data_9MFS
# 
_entry.id   9MFS 
# 
_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   9MFS         pdb_00009mfs 10.2210/pdb9mfs/pdb 
WWPDB D_1000284695 ?            ?                   
# 
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                        9MFS 
_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 '(4M)-N-[3-chloro-5-(methanesulfonamido)phenyl]-4-(3-methylpyridin-2-yl)thiophene-2-carboxamide' 421.921    1   
?        ? ?                   ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                                                                       427.201    1   
?        ? ?                   ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                                  24.305     1   
?        ? ?                   ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                                                   62.068     7   
?        ? ?                   ? 
6 non-polymer syn 'SULFATE ION'                                                                                    96.063     4   
?        ? ?                   ? 
7 non-polymer nat 'CHLORIDE ION'                                                                                   35.453     1   
?        ? ?                   ? 
8 water       nat water                                                                                            18.015     359 
?        ? ?                   ? 
# 
_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 '(4M)-N-[3-chloro-5-(methanesulfonamido)phenyl]-4-(3-methylpyridin-2-yl)thiophene-2-carboxamide' A1BKX 
3 "ADENOSINE-5'-DIPHOSPHATE"                                                                       ADP   
4 'MAGNESIUM ION'                                                                                  MG    
5 1,2-ETHANEDIOL                                                                                   EDO   
6 'SULFATE ION'                                                                                    SO4   
7 'CHLORIDE ION'                                                                                   CL    
8 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 
A1BKX non-polymer         . '(4M)-N-[3-chloro-5-(methanesulfonamido)phenyl]-4-(3-methylpyridin-2-yl)thiophene-2-carboxamide' ? 
'C18 H16 Cl N3 O3 S2' 421.921 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                                                   ? 
'Cl -1'               35.453  
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  ?    ?   ?   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  ?    ?   ?   A . n 
A 1 166  LYS 166  315  ?    ?   ?   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  326  ASN ASN A . n 
A 1 178  GLN 178  327  327  GLN GLN 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 1152 ASP ASP 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        A1BKX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BKX 
_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 A1BKX 1   1201 1201 A1BKX LIG A . 
C 3 ADP   1   1202 1202 ADP   ADP A . 
D 4 MG    1   1203 1203 MG    MG  A . 
E 5 EDO   1   1204 1204 EDO   EDO A . 
F 5 EDO   1   1205 1205 EDO   EDO A . 
G 5 EDO   1   1206 1206 EDO   EDO A . 
H 5 EDO   1   1207 1207 EDO   EDO A . 
I 5 EDO   1   1208 1208 EDO   EDO A . 
J 5 EDO   1   1209 1209 EDO   EDO A . 
K 5 EDO   1   1210 1210 EDO   EDO A . 
L 6 SO4   1   1211 1211 SO4   SO4 A . 
M 6 SO4   1   1212 1212 SO4   SO4 A . 
N 6 SO4   1   1213 1213 SO4   SO4 A . 
O 6 SO4   1   1214 1214 SO4   SO4 A . 
P 7 CL    1   1215 1215 CL    CL  A . 
Q 8 HOH   1   1301 1379 HOH   HOH A . 
Q 8 HOH   2   1302 1546 HOH   HOH A . 
Q 8 HOH   3   1303 1393 HOH   HOH A . 
Q 8 HOH   4   1304 1491 HOH   HOH A . 
Q 8 HOH   5   1305 1365 HOH   HOH A . 
Q 8 HOH   6   1306 1414 HOH   HOH A . 
Q 8 HOH   7   1307 1395 HOH   HOH A . 
Q 8 HOH   8   1308 1350 HOH   HOH A . 
Q 8 HOH   9   1309 1450 HOH   HOH A . 
Q 8 HOH   10  1310 1444 HOH   HOH A . 
Q 8 HOH   11  1311 1443 HOH   HOH A . 
Q 8 HOH   12  1312 1533 HOH   HOH A . 
Q 8 HOH   13  1313 1255 HOH   HOH A . 
Q 8 HOH   14  1314 1315 HOH   HOH A . 
Q 8 HOH   15  1315 1349 HOH   HOH A . 
Q 8 HOH   16  1316 1415 HOH   HOH A . 
Q 8 HOH   17  1317 1374 HOH   HOH A . 
Q 8 HOH   18  1318 1430 HOH   HOH A . 
Q 8 HOH   19  1319 1520 HOH   HOH A . 
Q 8 HOH   20  1320 1216 HOH   HOH A . 
Q 8 HOH   21  1321 1521 HOH   HOH A . 
Q 8 HOH   22  1322 1247 HOH   HOH A . 
Q 8 HOH   23  1323 1232 HOH   HOH A . 
Q 8 HOH   24  1324 1362 HOH   HOH A . 
Q 8 HOH   25  1325 1241 HOH   HOH A . 
Q 8 HOH   26  1326 1338 HOH   HOH A . 
Q 8 HOH   27  1327 1512 HOH   HOH A . 
Q 8 HOH   28  1328 1380 HOH   HOH A . 
Q 8 HOH   29  1329 1398 HOH   HOH A . 
Q 8 HOH   30  1330 1476 HOH   HOH A . 
Q 8 HOH   31  1331 1454 HOH   HOH A . 
Q 8 HOH   32  1332 1471 HOH   HOH A . 
Q 8 HOH   33  1333 1514 HOH   HOH A . 
Q 8 HOH   34  1334 1360 HOH   HOH A . 
Q 8 HOH   35  1335 1516 HOH   HOH A . 
Q 8 HOH   36  1336 1218 HOH   HOH A . 
Q 8 HOH   37  1337 1329 HOH   HOH A . 
Q 8 HOH   38  1338 1336 HOH   HOH A . 
Q 8 HOH   39  1339 1335 HOH   HOH A . 
Q 8 HOH   40  1340 1425 HOH   HOH A . 
Q 8 HOH   41  1341 1488 HOH   HOH A . 
Q 8 HOH   42  1342 1583 HOH   HOH A . 
Q 8 HOH   43  1343 1300 HOH   HOH A . 
Q 8 HOH   44  1344 1367 HOH   HOH A . 
Q 8 HOH   45  1345 1292 HOH   HOH A . 
Q 8 HOH   46  1346 1409 HOH   HOH A . 
Q 8 HOH   47  1347 1434 HOH   HOH A . 
Q 8 HOH   48  1348 1231 HOH   HOH A . 
Q 8 HOH   49  1349 1406 HOH   HOH A . 
Q 8 HOH   50  1350 1500 HOH   HOH A . 
Q 8 HOH   51  1351 1431 HOH   HOH A . 
Q 8 HOH   52  1352 1233 HOH   HOH A . 
Q 8 HOH   53  1353 1384 HOH   HOH A . 
Q 8 HOH   54  1354 1530 HOH   HOH A . 
Q 8 HOH   55  1355 1222 HOH   HOH A . 
Q 8 HOH   56  1356 1310 HOH   HOH A . 
Q 8 HOH   57  1357 1299 HOH   HOH A . 
Q 8 HOH   58  1358 1294 HOH   HOH A . 
Q 8 HOH   59  1359 1457 HOH   HOH A . 
Q 8 HOH   60  1360 1305 HOH   HOH A . 
Q 8 HOH   61  1361 1225 HOH   HOH A . 
Q 8 HOH   62  1362 1270 HOH   HOH A . 
Q 8 HOH   63  1363 1411 HOH   HOH A . 
Q 8 HOH   64  1364 1230 HOH   HOH A . 
Q 8 HOH   65  1365 1548 HOH   HOH A . 
Q 8 HOH   66  1366 1584 HOH   HOH A . 
Q 8 HOH   67  1367 1298 HOH   HOH A . 
Q 8 HOH   68  1368 1284 HOH   HOH A . 
Q 8 HOH   69  1369 1490 HOH   HOH A . 
Q 8 HOH   70  1370 1357 HOH   HOH A . 
Q 8 HOH   71  1371 1324 HOH   HOH A . 
Q 8 HOH   72  1372 1455 HOH   HOH A . 
Q 8 HOH   73  1373 1355 HOH   HOH A . 
Q 8 HOH   74  1374 1306 HOH   HOH A . 
Q 8 HOH   75  1375 1356 HOH   HOH A . 
Q 8 HOH   76  1376 1573 HOH   HOH A . 
Q 8 HOH   77  1377 1274 HOH   HOH A . 
Q 8 HOH   78  1378 1501 HOH   HOH A . 
Q 8 HOH   79  1379 1480 HOH   HOH A . 
Q 8 HOH   80  1380 1505 HOH   HOH A . 
Q 8 HOH   81  1381 1256 HOH   HOH A . 
Q 8 HOH   82  1382 1244 HOH   HOH A . 
Q 8 HOH   83  1383 1456 HOH   HOH A . 
Q 8 HOH   84  1384 1309 HOH   HOH A . 
Q 8 HOH   85  1385 1559 HOH   HOH A . 
Q 8 HOH   86  1386 1388 HOH   HOH A . 
Q 8 HOH   87  1387 1320 HOH   HOH A . 
Q 8 HOH   88  1388 1426 HOH   HOH A . 
Q 8 HOH   89  1389 1260 HOH   HOH A . 
Q 8 HOH   90  1390 1285 HOH   HOH A . 
Q 8 HOH   91  1391 1344 HOH   HOH A . 
Q 8 HOH   92  1392 1407 HOH   HOH A . 
Q 8 HOH   93  1393 1538 HOH   HOH A . 
Q 8 HOH   94  1394 1462 HOH   HOH A . 
Q 8 HOH   95  1395 1526 HOH   HOH A . 
Q 8 HOH   96  1396 1237 HOH   HOH A . 
Q 8 HOH   97  1397 1382 HOH   HOH A . 
Q 8 HOH   98  1398 1542 HOH   HOH A . 
Q 8 HOH   99  1399 1385 HOH   HOH A . 
Q 8 HOH   100 1400 1217 HOH   HOH A . 
Q 8 HOH   101 1401 1464 HOH   HOH A . 
Q 8 HOH   102 1402 1460 HOH   HOH A . 
Q 8 HOH   103 1403 1527 HOH   HOH A . 
Q 8 HOH   104 1404 1243 HOH   HOH A . 
Q 8 HOH   105 1405 1561 HOH   HOH A . 
Q 8 HOH   106 1406 1221 HOH   HOH A . 
Q 8 HOH   107 1407 1313 HOH   HOH A . 
Q 8 HOH   108 1408 1545 HOH   HOH A . 
Q 8 HOH   109 1409 1371 HOH   HOH A . 
Q 8 HOH   110 1410 1536 HOH   HOH A . 
Q 8 HOH   111 1411 1543 HOH   HOH A . 
Q 8 HOH   112 1412 1267 HOH   HOH A . 
Q 8 HOH   113 1413 1279 HOH   HOH A . 
Q 8 HOH   114 1414 1269 HOH   HOH A . 
Q 8 HOH   115 1415 1296 HOH   HOH A . 
Q 8 HOH   116 1416 1432 HOH   HOH A . 
Q 8 HOH   117 1417 1291 HOH   HOH A . 
Q 8 HOH   118 1418 1339 HOH   HOH A . 
Q 8 HOH   119 1419 1288 HOH   HOH A . 
Q 8 HOH   120 1420 1579 HOH   HOH A . 
Q 8 HOH   121 1421 1293 HOH   HOH A . 
Q 8 HOH   122 1422 1287 HOH   HOH A . 
Q 8 HOH   123 1423 1376 HOH   HOH A . 
Q 8 HOH   124 1424 1534 HOH   HOH A . 
Q 8 HOH   125 1425 1386 HOH   HOH A . 
Q 8 HOH   126 1426 1263 HOH   HOH A . 
Q 8 HOH   127 1427 1535 HOH   HOH A . 
Q 8 HOH   128 1428 1252 HOH   HOH A . 
Q 8 HOH   129 1429 1358 HOH   HOH A . 
Q 8 HOH   130 1430 1259 HOH   HOH A . 
Q 8 HOH   131 1431 1483 HOH   HOH A . 
Q 8 HOH   132 1432 1459 HOH   HOH A . 
Q 8 HOH   133 1433 1301 HOH   HOH A . 
Q 8 HOH   134 1434 1511 HOH   HOH A . 
Q 8 HOH   135 1435 1334 HOH   HOH A . 
Q 8 HOH   136 1436 1236 HOH   HOH A . 
Q 8 HOH   137 1437 1242 HOH   HOH A . 
Q 8 HOH   138 1438 1540 HOH   HOH A . 
Q 8 HOH   139 1439 1283 HOH   HOH A . 
Q 8 HOH   140 1440 1264 HOH   HOH A . 
Q 8 HOH   141 1441 1318 HOH   HOH A . 
Q 8 HOH   142 1442 1346 HOH   HOH A . 
Q 8 HOH   143 1443 1321 HOH   HOH A . 
Q 8 HOH   144 1444 1314 HOH   HOH A . 
Q 8 HOH   145 1445 1578 HOH   HOH A . 
Q 8 HOH   146 1446 1246 HOH   HOH A . 
Q 8 HOH   147 1447 1297 HOH   HOH A . 
Q 8 HOH   148 1448 1481 HOH   HOH A . 
Q 8 HOH   149 1449 1552 HOH   HOH A . 
Q 8 HOH   150 1450 1268 HOH   HOH A . 
Q 8 HOH   151 1451 1326 HOH   HOH A . 
Q 8 HOH   152 1452 1387 HOH   HOH A . 
Q 8 HOH   153 1453 1341 HOH   HOH A . 
Q 8 HOH   154 1454 1351 HOH   HOH A . 
Q 8 HOH   155 1455 1224 HOH   HOH A . 
Q 8 HOH   156 1456 1317 HOH   HOH A . 
Q 8 HOH   157 1457 1423 HOH   HOH A . 
Q 8 HOH   158 1458 1539 HOH   HOH A . 
Q 8 HOH   159 1459 1528 HOH   HOH A . 
Q 8 HOH   160 1460 1220 HOH   HOH A . 
Q 8 HOH   161 1461 1240 HOH   HOH A . 
Q 8 HOH   162 1462 1422 HOH   HOH A . 
Q 8 HOH   163 1463 1449 HOH   HOH A . 
Q 8 HOH   164 1464 1325 HOH   HOH A . 
Q 8 HOH   165 1465 1262 HOH   HOH A . 
Q 8 HOH   166 1466 1447 HOH   HOH A . 
Q 8 HOH   167 1467 1467 HOH   HOH A . 
Q 8 HOH   168 1468 1469 HOH   HOH A . 
Q 8 HOH   169 1469 1280 HOH   HOH A . 
Q 8 HOH   170 1470 1497 HOH   HOH A . 
Q 8 HOH   171 1471 1547 HOH   HOH A . 
Q 8 HOH   172 1472 1226 HOH   HOH A . 
Q 8 HOH   173 1473 1353 HOH   HOH A . 
Q 8 HOH   174 1474 1239 HOH   HOH A . 
Q 8 HOH   175 1475 1392 HOH   HOH A . 
Q 8 HOH   176 1476 1519 HOH   HOH A . 
Q 8 HOH   177 1477 1390 HOH   HOH A . 
Q 8 HOH   178 1478 1234 HOH   HOH A . 
Q 8 HOH   179 1479 1307 HOH   HOH A . 
Q 8 HOH   180 1480 1235 HOH   HOH A . 
Q 8 HOH   181 1481 1487 HOH   HOH A . 
Q 8 HOH   182 1482 1227 HOH   HOH A . 
Q 8 HOH   183 1483 1549 HOH   HOH A . 
Q 8 HOH   184 1484 1404 HOH   HOH A . 
Q 8 HOH   185 1485 1223 HOH   HOH A . 
Q 8 HOH   186 1486 1494 HOH   HOH A . 
Q 8 HOH   187 1487 1580 HOH   HOH A . 
Q 8 HOH   188 1488 1394 HOH   HOH A . 
Q 8 HOH   189 1489 1251 HOH   HOH A . 
Q 8 HOH   190 1490 1531 HOH   HOH A . 
Q 8 HOH   191 1491 1437 HOH   HOH A . 
Q 8 HOH   192 1492 1517 HOH   HOH A . 
Q 8 HOH   193 1493 1446 HOH   HOH A . 
Q 8 HOH   194 1494 1219 HOH   HOH A . 
Q 8 HOH   195 1495 1482 HOH   HOH A . 
Q 8 HOH   196 1496 1254 HOH   HOH A . 
Q 8 HOH   197 1497 1276 HOH   HOH A . 
Q 8 HOH   198 1498 1312 HOH   HOH A . 
Q 8 HOH   199 1499 1228 HOH   HOH A . 
Q 8 HOH   200 1500 1556 HOH   HOH A . 
Q 8 HOH   201 1501 1266 HOH   HOH A . 
Q 8 HOH   202 1502 1271 HOH   HOH A . 
Q 8 HOH   203 1503 1465 HOH   HOH A . 
Q 8 HOH   204 1504 1347 HOH   HOH A . 
Q 8 HOH   205 1505 1472 HOH   HOH A . 
Q 8 HOH   206 1506 1302 HOH   HOH A . 
Q 8 HOH   207 1507 1303 HOH   HOH A . 
Q 8 HOH   208 1508 1383 HOH   HOH A . 
Q 8 HOH   209 1509 1448 HOH   HOH A . 
Q 8 HOH   210 1510 1272 HOH   HOH A . 
Q 8 HOH   211 1511 1571 HOH   HOH A . 
Q 8 HOH   212 1512 1458 HOH   HOH A . 
Q 8 HOH   213 1513 1295 HOH   HOH A . 
Q 8 HOH   214 1514 1453 HOH   HOH A . 
Q 8 HOH   215 1515 1550 HOH   HOH A . 
Q 8 HOH   216 1516 1504 HOH   HOH A . 
Q 8 HOH   217 1517 1328 HOH   HOH A . 
Q 8 HOH   218 1518 1265 HOH   HOH A . 
Q 8 HOH   219 1519 1249 HOH   HOH A . 
Q 8 HOH   220 1520 1581 HOH   HOH A . 
Q 8 HOH   221 1521 1564 HOH   HOH A . 
Q 8 HOH   222 1522 1477 HOH   HOH A . 
Q 8 HOH   223 1523 1308 HOH   HOH A . 
Q 8 HOH   224 1524 1261 HOH   HOH A . 
Q 8 HOH   225 1525 1277 HOH   HOH A . 
Q 8 HOH   226 1526 1575 HOH   HOH A . 
Q 8 HOH   227 1527 1468 HOH   HOH A . 
Q 8 HOH   228 1528 1366 HOH   HOH A . 
Q 8 HOH   229 1529 1445 HOH   HOH A . 
Q 8 HOH   230 1530 1258 HOH   HOH A . 
Q 8 HOH   231 1531 1250 HOH   HOH A . 
Q 8 HOH   232 1532 1537 HOH   HOH A . 
Q 8 HOH   233 1533 1257 HOH   HOH A . 
Q 8 HOH   234 1534 1323 HOH   HOH A . 
Q 8 HOH   235 1535 1245 HOH   HOH A . 
Q 8 HOH   236 1536 1311 HOH   HOH A . 
Q 8 HOH   237 1537 1479 HOH   HOH A . 
Q 8 HOH   238 1538 1496 HOH   HOH A . 
Q 8 HOH   239 1539 1408 HOH   HOH A . 
Q 8 HOH   240 1540 1372 HOH   HOH A . 
Q 8 HOH   241 1541 1375 HOH   HOH A . 
Q 8 HOH   242 1542 1333 HOH   HOH A . 
Q 8 HOH   243 1543 1562 HOH   HOH A . 
Q 8 HOH   244 1544 1286 HOH   HOH A . 
Q 8 HOH   245 1545 1273 HOH   HOH A . 
Q 8 HOH   246 1546 1278 HOH   HOH A . 
Q 8 HOH   247 1547 1316 HOH   HOH A . 
Q 8 HOH   248 1548 1377 HOH   HOH A . 
Q 8 HOH   249 1549 1433 HOH   HOH A . 
Q 8 HOH   250 1550 1441 HOH   HOH A . 
Q 8 HOH   251 1551 1420 HOH   HOH A . 
Q 8 HOH   252 1552 1576 HOH   HOH A . 
Q 8 HOH   253 1553 1253 HOH   HOH A . 
Q 8 HOH   254 1554 1555 HOH   HOH A . 
Q 8 HOH   255 1555 1563 HOH   HOH A . 
Q 8 HOH   256 1556 1369 HOH   HOH A . 
Q 8 HOH   257 1557 1337 HOH   HOH A . 
Q 8 HOH   258 1558 1438 HOH   HOH A . 
Q 8 HOH   259 1559 1281 HOH   HOH A . 
Q 8 HOH   260 1560 1503 HOH   HOH A . 
Q 8 HOH   261 1561 1498 HOH   HOH A . 
Q 8 HOH   262 1562 1570 HOH   HOH A . 
Q 8 HOH   263 1563 1569 HOH   HOH A . 
Q 8 HOH   264 1564 1373 HOH   HOH A . 
Q 8 HOH   265 1565 1345 HOH   HOH A . 
Q 8 HOH   266 1566 1363 HOH   HOH A . 
Q 8 HOH   267 1567 1419 HOH   HOH A . 
Q 8 HOH   268 1568 1424 HOH   HOH A . 
Q 8 HOH   269 1569 1229 HOH   HOH A . 
Q 8 HOH   270 1570 1275 HOH   HOH A . 
Q 8 HOH   271 1571 1558 HOH   HOH A . 
Q 8 HOH   272 1572 1557 HOH   HOH A . 
Q 8 HOH   273 1573 1342 HOH   HOH A . 
Q 8 HOH   274 1574 1417 HOH   HOH A . 
Q 8 HOH   275 1575 1327 HOH   HOH A . 
Q 8 HOH   276 1576 1523 HOH   HOH A . 
Q 8 HOH   277 1577 1452 HOH   HOH A . 
Q 8 HOH   278 1578 1421 HOH   HOH A . 
Q 8 HOH   279 1579 1577 HOH   HOH A . 
Q 8 HOH   280 1580 1502 HOH   HOH A . 
Q 8 HOH   281 1581 1340 HOH   HOH A . 
Q 8 HOH   282 1582 1522 HOH   HOH A . 
Q 8 HOH   283 1583 1381 HOH   HOH A . 
Q 8 HOH   284 1584 1568 HOH   HOH A . 
Q 8 HOH   285 1585 1412 HOH   HOH A . 
Q 8 HOH   286 1586 1322 HOH   HOH A . 
Q 8 HOH   287 1587 1524 HOH   HOH A . 
Q 8 HOH   288 1588 1451 HOH   HOH A . 
Q 8 HOH   289 1589 1470 HOH   HOH A . 
Q 8 HOH   290 1590 1238 HOH   HOH A . 
Q 8 HOH   291 1591 1532 HOH   HOH A . 
Q 8 HOH   292 1592 1370 HOH   HOH A . 
Q 8 HOH   293 1593 1544 HOH   HOH A . 
Q 8 HOH   294 1594 1585 HOH   HOH A . 
Q 8 HOH   295 1595 1473 HOH   HOH A . 
Q 8 HOH   296 1596 1428 HOH   HOH A . 
Q 8 HOH   297 1597 1506 HOH   HOH A . 
Q 8 HOH   298 1598 1508 HOH   HOH A . 
Q 8 HOH   299 1599 1396 HOH   HOH A . 
Q 8 HOH   300 1600 1397 HOH   HOH A . 
Q 8 HOH   301 1601 1429 HOH   HOH A . 
Q 8 HOH   302 1602 1551 HOH   HOH A . 
Q 8 HOH   303 1603 1515 HOH   HOH A . 
Q 8 HOH   304 1604 1435 HOH   HOH A . 
Q 8 HOH   305 1605 1330 HOH   HOH A . 
Q 8 HOH   306 1606 1493 HOH   HOH A . 
Q 8 HOH   307 1607 1343 HOH   HOH A . 
Q 8 HOH   308 1608 1439 HOH   HOH A . 
Q 8 HOH   309 1609 1582 HOH   HOH A . 
Q 8 HOH   310 1610 1282 HOH   HOH A . 
Q 8 HOH   311 1611 1352 HOH   HOH A . 
Q 8 HOH   312 1612 1486 HOH   HOH A . 
Q 8 HOH   313 1613 1499 HOH   HOH A . 
Q 8 HOH   314 1614 1495 HOH   HOH A . 
Q 8 HOH   315 1615 1332 HOH   HOH A . 
Q 8 HOH   316 1616 1485 HOH   HOH A . 
Q 8 HOH   317 1617 1440 HOH   HOH A . 
Q 8 HOH   318 1618 1513 HOH   HOH A . 
Q 8 HOH   319 1619 1389 HOH   HOH A . 
Q 8 HOH   320 1620 1354 HOH   HOH A . 
Q 8 HOH   321 1621 1466 HOH   HOH A . 
Q 8 HOH   322 1622 1400 HOH   HOH A . 
Q 8 HOH   323 1623 1442 HOH   HOH A . 
Q 8 HOH   324 1624 1474 HOH   HOH A . 
Q 8 HOH   325 1625 1378 HOH   HOH A . 
Q 8 HOH   326 1626 1368 HOH   HOH A . 
Q 8 HOH   327 1627 1289 HOH   HOH A . 
Q 8 HOH   328 1628 1507 HOH   HOH A . 
Q 8 HOH   329 1629 1319 HOH   HOH A . 
Q 8 HOH   330 1630 1529 HOH   HOH A . 
Q 8 HOH   331 1631 1478 HOH   HOH A . 
Q 8 HOH   332 1632 1416 HOH   HOH A . 
Q 8 HOH   333 1633 1290 HOH   HOH A . 
Q 8 HOH   334 1634 1418 HOH   HOH A . 
Q 8 HOH   335 1635 1361 HOH   HOH A . 
Q 8 HOH   336 1636 1359 HOH   HOH A . 
Q 8 HOH   337 1637 1510 HOH   HOH A . 
Q 8 HOH   338 1638 1463 HOH   HOH A . 
Q 8 HOH   339 1639 1541 HOH   HOH A . 
Q 8 HOH   340 1640 1399 HOH   HOH A . 
Q 8 HOH   341 1641 1566 HOH   HOH A . 
Q 8 HOH   342 1642 1572 HOH   HOH A . 
Q 8 HOH   343 1643 1413 HOH   HOH A . 
Q 8 HOH   344 1644 1489 HOH   HOH A . 
Q 8 HOH   345 1645 1484 HOH   HOH A . 
Q 8 HOH   346 1646 1574 HOH   HOH A . 
Q 8 HOH   347 1647 1560 HOH   HOH A . 
Q 8 HOH   348 1648 1410 HOH   HOH A . 
Q 8 HOH   349 1649 1348 HOH   HOH A . 
Q 8 HOH   350 1650 1565 HOH   HOH A . 
Q 8 HOH   351 1651 1509 HOH   HOH A . 
Q 8 HOH   352 1652 1553 HOH   HOH A . 
Q 8 HOH   353 1653 1461 HOH   HOH A . 
Q 8 HOH   354 1654 1492 HOH   HOH A . 
Q 8 HOH   355 1655 1567 HOH   HOH A . 
Q 8 HOH   356 1656 1554 HOH   HOH A . 
Q 8 HOH   357 1657 1401 HOH   HOH A . 
Q 8 HOH   358 1658 1402 HOH   HOH A . 
Q 8 HOH   359 1659 1403 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                     9MFS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     86.450 
_cell.length_a_esd                 ? 
_cell.length_b                     86.450 
_cell.length_b_esd                 ? 
_cell.length_c                     351.040 
_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                         9MFS 
_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                   9MFS 
_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             2.86 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.02 
_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, 15% 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         2023-05-26 
_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                                       9MFS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.43 
_reflns.d_resolution_low                               54.50 
_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                                     51611 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.3 
_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                              0.141 
_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                                    2.43 
_reflns_shell.d_res_low                                     2.50 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4368 
_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                               22.1 
_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                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.953 
_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]                            0.03 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.03 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.07 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               56.293 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_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                                 9MFS 
_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                            2.43 
_refine.ls_d_res_low                             54.50 
_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                     48991 
_refine.ls_number_reflns_R_free                  2496 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19707 
_refine.ls_R_factor_R_free                       0.24616 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19446 
_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                       0.292 
_refine.pdbx_overall_ESU_R_Free                  0.235 
_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                             7.730 
_refine.overall_SU_ML                            0.174 
_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                       2.43 
_refine_hist.d_res_low                        54.50 
_refine_hist.number_atoms_solvent             359 
_refine_hist.number_atoms_total               7261 
_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        6798 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         104 
_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' ? 0.006  0.013  7090  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  6789  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.422  1.650  9624  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.202  1.573  15635 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.676  5.000  864   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.556 22.312 372   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.790 15.000 1220  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.996 15.000 49    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.063  0.200  935   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  7922  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1597  ? 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' ? 4.012  5.652  3438  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.007  5.651  3437  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.959  8.467  4296  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.960  8.469  4297  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.606  6.299  3652  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.572  6.288  3637  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.129  9.204  5301  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.536  66.203 7601  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.531  66.119 7556  ? 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                       2.430 
_refine_ls_shell.d_res_low                        2.493 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             151 
_refine_ls_shell.number_reflns_R_work             3577 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.280 
_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   20 
_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                  0.322 
# 
_struct.entry_id                     9MFS 
_struct.title                        'Cat DHX9 in Complex with ATX968 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        9MFS 
_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 5 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
P N N 7 ? 
Q N N 8 ? 
# 
_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              9MFS 
_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 9MFS MET A 1    ? UNP M3WPI7 ? ? 'initiating methionine' 150  1 
1 9MFS ASP A 1003 ? UNP M3WPI7 ? ? 'expression tag'        1152 2 
1 9MFS TYR A 1004 ? UNP M3WPI7 ? ? 'expression tag'        1153 3 
1 9MFS LYS A 1005 ? UNP M3WPI7 ? ? 'expression tag'        1154 4 
1 9MFS ASP A 1006 ? UNP M3WPI7 ? ? 'expression tag'        1155 5 
1 9MFS ASP A 1007 ? UNP M3WPI7 ? ? 'expression tag'        1156 6 
1 9MFS ASP A 1008 ? UNP M3WPI7 ? ? 'expression tag'        1157 7 
1 9MFS ASP A 1009 ? UNP M3WPI7 ? ? 'expression tag'        1158 8 
1 9MFS 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,P,Q 
# 
_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 ? LEU A 239 ? ASP A 376  LEU A 388  1 ? 13 
HELX_P HELX_P5  AA5 LEU A 240 ? LYS A 244 ? LEU A 389  LYS A 393  5 ? 5  
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 ? GLU A 312 ? ARG A 447  GLU A 461  1 ? 15 
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 351 ? GLY A 353 ? GLU A 500  GLY A 502  5 ? 3  
HELX_P HELX_P12 AB3 GLU A 364 ? ARG A 368 ? GLU A 513  ARG A 517  5 ? 5  
HELX_P HELX_P13 AB4 ASP A 369 ? TYR A 386 ? ASP A 518  TYR A 535  1 ? 18 
HELX_P HELX_P14 AB5 THR A 400 ? PHE A 407 ? THR A 549  PHE A 556  1 ? 8  
HELX_P HELX_P15 AB6 PHE A 426 ? HIS A 435 ? PHE A 575  HIS A 584  1 ? 10 
HELX_P HELX_P16 AB7 GLY A 469 ? ALA A 477 ? GLY A 618  ALA A 626  1 ? 9  
HELX_P HELX_P17 AB8 PRO A 485 ? THR A 498 ? PRO A 634  THR A 647  1 ? 14 
HELX_P HELX_P18 AB9 GLY A 511 ? ASN A 525 ? GLY A 660  ASN A 674  1 ? 15 
HELX_P HELX_P19 AC1 PRO A 526 ? GLY A 529 ? PRO A 675  GLY A 678  5 ? 4  
HELX_P HELX_P20 AC2 PRO A 543 ? LYS A 549 ? PRO A 692  LYS A 698  1 ? 7  
HELX_P HELX_P21 AC3 ASN A 566 ? SER A 571 ? ASN A 715  SER A 720  1 ? 6  
HELX_P HELX_P22 AC4 SER A 606 ? ARG A 616 ? SER A 755  ARG A 765  1 ? 11 
HELX_P HELX_P23 AC5 SER A 630 ? ARG A 636 ? SER A 779  ARG A 785  1 ? 7  
HELX_P HELX_P24 AC6 PRO A 643 ? ARG A 647 ? PRO A 792  ARG A 796  5 ? 5  
HELX_P HELX_P25 AC7 LEU A 650 ? LEU A 660 ? LEU A 799  LEU A 809  1 ? 11 
HELX_P HELX_P26 AC8 GLY A 664 ? ALA A 670 ? GLY A 813  ALA A 819  1 ? 7  
HELX_P HELX_P27 AC9 PRO A 677 ? LEU A 691 ? PRO A 826  LEU A 840  1 ? 15 
HELX_P HELX_P28 AD1 THR A 701 ? LEU A 710 ? THR A 850  LEU A 859  1 ? 10 
HELX_P HELX_P29 AD2 GLU A 713 ? PHE A 726 ? GLU A 862  PHE A 875  1 ? 14 
HELX_P HELX_P30 AD3 VAL A 728 ? THR A 739 ? VAL A 877  THR A 888  1 ? 12 
HELX_P HELX_P31 AD4 GLY A 753 ? PHE A 759 ? GLY A 902  PHE A 908  1 ? 7  
HELX_P HELX_P32 AD5 SER A 765 ? ARG A 781 ? SER A 914  ARG A 930  1 ? 17 
HELX_P HELX_P33 AD6 GLY A 784 ? LYS A 795 ? GLY A 933  LYS A 944  1 ? 12 
HELX_P HELX_P34 AD7 ASN A 798 ? ASN A 818 ? ASN A 947  ASN A 967  1 ? 21 
HELX_P HELX_P35 AD8 PRO A 822 ? LEU A 826 ? PRO A 971  LEU A 975  5 ? 5  
HELX_P HELX_P36 AD9 ASP A 837 ? TYR A 852 ? ASP A 986  TYR A 1001 1 ? 16 
HELX_P HELX_P37 AE1 THR A 915 ? ALA A 923 ? THR A 1064 ALA A 1072 1 ? 9  
HELX_P HELX_P38 AE2 SER A 945 ? GLN A 969 ? SER A 1094 GLN A 1118 1 ? 25 
HELX_P HELX_P39 AE3 ASN A 971 ? LEU A 976 ? ASN A 1120 LEU A 1125 1 ? 6  
HELX_P HELX_P40 AE4 ASP A 977 ? SER A 991 ? ASP A 1126 SER A 1140 1 ? 15 
HELX_P HELX_P41 AE5 ARG A 992 ? GLY A 997 ? ARG A 1141 GLY A 1146 5 ? 6  
# 
_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 ? ? ? ? ? ? ? 2.065 ? ? 
metalc2 metalc ? ? A GLU 364 OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 513  A MG  1203 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc3 metalc ? ? C ADP .   O3B ? ? ? 1_555 D MG  . MG ? ? A ADP 1202 A MG  1203 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc4 metalc ? ? D MG  .   MG  ? ? ? 1_555 Q HOH . O  ? ? A MG  1203 A HOH 1320 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc5 metalc ? ? D MG  .   MG  ? ? ? 1_555 Q HOH . O  ? ? A MG  1203 A HOH 1336 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc6 metalc ? ? D MG  .   MG  ? ? ? 1_555 Q HOH . O  ? ? A MG  1203 A HOH 1400 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
# 
_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 92.8  ? 
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 82.7  ? 
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_555 172.1 ? 
4  OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1320 ? 1_555 83.6  ? 
5  OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1320 ? 1_555 97.7  ? 
6  O3B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1320 ? 1_555 75.3  ? 
7  OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1336 ? 1_555 172.2 ? 
8  OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1336 ? 1_555 94.9  ? 
9  O3B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1336 ? 1_555 89.6  ? 
10 O   ? Q HOH .   ? A HOH 1320 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1336 ? 1_555 94.3  ? 
11 OG1 ? A THR 270 ? A THR 419  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1400 ? 1_555 88.2  ? 
12 OE2 ? A GLU 364 ? A GLU 513  ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1400 ? 1_555 88.4  ? 
13 O3B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1400 ? 1_555 97.9  ? 
14 O   ? Q HOH .   ? A HOH 1320 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1400 ? 1_555 170.0 ? 
15 O   ? Q HOH .   ? A HOH 1336 ? 1_555 MG ? D MG . ? A MG 1203 ? 1_555 O   ? Q HOH .   ? A HOH 1400 ? 1_555 93.0  ? 
# 
_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       10.87 
# 
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 ? 8 ? 
# 
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 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA6 7 8 ? 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 VAL A 422 ? TYR A 425 ? VAL A 571  TYR A 574  
AA5 2 GLY A 623 ? HIS A 627 ? GLY A 772  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  
AA6 3 PHE A 894 ? ARG A 902 ? PHE A 1043 ARG A 1051 
AA6 4 ILE A 906 ? VAL A 914 ? ILE A 1055 VAL A 1063 
AA6 5 ASN A 871 ? ILE A 874 ? ASN A 1020 ILE A 1023 
AA6 6 LYS A 863 ? LEU A 865 ? LYS A 1012 LEU A 1014 
AA6 7 VAL A 855 ? GLU A 860 ? VAL A 1004 GLU A 1009 
AA6 8 PHE A 894 ? ARG A 902 ? PHE A 1043 ARG A 1051 
# 
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 ILE A 940 ? O ILE A 1089 N VAL A 936 ? N VAL A 1085 
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 GLU A 328 ? O GLU A 477  N VAL A 325 ? N VAL A 474  
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 ILE A 292 ? N ILE A 441  
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 362 ? N VAL A 511  O VAL A 392 ? O VAL A 541  
AA4 6 7 O LEU A 393 ? O LEU A 542  N ILE A 259 ? N ILE A 408  
AA4 7 8 N ILE A 260 ? N ILE A 409  O ILE A 413 ? O ILE A 562  
AA5 1 2 N GLN A 423 ? N GLN A 572  O CYS A 625 ? O CYS A 774  
AA5 2 3 O PHE A 626 ? O PHE A 775  N VAL A 580 ? N VAL A 729  
AA5 3 4 O TYR A 579 ? O TYR A 728  N LEU A 506 ? N LEU A 655  
AA5 4 5 N VAL A 507 ? N VAL A 656  O ILE A 562 ? O ILE A 711  
AA5 5 6 O VAL A 561 ? O VAL A 710  N GLN A 534 ? N GLN A 683  
AA6 1 2 N GLN A 586 ? N GLN A 735  O VAL A 603 ? O VAL A 752  
AA6 2 3 N THR A 598 ? N THR A 747  O LYS A 900 ? O LYS A 1049 
AA6 3 4 N ILE A 901 ? N ILE A 1050 O SER A 907 ? O SER A 1056 
AA6 4 5 O ILE A 906 ? O ILE A 1055 N LEU A 873 ? N LEU A 1022 
AA6 5 6 O ALA A 872 ? O ALA A 1021 N ILE A 864 ? N ILE A 1013 
AA6 6 7 O LEU A 865 ? O LEU A 1014 N TYR A 857 ? N TYR A 1006 
AA6 7 8 N CYS A 856 ? N CYS A 1005 O PHE A 895 ? O PHE A 1044 
# 
_pdbx_entry_details.entry_id                   9MFS 
_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 LYS A 468  ? ? -115.28 -106.33 
2  1 ALA A 545  ? ? -57.50  -179.57 
3  1 PHE A 556  ? ? -100.12 43.40   
4  1 PRO A 588  ? ? -48.13  166.03  
5  1 PHE A 677  ? ? -96.63  34.88   
6  1 ASP A 725  ? ? 81.31   8.22    
7  1 LEU A 777  ? ? -92.35  31.98   
8  1 ARG A 796  ? ? -148.28 30.49   
9  1 ASP A 844  ? ? -79.42  -163.34 
10 1 GLU A 897  ? ? 72.80   34.60   
11 1 LYS A 1008 ? ? -78.33  -73.33  
12 1 LYS A 1010 ? ? 50.77   -126.85 
13 1 SER A 1033 ? ? -139.25 -125.22 
14 1 THR A 1052 ? ? -116.46 -104.81 
15 1 SER A 1094 ? ? -36.40  139.16  
16 1 GLN A 1118 ? ? -150.55 74.16   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    SO4 
_pdbx_struct_special_symmetry.auth_seq_id     1214 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   O 
_pdbx_struct_special_symmetry.label_comp_id   SO4 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 1650 ? 5.90  . 
2  1 O ? A HOH 1651 ? 5.92  . 
3  1 O ? A HOH 1652 ? 6.80  . 
4  1 O ? A HOH 1653 ? 6.89  . 
5  1 O ? A HOH 1654 ? 7.65  . 
6  1 O ? A HOH 1655 ? 8.04  . 
7  1 O ? A HOH 1656 ? 11.46 . 
8  1 O ? A HOH 1657 ? 11.87 . 
9  1 O ? A HOH 1658 ? 17.43 . 
10 1 O ? A HOH 1659 ? 23.40 . 
