422 C  CA    . LEU   A 1 700  ? -1.584  9.421   -76.281 1.00 72.30  ? 849  LEU   A CA    1 
ATOM   4423 C  C     . LEU   A 1 700  ? -2.756  10.208  -75.686 1.00 70.76  ? 849  LEU   A C     1 
ATOM   4424 O  O     . LEU   A 1 700  ? -2.904  11.399  -76.028 1.00 72.17  ? 849  LEU   A O     1 
ATOM   4425 C  CB    . LEU   A 1 700  ? -0.236  9.942   -75.770 1.00 71.14  ? 849  LEU   A CB    1 
ATOM   4426 C  CG    . LEU   A 1 700  ? 0.137   9.544   -74.344 1.00 69.73  ? 849  LEU   A CG    1 
ATOM   4427 C  CD1   . LEU   A 1 700  ? 0.261   8.032   -74.211 1.00 69.60  ? 849  LEU   A CD1   1 
ATOM   4428 C  CD2   . LEU   A 1 700  ? 1.430   10.225  -73.922 1.00 69.97  ? 849  LEU   A CD2   1 
ATOM   4429 N  N     . THR   A 1 701  ? -3.558  9.552   -74.842 1.00 68.04  ? 850  THR   A N     1 
ATOM   4430 C  CA    . THR   A 1 701  ? -4.707  10.147  -74.108 1.00 68.05  ? 850  THR   A CA    1 
ATOM   4431 C  C     . THR   A 1 701  ? -4.189  10.767  -72.813 1.00 69.21  ? 850  THR   A C     1 
ATOM   4432 O  O     . THR   A 1 701  ? -3.075  10.467  -72.392 1.00 71.18  ? 850  THR   A O     1 
ATOM   4433 C  CB    . THR   A 1 701  ? -5.786  9.094   -73.827 1.00 67.77  ? 850  THR   A CB    1 
ATOM   4434 O  OG1   . THR   A 1 701  ? -5.265  8.178   -72.863 1.00 67.72  ? 850  THR   A OG1   1 
ATOM   4435 C  CG2   . THR   A 1 701  ? -6.224  8.345   -75.067 1.00 67.97  ? 850  THR   A CG2   1 
ATOM   4436 N  N     . PRO   A 1 702  ? -4.965  11.653  -72.145 1.00 69.99  ? 851  PRO   A N     1 
ATOM   4437 C  CA    . PRO   A 1 702  ? -4.589  12.160  -70.824 1.00 70.58  ? 851  PRO   A CA    1 
ATOM   4438 C  C     . PRO   A 1 702  ? -4.303  11.034  -69.814 1.00 70.04  ? 851  PRO   A C     1 
ATOM   4439 O  O     . PRO   A 1 702  ? -3.398  11.189  -69.009 1.00 70.85  ? 851  PRO   A O     1 
ATOM   4440 C  CB    . PRO   A 1 702  ? -5.811  12.987  -70.390 1.00 71.08  ? 851  PRO   A CB    1 
ATOM   4441 C  CG    . PRO   A 1 702  ? -6.463  13.399  -71.692 1.00 70.61  ? 851  PRO   A CG    1 
ATOM   4442 C  CD    . PRO   A 1 702  ? -6.224  12.237  -72.633 1.00 70.37  ? 851  PRO   A CD    1 
ATOM   4443 N  N     . LEU   A 1 703  ? -5.081  9.946   -69.882 1.00 67.38  ? 852  LEU   A N     1 
ATOM   4444 C  CA    . LEU   A 1 703  ? -4.896  8.710   -69.070 1.00 66.43  ? 852  LEU   A CA    1 
ATOM   4445 C  C     . LEU   A 1 703  ? -3.544  8.072   -69.418 1.00 64.98  ? 852  LEU   A C     1 
ATOM   4446 O  O     . LEU   A 1 703  ? -2.770  7.782   -68.486 1.00 63.27  ? 852  LEU   A O     1 
ATOM   4447 C  CB    . LEU   A 1 703  ? -6.063  7.754   -69.349 1.00 66.55  ? 852  LEU   A CB    1 
ATOM   4448 C  CG    . LEU   A 1 703  ? -5.895  6.311   -68.872 1.00 66.78  ? 852  LEU   A CG    1 
ATOM   4449 C  CD1   . LEU   A 1 703  ? -5.579  6.237   -67.387 1.00 67.56  ? 852  LEU   A CD1   1 
ATOM   4450 C  CD2   . LEU   A 1 703  ? -7.145  5.503   -69.179 1.00 67.55  ? 852  LEU   A CD2   1 
ATOM   4451 N  N     . GLY   A 1 704  ? -3.278  7.872   -70.713 1.00 64.35  ? 853  GLY   A N     1 
ATOM   4452 C  CA    . GLY   A 1 704  ? -2.022  7.297   -71.235 1.00 64.18  ? 853  GLY   A CA    1 
ATOM   4453 C  C     . GLY   A 1 704  ? -0.803  8.101   -70.816 1.00 63.59  ? 853  GLY   A C     1 
ATOM   4454 O  O     . GLY   A 1 704  ? 0.257   7.485   -70.583 1.00 61.07  ? 853  GLY   A O     1 
ATOM   4455 N  N     . ARG   A 1 705  ? -0.943  9.429   -70.726 1.00 65.92  ? 854  ARG   A N     1 
ATOM   4456 C  CA    . ARG   A 1 705  ? 0.140   10.359  -70.308 1.00 68.33  ? 854  ARG   A CA    1 
ATOM   4457 C  C     . ARG   A 1 705  ? 0.507   10.076  -68.847 1.00 68.98  ? 854  ARG   A C     1 
ATOM   4458 O  O     . ARG   A 1 705  ? 1.716   10.043  -68.545 1.00 71.79  ? 854  ARG   A O     1 
ATOM   4459 C  CB    . ARG   A 1 705  ? -0.281  11.819  -70.499 1.00 70.80  ? 854  ARG   A CB    1 
ATOM   4460 C  CG    . ARG   A 1 705  ? 0.869   12.812  -70.380 1.00 74.06  ? 854  ARG   A CG    1 
ATOM   4461 C  CD    . ARG   A 1 705  ? 0.459   14.254  -70.621 1.00 75.10  ? 854  ARG   A CD    1 
ATOM   4462 N  NE    . ARG   A 1 705  ? -0.509  14.366  -71.705 1.00 76.81  ? 854  ARG   A NE    1 
ATOM   4463 C  CZ    . ARG   A 1 705  ? -0.231  14.241  -73.001 1.00 79.01  ? 854  ARG   A CZ    1 
ATOM   4464 N  NH1   . ARG   A 1 705  ? -1.204  14.354  -73.891 1.00 80.34  ? 854  ARG   A NH1   1 
ATOM   4465 N  NH2   . ARG   A 1 705  ? 1.005   14.002  -73.410 1.00 79.37  ? 854  ARG   A NH2   1 
ATOM   4466 N  N     . ILE   A 1 706  ? -0.497  9.870   -67.988 1.00 67.68  ? 855  ILE   A N     1 
ATOM   4467 C  CA    . ILE   A 1 706  ? -0.317  9.542   -66.541 1.00 67.44  ? 855  ILE   A CA    1 
ATOM   4468 C  C     . ILE   A 1 706  ? 0.404   8.193   -66.430 1.00 67.40  ? 855  ILE   A C     1 
ATOM   4469 O  O     . ILE   A 1 706  ? 1.412   8.124   -65.701 1.00 68.48  ? 855  ILE   A O     1 
ATOM   4470 C  CB    . ILE   A 1 706  ? -1.667  9.542   -65.792 1.00 67.79  ? 855  ILE   A CB    1 
ATOM   4471 C  CG1   . ILE   A 1 706  ? -2.298  10.937  -65.759 1.00 68.69  ? 855  ILE   A CG1   1 
ATOM   4472 C  CG2   . ILE   A 1 706  ? -1.509  8.969   -64.390 1.00 67.83  ? 855  ILE   A CG2   1 
ATOM   4473 C  CD1   . ILE   A 1 706  ? -3.780  10.936  -65.469 1.00 68.91  ? 855  ILE   A CD1   1 
ATOM   4474 N  N     . LEU   A 1 707  ? -0.087  7.169   -67.137 1.00 67.20  ? 856  LEU   A N     1 
ATOM   4475 C  CA    . LEU   A 1 707  ? 0.454   5.782   -67.091 1.00 67.53  ? 856  LEU   A CA    1 
ATOM   4476 C  C     . LEU   A 1 707  ? 1.933   5.784   -67.495 1.00 70.04  ? 856  LEU   A C     1 
ATOM   4477 O  O     . LEU   A 1 707  ? 2.693   4.988   -66.916 1.00 72.60  ? 856  LEU   A O     1 
ATOM   4478 C  CB    . LEU   A 1 707  ? -0.366  4.875   -68.015 1.00 64.70  ? 856  LEU   A CB    1 
ATOM   4479 C  CG    . LEU   A 1 707  ? -1.803  4.596   -67.578 1.00 61.95  ? 856  LEU   A CG    1 
ATOM   4480 C  CD1   . LEU   A 1 707  ? -2.464  3.596   -68.513 1.00 61.35  ? 856  LEU   A CD1   1 
ATOM   4481 C  CD2   . LEU   A 1 707  ? -1.857  4.088   -66.149 1.00 61.78  ? 856  LEU   A CD2   1 
ATOM   4482 N  N     . ALA   A 1 708  ? 2.318   6.638   -68.449 1.00 71.62  ? 857  ALA   A N     1 
ATOM   4483 C  CA    . ALA   A 1 708  ? 3.700   6.761   -68.973 1.00 73.19  ? 857  ALA   A CA    1 
ATOM   4484 C  C     . ALA   A 1 708  ? 4.631   7.297   -67.878 1.00 73.67  ? 857  ALA   A C     1 
ATOM   4485 O  O     . ALA   A 1 708  ? 5.773   6.801   -67.779 1.00 74.75  ? 857  ALA   A O     1 
ATOM   4486 C  CB    . ALA   A 1 708  ? 3.714   7.654   -70.189 1.00 74.39  ? 857  ALA   A CB    1 
ATOM   4487 N  N     . LYS   A 1 709  ? 4.158   8.272   -67.095 1.00 73.91  ? 858  LYS   A N     1 
ATOM   4488 C  CA    . LYS   A 1 709  ? 4.933   8.944   -66.016 1.00 74.92  ? 858  LYS   A CA    1 
ATOM   4489 C  C     . LYS   A 1 709  ? 5.102   7.992   -64.824 1.00 72.67  ? 858  LYS   A C     1 
ATOM   4490 O  O     . LYS   A 1 709  ? 6.168   8.047   -64.178 1.00 72.93  ? 858  LYS   A O     1 
ATOM   4491 C  CB    . LYS   A 1 709  ? 4.246   10.248  -65.596 1.00 77.29  ? 858  LYS   A CB    1 
ATOM   4492 C  CG    . LYS   A 1 709  ? 4.205   11.321  -66.675 1.00 79.65  ? 858  LYS   A CG    1 
ATOM   4493 C  CD    . LYS   A 1 709  ? 3.687   12.659  -66.195 1.00 81.67  ? 858  LYS   A CD    1 
ATOM   4494 C  CE    . LYS   A 1 709  ? 3.600   13.684  -67.306 1.00 83.22  ? 858  LYS   A CE    1 
ATOM   4495 N  NZ    . LYS   A 1 709  ? 3.379   15.049  -66.772 1.00 84.99  ? 858  LYS   A NZ    1 
ATOM   4496 N  N     . LEU   A 1 710  ? 4.090   7.165   -64.542 1.00 70.03  ? 859  LEU   A N     1 
ATOM   4497 C  CA    . LEU   A 1 710  ? 4.124   6.127   -63.475 1.00 67.33  ? 859  LEU   A CA    1 
ATOM   4498 C  C     . LEU   A 1 710  ? 5.056   4.996   -63.904 1.00 64.76  ? 859  LEU   A C     1 
ATOM   4499 O  O     . LEU   A 1 710  ? 4.835   4.368   -64.936 1.00 66.73  ? 859  LEU   A O     1 
ATOM   4500 C  CB    . LEU   A 1 710  ? 2.707   5.600   -63.224 1.00 67.20  ? 859  LEU   A CB    1 
ATOM   4501 C  CG    . LEU   A 1 710  ? 1.735   6.592   -62.587 1.00 67.62  ? 859  LEU   A CG    1 
ATOM   4502 C  CD1   . LEU   A 1 710  ? 0.320   6.032   -62.577 1.00 66.69  ? 859  LEU   A CD1   1 
ATOM   4503 C  CD2   . LEU   A 1 710  ? 2.176   6.959   -61.177 1.00 67.40  ? 859  LEU   A CD2   1 
ATOM   4504 N  N     . PRO   A 1 711  ? 6.127   4.700   -63.134 1.00 61.50  ? 860  PRO   A N     1 
ATOM   4505 C  CA    . PRO   A 1 711  ? 7.037   3.603   -63.468 1.00 59.76  ? 860  PRO   A CA    1 
ATOM   4506 C  C     . PRO   A 1 711  ? 6.593   2.234   -62.918 1.00 58.74  ? 860  PRO   A C     1 
ATOM   4507 O  O     . PRO   A 1 711  ? 7.357   1.603   -62.211 1.00 58.25  ? 860  PRO   A O     1 
ATOM   4508 C  CB    . PRO   A 1 711  ? 8.324   4.119   -62.811 1.00 59.88  ? 860  PRO   A CB    1 
ATOM   4509 C  CG    . PRO   A 1 711  ? 7.834   4.741   -61.525 1.00 59.69  ? 860  PRO   A CG    1 
ATOM   4510 C  CD    . PRO   A 1 711  ? 6.546   5.430   -61.925 1.00 60.41  ? 860  PRO   A CD    1 
ATOM   4511 N  N     . ILE   A 1 712  ? 5.370   1.809   -63.255 1.00 57.65  ? 861  ILE   A N     1 
ATOM   4512 C  CA    . ILE   A 1 712  ? 4.822   0.448   -62.962 1.00 58.17  ? 861  ILE   A CA    1 
ATOM   4513 C  C     . ILE   A 1 712  ? 3.942   0.019   -64.140 1.00 57.45  ? 861  ILE   A C     1 
ATOM   4514 O  O     . ILE   A 1 712  ? 3.603   0.888   -64.965 1.00 58.07  ? 861  ILE   A O     1 
ATOM   4515 C  CB    . ILE   A 1 712  ? 4.045   0.398   -61.624 1.00 57.98  ? 861  ILE   A CB    1 
ATOM   4516 C  CG1   . ILE   A 1 712  ? 3.343   1.718   -61.297 1.00 58.55  ? 861  ILE   A CG1   1 
ATOM   4517 C  CG2   . ILE   A 1 712  ? 4.950   -0.045  -60.486 1.00 57.74  ? 861  ILE   A CG2   1 
ATOM   4518 C  CD1   . ILE   A 1 712  ? 2.166   2.027   -62.190 1.00 59.88  ? 861  ILE   A CD1   1 
ATOM   4519 N  N     . GLU   A 1 713  ? 3.596   -1.272  -64.202 1.00 57.27  ? 862  GLU   A N     1 
ATOM   4520 C  CA    . GLU   A 1 713  ? 2.702   -1.866  -65.232 1.00 59.26  ? 862  GLU   A CA    1 
ATOM   4521 C  C     . GLU   A 1 713  ? 1.524   -0.925  -65.468 1.00 58.50  ? 862  GLU   A C     1 
ATOM   4522 O  O     . GLU   A 1 713  ? 0.825   -0.571  -64.522 1.00 59.55  ? 862  GLU   A O     1 
ATOM   4523 C  CB    . GLU   A 1 713  ? 2.206   -3.245  -64.787 1.00 62.57  ? 862  GLU   A CB    1 
ATOM   4524 C  CG    . GLU   A 1 713  ? 3.254   -4.340  -64.892 1.00 66.04  ? 862  GLU   A CG    1 
ATOM   4525 C  CD    . GLU   A 1 713  ? 3.754   -4.606  -66.302 1.00 69.29  ? 862  GLU   A CD    1 
ATOM   4526 O  OE1   . GLU   A 1 713  ? 2.978   -4.370  -67.254 1.00 71.90  ? 862  GLU   A OE1   1 
ATOM   4527 O  OE2   . GLU   A 1 713  ? 4.920   -5.036  -66.445 1.00 68.78  ? 862  GLU   A OE2   1 
ATOM   4528 N  N     . PRO   A 1 714  ? 1.276   -0.480  -66.723 1.00 55.84  ? 863  PRO   A N     1 
ATOM   4529 C  CA    . PRO   A 1 714  ? 0.145   0.399   -67.029 1.00 54.89  ? 863  PRO   A CA    1 
ATOM   4530 C  C     . PRO   A 1 714  ? -1.206  -0.026  -66.433 1.00 53.34  ? 863  PRO   A C     1 
ATOM   4531 O  O     . PRO   A 1 714  ? -2.015  0.844   -66.178 1.00 54.30  ? 863  PRO   A O     1 
ATOM   4532 C  CB    . PRO   A 1 714  ? 0.076   0.334   -68.560 1.00 55.82  ? 863  PRO   A CB    1 
ATOM   4533 C  CG    . PRO   A 1 714  ? 1.516   0.147   -68.972 1.00 56.17  ? 863  PRO   A CG    1 
ATOM   4534 C  CD    . PRO   A 1 714  ? 2.091   -0.771  -67.914 1.00 56.11  ? 863  PRO   A CD    1 
ATOM   4535 N  N     . ARG   A 1 715  ? -1.423  -1.328  -66.229 1.00 52.41  ? 864  ARG   A N     1 
ATOM   4536 C  CA    . ARG   A 1 715  ? -2.690  -1.867  -65.665 1.00 53.37  ? 864  ARG   A CA    1 
ATOM   4537 C  C     . ARG   A 1 715  ? -2.774  -1.526  -64.171 1.00 54.18  ? 864  ARG   A C     1 
ATOM   4538 O  O     . ARG   A 1 715  ? -3.894  -1.246  -63.696 1.00 54.40  ? 864  ARG   A O     1 
ATOM   4539 C  CB    . ARG   A 1 715  ? -2.817  -3.375  -65.909 1.00 53.63  ? 864  ARG   A CB    1 
ATOM   4540 C  CG    . ARG   A 1 715  ? -4.242  -3.782  -66.248 1.00 54.43  ? 864  ARG   A CG    1 
ATOM   4541 C  CD    . ARG   A 1 715  ? -4.525  -5.269  -66.329 1.00 55.08  ? 864  ARG   A CD    1 
ATOM   4542 N  NE    . ARG   A 1 715  ? -5.952  -5.492  -66.128 1.00 55.62  ? 864  ARG   A NE    1 
ATOM   4543 C  CZ    . ARG   A 1 715  ? -6.916  -5.145  -66.982 1.00 55.51  ? 864  ARG   A CZ    1 
ATOM   4544 N  NH1   . ARG   A 1 715  ? -8.181  -5.386  -66.678 1.00 56.53  ? 864  ARG   A NH1   1 
ATOM   4545 N  NH2   . ARG   A 1 715  ? -6.626  -4.563  -68.134 1.00 55.42  ? 864  ARG   A NH2   1 
ATOM   4546 N  N     . PHE   A 1 716  ? -1.638  -1.550  -63.464 1.00 54.87  ? 865  PHE   A N     1 
ATOM   4547 C  CA    . PHE   A 1 716  ? -1.516  -1.151  -62.036 1.00 55.51  ? 865  PHE   A CA    1 
ATOM   4548 C  C     . PHE   A 1 716  ? -1.577  0.377   -61.921 1.00 54.69  ? 865  PHE   A C     1 
ATOM   4549 O  O     . PHE   A 1 716  ? -2.105  0.886   -60.916 1.00 53.55  ? 865  PHE   A O     1 
ATOM   4550 C  CB    . PHE   A 1 716  ? -0.230  -1.714  -61.425 1.00 56.97  ? 865  PHE   A CB    1 
ATOM   4551 C  CG    . PHE   A 1 716  ? -0.315  -3.168  -61.039 1.00 59.55  ? 865  PHE   A CG    1 
ATOM   4552 C  CD1   . PHE   A 1 716  ? -0.169  -4.166  -61.991 1.00 62.10  ? 865  PHE   A CD1   1 
ATOM   4553 C  CD2   . PHE   A 1 716  ? -0.546  -3.540  -59.723 1.00 60.93  ? 865  PHE   A CD2   1 
ATOM   4554 C  CE1   . PHE   A 1 716  ? -0.248  -5.504  -61.635 1.00 64.20  ? 865  PHE   A CE1   1 
ATOM   4555 C  CE2   . PHE   A 1 716  ? -0.623  -4.877  -59.368 1.00 62.51  ? 865  PHE   A CE2   1 
ATOM   4556 C  CZ    . PHE   A 1 716  ? -0.476  -5.857  -60.323 1.00 64.09  ? 865  PHE   A CZ    1 
ATOM   4557 N  N     . GLY   A 1 717  ? -1.038  1.084   -62.919 1.00 54.86  ? 866  GLY   A N     1 
ATOM   4558 C  CA    . GLY   A 1 717  ? -1.128  2.551   -63.036 1.00 54.70  ? 866  GLY   A CA    1 
ATOM   4559 C  C     . GLY   A 1 717  ? -2.574  3.008   -63.113 1.00 54.84  ? 866  GLY   A C     1 
ATOM   4560 O  O     . GLY   A 1 717  ? -2.914  4.012   -62.457 1.00 57.13  ? 866  GLY   A O     1 
ATOM   4561 N  N     . LYS   A 1 718  ? -3.400  2.293   -63.883 1.00 53.18  ? 867  LYS   A N     1 
ATOM   4562 C  CA    . LYS   A 1 718  ? -4.851  2.576   -64.035 1.00 52.86  ? 867  LYS   A CA    1 
ATOM   4563 C  C     . LYS   A 1 718  ? -5.580  2.166   -62.748 1.00 52.69  ? 867  LYS   A C     1 
ATOM   4564 O  O     . LYS   A 1 718  ? -6.530  2.873   -62.360 1.00 52.89  ? 867  LYS   A O     1 
ATOM   4565 C  CB    . LYS   A 1 718  ? -5.408  1.852   -65.264 1.00 52.64  ? 867  LYS   A CB    1 
ATOM   4566 C  CG    . LYS   A 1 718  ? -6.875  2.128   -65.564 1.00 53.35  ? 867  LYS   A CG    1 
ATOM   4567 C  CD    . LYS   A 1 718  ? -7.240  1.911   -67.012 1.00 53.83  ? 867  LYS   A CD    1 
ATOM   4568 C  CE    . LYS   A 1 718  ? -8.719  2.072   -67.283 1.00 54.41  ? 867  LYS   A CE    1 
ATOM   4569 N  NZ    . LYS   A 1 718  ? -8.995  2.165   -68.736 1.00 55.48  ? 867  LYS   A NZ    1 
ATOM   4570 N  N     . MET   A 1 719  ? -5.145  1.074   -62.110 1.00 52.60  ? 868  MET   A N     1 
ATOM   4571 C  CA    . MET   A 1 719  ? -5.698  0.587   -60.816 1.00 53.68  ? 868  MET   A CA    1 
ATOM   4572 C  C     . MET   A 1 719  ? -5.482  1.656   -59.736 1.00 54.33  ? 868  MET   A C     1 
ATOM   4573 O  O     . MET   A 1 719  ? -6.373  1.821   -58.882 1.00 55.07  ? 868  MET   A O     1 
ATOM   4574 C  CB    . MET   A 1 719  ? -5.029  -0.722  -60.384 1.00 53.07  ? 868  MET   A CB    1 
ATOM   4575 C  CG    . MET   A 1 719  ? -5.576  -1.280  -59.083 1.00 53.05  ? 868  MET   A CG    1 
ATOM   4576 S  SD    . MET   A 1 719  ? -4.680  -2.745  -58.521 1.00 53.25  ? 868  MET   A SD    1 
ATOM   4577 C  CE    . MET   A 1 719  ? -3.136  -2.000  -57.999 1.00 53.66  ? 868  MET   A CE    1 
ATOM   4578 N  N     . MET   A 1 720  ? -4.338  2.347   -59.774 1.00 54.90  ? 869  MET   A N     1 
ATOM   4579 C  CA    . MET   A 1 720  ? -3.993  3.441   -58.828 1.00 55.17  ? 869  MET   A CA    1 
ATOM   4580 C  C     . MET   A 1 720  ? -4.905  4.645   -59.087 1.00 55.59  ? 869  MET   A C     1 
ATOM   4581 O  O     . MET   A 1 720  ? -5.402  5.217   -58.098 1.00 57.12  ? 869  MET   A O     1 
ATOM   4582 C  CB    . MET   A 1 720  ? -2.522  3.850   -58.959 1.00 54.66  ? 869  MET   A CB    1 
ATOM   4583 C  CG    . MET   A 1 720  ? -1.584  2.940   -58.189 1.00 55.00  ? 869  MET   A CG    1 
ATOM   4584 S  SD    . MET   A 1 720  ? 0.112   2.974   -58.816 1.00 56.10  ? 869  MET   A SD    1 
ATOM   4585 C  CE    . MET   A 1 720  ? 0.470   4.726   -58.697 1.00 57.13  ? 869  MET   A CE    1 
ATOM   4586 N  N     . ILE   A 1 721  ? -5.126  4.998   -60.359 1.00 56.28  ? 870  ILE   A N     1 
ATOM   4587 C  CA    . ILE   A 1 721  ? -6.042  6.102   -60.786 1.00 58.18  ? 870  ILE   A CA    1 
ATOM   4588 C  C     . ILE   A 1 721  ? -7.453  5.811   -60.257 1.00 59.33  ? 870  ILE   A C     1 
ATOM   4589 O  O     . ILE   A 1 721  ? -8.074  6.734   -59.691 1.00 59.39  ? 870  ILE   A O     1 
ATOM   4590 C  CB    . ILE   A 1 721  ? -6.033  6.287   -62.318 1.00 57.39  ? 870  ILE   A CB    1 
ATOM   4591 C  CG1   . ILE   A 1 721  ? -4.707  6.878   -62.806 1.00 57.88  ? 870  ILE   A CG1   1 
ATOM   4592 C  CG2   . ILE   A 1 721  ? -7.221  7.127   -62.771 1.00 56.36  ? 870  ILE   A CG2   1 
ATOM   4593 C  CD1   . ILE   A 1 721  ? -4.481  6.744   -64.294 1.00 57.69  ? 870  ILE   A CD1   1 
ATOM   4594 N  N     . MET   A 1 722  ? -7.939  4.582   -60.449 1.00 59.45  ? 871  MET   A N     1 
ATOM   4595 C  CA    . MET   A 1 722  ? -9.270  4.132   -59.960 1.00 60.73  ? 871  MET   A CA    1 
ATOM   4596 C  C     . MET   A 1 722  ? -9.290  4.212   -58.429 1.00 60.84  ? 871  MET   A C     1 
ATOM   4597 O  O     . MET   A 1 722  ? -10.287 4.709   -57.879 1.00 61.89  ? 871  MET   A O     1 
ATOM   4598 C  CB    . MET   A 1 722  ? -9.576  2.704   -60.422 1.00 61.82  ? 871  MET   A CB    1 
ATOM   4599 C  CG    . MET   A 1 722  ? -9.835  2.605   -61.915 1.00 62.76  ? 871  MET   A CG    1 
ATOM   4600 S  SD    . MET   A 1 722  ? -9.778  0.907   -62.539 1.00 63.94  ? 871  MET   A SD    1 
ATOM   4601 C  CE    . MET   A 1 722  ? -11.379 0.313   -61.999 1.00 63.10  ? 871  MET   A CE    1 
ATOM   4602 N  N     . GLY   A 1 723  ? -8.212  3.766   -57.778 1.00 61.88  ? 872  GLY   A N     1 
ATOM   4603 C  CA    . GLY   A 1 723  ? -8.035  3.821   -56.313 1.00 60.54  ? 872  GLY   A CA    1 
ATOM   4604 C  C     . GLY   A 1 723  ? -8.193  5.231   -55.772 1.00 58.94  ? 872  GLY   A C     1 
ATOM   4605 O  O     . GLY   A 1 723  ? -8.835  5.380   -54.717 1.00 59.31  ? 872  GLY   A O     1 
ATOM   4606 N  N     . CYS   A 1 724  ? -7.628  6.226   -56.463 1.00 57.77  ? 873  CYS   A N     1 
ATOM   4607 C  CA    . CYS   A 1 724  ? -7.732  7.668   -56.109 1.00 57.45  ? 873  CYS   A CA    1 
ATOM   4608 C  C     . CYS   A 1 724  ? -9.208  8.083   -56.088 1.00 57.67  ? 873  CYS   A C     1 
ATOM   4609 O  O     . CYS   A 1 724  ? -9.614  8.747   -55.115 1.00 60.64  ? 873  CYS   A O     1 
ATOM   4610 C  CB    . CYS   A 1 724  ? -6.948  8.548   -57.078 1.00 56.88  ? 873  CYS   A CB    1 
ATOM   4611 S  SG    . CYS   A 1 724  ? -5.152  8.440   -56.863 1.00 55.29  ? 873  CYS   A SG    1 
ATOM   4612 N  N     . ILE   A 1 725  ? -9.978  7.678   -57.103 1.00 56.56  ? 874  ILE   A N     1 
ATOM   4613 C  CA    . ILE   A 1 725  ? -11.425 8.016   -57.270 1.00 56.14  ? 874  ILE   A CA    1 
ATOM   4614 C  C     . ILE   A 1 725  ? -12.207 7.545   -56.035 1.00 56.32  ? 874  ILE   A C     1 
ATOM   4615 O  O     . ILE   A 1 725  ? -13.077 8.306   -55.569 1.00 57.92  ? 874  ILE   A O     1 
ATOM   4616 C  CB    . ILE   A 1 725  ? -11.985 7.415   -58.577 1.00 55.84  ? 874  ILE   A CB    1 
ATOM   4617 C  CG1   . ILE   A 1 725  ? -11.391 8.104   -59.809 1.00 55.80  ? 874  ILE   A CG1   1 
ATOM   4618 C  CG2   . ILE   A 1 725  ? -13.508 7.457   -58.589 1.00 56.40  ? 874  ILE   A CG2   1 
ATOM   4619 C  CD1   . ILE   A 1 725  ? -11.591 7.348   -61.102 1.00 55.92  ? 874  ILE   A CD1   1 
ATOM   4620 N  N     . PHE   A 1 726  ? -11.900 6.348   -55.524 1.00 56.05  ? 875  PHE   A N     1 
ATOM   4621 C  CA    . PHE   A 1 726  ? -12.601 5.694   -54.385 1.00 56.23  ? 875  PHE   A CA    1 
ATOM   4622 C  C     . PHE   A 1 726  ? -12.020 6.154   -53.039 1.00 57.43  ? 875  PHE   A C     1 
ATOM   4623 O  O     . PHE   A 1 726  ? -12.528 5.695   -51.993 1.00 58.24  ? 875  PHE   A O     1 
ATOM   4624 C  CB    . PHE   A 1 726  ? -12.514 4.170   -54.507 1.00 56.07  ? 875  PHE   A CB    1 
ATOM   4625 C  CG    . PHE   A 1 726  ? -13.460 3.558   -55.509 1.00 55.30  ? 875  PHE   A CG    1 
ATOM   4626 C  CD1   . PHE   A 1 726  ? -14.816 3.468   -55.238 1.00 55.70  ? 875  PHE   A CD1   1 
ATOM   4627 C  CD2   . PHE   A 1 726  ? -12.993 3.048   -56.711 1.00 55.10  ? 875  PHE   A CD2   1 
ATOM   4628 C  CE1   . PHE   A 1 726  ? -15.687 2.895   -56.151 1.00 55.38  ? 875  PHE   A CE1   1 
ATOM   4629 C  CE2   . PHE   A 1 726  ? -13.865 2.477   -57.624 1.00 55.79  ? 875  PHE   A CE2   1 
ATOM   4630 C  CZ    . PHE   A 1 726  ? -15.210 2.401   -57.343 1.00 56.17  ? 875  PHE   A CZ    1 
ATOM   4631 N  N     . TYR   A 1 727  ? -11.000 7.022   -53.061 1.00 58.49  ? 876  TYR   A N     1 
ATOM   4632 C  CA    . TYR   A 1 727  ? -10.275 7.550   -51.873 1.00 58.96  ? 876  TYR   A CA    1 
ATOM   4633 C  C     . TYR   A 1 727  ? -9.640  6.387   -51.096 1.00 59.14  ? 876  TYR   A C     1 
ATOM   4634 O  O     . TYR   A 1 727  ? -9.765  6.336   -49.855 1.00 61.51  ? 876  TYR   A O     1 
ATOM   4635 C  CB    . TYR   A 1 727  ? -11.206 8.416   -51.017 1.00 59.18  ? 876  TYR   A CB    1 
ATOM   4636 C  CG    . TYR   A 1 727  ? -11.397 9.813   -51.547 1.00 59.63  ? 876  TYR   A CG    1 
ATOM   4637 C  CD1   . TYR   A 1 727  ? -12.157 10.050  -52.681 1.00 60.09  ? 876  TYR   A CD1   1 
ATOM   4638 C  CD2   . TYR   A 1 727  ? -10.804 10.901  -50.927 1.00 60.20  ? 876  TYR   A CD2   1 
ATOM   4639 C  CE1   . TYR   A 1 727  ? -12.328 11.330  -53.181 1.00 61.27  ? 876  TYR   A CE1   1 
ATOM   4640 C  CE2   . TYR   A 1 727  ? -10.964 12.188  -51.413 1.00 60.39  ? 876  TYR   A CE2   1 
ATOM   4641 C  CZ    . TYR   A 1 727  ? -11.730 12.404  -52.545 1.00 61.21  ? 876  TYR   A CZ    1 
ATOM   4642 O  OH    . TYR   A 1 727  ? -11.893 13.668  -53.033 1.00 62.81  ? 876  TYR   A OH    1 
ATOM   4643 N  N     . VAL   A 1 728  ? -8.971  5.483   -51.819 1.00 57.68  ? 877  VAL   A N     1 
ATOM   4644 C  CA    . VAL   A 1 728  ? -8.141  4.375   -51.256 1.00 56.43  ? 877  VAL   A CA    1 
ATOM   4645 C  C     . VAL   A 1 728  ? -6.784  4.371   -51.978 1.00 54.35  ? 877  VAL   A C     1 
ATOM   4646 O  O     . VAL   A 1 728  ? -6.141  3.303   -52.044 1.00 50.97  ? 877  VAL   A O     1 
ATOM   4647 C  CB    . VAL   A 1 728  ? -8.871  3.021   -51.368 1.00 56.74  ? 877  VAL   A CB    1 
ATOM   4648 C  CG1   . VAL   A 1 728  ? -10.123 2.998   -50.504 1.00 57.24  ? 877  VAL   A CG1   1 
ATOM   4649 C  CG2   . VAL   A 1 728  ? -9.214  2.664   -52.807 1.00 57.17  ? 877  VAL   A CG2   1 
ATOM   4650 N  N     . GLY   A 1 729  ? -6.362  5.545   -52.464 1.00 54.32  ? 878  GLY   A N     1 
ATOM   4651 C  CA    . GLY   A 1 729  ? -5.170  5.741   -53.310 1.00 55.64  ? 878  GLY   A CA    1 
ATOM   4652 C  C     . GLY   A 1 729  ? -3.899  5.240   -52.647 1.00 56.13  ? 878  GLY   A C     1 
ATOM   4653 O  O     . GLY   A 1 729  ? -3.021  4.729   -53.371 1.00 56.83  ? 878  GLY   A O     1 
ATOM   4654 N  N     . ASP   A 1 730  ? -3.790  5.385   -51.324 1.00 56.55  ? 879  ASP   A N     1 
ATOM   4655 C  CA    . ASP   A 1 730  ? -2.584  4.983   -50.554 1.00 57.20  ? 879  ASP   A CA    1 
ATOM   4656 C  C     . ASP   A 1 730  ? -2.423  3.459   -50.601 1.00 57.15  ? 879  ASP   A C     1 
ATOM   4657 O  O     . ASP   A 1 730  ? -1.300  2.999   -50.879 1.00 59.16  ? 879  ASP   A O     1 
ATOM   4658 C  CB    . ASP   A 1 730  ? -2.641  5.468   -49.107 1.00 57.40  ? 879  ASP   A CB    1 
ATOM   4659 C  CG    . ASP   A 1 730  ? -1.364  5.153   -48.349 1.00 57.93  ? 879  ASP   A CG    1 
ATOM   4660 O  OD1   . ASP   A 1 730  ? -0.330  5.769   -48.675 1.00 56.51  ? 879  ASP   A OD1   1 
ATOM   4661 O  OD2   . ASP   A 1 730  ? -1.406  4.268   -47.468 1.00 58.84  ? 879  ASP   A OD2   1 
ATOM   4662 N  N     . ALA   A 1 731  ? -3.498  2.714   -50.327 1.00 55.87  ? 880  ALA   A N     1 
ATOM   4663 C  CA    . ALA   A 1 731  ? -3.501  1.233   -50.254 1.00 56.23  ? 880  ALA   A CA    1 
ATOM   4664 C  C     . ALA   A 1 731  ? -3.111  0.644   -51.616 1.00 56.92  ? 880  ALA   A C     1 
ATOM   4665 O  O     . ALA   A 1 731  ? -2.282  -0.285  -51.637 1.00 57.96  ? 880  ALA   A O     1 
ATOM   4666 C  CB    . ALA   A 1 731  ? -4.851  0.734   -49.800 1.00 56.32  ? 880  ALA   A CB    1 
ATOM   4667 N  N     . VAL   A 1 732  ? -3.683  1.162   -52.708 1.00 56.83  ? 881  VAL   A N     1 
ATOM   4668 C  CA    . VAL   A 1 732  ? -3.435  0.655   -54.093 1.00 56.63  ? 881  VAL   A CA    1 
ATOM   4669 C  C     . VAL   A 1 732  ? -2.002  1.015   -54.508 1.00 55.16  ? 881  VAL   A C     1 
ATOM   4670 O  O     . VAL   A 1 732  ? -1.380  0.206   -55.220 1.00 56.30  ? 881  VAL   A O     1 
ATOM   4671 C  CB    . VAL   A 1 732  ? -4.480  1.169   -55.105 1.00 56.74  ? 881  VAL   A CB    1 
ATOM   4672 C  CG1   . VAL   A 1 732  ? -5.874  0.663   -54.772 1.00 56.55  ? 881  VAL   A CG1   1 
ATOM   4673 C  CG2   . VAL   A 1 732  ? -4.484  2.683   -55.225 1.00 58.37  ? 881  VAL   A CG2   1 
ATOM   4674 N  N     . CYS   A 1 733  ? -1.498  2.172   -54.069 1.00 54.48  ? 882  CYS   A N     1 
ATOM   4675 C  CA    . CYS   A 1 733  ? -0.098  2.628   -54.297 1.00 54.99  ? 882  CYS   A CA    1 
ATOM   4676 C  C     . CYS   A 1 733  ? 0.881   1.702   -53.556 1.00 54.58  ? 882  CYS   A C     1 
ATOM   4677 O  O     . CYS   A 1 733  ? 1.940   1.385   -54.138 1.00 53.74  ? 882  CYS   A O     1 
ATOM   4678 C  CB    . CYS   A 1 733  ? 0.093   4.079   -53.867 1.00 54.96  ? 882  CYS   A CB    1 
ATOM   4679 S  SG    . CYS   A 1 733  ? -0.581  5.274   -55.051 1.00 55.76  ? 882  CYS   A SG    1 
ATOM   4680 N  N     . THR   A 1 734  ? 0.540   1.288   -52.329 1.00 53.36  ? 883  THR   A N     1 
ATOM   4681 C  CA    . THR   A 1 734  ? 1.308   0.309   -51.509 1.00 53.42  ? 883  THR   A CA    1 
ATOM   4682 C  C     . THR   A 1 734  ? 1.394   -1.027  -52.258 1.00 54.42  ? 883  THR   A C     1 
ATOM   4683 O  O     . THR   A 1 734  ? 2.518   -1.544  -52.411 1.00 56.85  ? 883  THR   A O     1 
ATOM   4684 C  CB    . THR   A 1 734  ? 0.680   0.123   -50.120 1.00 53.00  ? 883  THR   A CB    1 
ATOM   4685 O  OG1   . THR   A 1 734  ? 0.569   1.408   -49.509 1.00 54.00  ? 883  THR   A OG1   1 
ATOM   4686 C  CG2   . THR   A 1 734  ? 1.477   -0.794  -49.217 1.00 52.02  ? 883  THR   A CG2   1 
ATOM   4687 N  N     . ILE   A 1 735  ? 0.251   -1.561  -52.703 1.00 53.79  ? 884  ILE   A N     1 
ATOM   4688 C  CA    . ILE   A 1 735  ? 0.158   -2.853  -53.448 1.00 54.25  ? 884  ILE   A CA    1 
ATOM   4689 C  C     . ILE   A 1 735  ? 0.998   -2.750  -54.728 1.00 53.60  ? 884  ILE   A C     1 
ATOM   4690 O  O     . ILE   A 1 735  ? 1.790   -3.676  -54.979 1.00 54.77  ? 884  ILE   A O     1 
ATOM   4691 C  CB    . ILE   A 1 735  ? -1.312  -3.228  -53.739 1.00 55.05  ? 884  ILE   A CB    1 
ATOM   4692 C  CG1   . ILE   A 1 735  ? -2.025  -3.713  -52.473 1.00 55.10  ? 884  ILE   A CG1   1 
ATOM   4693 C  CG2   . ILE   A 1 735  ? -1.404  -4.256  -54.859 1.00 55.39  ? 884  ILE   A CG2   1 
ATOM   4694 C  CD1   . ILE   A 1 735  ? -3.533  -3.722  -52.575 1.00 55.47  ? 884  ILE   A CD1   1 
ATOM   4695 N  N     . SER   A 1 736  ? 0.822   -1.673  -55.500 1.00 52.80  ? 885  SER   A N     1 
ATOM   4696 C  CA    . SER   A 1 736  ? 1.522   -1.420  -56.789 1.00 52.70  ? 885  SER   A CA    1 
ATOM   4697 C  C     . SER   A 1 736  ? 3.040   -1.398  -56.572 1.00 51.70  ? 885  SER   A C     1 
ATOM   4698 O  O     . SER   A 1 736  ? 3.762   -1.997  -57.388 1.00 50.99  ? 885  SER   A O     1 
ATOM   4699 C  CB    . SER   A 1 736  ? 1.049   -0.139  -57.426 1.00 52.82  ? 885  SER   A CB    1 
ATOM   4700 O  OG    . SER   A 1 736  ? -0.291  -0.265  -57.875 1.00 53.79  ? 885  SER   A OG    1 
ATOM   4701 N  N     . ALA   A 1 737  ? 3.493   -0.720  -55.515 1.00 51.45  ? 886  ALA   A N     1 
ATOM   4702 C  CA    . ALA   A 1 737  ? 4.919   -0.573  -55.143 1.00 50.34  ? 886  ALA   A CA    1 
ATOM   4703 C  C     . ALA   A 1 737  ? 5.519   -1.952  -54.851 1.00 49.06  ? 886  ALA   A C     1 
ATOM   4704 O  O     . ALA   A 1 737  ? 6.594   -2.251  -55.394 1.00 51.20  ? 886  ALA   A O     1 
ATOM   4705 C  CB    . ALA   A 1 737  ? 5.051   0.347   -53.953 1.00 50.54  ? 886  ALA   A CB    1 
ATOM   4706 N  N     . ALA   A 1 738  ? 4.822   -2.762  -54.049 1.00 47.85  ? 887  ALA   A N     1 
ATOM   4707 C  CA    . ALA   A 1 738  ? 5.300   -4.054  -53.500 1.00 48.11  ? 887  ALA   A CA    1 
ATOM   4708 C  C     . ALA   A 1 738  ? 5.585   -5.066  -54.618 1.00 49.25  ? 887  ALA   A C     1 
ATOM   4709 O  O     . ALA   A 1 738  ? 6.324   -6.028  -54.348 1.00 50.48  ? 887  ALA   A O     1 
ATOM   4710 C  CB    . ALA   A 1 738  ? 4.290   -4.601  -52.524 1.00 47.36  ? 887  ALA   A CB    1 
ATOM   4711 N  N     . THR   A 1 739  ? 5.012   -4.874  -55.812 1.00 51.15  ? 888  THR   A N     1 
ATOM   4712 C  CA    . THR   A 1 739  ? 5.227   -5.746  -56.999 1.00 53.27  ? 888  THR   A CA    1 
ATOM   4713 C  C     . THR   A 1 739  ? 6.660   -5.570  -57.519 1.00 56.29  ? 888  THR   A C     1 
ATOM   4714 O  O     . THR   A 1 739  ? 7.179   -6.517  -58.139 1.00 59.71  ? 888  THR   A O     1 
ATOM   4715 C  CB    . THR   A 1 739  ? 4.215   -5.462  -58.119 1.00 52.80  ? 888  THR   A CB    1 
ATOM   4716 O  OG1   . THR   A 1 739  ? 4.451   -4.150  -58.630 1.00 52.66  ? 888  THR   A OG1   1 
ATOM   4717 C  CG2   . THR   A 1 739  ? 2.775   -5.587  -57.672 1.00 52.71  ? 888  THR   A CG2   1 
ATOM   4718 N  N     . CYS   A 1 740  ? 7.275   -4.408  -57.280 1.00 58.30  ? 889  CYS   A N     1 
ATOM   4719 C  CA    . CYS   A 1 740  ? 8.619   -4.038  -57.800 1.00 60.42  ? 889  CYS   A CA    1 
ATOM   4720 C  C     . CYS   A 1 740  ? 9.736   -4.644  -56.940 1.00 60.23  ? 889  CYS   A C     1 
ATOM   4721 O  O     . CYS   A 1 740  ? 10.902  -4.584  -57.378 1.00 60.88  ? 889  CYS   A O     1 
ATOM   4722 C  CB    . CYS   A 1 740  ? 8.778   -2.525  -57.859 1.00 62.08  ? 889  CYS   A CB    1 
ATOM   4723 S  SG    . CYS   A 1 740  ? 7.543   -1.731  -58.918 1.00 63.83  ? 889  CYS   A SG    1 
ATOM   4724 N  N     . PHE   A 1 741  ? 9.402   -5.201  -55.772 1.00 59.15  ? 890  PHE   A N     1 
ATOM   4725 C  CA    . PHE   A 1 741  ? 10.373  -5.750  -54.789 1.00 59.70  ? 890  PHE   A CA    1 
ATOM   4726 C  C     . PHE   A 1 741  ? 9.985   -7.181  -54.429 1.00 60.08  ? 890  PHE   A C     1 
ATOM   4727 O  O     . PHE   A 1 741  ? 8.841   -7.577  -54.628 1.00 60.13  ? 890  PHE   A O     1 
ATOM   4728 C  CB    . PHE   A 1 741  ? 10.418  -4.847  -53.554 1.00 59.37  ? 890  PHE   A CB    1 
ATOM   4729 C  CG    . PHE   A 1 741  ? 10.681  -3.399  -53.877 1.00 58.44  ? 890  PHE   A CG    1 
ATOM   4730 C  CD1   . PHE   A 1 741  ? 11.962  -2.962  -54.175 1.00 58.70  ? 890  PHE   A CD1   1 
ATOM   4731 C  CD2   . PHE   A 1 741  ? 9.645   -2.480  -53.913 1.00 57.89  ? 890  PHE   A CD2   1 
ATOM   4732 C  CE1   . PHE   A 1 741  ? 12.203  -1.634  -54.488 1.00 59.59  ? 890  PHE   A CE1   1 
ATOM   4733 C  CE2   . PHE   A 1 741  ? 9.888   -1.152  -54.224 1.00 59.16  ? 890  PHE   A CE2   1 
ATOM   4734 C  CZ    . PHE   A 1 741  ? 11.166  -0.730  -54.510 1.00 59.55  ? 890  PHE   A CZ    1 
ATOM   4735 N  N     . PRO   A 1 742  ? 10.921  -8.003  -53.898 1.00 62.11  ? 891  PRO   A N     1 
ATOM   4736 C  CA    . PRO   A 1 742  ? 10.573  -9.327  -53.383 1.00 64.15  ? 891  PRO   A CA    1 
ATOM   4737 C  C     . PRO   A 1 742  ? 9.583   -9.234  -52.212 1.00 65.72  ? 891  PRO   A C     1 
ATOM   4738 O  O     . PRO   A 1 742  ? 9.361   -8.144  -51.719 1.00 65.12  ? 891  PRO   A O     1 
ATOM   4739 C  CB    . PRO   A 1 742  ? 11.914  -9.922  -52.924 1.00 63.98  ? 891  PRO   A CB    1 
ATOM   4740 C  CG    . PRO   A 1 742  ? 12.818  -8.721  -52.737 1.00 62.85  ? 891  PRO   A CG    1 
ATOM   4741 C  CD    . PRO   A 1 742  ? 12.359  -7.720  -53.777 1.00 62.22  ? 891  PRO   A CD    1 
ATOM   4742 N  N     . GLU   A 1 743  ? 9.011   -10.373 -51.813 1.00 68.27  ? 892  GLU   A N     1 
ATOM   4743 C  CA    . GLU   A 1 743  ? 8.027   -10.462 -50.702 1.00 70.18  ? 892  GLU   A CA    1 
ATOM   4744 C  C     . GLU   A 1 743  ? 8.703   -9.979  -49.423 1.00 70.09  ? 892  GLU   A C     1 
ATOM   4745 O  O     . GLU   A 1 743  ? 9.847   -10.339 -49.161 1.00 71.40  ? 892  GLU   A O     1 
ATOM   4746 C  CB    . GLU   A 1 743  ? 7.513   -11.896 -50.549 1.00 73.15  ? 892  GLU   A CB    1 
ATOM   4747 C  CG    . GLU   A 1 743  ? 6.684   -12.379 -51.728 1.00 75.24  ? 892  GLU   A CG    1 
ATOM   4748 C  CD    . GLU   A 1 743  ? 5.283   -11.797 -51.829 1.00 77.60  ? 892  GLU   A CD    1 
ATOM   4749 O  OE1   . GLU   A 1 743  ? 4.886   -11.030 -50.926 1.00 79.11  ? 892  GLU   A OE1   1 
ATOM   4750 O  OE2   . GLU   A 1 743  ? 4.586   -12.119 -52.812 1.00 79.63  ? 892  GLU   A OE2   1 
ATOM   4751 N  N     . PRO   A 1 744  ? 8.036   -9.137  -48.599 1.00 71.10  ? 893  PRO   A N     1 
ATOM   4752 C  CA    . PRO   A 1 744  ? 8.617   -8.678  -47.337 1.00 71.51  ? 893  PRO   A CA    1 
ATOM   4753 C  C     . PRO   A 1 744  ? 8.737   -9.784  -46.276 1.00 72.70  ? 893  PRO   A C     1 
ATOM   4754 O  O     . PRO   A 1 744  ? 9.514   -9.609  -45.358 1.00 72.39  ? 893  PRO   A O     1 
ATOM   4755 C  CB    . PRO   A 1 744  ? 7.649   -7.581  -46.871 1.00 70.73  ? 893  PRO   A CB    1 
ATOM   4756 C  CG    . PRO   A 1 744  ? 6.328   -7.958  -47.505 1.00 70.90  ? 893  PRO   A CG    1 
ATOM   4757 C  CD    . PRO   A 1 744  ? 6.696   -8.577  -48.837 1.00 70.92  ? 893  PRO   A CD    1 
ATOM   4758 N  N     . PHE   A 1 745  ? 7.971   -10.874 -46.418 1.00 76.17  ? 894  PHE   A N     1 
ATOM   4759 C  CA    . PHE   A 1 745  ? 8.023   -12.071 -45.534 1.00 77.96  ? 894  PHE   A CA    1 
ATOM   4760 C  C     . PHE   A 1 745  ? 9.309   -12.858 -45.809 1.00 79.54  ? 894  PHE   A C     1 
ATOM   4761 O  O     . PHE   A 1 745  ? 9.703   -12.977 -46.987 1.00 81.05  ? 894  PHE   A O     1 
ATOM   4762 C  CB    . PHE   A 1 745  ? 6.813   -12.986 -45.750 1.00 78.19  ? 894  PHE   A CB    1 
ATOM   4763 C  CG    . PHE   A 1 745  ? 5.487   -12.426 -45.301 1.00 79.17  ? 894  PHE   A CG    1 
ATOM   4764 C  CD1   . PHE   A 1 745  ? 5.325   -11.918 -44.022 1.00 79.81  ? 894  PHE   A CD1   1 
ATOM   4765 C  CD2   . PHE   A 1 745  ? 4.389   -12.437 -46.148 1.00 82.54  ? 894  PHE   A CD2   1 
ATOM   4766 C  CE1   . PHE   A 1 745  ? 4.102   -11.413 -43.608 1.00 79.88  ? 894  PHE   A CE1   1 
ATOM   4767 C  CE2   . PHE   A 1 745  ? 3.166   -11.933 -45.732 1.00 83.68  ? 894  PHE   A CE2   1 
ATOM   4768 C  CZ    . PHE   A 1 745  ? 3.025   -11.422 -44.463 1.00 82.09  ? 894  PHE   A CZ    1 
ATOM   4769 N  N     . ILE   A 1 746  ? 9.935   -13.377 -44.747 1.00 80.51  ? 895  ILE   A N     1 
ATOM   4770 C  CA    . ILE   A 1 746  ? 11.074  -14.341 -44.813 1.00 82.00  ? 895  ILE   A CA    1 
ATOM   4771 C  C     . ILE   A 1 746  ? 10.509  -15.742 -44.542 1.00 84.81  ? 895  ILE   A C     1 
ATOM   4772 O  O     . ILE   A 1 746  ? 10.538  -16.183 -43.374 1.00 83.40  ? 895  ILE   A O     1 
ATOM   4773 C  CB    . ILE   A 1 746  ? 12.198  -13.950 -43.828 1.00 79.94  ? 895  ILE   A CB    1 
ATOM   4774 C  CG1   . ILE   A 1 746  ? 12.669  -12.509 -44.049 1.00 78.88  ? 895  ILE   A CG1   1 
ATOM   4775 C  CG2   . ILE   A 1 746  ? 13.358  -14.933 -43.910 1.00 79.12  ? 895  ILE   A CG2   1 
ATOM   4776 C  CD1   . ILE   A 1 746  ? 13.473  -11.938 -42.903 1.00 78.84  ? 895  ILE   A CD1   1 
ATOM   4777 N  N     . SER   A 1 747  ? 9.985   -16.392 -45.588 1.00 89.17  ? 896  SER   A N     1 
ATOM   4778 C  CA    . SER   A 1 747  ? 9.322   -17.723 -45.534 1.00 93.18  ? 896  SER   A CA    1 
ATOM   4779 C  C     . SER   A 1 747  ? 10.353  -18.840 -45.747 1.00 97.26  ? 896  SER   A C     1 
ATOM   4780 O  O     . SER   A 1 747  ? 10.152  -19.932 -45.180 1.00 100.43 ? 896  SER   A O     1 
ATOM   4781 C  CB    . SER   A 1 747  ? 8.196   -17.813 -46.536 1.00 93.22  ? 896  SER   A CB    1 
ATOM   4782 O  OG    . SER   A 1 747  ? 8.685   -17.720 -47.867 1.00 93.01  ? 896  SER   A OG    1 
ATOM   4783 N  N     . GLU   A 1 748  ? 11.403  -18.571 -46.535 1.00 100.44 ? 897  GLU   A N     1 
ATOM   4784 C  CA    . GLU   A 1 748  ? 12.514  -19.515 -46.842 1.00 103.04 ? 897  GLU   A CA    1 
ATOM   4785 C  C     . GLU   A 1 748  ? 11.982  -20.662 -47.716 1.00 104.17 ? 897  GLU   A C     1 
ATOM   4786 O  O     . GLU   A 1 748  ? 12.424  -21.813 -47.519 1.00 104.80 ? 897  GLU   A O     1 
ATOM   4787 C  CB    . GLU   A 1 748  ? 13.153  -20.037 -45.550 1.00 104.29 ? 897  GLU   A CB    1 
ATOM   4788 C  CG    . GLU   A 1 748  ? 13.616  -18.939 -44.606 1.00 104.28 ? 897  GLU   A CG    1 
ATOM   4789 C  CD    . GLU   A 1 748  ? 14.301  -19.424 -43.339 1.00 104.78 ? 897  GLU   A CD    1 
ATOM   4790 O  OE1   . GLU   A 1 748  ? 14.242  -20.638 -43.057 1.00 103.78 ? 897  GLU   A OE1   1 
ATOM   4791 O  OE2   . GLU   A 1 748  ? 14.895  -18.583 -42.634 1.00 103.60 ? 897  GLU   A OE2   1 
ATOM   4792 N  N     . GLY   A 1 749  ? 11.064  -20.352 -48.640 1.00 104.95 ? 898  GLY   A N     1 
ATOM   4793 C  CA    . GLY   A 1 749  ? 10.482  -21.303 -49.609 1.00 104.06 ? 898  GLY   A CA    1 
ATOM   4794 C  C     . GLY   A 1 749  ? 9.599   -22.354 -48.953 1.00 104.35 ? 898  GLY   A C     1 
ATOM   4795 O  O     . GLY   A 1 749  ? 9.315   -23.369 -49.620 1.00 108.27 ? 898  GLY   A O     1 
ATOM   4796 N  N     . LYS   A 1 750  ? 9.168   -22.124 -47.706 1.00 101.40 ? 899  LYS   A N     1 
ATOM   4797 C  CA    . LYS   A 1 750  ? 8.305   -23.047 -46.917 1.00 99.58  ? 899  LYS   A CA    1 
ATOM   4798 C  C     . LYS   A 1 750  ? 6.884   -22.474 -46.844 1.00 98.07  ? 899  LYS   A C     1 
ATOM   4799 O  O     . LYS   A 1 750  ? 6.669   -21.356 -47.355 1.00 97.85  ? 899  LYS   A O     1 
ATOM   4800 C  CB    . LYS   A 1 750  ? 8.867   -23.237 -45.504 1.00 99.71  ? 899  LYS   A CB    1 
ATOM   4801 C  CG    . LYS   A 1 750  ? 10.276  -23.810 -45.428 1.00 100.70 ? 899  LYS   A CG    1 
ATOM   4802 C  CD    . LYS   A 1 750  ? 10.605  -24.465 -44.096 1.00 101.28 ? 899  LYS   A CD    1 
ATOM   4803 C  CE    . LYS   A 1 750  ? 10.435  -23.549 -42.901 1.00 101.87 ? 899  LYS   A CE    1 
ATOM   4804 N  NZ    . LYS   A 1 750  ? 11.356  -22.389 -42.956 1.00 103.37 ? 899  LYS   A NZ    1 
ATOM   4805 N  N     . ARG   A 1 751  ? 5.957   -23.220 -46.233 1.00 96.25  ? 900  ARG   A N     1 
ATOM   4806 C  CA    . ARG   A 1 751  ? 4.588   -22.748 -45.886 1.00 95.15  ? 900  ARG   A CA    1 
ATOM   4807 C  C     . ARG   A 1 751  ? 4.704   -21.703 -44.769 1.00 91.17  ? 900  ARG   A C     1 
ATOM   4808 O  O     . ARG   A 1 751  ? 5.614   -21.840 -43.928 1.00 88.72  ? 900  ARG   A O     1 
ATOM   4809 C  CB    . ARG   A 1 751  ? 3.701   -23.923 -45.457 1.00 97.21  ? 900  ARG   A CB    1 
ATOM   4810 C  CG    . ARG   A 1 751  ? 3.278   -24.837 -46.598 1.00 99.47  ? 900  ARG   A CG    1 
ATOM   4811 C  CD    . ARG   A 1 751  ? 2.789   -26.183 -46.096 1.00 101.53 ? 900  ARG   A CD    1 
ATOM   4812 N  NE    . ARG   A 1 751  ? 2.042   -26.936 -47.098 1.00 103.26 ? 900  ARG   A NE    1 
ATOM   4813 C  CZ    . ARG   A 1 751  ? 2.576   -27.604 -48.121 1.00 103.56 ? 900  ARG   A CZ    1 
ATOM   4814 N  NH1   . ARG   A 1 751  ? 3.885   -27.617 -48.316 1.00 103.19 ? 900  ARG   A NH1   1 
ATOM   4815 N  NH2   . ARG   A 1 751  ? 1.789   -28.255 -48.960 1.00 103.69 ? 900  ARG   A NH2   1 
ATOM   4816 N  N     . LEU   A 1 752  ? 3.822   -20.697 -44.769 1.00 87.83  ? 901  LEU   A N     1 
ATOM   4817 C  CA    . LEU   A 1 752  ? 3.855   -19.559 -43.809 1.00 84.48  ? 901  LEU   A CA    1 
ATOM   4818 C  C     . LEU   A 1 752  ? 3.467   -20.058 -42.412 1.00 83.34  ? 901  LEU   A C     1 
ATOM   4819 O  O     . LEU   A 1 752  ? 2.625   -20.972 -42.325 1.00 82.40  ? 901  LEU   A O     1 
ATOM   4820 C  CB    . LEU   A 1 752  ? 2.903   -18.453 -44.280 1.00 82.62  ? 901  LEU   A CB    1 
ATOM   4821 C  CG    . LEU   A 1 752  ? 3.235   -17.801 -45.622 1.00 80.18  ? 901  LEU   A CG    1 
ATOM   4822 C  CD1   . LEU   A 1 752  ? 2.238   -16.695 -45.941 1.00 79.67  ? 901  LEU   A CD1   1 
ATOM   4823 C  CD2   . LEU   A 1 752  ? 4.657   -17.259 -45.639 1.00 79.40  ? 901  LEU   A CD2   1 
ATOM   4824 N  N     . GLY   A 1 753  ? 4.066   -19.470 -41.371 1.00 84.65  ? 902  GLY   A N     1 
ATOM   4825 C  CA    . GLY   A 1 753  ? 3.793   -19.781 -39.954 1.00 84.92  ? 902  GLY   A CA    1 
ATOM   4826 C  C     . GLY   A 1 753  ? 2.634   -18.962 -39.412 1.00 85.41  ? 902  GLY   A C     1 
ATOM   4827 O  O     . GLY   A 1 753  ? 2.118   -18.107 -40.158 1.00 85.37  ? 902  GLY   A O     1 
ATOM   4828 N  N     . TYR   A 1 754  ? 2.247   -19.215 -38.158 1.00 86.77  ? 903  TYR   A N     1 
ATOM   4829 C  CA    . TYR   A 1 754  ? 1.117   -18.558 -37.446 1.00 88.09  ? 903  TYR   A CA    1 
ATOM   4830 C  C     . TYR   A 1 754  ? 1.252   -17.032 -37.527 1.00 87.42  ? 903  TYR   A C     1 
ATOM   4831 O  O     . TYR   A 1 754  ? 0.232   -16.348 -37.754 1.00 86.52  ? 903  TYR   A O     1 
ATOM   4832 C  CB    . TYR   A 1 754  ? 1.070   -19.016 -35.986 1.00 91.15  ? 903  TYR   A CB    1 
ATOM   4833 C  CG    . TYR   A 1 754  ? 0.032   -18.324 -35.139 1.00 95.35  ? 903  TYR   A CG    1 
ATOM   4834 C  CD1   . TYR   A 1 754  ? -1.291  -18.739 -35.146 1.00 97.45  ? 903  TYR   A CD1   1 
ATOM   4835 C  CD2   . TYR   A 1 754  ? 0.369   -17.253 -34.324 1.00 97.32  ? 903  TYR   A CD2   1 
ATOM   4836 C  CE1   . TYR   A 1 754  ? -2.252  -18.111 -34.369 1.00 98.52  ? 903  TYR   A CE1   1 
ATOM   4837 C  CE2   . TYR   A 1 754  ? -0.580  -16.610 -33.544 1.00 98.44  ? 903  TYR   A CE2   1 
ATOM   4838 C  CZ    . TYR   A 1 754  ? -1.895  -17.043 -33.563 1.00 98.94  ? 903  TYR   A CZ    1 
ATOM   4839 O  OH    . TYR   A 1 754  ? -2.835  -16.418 -32.796 1.00 99.29  ? 903  TYR   A OH    1 
ATOM   4840 N  N     . VAL   A 1 755  ? 2.475   -16.523 -37.348 1.00 85.66  ? 904  VAL   A N     1 
ATOM   4841 C  CA    . VAL   A 1 755  ? 2.779   -15.063 -37.266 1.00 84.52  ? 904  VAL   A CA    1 
ATOM   4842 C  C     . VAL   A 1 755  ? 2.432   -14.406 -38.607 1.00 81.11  ? 904  VAL   A C     1 
ATOM   4843 O  O     . VAL   A 1 755  ? 1.704   -13.395 -38.593 1.00 83.55  ? 904  VAL   A O     1 
ATOM   4844 C  CB    . VAL   A 1 755  ? 4.250   -14.811 -36.876 1.00 87.53  ? 904  VAL   A CB    1 
ATOM   4845 C  CG1   . VAL   A 1 755  ? 4.571   -13.324 -36.815 1.00 88.53  ? 904  VAL   A CG1   1 
ATOM   4846 C  CG2   . VAL   A 1 755  ? 4.608   -15.491 -35.561 1.00 88.22  ? 904  VAL   A CG2   1 
ATOM   4847 N  N     . HIS   A 1 756  ? 2.932   -14.963 -39.715 1.00 76.14  ? 905  HIS   A N     1 
ATOM   4848 C  CA    . HIS   A 1 756  ? 2.760   -14.425 -41.092 1.00 72.85  ? 905  HIS   A CA    1 
ATOM   4849 C  C     . HIS   A 1 756  ? 1.303   -14.577 -41.547 1.00 72.19  ? 905  HIS   A C     1 
ATOM   4850 O  O     . HIS   A 1 756  ? 0.799   -13.655 -42.215 1.00 73.77  ? 905  HIS   A O     1 
ATOM   4851 C  CB    . HIS   A 1 756  ? 3.734   -15.093 -42.073 1.00 70.92  ? 905  HIS   A CB    1 
ATOM   4852 C  CG    . HIS   A 1 756  ? 5.156   -14.685 -41.883 1.00 70.63  ? 905  HIS   A CG    1 
ATOM   4853 N  ND1   . HIS   A 1 756  ? 6.207   -15.410 -42.411 1.00 70.87  ? 905  HIS   A ND1   1 
ATOM   4854 C  CD2   . HIS   A 1 756  ? 5.709   -13.646 -41.220 1.00 70.40  ? 905  HIS   A CD2   1 
ATOM   4855 C  CE1   . HIS   A 1 756  ? 7.344   -14.825 -42.093 1.00 70.52  ? 905  HIS   A CE1   1 
ATOM   4856 N  NE2   . HIS   A 1 756  ? 7.066   -13.741 -41.362 1.00 69.87  ? 905  HIS   A NE2   1 
ATOM   4857 N  N     . ARG   A 1 757  ? 0.658   -15.696 -41.205 1.00 71.03  ? 906  ARG   A N     1 
ATOM   4858 C  CA    . ARG   A 1 757  ? -0.738  -16.014 -41.615 1.00 70.91  ? 906  ARG   A CA    1 
ATOM   4859 C  C     . ARG   A 1 757  ? -1.723  -15.066 -40.918 1.00 68.93  ? 906  ARG   A C     1 
ATOM   4860 O  O     . ARG   A 1 757  ? -2.765  -14.761 -41.531 1.00 68.20  ? 906  ARG   A O     1 
ATOM   4861 C  CB    . ARG   A 1 757  ? -1.064  -17.481 -41.315 1.00 72.10  ? 906  ARG   A CB    1 
ATOM   4862 C  CG    . ARG   A 1 757  ? -0.419  -18.460 -42.284 1.00 73.19  ? 906  ARG   A CG    1 
ATOM   4863 C  CD    . ARG   A 1 757  ? -0.635  -19.906 -41.885 1.00 74.74  ? 906  ARG   A CD    1 
ATOM   4864 N  NE    . ARG   A 1 757  ? -0.025  -20.831 -42.835 1.00 75.88  ? 906  ARG   A NE    1 
ATOM   4865 C  CZ    . ARG   A 1 757  ? -0.633  -21.370 -43.892 1.00 78.72  ? 906  ARG   A CZ    1 
ATOM   4866 N  NH1   . ARG   A 1 757  ? 0.039   -22.194 -44.682 1.00 79.05  ? 906  ARG   A NH1   1 
ATOM   4867 N  NH2   . ARG   A 1 757  ? -1.900  -21.097 -44.163 1.00 79.13  ? 906  ARG   A NH2   1 
ATOM   4868 N  N     . ASN   A 1 758  ? -1.406  -14.620 -39.697 1.00 67.86  ? 907  ASN   A N     1 
ATOM   4869 C  CA    . ASN   A 1 758  ? -2.270  -13.723 -38.879 1.00 69.04  ? 907  ASN   A CA    1 
ATOM   4870 C  C     . ASN   A 1 758  ? -2.447  -12.365 -39.569 1.00 66.78  ? 907  ASN   A C     1 
ATOM   4871 O  O     . ASN   A 1 758  ? -3.526  -11.765 -39.395 1.00 67.32  ? 907  ASN   A O     1 
ATOM   4872 C  CB    . ASN   A 1 758  ? -1.730  -13.525 -37.460 1.00 70.89  ? 907  ASN   A CB    1 
ATOM   4873 C  CG    . ASN   A 1 758  ? -2.362  -14.458 -36.449 1.00 73.20  ? 907  ASN   A CG    1 
ATOM   4874 O  OD1   . ASN   A 1 758  ? -3.164  -15.321 -36.802 1.00 74.34  ? 907  ASN   A OD1   1 
ATOM   4875 N  ND2   . ASN   A 1 758  ? -2.009  -14.286 -35.186 1.00 75.20  ? 907  ASN   A ND2   1 
ATOM   4876 N  N     . PHE   A 1 759  ? -1.437  -11.895 -40.308 1.00 64.66  ? 908  PHE   A N     1 
ATOM   4877 C  CA    . PHE   A 1 759  ? -1.463  -10.600 -41.039 1.00 64.37  ? 908  PHE   A CA    1 
ATOM   4878 C  C     . PHE   A 1 759  ? -2.595  -10.613 -42.074 1.00 63.52  ? 908  PHE   A C     1 
ATOM   4879 O  O     . PHE   A 1 759  ? -3.155  -9.537  -42.357 1.00 66.58  ? 908  PHE   A O     1 
ATOM   4880 C  CB    . PHE   A 1 759  ? -0.112  -10.310 -41.699 1.00 65.21  ? 908  PHE   A CB    1 
ATOM   4881 C  CG    . PHE   A 1 759  ? 0.972   -9.864  -40.750 1.00 66.59  ? 908  PHE   A CG    1 
ATOM   4882 C  CD1   . PHE   A 1 759  ? 0.869   -8.659  -40.069 1.00 67.42  ? 908  PHE   A CD1   1 
ATOM   4883 C  CD2   . PHE   A 1 759  ? 2.107   -10.636 -40.552 1.00 66.30  ? 908  PHE   A CD2   1 
ATOM   4884 C  CE1   . PHE   A 1 759  ? 1.868   -8.246  -39.200 1.00 67.87  ? 908  PHE   A CE1   1 
ATOM   4885 C  CE2   . PHE   A 1 759  ? 3.108   -10.219 -39.686 1.00 67.06  ? 908  PHE   A CE2   1 
ATOM   4886 C  CZ    . PHE   A 1 759  ? 2.987   -9.025  -39.012 1.00 67.67  ? 908  PHE   A CZ    1 
ATOM   4887 N  N     . ALA   A 1 760  ? -2.923  -11.793 -42.608 1.00 62.59  ? 909  ALA   A N     1 
ATOM   4888 C  CA    . ALA   A 1 760  ? -3.959  -12.004 -43.647 1.00 62.84  ? 909  ALA   A CA    1 
ATOM   4889 C  C     . ALA   A 1 760  ? -5.350  -11.677 -43.092 1.00 61.61  ? 909  ALA   A C     1 
ATOM   4890 O  O     . ALA   A 1 760  ? -6.221  -11.294 -43.893 1.00 61.25  ? 909  ALA   A O     1 
ATOM   4891 C  CB    . ALA   A 1 760  ? -3.902  -13.424 -44.157 1.00 63.12  ? 909  ALA   A CB    1 
ATOM   4892 N  N     . GLY   A 1 761  ? -5.550  -11.835 -41.780 1.00 61.48  ? 910  GLY   A N     1 
ATOM   4893 C  CA    . GLY   A 1 761  ? -6.870  -11.723 -41.131 1.00 62.52  ? 910  GLY   A CA    1 
ATOM   4894 C  C     . GLY   A 1 761  ? -7.759  -12.891 -41.519 1.00 63.44  ? 910  GLY   A C     1 
ATOM   4895 O  O     . GLY   A 1 761  ? -7.283  -14.042 -41.439 1.00 64.71  ? 910  GLY   A O     1 
ATOM   4896 N  N     . ASN   A 1 762  ? -8.992  -12.609 -41.949 1.00 64.22  ? 911  ASN   A N     1 
ATOM   4897 C  CA    . ASN   A 1 762  ? -9.990  -13.624 -42.385 1.00 66.06  ? 911  ASN   A CA    1 
ATOM   4898 C  C     . ASN   A 1 762  ? -10.413 -13.341 -43.833 1.00 66.41  ? 911  ASN   A C     1 
ATOM   4899 O  O     . ASN   A 1 762  ? -11.503 -13.800 -44.230 1.00 68.11  ? 911  ASN   A O     1 
ATOM   4900 C  CB    . ASN   A 1 762  ? -11.188 -13.666 -41.430 1.00 67.32  ? 911  ASN   A CB    1 
ATOM   4901 C  CG    . ASN   A 1 762  ? -11.903 -12.337 -41.294 1.00 68.38  ? 911  ASN   A CG    1 
ATOM   4902 O  OD1   . ASN   A 1 762  ? -11.788 -11.464 -42.154 1.00 68.96  ? 911  ASN   A OD1   1 
ATOM   4903 N  ND2   . ASN   A 1 762  ? -12.647 -12.172 -40.213 1.00 69.40  ? 911  ASN   A ND2   1 
ATOM   4904 N  N     . ARG   A 1 763  ? -9.571  -12.630 -44.592 1.00 65.79  ? 912  ARG   A N     1 
ATOM   4905 C  CA    . ARG   A 1 763  ? -9.846  -12.179 -45.984 1.00 64.63  ? 912  ARG   A CA    1 
ATOM   4906 C  C     . ARG   A 1 763  ? -9.318  -13.207 -46.992 1.00 65.33  ? 912  ARG   A C     1 
ATOM   4907 O  O     . ARG   A 1 763  ? -9.593  -13.030 -48.196 1.00 66.78  ? 912  ARG   A O     1 
ATOM   4908 C  CB    . ARG   A 1 763  ? -9.192  -10.818 -46.242 1.00 63.61  ? 912  ARG   A CB    1 
ATOM   4909 C  CG    . ARG   A 1 763  ? -9.878  -9.658  -45.540 1.00 63.36  ? 912  ARG   A CG    1 
ATOM   4910 C  CD    . ARG   A 1 763  ? -11.020 -9.091  -46.357 1.00 63.26  ? 912  ARG   A CD    1 
ATOM   4911 N  NE    . ARG   A 1 763  ? -11.744 -8.065  -45.618 1.00 63.78  ? 912  ARG   A NE    1 
ATOM   4912 C  CZ    . ARG   A 1 763  ? -12.477 -7.098  -46.165 1.00 64.19  ? 912  ARG   A CZ    1 
ATOM   4913 N  NH1   . ARG   A 1 763  ? -12.593 -7.001  -47.478 1.00 63.16  ? 912  ARG   A NH1   1 
ATOM   4914 N  NH2   . ARG   A 1 763  ? -13.088 -6.218  -45.392 1.00 66.89  ? 912  ARG   A NH2   1 
ATOM   4915 N  N     . PHE   A 1 764  ? -8.583  -14.225 -46.529 1.00 64.82  ? 913  PHE   A N     1 
ATOM   4916 C  CA    . PHE   A 1 764  ? -7.933  -15.255 -47.382 1.00 65.24  ? 913  PHE   A CA    1 
ATOM   4917 C  C     . PHE   A 1 764  ? -7.180  -14.548 -48.515 1.00 64.01  ? 913  PHE   A C     1 
ATOM   4918 O  O     . PHE   A 1 764  ? -7.365  -14.919 -49.691 1.00 63.52  ? 913  PHE   A O     1 
ATOM   4919 C  CB    . PHE   A 1 764  ? -8.977  -16.239 -47.918 1.00 67.75  ? 913  PHE   A CB    1 
ATOM   4920 C  CG    . PHE   A 1 764  ? -9.701  -17.029 -46.857 1.00 70.71  ? 913  PHE   A CG    1 
ATOM   4921 C  CD1   . PHE   A 1 764  ? -9.206  -18.248 -46.419 1.00 71.42  ? 913  PHE   A CD1   1 
ATOM   4922 C  CD2   . PHE   A 1 764  ? -10.876 -16.552 -46.295 1.00 72.62  ? 913  PHE   A CD2   1 
ATOM   4923 C  CE1   . PHE   A 1 764  ? -9.871  -18.973 -45.441 1.00 72.06  ? 913  PHE   A CE1   1 
ATOM   4924 C  CE2   . PHE   A 1 764  ? -11.540 -17.278 -45.316 1.00 72.99  ? 913  PHE   A CE2   1 
ATOM   4925 C  CZ    . PHE   A 1 764  ? -11.037 -18.487 -44.891 1.00 72.84  ? 913  PHE   A CZ    1 
ATOM   4926 N  N     . SER   A 1 765  ? -6.363  -13.550 -48.163 1.00 63.03  ? 914  SER   A N     1 
ATOM   4927 C  CA    . SER   A 1 765  ? -5.671  -12.637 -49.111 1.00 61.21  ? 914  SER   A CA    1 
ATOM   4928 C  C     . SER   A 1 765  ? -4.220  -12.405 -48.680 1.00 61.33  ? 914  SER   A C     1 
ATOM   4929 O  O     . SER   A 1 765  ? -4.001  -12.016 -47.515 1.00 64.00  ? 914  SER   A O     1 
ATOM   4930 C  CB    . SER   A 1 765  ? -6.406  -11.332 -49.221 1.00 60.65  ? 914  SER   A CB    1 
ATOM   4931 O  OG    . SER   A 1 765  ? -5.691  -10.424 -50.046 1.00 60.63  ? 914  SER   A OG    1 
ATOM   4932 N  N     . ASP   A 1 766  ? -3.278  -12.616 -49.604 1.00 59.57  ? 915  ASP   A N     1 
ATOM   4933 C  CA    . ASP   A 1 766  ? -1.839  -12.278 -49.438 1.00 57.34  ? 915  ASP   A CA    1 
ATOM   4934 C  C     . ASP   A 1 766  ? -1.674  -10.755 -49.521 1.00 56.16  ? 915  ASP   A C     1 
ATOM   4935 O  O     . ASP   A 1 766  ? -0.768  -10.230 -48.856 1.00 56.92  ? 915  ASP   A O     1 
ATOM   4936 C  CB    . ASP   A 1 766  ? -0.978  -12.992 -50.484 1.00 56.80  ? 915  ASP   A CB    1 
ATOM   4937 C  CG    . ASP   A 1 766  ? -0.867  -14.493 -50.271 1.00 56.29  ? 915  ASP   A CG    1 
ATOM   4938 O  OD1   . ASP   A 1 766  ? -0.632  -14.904 -49.118 1.00 55.16  ? 915  ASP   A OD1   1 
ATOM   4939 O  OD2   . ASP   A 1 766  ? -1.014  -15.239 -51.259 1.00 56.51  ? 915  ASP   A OD2   1 
ATOM   4940 N  N     . HIS   A 1 767  ? -2.521  -10.083 -50.308 1.00 55.78  ? 916  HIS   A N     1 
ATOM   4941 C  CA    . HIS   A 1 767  ? -2.508  -8.609  -50.520 1.00 54.96  ? 916  HIS   A CA    1 
ATOM   4942 C  C     . HIS   A 1 767  ? -2.989  -7.878  -49.259 1.00 55.53  ? 916  HIS   A C     1 
ATOM   4943 O  O     . HIS   A 1 767  ? -2.496  -6.762  -49.010 1.00 58.02  ? 916  HIS   A O     1 
ATOM   4944 C  CB    . HIS   A 1 767  ? -3.342  -8.233  -51.750 1.00 53.81  ? 916  HIS   A CB    1 
ATOM   4945 C  CG    . HIS   A 1 767  ? -2.743  -8.690  -53.037 1.00 52.83  ? 916  HIS   A CG    1 
ATOM   4946 N  ND1   . HIS   A 1 767  ? -3.049  -9.911  -53.602 1.00 52.15  ? 916  HIS   A ND1   1 
ATOM   4947 C  CD2   . HIS   A 1 767  ? -1.858  -8.099  -53.867 1.00 52.21  ? 916  HIS   A CD2   1 
ATOM   4948 C  CE1   . HIS   A 1 767  ? -2.383  -10.049 -54.729 1.00 51.64  ? 916  HIS   A CE1   1 
ATOM   4949 N  NE2   . HIS   A 1 767  ? -1.643  -8.954  -54.912 1.00 51.60  ? 916  HIS   A NE2   1 
ATOM   4950 N  N     . VAL   A 1 768  ? -3.923  -8.466  -48.505 1.00 54.62  ? 917  VAL   A N     1 
ATOM   4951 C  CA    . VAL   A 1 768  ? -4.382  -7.924  -47.191 1.00 55.04  ? 917  VAL   A CA    1 
ATOM   4952 C  C     . VAL   A 1 768  ? -3.252  -8.127  -46.173 1.00 55.67  ? 917  VAL   A C     1 
ATOM   4953 O  O     . VAL   A 1 768  ? -2.987  -7.192  -45.394 1.00 58.23  ? 917  VAL   A O     1 
ATOM   4954 C  CB    . VAL   A 1 768  ? -5.705  -8.565  -46.725 1.00 54.22  ? 917  VAL   A CB    1 
ATOM   4955 C  CG1   . VAL   A 1 768  ? -6.048  -8.182  -45.292 1.00 54.13  ? 917  VAL   A CG1   1 
ATOM   4956 C  CG2   . VAL   A 1 768  ? -6.857  -8.215  -47.655 1.00 53.81  ? 917  VAL   A CG2   1 
ATOM   4957 N  N     . ALA   A 1 769  ? -2.609  -9.299  -46.189 1.00 55.69  ? 918  ALA   A N     1 
ATOM   4958 C  CA    . ALA   A 1 769  ? -1.417  -9.621  -45.368 1.00 56.19  ? 918  ALA   A CA    1 
ATOM   4959 C  C     . ALA   A 1 769  ? -0.325  -8.577  -45.627 1.00 56.19  ? 918  ALA   A C     1 
ATOM   4960 O  O     . ALA   A 1 769  ? 0.268   -8.086  -44.648 1.00 56.91  ? 918  ALA   A O     1 
ATOM   4961 C  CB    . ALA   A 1 769  ? -0.929  -11.018 -45.669 1.00 56.77  ? 918  ALA   A CB    1 
ATOM   4962 N  N     . LEU   A 1 770  ? -0.091  -8.243  -46.899 1.00 56.37  ? 919  LEU   A N     1 
ATOM   4963 C  CA    . LEU   A 1 770  ? 0.903   -7.225  -47.331 1.00 57.59  ? 919  LEU   A CA    1 
ATOM   4964 C  C     . LEU   A 1 770  ? 0.559   -5.876  -46.688 1.00 57.71  ? 919  LEU   A C     1 
ATOM   4965 O  O     . LEU   A 1 770  ? 1.406   -5.339  -45.959 1.00 56.41  ? 919  LEU   A O     1 
ATOM   4966 C  CB    . LEU   A 1 770  ? 0.896   -7.130  -48.860 1.00 58.96  ? 919  LEU   A CB    1 
ATOM   4967 C  CG    . LEU   A 1 770  ? 1.939   -6.190  -49.463 1.00 61.01  ? 919  LEU   A CG    1 
ATOM   4968 C  CD1   . LEU   A 1 770  ? 3.343   -6.750  -49.280 1.00 61.27  ? 919  LEU   A CD1   1 
ATOM   4969 C  CD2   . LEU   A 1 770  ? 1.652   -5.929  -50.934 1.00 61.53  ? 919  LEU   A CD2   1 
ATOM   4970 N  N     . LEU   A 1 771  ? -0.647  -5.361  -46.942 1.00 58.77  ? 920  LEU   A N     1 
ATOM   4971 C  CA    . LEU   A 1 771  ? -1.127  -4.055  -46.410 1.00 59.18  ? 920  LEU   A CA    1 
ATOM   4972 C  C     . LEU   A 1 771  ? -1.021  -4.041  -44.879 1.00 60.83  ? 920  LEU   A C     1 
ATOM   4973 O  O     . LEU   A 1 771  ? -0.716  -2.969  -44.320 1.00 63.41  ? 920  LEU   A O     1 
ATOM   4974 C  CB    . LEU   A 1 771  ? -2.574  -3.828  -46.855 1.00 58.39  ? 920  LEU   A CB    1 
ATOM   4975 C  CG    . LEU   A 1 771  ? -2.767  -3.525  -48.339 1.00 58.44  ? 920  LEU   A CG    1 
ATOM   4976 C  CD1   . LEU   A 1 771  ? -4.240  -3.586  -48.710 1.00 59.03  ? 920  LEU   A CD1   1 
ATOM   4977 C  CD2   . LEU   A 1 771  ? -2.178  -2.169  -48.696 1.00 59.00  ? 920  LEU   A CD2   1 
ATOM   4978 N  N     . SER   A 1 772  ? -1.266  -5.185  -44.233 1.00 61.03  ? 921  SER   A N     1 
ATOM   4979 C  CA    . SER   A 1 772  ? -1.330  -5.329  -42.755 1.00 61.42  ? 921  SER   A CA    1 
ATOM   4980 C  C     . SER   A 1 772  ? 0.072   -5.252  -42.133 1.00 62.65  ? 921  SER   A C     1 
ATOM   4981 O  O     . SER   A 1 772  ? 0.192   -4.616  -41.067 1.00 62.31  ? 921  SER   A O     1 
ATOM   4982 C  CB    . SER   A 1 772  ? -2.052  -6.592  -42.369 1.00 61.01  ? 921  SER   A CB    1 
ATOM   4983 O  OG    . SER   A 1 772  ? -3.421  -6.516  -42.739 1.00 59.00  ? 921  SER   A OG    1 
ATOM   4984 N  N     . VAL   A 1 773  ? 1.093   -5.860  -42.754 1.00 63.60  ? 922  VAL   A N     1 
ATOM   4985 C  CA    . VAL   A 1 773  ? 2.501   -5.795  -42.250 1.00 64.36  ? 922  VAL   A CA    1 
ATOM   4986 C  C     . VAL   A 1 773  ? 2.993   -4.346  -42.344 1.00 63.70  ? 922  VAL   A C     1 
ATOM   4987 O  O     . VAL   A 1 773  ? 3.796   -3.958  -41.485 1.00 66.89  ? 922  VAL   A O     1 
ATOM   4988 C  CB    . VAL   A 1 773  ? 3.475   -6.759  -42.961 1.00 64.77  ? 922  VAL   A CB    1 
ATOM   4989 C  CG1   . VAL   A 1 773  ? 3.097   -8.213  -42.744 1.00 66.23  ? 922  VAL   A CG1   1 
ATOM   4990 C  CG2   . VAL   A 1 773  ? 3.634   -6.469  -44.445 1.00 65.39  ? 922  VAL   A CG2   1 
ATOM   4991 N  N     . PHE   A 1 774  ? 2.532   -3.583  -43.342 1.00 62.85  ? 923  PHE   A N     1 
ATOM   4992 C  CA    . PHE   A 1 774  ? 2.891   -2.151  -43.532 1.00 63.32  ? 923  PHE   A CA    1 
ATOM   4993 C  C     . PHE   A 1 774  ? 2.261   -1.317  -42.413 1.00 63.76  ? 923  PHE   A C     1 
ATOM   4994 O  O     . PHE   A 1 774  ? 2.974   -0.482  -41.831 1.00 65.28  ? 923  PHE   A O     1 
ATOM   4995 C  CB    . PHE   A 1 774  ? 2.483   -1.645  -44.918 1.00 62.43  ? 923  PHE   A CB    1 
ATOM   4996 C  CG    . PHE   A 1 774  ? 3.542   -1.867  -45.965 1.00 62.40  ? 923  PHE   A CG    1 
ATOM   4997 C  CD1   . PHE   A 1 774  ? 4.563   -0.946  -46.147 1.00 61.74  ? 923  PHE   A CD1   1 
ATOM   4998 C  CD2   . PHE   A 1 774  ? 3.538   -3.015  -46.741 1.00 63.64  ? 923  PHE   A CD2   1 
ATOM   4999 C  CE1   . PHE   A 1 774  ? 5.545   -1.162  -47.101 1.00 61.59  ? 923  PHE   A CE1   1 
ATOM   5000 C  CE2   . PHE   A 1 774  ? 4.521   -3.229  -47.694 1.00 63.24  ? 923  PHE   A CE2   1 
ATOM   5001 C  CZ    . PHE   A 1 774  ? 5.521   -2.302  -47.872 1.00 62.13  ? 923  PHE   A CZ    1 
ATOM   5002 N  N     . GLN   A 1 775  ? 0.977   -1.548  -42.126 1.00 63.65  ? 924  GLN   A N     1 
ATOM   5003 C  CA    . GLN   A 1 775  ? 0.241   -0.901  -41.006 1.00 64.58  ? 924  GLN   A CA    1 
ATOM   5004 C  C     . GLN   A 1 775  ? 0.989   -1.182  -39.694 1.00 64.33  ? 924  GLN   A C     1 
ATOM   5005 O  O     . GLN   A 1 775  ? 1.242   -0.222  -38.940 1.00 66.00  ? 924  GLN   A O     1 
ATOM   5006 C  CB    . GLN   A 1 775  ? -1.205  -1.404  -40.972 1.00 65.43  ? 924  GLN   A CB    1 
ATOM   5007 C  CG    . GLN   A 1 775  ? -2.062  -0.760  -39.891 1.00 66.65  ? 924  GLN   A CG    1 
ATOM   5008 C  CD    . GLN   A 1 775  ? -3.537  -0.941  -40.157 1.00 67.85  ? 924  GLN   A CD    1 
ATOM   5009 O  OE1   . GLN   A 1 775  ? -4.135  -0.225  -40.958 1.00 69.42  ? 924  GLN   A OE1   1 
ATOM   5010 N  NE2   . GLN   A 1 775  ? -4.143  -1.903  -39.480 1.00 67.61  ? 924  GLN   A NE2   1 
ATOM   5011 N  N     . ALA   A 1 776  ? 1.354   -2.446  -39.454 1.00 62.19  ? 925  ALA   A N     1 
ATOM   5012 C  CA    . ALA   A 1 776  ? 2.050   -2.920  -38.234 1.00 61.50  ? 925  ALA   A CA    1 
ATOM   5013 C  C     . ALA   A 1 776  ? 3.484   -2.375  -38.191 1.00 62.64  ? 925  ALA   A C     1 
ATOM   5014 O  O     . ALA   A 1 776  ? 3.939   -2.005  -37.094 1.00 65.24  ? 925  ALA   A O     1 
ATOM   5015 C  CB    . ALA   A 1 776  ? 2.029   -4.427  -38.191 1.00 61.19  ? 925  ALA   A CB    1 
ATOM   5016 N  N     . TRP   A 1 777  ? 4.166   -2.338  -39.340 1.00 64.02  ? 926  TRP   A N     1 
ATOM   5017 C  CA    . TRP   A 1 777  ? 5.574   -1.875  -39.489 1.00 64.97  ? 926  TRP   A CA    1 
ATOM   5018 C  C     . TRP   A 1 777  ? 5.655   -0.358  -39.284 1.00 69.19  ? 926  TRP   A C     1 
ATOM   5019 O  O     . TRP   A 1 777  ? 6.529   0.085   -38.518 1.00 71.67  ? 926  TRP   A O     1 
ATOM   5020 C  CB    . TRP   A 1 777  ? 6.129   -2.286  -40.858 1.00 62.67  ? 926  TRP   A CB    1 
ATOM   5021 C  CG    . TRP   A 1 777  ? 7.436   -1.654  -41.223 1.00 61.23  ? 926  TRP   A CG    1 
ATOM   5022 C  CD1   . TRP   A 1 777  ? 8.674   -2.004  -40.773 1.00 61.05  ? 926  TRP   A CD1   1 
ATOM   5023 C  CD2   . TRP   A 1 777  ? 7.637   -0.572  -42.148 1.00 61.08  ? 926  TRP   A CD2   1 
ATOM   5024 N  NE1   . TRP   A 1 777  ? 9.630   -1.210  -41.345 1.00 60.31  ? 926  TRP   A NE1   1 
ATOM   5025 C  CE2   . TRP   A 1 777  ? 9.025   -0.321  -42.193 1.00 60.73  ? 926  TRP   A CE2   1 
ATOM   5026 C  CE3   . TRP   A 1 777  ? 6.784   0.211   -42.937 1.00 60.79  ? 926  TRP   A CE3   1 
ATOM   5027 C  CZ2   . TRP   A 1 777  ? 9.574   0.676   -42.998 1.00 60.93  ? 926  TRP   A CZ2   1 
ATOM   5028 C  CZ3   . TRP   A 1 777  ? 7.328   1.197   -43.730 1.00 60.17  ? 926  TRP   A CZ3   1 
ATOM   5029 C  CH2   . TRP   A 1 777  ? 8.705   1.426   -43.758 1.00 60.30  ? 926  TRP   A CH2   1 
ATOM   5030 N  N     . ASP   A 1 778  ? 4.774   0.395   -39.950 1.00 73.78  ? 927  ASP   A N     1 
ATOM   5031 C  CA    . ASP   A 1 778  ? 4.724   1.883   -39.919 1.00 74.80  ? 927  ASP   A CA    1 
ATOM   5032 C  C     . ASP   A 1 778  ? 4.375   2.352   -38.501 1.00 75.25  ? 927  ASP   A C     1 
ATOM   5033 O  O     . ASP   A 1 778  ? 4.757   3.483   -38.145 1.00 75.24  ? 927  ASP   A O     1 
ATOM   5034 C  CB    . ASP   A 1 778  ? 3.726   2.416   -40.952 1.00 75.84  ? 927  ASP   A CB    1 
ATOM   5035 C  CG    . ASP   A 1 778  ? 3.877   3.892   -41.270 1.00 78.07  ? 927  ASP   A CG    1 
ATOM   5036 O  OD1   . ASP   A 1 778  ? 5.021   4.390   -41.233 1.00 78.92  ? 927  ASP   A OD1   1 
ATOM   5037 O  OD2   . ASP   A 1 778  ? 2.847   4.531   -41.565 1.00 81.45  ? 927  ASP   A OD2   1 
ATOM   5038 N  N     . ASP   A 1 779  ? 3.668   1.515   -37.736 1.00 76.56  ? 928  ASP   A N     1 
ATOM   5039 C  CA    . ASP   A 1 779  ? 3.316   1.756   -36.311 1.00 77.34  ? 928  ASP   A CA    1 
ATOM   5040 C  C     . ASP   A 1 779  ? 4.555   1.508   -35.439 1.00 76.37  ? 928  ASP   A C     1 
ATOM   5041 O  O     . ASP   A 1 779  ? 4.770   2.289   -34.493 1.00 78.64  ? 928  ASP   A O     1 
ATOM   5042 C  CB    . ASP   A 1 779  ? 2.132   0.879   -35.889 1.00 79.28  ? 928  ASP   A CB    1 
ATOM   5043 C  CG    . ASP   A 1 779  ? 1.552   1.219   -34.526 1.00 82.57  ? 928  ASP   A CG    1 
ATOM   5044 O  OD1   . ASP   A 1 779  ? 1.397   2.423   -34.235 1.00 84.63  ? 928  ASP   A OD1   1 
ATOM   5045 O  OD2   . ASP   A 1 779  ? 1.257   0.275   -33.766 1.00 86.34  ? 928  ASP   A OD2   1 
ATOM   5046 N  N     . ALA   A 1 780  ? 5.338   0.469   -35.752 1.00 75.11  ? 929  ALA   A N     1 
ATOM   5047 C  CA    . ALA   A 1 780  ? 6.552   0.049   -35.007 1.00 74.59  ? 929  ALA   A CA    1 
ATOM   5048 C  C     . ALA   A 1 780  ? 7.680   1.076   -35.181 1.00 74.91  ? 929  ALA   A C     1 
ATOM   5049 O  O     . ALA   A 1 780  ? 8.473   1.233   -34.232 1.00 78.55  ? 929  ALA   A O     1 
ATOM   5050 C  CB    . ALA   A 1 780  ? 6.993   -1.322  -35.460 1.00 73.31  ? 929  ALA   A CB    1 
ATOM   5051 N  N     . ARG   A 1 781  ? 7.754   1.733   -36.345 1.00 74.26  ? 930  ARG   A N     1 
ATOM   5052 C  CA    . ARG   A 1 781  ? 8.772   2.768   -36.682 1.00 73.66  ? 930  ARG   A CA    1 
ATOM   5053 C  C     . ARG   A 1 781  ? 8.658   3.974   -35.741 1.00 76.21  ? 930  ARG   A C     1 
ATOM   5054 O  O     . ARG   A 1 781  ? 9.686   4.652   -35.542 1.00 77.14  ? 930  ARG   A O     1 
ATOM   5055 C  CB    . ARG   A 1 781  ? 8.599   3.265   -38.119 1.00 73.46  ? 930  ARG   A CB    1 
ATOM   5056 C  CG    . ARG   A 1 781  ? 9.081   2.297   -39.188 1.00 73.57  ? 930  ARG   A CG    1 
ATOM   5057 C  CD    . ARG   A 1 781  ? 9.428   3.031   -40.469 1.00 73.28  ? 930  ARG   A CD    1 
ATOM   5058 N  NE    . ARG   A 1 781  ? 8.300   3.788   -40.999 1.00 72.74  ? 930  ARG   A NE    1 
ATOM   5059 C  CZ    . ARG   A 1 781  ? 8.354   4.602   -42.050 1.00 72.53  ? 930  ARG   A CZ    1 
ATOM   5060 N  NH1   . ARG   A 1 781  ? 7.264   5.242   -42.443 1.00 72.06  ? 930  ARG   A NH1   1 
ATOM   5061 N  NH2   . ARG   A 1 781  ? 9.488   4.778   -42.708 1.00 72.57  ? 930  ARG   A NH2   1 
ATOM   5062 N  N     . MET   A 1 782  ? 7.459   4.237   -35.205 1.00 78.85  ? 931  MET   A N     1 
ATOM   5063 C  CA    . MET   A 1 782  ? 7.156   5.386   -34.304 1.00 83.27  ? 931  MET   A CA    1 
ATOM   5064 C  C     . MET   A 1 782  ? 8.172   5.441   -33.153 1.00 83.78  ? 931  MET   A C     1 
ATOM   5065 O  O     . MET   A 1 782  ? 8.459   6.562   -32.687 1.00 86.81  ? 931  MET   A O     1 
ATOM   5066 C  CB    . MET   A 1 782  ? 5.744   5.281   -33.714 1.00 87.81  ? 931  MET   A CB    1 
ATOM   5067 C  CG    . MET   A 1 782  ? 4.616   5.387   -34.737 1.00 90.65  ? 931  MET   A CG    1 
ATOM   5068 S  SD    . MET   A 1 782  ? 4.301   7.078   -35.319 1.00 92.47  ? 931  MET   A SD    1 