# 
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 THR 271  ? A THR 122  
123 1 Y 1 A GLY 314  ? A GLY 165  
124 1 Y 1 A LYS 315  ? A LYS 166  
125 1 Y 1 A LEU 316  ? A LEU 167  
126 1 Y 1 A ALA 317  ? A ALA 168  
127 1 Y 1 A HIS 318  ? A HIS 169  
128 1 Y 1 A PHE 319  ? A PHE 170  
129 1 Y 1 A GLU 320  ? A GLU 171  
130 1 Y 1 A LYS 590  ? A LYS 441  
131 1 Y 1 A ASP 591  ? A ASP 442  
132 1 Y 1 A LYS 592  ? A LYS 443  
133 1 Y 1 A LYS 593  ? A LYS 444  
134 1 Y 1 A LYS 594  ? A LYS 445  
135 1 Y 1 A LYS 595  ? A LYS 446  
136 1 Y 1 A GLU 596  ? A GLU 447  
137 1 Y 1 A LYS 597  ? A LYS 448  
138 1 Y 1 A ASP 598  ? A ASP 449  
139 1 Y 1 A ASP 599  ? A ASP 450  
140 1 Y 1 A ASP 600  ? A ASP 451  
141 1 Y 1 A GLY 601  ? A GLY 452  
142 1 Y 1 A PHE 602  ? A PHE 453  
143 1 Y 1 A GLU 603  ? A GLU 454  
144 1 Y 1 A ASP 604  ? A ASP 455  
145 1 Y 1 A ASP 605  ? A ASP 456  
146 1 Y 1 A ASP 606  ? A ASP 457  
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 
A1BKX C4     C  Y N 1   
A1BKX C5     C  Y N 2   
A1BKX C7     C  Y N 3   
A1BKX C8     C  Y N 4   
A1BKX C13    C  N N 5   
A1BKX C17    C  Y N 6   
A1BKX C20    C  Y N 7   
A1BKX C21    C  Y N 8   
A1BKX C26    C  N N 9   
A1BKX C1     C  N N 10  
A1BKX C2     C  Y N 11  
A1BKX C3     C  Y N 12  
A1BKX N6     N  Y N 13  
A1BKX C9     C  Y N 14  
A1BKX S10    S  Y N 15  
A1BKX C11    C  Y N 16  
A1BKX C12    C  Y N 17  
A1BKX O14    O  N N 18  
A1BKX N15    N  N N 19  
A1BKX C16    C  Y N 20  
A1BKX C18    C  Y N 21  
A1BKX C19    C  Y N 22  
A1BKX N22    N  N N 23  
A1BKX S23    S  N N 24  
A1BKX O24    O  N N 25  
A1BKX O25    O  N N 26  
A1BKX CL27   CL N N 27  
A1BKX H1     H  N N 28  
A1BKX H2     H  N N 29  
A1BKX H3     H  N N 30  
A1BKX H4     H  N N 31  
A1BKX H5     H  N N 32  
A1BKX H6     H  N N 33  
A1BKX H7     H  N N 34  
A1BKX H8     H  N N 35  
A1BKX H9     H  N N 36  
A1BKX H10    H  N N 37  
A1BKX H11    H  N N 38  
A1BKX H12    H  N N 39  
A1BKX H13    H  N N 40  
A1BKX H14    H  N N 41  
A1BKX H15    H  N N 42  
A1BKX H16    H  N N 43  
ADP   PB     P  N N 44  
ADP   O1B    O  N N 45  
ADP   O2B    O  N N 46  
ADP   O3B    O  N N 47  
ADP   PA     P  N S 48  
ADP   O1A    O  N N 49  
ADP   O2A    O  N N 50  
ADP   O3A    O  N N 51  
ADP   "O5'"  O  N N 52  
ADP   "C5'"  C  N N 53  
ADP   "C4'"  C  N R 54  
ADP   "O4'"  O  N N 55  
ADP   "C3'"  C  N S 56  
ADP   "O3'"  O  N N 57  
ADP   "C2'"  C  N R 58  
ADP   "O2'"  O  N N 59  
ADP   "C1'"  C  N R 60  
ADP   N9     N  Y N 61  
ADP   C8     C  Y N 62  
ADP   N7     N  Y N 63  
ADP   C5     C  Y N 64  
ADP   C6     C  Y N 65  
ADP   N6     N  N N 66  
ADP   N1     N  Y N 67  
ADP   C2     C  Y N 68  
ADP   N3     N  Y N 69  
ADP   C4     C  Y N 70  
ADP   HOB2   H  N N 71  
ADP   HOB3   H  N N 72  
ADP   HOA2   H  N N 73  
ADP   "H5'1" H  N N 74  
ADP   "H5'2" H  N N 75  
ADP   "H4'"  H  N N 76  
ADP   "H3'"  H  N N 77  
ADP   "HO3'" H  N N 78  
ADP   "H2'"  H  N N 79  
ADP   "HO2'" H  N N 80  
ADP   "H1'"  H  N N 81  
ADP   H8     H  N N 82  
ADP   HN61   H  N N 83  
ADP   HN62   H  N N 84  
ADP   H2     H  N N 85  
ALA   N      N  N N 86  
ALA   CA     C  N S 87  
ALA   C      C  N N 88  
ALA   O      O  N N 89  
ALA   CB     C  N N 90  
ALA   OXT    O  N N 91  
ALA   H      H  N N 92  
ALA   H2     H  N N 93  
ALA   HA     H  N N 94  
ALA   HB1    H  N N 95  
ALA   HB2    H  N N 96  
ALA   HB3    H  N N 97  
ALA   HXT    H  N N 98  
ARG   N      N  N N 99  
ARG   CA     C  N S 100 
ARG   C      C  N N 101 
ARG   O      O  N N 102 
ARG   CB     C  N N 103 
ARG   CG     C  N N 104 
ARG   CD     C  N N 105 
ARG   NE     N  N N 106 
ARG   CZ     C  N N 107 
ARG   NH1    N  N N 108 
ARG   NH2    N  N N 109 
ARG   OXT    O  N N 110 
ARG   H      H  N N 111 
ARG   H2     H  N N 112 
ARG   HA     H  N N 113 
ARG   HB2    H  N N 114 
ARG   HB3    H  N N 115 
ARG   HG2    H  N N 116 
ARG   HG3    H  N N 117 
ARG   HD2    H  N N 118 
ARG   HD3    H  N N 119 
ARG   HE     H  N N 120 
ARG   HH11   H  N N 121 
ARG   HH12   H  N N 122 
ARG   HH21   H  N N 123 
ARG   HH22   H  N N 124 
ARG   HXT    H  N N 125 
ASN   N      N  N N 126 
ASN   CA     C  N S 127 
ASN   C      C  N N 128 
ASN   O      O  N N 129 
ASN   CB     C  N N 130 
ASN   CG     C  N N 131 
ASN   OD1    O  N N 132 
ASN   ND2    N  N N 133 
ASN   OXT    O  N N 134 
ASN   H      H  N N 135 
ASN   H2     H  N N 136 
ASN   HA     H  N N 137 
ASN   HB2    H  N N 138 
ASN   HB3    H  N N 139 
ASN   HD21   H  N N 140 
ASN   HD22   H  N N 141 
ASN   HXT    H  N N 142 
ASP   N      N  N N 143 
ASP   CA     C  N S 144 
ASP   C      C  N N 145 
ASP   O      O  N N 146 
ASP   CB     C  N N 147 
ASP   CG     C  N N 148 
ASP   OD1    O  N N 149 
ASP   OD2    O  N N 150 
ASP   OXT    O  N N 151 
ASP   H      H  N N 152 
ASP   H2     H  N N 153 
ASP   HA     H  N N 154 
ASP   HB2    H  N N 155 
ASP   HB3    H  N N 156 
ASP   HD2    H  N N 157 
ASP   HXT    H  N N 158 
CL    CL     CL N N 159 
CYS   N      N  N N 160 
CYS   CA     C  N R 161 
CYS   C      C  N N 162 
CYS   O      O  N N 163 
CYS   CB     C  N N 164 
CYS   SG     S  N N 165 
CYS   OXT    O  N N 166 
CYS   H      H  N N 167 
CYS   H2     H  N N 168 
CYS   HA     H  N N 169 
CYS   HB2    H  N N 170 
CYS   HB3    H  N N 171 
CYS   HG     H  N N 172 
CYS   HXT    H  N N 173 
EDO   C1     C  N N 174 
EDO   O1     O  N N 175 
EDO   C2     C  N N 176 
EDO   O2     O  N N 177 
EDO   H11    H  N N 178 
EDO   H12    H  N N 179 
EDO   HO1    H  N N 180 
EDO   H21    H  N N 181 
EDO   H22    H  N N 182 
EDO   HO2    H  N N 183 
GLN   N      N  N N 184 
GLN   CA     C  N S 185 
GLN   C      C  N N 186 
GLN   O      O  N N 187 
GLN   CB     C  N N 188 
GLN   CG     C  N N 189 
GLN   CD     C  N N 190 
GLN   OE1    O  N N 191 
GLN   NE2    N  N N 192 
GLN   OXT    O  N N 193 
GLN   H      H  N N 194 
GLN   H2     H  N N 195 
GLN   HA     H  N N 196 
GLN   HB2    H  N N 197 
GLN   HB3    H  N N 198 
GLN   HG2    H  N N 199 
GLN   HG3    H  N N 200 
GLN   HE21   H  N N 201 
GLN   HE22   H  N N 202 
GLN   HXT    H  N N 203 
GLU   N      N  N N 204 
GLU   CA     C  N S 205 
GLU   C      C  N N 206 
GLU   O      O  N N 207 
GLU   CB     C  N N 208 
GLU   CG     C  N N 209 
GLU   CD     C  N N 210 
GLU   OE1    O  N N 211 
GLU   OE2    O  N N 212 
GLU   OXT    O  N N 213 
GLU   H      H  N N 214 
GLU   H2     H  N N 215 
GLU   HA     H  N N 216 
GLU   HB2    H  N N 217 
GLU   HB3    H  N N 218 
GLU   HG2    H  N N 219 
GLU   HG3    H  N N 220 
GLU   HE2    H  N N 221 
GLU   HXT    H  N N 222 
GLY   N      N  N N 223 
GLY   CA     C  N N 224 
GLY   C      C  N N 225 
GLY   O      O  N N 226 
GLY   OXT    O  N N 227 
GLY   H      H  N N 228 
GLY   H2     H  N N 229 
GLY   HA2    H  N N 230 
GLY   HA3    H  N N 231 
GLY   HXT    H  N N 232 
HIS   N      N  N N 233 
HIS   CA     C  N S 234 
HIS   C      C  N N 235 
HIS   O      O  N N 236 
HIS   CB     C  N N 237 
HIS   CG     C  Y N 238 
HIS   ND1    N  Y N 239 
HIS   CD2    C  Y N 240 
HIS   CE1    C  Y N 241 
HIS   NE2    N  Y N 242 
HIS   OXT    O  N N 243 
HIS   H      H  N N 244 
HIS   H2     H  N N 245 
HIS   HA     H  N N 246 
HIS   HB2    H  N N 247 
HIS   HB3    H  N N 248 
HIS   HD1    H  N N 249 
HIS   HD2    H  N N 250 
HIS   HE1    H  N N 251 
HIS   HE2    H  N N 252 
HIS   HXT    H  N N 253 
HOH   O      O  N N 254 
HOH   H1     H  N N 255 
HOH   H2     H  N N 256 
ILE   N      N  N N 257 
ILE   CA     C  N S 258 
ILE   C      C  N N 259 
ILE   O      O  N N 260 
ILE   CB     C  N S 261 
ILE   CG1    C  N N 262 
ILE   CG2    C  N N 263 
ILE   CD1    C  N N 264 
ILE   OXT    O  N N 265 
ILE   H      H  N N 266 
ILE   H2     H  N N 267 
ILE   HA     H  N N 268 
ILE   HB     H  N N 269 
ILE   HG12   H  N N 270 
ILE   HG13   H  N N 271 
ILE   HG21   H  N N 272 
ILE   HG22   H  N N 273 
ILE   HG23   H  N N 274 
ILE   HD11   H  N N 275 
ILE   HD12   H  N N 276 
ILE   HD13   H  N N 277 
ILE   HXT    H  N N 278 
LEU   N      N  N N 279 
LEU   CA     C  N S 280 
LEU   C      C  N N 281 
LEU   O      O  N N 282 
LEU   CB     C  N N 283 
LEU   CG     C  N N 284 
LEU   CD1    C  N N 285 
LEU   CD2    C  N N 286 
LEU   OXT    O  N N 287 
LEU   H      H  N N 288 
LEU   H2     H  N N 289 
LEU   HA     H  N N 290 
LEU   HB2    H  N N 291 
LEU   HB3    H  N N 292 
LEU   HG     H  N N 293 
LEU   HD11   H  N N 294 
LEU   HD12   H  N N 295 
LEU   HD13   H  N N 296 
LEU   HD21   H  N N 297 
LEU   HD22   H  N N 298 
LEU   HD23   H  N N 299 
LEU   HXT    H  N N 300 
LYS   N      N  N N 301 
LYS   CA     C  N S 302 
LYS   C      C  N N 303 
LYS   O      O  N N 304 
LYS   CB     C  N N 305 
LYS   CG     C  N N 306 
LYS   CD     C  N N 307 
LYS   CE     C  N N 308 
LYS   NZ     N  N N 309 
LYS   OXT    O  N N 310 
LYS   H      H  N N 311 
LYS   H2     H  N N 312 
LYS   HA     H  N N 313 
LYS   HB2    H  N N 314 
LYS   HB3    H  N N 315 
LYS   HG2    H  N N 316 
LYS   HG3    H  N N 317 
LYS   HD2    H  N N 318 
LYS   HD3    H  N N 319 
LYS   HE2    H  N N 320 
LYS   HE3    H  N N 321 
LYS   HZ1    H  N N 322 
LYS   HZ2    H  N N 323 
LYS   HZ3    H  N N 324 
LYS   HXT    H  N N 325 
MET   N      N  N N 326 
MET   CA     C  N S 327 
MET   C      C  N N 328 
MET   O      O  N N 329 
MET   CB     C  N N 330 
MET   CG     C  N N 331 
MET   SD     S  N N 332 
MET   CE     C  N N 333 
MET   OXT    O  N N 334 
MET   H      H  N N 335 
MET   H2     H  N N 336 
MET   HA     H  N N 337 
MET   HB2    H  N N 338 
MET   HB3    H  N N 339 
MET   HG2    H  N N 340 
MET   HG3    H  N N 341 
MET   HE1    H  N N 342 
MET   HE2    H  N N 343 
MET   HE3    H  N N 344 
MET   HXT    H  N N 345 
MG    MG     MG N N 346 
PHE   N      N  N N 347 
PHE   CA     C  N S 348 
PHE   C      C  N N 349 
PHE   O      O  N N 350 
PHE   CB     C  N N 351 
PHE   CG     C  Y N 352 
PHE   CD1    C  Y N 353 
PHE   CD2    C  Y N 354 
PHE   CE1    C  Y N 355 
PHE   CE2    C  Y N 356 
PHE   CZ     C  Y N 357 
PHE   OXT    O  N N 358 
PHE   H      H  N N 359 
PHE   H2     H  N N 360 
PHE   HA     H  N N 361 
PHE   HB2    H  N N 362 
PHE   HB3    H  N N 363 
PHE   HD1    H  N N 364 
PHE   HD2    H  N N 365 
PHE   HE1    H  N N 366 
PHE   HE2    H  N N 367 
PHE   HZ     H  N N 368 
PHE   HXT    H  N N 369 
PRO   N      N  N N 370 
PRO   CA     C  N S 371 
PRO   C      C  N N 372 
PRO   O      O  N N 373 
PRO   CB     C  N N 374 
PRO   CG     C  N N 375 
PRO   CD     C  N N 376 
PRO   OXT    O  N N 377 
PRO   H      H  N N 378 
PRO   HA     H  N N 379 
PRO   HB2    H  N N 380 
PRO   HB3    H  N N 381 
PRO   HG2    H  N N 382 
PRO   HG3    H  N N 383 
PRO   HD2    H  N N 384 
PRO   HD3    H  N N 385 
PRO   HXT    H  N N 386 
SER   N      N  N N 387 
SER   CA     C  N S 388 
SER   C      C  N N 389 
SER   O      O  N N 390 
SER   CB     C  N N 391 
SER   OG     O  N N 392 
SER   OXT    O  N N 393 
SER   H      H  N N 394 
SER   H2     H  N N 395 
SER   HA     H  N N 396 
SER   HB2    H  N N 397 
SER   HB3    H  N N 398 
SER   HG     H  N N 399 
SER   HXT    H  N N 400 
SO4   S      S  N N 401 
SO4   O1     O  N N 402 
SO4   O2     O  N N 403 
SO4   O3     O  N N 404 
SO4   O4     O  N N 405 
THR   N      N  N N 406 
THR   CA     C  N S 407 
THR   C      C  N N 408 
THR   O      O  N N 409 
THR   CB     C  N R 410 
THR   OG1    O  N N 411 
THR   CG2    C  N N 412 
THR   OXT    O  N N 413 
THR   H      H  N N 414 
THR   H2     H  N N 415 
THR   HA     H  N N 416 
THR   HB     H  N N 417 
THR   HG1    H  N N 418 
THR   HG21   H  N N 419 
THR   HG22   H  N N 420 
THR   HG23   H  N N 421 
THR   HXT    H  N N 422 
TRP   N      N  N N 423 
TRP   CA     C  N S 424 
TRP   C      C  N N 425 
TRP   O      O  N N 426 
TRP   CB     C  N N 427 
TRP   CG     C  Y N 428 
TRP   CD1    C  Y N 429 
TRP   CD2    C  Y N 430 
TRP   NE1    N  Y N 431 
TRP   CE2    C  Y N 432 
TRP   CE3    C  Y N 433 
TRP   CZ2    C  Y N 434 
TRP   CZ3    C  Y N 435 
TRP   CH2    C  Y N 436 
TRP   OXT    O  N N 437 
TRP   H      H  N N 438 
TRP   H2     H  N N 439 
TRP   HA     H  N N 440 
TRP   HB2    H  N N 441 
TRP   HB3    H  N N 442 
TRP   HD1    H  N N 443 
TRP   HE1    H  N N 444 
TRP   HE3    H  N N 445 
TRP   HZ2    H  N N 446 
TRP   HZ3    H  N N 447 
TRP   HH2    H  N N 448 
TRP   HXT    H  N N 449 
TYR   N      N  N N 450 
TYR   CA     C  N S 451 
TYR   C      C  N N 452 
TYR   O      O  N N 453 
TYR   CB     C  N N 454 
TYR   CG     C  Y N 455 
TYR   CD1    C  Y N 456 
TYR   CD2    C  Y N 457 
TYR   CE1    C  Y N 458 
TYR   CE2    C  Y N 459 
TYR   CZ     C  Y N 460 
TYR   OH     O  N N 461 
TYR   OXT    O  N N 462 
TYR   H      H  N N 463 
TYR   H2     H  N N 464 
TYR   HA     H  N N 465 
TYR   HB2    H  N N 466 
TYR   HB3    H  N N 467 
TYR   HD1    H  N N 468 
TYR   HD2    H  N N 469 
TYR   HE1    H  N N 470 
TYR   HE2    H  N N 471 
TYR   HH     H  N N 472 
TYR   HXT    H  N N 473 
VAL   N      N  N N 474 
VAL   CA     C  N S 475 
VAL   C      C  N N 476 
VAL   O      O  N N 477 
VAL   CB     C  N N 478 
VAL   CG1    C  N N 479 
VAL   CG2    C  N N 480 
VAL   OXT    O  N N 481 
VAL   H      H  N N 482 
VAL   H2     H  N N 483 
VAL   HA     H  N N 484 
VAL   HB     H  N N 485 
VAL   HG11   H  N N 486 
VAL   HG12   H  N N 487 
VAL   HG13   H  N N 488 
VAL   HG21   H  N N 489 
VAL   HG22   H  N N 490 
VAL   HG23   H  N N 491 
VAL   HXT    H  N N 492 
# 
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 
A1BKX O24   S23    doub N N 1   
A1BKX O25   S23    doub N N 2   
A1BKX S23   C26    sing N N 3   
A1BKX S23   N22    sing N N 4   
A1BKX N22   C20    sing N N 5   
A1BKX C19   C20    doub Y N 6   
A1BKX C19   C18    sing Y N 7   
A1BKX C20   C21    sing Y N 8   
A1BKX CL27  C18    sing N N 9   
A1BKX C18   C17    doub Y N 10  
A1BKX C21   C16    doub Y N 11  
A1BKX C17   C16    sing Y N 12  
A1BKX C16   N15    sing N N 13  
A1BKX N15   C13    sing N N 14  
A1BKX O14   C13    doub N N 15  
A1BKX C13   C11    sing N N 16  
A1BKX C11   C12    doub Y N 17  
A1BKX C11   S10    sing Y N 18  
A1BKX C12   C8     sing Y N 19  
A1BKX S10   C9     sing Y N 20  
A1BKX N6    C5     doub Y N 21  
A1BKX N6    C7     sing Y N 22  
A1BKX C8    C9     doub Y N 23  
A1BKX C8    C7     sing N N 24  
A1BKX C5    C4     sing Y N 25  
A1BKX C7    C2     doub Y N 26  
A1BKX C4    C3     doub Y N 27  
A1BKX C2    C3     sing Y N 28  
A1BKX C2    C1     sing N N 29  
A1BKX C4    H1     sing N N 30  
A1BKX C5    H2     sing N N 31  
A1BKX C17   H3     sing N N 32  
A1BKX C21   H4     sing N N 33  
A1BKX C26   H5     sing N N 34  
A1BKX C26   H6     sing N N 35  
A1BKX C26   H7     sing N N 36  
A1BKX C1    H8     sing N N 37  
A1BKX C1    H9     sing N N 38  
A1BKX C1    H10    sing N N 39  
A1BKX C3    H11    sing N N 40  
A1BKX C9    H12    sing N N 41  
A1BKX C12   H13    sing N N 42  
A1BKX N15   H14    sing N N 43  
A1BKX C19   H15    sing N N 44  
A1BKX N22   H16    sing N N 45  
ADP   PB    O1B    doub N N 46  
ADP   PB    O2B    sing N N 47  
ADP   PB    O3B    sing N N 48  
ADP   PB    O3A    sing N N 49  
ADP   O2B   HOB2   sing N N 50  
ADP   O3B   HOB3   sing N N 51  
ADP   PA    O1A    doub N N 52  
ADP   PA    O2A    sing N N 53  
ADP   PA    O3A    sing N N 54  
ADP   PA    "O5'"  sing N N 55  
ADP   O2A   HOA2   sing N N 56  
ADP   "O5'" "C5'"  sing N N 57  
ADP   "C5'" "C4'"  sing N N 58  
ADP   "C5'" "H5'1" sing N N 59  
ADP   "C5'" "H5'2" sing N N 60  
ADP   "C4'" "O4'"  sing N N 61  
ADP   "C4'" "C3'"  sing N N 62  
ADP   "C4'" "H4'"  sing N N 63  
ADP   "O4'" "C1'"  sing N N 64  
ADP   "C3'" "O3'"  sing N N 65  
ADP   "C3'" "C2'"  sing N N 66  
ADP   "C3'" "H3'"  sing N N 67  
ADP   "O3'" "HO3'" sing N N 68  
ADP   "C2'" "O2'"  sing N N 69  
ADP   "C2'" "C1'"  sing N N 70  
ADP   "C2'" "H2'"  sing N N 71  
ADP   "O2'" "HO2'" sing N N 72  
ADP   "C1'" N9     sing N N 73  
ADP   "C1'" "H1'"  sing N N 74  
ADP   N9    C8     sing Y N 75  
ADP   N9    C4     sing Y N 76  
ADP   C8    N7     doub Y N 77  
ADP   C8    H8     sing N N 78  
ADP   N7    C5     sing Y N 79  
ADP   C5    C6     sing Y N 80  
ADP   C5    C4     doub Y N 81  
ADP   C6    N6     sing N N 82  
ADP   C6    N1     doub Y N 83  
ADP   N6    HN61   sing N N 84  
ADP   N6    HN62   sing N N 85  
ADP   N1    C2     sing Y N 86  
ADP   C2    N3     doub Y N 87  
ADP   C2    H2     sing N N 88  
ADP   N3    C4     sing Y N 89  
ALA   N     CA     sing N N 90  
ALA   N     H      sing N N 91  
ALA   N     H2     sing N N 92  
ALA   CA    C      sing N N 93  
ALA   CA    CB     sing N N 94  
ALA   CA    HA     sing N N 95  
ALA   C     O      doub N N 96  
ALA   C     OXT    sing N N 97  
ALA   CB    HB1    sing N N 98  
ALA   CB    HB2    sing N N 99  
ALA   CB    HB3    sing N N 100 
ALA   OXT   HXT    sing N N 101 
ARG   N     CA     sing N N 102 
ARG   N     H      sing N N 103 
ARG   N     H2     sing N N 104 
ARG   CA    C      sing N N 105 
ARG   CA    CB     sing N N 106 
ARG   CA    HA     sing N N 107 
ARG   C     O      doub N N 108 
ARG   C     OXT    sing N N 109 
ARG   CB    CG     sing N N 110 
ARG   CB    HB2    sing N N 111 
ARG   CB    HB3    sing N N 112 
ARG   CG    CD     sing N N 113 
ARG   CG    HG2    sing N N 114 
ARG   CG    HG3    sing N N 115 
ARG   CD    NE     sing N N 116 
ARG   CD    HD2    sing N N 117 
ARG   CD    HD3    sing N N 118 
ARG   NE    CZ     sing N N 119 
ARG   NE    HE     sing N N 120 
ARG   CZ    NH1    sing N N 121 
ARG   CZ    NH2    doub N N 122 
ARG   NH1   HH11   sing N N 123 
ARG   NH1   HH12   sing N N 124 
ARG   NH2   HH21   sing N N 125 
ARG   NH2   HH22   sing N N 126 
ARG   OXT   HXT    sing N N 127 
ASN   N     CA     sing N N 128 
ASN   N     H      sing N N 129 
ASN   N     H2     sing N N 130 
ASN   CA    C      sing N N 131 
ASN   CA    CB     sing N N 132 
ASN   CA    HA     sing N N 133 
ASN   C     O      doub N N 134 
ASN   C     OXT    sing N N 135 
ASN   CB    CG     sing N N 136 
ASN   CB    HB2    sing N N 137 
ASN   CB    HB3    sing N N 138 
ASN   CG    OD1    doub N N 139 
ASN   CG    ND2    sing N N 140 
ASN   ND2   HD21   sing N N 141 
ASN   ND2   HD22   sing N N 142 
ASN   OXT   HXT    sing N N 143 
ASP   N     CA     sing N N 144 
ASP   N     H      sing N N 145 
ASP   N     H2     sing N N 146 
ASP   CA    C      sing N N 147 
ASP   CA    CB     sing N N 148 
ASP   CA    HA     sing N N 149 
ASP   C     O      doub N N 150 
ASP   C     OXT    sing N N 151 
ASP   CB    CG     sing N N 152 
ASP   CB    HB2    sing N N 153 
ASP   CB    HB3    sing N N 154 
ASP   CG    OD1    doub N N 155 
ASP   CG    OD2    sing N N 156 
ASP   OD2   HD2    sing N N 157 
ASP   OXT   HXT    sing N N 158 
CYS   N     CA     sing N N 159 
CYS   N     H      sing N N 160 
CYS   N     H2     sing N N 161 
CYS   CA    C      sing N N 162 
CYS   CA    CB     sing N N 163 
CYS   CA    HA     sing N N 164 
CYS   C     O      doub N N 165 
CYS   C     OXT    sing N N 166 
CYS   CB    SG     sing N N 167 
CYS   CB    HB2    sing N N 168 
CYS   CB    HB3    sing N N 169 
CYS   SG    HG     sing N N 170 
CYS   OXT   HXT    sing N N 171 
EDO   C1    O1     sing N N 172 
EDO   C1    C2     sing N N 173 
EDO   C1    H11    sing N N 174 
EDO   C1    H12    sing N N 175 
EDO   O1    HO1    sing N N 176 
EDO   C2    O2     sing N N 177 
EDO   C2    H21    sing N N 178 
EDO   C2    H22    sing N N 179 
EDO   O2    HO2    sing N N 180 
GLN   N     CA     sing N N 181 
GLN   N     H      sing N N 182 
GLN   N     H2     sing N N 183 
GLN   CA    C      sing N N 184 
GLN   CA    CB     sing N N 185 
GLN   CA    HA     sing N N 186 
GLN   C     O      doub N N 187 
GLN   C     OXT    sing N N 188 
GLN   CB    CG     sing N N 189 
GLN   CB    HB2    sing N N 190 
GLN   CB    HB3    sing N N 191 
GLN   CG    CD     sing N N 192 
GLN   CG    HG2    sing N N 193 
GLN   CG    HG3    sing N N 194 
GLN   CD    OE1    doub N N 195 
GLN   CD    NE2    sing N N 196 
GLN   NE2   HE21   sing N N 197 
GLN   NE2   HE22   sing N N 198 
GLN   OXT   HXT    sing N N 199 
GLU   N     CA     sing N N 200 
GLU   N     H      sing N N 201 
GLU   N     H2     sing N N 202 
GLU   CA    C      sing N N 203 
GLU   CA    CB     sing N N 204 
GLU   CA    HA     sing N N 205 
GLU   C     O      doub N N 206 
GLU   C     OXT    sing N N 207 
GLU   CB    CG     sing N N 208 
GLU   CB    HB2    sing N N 209 
GLU   CB    HB3    sing N N 210 
GLU   CG    CD     sing N N 211 
GLU   CG    HG2    sing N N 212 
GLU   CG    HG3    sing N N 213 
GLU   CD    OE1    doub N N 214 
GLU   CD    OE2    sing N N 215 
GLU   OE2   HE2    sing N N 216 
GLU   OXT   HXT    sing N N 217 
GLY   N     CA     sing N N 218 
GLY   N     H      sing N N 219 
GLY   N     H2     sing N N 220 
GLY   CA    C      sing N N 221 
GLY   CA    HA2    sing N N 222 
GLY   CA    HA3    sing N N 223 
GLY   C     O      doub N N 224 
GLY   C     OXT    sing N N 225 
GLY   OXT   HXT    sing N N 226 
HIS   N     CA     sing N N 227 
HIS   N     H      sing N N 228 
HIS   N     H2     sing N N 229 
HIS   CA    C      sing N N 230 
HIS   CA    CB     sing N N 231 
HIS   CA    HA     sing N N 232 
HIS   C     O      doub N N 233 
HIS   C     OXT    sing N N 234 
HIS   CB    CG     sing N N 235 
HIS   CB    HB2    sing N N 236 
HIS   CB    HB3    sing N N 237 
HIS   CG    ND1    sing Y N 238 
HIS   CG    CD2    doub Y N 239 
HIS   ND1   CE1    doub Y N 240 
HIS   ND1   HD1    sing N N 241 
HIS   CD2   NE2    sing Y N 242 
HIS   CD2   HD2    sing N N 243 
HIS   CE1   NE2    sing Y N 244 
HIS   CE1   HE1    sing N N 245 
HIS   NE2   HE2    sing N N 246 
HIS   OXT   HXT    sing N N 247 
HOH   O     H1     sing N N 248 
HOH   O     H2     sing N N 249 
ILE   N     CA     sing N N 250 
ILE   N     H      sing N N 251 
ILE   N     H2     sing N N 252 
ILE   CA    C      sing N N 253 
ILE   CA    CB     sing N N 254 
ILE   CA    HA     sing N N 255 
ILE   C     O      doub N N 256 
ILE   C     OXT    sing N N 257 
ILE   CB    CG1    sing N N 258 
ILE   CB    CG2    sing N N 259 
ILE   CB    HB     sing N N 260 
ILE   CG1   CD1    sing N N 261 
ILE   CG1   HG12   sing N N 262 
ILE   CG1   HG13   sing N N 263 
ILE   CG2   HG21   sing N N 264 
ILE   CG2   HG22   sing N N 265 
ILE   CG2   HG23   sing N N 266 
ILE   CD1   HD11   sing N N 267 
ILE   CD1   HD12   sing N N 268 
ILE   CD1   HD13   sing N N 269 
ILE   OXT   HXT    sing N N 270 
LEU   N     CA     sing N N 271 
LEU   N     H      sing N N 272 
LEU   N     H2     sing N N 273 
LEU   CA    C      sing N N 274 
LEU   CA    CB     sing N N 275 
LEU   CA    HA     sing N N 276 
LEU   C     O      doub N N 277 
LEU   C     OXT    sing N N 278 
LEU   CB    CG     sing N N 279 
LEU   CB    HB2    sing N N 280 
LEU   CB    HB3    sing N N 281 
LEU   CG    CD1    sing N N 282 
LEU   CG    CD2    sing N N 283 
LEU   CG    HG     sing N N 284 
LEU   CD1   HD11   sing N N 285 
LEU   CD1   HD12   sing N N 286 
LEU   CD1   HD13   sing N N 287 
LEU   CD2   HD21   sing N N 288 
LEU   CD2   HD22   sing N N 289 
LEU   CD2   HD23   sing N N 290 
LEU   OXT   HXT    sing N N 291 
LYS   N     CA     sing N N 292 
LYS   N     H      sing N N 293 
LYS   N     H2     sing N N 294 
LYS   CA    C      sing N N 295 
LYS   CA    CB     sing N N 296 
LYS   CA    HA     sing N N 297 
LYS   C     O      doub N N 298 
LYS   C     OXT    sing N N 299 
LYS   CB    CG     sing N N 300 
LYS   CB    HB2    sing N N 301 
LYS   CB    HB3    sing N N 302 
LYS   CG    CD     sing N N 303 
LYS   CG    HG2    sing N N 304 
LYS   CG    HG3    sing N N 305 
LYS   CD    CE     sing N N 306 
LYS   CD    HD2    sing N N 307 
LYS   CD    HD3    sing N N 308 
LYS   CE    NZ     sing N N 309 
LYS   CE    HE2    sing N N 310 
LYS   CE    HE3    sing N N 311 
LYS   NZ    HZ1    sing N N 312 
LYS   NZ    HZ2    sing N N 313 
LYS   NZ    HZ3    sing N N 314 
LYS   OXT   HXT    sing N N 315 
MET   N     CA     sing N N 316 
MET   N     H      sing N N 317 
MET   N     H2     sing N N 318 
MET   CA    C      sing N N 319 
MET   CA    CB     sing N N 320 
MET   CA    HA     sing N N 321 
MET   C     O      doub N N 322 
MET   C     OXT    sing N N 323 
MET   CB    CG     sing N N 324 
MET   CB    HB2    sing N N 325 
MET   CB    HB3    sing N N 326 
MET   CG    SD     sing N N 327 
MET   CG    HG2    sing N N 328 
MET   CG    HG3    sing N N 329 
MET   SD    CE     sing N N 330 
MET   CE    HE1    sing N N 331 
MET   CE    HE2    sing N N 332 
MET   CE    HE3    sing N N 333 
MET   OXT   HXT    sing N N 334 
PHE   N     CA     sing N N 335 
PHE   N     H      sing N N 336 
PHE   N     H2     sing N N 337 
PHE   CA    C      sing N N 338 
PHE   CA    CB     sing N N 339 
PHE   CA    HA     sing N N 340 
PHE   C     O      doub N N 341 
PHE   C     OXT    sing N N 342 
PHE   CB    CG     sing N N 343 
PHE   CB    HB2    sing N N 344 
PHE   CB    HB3    sing N N 345 
PHE   CG    CD1    doub Y N 346 
PHE   CG    CD2    sing Y N 347 
PHE   CD1   CE1    sing Y N 348 
PHE   CD1   HD1    sing N N 349 
PHE   CD2   CE2    doub Y N 350 
PHE   CD2   HD2    sing N N 351 
PHE   CE1   CZ     doub Y N 352 
PHE   CE1   HE1    sing N N 353 
PHE   CE2   CZ     sing Y N 354 
PHE   CE2   HE2    sing N N 355 
PHE   CZ    HZ     sing N N 356 
PHE   OXT   HXT    sing N N 357 
PRO   N     CA     sing N N 358 
PRO   N     CD     sing N N 359 
PRO   N     H      sing N N 360 
PRO   CA    C      sing N N 361 
PRO   CA    CB     sing N N 362 
PRO   CA    HA     sing N N 363 
PRO   C     O      doub N N 364 
PRO   C     OXT    sing N N 365 
PRO   CB    CG     sing N N 366 
PRO   CB    HB2    sing N N 367 
PRO   CB    HB3    sing N N 368 
PRO   CG    CD     sing N N 369 
PRO   CG    HG2    sing N N 370 
PRO   CG    HG3    sing N N 371 
PRO   CD    HD2    sing N N 372 
PRO   CD    HD3    sing N N 373 
PRO   OXT   HXT    sing N N 374 
SER   N     CA     sing N N 375 
SER   N     H      sing N N 376 
SER   N     H2     sing N N 377 
SER   CA    C      sing N N 378 
SER   CA    CB     sing N N 379 
SER   CA    HA     sing N N 380 
SER   C     O      doub N N 381 
SER   C     OXT    sing N N 382 
SER   CB    OG     sing N N 383 
SER   CB    HB2    sing N N 384 
SER   CB    HB3    sing N N 385 
SER   OG    HG     sing N N 386 
SER   OXT   HXT    sing N N 387 
SO4   S     O1     doub N N 388 
SO4   S     O2     doub N N 389 
SO4   S     O3     sing N N 390 
SO4   S     O4     sing N N 391 
THR   N     CA     sing N N 392 
THR   N     H      sing N N 393 
THR   N     H2     sing N N 394 
THR   CA    C      sing N N 395 
THR   CA    CB     sing N N 396 
THR   CA    HA     sing N N 397 
THR   C     O      doub N N 398 
THR   C     OXT    sing N N 399 
THR   CB    OG1    sing N N 400 
THR   CB    CG2    sing N N 401 
THR   CB    HB     sing N N 402 
THR   OG1   HG1    sing N N 403 
THR   CG2   HG21   sing N N 404 
THR   CG2   HG22   sing N N 405 
THR   CG2   HG23   sing N N 406 
THR   OXT   HXT    sing N N 407 
TRP   N     CA     sing N N 408 
TRP   N     H      sing N N 409 
TRP   N     H2     sing N N 410 
TRP   CA    C      sing N N 411 
TRP   CA    CB     sing N N 412 
TRP   CA    HA     sing N N 413 
TRP   C     O      doub N N 414 
TRP   C     OXT    sing N N 415 
TRP   CB    CG     sing N N 416 
TRP   CB    HB2    sing N N 417 
TRP   CB    HB3    sing N N 418 
TRP   CG    CD1    doub Y N 419 
TRP   CG    CD2    sing Y N 420 
TRP   CD1   NE1    sing Y N 421 
TRP   CD1   HD1    sing N N 422 
TRP   CD2   CE2    doub Y N 423 
TRP   CD2   CE3    sing Y N 424 
TRP   NE1   CE2    sing Y N 425 
TRP   NE1   HE1    sing N N 426 
TRP   CE2   CZ2    sing Y N 427 
TRP   CE3   CZ3    doub Y N 428 
TRP   CE3   HE3    sing N N 429 
TRP   CZ2   CH2    doub Y N 430 
TRP   CZ2   HZ2    sing N N 431 
TRP   CZ3   CH2    sing Y N 432 
TRP   CZ3   HZ3    sing N N 433 
TRP   CH2   HH2    sing N N 434 
TRP   OXT   HXT    sing N N 435 
TYR   N     CA     sing N N 436 
TYR   N     H      sing N N 437 
TYR   N     H2     sing N N 438 
TYR   CA    C      sing N N 439 
TYR   CA    CB     sing N N 440 
TYR   CA    HA     sing N N 441 
TYR   C     O      doub N N 442 
TYR   C     OXT    sing N N 443 
TYR   CB    CG     sing N N 444 
TYR   CB    HB2    sing N N 445 
TYR   CB    HB3    sing N N 446 
TYR   CG    CD1    doub Y N 447 
TYR   CG    CD2    sing Y N 448 
TYR   CD1   CE1    sing Y N 449 
TYR   CD1   HD1    sing N N 450 
TYR   CD2   CE2    doub Y N 451 
TYR   CD2   HD2    sing N N 452 
TYR   CE1   CZ     doub Y N 453 
TYR   CE1   HE1    sing N N 454 
TYR   CE2   CZ     sing Y N 455 
TYR   CE2   HE2    sing N N 456 
TYR   CZ    OH     sing N N 457 
TYR   OH    HH     sing N N 458 
TYR   OXT   HXT    sing N N 459 
VAL   N     CA     sing N N 460 
VAL   N     H      sing N N 461 
VAL   N     H2     sing N N 462 
VAL   CA    C      sing N N 463 
VAL   CA    CB     sing N N 464 
VAL   CA    HA     sing N N 465 
VAL   C     O      doub N N 466 
VAL   C     OXT    sing N N 467 
VAL   CB    CG1    sing N N 468 
VAL   CB    CG2    sing N N 469 
VAL   CB    HB     sing N N 470 
VAL   CG1   HG11   sing N N 471 
VAL   CG1   HG12   sing N N 472 
VAL   CG1   HG13   sing N N 473 
VAL   CG2   HG21   sing N N 474 
VAL   CG2   HG22   sing N N 475 
VAL   CG2   HG23   sing N N 476 
VAL   OXT   HXT    sing N N 477 
# 
_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                    9MFS 
_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]   0.011567 
_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]   0.011567 
_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]   0.002849 
_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  
CL 
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     . VAL   A 1 123  ? -17.250 -28.230 -65.347 1.00 104.49 ? 272  VAL   A N     1 
ATOM   2    C  CA    . VAL   A 1 123  ? -17.906 -28.484 -64.026 1.00 105.17 ? 272  VAL   A CA    1 
ATOM   3    C  C     . VAL   A 1 123  ? -19.300 -27.836 -64.005 1.00 95.61  ? 272  VAL   A C     1 
ATOM   4    O  O     . VAL   A 1 123  ? -19.567 -26.949 -64.836 1.00 91.06  ? 272  VAL   A O     1 
ATOM   5    C  CB    . VAL   A 1 123  ? -17.039 -27.974 -62.854 1.00 112.24 ? 272  VAL   A CB    1 
ATOM   6    C  CG1   . VAL   A 1 123  ? -15.594 -28.435 -62.974 1.00 114.17 ? 272  VAL   A CG1   1 
ATOM   7    C  CG2   . VAL   A 1 123  ? -17.100 -26.459 -62.701 1.00 115.08 ? 272  VAL   A CG2   1 
ATOM   8    N  N     . GLU   A 1 124  ? -20.147 -28.277 -63.071 1.00 95.22  ? 273  GLU   A N     1 
ATOM   9    C  CA    . GLU   A 1 124  ? -21.482 -27.692 -62.762 1.00 97.19  ? 273  GLU   A CA    1 
ATOM   10   C  C     . GLU   A 1 124  ? -21.392 -26.166 -62.734 1.00 87.01  ? 273  GLU   A C     1 
ATOM   11   O  O     . GLU   A 1 124  ? -20.441 -25.602 -62.198 1.00 82.60  ? 273  GLU   A O     1 
ATOM   12   C  CB    . GLU   A 1 124  ? -21.985 -28.206 -61.407 1.00 105.22 ? 273  GLU   A CB    1 
ATOM   13   C  CG    . GLU   A 1 124  ? -22.790 -29.493 -61.484 1.00 110.05 ? 273  GLU   A CG    1 
ATOM   14   C  CD    . GLU   A 1 124  ? -24.285 -29.297 -61.694 1.00 119.09 ? 273  GLU   A CD    1 
ATOM   15   O  OE1   . GLU   A 1 124  ? -25.043 -29.478 -60.715 1.00 113.61 ? 273  GLU   A OE1   1 
ATOM   16   O  OE2   . GLU   A 1 124  ? -24.695 -28.975 -62.838 1.00 114.31 ? 273  GLU   A OE2   1 
ATOM   17   N  N     . PRO   A 1 125  ? -22.392 -25.435 -63.271 1.00 76.22  ? 274  PRO   A N     1 
ATOM   18   C  CA    . PRO   A 1 125  ? -22.404 -23.985 -63.141 1.00 67.60  ? 274  PRO   A CA    1 
ATOM   19   C  C     . PRO   A 1 125  ? -22.482 -23.662 -61.643 1.00 66.39  ? 274  PRO   A C     1 
ATOM   20   O  O     . PRO   A 1 125  ? -23.193 -24.358 -60.944 1.00 63.70  ? 274  PRO   A O     1 
ATOM   21   C  CB    . PRO   A 1 125  ? -23.644 -23.520 -63.920 1.00 68.67  ? 274  PRO   A CB    1 
ATOM   22   C  CG    . PRO   A 1 125  ? -24.496 -24.758 -64.107 1.00 72.92  ? 274  PRO   A CG    1 
ATOM   23   C  CD    . PRO   A 1 125  ? -23.580 -25.955 -63.963 1.00 73.86  ? 274  PRO   A CD    1 
ATOM   24   N  N     . TYR   A 1 126  ? -21.723 -22.660 -61.188 1.00 62.01  ? 275  TYR   A N     1 
ATOM   25   C  CA    . TYR   A 1 126  ? -21.677 -22.217 -59.771 1.00 56.75  ? 275  TYR   A CA    1 
ATOM   26   C  C     . TYR   A 1 126  ? -22.878 -21.317 -59.506 1.00 53.68  ? 275  TYR   A C     1 
ATOM   27   O  O     . TYR   A 1 126  ? -23.112 -20.420 -60.315 1.00 54.44  ? 275  TYR   A O     1 
ATOM   28   C  CB    . TYR   A 1 126  ? -20.383 -21.462 -59.457 1.00 57.96  ? 275  TYR   A CB    1 
ATOM   29   C  CG    . TYR   A 1 126  ? -20.242 -21.096 -58.003 1.00 55.23  ? 275  TYR   A CG    1 
ATOM   30   C  CD1   . TYR   A 1 126  ? -19.782 -22.033 -57.096 1.00 50.82  ? 275  TYR   A CD1   1 
ATOM   31   C  CD2   . TYR   A 1 126  ? -20.600 -19.840 -57.523 1.00 53.75  ? 275  TYR   A CD2   1 
ATOM   32   C  CE1   . TYR   A 1 126  ? -19.653 -21.729 -55.754 1.00 50.75  ? 275  TYR   A CE1   1 
ATOM   33   C  CE2   . TYR   A 1 126  ? -20.492 -19.526 -56.175 1.00 53.31  ? 275  TYR   A CE2   1 
ATOM   34   C  CZ    . TYR   A 1 126  ? -20.008 -20.476 -55.291 1.00 52.98  ? 275  TYR   A CZ    1 
ATOM   35   O  OH    . TYR   A 1 126  ? -19.876 -20.231 -53.958 1.00 58.71  ? 275  TYR   A OH    1 
ATOM   36   N  N     . LYS   A 1 127  ? -23.588 -21.550 -58.401 1.00 60.57  ? 276  LYS   A N     1 
ATOM   37   C  CA    . LYS   A 1 127  ? -24.816 -20.805 -58.033 1.00 65.11  ? 276  LYS   A CA    1 
ATOM   38   C  C     . LYS   A 1 127  ? -24.414 -19.579 -57.220 1.00 63.59  ? 276  LYS   A C     1 
ATOM   39   O  O     . LYS   A 1 127  ? -23.869 -19.751 -56.121 1.00 68.01  ? 276  LYS   A O     1 
ATOM   40   C  CB    . LYS   A 1 127  ? -25.793 -21.674 -57.235 1.00 73.41  ? 276  LYS   A CB    1 
ATOM   41   C  CG    . LYS   A 1 127  ? -26.991 -20.916 -56.677 1.00 82.06  ? 276  LYS   A CG    1 
ATOM   42   C  CD    . LYS   A 1 127  ? -28.232 -21.767 -56.493 1.00 97.60  ? 276  LYS   A CD    1 
ATOM   43   C  CE    . LYS   A 1 127  ? -29.413 -20.981 -55.959 1.00 104.62 ? 276  LYS   A CE    1 
ATOM   44   N  NZ    . LYS   A 1 127  ? -30.445 -21.874 -55.380 1.00 103.83 ? 276  LYS   A NZ    1 
ATOM   45   N  N     . VAL   A 1 128  ? -24.683 -18.393 -57.756 1.00 64.05  ? 277  VAL   A N     1 
ATOM   46   C  CA    . VAL   A 1 128  ? -24.451 -17.096 -57.065 1.00 65.52  ? 277  VAL   A CA    1 
ATOM   47   C  C     . VAL   A 1 128  ? -25.675 -16.808 -56.193 1.00 68.72  ? 277  VAL   A C     1 
ATOM   48   O  O     . VAL   A 1 128  ? -26.789 -16.831 -56.741 1.00 61.80  ? 277  VAL   A O     1 
ATOM   49   C  CB    . VAL   A 1 128  ? -24.217 -15.963 -58.077 1.00 58.24  ? 277  VAL   A CB    1 
ATOM   50   C  CG1   . VAL   A 1 128  ? -23.785 -14.684 -57.377 1.00 59.89  ? 277  VAL   A CG1   1 
ATOM   51   C  CG2   . VAL   A 1 128  ? -23.227 -16.372 -59.149 1.00 53.37  ? 277  VAL   A CG2   1 
ATOM   52   N  N     . ASN   A 1 129  ? -25.475 -16.538 -54.901 1.00 78.68  ? 278  ASN   A N     1 
ATOM   53   C  CA    . ASN   A 1 129  ? -26.583 -16.242 -53.951 1.00 89.30  ? 278  ASN   A CA    1 
ATOM   54   C  C     . ASN   A 1 129  ? -26.711 -14.721 -53.835 1.00 85.87  ? 278  ASN   A C     1 
ATOM   55   O  O     . ASN   A 1 129  ? -26.109 -14.135 -52.922 1.00 92.56  ? 278  ASN   A O     1 