ATOM   5069 C  CE    . MET   A 1 782  ? 5.216   7.080   -36.861 1.00 91.23  ? 931  MET   A CE    1 
ATOM   5070 N  N     . GLY   A 1 783  ? 8.690   4.286   -32.714 1.00 82.03  ? 932  GLY   A N     1 
ATOM   5071 C  CA    . GLY   A 1 783  ? 9.639   4.166   -31.589 1.00 82.03  ? 932  GLY   A CA    1 
ATOM   5072 C  C     . GLY   A 1 783  ? 11.092  4.074   -32.034 1.00 81.84  ? 932  GLY   A C     1 
ATOM   5073 O  O     . GLY   A 1 783  ? 11.851  3.327   -31.388 1.00 85.54  ? 932  GLY   A O     1 
ATOM   5074 N  N     . GLY   A 1 784  ? 11.484  4.810   -33.079 1.00 79.82  ? 933  GLY   A N     1 
ATOM   5075 C  CA    . GLY   A 1 784  ? 12.889  4.928   -33.519 1.00 79.76  ? 933  GLY   A CA    1 
ATOM   5076 C  C     . GLY   A 1 784  ? 13.355  3.715   -34.309 1.00 79.99  ? 933  GLY   A C     1 
ATOM   5077 O  O     . GLY   A 1 784  ? 12.549  2.782   -34.497 1.00 81.03  ? 933  GLY   A O     1 
ATOM   5078 N  N     . GLU   A 1 785  ? 14.624  3.723   -34.734 1.00 80.72  ? 934  GLU   A N     1 
ATOM   5079 C  CA    . GLU   A 1 785  ? 15.211  2.763   -35.710 1.00 82.07  ? 934  GLU   A CA    1 
ATOM   5080 C  C     . GLU   A 1 785  ? 15.332  1.361   -35.102 1.00 84.56  ? 934  GLU   A C     1 
ATOM   5081 O  O     . GLU   A 1 785  ? 14.978  0.395   -35.799 1.00 89.36  ? 934  GLU   A O     1 
ATOM   5082 C  CB    . GLU   A 1 785  ? 16.587  3.237   -36.179 1.00 81.29  ? 934  GLU   A CB    1 
ATOM   5083 C  CG    . GLU   A 1 785  ? 17.290  2.241   -37.086 1.00 81.18  ? 934  GLU   A CG    1 
ATOM   5084 C  CD    . GLU   A 1 785  ? 18.352  2.845   -37.986 1.00 82.41  ? 934  GLU   A CD    1 
ATOM   5085 O  OE1   . GLU   A 1 785  ? 19.073  3.752   -37.522 1.00 83.31  ? 934  GLU   A OE1   1 
ATOM   5086 O  OE2   . GLU   A 1 785  ? 18.451  2.411   -39.151 1.00 82.50  ? 934  GLU   A OE2   1 
ATOM   5087 N  N     . GLU   A 1 786  ? 15.848  1.246   -33.875 1.00 86.48  ? 935  GLU   A N     1 
ATOM   5088 C  CA    . GLU   A 1 786  ? 16.160  -0.063  -33.238 1.00 86.50  ? 935  GLU   A CA    1 
ATOM   5089 C  C     . GLU   A 1 786  ? 14.859  -0.845  -33.009 1.00 84.86  ? 935  GLU   A C     1 
ATOM   5090 O  O     . GLU   A 1 786  ? 14.884  -2.077  -33.190 1.00 86.48  ? 935  GLU   A O     1 
ATOM   5091 C  CB    . GLU   A 1 786  ? 16.938  0.130   -31.934 1.00 87.29  ? 935  GLU   A CB    1 
ATOM   5092 C  CG    . GLU   A 1 786  ? 17.715  -1.104  -31.502 1.00 88.06  ? 935  GLU   A CG    1 
ATOM   5093 C  CD    . GLU   A 1 786  ? 18.829  -1.537  -32.443 1.00 89.91  ? 935  GLU   A CD    1 
ATOM   5094 O  OE1   . GLU   A 1 786  ? 19.370  -0.671  -33.166 1.00 89.35  ? 935  GLU   A OE1   1 
ATOM   5095 O  OE2   . GLU   A 1 786  ? 19.154  -2.744  -32.453 1.00 89.44  ? 935  GLU   A OE2   1 
ATOM   5096 N  N     . ALA   A 1 787  ? 13.769  -0.157  -32.645 1.00 82.23  ? 936  ALA   A N     1 
ATOM   5097 C  CA    . ALA   A 1 787  ? 12.423  -0.746  -32.433 1.00 82.09  ? 936  ALA   A CA    1 
ATOM   5098 C  C     . ALA   A 1 787  ? 11.887  -1.319  -33.752 1.00 81.16  ? 936  ALA   A C     1 
ATOM   5099 O  O     . ALA   A 1 787  ? 11.212  -2.369  -33.710 1.00 80.02  ? 936  ALA   A O     1 
ATOM   5100 C  CB    . ALA   A 1 787  ? 11.483  0.289   -31.864 1.00 81.54  ? 936  ALA   A CB    1 
ATOM   5101 N  N     . GLU   A 1 788  ? 12.167  -0.647  -34.874 1.00 79.10  ? 937  GLU   A N     1 
ATOM   5102 C  CA    . GLU   A 1 788  ? 11.818  -1.110  -36.244 1.00 78.07  ? 937  GLU   A CA    1 
ATOM   5103 C  C     . GLU   A 1 788  ? 12.547  -2.430  -36.521 1.00 78.19  ? 937  GLU   A C     1 
ATOM   5104 O  O     . GLU   A 1 788  ? 11.883  -3.380  -36.978 1.00 79.75  ? 937  GLU   A O     1 
ATOM   5105 C  CB    . GLU   A 1 788  ? 12.177  -0.040  -37.279 1.00 77.29  ? 937  GLU   A CB    1 
ATOM   5106 C  CG    . GLU   A 1 788  ? 11.783  -0.394  -38.703 1.00 76.90  ? 937  GLU   A CG    1 
ATOM   5107 C  CD    . GLU   A 1 788  ? 12.325  0.557   -39.758 1.00 78.08  ? 937  GLU   A CD    1 
ATOM   5108 O  OE1   . GLU   A 1 788  ? 12.547  1.741   -39.430 1.00 79.63  ? 937  GLU   A OE1   1 
ATOM   5109 O  OE2   . GLU   A 1 788  ? 12.534  0.112   -40.903 1.00 76.92  ? 937  GLU   A OE2   1 
ATOM   5110 N  N     . ILE   A 1 789  ? 13.855  -2.482  -36.239 1.00 78.67  ? 938  ILE   A N     1 
ATOM   5111 C  CA    . ILE   A 1 789  ? 14.729  -3.672  -36.482 1.00 78.69  ? 938  ILE   A CA    1 
ATOM   5112 C  C     . ILE   A 1 789  ? 14.229  -4.834  -35.613 1.00 78.06  ? 938  ILE   A C     1 
ATOM   5113 O  O     . ILE   A 1 789  ? 14.235  -5.978  -36.107 1.00 77.10  ? 938  ILE   A O     1 
ATOM   5114 C  CB    . ILE   A 1 789  ? 16.219  -3.357  -36.220 1.00 79.13  ? 938  ILE   A CB    1 
ATOM   5115 C  CG1   . ILE   A 1 789  ? 16.740  -2.244  -37.135 1.00 79.51  ? 938  ILE   A CG1   1 
ATOM   5116 C  CG2   . ILE   A 1 789  ? 17.065  -4.618  -36.347 1.00 80.18  ? 938  ILE   A CG2   1 
ATOM   5117 C  CD1   . ILE   A 1 789  ? 18.208  -1.922  -36.953 1.00 79.54  ? 938  ILE   A CD1   1 
ATOM   5118 N  N     . ARG   A 1 790  ? 13.814  -4.550  -34.374 1.00 79.00  ? 939  ARG   A N     1 
ATOM   5119 C  CA    . ARG   A 1 790  ? 13.327  -5.568  -33.403 1.00 80.00  ? 939  ARG   A CA    1 
ATOM   5120 C  C     . ARG   A 1 790  ? 11.997  -6.150  -33.894 1.00 79.83  ? 939  ARG   A C     1 
ATOM   5121 O  O     . ARG   A 1 790  ? 11.863  -7.391  -33.883 1.00 83.96  ? 939  ARG   A O     1 
ATOM   5122 C  CB    . ARG   A 1 790  ? 13.199  -4.969  -32.000 1.00 79.78  ? 939  ARG   A CB    1 
ATOM   5123 C  CG    . ARG   A 1 790  ? 14.540  -4.714  -31.327 1.00 81.42  ? 939  ARG   A CG    1 
ATOM   5124 C  CD    . ARG   A 1 790  ? 14.441  -4.617  -29.818 1.00 82.93  ? 939  ARG   A CD    1 
ATOM   5125 N  NE    . ARG   A 1 790  ? 15.759  -4.539  -29.201 1.00 82.81  ? 939  ARG   A NE    1 
ATOM   5126 C  CZ    . ARG   A 1 790  ? 15.981  -4.406  -27.897 1.00 81.62  ? 939  ARG   A CZ    1 
ATOM   5127 N  NH1   . ARG   A 1 790  ? 14.967  -4.334  -27.049 1.00 79.83  ? 939  ARG   A NH1   1 
ATOM   5128 N  NH2   . ARG   A 1 790  ? 17.223  -4.342  -27.446 1.00 81.92  ? 939  ARG   A NH2   1 
ATOM   5129 N  N     . PHE   A 1 791  ? 11.061  -5.290  -34.309 1.00 77.56  ? 940  PHE   A N     1 
ATOM   5130 C  CA    . PHE   A 1 791  ? 9.745   -5.679  -34.882 1.00 75.19  ? 940  PHE   A CA    1 
ATOM   5131 C  C     . PHE   A 1 791  ? 9.967   -6.624  -36.069 1.00 74.49  ? 940  PHE   A C     1 
ATOM   5132 O  O     . PHE   A 1 791  ? 9.311   -7.681  -36.124 1.00 74.75  ? 940  PHE   A O     1 
ATOM   5133 C  CB    . PHE   A 1 791  ? 8.942   -4.444  -35.301 1.00 74.34  ? 940  PHE   A CB    1 
ATOM   5134 C  CG    . PHE   A 1 791  ? 7.678   -4.747  -36.067 1.00 72.77  ? 940  PHE   A CG    1 
ATOM   5135 C  CD1   . PHE   A 1 791  ? 6.510   -5.091  -35.404 1.00 71.50  ? 940  PHE   A CD1   1 
ATOM   5136 C  CD2   . PHE   A 1 791  ? 7.659   -4.691  -37.453 1.00 72.91  ? 940  PHE   A CD2   1 
ATOM   5137 C  CE1   . PHE   A 1 791  ? 5.350   -5.371  -36.111 1.00 71.78  ? 940  PHE   A CE1   1 
ATOM   5138 C  CE2   . PHE   A 1 791  ? 6.499   -4.975  -38.159 1.00 72.29  ? 940  PHE   A CE2   1 
ATOM   5139 C  CZ    . PHE   A 1 791  ? 5.347   -5.312  -37.486 1.00 72.43  ? 940  PHE   A CZ    1 
ATOM   5140 N  N     . CYS   A 1 792  ? 10.871  -6.253  -36.980 1.00 73.51  ? 941  CYS   A N     1 
ATOM   5141 C  CA    . CYS   A 1 792  ? 11.175  -7.001  -38.231 1.00 75.10  ? 941  CYS   A CA    1 
ATOM   5142 C  C     . CYS   A 1 792  ? 11.779  -8.371  -37.892 1.00 79.26  ? 941  CYS   A C     1 
ATOM   5143 O  O     . CYS   A 1 792  ? 11.286  -9.377  -38.440 1.00 81.62  ? 941  CYS   A O     1 
ATOM   5144 C  CB    . CYS   A 1 792  ? 12.104  -6.204  -39.140 1.00 74.19  ? 941  CYS   A CB    1 
ATOM   5145 S  SG    . CYS   A 1 792  ? 11.278  -4.830  -39.985 1.00 71.95  ? 941  CYS   A SG    1 
ATOM   5146 N  N     . GLU   A 1 793  ? 12.796  -8.408  -37.022 1.00 82.02  ? 942  GLU   A N     1 
ATOM   5147 C  CA    . GLU   A 1 793  ? 13.470  -9.659  -36.570 1.00 82.70  ? 942  GLU   A CA    1 
ATOM   5148 C  C     . GLU   A 1 793  ? 12.443  -10.580 -35.898 1.00 82.02  ? 942  GLU   A C     1 
ATOM   5149 O  O     . GLU   A 1 793  ? 12.391  -11.771 -36.269 1.00 80.72  ? 942  GLU   A O     1 
ATOM   5150 C  CB    . GLU   A 1 793  ? 14.622  -9.356  -35.608 1.00 84.47  ? 942  GLU   A CB    1 
ATOM   5151 C  CG    . GLU   A 1 793  ? 15.936  -9.051  -36.304 1.00 86.41  ? 942  GLU   A CG    1 
ATOM   5152 C  CD    . GLU   A 1 793  ? 17.074  -8.651  -35.377 1.00 89.35  ? 942  GLU   A CD    1 
ATOM   5153 O  OE1   . GLU   A 1 793  ? 16.942  -8.846  -34.150 1.00 87.77  ? 942  GLU   A OE1   1 
ATOM   5154 O  OE2   . GLU   A 1 793  ? 18.092  -8.140  -35.884 1.00 93.63  ? 942  GLU   A OE2   1 
ATOM   5155 N  N     . HIS   A 1 794  ? 11.661  -10.042 -34.956 1.00 80.76  ? 943  HIS   A N     1 
ATOM   5156 C  CA    . HIS   A 1 794  ? 10.664  -10.787 -34.138 1.00 81.99  ? 943  HIS   A CA    1 
ATOM   5157 C  C     . HIS   A 1 794  ? 9.560   -11.372 -35.029 1.00 81.37  ? 943  HIS   A C     1 
ATOM   5158 O  O     . HIS   A 1 794  ? 9.083   -12.477 -34.706 1.00 84.21  ? 943  HIS   A O     1 
ATOM   5159 C  CB    . HIS   A 1 794  ? 10.080  -9.890  -33.036 1.00 83.20  ? 943  HIS   A CB    1 
ATOM   5160 C  CG    . HIS   A 1 794  ? 8.955   -10.521 -32.284 1.00 85.02  ? 943  HIS   A CG    1 
ATOM   5161 N  ND1   . HIS   A 1 794  ? 7.678   -9.990  -32.282 1.00 87.95  ? 943  HIS   A ND1   1 
ATOM   5162 C  CD2   . HIS   A 1 794  ? 8.901   -11.639 -31.530 1.00 86.52  ? 943  HIS   A CD2   1 
ATOM   5163 C  CE1   . HIS   A 1 794  ? 6.890   -10.749 -31.547 1.00 88.41  ? 943  HIS   A CE1   1 
ATOM   5164 N  NE2   . HIS   A 1 794  ? 7.616   -11.768 -31.075 1.00 88.78  ? 943  HIS   A NE2   1 
ATOM   5165 N  N     . LYS   A 1 795  ? 9.170   -10.661 -36.095 1.00 78.80  ? 944  LYS   A N     1 
ATOM   5166 C  CA    . LYS   A 1 795  ? 8.046   -11.040 -36.996 1.00 77.52  ? 944  LYS   A CA    1 
ATOM   5167 C  C     . LYS   A 1 795  ? 8.577   -11.688 -38.282 1.00 77.94  ? 944  LYS   A C     1 
ATOM   5168 O  O     . LYS   A 1 795  ? 7.750   -11.970 -39.172 1.00 79.16  ? 944  LYS   A O     1 
ATOM   5169 C  CB    . LYS   A 1 795  ? 7.192   -9.809  -37.320 1.00 77.51  ? 944  LYS   A CB    1 
ATOM   5170 C  CG    . LYS   A 1 795  ? 6.472   -9.184  -36.133 1.00 77.88  ? 944  LYS   A CG    1 
ATOM   5171 C  CD    . LYS   A 1 795  ? 5.390   -10.064 -35.544 1.00 77.98  ? 944  LYS   A CD    1 
ATOM   5172 C  CE    . LYS   A 1 795  ? 4.616   -9.384  -34.435 1.00 78.50  ? 944  LYS   A CE    1 
ATOM   5173 N  NZ    . LYS   A 1 795  ? 3.574   -10.276 -33.875 1.00 79.87  ? 944  LYS   A NZ    1 
ATOM   5174 N  N     . ARG   A 1 796  ? 9.892   -11.928 -38.374 1.00 78.24  ? 945  ARG   A N     1 
ATOM   5175 C  CA    . ARG   A 1 796  ? 10.564  -12.575 -39.537 1.00 78.31  ? 945  ARG   A CA    1 
ATOM   5176 C  C     . ARG   A 1 796  ? 10.254  -11.776 -40.812 1.00 73.83  ? 945  ARG   A C     1 
ATOM   5177 O  O     . ARG   A 1 796  ? 9.777   -12.384 -41.794 1.00 74.20  ? 945  ARG   A O     1 
ATOM   5178 C  CB    . ARG   A 1 796  ? 10.134  -14.043 -39.656 1.00 82.98  ? 945  ARG   A CB    1 
ATOM   5179 C  CG    . ARG   A 1 796  ? 11.010  -15.025 -38.891 1.00 87.39  ? 945  ARG   A CG    1 
ATOM   5180 C  CD    . ARG   A 1 796  ? 10.836  -14.952 -37.386 1.00 92.05  ? 945  ARG   A CD    1 
ATOM   5181 N  NE    . ARG   A 1 796  ? 11.846  -15.737 -36.685 1.00 97.26  ? 945  ARG   A NE    1 
ATOM   5182 C  CZ    . ARG   A 1 796  ? 12.050  -15.726 -35.367 1.00 99.57  ? 945  ARG   A CZ    1 
ATOM   5183 N  NH1   . ARG   A 1 796  ? 11.310  -14.965 -34.575 1.00 99.28  ? 945  ARG   A NH1   1 
ATOM   5184 N  NH2   . ARG   A 1 796  ? 13.003  -16.479 -34.844 1.00 99.80  ? 945  ARG   A NH2   1 
ATOM   5185 N  N     . LEU   A 1 797  ? 10.520  -10.465 -40.792 1.00 69.14  ? 946  LEU   A N     1 
ATOM   5186 C  CA    . LEU   A 1 797  ? 10.286  -9.530  -41.929 1.00 66.83  ? 946  LEU   A CA    1 
ATOM   5187 C  C     . LEU   A 1 797  ? 11.626  -8.962  -42.413 1.00 65.44  ? 946  LEU   A C     1 
ATOM   5188 O  O     . LEU   A 1 797  ? 12.511  -8.727  -41.569 1.00 66.04  ? 946  LEU   A O     1 
ATOM   5189 C  CB    . LEU   A 1 797  ? 9.352   -8.404  -41.476 1.00 66.49  ? 946  LEU   A CB    1 
ATOM   5190 C  CG    . LEU   A 1 797  ? 8.002   -8.842  -40.912 1.00 66.49  ? 946  LEU   A CG    1 
ATOM   5191 C  CD1   . LEU   A 1 797  ? 7.240   -7.650  -40.352 1.00 66.91  ? 946  LEU   A CD1   1 
ATOM   5192 C  CD2   . LEU   A 1 797  ? 7.173   -9.554  -41.968 1.00 66.57  ? 946  LEU   A CD2   1 
ATOM   5193 N  N     . ASN   A 1 798  ? 11.753  -8.752  -43.726 1.00 63.26  ? 947  ASN   A N     1 
ATOM   5194 C  CA    . ASN   A 1 798  ? 12.944  -8.154  -44.387 1.00 62.67  ? 947  ASN   A CA    1 
ATOM   5195 C  C     . ASN   A 1 798  ? 12.768  -6.632  -44.400 1.00 62.07  ? 947  ASN   A C     1 
ATOM   5196 O  O     . ASN   A 1 798  ? 12.053  -6.129  -45.288 1.00 61.95  ? 947  ASN   A O     1 
ATOM   5197 C  CB    . ASN   A 1 798  ? 13.139  -8.735  -45.790 1.00 64.27  ? 947  ASN   A CB    1 
ATOM   5198 C  CG    . ASN   A 1 798  ? 14.322  -8.154  -46.537 1.00 65.44  ? 947  ASN   A CG    1 
ATOM   5199 O  OD1   . ASN   A 1 798  ? 15.059  -7.322  -46.013 1.00 67.58  ? 947  ASN   A OD1   1 
ATOM   5200 N  ND2   . ASN   A 1 798  ? 14.510  -8.588  -47.772 1.00 65.93  ? 947  ASN   A ND2   1 
ATOM   5201 N  N     . MET   A 1 799  ? 13.403  -5.938  -43.451 1.00 62.64  ? 948  MET   A N     1 
ATOM   5202 C  CA    . MET   A 1 799  ? 13.238  -4.480  -43.198 1.00 63.67  ? 948  MET   A CA    1 
ATOM   5203 C  C     . MET   A 1 799  ? 13.598  -3.676  -44.455 1.00 63.72  ? 948  MET   A C     1 
ATOM   5204 O  O     . MET   A 1 799  ? 12.861  -2.723  -44.774 1.00 65.10  ? 948  MET   A O     1 
ATOM   5205 C  CB    . MET   A 1 799  ? 14.128  -4.029  -42.036 1.00 65.23  ? 948  MET   A CB    1 
ATOM   5206 C  CG    . MET   A 1 799  ? 13.865  -2.606  -41.582 1.00 66.35  ? 948  MET   A CG    1 
ATOM   5207 S  SD    . MET   A 1 799  ? 15.015  -2.066  -40.294 1.00 67.29  ? 948  MET   A SD    1 
ATOM   5208 C  CE    . MET   A 1 799  ? 16.563  -2.081  -41.198 1.00 65.15  ? 948  MET   A CE    1 
ATOM   5209 N  N     . ALA   A 1 800  ? 14.689  -4.045  -45.134 1.00 63.90  ? 949  ALA   A N     1 
ATOM   5210 C  CA    . ALA   A 1 800  ? 15.214  -3.371  -46.347 1.00 63.86  ? 949  ALA   A CA    1 
ATOM   5211 C  C     . ALA   A 1 800  ? 14.146  -3.341  -47.448 1.00 63.86  ? 949  ALA   A C     1 
ATOM   5212 O  O     . ALA   A 1 800  ? 14.123  -2.358  -48.212 1.00 63.97  ? 949  ALA   A O     1 
ATOM   5213 C  CB    . ALA   A 1 800  ? 16.469  -4.064  -46.820 1.00 64.26  ? 949  ALA   A CB    1 
ATOM   5214 N  N     . THR   A 1 801  ? 13.304  -4.378  -47.529 1.00 63.82  ? 950  THR   A N     1 
ATOM   5215 C  CA    . THR   A 1 801  ? 12.208  -4.513  -48.527 1.00 64.37  ? 950  THR   A CA    1 
ATOM   5216 C  C     . THR   A 1 801  ? 11.086  -3.521  -48.204 1.00 62.83  ? 950  THR   A C     1 
ATOM   5217 O  O     . THR   A 1 801  ? 10.638  -2.818  -49.127 1.00 60.90  ? 950  THR   A O     1 
ATOM   5218 C  CB    . THR   A 1 801  ? 11.668  -5.948  -48.570 1.00 66.80  ? 950  THR   A CB    1 
ATOM   5219 O  OG1   . THR   A 1 801  ? 12.755  -6.819  -48.882 1.00 69.25  ? 950  THR   A OG1   1 
ATOM   5220 C  CG2   . THR   A 1 801  ? 10.560  -6.139  -49.583 1.00 67.77  ? 950  THR   A CG2   1 
ATOM   5221 N  N     . LEU   A 1 802  ? 10.644  -3.483  -46.944 1.00 62.57  ? 951  LEU   A N     1 
ATOM   5222 C  CA    . LEU   A 1 802  ? 9.511   -2.637  -46.479 1.00 62.44  ? 951  LEU   A CA    1 
ATOM   5223 C  C     . LEU   A 1 802  ? 9.869   -1.156  -46.659 1.00 63.28  ? 951  LEU   A C     1 
ATOM   5224 O  O     . LEU   A 1 802  ? 8.986   -0.382  -47.079 1.00 63.11  ? 951  LEU   A O     1 
ATOM   5225 C  CB    . LEU   A 1 802  ? 9.196   -2.973  -45.016 1.00 61.20  ? 951  LEU   A CB    1 
ATOM   5226 C  CG    . LEU   A 1 802  ? 8.639   -4.376  -44.771 1.00 60.48  ? 951  LEU   A CG    1 
ATOM   5227 C  CD1   . LEU   A 1 802  ? 8.588   -4.694  -43.283 1.00 59.99  ? 951  LEU   A CD1   1 
ATOM   5228 C  CD2   . LEU   A 1 802  ? 7.261   -4.533  -45.395 1.00 59.75  ? 951  LEU   A CD2   1 
ATOM   5229 N  N     . ARG   A 1 803  ? 11.122  -0.787  -46.376 1.00 64.56  ? 952  ARG   A N     1 
ATOM   5230 C  CA    . ARG   A 1 803  ? 11.636  0.606   -46.481 1.00 65.74  ? 952  ARG   A CA    1 
ATOM   5231 C  C     . ARG   A 1 803  ? 11.638  1.048   -47.949 1.00 65.48  ? 952  ARG   A C     1 
ATOM   5232 O  O     . ARG   A 1 803  ? 11.122  2.146   -48.231 1.00 66.41  ? 952  ARG   A O     1 
ATOM   5233 C  CB    . ARG   A 1 803  ? 13.039  0.702   -45.875 1.00 66.89  ? 952  ARG   A CB    1 
ATOM   5234 C  CG    . ARG   A 1 803  ? 13.052  0.683   -44.354 1.00 67.71  ? 952  ARG   A CG    1 
ATOM   5235 C  CD    . ARG   A 1 803  ? 14.456  0.748   -43.789 1.00 69.16  ? 952  ARG   A CD    1 
ATOM   5236 N  NE    . ARG   A 1 803  ? 14.471  1.221   -42.411 1.00 69.84  ? 952  ARG   A NE    1 
ATOM   5237 C  CZ    . ARG   A 1 803  ? 15.558  1.322   -41.653 1.00 68.75  ? 952  ARG   A CZ    1 
ATOM   5238 N  NH1   . ARG   A 1 803  ? 16.742  0.975   -42.133 1.00 69.21  ? 952  ARG   A NH1   1 
ATOM   5239 N  NH2   . ARG   A 1 803  ? 15.457  1.768   -40.413 1.00 68.35  ? 952  ARG   A NH2   1 
ATOM   5240 N  N     . MET   A 1 804  ? 12.204  0.226   -48.838 1.00 65.53  ? 953  MET   A N     1 
ATOM   5241 C  CA    . MET   A 1 804  ? 12.299  0.498   -50.298 1.00 68.29  ? 953  MET   A CA    1 
ATOM   5242 C  C     . MET   A 1 804  ? 10.893  0.580   -50.906 1.00 66.40  ? 953  MET   A C     1 
ATOM   5243 O  O     . MET   A 1 804  ? 10.697  1.410   -51.815 1.00 67.11  ? 953  MET   A O     1 
ATOM   5244 C  CB    . MET   A 1 804  ? 13.097  -0.594  -51.018 1.00 72.95  ? 953  MET   A CB    1 
ATOM   5245 C  CG    . MET   A 1 804  ? 14.601  -0.439  -50.881 1.00 77.00  ? 953  MET   A CG    1 
ATOM   5246 S  SD    . MET   A 1 804  ? 15.521  -1.524  -52.006 1.00 84.96  ? 953  MET   A SD    1 
ATOM   5247 C  CE    . MET   A 1 804  ? 14.878  -3.130  -51.536 1.00 84.35  ? 953  MET   A CE    1 
ATOM   5248 N  N     . THR   A 1 805  ? 9.961   -0.253  -50.432 1.00 65.33  ? 954  THR   A N     1 
ATOM   5249 C  CA    . THR   A 1 805  ? 8.556   -0.317  -50.920 1.00 63.92  ? 954  THR   A CA    1 
ATOM   5250 C  C     . THR   A 1 805  ? 7.812   0.952   -50.491 1.00 63.42  ? 954  THR   A C     1 
ATOM   5251 O  O     . THR   A 1 805  ? 7.119   1.539   -51.347 1.00 62.95  ? 954  THR   A O     1 
ATOM   5252 C  CB    . THR   A 1 805  ? 7.832   -1.573  -50.420 1.00 63.08  ? 954  THR   A CB    1 
ATOM   5253 O  OG1   . THR   A 1 805  ? 8.616   -2.726  -50.725 1.00 62.38  ? 954  THR   A OG1   1 
ATOM   5254 C  CG2   . THR   A 1 805  ? 6.459   -1.734  -51.034 1.00 63.50  ? 954  THR   A CG2   1 
ATOM   5255 N  N     . TRP   A 1 806  ? 7.940   1.343   -49.218 1.00 63.75  ? 955  TRP   A N     1 
ATOM   5256 C  CA    . TRP   A 1 806  ? 7.375   2.606   -48.668 1.00 65.88  ? 955  TRP   A CA    1 
ATOM   5257 C  C     . TRP   A 1 806  ? 7.910   3.783   -49.487 1.00 64.95  ? 955  TRP   A C     1 
ATOM   5258 O  O     . TRP   A 1 806  ? 7.095   4.595   -49.959 1.00 64.62  ? 955  TRP   A O     1 
ATOM   5259 C  CB    . TRP   A 1 806  ? 7.705   2.765   -47.178 1.00 68.43  ? 955  TRP   A CB    1 
ATOM   5260 C  CG    . TRP   A 1 806  ? 7.199   4.041   -46.575 1.00 69.90  ? 955  TRP   A CG    1 
ATOM   5261 C  CD1   . TRP   A 1 806  ? 7.828   5.253   -46.568 1.00 71.36  ? 955  TRP   A CD1   1 
ATOM   5262 C  CD2   . TRP   A 1 806  ? 5.951   4.235   -45.884 1.00 71.45  ? 955  TRP   A CD2   1 
ATOM   5263 N  NE1   . TRP   A 1 806  ? 7.061   6.186   -45.924 1.00 72.18  ? 955  TRP   A NE1   1 
ATOM   5264 C  CE2   . TRP   A 1 806  ? 5.903   5.592   -45.494 1.00 72.18  ? 955  TRP   A CE2   1 
ATOM   5265 C  CE3   . TRP   A 1 806  ? 4.874   3.402   -45.557 1.00 73.12  ? 955  TRP   A CE3   1 
ATOM   5266 C  CZ2   . TRP   A 1 806  ? 4.822   6.128   -44.794 1.00 73.30  ? 955  TRP   A CZ2   1 
ATOM   5267 C  CZ3   . TRP   A 1 806  ? 3.806   3.932   -44.865 1.00 74.09  ? 955  TRP   A CZ3   1 
ATOM   5268 C  CH2   . TRP   A 1 806  ? 3.782   5.278   -44.490 1.00 73.72  ? 955  TRP   A CH2   1 
ATOM   5269 N  N     . GLU   A 1 807  ? 9.233   3.850   -49.657 1.00 65.52  ? 956  GLU   A N     1 
ATOM   5270 C  CA    . GLU   A 1 807  ? 9.927   4.903   -50.443 1.00 66.58  ? 956  GLU   A CA    1 
ATOM   5271 C  C     . GLU   A 1 807  ? 9.296   4.986   -51.838 1.00 65.01  ? 956  GLU   A C     1 
ATOM   5272 O  O     . GLU   A 1 807  ? 9.026   6.113   -52.297 1.00 64.02  ? 956  GLU   A O     1 
ATOM   5273 C  CB    . GLU   A 1 807  ? 11.429  4.612   -50.515 1.00 68.91  ? 956  GLU   A CB    1 
ATOM   5274 C  CG    . GLU   A 1 807  ? 12.242  5.746   -51.117 1.00 71.39  ? 956  GLU   A CG    1 
ATOM   5275 C  CD    . GLU   A 1 807  ? 11.944  7.111   -50.521 1.00 71.98  ? 956  GLU   A CD    1 
ATOM   5276 O  OE1   . GLU   A 1 807  ? 12.104  7.260   -49.290 1.00 71.91  ? 956  GLU   A OE1   1 
ATOM   5277 O  OE2   . GLU   A 1 807  ? 11.524  8.010   -51.282 1.00 71.32  ? 956  GLU   A OE2   1 
ATOM   5278 N  N     . ALA   A 1 808  ? 9.057   3.830   -52.468 1.00 65.42  ? 957  ALA   A N     1 
ATOM   5279 C  CA    . ALA   A 1 808  ? 8.453   3.691   -53.815 1.00 65.63  ? 957  ALA   A CA    1 
ATOM   5280 C  C     . ALA   A 1 808  ? 7.013   4.220   -53.805 1.00 65.45  ? 957  ALA   A C     1 
ATOM   5281 O  O     . ALA   A 1 808  ? 6.644   4.929   -54.765 1.00 65.40  ? 957  ALA   A O     1 
ATOM   5282 C  CB    . ALA   A 1 808  ? 8.505   2.249   -54.258 1.00 65.86  ? 957  ALA   A CB    1 
ATOM   5283 N  N     . LYS   A 1 809  ? 6.240   3.884   -52.765 1.00 64.12  ? 958  LYS   A N     1 
ATOM   5284 C  CA    . LYS   A 1 809  ? 4.833   4.333   -52.567 1.00 64.05  ? 958  LYS   A CA    1 
ATOM   5285 C  C     . LYS   A 1 809  ? 4.774   5.866   -52.533 1.00 64.91  ? 958  LYS   A C     1 
ATOM   5286 O  O     . LYS   A 1 809  ? 3.841   6.433   -53.137 1.00 65.40  ? 958  LYS   A O     1 
ATOM   5287 C  CB    . LYS   A 1 809  ? 4.262   3.754   -51.268 1.00 63.68  ? 958  LYS   A CB    1 
ATOM   5288 C  CG    . LYS   A 1 809  ? 2.794   4.068   -51.008 1.00 64.18  ? 958  LYS   A CG    1 
ATOM   5289 C  CD    . LYS   A 1 809  ? 2.389   3.926   -49.556 1.00 64.39  ? 958  LYS   A CD    1 
ATOM   5290 C  CE    . LYS   A 1 809  ? 2.950   5.017   -48.670 1.00 63.85  ? 958  LYS   A CE    1 
ATOM   5291 N  NZ    . LYS   A 1 809  ? 2.171   5.153   -47.418 1.00 63.74  ? 958  LYS   A NZ    1 
ATOM   5292 N  N     . VAL   A 1 810  ? 5.726   6.501   -51.842 1.00 65.28  ? 959  VAL   A N     1 
ATOM   5293 C  CA    . VAL   A 1 810  ? 5.820   7.985   -51.689 1.00 65.34  ? 959  VAL   A CA    1 
ATOM   5294 C  C     . VAL   A 1 810  ? 6.038   8.611   -53.073 1.00 64.14  ? 959  VAL   A C     1 
ATOM   5295 O  O     . VAL   A 1 810  ? 5.441   9.676   -53.334 1.00 64.17  ? 959  VAL   A O     1 
ATOM   5296 C  CB    . VAL   A 1 810  ? 6.934   8.386   -50.697 1.00 65.78  ? 959  VAL   A CB    1 
ATOM   5297 C  CG1   . VAL   A 1 810  ? 7.218   9.882   -50.725 1.00 65.82  ? 959  VAL   A CG1   1 
ATOM   5298 C  CG2   . VAL   A 1 810  ? 6.613   7.935   -49.278 1.00 65.12  ? 959  VAL   A CG2   1 
ATOM   5299 N  N     . GLN   A 1 811  ? 6.851   7.969   -53.920 1.00 62.87  ? 960  GLN   A N     1 
ATOM   5300 C  CA    . GLN   A 1 811  ? 7.233   8.472   -55.268 1.00 62.66  ? 960  GLN   A CA    1 
ATOM   5301 C  C     . GLN   A 1 811  ? 6.069   8.289   -56.249 1.00 61.68  ? 960  GLN   A C     1 
ATOM   5302 O  O     . GLN   A 1 811  ? 5.844   9.204   -57.065 1.00 61.25  ? 960  GLN   A O     1 
ATOM   5303 C  CB    . GLN   A 1 811  ? 8.487   7.763   -55.780 1.00 63.43  ? 960  GLN   A CB    1 
ATOM   5304 C  CG    . GLN   A 1 811  ? 9.759   8.189   -55.060 1.00 64.08  ? 960  GLN   A CG    1 
ATOM   5305 C  CD    . GLN   A 1 811  ? 11.002  7.932   -55.878 1.00 63.94  ? 960  GLN   A CD    1 
ATOM   5306 O  OE1   . GLN   A 1 811  ? 10.975  7.941   -57.107 1.00 62.54  ? 960  GLN   A OE1   1 
ATOM   5307 N  NE2   . GLN   A 1 811  ? 12.112  7.705   -55.194 1.00 64.79  ? 960  GLN   A NE2   1 
ATOM   5308 N  N     . LEU   A 1 812  ? 5.377   7.146   -56.192 1.00 60.79  ? 961  LEU   A N     1 
ATOM   5309 C  CA    . LEU   A 1 812  ? 4.154   6.883   -56.999 1.00 59.60  ? 961  LEU   A CA    1 
ATOM   5310 C  C     . LEU   A 1 812  ? 3.102   7.935   -56.640 1.00 59.67  ? 961  LEU   A C     1 
ATOM   5311 O  O     . LEU   A 1 812  ? 2.553   8.561   -57.564 1.00 60.42  ? 961  LEU   A O     1 
ATOM   5312 C  CB    . LEU   A 1 812  ? 3.635   5.467   -56.724 1.00 57.68  ? 961  LEU   A CB    1 
ATOM   5313 C  CG    . LEU   A 1 812  ? 4.443   4.325   -57.341 1.00 56.19  ? 961  LEU   A CG    1 
ATOM   5314 C  CD1   . LEU   A 1 812  ? 3.877   2.976   -56.923 1.00 55.99  ? 961  LEU   A CD1   1 
ATOM   5315 C  CD2   . LEU   A 1 812  ? 4.486   4.434   -58.856 1.00 55.44  ? 961  LEU   A CD2   1 
ATOM   5316 N  N     . LYS   A 1 813  ? 2.863   8.126   -55.340 1.00 61.30  ? 962  LYS   A N     1 
ATOM   5317 C  CA    . LYS   A 1 813  ? 1.890   9.106   -54.788 1.00 63.37  ? 962  LYS   A CA    1 
ATOM   5318 C  C     . LYS   A 1 813  ? 2.219   10.507  -55.320 1.00 64.69  ? 962  LYS   A C     1 
ATOM   5319 O  O     . LYS   A 1 813  ? 1.280   11.211  -55.723 1.00 64.37  ? 962  LYS   A O     1 
ATOM   5320 C  CB    . LYS   A 1 813  ? 1.917   9.069   -53.257 1.00 64.18  ? 962  LYS   A CB    1 
ATOM   5321 C  CG    . LYS   A 1 813  ? 0.799   9.841   -52.569 1.00 65.37  ? 962  LYS   A CG    1 
ATOM   5322 C  CD    . LYS   A 1 813  ? 0.821   9.745   -51.053 1.00 65.23  ? 962  LYS   A CD    1 
ATOM   5323 C  CE    . LYS   A 1 813  ? 0.606   8.341   -50.527 1.00 63.64  ? 962  LYS   A CE    1 
ATOM   5324 N  NZ    . LYS   A 1 813  ? 0.601   8.316   -49.046 1.00 63.95  ? 962  LYS   A NZ    1 
ATOM   5325 N  N     . GLU   A 1 814  ? 3.503   10.881  -55.328 1.00 67.61  ? 963  GLU   A N     1 
ATOM   5326 C  CA    . GLU   A 1 814  ? 4.000   12.211  -55.780 1.00 70.61  ? 963  GLU   A CA    1 
ATOM   5327 C  C     . GLU   A 1 814  ? 3.597   12.453  -57.241 1.00 68.81  ? 963  GLU   A C     1 
ATOM   5328 O  O     . GLU   A 1 814  ? 3.142   13.570  -57.547 1.00 68.45  ? 963  GLU   A O     1 
ATOM   5329 C  CB    . GLU   A 1 814  ? 5.521   12.294  -55.628 1.00 75.96  ? 963  GLU   A CB    1 
ATOM   5330 C  CG    . GLU   A 1 814  ? 6.099   13.656  -55.978 1.00 79.77  ? 963  GLU   A CG    1 
ATOM   5331 C  CD    . GLU   A 1 814  ? 7.618   13.730  -55.990 1.00 83.10  ? 963  GLU   A CD    1 
ATOM   5332 O  OE1   . GLU   A 1 814  ? 8.269   12.686  -55.768 1.00 83.83  ? 963  GLU   A OE1   1 
ATOM   5333 O  OE2   . GLU   A 1 814  ? 8.148   14.836  -56.225 1.00 85.59  ? 963  GLU   A OE2   1 
ATOM   5334 N  N     . ILE   A 1 815  ? 3.773   11.449  -58.106 1.00 67.09  ? 964  ILE   A N     1 
ATOM   5335 C  CA    . ILE   A 1 815  ? 3.519   11.544  -59.575 1.00 65.97  ? 964  ILE   A CA    1 
ATOM   5336 C  C     . ILE   A 1 815  ? 2.018   11.767  -59.818 1.00 66.11  ? 964  ILE   A C     1 
ATOM   5337 O  O     . ILE   A 1 815  ? 1.681   12.490  -60.779 1.00 65.61  ? 964  ILE   A O     1 
ATOM   5338 C  CB    . ILE   A 1 815  ? 4.069   10.302  -60.307 1.00 65.52  ? 964  ILE   A CB    1 
ATOM   5339 C  CG1   . ILE   A 1 815  ? 5.599   10.262  -60.255 1.00 65.62  ? 964  ILE   A CG1   1 
ATOM   5340 C  CG2   . ILE   A 1 815  ? 3.558   10.236  -61.740 1.00 66.36  ? 964  ILE   A CG2   1 
ATOM   5341 C  CD1   . ILE   A 1 815  ? 6.198   8.914   -60.585 1.00 66.64  ? 964  ILE   A CD1   1 
ATOM   5342 N  N     . LEU   A 1 816  ? 1.153   11.184  -58.981 1.00 65.23  ? 965  LEU   A N     1 
ATOM   5343 C  CA    . LEU   A 1 816  ? -0.323  11.380  -59.039 1.00 64.64  ? 965  LEU   A CA    1 
ATOM   5344 C  C     . LEU   A 1 816  ? -0.662  12.813  -58.609 1.00 66.11  ? 965  LEU   A C     1 
ATOM   5345 O  O     . LEU   A 1 816  ? -1.480  13.450  -59.296 1.00 69.98  ? 965  LEU   A O     1 
ATOM   5346 C  CB    . LEU   A 1 816  ? -1.019  10.352  -58.141 1.00 62.91  ? 965  LEU   A CB    1 
ATOM   5347 C  CG    . LEU   A 1 816  ? -0.864  8.892   -58.562 1.00 62.53  ? 965  LEU   A CG    1 
ATOM   5348 C  CD1   . LEU   A 1 816  ? -1.394  7.959   -57.485 1.00 62.28  ? 965  LEU   A CD1   1 
ATOM   5349 C  CD2   . LEU   A 1 816  ? -1.562  8.629   -59.887 1.00 63.04  ? 965  LEU   A CD2   1 
ATOM   5350 N  N     . ILE   A 1 817  ? -0.047  13.300  -57.525 1.00 65.25  ? 966  ILE   A N     1 
ATOM   5351 C  CA    . ILE   A 1 817  ? -0.242  14.683  -56.991 1.00 64.60  ? 966  ILE   A CA    1 
ATOM   5352 C  C     . ILE   A 1 817  ? 0.080   15.685  -58.106 1.00 65.55  ? 966  ILE   A C     1 
ATOM   5353 O  O     . ILE   A 1 817  ? -0.782  16.539  -58.392 1.00 65.42  ? 966  ILE   A O     1 
ATOM   5354 C  CB    . ILE   A 1 817  ? 0.618   14.927  -55.732 1.00 64.10  ? 966  ILE   A CB    1 
ATOM   5355 C  CG1   . ILE   A 1 817  ? 0.188   14.045  -54.555 1.00 64.14  ? 966  ILE   A CG1   1 
ATOM   5356 C  CG2   . ILE   A 1 817  ? 0.625   16.402  -55.353 1.00 64.14  ? 966  ILE   A CG2   1 
ATOM   5357 C  CD1   . ILE   A 1 817  ? -1.204  14.323  -54.032 1.00 64.65  ? 966  ILE   A CD1   1 
ATOM   5358 N  N     . ASN   A 1 818  ? 1.265   15.559  -58.715 1.00 67.01  ? 967  ASN   A N     1 
ATOM   5359 C  CA    . ASN   A 1 818  ? 1.780   16.454  -59.790 1.00 68.43  ? 967  ASN   A CA    1 
ATOM   5360 C  C     . ASN   A 1 818  ? 0.901   16.340  -61.043 1.00 69.48  ? 967  ASN   A C     1 
ATOM   5361 O  O     . ASN   A 1 818  ? 0.838   17.326  -61.802 1.00 70.48  ? 967  ASN   A O     1 
ATOM   5362 C  CB    . ASN   A 1 818  ? 3.241   16.150  -60.136 1.00 69.09  ? 967  ASN   A CB    1 
ATOM   5363 C  CG    . ASN   A 1 818  ? 4.206   16.475  -59.015 1.00 71.68  ? 967  ASN   A CG    1 
ATOM   5364 O  OD1   . ASN   A 1 818  ? 3.812   16.995  -57.972 1.00 72.69  ? 967  ASN   A OD1   1 
ATOM   5365 N  ND2   . ASN   A 1 818  ? 5.478   16.173  -59.219 1.00 74.02  ? 967  ASN   A ND2   1 
ATOM   5366 N  N     . SER   A 1 819  ? 0.265   15.184  -61.260 1.00 70.10  ? 968  SER   A N     1 
ATOM   5367 C  CA    . SER   A 1 819  ? -0.662  14.925  -62.395 1.00 69.03  ? 968  SER   A CA    1 
ATOM   5368 C  C     . SER   A 1 819  ? -2.019  15.591  -62.136 1.00 69.20  ? 968  SER   A C     1 
ATOM   5369 O  O     . SER   A 1 819  ? -2.821  15.666  -63.088 1.00 70.89  ? 968  SER   A O     1 
ATOM   5370 C  CB    . SER   A 1 819  ? -0.804  13.450  -62.666 1.00 69.98  ? 968  SER   A CB    1 
ATOM   5371 O  OG    . SER   A 1 819  ? 0.334   12.959  -63.360 1.00 71.44  ? 968  SER   A OG    1 
ATOM   5372 N  N     . GLY   A 1 820  ? -2.262  16.056  -60.903 1.00 68.06  ? 969  GLY   A N     1 
ATOM   5373 C  CA    . GLY   A 1 820  ? -3.398  16.931  -60.551 1.00 67.13  ? 969  GLY   A CA    1 
ATOM   5374 C  C     . GLY   A 1 820  ? -4.314  16.331  -59.497 1.00 66.14  ? 969  GLY   A C     1 
ATOM   5375 O  O     . GLY   A 1 820  ? -5.252  17.037  -59.081 1.00 67.72  ? 969  GLY   A O     1 
ATOM   5376 N  N     . PHE   A 1 821  ? -4.075  15.083  -59.080 1.00 66.00  ? 970  PHE   A N     1 
ATOM   5377 C  CA    . PHE   A 1 821  ? -4.930  14.343  -58.112 1.00 66.49  ? 970  PHE   A CA    1 
ATOM   5378 C  C     . PHE   A 1 821  ? -4.827  15.006  -56.740 1.00 66.79  ? 970  PHE   A C     1 
ATOM   5379 O  O     . PHE   A 1 821  ? -3.759  15.478  -56.356 1.00 66.36  ? 970  PHE   A O     1 
ATOM   5380 C  CB    . PHE   A 1 821  ? -4.556  12.858  -58.070 1.00 66.03  ? 970  PHE   A CB    1 
ATOM   5381 C  CG    . PHE   A 1 821  ? -5.078  12.055  -59.236 1.00 65.74  ? 970  PHE   A CG    1 
ATOM   5382 C  CD1   . PHE   A 1 821  ? -6.353  11.509  -59.203 1.00 65.89  ? 970  PHE   A CD1   1 
ATOM   5383 C  CD2   . PHE   A 1 821  ? -4.306  11.858  -60.370 1.00 65.75  ? 970  PHE   A CD2   1 
ATOM   5384 C  CE1   . PHE   A 1 821  ? -6.841  10.781  -60.278 1.00 66.89  ? 970  PHE   A CE1   1 
ATOM   5385 C  CE2   . PHE   A 1 821  ? -4.794  11.127  -61.443 1.00 66.31  ? 970  PHE   A CE2   1 
ATOM   5386 C  CZ    . PHE   A 1 821  ? -6.060  10.590  -61.396 1.00 66.84  ? 970  PHE   A CZ    1 
ATOM   5387 N  N     . PRO   A 1 822  ? -5.938  15.075  -55.969 1.00 67.73  ? 971  PRO   A N     1 
ATOM   5388 C  CA    . PRO   A 1 822  ? -5.935  15.740  -54.666 1.00 70.30  ? 971  PRO   A CA    1 
ATOM   5389 C  C     . PRO   A 1 822  ? -5.125  14.990  -53.597 1.00 73.74  ? 971  PRO   A C     1 
ATOM   5390 O  O     . PRO   A 1 822  ? -4.999  13.783  -53.691 1.00 75.61  ? 971  PRO   A O     1 
ATOM   5391 C  CB    . PRO   A 1 822  ? -7.422  15.802  -54.283 1.00 68.88  ? 971  PRO   A CB    1 
ATOM   5392 C  CG    . PRO   A 1 822  ? -8.050  14.648  -55.031 1.00 68.26  ? 971  PRO   A CG    1 
ATOM   5393 C  CD    . PRO   A 1 822  ? -7.260  14.533  -56.318 1.00 67.87  ? 971  PRO   A CD    1 
ATOM   5394 N  N     . GLU   A 1 823  ? -4.611  15.736  -52.614 1.00 78.06  ? 972  GLU   A N     1 
ATOM   5395 C  CA    . GLU   A 1 823  ? -3.757  15.239  -51.500 1.00 78.47  ? 972  GLU   A CA    1 
ATOM   5396 C  C     . GLU   A 1 823  ? -4.549  14.248  -50.640 1.00 77.73  ? 972  GLU   A C     1 
ATOM   5397 O  O     . GLU   A 1 823  ? -3.964  13.232  -50.217 1.00 77.12  ? 972  GLU   A O     1 
ATOM   5398 C  CB    . GLU   A 1 823  ? -3.288  16.407  -50.628 1.00 81.13  ? 972  GLU   A CB    1 
ATOM   5399 C  CG    . GLU   A 1 823  ? -2.374  17.392  -51.343 1.00 83.35  ? 972  GLU   A CG    1 
ATOM   5400 C  CD    . GLU   A 1 823  ? -0.893  17.047  -51.321 1.00 84.68  ? 972  GLU   A CD    1 
ATOM   5401 O  OE1   . GLU   A 1 823  ? -0.140  17.641  -52.121 1.00 84.92  ? 972  GLU   A OE1   1 
ATOM   5402 O  OE2   . GLU   A 1 823  ? -0.494  16.196  -50.500 1.00 85.95  ? 972  GLU   A OE2   1 
ATOM   5403 N  N     . ASP   A 1 824  ? -5.834  14.538  -50.410 1.00 78.21  ? 973  ASP   A N     1 
ATOM   5404 C  CA    . ASP   A 1 824  ? -6.682  13.886  -49.374 1.00 77.69  ? 973  ASP   A CA    1 
ATOM   5405 C  C     . ASP   A 1 824  ? -7.360  12.627  -49.936 1.00 74.35  ? 973  ASP   A C     1 
ATOM   5406 O  O     . ASP   A 1 824  ? -8.195  12.053  -49.215 1.00 74.97  ? 973  ASP   A O     1 
ATOM   5407 C  CB    . ASP   A 1 824  ? -7.701  14.875  -48.793 1.00 79.79  ? 973  ASP   A CB    1 
ATOM   5408 C  CG    . ASP   A 1 824  ? -8.537  15.605  -49.831 1.00 82.07  ? 973  ASP   A CG    1 
ATOM   5409 O  OD1   . ASP   A 1 824  ? -7.976  15.975  -50.883 1.00 82.89  ? 973  ASP   A OD1   1 
ATOM   5410 O  OD2   . ASP   A 1 824  ? -9.742  15.805  -49.577 1.00 83.66  ? 973  ASP   A OD2   1 
ATOM   5411 N  N     . CYS   A 1 825  ? -7.013  12.204  -51.159 1.00 71.92  ? 974  CYS   A N     1 
ATOM   5412 C  CA    . CYS   A 1 825  ? -7.461  10.921  -51.770 1.00 70.25  ? 974  CYS   A CA    1 
ATOM   5413 C  C     . CYS   A 1 825  ? -6.298  9.921   -51.810 1.00 68.75  ? 974  CYS   A C     1 
ATOM   5414 O  O     . CYS   A 1 825  ? -6.454  8.868   -52.458 1.00 69.22  ? 974  CYS   A O     1 
ATOM   5415 C  CB    . CYS   A 1 825  ? -8.022  11.134  -53.173 1.00 70.07  ? 974  CYS   A CB    1 
ATOM   5416 S  SG    . CYS   A 1 825  ? -6.768  11.124  -54.483 1.00 68.98  ? 974  CYS   A SG    1 
ATOM   5417 N  N     . LEU   A 1 826  ? -5.183  10.240  -51.143 1.00 67.95  ? 975  LEU   A N     1 
ATOM   5418 C  CA    . LEU   A 1 826  ? -3.967  9.386   -51.067 1.00 66.84  ? 975  LEU   A CA    1 
ATOM   5419 C  C     . LEU   A 1 826  ? -3.451  9.320   -49.621 1.00 66.27  ? 975  LEU   A C     1 
ATOM   5420 O  O     . LEU   A 1 826  ? -2.256  9.025   -49.444 1.00 69.56  ? 975  LEU   A O     1 
ATOM   5421 C  CB    . LEU   A 1 826  ? -2.909  9.967   -52.011 1.00 65.46  ? 975  LEU   A CB    1 
ATOM   5422 C  CG    . LEU   A 1 826  ? -3.204  9.815   -53.503 1.00 64.44  ? 975  LEU   A CG    1 
ATOM   5423 C  CD1   . LEU   A 1 826  ? -2.610  10.966  -54.299 1.00 63.62  ? 975  LEU   A CD1   1 
ATOM   5424 C  CD2   . LEU   A 1 826  ? -2.689  8.482   -54.025 1.00 64.23  ? 975  LEU   A CD2   1 
ATOM   5425 N  N     . LEU   A 1 827  ? -4.317  9.555   -48.628 1.00 65.35  ? 976  LEU   A N     1 
ATOM   5426 C  CA    . LEU   A 1 827  ? -3.960  9.521   -47.182 1.00 66.60  ? 976  LEU   A CA    1 
ATOM   5427 C  C     . LEU   A 1 827  ? -3.843  8.065   -46.720 1.00 67.48  ? 976  LEU   A C     1 
ATOM   5428 O  O     . LEU   A 1 827  ? -4.590  7.219   -47.247 1.00 68.33  ? 976  LEU   A O     1 
ATOM   5429 C  CB    . LEU   A 1 827  ? -5.031  10.246  -46.360 1.00 66.56  ? 976  LEU   A CB    1 
ATOM   5430 C  CG    . LEU   A 1 827  ? -5.246  11.721  -46.687 1.00 65.72  ? 976  LEU   A CG    1 
ATOM   5431 C  CD1   . LEU   A 1 827  ? -6.448  12.263  -45.928 1.00 65.78  ? 976  LEU   A CD1   1 
ATOM   5432 C  CD2   . LEU   A 1 827  ? -3.999  12.537  -46.380 1.00 64.68  ? 976  LEU   A CD2   1 
ATOM   5433 N  N     . THR   A 1 828  ? -2.960  7.803   -45.751 1.00 68.59  ? 977  THR   A N     1 
ATOM   5434 C  CA    . THR   A 1 828  ? -2.773  6.473   -45.110 1.00 69.87  ? 977  THR   A CA    1 
ATOM   5435 C  C     . THR   A 1 828  ? -3.951  6.226   -44.161 1.00 71.50  ? 977  THR   A C     1 
ATOM   5436 O  O     . THR   A 1 828  ? -3.865  6.639   -42.989 1.00 74.68  ? 977  THR   A O     1 
ATOM   5437 C  CB    . THR   A 1 828  ? -1.425  6.365   -44.381 1.00 69.87  ? 977  THR   A CB    1 
ATOM   5438 O  OG1   . THR   A 1 828  ? -1.439  7.232   -43.247 1.00 70.73  ? 977  THR   A OG1   1 
ATOM   5439 C  CG2   . THR   A 1 828  ? -0.239  6.711   -45.254 1.00 71.34  ? 977  THR   A CG2   1 
ATOM   5440 N  N     . GLN   A 1 829  ? -5.013  5.591   -44.662 1.00 71.41  ? 978  GLN   A N     1 
ATOM   5441 C  CA    . GLN   A 1 829  ? -6.244  5.273   -43.893 1.00 70.75  ? 978  GLN   A CA    1 
ATOM   5442 C  C     . GLN   A 1 829  ? -6.034  3.958   -43.137 1.00 68.67  ? 978  GLN   A C     1 
ATOM   5443 O  O     . GLN   A 1 829  ? -5.718  2.948   -43.788 1.00 68.09  ? 978  GLN   A O     1 
ATOM   5444 C  CB    . GLN   A 1 829  ? -7.443  5.194   -44.837 1.00 72.07  ? 978  GLN   A CB    1 
ATOM   5445 C  CG    . GLN   A 1 829  ? -7.727  6.509   -45.549 1.00 74.35  ? 978  GLN   A CG    1 
ATOM   5446 C  CD    . GLN   A 1 829  ? -8.759  6.369   -46.640 1.00 76.45  ? 978  GLN   A CD    1 
ATOM   5447 O  OE1   . GLN   A 1 829  ? -9.001  5.281   -47.160 1.00 78.65  ? 978  GLN   A OE1   1 
ATOM   5448 N  NE2   . GLN   A 1 829  ? -9.376  7.483   -47.000 1.00 77.07  ? 978  GLN   A NE2   1 
ATOM   5449 N  N     . VAL   A 1 830  ? -6.186  3.983   -41.810 1.00 68.94  ? 979  VAL   A N     1 
ATOM   5450 C  CA    . VAL   A 1 830  ? -6.118  2.771   -40.941 1.00 68.99  ? 979  VAL   A CA    1 
ATOM   5451 C  C     . VAL   A 1 830  ? -7.287  1.858   -41.325 1.00 66.43  ? 979  VAL   A C     1 
ATOM   5452 O  O     . VAL   A 1 830  ? -8.340  2.388   -41.730 1.00 64.85  ? 979  VAL   A O     1 
ATOM   5453 C  CB    . VAL   A 1 830  ? -6.142  3.135   -39.443 1.00 70.75  ? 979  VAL   A CB    1 
ATOM   5454 C  CG1   . VAL   A 1 830  ? -7.508  3.638   -38.995 1.00 71.25  ? 979  VAL   A CG1   1 
ATOM   5455 C  CG2   . VAL   A 1 830  ? -5.690  1.968   -38.578 1.00 71.75  ? 979  VAL   A CG2   1 
ATOM   5456 N  N     . PHE   A 1 831  ? -7.099  0.542   -41.217 1.00 64.47  ? 980  PHE   A N     1 
ATOM   5457 C  CA    . PHE   A 1 831  ? -8.099  -0.478  -41.621 1.00 64.79  ? 980  PHE   A CA    1 
ATOM   5458 C  C     . PHE   A 1 831  ? -8.005  -1.695  -40.699 1.00 63.56  ? 980  PHE   A C     1 
ATOM   5459 O  O     . PHE   A 1 831  ? -6.968  -1.876  -40.038 1.00 64.55  ? 980  PHE   A O     1 
ATOM   5460 C  CB    . PHE   A 1 831  ? -7.889  -0.885  -43.081 1.00 67.16  ? 980  PHE   A CB    1 
ATOM   5461 C  CG    . PHE   A 1 831  ? -6.663  -1.726  -43.329 1.00 68.48  ? 980  PHE   A CG    1 
ATOM   5462 C  CD1   . PHE   A 1 831  ? -5.441  -1.135  -43.612 1.00 68.72  ? 980  PHE   A CD1   1 
ATOM   5463 C  CD2   . PHE   A 1 831  ? -6.730  -3.111  -43.280 1.00 70.22  ? 980  PHE   A CD2   1 
ATOM   5464 C  CE1   . PHE   A 1 831  ? -4.314  -1.910  -43.838 1.00 69.15  ? 980  PHE   A CE1   1 
ATOM   5465 C  CE2   . PHE   A 1 831  ? -5.602  -3.884  -43.507 1.00 70.92  ? 980  PHE   A CE2   1 
ATOM   5466 C  CZ    . PHE   A 1 831  ? -4.396  -3.283  -43.785 1.00 70.25  ? 980  PHE   A CZ    1 
ATOM   5467 N  N     . THR   A 1 832  ? -9.072  -2.496  -40.681 1.00 63.73  ? 981  THR   A N     1 
ATOM   5468 C  CA    . THR   A 1 832  ? -9.167  -3.799  -39.971 1.00 65.38  ? 981  THR   A CA    1 
ATOM   5469 C  C     . THR   A 1 832  ? -9.216  -4.906  -41.031 1.00 64.58  ? 981  THR   A C     1 
ATOM   5470 O  O     . THR   A 1 832  ? -9.874  -4.695  -42.067 1.00 65.83  ? 981  THR   A O     1 
ATOM   5471 C  CB    . THR   A 1 832  ? -10.360 -3.820  -39.003 1.00 68.03  ? 981  THR   A CB    1 
ATOM   5472 O  OG1   . THR   A 1 832  ? -10.336 -5.061  -38.295 1.00 70.78  ? 981  THR   A OG1   1 
ATOM   5473 C  CG2   . THR   A 1 832  ? -11.705 -3.652  -39.680 1.00 68.42  ? 981  THR   A CG2   1 
ATOM   5474 N  N     . ASN   A 1 833  ? -8.530  -6.026  -40.785 1.00 63.88  ? 982  ASN   A N     1 
ATOM   5475 C  CA    . ASN   A 1 833  ? -8.442  -7.177  -41.725 1.00 62.98  ? 982  ASN   A CA    1 
ATOM   5476 C  C     . ASN   A 1 833  ? -9.326  -8.328  -41.224 1.00 63.58  ? 982  ASN   A C     1 
ATOM   5477 O  O     . ASN   A 1 833  ? -9.266  -9.413  -41.834 1.00 64.47  ? 982  ASN   A O     1 
ATOM   5478 C  CB    . ASN   A 1 833  ? -6.991  -7.618  -41.943 1.00 61.72  ? 982  ASN   A CB    1 
ATOM   5479 C  CG    . ASN   A 1 833  ? -6.304  -8.104  -40.684 1.00 60.14  ? 982  ASN   A CG    1 
ATOM   5480 O  OD1   . ASN   A 1 833  ? -6.952  -8.383  -39.678 1.00 59.04  ? 982  ASN   A OD1   1 
ATOM   5481 N  ND2   . ASN   A 1 833  ? -4.986  -8.207  -40.732 1.00 59.39  ? 982  ASN   A ND2   1 
ATOM   5482 N  N     . THR   A 1 834  ? -10.116 -8.097  -40.168 1.00 63.59  ? 983  THR   A N     1 
ATOM   5483 C  CA    . THR   A 1 834  ? -11.048 -9.091  -39.564 1.00 63.87  ? 983  THR   A CA    1 
ATOM   5484 C  C     . THR   A 1 834  ? -12.486 -8.561  -39.625 1.00 65.00  ? 983  THR   A C     1 
ATOM   5485 O  O     . THR   A 1 834  ? -13.350 -9.274  -40.175 1.00 64.09  ? 983  THR   A O     1 
ATOM   5486 C  CB    . THR   A 1 834  ? -10.639 -9.436  -38.127 1.00 63.02  ? 983  THR   A CB    1 
ATOM   5487 O  OG1   . THR   A 1 834  ? -10.287 -8.224  -37.458 1.00 63.41  ? 983  THR   A OG1   1 
ATOM   5488 C  CG2   . THR   A 1 834  ? -9.483  -10.411 -38.065 1.00 62.92  ? 983  THR   A CG2   1 
ATOM   5489 N  N     . GLY   A 1 835  ? -12.727 -7.365  -39.074 1.00 65.65  ? 984  GLY   A N     1 
ATOM   5490 C  CA    . GLY   A 1 835  ? -14.062 -6.740  -38.993 1.00 66.46  ? 984  GLY   A CA    1 
ATOM   5491 C  C     . GLY   A 1 835  ? -14.486 -6.120  -40.323 1.00 67.06  ? 984  GLY   A C     1 
ATOM   5492 O  O     . GLY   A 1 835  ? -13.703 -6.082  -41.269 1.00 69.05  ? 984  GLY   A O     1 
ATOM   5493 N  N     . PRO   A 1 836  ? -15.740 -5.624  -40.440 1.00 68.43  ? 985  PRO   A N     1 
ATOM   5494 C  CA    . PRO   A 1 836  ? -16.193 -4.950  -41.658 1.00 69.11  ? 985  PRO   A CA    1 
ATOM   5495 C  C     . PRO   A 1 836  ? -15.362 -3.695  -41.973 1.00 69.47  ? 985  PRO   A C     1 
ATOM   5496 O  O     . PRO   A 1 836  ? -15.209 -2.859  -41.097 1.00 69.18  ? 985  PRO   A O     1 
ATOM   5497 C  CB    . PRO   A 1 836  ? -17.652 -4.566  -41.358 1.00 68.85  ? 985  PRO   A CB    1 
ATOM   5498 C  CG    . PRO   A 1 836  ? -18.063 -5.485  -40.225 1.00 68.80  ? 985  PRO   A CG    1 
ATOM   5499 C  CD    . PRO   A 1 836  ? -16.798 -5.709  -39.422 1.00 68.65  ? 985  PRO   A CD    1 
ATOM   5500 N  N     . ASP   A 1 837  ? -14.849 -3.605  -43.205 1.00 69.40  ? 986  ASP   A N     1 
ATOM   5501 C  CA    . ASP   A 1 837  ? -14.031 -2.467  -43.706 1.00 69.36  ? 986  ASP   A CA    1 
ATOM   5502 C  C     . ASP   A 1 837  ? -14.297 -2.294  -45.206 1.00 68.29  ? 986  ASP   A C     1 
ATOM   5503 O  O     . ASP   A 1 837  ? -13.810 -3.128  -45.990 1.00 68.89  ? 986  ASP   A O     1 
ATOM   5504 C  CB    . ASP   A 1 837  ? -12.546 -2.687  -43.405 1.00 69.77  ? 986  ASP   A CB    1 
ATOM   5505 C  CG    . ASP   A 1 837  ? -11.722 -1.413  -43.446 1.00 69.98  ? 986  ASP   A CG    1 
ATOM   5506 O  OD1   . ASP   A 1 837  ? -11.673 -0.776  -44.518 1.00 70.72  ? 986  ASP   A OD1   1 
ATOM   5507 O  OD2   . ASP   A 1 837  ? -11.149 -1.060  -42.399 1.00 70.76  ? 986  ASP   A OD2   1 
ATOM   5508 N  N     . ASN   A 1 838  ? -15.045 -1.250  -45.580 1.00 67.16  ? 987  ASN   A N     1 
ATOM   5509 C  CA    . ASN   A 1 838  ? -15.513 -1.011  -46.972 1.00 66.31  ? 987  ASN   A CA    1 
ATOM   5510 C  C     . ASN   A 1 838  ? -14.359 -0.470  -47.825 1.00 64.41  ? 987  ASN   A C     1 
ATOM   5511 O  O     . ASN   A 1 838  ? -14.398 -0.668  -49.053 1.00 64.73  ? 987  ASN   A O     1 
ATOM   5512 C  CB    . ASN   A 1 838  ? -16.722 -0.071  -47.015 1.00 67.51  ? 987  ASN   A CB    1 
ATOM   5513 C  CG    . ASN   A 1 838  ? -17.347 0.027   -48.391 1.00 67.70  ? 987  ASN   A CG    1 
ATOM   5514 O  OD1   . ASN   A 1 838  ? -17.597 1.124   -48.887 1.00 70.66  ? 987  ASN   A OD1   1 
ATOM   5515 N  ND2   . ASN   A 1 838  ? -17.595 -1.110  -49.021 1.00 65.68  ? 987  ASN   A ND2   1 
ATOM   5516 N  N     . ASN   A 1 839  ? -13.381 0.198   -47.208 1.00 62.63  ? 988  ASN   A N     1 
ATOM   5517 C  CA    . ASN   A 1 839  ? -12.183 0.730   -47.912 1.00 61.62  ? 988  ASN   A CA    1 
ATOM   5518 C  C     . ASN   A 1 839  ? -11.315 -0.444  -48.379 1.00 60.43  ? 988  ASN   A C     1 
ATOM   5519 O  O     . ASN   A 1 839  ? -10.781 -0.364  -49.501 1.00 61.11  ? 988  ASN   A O     1 
ATOM   5520 C  CB    . ASN   A 1 839  ? -11.404 1.728   -47.050 1.00 60.73  ? 988  ASN   A CB    1 
ATOM   5521 C  CG    . ASN   A 1 839  ? -12.036 3.104   -47.026 1.00 59.65  ? 988  ASN   A CG    1 
ATOM   5522 O  OD1   . ASN   A 1 839  ? -12.782 3.469   -47.932 1.00 59.33  ? 988  ASN   A OD1   1 
ATOM   5523 N  ND2   . ASN   A 1 839  ? -11.738 3.881   -45.998 1.00 59.90  ? 988  ASN   A ND2   1 
ATOM   5524 N  N     . LEU   A 1 840  ? -11.199 -1.497  -47.565 1.00 59.32  ? 989  LEU   A N     1 
ATOM   5525 C  CA    . LEU   A 1 840  ? -10.447 -2.734  -47.914 1.00 59.82  ? 989  LEU   A CA    1 
ATOM   5526 C  C     . LEU   A 1 840  ? -11.227 -3.526  -48.974 1.00 60.99  ? 989  LEU   A C     1 
ATOM   5527 O  O     . LEU   A 1 840  ? -10.578 -4.087  -49.878 1.00 61.38  ? 989  LEU   A O     1 
ATOM   5528 C  CB    . LEU   A 1 840  ? -10.213 -3.567  -46.649 1.00 58.31  ? 989  LEU   A CB    1 
ATOM   5529 C  CG    . LEU   A 1 840  ? -9.201  -4.703  -46.788 1.00 57.42  ? 989  LEU   A CG    1 
ATOM   5530 C  CD1   . LEU   A 1 840  ? -7.844  -4.181  -47.239 1.00 57.76  ? 989  LEU   A CD1   1 
ATOM   5531 C  CD2   . LEU   A 1 840  ? -9.064  -5.468  -45.482 1.00 57.84  ? 989  LEU   A CD2   1 
ATOM   5532 N  N     . ASP   A 1 841  ? -12.561 -3.562  -48.864 1.00 63.15  ? 990  ASP   A N     1 
ATOM   5533 C  CA    . ASP   A 1 841  ? -13.480 -4.207  -49.844 1.00 64.88  ? 990  ASP   A CA    1 
ATOM   5534 C  C     . ASP   A 1 841  ? -13.189 -3.661  -51.249 1.00 64.77  ? 990  ASP   A C     1 
ATOM   5535 O  O     . ASP   A 1 841  ? -13.063 -4.472  -52.189 1.00 65.86  ? 990  ASP   A O     1 
ATOM   5536 C  CB    . ASP   A 1 841  ? -14.953 -3.972  -49.485 1.00 67.37  ? 990  ASP   A CB    1 
ATOM   5537 C  CG    . ASP   A 1 841  ? -15.418 -4.600  -48.179 1.00 70.27  ? 990  ASP   A CG    1 
ATOM   5538 O  OD1   . ASP   A 1 841  ? -14.699 -5.469  -47.649 1.00 75.11  ? 990  ASP   A OD1   1 
ATOM   5539 O  OD2   . ASP   A 1 841  ? -16.505 -4.215  -47.700 1.00 70.35  ? 990  ASP   A OD2   1 
ATOM   5540 N  N     . VAL   A 1 842  ? -13.079 -2.335  -51.374 1.00 63.55  ? 991  VAL   A N     1 
ATOM   5541 C  CA    . VAL   A 1 842  ? -12.887 -1.608  -52.664 1.00 63.02  ? 991  VAL   A CA    1 
ATOM   5542 C  C     . VAL   A 1 842  ? -11.468 -1.858  -53.194 1.00 62.86  ? 991  VAL   A C     1 
ATOM   5543 O  O     . VAL   A 1 842  ? -11.318 -1.986  -54.426 1.00 64.07  ? 991  VAL   A O     1 
ATOM   5544 C  CB    . VAL   A 1 842  ? -13.182 -0.105  -52.497 1.00 63.32  ? 991  VAL   A CB    1 
ATOM   5545 C  CG1   . VAL   A 1 842  ? -12.766 0.705   -53.717 1.00 63.02  ? 991  VAL   A CG1   1 
ATOM   5546 C  CG2   . VAL   A 1 842  ? -14.647 0.136   -52.172 1.00 63.64  ? 991  VAL   A CG2   1 
ATOM   5547 N  N     . VAL   A 1 843  ? -10.465 -1.915  -52.311 1.00 61.16  ? 992  VAL   A N     1 
ATOM   5548 C  CA    . VAL   A 1 843  ? -9.046  -2.194  -52.688 1.00 59.53  ? 992  VAL   A CA    1 
ATOM   5549 C  C     . VAL   A 1 843  ? -8.981  -3.554  -53.396 1.00 58.44  ? 992  VAL   A C     1 
ATOM   5550 O  O     . VAL   A 1 843  ? -8.345  -3.628  -54.465 1.00 60.57  ? 992  VAL   A O     1 
ATOM   5551 C  CB    . VAL   A 1 843  ? -8.104  -2.134  -51.469 1.00 58.53  ? 992  VAL   A CB    1 
ATOM   5552 C  CG1   . VAL   A 1 843  ? -6.777  -2.833  -51.732 1.00 58.44  ? 992  VAL   A CG1   1 
ATOM   5553 C  CG2   . VAL   A 1 843  ? -7.869  -0.698  -51.025 1.00 58.19  ? 992  VAL   A CG2   1 
ATOM   5554 N  N     . ILE   A 1 844  ? -9.627  -4.578  -52.830 1.00 55.32  ? 993  ILE   A N     1 
ATOM   5555 C  CA    . ILE   A 1 844  ? -9.623  -5.976  -53.358 1.00 54.24  ? 993  ILE   A CA    1 
ATOM   5556 C  C     . ILE   A 1 844  ? -10.402 -6.027  -54.682 1.00 54.05  ? 993  ILE   A C     1 
ATOM   5557 O  O     . ILE   A 1 844  ? -10.021 -6.831  -55.556 1.00 52.94  ? 993  ILE   A O     1 
ATOM   5558 C  CB    . ILE   A 1 844  ? -10.170 -6.956  -52.301 1.00 53.66  ? 993  ILE   A CB    1 
ATOM   5559 C  CG1   . ILE   A 1 844  ? -9.237  -7.029  -51.089 1.00 53.58  ? 993  ILE   A CG1   1 
ATOM   5560 C  CG2   . ILE   A 1 844  ? -10.417 -8.333  -52.898 1.00 54.02  ? 993  ILE   A CG2   1 
ATOM   5561 C  CD1   . ILE   A 1 844  ? -9.907  -7.508  -49.826 1.00 54.06  ? 993  ILE   A CD1   1 
ATOM   5562 N  N     . SER   A 1 845  ? -11.447 -5.208  -54.835 1.00 54.12  ? 994  SER   A N     1 
ATOM   5563 C  CA    . SER   A 1 845  ? -12.172 -5.020  -56.122 1.00 53.37  ? 994  SER   A CA    1 
ATOM   5564 C  C     . SER   A 1 845  ? -11.199 -4.471  -57.172 1.00 52.30  ? 994  SER   A C     1 
ATOM   5565 O  O     . SER   A 1 845  ? -11.167 -5.012  -58.289 1.00 51.32  ? 994  SER   A O     1 
ATOM   5566 C  CB    . SER   A 1 845  ? -13.377 -4.124  -55.969 1.00 52.86  ? 994  SER   A CB    1 
ATOM   5567 O  OG    . SER   A 1 845  ? -14.465 -4.837  -55.404 1.00 53.66  ? 994  SER   A OG    1 
ATOM   5568 N  N     . LEU   A 1 846  ? -10.422 -3.448  -56.810 1.00 52.10  ? 995  LEU   A N     1 
ATOM   5569 C  CA    . LEU   A 1 846  ? -9.446  -2.787  -57.715 1.00 52.41  ? 995  LEU   A CA    1 
ATOM   5570 C  C     . LEU   A 1 846  ? -8.247  -3.713  -57.961 1.00 51.97  ? 995  LEU   A C     1 
ATOM   5571 O  O     . LEU   A 1 846  ? -7.675  -3.645  -59.060 1.00 52.16  ? 995  LEU   A O     1 
ATOM   5572 C  CB    . LEU   A 1 846  ? -9.015  -1.451  -57.102 1.00 52.02  ? 995  LEU   A CB    1 
ATOM   5573 C  CG    . LEU   A 1 846  ? -10.117 -0.399  -56.992 1.00 50.91  ? 995  LEU   A CG    1 
ATOM   5574 C  CD1   . LEU   A 1 846  ? -9.629  0.807   -56.211 1.00 50.56  ? 995  LEU   A CD1   1 
ATOM   5575 C  CD2   . LEU   A 1 846  ? -10.611 0.020   -58.368 1.00 50.88  ? 995  LEU   A CD2   1 
ATOM   5576 N  N     . LEU   A 1 847  ? -7.886  -4.552  -56.987 1.00 53.33  ? 996  LEU   A N     1 
ATOM   5577 C  CA    . LEU   A 1 847  ? -6.830  -5.591  -57.146 1.00 54.78  ? 996  LEU   A CA    1 
ATOM   5578 C  C     . LEU   A 1 847  ? -7.219  -6.529  -58.295 1.00 55.06  ? 996  LEU   A C     1 
ATOM   5579 O  O     . LEU   A 1 847  ? -6.368  -6.781  -59.171 1.00 56.17  ? 996  LEU   A O     1 
ATOM   5580 C  CB    . LEU   A 1 847  ? -6.668  -6.368  -55.837 1.00 54.86  ? 996  LEU   A CB    1 
ATOM   5581 C  CG    . LEU   A 1 847  ? -5.678  -7.530  -55.888 1.00 55.48  ? 996  LEU   A CG    1 
ATOM   5582 C  CD1   . LEU   A 1 847  ? -4.264  -7.029  -56.140 1.00 55.51  ? 996  LEU   A CD1   1 
ATOM   5583 C  CD2   . LEU   A 1 847  ? -5.739  -8.344  -54.607 1.00 56.86  ? 996  LEU   A CD2   1 
ATOM   5584 N  N     . ALA   A 1 848  ? -8.461  -7.020  -58.281 1.00 54.84  ? 997  ALA   A N     1 
ATOM   5585 C  CA    . ALA   A 1 848  ? -9.037  -7.922  -59.306 1.00 54.32  ? 997  ALA   A CA    1 
ATOM   5586 C  C     . ALA   A 1 848  ? -8.796  -7.341  -60.705 1.00 53.83  ? 997  ALA   A C     1 
ATOM   5587 O  O     . ALA   A 1 848  ? -8.410  -8.115  -61.606 1.00 54.57  ? 997  ALA   A O     1 
ATOM   5588 C  CB    . ALA   A 1 848  ? -10.507 -8.132  -59.039 1.00 54.54  ? 997  ALA   A CB    1 
ATOM   5589 N  N     . PHE   A 1 849  ? -9.012  -6.033  -60.874 1.00 53.17  ? 998  PHE   A N     1 
ATOM   5590 C  CA    . PHE   A 1 849  ? -8.778  -5.295  -62.143 1.00 53.89  ? 998  PHE   A CA    1 
ATOM   5591 C  C     . PHE   A 1 849  ? -7.293  -5.368  -62.513 1.00 54.81  ? 998  PHE   A C     1 
ATOM   5592 O  O     . PHE   A 1 849  ? -6.977  -5.745  -63.655 1.00 56.34  ? 998  PHE   A O     1 
ATOM   5593 C  CB    . PHE   A 1 849  ? -9.231  -3.836  -62.033 1.00 53.85  ? 998  PHE   A CB    1 
ATOM   5594 C  CG    . PHE   A 1 849  ? -8.890  -2.994  -63.236 1.00 55.14  ? 998  PHE   A CG    1 
ATOM   5595 C  CD1   . PHE   A 1 849  ? -7.643  -2.399  -63.357 1.00 55.59  ? 998  PHE   A CD1   1 
ATOM   5596 C  CD2   . PHE   A 1 849  ? -9.810  -2.810  -64.258 1.00 55.58  ? 998  PHE   A CD2   1 
ATOM   5597 C  CE1   . PHE   A 1 849  ? -7.326  -1.635  -64.469 1.00 55.71  ? 998  PHE   A CE1   1 
ATOM   5598 C  CE2   . PHE   A 1 849  ? -9.492  -2.044  -65.369 1.00 56.10  ? 998  PHE   A CE2   1 
ATOM   5599 C  CZ    . PHE   A 1 849  ? -8.252  -1.457  -65.472 1.00 56.56  ? 998  PHE   A CZ    1 
ATOM   5600 N  N     . GLY   A 1 850  ? -6.417  -5.012  -61.569 1.00 55.67  ? 999  GLY   A N     1 
ATOM   5601 C  CA    . GLY   A 1 850  ? -4.963  -4.863  -61.782 1.00 56.67  ? 999  GLY   A CA    1 
ATOM   5602 C  C     . GLY   A 1 850  ? -4.300  -6.148  -62.249 1.00 57.39  ? 999  GLY   A C     1 
ATOM   5603 O  O     . GLY   A 1 850  ? -3.469  -6.073  -63.176 1.00 58.71  ? 999  GLY   A O     1 
ATOM   5604 N  N     . VAL   A 1 851  ? -4.646  -7.285  -61.638 1.00 57.83  ? 1000 VAL   A N     1 
ATOM   5605 C  CA    . VAL   A 1 851  ? -3.955  -8.592  -61.854 1.00 59.33  ? 1000 VAL   A CA    1 
ATOM   5606 C  C     . VAL   A 1 851  ? -4.633  -9.380  -62.983 1.00 62.23  ? 1000 VAL   A C     1 
ATOM   5607 O  O     . VAL   A 1 851  ? -4.046  -10.394 -63.404 1.00 62.83  ? 1000 VAL   A O     1 
ATOM   5608 C  CB    . VAL   A 1 851  ? -3.881  -9.423  -60.559 1.00 58.89  ? 1000 VAL   A CB    1 
ATOM   5609 C  CG1   . VAL   A 1 851  ? -3.198  -8.658  -59.436 1.00 59.41  ? 1000 VAL   A CG1   1 
ATOM   5610 C  CG2   . VAL   A 1 851  ? -5.245  -9.928  -60.112 1.00 58.94  ? 1000 VAL   A CG2   1 
ATOM   5611 N  N     . TYR   A 1 852  ? -5.807  -8.947  -63.460 1.00 65.90  ? 1001 TYR   A N     1 
ATOM   5612 C  CA    . TYR   A 1 852  ? -6.518  -9.574  -64.609 1.00 68.62  ? 1001 TYR   A CA    1 
ATOM   5613 C  C     . TYR   A 1 852  ? -5.555  -9.675  -65.791 1.00 68.76  ? 1001 TYR   A C     1 
ATOM   5614 O  O     . TYR   A 1 852  ? -4.811  -8.731  -66.055 1.00 67.23  ? 1001 TYR   A O     1 
ATOM   5615 C  CB    . TYR   A 1 852  ? -7.771  -8.781  -64.994 1.00 71.71  ? 1001 TYR   A CB    1 
ATOM   5616 C  CG    . TYR   A 1 852  ? -8.578  -9.423  -66.094 1.00 74.36  ? 1001 TYR   A CG    1 
ATOM   5617 C  CD1   . TYR   A 1 852  ? -9.472  -10.446 -65.817 1.00 76.57  ? 1001 TYR   A CD1   1 
ATOM   5618 C  CD2   . TYR   A 1 852  ? -8.413  -9.047  -67.418 1.00 75.56  ? 1001 TYR   A CD2   1 
ATOM   5619 C  CE1   . TYR   A 1 852  ? -10.197 -11.066 -66.823 1.00 77.75  ? 1001 TYR   A CE1   1 
ATOM   5620 C  CE2   . TYR   A 1 852  ? -9.132  -9.654  -68.436 1.00 77.57  ? 1001 TYR   A CE2   1 
ATOM   5621 C  CZ    . TYR   A 1 852  ? -10.027 -10.668 -68.137 1.00 78.22  ? 1001 TYR   A CZ    1 
ATOM   5622 O  OH    . TYR   A 1 852  ? -10.742 -11.270 -69.132 1.00 79.33  ? 1001 TYR   A OH    1 
ATOM   5623 N  N     . PRO   A 1 853  ? -5.539  -10.787 -66.566 1.00 69.44  ? 1002 PRO   A N     1 
ATOM   5624 C  CA    . PRO   A 1 853  ? -6.509  -11.880 -66.446 1.00 69.16  ? 1002 PRO   A CA    1 
ATOM   5625 C  C     . PRO   A 1 853  ? -6.128  -13.066 -65.541 1.00 69.00  ? 1002 PRO   A C     1 
ATOM   5626 O  O     . PRO   A 1 853  ? -6.504  -14.182 -65.861 1.00 68.90  ? 1002 PRO   A O     1 
ATOM   5627 C  CB    . PRO   A 1 853  ? -6.579  -12.325 -67.915 1.00 69.61  ? 1002 PRO   A CB    1 
ATOM   5628 C  CG    . PRO   A 1 853  ? -5.144  -12.230 -68.385 1.00 69.25  ? 1002 PRO   A CG    1 
ATOM   5629 C  CD    . PRO   A 1 853  ? -4.587  -11.019 -67.665 1.00 69.30  ? 1002 PRO   A CD    1 
ATOM   5630 N  N     . ASN   A 1 854  ? -5.423  -12.813 -64.433 1.00 68.68  ? 1003 ASN   A N     1 
ATOM   5631 C  CA    . ASN   A 1 854  ? -5.083  -13.851 -63.421 1.00 67.64  ? 1003 ASN   A CA    1 
ATOM   5632 C  C     . ASN   A 1 854  ? -6.252  -14.005 -62.443 1.00 67.48  ? 1003 ASN   A C     1 
ATOM   5633 O  O     . ASN   A 1 854  ? -6.233  -13.351 -61.383 1.00 68.10  ? 1003 ASN   A O     1 
ATOM   5634 C  CB    . ASN   A 1 854  ? -3.777  -13.547 -62.684 1.00 66.22  ? 1003 ASN   A CB    1 
ATOM   5635 C  CG    . ASN   A 1 854  ? -2.554  -13.797 -63.538 1.00 66.69  ? 1003 ASN   A CG    1 
ATOM   5636 O  OD1   . ASN   A 1 854  ? -2.669  -14.203 -64.692 1.00 66.75  ? 1003 ASN   A OD1   1 
ATOM   5637 N  ND2   . ASN   A 1 854  ? -1.379  -13.566 -62.977 1.00 68.40  ? 1003 ASN   A ND2   1 
ATOM   5638 N  N     . VAL   A 1 855  ? -7.231  -14.836 -62.809 1.00 66.98  ? 1004 VAL   A N     1 
ATOM   5639 C  CA    . VAL   A 1 855  ? -8.303  -15.347 -61.903 1.00 66.76  ? 1004 VAL   A CA    1 
ATOM   5640 C  C     . VAL   A 1 855  ? -8.298  -16.878 -62.002 1.00 66.43  ? 1004 VAL   A C     1 
ATOM   5641 O  O     . VAL   A 1 855  ? -7.836  -17.396 -63.037 1.00 66.30  ? 1004 VAL   A O     1 
ATOM   5642 C  CB    . VAL   A 1 855  ? -9.675  -14.732 -62.241 1.00 66.30  ? 1004 VAL   A CB    1 
ATOM   5643 C  CG1   . VAL   A 1 855  ? -10.150 -15.096 -63.640 1.00 67.83  ? 1004 VAL   A CG1   1 
ATOM   5644 C  CG2   . VAL   A 1 855  ? -10.728 -15.097 -61.206 1.00 66.40  ? 1004 VAL   A CG2   1 
ATOM   5645 N  N     . CYS   A 1 856  ? -8.748  -17.574 -60.953 1.00 68.05  ? 1005 CYS   A N     1 
ATOM   5646 C  CA    . CYS   A 1 856  ? -8.773  -19.060 -60.883 1.00 69.38  ? 1005 CYS   A CA    1 
ATOM   5647 C  C     . CYS   A 1 856  ? -9.903  -19.540 -59.965 1.00 72.14  ? 1005 CYS   A C     1 
ATOM   5648 O  O     . CYS   A 1 856  ? -10.342 -18.758 -59.100 1.00 70.02  ? 1005 CYS   A O     1 
ATOM   5649 C  CB    . CYS   A 1 856  ? -7.437  -19.606 -60.395 1.00 69.11  ? 1005 CYS   A CB    1 
ATOM   5650 S  SG    . CYS   A 1 856  ? -7.071  -19.174 -58.675 1.00 70.05  ? 1005 CYS   A SG    1 
ATOM   5651 N  N     . TYR   A 1 857  ? -10.338 -20.789 -60.165 1.00 77.72  ? 1006 TYR   A N     1 
ATOM   5652 C  CA    . TYR   A 1 857  ? -11.409 -21.489 -59.405 1.00 79.83  ? 1006 TYR   A CA    1 
ATOM   5653 C  C     . TYR   A 1 857  ? -10.764 -22.588 -58.551 1.00 79.71  ? 1006 TYR   A C     1 
ATOM   5654 O  O     . TYR   A 1 857  ? -9.900  -23.315 -59.077 1.00 79.02  ? 1006 TYR   A O     1 
ATOM   5655 C  CB    . TYR   A 1 857  ? -12.443 -22.060 -60.380 1.00 81.27  ? 1006 TYR   A CB    1 
ATOM   5656 C  CG    . TYR   A 1 857  ? -13.649 -22.717 -59.756 1.00 83.22  ? 1006 TYR   A CG    1 
ATOM   5657 C  CD1   . TYR   A 1 857  ? -14.766 -21.976 -59.404 1.00 83.71  ? 1006 TYR   A CD1   1 
ATOM   5658 C  CD2   . TYR   A 1 857  ? -13.692 -24.088 -59.549 1.00 83.63  ? 1006 TYR   A CD2   1 
ATOM   5659 C  CE1   . TYR   A 1 857  ? -15.884 -22.573 -58.843 1.00 84.14  ? 1006 TYR   A CE1   1 
ATOM   5660 C  CE2   . TYR   A 1 857  ? -14.802 -24.701 -58.989 1.00 83.82  ? 1006 TYR   A CE2   1 
ATOM   5661 C  CZ    . TYR   A 1 857  ? -15.903 -23.941 -58.635 1.00 84.02  ? 1006 TYR   A CZ    1 
ATOM   5662 O  OH    . TYR   A 1 857  ? -17.001 -24.535 -58.083 1.00 83.91  ? 1006 TYR   A OH    1 
ATOM   5663 N  N     . HIS   A 1 858  ? -11.158 -22.694 -57.278 1.00 80.48  ? 1007 HIS   A N     1 
ATOM   5664 C  CA    . HIS   A 1 858  ? -10.662 -23.727 -56.327 1.00 82.05  ? 1007 HIS   A CA    1 
ATOM   5665 C  C     . HIS   A 1 858  ? -11.556 -24.971 -56.399 1.00 84.69  ? 1007 HIS   A C     1 
ATOM   5666 O  O     . HIS   A 1 858  ? -12.793 -24.814 -56.348 1.00 84.21  ? 1007 HIS   A O     1 
ATOM   5667 C  CB    . HIS   A 1 858  ? -10.577 -23.173 -54.899 1.00 80.70  ? 1007 HIS   A CB    1 
ATOM   5668 C  CG    . HIS   A 1 858  ? -10.201 -24.210 -53.894 1.00 79.75  ? 1007 HIS   A CG    1 
ATOM   5669 N  ND1   . HIS   A 1 858  ? -11.109 -24.725 -52.989 1.00 80.45  ? 1007 HIS   A ND1   1 
ATOM   5670 C  CD2   . HIS   A 1 858  ? -9.035  -24.855 -53.671 1.00 79.01  ? 1007 HIS   A CD2   1 
ATOM   5671 C  CE1   . HIS   A 1 858  ? -10.513 -25.630 -52.239 1.00 81.14  ? 1007 HIS   A CE1   1 
ATOM   5672 N  NE2   . HIS   A 1 858  ? -9.240  -25.729 -52.639 1.00 79.34  ? 1007 HIS   A NE2   1 
ATOM   5673 N  N     . LYS   A 1 859  ? -10.939 -26.153 -56.504 1.00 87.58  ? 1008 LYS   A N     1 
ATOM   5674 C  CA    . LYS   A 1 859  ? -11.624 -27.474 -56.531 1.00 90.10  ? 1008 LYS   A CA    1 
ATOM   5675 C  C     . LYS   A 1 859  ? -11.434 -28.161 -55.174 1.00 88.95  ? 1008 LYS   A C     1 
ATOM   5676 O  O     . LYS   A 1 859  ? -12.405 -28.192 -54.394 1.00 88.65  ? 1008 LYS   A O     1 
ATOM   5677 C  CB    . LYS   A 1 859  ? -11.087 -28.323 -57.688 1.00 93.21  ? 1008 LYS   A CB    1 
ATOM   5678 C  CG    . LYS   A 1 859  ? -11.434 -27.808 -59.078 1.00 97.73  ? 1008 LYS   A CG    1 
ATOM   5679 C  CD    . LYS   A 1 859  ? -10.836 -28.639 -60.193 1.00 101.54 ? 1008 LYS   A CD    1 
ATOM   5680 C  CE    . LYS   A 1 859  ? -11.330 -28.240 -61.568 1.00 103.21 ? 1008 LYS   A CE    1 
ATOM   5681 N  NZ    . LYS   A 1 859  ? -10.630 -28.987 -62.640 1.00 104.37 ? 1008 LYS   A NZ    1 
ATOM   5682 N  N     . GLU   A 1 860  ? -10.228 -28.673 -54.901 1.00 90.24  ? 1009 GLU   A N     1 
ATOM   5683 C  CA    . GLU   A 1 860  ? -9.873  -29.383 -53.641 1.00 93.18  ? 1009 GLU   A CA    1 
ATOM   5684 C  C     . GLU   A 1 860  ? -8.396  -29.132 -53.302 1.00 92.85  ? 1009 GLU   A C     1 
ATOM   5685 O  O     . GLU   A 1 860  ? -7.570  -29.114 -54.237 1.00 93.77  ? 1009 GLU   A O     1 
ATOM   5686 C  CB    . GLU   A 1 860  ? -10.167 -30.883 -53.759 1.00 95.53  ? 1009 GLU   A CB    1 
ATOM   5687 C  CG    . GLU   A 1 860  ? -9.616  -31.540 -55.019 1.00 97.30  ? 1009 GLU   A CG    1 
ATOM   5688 C  CD    . GLU   A 1 860  ? -10.620 -31.806 -56.130 1.00 99.07  ? 1009 GLU   A CD    1 
ATOM   5689 O  OE1   . GLU   A 1 860  ? -11.829 -31.905 -55.832 1.00 100.75 ? 1009 GLU   A OE1   1 
ATOM   5690 O  OE2   . GLU   A 1 860  ? -10.188 -31.927 -57.295 1.00 99.02  ? 1009 GLU   A OE2   1 
ATOM   5691 N  N     . LYS   A 1 861  ? -8.090  -28.945 -52.012 1.00 91.58  ? 1010 LYS   A N     1 
ATOM   5692 C  CA    . LYS   A 1 861  ? -6.716  -28.749 -51.467 1.00 89.69  ? 1010 LYS   A CA    1 
ATOM   5693 C  C     . LYS   A 1 861  ? -6.027  -27.605 -52.228 1.00 86.51  ? 1010 LYS   A C     1 
ATOM   5694 O  O     . LYS   A 1 861  ? -6.565  -26.482 -52.193 1.00 83.89  ? 1010 LYS   A O     1 
ATOM   5695 C  CB    . LYS   A 1 861  ? -5.951  -30.080 -51.497 1.00 91.22  ? 1010 LYS   A CB    1 
ATOM   5696 C  CG    . LYS   A 1 861  ? -5.987  -30.873 -50.198 1.00 93.27  ? 1010 LYS   A CG    1 
ATOM   5697 C  CD    . LYS   A 1 861  ? -6.384  -32.324 -50.370 1.00 94.52  ? 1010 LYS   A CD    1 
ATOM   5698 C  CE    . LYS   A 1 861  ? -7.821  -32.487 -50.817 1.00 95.59  ? 1010 LYS   A CE    1 
ATOM   5699 N  NZ    . LYS   A 1 861  ? -8.463  -33.665 -50.186 1.00 95.89  ? 1010 LYS   A NZ    1 
ATOM   5700 N  N     . ARG   A 1 862  ? -4.894  -27.879 -52.888 1.00 84.35  ? 1011 ARG   A N     1 
ATOM   5701 C  CA    . ARG   A 1 862  ? -4.049  -26.873 -53.585 1.00 83.21  ? 1011 ARG   A CA    1 
ATOM   5702 C  C     . ARG   A 1 862  ? -4.438  -26.794 -55.067 1.00 86.26  ? 1011 ARG   A C     1 
ATOM   5703 O  O     . ARG   A 1 862  ? -4.027  -25.821 -55.727 1.00 89.51  ? 1011 ARG   A O     1 
ATOM   5704 C  CB    . ARG   A 1 862  ? -2.567  -27.234 -53.443 1.00 80.10  ? 1011 ARG   A CB    1 
ATOM   5705 C  CG    . ARG   A 1 862  ? -1.951  -26.843 -52.107 1.00 78.68  ? 1011 ARG   A CG    1 
ATOM   5706 C  CD    . ARG   A 1 862  ? -0.471  -27.174 -52.030 1.00 78.18  ? 1011 ARG   A CD    1 
ATOM   5707 N  NE    . ARG   A 1 862  ? 0.306   -26.520 -53.077 1.00 78.61  ? 1011 ARG   A NE    1 
ATOM   5708 C  CZ    . ARG   A 1 862  ? 1.608   -26.698 -53.289 1.00 79.89  ? 1011 ARG   A CZ    1 
ATOM   5709 N  NH1   . ARG   A 1 862  ? 2.309   -27.520 -52.525 1.00 81.20  ? 1011 ARG   A NH1   1 
ATOM   5710 N  NH2   . ARG   A 1 862  ? 2.210   -26.051 -54.272 1.00 80.21  ? 1011 ARG   A NH2   1 
ATOM   5711 N  N     . LYS   A 1 863  ? -5.198  -27.771 -55.571 1.00 87.94  ? 1012 LYS   A N     1 
ATOM   5712 C  CA    . LYS   A 1 863  ? -5.549  -27.888 -57.012 1.00 89.48  ? 1012 LYS   A CA    1 
ATOM   5713 C  C     . LYS   A 1 863  ? -6.591  -26.815 -57.356 1.00 86.65  ? 1012 LYS   A C     1 
ATOM   5714 O  O     . LYS   A 1 863  ? -7.675  -26.827 -56.743 1.00 82.73  ? 1012 LYS   A O     1 
ATOM   5715 C  CB    . LYS   A 1 863  ? -6.048  -29.302 -57.330 1.00 94.01  ? 1012 LYS   A CB    1 