ATOM   56   C  CB    . ASN   A 1 129  ? -26.400 -16.965 -52.612 1.00 96.29  ? 278  ASN   A CB    1 
ATOM   57   C  CG    . ASN   A 1 129  ? -26.535 -18.472 -52.743 1.00 101.44 ? 278  ASN   A CG    1 
ATOM   58   O  OD1   . ASN   A 1 129  ? -27.541 -18.979 -53.246 1.00 97.40  ? 278  ASN   A OD1   1 
ATOM   59   N  ND2   . ASN   A 1 129  ? -25.520 -19.201 -52.303 1.00 97.95  ? 278  ASN   A ND2   1 
ATOM   60   N  N     . LEU   A 1 130  ? -27.479 -14.129 -54.753 1.00 81.84  ? 279  LEU   A N     1 
ATOM   61   C  CA    . LEU   A 1 130  ? -27.741 -12.673 -54.860 1.00 78.59  ? 279  LEU   A CA    1 
ATOM   62   C  C     . LEU   A 1 130  ? -29.143 -12.378 -54.322 1.00 74.43  ? 279  LEU   A C     1 
ATOM   63   O  O     . LEU   A 1 130  ? -30.089 -13.004 -54.836 1.00 73.51  ? 279  LEU   A O     1 
ATOM   64   C  CB    . LEU   A 1 130  ? -27.634 -12.296 -56.339 1.00 83.11  ? 279  LEU   A CB    1 
ATOM   65   C  CG    . LEU   A 1 130  ? -27.175 -10.871 -56.610 1.00 88.72  ? 279  LEU   A CG    1 
ATOM   66   C  CD1   . LEU   A 1 130  ? -25.737 -10.696 -56.167 1.00 90.93  ? 279  LEU   A CD1   1 
ATOM   67   C  CD2   . LEU   A 1 130  ? -27.325 -10.523 -58.081 1.00 94.60  ? 279  LEU   A CD2   1 
ATOM   68   N  N     . SER   A 1 131  ? -29.278 -11.469 -53.345 1.00 67.13  ? 280  SER   A N     1 
ATOM   69   C  CA    . SER   A 1 131  ? -30.573 -11.130 -52.686 1.00 65.75  ? 280  SER   A CA    1 
ATOM   70   C  C     . SER   A 1 131  ? -31.473 -10.358 -53.666 1.00 75.87  ? 280  SER   A C     1 
ATOM   71   O  O     . SER   A 1 131  ? -30.956 -9.863  -54.691 1.00 72.93  ? 280  SER   A O     1 
ATOM   72   C  CB    . SER   A 1 131  ? -30.375 -10.365 -51.391 1.00 60.07  ? 280  SER   A CB    1 
ATOM   73   O  OG    . SER   A 1 131  ? -30.304 -8.966  -51.626 1.00 57.55  ? 280  SER   A OG    1 
ATOM   74   N  N     . GLN   A 1 132  ? -32.778 -10.266 -53.374 1.00 83.67  ? 281  GLN   A N     1 
ATOM   75   C  CA    . GLN   A 1 132  ? -33.758 -9.530  -54.224 1.00 83.17  ? 281  GLN   A CA    1 
ATOM   76   C  C     . GLN   A 1 132  ? -33.474 -8.025  -54.109 1.00 72.47  ? 281  GLN   A C     1 
ATOM   77   O  O     . GLN   A 1 132  ? -33.491 -7.352  -55.164 1.00 69.07  ? 281  GLN   A O     1 
ATOM   78   C  CB    . GLN   A 1 132  ? -35.209 -9.868  -53.850 1.00 93.03  ? 281  GLN   A CB    1 
ATOM   79   C  CG    . GLN   A 1 132  ? -35.705 -11.199 -54.411 1.00 98.80  ? 281  GLN   A CG    1 
ATOM   80   C  CD    . GLN   A 1 132  ? -36.261 -11.105 -55.816 1.00 106.56 ? 281  GLN   A CD    1 
ATOM   81   O  OE1   . GLN   A 1 132  ? -37.312 -10.510 -56.055 1.00 108.46 ? 281  GLN   A OE1   1 
ATOM   82   N  NE2   . GLN   A 1 132  ? -35.572 -11.721 -56.764 1.00 103.14 ? 281  GLN   A NE2   1 
ATOM   83   N  N     . ASP   A 1 133  ? -33.217 -7.533  -52.887 1.00 63.70  ? 282  ASP   A N     1 
ATOM   84   C  CA    . ASP   A 1 133  ? -32.911 -6.108  -52.578 1.00 68.83  ? 282  ASP   A CA    1 
ATOM   85   C  C     . ASP   A 1 133  ? -31.819 -5.598  -53.520 1.00 68.67  ? 282  ASP   A C     1 
ATOM   86   O  O     . ASP   A 1 133  ? -31.979 -4.502  -54.077 1.00 74.71  ? 282  ASP   A O     1 
ATOM   87   C  CB    . ASP   A 1 133  ? -32.419 -5.925  -51.140 1.00 76.58  ? 282  ASP   A CB    1 
ATOM   88   C  CG    . ASP   A 1 133  ? -33.519 -5.817  -50.099 1.00 88.05  ? 282  ASP   A CG    1 
ATOM   89   O  OD1   . ASP   A 1 133  ? -34.671 -6.200  -50.423 1.00 91.16  ? 282  ASP   A OD1   1 
ATOM   90   O  OD2   . ASP   A 1 133  ? -33.214 -5.341  -48.968 1.00 89.42  ? 282  ASP   A OD2   1 
ATOM   91   N  N     . LEU   A 1 134  ? -30.761 -6.391  -53.687 1.00 66.67  ? 283  LEU   A N     1 
ATOM   92   C  CA    . LEU   A 1 134  ? -29.522 -6.006  -54.408 1.00 65.62  ? 283  LEU   A CA    1 
ATOM   93   C  C     . LEU   A 1 134  ? -29.798 -6.031  -55.904 1.00 59.35  ? 283  LEU   A C     1 
ATOM   94   O  O     . LEU   A 1 134  ? -29.369 -5.103  -56.612 1.00 57.97  ? 283  LEU   A O     1 
ATOM   95   C  CB    . LEU   A 1 134  ? -28.400 -6.984  -54.056 1.00 64.76  ? 283  LEU   A CB    1 
ATOM   96   C  CG    . LEU   A 1 134  ? -27.076 -6.731  -54.771 1.00 66.07  ? 283  LEU   A CG    1 
ATOM   97   C  CD1   . LEU   A 1 134  ? -26.468 -5.412  -54.326 1.00 62.67  ? 283  LEU   A CD1   1 
ATOM   98   C  CD2   . LEU   A 1 134  ? -26.115 -7.883  -54.536 1.00 67.06  ? 283  LEU   A CD2   1 
ATOM   99   N  N     . GLU   A 1 135  ? -30.448 -7.094  -56.365 1.00 61.54  ? 284  GLU   A N     1 
ATOM   100  C  CA    . GLU   A 1 135  ? -30.838 -7.236  -57.785 1.00 58.17  ? 284  GLU   A CA    1 
ATOM   101  C  C     . GLU   A 1 135  ? -31.611 -5.979  -58.218 1.00 55.40  ? 284  GLU   A C     1 
ATOM   102  O  O     . GLU   A 1 135  ? -31.308 -5.439  -59.285 1.00 48.65  ? 284  GLU   A O     1 
ATOM   103  C  CB    . GLU   A 1 135  ? -31.637 -8.516  -57.971 1.00 66.12  ? 284  GLU   A CB    1 
ATOM   104  C  CG    . GLU   A 1 135  ? -31.622 -8.985  -59.409 1.00 77.66  ? 284  GLU   A CG    1 
ATOM   105  C  CD    . GLU   A 1 135  ? -31.890 -10.464 -59.568 1.00 82.91  ? 284  GLU   A CD    1 
ATOM   106  O  OE1   . GLU   A 1 135  ? -32.519 -10.824 -60.581 1.00 86.23  ? 284  GLU   A OE1   1 
ATOM   107  O  OE2   . GLU   A 1 135  ? -31.466 -11.241 -58.677 1.00 86.43  ? 284  GLU   A OE2   1 
ATOM   108  N  N     . HIS   A 1 136  ? -32.523 -5.482  -57.385 1.00 53.57  ? 285  HIS   A N     1 
ATOM   109  C  CA    . HIS   A 1 136  ? -33.386 -4.321  -57.725 1.00 60.20  ? 285  HIS   A CA    1 
ATOM   110  C  C     . HIS   A 1 136  ? -32.560 -3.038  -57.629 1.00 54.89  ? 285  HIS   A C     1 
ATOM   111  O  O     . HIS   A 1 136  ? -32.744 -2.161  -58.498 1.00 54.84  ? 285  HIS   A O     1 
ATOM   112  C  CB    . HIS   A 1 136  ? -34.673 -4.310  -56.871 1.00 62.94  ? 285  HIS   A CB    1 
ATOM   113  C  CG    . HIS   A 1 136  ? -35.616 -5.418  -57.227 1.00 67.78  ? 285  HIS   A CG    1 
ATOM   114  N  ND1   . HIS   A 1 136  ? -36.532 -5.939  -56.327 1.00 66.60  ? 285  HIS   A ND1   1 
ATOM   115  C  CD2   . HIS   A 1 136  ? -35.766 -6.124  -58.374 1.00 65.64  ? 285  HIS   A CD2   1 
ATOM   116  C  CE1   . HIS   A 1 136  ? -37.208 -6.910  -56.907 1.00 68.46  ? 285  HIS   A CE1   1 
ATOM   117  N  NE2   . HIS   A 1 136  ? -36.757 -7.043  -58.168 1.00 66.92  ? 285  HIS   A NE2   1 
ATOM   118  N  N     . GLN   A 1 137  ? -31.704 -2.923  -56.610 1.00 53.54  ? 286  GLN   A N     1 
ATOM   119  C  CA    . GLN   A 1 137  ? -30.732 -1.804  -56.491 1.00 58.11  ? 286  GLN   A CA    1 
ATOM   120  C  C     . GLN   A 1 137  ? -29.884 -1.706  -57.770 1.00 54.53  ? 286  GLN   A C     1 
ATOM   121  O  O     . GLN   A 1 137  ? -29.725 -0.585  -58.286 1.00 51.19  ? 286  GLN   A O     1 
ATOM   122  C  CB    . GLN   A 1 137  ? -29.811 -2.008  -55.298 1.00 61.68  ? 286  GLN   A CB    1 
ATOM   123  C  CG    . GLN   A 1 137  ? -30.421 -1.613  -53.965 1.00 68.22  ? 286  GLN   A CG    1 
ATOM   124  C  CD    . GLN   A 1 137  ? -29.425 -1.957  -52.885 1.00 75.43  ? 286  GLN   A CD    1 
ATOM   125  O  OE1   . GLN   A 1 137  ? -28.349 -1.357  -52.797 1.00 85.75  ? 286  GLN   A OE1   1 
ATOM   126  N  NE2   . GLN   A 1 137  ? -29.739 -2.983  -52.110 1.00 73.14  ? 286  GLN   A NE2   1 
ATOM   127  N  N     . LEU   A 1 138  ? -29.346 -2.831  -58.249 1.00 49.23  ? 287  LEU   A N     1 
ATOM   128  C  CA    . LEU   A 1 138  ? -28.547 -2.872  -59.500 1.00 55.03  ? 287  LEU   A CA    1 
ATOM   129  C  C     . LEU   A 1 138  ? -29.381 -2.304  -60.649 1.00 51.85  ? 287  LEU   A C     1 
ATOM   130  O  O     . LEU   A 1 138  ? -28.914 -1.371  -61.321 1.00 51.12  ? 287  LEU   A O     1 
ATOM   131  C  CB    . LEU   A 1 138  ? -28.118 -4.308  -59.796 1.00 54.04  ? 287  LEU   A CB    1 
ATOM   132  C  CG    . LEU   A 1 138  ? -26.790 -4.729  -59.177 1.00 57.37  ? 287  LEU   A CG    1 
ATOM   133  C  CD1   . LEU   A 1 138  ? -26.518 -6.200  -59.464 1.00 57.25  ? 287  LEU   A CD1   1 
ATOM   134  C  CD2   . LEU   A 1 138  ? -25.655 -3.860  -59.707 1.00 59.90  ? 287  LEU   A CD2   1 
ATOM   135  N  N     . GLN   A 1 139  ? -30.588 -2.835  -60.832 1.00 51.20  ? 288  GLN   A N     1 
ATOM   136  C  CA    . GLN   A 1 139  ? -31.486 -2.460  -61.950 1.00 51.51  ? 288  GLN   A CA    1 
ATOM   137  C  C     . GLN   A 1 139  ? -31.799 -0.965  -61.858 1.00 46.94  ? 288  GLN   A C     1 
ATOM   138  O  O     . GLN   A 1 139  ? -31.768 -0.298  -62.897 1.00 49.42  ? 288  GLN   A O     1 
ATOM   139  C  CB    . GLN   A 1 139  ? -32.713 -3.363  -61.935 1.00 55.20  ? 288  GLN   A CB    1 
ATOM   140  C  CG    . GLN   A 1 139  ? -32.370 -4.766  -62.395 1.00 61.31  ? 288  GLN   A CG    1 
ATOM   141  C  CD    . GLN   A 1 139  ? -33.587 -5.649  -62.483 1.00 63.87  ? 288  GLN   A CD    1 
ATOM   142  O  OE1   . GLN   A 1 139  ? -34.234 -5.943  -61.489 1.00 67.87  ? 288  GLN   A OE1   1 
ATOM   143  N  NE2   . GLN   A 1 139  ? -33.887 -6.097  -63.688 1.00 67.45  ? 288  GLN   A NE2   1 
ATOM   144  N  N     . ASN   A 1 140  ? -32.030 -0.464  -60.650 1.00 44.59  ? 289  ASN   A N     1 
ATOM   145  C  CA    . ASN   A 1 140  ? -32.401 0.950   -60.392 1.00 48.96  ? 289  ASN   A CA    1 
ATOM   146  C  C     . ASN   A 1 140  ? -31.238 1.855   -60.788 1.00 51.30  ? 289  ASN   A C     1 
ATOM   147  O  O     . ASN   A 1 140  ? -31.482 2.830   -61.521 1.00 50.73  ? 289  ASN   A O     1 
ATOM   148  C  CB    . ASN   A 1 140  ? -32.913 1.155   -58.959 1.00 50.05  ? 289  ASN   A CB    1 
ATOM   149  C  CG    . ASN   A 1 140  ? -34.399 0.844   -58.872 1.00 53.61  ? 289  ASN   A CG    1 
ATOM   150  O  OD1   . ASN   A 1 140  ? -34.841 0.047   -58.044 1.00 51.34  ? 289  ASN   A OD1   1 
ATOM   151  N  ND2   . ASN   A 1 140  ? -35.176 1.420   -59.784 1.00 51.83  ? 289  ASN   A ND2   1 
ATOM   152  N  N     . VAL   A 1 141  ? -30.011 1.532   -60.377 1.00 56.73  ? 290  VAL   A N     1 
ATOM   153  C  CA    . VAL   A 1 141  ? -28.824 2.359   -60.749 1.00 52.88  ? 290  VAL   A CA    1 
ATOM   154  C  C     . VAL   A 1 141  ? -28.625 2.337   -62.269 1.00 49.99  ? 290  VAL   A C     1 
ATOM   155  O  O     . VAL   A 1 141  ? -28.383 3.400   -62.818 1.00 51.69  ? 290  VAL   A O     1 
ATOM   156  C  CB    . VAL   A 1 141  ? -27.558 1.922   -60.003 1.00 53.01  ? 290  VAL   A CB    1 
ATOM   157  C  CG1   . VAL   A 1 141  ? -26.306 2.505   -60.649 1.00 49.53  ? 290  VAL   A CG1   1 
ATOM   158  C  CG2   . VAL   A 1 141  ? -27.672 2.306   -58.535 1.00 50.15  ? 290  VAL   A CG2   1 
ATOM   159  N  N     . ILE   A 1 142  ? -28.717 1.183   -62.929 1.00 50.71  ? 291  ILE   A N     1 
ATOM   160  C  CA    . ILE   A 1 142  ? -28.623 1.105   -64.421 1.00 51.89  ? 291  ILE   A CA    1 
ATOM   161  C  C     . ILE   A 1 142  ? -29.725 1.985   -65.042 1.00 53.92  ? 291  ILE   A C     1 
ATOM   162  O  O     . ILE   A 1 142  ? -29.423 2.697   -66.024 1.00 53.04  ? 291  ILE   A O     1 
ATOM   163  C  CB    . ILE   A 1 142  ? -28.668 -0.361  -64.894 1.00 56.50  ? 291  ILE   A CB    1 
ATOM   164  C  CG1   . ILE   A 1 142  ? -27.265 -0.972  -64.979 1.00 57.52  ? 291  ILE   A CG1   1 
ATOM   165  C  CG2   . ILE   A 1 142  ? -29.399 -0.500  -66.219 1.00 54.58  ? 291  ILE   A CG2   1 
ATOM   166  C  CD1   . ILE   A 1 142  ? -26.442 -0.830  -63.731 1.00 54.95  ? 291  ILE   A CD1   1 
ATOM   167  N  N     . GLN   A 1 143  ? -30.933 2.011   -64.462 1.00 55.80  ? 292  GLN   A N     1 
ATOM   168  C  CA    . GLN   A 1 143  ? -32.070 2.816   -64.989 1.00 60.99  ? 292  GLN   A CA    1 
ATOM   169  C  C     . GLN   A 1 143  ? -31.859 4.312   -64.692 1.00 63.08  ? 292  GLN   A C     1 
ATOM   170  O  O     . GLN   A 1 143  ? -32.027 5.107   -65.634 1.00 58.41  ? 292  GLN   A O     1 
ATOM   171  C  CB    . GLN   A 1 143  ? -33.405 2.301   -64.448 1.00 64.38  ? 292  GLN   A CB    1 
ATOM   172  C  CG    . GLN   A 1 143  ? -34.598 2.671   -65.329 1.00 63.89  ? 292  GLN   A CG    1 
ATOM   173  C  CD    . GLN   A 1 143  ? -35.053 4.091   -65.081 1.00 63.16  ? 292  GLN   A CD    1 
ATOM   174  O  OE1   . GLN   A 1 143  ? -35.055 4.571   -63.946 1.00 60.54  ? 292  GLN   A OE1   1 
ATOM   175  N  NE2   . GLN   A 1 143  ? -35.434 4.779   -66.148 1.00 61.98  ? 292  GLN   A NE2   1 
ATOM   176  N  N     . GLU   A 1 144  ? -31.517 4.689   -63.450 1.00 72.44  ? 293  GLU   A N     1 
ATOM   177  C  CA    . GLU   A 1 144  ? -31.268 6.105   -63.029 1.00 74.58  ? 293  GLU   A CA    1 
ATOM   178  C  C     . GLU   A 1 144  ? -30.227 6.751   -63.955 1.00 70.88  ? 293  GLU   A C     1 
ATOM   179  O  O     . GLU   A 1 144  ? -30.419 7.917   -64.321 1.00 73.67  ? 293  GLU   A O     1 
ATOM   180  C  CB    . GLU   A 1 144  ? -30.794 6.204   -61.572 1.00 77.82  ? 293  GLU   A CB    1 
ATOM   181  C  CG    . GLU   A 1 144  ? -31.903 6.470   -60.558 1.00 86.51  ? 293  GLU   A CG    1 
ATOM   182  C  CD    . GLU   A 1 144  ? -32.004 5.467   -59.410 1.00 96.08  ? 293  GLU   A CD    1 
ATOM   183  O  OE1   . GLU   A 1 144  ? -30.941 5.028   -58.897 1.00 106.30 ? 293  GLU   A OE1   1 
ATOM   184  O  OE2   . GLU   A 1 144  ? -33.149 5.102   -59.035 1.00 82.36  ? 293  GLU   A OE2   1 
ATOM   185  N  N     . LEU   A 1 145  ? -29.179 6.014   -64.324 1.00 65.42  ? 294  LEU   A N     1 
ATOM   186  C  CA    . LEU   A 1 145  ? -28.026 6.522   -65.113 1.00 67.20  ? 294  LEU   A CA    1 
ATOM   187  C  C     . LEU   A 1 145  ? -28.246 6.311   -66.612 1.00 68.76  ? 294  LEU   A C     1 
ATOM   188  O  O     . LEU   A 1 145  ? -27.390 6.778   -67.388 1.00 75.17  ? 294  LEU   A O     1 
ATOM   189  C  CB    . LEU   A 1 145  ? -26.760 5.792   -64.656 1.00 67.24  ? 294  LEU   A CB    1 
ATOM   190  C  CG    . LEU   A 1 145  ? -26.406 5.961   -63.179 1.00 69.74  ? 294  LEU   A CG    1 
ATOM   191  C  CD1   . LEU   A 1 145  ? -25.085 5.260   -62.862 1.00 71.59  ? 294  LEU   A CD1   1 
ATOM   192  C  CD2   . LEU   A 1 145  ? -26.358 7.433   -62.789 1.00 63.74  ? 294  LEU   A CD2   1 
ATOM   193  N  N     . ASN   A 1 146  ? -29.309 5.600   -67.001 1.00 69.79  ? 295  ASN   A N     1 
ATOM   194  C  CA    . ASN   A 1 146  ? -29.729 5.433   -68.417 1.00 66.36  ? 295  ASN   A CA    1 
ATOM   195  C  C     . ASN   A 1 146  ? -28.631 4.668   -69.167 1.00 64.05  ? 295  ASN   A C     1 
ATOM   196  O  O     . ASN   A 1 146  ? -28.348 5.010   -70.324 1.00 66.35  ? 295  ASN   A O     1 
ATOM   197  C  CB    . ASN   A 1 146  ? -30.080 6.796   -69.025 1.00 74.40  ? 295  ASN   A CB    1 
ATOM   198  C  CG    . ASN   A 1 146  ? -30.544 6.749   -70.468 1.00 79.09  ? 295  ASN   A CG    1 
ATOM   199  O  OD1   . ASN   A 1 146  ? -31.021 5.726   -70.959 1.00 83.44  ? 295  ASN   A OD1   1 
ATOM   200  N  ND2   . ASN   A 1 146  ? -30.405 7.867   -71.160 1.00 83.97  ? 295  ASN   A ND2   1 
ATOM   201  N  N     . LEU   A 1 147  ? -28.047 3.654   -68.527 1.00 67.89  ? 296  LEU   A N     1 
ATOM   202  C  CA    . LEU   A 1 147  ? -26.940 2.843   -69.104 1.00 70.25  ? 296  LEU   A CA    1 
ATOM   203  C  C     . LEU   A 1 147  ? -27.556 1.790   -70.026 1.00 71.02  ? 296  LEU   A C     1 
ATOM   204  O  O     . LEU   A 1 147  ? -28.644 1.285   -69.708 1.00 62.19  ? 296  LEU   A O     1 
ATOM   205  C  CB    . LEU   A 1 147  ? -26.095 2.216   -67.984 1.00 72.80  ? 296  LEU   A CB    1 
ATOM   206  C  CG    . LEU   A 1 147  ? -25.548 3.198   -66.939 1.00 74.23  ? 296  LEU   A CG    1 
ATOM   207  C  CD1   . LEU   A 1 147  ? -24.818 2.469   -65.821 1.00 73.34  ? 296  LEU   A CD1   1 
ATOM   208  C  CD2   . LEU   A 1 147  ? -24.627 4.238   -67.571 1.00 73.09  ? 296  LEU   A CD2   1 
ATOM   209  N  N     . GLU   A 1 148  ? -26.895 1.517   -71.150 1.00 80.63  ? 297  GLU   A N     1 
ATOM   210  C  CA    . GLU   A 1 148  ? -27.347 0.522   -72.155 1.00 85.72  ? 297  GLU   A CA    1 
ATOM   211  C  C     . GLU   A 1 148  ? -27.173 -0.878  -71.547 1.00 88.55  ? 297  GLU   A C     1 
ATOM   212  O  O     . GLU   A 1 148  ? -26.063 -1.172  -71.038 1.00 81.49  ? 297  GLU   A O     1 
ATOM   213  C  CB    . GLU   A 1 148  ? -26.552 0.707   -73.450 1.00 89.30  ? 297  GLU   A CB    1 
ATOM   214  C  CG    . GLU   A 1 148  ? -27.298 0.276   -74.703 1.00 106.40 ? 297  GLU   A CG    1 
ATOM   215  C  CD    . GLU   A 1 148  ? -26.735 0.810   -76.016 1.00 115.16 ? 297  GLU   A CD    1 
ATOM   216  O  OE1   . GLU   A 1 148  ? -25.682 1.497   -75.989 1.00 118.33 ? 297  GLU   A OE1   1 
ATOM   217  O  OE2   . GLU   A 1 148  ? -27.353 0.543   -77.070 1.00 112.60 ? 297  GLU   A OE2   1 
ATOM   218  N  N     . ILE   A 1 149  ? -28.234 -1.692  -71.552 1.00 84.86  ? 298  ILE   A N     1 
ATOM   219  C  CA    . ILE   A 1 149  ? -28.172 -3.140  -71.180 1.00 84.22  ? 298  ILE   A CA    1 
ATOM   220  C  C     . ILE   A 1 149  ? -28.572 -3.966  -72.401 1.00 80.62  ? 298  ILE   A C     1 
ATOM   221  O  O     . ILE   A 1 149  ? -29.361 -3.463  -73.221 1.00 94.20  ? 298  ILE   A O     1 
ATOM   222  C  CB    . ILE   A 1 149  ? -29.039 -3.497  -69.949 1.00 79.82  ? 298  ILE   A CB    1 
ATOM   223  C  CG1   . ILE   A 1 149  ? -30.324 -2.667  -69.866 1.00 77.36  ? 298  ILE   A CG1   1 
ATOM   224  C  CG2   . ILE   A 1 149  ? -28.218 -3.404  -68.668 1.00 75.09  ? 298  ILE   A CG2   1 
ATOM   225  C  CD1   . ILE   A 1 149  ? -31.290 -3.151  -68.813 1.00 77.98  ? 298  ILE   A CD1   1 
ATOM   226  N  N     . VAL   A 1 150  ? -28.025 -5.177  -72.510 1.00 78.52  ? 299  VAL   A N     1 
ATOM   227  C  CA    . VAL   A 1 150  ? -28.477 -6.219  -73.475 1.00 80.59  ? 299  VAL   A CA    1 
ATOM   228  C  C     . VAL   A 1 150  ? -29.641 -6.972  -72.843 1.00 76.14  ? 299  VAL   A C     1 
ATOM   229  O  O     . VAL   A 1 150  ? -29.498 -7.524  -71.755 1.00 69.15  ? 299  VAL   A O     1 
ATOM   230  C  CB    . VAL   A 1 150  ? -27.332 -7.169  -73.863 1.00 81.01  ? 299  VAL   A CB    1 
ATOM   231  C  CG1   . VAL   A 1 150  ? -27.848 -8.414  -74.568 1.00 84.35  ? 299  VAL   A CG1   1 
ATOM   232  C  CG2   . VAL   A 1 150  ? -26.289 -6.456  -74.710 1.00 79.34  ? 299  VAL   A CG2   1 
ATOM   233  N  N     . PRO   A 1 151  ? -30.822 -7.011  -73.504 1.00 82.59  ? 300  PRO   A N     1 
ATOM   234  C  CA    . PRO   A 1 151  ? -31.984 -7.708  -72.957 1.00 83.79  ? 300  PRO   A CA    1 
ATOM   235  C  C     . PRO   A 1 151  ? -31.812 -9.223  -73.017 1.00 75.97  ? 300  PRO   A C     1 
ATOM   236  O  O     . PRO   A 1 151  ? -30.997 -9.727  -73.786 1.00 76.09  ? 300  PRO   A O     1 
ATOM   237  C  CB    . PRO   A 1 151  ? -33.145 -7.241  -73.851 1.00 84.06  ? 300  PRO   A CB    1 
ATOM   238  C  CG    . PRO   A 1 151  ? -32.487 -6.905  -75.170 1.00 84.65  ? 300  PRO   A CG    1 
ATOM   239  C  CD    . PRO   A 1 151  ? -31.107 -6.389  -74.808 1.00 85.40  ? 300  PRO   A CD    1 
ATOM   240  N  N     . PRO   A 1 152  ? -32.578 -9.990  -72.207 1.00 78.49  ? 301  PRO   A N     1 
ATOM   241  C  CA    . PRO   A 1 152  ? -32.485 -11.451 -72.205 1.00 77.74  ? 301  PRO   A CA    1 
ATOM   242  C  C     . PRO   A 1 152  ? -32.736 -12.048 -73.584 1.00 80.18  ? 301  PRO   A C     1 
ATOM   243  O  O     . PRO   A 1 152  ? -33.395 -11.427 -74.414 1.00 77.05  ? 301  PRO   A O     1 
ATOM   244  C  CB    . PRO   A 1 152  ? -33.586 -11.917 -71.240 1.00 78.68  ? 301  PRO   A CB    1 
ATOM   245  C  CG    . PRO   A 1 152  ? -33.913 -10.691 -70.389 1.00 80.71  ? 301  PRO   A CG    1 
ATOM   246  C  CD    . PRO   A 1 152  ? -33.566 -9.484  -71.238 1.00 81.35  ? 301  PRO   A CD    1 
ATOM   247  N  N     . PRO   A 1 153  ? -32.237 -13.274 -73.860 1.00 89.82  ? 302  PRO   A N     1 
ATOM   248  C  CA    . PRO   A 1 153  ? -32.369 -13.874 -75.185 1.00 95.94  ? 302  PRO   A CA    1 
ATOM   249  C  C     . PRO   A 1 153  ? -33.767 -14.481 -75.392 1.00 106.47 ? 302  PRO   A C     1 
ATOM   250  O  O     . PRO   A 1 153  ? -34.466 -14.710 -74.415 1.00 90.91  ? 302  PRO   A O     1 
ATOM   251  C  CB    . PRO   A 1 153  ? -31.245 -14.921 -75.195 1.00 92.12  ? 302  PRO   A CB    1 
ATOM   252  C  CG    . PRO   A 1 153  ? -31.118 -15.353 -73.748 1.00 90.56  ? 302  PRO   A CG    1 
ATOM   253  C  CD    . PRO   A 1 153  ? -31.534 -14.156 -72.915 1.00 92.25  ? 302  PRO   A CD    1 
ATOM   254  N  N     . GLU   A 1 154  ? -34.142 -14.688 -76.661 1.00 120.29 ? 303  GLU   A N     1 
ATOM   255  C  CA    . GLU   A 1 154  ? -35.463 -15.218 -77.096 1.00 118.31 ? 303  GLU   A CA    1 
ATOM   256  C  C     . GLU   A 1 154  ? -35.542 -16.708 -76.751 1.00 113.98 ? 303  GLU   A C     1 
ATOM   257  O  O     . GLU   A 1 154  ? -36.528 -17.105 -76.104 1.00 114.18 ? 303  GLU   A O     1 
ATOM   258  C  CB    . GLU   A 1 154  ? -35.672 -14.991 -78.598 1.00 124.79 ? 303  GLU   A CB    1 
ATOM   259  C  CG    . GLU   A 1 154  ? -35.959 -13.544 -78.973 1.00 124.76 ? 303  GLU   A CG    1 
ATOM   260  C  CD    . GLU   A 1 154  ? -37.292 -12.990 -78.490 1.00 127.39 ? 303  GLU   A CD    1 
ATOM   261  O  OE1   . GLU   A 1 154  ? -38.113 -13.776 -77.966 1.00 122.74 ? 303  GLU   A OE1   1 
ATOM   262  O  OE2   . GLU   A 1 154  ? -37.510 -11.769 -78.637 1.00 124.74 ? 303  GLU   A OE2   1 
ATOM   263  N  N     . ASP   A 1 155  ? -34.543 -17.491 -77.178 1.00 109.86 ? 304  ASP   A N     1 
ATOM   264  C  CA    . ASP   A 1 155  ? -34.429 -18.947 -76.887 1.00 110.28 ? 304  ASP   A CA    1 
ATOM   265  C  C     . ASP   A 1 155  ? -33.034 -19.243 -76.338 1.00 111.33 ? 304  ASP   A C     1 
ATOM   266  O  O     . ASP   A 1 155  ? -32.073 -18.542 -76.659 1.00 108.36 ? 304  ASP   A O     1 
ATOM   267  C  CB    . ASP   A 1 155  ? -34.754 -19.799 -78.119 1.00 108.89 ? 304  ASP   A CB    1 
ATOM   268  C  CG    . ASP   A 1 155  ? -33.939 -19.455 -79.354 1.00 110.11 ? 304  ASP   A CG    1 
ATOM   269  O  OD1   . ASP   A 1 155  ? -33.733 -18.249 -79.593 1.00 116.06 ? 304  ASP   A OD1   1 
ATOM   270  O  OD2   . ASP   A 1 155  ? -33.504 -20.396 -80.060 1.00 100.89 ? 304  ASP   A OD2   1 
ATOM   271  N  N     . PRO   A 1 156  ? -32.881 -20.292 -75.494 1.00 113.78 ? 305  PRO   A N     1 
ATOM   272  C  CA    . PRO   A 1 156  ? -31.598 -20.605 -74.856 1.00 119.08 ? 305  PRO   A CA    1 
ATOM   273  C  C     . PRO   A 1 156  ? -30.468 -21.115 -75.769 1.00 121.42 ? 305  PRO   A C     1 
ATOM   274  O  O     . PRO   A 1 156  ? -29.377 -21.310 -75.261 1.00 114.58 ? 305  PRO   A O     1 
ATOM   275  C  CB    . PRO   A 1 156  ? -31.941 -21.732 -73.862 1.00 119.27 ? 305  PRO   A CB    1 
ATOM   276  C  CG    . PRO   A 1 156  ? -33.447 -21.676 -73.711 1.00 118.00 ? 305  PRO   A CG    1 
ATOM   277  C  CD    . PRO   A 1 156  ? -33.949 -21.206 -75.059 1.00 116.75 ? 305  PRO   A CD    1 
ATOM   278  N  N     . PHE   A 1 157  ? -30.734 -21.336 -77.061 1.00 124.50 ? 306  PHE   A N     1 
ATOM   279  C  CA    . PHE   A 1 157  ? -29.770 -21.944 -78.018 1.00 124.60 ? 306  PHE   A CA    1 
ATOM   280  C  C     . PHE   A 1 157  ? -29.072 -20.853 -78.843 1.00 119.84 ? 306  PHE   A C     1 
ATOM   281  O  O     . PHE   A 1 157  ? -28.096 -21.188 -79.537 1.00 114.67 ? 306  PHE   A O     1 
ATOM   282  C  CB    . PHE   A 1 157  ? -30.472 -23.004 -78.873 1.00 132.74 ? 306  PHE   A CB    1 
ATOM   283  C  CG    . PHE   A 1 157  ? -30.746 -24.293 -78.137 1.00 137.82 ? 306  PHE   A CG    1 
ATOM   284  C  CD1   . PHE   A 1 157  ? -29.700 -25.109 -77.725 1.00 131.52 ? 306  PHE   A CD1   1 
ATOM   285  C  CD2   . PHE   A 1 157  ? -32.045 -24.688 -77.845 1.00 136.49 ? 306  PHE   A CD2   1 
ATOM   286  C  CE1   . PHE   A 1 157  ? -29.945 -26.291 -77.044 1.00 129.77 ? 306  PHE   A CE1   1 
ATOM   287  C  CE2   . PHE   A 1 157  ? -32.287 -25.872 -77.164 1.00 137.99 ? 306  PHE   A CE2   1 
ATOM   288  C  CZ    . PHE   A 1 157  ? -31.238 -26.671 -76.765 1.00 135.13 ? 306  PHE   A CZ    1 
ATOM   289  N  N     . LEU   A 1 158  ? -29.542 -19.601 -78.762 1.00 120.89 ? 307  LEU   A N     1 
ATOM   290  C  CA    . LEU   A 1 158  ? -28.822 -18.392 -79.255 1.00 114.27 ? 307  LEU   A CA    1 
ATOM   291  C  C     . LEU   A 1 158  ? -28.522 -17.485 -78.063 1.00 105.24 ? 307  LEU   A C     1 
ATOM   292  O  O     . LEU   A 1 158  ? -29.293 -16.572 -77.765 1.00 100.80 ? 307  LEU   A O     1 
ATOM   293  C  CB    . LEU   A 1 158  ? -29.667 -17.666 -80.308 1.00 117.56 ? 307  LEU   A CB    1 
ATOM   294  C  CG    . LEU   A 1 158  ? -29.749 -18.349 -81.674 1.00 120.24 ? 307  LEU   A CG    1 
ATOM   295  C  CD1   . LEU   A 1 158  ? -31.000 -19.214 -81.782 1.00 118.77 ? 307  LEU   A CD1   1 
ATOM   296  C  CD2   . LEU   A 1 158  ? -29.713 -17.322 -82.798 1.00 119.00 ? 307  LEU   A CD2   1 
ATOM   297  N  N     . PRO   A 1 159  ? -27.408 -17.725 -77.332 1.00 97.15  ? 308  PRO   A N     1 
ATOM   298  C  CA    . PRO   A 1 159  ? -27.024 -16.870 -76.208 1.00 93.19  ? 308  PRO   A CA    1 
ATOM   299  C  C     . PRO   A 1 159  ? -26.430 -15.553 -76.728 1.00 87.43  ? 308  PRO   A C     1 
ATOM   300  O  O     . PRO   A 1 159  ? -25.887 -15.577 -77.817 1.00 82.93  ? 308  PRO   A O     1 
ATOM   301  C  CB    . PRO   A 1 159  ? -25.981 -17.719 -75.468 1.00 92.28  ? 308  PRO   A CB    1 
ATOM   302  C  CG    . PRO   A 1 159  ? -25.337 -18.550 -76.562 1.00 93.13  ? 308  PRO   A CG    1 
ATOM   303  C  CD    . PRO   A 1 159  ? -26.447 -18.819 -77.558 1.00 95.75  ? 308  PRO   A CD    1 
ATOM   304  N  N     . VAL   A 1 160  ? -26.554 -14.461 -75.962 1.00 82.04  ? 309  VAL   A N     1 
ATOM   305  C  CA    . VAL   A 1 160  ? -26.087 -13.093 -76.353 1.00 81.59  ? 309  VAL   A CA    1 
ATOM   306  C  C     . VAL   A 1 160  ? -24.949 -12.629 -75.429 1.00 78.31  ? 309  VAL   A C     1 
ATOM   307  O  O     . VAL   A 1 160  ? -25.027 -12.862 -74.200 1.00 69.06  ? 309  VAL   A O     1 
ATOM   308  C  CB    . VAL   A 1 160  ? -27.244 -12.075 -76.365 1.00 84.42  ? 309  VAL   A CB    1 
ATOM   309  C  CG1   . VAL   A 1 160  ? -28.161 -12.314 -77.556 1.00 92.84  ? 309  VAL   A CG1   1 
ATOM   310  C  CG2   . VAL   A 1 160  ? -28.039 -12.060 -75.064 1.00 77.39  ? 309  VAL   A CG2   1 
ATOM   311  N  N     . VAL   A 1 161  ? -23.934 -11.983 -76.011 1.00 72.19  ? 310  VAL   A N     1 
ATOM   312  C  CA    . VAL   A 1 161  ? -22.847 -11.284 -75.264 1.00 72.21  ? 310  VAL   A CA    1 
ATOM   313  C  C     . VAL   A 1 161  ? -23.469 -10.080 -74.546 1.00 69.76  ? 310  VAL   A C     1 
ATOM   314  O  O     . VAL   A 1 161  ? -24.244 -9.351  -75.199 1.00 67.98  ? 310  VAL   A O     1 
ATOM   315  C  CB    . VAL   A 1 161  ? -21.687 -10.851 -76.186 1.00 71.11  ? 310  VAL   A CB    1 
ATOM   316  C  CG1   . VAL   A 1 161  ? -21.104 -12.022 -76.961 1.00 70.19  ? 310  VAL   A CG1   1 
ATOM   317  C  CG2   . VAL   A 1 161  ? -22.097 -9.739  -77.133 1.00 80.73  ? 310  VAL   A CG2   1 
ATOM   318  N  N     . LEU   A 1 162  ? -23.134 -9.867  -73.265 1.00 69.08  ? 311  LEU   A N     1 
ATOM   319  C  CA    . LEU   A 1 162  ? -23.641 -8.720  -72.459 1.00 65.15  ? 311  LEU   A CA    1 
ATOM   320  C  C     . LEU   A 1 162  ? -22.788 -7.464  -72.694 1.00 66.76  ? 311  LEU   A C     1 
ATOM   321  O  O     . LEU   A 1 162  ? -23.305 -6.355  -72.396 1.00 64.96  ? 311  LEU   A O     1 
ATOM   322  C  CB    . LEU   A 1 162  ? -23.657 -9.104  -70.980 1.00 60.02  ? 311  LEU   A CB    1 
ATOM   323  C  CG    . LEU   A 1 162  ? -24.378 -10.407 -70.645 1.00 58.92  ? 311  LEU   A CG    1 
ATOM   324  C  CD1   . LEU   A 1 162  ? -24.440 -10.600 -69.140 1.00 61.32  ? 311  LEU   A CD1   1 
ATOM   325  C  CD2   . LEU   A 1 162  ? -25.776 -10.439 -71.237 1.00 57.79  ? 311  LEU   A CD2   1 
ATOM   326  N  N     . ASN   A 1 163  ? -21.576 -7.621  -73.254 1.00 67.42  ? 312  ASN   A N     1 
ATOM   327  C  CA    . ASN   A 1 163  ? -20.581 -6.529  -73.469 1.00 76.53  ? 312  ASN   A CA    1 
ATOM   328  C  C     . ASN   A 1 163  ? -20.887 -5.781  -74.770 1.00 87.81  ? 312  ASN   A C     1 
ATOM   329  O  O     . ASN   A 1 163  ? -21.190 -6.470  -75.766 1.00 90.74  ? 312  ASN   A O     1 
ATOM   330  C  CB    . ASN   A 1 163  ? -19.145 -7.044  -73.616 1.00 77.48  ? 312  ASN   A CB    1 
ATOM   331  C  CG    . ASN   A 1 163  ? -18.823 -8.225  -72.729 1.00 73.92  ? 312  ASN   A CG    1 
ATOM   332  O  OD1   . ASN   A 1 163  ? -18.392 -8.049  -71.593 1.00 84.23  ? 312  ASN   A OD1   1 
ATOM   333  N  ND2   . ASN   A 1 163  ? -19.016 -9.424  -73.249 1.00 61.74  ? 312  ASN   A ND2   1 
ATOM   334  N  N     . LEU   A 1 164  ? -20.736 -4.448  -74.788 1.00 95.47  ? 313  LEU   A N     1 
ATOM   335  C  CA    . LEU   A 1 164  ? -20.914 -3.604  -76.009 1.00 100.46 ? 313  LEU   A CA    1 
ATOM   336  C  C     . LEU   A 1 164  ? -19.619 -2.827  -76.304 1.00 94.52  ? 313  LEU   A C     1 
ATOM   337  O  O     . LEU   A 1 164  ? -19.365 -1.824  -75.603 1.00 91.60  ? 313  LEU   A O     1 
ATOM   338  C  CB    . LEU   A 1 164  ? -22.116 -2.670  -75.809 1.00 101.33 ? 313  LEU   A CB    1 
ATOM   339  C  CG    . LEU   A 1 164  ? -23.474 -3.361  -75.646 1.00 101.49 ? 313  LEU   A CG    1 
ATOM   340  C  CD1   . LEU   A 1 164  ? -24.429 -2.508  -74.821 1.00 102.59 ? 313  LEU   A CD1   1 
ATOM   341  C  CD2   . LEU   A 1 164  ? -24.099 -3.703  -76.993 1.00 96.58  ? 313  LEU   A CD2   1 
ATOM   342  N  N     . PRO   A 1 172  ? -10.383 11.493  -80.514 1.00 132.08 ? 321  PRO   A N     1 
ATOM   343  C  CA    . PRO   A 1 172  ? -9.448  11.272  -81.630 1.00 132.36 ? 321  PRO   A CA    1 
ATOM   344  C  C     . PRO   A 1 172  ? -8.524  12.482  -81.852 1.00 133.82 ? 321  PRO   A C     1 
ATOM   345  O  O     . PRO   A 1 172  ? -9.006  13.514  -82.276 1.00 134.57 ? 321  PRO   A O     1 
ATOM   346  C  CB    . PRO   A 1 172  ? -10.383 11.021  -82.822 1.00 129.97 ? 321  PRO   A CB    1 
ATOM   347  C  CG    . PRO   A 1 172  ? -11.547 10.288  -82.202 1.00 130.58 ? 321  PRO   A CG    1 
ATOM   348  C  CD    . PRO   A 1 172  ? -11.695 10.907  -80.826 1.00 132.37 ? 321  PRO   A CD    1 
ATOM   349  N  N     . SER   A 1 173  ? -7.226  12.319  -81.566 1.00 135.80 ? 322  SER   A N     1 
ATOM   350  C  CA    . SER   A 1 173  ? -6.202  13.400  -81.504 1.00 136.90 ? 322  SER   A CA    1 
ATOM   351  C  C     . SER   A 1 173  ? -5.496  13.570  -82.859 1.00 142.98 ? 322  SER   A C     1 
ATOM   352  O  O     . SER   A 1 173  ? -5.724  12.735  -83.763 1.00 142.88 ? 322  SER   A O     1 
ATOM   353  C  CB    . SER   A 1 173  ? -5.213  13.124  -80.396 1.00 133.68 ? 322  SER   A CB    1 
ATOM   354  O  OG    . SER   A 1 173  ? -4.235  14.150  -80.308 1.00 126.80 ? 322  SER   A OG    1 
ATOM   355  N  N     . GLN   A 1 174  ? -4.654  14.605  -82.977 1.00 143.24 ? 323  GLN   A N     1 
ATOM   356  C  CA    . GLN   A 1 174  ? -4.014  15.052  -84.248 1.00 144.08 ? 323  GLN   A CA    1 
ATOM   357  C  C     . GLN   A 1 174  ? -2.752  14.218  -84.518 1.00 137.72 ? 323  GLN   A C     1 
ATOM   358  O  O     . GLN   A 1 174  ? -1.709  14.499  -83.894 1.00 130.02 ? 323  GLN   A O     1 
ATOM   359  C  CB    . GLN   A 1 174  ? -3.700  16.552  -84.183 1.00 146.06 ? 323  GLN   A CB    1 
ATOM   360  C  CG    . GLN   A 1 174  ? -3.733  17.242  -85.540 1.00 147.96 ? 323  GLN   A CG    1 
ATOM   361  C  CD    . GLN   A 1 174  ? -5.105  17.204  -86.168 1.00 146.49 ? 323  GLN   A CD    1 
ATOM   362  O  OE1   . GLN   A 1 174  ? -5.296  16.646  -87.246 1.00 146.02 ? 323  GLN   A OE1   1 
ATOM   363  N  NE2   . GLN   A 1 174  ? -6.079  17.787  -85.487 1.00 141.21 ? 323  GLN   A NE2   1 
ATOM   364  N  N     . ARG   A 1 175  ? -2.852  13.244  -85.432 1.00 134.16 ? 324  ARG   A N     1 
ATOM   365  C  CA    . ARG   A 1 175  ? -1.762  12.304  -85.821 1.00 131.57 ? 324  ARG   A CA    1 
ATOM   366  C  C     . ARG   A 1 175  ? -0.595  13.078  -86.451 1.00 139.71 ? 324  ARG   A C     1 
ATOM   367  O  O     . ARG   A 1 175  ? -0.804  14.238  -86.868 1.00 141.87 ? 324  ARG   A O     1 
ATOM   368  C  CB    . ARG   A 1 175  ? -2.298  11.257  -86.806 1.00 123.49 ? 324  ARG   A CB    1 
ATOM   369  C  CG    . ARG   A 1 175  ? -1.292  10.184  -87.208 1.00 119.59 ? 324  ARG   A CG    1 
ATOM   370  C  CD    . ARG   A 1 175  ? -1.744  9.393   -88.416 1.00 119.98 ? 324  ARG   A CD    1 
ATOM   371  N  NE    . ARG   A 1 175  ? -3.042  8.757   -88.214 1.00 127.02 ? 324  ARG   A NE    1 
ATOM   372  C  CZ    . ARG   A 1 175  ? -3.241  7.484   -87.860 1.00 122.21 ? 324  ARG   A CZ    1 
ATOM   373  N  NH1   . ARG   A 1 175  ? -2.221  6.664   -87.654 1.00 114.83 ? 324  ARG   A NH1   1 
ATOM   374  N  NH2   . ARG   A 1 175  ? -4.476  7.029   -87.718 1.00 120.62 ? 324  ARG   A NH2   1 
ATOM   375  N  N     . GLN   A 1 176  ? 0.591   12.455  -86.486 1.00 146.48 ? 325  GLN   A N     1 
ATOM   376  C  CA    . GLN   A 1 176  ? 1.726   12.805  -87.387 1.00 146.77 ? 325  GLN   A CA    1 
ATOM   377  C  C     . GLN   A 1 176  ? 2.497   11.527  -87.753 1.00 146.22 ? 325  GLN   A C     1 
ATOM   378  O  O     . GLN   A 1 176  ? 2.377   10.528  -87.014 1.00 133.20 ? 325  GLN   A O     1 
ATOM   379  C  CB    . GLN   A 1 176  ? 2.640   13.851  -86.741 1.00 138.52 ? 325  GLN   A CB    1 
ATOM   380  C  CG    . GLN   A 1 176  ? 2.171   15.284  -86.958 1.00 130.86 ? 325  GLN   A CG    1 
ATOM   381  C  CD    . GLN   A 1 176  ? 3.239   16.299  -86.634 1.00 130.64 ? 325  GLN   A CD    1 
ATOM   382  O  OE1   . GLN   A 1 176  ? 3.107   17.083  -85.697 1.00 121.13 ? 325  GLN   A OE1   1 
ATOM   383  N  NE2   . GLN   A 1 176  ? 4.313   16.291  -87.408 1.00 128.99 ? 325  GLN   A NE2   1 
ATOM   384  N  N     . ASN   A 1 177  ? 3.243   11.560  -88.863 1.00 154.04 ? 326  ASN   A N     1 
ATOM   385  C  CA    . ASN   A 1 177  ? 4.076   10.432  -89.368 1.00 155.46 ? 326  ASN   A CA    1 
ATOM   386  C  C     . ASN   A 1 177  ? 5.572   10.771  -89.236 1.00 156.60 ? 326  ASN   A C     1 
ATOM   387  O  O     . ASN   A 1 177  ? 6.393   9.894   -89.581 1.00 148.73 ? 326  ASN   A O     1 
ATOM   388  C  CB    . ASN   A 1 177  ? 3.707   10.065  -90.811 1.00 148.78 ? 326  ASN   A CB    1 
ATOM   389  C  CG    . ASN   A 1 177  ? 2.569   9.067   -90.898 1.00 144.80 ? 326  ASN   A CG    1 
ATOM   390  O  OD1   . ASN   A 1 177  ? 1.421   9.391   -90.602 1.00 133.88 ? 326  ASN   A OD1   1 
ATOM   391  N  ND2   . ASN   A 1 177  ? 2.878   7.848   -91.310 1.00 141.85 ? 326  ASN   A ND2   1 
ATOM   392  N  N     . GLN   A 1 178  ? 5.914   11.974  -88.746 1.00 157.27 ? 327  GLN   A N     1 
ATOM   393  C  CA    . GLN   A 1 178  ? 7.316   12.456  -88.569 1.00 145.35 ? 327  GLN   A CA    1 
ATOM   394  C  C     . GLN   A 1 178  ? 8.071   11.523  -87.612 1.00 132.82 ? 327  GLN   A C     1 
ATOM   395  O  O     . GLN   A 1 178  ? 7.451   11.005  -86.659 1.00 115.33 ? 327  GLN   A O     1 
ATOM   396  C  CB    . GLN   A 1 178  ? 7.366   13.897  -88.041 1.00 146.05 ? 327  GLN   A CB    1 
ATOM   397  C  CG    . GLN   A 1 178  ? 6.742   14.083  -86.657 1.00 149.69 ? 327  GLN   A CG    1 
ATOM   398  C  CD    . GLN   A 1 178  ? 7.550   14.940  -85.710 1.00 141.96 ? 327  GLN   A CD    1 
ATOM   399  O  OE1   . GLN   A 1 178  ? 8.773   15.030  -85.804 1.00 137.26 ? 327  GLN   A OE1   1 
ATOM   400  N  NE2   . GLN   A 1 178  ? 6.866   15.556  -84.758 1.00 133.04 ? 327  GLN   A NE2   1 
ATOM   401  N  N     . ILE   A 1 179  ? 9.363   11.315  -87.874 1.00 125.11 ? 328  ILE   A N     1 
ATOM   402  C  CA    . ILE   A 1 179  ? 10.329  10.671  -86.938 1.00 120.30 ? 328  ILE   A CA    1 
ATOM   403  C  C     . ILE   A 1 179  ? 10.973  11.797  -86.111 1.00 116.53 ? 328  ILE   A C     1 
ATOM   404  O  O     . ILE   A 1 179  ? 11.902  12.469  -86.627 1.00 120.54 ? 328  ILE   A O     1 
ATOM   405  C  CB    . ILE   A 1 179  ? 11.344  9.797   -87.717 1.00 125.03 ? 328  ILE   A CB    1 
ATOM   406  C  CG1   . ILE   A 1 179  ? 10.729  8.465   -88.166 1.00 124.55 ? 328  ILE   A CG1   1 
ATOM   407  C  CG2   . ILE   A 1 179  ? 12.635  9.579   -86.937 1.00 128.94 ? 328  ILE   A CG2   1 
ATOM   408  C  CD1   . ILE   A 1 179  ? 10.329  7.519   -87.042 1.00 117.79 ? 328  ILE   A CD1   1 
ATOM   409  N  N     . GLY   A 1 180  ? 10.455  12.029  -84.897 1.00 92.41  ? 329  GLY   A N     1 
ATOM   410  C  CA    . GLY   A 1 180  ? 10.989  13.014  -83.936 1.00 76.13  ? 329  GLY   A CA    1 
ATOM   411  C  C     . GLY   A 1 180  ? 12.360  12.596  -83.425 1.00 67.26  ? 329  GLY   A C     1 
ATOM   412  O  O     . GLY   A 1 180  ? 12.677  11.388  -83.477 1.00 63.14  ? 329  GLY   A O     1 
ATOM   413  N  N     . VAL   A 1 181  ? 13.160  13.565  -82.978 1.00 57.38  ? 330  VAL   A N     1 
ATOM   414  C  CA    . VAL   A 1 181  ? 14.520  13.343  -82.410 1.00 56.65  ? 330  VAL   A CA    1 
ATOM   415  C  C     . VAL   A 1 181  ? 14.522  13.914  -80.996 1.00 53.56  ? 330  VAL   A C     1 
ATOM   416  O  O     . VAL   A 1 181  ? 14.004  15.029  -80.799 1.00 55.24  ? 330  VAL   A O     1 
ATOM   417  C  CB    . VAL   A 1 181  ? 15.621  13.985  -83.275 1.00 59.30  ? 330  VAL   A CB    1 
ATOM   418  C  CG1   . VAL   A 1 181  ? 17.006  13.638  -82.759 1.00 61.03  ? 330  VAL   A CG1   1 
ATOM   419  C  CG2   . VAL   A 1 181  ? 15.499  13.579  -84.734 1.00 66.73  ? 330  VAL   A CG2   1 
ATOM   420  N  N     . VAL   A 1 182  ? 15.083  13.185  -80.037 1.00 49.89  ? 331  VAL   A N     1 
ATOM   421  C  CA    . VAL   A 1 182  ? 15.253  13.726  -78.660 1.00 48.36  ? 331  VAL   A CA    1 
ATOM   422  C  C     . VAL   A 1 182  ? 16.261  14.870  -78.749 1.00 45.63  ? 331  VAL   A C     1 
ATOM   423  O  O     . VAL   A 1 182  ? 17.364  14.678  -79.269 1.00 41.20  ? 331  VAL   A O     1 
ATOM   424  C  CB    . VAL   A 1 182  ? 15.699  12.643  -77.666 1.00 48.84  ? 331  VAL   A CB    1 
ATOM   425  C  CG1   . VAL   A 1 182  ? 15.958  13.242  -76.300 1.00 51.07  ? 331  VAL   A CG1   1 
ATOM   426  C  CG2   . VAL   A 1 182  ? 14.680  11.519  -77.572 1.00 48.48  ? 331  VAL   A CG2   1 
ATOM   427  N  N     . PRO   A 1 183  ? 15.913  16.094  -78.286 1.00 43.20  ? 332  PRO   A N     1 
ATOM   428  C  CA    . PRO   A 1 183  ? 16.837  17.221  -78.368 1.00 44.22  ? 332  PRO   A CA    1 
ATOM   429  C  C     . PRO   A 1 183  ? 18.011  17.043  -77.393 1.00 46.25  ? 332  PRO   A C     1 
ATOM   430  O  O     . PRO   A 1 183  ? 17.845  16.437  -76.348 1.00 48.76  ? 332  PRO   A O     1 
ATOM   431  C  CB    . PRO   A 1 183  ? 15.992  18.458  -78.022 1.00 43.45  ? 332  PRO   A CB    1 
ATOM   432  C  CG    . PRO   A 1 183  ? 14.760  17.933  -77.305 1.00 43.40  ? 332  PRO   A CG    1 
ATOM   433  C  CD    . PRO   A 1 183  ? 14.634  16.461  -77.654 1.00 45.43  ? 332  PRO   A CD    1 
ATOM   434  N  N     . TRP   A 1 184  ? 19.164  17.597  -77.755 1.00 48.25  ? 333  TRP   A N     1 
ATOM   435  C  CA    . TRP   A 1 184  ? 20.408  17.589  -76.947 1.00 48.46  ? 333  TRP   A CA    1 
ATOM   436  C  C     . TRP   A 1 184  ? 20.922  19.021  -76.750 1.00 49.45  ? 333  TRP   A C     1 
ATOM   437  O  O     . TRP   A 1 184  ? 20.744  19.856  -77.651 1.00 51.25  ? 333  TRP   A O     1 
ATOM   438  C  CB    . TRP   A 1 184  ? 21.460  16.715  -77.622 1.00 47.00  ? 333  TRP   A CB    1 
ATOM   439  C  CG    . TRP   A 1 184  ? 22.779  16.765  -76.927 1.00 50.72  ? 333  TRP   A CG    1 
ATOM   440  C  CD1   . TRP   A 1 184  ? 23.167  16.008  -75.867 1.00 52.25  ? 333  TRP   A CD1   1 
ATOM   441  C  CD2   . TRP   A 1 184  ? 23.883  17.630  -77.231 1.00 53.00  ? 333  TRP   A CD2   1 
ATOM   442  N  NE1   . TRP   A 1 184  ? 24.439  16.327  -75.497 1.00 51.82  ? 333  TRP   A NE1   1 
ATOM   443  C  CE2   . TRP   A 1 184  ? 24.911  17.314  -76.317 1.00 54.29  ? 333  TRP   A CE2   1 
ATOM   444  C  CE3   . TRP   A 1 184  ? 24.109  18.623  -78.190 1.00 51.86  ? 333  TRP   A CE3   1 
ATOM   445  C  CZ2   . TRP   A 1 184  ? 26.143  17.971  -76.321 1.00 54.62  ? 333  TRP   A CZ2   1 
ATOM   446  C  CZ3   . TRP   A 1 184  ? 25.331  19.261  -78.205 1.00 55.73  ? 333  TRP   A CZ3   1 
ATOM   447  C  CH2   . TRP   A 1 184  ? 26.333  18.939  -77.282 1.00 56.31  ? 333  TRP   A CH2   1 
ATOM   448  N  N     . SER   A 1 185  ? 21.533  19.293  -75.599 1.00 50.91  ? 334  SER   A N     1 
ATOM   449  C  CA    . SER   A 1 185  ? 22.246  20.564  -75.322 1.00 49.76  ? 334  SER   A CA    1 
ATOM   450  C  C     . SER   A 1 185  ? 23.365  20.313  -74.321 1.00 53.57  ? 334  SER   A C     1 
ATOM   451  O  O     . SER   A 1 185  ? 23.239  19.494  -73.402 1.00 50.01  ? 334  SER   A O     1 
ATOM   452  C  CB    . SER   A 1 185  ? 21.307  21.679  -74.906 1.00 50.51  ? 334  SER   A CB    1 
ATOM   453  O  OG    . SER   A 1 185  ? 20.708  21.469  -73.640 1.00 51.77  ? 334  SER   A OG    1 
ATOM   454  N  N     . PRO   A 1 186  ? 24.528  20.968  -74.536 1.00 55.15  ? 335  PRO   A N     1 
ATOM   455  C  CA    . PRO   A 1 186  ? 25.712  20.757  -73.698 1.00 52.73  ? 335  PRO   A CA    1 
ATOM   456  C  C     . PRO   A 1 186  ? 25.577  21.227  -72.248 1.00 51.41  ? 335  PRO   A C     1 
ATOM   457  O  O     . PRO   A 1 186  ? 24.651  21.961  -71.901 1.00 50.47  ? 335  PRO   A O     1 
ATOM   458  C  CB    . PRO   A 1 186  ? 26.794  21.581  -74.415 1.00 53.04  ? 335  PRO   A CB    1 
ATOM   459  C  CG    . PRO   A 1 186  ? 26.004  22.655  -75.135 1.00 52.79  ? 335  PRO   A CG    1 
ATOM   460  C  CD    . PRO   A 1 186  ? 24.762  21.937  -75.619 1.00 53.32  ? 335  PRO   A CD    1 
ATOM   461  N  N     . PRO   A 1 187  ? 26.508  20.821  -71.355 1.00 46.82  ? 336  PRO   A N     1 
ATOM   462  C  CA    . PRO   A 1 187  ? 26.551  21.356  -69.994 1.00 51.30  ? 336  PRO   A CA    1 
ATOM   463  C  C     . PRO   A 1 187  ? 26.601  22.889  -69.969 1.00 51.62  ? 336  PRO   A C     1 
ATOM   464  O  O     . PRO   A 1 187  ? 27.184  23.491  -70.853 1.00 54.41  ? 336  PRO   A O     1 
ATOM   465  C  CB    . PRO   A 1 187  ? 27.835  20.756  -69.398 1.00 47.96  ? 336  PRO   A CB    1 
ATOM   466  C  CG    . PRO   A 1 187  ? 28.057  19.494  -70.209 1.00 47.33  ? 336  PRO   A CG    1 
ATOM   467  C  CD    . PRO   A 1 187  ? 27.582  19.848  -71.603 1.00 43.88  ? 336  PRO   A CD    1 
ATOM   468  N  N     . GLN   A 1 188  ? 25.977  23.460  -68.946 1.00 57.82  ? 337  GLN   A N     1 
ATOM   469  C  CA    . GLN   A 1 188  ? 25.861  24.916  -68.688 1.00 64.98  ? 337  GLN   A CA    1 
ATOM   470  C  C     . GLN   A 1 188  ? 26.061  25.132  -67.181 1.00 63.03  ? 337  GLN   A C     1 
ATOM   471  O  O     . GLN   A 1 188  ? 25.491  24.342  -66.389 1.00 55.54  ? 337  GLN   A O     1 
ATOM   472  C  CB    . GLN   A 1 188  ? 24.499  25.402  -69.177 1.00 71.76  ? 337  GLN   A CB    1 
ATOM   473  C  CG    . GLN   A 1 188  ? 24.497  26.829  -69.706 1.00 81.73  ? 337  GLN   A CG    1 
ATOM   474  C  CD    . GLN   A 1 188  ? 23.084  27.273  -70.004 1.00 88.05  ? 337  GLN   A CD    1 
ATOM   475  O  OE1   . GLN   A 1 188  ? 22.200  27.237  -69.147 1.00 88.65  ? 337  GLN   A OE1   1 
ATOM   476  N  NE2   . GLN   A 1 188  ? 22.847  27.683  -71.238 1.00 93.91  ? 337  GLN   A NE2   1 
ATOM   477  N  N     . SER   A 1 189  ? 26.847  26.148  -66.810 1.00 61.23  ? 338  SER   A N     1 
ATOM   478  C  CA    . SER   A 1 189  ? 27.339  26.410  -65.431 1.00 58.14  ? 338  SER   A CA    1 
ATOM   479  C  C     . SER   A 1 189  ? 26.168  26.582  -64.451 1.00 53.01  ? 338  SER   A C     1 
ATOM   480  O  O     . SER   A 1 189  ? 26.270  26.077  -63.312 1.00 57.29  ? 338  SER   A O     1 
ATOM   481  C  CB    . SER   A 1 189  ? 28.262  27.609  -65.414 1.00 59.68  ? 338  SER   A CB    1 
ATOM   482  O  OG    . SER   A 1 189  ? 27.583  28.794  -65.814 1.00 55.02  ? 338  SER   A OG    1 
ATOM   483  N  N     . ASN   A 1 190  ? 25.089  27.250  -64.862 1.00 47.61  ? 339  ASN   A N     1 
ATOM   484  C  CA    . ASN   A 1 190  ? 23.922  27.525  -63.977 1.00 54.71  ? 339  ASN   A CA    1 
ATOM   485  C  C     . ASN   A 1 190  ? 22.808  26.473  -64.164 1.00 52.71  ? 339  ASN   A C     1 
ATOM   486  O  O     . ASN   A 1 190  ? 21.641  26.788  -63.887 1.00 51.12  ? 339  ASN   A O     1 
ATOM   487  C  CB    . ASN   A 1 190  ? 23.388  28.932  -64.235 1.00 58.41  ? 339  ASN   A CB    1 
ATOM   488  C  CG    . ASN   A 1 190  ? 22.915  29.090  -65.661 1.00 60.45  ? 339  ASN   A CG    1 
ATOM   489  O  OD1   . ASN   A 1 190  ? 23.360  28.365  -66.546 1.00 61.70  ? 339  ASN   A OD1   1 
ATOM   490  N  ND2   . ASN   A 1 190  ? 22.021  30.033  -65.892 1.00 68.66  ? 339  ASN   A ND2   1 
ATOM   491  N  N     . TRP   A 1 191  ? 23.143  25.259  -64.607 1.00 53.08  ? 340  TRP   A N     1 
ATOM   492  C  CA    . TRP   A 1 191  ? 22.167  24.177  -64.902 1.00 50.85  ? 340  TRP   A CA    1 
ATOM   493  C  C     . TRP   A 1 191  ? 22.558  22.910  -64.145 1.00 46.63  ? 340  TRP   A C     1 
ATOM   494  O  O     . TRP   A 1 191  ? 23.728  22.477  -64.257 1.00 51.43  ? 340  TRP   A O     1 
ATOM   495  C  CB    . TRP   A 1 191  ? 22.079  23.915  -66.404 1.00 51.43  ? 340  TRP   A CB    1 
ATOM   496  C  CG    . TRP   A 1 191  ? 21.051  22.899  -66.794 1.00 56.41  ? 340  TRP   A CG    1 
ATOM   497  C  CD1   . TRP   A 1 191  ? 21.287  21.632  -67.237 1.00 56.81  ? 340  TRP   A CD1   1 
ATOM   498  C  CD2   . TRP   A 1 191  ? 19.623  23.060  -66.785 1.00 57.21  ? 340  TRP   A CD2   1 
ATOM   499  N  NE1   . TRP   A 1 191  ? 20.109  21.001  -67.511 1.00 51.34  ? 340  TRP   A NE1   1 
ATOM   500  C  CE2   . TRP   A 1 191  ? 19.072  21.842  -67.231 1.00 53.74  ? 340  TRP   A CE2   1 
ATOM   501  C  CE3   . TRP   A 1 191  ? 18.756  24.096  -66.418 1.00 60.73  ? 340  TRP   A CE3   1 
ATOM   502  C  CZ2   . TRP   A 1 191  ? 17.696  21.635  -67.333 1.00 57.12  ? 340  TRP   A CZ2   1 
ATOM   503  C  CZ3   . TRP   A 1 191  ? 17.396  23.894  -66.519 1.00 60.72  ? 340  TRP   A CZ3   1 
ATOM   504  C  CH2   . TRP   A 1 191  ? 16.875  22.681  -66.974 1.00 60.03  ? 340  TRP   A CH2   1 
ATOM   505  N  N     . ASN   A 1 192  ? 21.606  22.355  -63.401 1.00 42.55  ? 341  ASN   A N     1 
ATOM   506  C  CA    . ASN   A 1 192  ? 21.736  21.022  -62.770 1.00 45.52  ? 341  ASN   A CA    1 
ATOM   507  C  C     . ASN   A 1 192  ? 21.063  20.017  -63.697 1.00 44.52  ? 341  ASN   A C     1 
ATOM   508  O  O     . ASN   A 1 192  ? 19.838  19.954  -63.766 1.00 49.34  ? 341  ASN   A O     1 
ATOM   509  C  CB    . ASN   A 1 192  ? 21.135  20.984  -61.369 1.00 45.36  ? 341  ASN   A CB    1 
ATOM   510  C  CG    . ASN   A 1 192  ? 21.442  19.682  -60.670 1.00 44.28  ? 341  ASN   A CG    1 
ATOM   511  O  OD1   . ASN   A 1 192  ? 21.562  18.650  -61.318 1.00 43.31  ? 341  ASN   A OD1   1 
ATOM   512  N  ND2   . ASN   A 1 192  ? 21.628  19.734  -59.366 1.00 45.66  ? 341  ASN   A ND2   1 
ATOM   513  N  N     . PRO   A 1 193  ? 21.843  19.218  -64.444 1.00 40.79  ? 342  PRO   A N     1 
ATOM   514  C  CA    . PRO   A 1 193  ? 21.276  18.319  -65.443 1.00 42.96  ? 342  PRO   A CA    1 
ATOM   515  C  C     . PRO   A 1 193  ? 20.581  17.104  -64.812 1.00 45.67  ? 342  PRO   A C     1 
ATOM   516  O  O     . PRO   A 1 193  ? 19.773  16.500  -65.485 1.00 51.27  ? 342  PRO   A O     1 
ATOM   517  C  CB    . PRO   A 1 193  ? 22.507  17.888  -66.240 1.00 41.68  ? 342  PRO   A CB    1 
ATOM   518  C  CG    . PRO   A 1 193  ? 23.610  17.898  -65.210 1.00 40.80  ? 342  PRO   A CG    1 
ATOM   519  C  CD    . PRO   A 1 193  ? 23.299  19.091  -64.329 1.00 38.82  ? 342  PRO   A CD    1 
ATOM   520  N  N     . TRP   A 1 194  ? 20.885  16.794  -63.547 1.00 42.29  ? 343  TRP   A N     1 
ATOM   521  C  CA    . TRP   A 1 194  ? 20.306  15.634  -62.830 1.00 40.94  ? 343  TRP   A CA    1 
ATOM   522  C  C     . TRP   A 1 194  ? 18.891  15.951  -62.340 1.00 44.82  ? 343  TRP   A C     1 
ATOM   523  O  O     . TRP   A 1 194  ? 18.017  15.062  -62.480 1.00 43.92  ? 343  TRP   A O     1 
ATOM   524  C  CB    . TRP   A 1 194  ? 21.237  15.189  -61.707 1.00 42.28  ? 343  TRP   A CB    1 
ATOM   525  C  CG    . TRP   A 1 194  ? 22.664  15.099  -62.150 1.00 41.97  ? 343  TRP   A CG    1 
ATOM   526  C  CD1   . TRP   A 1 194  ? 23.741  15.681  -61.554 1.00 41.44  ? 343  TRP   A CD1   1 
ATOM   527  C  CD2   . TRP   A 1 194  ? 23.170  14.403  -63.300 1.00 41.60  ? 343  TRP   A CD2   1 
ATOM   528  N  NE1   . TRP   A 1 194  ? 24.882  15.387  -62.244 1.00 43.66  ? 343  TRP   A NE1   1 
ATOM   529  C  CE2   . TRP   A 1 194  ? 24.567  14.603  -63.320 1.00 43.81  ? 343  TRP   A CE2   1 
ATOM   530  C  CE3   . TRP   A 1 194  ? 22.594  13.625  -64.305 1.00 38.78  ? 343  TRP   A CE3   1 
ATOM   531  C  CZ2   . TRP   A 1 194  ? 25.389  14.067  -64.311 1.00 42.25  ? 343  TRP   A CZ2   1 
ATOM   532  C  CZ3   . TRP   A 1 194  ? 23.408  13.102  -65.286 1.00 42.37  ? 343  TRP   A CZ3   1 
ATOM   533  C  CH2   . TRP   A 1 194  ? 24.784  13.325  -65.294 1.00 40.70  ? 343  TRP   A CH2   1 
ATOM   534  N  N     . THR   A 1 195  ? 18.673  17.159  -61.808 1.00 47.01  ? 344  THR   A N     1 
ATOM   535  C  CA    . THR   A 1 195  ? 17.357  17.673  -61.334 1.00 47.71  ? 344  THR   A CA    1 
ATOM   536  C  C     . THR   A 1 195  ? 16.633  18.397  -62.467 1.00 47.52  ? 344  THR   A C     1 
ATOM   537  O  O     . THR   A 1 195  ? 15.454  18.738  -62.283 1.00 51.35  ? 344  THR   A O     1 
ATOM   538  C  CB    . THR   A 1 195  ? 17.500  18.621  -60.137 1.00 48.18  ? 344  THR   A CB    1 
ATOM   539  O  OG1   . THR   A 1 195  ? 18.279  19.743  -60.555 1.00 45.89  ? 344  THR   A OG1   1 
ATOM   540  C  CG2   . THR   A 1 195  ? 18.137  17.948  -58.937 1.00 50.13  ? 344  THR   A CG2   1 
ATOM   541  N  N     . SER   A 1 196  ? 17.303  18.629  -63.593 1.00 51.52  ? 345  SER   A N     1 
ATOM   542  C  CA    . SER   A 1 196  ? 16.708  19.312  -64.768 1.00 52.56  ? 345  SER   A CA    1 
ATOM   543  C  C     . SER   A 1 196  ? 16.097  20.635  -64.307 1.00 56.32  ? 345  SER   A C     1 
ATOM   544  O  O     . SER   A 1 196  ? 14.890  20.850  -64.537 1.00 59.48  ? 345  SER   A O     1 
ATOM   545  C  CB    . SER   A 1 196  ? 15.677  18.438  -65.446 1.00 53.48  ? 345  SER   A CB    1 
ATOM   546  O  OG    . SER   A 1 196  ? 16.293  17.303  -66.034 1.00 60.01  ? 345  SER   A OG    1 
ATOM   547  N  N     . SER   A 1 197  ? 16.902  21.482  -63.667 1.00 57.68  ? 346  SER   A N     1 
ATOM   548  C  CA    . SER   A 1 197  ? 16.473  22.820  -63.192 1.00 58.03  ? 346  SER   A CA    1 
ATOM   549  C  C     . SER   A 1 197  ? 17.658  23.787  -63.107 1.00 60.52  ? 346  SER   A C     1 
ATOM   550  O  O     . SER   A 1 197  ? 18.838  23.339  -63.086 1.00 59.25  ? 346  SER   A O     1 
ATOM   551  C  CB    . SER   A 1 197  ? 15.781  22.703  -61.882 1.00 57.58  ? 346  SER   A CB    1 
ATOM   552  O  OG    . SER   A 1 197  ? 16.706  22.331  -60.885 1.00 57.36  ? 346  SER   A OG    1 
ATOM   553  N  N     . ASN   A 1 198  ? 17.340  25.081  -63.084 1.00 65.89  ? 347  ASN   A N     1 
ATOM   554  C  CA    . ASN   A 1 198  ? 18.323  26.180  -62.900 1.00 63.45  ? 347  ASN   A CA    1 
ATOM   555  C  C     . ASN   A 1 198  ? 18.891  26.086  -61.482 1.00 56.55  ? 347  ASN   A C     1 
ATOM   556  O  O     . ASN   A 1 198  ? 18.122  25.770  -60.535 1.00 56.69  ? 347  ASN   A O     1 
ATOM   557  C  CB    . ASN   A 1 198  ? 17.691  27.545  -63.185 1.00 66.87  ? 347  ASN   A CB    1 
ATOM   558  C  CG    . ASN   A 1 198  ? 17.326  27.732  -64.643 1.00 72.14  ? 347  ASN   A CG    1 
ATOM   559  O  OD1   . ASN   A 1 198  ? 16.200  28.114  -64.959 1.00 76.21  ? 347  ASN   A OD1   1 
ATOM   560  N  ND2   . ASN   A 1 198  ? 18.265  27.468  -65.539 1.00 69.73  ? 347  ASN   A ND2   1 
ATOM   561  N  N     . ILE   A 1 199  ? 20.195  26.295  -61.343 1.00 53.89  ? 348  ILE   A N     1 
ATOM   562  C  CA    . ILE   A 1 199  ? 20.816  26.612  -60.024 1.00 63.34  ? 348  ILE   A CA    1 
ATOM   563  C  C     . ILE   A 1 199  ? 20.521  28.098  -59.754 1.00 67.11  ? 348  ILE   A C     1 
ATOM   564  O  O     . ILE   A 1 199  ? 20.928  28.949  -60.590 1.00 65.47  ? 348  ILE   A O     1 
ATOM   565  C  CB    . ILE   A 1 199  ? 22.321  26.263  -60.020 1.00 61.35  ? 348  ILE   A CB    1 
ATOM   566  C  CG1   . ILE   A 1 199  ? 22.570  24.782  -60.334 1.00 60.83  ? 348  ILE   A CG1   1 
ATOM   567  C  CG2   . ILE   A 1 199  ? 22.955  26.663  -58.700 1.00 58.48  ? 348  ILE   A CG2   1 
ATOM   568  C  CD1   . ILE   A 1 199  ? 23.947  24.481  -60.905 1.00 60.04  ? 348  ILE   A CD1   1 
ATOM   569  N  N     . ASP   A 1 200  ? 19.781  28.390  -58.676 1.00 78.79  ? 349  ASP   A N     1 
ATOM   570  C  CA    . ASP   A 1 200  ? 19.246  29.743  -58.335 1.00 91.38  ? 349  ASP   A CA    1 
ATOM   571  C  C     . ASP   A 1 200  ? 19.929  30.298  -57.078 1.00 88.60  ? 349  ASP   A C     1 
ATOM   572  O  O     . ASP   A 1 200  ? 20.271  31.494  -57.069 1.00 86.73  ? 349  ASP   A O     1 
ATOM   573  C  CB    . ASP   A 1 200  ? 17.733  29.700  -58.099 1.00 93.13  ? 349  ASP   A CB    1 
ATOM   574  C  CG    . ASP   A 1 200  ? 16.905  29.895  -59.358 1.00 102.74 ? 349  ASP   A CG    1 
ATOM   575  O  OD1   . ASP   A 1 200  ? 17.469  30.368  -60.378 1.00 97.56  ? 349  ASP   A OD1   1 
ATOM   576  O  OD2   . ASP   A 1 200  ? 15.699  29.578  -59.306 1.00 101.87 ? 349  ASP   A OD2   1 
ATOM   577  N  N     . GLU   A 1 201  ? 20.064  29.467  -56.043 1.00 83.46  ? 350  GLU   A N     1 
ATOM   578  C  CA    . GLU   A 1 201  ? 20.715  29.815  -54.757 1.00 88.98  ? 350  GLU   A CA    1 
ATOM   579  C  C     . GLU   A 1 201  ? 22.214  29.536  -54.887 1.00 82.87  ? 350  GLU   A C     1 
ATOM   580  O  O     . GLU   A 1 201  ? 22.603  28.819  -55.826 1.00 81.75  ? 350  GLU   A O     1 
ATOM   581  C  CB    . GLU   A 1 201  ? 20.070  29.020  -53.618 1.00 93.98  ? 350  GLU   A CB    1 
ATOM   582  C  CG    . GLU   A 1 201  ? 18.620  29.407  -53.356 1.00 100.12 ? 350  GLU   A CG    1 
ATOM   583  C  CD    . GLU   A 1 201  ? 17.691  28.261  -52.970 1.00 107.01 ? 350  GLU   A CD    1 
ATOM   584  O  OE1   . GLU   A 1 201  ? 18.121  27.363  -52.202 1.00 101.70 ? 350  GLU   A OE1   1 
ATOM   585  O  OE2   . GLU   A 1 201  ? 16.531  28.266  -53.441 1.00 101.06 ? 350  GLU   A OE2   1 
ATOM   586  N  N     . GLY   A 1 202  ? 23.017  30.122  -53.995 1.00 83.16  ? 351  GLY   A N     1 
ATOM   587  C  CA    . GLY   A 1 202  ? 24.442  29.788  -53.806 1.00 73.91  ? 351  GLY   A CA    1 
ATOM   588  C  C     . GLY   A 1 202  ? 25.336  30.347  -54.908 1.00 67.66  ? 351  GLY   A C     1 
ATOM   589  O  O     . GLY   A 1 202  ? 24.861  30.914  -55.896 1.00 66.07  ? 351  GLY   A O     1 
ATOM   590  N  N     . PRO   A 1 203  ? 26.670  30.183  -54.754 1.00 69.96  ? 352  PRO   A N     1 
ATOM   591  C  CA    . PRO   A 1 203  ? 27.653  30.756  -55.680 1.00 68.10  ? 352  PRO   A CA    1 
ATOM   592  C  C     . PRO   A 1 203  ? 27.591  30.239  -57.126 1.00 71.07  ? 352  PRO   A C     1 
ATOM   593  O  O     . PRO   A 1 203  ? 28.038  30.955  -58.016 1.00 69.17  ? 352  PRO   A O     1 
ATOM   594  C  CB    . PRO   A 1 203  ? 29.028  30.380  -55.082 1.00 66.67  ? 352  PRO   A CB    1 
ATOM   595  C  CG    . PRO   A 1 203  ? 28.750  29.288  -54.061 1.00 64.44  ? 352  PRO   A CG    1 
ATOM   596  C  CD    . PRO   A 1 203  ? 27.307  29.472  -53.631 1.00 68.04  ? 352  PRO   A CD    1 
ATOM   597  N  N     . LEU   A 1 204  ? 27.062  29.029  -57.336 1.00 65.49  ? 353  LEU   A N     1 
ATOM   598  C  CA    . LEU   A 1 204  ? 27.127  28.354  -58.658 1.00 66.20  ? 353  LEU   A CA    1 
ATOM   599  C  C     . LEU   A 1 204  ? 26.117  28.987  -59.625 1.00 66.69  ? 353  LEU   A C     1 
ATOM   600  O  O     . LEU   A 1 204  ? 26.225  28.704  -60.837 1.00 68.76  ? 353  LEU   A O     1 
ATOM   601  C  CB    . LEU   A 1 204  ? 26.889  26.855  -58.458 1.00 68.65  ? 353  LEU   A CB    1 
ATOM   602  C  CG    . LEU   A 1 204  ? 27.957  26.152  -57.619 1.00 68.76  ? 353  LEU   A CG    1 
ATOM   603  C  CD1   . LEU   A 1 204  ? 27.477  24.794  -57.119 1.00 69.57  ? 353  LEU   A CD1   1 
ATOM   604  C  CD2   . LEU   A 1 204  ? 29.257  26.024  -58.403 1.00 64.37  ? 353  LEU   A CD2   1 
ATOM   605  N  N     . ALA   A 1 205  ? 25.201  29.830  -59.126 1.00 65.81  ? 354  ALA   A N     1 
ATOM   606  C  CA    . ALA   A 1 205  ? 24.183  30.547  -59.937 1.00 65.71  ? 354  ALA   A CA    1 
ATOM   607  C  C     . ALA   A 1 205  ? 24.845  31.555  -60.887 1.00 71.02  ? 354  ALA   A C     1 
ATOM   608  O  O     . ALA   A 1 205  ? 24.271  31.775  -61.970 1.00 84.06  ? 354  ALA   A O     1 
ATOM   609  C  CB    . ALA   A 1 205  ? 23.173  31.230  -59.046 1.00 62.45  ? 354  ALA   A CB    1 
ATOM   610  N  N     . TYR   A 1 206  ? 25.987  32.151  -60.512 1.00 70.42  ? 355  TYR   A N     1 
ATOM   611  C  CA    . TYR   A 1 206  ? 26.672  33.224  -61.293 1.00 64.55  ? 355  TYR   A CA    1 
ATOM   612  C  C     . TYR   A 1 206  ? 28.120  32.827  -61.622 1.00 62.75  ? 355  TYR   A C     1 
ATOM   613  O  O     . TYR   A 1 206  ? 28.636  33.294  -62.649 1.00 70.33  ? 355  TYR   A O     1 
ATOM   614  C  CB    . TYR   A 1 206  ? 26.613  34.564  -60.547 1.00 63.67  ? 355  TYR   A CB    1 
ATOM   615  C  CG    . TYR   A 1 206  ? 26.957  34.475  -59.078 1.00 62.75  ? 355  TYR   A CG    1 
ATOM   616  C  CD1   . TYR   A 1 206  ? 28.279  34.481  -58.657 1.00 59.12  ? 355  TYR   A CD1   1 
ATOM   617  C  CD2   . TYR   A 1 206  ? 25.966  34.352  -58.112 1.00 59.61  ? 355  TYR   A CD2   1 
ATOM   618  C  CE1   . TYR   A 1 206  ? 28.614  34.371  -57.315 1.00 62.30  ? 355  TYR   A CE1   1 
ATOM   619  C  CE2   . TYR   A 1 206  ? 26.283  34.247  -56.765 1.00 62.73  ? 355  TYR   A CE2   1 
ATOM   620  C  CZ    . TYR   A 1 206  ? 27.613  34.257  -56.362 1.00 64.68  ? 355  TYR   A CZ    1 
ATOM   621  O  OH    . TYR   A 1 206  ? 27.957  34.150  -55.041 1.00 55.76  ? 355  TYR   A OH    1 
ATOM   622  N  N     . ALA   A 1 207  ? 28.765  32.009  -60.787 1.00 63.46  ? 356  ALA   A N     1 
ATOM   623  C  CA    . ALA   A 1 207  ? 30.167  31.555  -60.965 1.00 64.56  ? 356  ALA   A CA    1 
ATOM   624  C  C     . ALA   A 1 207  ? 30.404  31.171  -62.430 1.00 67.59  ? 356  ALA   A C     1 
ATOM   625  O  O     . ALA   A 1 207  ? 29.547  30.469  -62.994 1.00 73.49  ? 356  ALA   A O     1 
ATOM   626  C  CB    . ALA   A 1 207  ? 30.440  30.393  -60.047 1.00 67.63  ? 356  ALA   A CB    1 
ATOM   627  N  N     . THR   A 1 208  ? 31.508  31.622  -63.034 1.00 68.86  ? 357  THR   A N     1 
ATOM   628  C  CA    . THR   A 1 208  ? 31.844  31.305  -64.446 1.00 67.16  ? 357  THR   A CA    1 
ATOM   629  C  C     . THR   A 1 208  ? 32.365  29.875  -64.537 1.00 68.90  ? 357  THR   A C     1 
ATOM   630  O  O     . THR   A 1 208  ? 32.858  29.304  -63.554 1.00 67.87  ? 357  THR   A O     1 
ATOM   631  C  CB    . THR   A 1 208  ? 32.873  32.268  -65.056 1.00 68.57  ? 357  THR   A CB    1 
ATOM   632  O  OG1   . THR   A 1 208  ? 34.070  32.179  -64.285 1.00 69.17  ? 357  THR   A OG1   1 
ATOM   633  C  CG2   . THR   A 1 208  ? 32.379  33.699  -65.130 1.00 65.91  ? 357  THR   A CG2   1 
ATOM   634  N  N     . PRO   A 1 209  ? 32.266  29.265  -65.738 1.00 63.66  ? 358  PRO   A N     1 
ATOM   635  C  CA    . PRO   A 1 209  ? 32.885  27.970  -66.004 1.00 62.61  ? 358  PRO   A CA    1 
ATOM   636  C  C     . PRO   A 1 209  ? 34.333  27.873  -65.510 1.00 60.83  ? 358  PRO   A C     1 
ATOM   637  O  O     . PRO   A 1 209  ? 34.685  26.858  -64.921 1.00 63.54  ? 358  PRO   A O     1 
ATOM   638  C  CB    . PRO   A 1 209  ? 32.809  27.875  -67.538 1.00 67.40  ? 358  PRO   A CB    1 
ATOM   639  C  CG    . PRO   A 1 209  ? 31.545  28.627  -67.891 1.00 62.02  ? 358  PRO   A CG    1 
ATOM   640  C  CD    . PRO   A 1 209  ? 31.504  29.771  -66.896 1.00 64.84  ? 358  PRO   A CD    1 
ATOM   641  N  N     . GLU   A 1 210  ? 35.119  28.923  -65.750 1.00 66.72  ? 359  GLU   A N     1 
ATOM   642  C  CA    . GLU   A 1 210  ? 36.560  29.008  -65.383 1.00 67.18  ? 359  GLU   A CA    1 
ATOM   643  C  C     . GLU   A 1 210  ? 36.694  28.913  -63.860 1.00 65.89  ? 359  GLU   A C     1 
ATOM   644  O  O     . GLU   A 1 210  ? 37.477  28.056  -63.387 1.00 60.69  ? 359  GLU   A O     1 
ATOM   645  C  CB    . GLU   A 1 210  ? 37.180  30.303  -65.915 1.00 74.54  ? 359  GLU   A CB    1 
ATOM   646  C  CG    . GLU   A 1 210  ? 37.278  30.362  -67.439 1.00 81.10  ? 359  GLU   A CG    1 
ATOM   647  C  CD    . GLU   A 1 210  ? 35.973  30.569  -68.203 1.00 79.11  ? 359  GLU   A CD    1 
ATOM   648  O  OE1   . GLU   A 1 210  ? 35.042  31.189  -67.646 1.00 68.97  ? 359  GLU   A OE1   1 
ATOM   649  O  OE2   . GLU   A 1 210  ? 35.887  30.100  -69.356 1.00 79.22  ? 359  GLU   A OE2   1 
ATOM   650  N  N     . GLN   A 1 211  ? 35.945  29.736  -63.120 1.00 63.39  ? 360  GLN   A N     1 
ATOM   651  C  CA    . GLN   A 1 211  ? 35.933  29.697  -61.631 1.00 67.12  ? 360  GLN   A CA    1 
ATOM   652  C  C     . GLN   A 1 211  ? 35.682  28.252  -61.175 1.00 64.68  ? 360  GLN   A C     1 
ATOM   653  O  O     . GLN   A 1 211  ? 36.475  27.724  -60.360 1.00 61.91  ? 360  GLN   A O     1 
ATOM   654  C  CB    . GLN   A 1 211  ? 34.872  30.642  -61.059 1.00 76.56  ? 360  GLN   A CB    1 
ATOM   655  C  CG    . GLN   A 1 211  ? 35.211  32.126  -61.184 1.00 88.66  ? 360  GLN   A CG    1 
ATOM   656  C  CD    . GLN   A 1 211  ? 34.103  33.026  -60.680 1.00 89.94  ? 360  GLN   A CD    1 
ATOM   657  O  OE1   . GLN   A 1 211  ? 33.136  33.318  -61.385 1.00 87.40  ? 360  GLN   A OE1   1 
ATOM   658  N  NE2   . GLN   A 1 211  ? 34.241  33.480  -59.444 1.00 87.94  ? 360  GLN   A NE2   1 
ATOM   659  N  N     . ILE   A 1 212  ? 34.617  27.635  -61.697 1.00 64.82  ? 361  ILE   A N     1 
ATOM   660  C  CA    . ILE   A 1 212  ? 34.150  26.278  -61.290 1.00 56.59  ? 361  ILE   A CA    1 
ATOM   661  C  C     . ILE   A 1 212  ? 35.269  25.276  -61.594 1.00 53.64  ? 361  ILE   A C     1 
ATOM   662  O  O     . ILE   A 1 212  ? 35.565  24.451  -60.709 1.00 53.60  ? 361  ILE   A O     1 
ATOM   663  C  CB    . ILE   A 1 212  ? 32.799  25.931  -61.964 1.00 58.79  ? 361  ILE   A CB    1 
ATOM   664  C  CG1   . ILE   A 1 212  ? 31.647  26.707  -61.314 1.00 59.77  ? 361  ILE   A CG1   1 
ATOM   665  C  CG2   . ILE   A 1 212  ? 32.528  24.431  -61.950 1.00 55.57  ? 361  ILE   A CG2   1 
ATOM   666  C  CD1   . ILE   A 1 212  ? 30.495  27.014  -62.242 1.00 60.66  ? 361  ILE   A CD1   1 
ATOM   667  N  N     . SER   A 1 213  ? 35.903  25.379  -62.765 1.00 52.70  ? 362  SER   A N     1 
ATOM   668  C  CA    . SER   A 1 213  ? 36.923  24.403  -63.241 1.00 57.01  ? 362  SER   A CA    1 
ATOM   669  C  C     . SER   A 1 213  ? 38.194  24.473  -62.385 1.00 53.52  ? 362  SER   A C     1 
ATOM   670  O  O     . SER   A 1 213  ? 38.782  23.401  -62.075 1.00 52.22  ? 362  SER   A O     1 
ATOM   671  C  CB    . SER   A 1 213  ? 37.222  24.596  -64.709 1.00 59.53  ? 362  SER   A CB    1 
ATOM   672  O  OG    . SER   A 1 213  ? 36.045  24.422  -65.498 1.00 55.84  ? 362  SER   A OG    1 
ATOM   673  N  N     . MET   A 1 214  ? 38.602  25.689  -62.021 1.00 62.73  ? 363  MET   A N     1 
ATOM   674  C  CA    . MET   A 1 214  ? 39.817  25.984  -61.214 1.00 59.46  ? 363  MET   A CA    1 
ATOM   675  C  C     . MET   A 1 214  ? 39.625  25.349  -59.839 1.00 53.37  ? 363  MET   A C     1 
ATOM   676  O  O     . MET   A 1 214  ? 40.515  24.579  -59.414 1.00 45.00  ? 363  MET   A O     1 
ATOM   677  C  CB    . MET   A 1 214  ? 40.002  27.500  -61.086 1.00 72.73  ? 363  MET   A CB    1 
ATOM   678  C  CG    . MET   A 1 214  ? 41.361  27.954  -60.567 1.00 84.79  ? 363  MET   A CG    1 
ATOM   679  S  SD    . MET   A 1 214  ? 41.802  29.630  -61.176 1.00 93.51  ? 363  MET   A SD    1 
ATOM   680  C  CE    . MET   A 1 214  ? 40.384  30.605  -60.665 1.00 87.75  ? 363  MET   A CE    1 
ATOM   681  N  N     . ASP   A 1 215  ? 38.469  25.610  -59.213 1.00 53.43  ? 364  ASP   A N     1 
ATOM   682  C  CA    . ASP   A 1 215  ? 38.158  25.172  -57.828 1.00 56.63  ? 364  ASP   A CA    1 
ATOM   683  C  C     . ASP   A 1 215  ? 38.224  23.644  -57.787 1.00 60.10  ? 364  ASP   A C     1 
ATOM   684  O  O     . ASP   A 1 215  ? 38.949  23.088  -56.903 1.00 54.82  ? 364  ASP   A O     1 
ATOM   685  C  CB    . ASP   A 1 215  ? 36.814  25.715  -57.328 1.00 66.06  ? 364  ASP   A CB    1 
ATOM   686  C  CG    . ASP   A 1 215  ? 36.832  27.163  -56.837 1.00 76.60  ? 364  ASP   A CG    1 
ATOM   687  O  OD1   . ASP   A 1 215  ? 37.869  27.854  -57.030 1.00 73.40  ? 364  ASP   A OD1   1 
ATOM   688  O  OD2   . ASP   A 1 215  ? 35.798  27.600  -56.260 1.00 80.49  ? 364  ASP   A OD2   1 
ATOM   689  N  N     . LEU   A 1 216  ? 37.538  22.989  -58.728 1.00 57.17  ? 365  LEU   A N     1 
ATOM   690  C  CA    . LEU   A 1 216  ? 37.497  21.507  -58.797 1.00 54.75  ? 365  LEU   A CA    1 
ATOM   691  C  C     . LEU   A 1 216  ? 38.910  21.008  -59.112 1.00 50.06  ? 365  LEU   A C     1 
ATOM   692  O  O     . LEU   A 1 216  ? 39.373  20.092  -58.416 1.00 42.25  ? 365  LEU   A O     1 
ATOM   693  C  CB    . LEU   A 1 216  ? 36.472  21.064  -59.844 1.00 56.35  ? 365  LEU   A CB    1 
ATOM   694  C  CG    . LEU   A 1 216  ? 35.014  21.378  -59.503 1.00 53.26  ? 365  LEU   A CG    1 
ATOM   695  C  CD1   . LEU   A 1 216  ? 34.142  21.203  -60.732 1.00 55.06  ? 365  LEU   A CD1   1 
ATOM   696  C  CD2   . LEU   A 1 216  ? 34.497  20.519  -58.363 1.00 55.76  ? 365  LEU   A CD2   1 
ATOM   697  N  N     . LYS   A 1 217  ? 39.614  21.627  -60.059 1.00 48.40  ? 366  LYS   A N     1 
ATOM   698  C  CA    . LYS   A 1 217  ? 41.022  21.226  -60.331 1.00 53.51  ? 366  LYS   A CA    1 
ATOM   699  C  C     . LYS   A 1 217  ? 41.849  21.282  -59.033 1.00 53.68  ? 366  LYS   A C     1 
ATOM   700  O  O     . LYS   A 1 217  ? 42.466  20.263  -58.689 1.00 51.67  ? 366  LYS   A O     1 
ATOM   701  C  CB    . LYS   A 1 217  ? 41.668  22.074  -61.428 1.00 56.23  ? 366  LYS   A CB    1 
ATOM   702  C  CG    . LYS   A 1 217  ? 42.985  21.496  -61.928 1.00 59.12  ? 366  LYS   A CG    1 
ATOM   703  C  CD    . LYS   A 1 217  ? 43.664  22.315  -63.013 1.00 65.94  ? 366  LYS   A CD    1 
ATOM   704  C  CE    . LYS   A 1 217  ? 45.104  21.889  -63.238 1.00 66.48  ? 366  LYS   A CE    1 
ATOM   705  N  NZ    . LYS   A 1 217  ? 45.568  22.225  -64.604 1.00 68.91  ? 366  LYS   A NZ    1 
ATOM   706  N  N     . ASN   A 1 218  ? 41.845  22.417  -58.325 1.00 54.74  ? 367  ASN   A N     1 
ATOM   707  C  CA    . ASN   A 1 218  ? 42.662  22.644  -57.099 1.00 54.12  ? 367  ASN   A CA    1 
ATOM   708  C  C     . ASN   A 1 218  ? 42.230  21.674  -55.994 1.00 56.57  ? 367  ASN   A C     1 
ATOM   709  O  O     . ASN   A 1 218  ? 43.128  21.144  -55.295 1.00 58.11  ? 367  ASN   A O     1 
ATOM   710  C  CB    . ASN   A 1 218  ? 42.595  24.106  -56.627 1.00 55.87  ? 367  ASN   A CB    1 
ATOM   711  C  CG    . ASN   A 1 218  ? 43.307  25.074  -57.559 1.00 54.35  ? 367  ASN   A CG    1 
ATOM   712  O  OD1   . ASN   A 1 218  ? 44.359  24.766  -58.131 1.00 57.41  ? 367  ASN   A OD1   1 
ATOM   713  N  ND2   . ASN   A 1 218  ? 42.736  26.252  -57.740 1.00 54.03  ? 367  ASN   A ND2   1 
ATOM   714  N  N     . GLU   A 1 219  ? 40.917  21.450  -55.847 1.00 57.76  ? 368  GLU   A N     1 
ATOM   715  C  CA    . GLU   A 1 219  ? 40.312  20.560  -54.811 1.00 58.94  ? 368  GLU   A CA    1 
ATOM   716  C  C     . GLU   A 1 219  ? 40.856  19.145  -55.009 1.00 55.21  ? 368  GLU   A C     1 
ATOM   717  O  O     . GLU   A 1 219  ? 41.234  18.516  -54.008 1.00 59.33  ? 368  GLU   A O     1 
ATOM   718  C  CB    . GLU   A 1 219  ? 38.783  20.625  -54.892 1.00 64.26  ? 368  GLU   A CB    1 
ATOM   719  C  CG    . GLU   A 1 219  ? 38.021  19.658  -53.996 1.00 69.00  ? 368  GLU   A CG    1 
ATOM   720  C  CD    . GLU   A 1 219  ? 36.508  19.825  -54.125 1.00 80.14  ? 368  GLU   A CD    1 
ATOM   721  O  OE1   . GLU   A 1 219  ? 35.802  18.819  -54.378 1.00 71.77  ? 368  GLU   A OE1   1 
ATOM   722  O  OE2   . GLU   A 1 219  ? 36.032  20.979  -54.010 1.00 90.11  ? 368  GLU   A OE2   1 
ATOM   723  N  N     . LEU   A 1 220  ? 40.936  18.693  -56.260 1.00 54.99  ? 369  LEU   A N     1 
ATOM   724  C  CA    . LEU   A 1 220  ? 41.433  17.344  -56.629 1.00 57.78  ? 369  LEU   A CA    1 
ATOM   725  C  C     . LEU   A 1 220  ? 42.943  17.260  -56.375 1.00 56.78  ? 369  LEU   A C     1 
ATOM   726  O  O     . LEU   A 1 220  ? 43.373  16.278  -55.738 1.00 55.63  ? 369  LEU   A O     1 
ATOM   727  C  CB    . LEU   A 1 220  ? 41.100  17.065  -58.097 1.00 60.27  ? 369  LEU   A CB    1 
ATOM   728  C  CG    . LEU   A 1 220  ? 41.427  15.658  -58.596 1.00 60.43  ? 369  LEU   A CG    1 
ATOM   729  C  CD1   . LEU   A 1 220  ? 40.620  14.614  -57.836 1.00 58.43  ? 369  LEU   A CD1   1 
ATOM   730  C  CD2   . LEU   A 1 220  ? 41.173  15.553  -60.095 1.00 65.26  ? 369  LEU   A CD2   1 
ATOM   731  N  N     . MET   A 1 221  ? 43.719  18.236  -56.852 1.00 59.58  ? 370  MET   A N     1 
ATOM   732  C  CA    . MET   A 1 221  ? 45.196  18.257  -56.655 1.00 63.46  ? 370  MET   A CA    1 
ATOM   733  C  C     . MET   A 1 221  ? 45.506  18.194  -55.153 1.00 59.49  ? 370  MET   A C     1 
ATOM   734  O  O     . MET   A 1 221  ? 46.374  17.398  -54.791 1.00 51.37  ? 370  MET   A O     1 
ATOM   735  C  CB    . MET   A 1 221  ? 45.854  19.486  -57.287 1.00 70.14  ? 370  MET   A CB    1 
ATOM   736  C  CG    . MET   A 1 221  ? 46.086  19.350  -58.792 1.00 82.70  ? 370  MET   A CG    1 
ATOM   737  S  SD    . MET   A 1 221  ? 47.242  20.600  -59.464 1.00 104.19 ? 370  MET   A SD    1 
ATOM   738  C  CE    . MET   A 1 221  ? 46.389  22.134  -59.089 1.00 101.83 ? 370  MET   A CE    1 
ATOM   739  N  N     . TYR   A 1 222  ? 44.778  18.930  -54.300 1.00 58.33  ? 371  TYR   A N     1 
ATOM   740  C  CA    . TYR   A 1 222  ? 45.029  18.954  -52.833 1.00 57.91  ? 371  TYR   A CA    1 
ATOM   741  C  C     . TYR   A 1 222  ? 44.749  17.564  -52.245 1.00 62.75  ? 371  TYR   A C     1 
ATOM   742  O  O     . TYR   A 1 222  ? 45.605  17.023  -51.494 1.00 66.90  ? 371  TYR   A O     1 
ATOM   743  C  CB    . TYR   A 1 222  ? 44.237  20.063  -52.128 1.00 58.73  ? 371  TYR   A CB    1 
ATOM   744  C  CG    . TYR   A 1 222  ? 44.568  20.208  -50.661 1.00 60.96  ? 371  TYR   A CG    1 
ATOM   745  C  CD1   . TYR   A 1 222  ? 45.857  20.527  -50.254 1.00 61.58  ? 371  TYR   A CD1   1 
ATOM   746  C  CD2   . TYR   A 1 222  ? 43.610  20.004  -49.675 1.00 59.00  ? 371  TYR   A CD2   1 
ATOM   747  C  CE1   . TYR   A 1 222  ? 46.185  20.637  -48.913 1.00 61.71  ? 371  TYR   A CE1   1 
ATOM   748  C  CE2   . TYR   A 1 222  ? 43.920  20.119  -48.329 1.00 59.83  ? 371  TYR   A CE2   1 
ATOM   749  C  CZ    . TYR   A 1 222  ? 45.215  20.434  -47.946 1.00 62.89  ? 371  TYR   A CZ    1 
ATOM   750  O  OH    . TYR   A 1 222  ? 45.554  20.542  -46.626 1.00 61.94  ? 371  TYR   A OH    1 
ATOM   751  N  N     . GLN   A 1 223  ? 43.588  16.995  -52.573 1.00 64.12  ? 372  GLN   A N     1 
ATOM   752  C  CA    . GLN   A 1 223  ? 43.123  15.681  -52.049 1.00 62.38  ? 372  GLN   A CA    1 
ATOM   753  C  C     . GLN   A 1 223  ? 44.193  14.617  -52.345 1.00 60.28  ? 372  GLN   A C     1 
ATOM   754  O  O     . GLN   A 1 223  ? 44.487  13.825  -51.423 1.00 57.68  ? 372  GLN   A O     1 