ATOM   5716 C  CG    . LYS   A 1 863  ? -5.660  -29.828 -58.707 1.00 97.98  ? 1012 LYS   A CG    1 
ATOM   5717 C  CD    . LYS   A 1 863  ? -6.268  -31.176 -59.039 1.00 101.15 ? 1012 LYS   A CD    1 
ATOM   5718 C  CE    . LYS   A 1 863  ? -7.738  -31.091 -59.397 1.00 102.42 ? 1012 LYS   A CE    1 
ATOM   5719 N  NZ    . LYS   A 1 863  ? -8.312  -32.425 -59.695 1.00 102.08 ? 1012 LYS   A NZ    1 
ATOM   5720 N  N     . ILE   A 1 864  ? -6.256  -25.919 -58.293 1.00 87.69  ? 1013 ILE   A N     1 
ATOM   5721 C  CA    . ILE   A 1 864  ? -7.130  -24.805 -58.776 1.00 88.65  ? 1013 ILE   A CA    1 
ATOM   5722 C  C     . ILE   A 1 864  ? -7.233  -24.876 -60.306 1.00 90.19  ? 1013 ILE   A C     1 
ATOM   5723 O  O     . ILE   A 1 864  ? -6.326  -25.458 -60.937 1.00 90.01  ? 1013 ILE   A O     1 
ATOM   5724 C  CB    . ILE   A 1 864  ? -6.601  -23.433 -58.306 1.00 87.40  ? 1013 ILE   A CB    1 
ATOM   5725 C  CG1   . ILE   A 1 864  ? -5.135  -23.213 -58.694 1.00 86.22  ? 1013 ILE   A CG1   1 
ATOM   5726 C  CG2   . ILE   A 1 864  ? -6.811  -23.255 -56.811 1.00 87.60  ? 1013 ILE   A CG2   1 
ATOM   5727 C  CD1   . ILE   A 1 864  ? -4.744  -21.760 -58.814 1.00 85.88  ? 1013 ILE   A CD1   1 
ATOM   5728 N  N     . LEU   A 1 865  ? -8.295  -24.289 -60.868 1.00 91.78  ? 1014 LEU   A N     1 
ATOM   5729 C  CA    . LEU   A 1 865  ? -8.574  -24.229 -62.329 1.00 94.64  ? 1014 LEU   A CA    1 
ATOM   5730 C  C     . LEU   A 1 865  ? -8.234  -22.828 -62.852 1.00 95.07  ? 1014 LEU   A C     1 
ATOM   5731 O  O     . LEU   A 1 865  ? -8.761  -21.851 -62.289 1.00 92.79  ? 1014 LEU   A O     1 
ATOM   5732 C  CB    . LEU   A 1 865  ? -10.053 -24.556 -62.564 1.00 97.26  ? 1014 LEU   A CB    1 
ATOM   5733 C  CG    . LEU   A 1 865  ? -10.488 -24.674 -64.026 1.00 100.38 ? 1014 LEU   A CG    1 
ATOM   5734 C  CD1   . LEU   A 1 865  ? -10.061 -26.011 -64.614 1.00 100.80 ? 1014 LEU   A CD1   1 
ATOM   5735 C  CD2   . LEU   A 1 865  ? -11.992 -24.487 -64.167 1.00 100.14 ? 1014 LEU   A CD2   1 
ATOM   5736 N  N     . THR   A 1 866  ? -7.403  -22.746 -63.898 1.00 96.63  ? 1015 THR   A N     1 
ATOM   5737 C  CA    . THR   A 1 866  ? -6.965  -21.483 -64.555 1.00 97.67  ? 1015 THR   A CA    1 
ATOM   5738 C  C     . THR   A 1 866  ? -8.021  -21.049 -65.582 1.00 101.93 ? 1015 THR   A C     1 
ATOM   5739 O  O     . THR   A 1 866  ? -9.057  -21.738 -65.693 1.00 101.18 ? 1015 THR   A O     1 
ATOM   5740 C  CB    . THR   A 1 866  ? -5.575  -21.651 -65.183 1.00 95.73  ? 1015 THR   A CB    1 
ATOM   5741 O  OG1   . THR   A 1 866  ? -5.663  -22.629 -66.219 1.00 96.01  ? 1015 THR   A OG1   1 
ATOM   5742 C  CG2   . THR   A 1 866  ? -4.523  -22.071 -64.181 1.00 95.70  ? 1015 THR   A CG2   1 
ATOM   5743 N  N     . THR   A 1 867  ? -7.765  -19.951 -66.303 1.00 106.72 ? 1016 THR   A N     1 
ATOM   5744 C  CA    . THR   A 1 867  ? -8.679  -19.356 -67.319 1.00 108.94 ? 1016 THR   A CA    1 
ATOM   5745 C  C     . THR   A 1 867  ? -8.697  -20.205 -68.598 1.00 111.40 ? 1016 THR   A C     1 
ATOM   5746 O  O     . THR   A 1 867  ? -9.617  -20.003 -69.412 1.00 113.63 ? 1016 THR   A O     1 
ATOM   5747 C  CB    . THR   A 1 867  ? -8.284  -17.911 -67.650 1.00 108.31 ? 1016 THR   A CB    1 
ATOM   5748 O  OG1   . THR   A 1 867  ? -6.894  -17.897 -67.977 1.00 109.35 ? 1016 THR   A OG1   1 
ATOM   5749 C  CG2   . THR   A 1 867  ? -8.554  -16.950 -66.513 1.00 107.26 ? 1016 THR   A CG2   1 
ATOM   5750 N  N     . GLU   A 1 868  ? -7.726  -21.109 -68.770 1.00 113.40 ? 1017 GLU   A N     1 
ATOM   5751 C  CA    . GLU   A 1 868  ? -7.601  -21.994 -69.962 1.00 115.05 ? 1017 GLU   A CA    1 
ATOM   5752 C  C     . GLU   A 1 868  ? -8.322  -23.322 -69.700 1.00 113.69 ? 1017 GLU   A C     1 
ATOM   5753 O  O     . GLU   A 1 868  ? -8.347  -24.162 -70.618 1.00 112.90 ? 1017 GLU   A O     1 
ATOM   5754 C  CB    . GLU   A 1 868  ? -6.130  -22.252 -70.300 1.00 118.70 ? 1017 GLU   A CB    1 
ATOM   5755 C  CG    . GLU   A 1 868  ? -5.267  -21.000 -70.303 1.00 121.24 ? 1017 GLU   A CG    1 
ATOM   5756 C  CD    . GLU   A 1 868  ? -4.581  -20.681 -68.984 1.00 122.92 ? 1017 GLU   A CD    1 
ATOM   5757 O  OE1   . GLU   A 1 868  ? -3.990  -21.604 -68.381 1.00 120.95 ? 1017 GLU   A OE1   1 
ATOM   5758 O  OE2   . GLU   A 1 868  ? -4.642  -19.510 -68.559 1.00 123.44 ? 1017 GLU   A OE2   1 
ATOM   5759 N  N     . GLY   A 1 869  ? -8.883  -23.499 -68.498 1.00 114.43 ? 1018 GLY   A N     1 
ATOM   5760 C  CA    . GLY   A 1 869  ? -9.512  -24.755 -68.044 1.00 113.96 ? 1018 GLY   A CA    1 
ATOM   5761 C  C     . GLY   A 1 869  ? -8.475  -25.807 -67.683 1.00 114.37 ? 1018 GLY   A C     1 
ATOM   5762 O  O     . GLY   A 1 869  ? -8.829  -27.002 -67.689 1.00 117.28 ? 1018 GLY   A O     1 
ATOM   5763 N  N     . ARG   A 1 870  ? -7.245  -25.381 -67.367 1.00 113.63 ? 1019 ARG   A N     1 
ATOM   5764 C  CA    . ARG   A 1 870  ? -6.095  -26.266 -67.032 1.00 113.39 ? 1019 ARG   A CA    1 
ATOM   5765 C  C     . ARG   A 1 870  ? -5.910  -26.324 -65.511 1.00 110.62 ? 1019 ARG   A C     1 
ATOM   5766 O  O     . ARG   A 1 870  ? -6.367  -25.393 -64.818 1.00 109.84 ? 1019 ARG   A O     1 
ATOM   5767 C  CB    . ARG   A 1 870  ? -4.814  -25.776 -67.717 1.00 115.06 ? 1019 ARG   A CB    1 
ATOM   5768 C  CG    . ARG   A 1 870  ? -4.554  -26.417 -69.073 1.00 117.76 ? 1019 ARG   A CG    1 
ATOM   5769 C  CD    . ARG   A 1 870  ? -3.167  -26.113 -69.606 1.00 120.44 ? 1019 ARG   A CD    1 
ATOM   5770 N  NE    . ARG   A 1 870  ? -3.079  -24.797 -70.226 1.00 123.00 ? 1019 ARG   A NE    1 
ATOM   5771 C  CZ    . ARG   A 1 870  ? -1.987  -24.294 -70.797 1.00 122.62 ? 1019 ARG   A CZ    1 
ATOM   5772 N  NH1   . ARG   A 1 870  ? -0.862  -24.991 -70.831 1.00 121.25 ? 1019 ARG   A NH1   1 
ATOM   5773 N  NH2   . ARG   A 1 870  ? -2.023  -23.087 -71.336 1.00 121.24 ? 1019 ARG   A NH2   1 
ATOM   5774 N  N     . ASN   A 1 871  ? -5.256  -27.383 -65.027 1.00 108.71 ? 1020 ASN   A N     1 
ATOM   5775 C  CA    . ASN   A 1 871  ? -4.996  -27.639 -63.584 1.00 105.07 ? 1020 ASN   A CA    1 
ATOM   5776 C  C     . ASN   A 1 871  ? -3.766  -26.838 -63.145 1.00 100.19 ? 1020 ASN   A C     1 
ATOM   5777 O  O     . ASN   A 1 871  ? -2.762  -26.838 -63.886 1.00 97.76  ? 1020 ASN   A O     1 
ATOM   5778 C  CB    . ASN   A 1 871  ? -4.821  -29.134 -63.301 1.00 105.25 ? 1020 ASN   A CB    1 
ATOM   5779 C  CG    . ASN   A 1 871  ? -6.089  -29.926 -63.542 1.00 105.38 ? 1020 ASN   A CG    1 
ATOM   5780 O  OD1   . ASN   A 1 871  ? -6.171  -30.697 -64.495 1.00 105.50 ? 1020 ASN   A OD1   1 
ATOM   5781 N  ND2   . ASN   A 1 871  ? -7.087  -29.732 -62.694 1.00 103.99 ? 1020 ASN   A ND2   1 
ATOM   5782 N  N     . ALA   A 1 872  ? -3.854  -26.184 -61.982 1.00 96.44  ? 1021 ALA   A N     1 
ATOM   5783 C  CA    . ALA   A 1 872  ? -2.776  -25.377 -61.365 1.00 92.53  ? 1021 ALA   A CA    1 
ATOM   5784 C  C     . ALA   A 1 872  ? -2.767  -25.592 -59.846 1.00 87.54  ? 1021 ALA   A C     1 
ATOM   5785 O  O     . ALA   A 1 872  ? -3.756  -26.138 -59.317 1.00 84.83  ? 1021 ALA   A O     1 
ATOM   5786 C  CB    . ALA   A 1 872  ? -2.966  -23.922 -61.717 1.00 93.87  ? 1021 ALA   A CB    1 
ATOM   5787 N  N     . LEU   A 1 873  ? -1.686  -25.171 -59.179 1.00 82.52  ? 1022 LEU   A N     1 
ATOM   5788 C  CA    . LEU   A 1 873  ? -1.476  -25.331 -57.714 1.00 80.77  ? 1022 LEU   A CA    1 
ATOM   5789 C  C     . LEU   A 1 873  ? -1.506  -23.961 -57.027 1.00 79.01  ? 1022 LEU   A C     1 
ATOM   5790 O  O     . LEU   A 1 873  ? -1.127  -22.961 -57.670 1.00 78.16  ? 1022 LEU   A O     1 
ATOM   5791 C  CB    . LEU   A 1 873  ? -0.132  -26.027 -57.472 1.00 80.85  ? 1022 LEU   A CB    1 
ATOM   5792 C  CG    . LEU   A 1 873  ? -0.066  -27.505 -57.852 1.00 80.60  ? 1022 LEU   A CG    1 
ATOM   5793 C  CD1   . LEU   A 1 873  ? 1.370   -28.007 -57.822 1.00 81.08  ? 1022 LEU   A CD1   1 
ATOM   5794 C  CD2   . LEU   A 1 873  ? -0.943  -28.345 -56.936 1.00 79.81  ? 1022 LEU   A CD2   1 
ATOM   5795 N  N     . ILE   A 1 874  ? -1.951  -23.930 -55.766 1.00 76.30  ? 1023 ILE   A N     1 
ATOM   5796 C  CA    . ILE   A 1 874  ? -1.777  -22.785 -54.823 1.00 72.96  ? 1023 ILE   A CA    1 
ATOM   5797 C  C     . ILE   A 1 874  ? -0.327  -22.819 -54.330 1.00 73.58  ? 1023 ILE   A C     1 
ATOM   5798 O  O     . ILE   A 1 874  ? 0.068   -23.854 -53.760 1.00 74.80  ? 1023 ILE   A O     1 
ATOM   5799 C  CB    . ILE   A 1 874  ? -2.784  -22.863 -53.657 1.00 69.87  ? 1023 ILE   A CB    1 
ATOM   5800 C  CG1   . ILE   A 1 874  ? -4.227  -22.707 -54.145 1.00 69.57  ? 1023 ILE   A CG1   1 
ATOM   5801 C  CG2   . ILE   A 1 874  ? -2.437  -21.851 -52.574 1.00 69.85  ? 1023 ILE   A CG2   1 
ATOM   5802 C  CD1   . ILE   A 1 874  ? -5.274  -22.879 -53.065 1.00 69.35  ? 1023 ILE   A CD1   1 
ATOM   5803 N  N     . HIS   A 1 875  ? 0.430   -21.739 -54.545 1.00 74.20  ? 1024 HIS   A N     1 
ATOM   5804 C  CA    . HIS   A 1 875  ? 1.875   -21.638 -54.199 1.00 76.50  ? 1024 HIS   A CA    1 
ATOM   5805 C  C     . HIS   A 1 875  ? 2.052   -21.831 -52.688 1.00 76.50  ? 1024 HIS   A C     1 
ATOM   5806 O  O     . HIS   A 1 875  ? 1.214   -21.311 -51.928 1.00 74.40  ? 1024 HIS   A O     1 
ATOM   5807 C  CB    . HIS   A 1 875  ? 2.463   -20.309 -54.692 1.00 78.57  ? 1024 HIS   A CB    1 
ATOM   5808 C  CG    . HIS   A 1 875  ? 3.952   -20.311 -54.792 1.00 80.34  ? 1024 HIS   A CG    1 
ATOM   5809 N  ND1   . HIS   A 1 875  ? 4.765   -19.956 -53.733 1.00 81.21  ? 1024 HIS   A ND1   1 
ATOM   5810 C  CD2   . HIS   A 1 875  ? 4.777   -20.622 -55.816 1.00 82.35  ? 1024 HIS   A CD2   1 
ATOM   5811 C  CE1   . HIS   A 1 875  ? 6.027   -20.047 -54.099 1.00 83.54  ? 1024 HIS   A CE1   1 
ATOM   5812 N  NE2   . HIS   A 1 875  ? 6.062   -20.454 -55.374 1.00 84.91  ? 1024 HIS   A NE2   1 
ATOM   5813 N  N     . LYS   A 1 876  ? 3.107   -22.547 -52.285 1.00 79.11  ? 1025 LYS   A N     1 
ATOM   5814 C  CA    . LYS   A 1 876  ? 3.411   -22.914 -50.872 1.00 82.72  ? 1025 LYS   A CA    1 
ATOM   5815 C  C     . LYS   A 1 876  ? 3.428   -21.649 -50.002 1.00 80.96  ? 1025 LYS   A C     1 
ATOM   5816 O  O     . LYS   A 1 876  ? 2.901   -21.695 -48.868 1.00 78.10  ? 1025 LYS   A O     1 
ATOM   5817 C  CB    . LYS   A 1 876  ? 4.763   -23.630 -50.775 1.00 88.70  ? 1025 LYS   A CB    1 
ATOM   5818 C  CG    . LYS   A 1 876  ? 4.888   -24.930 -51.564 1.00 94.37  ? 1025 LYS   A CG    1 
ATOM   5819 C  CD    . LYS   A 1 876  ? 6.299   -25.502 -51.586 1.00 97.11  ? 1025 LYS   A CD    1 
ATOM   5820 C  CE    . LYS   A 1 876  ? 6.517   -26.626 -50.593 1.00 97.35  ? 1025 LYS   A CE    1 
ATOM   5821 N  NZ    . LYS   A 1 876  ? 6.008   -27.920 -51.106 1.00 96.05  ? 1025 LYS   A NZ    1 
ATOM   5822 N  N     . SER   A 1 877  ? 4.003   -20.564 -50.533 1.00 78.62  ? 1026 SER   A N     1 
ATOM   5823 C  CA    . SER   A 1 877  ? 4.272   -19.282 -49.827 1.00 76.05  ? 1026 SER   A CA    1 
ATOM   5824 C  C     . SER   A 1 877  ? 2.973   -18.519 -49.533 1.00 72.38  ? 1026 SER   A C     1 
ATOM   5825 O  O     . SER   A 1 877  ? 3.038   -17.571 -48.732 1.00 70.54  ? 1026 SER   A O     1 
ATOM   5826 C  CB    . SER   A 1 877  ? 5.233   -18.429 -50.618 1.00 76.38  ? 1026 SER   A CB    1 
ATOM   5827 O  OG    . SER   A 1 877  ? 4.636   -17.970 -51.822 1.00 74.62  ? 1026 SER   A OG    1 
ATOM   5828 N  N     . SER   A 1 878  ? 1.853   -18.896 -50.161 1.00 71.03  ? 1027 SER   A N     1 
ATOM   5829 C  CA    . SER   A 1 878  ? 0.521   -18.255 -49.977 1.00 70.07  ? 1027 SER   A CA    1 
ATOM   5830 C  C     . SER   A 1 878  ? -0.028  -18.553 -48.576 1.00 69.42  ? 1027 SER   A C     1 
ATOM   5831 O  O     . SER   A 1 878  ? 0.297   -19.623 -48.018 1.00 70.26  ? 1027 SER   A O     1 
ATOM   5832 C  CB    . SER   A 1 878  ? -0.458  -18.694 -51.036 1.00 69.25  ? 1027 SER   A CB    1 
ATOM   5833 O  OG    . SER   A 1 878  ? -1.732  -18.103 -50.821 1.00 67.09  ? 1027 SER   A OG    1 
ATOM   5834 N  N     . VAL   A 1 879  ? -0.832  -17.628 -48.043 1.00 68.86  ? 1028 VAL   A N     1 
ATOM   5835 C  CA    . VAL   A 1 879  ? -1.610  -17.802 -46.778 1.00 68.51  ? 1028 VAL   A CA    1 
ATOM   5836 C  C     . VAL   A 1 879  ? -2.774  -18.757 -47.061 1.00 68.40  ? 1028 VAL   A C     1 
ATOM   5837 O  O     . VAL   A 1 879  ? -3.207  -19.449 -46.121 1.00 71.85  ? 1028 VAL   A O     1 
ATOM   5838 C  CB    . VAL   A 1 879  ? -2.116  -16.461 -46.205 1.00 67.39  ? 1028 VAL   A CB    1 
ATOM   5839 C  CG1   . VAL   A 1 879  ? -0.969  -15.506 -45.901 1.00 68.09  ? 1028 VAL   A CG1   1 
ATOM   5840 C  CG2   . VAL   A 1 879  ? -3.156  -15.798 -47.100 1.00 65.84  ? 1028 VAL   A CG2   1 
ATOM   5841 N  N     . ASN   A 1 880  ? -3.254  -18.784 -48.310 1.00 66.99  ? 1029 ASN   A N     1 
ATOM   5842 C  CA    . ASN   A 1 880  ? -4.401  -19.619 -48.758 1.00 67.27  ? 1029 ASN   A CA    1 
ATOM   5843 C  C     . ASN   A 1 880  ? -3.946  -21.064 -48.992 1.00 67.75  ? 1029 ASN   A C     1 
ATOM   5844 O  O     . ASN   A 1 880  ? -4.828  -21.924 -49.180 1.00 67.74  ? 1029 ASN   A O     1 
ATOM   5845 C  CB    . ASN   A 1 880  ? -5.061  -19.040 -50.012 1.00 67.06  ? 1029 ASN   A CB    1 
ATOM   5846 C  CG    . ASN   A 1 880  ? -5.696  -17.689 -49.768 1.00 65.64  ? 1029 ASN   A CG    1 
ATOM   5847 O  OD1   . ASN   A 1 880  ? -6.014  -17.345 -48.633 1.00 65.51  ? 1029 ASN   A OD1   1 
ATOM   5848 N  ND2   . ASN   A 1 880  ? -5.885  -16.917 -50.824 1.00 66.22  ? 1029 ASN   A ND2   1 
ATOM   5849 N  N     . CYS   A 1 881  ? -2.635  -21.328 -48.994 1.00 68.57  ? 1030 CYS   A N     1 
ATOM   5850 C  CA    . CYS   A 1 881  ? -2.070  -22.702 -49.048 1.00 69.83  ? 1030 CYS   A CA    1 
ATOM   5851 C  C     . CYS   A 1 881  ? -2.387  -23.414 -47.738 1.00 72.42  ? 1030 CYS   A C     1 
ATOM   5852 O  O     . CYS   A 1 881  ? -2.046  -22.914 -46.667 1.00 70.37  ? 1030 CYS   A O     1 
ATOM   5853 C  CB    . CYS   A 1 881  ? -0.564  -22.703 -49.277 1.00 70.54  ? 1030 CYS   A CB    1 
ATOM   5854 S  SG    . CYS   A 1 881  ? 0.106   -24.363 -49.560 1.00 69.92  ? 1030 CYS   A SG    1 
ATOM   5855 N  N     . PRO   A 1 882  ? -3.053  -24.591 -47.778 1.00 77.04  ? 1031 PRO   A N     1 
ATOM   5856 C  CA    . PRO   A 1 882  ? -3.447  -25.286 -46.556 1.00 80.09  ? 1031 PRO   A CA    1 
ATOM   5857 C  C     . PRO   A 1 882  ? -2.224  -25.840 -45.811 1.00 84.42  ? 1031 PRO   A C     1 
ATOM   5858 O  O     . PRO   A 1 882  ? -1.522  -26.668 -46.363 1.00 83.84  ? 1031 PRO   A O     1 
ATOM   5859 C  CB    . PRO   A 1 882  ? -4.382  -26.397 -47.054 1.00 79.36  ? 1031 PRO   A CB    1 
ATOM   5860 C  CG    . PRO   A 1 882  ? -3.927  -26.660 -48.472 1.00 79.14  ? 1031 PRO   A CG    1 
ATOM   5861 C  CD    . PRO   A 1 882  ? -3.452  -25.319 -48.992 1.00 78.30  ? 1031 PRO   A CD    1 
ATOM   5862 N  N     . PHE   A 1 883  ? -1.992  -25.333 -44.596 1.00 91.78  ? 1032 PHE   A N     1 
ATOM   5863 C  CA    . PHE   A 1 883  ? -0.990  -25.840 -43.622 1.00 96.78  ? 1032 PHE   A CA    1 
ATOM   5864 C  C     . PHE   A 1 883  ? -1.396  -27.264 -43.226 1.00 100.98 ? 1032 PHE   A C     1 
ATOM   5865 O  O     . PHE   A 1 883  ? -2.517  -27.437 -42.701 1.00 104.35 ? 1032 PHE   A O     1 
ATOM   5866 C  CB    . PHE   A 1 883  ? -0.914  -24.902 -42.413 1.00 97.71  ? 1032 PHE   A CB    1 
ATOM   5867 C  CG    . PHE   A 1 883  ? 0.325   -25.020 -41.559 1.00 97.33  ? 1032 PHE   A CG    1 
ATOM   5868 C  CD1   . PHE   A 1 883  ? 1.515   -24.424 -41.949 1.00 97.78  ? 1032 PHE   A CD1   1 
ATOM   5869 C  CD2   . PHE   A 1 883  ? 0.292   -25.688 -40.344 1.00 97.41  ? 1032 PHE   A CD2   1 
ATOM   5870 C  CE1   . PHE   A 1 883  ? 2.650   -24.517 -41.156 1.00 96.45  ? 1032 PHE   A CE1   1 
ATOM   5871 C  CE2   . PHE   A 1 883  ? 1.427   -25.779 -39.552 1.00 96.84  ? 1032 PHE   A CE2   1 
ATOM   5872 C  CZ    . PHE   A 1 883  ? 2.603   -25.193 -39.958 1.00 95.62  ? 1032 PHE   A CZ    1 
ATOM   5873 N  N     . SER   A 1 884  ? -0.534  -28.246 -43.515 1.00 102.15 ? 1033 SER   A N     1 
ATOM   5874 C  CA    A SER   A 1 884  ? -0.742  -29.681 -43.179 0.50 103.03 ? 1033 SER   A CA    1 
ATOM   5875 C  CA    B SER   A 1 884  ? -0.738  -29.683 -43.185 0.50 103.13 ? 1033 SER   A CA    1 
ATOM   5876 C  C     . SER   A 1 884  ? -2.001  -30.212 -43.885 1.00 104.67 ? 1033 SER   A C     1 
ATOM   5877 O  O     . SER   A 1 884  ? -2.218  -29.829 -45.054 1.00 104.33 ? 1033 SER   A O     1 
ATOM   5878 C  CB    A SER   A 1 884  ? -0.792  -29.879 -41.681 0.50 101.83 ? 1033 SER   A CB    1 
ATOM   5879 C  CB    B SER   A 1 884  ? -0.775  -29.888 -41.692 0.50 102.03 ? 1033 SER   A CB    1 
ATOM   5880 O  OG    A SER   A 1 884  ? -2.023  -29.416 -41.143 0.50 100.67 ? 1033 SER   A OG    1 
ATOM   5881 O  OG    B SER   A 1 884  ? -0.666  -31.267 -41.374 0.50 101.13 ? 1033 SER   A OG    1 
ATOM   5882 N  N     . SER   A 1 885  ? -2.792  -31.055 -43.201 1.00 105.72 ? 1034 SER   A N     1 
ATOM   5883 C  CA    . SER   A 1 885  ? -3.932  -31.827 -43.770 1.00 105.13 ? 1034 SER   A CA    1 
ATOM   5884 C  C     . SER   A 1 885  ? -5.255  -31.050 -43.702 1.00 105.43 ? 1034 SER   A C     1 
ATOM   5885 O  O     . SER   A 1 885  ? -6.145  -31.362 -44.521 1.00 104.58 ? 1034 SER   A O     1 
ATOM   5886 C  CB    . SER   A 1 885  ? -4.057  -33.169 -43.089 1.00 105.77 ? 1034 SER   A CB    1 
ATOM   5887 O  OG    . SER   A 1 885  ? -3.688  -33.086 -41.721 1.00 106.68 ? 1034 SER   A OG    1 
ATOM   5888 N  N     . GLN   A 1 886  ? -5.400  -30.103 -42.766 1.00 105.75 ? 1035 GLN   A N     1 
ATOM   5889 C  CA    . GLN   A 1 886  ? -6.650  -29.314 -42.573 1.00 105.16 ? 1035 GLN   A CA    1 
ATOM   5890 C  C     . GLN   A 1 886  ? -6.956  -28.529 -43.856 1.00 104.50 ? 1035 GLN   A C     1 
ATOM   5891 O  O     . GLN   A 1 886  ? -6.269  -27.518 -44.105 1.00 103.81 ? 1035 GLN   A O     1 
ATOM   5892 C  CB    . GLN   A 1 886  ? -6.530  -28.374 -41.369 1.00 105.31 ? 1035 GLN   A CB    1 
ATOM   5893 C  CG    . GLN   A 1 886  ? -7.752  -27.490 -41.146 1.00 105.23 ? 1035 GLN   A CG    1 
ATOM   5894 C  CD    . GLN   A 1 886  ? -9.019  -28.286 -40.938 1.00 104.52 ? 1035 GLN   A CD    1 
ATOM   5895 O  OE1   . GLN   A 1 886  ? -9.281  -28.798 -39.852 1.00 101.94 ? 1035 GLN   A OE1   1 
ATOM   5896 N  NE2   . GLN   A 1 886  ? -9.822  -28.395 -41.985 1.00 104.97 ? 1035 GLN   A NE2   1 
ATOM   5897 N  N     . ASP   A 1 887  ? -7.946  -28.989 -44.630 1.00 104.68 ? 1036 ASP   A N     1 
ATOM   5898 C  CA    . ASP   A 1 887  ? -8.429  -28.329 -45.873 1.00 104.22 ? 1036 ASP   A CA    1 
ATOM   5899 C  C     . ASP   A 1 887  ? -9.178  -27.048 -45.490 1.00 99.89  ? 1036 ASP   A C     1 
ATOM   5900 O  O     . ASP   A 1 887  ? -9.987  -27.097 -44.542 1.00 98.06  ? 1036 ASP   A O     1 
ATOM   5901 C  CB    . ASP   A 1 887  ? -9.319  -29.264 -46.699 1.00 106.79 ? 1036 ASP   A CB    1 
ATOM   5902 C  CG    . ASP   A 1 887  ? -8.600  -30.487 -47.244 1.00 109.93 ? 1036 ASP   A CG    1 
ATOM   5903 O  OD1   . ASP   A 1 887  ? -7.353  -30.519 -47.174 1.00 111.19 ? 1036 ASP   A OD1   1 
ATOM   5904 O  OD2   . ASP   A 1 887  ? -9.295  -31.400 -47.734 1.00 111.19 ? 1036 ASP   A OD2   1 
ATOM   5905 N  N     . MET   A 1 888  ? -8.912  -25.951 -46.203 1.00 95.48  ? 1037 MET   A N     1 
ATOM   5906 C  CA    . MET   A 1 888  ? -9.479  -24.608 -45.915 1.00 93.88  ? 1037 MET   A CA    1 
ATOM   5907 C  C     . MET   A 1 888  ? -10.903 -24.523 -46.473 1.00 93.37  ? 1037 MET   A C     1 
ATOM   5908 O  O     . MET   A 1 888  ? -11.113 -24.932 -47.634 1.00 92.83  ? 1037 MET   A O     1 
ATOM   5909 C  CB    . MET   A 1 888  ? -8.615  -23.507 -46.535 1.00 93.91  ? 1037 MET   A CB    1 
ATOM   5910 C  CG    . MET   A 1 888  ? -7.203  -23.488 -45.989 1.00 94.38  ? 1037 MET   A CG    1 
ATOM   5911 S  SD    . MET   A 1 888  ? -6.396  -21.887 -46.209 1.00 94.22  ? 1037 MET   A SD    1 
ATOM   5912 C  CE    . MET   A 1 888  ? -5.133  -21.987 -44.942 1.00 96.93  ? 1037 MET   A CE    1 
ATOM   5913 N  N     . LYS   A 1 889  ? -11.837 -24.019 -45.660 1.00 92.63  ? 1038 LYS   A N     1 
ATOM   5914 C  CA    . LYS   A 1 889  ? -13.256 -23.783 -46.036 1.00 92.17  ? 1038 LYS   A CA    1 
ATOM   5915 C  C     . LYS   A 1 889  ? -13.394 -22.340 -46.533 1.00 88.06  ? 1038 LYS   A C     1 
ATOM   5916 O  O     . LYS   A 1 889  ? -13.783 -21.465 -45.730 1.00 88.43  ? 1038 LYS   A O     1 
ATOM   5917 C  CB    . LYS   A 1 889  ? -14.181 -24.066 -44.847 1.00 95.29  ? 1038 LYS   A CB    1 
ATOM   5918 C  CG    . LYS   A 1 889  ? -14.259 -25.527 -44.426 1.00 97.99  ? 1038 LYS   A CG    1 
ATOM   5919 C  CD    . LYS   A 1 889  ? -15.319 -25.799 -43.382 1.00 100.38 ? 1038 LYS   A CD    1 
ATOM   5920 C  CE    . LYS   A 1 889  ? -15.525 -27.276 -43.122 1.00 101.33 ? 1038 LYS   A CE    1 
ATOM   5921 N  NZ    . LYS   A 1 889  ? -16.598 -27.509 -42.129 1.00 102.07 ? 1038 LYS   A NZ    1 
ATOM   5922 N  N     . TYR   A 1 890  ? -13.071 -22.108 -47.809 1.00 81.47  ? 1039 TYR   A N     1 
ATOM   5923 C  CA    . TYR   A 1 890  ? -13.154 -20.782 -48.474 1.00 76.65  ? 1039 TYR   A CA    1 
ATOM   5924 C  C     . TYR   A 1 890  ? -14.622 -20.408 -48.652 1.00 75.08  ? 1039 TYR   A C     1 
ATOM   5925 O  O     . TYR   A 1 890  ? -15.394 -21.203 -49.180 1.00 76.52  ? 1039 TYR   A O     1 
ATOM   5926 C  CB    . TYR   A 1 890  ? -12.457 -20.797 -49.837 1.00 73.73  ? 1039 TYR   A CB    1 
ATOM   5927 C  CG    . TYR   A 1 890  ? -11.024 -21.263 -49.830 1.00 71.23  ? 1039 TYR   A CG    1 
ATOM   5928 C  CD1   . TYR   A 1 890  ? -10.075 -20.665 -49.016 1.00 70.93  ? 1039 TYR   A CD1   1 
ATOM   5929 C  CD2   . TYR   A 1 890  ? -10.607 -22.288 -50.664 1.00 69.84  ? 1039 TYR   A CD2   1 
ATOM   5930 C  CE1   . TYR   A 1 890  ? -8.754  -21.083 -49.018 1.00 70.46  ? 1039 TYR   A CE1   1 
ATOM   5931 C  CE2   . TYR   A 1 890  ? -9.290  -22.717 -50.679 1.00 69.22  ? 1039 TYR   A CE2   1 
ATOM   5932 C  CZ    . TYR   A 1 890  ? -8.359  -22.113 -49.854 1.00 69.54  ? 1039 TYR   A CZ    1 
ATOM   5933 O  OH    . TYR   A 1 890  ? -7.064  -22.540 -49.868 1.00 68.49  ? 1039 TYR   A OH    1 
ATOM   5934 N  N     . PRO   A 1 891  ? -15.056 -19.195 -48.233 1.00 74.41  ? 1040 PRO   A N     1 
ATOM   5935 C  CA    . PRO   A 1 891  ? -16.432 -18.750 -48.468 1.00 73.49  ? 1040 PRO   A CA    1 
ATOM   5936 C  C     . PRO   A 1 891  ? -16.736 -18.467 -49.949 1.00 72.37  ? 1040 PRO   A C     1 
ATOM   5937 O  O     . PRO   A 1 891  ? -17.897 -18.285 -50.272 1.00 72.77  ? 1040 PRO   A O     1 
ATOM   5938 C  CB    . PRO   A 1 891  ? -16.544 -17.465 -47.633 1.00 74.13  ? 1040 PRO   A CB    1 
ATOM   5939 C  CG    . PRO   A 1 891  ? -15.122 -16.951 -47.546 1.00 75.16  ? 1040 PRO   A CG    1 
ATOM   5940 C  CD    . PRO   A 1 891  ? -14.256 -18.193 -47.511 1.00 75.09  ? 1040 PRO   A CD    1 
ATOM   5941 N  N     . SER   A 1 892  ? -15.699 -18.418 -50.794 1.00 69.62  ? 1041 SER   A N     1 
ATOM   5942 C  CA    . SER   A 1 892  ? -15.786 -18.311 -52.275 1.00 70.09  ? 1041 SER   A CA    1 
ATOM   5943 C  C     . SER   A 1 892  ? -14.666 -19.135 -52.908 1.00 70.09  ? 1041 SER   A C     1 
ATOM   5944 O  O     . SER   A 1 892  ? -13.546 -19.140 -52.404 1.00 73.62  ? 1041 SER   A O     1 
ATOM   5945 C  CB    . SER   A 1 892  ? -15.725 -16.869 -52.718 1.00 71.13  ? 1041 SER   A CB    1 
ATOM   5946 O  OG    . SER   A 1 892  ? -15.560 -16.771 -54.128 1.00 72.03  ? 1041 SER   A OG    1 
ATOM   5947 N  N     . PRO   A 1 893  ? -14.921 -19.850 -54.028 1.00 68.12  ? 1042 PRO   A N     1 
ATOM   5948 C  CA    . PRO   A 1 893  ? -13.874 -20.611 -54.712 1.00 68.62  ? 1042 PRO   A CA    1 
ATOM   5949 C  C     . PRO   A 1 893  ? -12.999 -19.774 -55.662 1.00 69.38  ? 1042 PRO   A C     1 
ATOM   5950 O  O     . PRO   A 1 893  ? -12.037 -20.314 -56.187 1.00 68.08  ? 1042 PRO   A O     1 
ATOM   5951 C  CB    . PRO   A 1 893  ? -14.698 -21.630 -55.511 1.00 68.77  ? 1042 PRO   A CB    1 
ATOM   5952 C  CG    . PRO   A 1 893  ? -15.947 -20.863 -55.886 1.00 68.80  ? 1042 PRO   A CG    1 
ATOM   5953 C  CD    . PRO   A 1 893  ? -16.229 -19.975 -54.691 1.00 68.00  ? 1042 PRO   A CD    1 
ATOM   5954 N  N     . PHE   A 1 894  ? -13.347 -18.496 -55.858 1.00 69.40  ? 1043 PHE   A N     1 
ATOM   5955 C  CA    . PHE   A 1 894  ? -12.719 -17.575 -56.843 1.00 68.62  ? 1043 PHE   A CA    1 
ATOM   5956 C  C     . PHE   A 1 894  ? -11.566 -16.808 -56.186 1.00 66.16  ? 1043 PHE   A C     1 
ATOM   5957 O  O     . PHE   A 1 894  ? -11.753 -16.259 -55.084 1.00 65.71  ? 1043 PHE   A O     1 
ATOM   5958 C  CB    . PHE   A 1 894  ? -13.769 -16.626 -57.423 1.00 70.22  ? 1043 PHE   A CB    1 
ATOM   5959 C  CG    . PHE   A 1 894  ? -14.816 -17.321 -58.255 1.00 72.57  ? 1043 PHE   A CG    1 
ATOM   5960 C  CD1   . PHE   A 1 894  ? -14.525 -17.749 -59.542 1.00 72.75  ? 1043 PHE   A CD1   1 
ATOM   5961 C  CD2   . PHE   A 1 894  ? -16.083 -17.566 -57.748 1.00 73.88  ? 1043 PHE   A CD2   1 
ATOM   5962 C  CE1   . PHE   A 1 894  ? -15.483 -18.397 -60.306 1.00 72.29  ? 1043 PHE   A CE1   1 
ATOM   5963 C  CE2   . PHE   A 1 894  ? -17.041 -18.213 -58.515 1.00 73.23  ? 1043 PHE   A CE2   1 
ATOM   5964 C  CZ    . PHE   A 1 894  ? -16.738 -18.628 -59.792 1.00 73.07  ? 1043 PHE   A CZ    1 
ATOM   5965 N  N     . PHE   A 1 895  ? -10.414 -16.779 -56.862 1.00 64.70  ? 1044 PHE   A N     1 
ATOM   5966 C  CA    . PHE   A 1 895  ? -9.168  -16.097 -56.425 1.00 63.87  ? 1044 PHE   A CA    1 
ATOM   5967 C  C     . PHE   A 1 895  ? -8.523  -15.379 -57.614 1.00 62.37  ? 1044 PHE   A C     1 
ATOM   5968 O  O     . PHE   A 1 895  ? -8.279  -16.038 -58.642 1.00 61.98  ? 1044 PHE   A O     1 
ATOM   5969 C  CB    . PHE   A 1 895  ? -8.166  -17.101 -55.849 1.00 64.14  ? 1044 PHE   A CB    1 
ATOM   5970 C  CG    . PHE   A 1 895  ? -8.573  -17.732 -54.543 1.00 65.15  ? 1044 PHE   A CG    1 
ATOM   5971 C  CD1   . PHE   A 1 895  ? -8.308  -17.101 -53.339 1.00 65.11  ? 1044 PHE   A CD1   1 
ATOM   5972 C  CD2   . PHE   A 1 895  ? -9.208  -18.964 -54.518 1.00 65.46  ? 1044 PHE   A CD2   1 
ATOM   5973 C  CE1   . PHE   A 1 895  ? -8.679  -17.683 -52.137 1.00 65.90  ? 1044 PHE   A CE1   1 
ATOM   5974 C  CE2   . PHE   A 1 895  ? -9.576  -19.546 -53.315 1.00 66.04  ? 1044 PHE   A CE2   1 
ATOM   5975 C  CZ    . PHE   A 1 895  ? -9.312  -18.904 -52.127 1.00 65.67  ? 1044 PHE   A CZ    1 
ATOM   5976 N  N     . VAL   A 1 896  ? -8.268  -14.075 -57.468 1.00 60.70  ? 1045 VAL   A N     1 
ATOM   5977 C  CA    . VAL   A 1 896  ? -7.328  -13.293 -58.326 1.00 60.33  ? 1045 VAL   A CA    1 
ATOM   5978 C  C     . VAL   A 1 896  ? -5.946  -13.372 -57.664 1.00 59.85  ? 1045 VAL   A C     1 
ATOM   5979 O  O     . VAL   A 1 896  ? -5.900  -13.531 -56.427 1.00 58.24  ? 1045 VAL   A O     1 
ATOM   5980 C  CB    . VAL   A 1 896  ? -7.801  -11.839 -58.529 1.00 60.88  ? 1045 VAL   A CB    1 
ATOM   5981 C  CG1   . VAL   A 1 896  ? -9.245  -11.783 -59.002 1.00 61.56  ? 1045 VAL   A CG1   1 
ATOM   5982 C  CG2   . VAL   A 1 896  ? -7.614  -10.983 -57.284 1.00 61.26  ? 1045 VAL   A CG2   1 
ATOM   5983 N  N     . PHE   A 1 897  ? -4.866  -13.295 -58.449 1.00 59.29  ? 1046 PHE   A N     1 
ATOM   5984 C  CA    . PHE   A 1 897  ? -3.480  -13.534 -57.966 1.00 59.31  ? 1046 PHE   A CA    1 
ATOM   5985 C  C     . PHE   A 1 897  ? -2.458  -12.751 -58.799 1.00 60.40  ? 1046 PHE   A C     1 
ATOM   5986 O  O     . PHE   A 1 897  ? -2.779  -12.322 -59.921 1.00 58.84  ? 1046 PHE   A O     1 
ATOM   5987 C  CB    . PHE   A 1 897  ? -3.183  -15.036 -57.960 1.00 59.24  ? 1046 PHE   A CB    1 
ATOM   5988 C  CG    . PHE   A 1 897  ? -3.240  -15.709 -59.307 1.00 58.16  ? 1046 PHE   A CG    1 
ATOM   5989 C  CD1   . PHE   A 1 897  ? -4.434  -16.210 -59.804 1.00 57.60  ? 1046 PHE   A CD1   1 
ATOM   5990 C  CD2   . PHE   A 1 897  ? -2.094  -15.856 -60.071 1.00 58.20  ? 1046 PHE   A CD2   1 
ATOM   5991 C  CE1   . PHE   A 1 897  ? -4.480  -16.831 -61.043 1.00 58.61  ? 1046 PHE   A CE1   1 
ATOM   5992 C  CE2   . PHE   A 1 897  ? -2.142  -16.477 -61.310 1.00 58.55  ? 1046 PHE   A CE2   1 
ATOM   5993 C  CZ    . PHE   A 1 897  ? -3.334  -16.964 -61.794 1.00 58.37  ? 1046 PHE   A CZ    1 
ATOM   5994 N  N     . GLY   A 1 898  ? -1.252  -12.591 -58.244 1.00 64.73  ? 1047 GLY   A N     1 
ATOM   5995 C  CA    . GLY   A 1 898  ? -0.157  -11.779 -58.807 1.00 70.17  ? 1047 GLY   A CA    1 
ATOM   5996 C  C     . GLY   A 1 898  ? 0.406   -12.382 -60.081 1.00 75.11  ? 1047 GLY   A C     1 
ATOM   5997 O  O     . GLY   A 1 898  ? 0.044   -11.891 -61.167 1.00 77.80  ? 1047 GLY   A O     1 
ATOM   5998 N  N     . GLU   A 1 899  ? 1.255   -13.408 -59.951 1.00 81.53  ? 1048 GLU   A N     1 
ATOM   5999 C  CA    . GLU   A 1 899  ? 1.992   -14.056 -61.072 1.00 86.81  ? 1048 GLU   A CA    1 
ATOM   6000 C  C     . GLU   A 1 899  ? 1.400   -15.444 -61.348 1.00 92.14  ? 1048 GLU   A C     1 
ATOM   6001 O  O     . GLU   A 1 899  ? 1.091   -16.154 -60.368 1.00 94.18  ? 1048 GLU   A O     1 
ATOM   6002 C  CB    . GLU   A 1 899  ? 3.478   -14.203 -60.732 1.00 87.28  ? 1048 GLU   A CB    1 
ATOM   6003 C  CG    . GLU   A 1 899  ? 4.100   -12.973 -60.096 1.00 87.84  ? 1048 GLU   A CG    1 
ATOM   6004 C  CD    . GLU   A 1 899  ? 5.506   -13.199 -59.564 1.00 88.71  ? 1048 GLU   A CD    1 
ATOM   6005 O  OE1   . GLU   A 1 899  ? 5.717   -12.997 -58.351 1.00 88.46  ? 1048 GLU   A OE1   1 
ATOM   6006 O  OE2   . GLU   A 1 899  ? 6.384   -13.578 -60.364 1.00 88.78  ? 1048 GLU   A OE2   1 
ATOM   6007 N  N     . LYS   A 1 900  ? 1.266   -15.815 -62.628 1.00 96.55  ? 1049 LYS   A N     1 
ATOM   6008 C  CA    . LYS   A 1 900  ? 0.936   -17.196 -63.080 1.00 98.78  ? 1049 LYS   A CA    1 
ATOM   6009 C  C     . LYS   A 1 900  ? 2.242   -17.904 -63.463 1.00 101.00 ? 1049 LYS   A C     1 
ATOM   6010 O  O     . LYS   A 1 900  ? 2.546   -17.985 -64.671 1.00 103.46 ? 1049 LYS   A O     1 
ATOM   6011 C  CB    . LYS   A 1 900  ? -0.067  -17.171 -64.240 1.00 98.33  ? 1049 LYS   A CB    1 
ATOM   6012 C  CG    . LYS   A 1 900  ? -0.656  -18.530 -64.606 1.00 98.20  ? 1049 LYS   A CG    1 
ATOM   6013 C  CD    . LYS   A 1 900  ? -1.600  -18.498 -65.792 1.00 97.70  ? 1049 LYS   A CD    1 
ATOM   6014 C  CE    . LYS   A 1 900  ? -2.946  -17.889 -65.464 1.00 97.15  ? 1049 LYS   A CE    1 
ATOM   6015 N  NZ    . LYS   A 1 900  ? -3.828  -17.834 -66.653 1.00 95.54  ? 1049 LYS   A NZ    1 
ATOM   6016 N  N     . ILE   A 1 901  ? 2.981   -18.389 -62.460 1.00 101.27 ? 1050 ILE   A N     1 
ATOM   6017 C  CA    . ILE   A 1 901  ? 4.319   -19.038 -62.614 1.00 102.57 ? 1050 ILE   A CA    1 
ATOM   6018 C  C     . ILE   A 1 901  ? 4.128   -20.432 -63.228 1.00 105.08 ? 1050 ILE   A C     1 
ATOM   6019 O  O     . ILE   A 1 901  ? 3.360   -21.230 -62.652 1.00 107.53 ? 1050 ILE   A O     1 
ATOM   6020 C  CB    . ILE   A 1 901  ? 5.055   -19.094 -61.257 1.00 103.42 ? 1050 ILE   A CB    1 
ATOM   6021 C  CG1   . ILE   A 1 901  ? 5.388   -17.691 -60.740 1.00 104.01 ? 1050 ILE   A CG1   1 
ATOM   6022 C  CG2   . ILE   A 1 901  ? 6.296   -19.972 -61.341 1.00 103.32 ? 1050 ILE   A CG2   1 
ATOM   6023 C  CD1   . ILE   A 1 901  ? 5.769   -17.645 -59.277 1.00 105.28 ? 1050 ILE   A CD1   1 
ATOM   6024 N  N     . ARG   A 1 902  ? 4.797   -20.700 -64.357 1.00 106.38 ? 1051 ARG   A N     1 
ATOM   6025 C  CA    . ARG   A 1 902  ? 4.885   -22.040 -65.003 1.00 106.57 ? 1051 ARG   A CA    1 
ATOM   6026 C  C     . ARG   A 1 902  ? 6.255   -22.648 -64.679 1.00 106.23 ? 1051 ARG   A C     1 
ATOM   6027 O  O     . ARG   A 1 902  ? 7.272   -22.059 -65.091 1.00 104.60 ? 1051 ARG   A O     1 
ATOM   6028 C  CB    . ARG   A 1 902  ? 4.661   -21.935 -66.517 1.00 108.73 ? 1051 ARG   A CB    1 
ATOM   6029 C  CG    . ARG   A 1 902  ? 5.228   -23.098 -67.323 1.00 110.04 ? 1051 ARG   A CG    1 
ATOM   6030 C  CD    . ARG   A 1 902  ? 4.639   -23.217 -68.718 1.00 110.74 ? 1051 ARG   A CD    1 
ATOM   6031 N  NE    . ARG   A 1 902  ? 3.335   -23.874 -68.730 1.00 113.52 ? 1051 ARG   A NE    1 
ATOM   6032 C  CZ    . ARG   A 1 902  ? 3.132   -25.190 -68.646 1.00 114.34 ? 1051 ARG   A CZ    1 
ATOM   6033 N  NH1   . ARG   A 1 902  ? 4.150   -26.028 -68.533 1.00 115.44 ? 1051 ARG   A NH1   1 
ATOM   6034 N  NH2   . ARG   A 1 902  ? 1.899   -25.667 -68.670 1.00 114.24 ? 1051 ARG   A NH2   1 
ATOM   6035 N  N     . THR   A 1 903  ? 6.267   -23.777 -63.963 1.00 108.51 ? 1052 THR   A N     1 
ATOM   6036 C  CA    . THR   A 1 903  ? 7.481   -24.564 -63.605 1.00 109.56 ? 1052 THR   A CA    1 
ATOM   6037 C  C     . THR   A 1 903  ? 7.271   -26.009 -64.081 1.00 110.88 ? 1052 THR   A C     1 
ATOM   6038 O  O     . THR   A 1 903  ? 7.240   -26.211 -65.312 1.00 108.38 ? 1052 THR   A O     1 