ATOM   755  C  CB    . GLN   A 1 223  ? 41.749  15.368  -52.651 1.00 65.47  ? 372  GLN   A CB    1 
ATOM   756  C  CG    . GLN   A 1 223  ? 41.124  14.050  -52.208 1.00 66.21  ? 372  GLN   A CG    1 
ATOM   757  C  CD    . GLN   A 1 223  ? 40.020  13.610  -53.148 1.00 69.13  ? 372  GLN   A CD    1 
ATOM   758  O  OE1   . GLN   A 1 223  ? 39.693  14.273  -54.133 1.00 69.68  ? 372  GLN   A OE1   1 
ATOM   759  N  NE2   . GLN   A 1 223  ? 39.409  12.482  -52.835 1.00 67.42  ? 372  GLN   A NE2   1 
ATOM   760  N  N     . LEU   A 1 224  ? 44.773  14.632  -53.556 1.00 59.99  ? 373  LEU   A N     1 
ATOM   761  C  CA    . LEU   A 1 224  ? 45.817  13.671  -54.036 1.00 66.54  ? 373  LEU   A CA    1 
ATOM   762  C  C     . LEU   A 1 224  ? 47.169  13.906  -53.339 1.00 64.20  ? 373  LEU   A C     1 
ATOM   763  O  O     . LEU   A 1 224  ? 47.934  12.929  -53.263 1.00 71.56  ? 373  LEU   A O     1 
ATOM   764  C  CB    . LEU   A 1 224  ? 45.987  13.781  -55.561 1.00 70.78  ? 373  LEU   A CB    1 
ATOM   765  C  CG    . LEU   A 1 224  ? 45.226  12.758  -56.409 1.00 77.45  ? 373  LEU   A CG    1 
ATOM   766  C  CD1   . LEU   A 1 224  ? 43.739  12.740  -56.076 1.00 80.29  ? 373  LEU   A CD1   1 
ATOM   767  C  CD2   . LEU   A 1 224  ? 45.418  13.028  -57.895 1.00 79.66  ? 373  LEU   A CD2   1 
ATOM   768  N  N     . GLU   A 1 225  ? 47.486  15.134  -52.903 1.00 64.98  ? 374  GLU   A N     1 
ATOM   769  C  CA    . GLU   A 1 225  ? 48.736  15.456  -52.142 1.00 69.19  ? 374  GLU   A CA    1 
ATOM   770  C  C     . GLU   A 1 225  ? 48.623  14.918  -50.707 1.00 68.99  ? 374  GLU   A C     1 
ATOM   771  O  O     . GLU   A 1 225  ? 49.654  14.451  -50.156 1.00 62.00  ? 374  GLU   A O     1 
ATOM   772  C  CB    . GLU   A 1 225  ? 49.000  16.962  -52.045 1.00 70.13  ? 374  GLU   A CB    1 
ATOM   773  C  CG    . GLU   A 1 225  ? 49.289  17.654  -53.367 1.00 73.51  ? 374  GLU   A CG    1 
ATOM   774  C  CD    . GLU   A 1 225  ? 49.106  19.167  -53.332 1.00 87.47  ? 374  GLU   A CD    1 
ATOM   775  O  OE1   . GLU   A 1 225  ? 49.162  19.746  -52.210 1.00 96.55  ? 374  GLU   A OE1   1 
ATOM   776  O  OE2   . GLU   A 1 225  ? 48.902  19.775  -54.418 1.00 88.54  ? 374  GLU   A OE2   1 
ATOM   777  N  N     . GLN   A 1 226  ? 47.413  14.982  -50.134 1.00 60.25  ? 375  GLN   A N     1 
ATOM   778  C  CA    . GLN   A 1 226  ? 47.165  14.782  -48.689 1.00 55.13  ? 375  GLN   A CA    1 
ATOM   779  C  C     . GLN   A 1 226  ? 46.843  13.317  -48.361 1.00 56.66  ? 375  GLN   A C     1 
ATOM   780  O  O     . GLN   A 1 226  ? 47.200  12.900  -47.232 1.00 55.65  ? 375  GLN   A O     1 
ATOM   781  C  CB    . GLN   A 1 226  ? 46.040  15.710  -48.215 1.00 57.24  ? 375  GLN   A CB    1 
ATOM   782  C  CG    . GLN   A 1 226  ? 46.431  17.180  -48.083 1.00 60.36  ? 375  GLN   A CG    1 
ATOM   783  C  CD    . GLN   A 1 226  ? 47.721  17.406  -47.317 1.00 65.01  ? 375  GLN   A CD    1 
ATOM   784  O  OE1   . GLN   A 1 226  ? 47.842  17.089  -46.127 1.00 60.18  ? 375  GLN   A OE1   1 
ATOM   785  N  NE2   . GLN   A 1 226  ? 48.715  17.943  -48.010 1.00 52.62  ? 375  GLN   A NE2   1 
ATOM   786  N  N     . ASP   A 1 227  ? 46.151  12.575  -49.239 1.00 56.16  ? 376  ASP   A N     1 
ATOM   787  C  CA    . ASP   A 1 227  ? 45.503  11.287  -48.856 1.00 58.41  ? 376  ASP   A CA    1 
ATOM   788  C  C     . ASP   A 1 227  ? 46.391  10.123  -49.303 1.00 51.42  ? 376  ASP   A C     1 
ATOM   789  O  O     . ASP   A 1 227  ? 46.329  9.774   -50.482 1.00 54.29  ? 376  ASP   A O     1 
ATOM   790  C  CB    . ASP   A 1 227  ? 44.058  11.182  -49.386 1.00 56.88  ? 376  ASP   A CB    1 
ATOM   791  C  CG    . ASP   A 1 227  ? 43.251  10.006  -48.829 1.00 57.48  ? 376  ASP   A CG    1 
ATOM   792  O  OD1   . ASP   A 1 227  ? 43.869  8.995   -48.402 1.00 61.04  ? 376  ASP   A OD1   1 
ATOM   793  O  OD2   . ASP   A 1 227  ? 42.007  10.094  -48.817 1.00 57.47  ? 376  ASP   A OD2   1 
ATOM   794  N  N     . HIS   A 1 228  ? 47.124  9.499   -48.377 1.00 54.84  ? 377  HIS   A N     1 
ATOM   795  C  CA    . HIS   A 1 228  ? 48.035  8.353   -48.662 1.00 63.58  ? 377  HIS   A CA    1 
ATOM   796  C  C     . HIS   A 1 228  ? 47.249  7.105   -49.067 1.00 56.53  ? 377  HIS   A C     1 
ATOM   797  O  O     . HIS   A 1 228  ? 47.756  6.362   -49.934 1.00 62.69  ? 377  HIS   A O     1 
ATOM   798  C  CB    . HIS   A 1 228  ? 48.971  8.028   -47.484 1.00 74.43  ? 377  HIS   A CB    1 
ATOM   799  C  CG    . HIS   A 1 228  ? 50.089  9.004   -47.305 1.00 85.75  ? 377  HIS   A CG    1 
ATOM   800  N  ND1   . HIS   A 1 228  ? 50.610  9.735   -48.359 1.00 93.43  ? 377  HIS   A ND1   1 
ATOM   801  C  CD2   . HIS   A 1 228  ? 50.797  9.361   -46.209 1.00 90.56  ? 377  HIS   A CD2   1 
ATOM   802  C  CE1   . HIS   A 1 228  ? 51.577  10.514  -47.917 1.00 96.95  ? 377  HIS   A CE1   1 
ATOM   803  N  NE2   . HIS   A 1 228  ? 51.711  10.303  -46.599 1.00 96.85  ? 377  HIS   A NE2   1 
ATOM   804  N  N     . ASP   A 1 229  ? 46.095  6.845   -48.449 1.00 55.00  ? 378  ASP   A N     1 
ATOM   805  C  CA    . ASP   A 1 229  ? 45.228  5.691   -48.817 1.00 58.13  ? 378  ASP   A CA    1 
ATOM   806  C  C     . ASP   A 1 229  ? 44.739  5.850   -50.265 1.00 59.08  ? 378  ASP   A C     1 
ATOM   807  O  O     . ASP   A 1 229  ? 44.769  4.835   -51.002 1.00 61.85  ? 378  ASP   A O     1 
ATOM   808  C  CB    . ASP   A 1 229  ? 44.068  5.505   -47.837 1.00 63.66  ? 378  ASP   A CB    1 
ATOM   809  C  CG    . ASP   A 1 229  ? 44.514  5.025   -46.467 1.00 67.59  ? 378  ASP   A CG    1 
ATOM   810  O  OD1   . ASP   A 1 229  ? 45.688  4.630   -46.335 1.00 70.42  ? 378  ASP   A OD1   1 
ATOM   811  O  OD2   . ASP   A 1 229  ? 43.689  5.066   -45.540 1.00 75.46  ? 378  ASP   A OD2   1 
ATOM   812  N  N     . LEU   A 1 230  ? 44.330  7.058   -50.666 1.00 50.77  ? 379  LEU   A N     1 
ATOM   813  C  CA    . LEU   A 1 230  ? 43.885  7.362   -52.053 1.00 51.99  ? 379  LEU   A CA    1 
ATOM   814  C  C     . LEU   A 1 230  ? 45.050  7.163   -53.034 1.00 52.97  ? 379  LEU   A C     1 
ATOM   815  O  O     . LEU   A 1 230  ? 44.812  6.607   -54.123 1.00 59.42  ? 379  LEU   A O     1 
ATOM   816  C  CB    . LEU   A 1 230  ? 43.334  8.788   -52.128 1.00 51.31  ? 379  LEU   A CB    1 
ATOM   817  C  CG    . LEU   A 1 230  ? 42.715  9.166   -53.473 1.00 59.88  ? 379  LEU   A CG    1 
ATOM   818  C  CD1   . LEU   A 1 230  ? 41.709  8.122   -53.936 1.00 57.18  ? 379  LEU   A CD1   1 
ATOM   819  C  CD2   . LEU   A 1 230  ? 42.067  10.542  -53.420 1.00 58.91  ? 379  LEU   A CD2   1 
ATOM   820  N  N     . GLN   A 1 231  ? 46.263  7.590   -52.677 1.00 54.00  ? 380  GLN   A N     1 
ATOM   821  C  CA    . GLN   A 1 231  ? 47.477  7.407   -53.523 1.00 52.81  ? 380  GLN   A CA    1 
ATOM   822  C  C     . GLN   A 1 231  ? 47.667  5.917   -53.825 1.00 48.17  ? 380  GLN   A C     1 
ATOM   823  O  O     . GLN   A 1 231  ? 47.941  5.588   -54.985 1.00 53.49  ? 380  GLN   A O     1 
ATOM   824  C  CB    . GLN   A 1 231  ? 48.722  7.968   -52.835 1.00 58.07  ? 380  GLN   A CB    1 
ATOM   825  C  CG    . GLN   A 1 231  ? 48.945  9.463   -53.040 1.00 61.50  ? 380  GLN   A CG    1 
ATOM   826  C  CD    . GLN   A 1 231  ? 49.997  9.994   -52.090 1.00 68.34  ? 380  GLN   A CD    1 
ATOM   827  O  OE1   . GLN   A 1 231  ? 50.958  9.305   -51.735 1.00 72.85  ? 380  GLN   A OE1   1 
ATOM   828  N  NE2   . GLN   A 1 231  ? 49.818  11.229  -51.648 1.00 66.88  ? 380  GLN   A NE2   1 
ATOM   829  N  N     . ALA   A 1 232  ? 47.506  5.047   -52.826 1.00 46.54  ? 381  ALA   A N     1 
ATOM   830  C  CA    . ALA   A 1 232  ? 47.595  3.574   -52.984 1.00 51.42  ? 381  ALA   A CA    1 
ATOM   831  C  C     . ALA   A 1 232  ? 46.494  3.060   -53.934 1.00 54.27  ? 381  ALA   A C     1 
ATOM   832  O  O     . ALA   A 1 232  ? 46.795  2.176   -54.763 1.00 54.87  ? 381  ALA   A O     1 
ATOM   833  C  CB    . ALA   A 1 232  ? 47.535  2.892   -51.638 1.00 48.77  ? 381  ALA   A CB    1 
ATOM   834  N  N     . ILE   A 1 233  ? 45.271  3.598   -53.835 1.00 55.36  ? 382  ILE   A N     1 
ATOM   835  C  CA    . ILE   A 1 233  ? 44.113  3.223   -54.706 1.00 52.39  ? 382  ILE   A CA    1 
ATOM   836  C  C     . ILE   A 1 233  ? 44.409  3.595   -56.166 1.00 49.66  ? 382  ILE   A C     1 
ATOM   837  O  O     . ILE   A 1 233  ? 44.162  2.741   -57.040 1.00 49.81  ? 382  ILE   A O     1 
ATOM   838  C  CB    . ILE   A 1 233  ? 42.804  3.841   -54.185 1.00 50.00  ? 382  ILE   A CB    1 
ATOM   839  C  CG1   . ILE   A 1 233  ? 42.346  3.107   -52.926 1.00 47.78  ? 382  ILE   A CG1   1 
ATOM   840  C  CG2   . ILE   A 1 233  ? 41.725  3.851   -55.258 1.00 49.84  ? 382  ILE   A CG2   1 
ATOM   841  C  CD1   . ILE   A 1 233  ? 41.407  3.901   -52.067 1.00 49.68  ? 382  ILE   A CD1   1 
ATOM   842  N  N     . LEU   A 1 234  ? 44.933  4.793   -56.422 1.00 50.12  ? 383  LEU   A N     1 
ATOM   843  C  CA    . LEU   A 1 234  ? 45.360  5.228   -57.781 1.00 51.54  ? 383  LEU   A CA    1 
ATOM   844  C  C     . LEU   A 1 234  ? 46.458  4.303   -58.318 1.00 57.63  ? 383  LEU   A C     1 
ATOM   845  O  O     . LEU   A 1 234  ? 46.480  4.078   -59.536 1.00 59.63  ? 383  LEU   A O     1 
ATOM   846  C  CB    . LEU   A 1 234  ? 45.847  6.679   -57.756 1.00 50.84  ? 383  LEU   A CB    1 
ATOM   847  C  CG    . LEU   A 1 234  ? 44.786  7.703   -58.164 1.00 59.08  ? 383  LEU   A CG    1 
ATOM   848  C  CD1   . LEU   A 1 234  ? 43.732  7.839   -57.077 1.00 59.24  ? 383  LEU   A CD1   1 
ATOM   849  C  CD2   . LEU   A 1 234  ? 45.397  9.056   -58.503 1.00 59.46  ? 383  LEU   A CD2   1 
ATOM   850  N  N     . GLN   A 1 235  ? 47.326  3.773   -57.457 1.00 55.74  ? 384  GLN   A N     1 
ATOM   851  C  CA    . GLN   A 1 235  ? 48.431  2.903   -57.915 1.00 54.93  ? 384  GLN   A CA    1 
ATOM   852  C  C     . GLN   A 1 235  ? 47.840  1.599   -58.447 1.00 52.36  ? 384  GLN   A C     1 
ATOM   853  O  O     . GLN   A 1 235  ? 48.292  1.174   -59.535 1.00 48.62  ? 384  GLN   A O     1 
ATOM   854  C  CB    . GLN   A 1 235  ? 49.493  2.737   -56.830 1.00 59.60  ? 384  GLN   A CB    1 
ATOM   855  C  CG    . GLN   A 1 235  ? 50.532  3.843   -56.941 1.00 61.46  ? 384  GLN   A CG    1 
ATOM   856  C  CD    . GLN   A 1 235  ? 51.490  3.905   -55.779 1.00 68.66  ? 384  GLN   A CD    1 
ATOM   857  O  OE1   . GLN   A 1 235  ? 51.128  3.664   -54.620 1.00 61.94  ? 384  GLN   A OE1   1 
ATOM   858  N  NE2   . GLN   A 1 235  ? 52.725  4.262   -56.097 1.00 61.15  ? 384  GLN   A NE2   1 
ATOM   859  N  N     . GLU   A 1 236  ? 46.852  1.019   -57.756 1.00 51.47  ? 385  GLU   A N     1 
ATOM   860  C  CA    . GLU   A 1 236  ? 46.074  -0.147  -58.271 1.00 53.34  ? 385  GLU   A CA    1 
ATOM   861  C  C     . GLU   A 1 236  ? 45.438  0.204   -59.628 1.00 48.06  ? 385  GLU   A C     1 
ATOM   862  O  O     . GLU   A 1 236  ? 45.532  -0.632  -60.549 1.00 48.46  ? 385  GLU   A O     1 
ATOM   863  C  CB    . GLU   A 1 236  ? 44.986  -0.574  -57.291 1.00 59.09  ? 385  GLU   A CB    1 
ATOM   864  C  CG    . GLU   A 1 236  ? 45.472  -1.504  -56.200 1.00 71.83  ? 385  GLU   A CG    1 
ATOM   865  C  CD    . GLU   A 1 236  ? 44.349  -2.297  -55.550 1.00 81.43  ? 385  GLU   A CD    1 
ATOM   866  O  OE1   . GLU   A 1 236  ? 43.544  -2.899  -56.302 1.00 86.33  ? 385  GLU   A OE1   1 
ATOM   867  O  OE2   . GLU   A 1 236  ? 44.265  -2.293  -54.299 1.00 86.20  ? 385  GLU   A OE2   1 
ATOM   868  N  N     . ARG   A 1 237  ? 44.841  1.396   -59.758 1.00 43.06  ? 386  ARG   A N     1 
ATOM   869  C  CA    . ARG   A 1 237  ? 44.158  1.850   -61.000 1.00 48.64  ? 386  ARG   A CA    1 
ATOM   870  C  C     . ARG   A 1 237  ? 45.146  1.789   -62.168 1.00 52.30  ? 386  ARG   A C     1 
ATOM   871  O  O     . ARG   A 1 237  ? 44.740  1.319   -63.268 1.00 53.14  ? 386  ARG   A O     1 
ATOM   872  C  CB    . ARG   A 1 237  ? 43.596  3.275   -60.885 1.00 47.76  ? 386  ARG   A CB    1 
ATOM   873  C  CG    . ARG   A 1 237  ? 42.338  3.406   -60.033 1.00 45.25  ? 386  ARG   A CG    1 
ATOM   874  C  CD    . ARG   A 1 237  ? 41.783  4.818   -60.095 1.00 45.20  ? 386  ARG   A CD    1 
ATOM   875  N  NE    . ARG   A 1 237  ? 41.328  5.138   -61.451 1.00 44.25  ? 386  ARG   A NE    1 
ATOM   876  C  CZ    . ARG   A 1 237  ? 41.328  6.350   -61.998 1.00 44.47  ? 386  ARG   A CZ    1 
ATOM   877  N  NH1   . ARG   A 1 237  ? 41.746  7.403   -61.316 1.00 42.35  ? 386  ARG   A NH1   1 
ATOM   878  N  NH2   . ARG   A 1 237  ? 40.908  6.507   -63.238 1.00 48.32  ? 386  ARG   A NH2   1 
ATOM   879  N  N     . GLU   A 1 238  ? 46.387  2.238   -61.945 1.00 51.83  ? 387  GLU   A N     1 
ATOM   880  C  CA    . GLU   A 1 238  ? 47.365  2.486   -63.037 1.00 51.82  ? 387  GLU   A CA    1 
ATOM   881  C  C     . GLU   A 1 238  ? 47.913  1.140   -63.529 1.00 46.43  ? 387  GLU   A C     1 
ATOM   882  O  O     . GLU   A 1 238  ? 48.540  1.139   -64.568 1.00 51.69  ? 387  GLU   A O     1 
ATOM   883  C  CB    . GLU   A 1 238  ? 48.436  3.476   -62.569 1.00 60.36  ? 387  GLU   A CB    1 
ATOM   884  C  CG    . GLU   A 1 238  ? 47.901  4.886   -62.308 1.00 63.74  ? 387  GLU   A CG    1 
ATOM   885  C  CD    . GLU   A 1 238  ? 48.448  5.646   -61.100 1.00 75.72  ? 387  GLU   A CD    1 
ATOM   886  O  OE1   . GLU   A 1 238  ? 49.433  5.178   -60.463 1.00 76.13  ? 387  GLU   A OE1   1 
ATOM   887  O  OE2   . GLU   A 1 238  ? 47.881  6.720   -60.782 1.00 81.52  ? 387  GLU   A OE2   1 
ATOM   888  N  N     . LEU   A 1 239  ? 47.630  0.029   -62.841 1.00 44.25  ? 388  LEU   A N     1 
ATOM   889  C  CA    . LEU   A 1 239  ? 48.054  -1.335  -63.256 1.00 47.77  ? 388  LEU   A CA    1 
ATOM   890  C  C     . LEU   A 1 239  ? 46.936  -2.113  -63.978 1.00 51.11  ? 388  LEU   A C     1 
ATOM   891  O  O     . LEU   A 1 239  ? 47.220  -3.264  -64.376 1.00 49.57  ? 388  LEU   A O     1 
ATOM   892  C  CB    . LEU   A 1 239  ? 48.515  -2.110  -62.018 1.00 50.81  ? 388  LEU   A CB    1 
ATOM   893  C  CG    . LEU   A 1 239  ? 49.753  -1.551  -61.309 1.00 52.50  ? 388  LEU   A CG    1 
ATOM   894  C  CD1   . LEU   A 1 239  ? 50.222  -2.505  -60.213 1.00 53.67  ? 388  LEU   A CD1   1 
ATOM   895  C  CD2   . LEU   A 1 239  ? 50.876  -1.282  -62.298 1.00 50.39  ? 388  LEU   A CD2   1 
ATOM   896  N  N     . LEU   A 1 240  ? 45.721  -1.558  -64.127 1.00 51.51  ? 389  LEU   A N     1 
ATOM   897  C  CA    . LEU   A 1 240  ? 44.613  -2.212  -64.876 1.00 46.19  ? 389  LEU   A CA    1 
ATOM   898  C  C     . LEU   A 1 240  ? 44.950  -2.173  -66.362 1.00 44.82  ? 389  LEU   A C     1 
ATOM   899  O  O     . LEU   A 1 240  ? 45.481  -1.178  -66.858 1.00 46.61  ? 389  LEU   A O     1 
ATOM   900  C  CB    . LEU   A 1 240  ? 43.276  -1.514  -64.608 1.00 47.47  ? 389  LEU   A CB    1 
ATOM   901  C  CG    . LEU   A 1 240  ? 42.665  -1.776  -63.235 1.00 48.85  ? 389  LEU   A CG    1 
ATOM   902  C  CD1   . LEU   A 1 240  ? 41.448  -0.909  -63.033 1.00 44.02  ? 389  LEU   A CD1   1 
ATOM   903  C  CD2   . LEU   A 1 240  ? 42.321  -3.254  -63.045 1.00 52.16  ? 389  LEU   A CD2   1 
ATOM   904  N  N     . PRO   A 1 241  ? 44.688  -3.273  -67.104 1.00 43.24  ? 390  PRO   A N     1 
ATOM   905  C  CA    . PRO   A 1 241  ? 45.010  -3.342  -68.530 1.00 41.78  ? 390  PRO   A CA    1 
ATOM   906  C  C     . PRO   A 1 241  ? 44.549  -2.143  -69.361 1.00 42.17  ? 390  PRO   A C     1 
ATOM   907  O  O     . PRO   A 1 241  ? 45.213  -1.825  -70.326 1.00 43.58  ? 390  PRO   A O     1 
ATOM   908  C  CB    . PRO   A 1 241  ? 44.278  -4.602  -68.994 1.00 44.34  ? 390  PRO   A CB    1 
ATOM   909  C  CG    . PRO   A 1 241  ? 44.267  -5.503  -67.764 1.00 43.44  ? 390  PRO   A CG    1 
ATOM   910  C  CD    . PRO   A 1 241  ? 44.147  -4.547  -66.589 1.00 44.94  ? 390  PRO   A CD    1 
ATOM   911  N  N     . VAL   A 1 242  ? 43.438  -1.504  -68.994 1.00 42.99  ? 391  VAL   A N     1 
ATOM   912  C  CA    . VAL   A 1 242  ? 42.872  -0.408  -69.832 1.00 45.28  ? 391  VAL   A CA    1 
ATOM   913  C  C     . VAL   A 1 242  ? 43.774  0.827   -69.710 1.00 45.36  ? 391  VAL   A C     1 
ATOM   914  O  O     . VAL   A 1 242  ? 43.657  1.745   -70.563 1.00 45.58  ? 391  VAL   A O     1 
ATOM   915  C  CB    . VAL   A 1 242  ? 41.397  -0.098  -69.504 1.00 45.74  ? 391  VAL   A CB    1 
ATOM   916  C  CG1   . VAL   A 1 242  ? 41.203  0.547   -68.141 1.00 44.26  ? 391  VAL   A CG1   1 
ATOM   917  C  CG2   . VAL   A 1 242  ? 40.788  0.785   -70.583 1.00 45.70  ? 391  VAL   A CG2   1 
ATOM   918  N  N     . LYS   A 1 243  ? 44.633  0.874   -68.688 1.00 48.73  ? 392  LYS   A N     1 
ATOM   919  C  CA    . LYS   A 1 243  ? 45.426  2.091   -68.358 1.00 49.98  ? 392  LYS   A CA    1 
ATOM   920  C  C     . LYS   A 1 243  ? 46.305  2.483   -69.549 1.00 48.51  ? 392  LYS   A C     1 
ATOM   921  O  O     . LYS   A 1 243  ? 46.266  3.660   -69.934 1.00 45.57  ? 392  LYS   A O     1 
ATOM   922  C  CB    . LYS   A 1 243  ? 46.275  1.872   -67.105 1.00 49.70  ? 392  LYS   A CB    1 
ATOM   923  C  CG    . LYS   A 1 243  ? 47.157  3.054   -66.725 1.00 52.67  ? 392  LYS   A CG    1 
ATOM   924  C  CD    . LYS   A 1 243  ? 46.440  4.393   -66.640 1.00 50.37  ? 392  LYS   A CD    1 
ATOM   925  C  CE    . LYS   A 1 243  ? 47.304  5.462   -65.993 1.00 50.07  ? 392  LYS   A CE    1 
ATOM   926  N  NZ    . LYS   A 1 243  ? 46.526  6.674   -65.647 1.00 50.37  ? 392  LYS   A NZ    1 
ATOM   927  N  N     . LYS   A 1 244  ? 47.021  1.517   -70.136 1.00 52.95  ? 393  LYS   A N     1 
ATOM   928  C  CA    . LYS   A 1 244  ? 47.995  1.760   -71.238 1.00 57.80  ? 393  LYS   A CA    1 
ATOM   929  C  C     . LYS   A 1 244  ? 47.298  2.343   -72.480 1.00 56.16  ? 393  LYS   A C     1 
ATOM   930  O  O     . LYS   A 1 244  ? 48.046  2.902   -73.321 1.00 55.90  ? 393  LYS   A O     1 
ATOM   931  C  CB    . LYS   A 1 244  ? 48.813  0.501   -71.559 1.00 64.96  ? 393  LYS   A CB    1 
ATOM   932  C  CG    . LYS   A 1 244  ? 48.059  -0.721  -72.083 1.00 68.80  ? 393  LYS   A CG    1 
ATOM   933  C  CD    . LYS   A 1 244  ? 48.923  -1.974  -72.078 1.00 70.59  ? 393  LYS   A CD    1 
ATOM   934  C  CE    . LYS   A 1 244  ? 48.235  -3.220  -72.601 1.00 74.11  ? 393  LYS   A CE    1 
ATOM   935  N  NZ    . LYS   A 1 244  ? 47.588  -4.005  -71.518 1.00 71.22  ? 393  LYS   A NZ    1 
ATOM   936  N  N     . PHE   A 1 245  ? 45.955  2.267   -72.577 1.00 52.32  ? 394  PHE   A N     1 
ATOM   937  C  CA    . PHE   A 1 245  ? 45.144  2.715   -73.750 1.00 50.97  ? 394  PHE   A CA    1 
ATOM   938  C  C     . PHE   A 1 245  ? 44.451  4.058   -73.485 1.00 48.71  ? 394  PHE   A C     1 
ATOM   939  O  O     . PHE   A 1 245  ? 43.736  4.550   -74.390 1.00 48.67  ? 394  PHE   A O     1 
ATOM   940  C  CB    . PHE   A 1 245  ? 44.082  1.676   -74.133 1.00 48.73  ? 394  PHE   A CB    1 
ATOM   941  C  CG    . PHE   A 1 245  ? 44.607  0.304   -74.478 1.00 45.60  ? 394  PHE   A CG    1 
ATOM   942  C  CD1   . PHE   A 1 245  ? 45.064  0.014   -75.752 1.00 47.28  ? 394  PHE   A CD1   1 
ATOM   943  C  CD2   . PHE   A 1 245  ? 44.640  -0.700  -73.522 1.00 46.19  ? 394  PHE   A CD2   1 
ATOM   944  C  CE1   . PHE   A 1 245  ? 45.538  -1.254  -76.062 1.00 50.80  ? 394  PHE   A CE1   1 
ATOM   945  C  CE2   . PHE   A 1 245  ? 45.112  -1.965  -73.828 1.00 45.89  ? 394  PHE   A CE2   1 
ATOM   946  C  CZ    . PHE   A 1 245  ? 45.559  -2.243  -75.098 1.00 51.24  ? 394  PHE   A CZ    1 
ATOM   947  N  N     . GLU   A 1 246  ? 44.664  4.645   -72.306 1.00 55.60  ? 395  GLU   A N     1 
ATOM   948  C  CA    . GLU   A 1 246  ? 44.006  5.909   -71.858 1.00 59.62  ? 395  GLU   A CA    1 
ATOM   949  C  C     . GLU   A 1 246  ? 44.059  6.944   -72.988 1.00 55.86  ? 395  GLU   A C     1 
ATOM   950  O  O     . GLU   A 1 246  ? 42.996  7.461   -73.357 1.00 58.86  ? 395  GLU   A O     1 
ATOM   951  C  CB    . GLU   A 1 246  ? 44.664  6.406   -70.562 1.00 60.41  ? 395  GLU   A CB    1 
ATOM   952  C  CG    . GLU   A 1 246  ? 44.070  7.689   -69.996 1.00 64.81  ? 395  GLU   A CG    1 
ATOM   953  C  CD    . GLU   A 1 246  ? 44.505  8.039   -68.576 1.00 66.39  ? 395  GLU   A CD    1 
ATOM   954  O  OE1   . GLU   A 1 246  ? 45.503  7.455   -68.093 1.00 67.68  ? 395  GLU   A OE1   1 
ATOM   955  O  OE2   . GLU   A 1 246  ? 43.839  8.893   -67.941 1.00 67.39  ? 395  GLU   A OE2   1 
ATOM   956  N  N     . SER   A 1 247  ? 45.247  7.205   -73.539 1.00 57.94  ? 396  SER   A N     1 
ATOM   957  C  CA    . SER   A 1 247  ? 45.502  8.287   -74.531 1.00 63.70  ? 396  SER   A CA    1 
ATOM   958  C  C     . SER   A 1 247  ? 44.756  7.995   -75.831 1.00 55.97  ? 396  SER   A C     1 
ATOM   959  O  O     . SER   A 1 247  ? 44.138  8.919   -76.384 1.00 52.61  ? 396  SER   A O     1 
ATOM   960  C  CB    . SER   A 1 247  ? 46.978  8.472   -74.802 1.00 68.00  ? 396  SER   A CB    1 
ATOM   961  O  OG    . SER   A 1 247  ? 47.618  9.076   -73.689 1.00 79.52  ? 396  SER   A OG    1 
ATOM   962  N  N     . GLU   A 1 248  ? 44.855  6.760   -76.318 1.00 55.11  ? 397  GLU   A N     1 
ATOM   963  C  CA    . GLU   A 1 248  ? 44.204  6.348   -77.585 1.00 56.36  ? 397  GLU   A CA    1 
ATOM   964  C  C     . GLU   A 1 248  ? 42.685  6.539   -77.447 1.00 56.69  ? 397  GLU   A C     1 
ATOM   965  O  O     . GLU   A 1 248  ? 42.088  7.093   -78.402 1.00 51.49  ? 397  GLU   A O     1 
ATOM   966  C  CB    . GLU   A 1 248  ? 44.585  4.911   -77.931 1.00 57.12  ? 397  GLU   A CB    1 
ATOM   967  C  CG    . GLU   A 1 248  ? 44.151  4.481   -79.321 1.00 56.51  ? 397  GLU   A CG    1 
ATOM   968  C  CD    . GLU   A 1 248  ? 44.230  2.979   -79.516 1.00 61.15  ? 397  GLU   A CD    1 
ATOM   969  O  OE1   . GLU   A 1 248  ? 44.829  2.307   -78.634 1.00 66.22  ? 397  GLU   A OE1   1 
ATOM   970  O  OE2   . GLU   A 1 248  ? 43.697  2.480   -80.539 1.00 63.75  ? 397  GLU   A OE2   1 
ATOM   971  N  N     . ILE   A 1 249  ? 42.098  6.145   -76.298 1.00 55.43  ? 398  ILE   A N     1 
ATOM   972  C  CA    . ILE   A 1 249  ? 40.626  6.244   -76.014 1.00 51.25  ? 398  ILE   A CA    1 
ATOM   973  C  C     . ILE   A 1 249  ? 40.211  7.717   -76.033 1.00 47.69  ? 398  ILE   A C     1 
ATOM   974  O  O     . ILE   A 1 249  ? 39.238  8.029   -76.716 1.00 50.76  ? 398  ILE   A O     1 
ATOM   975  C  CB    . ILE   A 1 249  ? 40.242  5.572   -74.679 1.00 48.71  ? 398  ILE   A CB    1 
ATOM   976  C  CG1   . ILE   A 1 249  ? 40.411  4.050   -74.739 1.00 50.09  ? 398  ILE   A CG1   1 
ATOM   977  C  CG2   . ILE   A 1 249  ? 38.833  5.964   -74.266 1.00 48.00  ? 398  ILE   A CG2   1 
ATOM   978  C  CD1   . ILE   A 1 249  ? 40.616  3.384   -73.386 1.00 48.97  ? 398  ILE   A CD1   1 
ATOM   979  N  N     . LEU   A 1 250  ? 40.933  8.583   -75.321 1.00 49.66  ? 399  LEU   A N     1 
ATOM   980  C  CA    . LEU   A 1 250  ? 40.565  10.017  -75.167 1.00 53.56  ? 399  LEU   A CA    1 
ATOM   981  C  C     . LEU   A 1 250  ? 40.681  10.736  -76.504 1.00 54.56  ? 399  LEU   A C     1 
ATOM   982  O  O     . LEU   A 1 250  ? 39.907  11.681  -76.702 1.00 49.04  ? 399  LEU   A O     1 
ATOM   983  C  CB    . LEU   A 1 250  ? 41.466  10.690  -74.132 1.00 52.81  ? 399  LEU   A CB    1 
ATOM   984  C  CG    . LEU   A 1 250  ? 41.242  10.221  -72.697 1.00 53.12  ? 399  LEU   A CG    1 
ATOM   985  C  CD1   . LEU   A 1 250  ? 42.235  10.880  -71.741 1.00 50.84  ? 399  LEU   A CD1   1 
ATOM   986  C  CD2   . LEU   A 1 250  ? 39.809  10.496  -72.273 1.00 48.58  ? 399  LEU   A CD2   1 
ATOM   987  N  N     . GLU   A 1 251  ? 41.619  10.310  -77.361 1.00 57.08  ? 400  GLU   A N     1 
ATOM   988  C  CA    . GLU   A 1 251  ? 41.860  10.930  -78.691 1.00 61.07  ? 400  GLU   A CA    1 
ATOM   989  C  C     . GLU   A 1 251  ? 40.720  10.500  -79.618 1.00 55.83  ? 400  GLU   A C     1 
ATOM   990  O  O     . GLU   A 1 251  ? 40.172  11.366  -80.330 1.00 43.93  ? 400  GLU   A O     1 
ATOM   991  C  CB    . GLU   A 1 251  ? 43.227  10.520  -79.247 1.00 73.27  ? 400  GLU   A CB    1 
ATOM   992  C  CG    . GLU   A 1 251  ? 43.561  11.162  -80.590 1.00 84.64  ? 400  GLU   A CG    1 
ATOM   993  C  CD    . GLU   A 1 251  ? 44.729  10.534  -81.345 1.00 97.86  ? 400  GLU   A CD    1 
ATOM   994  O  OE1   . GLU   A 1 251  ? 45.117  9.389   -81.009 1.00 100.63 ? 400  GLU   A OE1   1 
ATOM   995  O  OE2   . GLU   A 1 251  ? 45.252  11.191  -82.276 1.00 100.67 ? 400  GLU   A OE2   1 
ATOM   996  N  N     . ALA   A 1 252  ? 40.388  9.204   -79.604 1.00 53.78  ? 401  ALA   A N     1 
ATOM   997  C  CA    . ALA   A 1 252  ? 39.234  8.627   -80.334 1.00 56.95  ? 401  ALA   A CA    1 
ATOM   998  C  C     . ALA   A 1 252  ? 37.937  9.367   -79.937 1.00 56.93  ? 401  ALA   A C     1 
ATOM   999  O  O     . ALA   A 1 252  ? 37.229  9.806   -80.858 1.00 60.60  ? 401  ALA   A O     1 
ATOM   1000 C  CB    . ALA   A 1 252  ? 39.160  7.136   -80.095 1.00 56.49  ? 401  ALA   A CB    1 
ATOM   1001 N  N     . ILE   A 1 253  ? 37.646  9.572   -78.643 1.00 50.08  ? 402  ILE   A N     1 
ATOM   1002 C  CA    . ILE   A 1 253  ? 36.369  10.231  -78.211 1.00 53.38  ? 402  ILE   A CA    1 
ATOM   1003 C  C     . ILE   A 1 253  ? 36.346  11.685  -78.698 1.00 56.04  ? 402  ILE   A C     1 
ATOM   1004 O  O     . ILE   A 1 253  ? 35.290  12.124  -79.205 1.00 55.14  ? 402  ILE   A O     1 
ATOM   1005 C  CB    . ILE   A 1 253  ? 36.144  10.178  -76.685 1.00 49.82  ? 402  ILE   A CB    1 
ATOM   1006 C  CG1   . ILE   A 1 253  ? 35.926  8.758   -76.166 1.00 50.92  ? 402  ILE   A CG1   1 
ATOM   1007 C  CG2   . ILE   A 1 253  ? 34.997  11.089  -76.292 1.00 47.93  ? 402  ILE   A CG2   1 
ATOM   1008 C  CD1   . ILE   A 1 253  ? 35.945  8.653   -74.658 1.00 53.74  ? 402  ILE   A CD1   1 
ATOM   1009 N  N     . SER   A 1 254  ? 37.441  12.425  -78.522 1.00 56.08  ? 403  SER   A N     1 
ATOM   1010 C  CA    . SER   A 1 254  ? 37.518  13.862  -78.900 1.00 60.58  ? 403  SER   A CA    1 
ATOM   1011 C  C     . SER   A 1 254  ? 37.278  14.045  -80.403 1.00 54.92  ? 403  SER   A C     1 
ATOM   1012 O  O     . SER   A 1 254  ? 36.694  15.080  -80.763 1.00 49.75  ? 403  SER   A O     1 
ATOM   1013 C  CB    . SER   A 1 254  ? 38.827  14.468  -78.496 1.00 61.86  ? 403  SER   A CB    1 
ATOM   1014 O  OG    . SER   A 1 254  ? 39.890  13.697  -79.020 1.00 74.06  ? 403  SER   A OG    1 
ATOM   1015 N  N     . GLN   A 1 255  ? 37.678  13.073  -81.233 1.00 55.79  ? 404  GLN   A N     1 
ATOM   1016 C  CA    A GLN   A 1 255  ? 37.670  13.173  -82.722 0.50 60.23  ? 404  GLN   A CA    1 
ATOM   1017 C  CA    B GLN   A 1 255  ? 37.651  13.208  -82.717 0.50 58.01  ? 404  GLN   A CA    1 
ATOM   1018 C  C     . GLN   A 1 255  ? 36.367  12.606  -83.312 1.00 61.96  ? 404  GLN   A C     1 
ATOM   1019 O  O     . GLN   A 1 255  ? 36.054  12.950  -84.471 1.00 62.56  ? 404  GLN   A O     1 
ATOM   1020 C  CB    A GLN   A 1 255  ? 38.859  12.413  -83.320 0.50 63.86  ? 404  GLN   A CB    1 
ATOM   1021 C  CB    B GLN   A 1 255  ? 38.900  12.566  -83.322 0.50 58.51  ? 404  GLN   A CB    1 
ATOM   1022 C  CG    A GLN   A 1 255  ? 40.211  13.076  -83.078 0.50 68.02  ? 404  GLN   A CG    1 
ATOM   1023 C  CG    B GLN   A 1 255  ? 40.166  13.374  -83.069 0.50 59.50  ? 404  GLN   A CG    1 
ATOM   1024 C  CD    A GLN   A 1 255  ? 41.368  12.180  -83.452 0.50 70.52  ? 404  GLN   A CD    1 
ATOM   1025 C  CD    B GLN   A 1 255  ? 40.052  14.774  -83.620 0.50 58.56  ? 404  GLN   A CD    1 
ATOM   1026 O  OE1   A GLN   A 1 255  ? 41.201  10.986  -83.699 0.50 72.16  ? 404  GLN   A OE1   1 
ATOM   1027 O  OE1   B GLN   A 1 255  ? 39.948  14.975  -84.829 0.50 59.01  ? 404  GLN   A OE1   1 
ATOM   1028 N  NE2   A GLN   A 1 255  ? 42.561  12.752  -83.485 0.50 70.34  ? 404  GLN   A NE2   1 
ATOM   1029 N  NE2   B GLN   A 1 255  ? 40.059  15.754  -82.731 0.50 54.35  ? 404  GLN   A NE2   1 
ATOM   1030 N  N     . ASN   A 1 256  ? 35.637  11.772  -82.560 1.00 58.14  ? 405  ASN   A N     1 
ATOM   1031 C  CA    . ASN   A 1 256  ? 34.466  11.029  -83.102 1.00 57.06  ? 405  ASN   A CA    1 
ATOM   1032 C  C     . ASN   A 1 256  ? 33.215  11.142  -82.209 1.00 56.00  ? 405  ASN   A C     1 
ATOM   1033 O  O     . ASN   A 1 256  ? 33.309  10.926  -80.972 1.00 50.60  ? 405  ASN   A O     1 
ATOM   1034 C  CB    . ASN   A 1 256  ? 34.861  9.576   -83.332 1.00 58.88  ? 405  ASN   A CB    1 
ATOM   1035 C  CG    . ASN   A 1 256  ? 35.986  9.457   -84.337 1.00 57.69  ? 405  ASN   A CG    1 
ATOM   1036 O  OD1   . ASN   A 1 256  ? 35.746  9.531   -85.537 1.00 60.62  ? 405  ASN   A OD1   1 
ATOM   1037 N  ND2   . ASN   A 1 256  ? 37.205  9.275   -83.854 1.00 52.43  ? 405  ASN   A ND2   1 
ATOM   1038 N  N     . SER   A 1 257  ? 32.063  11.406  -82.839 1.00 49.96  ? 406  SER   A N     1 
ATOM   1039 C  CA    . SER   A 1 257  ? 30.716  11.415  -82.212 1.00 47.24  ? 406  SER   A CA    1 
ATOM   1040 C  C     . SER   A 1 257  ? 30.441  10.075  -81.515 1.00 48.42  ? 406  SER   A C     1 
ATOM   1041 O  O     . SER   A 1 257  ? 29.917  10.071  -80.378 1.00 52.45  ? 406  SER   A O     1 
ATOM   1042 C  CB    . SER   A 1 257  ? 29.681  11.729  -83.237 1.00 47.30  ? 406  SER   A CB    1 
ATOM   1043 O  OG    . SER   A 1 257  ? 29.852  13.059  -83.708 1.00 50.46  ? 406  SER   A OG    1 
ATOM   1044 N  N     . VAL   A 1 258  ? 30.825  8.971   -82.151 1.00 41.35  ? 407  VAL   A N     1 
ATOM   1045 C  CA    . VAL   A 1 258  ? 30.573  7.609   -81.628 1.00 40.22  ? 407  VAL   A CA    1 
ATOM   1046 C  C     . VAL   A 1 258  ? 31.876  6.824   -81.701 1.00 40.78  ? 407  VAL   A C     1 
ATOM   1047 O  O     . VAL   A 1 258  ? 32.533  6.904   -82.741 1.00 43.86  ? 407  VAL   A O     1 
ATOM   1048 C  CB    . VAL   A 1 258  ? 29.458  6.889   -82.413 1.00 44.63  ? 407  VAL   A CB    1 
ATOM   1049 C  CG1   . VAL   A 1 258  ? 29.019  5.627   -81.695 1.00 45.18  ? 407  VAL   A CG1   1 
ATOM   1050 C  CG2   . VAL   A 1 258  ? 28.256  7.778   -82.708 1.00 45.50  ? 407  VAL   A CG2   1 
ATOM   1051 N  N     . ILE   A 1 259  ? 32.180  6.042   -80.664 1.00 41.14  ? 408  ILE   A N     1 
ATOM   1052 C  CA    . ILE   A 1 259  ? 33.247  4.999   -80.701 1.00 46.91  ? 408  ILE   A CA    1 
ATOM   1053 C  C     . ILE   A 1 259  ? 32.741  3.761   -79.962 1.00 47.60  ? 408  ILE   A C     1 
ATOM   1054 O  O     . ILE   A 1 259  ? 31.826  3.862   -79.110 1.00 46.30  ? 408  ILE   A O     1 
ATOM   1055 C  CB    . ILE   A 1 259  ? 34.599  5.479   -80.115 1.00 47.61  ? 408  ILE   A CB    1 
ATOM   1056 C  CG1   . ILE   A 1 259  ? 34.571  5.640   -78.593 1.00 52.46  ? 408  ILE   A CG1   1 
ATOM   1057 C  CG2   . ILE   A 1 259  ? 35.065  6.761   -80.792 1.00 48.56  ? 408  ILE   A CG2   1 
ATOM   1058 C  CD1   . ILE   A 1 259  ? 35.814  5.119   -77.910 1.00 56.22  ? 408  ILE   A CD1   1 
ATOM   1059 N  N     . ILE   A 1 260  ? 33.385  2.642   -80.246 1.00 43.52  ? 409  ILE   A N     1 
ATOM   1060 C  CA    . ILE   A 1 260  ? 33.199  1.375   -79.504 1.00 43.51  ? 409  ILE   A CA    1 
ATOM   1061 C  C     . ILE   A 1 260  ? 34.529  1.085   -78.816 1.00 43.13  ? 409  ILE   A C     1 
ATOM   1062 O  O     . ILE   A 1 260  ? 35.575  1.272   -79.457 1.00 51.57  ? 409  ILE   A O     1 
ATOM   1063 C  CB    . ILE   A 1 260  ? 32.761  0.251   -80.461 1.00 45.28  ? 409  ILE   A CB    1 
ATOM   1064 C  CG1   . ILE   A 1 260  ? 31.437  0.601   -81.145 1.00 49.17  ? 409  ILE   A CG1   1 
ATOM   1065 C  CG2   . ILE   A 1 260  ? 32.708  -1.089  -79.740 1.00 42.91  ? 409  ILE   A CG2   1 
ATOM   1066 C  CD1   . ILE   A 1 260  ? 31.077  -0.310  -82.299 1.00 52.18  ? 409  ILE   A CD1   1 
ATOM   1067 N  N     . ILE   A 1 261  ? 34.483  0.680   -77.552 1.00 39.59  ? 410  ILE   A N     1 
ATOM   1068 C  CA    . ILE   A 1 261  ? 35.667  0.174   -76.831 1.00 40.51  ? 410  ILE   A CA    1 
ATOM   1069 C  C     . ILE   A 1 261  ? 35.427  -1.314  -76.640 1.00 43.52  ? 410  ILE   A C     1 
ATOM   1070 O  O     . ILE   A 1 261  ? 34.415  -1.686  -75.990 1.00 46.42  ? 410  ILE   A O     1 
ATOM   1071 C  CB    . ILE   A 1 261  ? 35.905  0.930   -75.511 1.00 41.54  ? 410  ILE   A CB    1 
ATOM   1072 C  CG1   . ILE   A 1 261  ? 36.163  2.418   -75.746 1.00 44.54  ? 410  ILE   A CG1   1 
ATOM   1073 C  CG2   . ILE   A 1 261  ? 37.031  0.276   -74.725 1.00 41.96  ? 410  ILE   A CG2   1 
ATOM   1074 C  CD1   . ILE   A 1 261  ? 36.180  3.249   -74.468 1.00 48.12  ? 410  ILE   A CD1   1 
ATOM   1075 N  N     . ARG   A 1 262  ? 36.309  -2.130  -77.208 1.00 42.60  ? 411  ARG   A N     1 
ATOM   1076 C  CA    . ARG   A 1 262  ? 36.158  -3.599  -77.184 1.00 43.85  ? 411  ARG   A CA    1 
ATOM   1077 C  C     . ARG   A 1 262  ? 37.314  -4.209  -76.390 1.00 42.19  ? 411  ARG   A C     1 
ATOM   1078 O  O     . ARG   A 1 262  ? 38.448  -3.860  -76.655 1.00 47.87  ? 411  ARG   A O     1 
ATOM   1079 C  CB    . ARG   A 1 262  ? 36.104  -4.084  -78.629 1.00 44.60  ? 411  ARG   A CB    1 
ATOM   1080 C  CG    . ARG   A 1 262  ? 35.847  -5.574  -78.787 1.00 48.83  ? 411  ARG   A CG    1 
ATOM   1081 C  CD    . ARG   A 1 262  ? 35.736  -5.889  -80.274 1.00 51.90  ? 411  ARG   A CD    1 
ATOM   1082 N  NE    . ARG   A 1 262  ? 35.675  -7.325  -80.479 1.00 57.68  ? 411  ARG   A NE    1 
ATOM   1083 C  CZ    . ARG   A 1 262  ? 36.723  -8.143  -80.509 1.00 63.56  ? 411  ARG   A CZ    1 
ATOM   1084 N  NH1   . ARG   A 1 262  ? 36.532  -9.440  -80.690 1.00 62.59  ? 411  ARG   A NH1   1 
ATOM   1085 N  NH2   . ARG   A 1 262  ? 37.950  -7.671  -80.352 1.00 63.52  ? 411  ARG   A NH2   1 
ATOM   1086 N  N     . GLY   A 1 263  ? 37.026  -5.091  -75.443 1.00 41.22  ? 412  GLY   A N     1 
ATOM   1087 C  CA    . GLY   A 1 263  ? 38.059  -5.908  -74.802 1.00 41.19  ? 412  GLY   A CA    1 
ATOM   1088 C  C     . GLY   A 1 263  ? 37.507  -6.847  -73.764 1.00 44.10  ? 412  GLY   A C     1 
ATOM   1089 O  O     . GLY   A 1 263  ? 36.322  -6.712  -73.406 1.00 48.75  ? 412  GLY   A O     1 
ATOM   1090 N  N     . ALA   A 1 264  ? 38.369  -7.739  -73.269 1.00 49.25  ? 413  ALA   A N     1 
ATOM   1091 C  CA    . ALA   A 1 264  ? 37.999  -8.827  -72.338 1.00 52.31  ? 413  ALA   A CA    1 
ATOM   1092 C  C     . ALA   A 1 264  ? 37.390  -8.227  -71.067 1.00 50.19  ? 413  ALA   A C     1 
ATOM   1093 O  O     . ALA   A 1 264  ? 37.706  -7.089  -70.720 1.00 49.13  ? 413  ALA   A O     1 
ATOM   1094 C  CB    . ALA   A 1 264  ? 39.198  -9.687  -72.028 1.00 53.61  ? 413  ALA   A CB    1 
ATOM   1095 N  N     . THR   A 1 265  ? 36.506  -8.978  -70.430 1.00 52.56  ? 414  THR   A N     1 
ATOM   1096 C  CA    . THR   A 1 265  ? 35.965  -8.676  -69.089 1.00 56.47  ? 414  THR   A CA    1 
ATOM   1097 C  C     . THR   A 1 265  ? 37.137  -8.659  -68.099 1.00 55.77  ? 414  THR   A C     1 
ATOM   1098 O  O     . THR   A 1 265  ? 37.945  -9.618  -68.113 1.00 58.37  ? 414  THR   A O     1 
ATOM   1099 C  CB    . THR   A 1 265  ? 34.852  -9.678  -68.775 1.00 56.18  ? 414  THR   A CB    1 
ATOM   1100 O  OG1   . THR   A 1 265  ? 33.901  -9.443  -69.814 1.00 55.38  ? 414  THR   A OG1   1 
ATOM   1101 C  CG2   . THR   A 1 265  ? 34.269  -9.520  -67.388 1.00 55.54  ? 414  THR   A CG2   1 
ATOM   1102 N  N     . GLY   A 1 266  ? 37.243  -7.580  -67.319 1.00 52.93  ? 415  GLY   A N     1 
ATOM   1103 C  CA    . GLY   A 1 266  ? 38.253  -7.394  -66.260 1.00 48.85  ? 415  GLY   A CA    1 
ATOM   1104 C  C     . GLY   A 1 266  ? 39.338  -6.393  -66.633 1.00 50.22  ? 415  GLY   A C     1 
ATOM   1105 O  O     . GLY   A 1 266  ? 40.206  -6.165  -65.777 1.00 59.08  ? 415  GLY   A O     1 
ATOM   1106 N  N     . CYS   A 1 267  ? 39.318  -5.814  -67.841 1.00 46.17  ? 416  CYS   A N     1 
ATOM   1107 C  CA    . CYS   A 1 267  ? 40.341  -4.841  -68.315 1.00 47.68  ? 416  CYS   A CA    1 
ATOM   1108 C  C     . CYS   A 1 267  ? 40.184  -3.483  -67.622 1.00 47.91  ? 416  CYS   A C     1 
ATOM   1109 O  O     . CYS   A 1 267  ? 41.185  -2.747  -67.562 1.00 45.84  ? 416  CYS   A O     1 
ATOM   1110 C  CB    . CYS   A 1 267  ? 40.283  -4.627  -69.823 1.00 51.03  ? 416  CYS   A CB    1 
ATOM   1111 S  SG    . CYS   A 1 267  ? 40.920  -6.041  -70.764 1.00 66.88  ? 416  CYS   A SG    1 
ATOM   1112 N  N     . GLY   A 1 268  ? 38.970  -3.132  -67.184 1.00 45.24  ? 417  GLY   A N     1 
ATOM   1113 C  CA    . GLY   A 1 268  ? 38.684  -1.837  -66.536 1.00 42.59  ? 417  GLY   A CA    1 
ATOM   1114 C  C     . GLY   A 1 268  ? 37.873  -0.883  -67.390 1.00 41.01  ? 417  GLY   A C     1 
ATOM   1115 O  O     . GLY   A 1 268  ? 37.928  0.315   -67.111 1.00 41.08  ? 417  GLY   A O     1 
ATOM   1116 N  N     . LYS   A 1 269  ? 37.103  -1.366  -68.370 1.00 44.98  ? 418  LYS   A N     1 
ATOM   1117 C  CA    . LYS   A 1 269  ? 36.276  -0.484  -69.237 1.00 43.22  ? 418  LYS   A CA    1 
ATOM   1118 C  C     . LYS   A 1 269  ? 35.287  0.297   -68.361 1.00 40.28  ? 418  LYS   A C     1 
ATOM   1119 O  O     . LYS   A 1 269  ? 35.215  1.528   -68.478 1.00 37.89  ? 418  LYS   A O     1 
ATOM   1120 C  CB    . LYS   A 1 269  ? 35.568  -1.312  -70.313 1.00 45.22  ? 418  LYS   A CB    1 
ATOM   1121 C  CG    . LYS   A 1 269  ? 36.512  -1.969  -71.315 1.00 45.89  ? 418  LYS   A CG    1 
ATOM   1122 C  CD    . LYS   A 1 269  ? 35.834  -2.663  -72.490 1.00 43.38  ? 418  LYS   A CD    1 
ATOM   1123 C  CE    . LYS   A 1 269  ? 34.831  -3.715  -72.068 1.00 41.30  ? 418  LYS   A CE    1 
ATOM   1124 N  NZ    . LYS   A 1 269  ? 35.442  -4.737  -71.190 1.00 43.36  ? 418  LYS   A NZ    1 
ATOM   1125 N  N     . THR   A 1 270  ? 34.546  -0.397  -67.504 1.00 43.82  ? 419  THR   A N     1 
ATOM   1126 C  CA    . THR   A 1 270  ? 33.376  0.161   -66.772 1.00 44.77  ? 419  THR   A CA    1 
ATOM   1127 C  C     . THR   A 1 270  ? 33.836  1.155   -65.698 1.00 43.47  ? 419  THR   A C     1 
ATOM   1128 O  O     . THR   A 1 270  ? 33.313  2.285   -65.667 1.00 45.37  ? 419  THR   A O     1 
ATOM   1129 C  CB    . THR   A 1 270  ? 32.549  -0.961  -66.135 1.00 43.36  ? 419  THR   A CB    1 
ATOM   1130 O  OG1   . THR   A 1 270  ? 32.014  -1.766  -67.187 1.00 40.82  ? 419  THR   A OG1   1 
ATOM   1131 C  CG2   . THR   A 1 270  ? 31.445  -0.422  -65.253 1.00 44.89  ? 419  THR   A CG2   1 
ATOM   1132 N  N     . THR   A 1 271  ? 34.766  0.743   -64.835 1.00 40.36  ? 420  THR   A N     1 
ATOM   1133 C  CA    . THR   A 1 271  ? 35.231  1.571   -63.693 1.00 43.53  ? 420  THR   A CA    1 
ATOM   1134 C  C     . THR   A 1 271  ? 36.162  2.684   -64.178 1.00 41.54  ? 420  THR   A C     1 
ATOM   1135 O  O     . THR   A 1 271  ? 36.020  3.782   -63.659 1.00 43.97  ? 420  THR   A O     1 
ATOM   1136 C  CB    . THR   A 1 271  ? 35.828  0.713   -62.576 1.00 44.11  ? 420  THR   A CB    1 
ATOM   1137 O  OG1   . THR   A 1 271  ? 36.902  -0.065  -63.096 1.00 44.98  ? 420  THR   A OG1   1 
ATOM   1138 C  CG2   . THR   A 1 271  ? 34.785  -0.194  -61.963 1.00 42.58  ? 420  THR   A CG2   1 
ATOM   1139 N  N     . GLN   A 1 272  ? 37.012  2.462   -65.177 1.00 40.27  ? 421  GLN   A N     1 
ATOM   1140 C  CA    . GLN   A 1 272  ? 38.092  3.432   -65.518 1.00 42.02  ? 421  GLN   A CA    1 
ATOM   1141 C  C     . GLN   A 1 272  ? 37.641  4.458   -66.575 1.00 42.47  ? 421  GLN   A C     1 
ATOM   1142 O  O     . GLN   A 1 272  ? 37.932  5.634   -66.387 1.00 48.69  ? 421  GLN   A O     1 
ATOM   1143 C  CB    . GLN   A 1 272  ? 39.343  2.661   -65.950 1.00 42.51  ? 421  GLN   A CB    1 
ATOM   1144 C  CG    . GLN   A 1 272  ? 39.791  1.645   -64.908 1.00 40.18  ? 421  GLN   A CG    1 
ATOM   1145 C  CD    . GLN   A 1 272  ? 39.938  2.333   -63.570 1.00 42.49  ? 421  GLN   A CD    1 
ATOM   1146 O  OE1   . GLN   A 1 272  ? 40.739  3.259   -63.395 1.00 43.56  ? 421  GLN   A OE1   1 
ATOM   1147 N  NE2   . GLN   A 1 272  ? 39.126  1.916   -62.619 1.00 43.38  ? 421  GLN   A NE2   1 
ATOM   1148 N  N     . VAL   A 1 273  ? 36.977  4.062   -67.662 1.00 39.93  ? 422  VAL   A N     1 
ATOM   1149 C  CA    . VAL   A 1 273  ? 36.787  4.956   -68.848 1.00 39.46  ? 422  VAL   A CA    1 
ATOM   1150 C  C     . VAL   A 1 273  ? 36.043  6.240   -68.484 1.00 39.88  ? 422  VAL   A C     1 
ATOM   1151 O  O     . VAL   A 1 273  ? 36.387  7.290   -68.999 1.00 40.42  ? 422  VAL   A O     1 
ATOM   1152 C  CB    . VAL   A 1 273  ? 36.098  4.234   -70.020 1.00 39.70  ? 422  VAL   A CB    1 
ATOM   1153 C  CG1   . VAL   A 1 273  ? 35.683  5.222   -71.107 1.00 38.63  ? 422  VAL   A CG1   1 
ATOM   1154 C  CG2   . VAL   A 1 273  ? 37.002  3.148   -70.594 1.00 39.69  ? 422  VAL   A CG2   1 
ATOM   1155 N  N     . PRO   A 1 274  ? 34.939  6.221   -67.702 1.00 39.21  ? 423  PRO   A N     1 
ATOM   1156 C  CA    . PRO   A 1 274  ? 34.282  7.460   -67.299 1.00 41.20  ? 423  PRO   A CA    1 
ATOM   1157 C  C     . PRO   A 1 274  ? 35.185  8.407   -66.480 1.00 42.83  ? 423  PRO   A C     1 
ATOM   1158 O  O     . PRO   A 1 274  ? 35.058  9.598   -66.647 1.00 44.64  ? 423  PRO   A O     1 
ATOM   1159 C  CB    . PRO   A 1 274  ? 33.103  6.997   -66.423 1.00 40.42  ? 423  PRO   A CB    1 
ATOM   1160 C  CG    . PRO   A 1 274  ? 32.906  5.537   -66.739 1.00 39.55  ? 423  PRO   A CG    1 
ATOM   1161 C  CD    . PRO   A 1 274  ? 34.242  5.027   -67.211 1.00 39.94  ? 423  PRO   A CD    1 
ATOM   1162 N  N     . GLN   A 1 275  ? 36.023  7.862   -65.587 1.00 41.96  ? 424  GLN   A N     1 
ATOM   1163 C  CA    . GLN   A 1 275  ? 37.055  8.612   -64.809 1.00 41.26  ? 424  GLN   A CA    1 
ATOM   1164 C  C     . GLN   A 1 275  ? 38.096  9.207   -65.760 1.00 40.85  ? 424  GLN   A C     1 
ATOM   1165 O  O     . GLN   A 1 275  ? 38.432  10.374  -65.564 1.00 38.83  ? 424  GLN   A O     1 
ATOM   1166 C  CB    . GLN   A 1 275  ? 37.776  7.719   -63.797 1.00 41.74  ? 424  GLN   A CB    1 
ATOM   1167 C  CG    . GLN   A 1 275  ? 36.860  7.172   -62.724 1.00 43.04  ? 424  GLN   A CG    1 
ATOM   1168 C  CD    . GLN   A 1 275  ? 37.658  6.549   -61.608 1.00 45.49  ? 424  GLN   A CD    1 
ATOM   1169 O  OE1   . GLN   A 1 275  ? 38.281  7.248   -60.816 1.00 43.43  ? 424  GLN   A OE1   1 
ATOM   1170 N  NE2   . GLN   A 1 275  ? 37.618  5.227   -61.516 1.00 44.88  ? 424  GLN   A NE2   1 
ATOM   1171 N  N     . PHE   A 1 276  ? 38.569  8.457   -66.765 1.00 41.88  ? 425  PHE   A N     1 
ATOM   1172 C  CA    . PHE   A 1 276  ? 39.553  8.983   -67.747 1.00 44.78  ? 425  PHE   A CA    1 
ATOM   1173 C  C     . PHE   A 1 276  ? 39.022  10.257  -68.381 1.00 46.67  ? 425  PHE   A C     1 
ATOM   1174 O  O     . PHE   A 1 276  ? 39.777  11.228  -68.485 1.00 55.83  ? 425  PHE   A O     1 
ATOM   1175 C  CB    . PHE   A 1 276  ? 39.897  7.996   -68.858 1.00 42.19  ? 425  PHE   A CB    1 
ATOM   1176 C  CG    . PHE   A 1 276  ? 40.735  6.837   -68.394 1.00 42.34  ? 425  PHE   A CG    1 
ATOM   1177 C  CD1   . PHE   A 1 276  ? 41.358  6.856   -67.161 1.00 41.64  ? 425  PHE   A CD1   1 
ATOM   1178 C  CD2   . PHE   A 1 276  ? 40.883  5.714   -69.189 1.00 46.04  ? 425  PHE   A CD2   1 
ATOM   1179 C  CE1   . PHE   A 1 276  ? 42.094  5.767   -66.723 1.00 46.33  ? 425  PHE   A CE1   1 
ATOM   1180 C  CE2   . PHE   A 1 276  ? 41.626  4.629   -68.754 1.00 46.67  ? 425  PHE   A CE2   1 
ATOM   1181 C  CZ    . PHE   A 1 276  ? 42.238  4.661   -67.526 1.00 46.42  ? 425  PHE   A CZ    1 
ATOM   1182 N  N     . ILE   A 1 277  ? 37.762  10.234  -68.799 1.00 50.68  ? 426  ILE   A N     1 
ATOM   1183 C  CA    . ILE   A 1 277  ? 37.120  11.374  -69.507 1.00 46.81  ? 426  ILE   A CA    1 
ATOM   1184 C  C     . ILE   A 1 277  ? 36.998  12.538  -68.523 1.00 48.29  ? 426  ILE   A C     1 
ATOM   1185 O  O     . ILE   A 1 277  ? 37.330  13.663  -68.902 1.00 47.41  ? 426  ILE   A O     1 
ATOM   1186 C  CB    . ILE   A 1 277  ? 35.760  10.957  -70.082 1.00 44.49  ? 426  ILE   A CB    1 
ATOM   1187 C  CG1   . ILE   A 1 277  ? 35.912  9.875   -71.150 1.00 45.40  ? 426  ILE   A CG1   1 
ATOM   1188 C  CG2   . ILE   A 1 277  ? 35.001  12.165  -70.606 1.00 46.11  ? 426  ILE   A CG2   1 
ATOM   1189 C  CD1   . ILE   A 1 277  ? 34.623  9.141   -71.447 1.00 47.57  ? 426  ILE   A CD1   1 
ATOM   1190 N  N     . LEU   A 1 278  ? 36.514  12.270  -67.312 1.00 48.26  ? 427  LEU   A N     1 
ATOM   1191 C  CA    . LEU   A 1 278  ? 36.241  13.325  -66.303 1.00 51.73  ? 427  LEU   A CA    1 
ATOM   1192 C  C     . LEU   A 1 278  ? 37.571  13.990  -65.921 1.00 51.80  ? 427  LEU   A C     1 
ATOM   1193 O  O     . LEU   A 1 278  ? 37.663  15.228  -66.019 1.00 49.21  ? 427  LEU   A O     1 
ATOM   1194 C  CB    . LEU   A 1 278  ? 35.550  12.698  -65.090 1.00 45.64  ? 427  LEU   A CB    1 
ATOM   1195 C  CG    . LEU   A 1 278  ? 35.302  13.641  -63.917 1.00 44.94  ? 427  LEU   A CG    1 
ATOM   1196 C  CD1   . LEU   A 1 278  ? 34.518  14.870  -64.345 1.00 43.62  ? 427  LEU   A CD1   1 
ATOM   1197 C  CD2   . LEU   A 1 278  ? 34.589  12.919  -62.783 1.00 46.82  ? 427  LEU   A CD2   1 
ATOM   1198 N  N     . ASP   A 1 279  ? 38.565  13.178  -65.561 1.00 46.16  ? 428  ASP   A N     1 
ATOM   1199 C  CA    . ASP   A 1 279  ? 39.932  13.630  -65.186 1.00 47.89  ? 428  ASP   A CA    1 
ATOM   1200 C  C     . ASP   A 1 279  ? 40.588  14.351  -66.374 1.00 53.43  ? 428  ASP   A C     1 
ATOM   1201 O  O     . ASP   A 1 279  ? 41.219  15.382  -66.127 1.00 48.64  ? 428  ASP   A O     1 
ATOM   1202 C  CB    . ASP   A 1 279  ? 40.775  12.475  -64.650 1.00 43.59  ? 428  ASP   A CB    1 
ATOM   1203 C  CG    . ASP   A 1 279  ? 40.306  12.014  -63.280 1.00 51.27  ? 428  ASP   A CG    1 
ATOM   1204 O  OD1   . ASP   A 1 279  ? 39.726  12.854  -62.542 1.00 55.85  ? 428  ASP   A OD1   1 
ATOM   1205 O  OD2   . ASP   A 1 279  ? 40.507  10.816  -62.957 1.00 52.46  ? 428  ASP   A OD2   1 
ATOM   1206 N  N     . ASP   A 1 280  ? 40.402  13.894  -67.617 1.00 54.85  ? 429  ASP   A N     1 
ATOM   1207 C  CA    . ASP   A 1 280  ? 40.887  14.657  -68.801 1.00 57.00  ? 429  ASP   A CA    1 
ATOM   1208 C  C     . ASP   A 1 280  ? 40.338  16.096  -68.764 1.00 51.93  ? 429  ASP   A C     1 
ATOM   1209 O  O     . ASP   A 1 280  ? 41.124  17.020  -68.979 1.00 55.92  ? 429  ASP   A O     1 
ATOM   1210 C  CB    . ASP   A 1 280  ? 40.554  13.974  -70.124 1.00 59.00  ? 429  ASP   A CB    1 
ATOM   1211 C  CG    . ASP   A 1 280  ? 41.180  14.661  -71.324 1.00 58.20  ? 429  ASP   A CG    1 
ATOM   1212 O  OD1   . ASP   A 1 280  ? 42.422  14.700  -71.385 1.00 57.26  ? 429  ASP   A OD1   1 
ATOM   1213 O  OD2   . ASP   A 1 280  ? 40.417  15.154  -72.180 1.00 63.46  ? 429  ASP   A OD2   1 
ATOM   1214 N  N     . PHE   A 1 281  ? 39.053  16.299  -68.484 1.00 49.83  ? 430  PHE   A N     1 
ATOM   1215 C  CA    . PHE   A 1 281  ? 38.423  17.649  -68.464 1.00 50.46  ? 430  PHE   A CA    1 
ATOM   1216 C  C     . PHE   A 1 281  ? 38.924  18.444  -67.242 1.00 54.39  ? 430  PHE   A C     1 
ATOM   1217 O  O     . PHE   A 1 281  ? 39.170  19.650  -67.369 1.00 55.83  ? 430  PHE   A O     1 
ATOM   1218 C  CB    . PHE   A 1 281  ? 36.893  17.548  -68.510 1.00 51.15  ? 430  PHE   A CB    1 
ATOM   1219 C  CG    . PHE   A 1 281  ? 36.299  17.431  -69.895 1.00 49.08  ? 430  PHE   A CG    1 
ATOM   1220 C  CD1   . PHE   A 1 281  ? 36.303  16.220  -70.578 1.00 51.49  ? 430  PHE   A CD1   1 
ATOM   1221 C  CD2   . PHE   A 1 281  ? 35.744  18.535  -70.526 1.00 48.64  ? 430  PHE   A CD2   1 
ATOM   1222 C  CE1   . PHE   A 1 281  ? 35.781  16.122  -71.864 1.00 51.34  ? 430  PHE   A CE1   1 
ATOM   1223 C  CE2   . PHE   A 1 281  ? 35.226  18.439  -71.812 1.00 50.87  ? 430  PHE   A CE2   1 
ATOM   1224 C  CZ    . PHE   A 1 281  ? 35.230  17.228  -72.475 1.00 49.14  ? 430  PHE   A CZ    1 
ATOM   1225 N  N     . ILE   A 1 282  ? 39.069  17.796  -66.086 1.00 57.41  ? 431  ILE   A N     1 
ATOM   1226 C  CA    . ILE   A 1 282  ? 39.502  18.454  -64.817 1.00 62.14  ? 431  ILE   A CA    1 
ATOM   1227 C  C     . ILE   A 1 282  ? 40.951  18.937  -64.981 1.00 63.96  ? 431  ILE   A C     1 
ATOM   1228 O  O     . ILE   A 1 282  ? 41.220  20.099  -64.657 1.00 57.96  ? 431  ILE   A O     1 
ATOM   1229 C  CB    . ILE   A 1 282  ? 39.337  17.523  -63.599 1.00 56.95  ? 431  ILE   A CB    1 
ATOM   1230 C  CG1   . ILE   A 1 282  ? 37.861  17.215  -63.323 1.00 58.24  ? 431  ILE   A CG1   1 
ATOM   1231 C  CG2   . ILE   A 1 282  ? 40.014  18.131  -62.381 1.00 57.41  ? 431  ILE   A CG2   1 
ATOM   1232 C  CD1   . ILE   A 1 282  ? 37.624  16.020  -62.429 1.00 56.52  ? 431  ILE   A CD1   1 
ATOM   1233 N  N     . GLN   A 1 283  ? 41.838  18.083  -65.492 1.00 67.46  ? 432  GLN   A N     1 
ATOM   1234 C  CA    . GLN   A 1 283  ? 43.295  18.358  -65.574 1.00 68.55  ? 432  GLN   A CA    1 
ATOM   1235 C  C     . GLN   A 1 283  ? 43.590  19.342  -66.709 1.00 67.87  ? 432  GLN   A C     1 
ATOM   1236 O  O     . GLN   A 1 283  ? 44.683  19.909  -66.676 1.00 75.69  ? 432  GLN   A O     1 
ATOM   1237 C  CB    . GLN   A 1 283  ? 44.091  17.058  -65.720 1.00 76.69  ? 432  GLN   A CB    1 
ATOM   1238 C  CG    . GLN   A 1 283  ? 44.160  16.241  -64.431 1.00 86.56  ? 432  GLN   A CG    1 
ATOM   1239 C  CD    . GLN   A 1 283  ? 44.680  17.045  -63.261 1.00 90.64  ? 432  GLN   A CD    1 
ATOM   1240 O  OE1   . GLN   A 1 283  ? 45.672  17.767  -63.369 1.00 100.30 ? 432  GLN   A OE1   1 
ATOM   1241 N  NE2   . GLN   A 1 283  ? 43.999  16.943  -62.130 1.00 87.70  ? 432  GLN   A NE2   1 
ATOM   1242 N  N     . ASN   A 1 284  ? 42.651  19.570  -67.637 1.00 65.75  ? 433  ASN   A N     1 
ATOM   1243 C  CA    . ASN   A 1 284  ? 42.796  20.545  -68.753 1.00 58.50  ? 433  ASN   A CA    1 
ATOM   1244 C  C     . ASN   A 1 284  ? 41.927  21.788  -68.506 1.00 54.68  ? 433  ASN   A C     1 
ATOM   1245 O  O     . ASN   A 1 284  ? 41.670  22.526  -69.487 1.00 50.97  ? 433  ASN   A O     1 
ATOM   1246 C  CB    . ASN   A 1 284  ? 42.492  19.895  -70.106 1.00 65.39  ? 433  ASN   A CB    1 
ATOM   1247 C  CG    . ASN   A 1 284  ? 43.631  19.035  -70.618 1.00 73.96  ? 433  ASN   A CG    1 
ATOM   1248 O  OD1   . ASN   A 1 284  ? 44.426  19.476  -71.449 1.00 83.46  ? 433  ASN   A OD1   1 
ATOM   1249 N  ND2   . ASN   A 1 284  ? 43.728  17.809  -70.129 1.00 71.77  ? 433  ASN   A ND2   1 
ATOM   1250 N  N     . ASP   A 1 285  ? 41.481  22.017  -67.260 1.00 57.83  ? 434  ASP   A N     1 
ATOM   1251 C  CA    . ASP   A 1 285  ? 40.804  23.269  -66.813 1.00 62.14  ? 434  ASP   A CA    1 
ATOM   1252 C  C     . ASP   A 1 285  ? 39.425  23.423  -67.471 1.00 66.73  ? 434  ASP   A C     1 
ATOM   1253 O  O     . ASP   A 1 285  ? 38.995  24.577  -67.672 1.00 63.09  ? 434  ASP   A O     1 
ATOM   1254 C  CB    . ASP   A 1 285  ? 41.658  24.508  -67.128 1.00 72.98  ? 434  ASP   A CB    1 
ATOM   1255 C  CG    . ASP   A 1 285  ? 43.132  24.396  -66.751 1.00 73.87  ? 434  ASP   A CG    1 
ATOM   1256 O  OD1   . ASP   A 1 285  ? 43.434  24.305  -65.536 1.00 72.30  ? 434  ASP   A OD1   1 
ATOM   1257 O  OD2   . ASP   A 1 285  ? 43.973  24.387  -67.681 1.00 80.89  ? 434  ASP   A OD2   1 
ATOM   1258 N  N     . ARG   A 1 286  ? 38.744  22.315  -67.785 1.00 71.14  ? 435  ARG   A N     1 
ATOM   1259 C  CA    . ARG   A 1 286  ? 37.404  22.323  -68.436 1.00 70.04  ? 435  ARG   A CA    1 
ATOM   1260 C  C     . ARG   A 1 286  ? 36.412  21.487  -67.604 1.00 57.30  ? 435  ARG   A C     1 
ATOM   1261 O  O     . ARG   A 1 286  ? 35.366  21.110  -68.146 1.00 52.11  ? 435  ARG   A O     1 
ATOM   1262 C  CB    . ARG   A 1 286  ? 37.518  21.825  -69.886 1.00 79.30  ? 435  ARG   A CB    1 
ATOM   1263 C  CG    . ARG   A 1 286  ? 38.429  22.645  -70.799 1.00 89.29  ? 435  ARG   A CG    1 
ATOM   1264 C  CD    . ARG   A 1 286  ? 38.468  22.170  -72.259 1.00 99.93  ? 435  ARG   A CD    1 
ATOM   1265 N  NE    . ARG   A 1 286  ? 38.338  20.712  -72.434 1.00 111.19 ? 435  ARG   A NE    1 
ATOM   1266 C  CZ    . ARG   A 1 286  ? 39.301  19.854  -72.803 1.00 104.26 ? 435  ARG   A CZ    1 
ATOM   1267 N  NH1   . ARG   A 1 286  ? 40.526  20.274  -73.078 1.00 110.21 ? 435  ARG   A NH1   1 
ATOM   1268 N  NH2   . ARG   A 1 286  ? 39.031  18.560  -72.890 1.00 94.74  ? 435  ARG   A NH2   1 
ATOM   1269 N  N     . ALA   A 1 287  ? 36.684  21.256  -66.317 1.00 54.08  ? 436  ALA   A N     1 
ATOM   1270 C  CA    . ALA   A 1 287  ? 35.808  20.495  -65.384 1.00 53.20  ? 436  ALA   A CA    1 
ATOM   1271 C  C     . ALA   A 1 287  ? 34.334  20.808  -65.650 1.00 49.73  ? 436  ALA   A C     1 
ATOM   1272 O  O     . ALA   A 1 287  ? 33.544  19.849  -65.707 1.00 54.47  ? 436  ALA   A O     1 
ATOM   1273 C  CB    . ALA   A 1 287  ? 36.137  20.769  -63.935 1.00 51.86  ? 436  ALA   A CB    1 
ATOM   1274 N  N     . ALA   A 1 288  ? 33.975  22.078  -65.833 1.00 46.82  ? 437  ALA   A N     1 
ATOM   1275 C  CA    . ALA   A 1 288  ? 32.564  22.534  -65.927 1.00 48.65  ? 437  ALA   A CA    1 
ATOM   1276 C  C     . ALA   A 1 288  ? 31.877  22.017  -67.206 1.00 49.04  ? 437  ALA   A C     1 
ATOM   1277 O  O     . ALA   A 1 288  ? 30.619  22.011  -67.227 1.00 50.42  ? 437  ALA   A O     1 
ATOM   1278 C  CB    . ALA   A 1 288  ? 32.501  24.036  -65.848 1.00 43.24  ? 437  ALA   A CB    1 
ATOM   1279 N  N     . GLU   A 1 289  ? 32.659  21.611  -68.214 1.00 52.38  ? 438  GLU   A N     1 
ATOM   1280 C  CA    . GLU   A 1 289  ? 32.193  21.198  -69.573 1.00 56.25  ? 438  GLU   A CA    1 
ATOM   1281 C  C     . GLU   A 1 289  ? 31.878  19.690  -69.631 1.00 51.41  ? 438  GLU   A C     1 
ATOM   1282 O  O     . GLU   A 1 289  ? 31.563  19.199  -70.749 1.00 56.27  ? 438  GLU   A O     1 
ATOM   1283 C  CB    . GLU   A 1 289  ? 33.262  21.538  -70.620 1.00 60.76  ? 438  GLU   A CB    1 
ATOM   1284 C  CG    . GLU   A 1 289  ? 33.339  23.018  -70.984 1.00 66.52  ? 438  GLU   A CG    1 
ATOM   1285 C  CD    . GLU   A 1 289  ? 34.492  23.380  -71.916 1.00 76.07  ? 438  GLU   A CD    1 
ATOM   1286 O  OE1   . GLU   A 1 289  ? 34.760  22.615  -72.877 1.00 72.94  ? 438  GLU   A OE1   1 
ATOM   1287 O  OE2   . GLU   A 1 289  ? 35.146  24.417  -71.669 1.00 86.05  ? 438  GLU   A OE2   1 
ATOM   1288 N  N     . CYS   A 1 290  ? 31.925  18.984  -68.493 1.00 46.78  ? 439  CYS   A N     1 
ATOM   1289 C  CA    . CYS   A 1 290  ? 31.846  17.499  -68.402 1.00 46.85  ? 439  CYS   A CA    1 
ATOM   1290 C  C     . CYS   A 1 290  ? 30.689  17.074  -67.489 1.00 49.41  ? 439  CYS   A C     1 
ATOM   1291 O  O     . CYS   A 1 290  ? 30.700  17.424  -66.307 1.00 51.25  ? 439  CYS   A O     1 
ATOM   1292 C  CB    . CYS   A 1 290  ? 33.147  16.911  -67.885 1.00 45.70  ? 439  CYS   A CB    1 
ATOM   1293 S  SG    . CYS   A 1 290  ? 33.283  15.118  -68.097 1.00 48.29  ? 439  CYS   A SG    1 
ATOM   1294 N  N     . ASN   A 1 291  ? 29.713  16.361  -68.056 1.00 50.70  ? 440  ASN   A N     1 
ATOM   1295 C  CA    . ASN   A 1 291  ? 28.684  15.580  -67.324 1.00 45.92  ? 440  ASN   A CA    1 
ATOM   1296 C  C     . ASN   A 1 291  ? 28.462  14.280  -68.099 1.00 44.38  ? 440  ASN   A C     1 
ATOM   1297 O  O     . ASN   A 1 291  ? 28.175  14.343  -69.292 1.00 46.48  ? 440  ASN   A O     1 
ATOM   1298 C  CB    . ASN   A 1 291  ? 27.390  16.366  -67.146 1.00 45.55  ? 440  ASN   A CB    1 
ATOM   1299 C  CG    . ASN   A 1 291  ? 27.499  17.579  -66.239 1.00 42.56  ? 440  ASN   A CG    1 
ATOM   1300 O  OD1   . ASN   A 1 291  ? 27.408  18.705  -66.710 1.00 51.87  ? 440  ASN   A OD1   1 
ATOM   1301 N  ND2   . ASN   A 1 291  ? 27.605  17.370  -64.935 1.00 40.46  ? 440  ASN   A ND2   1 
ATOM   1302 N  N     . ILE   A 1 292  ? 28.653  13.137  -67.452 1.00 43.76  ? 441  ILE   A N     1 
ATOM   1303 C  CA    . ILE   A 1 292  ? 28.634  11.812  -68.124 1.00 39.25  ? 441  ILE   A CA    1 
ATOM   1304 C  C     . ILE   A 1 292  ? 27.447  11.014  -67.579 1.00 40.61  ? 441  ILE   A C     1 
ATOM   1305 O  O     . ILE   A 1 292  ? 27.275  10.951  -66.343 1.00 41.89  ? 441  ILE   A O     1 
ATOM   1306 C  CB    . ILE   A 1 292  ? 29.973  11.078  -67.924 1.00 38.48  ? 441  ILE   A CB    1 
ATOM   1307 C  CG1   . ILE   A 1 292  ? 31.191  11.982  -68.157 1.00 38.63  ? 441  ILE   A CG1   1 
ATOM   1308 C  CG2   . ILE   A 1 292  ? 30.010  9.836   -68.793 1.00 37.54  ? 441  ILE   A CG2   1 
ATOM   1309 C  CD1   . ILE   A 1 292  ? 32.545  11.301  -67.953 1.00 39.53  ? 441  ILE   A CD1   1 
ATOM   1310 N  N     . VAL   A 1 293  ? 26.649  10.455  -68.486 1.00 42.06  ? 442  VAL   A N     1 
ATOM   1311 C  CA    . VAL   A 1 293  ? 25.637  9.397   -68.213 1.00 35.44  ? 442  VAL   A CA    1 
ATOM   1312 C  C     . VAL   A 1 293  ? 26.268  8.058   -68.595 1.00 34.30  ? 442  VAL   A C     1 
ATOM   1313 O  O     . VAL   A 1 293  ? 26.772  7.946   -69.701 1.00 36.72  ? 442  VAL   A O     1 
ATOM   1314 C  CB    . VAL   A 1 293  ? 24.356  9.662   -69.013 1.00 39.37  ? 442  VAL   A CB    1 
ATOM   1315 C  CG1   . VAL   A 1 293  ? 23.336  8.556   -68.813 1.00 43.10  ? 442  VAL   A CG1   1 
ATOM   1316 C  CG2   . VAL   A 1 293  ? 23.763  11.022  -68.683 1.00 41.44  ? 442  VAL   A CG2   1 
ATOM   1317 N  N     . VAL   A 1 294  ? 26.288  7.100   -67.681 1.00 33.34  ? 443  VAL   A N     1 
ATOM   1318 C  CA    . VAL   A 1 294  ? 26.714  5.704   -67.937 1.00 36.87  ? 443  VAL   A CA    1 
ATOM   1319 C  C     . VAL   A 1 294  ? 25.480  4.821   -67.727 1.00 38.65  ? 443  VAL   A C     1 
ATOM   1320 O  O     . VAL   A 1 294  ? 24.996  4.741   -66.564 1.00 39.43  ? 443  VAL   A O     1 
ATOM   1321 C  CB    . VAL   A 1 294  ? 27.865  5.253   -67.017 1.00 39.64  ? 443  VAL   A CB    1 
ATOM   1322 C  CG1   . VAL   A 1 294  ? 28.462  3.941   -67.494 1.00 38.47  ? 443  VAL   A CG1   1 
ATOM   1323 C  CG2   . VAL   A 1 294  ? 28.947  6.311   -66.873 1.00 41.10  ? 443  VAL   A CG2   1 
ATOM   1324 N  N     . THR   A 1 295  ? 25.029  4.137   -68.780 1.00 36.49  ? 444  THR   A N     1 
ATOM   1325 C  CA    . THR   A 1 295  ? 23.894  3.184   -68.693 1.00 36.99  ? 444  THR   A CA    1 
ATOM   1326 C  C     . THR   A 1 295  ? 24.445  1.791   -68.379 1.00 40.61  ? 444  THR   A C     1 
ATOM   1327 O  O     . THR   A 1 295  ? 25.519  1.414   -68.910 1.00 43.20  ? 444  THR   A O     1 
ATOM   1328 C  CB    . THR   A 1 295  ? 23.016  3.245   -69.947 1.00 35.09  ? 444  THR   A CB    1 
ATOM   1329 O  OG1   . THR   A 1 295  ? 23.698  2.565   -70.997 1.00 36.18  ? 444  THR   A OG1   1 
ATOM   1330 C  CG2   . THR   A 1 295  ? 22.680  4.663   -70.355 1.00 34.11  ? 444  THR   A CG2   1 
ATOM   1331 N  N     . GLN   A 1 296  ? 23.763  1.076   -67.489 1.00 38.42  ? 445  GLN   A N     1 
ATOM   1332 C  CA    . GLN   A 1 296  ? 24.048  -0.345  -67.193 1.00 41.47  ? 445  GLN   A CA    1 
ATOM   1333 C  C     . GLN   A 1 296  ? 22.767  -1.109  -67.491 1.00 39.77  ? 445  GLN   A C     1 
ATOM   1334 O  O     . GLN   A 1 296  ? 21.686  -0.589  -67.312 1.00 37.74  ? 445  GLN   A O     1 
ATOM   1335 C  CB    . GLN   A 1 296  ? 24.482  -0.540  -65.734 1.00 41.92  ? 445  GLN   A CB    1 
ATOM   1336 C  CG    . GLN   A 1 296  ? 25.749  0.209   -65.346 1.00 43.62  ? 445  GLN   A CG    1 
ATOM   1337 C  CD    . GLN   A 1 296  ? 26.969  -0.340  -66.045 1.00 47.10  ? 445  GLN   A CD    1 
ATOM   1338 O  OE1   . GLN   A 1 296  ? 27.125  -1.540  -66.225 1.00 52.74  ? 445  GLN   A OE1   1 
ATOM   1339 N  NE2   . GLN   A 1 296  ? 27.855  0.542   -66.469 1.00 52.33  ? 445  GLN   A NE2   1 
ATOM   1340 N  N     . PRO   A 1 297  ? 22.826  -2.370  -67.936 1.00 45.09  ? 446  PRO   A N     1 
ATOM   1341 C  CA    . PRO   A 1 297  ? 21.613  -3.138  -68.152 1.00 45.01  ? 446  PRO   A CA    1 
ATOM   1342 C  C     . PRO   A 1 297  ? 20.963  -3.644  -66.859 1.00 47.04  ? 446  PRO   A C     1 
ATOM   1343 O  O     . PRO   A 1 297  ? 19.854  -4.083  -66.971 1.00 55.28  ? 446  PRO   A O     1 
ATOM   1344 C  CB    . PRO   A 1 297  ? 22.080  -4.337  -68.989 1.00 47.29  ? 446  PRO   A CB    1 
ATOM   1345 C  CG    . PRO   A 1 297  ? 23.491  -4.003  -69.405 1.00 51.78  ? 446  PRO   A CG    1 
ATOM   1346 C  CD    . PRO   A 1 297  ? 24.035  -3.113  -68.308 1.00 51.28  ? 446  PRO   A CD    1 
ATOM   1347 N  N     . ARG   A 1 298  ? 21.650  -3.593  -65.712 1.00 47.89  ? 447  ARG   A N     1 
ATOM   1348 C  CA    . ARG   A 1 298  ? 21.154  -4.163  -64.427 1.00 55.32  ? 447  ARG   A CA    1 
ATOM   1349 C  C     . ARG   A 1 298  ? 21.177  -3.107  -63.315 1.00 50.34  ? 447  ARG   A C     1 
ATOM   1350 O  O     . ARG   A 1 298  ? 22.186  -2.412  -63.200 1.00 43.73  ? 447  ARG   A O     1 
ATOM   1351 C  CB    . ARG   A 1 298  ? 22.019  -5.340  -63.962 1.00 61.08  ? 447  ARG   A CB    1 
ATOM   1352 C  CG    . ARG   A 1 298  ? 22.094  -6.517  -64.925 1.00 66.71  ? 447  ARG   A CG    1 
ATOM   1353 C  CD    . ARG   A 1 298  ? 23.355  -7.327  -64.665 1.00 70.32  ? 447  ARG   A CD    1 
ATOM   1354 N  NE    . ARG   A 1 298  ? 23.708  -8.288  -65.703 1.00 72.49  ? 447  ARG   A NE    1 
ATOM   1355 C  CZ    . ARG   A 1 298  ? 23.359  -9.579  -65.708 1.00 74.76  ? 447  ARG   A CZ    1 
ATOM   1356 N  NH1   . ARG   A 1 298  ? 23.752  -10.362 -66.699 1.00 72.95  ? 447  ARG   A NH1   1 
ATOM   1357 N  NH2   . ARG   A 1 298  ? 22.631  -10.093 -64.729 1.00 74.93  ? 447  ARG   A NH2   1 
ATOM   1358 N  N     . ARG   A 1 299  ? 20.113  -3.060  -62.499 1.00 50.38  ? 448  ARG   A N     1 
ATOM   1359 C  CA    . ARG   A 1 299  ? 20.004  -2.275  -61.239 1.00 46.72  ? 448  ARG   A CA    1 
ATOM   1360 C  C     . ARG   A 1 299  ? 21.265  -2.470  -60.389 1.00 43.93  ? 448  ARG   A C     1 
ATOM   1361 O  O     . ARG   A 1 299  ? 21.837  -1.475  -59.965 1.00 39.75  ? 448  ARG   A O     1 
ATOM   1362 C  CB    . ARG   A 1 299  ? 18.783  -2.711  -60.422 1.00 47.20  ? 448  ARG   A CB    1 
ATOM   1363 C  CG    . ARG   A 1 299  ? 18.569  -1.915  -59.141 1.00 51.93  ? 448  ARG   A CG    1 
ATOM   1364 C  CD    . ARG   A 1 299  ? 17.558  -2.519  -58.177 1.00 57.45  ? 448  ARG   A CD    1 
ATOM   1365 N  NE    . ARG   A 1 299  ? 17.173  -1.547  -57.155 1.00 63.17  ? 448  ARG   A NE    1 
ATOM   1366 C  CZ    . ARG   A 1 299  ? 17.901  -1.215  -56.077 1.00 67.11  ? 448  ARG   A CZ    1 
ATOM   1367 N  NH1   . ARG   A 1 299  ? 19.080  -1.780  -55.843 1.00 60.59  ? 448  ARG   A NH1   1 
ATOM   1368 N  NH2   . ARG   A 1 299  ? 17.440  -0.305  -55.232 1.00 67.68  ? 448  ARG   A NH2   1 
ATOM   1369 N  N     . ILE   A 1 300  ? 21.646  -3.715  -60.126 1.00 42.50  ? 449  ILE   A N     1 
ATOM   1370 C  CA    . ILE   A 1 300  ? 22.778  -4.065  -59.221 1.00 47.43  ? 449  ILE   A CA    1 
ATOM   1371 C  C     . ILE   A 1 300  ? 24.082  -3.477  -59.782 1.00 47.87  ? 449  ILE   A C     1 
ATOM   1372 O  O     . ILE   A 1 300  ? 24.939  -3.069  -58.985 1.00 50.60  ? 449  ILE   A O     1 
ATOM   1373 C  CB    . ILE   A 1 300  ? 22.876  -5.592  -58.980 1.00 48.81  ? 449  ILE   A CB    1 
ATOM   1374 C  CG1   . ILE   A 1 300  ? 23.918  -5.945  -57.921 1.00 50.84  ? 449  ILE   A CG1   1 
ATOM   1375 C  CG2   . ILE   A 1 300  ? 23.171  -6.337  -60.269 1.00 54.37  ? 449  ILE   A CG2   1 
ATOM   1376 C  CD1   . ILE   A 1 300  ? 23.902  -5.029  -56.717 1.00 60.40  ? 449  ILE   A CD1   1 
ATOM   1377 N  N     . SER   A 1 301  ? 24.244  -3.422  -61.099 1.00 46.62  ? 450  SER   A N     1 
ATOM   1378 C  CA    . SER   A 1 301  ? 25.493  -2.921  -61.727 1.00 48.26  ? 450  SER   A CA    1 
ATOM   1379 C  C     . SER   A 1 301  ? 25.567  -1.393  -61.599 1.00 47.29  ? 450  SER   A C     1 
ATOM   1380 O  O     . SER   A 1 301  ? 26.668  -0.871  -61.417 1.00 49.90  ? 450  SER   A O     1 
ATOM   1381 C  CB    . SER   A 1 301  ? 25.613  -3.380  -63.153 1.00 49.82  ? 450  SER   A CB    1 
ATOM   1382 O  OG    . SER   A 1 301  ? 25.899  -4.766  -63.201 1.00 62.18  ? 450  SER   A OG    1 
ATOM   1383 N  N     . ALA   A 1 302  ? 24.445  -0.688  -61.691 1.00 43.32  ? 451  ALA   A N     1 
ATOM   1384 C  CA    . ALA   A 1 302  ? 24.428  0.792   -61.647 1.00 40.92  ? 451  ALA   A CA    1 
ATOM   1385 C  C     . ALA   A 1 302  ? 24.848  1.229   -60.258 1.00 39.65  ? 451  ALA   A C     1 
ATOM   1386 O  O     . ALA   A 1 302  ? 25.654  2.159   -60.140 1.00 40.67  ? 451  ALA   A O     1 
ATOM   1387 C  CB    . ALA   A 1 302  ? 23.063  1.334   -61.973 1.00 42.95  ? 451  ALA   A CB    1 
ATOM   1388 N  N     . VAL   A 1 303  ? 24.294  0.577   -59.247 1.00 39.91  ? 452  VAL   A N     1 
ATOM   1389 C  CA    . VAL   A 1 303  ? 24.537  0.905   -57.818 1.00 43.77  ? 452  VAL   A CA    1 
ATOM   1390 C  C     . VAL   A 1 303  ? 26.006  0.575   -57.475 1.00 42.36  ? 452  VAL   A C     1 
ATOM   1391 O  O     . VAL   A 1 303  ? 26.748  1.490   -57.093 1.00 46.69  ? 452  VAL   A O     1 
ATOM   1392 C  CB    . VAL   A 1 303  ? 23.530  0.139   -56.944 1.00 47.28  ? 452  VAL   A CB    1 
ATOM   1393 C  CG1   . VAL   A 1 303  ? 23.864  0.277   -55.475 1.00 48.44  ? 452  VAL   A CG1   1 
ATOM   1394 C  CG2   . VAL   A 1 303  ? 22.100  0.576   -57.225 1.00 50.36  ? 452  VAL   A CG2   1 
ATOM   1395 N  N     . SER   A 1 304  ? 26.391  -0.690  -57.612 1.00 43.12  ? 453  SER   A N     1 
ATOM   1396 C  CA    . SER   A 1 304  ? 27.745  -1.261  -57.369 1.00 45.65  ? 453  SER   A CA    1 
ATOM   1397 C  C     . SER   A 1 304  ? 28.832  -0.444  -58.065 1.00 45.34  ? 453  SER   A C     1 
ATOM   1398 O  O     . SER   A 1 304  ? 29.881  -0.209  -57.441 1.00 41.14  ? 453  SER   A O     1 
ATOM   1399 C  CB    . SER   A 1 304  ? 27.823  -2.676  -57.864 1.00 44.99  ? 453  SER   A CB    1 
ATOM   1400 O  OG    . SER   A 1 304  ? 27.041  -3.509  -57.037 1.00 62.81  ? 453  SER   A OG    1 
ATOM   1401 N  N     . VAL   A 1 305  ? 28.631  -0.092  -59.336 1.00 41.64  ? 454  VAL   A N     1 
ATOM   1402 C  CA    . VAL   A 1 305  ? 29.685  0.631   -60.101 1.00 43.99  ? 454  VAL   A CA    1 
ATOM   1403 C  C     . VAL   A 1 305  ? 29.840  2.038   -59.515 1.00 41.17  ? 454  VAL   A C     1 
ATOM   1404 O  O     . VAL   A 1 305  ? 30.989  2.509   -59.385 1.00 45.82  ? 454  VAL   A O     1 
ATOM   1405 C  CB    . VAL   A 1 305  ? 29.424  0.636   -61.617 1.00 42.52  ? 454  VAL   A CB    1 
ATOM   1406 C  CG1   . VAL   A 1 305  ? 30.374  1.581   -62.338 1.00 38.27  ? 454  VAL   A CG1   1 
ATOM   1407 C  CG2   . VAL   A 1 305  ? 29.530  -0.782  -62.180 1.00 43.59  ? 454  VAL   A CG2   1 
ATOM   1408 N  N     . ALA   A 1 306  ? 28.736  2.678   -59.159 1.00 39.65  ? 455  ALA   A N     1 
ATOM   1409 C  CA    . ALA   A 1 306  ? 28.736  4.031   -58.567 1.00 42.82  ? 455  ALA   A CA    1 
ATOM   1410 C  C     . ALA   A 1 306  ? 29.450  3.969   -57.208 1.00 38.42  ? 455  ALA   A C     1 
ATOM   1411 O  O     . ALA   A 1 306  ? 30.259  4.838   -56.939 1.00 39.13  ? 455  ALA   A O     1 
ATOM   1412 C  CB    . ALA   A 1 306  ? 27.323  4.560   -58.464 1.00 42.56  ? 455  ALA   A CB    1 
ATOM   1413 N  N     . GLU   A 1 307  ? 29.215  2.935   -56.414 1.00 40.33  ? 456  GLU   A N     1 
ATOM   1414 C  CA    . GLU   A 1 307  ? 29.893  2.760   -55.099 1.00 41.85  ? 456  GLU   A CA    1 
ATOM   1415 C  C     . GLU   A 1 307  ? 31.389  2.530   -55.339 1.00 46.68  ? 456  GLU   A C     1 
ATOM   1416 O  O     . GLU   A 1 307  ? 32.196  3.150   -54.629 1.00 53.93  ? 456  GLU   A O     1 
ATOM   1417 C  CB    . GLU   A 1 307  ? 29.236  1.637   -54.294 1.00 44.91  ? 456  GLU   A CB    1 
ATOM   1418 C  CG    . GLU   A 1 307  ? 27.955  2.094   -53.607 1.00 48.72  ? 456  GLU   A CG    1 
ATOM   1419 C  CD    . GLU   A 1 307  ? 27.054  1.012   -53.037 1.00 57.02  ? 456  GLU   A CD    1 
ATOM   1420 O  OE1   . GLU   A 1 307  ? 27.384  -0.190  -53.178 1.00 58.28  ? 456  GLU   A OE1   1 
ATOM   1421 O  OE2   . GLU   A 1 307  ? 26.017  1.382   -52.437 1.00 64.69  ? 456  GLU   A OE2   1 
ATOM   1422 N  N     . ARG   A 1 308  ? 31.739  1.742   -56.358 1.00 45.37  ? 457  ARG   A N     1 
ATOM   1423 C  CA    . ARG   A 1 308  ? 33.140  1.373   -56.664 1.00 45.68  ? 457  ARG   A CA    1 
ATOM   1424 C  C     . ARG   A 1 308  ? 33.884  2.597   -57.185 1.00 42.25  ? 457  ARG   A C     1 
ATOM   1425 O  O     . ARG   A 1 308  ? 35.014  2.839   -56.719 1.00 42.53  ? 457  ARG   A O     1 
ATOM   1426 C  CB    . ARG   A 1 308  ? 33.234  0.232   -57.678 1.00 46.92  ? 457  ARG   A CB    1 
ATOM   1427 C  CG    . ARG   A 1 308  ? 34.659  -0.110  -58.092 1.00 50.63  ? 457  ARG   A CG    1 
ATOM   1428 C  CD    . ARG   A 1 308  ? 35.517  -0.450  -56.889 1.00 56.09  ? 457  ARG   A CD    1 
ATOM   1429 N  NE    . ARG   A 1 308  ? 36.900  -0.733  -57.248 1.00 54.08  ? 457  ARG   A NE    1 
ATOM   1430 C  CZ    . ARG   A 1 308  ? 37.806  -1.265  -56.424 1.00 52.68  ? 457  ARG   A CZ    1 
ATOM   1431 N  NH1   . ARG   A 1 308  ? 37.497  -1.604  -55.176 1.00 48.91  ? 457  ARG   A NH1   1 
ATOM   1432 N  NH2   . ARG   A 1 308  ? 39.020  -1.491  -56.877 1.00 48.29  ? 457  ARG   A NH2   1 
ATOM   1433 N  N     . VAL   A 1 309  ? 33.277  3.359   -58.085 1.00 37.97  ? 458  VAL   A N     1 
ATOM   1434 C  CA    . VAL   A 1 309  ? 33.971  4.531   -58.680 1.00 42.15  ? 458  VAL   A CA    1 
ATOM   1435 C  C     . VAL   A 1 309  ? 34.101  5.640   -57.620 1.00 43.95  ? 458  VAL   A C     1 
ATOM   1436 O  O     . VAL   A 1 309  ? 35.141  6.295   -57.604 1.00 43.85  ? 458  VAL   A O     1 
ATOM   1437 C  CB    . VAL   A 1 309  ? 33.293  4.976   -59.989 1.00 44.22  ? 458  VAL   A CB    1 
ATOM   1438 C  CG1   . VAL   A 1 309  ? 33.895  6.251   -60.559 1.00 42.13  ? 458  VAL   A CG1   1 
ATOM   1439 C  CG2   . VAL   A 1 309  ? 33.372  3.860   -61.025 1.00 42.70  ? 458  VAL   A CG2   1 
ATOM   1440 N  N     . ALA   A 1 310  ? 33.115  5.835   -56.742 1.00 45.03  ? 459  ALA   A N     1 
ATOM   1441 C  CA    . ALA   A 1 310  ? 33.218  6.804   -55.625 1.00 43.80  ? 459  ALA   A CA    1 
ATOM   1442 C  C     . ALA   A 1 310  ? 34.424  6.415   -54.751 1.00 43.73  ? 459  ALA   A C     1 
ATOM   1443 O  O     . ALA   A 1 310  ? 35.304  7.255   -54.568 1.00 42.46  ? 459  ALA   A O     1 
ATOM   1444 C  CB    . ALA   A 1 310  ? 31.927  6.846   -54.840 1.00 42.43  ? 459  ALA   A CB    1 
ATOM   1445 N  N     . TYR   A 1 311  ? 34.485  5.162   -54.290 1.00 47.39  ? 460  TYR   A N     1 
ATOM   1446 C  CA    . TYR   A 1 311  ? 35.607  4.590   -53.497 1.00 49.17  ? 460  TYR   A CA    1 
ATOM   1447 C  C     . TYR   A 1 311  ? 36.935  4.900   -54.202 1.00 48.29  ? 460  TYR   A C     1 
ATOM   1448 O  O     . TYR   A 1 311  ? 37.841  5.379   -53.513 1.00 54.67  ? 460  TYR   A O     1 
ATOM   1449 C  CB    . TYR   A 1 311  ? 35.416  3.090   -53.219 1.00 49.02  ? 460  TYR   A CB    1 
ATOM   1450 C  CG    . TYR   A 1 311  ? 36.664  2.376   -52.758 1.00 51.02  ? 460  TYR   A CG    1 
ATOM   1451 C  CD1   . TYR   A 1 311  ? 37.013  2.316   -51.414 1.00 50.38  ? 460  TYR   A CD1   1 
ATOM   1452 C  CD2   . TYR   A 1 311  ? 37.532  1.802   -53.678 1.00 53.22  ? 460  TYR   A CD2   1 
ATOM   1453 C  CE1   . TYR   A 1 311  ? 38.181  1.693   -50.997 1.00 54.57  ? 460  TYR   A CE1   1 
ATOM   1454 C  CE2   . TYR   A 1 311  ? 38.697  1.164   -53.280 1.00 56.52  ? 460  TYR   A CE2   1 