ATOM   6039 C  CB    . THR   A 1 903  ? 7.789   -24.420 -62.108 1.00 108.34 ? 1052 THR   A CB    1 
ATOM   6040 O  OG1   . THR   A 1 903  ? 6.596   -24.719 -61.381 1.00 109.35 ? 1052 THR   A OG1   1 
ATOM   6041 C  CG2   . THR   A 1 903  ? 8.278   -23.037 -61.737 1.00 107.57 ? 1052 THR   A CG2   1 
ATOM   6042 N  N     . ARG   A 1 904  ? 7.124   -26.969 -63.159 1.00 113.58 ? 1053 ARG   A N     1 
ATOM   6043 C  CA    . ARG   A 1 904  ? 6.702   -28.362 -63.471 1.00 115.54 ? 1053 ARG   A CA    1 
ATOM   6044 C  C     . ARG   A 1 904  ? 5.195   -28.351 -63.743 1.00 113.42 ? 1053 ARG   A C     1 
ATOM   6045 O  O     . ARG   A 1 904  ? 4.769   -28.951 -64.749 1.00 114.45 ? 1053 ARG   A O     1 
ATOM   6046 C  CB    . ARG   A 1 904  ? 7.041   -29.323 -62.325 1.00 118.12 ? 1053 ARG   A CB    1 
ATOM   6047 C  CG    . ARG   A 1 904  ? 8.522   -29.416 -61.982 1.00 119.22 ? 1053 ARG   A CG    1 
ATOM   6048 C  CD    . ARG   A 1 904  ? 9.437   -29.516 -63.190 1.00 120.57 ? 1053 ARG   A CD    1 
ATOM   6049 N  NE    . ARG   A 1 904  ? 10.694  -30.188 -62.882 1.00 122.07 ? 1053 ARG   A NE    1 
ATOM   6050 C  CZ    . ARG   A 1 904  ? 11.712  -29.656 -62.205 1.00 123.62 ? 1053 ARG   A CZ    1 
ATOM   6051 N  NH1   . ARG   A 1 904  ? 12.804  -30.373 -61.993 1.00 122.32 ? 1053 ARG   A NH1   1 
ATOM   6052 N  NH2   . ARG   A 1 904  ? 11.645  -28.421 -61.735 1.00 124.82 ? 1053 ARG   A NH2   1 
ATOM   6053 N  N     . ALA   A 1 905  ? 4.435   -27.688 -62.866 1.00 110.98 ? 1054 ALA   A N     1 
ATOM   6054 C  CA    . ALA   A 1 905  ? 2.991   -27.391 -63.016 1.00 107.77 ? 1054 ALA   A CA    1 
ATOM   6055 C  C     . ALA   A 1 905  ? 2.773   -25.879 -62.884 1.00 104.52 ? 1054 ALA   A C     1 
ATOM   6056 O  O     . ALA   A 1 905  ? 3.728   -25.169 -62.506 1.00 101.79 ? 1054 ALA   A O     1 
ATOM   6057 C  CB    . ALA   A 1 905  ? 2.197   -28.156 -61.986 1.00 107.74 ? 1054 ALA   A CB    1 
ATOM   6058 N  N     . ILE   A 1 906  ? 1.558   -25.414 -63.187 1.00 103.07 ? 1055 ILE   A N     1 
ATOM   6059 C  CA    . ILE   A 1 906  ? 1.138   -23.986 -63.061 1.00 101.58 ? 1055 ILE   A CA    1 
ATOM   6060 C  C     . ILE   A 1 906  ? 0.923   -23.690 -61.571 1.00 99.99  ? 1055 ILE   A C     1 
ATOM   6061 O  O     . ILE   A 1 906  ? 0.158   -24.438 -60.931 1.00 99.71  ? 1055 ILE   A O     1 
ATOM   6062 C  CB    . ILE   A 1 906  ? -0.124  -23.707 -63.906 1.00 101.49 ? 1055 ILE   A CB    1 
ATOM   6063 C  CG1   . ILE   A 1 906  ? 0.095   -24.034 -65.387 1.00 102.05 ? 1055 ILE   A CG1   1 
ATOM   6064 C  CG2   . ILE   A 1 906  ? -0.599  -22.273 -63.717 1.00 101.28 ? 1055 ILE   A CG2   1 
ATOM   6065 C  CD1   . ILE   A 1 906  ? -1.181  -24.291 -66.157 1.00 102.60 ? 1055 ILE   A CD1   1 
ATOM   6066 N  N     . SER   A 1 907  ? 1.582   -22.651 -61.044 1.00 97.53  ? 1056 SER   A N     1 
ATOM   6067 C  CA    . SER   A 1 907  ? 1.577   -22.270 -59.605 1.00 94.43  ? 1056 SER   A CA    1 
ATOM   6068 C  C     . SER   A 1 907  ? 1.144   -20.807 -59.447 1.00 91.48  ? 1056 SER   A C     1 
ATOM   6069 O  O     . SER   A 1 907  ? 1.951   -19.916 -59.773 1.00 96.34  ? 1056 SER   A O     1 
ATOM   6070 C  CB    . SER   A 1 907  ? 2.931   -22.512 -58.986 1.00 93.89  ? 1056 SER   A CB    1 
ATOM   6071 O  OG    . SER   A 1 907  ? 3.403   -23.813 -59.300 1.00 93.60  ? 1056 SER   A OG    1 
ATOM   6072 N  N     . ALA   A 1 908  ? -0.082  -20.572 -58.966 1.00 85.97  ? 1057 ALA   A N     1 
ATOM   6073 C  CA    . ALA   A 1 908  ? -0.644  -19.226 -58.694 1.00 80.70  ? 1057 ALA   A CA    1 
ATOM   6074 C  C     . ALA   A 1 908  ? -0.048  -18.686 -57.388 1.00 77.73  ? 1057 ALA   A C     1 
ATOM   6075 O  O     . ALA   A 1 908  ? -0.313  -19.289 -56.329 1.00 77.11  ? 1057 ALA   A O     1 
ATOM   6076 C  CB    . ALA   A 1 908  ? -2.150  -19.291 -58.632 1.00 79.63  ? 1057 ALA   A CB    1 
ATOM   6077 N  N     . LYS   A 1 909  ? 0.730   -17.601 -57.470 1.00 74.85  ? 1058 LYS   A N     1 
ATOM   6078 C  CA    . LYS   A 1 909  ? 1.438   -16.973 -56.320 1.00 72.98  ? 1058 LYS   A CA    1 
ATOM   6079 C  C     . LYS   A 1 909  ? 0.787   -15.625 -55.986 1.00 70.37  ? 1058 LYS   A C     1 
ATOM   6080 O  O     . LYS   A 1 909  ? 0.402   -14.900 -56.929 1.00 68.89  ? 1058 LYS   A O     1 
ATOM   6081 C  CB    . LYS   A 1 909  ? 2.924   -16.790 -56.642 1.00 73.24  ? 1058 LYS   A CB    1 
ATOM   6082 C  CG    . LYS   A 1 909  ? 3.762   -16.225 -55.504 1.00 73.97  ? 1058 LYS   A CG    1 
ATOM   6083 C  CD    . LYS   A 1 909  ? 5.248   -16.239 -55.775 1.00 75.94  ? 1058 LYS   A CD    1 
ATOM   6084 C  CE    . LYS   A 1 909  ? 6.047   -15.602 -54.659 1.00 78.92  ? 1058 LYS   A CE    1 
ATOM   6085 N  NZ    . LYS   A 1 909  ? 7.506   -15.739 -54.883 1.00 81.52  ? 1058 LYS   A NZ    1 
ATOM   6086 N  N     . GLY   A 1 910  ? 0.689   -15.305 -54.690 1.00 67.29  ? 1059 GLY   A N     1 
ATOM   6087 C  CA    . GLY   A 1 910  ? 0.097   -14.054 -54.177 1.00 64.73  ? 1059 GLY   A CA    1 
ATOM   6088 C  C     . GLY   A 1 910  ? -1.392  -13.984 -54.469 1.00 61.05  ? 1059 GLY   A C     1 
ATOM   6089 O  O     . GLY   A 1 910  ? -1.786  -13.162 -55.311 1.00 58.24  ? 1059 GLY   A O     1 
ATOM   6090 N  N     . MET   A 1 911  ? -2.188  -14.809 -53.783 1.00 58.45  ? 1060 MET   A N     1 
ATOM   6091 C  CA    . MET   A 1 911  ? -3.623  -15.046 -54.089 1.00 57.69  ? 1060 MET   A CA    1 
ATOM   6092 C  C     . MET   A 1 911  ? -4.512  -14.237 -53.141 1.00 55.08  ? 1060 MET   A C     1 
ATOM   6093 O  O     . MET   A 1 911  ? -4.185  -14.159 -51.945 1.00 55.95  ? 1060 MET   A O     1 
ATOM   6094 C  CB    . MET   A 1 911  ? -3.960  -16.532 -53.950 1.00 59.37  ? 1060 MET   A CB    1 
ATOM   6095 C  CG    . MET   A 1 911  ? -3.340  -17.382 -55.040 1.00 60.53  ? 1060 MET   A CG    1 
ATOM   6096 S  SD    . MET   A 1 911  ? -3.671  -19.141 -54.825 1.00 61.62  ? 1060 MET   A SD    1 
ATOM   6097 C  CE    . MET   A 1 911  ? -5.451  -19.117 -54.622 1.00 62.26  ? 1060 MET   A CE    1 
ATOM   6098 N  N     . THR   A 1 912  ? -5.603  -13.679 -53.674 1.00 53.62  ? 1061 THR   A N     1 
ATOM   6099 C  CA    . THR   A 1 912  ? -6.644  -12.926 -52.926 1.00 52.91  ? 1061 THR   A CA    1 
ATOM   6100 C  C     . THR   A 1 912  ? -8.029  -13.454 -53.313 1.00 53.47  ? 1061 THR   A C     1 
ATOM   6101 O  O     . THR   A 1 912  ? -8.365  -13.412 -54.511 1.00 52.76  ? 1061 THR   A O     1 
ATOM   6102 C  CB    . THR   A 1 912  ? -6.540  -11.419 -53.189 1.00 52.59  ? 1061 THR   A CB    1 
ATOM   6103 O  OG1   . THR   A 1 912  ? -5.290  -10.977 -52.659 1.00 51.59  ? 1061 THR   A OG1   1 
ATOM   6104 C  CG2   . THR   A 1 912  ? -7.676  -10.630 -52.572 1.00 52.74  ? 1061 THR   A CG2   1 
ATOM   6105 N  N     . LEU   A 1 913  ? -8.792  -13.931 -52.326 1.00 55.28  ? 1062 LEU   A N     1 
ATOM   6106 C  CA    . LEU   A 1 913  ? -10.213 -14.340 -52.482 1.00 56.46  ? 1062 LEU   A CA    1 
ATOM   6107 C  C     . LEU   A 1 913  ? -11.021 -13.132 -52.963 1.00 56.33  ? 1062 LEU   A C     1 
ATOM   6108 O  O     . LEU   A 1 913  ? -10.792 -12.024 -52.440 1.00 56.84  ? 1062 LEU   A O     1 
ATOM   6109 C  CB    . LEU   A 1 913  ? -10.734 -14.853 -51.135 1.00 58.05  ? 1062 LEU   A CB    1 
ATOM   6110 C  CG    . LEU   A 1 913  ? -12.157 -15.414 -51.137 1.00 59.33  ? 1062 LEU   A CG    1 
ATOM   6111 C  CD1   . LEU   A 1 913  ? -12.290 -16.535 -50.116 1.00 60.49  ? 1062 LEU   A CD1   1 
ATOM   6112 C  CD2   . LEU   A 1 913  ? -13.190 -14.326 -50.868 1.00 58.93  ? 1062 LEU   A CD2   1 
ATOM   6113 N  N     . VAL   A 1 914  ? -11.916 -13.346 -53.929 1.00 56.33  ? 1063 VAL   A N     1 
ATOM   6114 C  CA    . VAL   A 1 914  ? -12.896 -12.330 -54.415 1.00 57.01  ? 1063 VAL   A CA    1 
ATOM   6115 C  C     . VAL   A 1 914  ? -14.263 -13.007 -54.543 1.00 58.38  ? 1063 VAL   A C     1 
ATOM   6116 O  O     . VAL   A 1 914  ? -14.295 -14.225 -54.813 1.00 60.86  ? 1063 VAL   A O     1 
ATOM   6117 C  CB    . VAL   A 1 914  ? -12.447 -11.698 -55.746 1.00 56.41  ? 1063 VAL   A CB    1 
ATOM   6118 C  CG1   . VAL   A 1 914  ? -11.148 -10.923 -55.587 1.00 56.51  ? 1063 VAL   A CG1   1 
ATOM   6119 C  CG2   . VAL   A 1 914  ? -12.322 -12.729 -56.858 1.00 56.51  ? 1063 VAL   A CG2   1 
ATOM   6120 N  N     . THR   A 1 915  ? -15.343 -12.246 -54.354 1.00 58.92  ? 1064 THR   A N     1 
ATOM   6121 C  CA    . THR   A 1 915  ? -16.743 -12.722 -54.507 1.00 60.60  ? 1064 THR   A CA    1 
ATOM   6122 C  C     . THR   A 1 915  ? -17.037 -12.876 -55.998 1.00 61.13  ? 1064 THR   A C     1 
ATOM   6123 O  O     . THR   A 1 915  ? -16.306 -12.342 -56.832 1.00 59.85  ? 1064 THR   A O     1 
ATOM   6124 C  CB    . THR   A 1 915  ? -17.732 -11.787 -53.795 1.00 61.89  ? 1064 THR   A CB    1 
ATOM   6125 O  OG1   . THR   A 1 915  ? -17.708 -10.508 -54.430 1.00 63.91  ? 1064 THR   A OG1   1 
ATOM   6126 C  CG2   . THR   A 1 915  ? -17.427 -11.622 -52.322 1.00 62.51  ? 1064 THR   A CG2   1 
ATOM   6127 N  N     . PRO   A 1 916  ? -18.090 -13.635 -56.386 1.00 62.20  ? 1065 PRO   A N     1 
ATOM   6128 C  CA    . PRO   A 1 916  ? -18.491 -13.737 -57.791 1.00 61.70  ? 1065 PRO   A CA    1 
ATOM   6129 C  C     . PRO   A 1 916  ? -18.919 -12.389 -58.397 1.00 60.38  ? 1065 PRO   A C     1 
ATOM   6130 O  O     . PRO   A 1 916  ? -18.806 -12.236 -59.602 1.00 58.31  ? 1065 PRO   A O     1 
ATOM   6131 C  CB    . PRO   A 1 916  ? -19.682 -14.708 -57.767 1.00 62.73  ? 1065 PRO   A CB    1 
ATOM   6132 C  CG    . PRO   A 1 916  ? -19.526 -15.470 -56.467 1.00 62.90  ? 1065 PRO   A CG    1 
ATOM   6133 C  CD    . PRO   A 1 916  ? -18.925 -14.466 -55.506 1.00 62.87  ? 1065 PRO   A CD    1 
ATOM   6134 N  N     . LEU   A 1 917  ? -19.403 -11.462 -57.562 1.00 59.50  ? 1066 LEU   A N     1 
ATOM   6135 C  CA    . LEU   A 1 917  ? -19.795 -10.085 -57.972 1.00 59.29  ? 1066 LEU   A CA    1 
ATOM   6136 C  C     . LEU   A 1 917  ? -18.541 -9.311  -58.388 1.00 58.88  ? 1066 LEU   A C     1 
ATOM   6137 O  O     . LEU   A 1 917  ? -18.593 -8.619  -59.425 1.00 59.55  ? 1066 LEU   A O     1 
ATOM   6138 C  CB    . LEU   A 1 917  ? -20.514 -9.383  -56.815 1.00 59.89  ? 1066 LEU   A CB    1 
ATOM   6139 C  CG    . LEU   A 1 917  ? -21.807 -10.037 -56.328 1.00 60.27  ? 1066 LEU   A CG    1 
ATOM   6140 C  CD1   . LEU   A 1 917  ? -22.418 -9.231  -55.192 1.00 60.97  ? 1066 LEU   A CD1   1 
ATOM   6141 C  CD2   . LEU   A 1 917  ? -22.811 -10.199 -57.459 1.00 59.96  ? 1066 LEU   A CD2   1 
ATOM   6142 N  N     . GLN   A 1 918  ? -17.462 -9.434  -57.607 1.00 58.49  ? 1067 GLN   A N     1 
ATOM   6143 C  CA    . GLN   A 1 918  ? -16.134 -8.830  -57.900 1.00 60.03  ? 1067 GLN   A CA    1 
ATOM   6144 C  C     . GLN   A 1 918  ? -15.542 -9.472  -59.161 1.00 61.56  ? 1067 GLN   A C     1 
ATOM   6145 O  O     . GLN   A 1 918  ? -14.844 -8.759  -59.906 1.00 62.15  ? 1067 GLN   A O     1 
ATOM   6146 C  CB    . GLN   A 1 918  ? -15.192 -8.996  -56.707 1.00 60.14  ? 1067 GLN   A CB    1 
ATOM   6147 C  CG    . GLN   A 1 918  ? -15.544 -8.097  -55.532 1.00 60.14  ? 1067 GLN   A CG    1 
ATOM   6148 C  CD    . GLN   A 1 918  ? -14.616 -8.306  -54.361 1.00 60.26  ? 1067 GLN   A CD    1 
ATOM   6149 O  OE1   . GLN   A 1 918  ? -14.397 -9.430  -53.915 1.00 59.98  ? 1067 GLN   A OE1   1 
ATOM   6150 N  NE2   . GLN   A 1 918  ? -14.065 -7.218  -53.845 1.00 60.92  ? 1067 GLN   A NE2   1 
ATOM   6151 N  N     . LEU   A 1 919  ? -15.805 -10.766 -59.381 1.00 64.08  ? 1068 LEU   A N     1 
ATOM   6152 C  CA    . LEU   A 1 919  ? -15.394 -11.507 -60.604 1.00 66.30  ? 1068 LEU   A CA    1 
ATOM   6153 C  C     . LEU   A 1 919  ? -16.012 -10.836 -61.837 1.00 66.24  ? 1068 LEU   A C     1 
ATOM   6154 O  O     . LEU   A 1 919  ? -15.263 -10.561 -62.791 1.00 66.11  ? 1068 LEU   A O     1 
ATOM   6155 C  CB    . LEU   A 1 919  ? -15.835 -12.971 -60.490 1.00 69.00  ? 1068 LEU   A CB    1 
ATOM   6156 C  CG    . LEU   A 1 919  ? -15.672 -13.820 -61.752 1.00 70.84  ? 1068 LEU   A CG    1 
ATOM   6157 C  CD1   . LEU   A 1 919  ? -14.203 -14.019 -62.093 1.00 71.87  ? 1068 LEU   A CD1   1 
ATOM   6158 C  CD2   . LEU   A 1 919  ? -16.363 -15.163 -61.592 1.00 71.38  ? 1068 LEU   A CD2   1 
ATOM   6159 N  N     . LEU   A 1 920  ? -17.325 -10.584 -61.805 1.00 66.29  ? 1069 LEU   A N     1 
ATOM   6160 C  CA    . LEU   A 1 920  ? -18.113 -10.036 -62.944 1.00 66.41  ? 1069 LEU   A CA    1 
ATOM   6161 C  C     . LEU   A 1 920  ? -17.773 -8.556  -63.170 1.00 66.37  ? 1069 LEU   A C     1 
ATOM   6162 O  O     . LEU   A 1 920  ? -17.833 -8.117  -64.335 1.00 68.47  ? 1069 LEU   A O     1 
ATOM   6163 C  CB    . LEU   A 1 920  ? -19.609 -10.212 -62.658 1.00 67.30  ? 1069 LEU   A CB    1 
ATOM   6164 C  CG    . LEU   A 1 920  ? -20.151 -11.632 -62.814 1.00 66.92  ? 1069 LEU   A CG    1 
ATOM   6165 C  CD1   . LEU   A 1 920  ? -21.482 -11.791 -62.096 1.00 66.17  ? 1069 LEU   A CD1   1 
ATOM   6166 C  CD2   . LEU   A 1 920  ? -20.293 -12.000 -64.283 1.00 67.37  ? 1069 LEU   A CD2   1 
ATOM   6167 N  N     . LEU   A 1 921  ? -17.440 -7.815  -62.107 1.00 65.06  ? 1070 LEU   A N     1 
ATOM   6168 C  CA    . LEU   A 1 921  ? -17.216 -6.344  -62.166 1.00 64.88  ? 1070 LEU   A CA    1 
ATOM   6169 C  C     . LEU   A 1 921  ? -15.864 -6.034  -62.825 1.00 65.42  ? 1070 LEU   A C     1 
ATOM   6170 O  O     . LEU   A 1 921  ? -15.857 -5.220  -63.768 1.00 66.41  ? 1070 LEU   A O     1 
ATOM   6171 C  CB    . LEU   A 1 921  ? -17.284 -5.753  -60.754 1.00 64.34  ? 1070 LEU   A CB    1 
ATOM   6172 C  CG    . LEU   A 1 921  ? -17.053 -4.243  -60.659 1.00 63.36  ? 1070 LEU   A CG    1 
ATOM   6173 C  CD1   . LEU   A 1 921  ? -18.088 -3.477  -61.467 1.00 62.98  ? 1070 LEU   A CD1   1 
ATOM   6174 C  CD2   . LEU   A 1 921  ? -17.061 -3.784  -59.209 1.00 63.30  ? 1070 LEU   A CD2   1 
ATOM   6175 N  N     . PHE   A 1 922  ? -14.769 -6.637  -62.343 1.00 64.93  ? 1071 PHE   A N     1 
ATOM   6176 C  CA    . PHE   A 1 922  ? -13.377 -6.242  -62.695 1.00 64.17  ? 1071 PHE   A CA    1 
ATOM   6177 C  C     . PHE   A 1 922  ? -12.536 -7.414  -63.222 1.00 65.12  ? 1071 PHE   A C     1 
ATOM   6178 O  O     . PHE   A 1 922  ? -11.643 -7.139  -64.049 1.00 64.17  ? 1071 PHE   A O     1 
ATOM   6179 C  CB    . PHE   A 1 922  ? -12.702 -5.582  -61.490 1.00 62.89  ? 1071 PHE   A CB    1 
ATOM   6180 C  CG    . PHE   A 1 922  ? -13.209 -4.196  -61.179 1.00 62.18  ? 1071 PHE   A CG    1 
ATOM   6181 C  CD1   . PHE   A 1 922  ? -13.258 -3.219  -62.163 1.00 61.23  ? 1071 PHE   A CD1   1 
ATOM   6182 C  CD2   . PHE   A 1 922  ? -13.633 -3.863  -59.902 1.00 62.52  ? 1071 PHE   A CD2   1 
ATOM   6183 C  CE1   . PHE   A 1 922  ? -13.726 -1.947  -61.878 1.00 61.14  ? 1071 PHE   A CE1   1 
ATOM   6184 C  CE2   . PHE   A 1 922  ? -14.097 -2.587  -59.618 1.00 62.22  ? 1071 PHE   A CE2   1 
ATOM   6185 C  CZ    . PHE   A 1 922  ? -14.141 -1.631  -60.606 1.00 61.49  ? 1071 PHE   A CZ    1 
ATOM   6186 N  N     . ALA   A 1 923  ? -12.787 -8.654  -62.780 1.00 67.71  ? 1072 ALA   A N     1 
ATOM   6187 C  CA    . ALA   A 1 923  ? -11.957 -9.843  -63.101 1.00 70.36  ? 1072 ALA   A CA    1 
ATOM   6188 C  C     . ALA   A 1 923  ? -12.551 -10.634 -64.278 1.00 71.34  ? 1072 ALA   A C     1 
ATOM   6189 O  O     . ALA   A 1 923  ? -12.518 -11.880 -64.229 1.00 71.62  ? 1072 ALA   A O     1 
ATOM   6190 C  CB    . ALA   A 1 923  ? -11.813 -10.711 -61.875 1.00 70.79  ? 1072 ALA   A CB    1 
ATOM   6191 N  N     . SER   A 1 924  ? -13.043 -9.941  -65.309 1.00 73.10  ? 1073 SER   A N     1 
ATOM   6192 C  CA    . SER   A 1 924  ? -13.657 -10.549 -66.520 1.00 75.34  ? 1073 SER   A CA    1 
ATOM   6193 C  C     . SER   A 1 924  ? -13.746 -9.514  -67.647 1.00 77.95  ? 1073 SER   A C     1 
ATOM   6194 O  O     . SER   A 1 924  ? -13.851 -8.307  -67.338 1.00 77.58  ? 1073 SER   A O     1 
ATOM   6195 C  CB    . SER   A 1 924  ? -15.011 -11.128 -66.204 1.00 75.01  ? 1073 SER   A CB    1 
ATOM   6196 O  OG    . SER   A 1 924  ? -15.895 -10.126 -65.722 1.00 74.26  ? 1073 SER   A OG    1 
ATOM   6197 N  N     . LYS   A 1 925  ? -13.699 -9.981  -68.901 1.00 80.80  ? 1074 LYS   A N     1 
ATOM   6198 C  CA    . LYS   A 1 925  ? -13.876 -9.154  -70.125 1.00 83.83  ? 1074 LYS   A CA    1 
ATOM   6199 C  C     . LYS   A 1 925  ? -15.187 -9.559  -70.808 1.00 85.88  ? 1074 LYS   A C     1 
ATOM   6200 O  O     . LYS   A 1 925  ? -16.109 -8.722  -70.842 1.00 86.66  ? 1074 LYS   A O     1 
ATOM   6201 C  CB    . LYS   A 1 925  ? -12.681 -9.312  -71.071 1.00 84.74  ? 1074 LYS   A CB    1 
ATOM   6202 C  CG    . LYS   A 1 925  ? -12.643 -8.323  -72.231 1.00 86.67  ? 1074 LYS   A CG    1 
ATOM   6203 C  CD    . LYS   A 1 925  ? -11.546 -8.600  -73.242 1.00 89.28  ? 1074 LYS   A CD    1 
ATOM   6204 C  CE    . LYS   A 1 925  ? -10.151 -8.500  -72.660 1.00 90.63  ? 1074 LYS   A CE    1 
ATOM   6205 N  NZ    . LYS   A 1 925  ? -9.112  -8.572  -73.714 1.00 91.04  ? 1074 LYS   A NZ    1 
ATOM   6206 N  N     . LYS   A 1 926  ? -15.268 -10.797 -71.306 1.00 88.29  ? 1075 LYS   A N     1 
ATOM   6207 C  CA    . LYS   A 1 926  ? -16.429 -11.316 -72.080 1.00 88.56  ? 1075 LYS   A CA    1 
ATOM   6208 C  C     . LYS   A 1 926  ? -17.380 -12.061 -71.136 1.00 86.60  ? 1075 LYS   A C     1 
ATOM   6209 O  O     . LYS   A 1 926  ? -16.895 -12.898 -70.348 1.00 84.25  ? 1075 LYS   A O     1 
ATOM   6210 C  CB    . LYS   A 1 926  ? -15.953 -12.222 -73.220 1.00 92.25  ? 1075 LYS   A CB    1 
ATOM   6211 C  CG    . LYS   A 1 926  ? -16.999 -12.508 -74.290 1.00 95.21  ? 1075 LYS   A CG    1 
ATOM   6212 C  CD    . LYS   A 1 926  ? -16.439 -13.182 -75.526 1.00 97.72  ? 1075 LYS   A CD    1 
ATOM   6213 C  CE    . LYS   A 1 926  ? -15.921 -14.581 -75.261 1.00 98.99  ? 1075 LYS   A CE    1 
ATOM   6214 N  NZ    . LYS   A 1 926  ? -15.342 -15.191 -76.482 1.00 99.32  ? 1075 LYS   A NZ    1 
ATOM   6215 N  N     . VAL   A 1 927  ? -18.679 -11.754 -71.222 1.00 87.75  ? 1076 VAL   A N     1 
ATOM   6216 C  CA    . VAL   A 1 927  ? -19.772 -12.378 -70.416 1.00 87.95  ? 1076 VAL   A CA    1 
ATOM   6217 C  C     . VAL   A 1 927  ? -20.970 -12.632 -71.341 1.00 88.70  ? 1076 VAL   A C     1 
ATOM   6218 O  O     . VAL   A 1 927  ? -21.496 -11.650 -71.903 1.00 84.26  ? 1076 VAL   A O     1 
ATOM   6219 C  CB    . VAL   A 1 927  ? -20.172 -11.497 -69.215 1.00 87.55  ? 1076 VAL   A CB    1 
ATOM   6220 C  CG1   . VAL   A 1 927  ? -21.168 -12.203 -68.306 1.00 88.47  ? 1076 VAL   A CG1   1 
ATOM   6221 C  CG2   . VAL   A 1 927  ? -18.962 -11.036 -68.419 1.00 88.08  ? 1076 VAL   A CG2   1 
ATOM   6222 N  N     . GLN   A 1 928  ? -21.370 -13.901 -71.487 1.00 91.54  ? 1077 GLN   A N     1 
ATOM   6223 C  CA    . GLN   A 1 928  ? -22.555 -14.349 -72.269 1.00 92.13  ? 1077 GLN   A CA    1 
ATOM   6224 C  C     . GLN   A 1 928  ? -23.602 -14.912 -71.301 1.00 91.32  ? 1077 GLN   A C     1 
ATOM   6225 O  O     . GLN   A 1 928  ? -23.201 -15.631 -70.370 1.00 92.86  ? 1077 GLN   A O     1 
ATOM   6226 C  CB    . GLN   A 1 928  ? -22.147 -15.410 -73.294 1.00 93.70  ? 1077 GLN   A CB    1 
ATOM   6227 C  CG    . GLN   A 1 928  ? -21.144 -14.915 -74.327 1.00 95.92  ? 1077 GLN   A CG    1 
ATOM   6228 C  CD    . GLN   A 1 928  ? -20.613 -16.033 -75.191 1.00 97.83  ? 1077 GLN   A CD    1 
ATOM   6229 O  OE1   . GLN   A 1 928  ? -21.330 -16.967 -75.544 1.00 97.61  ? 1077 GLN   A OE1   1 
ATOM   6230 N  NE2   . GLN   A 1 928  ? -19.340 -15.943 -75.541 1.00 98.32  ? 1077 GLN   A NE2   1 
ATOM   6231 N  N     . SER   A 1 929  ? -24.885 -14.599 -71.517 1.00 91.37  ? 1078 SER   A N     1 
ATOM   6232 C  CA    . SER   A 1 929  ? -26.035 -15.049 -70.685 1.00 92.67  ? 1078 SER   A CA    1 
ATOM   6233 C  C     . SER   A 1 929  ? -27.047 -15.812 -71.548 1.00 95.00  ? 1078 SER   A C     1 
ATOM   6234 O  O     . SER   A 1 929  ? -27.272 -15.391 -72.701 1.00 97.03  ? 1078 SER   A O     1 
ATOM   6235 C  CB    . SER   A 1 929  ? -26.693 -13.883 -69.995 1.00 91.93  ? 1078 SER   A CB    1 
ATOM   6236 O  OG    . SER   A 1 929  ? -27.675 -14.332 -69.071 1.00 91.30  ? 1078 SER   A OG    1 
ATOM   6237 N  N     . ASP   A 1 930  ? -27.635 -16.883 -71.000 1.00 95.26  ? 1079 ASP   A N     1 
ATOM   6238 C  CA    . ASP   A 1 930  ? -28.735 -17.665 -71.631 1.00 94.88  ? 1079 ASP   A CA    1 
ATOM   6239 C  C     . ASP   A 1 930  ? -30.057 -17.386 -70.902 1.00 95.09  ? 1079 ASP   A C     1 
ATOM   6240 O  O     . ASP   A 1 930  ? -31.084 -17.948 -71.334 1.00 98.95  ? 1079 ASP   A O     1 
ATOM   6241 C  CB    . ASP   A 1 930  ? -28.409 -19.164 -71.669 1.00 93.96  ? 1079 ASP   A CB    1 
ATOM   6242 C  CG    . ASP   A 1 930  ? -28.507 -19.890 -70.335 1.00 93.84  ? 1079 ASP   A CG    1 
ATOM   6243 O  OD1   . ASP   A 1 930  ? -28.977 -19.278 -69.354 1.00 93.60  ? 1079 ASP   A OD1   1 
ATOM   6244 O  OD2   . ASP   A 1 930  ? -28.113 -21.074 -70.290 1.00 92.65  ? 1079 ASP   A OD2   1 
ATOM   6245 N  N     . GLY   A 1 931  ? -30.031 -16.564 -69.844 1.00 92.43  ? 1080 GLY   A N     1 
ATOM   6246 C  CA    . GLY   A 1 931  ? -31.210 -16.202 -69.031 1.00 91.64  ? 1080 GLY   A CA    1 
ATOM   6247 C  C     . GLY   A 1 931  ? -31.095 -16.701 -67.600 1.00 91.61  ? 1080 GLY   A C     1 
ATOM   6248 O  O     . GLY   A 1 931  ? -31.530 -15.969 -66.689 1.00 89.81  ? 1080 GLY   A O     1 
ATOM   6249 N  N     . GLN   A 1 932  ? -30.544 -17.905 -67.410 1.00 93.79  ? 1081 GLN   A N     1 
ATOM   6250 C  CA    . GLN   A 1 932  ? -30.348 -18.558 -66.085 1.00 96.72  ? 1081 GLN   A CA    1 
ATOM   6251 C  C     . GLN   A 1 932  ? -28.855 -18.591 -65.735 1.00 97.15  ? 1081 GLN   A C     1 
ATOM   6252 O  O     . GLN   A 1 932  ? -28.503 -18.186 -64.607 1.00 98.68  ? 1081 GLN   A O     1 
ATOM   6253 C  CB    . GLN   A 1 932  ? -30.917 -19.980 -66.098 1.00 97.58  ? 1081 GLN   A CB    1 
ATOM   6254 C  CG    . GLN   A 1 932  ? -32.427 -20.044 -66.283 1.00 97.08  ? 1081 GLN   A CG    1 
ATOM   6255 C  CD    . GLN   A 1 932  ? -33.175 -19.440 -65.119 1.00 96.20  ? 1081 GLN   A CD    1 
ATOM   6256 O  OE1   . GLN   A 1 932  ? -33.334 -18.225 -65.023 1.00 94.86  ? 1081 GLN   A OE1   1 
ATOM   6257 N  NE2   . GLN   A 1 932  ? -33.650 -20.292 -64.224 1.00 96.04  ? 1081 GLN   A NE2   1 
ATOM   6258 N  N     . ILE   A 1 933  ? -28.023 -19.074 -66.664 1.00 94.55  ? 1082 ILE   A N     1 
ATOM   6259 C  CA    . ILE   A 1 933  ? -26.547 -19.231 -66.502 1.00 93.83  ? 1082 ILE   A CA    1 
ATOM   6260 C  C     . ILE   A 1 933  ? -25.845 -18.104 -67.270 1.00 92.56  ? 1082 ILE   A C     1 
ATOM   6261 O  O     . ILE   A 1 933  ? -26.402 -17.652 -68.290 1.00 95.10  ? 1082 ILE   A O     1 
ATOM   6262 C  CB    . ILE   A 1 933  ? -26.096 -20.626 -66.988 1.00 94.93  ? 1082 ILE   A CB    1 
ATOM   6263 C  CG1   . ILE   A 1 933  ? -26.939 -21.751 -66.375 1.00 96.20  ? 1082 ILE   A CG1   1 
ATOM   6264 C  CG2   . ILE   A 1 933  ? -24.610 -20.840 -66.742 1.00 95.01  ? 1082 ILE   A CG2   1 
ATOM   6265 C  CD1   . ILE   A 1 933  ? -26.986 -21.746 -64.861 1.00 95.81  ? 1082 ILE   A CD1   1 
ATOM   6266 N  N     . VAL   A 1 934  ? -24.675 -17.671 -66.786 1.00 90.12  ? 1083 VAL   A N     1 
ATOM   6267 C  CA    . VAL   A 1 934  ? -23.757 -16.720 -67.486 1.00 86.93  ? 1083 VAL   A CA    1 
ATOM   6268 C  C     . VAL   A 1 934  ? -22.403 -17.415 -67.673 1.00 83.70  ? 1083 VAL   A C     1 
ATOM   6269 O  O     . VAL   A 1 934  ? -22.042 -18.234 -66.809 1.00 80.20  ? 1083 VAL   A O     1 
ATOM   6270 C  CB    . VAL   A 1 934  ? -23.610 -15.380 -66.737 1.00 87.37  ? 1083 VAL   A CB    1 
ATOM   6271 C  CG1   . VAL   A 1 934  ? -24.892 -14.566 -66.781 1.00 87.69  ? 1083 VAL   A CG1   1 
ATOM   6272 C  CG2   . VAL   A 1 934  ? -23.150 -15.562 -65.299 1.00 88.56  ? 1083 VAL   A CG2   1 
ATOM   6273 N  N     . LEU   A 1 935  ? -21.700 -17.101 -68.767 1.00 83.28  ? 1084 LEU   A N     1 
ATOM   6274 C  CA    . LEU   A 1 935  ? -20.391 -17.701 -69.143 1.00 83.81  ? 1084 LEU   A CA    1 
ATOM   6275 C  C     . LEU   A 1 935  ? -19.312 -16.611 -69.098 1.00 82.92  ? 1084 LEU   A C     1 
ATOM   6276 O  O     . LEU   A 1 935  ? -19.287 -15.764 -70.014 1.00 81.65  ? 1084 LEU   A O     1 
ATOM   6277 C  CB    . LEU   A 1 935  ? -20.507 -18.322 -70.540 1.00 85.36  ? 1084 LEU   A CB    1 
ATOM   6278 C  CG    . LEU   A 1 935  ? -19.256 -19.024 -71.072 1.00 85.80  ? 1084 LEU   A CG    1 
ATOM   6279 C  CD1   . LEU   A 1 935  ? -18.900 -20.236 -70.223 1.00 85.30  ? 1084 LEU   A CD1   1 
ATOM   6280 C  CD2   . LEU   A 1 935  ? -19.443 -19.435 -72.525 1.00 86.21  ? 1084 LEU   A CD2   1 
ATOM   6281 N  N     . VAL   A 1 936  ? -18.460 -16.647 -68.069 1.00 82.07  ? 1085 VAL   A N     1 
ATOM   6282 C  CA    . VAL   A 1 936  ? -17.361 -15.664 -67.835 1.00 81.20  ? 1085 VAL   A CA    1 
ATOM   6283 C  C     . VAL   A 1 936  ? -16.114 -16.144 -68.588 1.00 81.07  ? 1085 VAL   A C     1 
ATOM   6284 O  O     . VAL   A 1 936  ? -15.525 -17.154 -68.158 1.00 80.27  ? 1085 VAL   A O     1 
ATOM   6285 C  CB    . VAL   A 1 936  ? -17.085 -15.484 -66.328 1.00 80.53  ? 1085 VAL   A CB    1 
ATOM   6286 C  CG1   . VAL   A 1 936  ? -16.000 -14.449 -66.069 1.00 80.14  ? 1085 VAL   A CG1   1 
ATOM   6287 C  CG2   . VAL   A 1 936  ? -18.353 -15.134 -65.558 1.00 79.15  ? 1085 VAL   A CG2   1 
ATOM   6288 N  N     . ASP   A 1 937  ? -15.759 -15.458 -69.682 1.00 83.29  ? 1086 ASP   A N     1 
ATOM   6289 C  CA    . ASP   A 1 937  ? -14.530 -15.680 -70.496 1.00 85.35  ? 1086 ASP   A CA    1 
ATOM   6290 C  C     . ASP   A 1 937  ? -14.380 -17.167 -70.854 1.00 86.96  ? 1086 ASP   A C     1 
ATOM   6291 O  O     . ASP   A 1 937  ? -13.244 -17.679 -70.782 1.00 82.92  ? 1086 ASP   A O     1 
ATOM   6292 C  CB    . ASP   A 1 937  ? -13.288 -15.144 -69.774 1.00 85.48  ? 1086 ASP   A CB    1 
ATOM   6293 C  CG    . ASP   A 1 937  ? -13.254 -13.632 -69.627 1.00 85.80  ? 1086 ASP   A CG    1 
ATOM   6294 O  OD1   . ASP   A 1 937  ? -13.769 -12.938 -70.529 1.00 85.90  ? 1086 ASP   A OD1   1 
ATOM   6295 O  OD2   . ASP   A 1 937  ? -12.706 -13.157 -68.612 1.00 84.22  ? 1086 ASP   A OD2   1 
ATOM   6296 N  N     . ASP   A 1 938  ? -15.486 -17.822 -71.230 1.00 92.29  ? 1087 ASP   A N     1 
ATOM   6297 C  CA    . ASP   A 1 938  ? -15.538 -19.200 -71.796 1.00 95.48  ? 1087 ASP   A CA    1 
ATOM   6298 C  C     . ASP   A 1 938  ? -14.653 -20.162 -70.986 1.00 94.21  ? 1087 ASP   A C     1 
ATOM   6299 O  O     . ASP   A 1 938  ? -13.934 -20.964 -71.619 1.00 93.86  ? 1087 ASP   A O     1 
ATOM   6300 C  CB    . ASP   A 1 938  ? -15.109 -19.207 -73.269 1.00 98.47  ? 1087 ASP   A CB    1 
ATOM   6301 C  CG    . ASP   A 1 938  ? -15.849 -18.218 -74.157 1.00 101.06 ? 1087 ASP   A CG    1 
ATOM   6302 O  OD1   . ASP   A 1 938  ? -17.089 -18.137 -74.046 1.00 104.29 ? 1087 ASP   A OD1   1 
ATOM   6303 O  OD2   . ASP   A 1 938  ? -15.176 -17.541 -74.960 1.00 100.34 ? 1087 ASP   A OD2   1 
ATOM   6304 N  N     . TRP   A 1 939  ? -14.699 -20.101 -69.650 1.00 93.53  ? 1088 TRP   A N     1 
ATOM   6305 C  CA    . TRP   A 1 939  ? -13.892 -20.987 -68.762 1.00 93.48  ? 1088 TRP   A CA    1 
ATOM   6306 C  C     . TRP   A 1 939  ? -14.646 -21.347 -67.473 1.00 89.89  ? 1088 TRP   A C     1 
ATOM   6307 O  O     . TRP   A 1 939  ? -14.432 -22.475 -66.987 1.00 89.88  ? 1088 TRP   A O     1 
ATOM   6308 C  CB    . TRP   A 1 939  ? -12.514 -20.369 -68.476 1.00 97.36  ? 1088 TRP   A CB    1 
ATOM   6309 C  CG    . TRP   A 1 939  ? -12.481 -19.370 -67.360 1.00 100.35 ? 1088 TRP   A CG    1 
ATOM   6310 C  CD1   . TRP   A 1 939  ? -12.631 -18.018 -67.462 1.00 101.44 ? 1088 TRP   A CD1   1 
ATOM   6311 C  CD2   . TRP   A 1 939  ? -12.262 -19.643 -65.964 1.00 102.36 ? 1088 TRP   A CD2   1 
ATOM   6312 N  NE1   . TRP   A 1 939  ? -12.534 -17.432 -66.229 1.00 102.72 ? 1088 TRP   A NE1   1 
ATOM   6313 C  CE2   . TRP   A 1 939  ? -12.309 -18.403 -65.289 1.00 103.27 ? 1088 TRP   A CE2   1 
ATOM   6314 C  CE3   . TRP   A 1 939  ? -12.039 -20.808 -65.219 1.00 102.44 ? 1088 TRP   A CE3   1 
ATOM   6315 C  CZ2   . TRP   A 1 939  ? -12.141 -18.300 -63.909 1.00 103.25 ? 1088 TRP   A CZ2   1 
ATOM   6316 C  CZ3   . TRP   A 1 939  ? -11.874 -20.705 -63.855 1.00 103.43 ? 1088 TRP   A CZ3   1 
ATOM   6317 C  CH2   . TRP   A 1 939  ? -11.925 -19.467 -63.211 1.00 104.06 ? 1088 TRP   A CH2   1 
ATOM   6318 N  N     . ILE   A 1 940  ? -15.468 -20.444 -66.922 1.00 86.94  ? 1089 ILE   A N     1 
ATOM   6319 C  CA    . ILE   A 1 940  ? -16.302 -20.723 -65.711 1.00 87.48  ? 1089 ILE   A CA    1 
ATOM   6320 C  C     . ILE   A 1 940  ? -17.687 -20.089 -65.879 1.00 85.92  ? 1089 ILE   A C     1 
ATOM   6321 O  O     . ILE   A 1 940  ? -17.784 -19.020 -66.517 1.00 82.87  ? 1089 ILE   A O     1 
ATOM   6322 C  CB    . ILE   A 1 940  ? -15.602 -20.249 -64.420 1.00 88.59  ? 1089 ILE   A CB    1 
ATOM   6323 C  CG1   . ILE   A 1 940  ? -16.239 -20.860 -63.167 1.00 89.72  ? 1089 ILE   A CG1   1 
ATOM   6324 C  CG2   . ILE   A 1 940  ? -15.556 -18.729 -64.342 1.00 87.65  ? 1089 ILE   A CG2   1 
ATOM   6325 C  CD1   . ILE   A 1 940  ? -16.116 -22.367 -63.077 1.00 89.59  ? 1089 ILE   A CD1   1 
ATOM   6326 N  N     . ARG   A 1 941  ? -18.706 -20.739 -65.305 1.00 85.52  ? 1090 ARG   A N     1 
ATOM   6327 C  CA    . ARG   A 1 941  ? -20.138 -20.356 -65.405 1.00 86.62  ? 1090 ARG   A CA    1 
ATOM   6328 C  C     . ARG   A 1 941  ? -20.677 -20.016 -64.013 1.00 83.64  ? 1090 ARG   A C     1 
ATOM   6329 O  O     . ARG   A 1 941  ? -20.267 -20.681 -63.043 1.00 84.85  ? 1090 ARG   A O     1 
ATOM   6330 C  CB    . ARG   A 1 941  ? -20.948 -21.500 -66.024 1.00 89.45  ? 1090 ARG   A CB    1 
ATOM   6331 C  CG    . ARG   A 1 941  ? -20.481 -21.909 -67.413 1.00 92.29  ? 1090 ARG   A CG    1 
ATOM   6332 C  CD    . ARG   A 1 941  ? -21.481 -22.790 -68.137 1.00 94.39  ? 1090 ARG   A CD    1 
ATOM   6333 N  NE    . ARG   A 1 941  ? -21.773 -24.017 -67.407 1.00 96.70  ? 1090 ARG   A NE    1 
ATOM   6334 C  CZ    . ARG   A 1 941  ? -20.975 -25.082 -67.342 1.00 98.14  ? 1090 ARG   A CZ    1 
ATOM   6335 N  NH1   . ARG   A 1 941  ? -19.805 -25.092 -67.963 1.00 98.64  ? 1090 ARG   A NH1   1 
ATOM   6336 N  NH2   . ARG   A 1 941  ? -21.352 -26.141 -66.646 1.00 98.02  ? 1090 ARG   A NH2   1 
ATOM   6337 N  N     . LEU   A 1 942  ? -21.567 -19.021 -63.934 1.00 81.47  ? 1091 LEU   A N     1 
ATOM   6338 C  CA    . LEU   A 1 942  ? -22.289 -18.623 -62.696 1.00 82.04  ? 1091 LEU   A CA    1 
ATOM   6339 C  C     . LEU   A 1 942  ? -23.795 -18.779 -62.931 1.00 82.97  ? 1091 LEU   A C     1 
ATOM   6340 O  O     . LEU   A 1 942  ? -24.235 -18.582 -64.080 1.00 82.46  ? 1091 LEU   A O     1 
ATOM   6341 C  CB    . LEU   A 1 942  ? -21.945 -17.172 -62.339 1.00 81.04  ? 1091 LEU   A CB    1 
ATOM   6342 C  CG    . LEU   A 1 942  ? -20.460 -16.810 -62.341 1.00 79.97  ? 1091 LEU   A CG    1 
ATOM   6343 C  CD1   . LEU   A 1 942  ? -20.271 -15.302 -62.281 1.00 79.37  ? 1091 LEU   A CD1   1 
ATOM   6344 C  CD2   . LEU   A 1 942  ? -19.734 -17.487 -61.190 1.00 79.78  ? 1091 LEU   A CD2   1 
ATOM   6345 N  N     . GLN   A 1 943  ? -24.543 -19.129 -61.881 1.00 85.43  ? 1092 GLN   A N     1 
ATOM   6346 C  CA    . GLN   A 1 943  ? -26.030 -19.124 -61.858 1.00 87.55  ? 1092 GLN   A CA    1 
ATOM   6347 C  C     . GLN   A 1 943  ? -26.483 -17.851 -61.133 1.00 86.99  ? 1092 GLN   A C     1 
ATOM   6348 O  O     . GLN   A 1 943  ? -26.607 -17.882 -59.891 1.00 85.68  ? 1092 GLN   A O     1 
ATOM   6349 C  CB    . GLN   A 1 943  ? -26.563 -20.396 -61.194 1.00 90.32  ? 1092 GLN   A CB    1 
ATOM   6350 C  CG    . GLN   A 1 943  ? -28.082 -20.510 -61.206 1.00 91.46  ? 1092 GLN   A CG    1 
ATOM   6351 C  CD    . GLN   A 1 943  ? -28.580 -21.641 -60.340 1.00 92.44  ? 1092 GLN   A CD    1 
ATOM   6352 O  OE1   . GLN   A 1 943  ? -27.850 -22.580 -60.028 1.00 92.36  ? 1092 GLN   A OE1   1 
ATOM   6353 N  NE2   . GLN   A 1 943  ? -29.840 -21.560 -59.942 1.00 93.15  ? 1092 GLN   A NE2   1 
ATOM   6354 N  N     . ILE   A 1 944  ? -26.689 -16.770 -61.891 1.00 87.36  ? 1093 ILE   A N     1 
ATOM   6355 C  CA    . ILE   A 1 944  ? -27.082 -15.425 -61.374 1.00 87.90  ? 1093 ILE   A CA    1 
ATOM   6356 C  C     . ILE   A 1 944  ? -28.121 -14.819 -62.323 1.00 84.26  ? 1093 ILE   A C     1 
ATOM   6357 O  O     . ILE   A 1 944  ? -28.055 -15.105 -63.536 1.00 83.45  ? 1093 ILE   A O     1 
ATOM   6358 C  CB    . ILE   A 1 944  ? -25.846 -14.514 -61.208 1.00 90.82  ? 1093 ILE   A CB    1 
ATOM   6359 C  CG1   . ILE   A 1 944  ? -26.211 -13.180 -60.550 1.00 93.81  ? 1093 ILE   A CG1   1 
ATOM   6360 C  CG2   . ILE   A 1 944  ? -25.125 -14.307 -62.534 1.00 89.58  ? 1093 ILE   A CG2   1 
ATOM   6361 C  CD1   . ILE   A 1 944  ? -25.020 -12.391 -60.059 1.00 96.04  ? 1093 ILE   A CD1   1 