ATOM   1455 C  CZ    . TYR   A 1 311  ? 39.028  1.118   -51.934 1.00 61.01  ? 460  TYR   A CZ    1 
ATOM   1456 O  OH    . TYR   A 1 311  ? 40.186  0.500   -51.557 1.00 63.65  ? 460  TYR   A OH    1 
ATOM   1457 N  N     . GLU   A 1 312  ? 37.031  4.694   -55.520 1.00 48.25  ? 461  GLU   A N     1 
ATOM   1458 C  CA    . GLU   A 1 312  ? 38.275  4.942   -56.309 1.00 46.30  ? 461  GLU   A CA    1 
ATOM   1459 C  C     . GLU   A 1 312  ? 38.619  6.438   -56.347 1.00 48.02  ? 461  GLU   A C     1 
ATOM   1460 O  O     . GLU   A 1 312  ? 39.743  6.779   -56.795 1.00 45.12  ? 461  GLU   A O     1 
ATOM   1461 C  CB    . GLU   A 1 312  ? 38.160  4.395   -57.732 1.00 45.43  ? 461  GLU   A CB    1 
ATOM   1462 C  CG    . GLU   A 1 312  ? 38.317  2.881   -57.807 1.00 49.93  ? 461  GLU   A CG    1 
ATOM   1463 C  CD    . GLU   A 1 312  ? 38.409  2.278   -59.204 1.00 53.06  ? 461  GLU   A CD    1 
ATOM   1464 O  OE1   . GLU   A 1 312  ? 38.819  2.992   -60.146 1.00 54.87  ? 461  GLU   A OE1   1 
ATOM   1465 O  OE2   . GLU   A 1 312  ? 38.066  1.093   -59.355 1.00 59.18  ? 461  GLU   A OE2   1 
ATOM   1466 N  N     . ARG   A 1 313  ? 37.708  7.313   -55.917 1.00 46.54  ? 462  ARG   A N     1 
ATOM   1467 C  CA    . ARG   A 1 313  ? 37.946  8.779   -55.926 1.00 45.99  ? 462  ARG   A CA    1 
ATOM   1468 C  C     . ARG   A 1 313  ? 37.940  9.328   -54.490 1.00 46.19  ? 462  ARG   A C     1 
ATOM   1469 O  O     . ARG   A 1 313  ? 37.964  10.575  -54.331 1.00 40.78  ? 462  ARG   A O     1 
ATOM   1470 C  CB    . ARG   A 1 313  ? 36.903  9.429   -56.832 1.00 42.45  ? 462  ARG   A CB    1 
ATOM   1471 C  CG    . ARG   A 1 313  ? 37.013  8.983   -58.280 1.00 45.90  ? 462  ARG   A CG    1 
ATOM   1472 C  CD    . ARG   A 1 313  ? 36.002  9.701   -59.152 1.00 47.59  ? 462  ARG   A CD    1 
ATOM   1473 N  NE    . ARG   A 1 313  ? 36.487  11.030  -59.479 1.00 45.40  ? 462  ARG   A NE    1 
ATOM   1474 C  CZ    . ARG   A 1 313  ? 37.456  11.262  -60.351 1.00 47.47  ? 462  ARG   A CZ    1 
ATOM   1475 N  NH1   . ARG   A 1 313  ? 38.030  10.253  -61.001 1.00 44.28  ? 462  ARG   A NH1   1 
ATOM   1476 N  NH2   . ARG   A 1 313  ? 37.838  12.503  -60.585 1.00 49.05  ? 462  ARG   A NH2   1 
ATOM   1477 N  N     . GLY   A 1 314  ? 37.912  8.441   -53.488 1.00 50.19  ? 463  GLY   A N     1 
ATOM   1478 C  CA    . GLY   A 1 314  ? 37.965  8.814   -52.060 1.00 53.66  ? 463  GLY   A CA    1 
ATOM   1479 C  C     . GLY   A 1 314  ? 36.662  9.409   -51.563 1.00 56.88  ? 463  GLY   A C     1 
ATOM   1480 O  O     . GLY   A 1 314  ? 36.721  10.279  -50.683 1.00 71.41  ? 463  GLY   A O     1 
ATOM   1481 N  N     . GLU   A 1 315  ? 35.523  8.934   -52.075 1.00 56.61  ? 464  GLU   A N     1 
ATOM   1482 C  CA    . GLU   A 1 315  ? 34.178  9.505   -51.793 1.00 53.06  ? 464  GLU   A CA    1 
ATOM   1483 C  C     . GLU   A 1 315  ? 33.160  8.379   -51.564 1.00 49.88  ? 464  GLU   A C     1 
ATOM   1484 O  O     . GLU   A 1 315  ? 33.484  7.198   -51.813 1.00 49.21  ? 464  GLU   A O     1 
ATOM   1485 C  CB    . GLU   A 1 315  ? 33.701  10.393  -52.948 1.00 49.76  ? 464  GLU   A CB    1 
ATOM   1486 C  CG    . GLU   A 1 315  ? 34.697  11.445  -53.424 1.00 48.63  ? 464  GLU   A CG    1 
ATOM   1487 C  CD    . GLU   A 1 315  ? 34.306  12.121  -54.731 1.00 50.00  ? 464  GLU   A CD    1 
ATOM   1488 O  OE1   . GLU   A 1 315  ? 33.325  11.674  -55.337 1.00 53.68  ? 464  GLU   A OE1   1 
ATOM   1489 O  OE2   . GLU   A 1 315  ? 34.985  13.082  -55.160 1.00 53.01  ? 464  GLU   A OE2   1 
ATOM   1490 N  N     . GLU   A 1 316  ? 31.998  8.762   -51.039 1.00 52.08  ? 465  GLU   A N     1 
ATOM   1491 C  CA    . GLU   A 1 316  ? 30.715  8.020   -51.104 1.00 56.74  ? 465  GLU   A CA    1 
ATOM   1492 C  C     . GLU   A 1 316  ? 29.950  8.604   -52.288 1.00 50.04  ? 465  GLU   A C     1 
ATOM   1493 O  O     . GLU   A 1 316  ? 30.231  9.729   -52.714 1.00 42.06  ? 465  GLU   A O     1 
ATOM   1494 C  CB    . GLU   A 1 316  ? 29.900  8.196   -49.816 1.00 65.32  ? 465  GLU   A CB    1 
ATOM   1495 C  CG    . GLU   A 1 316  ? 30.661  7.914   -48.524 1.00 73.56  ? 465  GLU   A CG    1 
ATOM   1496 C  CD    . GLU   A 1 316  ? 30.265  6.643   -47.786 1.00 78.09  ? 465  GLU   A CD    1 
ATOM   1497 O  OE1   . GLU   A 1 316  ? 30.317  5.557   -48.397 1.00 81.17  ? 465  GLU   A OE1   1 
ATOM   1498 O  OE2   . GLU   A 1 316  ? 29.898  6.744   -46.603 1.00 78.53  ? 465  GLU   A OE2   1 
ATOM   1499 N  N     . PRO   A 1 317  ? 28.985  7.878   -52.891 1.00 43.24  ? 466  PRO   A N     1 
ATOM   1500 C  CA    . PRO   A 1 317  ? 28.162  8.473   -53.948 1.00 45.45  ? 466  PRO   A CA    1 
ATOM   1501 C  C     . PRO   A 1 317  ? 27.521  9.769   -53.437 1.00 45.45  ? 466  PRO   A C     1 
ATOM   1502 O  O     . PRO   A 1 317  ? 27.085  9.810   -52.285 1.00 41.56  ? 466  PRO   A O     1 
ATOM   1503 C  CB    . PRO   A 1 317  ? 27.117  7.395   -54.273 1.00 42.61  ? 466  PRO   A CB    1 
ATOM   1504 C  CG    . PRO   A 1 317  ? 27.801  6.107   -53.856 1.00 43.74  ? 466  PRO   A CG    1 
ATOM   1505 C  CD    . PRO   A 1 317  ? 28.654  6.470   -52.647 1.00 43.47  ? 466  PRO   A CD    1 
ATOM   1506 N  N     . GLY   A 1 318  ? 27.473  10.795  -54.282 1.00 44.14  ? 467  GLY   A N     1 
ATOM   1507 C  CA    . GLY   A 1 318  ? 26.837  12.070  -53.910 1.00 46.62  ? 467  GLY   A CA    1 
ATOM   1508 C  C     . GLY   A 1 318  ? 27.657  13.275  -54.305 1.00 44.02  ? 467  GLY   A C     1 
ATOM   1509 O  O     . GLY   A 1 318  ? 27.114  14.366  -54.200 1.00 41.74  ? 467  GLY   A O     1 
ATOM   1510 N  N     . LYS   A 1 319  ? 28.898  13.077  -54.756 1.00 46.47  ? 468  LYS   A N     1 
ATOM   1511 C  CA    . LYS   A 1 319  ? 29.821  14.153  -55.186 1.00 49.71  ? 468  LYS   A CA    1 
ATOM   1512 C  C     . LYS   A 1 319  ? 30.103  13.996  -56.682 1.00 46.91  ? 468  LYS   A C     1 
ATOM   1513 O  O     . LYS   A 1 319  ? 29.224  14.333  -57.472 1.00 49.02  ? 468  LYS   A O     1 
ATOM   1514 C  CB    . LYS   A 1 319  ? 31.109  14.102  -54.362 1.00 58.41  ? 468  LYS   A CB    1 
ATOM   1515 C  CG    . LYS   A 1 319  ? 31.036  14.739  -52.981 1.00 71.30  ? 468  LYS   A CG    1 
ATOM   1516 C  CD    . LYS   A 1 319  ? 32.382  15.259  -52.486 1.00 79.99  ? 468  LYS   A CD    1 
ATOM   1517 C  CE    . LYS   A 1 319  ? 33.022  16.235  -53.455 1.00 84.32  ? 468  LYS   A CE    1 
ATOM   1518 N  NZ    . LYS   A 1 319  ? 34.040  17.089  -52.800 1.00 84.77  ? 468  LYS   A NZ    1 
ATOM   1519 N  N     . SER   A 1 320  ? 31.295  13.535  -57.062 1.00 41.59  ? 469  SER   A N     1 
ATOM   1520 C  CA    . SER   A 1 320  ? 31.676  13.337  -58.475 1.00 40.52  ? 469  SER   A CA    1 
ATOM   1521 C  C     . SER   A 1 320  ? 30.796  12.237  -59.111 1.00 40.81  ? 469  SER   A C     1 
ATOM   1522 O  O     . SER   A 1 320  ? 30.579  12.341  -60.310 1.00 36.38  ? 469  SER   A O     1 
ATOM   1523 C  CB    . SER   A 1 320  ? 33.167  13.059  -58.615 1.00 40.67  ? 469  SER   A CB    1 
ATOM   1524 O  OG    . SER   A 1 320  ? 33.508  11.744  -58.175 1.00 45.97  ? 469  SER   A OG    1 
ATOM   1525 N  N     . CYS   A 1 321  ? 30.334  11.223  -58.349 1.00 41.22  ? 470  CYS   A N     1 
ATOM   1526 C  CA    . CYS   A 1 321  ? 29.520  10.075  -58.841 1.00 41.22  ? 470  CYS   A CA    1 
ATOM   1527 C  C     . CYS   A 1 321  ? 28.167  10.003  -58.140 1.00 43.57  ? 470  CYS   A C     1 
ATOM   1528 O  O     . CYS   A 1 321  ? 28.080  10.369  -56.960 1.00 42.89  ? 470  CYS   A O     1 
ATOM   1529 C  CB    . CYS   A 1 321  ? 30.185  8.733   -58.589 1.00 43.03  ? 470  CYS   A CB    1 
ATOM   1530 S  SG    . CYS   A 1 321  ? 31.877  8.698   -59.206 1.00 60.24  ? 470  CYS   A SG    1 
ATOM   1531 N  N     . GLY   A 1 322  ? 27.170  9.487   -58.856 1.00 41.99  ? 471  GLY   A N     1 
ATOM   1532 C  CA    . GLY   A 1 322  ? 25.830  9.179   -58.331 1.00 41.83  ? 471  GLY   A CA    1 
ATOM   1533 C  C     . GLY   A 1 322  ? 25.228  8.012   -59.094 1.00 43.07  ? 471  GLY   A C     1 
ATOM   1534 O  O     . GLY   A 1 322  ? 25.879  7.502   -60.047 1.00 40.77  ? 471  GLY   A O     1 
ATOM   1535 N  N     . TYR   A 1 323  ? 24.055  7.569   -58.665 1.00 35.02  ? 472  TYR   A N     1 
ATOM   1536 C  CA    . TYR   A 1 323  ? 23.308  6.477   -59.312 1.00 37.96  ? 472  TYR   A CA    1 
ATOM   1537 C  C     . TYR   A 1 323  ? 21.825  6.862   -59.320 1.00 38.78  ? 472  TYR   A C     1 
ATOM   1538 O  O     . TYR   A 1 323  ? 21.360  7.597   -58.415 1.00 37.04  ? 472  TYR   A O     1 
ATOM   1539 C  CB    . TYR   A 1 323  ? 23.651  5.139   -58.645 1.00 41.39  ? 472  TYR   A CB    1 
ATOM   1540 C  CG    . TYR   A 1 323  ? 23.069  4.889   -57.275 1.00 41.30  ? 472  TYR   A CG    1 
ATOM   1541 C  CD1   . TYR   A 1 323  ? 21.770  4.434   -57.126 1.00 41.77  ? 472  TYR   A CD1   1 
ATOM   1542 C  CD2   . TYR   A 1 323  ? 23.828  5.073   -56.127 1.00 43.15  ? 472  TYR   A CD2   1 
ATOM   1543 C  CE1   . TYR   A 1 323  ? 21.239  4.178   -55.873 1.00 44.34  ? 472  TYR   A CE1   1 
ATOM   1544 C  CE2   . TYR   A 1 323  ? 23.309  4.836   -54.865 1.00 42.59  ? 472  TYR   A CE2   1 
ATOM   1545 C  CZ    . TYR   A 1 323  ? 22.008  4.384   -54.736 1.00 46.05  ? 472  TYR   A CZ    1 
ATOM   1546 O  OH    . TYR   A 1 323  ? 21.487  4.108   -53.501 1.00 47.09  ? 472  TYR   A OH    1 
ATOM   1547 N  N     . SER   A 1 324  ? 21.117  6.422   -60.357 1.00 36.35  ? 473  SER   A N     1 
ATOM   1548 C  CA    . SER   A 1 324  ? 19.637  6.511   -60.468 1.00 37.42  ? 473  SER   A CA    1 
ATOM   1549 C  C     . SER   A 1 324  ? 19.127  5.199   -61.070 1.00 37.39  ? 473  SER   A C     1 
ATOM   1550 O  O     . SER   A 1 324  ? 19.481  4.859   -62.231 1.00 36.79  ? 473  SER   A O     1 
ATOM   1551 C  CB    . SER   A 1 324  ? 19.203  7.717   -61.256 1.00 37.24  ? 473  SER   A CB    1 
ATOM   1552 O  OG    . SER   A 1 324  ? 17.817  7.985   -61.035 1.00 39.18  ? 473  SER   A OG    1 
ATOM   1553 N  N     . VAL   A 1 325  ? 18.403  4.441   -60.257 1.00 37.06  ? 474  VAL   A N     1 
ATOM   1554 C  CA    . VAL   A 1 325  ? 17.720  3.191   -60.668 1.00 33.89  ? 474  VAL   A CA    1 
ATOM   1555 C  C     . VAL   A 1 325  ? 16.245  3.308   -60.317 1.00 36.39  ? 474  VAL   A C     1 
ATOM   1556 O  O     . VAL   A 1 325  ? 15.811  4.381   -59.810 1.00 34.06  ? 474  VAL   A O     1 
ATOM   1557 C  CB    . VAL   A 1 325  ? 18.380  1.984   -60.007 1.00 34.45  ? 474  VAL   A CB    1 
ATOM   1558 C  CG1   . VAL   A 1 325  ? 19.852  1.962   -60.362 1.00 34.77  ? 474  VAL   A CG1   1 
ATOM   1559 C  CG2   . VAL   A 1 325  ? 18.164  1.966   -58.502 1.00 37.64  ? 474  VAL   A CG2   1 
ATOM   1560 N  N     . ARG   A 1 326  ? 15.471  2.285   -60.652 1.00 37.88  ? 475  ARG   A N     1 
ATOM   1561 C  CA    . ARG   A 1 326  ? 14.017  2.395   -60.447 1.00 40.46  ? 475  ARG   A CA    1 
ATOM   1562 C  C     . ARG   A 1 326  ? 13.783  2.500   -58.935 1.00 41.56  ? 475  ARG   A C     1 
ATOM   1563 O  O     . ARG   A 1 326  ? 14.225  1.609   -58.192 1.00 42.15  ? 475  ARG   A O     1 
ATOM   1564 C  CB    . ARG   A 1 326  ? 13.284  1.238   -61.112 1.00 44.03  ? 475  ARG   A CB    1 
ATOM   1565 C  CG    . ARG   A 1 326  ? 11.806  1.559   -61.274 1.00 53.27  ? 475  ARG   A CG    1 
ATOM   1566 C  CD    . ARG   A 1 326  ? 10.959  0.319   -61.379 1.00 53.98  ? 475  ARG   A CD    1 
ATOM   1567 N  NE    . ARG   A 1 326  ? 11.026  -0.200  -62.717 1.00 54.97  ? 475  ARG   A NE    1 
ATOM   1568 C  CZ    . ARG   A 1 326  ? 10.353  -1.256  -63.127 1.00 70.09  ? 475  ARG   A CZ    1 
ATOM   1569 N  NH1   . ARG   A 1 326  ? 9.567   -1.910  -62.277 1.00 71.00  ? 475  ARG   A NH1   1 
ATOM   1570 N  NH2   . ARG   A 1 326  ? 10.483  -1.647  -64.385 1.00 67.24  ? 475  ARG   A NH2   1 
ATOM   1571 N  N     . PHE   A 1 327  ? 13.215  3.616   -58.494 1.00 42.26  ? 476  PHE   A N     1 
ATOM   1572 C  CA    . PHE   A 1 327  ? 12.775  3.862   -57.093 1.00 43.68  ? 476  PHE   A CA    1 
ATOM   1573 C  C     . PHE   A 1 327  ? 13.934  4.115   -56.119 1.00 43.42  ? 476  PHE   A C     1 
ATOM   1574 O  O     . PHE   A 1 327  ? 13.656  4.066   -54.901 1.00 45.43  ? 476  PHE   A O     1 
ATOM   1575 C  CB    . PHE   A 1 327  ? 11.949  2.683   -56.579 1.00 44.90  ? 476  PHE   A CB    1 
ATOM   1576 C  CG    . PHE   A 1 327  ? 10.744  2.375   -57.416 1.00 44.24  ? 476  PHE   A CG    1 
ATOM   1577 C  CD1   . PHE   A 1 327  ? 9.917   3.400   -57.863 1.00 42.16  ? 476  PHE   A CD1   1 
ATOM   1578 C  CD2   . PHE   A 1 327  ? 10.442  1.066   -57.746 1.00 43.06  ? 476  PHE   A CD2   1 
ATOM   1579 C  CE1   . PHE   A 1 327  ? 8.810   3.110   -58.638 1.00 44.42  ? 476  PHE   A CE1   1 
ATOM   1580 C  CE2   . PHE   A 1 327  ? 9.333   0.781   -58.517 1.00 41.56  ? 476  PHE   A CE2   1 
ATOM   1581 C  CZ    . PHE   A 1 327  ? 8.523   1.804   -58.960 1.00 45.51  ? 476  PHE   A CZ    1 
ATOM   1582 N  N     . GLU   A 1 328  ? 15.153  4.405   -56.586 1.00 41.28  ? 477  GLU   A N     1 
ATOM   1583 C  CA    . GLU   A 1 328  ? 16.277  4.790   -55.682 1.00 41.46  ? 477  GLU   A CA    1 
ATOM   1584 C  C     . GLU   A 1 328  ? 17.309  5.621   -56.447 1.00 40.12  ? 477  GLU   A C     1 
ATOM   1585 O  O     . GLU   A 1 328  ? 17.670  5.258   -57.583 1.00 40.83  ? 477  GLU   A O     1 
ATOM   1586 C  CB    . GLU   A 1 328  ? 16.915  3.540   -55.080 1.00 42.54  ? 477  GLU   A CB    1 
ATOM   1587 C  CG    . GLU   A 1 328  ? 17.963  3.823   -54.016 1.00 49.32  ? 477  GLU   A CG    1 
ATOM   1588 C  CD    . GLU   A 1 328  ? 18.565  2.569   -53.400 1.00 52.48  ? 477  GLU   A CD    1 
ATOM   1589 O  OE1   . GLU   A 1 328  ? 17.792  1.761   -52.845 1.00 56.67  ? 477  GLU   A OE1   1 
ATOM   1590 O  OE2   . GLU   A 1 328  ? 19.794  2.383   -53.506 1.00 53.68  ? 477  GLU   A OE2   1 
ATOM   1591 N  N     . SER   A 1 329  ? 17.774  6.707   -55.850 1.00 40.56  ? 478  SER   A N     1 
ATOM   1592 C  CA    . SER   A 1 329  ? 18.850  7.545   -56.431 1.00 41.18  ? 478  SER   A CA    1 
ATOM   1593 C  C     . SER   A 1 329  ? 19.701  8.191   -55.329 1.00 38.46  ? 478  SER   A C     1 
ATOM   1594 O  O     . SER   A 1 329  ? 19.202  8.414   -54.228 1.00 36.95  ? 478  SER   A O     1 
ATOM   1595 C  CB    . SER   A 1 329  ? 18.266  8.581   -57.337 1.00 38.94  ? 478  SER   A CB    1 
ATOM   1596 O  OG    . SER   A 1 329  ? 17.312  9.347   -56.635 1.00 38.83  ? 478  SER   A OG    1 
ATOM   1597 N  N     . VAL   A 1 330  ? 20.952  8.475   -55.664 1.00 38.65  ? 479  VAL   A N     1 
ATOM   1598 C  CA    . VAL   A 1 330  ? 21.841  9.436   -54.967 1.00 38.76  ? 479  VAL   A CA    1 
ATOM   1599 C  C     . VAL   A 1 330  ? 22.425  10.312  -56.067 1.00 37.39  ? 479  VAL   A C     1 
ATOM   1600 O  O     . VAL   A 1 330  ? 23.286  9.823   -56.811 1.00 42.79  ? 479  VAL   A O     1 
ATOM   1601 C  CB    . VAL   A 1 330  ? 22.928  8.738   -54.125 1.00 42.25  ? 479  VAL   A CB    1 
ATOM   1602 C  CG1   . VAL   A 1 330  ? 23.845  9.751   -53.469 1.00 39.86  ? 479  VAL   A CG1   1 
ATOM   1603 C  CG2   . VAL   A 1 330  ? 22.337  7.808   -53.071 1.00 41.24  ? 479  VAL   A CG2   1 
ATOM   1604 N  N     . LEU   A 1 331  ? 21.908  11.527  -56.200 1.00 39.30  ? 480  LEU   A N     1 
ATOM   1605 C  CA    . LEU   A 1 331  ? 22.260  12.477  -57.280 1.00 40.39  ? 480  LEU   A CA    1 
ATOM   1606 C  C     . LEU   A 1 331  ? 23.713  12.892  -57.098 1.00 44.77  ? 480  LEU   A C     1 
ATOM   1607 O  O     . LEU   A 1 331  ? 24.163  13.123  -55.976 1.00 47.72  ? 480  LEU   A O     1 
ATOM   1608 C  CB    . LEU   A 1 331  ? 21.331  13.689  -57.186 1.00 42.91  ? 480  LEU   A CB    1 
ATOM   1609 C  CG    . LEU   A 1 331  ? 19.854  13.463  -57.528 1.00 45.97  ? 480  LEU   A CG    1 
ATOM   1610 C  CD1   . LEU   A 1 331  ? 19.260  14.713  -58.159 1.00 46.17  ? 480  LEU   A CD1   1 
ATOM   1611 C  CD2   . LEU   A 1 331  ? 19.656  12.292  -58.476 1.00 44.21  ? 480  LEU   A CD2   1 
ATOM   1612 N  N     . PRO   A 1 332  ? 24.508  12.961  -58.182 1.00 48.17  ? 481  PRO   A N     1 
ATOM   1613 C  CA    . PRO   A 1 332  ? 25.844  13.540  -58.104 1.00 49.52  ? 481  PRO   A CA    1 
ATOM   1614 C  C     . PRO   A 1 332  ? 25.716  15.064  -57.983 1.00 47.56  ? 481  PRO   A C     1 
ATOM   1615 O  O     . PRO   A 1 332  ? 24.613  15.570  -58.088 1.00 42.90  ? 481  PRO   A O     1 
ATOM   1616 C  CB    . PRO   A 1 332  ? 26.527  13.196  -59.433 1.00 48.29  ? 481  PRO   A CB    1 
ATOM   1617 C  CG    . PRO   A 1 332  ? 25.513  12.353  -60.202 1.00 47.85  ? 481  PRO   A CG    1 
ATOM   1618 C  CD    . PRO   A 1 332  ? 24.164  12.557  -59.549 1.00 47.83  ? 481  PRO   A CD    1 
ATOM   1619 N  N     . ARG   A 1 333  ? 26.846  15.741  -57.781 1.00 45.88  ? 482  ARG   A N     1 
ATOM   1620 C  CA    . ARG   A 1 333  ? 26.944  17.226  -57.824 1.00 48.52  ? 482  ARG   A CA    1 
ATOM   1621 C  C     . ARG   A 1 333  ? 26.622  17.656  -59.251 1.00 46.44  ? 482  ARG   A C     1 
ATOM   1622 O  O     . ARG   A 1 333  ? 26.750  16.867  -60.176 1.00 46.27  ? 482  ARG   A O     1 
ATOM   1623 C  CB    . ARG   A 1 333  ? 28.329  17.692  -57.359 1.00 48.10  ? 482  ARG   A CB    1 
ATOM   1624 C  CG    . ARG   A 1 333  ? 29.454  17.359  -58.327 1.00 46.30  ? 482  ARG   A CG    1 
ATOM   1625 C  CD    . ARG   A 1 333  ? 30.842  17.596  -57.776 1.00 48.19  ? 482  ARG   A CD    1 
ATOM   1626 N  NE    . ARG   A 1 333  ? 31.856  17.250  -58.778 1.00 51.10  ? 482  ARG   A NE    1 
ATOM   1627 C  CZ    . ARG   A 1 333  ? 33.118  16.909  -58.513 1.00 51.10  ? 482  ARG   A CZ    1 
ATOM   1628 N  NH1   . ARG   A 1 333  ? 33.554  16.902  -57.265 1.00 51.93  ? 482  ARG   A NH1   1 
ATOM   1629 N  NH2   . ARG   A 1 333  ? 33.942  16.570  -59.494 1.00 49.30  ? 482  ARG   A NH2   1 
ATOM   1630 N  N     . PRO   A 1 334  ? 26.144  18.897  -59.461 1.00 47.28  ? 483  PRO   A N     1 
ATOM   1631 C  CA    . PRO   A 1 334  ? 25.769  19.358  -60.799 1.00 44.46  ? 483  PRO   A CA    1 
ATOM   1632 C  C     . PRO   A 1 334  ? 26.870  19.525  -61.863 1.00 47.23  ? 483  PRO   A C     1 
ATOM   1633 O  O     . PRO   A 1 334  ? 26.507  19.673  -63.030 1.00 43.15  ? 483  PRO   A O     1 
ATOM   1634 C  CB    . PRO   A 1 334  ? 25.144  20.741  -60.570 1.00 46.26  ? 483  PRO   A CB    1 
ATOM   1635 C  CG    . PRO   A 1 334  ? 25.387  21.099  -59.107 1.00 43.68  ? 483  PRO   A CG    1 
ATOM   1636 C  CD    . PRO   A 1 334  ? 25.820  19.847  -58.386 1.00 44.04  ? 483  PRO   A CD    1 
ATOM   1637 N  N     . HIS   A 1 335  ? 28.154  19.484  -61.477 1.00 44.82  ? 484  HIS   A N     1 
ATOM   1638 C  CA    . HIS   A 1 335  ? 29.317  19.798  -62.352 1.00 44.58  ? 484  HIS   A CA    1 
ATOM   1639 C  C     . HIS   A 1 335  ? 30.349  18.679  -62.313 1.00 46.07  ? 484  HIS   A C     1 
ATOM   1640 O  O     . HIS   A 1 335  ? 30.602  18.140  -61.219 1.00 46.04  ? 484  HIS   A O     1 
ATOM   1641 C  CB    . HIS   A 1 335  ? 30.006  21.096  -61.900 1.00 48.22  ? 484  HIS   A CB    1 
ATOM   1642 C  CG    . HIS   A 1 335  ? 29.117  22.285  -62.004 1.00 50.40  ? 484  HIS   A CG    1 
ATOM   1643 N  ND1   . HIS   A 1 335  ? 28.509  22.854  -60.891 1.00 50.72  ? 484  HIS   A ND1   1 
ATOM   1644 C  CD2   . HIS   A 1 335  ? 28.676  22.964  -63.085 1.00 46.49  ? 484  HIS   A CD2   1 
ATOM   1645 C  CE1   . HIS   A 1 335  ? 27.745  23.855  -61.291 1.00 51.05  ? 484  HIS   A CE1   1 
ATOM   1646 N  NE2   . HIS   A 1 335  ? 27.847  23.951  -62.638 1.00 50.48  ? 484  HIS   A NE2   1 
ATOM   1647 N  N     . ALA   A 1 336  ? 30.993  18.409  -63.447 1.00 43.50  ? 485  ALA   A N     1 
ATOM   1648 C  CA    . ALA   A 1 336  ? 32.153  17.506  -63.494 1.00 45.20  ? 485  ALA   A CA    1 
ATOM   1649 C  C     . ALA   A 1 336  ? 31.783  16.220  -62.747 1.00 44.62  ? 485  ALA   A C     1 
ATOM   1650 O  O     . ALA   A 1 336  ? 32.486  15.826  -61.806 1.00 45.24  ? 485  ALA   A O     1 
ATOM   1651 C  CB    . ALA   A 1 336  ? 33.332  18.222  -62.880 1.00 47.94  ? 485  ALA   A CB    1 
ATOM   1652 N  N     . SER   A 1 337  ? 30.666  15.613  -63.135 1.00 46.56  ? 486  SER   A N     1 
ATOM   1653 C  CA    . SER   A 1 337  ? 30.038  14.488  -62.403 1.00 41.21  ? 486  SER   A CA    1 
ATOM   1654 C  C     . SER   A 1 337  ? 29.661  13.374  -63.372 1.00 38.78  ? 486  SER   A C     1 
ATOM   1655 O  O     . SER   A 1 337  ? 29.477  13.670  -64.537 1.00 40.83  ? 486  SER   A O     1 
ATOM   1656 C  CB    . SER   A 1 337  ? 28.838  14.975  -61.669 1.00 40.72  ? 486  SER   A CB    1 
ATOM   1657 O  OG    . SER   A 1 337  ? 27.986  15.707  -62.541 1.00 41.95  ? 486  SER   A OG    1 
ATOM   1658 N  N     . ILE   A 1 338  ? 29.506  12.159  -62.852 1.00 40.40  ? 487  ILE   A N     1 
ATOM   1659 C  CA    . ILE   A 1 338  ? 29.108  10.911  -63.573 1.00 41.98  ? 487  ILE   A CA    1 
ATOM   1660 C  C     . ILE   A 1 338  ? 27.869  10.341  -62.872 1.00 39.28  ? 487  ILE   A C     1 
ATOM   1661 O  O     . ILE   A 1 338  ? 27.955  10.119  -61.659 1.00 39.54  ? 487  ILE   A O     1 
ATOM   1662 C  CB    . ILE   A 1 338  ? 30.252  9.881   -63.554 1.00 42.90  ? 487  ILE   A CB    1 
ATOM   1663 C  CG1   . ILE   A 1 338  ? 31.576  10.486  -64.022 1.00 41.44  ? 487  ILE   A CG1   1 
ATOM   1664 C  CG2   . ILE   A 1 338  ? 29.893  8.623   -64.344 1.00 42.29  ? 487  ILE   A CG2   1 
ATOM   1665 C  CD1   . ILE   A 1 338  ? 32.778  9.710   -63.528 1.00 38.11  ? 487  ILE   A CD1   1 
ATOM   1666 N  N     . MET   A 1 339  ? 26.775  10.134  -63.614 1.00 38.37  ? 488  MET   A N     1 
ATOM   1667 C  CA    . MET   A 1 339  ? 25.533  9.448   -63.170 1.00 37.04  ? 488  MET   A CA    1 
ATOM   1668 C  C     . MET   A 1 339  ? 25.516  8.035   -63.772 1.00 37.69  ? 488  MET   A C     1 
ATOM   1669 O  O     . MET   A 1 339  ? 25.505  7.944   -65.005 1.00 33.82  ? 488  MET   A O     1 
ATOM   1670 C  CB    . MET   A 1 339  ? 24.302  10.216  -63.655 1.00 39.12  ? 488  MET   A CB    1 
ATOM   1671 C  CG    . MET   A 1 339  ? 22.982  9.510   -63.364 1.00 40.72  ? 488  MET   A CG    1 
ATOM   1672 S  SD    . MET   A 1 339  ? 22.593  9.497   -61.604 1.00 44.80  ? 488  MET   A SD    1 
ATOM   1673 C  CE    . MET   A 1 339  ? 21.590  10.973  -61.497 1.00 43.19  ? 488  MET   A CE    1 
ATOM   1674 N  N     . PHE   A 1 340  ? 25.565  6.997   -62.937 1.00 32.61  ? 489  PHE   A N     1 
ATOM   1675 C  CA    . PHE   A 1 340  ? 25.344  5.583   -63.314 1.00 36.92  ? 489  PHE   A CA    1 
ATOM   1676 C  C     . PHE   A 1 340  ? 23.844  5.275   -63.143 1.00 42.91  ? 489  PHE   A C     1 
ATOM   1677 O  O     . PHE   A 1 340  ? 23.256  5.615   -62.100 1.00 42.44  ? 489  PHE   A O     1 
ATOM   1678 C  CB    . PHE   A 1 340  ? 26.232  4.656   -62.483 1.00 38.34  ? 489  PHE   A CB    1 
ATOM   1679 C  CG    . PHE   A 1 340  ? 27.714  4.907   -62.633 1.00 39.62  ? 489  PHE   A CG    1 
ATOM   1680 C  CD1   . PHE   A 1 340  ? 28.443  4.288   -63.637 1.00 41.69  ? 489  PHE   A CD1   1 
ATOM   1681 C  CD2   . PHE   A 1 340  ? 28.377  5.785   -61.783 1.00 41.71  ? 489  PHE   A CD2   1 
ATOM   1682 C  CE1   . PHE   A 1 340  ? 29.801  4.547   -63.783 1.00 42.38  ? 489  PHE   A CE1   1 
ATOM   1683 C  CE2   . PHE   A 1 340  ? 29.737  6.031   -61.925 1.00 41.91  ? 489  PHE   A CE2   1 
ATOM   1684 C  CZ    . PHE   A 1 340  ? 30.445  5.410   -62.924 1.00 38.67  ? 489  PHE   A CZ    1 
ATOM   1685 N  N     . CYS   A 1 341  ? 23.211  4.712   -64.173 1.00 40.47  ? 490  CYS   A N     1 
ATOM   1686 C  CA    . CYS   A 1 341  ? 21.743  4.515   -64.222 1.00 40.66  ? 490  CYS   A CA    1 
ATOM   1687 C  C     . CYS   A 1 341  ? 21.408  3.254   -65.009 1.00 38.83  ? 490  CYS   A C     1 
ATOM   1688 O  O     . CYS   A 1 341  ? 22.268  2.712   -65.719 1.00 39.48  ? 490  CYS   A O     1 
ATOM   1689 C  CB    . CYS   A 1 341  ? 21.035  5.704   -64.858 1.00 40.36  ? 490  CYS   A CB    1 
ATOM   1690 S  SG    . CYS   A 1 341  ? 21.389  5.912   -66.626 1.00 43.15  ? 490  CYS   A SG    1 
ATOM   1691 N  N     . THR   A 1 342  ? 20.182  2.803   -64.840 1.00 39.46  ? 491  THR   A N     1 
ATOM   1692 C  CA    . THR   A 1 342  ? 19.526  1.814   -65.716 1.00 38.77  ? 491  THR   A CA    1 
ATOM   1693 C  C     . THR   A 1 342  ? 18.900  2.607   -66.856 1.00 41.85  ? 491  THR   A C     1 
ATOM   1694 O  O     . THR   A 1 342  ? 18.628  3.823   -66.649 1.00 37.90  ? 491  THR   A O     1 
ATOM   1695 C  CB    . THR   A 1 342  ? 18.561  0.974   -64.884 1.00 39.90  ? 491  THR   A CB    1 
ATOM   1696 O  OG1   . THR   A 1 342  ? 17.723  1.844   -64.118 1.00 41.04  ? 491  THR   A OG1   1 
ATOM   1697 C  CG2   . THR   A 1 342  ? 19.304  0.044   -63.951 1.00 39.31  ? 491  THR   A CG2   1 
ATOM   1698 N  N     . VAL   A 1 343  ? 18.715  1.968   -68.014 1.00 43.31  ? 492  VAL   A N     1 
ATOM   1699 C  CA    . VAL   A 1 343  ? 18.239  2.653   -69.245 1.00 38.58  ? 492  VAL   A CA    1 
ATOM   1700 C  C     . VAL   A 1 343  ? 16.822  3.149   -69.006 1.00 37.89  ? 492  VAL   A C     1 
ATOM   1701 O  O     . VAL   A 1 343  ? 16.473  4.224   -69.536 1.00 43.15  ? 492  VAL   A O     1 
ATOM   1702 C  CB    . VAL   A 1 343  ? 18.307  1.749   -70.484 1.00 42.99  ? 492  VAL   A CB    1 
ATOM   1703 C  CG1   . VAL   A 1 343  ? 17.797  2.477   -71.725 1.00 41.79  ? 492  VAL   A CG1   1 
ATOM   1704 C  CG2   . VAL   A 1 343  ? 19.715  1.228   -70.716 1.00 46.78  ? 492  VAL   A CG2   1 
ATOM   1705 N  N     . GLY   A 1 344  ? 16.024  2.387   -68.266 1.00 37.25  ? 493  GLY   A N     1 
ATOM   1706 C  CA    . GLY   A 1 344  ? 14.628  2.759   -67.974 1.00 37.41  ? 493  GLY   A CA    1 
ATOM   1707 C  C     . GLY   A 1 344  ? 14.537  4.137   -67.355 1.00 40.36  ? 493  GLY   A C     1 
ATOM   1708 O  O     . GLY   A 1 344  ? 13.654  4.947   -67.766 1.00 46.77  ? 493  GLY   A O     1 
ATOM   1709 N  N     . VAL   A 1 345  ? 15.430  4.414   -66.410 1.00 37.80  ? 494  VAL   A N     1 
ATOM   1710 C  CA    . VAL   A 1 345  ? 15.443  5.705   -65.670 1.00 39.08  ? 494  VAL   A CA    1 
ATOM   1711 C  C     . VAL   A 1 345  ? 15.770  6.803   -66.686 1.00 36.96  ? 494  VAL   A C     1 
ATOM   1712 O  O     . VAL   A 1 345  ? 15.001  7.762   -66.772 1.00 41.93  ? 494  VAL   A O     1 
ATOM   1713 C  CB    . VAL   A 1 345  ? 16.403  5.635   -64.465 1.00 37.68  ? 494  VAL   A CB    1 
ATOM   1714 C  CG1   . VAL   A 1 345  ? 16.911  6.986   -64.034 1.00 36.66  ? 494  VAL   A CG1   1 
ATOM   1715 C  CG2   . VAL   A 1 345  ? 15.745  4.916   -63.297 1.00 39.73  ? 494  VAL   A CG2   1 
ATOM   1716 N  N     . LEU   A 1 346  ? 16.850  6.646   -67.444 1.00 37.46  ? 495  LEU   A N     1 
ATOM   1717 C  CA    . LEU   A 1 346  ? 17.269  7.625   -68.477 1.00 38.33  ? 495  LEU   A CA    1 
ATOM   1718 C  C     . LEU   A 1 346  ? 16.082  7.912   -69.409 1.00 43.20  ? 495  LEU   A C     1 
ATOM   1719 O  O     . LEU   A 1 346  ? 15.733  9.100   -69.548 1.00 43.41  ? 495  LEU   A O     1 
ATOM   1720 C  CB    . LEU   A 1 346  ? 18.463  7.069   -69.250 1.00 35.16  ? 495  LEU   A CB    1 
ATOM   1721 C  CG    . LEU   A 1 346  ? 18.950  7.942   -70.403 1.00 37.38  ? 495  LEU   A CG    1 
ATOM   1722 C  CD1   . LEU   A 1 346  ? 19.350  9.323   -69.908 1.00 38.22  ? 495  LEU   A CD1   1 
ATOM   1723 C  CD2   . LEU   A 1 346  ? 20.106  7.280   -71.137 1.00 36.94  ? 495  LEU   A CD2   1 
ATOM   1724 N  N     . LEU   A 1 347  ? 15.444  6.883   -69.980 1.00 43.29  ? 496  LEU   A N     1 
ATOM   1725 C  CA    . LEU   A 1 347  ? 14.324  7.086   -70.951 1.00 47.82  ? 496  LEU   A CA    1 
ATOM   1726 C  C     . LEU   A 1 347  ? 13.179  7.853   -70.281 1.00 45.77  ? 496  LEU   A C     1 
ATOM   1727 O  O     . LEU   A 1 347  ? 12.604  8.723   -70.957 1.00 48.69  ? 496  LEU   A O     1 
ATOM   1728 C  CB    . LEU   A 1 347  ? 13.829  5.751   -71.529 1.00 45.64  ? 496  LEU   A CB    1 
ATOM   1729 C  CG    . LEU   A 1 347  ? 14.850  4.986   -72.373 1.00 42.87  ? 496  LEU   A CG    1 
ATOM   1730 C  CD1   . LEU   A 1 347  ? 14.397  3.567   -72.605 1.00 45.35  ? 496  LEU   A CD1   1 
ATOM   1731 C  CD2   . LEU   A 1 347  ? 15.112  5.674   -73.695 1.00 43.80  ? 496  LEU   A CD2   1 
ATOM   1732 N  N     . ARG   A 1 348  ? 12.855  7.560   -69.017 1.00 47.01  ? 497  ARG   A N     1 
ATOM   1733 C  CA    . ARG   A 1 348  ? 11.755  8.268   -68.292 1.00 50.03  ? 497  ARG   A CA    1 
ATOM   1734 C  C     . ARG   A 1 348  ? 12.102  9.748   -68.079 1.00 49.82  ? 497  ARG   A C     1 
ATOM   1735 O  O     . ARG   A 1 348  ? 11.156  10.559  -67.941 1.00 50.67  ? 497  ARG   A O     1 
ATOM   1736 C  CB    . ARG   A 1 348  ? 11.447  7.636   -66.933 1.00 54.80  ? 497  ARG   A CB    1 
ATOM   1737 C  CG    . ARG   A 1 348  ? 10.430  6.508   -66.971 1.00 62.58  ? 497  ARG   A CG    1 
ATOM   1738 C  CD    . ARG   A 1 348  ? 10.252  5.862   -65.604 1.00 66.25  ? 497  ARG   A CD    1 
ATOM   1739 N  NE    . ARG   A 1 348  ? 11.002  4.607   -65.519 1.00 72.31  ? 497  ARG   A NE    1 
ATOM   1740 C  CZ    . ARG   A 1 348  ? 11.877  4.267   -64.565 1.00 68.04  ? 497  ARG   A CZ    1 
ATOM   1741 N  NH1   . ARG   A 1 348  ? 12.486  3.094   -64.649 1.00 57.16  ? 497  ARG   A NH1   1 
ATOM   1742 N  NH2   . ARG   A 1 348  ? 12.122  5.064   -63.528 1.00 64.97  ? 497  ARG   A NH2   1 
ATOM   1743 N  N     . LYS   A 1 349  ? 13.394  10.085  -68.042 1.00 46.96  ? 498  LYS   A N     1 
ATOM   1744 C  CA    . LYS   A 1 349  ? 13.898  11.462  -67.787 1.00 46.90  ? 498  LYS   A CA    1 
ATOM   1745 C  C     . LYS   A 1 349  ? 14.156  12.212  -69.101 1.00 45.75  ? 498  LYS   A C     1 
ATOM   1746 O  O     . LYS   A 1 349  ? 14.493  13.385  -69.002 1.00 42.01  ? 498  LYS   A O     1 
ATOM   1747 C  CB    . LYS   A 1 349  ? 15.190  11.427  -66.964 1.00 45.78  ? 498  LYS   A CB    1 
ATOM   1748 C  CG    . LYS   A 1 349  ? 15.054  10.841  -65.573 1.00 48.55  ? 498  LYS   A CG    1 
ATOM   1749 C  CD    . LYS   A 1 349  ? 14.232  11.691  -64.632 1.00 51.23  ? 498  LYS   A CD    1 
ATOM   1750 C  CE    . LYS   A 1 349  ? 13.830  10.947  -63.379 1.00 52.28  ? 498  LYS   A CE    1 
ATOM   1751 N  NZ    . LYS   A 1 349  ? 13.075  11.831  -62.464 1.00 57.61  ? 498  LYS   A NZ    1 
ATOM   1752 N  N     . LEU   A 1 350  ? 13.972  11.595  -70.278 1.00 54.55  ? 499  LEU   A N     1 
ATOM   1753 C  CA    . LEU   A 1 350  ? 14.243  12.236  -71.605 1.00 50.10  ? 499  LEU   A CA    1 
ATOM   1754 C  C     . LEU   A 1 350  ? 13.049  13.061  -72.095 1.00 45.83  ? 499  LEU   A C     1 
ATOM   1755 O  O     . LEU   A 1 350  ? 13.146  13.620  -73.197 1.00 53.09  ? 499  LEU   A O     1 
ATOM   1756 C  CB    . LEU   A 1 350  ? 14.575  11.165  -72.646 1.00 51.86  ? 499  LEU   A CB    1 
ATOM   1757 C  CG    . LEU   A 1 350  ? 15.935  10.501  -72.500 1.00 54.81  ? 499  LEU   A CG    1 
ATOM   1758 C  CD1   . LEU   A 1 350  ? 16.276  9.718   -73.752 1.00 56.46  ? 499  LEU   A CD1   1 
ATOM   1759 C  CD2   . LEU   A 1 350  ? 17.000  11.535  -72.216 1.00 58.87  ? 499  LEU   A CD2   1 
ATOM   1760 N  N     . GLU   A 1 351  ? 11.976  13.169  -71.321 1.00 51.44  ? 500  GLU   A N     1 
ATOM   1761 C  CA    . GLU   A 1 351  ? 10.736  13.899  -71.717 1.00 59.41  ? 500  GLU   A CA    1 
ATOM   1762 C  C     . GLU   A 1 351  ? 11.072  15.348  -72.131 1.00 60.40  ? 500  GLU   A C     1 
ATOM   1763 O  O     . GLU   A 1 351  ? 10.357  15.879  -73.007 1.00 69.04  ? 500  GLU   A O     1 
ATOM   1764 C  CB    . GLU   A 1 351  ? 9.718   13.814  -70.575 1.00 66.79  ? 500  GLU   A CB    1 
ATOM   1765 C  CG    . GLU   A 1 351  ? 8.268   13.845  -71.016 1.00 69.88  ? 500  GLU   A CG    1 
ATOM   1766 C  CD    . GLU   A 1 351  ? 7.268   13.635  -69.883 1.00 74.66  ? 500  GLU   A CD    1 
ATOM   1767 O  OE1   . GLU   A 1 351  ? 6.153   14.205  -69.971 1.00 79.54  ? 500  GLU   A OE1   1 
ATOM   1768 O  OE2   . GLU   A 1 351  ? 7.595   12.902  -68.913 1.00 67.39  ? 500  GLU   A OE2   1 
ATOM   1769 N  N     . ALA   A 1 352  ? 12.119  15.962  -71.564 1.00 58.66  ? 501  ALA   A N     1 
ATOM   1770 C  CA    . ALA   A 1 352  ? 12.586  17.334  -71.902 1.00 59.11  ? 501  ALA   A CA    1 
ATOM   1771 C  C     . ALA   A 1 352  ? 13.928  17.312  -72.647 1.00 57.94  ? 501  ALA   A C     1 
ATOM   1772 O  O     . ALA   A 1 352  ? 14.550  18.384  -72.773 1.00 65.53  ? 501  ALA   A O     1 
ATOM   1773 C  CB    . ALA   A 1 352  ? 12.699  18.163  -70.645 1.00 62.03  ? 501  ALA   A CB    1 
ATOM   1774 N  N     . GLY   A 1 353  ? 14.370  16.150  -73.126 1.00 51.19  ? 502  GLY   A N     1 
ATOM   1775 C  CA    . GLY   A 1 353  ? 15.639  16.010  -73.854 1.00 48.71  ? 502  GLY   A CA    1 
ATOM   1776 C  C     . GLY   A 1 353  ? 16.809  15.652  -72.952 1.00 44.97  ? 502  GLY   A C     1 
ATOM   1777 O  O     . GLY   A 1 353  ? 16.623  15.520  -71.742 1.00 45.06  ? 502  GLY   A O     1 
ATOM   1778 N  N     . ILE   A 1 354  ? 17.972  15.465  -73.568 1.00 42.80  ? 503  ILE   A N     1 
ATOM   1779 C  CA    . ILE   A 1 354  ? 19.291  15.235  -72.927 1.00 45.68  ? 503  ILE   A CA    1 
ATOM   1780 C  C     . ILE   A 1 354  ? 19.945  16.613  -72.740 1.00 48.71  ? 503  ILE   A C     1 
ATOM   1781 O  O     . ILE   A 1 354  ? 20.709  17.020  -73.636 1.00 48.06  ? 503  ILE   A O     1 
ATOM   1782 C  CB    . ILE   A 1 354  ? 20.133  14.299  -73.820 1.00 46.39  ? 503  ILE   A CB    1 
ATOM   1783 C  CG1   . ILE   A 1 354  ? 19.424  12.967  -74.089 1.00 50.00  ? 503  ILE   A CG1   1 
ATOM   1784 C  CG2   . ILE   A 1 354  ? 21.514  14.087  -73.225 1.00 51.59  ? 503  ILE   A CG2   1 
ATOM   1785 C  CD1   . ILE   A 1 354  ? 20.080  12.095  -75.155 1.00 49.56  ? 503  ILE   A CD1   1 
ATOM   1786 N  N     . ARG   A 1 355  ? 19.634  17.319  -71.645 1.00 49.95  ? 504  ARG   A N     1 
ATOM   1787 C  CA    . ARG   A 1 355  ? 20.043  18.736  -71.427 1.00 56.80  ? 504  ARG   A CA    1 
ATOM   1788 C  C     . ARG   A 1 355  ? 21.134  18.821  -70.348 1.00 54.73  ? 504  ARG   A C     1 
ATOM   1789 O  O     . ARG   A 1 355  ? 20.835  18.542  -69.159 1.00 47.45  ? 504  ARG   A O     1 
ATOM   1790 C  CB    . ARG   A 1 355  ? 18.828  19.591  -71.062 1.00 66.60  ? 504  ARG   A CB    1 
ATOM   1791 C  CG    . ARG   A 1 355  ? 17.752  19.619  -72.140 1.00 81.61  ? 504  ARG   A CG    1 
ATOM   1792 C  CD    . ARG   A 1 355  ? 17.355  21.034  -72.539 1.00 93.83  ? 504  ARG   A CD    1 
ATOM   1793 N  NE    . ARG   A 1 355  ? 16.311  21.100  -73.564 1.00 97.62  ? 504  ARG   A NE    1 
ATOM   1794 C  CZ    . ARG   A 1 355  ? 16.515  21.292  -74.869 1.00 97.23  ? 504  ARG   A CZ    1 
ATOM   1795 N  NH1   . ARG   A 1 355  ? 17.741  21.436  -75.347 1.00 103.12 ? 504  ARG   A NH1   1 
ATOM   1796 N  NH2   . ARG   A 1 355  ? 15.483  21.336  -75.697 1.00 92.99  ? 504  ARG   A NH2   1 
ATOM   1797 N  N     . GLY   A 1 356  ? 22.354  19.197  -70.755 1.00 47.16  ? 505  GLY   A N     1 
ATOM   1798 C  CA    . GLY   A 1 356  ? 23.470  19.522  -69.846 1.00 46.11  ? 505  GLY   A CA    1 
ATOM   1799 C  C     . GLY   A 1 356  ? 24.440  18.366  -69.680 1.00 44.36  ? 505  GLY   A C     1 
ATOM   1800 O  O     . GLY   A 1 356  ? 24.963  18.192  -68.572 1.00 46.55  ? 505  GLY   A O     1 
ATOM   1801 N  N     . ILE   A 1 357  ? 24.648  17.599  -70.747 1.00 42.17  ? 506  ILE   A N     1 
ATOM   1802 C  CA    . ILE   A 1 357  ? 25.359  16.290  -70.760 1.00 41.89  ? 506  ILE   A CA    1 
ATOM   1803 C  C     . ILE   A 1 357  ? 26.352  16.320  -71.913 1.00 39.74  ? 506  ILE   A C     1 