ATOM   6362 N  N     . SER   A 1 945  ? -29.041 -14.016 -61.781 1.00 82.28  ? 1094 SER   A N     1 
ATOM   6363 C  CA    . SER   A 1 945  ? -30.093 -13.295 -62.543 1.00 83.43  ? 1094 SER   A CA    1 
ATOM   6364 C  C     . SER   A 1 945  ? -29.435 -12.492 -63.671 1.00 83.76  ? 1094 SER   A C     1 
ATOM   6365 O  O     . SER   A 1 945  ? -28.475 -11.752 -63.381 1.00 83.57  ? 1094 SER   A O     1 
ATOM   6366 C  CB    . SER   A 1 945  ? -30.910 -12.404 -61.645 1.00 83.74  ? 1094 SER   A CB    1 
ATOM   6367 O  OG    . SER   A 1 945  ? -30.186 -11.231 -61.301 1.00 83.99  ? 1094 SER   A OG    1 
ATOM   6368 N  N     . HIS   A 1 946  ? -29.928 -12.648 -64.903 1.00 84.90  ? 1095 HIS   A N     1 
ATOM   6369 C  CA    . HIS   A 1 946  ? -29.473 -11.906 -66.110 1.00 86.13  ? 1095 HIS   A CA    1 
ATOM   6370 C  C     . HIS   A 1 946  ? -29.426 -10.400 -65.812 1.00 84.97  ? 1095 HIS   A C     1 
ATOM   6371 O  O     . HIS   A 1 946  ? -28.485 -9.735  -66.289 1.00 83.80  ? 1095 HIS   A O     1 
ATOM   6372 C  CB    . HIS   A 1 946  ? -30.377 -12.236 -67.309 1.00 85.75  ? 1095 HIS   A CB    1 
ATOM   6373 C  CG    . HIS   A 1 946  ? -30.090 -11.428 -68.530 1.00 84.59  ? 1095 HIS   A CG    1 
ATOM   6374 N  ND1   . HIS   A 1 946  ? -29.265 -11.883 -69.541 1.00 84.40  ? 1095 HIS   A ND1   1 
ATOM   6375 C  CD2   . HIS   A 1 946  ? -30.510 -10.200 -68.907 1.00 83.68  ? 1095 HIS   A CD2   1 
ATOM   6376 C  CE1   . HIS   A 1 946  ? -29.192 -10.970 -70.489 1.00 84.52  ? 1095 HIS   A CE1   1 
ATOM   6377 N  NE2   . HIS   A 1 946  ? -29.944 -9.926  -70.123 1.00 84.17  ? 1095 HIS   A NE2   1 
ATOM   6378 N  N     . GLU   A 1 947  ? -30.402 -9.893  -65.049 1.00 84.88  ? 1096 GLU   A N     1 
ATOM   6379 C  CA    . GLU   A 1 947  ? -30.555 -8.452  -64.701 1.00 86.76  ? 1096 GLU   A CA    1 
ATOM   6380 C  C     . GLU   A 1 947  ? -29.307 -7.960  -63.954 1.00 84.70  ? 1096 GLU   A C     1 
ATOM   6381 O  O     . GLU   A 1 947  ? -28.736 -6.936  -64.376 1.00 83.04  ? 1096 GLU   A O     1 
ATOM   6382 C  CB    . GLU   A 1 947  ? -31.817 -8.232  -63.862 1.00 89.67  ? 1096 GLU   A CB    1 
ATOM   6383 C  CG    . GLU   A 1 947  ? -33.085 -8.081  -64.687 1.00 91.69  ? 1096 GLU   A CG    1 
ATOM   6384 C  CD    . GLU   A 1 947  ? -33.412 -9.238  -65.615 1.00 94.86  ? 1096 GLU   A CD    1 
ATOM   6385 O  OE1   . GLU   A 1 947  ? -33.168 -10.399 -65.225 1.00 98.07  ? 1096 GLU   A OE1   1 
ATOM   6386 O  OE2   . GLU   A 1 947  ? -33.912 -8.973  -66.727 1.00 96.93  ? 1096 GLU   A OE2   1 
ATOM   6387 N  N     . ALA   A 1 948  ? -28.905 -8.666  -62.892 1.00 83.34  ? 1097 ALA   A N     1 
ATOM   6388 C  CA    . ALA   A 1 948  ? -27.775 -8.304  -62.002 1.00 80.97  ? 1097 ALA   A CA    1 
ATOM   6389 C  C     . ALA   A 1 948  ? -26.450 -8.368  -62.771 1.00 79.17  ? 1097 ALA   A C     1 
ATOM   6390 O  O     . ALA   A 1 948  ? -25.640 -7.438  -62.613 1.00 81.03  ? 1097 ALA   A O     1 
ATOM   6391 C  CB    . ALA   A 1 948  ? -27.752 -9.211  -60.796 1.00 81.33  ? 1097 ALA   A CB    1 
ATOM   6392 N  N     . ALA   A 1 949  ? -26.244 -9.424  -63.567 1.00 77.76  ? 1098 ALA   A N     1 
ATOM   6393 C  CA    . ALA   A 1 949  ? -24.999 -9.696  -64.327 1.00 77.84  ? 1098 ALA   A CA    1 
ATOM   6394 C  C     . ALA   A 1 949  ? -24.757 -8.599  -65.374 1.00 79.45  ? 1098 ALA   A C     1 
ATOM   6395 O  O     . ALA   A 1 949  ? -23.592 -8.181  -65.529 1.00 82.90  ? 1098 ALA   A O     1 
ATOM   6396 C  CB    . ALA   A 1 949  ? -25.070 -11.061 -64.968 1.00 76.51  ? 1098 ALA   A CB    1 
ATOM   6397 N  N     . ALA   A 1 950  ? -25.811 -8.158  -66.070 1.00 78.99  ? 1099 ALA   A N     1 
ATOM   6398 C  CA    . ALA   A 1 950  ? -25.752 -7.123  -67.130 1.00 79.74  ? 1099 ALA   A CA    1 
ATOM   6399 C  C     . ALA   A 1 950  ? -25.574 -5.737  -66.499 1.00 80.27  ? 1099 ALA   A C     1 
ATOM   6400 O  O     . ALA   A 1 950  ? -24.954 -4.871  -67.149 1.00 82.44  ? 1099 ALA   A O     1 
ATOM   6401 C  CB    . ALA   A 1 950  ? -26.994 -7.182  -67.985 1.00 80.72  ? 1099 ALA   A CB    1 
ATOM   6402 N  N     . CYS   A 1 951  ? -26.107 -5.540  -65.287 1.00 79.49  ? 1100 CYS   A N     1 
ATOM   6403 C  CA    . CYS   A 1 951  ? -26.001 -4.282  -64.497 1.00 79.75  ? 1100 CYS   A CA    1 
ATOM   6404 C  C     . CYS   A 1 951  ? -24.569 -4.113  -63.974 1.00 80.80  ? 1100 CYS   A C     1 
ATOM   6405 O  O     . CYS   A 1 951  ? -24.025 -2.998  -64.098 1.00 82.49  ? 1100 CYS   A O     1 
ATOM   6406 C  CB    . CYS   A 1 951  ? -26.988 -4.264  -63.335 1.00 80.00  ? 1100 CYS   A CB    1 
ATOM   6407 S  SG    . CYS   A 1 951  ? -28.700 -3.957  -63.845 1.00 80.62  ? 1100 CYS   A SG    1 
ATOM   6408 N  N     . ILE   A 1 952  ? -23.986 -5.179  -63.413 1.00 79.34  ? 1101 ILE   A N     1 
ATOM   6409 C  CA    . ILE   A 1 952  ? -22.578 -5.213  -62.913 1.00 77.33  ? 1101 ILE   A CA    1 
ATOM   6410 C  C     . ILE   A 1 952  ? -21.629 -4.970  -64.094 1.00 78.21  ? 1101 ILE   A C     1 
ATOM   6411 O  O     . ILE   A 1 952  ? -20.596 -4.302  -63.893 1.00 81.19  ? 1101 ILE   A O     1 
ATOM   6412 C  CB    . ILE   A 1 952  ? -22.285 -6.541  -62.184 1.00 75.28  ? 1101 ILE   A CB    1 
ATOM   6413 C  CG1   . ILE   A 1 952  ? -23.041 -6.620  -60.854 1.00 74.49  ? 1101 ILE   A CG1   1 
ATOM   6414 C  CG2   . ILE   A 1 952  ? -20.788 -6.745  -61.990 1.00 75.57  ? 1101 ILE   A CG2   1 
ATOM   6415 C  CD1   . ILE   A 1 952  ? -23.184 -8.019  -60.307 1.00 74.47  ? 1101 ILE   A CD1   1 
ATOM   6416 N  N     . THR   A 1 953  ? -21.977 -5.486  -65.275 1.00 77.56  ? 1102 THR   A N     1 
ATOM   6417 C  CA    . THR   A 1 953  ? -21.222 -5.304  -66.544 1.00 78.19  ? 1102 THR   A CA    1 
ATOM   6418 C  C     . THR   A 1 953  ? -21.336 -3.849  -67.018 1.00 76.28  ? 1102 THR   A C     1 
ATOM   6419 O  O     . THR   A 1 953  ? -20.382 -3.371  -67.666 1.00 76.11  ? 1102 THR   A O     1 
ATOM   6420 C  CB    . THR   A 1 953  ? -21.715 -6.281  -67.618 1.00 80.32  ? 1102 THR   A CB    1 
ATOM   6421 O  OG1   . THR   A 1 953  ? -21.569 -7.605  -67.101 1.00 80.55  ? 1102 THR   A OG1   1 
ATOM   6422 C  CG2   . THR   A 1 953  ? -20.963 -6.144  -68.924 1.00 81.49  ? 1102 THR   A CG2   1 
ATOM   6423 N  N     . ALA   A 1 954  ? -22.459 -3.185  -66.723 1.00 73.47  ? 1103 ALA   A N     1 
ATOM   6424 C  CA    . ALA   A 1 954  ? -22.741 -1.777  -67.095 1.00 73.11  ? 1103 ALA   A CA    1 
ATOM   6425 C  C     . ALA   A 1 954  ? -21.964 -0.822  -66.179 1.00 71.54  ? 1103 ALA   A C     1 
ATOM   6426 O  O     . ALA   A 1 954  ? -21.490 0.216   -66.681 1.00 71.11  ? 1103 ALA   A O     1 
ATOM   6427 C  CB    . ALA   A 1 954  ? -24.226 -1.510  -67.037 1.00 74.31  ? 1103 ALA   A CB    1 
ATOM   6428 N  N     . LEU   A 1 955  ? -21.853 -1.150  -64.887 1.00 70.00  ? 1104 LEU   A N     1 
ATOM   6429 C  CA    . LEU   A 1 955  ? -21.055 -0.376  -63.897 1.00 68.48  ? 1104 LEU   A CA    1 
ATOM   6430 C  C     . LEU   A 1 955  ? -19.601 -0.297  -64.376 1.00 70.34  ? 1104 LEU   A C     1 
ATOM   6431 O  O     . LEU   A 1 955  ? -19.020 0.805   -64.306 1.00 72.01  ? 1104 LEU   A O     1 
ATOM   6432 C  CB    . LEU   A 1 955  ? -21.140 -1.043  -62.519 1.00 66.22  ? 1104 LEU   A CB    1 
ATOM   6433 C  CG    . LEU   A 1 955  ? -22.389 -0.722  -61.699 1.00 64.63  ? 1104 LEU   A CG    1 
ATOM   6434 C  CD1   . LEU   A 1 955  ? -22.478 -1.625  -60.480 1.00 64.70  ? 1104 LEU   A CD1   1 
ATOM   6435 C  CD2   . LEU   A 1 955  ? -22.408 0.740   -61.278 1.00 63.88  ? 1104 LEU   A CD2   1 
ATOM   6436 N  N     . ARG   A 1 956  ? -19.046 -1.423  -64.841 1.00 70.01  ? 1105 ARG   A N     1 
ATOM   6437 C  CA    . ARG   A 1 956  ? -17.660 -1.525  -65.375 1.00 70.66  ? 1105 ARG   A CA    1 
ATOM   6438 C  C     . ARG   A 1 956  ? -17.461 -0.463  -66.462 1.00 70.30  ? 1105 ARG   A C     1 
ATOM   6439 O  O     . ARG   A 1 956  ? -16.436 0.240   -66.412 1.00 72.70  ? 1105 ARG   A O     1 
ATOM   6440 C  CB    . ARG   A 1 956  ? -17.394 -2.926  -65.933 1.00 73.38  ? 1105 ARG   A CB    1 
ATOM   6441 C  CG    . ARG   A 1 956  ? -15.934 -3.198  -66.269 1.00 77.73  ? 1105 ARG   A CG    1 
ATOM   6442 C  CD    . ARG   A 1 956  ? -15.770 -4.377  -67.211 1.00 82.18  ? 1105 ARG   A CD    1 
ATOM   6443 N  NE    . ARG   A 1 956  ? -16.444 -5.582  -66.739 1.00 86.09  ? 1105 ARG   A NE    1 
ATOM   6444 C  CZ    . ARG   A 1 956  ? -16.629 -6.686  -67.461 1.00 89.15  ? 1105 ARG   A CZ    1 
ATOM   6445 N  NH1   . ARG   A 1 956  ? -16.192 -6.755  -68.709 1.00 89.97  ? 1105 ARG   A NH1   1 
ATOM   6446 N  NH2   . ARG   A 1 956  ? -17.259 -7.722  -66.932 1.00 89.33  ? 1105 ARG   A NH2   1 
ATOM   6447 N  N     . ALA   A 1 957  ? -18.409 -0.354  -67.399 1.00 68.90  ? 1106 ALA   A N     1 
ATOM   6448 C  CA    . ALA   A 1 957  ? -18.389 0.609   -68.526 1.00 70.04  ? 1106 ALA   A CA    1 
ATOM   6449 C  C     . ALA   A 1 957  ? -18.572 2.034   -67.991 1.00 69.18  ? 1106 ALA   A C     1 
ATOM   6450 O  O     . ALA   A 1 957  ? -17.887 2.950   -68.494 1.00 69.31  ? 1106 ALA   A O     1 
ATOM   6451 C  CB    . ALA   A 1 957  ? -19.461 0.259   -69.529 1.00 72.00  ? 1106 ALA   A CB    1 
ATOM   6452 N  N     . ALA   A 1 958  ? -19.474 2.206   -67.019 1.00 68.08  ? 1107 ALA   A N     1 
ATOM   6453 C  CA    . ALA   A 1 958  ? -19.748 3.485   -66.322 1.00 67.26  ? 1107 ALA   A CA    1 
ATOM   6454 C  C     . ALA   A 1 958  ? -18.468 3.977   -65.638 1.00 65.98  ? 1107 ALA   A C     1 
ATOM   6455 O  O     . ALA   A 1 958  ? -18.216 5.199   -65.666 1.00 65.49  ? 1107 ALA   A O     1 
ATOM   6456 C  CB    . ALA   A 1 958  ? -20.869 3.305   -65.326 1.00 67.48  ? 1107 ALA   A CB    1 
ATOM   6457 N  N     . MET   A 1 959  ? -17.702 3.049   -65.054 1.00 64.77  ? 1108 MET   A N     1 
ATOM   6458 C  CA    . MET   A 1 959  ? -16.436 3.321   -64.322 1.00 65.64  ? 1108 MET   A CA    1 
ATOM   6459 C  C     . MET   A 1 959  ? -15.351 3.742   -65.320 1.00 67.05  ? 1108 MET   A C     1 
ATOM   6460 O  O     . MET   A 1 959  ? -14.670 4.752   -65.055 1.00 68.70  ? 1108 MET   A O     1 
ATOM   6461 C  CB    . MET   A 1 959  ? -15.974 2.078   -63.552 1.00 65.58  ? 1108 MET   A CB    1 
ATOM   6462 C  CG    . MET   A 1 959  ? -14.803 2.332   -62.620 1.00 65.35  ? 1108 MET   A CG    1 
ATOM   6463 S  SD    . MET   A 1 959  ? -15.183 3.531   -61.319 1.00 64.60  ? 1108 MET   A SD    1 
ATOM   6464 C  CE    . MET   A 1 959  ? -13.538 3.851   -60.683 1.00 65.52  ? 1108 MET   A CE    1 
ATOM   6465 N  N     . GLU   A 1 960  ? -15.197 2.992   -66.416 1.00 68.35  ? 1109 GLU   A N     1 
ATOM   6466 C  CA    . GLU   A 1 960  ? -14.238 3.292   -67.515 1.00 70.55  ? 1109 GLU   A CA    1 
ATOM   6467 C  C     . GLU   A 1 960  ? -14.482 4.719   -68.018 1.00 70.40  ? 1109 GLU   A C     1 
ATOM   6468 O  O     . GLU   A 1 960  ? -13.497 5.467   -68.166 1.00 72.12  ? 1109 GLU   A O     1 
ATOM   6469 C  CB    . GLU   A 1 960  ? -14.385 2.283   -68.657 1.00 73.97  ? 1109 GLU   A CB    1 
ATOM   6470 C  CG    . GLU   A 1 960  ? -13.754 0.931   -68.365 1.00 76.83  ? 1109 GLU   A CG    1 
ATOM   6471 C  CD    . GLU   A 1 960  ? -12.236 0.911   -68.406 1.00 79.93  ? 1109 GLU   A CD    1 
ATOM   6472 O  OE1   . GLU   A 1 960  ? -11.640 1.956   -68.746 1.00 81.56  ? 1109 GLU   A OE1   1 
ATOM   6473 O  OE2   . GLU   A 1 960  ? -11.651 -0.149  -68.098 1.00 81.80  ? 1109 GLU   A OE2   1 
ATOM   6474 N  N     . ALA   A 1 961  ? -15.749 5.072   -68.259 1.00 69.57  ? 1110 ALA   A N     1 
ATOM   6475 C  CA    . ALA   A 1 961  ? -16.189 6.410   -68.723 1.00 67.54  ? 1110 ALA   A CA    1 
ATOM   6476 C  C     . ALA   A 1 961  ? -15.758 7.476   -67.709 1.00 65.71  ? 1110 ALA   A C     1 
ATOM   6477 O  O     . ALA   A 1 961  ? -15.261 8.531   -68.144 1.00 65.21  ? 1110 ALA   A O     1 
ATOM   6478 C  CB    . ALA   A 1 961  ? -17.683 6.422   -68.935 1.00 67.82  ? 1110 ALA   A CB    1 
ATOM   6479 N  N     . LEU   A 1 962  ? -15.939 7.203   -66.411 1.00 64.69  ? 1111 LEU   A N     1 
ATOM   6480 C  CA    . LEU   A 1 962  ? -15.566 8.127   -65.304 1.00 63.67  ? 1111 LEU   A CA    1 
ATOM   6481 C  C     . LEU   A 1 962  ? -14.040 8.270   -65.254 1.00 63.43  ? 1111 LEU   A C     1 
ATOM   6482 O  O     . LEU   A 1 962  ? -13.565 9.409   -65.081 1.00 63.66  ? 1111 LEU   A O     1 
ATOM   6483 C  CB    . LEU   A 1 962  ? -16.122 7.605   -63.974 1.00 61.98  ? 1111 LEU   A CB    1 
ATOM   6484 C  CG    . LEU   A 1 962  ? -15.760 8.427   -62.734 1.00 61.07  ? 1111 LEU   A CG    1 
ATOM   6485 C  CD1   . LEU   A 1 962  ? -16.145 9.889   -62.906 1.00 59.22  ? 1111 LEU   A CD1   1 
ATOM   6486 C  CD2   . LEU   A 1 962  ? -16.417 7.849   -61.489 1.00 61.54  ? 1111 LEU   A CD2   1 
ATOM   6487 N  N     . VAL   A 1 963  ? -13.307 7.160   -65.398 1.00 63.49  ? 1112 VAL   A N     1 
ATOM   6488 C  CA    . VAL   A 1 963  ? -11.813 7.141   -65.404 1.00 63.98  ? 1112 VAL   A CA    1 
ATOM   6489 C  C     . VAL   A 1 963  ? -11.318 8.073   -66.518 1.00 64.82  ? 1112 VAL   A C     1 
ATOM   6490 O  O     . VAL   A 1 963  ? -10.381 8.849   -66.256 1.00 63.79  ? 1112 VAL   A O     1 
ATOM   6491 C  CB    . VAL   A 1 963  ? -11.257 5.710   -65.553 1.00 62.65  ? 1112 VAL   A CB    1 
ATOM   6492 C  CG1   . VAL   A 1 963  ? -9.783  5.701   -65.931 1.00 62.59  ? 1112 VAL   A CG1   1 
ATOM   6493 C  CG2   . VAL   A 1 963  ? -11.484 4.891   -64.292 1.00 62.26  ? 1112 VAL   A CG2   1 
ATOM   6494 N  N     . VAL   A 1 964  ? -11.939 8.014   -67.701 1.00 67.05  ? 1113 VAL   A N     1 
ATOM   6495 C  CA    . VAL   A 1 964  ? -11.586 8.870   -68.875 1.00 69.89  ? 1113 VAL   A CA    1 
ATOM   6496 C  C     . VAL   A 1 964  ? -11.852 10.337  -68.513 1.00 71.86  ? 1113 VAL   A C     1 
ATOM   6497 O  O     . VAL   A 1 964  ? -10.935 11.160  -68.688 1.00 72.18  ? 1113 VAL   A O     1 
ATOM   6498 C  CB    . VAL   A 1 964  ? -12.354 8.451   -70.144 1.00 69.59  ? 1113 VAL   A CB    1 
ATOM   6499 C  CG1   . VAL   A 1 964  ? -12.206 9.474   -71.261 1.00 69.16  ? 1113 VAL   A CG1   1 
ATOM   6500 C  CG2   . VAL   A 1 964  ? -11.928 7.072   -70.627 1.00 70.85  ? 1113 VAL   A CG2   1 
ATOM   6501 N  N     . GLU   A 1 965  ? -13.060 10.642  -68.027 1.00 75.45  ? 1114 GLU   A N     1 
ATOM   6502 C  CA    . GLU   A 1 965  ? -13.486 12.009  -67.616 1.00 76.85  ? 1114 GLU   A CA    1 
ATOM   6503 C  C     . GLU   A 1 965  ? -12.550 12.536  -66.521 1.00 74.41  ? 1114 GLU   A C     1 
ATOM   6504 O  O     . GLU   A 1 965  ? -12.161 13.715  -66.604 1.00 74.85  ? 1114 GLU   A O     1 
ATOM   6505 C  CB    . GLU   A 1 965  ? -14.940 12.004  -67.135 1.00 79.86  ? 1114 GLU   A CB    1 
ATOM   6506 C  CG    . GLU   A 1 965  ? -15.954 11.875  -68.259 1.00 83.15  ? 1114 GLU   A CG    1 
ATOM   6507 C  CD    . GLU   A 1 965  ? -15.908 12.987  -69.296 1.00 86.80  ? 1114 GLU   A CD    1 
ATOM   6508 O  OE1   . GLU   A 1 965  ? -15.699 14.156  -68.905 1.00 88.82  ? 1114 GLU   A OE1   1 
ATOM   6509 O  OE2   . GLU   A 1 965  ? -16.070 12.681  -70.496 1.00 87.28  ? 1114 GLU   A OE2   1 
ATOM   6510 N  N     . VAL   A 1 966  ? -12.204 11.692  -65.542 1.00 72.24  ? 1115 VAL   A N     1 
ATOM   6511 C  CA    . VAL   A 1 966  ? -11.341 12.056  -64.377 1.00 71.57  ? 1115 VAL   A CA    1 
ATOM   6512 C  C     . VAL   A 1 966  ? -9.936  12.419  -64.879 1.00 71.35  ? 1115 VAL   A C     1 
ATOM   6513 O  O     . VAL   A 1 966  ? -9.381  13.404  -64.375 1.00 73.35  ? 1115 VAL   A O     1 
ATOM   6514 C  CB    . VAL   A 1 966  ? -11.301 10.932  -63.321 1.00 70.65  ? 1115 VAL   A CB    1 
ATOM   6515 C  CG1   . VAL   A 1 966  ? -10.106 11.057  -62.384 1.00 70.83  ? 1115 VAL   A CG1   1 
ATOM   6516 C  CG2   . VAL   A 1 966  ? -12.593 10.872  -62.522 1.00 70.25  ? 1115 VAL   A CG2   1 
ATOM   6517 N  N     . THR   A 1 967  ? -9.385  11.665  -65.833 1.00 71.37  ? 1116 THR   A N     1 
ATOM   6518 C  CA    . THR   A 1 967  ? -7.986  11.825  -66.318 1.00 72.62  ? 1116 THR   A CA    1 
ATOM   6519 C  C     . THR   A 1 967  ? -7.845  13.121  -67.131 1.00 74.30  ? 1116 THR   A C     1 
ATOM   6520 O  O     . THR   A 1 967  ? -6.707  13.626  -67.221 1.00 74.51  ? 1116 THR   A O     1 
ATOM   6521 C  CB    . THR   A 1 967  ? -7.518  10.588  -67.096 1.00 72.33  ? 1116 THR   A CB    1 
ATOM   6522 O  OG1   . THR   A 1 967  ? -8.553  10.180  -67.992 1.00 72.46  ? 1116 THR   A OG1   1 
ATOM   6523 C  CG2   . THR   A 1 967  ? -7.151  9.440   -66.181 1.00 70.63  ? 1116 THR   A CG2   1 
ATOM   6524 N  N     . LYS   A 1 968  ? -8.942  13.640  -67.694 1.00 77.38  ? 1117 LYS   A N     1 
ATOM   6525 C  CA    . LYS   A 1 968  ? -8.978  14.950  -68.404 1.00 79.35  ? 1117 LYS   A CA    1 
ATOM   6526 C  C     . LYS   A 1 968  ? -8.781  16.088  -67.394 1.00 81.10  ? 1117 LYS   A C     1 
ATOM   6527 O  O     . LYS   A 1 968  ? -8.176  17.109  -67.775 1.00 82.85  ? 1117 LYS   A O     1 
ATOM   6528 C  CB    . LYS   A 1 968  ? -10.301 15.143  -69.152 1.00 79.37  ? 1117 LYS   A CB    1 
ATOM   6529 C  CG    . LYS   A 1 968  ? -10.513 14.243  -70.361 1.00 79.30  ? 1117 LYS   A CG    1 
ATOM   6530 C  CD    . LYS   A 1 968  ? -11.910 14.346  -70.936 1.00 79.43  ? 1117 LYS   A CD    1 
ATOM   6531 C  CE    . LYS   A 1 968  ? -12.196 13.314  -72.006 1.00 79.11  ? 1117 LYS   A CE    1 
ATOM   6532 N  NZ    . LYS   A 1 968  ? -13.643 13.237  -72.316 1.00 78.41  ? 1117 LYS   A NZ    1 
ATOM   6533 N  N     . GLN   A 1 969  ? -9.288  15.919  -66.167 1.00 82.44  ? 1118 GLN   A N     1 
ATOM   6534 C  CA    . GLN   A 1 969  ? -9.209  16.919  -65.067 1.00 84.13  ? 1118 GLN   A CA    1 
ATOM   6535 C  C     . GLN   A 1 969  ? -9.280  16.181  -63.729 1.00 82.00  ? 1118 GLN   A C     1 
ATOM   6536 O  O     . GLN   A 1 969  ? -10.356 16.034  -63.155 1.00 79.65  ? 1118 GLN   A O     1 
ATOM   6537 C  CB    . GLN   A 1 969  ? -10.325 17.953  -65.242 1.00 88.62  ? 1118 GLN   A CB    1 
ATOM   6538 C  CG    . GLN   A 1 969  ? -10.043 19.291  -64.570 1.00 91.50  ? 1118 GLN   A CG    1 
ATOM   6539 C  CD    . GLN   A 1 969  ? -10.962 20.389  -65.051 1.00 93.40  ? 1118 GLN   A CD    1 
ATOM   6540 O  OE1   . GLN   A 1 969  ? -11.916 20.153  -65.791 1.00 93.64  ? 1118 GLN   A OE1   1 
ATOM   6541 N  NE2   . GLN   A 1 969  ? -10.679 21.612  -64.632 1.00 94.19  ? 1118 GLN   A NE2   1 
ATOM   6542 N  N     . PRO   A 1 970  ? -8.142  15.665  -63.205 1.00 81.46  ? 1119 PRO   A N     1 
ATOM   6543 C  CA    . PRO   A 1 970  ? -8.150  14.791  -62.026 1.00 81.45  ? 1119 PRO   A CA    1 
ATOM   6544 C  C     . PRO   A 1 970  ? -8.779  15.354  -60.741 1.00 81.87  ? 1119 PRO   A C     1 
ATOM   6545 O  O     . PRO   A 1 970  ? -9.171  14.559  -59.909 1.00 85.00  ? 1119 PRO   A O     1 
ATOM   6546 C  CB    . PRO   A 1 970  ? -6.657  14.524  -61.772 1.00 81.24  ? 1119 PRO   A CB    1 
ATOM   6547 C  CG    . PRO   A 1 970  ? -6.014  14.707  -63.125 1.00 80.70  ? 1119 PRO   A CG    1 
ATOM   6548 C  CD    . PRO   A 1 970  ? -6.788  15.845  -63.753 1.00 80.63  ? 1119 PRO   A CD    1 
ATOM   6549 N  N     . ASN   A 1 971  ? -8.873  16.681  -60.606 1.00 82.29  ? 1120 ASN   A N     1 
ATOM   6550 C  CA    . ASN   A 1 971  ? -9.344  17.358  -59.365 1.00 83.40  ? 1120 ASN   A CA    1 
ATOM   6551 C  C     . ASN   A 1 971  ? -10.872 17.250  -59.221 1.00 81.30  ? 1120 ASN   A C     1 
ATOM   6552 O  O     . ASN   A 1 971  ? -11.381 17.709  -58.181 1.00 81.59  ? 1120 ASN   A O     1 
ATOM   6553 C  CB    . ASN   A 1 971  ? -8.882  18.818  -59.304 1.00 84.95  ? 1120 ASN   A CB    1 
ATOM   6554 C  CG    . ASN   A 1 971  ? -9.403  19.664  -60.448 1.00 87.20  ? 1120 ASN   A CG    1 
ATOM   6555 O  OD1   . ASN   A 1 971  ? -10.579 20.020  -60.478 1.00 89.04  ? 1120 ASN   A OD1   1 
ATOM   6556 N  ND2   . ASN   A 1 971  ? -8.535  19.997  -61.390 1.00 88.72  ? 1120 ASN   A ND2   1 
ATOM   6557 N  N     . ILE   A 1 972  ? -11.579 16.658  -60.194 1.00 80.12  ? 1121 ILE   A N     1 
ATOM   6558 C  CA    . ILE   A 1 972  ? -13.073 16.577  -60.201 1.00 81.83  ? 1121 ILE   A CA    1 
ATOM   6559 C  C     . ILE   A 1 972  ? -13.552 15.496  -59.222 1.00 82.15  ? 1121 ILE   A C     1 
ATOM   6560 O  O     . ILE   A 1 972  ? -14.768 15.457  -58.959 1.00 82.68  ? 1121 ILE   A O     1 
ATOM   6561 C  CB    . ILE   A 1 972  ? -13.638 16.343  -61.620 1.00 83.73  ? 1121 ILE   A CB    1 
ATOM   6562 C  CG1   . ILE   A 1 972  ? -13.289 14.957  -62.173 1.00 85.18  ? 1121 ILE   A CG1   1 
ATOM   6563 C  CG2   . ILE   A 1 972  ? -13.217 17.458  -62.568 1.00 83.65  ? 1121 ILE   A CG2   1 
ATOM   6564 C  CD1   . ILE   A 1 972  ? -14.202 14.494  -63.287 1.00 85.79  ? 1121 ILE   A CD1   1 
ATOM   6565 N  N     . ILE   A 1 973  ? -12.654 14.650  -58.705 1.00 84.19  ? 1122 ILE   A N     1 
ATOM   6566 C  CA    . ILE   A 1 973  ? -13.010 13.564  -57.740 1.00 86.37  ? 1122 ILE   A CA    1 
ATOM   6567 C  C     . ILE   A 1 973  ? -13.316 14.182  -56.367 1.00 88.95  ? 1122 ILE   A C     1 
ATOM   6568 O  O     . ILE   A 1 973  ? -13.884 13.463  -55.521 1.00 90.06  ? 1122 ILE   A O     1 
ATOM   6569 C  CB    . ILE   A 1 973  ? -11.919 12.473  -57.668 1.00 85.90  ? 1122 ILE   A CB    1 
ATOM   6570 C  CG1   . ILE   A 1 973  ? -10.625 12.966  -57.013 1.00 86.43  ? 1122 ILE   A CG1   1 
ATOM   6571 C  CG2   . ILE   A 1 973  ? -11.659 11.883  -59.046 1.00 85.18  ? 1122 ILE   A CG2   1 
ATOM   6572 C  CD1   . ILE   A 1 973  ? -9.633  11.861  -56.729 1.00 86.41  ? 1122 ILE   A CD1   1 
ATOM   6573 N  N     . SER   A 1 974  ? -12.952 15.456  -56.159 1.00 91.84  ? 1123 SER   A N     1 
ATOM   6574 C  CA    . SER   A 1 974  ? -13.299 16.269  -54.960 1.00 93.11  ? 1123 SER   A CA    1 
ATOM   6575 C  C     . SER   A 1 974  ? -14.822 16.413  -54.853 1.00 96.28  ? 1123 SER   A C     1 
ATOM   6576 O  O     . SER   A 1 974  ? -15.384 15.962  -53.834 1.00 97.51  ? 1123 SER   A O     1 
ATOM   6577 C  CB    . SER   A 1 974  ? -12.623 17.620  -54.995 1.00 91.83  ? 1123 SER   A CB    1 
ATOM   6578 O  OG    . SER   A 1 974  ? -11.223 17.497  -54.793 1.00 89.94  ? 1123 SER   A OG    1 
ATOM   6579 N  N     . GLN   A 1 975  ? -15.457 17.014  -55.866 1.00 98.95  ? 1124 GLN   A N     1 
ATOM   6580 C  CA    . GLN   A 1 975  ? -16.936 17.165  -55.965 1.00 101.34 ? 1124 GLN   A CA    1 
ATOM   6581 C  C     . GLN   A 1 975  ? -17.401 16.531  -57.285 1.00 98.48  ? 1124 GLN   A C     1 
ATOM   6582 O  O     . GLN   A 1 975  ? -17.120 17.100  -58.359 1.00 93.42  ? 1124 GLN   A O     1 
ATOM   6583 C  CB    . GLN   A 1 975  ? -17.356 18.630  -55.769 1.00 107.65 ? 1124 GLN   A CB    1 
ATOM   6584 C  CG    . GLN   A 1 975  ? -17.185 19.552  -56.975 1.00 111.70 ? 1124 GLN   A CG    1 
ATOM   6585 C  CD    . GLN   A 1 975  ? -15.747 19.842  -57.332 1.00 115.01 ? 1124 GLN   A CD    1 
ATOM   6586 O  OE1   . GLN   A 1 975  ? -14.883 19.977  -56.466 1.00 119.47 ? 1124 GLN   A OE1   1 
ATOM   6587 N  NE2   . GLN   A 1 975  ? -15.480 19.961  -58.623 1.00 114.14 ? 1124 GLN   A NE2   1 
ATOM   6588 N  N     . LEU   A 1 976  ? -18.060 15.370  -57.193 1.00 97.41  ? 1125 LEU   A N     1 
ATOM   6589 C  CA    . LEU   A 1 976  ? -18.588 14.587  -58.344 1.00 96.18  ? 1125 LEU   A CA    1 
ATOM   6590 C  C     . LEU   A 1 976  ? -20.103 14.789  -58.444 1.00 96.77  ? 1125 LEU   A C     1 
ATOM   6591 O  O     . LEU   A 1 976  ? -20.729 15.085  -57.408 1.00 94.73  ? 1125 LEU   A O     1 
ATOM   6592 C  CB    . LEU   A 1 976  ? -18.250 13.105  -58.148 1.00 95.46  ? 1125 LEU   A CB    1 
ATOM   6593 C  CG    . LEU   A 1 976  ? -16.904 12.650  -58.709 1.00 94.73  ? 1125 LEU   A CG    1 
ATOM   6594 C  CD1   . LEU   A 1 976  ? -16.530 11.276  -58.174 1.00 94.08  ? 1125 LEU   A CD1   1 
ATOM   6595 C  CD2   . LEU   A 1 976  ? -16.926 12.645  -60.230 1.00 94.84  ? 1125 LEU   A CD2   1 
ATOM   6596 N  N     . ASP   A 1 977  ? -20.660 14.620  -59.647 1.00 101.76 ? 1126 ASP   A N     1 
ATOM   6597 C  CA    . ASP   A 1 977  ? -22.122 14.669  -59.917 1.00 104.94 ? 1126 ASP   A CA    1 
ATOM   6598 C  C     . ASP   A 1 977  ? -22.811 13.616  -59.053 1.00 105.20 ? 1126 ASP   A C     1 
ATOM   6599 O  O     . ASP   A 1 977  ? -22.344 12.481  -58.985 1.00 104.58 ? 1126 ASP   A O     1 
ATOM   6600 C  CB    . ASP   A 1 977  ? -22.435 14.425  -61.396 1.00 108.11 ? 1126 ASP   A CB    1 
ATOM   6601 C  CG    . ASP   A 1 977  ? -21.847 15.460  -62.342 1.00 113.71 ? 1126 ASP   A CG    1 
ATOM   6602 O  OD1   . ASP   A 1 977  ? -21.239 16.432  -61.849 1.00 116.29 ? 1126 ASP   A OD1   1 
ATOM   6603 O  OD2   . ASP   A 1 977  ? -22.002 15.283  -63.568 1.00 118.46 ? 1126 ASP   A OD2   1 
ATOM   6604 N  N     . PRO   A 1 978  ? -23.931 13.952  -58.368 1.00 104.89 ? 1127 PRO   A N     1 
ATOM   6605 C  CA    . PRO   A 1 978  ? -24.680 12.971  -57.580 1.00 102.61 ? 1127 PRO   A CA    1 
ATOM   6606 C  C     . PRO   A 1 978  ? -24.812 11.606  -58.273 1.00 99.08  ? 1127 PRO   A C     1 
ATOM   6607 O  O     . PRO   A 1 978  ? -24.679 10.601  -57.602 1.00 98.71  ? 1127 PRO   A O     1 
ATOM   6608 C  CB    . PRO   A 1 978  ? -26.055 13.640  -57.433 1.00 104.21 ? 1127 PRO   A CB    1 
ATOM   6609 C  CG    . PRO   A 1 978  ? -25.741 15.122  -57.409 1.00 105.46 ? 1127 PRO   A CG    1 
ATOM   6610 C  CD    . PRO   A 1 978  ? -24.535 15.293  -58.311 1.00 104.38 ? 1127 PRO   A CD    1 
ATOM   6611 N  N     . VAL   A 1 979  ? -25.055 11.617  -59.589 1.00 96.31  ? 1128 VAL   A N     1 
ATOM   6612 C  CA    . VAL   A 1 979  ? -25.228 10.406  -60.449 1.00 95.67  ? 1128 VAL   A CA    1 
ATOM   6613 C  C     . VAL   A 1 979  ? -23.934 9.576   -60.454 1.00 94.25  ? 1128 VAL   A C     1 
ATOM   6614 O  O     . VAL   A 1 979  ? -24.036 8.336   -60.361 1.00 95.29  ? 1128 VAL   A O     1 
ATOM   6615 C  CB    . VAL   A 1 979  ? -25.674 10.788  -61.876 1.00 94.50  ? 1128 VAL   A CB    1 
ATOM   6616 C  CG1   . VAL   A 1 979  ? -24.614 11.579  -62.632 1.00 94.62  ? 1128 VAL   A CG1   1 
ATOM   6617 C  CG2   . VAL   A 1 979  ? -26.100 9.568   -62.678 1.00 93.15  ? 1128 VAL   A CG2   1 
ATOM   6618 N  N     . ASN   A 1 980  ? -22.766 10.222  -60.559 1.00 91.05  ? 1129 ASN   A N     1 
ATOM   6619 C  CA    . ASN   A 1 980  ? -21.442 9.542   -60.616 1.00 87.60  ? 1129 ASN   A CA    1 
ATOM   6620 C  C     . ASN   A 1 980  ? -21.138 8.892   -59.260 1.00 86.45  ? 1129 ASN   A C     1 
ATOM   6621 O  O     . ASN   A 1 980  ? -20.627 7.762   -59.259 1.00 86.59  ? 1129 ASN   A O     1 
ATOM   6622 C  CB    . ASN   A 1 980  ? -20.315 10.492  -61.040 1.00 86.44  ? 1129 ASN   A CB    1 
ATOM   6623 C  CG    . ASN   A 1 980  ? -20.143 10.595  -62.542 1.00 84.57  ? 1129 ASN   A CG    1 
ATOM   6624 O  OD1   . ASN   A 1 980  ? -20.422 9.648   -63.276 1.00 79.27  ? 1129 ASN   A OD1   1 
ATOM   6625 N  ND2   . ASN   A 1 980  ? -19.667 11.738  -63.010 1.00 83.57  ? 1129 ASN   A ND2   1 
ATOM   6626 N  N     . GLU   A 1 981  ? -21.441 9.578   -58.153 1.00 86.54  ? 1130 GLU   A N     1 
ATOM   6627 C  CA    . GLU   A 1 981  ? -21.198 9.074   -56.773 1.00 86.19  ? 1130 GLU   A CA    1 
ATOM   6628 C  C     . GLU   A 1 981  ? -22.164 7.926   -56.453 1.00 83.63  ? 1130 GLU   A C     1 
ATOM   6629 O  O     . GLU   A 1 981  ? -21.822 7.110   -55.578 1.00 83.95  ? 1130 GLU   A O     1 
ATOM   6630 C  CB    . GLU   A 1 981  ? -21.325 10.199  -55.742 1.00 88.56  ? 1130 GLU   A CB    1 
ATOM   6631 C  CG    . GLU   A 1 981  ? -20.123 11.128  -55.714 1.00 90.84  ? 1130 GLU   A CG    1 
ATOM   6632 C  CD    . GLU   A 1 981  ? -19.944 11.914  -54.425 1.00 92.89  ? 1130 GLU   A CD    1 
ATOM   6633 O  OE1   . GLU   A 1 981  ? -20.962 12.216  -53.768 1.00 94.03  ? 1130 GLU   A OE1   1 
ATOM   6634 O  OE2   . GLU   A 1 981  ? -18.784 12.218  -54.081 1.00 92.59  ? 1130 GLU   A OE2   1 
ATOM   6635 N  N     . HIS   A 1 982  ? -23.318 7.860   -57.126 1.00 82.55  ? 1131 HIS   A N     1 
ATOM   6636 C  CA    . HIS   A 1 982  ? -24.337 6.792   -56.926 1.00 84.17  ? 1131 HIS   A CA    1 
ATOM   6637 C  C     . HIS   A 1 982  ? -23.825 5.462   -57.495 1.00 81.43  ? 1131 HIS   A C     1 
ATOM   6638 O  O     . HIS   A 1 982  ? -24.131 4.421   -56.882 1.00 82.35  ? 1131 HIS   A O     1 
ATOM   6639 C  CB    . HIS   A 1 982  ? -25.702 7.198   -57.507 1.00 87.16  ? 1131 HIS   A CB    1 
ATOM   6640 C  CG    . HIS   A 1 982  ? -26.436 8.204   -56.682 1.00 88.86  ? 1131 HIS   A CG    1 
ATOM   6641 N  ND1   . HIS   A 1 982  ? -27.246 9.171   -57.245 1.00 89.45  ? 1131 HIS   A ND1   1 
ATOM   6642 C  CD2   . HIS   A 1 982  ? -26.475 8.409   -55.346 1.00 89.17  ? 1131 HIS   A CD2   1 
ATOM   6643 C  CE1   . HIS   A 1 982  ? -27.758 9.923   -56.292 1.00 90.50  ? 1131 HIS   A CE1   1 
ATOM   6644 N  NE2   . HIS   A 1 982  ? -27.298 9.478   -55.117 1.00 89.67  ? 1131 HIS   A NE2   1 
ATOM   6645 N  N     . MET   A 1 983  ? -23.078 5.486   -58.607 1.00 79.19  ? 1132 MET   A N     1 
ATOM   6646 C  CA    . MET   A 1 983  ? -22.494 4.261   -59.225 1.00 77.96  ? 1132 MET   A CA    1 
ATOM   6647 C  C     . MET   A 1 983  ? -21.228 3.852   -58.462 1.00 77.09  ? 1132 MET   A C     1 
ATOM   6648 O  O     . MET   A 1 983  ? -20.945 2.637   -58.416 1.00 79.03  ? 1132 MET   A O     1 
ATOM   6649 C  CB    . MET   A 1 983  ? -22.166 4.449   -60.711 1.00 78.93  ? 1132 MET   A CB    1 
ATOM   6650 C  CG    . MET   A 1 983  ? -20.979 5.353   -60.994 1.00 81.27  ? 1132 MET   A CG    1 
ATOM   6651 S  SD    . MET   A 1 983  ? -19.813 4.621   -62.168 1.00 82.85  ? 1132 MET   A SD    1 
ATOM   6652 C  CE    . MET   A 1 983  ? -19.030 3.391   -61.129 1.00 79.29  ? 1132 MET   A CE    1 
ATOM   6653 N  N     . LEU   A 1 984  ? -20.501 4.820   -57.890 1.00 73.26  ? 1133 LEU   A N     1 
ATOM   6654 C  CA    . LEU   A 1 984  ? -19.315 4.567   -57.028 1.00 70.39  ? 1133 LEU   A CA    1 
ATOM   6655 C  C     . LEU   A 1 984  ? -19.790 3.862   -55.753 1.00 70.49  ? 1133 LEU   A C     1 
ATOM   6656 O  O     . LEU   A 1 984  ? -19.182 2.839   -55.387 1.00 71.26  ? 1133 LEU   A O     1 
ATOM   6657 C  CB    . LEU   A 1 984  ? -18.604 5.887   -56.703 1.00 69.54  ? 1133 LEU   A CB    1 
ATOM   6658 C  CG    . LEU   A 1 984  ? -17.757 6.489   -57.826 1.00 69.37  ? 1133 LEU   A CG    1 
ATOM   6659 C  CD1   . LEU   A 1 984  ? -17.209 7.849   -57.420 1.00 68.52  ? 1133 LEU   A CD1   1 
ATOM   6660 C  CD2   . LEU   A 1 984  ? -16.616 5.563   -58.224 1.00 68.75  ? 1133 LEU   A CD2   1 
ATOM   6661 N  N     . ASN   A 1 985  ? -20.852 4.384   -55.130 1.00 70.05  ? 1134 ASN   A N     1 
ATOM   6662 C  CA    . ASN   A 1 985  ? -21.490 3.807   -53.915 1.00 69.73  ? 1134 ASN   A CA    1 
ATOM   6663 C  C     . ASN   A 1 985  ? -22.002 2.397   -54.230 1.00 67.79  ? 1134 ASN   A C     1 
ATOM   6664 O  O     . ASN   A 1 985  ? -21.936 1.535   -53.335 1.00 68.23  ? 1134 ASN   A O     1 
ATOM   6665 C  CB    . ASN   A 1 985  ? -22.617 4.701   -53.385 1.00 71.69  ? 1134 ASN   A CB    1 
ATOM   6666 C  CG    . ASN   A 1 985  ? -22.124 5.990   -52.759 1.00 72.67  ? 1134 ASN   A CG    1 
ATOM   6667 O  OD1   . ASN   A 1 985  ? -20.923 6.190   -52.585 1.00 74.62  ? 1134 ASN   A OD1   1 
ATOM   6668 N  ND2   . ASN   A 1 985  ? -23.044 6.875   -52.414 1.00 73.23  ? 1134 ASN   A ND2   1 
ATOM   6669 N  N     . MET   A 1 986  ? -22.487 2.172   -55.454 1.00 67.11  ? 1135 MET   A N     1 
ATOM   6670 C  CA    . MET   A 1 986  ? -23.040 0.867   -55.905 1.00 68.47  ? 1135 MET   A CA    1 
ATOM   6671 C  C     . MET   A 1 986  ? -21.897 -0.137  -56.101 1.00 68.68  ? 1135 MET   A C     1 
ATOM   6672 O  O     . MET   A 1 986  ? -22.104 -1.325  -55.781 1.00 69.91  ? 1135 MET   A O     1 
ATOM   6673 C  CB    . MET   A 1 986  ? -23.835 1.028   -57.207 1.00 69.70  ? 1135 MET   A CB    1 
ATOM   6674 C  CG    . MET   A 1 986  ? -24.657 -0.197  -57.604 1.00 69.90  ? 1135 MET   A CG    1 
ATOM   6675 S  SD    . MET   A 1 986  ? -25.639 -0.937  -56.265 1.00 70.37  ? 1135 MET   A SD    1 
ATOM   6676 C  CE    . MET   A 1 986  ? -26.426 0.506   -55.548 1.00 70.36  ? 1135 MET   A CE    1 
ATOM   6677 N  N     . ILE   A 1 987  ? -20.740 0.313   -56.601 1.00 67.81  ? 1136 ILE   A N     1 
ATOM   6678 C  CA    . ILE   A 1 987  ? -19.510 -0.529  -56.725 1.00 66.52  ? 1136 ILE   A CA    1 
ATOM   6679 C  C     . ILE   A 1 987  ? -19.002 -0.848  -55.314 1.00 65.71  ? 1136 ILE   A C     1 
ATOM   6680 O  O     . ILE   A 1 987  ? -18.657 -2.020  -55.070 1.00 66.12  ? 1136 ILE   A O     1 
ATOM   6681 C  CB    . ILE   A 1 987  ? -18.434 0.141   -57.607 1.00 66.00  ? 1136 ILE   A CB    1 
ATOM   6682 C  CG1   . ILE   A 1 987  ? -18.799 0.039   -59.091 1.00 66.29  ? 1136 ILE   A CG1   1 
ATOM   6683 C  CG2   . ILE   A 1 987  ? -17.056 -0.447  -57.322 1.00 65.71  ? 1136 ILE   A CG2   1 
ATOM   6684 C  CD1   . ILE   A 1 987  ? -17.795 0.662   -60.035 1.00 66.41  ? 1136 ILE   A CD1   1 
ATOM   6685 N  N     . ARG   A 1 988  ? -18.968 0.152   -54.426 1.00 65.67  ? 1137 ARG   A N     1 
ATOM   6686 C  CA    . ARG   A 1 988  ? -18.625 -0.014  -52.988 1.00 66.95  ? 1137 ARG   A CA    1 
ATOM   6687 C  C     . ARG   A 1 988  ? -19.510 -1.112  -52.386 1.00 69.41  ? 1137 ARG   A C     1 
ATOM   6688 O  O     . ARG   A 1 988  ? -18.974 -1.949  -51.636 1.00 70.25  ? 1137 ARG   A O     1 
ATOM   6689 C  CB    . ARG   A 1 988  ? -18.801 1.300   -52.218 1.00 66.97  ? 1137 ARG   A CB    1 
ATOM   6690 C  CG    . ARG   A 1 988  ? -17.708 2.329   -52.468 1.00 67.90  ? 1137 ARG   A CG    1 
ATOM   6691 C  CD    . ARG   A 1 988  ? -17.727 3.454   -51.450 1.00 69.03  ? 1137 ARG   A CD    1 
ATOM   6692 N  NE    . ARG   A 1 988  ? -16.709 4.464   -51.722 1.00 70.83  ? 1137 ARG   A NE    1 
ATOM   6693 C  CZ    . ARG   A 1 988  ? -16.869 5.533   -52.504 1.00 71.59  ? 1137 ARG   A CZ    1 
ATOM   6694 N  NH1   . ARG   A 1 988  ? -18.020 5.762   -53.117 1.00 70.59  ? 1137 ARG   A NH1   1 
ATOM   6695 N  NH2   . ARG   A 1 988  ? -15.865 6.377   -52.671 1.00 71.03  ? 1137 ARG   A NH2   1 
ATOM   6696 N  N     . GLN   A 1 989  ? -20.806 -1.109  -52.720 1.00 71.99  ? 1138 GLN   A N     1 
ATOM   6697 C  CA    . GLN   A 1 989  ? -21.820 -2.061  -52.186 1.00 72.99  ? 1138 GLN   A CA    1 
ATOM   6698 C  C     . GLN   A 1 989  ? -21.475 -3.493  -52.612 1.00 71.82  ? 1138 GLN   A C     1 
ATOM   6699 O  O     . GLN   A 1 989  ? -21.370 -4.353  -51.719 1.00 71.57  ? 1138 GLN   A O     1 
ATOM   6700 C  CB    . GLN   A 1 989  ? -23.230 -1.677  -52.646 1.00 75.53  ? 1138 GLN   A CB    1 
ATOM   6701 C  CG    . GLN   A 1 989  ? -23.895 -0.626  -51.765 1.00 78.90  ? 1138 GLN   A CG    1 
ATOM   6702 C  CD    . GLN   A 1 989  ? -24.089 -1.092  -50.343 1.00 80.80  ? 1138 GLN   A CD    1 
ATOM   6703 O  OE1   . GLN   A 1 989  ? -23.837 -0.357  -49.390 1.00 82.40  ? 1138 GLN   A OE1   1 
ATOM   6704 N  NE2   . GLN   A 1 989  ? -24.532 -2.329  -50.187 1.00 81.29  ? 1138 GLN   A NE2   1 
ATOM   6705 N  N     . ILE   A 1 990  ? -21.298 -3.739  -53.915 1.00 69.93  ? 1139 ILE   A N     1 
ATOM   6706 C  CA    . ILE   A 1 990  ? -21.070 -5.105  -54.480 1.00 69.79  ? 1139 ILE   A CA    1 
ATOM   6707 C  C     . ILE   A 1 990  ? -19.611 -5.532  -54.255 1.00 69.57  ? 1139 ILE   A C     1 
ATOM   6708 O  O     . ILE   A 1 990  ? -19.297 -6.711  -54.531 1.00 69.07  ? 1139 ILE   A O     1 
ATOM   6709 C  CB    . ILE   A 1 990  ? -21.483 -5.185  -55.965 1.00 69.30  ? 1139 ILE   A CB    1 
ATOM   6710 C  CG1   . ILE   A 1 990  ? -20.570 -4.365  -56.882 1.00 69.78  ? 1139 ILE   A CG1   1 
ATOM   6711 C  CG2   . ILE   A 1 990  ? -22.942 -4.790  -56.129 1.00 69.04  ? 1139 ILE   A CG2   1 
ATOM   6712 C  CD1   . ILE   A 1 990  ? -20.786 -4.634  -58.354 1.00 69.95  ? 1139 ILE   A CD1   1 
ATOM   6713 N  N     . SER   A 1 991  ? -18.755 -4.623  -53.773 1.00 69.29  ? 1140 SER   A N     1 
ATOM   6714 C  CA    . SER   A 1 991  ? -17.367 -4.922  -53.328 1.00 68.73  ? 1140 SER   A CA    1 
ATOM   6715 C  C     . SER   A 1 991  ? -17.393 -5.661  -51.983 1.00 68.99  ? 1140 SER   A C     1 
ATOM   6716 O  O     . SER   A 1 991  ? -16.411 -6.367  -51.685 1.00 69.66  ? 1140 SER   A O     1 
ATOM   6717 C  CB    . SER   A 1 991  ? -16.530 -3.669  -53.248 1.00 66.82  ? 1140 SER   A CB    1 
ATOM   6718 O  OG    . SER   A 1 991  ? -16.304 -3.126  -54.540 1.00 65.75  ? 1140 SER   A OG    1 
ATOM   6719 N  N     . ARG   A 1 992  ? -18.473 -5.504  -51.207 1.00 69.84  ? 1141 ARG   A N     1 
ATOM   6720 C  CA    . ARG   A 1 992  ? -18.631 -6.090  -49.847 1.00 70.19  ? 1141 ARG   A CA    1 
ATOM   6721 C  C     . ARG   A 1 992  ? -18.780 -7.606  -49.959 1.00 70.29  ? 1141 ARG   A C     1 
ATOM   6722 O  O     . ARG   A 1 992  ? -19.320 -8.103  -50.947 1.00 71.01  ? 1141 ARG   A O     1 
ATOM   6723 C  CB    . ARG   A 1 992  ? -19.846 -5.493  -49.129 1.00 70.86  ? 1141 ARG   A CB    1 
ATOM   6724 C  CG    . ARG   A 1 992  ? -19.765 -3.990  -48.902 1.00 72.41  ? 1141 ARG   A CG    1 
ATOM   6725 C  CD    . ARG   A 1 992  ? -21.046 -3.403  -48.338 1.00 73.07  ? 1141 ARG   A CD    1 
ATOM   6726 N  NE    . ARG   A 1 992  ? -21.322 -3.870  -46.985 1.00 72.89  ? 1141 ARG   A NE    1 
ATOM   6727 C  CZ    . ARG   A 1 992  ? -22.371 -3.508  -46.253 1.00 72.72  ? 1141 ARG   A CZ    1 
ATOM   6728 N  NH1   . ARG   A 1 992  ? -23.266 -2.662  -46.736 1.00 74.39  ? 1141 ARG   A NH1   1 
ATOM   6729 N  NH2   . ARG   A 1 992  ? -22.522 -3.994  -45.033 1.00 73.12  ? 1141 ARG   A NH2   1 
ATOM   6730 N  N     . PRO   A 1 993  ? -18.286 -8.386  -48.967 1.00 69.95  ? 1142 PRO   A N     1 
ATOM   6731 C  CA    . PRO   A 1 993  ? -18.570 -9.820  -48.893 1.00 70.59  ? 1142 PRO   A CA    1 
ATOM   6732 C  C     . PRO   A 1 993  ? -20.069 -10.119 -48.734 1.00 70.06  ? 1142 PRO   A C     1 
ATOM   6733 O  O     . PRO   A 1 993  ? -20.562 -10.993 -49.424 1.00 70.43  ? 1142 PRO   A O     1 
ATOM   6734 C  CB    . PRO   A 1 993  ? -17.804 -10.296 -47.646 1.00 70.05  ? 1142 PRO   A CB    1 
ATOM   6735 C  CG    . PRO   A 1 993  ? -16.757 -9.232  -47.410 1.00 69.31  ? 1142 PRO   A CG    1 
ATOM   6736 C  CD    . PRO   A 1 993  ? -17.387 -7.943  -47.891 1.00 69.59  ? 1142 PRO   A CD    1 
ATOM   6737 N  N     . SER   A 1 994  ? -20.743 -9.386  -47.839 1.00 70.11  ? 1143 SER   A N     1 
ATOM   6738 C  CA    . SER   A 1 994  ? -22.184 -9.535  -47.494 1.00 70.43  ? 1143 SER   A CA    1 
ATOM   6739 C  C     . SER   A 1 994  ? -23.054 -9.474  -48.757 1.00 68.42  ? 1143 SER   A C     1 
ATOM   6740 O  O     . SER   A 1 994  ? -24.070 -10.192 -48.800 1.00 68.43  ? 1143 SER   A O     1 
ATOM   6741 C  CB    . SER   A 1 994  ? -22.611 -8.493  -46.492 1.00 71.12  ? 1143 SER   A CB    1 
ATOM   6742 O  OG    . SER   A 1 994  ? -22.526 -7.189  -47.048 1.00 72.25  ? 1143 SER   A OG    1 
ATOM   6743 N  N     . ALA   A 1 995  ? -22.661 -8.657  -49.741 1.00 67.10  ? 1144 ALA   A N     1 
ATOM   6744 C  CA    . ALA   A 1 995  ? -23.349 -8.479  -51.043 1.00 67.23  ? 1144 ALA   A CA    1 
ATOM   6745 C  C     . ALA   A 1 995  ? -23.530 -9.828  -51.750 1.00 66.17  ? 1144 ALA   A C     1 
ATOM   6746 O  O     . ALA   A 1 995  ? -24.531 -9.969  -52.478 1.00 67.10  ? 1144 ALA   A O     1 
ATOM   6747 C  CB    . ALA   A 1 995  ? -22.579 -7.513  -51.911 1.00 67.62  ? 1144 ALA   A CB    1 
ATOM   6748 N  N     . ALA   A 1 996  ? -22.596 -10.769 -51.560 1.00 65.16  ? 1145 ALA   A N     1 
ATOM   6749 C  CA    . ALA   A 1 996  ? -22.649 -12.147 -52.108 1.00 66.23  ? 1145 ALA   A CA    1 
ATOM   6750 C  C     . ALA   A 1 996  ? -22.993 -13.148 -50.995 1.00 68.04  ? 1145 ALA   A C     1 
ATOM   6751 O  O     . ALA   A 1 996  ? -22.628 -14.335 -51.137 1.00 66.98  ? 1145 ALA   A O     1 
ATOM   6752 C  CB    . ALA   A 1 996  ? -21.338 -12.486 -52.774 1.00 65.82  ? 1145 ALA   A CB    1 
ATOM   6753 N  N     . GLY   A 1 997  ? -23.685 -12.687 -49.944 1.00 69.87  ? 1146 GLY   A N     1 
ATOM   6754 C  CA    . GLY   A 1 997  ? -24.135 -13.500 -48.796 1.00 72.41  ? 1146 GLY   A CA    1 
ATOM   6755 C  C     . GLY   A 1 997  ? -22.986 -14.212 -48.098 1.00 74.16  ? 1146 GLY   A C     1 
ATOM   6756 O  O     . GLY   A 1 997  ? -23.156 -15.400 -47.754 1.00 75.73  ? 1146 GLY   A O     1 
ATOM   6757 N  N     . ILE   A 1 998  ? -21.864 -13.513 -47.890 1.00 74.68  ? 1147 ILE   A N     1 
ATOM   6758 C  CA    . ILE   A 1 998  ? -20.639 -14.042 -47.215 1.00 74.26  ? 1147 ILE   A CA    1 
ATOM   6759 C  C     . ILE   A 1 998  ? -20.360 -13.197 -45.967 1.00 75.46  ? 1147 ILE   A C     1 
ATOM   6760 O  O     . ILE   A 1 998  ? -20.397 -11.955 -46.072 1.00 75.38  ? 1147 ILE   A O     1 
ATOM   6761 C  CB    . ILE   A 1 998  ? -19.437 -14.054 -48.181 1.00 73.58  ? 1147 ILE   A CB    1 
ATOM   6762 C  CG1   . ILE   A 1 998  ? -19.596 -15.129 -49.259 1.00 73.77  ? 1147 ILE   A CG1   1 
ATOM   6763 C  CG2   . ILE   A 1 998  ? -18.129 -14.210 -47.419 1.00 74.07  ? 1147 ILE   A CG2   1 
ATOM   6764 C  CD1   . ILE   A 1 998  ? -18.595 -15.028 -50.388 1.00 73.95  ? 1147 ILE   A CD1   1 
ATOM   6765 N  N     . ASN   A 1 999  ? -20.100 -13.860 -44.836 1.00 77.52  ? 1148 ASN   A N     1 
ATOM   6766 C  CA    . ASN   A 1 999  ? -19.619 -13.239 -43.573 1.00 80.24  ? 1148 ASN   A CA    1 
ATOM   6767 C  C     . ASN   A 1 999  ? -18.273 -13.880 -43.218 1.00 82.55  ? 1148 ASN   A C     1 
ATOM   6768 O  O     . ASN   A 1 999  ? -18.260 -15.075 -42.863 1.00 84.32  ? 1148 ASN   A O     1 
ATOM   6769 C  CB    . ASN   A 1 999  ? -20.646 -13.372 -42.445 1.00 80.37  ? 1148 ASN   A CB    1 
ATOM   6770 C  CG    . ASN   A 1 999  ? -20.368 -12.452 -41.272 1.00 80.79  ? 1148 ASN   A CG    1 
ATOM   6771 O  OD1   . ASN   A 1 999  ? -19.232 -12.035 -41.054 1.00 79.37  ? 1148 ASN   A OD1   1 
ATOM   6772 N  ND2   . ASN   A 1 999  ? -21.399 -12.134 -40.505 1.00 80.58  ? 1148 ASN   A ND2   1 
ATOM   6773 N  N     . LEU   A 1 1000 ? -17.188 -13.107 -43.315 1.00 84.80  ? 1149 LEU   A N     1 
ATOM   6774 C  CA    . LEU   A 1 1000 ? -15.787 -13.588 -43.167 1.00 87.54  ? 1149 LEU   A CA    1 
ATOM   6775 C  C     . LEU   A 1 1000 ? -15.461 -13.840 -41.687 1.00 89.70  ? 1149 LEU   A C     1 
ATOM   6776 O  O     . LEU   A 1 1000 ? -14.436 -14.499 -41.424 1.00 88.02  ? 1149 LEU   A O     1 
ATOM   6777 C  CB    . LEU   A 1 1000 ? -14.838 -12.549 -43.776 1.00 86.33  ? 1149 LEU   A CB    1 
ATOM   6778 C  CG    . LEU   A 1 1000 ? -15.034 -12.266 -45.265 1.00 84.73  ? 1149 LEU   A CG    1 
ATOM   6779 C  CD1   . LEU   A 1 1000 ? -14.222 -11.055 -45.698 1.00 85.53  ? 1149 LEU   A CD1   1 
ATOM   6780 C  CD2   . LEU   A 1 1000 ? -14.668 -13.479 -46.107 1.00 83.89  ? 1149 LEU   A CD2   1 
ATOM   6781 N  N     . MET   A 1 1001 ? -16.299 -13.347 -40.765 1.00 92.92  ? 1150 MET   A N     1 
ATOM   6782 C  CA    . MET   A 1 1001 ? -16.103 -13.465 -39.293 1.00 96.42  ? 1150 MET   A CA    1 
ATOM   6783 C  C     . MET   A 1 1001 ? -16.630 -14.813 -38.778 1.00 97.76  ? 1150 MET   A C     1 
ATOM   6784 O  O     . MET   A 1 1001 ? -16.335 -15.144 -37.612 1.00 99.08  ? 1150 MET   A O     1 
ATOM   6785 C  CB    . MET   A 1 1001 ? -16.822 -12.330 -38.556 1.00 97.20  ? 1150 MET   A CB    1 
ATOM   6786 C  CG    . MET   A 1 1001 ? -16.360 -10.949 -38.981 1.00 99.97  ? 1150 MET   A CG    1 
ATOM   6787 S  SD    . MET   A 1 1001 ? -16.712 -9.679  -37.739 1.00 105.11 ? 1150 MET   A SD    1 
ATOM   6788 C  CE    . MET   A 1 1001 ? -15.560 -10.149 -36.449 1.00 103.58 ? 1150 MET   A CE    1 
ATOM   6789 N  N     . ILE   A 1 1002 ? -17.372 -15.559 -39.606 1.00 96.90  ? 1151 ILE   A N     1 
ATOM   6790 C  CA    . ILE   A 1 1002 ? -17.998 -16.866 -39.240 1.00 96.21  ? 1151 ILE   A CA    1 
ATOM   6791 C  C     . ILE   A 1 1002 ? -17.304 -17.982 -40.035 1.00 92.67  ? 1151 ILE   A C     1 
ATOM   6792 O  O     . ILE   A 1 1002 ? -17.821 -18.562 -40.992 1.00 87.06  ? 1151 ILE   A O     1 
ATOM   6793 C  CB    . ILE   A 1 1002 ? -19.525 -16.823 -39.473 1.00 98.68  ? 1151 ILE   A CB    1 
ATOM   6794 C  CG1   . ILE   A 1 1002 ? -20.120 -15.472 -39.059 1.00 98.82  ? 1151 ILE   A CG1   1 
ATOM   6795 C  CG2   . ILE   A 1 1002 ? -20.212 -17.987 -38.769 1.00 99.17  ? 1151 ILE   A CG2   1 
ATOM   6796 C  CD1   . ILE   A 1 1002 ? -21.633 -15.417 -39.085 1.00 98.39  ? 1151 ILE   A CD1   1 
HETATM 6797 C  C6    . A1BKZ B 2 .    ? 19.317  13.468  -66.146 1.00 51.37  ? 1201 A1BKZ A C6    1 
HETATM 6798 C  C7    . A1BKZ B 2 .    ? 19.736  12.184  -66.480 1.00 51.55  ? 1201 A1BKZ A C7    1 
HETATM 6799 C  C8    . A1BKZ B 2 .    ? 19.408  11.120  -65.663 1.00 50.82  ? 1201 A1BKZ A C8    1 
HETATM 6800 C  C10   . A1BKZ B 2 .    ? 18.240  12.607  -64.153 1.00 50.84  ? 1201 A1BKZ A C10   1 
HETATM 6801 C  C15   . A1BKZ B 2 .    ? 16.083  13.701  -60.437 1.00 52.32  ? 1201 A1BKZ A C15   1 
HETATM 6802 C  C17   . A1BKZ B 2 .    ? 15.205  12.569  -58.636 1.00 53.72  ? 1201 A1BKZ A C17   1 
HETATM 6803 C  C20   . A1BKZ B 2 .    ? 14.957  15.258  -57.277 1.00 55.91  ? 1201 A1BKZ A C20   1 
HETATM 6804 C  C21   . A1BKZ B 2 .    ? 14.530  16.455  -56.736 1.00 55.48  ? 1201 A1BKZ A C21   1 
HETATM 6805 C  C22   . A1BKZ B 2 .    ? 14.073  17.464  -57.564 1.00 55.58  ? 1201 A1BKZ A C22   1 
HETATM 6806 C  C24   . A1BKZ B 2 .    ? 14.465  16.084  -59.487 1.00 54.70  ? 1201 A1BKZ A C24   1 
HETATM 6807 C  C1    . A1BKZ B 2 .    ? 17.272  14.927  -68.264 1.00 52.58  ? 1201 A1BKZ A C1    1 
HETATM 6808 S  S2    . A1BKZ B 2 .    ? 19.058  14.725  -68.483 1.00 52.64  ? 1201 A1BKZ A S2    1 
HETATM 6809 O  O3    . A1BKZ B 2 .    ? 19.634  15.927  -68.976 1.00 53.17  ? 1201 A1BKZ A O3    1 
HETATM 6810 O  O4    . A1BKZ B 2 .    ? 19.355  13.491  -69.120 1.00 54.18  ? 1201 A1BKZ A O4    1 
HETATM 6811 N  N5    . A1BKZ B 2 .    ? 19.645  14.564  -66.948 1.00 51.58  ? 1201 A1BKZ A N5    1 
HETATM 6812 C  C9    . A1BKZ B 2 .    ? 18.674  11.323  -64.508 1.00 51.03  ? 1201 A1BKZ A C9    1 
HETATM 6813 N  N11   . A1BKZ B 2 .    ? 17.500  12.912  -62.988 1.00 50.60  ? 1201 A1BKZ A N11   1 
HETATM 6814 C  C12   . A1BKZ B 2 .    ? 17.182  12.030  -62.008 1.00 51.17  ? 1201 A1BKZ A C12   1 
HETATM 6815 O  O13   . A1BKZ B 2 .    ? 17.522  10.871  -62.084 1.00 50.50  ? 1201 A1BKZ A O13   1 
HETATM 6816 C  C14   . A1BKZ B 2 .    ? 16.435  12.436  -60.806 1.00 52.21  ? 1201 A1BKZ A C14   1 
HETATM 6817 C  C16   . A1BKZ B 2 .    ? 15.395  13.771  -59.239 1.00 53.48  ? 1201 A1BKZ A C16   1 
HETATM 6818 S  S18   . A1BKZ B 2 .    ? 15.885  11.317  -59.569 1.00 54.30  ? 1201 A1BKZ A S18   1 
HETATM 6819 C  C19   . A1BKZ B 2 .    ? 14.925  15.058  -58.661 1.00 54.80  ? 1201 A1BKZ A C19   1 
HETATM 6820 C  C23   . A1BKZ B 2 .    ? 14.042  17.277  -58.935 1.00 55.30  ? 1201 A1BKZ A C23   1 
HETATM 6821 C  C25   . A1BKZ B 2 .    ? 18.583  13.672  -64.985 1.00 51.05  ? 1201 A1BKZ A C25   1 
HETATM 6822 P  PB    . ADP   C 3 .    ? 34.947  -3.614  -67.084 1.00 62.22  ? 1202 ADP   A PB    1 
HETATM 6823 O  O1B   . ADP   C 3 .    ? 35.865  -3.004  -68.106 1.00 59.77  ? 1202 ADP   A O1B   1 
HETATM 6824 O  O2B   . ADP   C 3 .    ? 34.810  -5.107  -67.247 1.00 62.31  ? 1202 ADP   A O2B   1 
HETATM 6825 O  O3B   . ADP   C 3 .    ? 33.612  -2.909  -67.013 1.00 63.60  ? 1202 ADP   A O3B   1 
HETATM 6826 P  PA    . ADP   C 3 .    ? 35.253  -2.631  -64.304 1.00 64.02  ? 1202 ADP   A PA    1 
HETATM 6827 O  O1A   . ADP   C 3 .    ? 35.471  -1.169  -64.513 1.00 63.97  ? 1202 ADP   A O1A   1 
HETATM 6828 O  O2A   . ADP   C 3 .    ? 33.892  -3.073  -63.883 1.00 66.57  ? 1202 ADP   A O2A   1 
HETATM 6829 O  O3A   . ADP   C 3 .    ? 35.659  -3.411  -65.647 1.00 63.09  ? 1202 ADP   A O3A   1 
HETATM 6830 O  "O5'" . ADP   C 3 .    ? 36.336  -3.199  -63.261 1.00 65.95  ? 1202 ADP   A "O5'" 1 
HETATM 6831 C  "C5'" . ADP   C 3 .    ? 37.712  -2.750  -63.345 1.00 66.72  ? 1202 ADP   A "C5'" 1 
HETATM 6832 C  "C4'" . ADP   C 3 .    ? 38.494  -3.257  -62.157 1.00 67.85  ? 1202 ADP   A "C4'" 1 
HETATM 6833 O  "O4'" . ADP   C 3 .    ? 37.895  -2.750  -60.936 1.00 66.34  ? 1202 ADP   A "O4'" 1 
HETATM 6834 C  "C3'" . ADP   C 3 .    ? 38.571  -4.783  -61.999 1.00 69.57  ? 1202 ADP   A "C3'" 1 
HETATM 6835 O  "O3'" . ADP   C 3 .    ? 39.889  -5.208  -61.675 1.00 72.28  ? 1202 ADP   A "O3'" 1 
HETATM 6836 C  "C2'" . ADP   C 3 .    ? 37.608  -5.074  -60.845 1.00 69.56  ? 1202 ADP   A "C2'" 1 
HETATM 6837 O  "O2'" . ADP   C 3 .    ? 37.994  -6.218  -60.114 1.00 70.44  ? 1202 ADP   A "O2'" 1 
HETATM 6838 C  "C1'" . ADP   C 3 .    ? 37.726  -3.799  -60.014 1.00 69.02  ? 1202 ADP   A "C1'" 1 
HETATM 6839 N  N9    . ADP   C 3 .    ? 36.539  -3.524  -59.213 1.00 70.98  ? 1202 ADP   A N9    1 
HETATM 6840 C  C8    . ADP   C 3 .    ? 35.343  -3.033  -59.670 1.00 71.99  ? 1202 ADP   A C8    1 
HETATM 6841 N  N7    . ADP   C 3 .    ? 34.441  -2.902  -58.731 1.00 72.90  ? 1202 ADP   A N7    1 
HETATM 6842 C  C5    . ADP   C 3 .    ? 35.078  -3.342  -57.580 1.00 73.51  ? 1202 ADP   A C5    1 
HETATM 6843 C  C6    . ADP   C 3 .    ? 34.647  -3.451  -56.243 1.00 75.10  ? 1202 ADP   A C6    1 
HETATM 6844 N  N6    . ADP   C 3 .    ? 33.426  -3.119  -55.832 1.00 75.45  ? 1202 ADP   A N6    1 
HETATM 6845 N  N1    . ADP   C 3 .    ? 35.534  -3.929  -55.336 1.00 76.18  ? 1202 ADP   A N1    1 
HETATM 6846 C  C2    . ADP   C 3 .    ? 36.760  -4.267  -55.759 1.00 75.45  ? 1202 ADP   A C2    1 
HETATM 6847 N  N3    . ADP   C 3 .    ? 37.274  -4.207  -56.986 1.00 74.14  ? 1202 ADP   A N3    1 
HETATM 6848 C  C4    . ADP   C 3 .    ? 36.374  -3.730  -57.864 1.00 73.44  ? 1202 ADP   A C4    1 
HETATM 6849 MG MG    . MG    D 4 .    ? 31.642  -3.136  -67.653 1.00 62.64  ? 1203 MG    A MG    1 
HETATM 6850 S  S     . SO4   E 5 .    ? 18.001  -12.961 -59.565 1.00 113.43 ? 1204 SO4   A S     1 
HETATM 6851 O  O1    . SO4   E 5 .    ? 19.228  -12.329 -59.975 1.00 112.69 ? 1204 SO4   A O1    1 
HETATM 6852 O  O2    . SO4   E 5 .    ? 16.886  -12.260 -60.141 1.00 113.91 ? 1204 SO4   A O2    1 
HETATM 6853 O  O3    . SO4   E 5 .    ? 17.989  -14.326 -60.016 1.00 113.00 ? 1204 SO4   A O3    1 
HETATM 6854 O  O4    . SO4   E 5 .    ? 17.898  -12.929 -58.131 1.00 112.25 ? 1204 SO4   A O4    1 
HETATM 6855 S  S     . SO4   F 5 .    ? 14.487  0.726   -64.472 1.00 88.48  ? 1205 SO4   A S     1 
HETATM 6856 O  O1    . SO4   F 5 .    ? 13.417  -0.173  -64.129 1.00 87.50  ? 1205 SO4   A O1    1 
HETATM 6857 O  O2    . SO4   F 5 .    ? 15.571  0.553   -63.541 1.00 88.17  ? 1205 SO4   A O2    1 
HETATM 6858 O  O3    . SO4   F 5 .    ? 14.948  0.437   -65.805 1.00 86.08  ? 1205 SO4   A O3    1 
HETATM 6859 O  O4    . SO4   F 5 .    ? 14.012  2.084   -64.409 1.00 84.34  ? 1205 SO4   A O4    1 
HETATM 6860 S  S     . SO4   G 5 .    ? -19.515 -6.867  -44.714 1.00 89.06  ? 1206 SO4   A S     1 
HETATM 6861 O  O1    . SO4   G 5 .    ? -20.590 -6.308  -45.487 1.00 89.44  ? 1206 SO4   A O1    1 
HETATM 6862 O  O2    . SO4   G 5 .    ? -19.814 -6.729  -43.314 1.00 89.05  ? 1206 SO4   A O2    1 
HETATM 6863 O  O3    . SO4   G 5 .    ? -18.295 -6.166  -45.012 1.00 90.13  ? 1206 SO4   A O3    1 
HETATM 6864 O  O4    . SO4   G 5 .    ? -19.363 -8.262  -45.039 1.00 87.33  ? 1206 SO4   A O4    1 
HETATM 6865 S  S     . SO4   H 5 .    ? 1.819   -0.888  -87.010 0.50 126.04 ? 1207 SO4   A S     1 
HETATM 6866 O  O1    . SO4   H 5 .    ? 1.805   0.537   -87.202 0.50 124.05 ? 1207 SO4   A O1    1 
HETATM 6867 O  O2    . SO4   H 5 .    ? 0.469   -1.387  -87.010 0.50 126.41 ? 1207 SO4   A O2    1 
HETATM 6868 O  O3    . SO4   H 5 .    ? 2.559   -1.509  -88.075 0.50 125.93 ? 1207 SO4   A O3    1 
HETATM 6869 O  O4    . SO4   H 5 .    ? 2.444   -1.195  -85.752 0.50 125.39 ? 1207 SO4   A O4    1 
HETATM 6870 S  S     . SO4   I 5 .    ? 8.719   -27.051 -59.257 1.00 145.01 ? 1208 SO4   A S     1 
HETATM 6871 O  O1    . SO4   I 5 .    ? 9.779   -26.628 -60.132 1.00 145.21 ? 1208 SO4   A O1    1 
HETATM 6872 O  O2    . SO4   I 5 .    ? 7.462   -26.972 -59.951 1.00 143.51 ? 1208 SO4   A O2    1 
HETATM 6873 O  O3    . SO4   I 5 .    ? 8.953   -28.409 -58.845 1.00 146.85 ? 1208 SO4   A O3    1 
HETATM 6874 O  O4    . SO4   I 5 .    ? 8.684   -26.197 -58.102 1.00 147.58 ? 1208 SO4   A O4    1 
HETATM 6875 C  C1    . EDO   J 6 .    ? 7.693   -26.782 -45.369 1.00 87.52  ? 1209 EDO   A C1    1 
HETATM 6876 O  O1    . EDO   J 6 .    ? 9.076   -26.874 -45.640 1.00 87.86  ? 1209 EDO   A O1    1 
HETATM 6877 C  C2    . EDO   J 6 .    ? 6.880   -26.735 -46.604 1.00 88.28  ? 1209 EDO   A C2    1 
HETATM 6878 O  O2    . EDO   J 6 .    ? 7.093   -27.843 -47.459 1.00 87.78  ? 1209 EDO   A O2    1 
HETATM 6879 C  C1    . EDO   K 6 .    ? -13.279 -9.607  -49.522 1.00 67.14  ? 1210 EDO   A C1    1 
HETATM 6880 O  O1    . EDO   K 6 .    ? -13.381 -10.776 -50.312 1.00 66.07  ? 1210 EDO   A O1    1 
HETATM 6881 C  C2    . EDO   K 6 .    ? -13.546 -8.350  -50.276 1.00 67.80  ? 1210 EDO   A C2    1 
HETATM 6882 O  O2    . EDO   K 6 .    ? -14.557 -8.468  -51.258 1.00 68.65  ? 1210 EDO   A O2    1 
HETATM 6883 C  C1    . EDO   L 6 .    ? -7.399  0.494   -46.767 1.00 83.87  ? 1211 EDO   A C1    1 
HETATM 6884 O  O1    . EDO   L 6 .    ? -6.051  0.206   -46.447 1.00 83.59  ? 1211 EDO   A O1    1 
HETATM 6885 C  C2    . EDO   L 6 .    ? -7.789  1.886   -46.434 1.00 84.02  ? 1211 EDO   A C2    1 
HETATM 6886 O  O2    . EDO   L 6 .    ? -7.854  2.738   -47.562 1.00 83.74  ? 1211 EDO   A O2    1 
HETATM 6887 C  C1    . EDO   M 6 .    ? 18.827  -6.444  -67.213 1.00 94.04  ? 1212 EDO   A C1    1 
HETATM 6888 O  O1    . EDO   M 6 .    ? 17.576  -6.798  -67.774 1.00 91.15  ? 1212 EDO   A O1    1 
HETATM 6889 C  C2    . EDO   M 6 .    ? 19.905  -7.423  -67.508 1.00 94.85  ? 1212 EDO   A C2    1 
HETATM 6890 O  O2    . EDO   M 6 .    ? 20.457  -7.280  -68.804 1.00 93.73  ? 1212 EDO   A O2    1 
HETATM 6891 C  C1    . EDO   N 6 .    ? 12.190  -15.650 -59.750 1.00 99.81  ? 1213 EDO   A C1    1 
HETATM 6892 O  O1    . EDO   N 6 .    ? 12.834  -14.390 -59.802 1.00 100.78 ? 1213 EDO   A O1    1 
HETATM 6893 C  C2    . EDO   N 6 .    ? 10.811  -15.583 -59.202 1.00 98.49  ? 1213 EDO   A C2    1 
HETATM 6894 O  O2    . EDO   N 6 .    ? 10.628  -14.555 -58.245 1.00 97.48  ? 1213 EDO   A O2    1 
HETATM 6895 O  O     . HOH   O 7 .    ? 32.024  -3.828  -65.735 1.00 58.05  ? 1301 HOH   A O     1 
HETATM 6896 O  O     . HOH   O 7 .    ? 31.730  -2.129  -69.468 1.00 62.04  ? 1302 HOH   A O     1 
HETATM 6897 O  O     . HOH   O 7 .    ? -10.259 -11.035 -50.100 1.00 42.99  ? 1303 HOH   A O     1 
HETATM 6898 O  O     . HOH   O 7 .    ? 38.933  17.719  -72.607 1.00 55.08  ? 1304 HOH   A O     1 
HETATM 6899 O  O     . HOH   O 7 .    ? 15.382  -0.452  -61.126 1.00 65.32  ? 1305 HOH   A O     1 
HETATM 6900 O  O     . HOH   O 7 .    ? 13.571  9.001   -61.102 1.00 55.63  ? 1306 HOH   A O     1 
HETATM 6901 O  O     . HOH   O 7 .    ? -12.198 -14.030 -66.181 1.00 53.93  ? 1307 HOH   A O     1 
HETATM 6902 O  O     . HOH   O 7 .    ? 25.757  22.241  -64.725 1.00 69.54  ? 1308 HOH   A O     1 
HETATM 6903 O  O     . HOH   O 7 .    ? 14.310  -0.209  -58.072 1.00 46.85  ? 1309 HOH   A O     1 
HETATM 6904 O  O     . HOH   O 7 .    ? 40.156  8.414   -48.468 1.00 50.11  ? 1310 HOH   A O     1 
HETATM 6905 O  O     . HOH   O 7 .    ? 16.697  -11.679 -70.532 1.00 48.88  ? 1311 HOH   A O     1 
HETATM 6906 O  O     . HOH   O 7 .    ? -18.684 14.218  -62.536 1.00 71.59  ? 1312 HOH   A O     1 
HETATM 6907 O  O     . HOH   O 7 .    ? -6.248  -5.162  -39.584 1.00 52.23  ? 1313 HOH   A O     1 
HETATM 6908 O  O     . HOH   O 7 .    ? 32.309  33.916  -57.342 1.00 59.05  ? 1314 HOH   A O     1 
HETATM 6909 O  O     . HOH   O 7 .    ? 15.316  7.949   -59.371 1.00 46.57  ? 1315 HOH   A O     1 
HETATM 6910 O  O     . HOH   O 7 .    ? 11.811  -32.685 -72.575 1.00 75.73  ? 1316 HOH   A O     1 
HETATM 6911 O  O     . HOH   O 7 .    ? 3.897   -6.657  -76.384 1.00 47.55  ? 1317 HOH   A O     1 
HETATM 6912 O  O     . HOH   O 7 .    ? -29.159 8.730   -59.301 1.00 67.24  ? 1318 HOH   A O     1 
HETATM 6913 O  O     . HOH   O 7 .    ? -27.193 -9.485  -51.526 1.00 56.59  ? 1319 HOH   A O     1 
HETATM 6914 O  O     . HOH   O 7 .    ? -5.820  3.967   -48.985 1.00 55.96  ? 1320 HOH   A O     1 
HETATM 6915 O  O     . HOH   O 7 .    ? 31.958  -4.788  -68.886 1.00 60.70  ? 1321 HOH   A O     1 
HETATM 6916 O  O     . HOH   O 7 .    ? 24.123  16.191  -54.000 1.00 53.19  ? 1322 HOH   A O     1 
HETATM 6917 O  O     . HOH   O 7 .    ? 0.029   -31.136 -46.070 1.00 44.53  ? 1323 HOH   A O     1 
HETATM 6918 O  O     . HOH   O 7 .    ? -14.862 3.156   -50.073 1.00 48.44  ? 1324 HOH   A O     1 
HETATM 6919 O  O     . HOH   O 7 .    ? -12.402 6.220   -48.355 1.00 42.80  ? 1325 HOH   A O     1 
HETATM 6920 O  O     . HOH   O 7 .    ? 46.346  19.700  -63.926 1.00 65.43  ? 1326 HOH   A O     1 
HETATM 6921 O  O     . HOH   O 7 .    ? -12.127 7.780   -46.366 1.00 39.88  ? 1327 HOH   A O     1 
HETATM 6922 O  O     . HOH   O 7 .    ? 22.204  18.282  -57.594 1.00 57.82  ? 1328 HOH   A O     1 
HETATM 6923 O  O     . HOH   O 7 .    ? 13.238  1.788   -53.113 1.00 39.24  ? 1329 HOH   A O     1 
HETATM 6924 O  O     . HOH   O 7 .    ? -4.882  -31.942 -47.111 1.00 62.20  ? 1330 HOH   A O     1 
HETATM 6925 O  O     . HOH   O 7 .    ? 1.975   -5.882  -74.673 1.00 55.21  ? 1331 HOH   A O     1 
HETATM 6926 O  O     . HOH   O 7 .    ? 2.803   8.260   -47.170 1.00 42.43  ? 1332 HOH   A O     1 
HETATM 6927 O  O     . HOH   O 7 .    ? 14.134  -23.776 -56.340 1.00 60.77  ? 1333 HOH   A O     1 
HETATM 6928 O  O     . HOH   O 7 .    ? -3.191  -18.037 -37.880 1.00 62.79  ? 1334 HOH   A O     1 
HETATM 6929 O  O     . HOH   O 7 .    ? 43.721  4.918   -64.024 1.00 46.27  ? 1335 HOH   A O     1 
HETATM 6930 O  O     . HOH   O 7 .    ? -16.594 -0.735  -42.580 1.00 57.31  ? 1336 HOH   A O     1 
HETATM 6931 O  O     . HOH   O 7 .    ? 17.574  -4.566  -62.740 1.00 42.09  ? 1337 HOH   A O     1 
HETATM 6932 O  O     . HOH   O 7 .    ? 41.993  0.667   -81.662 1.00 51.45  ? 1338 HOH   A O     1 
HETATM 6933 O  O     . HOH   O 7 .    ? 1.875   -11.205 -36.553 1.00 66.15  ? 1339 HOH   A O     1 
HETATM 6934 O  O     . HOH   O 7 .    ? -6.055  -12.242 -37.737 1.00 36.04  ? 1340 HOH   A O     1 
HETATM 6935 O  O     . HOH   O 7 .    ? 10.995  13.629  -56.875 1.00 44.81  ? 1341 HOH   A O     1 
HETATM 6936 O  O     . HOH   O 7 .    ? -24.678 -1.727  -44.136 1.00 67.72  ? 1342 HOH   A O     1 
HETATM 6937 O  O     . HOH   O 7 .    ? 17.198  -20.453 -60.198 1.00 58.10  ? 1343 HOH   A O     1 
HETATM 6938 O  O     . HOH   O 7 .    ? -11.576 0.917   -74.532 1.00 43.14  ? 1344 HOH   A O     1 
HETATM 6939 O  O     . HOH   O 7 .    ? 9.097   -19.731 -55.024 1.00 60.06  ? 1345 HOH   A O     1 
HETATM 6940 O  O     . HOH   O 7 .    ? 3.494   -9.115  -30.956 1.00 69.25  ? 1346 HOH   A O     1 
HETATM 6941 O  O     . HOH   O 7 .    ? 42.461  15.594  -74.440 1.00 44.82  ? 1347 HOH   A O     1 
HETATM 6942 O  O     . HOH   O 7 .    ? 10.030  -6.833  -31.388 1.00 60.91  ? 1348 HOH   A O     1 
HETATM 6943 O  O     . HOH   O 7 .    ? 1.682   -11.051 -52.204 1.00 47.80  ? 1349 HOH   A O     1 
HETATM 6944 O  O     . HOH   O 7 .    ? 6.355   -11.307 -75.099 1.00 46.67  ? 1350 HOH   A O     1 
HETATM 6945 O  O     . HOH   O 7 .    ? 21.892  22.464  -79.621 1.00 50.79  ? 1351 HOH   A O     1 
HETATM 6946 O  O     . HOH   O 7 .    ? -8.521  -4.265  -35.819 1.00 52.99  ? 1352 HOH   A O     1 
HETATM 6947 O  O     . HOH   O 7 .    ? -11.617 -5.761  -66.909 1.00 65.03  ? 1353 HOH   A O     1 
HETATM 6948 O  O     . HOH   O 7 .    ? 14.212  9.349   -57.275 1.00 48.88  ? 1354 HOH   A O     1 
HETATM 6949 O  O     . HOH   O 7 .    ? -3.769  -4.709  -69.544 1.00 46.28  ? 1355 HOH   A O     1 
HETATM 6950 O  O     . HOH   O 7 .    ? 21.674  -11.296 -82.706 1.00 55.88  ? 1356 HOH   A O     1 
HETATM 6951 O  O     . HOH   O 7 .    ? 5.142   -27.309 -54.188 1.00 38.94  ? 1357 HOH   A O     1 
HETATM 6952 O  O     . HOH   O 7 .    ? 39.403  -9.583  -81.433 1.00 65.35  ? 1358 HOH   A O     1 
HETATM 6953 O  O     . HOH   O 7 .    ? 16.969  -2.404  -64.256 1.00 45.70  ? 1359 HOH   A O     1 
HETATM 6954 O  O     . HOH   O 7 .    ? 22.519  -23.829 -83.162 1.00 56.75  ? 1360 HOH   A O     1 
HETATM 6955 O  O     . HOH   O 7 .    ? 17.863  -26.580 -70.063 1.00 69.80  ? 1361 HOH   A O     1 
HETATM 6956 O  O     . HOH   O 7 .    ? 11.550  15.238  -67.259 1.00 69.70  ? 1362 HOH   A O     1 
HETATM 6957 O  O     . HOH   O 7 .    ? 35.656  -0.969  -52.496 1.00 57.04  ? 1363 HOH   A O     1 
HETATM 6958 O  O     . HOH   O 7 .    ? 29.708  -13.053 -83.734 1.00 71.63  ? 1364 HOH   A O     1 
HETATM 6959 O  O     . HOH   O 7 .    ? 19.333  -5.579  -60.363 1.00 47.52  ? 1365 HOH   A O     1 
HETATM 6960 O  O     . HOH   O 7 .    ? 34.493  -10.562 -72.315 1.00 34.21  ? 1366 HOH   A O     1 
HETATM 6961 O  O     . HOH   O 7 .    ? 31.946  -2.835  -60.931 1.00 45.16  ? 1367 HOH   A O     1 
HETATM 6962 O  O     . HOH   O 7 .    ? 24.715  -8.960  -80.182 1.00 47.28  ? 1368 HOH   A O     1 
HETATM 6963 O  O     . HOH   O 7 .    ? 10.596  -0.157  -68.835 1.00 57.57  ? 1369 HOH   A O     1 
HETATM 6964 O  O     . HOH   O 7 .    ? 6.203   -10.380 -67.919 1.00 60.34  ? 1370 HOH   A O     1 
HETATM 6965 O  O     . HOH   O 7 .    ? 15.219  -18.402 -59.282 1.00 55.02  ? 1371 HOH   A O     1 
HETATM 6966 O  O     . HOH   O 7 .    ? 12.331  10.962  -59.141 1.00 46.94  ? 1372 HOH   A O     1 
HETATM 6967 O  O     . HOH   O 7 .    ? -20.775 -0.219  -46.373 1.00 52.96  ? 1373 HOH   A O     1 
HETATM 6968 O  O     . HOH   O 7 .    ? 1.438   -12.441 -32.091 1.00 44.20  ? 1374 HOH   A O     1 
HETATM 6969 O  O     . HOH   O 7 .    ? 7.971   15.685  -76.007 1.00 51.19  ? 1375 HOH   A O     1 
HETATM 6970 O  O     . HOH   O 7 .    ? 8.776   7.150   -70.315 1.00 50.96  ? 1376 HOH   A O     1 
HETATM 6971 O  O     . HOH   O 7 .    ? 25.291  -31.027 -39.305 1.00 54.34  ? 1377 HOH   A O     1 
HETATM 6972 O  O     . HOH   O 7 .    ? 20.993  -7.935  -61.415 1.00 44.85  ? 1378 HOH   A O     1 
HETATM 6973 O  O     . HOH   O 7 .    ? -13.840 10.300  -74.502 1.00 44.04  ? 1379 HOH   A O     1 
HETATM 6974 O  O     . HOH   O 7 .    ? 15.945  -4.344  -55.245 1.00 55.66  ? 1380 HOH   A O     1 
HETATM 6975 O  O     . HOH   O 7 .    ? -1.534  0.918   -36.793 1.00 54.40  ? 1381 HOH   A O     1 
HETATM 6976 O  O     . HOH   O 7 .    ? 40.407  11.669  -58.839 1.00 49.85  ? 1382 HOH   A O     1 
HETATM 6977 O  O     . HOH   O 7 .    ? 14.936  7.580   -52.646 1.00 54.11  ? 1383 HOH   A O     1 
HETATM 6978 O  O     . HOH   O 7 .    ? 4.895   12.894  -82.799 1.00 65.97  ? 1384 HOH   A O     1 
HETATM 6979 O  O     . HOH   O 7 .    ? 39.125  20.166  -71.826 1.00 64.31  ? 1385 HOH   A O     1 
HETATM 6980 O  O     . HOH   O 7 .    ? 39.672  -10.360 -78.960 1.00 53.67  ? 1386 HOH   A O     1 
HETATM 6981 O  O     . HOH   O 7 .    ? 3.927   -11.464 -78.500 1.00 49.07  ? 1387 HOH   A O     1 
HETATM 6982 O  O     . HOH   O 7 .    ? 10.390  1.885   -70.472 1.00 33.84  ? 1388 HOH   A O     1 
HETATM 6983 O  O     . HOH   O 7 .    ? 18.539  -9.871  -65.578 1.00 69.83  ? 1389 HOH   A O     1 
HETATM 6984 O  O     . HOH   O 7 .    ? 17.843  20.502  -84.836 1.00 59.40  ? 1390 HOH   A O     1 
HETATM 6985 O  O     . HOH   O 7 .    ? 12.593  -6.093  -60.557 1.00 49.08  ? 1391 HOH   A O     1 
HETATM 6986 O  O     . HOH   O 7 .    ? -15.634 7.749   -73.415 1.00 46.60  ? 1392 HOH   A O     1 
HETATM 6987 O  O     . HOH   O 7 .    ? 30.622  -47.937 -80.947 1.00 59.69  ? 1393 HOH   A O     1 
HETATM 6988 O  O     . HOH   O 7 .    ? 10.575  13.939  -64.489 1.00 56.52  ? 1394 HOH   A O     1 
HETATM 6989 O  O     . HOH   O 7 .    ? 9.337   9.719   -62.292 1.00 55.33  ? 1395 HOH   A O     1 
HETATM 6990 O  O     . HOH   O 7 .    ? 2.165   -8.498  -60.490 1.00 55.09  ? 1396 HOH   A O     1 
HETATM 6991 O  O     . HOH   O 7 .    ? 16.095  -17.766 -74.659 1.00 48.20  ? 1397 HOH   A O     1 
HETATM 6992 O  O     . HOH   O 7 .    ? -6.296  -5.166  -37.011 1.00 57.25  ? 1398 HOH   A O     1 
HETATM 6993 O  O     . HOH   O 7 .    ? -17.152 6.782   -77.686 1.00 61.23  ? 1399 HOH   A O     1 
HETATM 6994 O  O     . HOH   O 7 .    ? 4.152   -9.644  -76.079 1.00 50.94  ? 1400 HOH   A O     1 
HETATM 6995 O  O     . HOH   O 7 .    ? -9.732  0.222   -37.379 1.00 63.67  ? 1401 HOH   A O     1 
HETATM 6996 O  O     . HOH   O 7 .    ? 36.607  -32.969 -43.798 1.00 58.86  ? 1402 HOH   A O     1 
HETATM 6997 O  O     . HOH   O 7 .    ? 12.324  -18.778 -60.163 1.00 57.09  ? 1403 HOH   A O     1 
HETATM 6998 O  O     . HOH   O 7 .    ? 35.141  -49.268 -81.692 1.00 55.75  ? 1404 HOH   A O     1 
HETATM 6999 O  O     . HOH   O 7 .    ? -1.173  -5.146  -69.347 1.00 43.85  ? 1405 HOH   A O     1 
HETATM 7000 O  O     . HOH   O 7 .    ? 15.842  -4.574  -60.664 1.00 51.29  ? 1406 HOH   A O     1 
HETATM 7001 O  O     . HOH   O 7 .    ? -15.406 10.327  -50.365 1.00 54.24  ? 1407 HOH   A O     1 
HETATM 7002 O  O     . HOH   O 7 .    ? -9.315  15.084  -44.973 1.00 55.42  ? 1408 HOH   A O     1 
HETATM 7003 O  O     . HOH   O 7 .    ? 11.614  -9.520  -66.767 1.00 49.97  ? 1409 HOH   A O     1 
HETATM 7004 O  O     . HOH   O 7 .    ? 8.913   -29.698 -73.903 1.00 56.61  ? 1410 HOH   A O     1 
HETATM 7005 O  O     . HOH   O 7 .    ? 11.599  -31.915 -77.588 1.00 60.21  ? 1411 HOH   A O     1 
HETATM 7006 O  O     . HOH   O 7 .    ? -29.006 15.197  -59.971 1.00 51.18  ? 1412 HOH   A O     1 
HETATM 7007 O  O     . HOH   O 7 .    ? 4.341   -27.660 -40.808 1.00 62.53  ? 1413 HOH   A O     1 
HETATM 7008 O  O     . HOH   O 7 .    ? -7.095  15.687  -43.651 1.00 55.55  ? 1414 HOH   A O     1 
# 