ATOM   1804 O  O     . ILE   A 1 357  ? 25.979  16.743  -72.984 1.00 42.76  ? 506  ILE   A O     1 
ATOM   1805 C  CB    . ILE   A 1 357  ? 24.347  15.142  -70.921 1.00 42.61  ? 506  ILE   A CB    1 
ATOM   1806 C  CG1   . ILE   A 1 357  ? 23.398  15.094  -69.733 1.00 41.76  ? 506  ILE   A CG1   1 
ATOM   1807 C  CG2   . ILE   A 1 357  ? 25.043  13.808  -71.132 1.00 45.32  ? 506  ILE   A CG2   1 
ATOM   1808 C  CD1   . ILE   A 1 357  ? 24.089  14.772  -68.452 1.00 46.10  ? 506  ILE   A CD1   1 
ATOM   1809 N  N     . SER   A 1 358  ? 27.583  15.903  -71.685 1.00 38.61  ? 507  SER   A N     1 
ATOM   1810 C  CA    . SER   A 1 358  ? 28.648  15.980  -72.708 1.00 40.84  ? 507  SER   A CA    1 
ATOM   1811 C  C     . SER   A 1 358  ? 28.870  14.586  -73.303 1.00 40.60  ? 507  SER   A C     1 
ATOM   1812 O  O     . SER   A 1 358  ? 29.160  14.491  -74.488 1.00 46.67  ? 507  SER   A O     1 
ATOM   1813 C  CB    . SER   A 1 358  ? 29.902  16.588  -72.124 1.00 36.33  ? 507  SER   A CB    1 
ATOM   1814 O  OG    . SER   A 1 358  ? 30.376  15.852  -71.008 1.00 39.22  ? 507  SER   A OG    1 
ATOM   1815 N  N     . HIS   A 1 359  ? 28.714  13.544  -72.499 1.00 40.68  ? 508  HIS   A N     1 
ATOM   1816 C  CA    . HIS   A 1 359  ? 29.072  12.151  -72.856 1.00 43.96  ? 508  HIS   A CA    1 
ATOM   1817 C  C     . HIS   A 1 359  ? 27.924  11.227  -72.433 1.00 44.83  ? 508  HIS   A C     1 
ATOM   1818 O  O     . HIS   A 1 359  ? 27.364  11.437  -71.333 1.00 43.77  ? 508  HIS   A O     1 
ATOM   1819 C  CB    . HIS   A 1 359  ? 30.410  11.753  -72.203 1.00 45.55  ? 508  HIS   A CB    1 
ATOM   1820 C  CG    . HIS   A 1 359  ? 31.590  12.557  -72.652 1.00 50.42  ? 508  HIS   A CG    1 
ATOM   1821 N  ND1   . HIS   A 1 359  ? 31.790  13.869  -72.258 1.00 48.87  ? 508  HIS   A ND1   1 
ATOM   1822 C  CD2   . HIS   A 1 359  ? 32.631  12.244  -73.457 1.00 51.61  ? 508  HIS   A CD2   1 
ATOM   1823 C  CE1   . HIS   A 1 359  ? 32.888  14.330  -72.816 1.00 52.09  ? 508  HIS   A CE1   1 
ATOM   1824 N  NE2   . HIS   A 1 359  ? 33.418  13.361  -73.570 1.00 51.88  ? 508  HIS   A NE2   1 
ATOM   1825 N  N     . VAL   A 1 360  ? 27.574  10.267  -73.298 1.00 45.47  ? 509  VAL   A N     1 
ATOM   1826 C  CA    . VAL   A 1 360  ? 26.682  9.119   -72.979 1.00 41.30  ? 509  VAL   A CA    1 
ATOM   1827 C  C     . VAL   A 1 360  ? 27.496  7.858   -73.206 1.00 38.65  ? 509  VAL   A C     1 
ATOM   1828 O  O     . VAL   A 1 360  ? 27.878  7.603   -74.341 1.00 42.82  ? 509  VAL   A O     1 
ATOM   1829 C  CB    . VAL   A 1 360  ? 25.389  9.141   -73.815 1.00 45.03  ? 509  VAL   A CB    1 
ATOM   1830 C  CG1   . VAL   A 1 360  ? 24.457  7.998   -73.438 1.00 44.10  ? 509  VAL   A CG1   1 
ATOM   1831 C  CG2   . VAL   A 1 360  ? 24.659  10.472  -73.675 1.00 44.41  ? 509  VAL   A CG2   1 
ATOM   1832 N  N     . ILE   A 1 361  ? 27.791  7.132   -72.137 1.00 39.96  ? 510  ILE   A N     1 
ATOM   1833 C  CA    . ILE   A 1 361  ? 28.518  5.839   -72.201 1.00 41.28  ? 510  ILE   A CA    1 
ATOM   1834 C  C     . ILE   A 1 361  ? 27.465  4.754   -72.031 1.00 41.90  ? 510  ILE   A C     1 
ATOM   1835 O  O     . ILE   A 1 361  ? 26.807  4.737   -70.973 1.00 44.36  ? 510  ILE   A O     1 
ATOM   1836 C  CB    . ILE   A 1 361  ? 29.633  5.747   -71.151 1.00 41.49  ? 510  ILE   A CB    1 
ATOM   1837 C  CG1   . ILE   A 1 361  ? 30.562  6.961   -71.191 1.00 43.29  ? 510  ILE   A CG1   1 
ATOM   1838 C  CG2   . ILE   A 1 361  ? 30.396  4.450   -71.311 1.00 42.66  ? 510  ILE   A CG2   1 
ATOM   1839 C  CD1   . ILE   A 1 361  ? 31.693  6.884   -70.187 1.00 42.70  ? 510  ILE   A CD1   1 
ATOM   1840 N  N     . VAL   A 1 362  ? 27.275  3.939   -73.069 1.00 40.09  ? 511  VAL   A N     1 
ATOM   1841 C  CA    . VAL   A 1 362  ? 26.309  2.808   -73.057 1.00 39.35  ? 511  VAL   A CA    1 
ATOM   1842 C  C     . VAL   A 1 362  ? 27.121  1.541   -72.797 1.00 37.81  ? 511  VAL   A C     1 
ATOM   1843 O  O     . VAL   A 1 362  ? 27.885  1.138   -73.653 1.00 40.79  ? 511  VAL   A O     1 
ATOM   1844 C  CB    . VAL   A 1 362  ? 25.498  2.754   -74.366 1.00 39.02  ? 511  VAL   A CB    1 
ATOM   1845 C  CG1   . VAL   A 1 362  ? 24.477  1.634   -74.336 1.00 41.76  ? 511  VAL   A CG1   1 
ATOM   1846 C  CG2   . VAL   A 1 362  ? 24.816  4.082   -74.655 1.00 38.73  ? 511  VAL   A CG2   1 
ATOM   1847 N  N     . ASP   A 1 363  ? 27.003  0.966   -71.617 1.00 39.27  ? 512  ASP   A N     1 
ATOM   1848 C  CA    . ASP   A 1 363  ? 27.876  -0.152  -71.202 1.00 44.24  ? 512  ASP   A CA    1 
ATOM   1849 C  C     . ASP   A 1 363  ? 27.191  -1.494  -71.518 1.00 42.58  ? 512  ASP   A C     1 
ATOM   1850 O  O     . ASP   A 1 363  ? 25.925  -1.557  -71.573 1.00 44.53  ? 512  ASP   A O     1 
ATOM   1851 C  CB    . ASP   A 1 363  ? 28.283  0.055   -69.738 1.00 46.79  ? 512  ASP   A CB    1 
ATOM   1852 C  CG    . ASP   A 1 363  ? 29.575  -0.632  -69.310 1.00 50.05  ? 512  ASP   A CG    1 
ATOM   1853 O  OD1   . ASP   A 1 363  ? 30.175  -1.348  -70.141 1.00 52.51  ? 512  ASP   A OD1   1 
ATOM   1854 O  OD2   . ASP   A 1 363  ? 29.955  -0.476  -68.118 1.00 50.89  ? 512  ASP   A OD2   1 
ATOM   1855 N  N     . GLU   A 1 364  ? 28.018  -2.522  -71.722 1.00 41.40  ? 513  GLU   A N     1 
ATOM   1856 C  CA    . GLU   A 1 364  ? 27.643  -3.963  -71.776 1.00 44.81  ? 513  GLU   A CA    1 
ATOM   1857 C  C     . GLU   A 1 364  ? 26.619  -4.171  -72.909 1.00 38.51  ? 513  GLU   A C     1 
ATOM   1858 O  O     . GLU   A 1 364  ? 25.631  -4.865  -72.715 1.00 40.32  ? 513  GLU   A O     1 
ATOM   1859 C  CB    . GLU   A 1 364  ? 27.171  -4.446  -70.395 1.00 49.74  ? 513  GLU   A CB    1 
ATOM   1860 C  CG    . GLU   A 1 364  ? 27.985  -3.942  -69.193 1.00 58.14  ? 513  GLU   A CG    1 
ATOM   1861 C  CD    . GLU   A 1 364  ? 29.459  -4.342  -69.046 1.00 64.81  ? 513  GLU   A CD    1 
ATOM   1862 O  OE1   . GLU   A 1 364  ? 29.994  -5.043  -69.959 1.00 66.10  ? 513  GLU   A OE1   1 
ATOM   1863 O  OE2   . GLU   A 1 364  ? 30.093  -3.941  -68.002 1.00 55.12  ? 513  GLU   A OE2   1 
ATOM   1864 N  N     . ILE   A 1 365  ? 26.870  -3.575  -74.066 1.00 38.81  ? 514  ILE   A N     1 
ATOM   1865 C  CA    . ILE   A 1 365  ? 25.973  -3.637  -75.258 1.00 42.79  ? 514  ILE   A CA    1 
ATOM   1866 C  C     . ILE   A 1 365  ? 25.794  -5.087  -75.726 1.00 45.66  ? 514  ILE   A C     1 
ATOM   1867 O  O     . ILE   A 1 365  ? 24.729  -5.369  -76.336 1.00 45.98  ? 514  ILE   A O     1 
ATOM   1868 C  CB    . ILE   A 1 365  ? 26.506  -2.781  -76.412 1.00 40.83  ? 514  ILE   A CB    1 
ATOM   1869 C  CG1   . ILE   A 1 365  ? 27.884  -3.246  -76.891 1.00 41.59  ? 514  ILE   A CG1   1 
ATOM   1870 C  CG2   . ILE   A 1 365  ? 26.489  -1.317  -76.045 1.00 42.52  ? 514  ILE   A CG2   1 
ATOM   1871 C  CD1   . ILE   A 1 365  ? 28.418  -2.418  -78.030 1.00 45.79  ? 514  ILE   A CD1   1 
ATOM   1872 N  N     . HIS   A 1 366  ? 26.805  -5.935  -75.502 1.00 39.50  ? 515  HIS   A N     1 
ATOM   1873 C  CA    . HIS   A 1 366  ? 26.851  -7.351  -75.952 1.00 42.52  ? 515  HIS   A CA    1 
ATOM   1874 C  C     . HIS   A 1 366  ? 25.824  -8.185  -75.187 1.00 46.49  ? 515  HIS   A C     1 
ATOM   1875 O  O     . HIS   A 1 366  ? 25.642  -9.344  -75.563 1.00 52.48  ? 515  HIS   A O     1 
ATOM   1876 C  CB    . HIS   A 1 366  ? 28.246  -7.951  -75.739 1.00 44.04  ? 515  HIS   A CB    1 
ATOM   1877 C  CG    . HIS   A 1 366  ? 28.635  -7.965  -74.302 1.00 42.95  ? 515  HIS   A CG    1 
ATOM   1878 N  ND1   . HIS   A 1 366  ? 29.246  -6.885  -73.703 1.00 44.28  ? 515  HIS   A ND1   1 
ATOM   1879 C  CD2   . HIS   A 1 366  ? 28.428  -8.873  -73.331 1.00 45.63  ? 515  HIS   A CD2   1 
ATOM   1880 C  CE1   . HIS   A 1 366  ? 29.419  -7.139  -72.431 1.00 44.74  ? 515  HIS   A CE1   1 
ATOM   1881 N  NE2   . HIS   A 1 366  ? 28.925  -8.354  -72.174 1.00 48.32  ? 515  HIS   A NE2   1 
ATOM   1882 N  N     . GLU   A 1 367  ? 25.243  -7.652  -74.110 1.00 44.87  ? 516  GLU   A N     1 
ATOM   1883 C  CA    . GLU   A 1 367  ? 24.222  -8.378  -73.315 1.00 47.02  ? 516  GLU   A CA    1 
ATOM   1884 C  C     . GLU   A 1 367  ? 22.893  -8.400  -74.088 1.00 47.84  ? 516  GLU   A C     1 
ATOM   1885 O  O     . GLU   A 1 367  ? 22.074  -9.278  -73.797 1.00 48.07  ? 516  GLU   A O     1 
ATOM   1886 C  CB    . GLU   A 1 367  ? 24.113  -7.786  -71.907 1.00 53.54  ? 516  GLU   A CB    1 
ATOM   1887 C  CG    . GLU   A 1 367  ? 25.262  -8.237  -71.005 1.00 61.55  ? 516  GLU   A CG    1 
ATOM   1888 C  CD    . GLU   A 1 367  ? 25.006  -8.279  -69.506 1.00 70.06  ? 516  GLU   A CD    1 
ATOM   1889 O  OE1   . GLU   A 1 367  ? 23.832  -8.126  -69.092 1.00 80.33  ? 516  GLU   A OE1   1 
ATOM   1890 O  OE2   . GLU   A 1 367  ? 25.991  -8.461  -68.748 1.00 89.15  ? 516  GLU   A OE2   1 
ATOM   1891 N  N     . ARG   A 1 368  ? 22.707  -7.504  -75.064 1.00 44.08  ? 517  ARG   A N     1 
ATOM   1892 C  CA    . ARG   A 1 368  ? 21.465  -7.388  -75.867 1.00 45.53  ? 517  ARG   A CA    1 
ATOM   1893 C  C     . ARG   A 1 368  ? 20.271  -7.287  -74.913 1.00 46.00  ? 517  ARG   A C     1 
ATOM   1894 O  O     . ARG   A 1 368  ? 19.242  -7.883  -75.184 1.00 49.94  ? 517  ARG   A O     1 
ATOM   1895 C  CB    . ARG   A 1 368  ? 21.345  -8.551  -76.862 1.00 43.78  ? 517  ARG   A CB    1 
ATOM   1896 C  CG    . ARG   A 1 368  ? 22.585  -8.752  -77.732 1.00 43.97  ? 517  ARG   A CG    1 
ATOM   1897 C  CD    . ARG   A 1 368  ? 23.052  -7.492  -78.448 1.00 47.10  ? 517  ARG   A CD    1 
ATOM   1898 N  NE    . ARG   A 1 368  ? 21.945  -6.953  -79.227 1.00 48.63  ? 517  ARG   A NE    1 
ATOM   1899 C  CZ    . ARG   A 1 368  ? 21.553  -7.438  -80.402 1.00 48.84  ? 517  ARG   A CZ    1 
ATOM   1900 N  NH1   . ARG   A 1 368  ? 22.212  -8.444  -80.959 1.00 44.05  ? 517  ARG   A NH1   1 
ATOM   1901 N  NH2   . ARG   A 1 368  ? 20.488  -6.930  -81.000 1.00 47.65  ? 517  ARG   A NH2   1 
ATOM   1902 N  N     . ASP   A 1 369  ? 20.433  -6.534  -73.828 1.00 46.61  ? 518  ASP   A N     1 
ATOM   1903 C  CA    . ASP   A 1 369  ? 19.330  -5.990  -72.999 1.00 45.77  ? 518  ASP   A CA    1 
ATOM   1904 C  C     . ASP   A 1 369  ? 18.375  -5.200  -73.910 1.00 45.38  ? 518  ASP   A C     1 
ATOM   1905 O  O     . ASP   A 1 369  ? 18.817  -4.267  -74.618 1.00 43.15  ? 518  ASP   A O     1 
ATOM   1906 C  CB    . ASP   A 1 369  ? 19.928  -5.123  -71.886 1.00 46.62  ? 518  ASP   A CB    1 
ATOM   1907 C  CG    . ASP   A 1 369  ? 18.936  -4.294  -71.088 1.00 50.21  ? 518  ASP   A CG    1 
ATOM   1908 O  OD1   . ASP   A 1 369  ? 18.113  -4.902  -70.367 1.00 54.11  ? 518  ASP   A OD1   1 
ATOM   1909 O  OD2   . ASP   A 1 369  ? 19.008  -3.046  -71.188 1.00 50.38  ? 518  ASP   A OD2   1 
ATOM   1910 N  N     . ILE   A 1 370  ? 17.090  -5.508  -73.863 1.00 43.98  ? 519  ILE   A N     1 
ATOM   1911 C  CA    . ILE   A 1 370  ? 16.106  -4.890  -74.794 1.00 43.39  ? 519  ILE   A CA    1 
ATOM   1912 C  C     . ILE   A 1 370  ? 16.148  -3.363  -74.668 1.00 41.91  ? 519  ILE   A C     1 
ATOM   1913 O  O     . ILE   A 1 370  ? 16.201  -2.696  -75.721 1.00 41.05  ? 519  ILE   A O     1 
ATOM   1914 C  CB    . ILE   A 1 370  ? 14.686  -5.436  -74.586 1.00 44.45  ? 519  ILE   A CB    1 
ATOM   1915 C  CG1   . ILE   A 1 370  ? 13.765  -4.905  -75.687 1.00 44.01  ? 519  ILE   A CG1   1 
ATOM   1916 C  CG2   . ILE   A 1 370  ? 14.154  -5.124  -73.190 1.00 42.94  ? 519  ILE   A CG2   1 
ATOM   1917 C  CD1   . ILE   A 1 370  ? 12.446  -5.593  -75.729 1.00 45.67  ? 519  ILE   A CD1   1 
ATOM   1918 N  N     . ASN   A 1 371  ? 16.116  -2.819  -73.446 1.00 41.37  ? 520  ASN   A N     1 
ATOM   1919 C  CA    . ASN   A 1 371  ? 16.102  -1.346  -73.218 1.00 38.66  ? 520  ASN   A CA    1 
ATOM   1920 C  C     . ASN   A 1 371  ? 17.364  -0.691  -73.792 1.00 36.57  ? 520  ASN   A C     1 
ATOM   1921 O  O     . ASN   A 1 371  ? 17.263  0.442   -74.234 1.00 34.70  ? 520  ASN   A O     1 
ATOM   1922 C  CB    . ASN   A 1 371  ? 15.958  -1.005  -71.745 1.00 40.47  ? 520  ASN   A CB    1 
ATOM   1923 C  CG    . ASN   A 1 371  ? 14.547  -1.184  -71.233 1.00 44.09  ? 520  ASN   A CG    1 
ATOM   1924 O  OD1   . ASN   A 1 371  ? 13.599  -1.357  -72.001 1.00 52.16  ? 520  ASN   A OD1   1 
ATOM   1925 N  ND2   . ASN   A 1 371  ? 14.400  -1.123  -69.926 1.00 47.47  ? 520  ASN   A ND2   1 
ATOM   1926 N  N     . THR   A 1 372  ? 18.507  -1.381  -73.790 1.00 37.87  ? 521  THR   A N     1 
ATOM   1927 C  CA    . THR   A 1 372  ? 19.790  -0.870  -74.344 1.00 40.38  ? 521  THR   A CA    1 
ATOM   1928 C  C     . THR   A 1 372  ? 19.664  -0.820  -75.873 1.00 36.66  ? 521  THR   A C     1 
ATOM   1929 O  O     . THR   A 1 372  ? 20.010  0.193   -76.459 1.00 40.24  ? 521  THR   A O     1 
ATOM   1930 C  CB    . THR   A 1 372  ? 20.984  -1.711  -73.862 1.00 41.65  ? 521  THR   A CB    1 
ATOM   1931 O  OG1   . THR   A 1 372  ? 21.103  -1.646  -72.439 1.00 42.74  ? 521  THR   A OG1   1 
ATOM   1932 C  CG2   . THR   A 1 372  ? 22.287  -1.268  -74.483 1.00 42.51  ? 521  THR   A CG2   1 
ATOM   1933 N  N     . ASP   A 1 373  ? 19.175  -1.889  -76.495 1.00 40.42  ? 522  ASP   A N     1 
ATOM   1934 C  CA    . ASP   A 1 373  ? 18.890  -1.945  -77.960 1.00 39.85  ? 522  ASP   A CA    1 
ATOM   1935 C  C     . ASP   A 1 373  ? 17.986  -0.762  -78.336 1.00 36.98  ? 522  ASP   A C     1 
ATOM   1936 O  O     . ASP   A 1 373  ? 18.339  -0.024  -79.277 1.00 39.13  ? 522  ASP   A O     1 
ATOM   1937 C  CB    . ASP   A 1 373  ? 18.279  -3.292  -78.359 1.00 41.35  ? 522  ASP   A CB    1 
ATOM   1938 C  CG    . ASP   A 1 373  ? 19.285  -4.419  -78.544 1.00 44.48  ? 522  ASP   A CG    1 
ATOM   1939 O  OD1   . ASP   A 1 373  ? 20.485  -4.199  -78.249 1.00 44.78  ? 522  ASP   A OD1   1 
ATOM   1940 O  OD2   . ASP   A 1 373  ? 18.858  -5.516  -78.994 1.00 50.14  ? 522  ASP   A OD2   1 
ATOM   1941 N  N     . PHE   A 1 374  ? 16.898  -0.536  -77.596 1.00 34.66  ? 523  PHE   A N     1 
ATOM   1942 C  CA    . PHE   A 1 374  ? 15.967  0.601   -77.828 1.00 36.23  ? 523  PHE   A CA    1 
ATOM   1943 C  C     . PHE   A 1 374  ? 16.709  1.942   -77.742 1.00 37.57  ? 523  PHE   A C     1 
ATOM   1944 O  O     . PHE   A 1 374  ? 16.602  2.762   -78.656 1.00 38.95  ? 523  PHE   A O     1 
ATOM   1945 C  CB    . PHE   A 1 374  ? 14.812  0.536   -76.833 1.00 37.77  ? 523  PHE   A CB    1 
ATOM   1946 C  CG    . PHE   A 1 374  ? 13.848  1.685   -76.916 1.00 37.83  ? 523  PHE   A CG    1 
ATOM   1947 C  CD1   . PHE   A 1 374  ? 13.216  2.003   -78.100 1.00 43.46  ? 523  PHE   A CD1   1 
ATOM   1948 C  CD2   . PHE   A 1 374  ? 13.537  2.418   -75.793 1.00 41.36  ? 523  PHE   A CD2   1 
ATOM   1949 C  CE1   . PHE   A 1 374  ? 12.321  3.060   -78.160 1.00 44.76  ? 523  PHE   A CE1   1 
ATOM   1950 C  CE2   . PHE   A 1 374  ? 12.634  3.464   -75.856 1.00 43.18  ? 523  PHE   A CE2   1 
ATOM   1951 C  CZ    . PHE   A 1 374  ? 12.030  3.786   -77.038 1.00 40.43  ? 523  PHE   A CZ    1 
ATOM   1952 N  N     . LEU   A 1 375  ? 17.476  2.155   -76.673 1.00 41.26  ? 524  LEU   A N     1 
ATOM   1953 C  CA    . LEU   A 1 375  ? 18.238  3.411   -76.462 1.00 41.53  ? 524  LEU   A CA    1 
ATOM   1954 C  C     . LEU   A 1 375  ? 19.219  3.612   -77.621 1.00 39.97  ? 524  LEU   A C     1 
ATOM   1955 O  O     . LEU   A 1 375  ? 19.408  4.785   -78.041 1.00 38.90  ? 524  LEU   A O     1 
ATOM   1956 C  CB    . LEU   A 1 375  ? 18.992  3.351   -75.128 1.00 42.89  ? 524  LEU   A CB    1 
ATOM   1957 C  CG    . LEU   A 1 375  ? 19.866  4.568   -74.825 1.00 39.13  ? 524  LEU   A CG    1 
ATOM   1958 C  CD1   . LEU   A 1 375  ? 19.007  5.774   -74.529 1.00 37.24  ? 524  LEU   A CD1   1 
ATOM   1959 C  CD2   . LEU   A 1 375  ? 20.818  4.280   -73.678 1.00 40.86  ? 524  LEU   A CD2   1 
ATOM   1960 N  N     . LEU   A 1 376  ? 19.843  2.544   -78.126 1.00 38.72  ? 525  LEU   A N     1 
ATOM   1961 C  CA    . LEU   A 1 376  ? 20.780  2.711   -79.276 1.00 41.07  ? 525  LEU   A CA    1 
ATOM   1962 C  C     . LEU   A 1 376  ? 20.025  3.326   -80.469 1.00 40.43  ? 525  LEU   A C     1 
ATOM   1963 O  O     . LEU   A 1 376  ? 20.634  4.126   -81.183 1.00 44.27  ? 525  LEU   A O     1 
ATOM   1964 C  CB    . LEU   A 1 376  ? 21.470  1.387   -79.615 1.00 38.73  ? 525  LEU   A CB    1 
ATOM   1965 C  CG    . LEU   A 1 376  ? 22.415  0.857   -78.532 1.00 40.70  ? 525  LEU   A CG    1 
ATOM   1966 C  CD1   . LEU   A 1 376  ? 23.010  -0.492  -78.928 1.00 40.37  ? 525  LEU   A CD1   1 
ATOM   1967 C  CD2   . LEU   A 1 376  ? 23.528  1.851   -78.210 1.00 38.60  ? 525  LEU   A CD2   1 
ATOM   1968 N  N     . VAL   A 1 377  ? 18.719  3.076   -80.631 1.00 40.30  ? 526  VAL   A N     1 
ATOM   1969 C  CA    . VAL   A 1 377  ? 17.940  3.682   -81.756 1.00 38.51  ? 526  VAL   A CA    1 
ATOM   1970 C  C     . VAL   A 1 377  ? 17.824  5.169   -81.467 1.00 37.34  ? 526  VAL   A C     1 
ATOM   1971 O  O     . VAL   A 1 377  ? 18.023  5.963   -82.358 1.00 38.60  ? 526  VAL   A O     1 
ATOM   1972 C  CB    . VAL   A 1 377  ? 16.547  3.053   -81.957 1.00 39.75  ? 526  VAL   A CB    1 
ATOM   1973 C  CG1   . VAL   A 1 377  ? 15.871  3.559   -83.220 1.00 40.89  ? 526  VAL   A CG1   1 
ATOM   1974 C  CG2   . VAL   A 1 377  ? 16.607  1.535   -81.946 1.00 41.52  ? 526  VAL   A CG2   1 
ATOM   1975 N  N     . VAL   A 1 378  ? 17.498  5.533   -80.236 1.00 43.37  ? 527  VAL   A N     1 
ATOM   1976 C  CA    . VAL   A 1 378  ? 17.324  6.967   -79.880 1.00 40.80  ? 527  VAL   A CA    1 
ATOM   1977 C  C     . VAL   A 1 378  ? 18.644  7.703   -80.106 1.00 40.62  ? 527  VAL   A C     1 
ATOM   1978 O  O     . VAL   A 1 378  ? 18.604  8.774   -80.686 1.00 43.33  ? 527  VAL   A O     1 
ATOM   1979 C  CB    . VAL   A 1 378  ? 16.830  7.140   -78.442 1.00 38.63  ? 527  VAL   A CB    1 
ATOM   1980 C  CG1   . VAL   A 1 378  ? 16.840  8.611   -78.060 1.00 39.26  ? 527  VAL   A CG1   1 
ATOM   1981 C  CG2   . VAL   A 1 378  ? 15.447  6.528   -78.271 1.00 37.10  ? 527  VAL   A CG2   1 
ATOM   1982 N  N     . LEU   A 1 379  ? 19.764  7.148   -79.653 1.00 42.81  ? 528  LEU   A N     1 
ATOM   1983 C  CA    . LEU   A 1 379  ? 21.054  7.882   -79.636 1.00 46.02  ? 528  LEU   A CA    1 
ATOM   1984 C  C     . LEU   A 1 379  ? 21.596  7.992   -81.058 1.00 49.68  ? 528  LEU   A C     1 
ATOM   1985 O  O     . LEU   A 1 379  ? 22.294  8.964   -81.332 1.00 50.97  ? 528  LEU   A O     1 
ATOM   1986 C  CB    . LEU   A 1 379  ? 22.057  7.179   -78.720 1.00 45.57  ? 528  LEU   A CB    1 
ATOM   1987 C  CG    . LEU   A 1 379  ? 21.740  7.246   -77.233 1.00 45.73  ? 528  LEU   A CG    1 
ATOM   1988 C  CD1   . LEU   A 1 379  ? 22.798  6.496   -76.443 1.00 46.05  ? 528  LEU   A CD1   1 
ATOM   1989 C  CD2   . LEU   A 1 379  ? 21.622  8.688   -76.768 1.00 47.38  ? 528  LEU   A CD2   1 
ATOM   1990 N  N     . ARG   A 1 380  ? 21.302  7.034   -81.935 1.00 55.60  ? 529  ARG   A N     1 
ATOM   1991 C  CA    . ARG   A 1 380  ? 21.750  7.158   -83.341 1.00 53.79  ? 529  ARG   A CA    1 
ATOM   1992 C  C     . ARG   A 1 380  ? 21.085  8.384   -83.964 1.00 51.60  ? 529  ARG   A C     1 
ATOM   1993 O  O     . ARG   A 1 380  ? 21.791  9.113   -84.687 1.00 51.56  ? 529  ARG   A O     1 
ATOM   1994 C  CB    . ARG   A 1 380  ? 21.446  5.932   -84.190 1.00 56.39  ? 529  ARG   A CB    1 
ATOM   1995 C  CG    . ARG   A 1 380  ? 22.031  6.071   -85.583 1.00 58.36  ? 529  ARG   A CG    1 
ATOM   1996 C  CD    . ARG   A 1 380  ? 21.846  4.810   -86.370 1.00 63.44  ? 529  ARG   A CD    1 
ATOM   1997 N  NE    . ARG   A 1 380  ? 20.458  4.642   -86.741 1.00 69.05  ? 529  ARG   A NE    1 
ATOM   1998 C  CZ    . ARG   A 1 380  ? 20.006  3.660   -87.499 1.00 68.91  ? 529  ARG   A CZ    1 
ATOM   1999 N  NH1   . ARG   A 1 380  ? 20.841  2.741   -87.954 1.00 76.22  ? 529  ARG   A NH1   1 
ATOM   2000 N  NH2   . ARG   A 1 380  ? 18.720  3.595   -87.791 1.00 68.64  ? 529  ARG   A NH2   1 
ATOM   2001 N  N     . ASP   A 1 381  ? 19.794  8.604   -83.700 1.00 46.59  ? 530  ASP   A N     1 
ATOM   2002 C  CA    . ASP   A 1 381  ? 19.049  9.783   -84.227 1.00 50.72  ? 530  ASP   A CA    1 
ATOM   2003 C  C     . ASP   A 1 381  ? 19.651  11.069  -83.633 1.00 53.91  ? 530  ASP   A C     1 
ATOM   2004 O  O     . ASP   A 1 381  ? 19.845  12.021  -84.399 1.00 53.62  ? 530  ASP   A O     1 
ATOM   2005 C  CB    . ASP   A 1 381  ? 17.543  9.670   -83.964 1.00 54.69  ? 530  ASP   A CB    1 
ATOM   2006 C  CG    . ASP   A 1 381  ? 16.814  8.583   -84.758 1.00 58.60  ? 530  ASP   A CG    1 
ATOM   2007 O  OD1   . ASP   A 1 381  ? 17.398  8.054   -85.736 1.00 52.55  ? 530  ASP   A OD1   1 
ATOM   2008 O  OD2   . ASP   A 1 381  ? 15.646  8.275   -84.399 1.00 57.33  ? 530  ASP   A OD2   1 
ATOM   2009 N  N     . VAL   A 1 382  ? 19.958  11.079  -82.329 1.00 52.97  ? 531  VAL   A N     1 
ATOM   2010 C  CA    . VAL   A 1 382  ? 20.550  12.241  -81.597 1.00 54.76  ? 531  VAL   A CA    1 
ATOM   2011 C  C     . VAL   A 1 382  ? 21.909  12.602  -82.228 1.00 54.06  ? 531  VAL   A C     1 
ATOM   2012 O  O     . VAL   A 1 382  ? 22.106  13.775  -82.581 1.00 50.70  ? 531  VAL   A O     1 
ATOM   2013 C  CB    . VAL   A 1 382  ? 20.684  11.945  -80.088 1.00 50.22  ? 531  VAL   A CB    1 
ATOM   2014 C  CG1   . VAL   A 1 382  ? 21.573  12.946  -79.377 1.00 53.67  ? 531  VAL   A CG1   1 
ATOM   2015 C  CG2   . VAL   A 1 382  ? 19.335  11.886  -79.400 1.00 50.21  ? 531  VAL   A CG2   1 
ATOM   2016 N  N     . VAL   A 1 383  ? 22.818  11.636  -82.334 1.00 48.08  ? 532  VAL   A N     1 
ATOM   2017 C  CA    . VAL   A 1 383  ? 24.167  11.787  -82.960 1.00 55.03  ? 532  VAL   A CA    1 
ATOM   2018 C  C     . VAL   A 1 383  ? 24.040  12.517  -84.298 1.00 55.60  ? 532  VAL   A C     1 
ATOM   2019 O  O     . VAL   A 1 383  ? 24.863  13.408  -84.555 1.00 60.88  ? 532  VAL   A O     1 
ATOM   2020 C  CB    . VAL   A 1 383  ? 24.842  10.418  -83.182 1.00 60.48  ? 532  VAL   A CB    1 
ATOM   2021 C  CG1   . VAL   A 1 383  ? 25.876  10.455  -84.296 1.00 70.24  ? 532  VAL   A CG1   1 
ATOM   2022 C  CG2   . VAL   A 1 383  ? 25.473  9.897   -81.914 1.00 63.07  ? 532  VAL   A CG2   1 
ATOM   2023 N  N     . GLN   A 1 384  ? 23.102  12.085  -85.144 1.00 59.89  ? 533  GLN   A N     1 
ATOM   2024 C  CA    . GLN   A 1 384  ? 22.949  12.541  -86.555 1.00 61.19  ? 533  GLN   A CA    1 
ATOM   2025 C  C     . GLN   A 1 384  ? 22.578  14.031  -86.569 1.00 55.93  ? 533  GLN   A C     1 
ATOM   2026 O  O     . GLN   A 1 384  ? 23.165  14.775  -87.375 1.00 55.75  ? 533  GLN   A O     1 
ATOM   2027 C  CB    . GLN   A 1 384  ? 21.903  11.676  -87.258 1.00 67.93  ? 533  GLN   A CB    1 
ATOM   2028 C  CG    . GLN   A 1 384  ? 22.007  11.668  -88.775 1.00 78.89  ? 533  GLN   A CG    1 
ATOM   2029 C  CD    . GLN   A 1 384  ? 21.239  10.510  -89.372 1.00 83.00  ? 533  GLN   A CD    1 
ATOM   2030 O  OE1   . GLN   A 1 384  ? 21.726  9.812   -90.261 1.00 82.95  ? 533  GLN   A OE1   1 
ATOM   2031 N  NE2   . GLN   A 1 384  ? 20.035  10.277  -88.867 1.00 77.83  ? 533  GLN   A NE2   1 
ATOM   2032 N  N     . ALA   A 1 385  ? 21.676  14.443  -85.676 1.00 48.80  ? 534  ALA   A N     1 
ATOM   2033 C  CA    . ALA   A 1 385  ? 21.103  15.809  -85.576 1.00 50.47  ? 534  ALA   A CA    1 
ATOM   2034 C  C     . ALA   A 1 385  ? 21.952  16.716  -84.675 1.00 51.84  ? 534  ALA   A C     1 
ATOM   2035 O  O     . ALA   A 1 385  ? 21.775  17.942  -84.779 1.00 59.79  ? 534  ALA   A O     1 
ATOM   2036 C  CB    . ALA   A 1 385  ? 19.688  15.740  -85.049 1.00 46.62  ? 534  ALA   A CB    1 
ATOM   2037 N  N     . TYR   A 1 386  ? 22.796  16.143  -83.806 1.00 54.18  ? 535  TYR   A N     1 
ATOM   2038 C  CA    . TYR   A 1 386  ? 23.620  16.862  -82.795 1.00 49.48  ? 535  TYR   A CA    1 
ATOM   2039 C  C     . TYR   A 1 386  ? 25.003  16.218  -82.693 1.00 49.11  ? 535  TYR   A C     1 
ATOM   2040 O  O     . TYR   A 1 386  ? 25.315  15.529  -81.728 1.00 50.40  ? 535  TYR   A O     1 
ATOM   2041 C  CB    . TYR   A 1 386  ? 22.905  16.841  -81.451 1.00 47.39  ? 535  TYR   A CB    1 
ATOM   2042 C  CG    . TYR   A 1 386  ? 21.513  17.412  -81.464 1.00 50.58  ? 535  TYR   A CG    1 
ATOM   2043 C  CD1   . TYR   A 1 386  ? 21.291  18.781  -81.378 1.00 50.59  ? 535  TYR   A CD1   1 
ATOM   2044 C  CD2   . TYR   A 1 386  ? 20.412  16.578  -81.515 1.00 47.49  ? 535  TYR   A CD2   1 
ATOM   2045 C  CE1   . TYR   A 1 386  ? 20.011  19.307  -81.347 1.00 47.97  ? 535  TYR   A CE1   1 
ATOM   2046 C  CE2   . TYR   A 1 386  ? 19.127  17.089  -81.518 1.00 48.47  ? 535  TYR   A CE2   1 
ATOM   2047 C  CZ    . TYR   A 1 386  ? 18.926  18.455  -81.432 1.00 49.48  ? 535  TYR   A CZ    1 
ATOM   2048 O  OH    . TYR   A 1 386  ? 17.655  18.938  -81.425 1.00 52.18  ? 535  TYR   A OH    1 
ATOM   2049 N  N     . PRO   A 1 387  ? 25.881  16.421  -83.693 1.00 49.87  ? 536  PRO   A N     1 
ATOM   2050 C  CA    . PRO   A 1 387  ? 27.151  15.698  -83.756 1.00 56.16  ? 536  PRO   A CA    1 
ATOM   2051 C  C     . PRO   A 1 387  ? 28.182  16.037  -82.663 1.00 56.60  ? 536  PRO   A C     1 
ATOM   2052 O  O     . PRO   A 1 387  ? 29.123  15.287  -82.533 1.00 50.99  ? 536  PRO   A O     1 
ATOM   2053 C  CB    . PRO   A 1 387  ? 27.703  16.029  -85.153 1.00 55.07  ? 536  PRO   A CB    1 
ATOM   2054 C  CG    . PRO   A 1 387  ? 26.957  17.267  -85.612 1.00 52.14  ? 536  PRO   A CG    1 
ATOM   2055 C  CD    . PRO   A 1 387  ? 25.669  17.324  -84.828 1.00 52.00  ? 536  PRO   A CD    1 
ATOM   2056 N  N     . GLU   A 1 388  ? 27.959  17.098  -81.881 1.00 57.84  ? 537  GLU   A N     1 
ATOM   2057 C  CA    . GLU   A 1 388  ? 28.860  17.540  -80.781 1.00 61.16  ? 537  GLU   A CA    1 
ATOM   2058 C  C     . GLU   A 1 388  ? 28.709  16.607  -79.571 1.00 58.26  ? 537  GLU   A C     1 
ATOM   2059 O  O     . GLU   A 1 388  ? 29.614  16.609  -78.711 1.00 52.21  ? 537  GLU   A O     1 
ATOM   2060 C  CB    . GLU   A 1 388  ? 28.553  18.983  -80.364 1.00 69.12  ? 537  GLU   A CB    1 
ATOM   2061 C  CG    . GLU   A 1 388  ? 28.748  20.009  -81.470 1.00 77.40  ? 537  GLU   A CG    1 
ATOM   2062 C  CD    . GLU   A 1 388  ? 30.193  20.418  -81.696 1.00 91.65  ? 537  GLU   A CD    1 
ATOM   2063 O  OE1   . GLU   A 1 388  ? 30.743  20.065  -82.762 1.00 95.97  ? 537  GLU   A OE1   1 
ATOM   2064 O  OE2   . GLU   A 1 388  ? 30.763  21.097  -80.809 1.00 103.22 ? 537  GLU   A OE2   1 
ATOM   2065 N  N     . VAL   A 1 389  ? 27.596  15.872  -79.467 1.00 49.29  ? 538  VAL   A N     1 
ATOM   2066 C  CA    . VAL   A 1 389  ? 27.398  14.896  -78.365 1.00 45.09  ? 538  VAL   A CA    1 
ATOM   2067 C  C     . VAL   A 1 389  ? 28.510  13.853  -78.489 1.00 46.86  ? 538  VAL   A C     1 
ATOM   2068 O  O     . VAL   A 1 389  ? 29.009  13.663  -79.601 1.00 44.54  ? 538  VAL   A O     1 
ATOM   2069 C  CB    . VAL   A 1 389  ? 26.010  14.239  -78.395 1.00 47.06  ? 538  VAL   A CB    1 
ATOM   2070 C  CG1   . VAL   A 1 389  ? 25.963  13.029  -79.324 1.00 45.84  ? 538  VAL   A CG1   1 
ATOM   2071 C  CG2   . VAL   A 1 389  ? 25.572  13.854  -76.992 1.00 46.91  ? 538  VAL   A CG2   1 
ATOM   2072 N  N     . ARG   A 1 390  ? 28.895  13.212  -77.393 1.00 41.81  ? 539  ARG   A N     1 
ATOM   2073 C  CA    . ARG   A 1 390  ? 29.867  12.099  -77.438 1.00 45.20  ? 539  ARG   A CA    1 
ATOM   2074 C  C     . ARG   A 1 390  ? 29.162  10.839  -76.939 1.00 47.10  ? 539  ARG   A C     1 
ATOM   2075 O  O     . ARG   A 1 390  ? 28.704  10.822  -75.779 1.00 48.90  ? 539  ARG   A O     1 
ATOM   2076 C  CB    . ARG   A 1 390  ? 31.141  12.436  -76.646 1.00 50.00  ? 539  ARG   A CB    1 
ATOM   2077 C  CG    . ARG   A 1 390  ? 32.060  13.455  -77.314 1.00 52.16  ? 539  ARG   A CG    1 
ATOM   2078 C  CD    . ARG   A 1 390  ? 32.032  13.220  -78.804 1.00 55.13  ? 539  ARG   A CD    1 
ATOM   2079 N  NE    . ARG   A 1 390  ? 33.075  13.819  -79.594 1.00 52.43  ? 539  ARG   A NE    1 
ATOM   2080 C  CZ    . ARG   A 1 390  ? 32.867  14.580  -80.647 1.00 53.80  ? 539  ARG   A CZ    1 
ATOM   2081 N  NH1   . ARG   A 1 390  ? 33.899  15.039  -81.331 1.00 67.52  ? 539  ARG   A NH1   1 
ATOM   2082 N  NH2   . ARG   A 1 390  ? 31.644  14.905  -81.014 1.00 54.70  ? 539  ARG   A NH2   1 
ATOM   2083 N  N     . ILE   A 1 391  ? 29.071  9.827   -77.797 1.00 43.33  ? 540  ILE   A N     1 
ATOM   2084 C  CA    . ILE   A 1 391  ? 28.529  8.497   -77.420 1.00 39.79  ? 540  ILE   A CA    1 
ATOM   2085 C  C     . ILE   A 1 391  ? 29.699  7.538   -77.339 1.00 37.71  ? 540  ILE   A C     1 
ATOM   2086 O  O     . ILE   A 1 391  ? 30.485  7.556   -78.262 1.00 39.63  ? 540  ILE   A O     1 
ATOM   2087 C  CB    . ILE   A 1 391  ? 27.513  8.012   -78.458 1.00 40.50  ? 540  ILE   A CB    1 
ATOM   2088 C  CG1   . ILE   A 1 391  ? 26.447  9.070   -78.737 1.00 39.75  ? 540  ILE   A CG1   1 
ATOM   2089 C  CG2   . ILE   A 1 391  ? 26.924  6.676   -78.031 1.00 41.37  ? 540  ILE   A CG2   1 
ATOM   2090 C  CD1   . ILE   A 1 391  ? 25.633  9.467   -77.529 1.00 44.35  ? 540  ILE   A CD1   1 
ATOM   2091 N  N     . VAL   A 1 392  ? 29.743  6.690   -76.320 1.00 36.97  ? 541  VAL   A N     1 
ATOM   2092 C  CA    . VAL   A 1 392  ? 30.782  5.641   -76.159 1.00 34.85  ? 541  VAL   A CA    1 
ATOM   2093 C  C     . VAL   A 1 392  ? 30.082  4.314   -75.857 1.00 38.95  ? 541  VAL   A C     1 
ATOM   2094 O  O     . VAL   A 1 392  ? 29.360  4.226   -74.843 1.00 42.13  ? 541  VAL   A O     1 
ATOM   2095 C  CB    . VAL   A 1 392  ? 31.744  6.039   -75.038 1.00 39.62  ? 541  VAL   A CB    1 
ATOM   2096 C  CG1   . VAL   A 1 392  ? 32.862  5.025   -74.858 1.00 43.25  ? 541  VAL   A CG1   1 
ATOM   2097 C  CG2   . VAL   A 1 392  ? 32.285  7.439   -75.265 1.00 41.78  ? 541  VAL   A CG2   1 
ATOM   2098 N  N     . LEU   A 1 393  ? 30.252  3.319   -76.727 1.00 40.91  ? 542  LEU   A N     1 
ATOM   2099 C  CA    . LEU   A 1 393  ? 29.645  1.982   -76.553 1.00 40.09  ? 542  LEU   A CA    1 
ATOM   2100 C  C     . LEU   A 1 393  ? 30.748  1.060   -76.069 1.00 36.70  ? 542  LEU   A C     1 
ATOM   2101 O  O     . LEU   A 1 393  ? 31.806  1.078   -76.681 1.00 39.58  ? 542  LEU   A O     1 
ATOM   2102 C  CB    . LEU   A 1 393  ? 29.073  1.500   -77.888 1.00 42.76  ? 542  LEU   A CB    1 
ATOM   2103 C  CG    . LEU   A 1 393  ? 28.280  2.540   -78.672 1.00 47.32  ? 542  LEU   A CG    1 
ATOM   2104 C  CD1   . LEU   A 1 393  ? 27.877  1.972   -80.026 1.00 53.22  ? 542  LEU   A CD1   1 
ATOM   2105 C  CD2   . LEU   A 1 393  ? 27.061  3.002   -77.891 1.00 46.67  ? 542  LEU   A CD2   1 
ATOM   2106 N  N     . MET   A 1 394  ? 30.491  0.253   -75.050 1.00 34.27  ? 543  MET   A N     1 
ATOM   2107 C  CA    . MET   A 1 394  ? 31.529  -0.643  -74.500 1.00 38.77  ? 543  MET   A CA    1 
ATOM   2108 C  C     . MET   A 1 394  ? 31.010  -2.078  -74.554 1.00 42.87  ? 543  MET   A C     1 
ATOM   2109 O  O     . MET   A 1 394  ? 29.827  -2.317  -74.193 1.00 43.58  ? 543  MET   A O     1 
ATOM   2110 C  CB    . MET   A 1 394  ? 31.904  -0.198  -73.086 1.00 41.75  ? 543  MET   A CB    1 
ATOM   2111 C  CG    . MET   A 1 394  ? 32.294  1.299   -73.058 1.00 44.23  ? 543  MET   A CG    1 
ATOM   2112 S  SD    . MET   A 1 394  ? 33.394  1.792   -71.702 1.00 48.58  ? 543  MET   A SD    1 
ATOM   2113 C  CE    . MET   A 1 394  ? 32.334  1.478   -70.292 1.00 48.40  ? 543  MET   A CE    1 
ATOM   2114 N  N     . SER   A 1 395  ? 31.863  -2.971  -75.055 1.00 43.86  ? 544  SER   A N     1 
ATOM   2115 C  CA    . SER   A 1 395  ? 31.523  -4.359  -75.428 1.00 45.41  ? 544  SER   A CA    1 
ATOM   2116 C  C     . SER   A 1 395  ? 32.605  -5.307  -74.936 1.00 43.80  ? 544  SER   A C     1 
ATOM   2117 O  O     . SER   A 1 395  ? 33.781  -4.966  -75.078 1.00 49.29  ? 544  SER   A O     1 
ATOM   2118 C  CB    . SER   A 1 395  ? 31.370  -4.477  -76.918 1.00 47.75  ? 544  SER   A CB    1 
ATOM   2119 O  OG    . SER   A 1 395  ? 31.082  -5.824  -77.270 1.00 52.53  ? 544  SER   A OG    1 
ATOM   2120 N  N     . ALA   A 1 396  ? 32.207  -6.483  -74.454 1.00 42.67  ? 545  ALA   A N     1 
ATOM   2121 C  CA    . ALA   A 1 396  ? 33.093  -7.655  -74.318 1.00 46.36  ? 545  ALA   A CA    1 
ATOM   2122 C  C     . ALA   A 1 396  ? 33.676  -7.988  -75.698 1.00 47.75  ? 545  ALA   A C     1 
ATOM   2123 O  O     . ALA   A 1 396  ? 33.400  -7.247  -76.654 1.00 52.09  ? 545  ALA   A O     1 
ATOM   2124 C  CB    . ALA   A 1 396  ? 32.332  -8.813  -73.730 1.00 47.77  ? 545  ALA   A CB    1 
ATOM   2125 N  N     . THR   A 1 397  ? 34.498  -9.029  -75.776 1.00 50.42  ? 546  THR   A N     1 
ATOM   2126 C  CA    . THR   A 1 397  ? 35.129  -9.533  -77.023 1.00 56.42  ? 546  THR   A CA    1 
ATOM   2127 C  C     . THR   A 1 397  ? 34.098  -10.379 -77.781 1.00 51.53  ? 546  THR   A C     1 
ATOM   2128 O  O     . THR   A 1 397  ? 34.031  -11.581 -77.550 1.00 60.72  ? 546  THR   A O     1 
ATOM   2129 C  CB    . THR   A 1 397  ? 36.442  -10.248 -76.686 1.00 57.98  ? 546  THR   A CB    1 
ATOM   2130 O  OG1   . THR   A 1 397  ? 36.266  -10.953 -75.454 1.00 58.99  ? 546  THR   A OG1   1 
ATOM   2131 C  CG2   . THR   A 1 397  ? 37.586  -9.276  -76.534 1.00 60.30  ? 546  THR   A CG2   1 
ATOM   2132 N  N     . ILE   A 1 398  ? 33.281  -9.716  -78.593 1.00 51.96  ? 547  ILE   A N     1 
ATOM   2133 C  CA    . ILE   A 1 398  ? 32.319  -10.305 -79.564 1.00 54.67  ? 547  ILE   A CA    1 
ATOM   2134 C  C     . ILE   A 1 398  ? 32.580  -9.627  -80.909 1.00 57.17  ? 547  ILE   A C     1 
ATOM   2135 O  O     . ILE   A 1 398  ? 33.285  -8.606  -80.921 1.00 64.21  ? 547  ILE   A O     1 
ATOM   2136 C  CB    . ILE   A 1 398  ? 30.856  -10.080 -79.129 1.00 54.12  ? 547  ILE   A CB    1 
ATOM   2137 C  CG1   . ILE   A 1 398  ? 30.537  -8.590  -78.970 1.00 57.56  ? 547  ILE   A CG1   1 
ATOM   2138 C  CG2   . ILE   A 1 398  ? 30.520  -10.879 -77.880 1.00 55.32  ? 547  ILE   A CG2   1 
ATOM   2139 C  CD1   . ILE   A 1 398  ? 29.071  -8.245  -79.124 1.00 60.95  ? 547  ILE   A CD1   1 
ATOM   2140 N  N     . ASP   A 1 399  ? 31.962  -10.125 -81.976 1.00 57.27  ? 548  ASP   A N     1 
ATOM   2141 C  CA    . ASP   A 1 399  ? 31.885  -9.412  -83.272 1.00 59.46  ? 548  ASP   A CA    1 
ATOM   2142 C  C     . ASP   A 1 399  ? 31.016  -8.163  -83.050 1.00 56.78  ? 548  ASP   A C     1 
ATOM   2143 O  O     . ASP   A 1 399  ? 29.812  -8.341  -82.761 1.00 58.27  ? 548  ASP   A O     1 
ATOM   2144 C  CB    . ASP   A 1 399  ? 31.352  -10.346 -84.368 1.00 60.05  ? 548  ASP   A CB    1 
ATOM   2145 C  CG    . ASP   A 1 399  ? 31.518  -9.786  -85.774 1.00 66.00  ? 548  ASP   A CG    1 
ATOM   2146 O  OD1   . ASP   A 1 399  ? 31.670  -8.541  -85.904 1.00 61.73  ? 548  ASP   A OD1   1 
ATOM   2147 O  OD2   . ASP   A 1 399  ? 31.501  -10.595 -86.735 1.00 70.57  ? 548  ASP   A OD2   1 
ATOM   2148 N  N     . THR   A 1 400  ? 31.593  -6.961  -83.173 1.00 54.09  ? 549  THR   A N     1 
ATOM   2149 C  CA    . THR   A 1 400  ? 30.907  -5.652  -82.971 1.00 54.94  ? 549  THR   A CA    1 
ATOM   2150 C  C     . THR   A 1 400  ? 30.631  -4.969  -84.314 1.00 54.06  ? 549  THR   A C     1 
ATOM   2151 O  O     . THR   A 1 400  ? 30.209  -3.789  -84.298 1.00 61.13  ? 549  THR   A O     1 
ATOM   2152 C  CB    . THR   A 1 400  ? 31.720  -4.697  -82.079 1.00 55.43  ? 549  THR   A CB    1 
ATOM   2153 O  OG1   . THR   A 1 400  ? 32.946  -4.372  -82.736 1.00 57.97  ? 549  THR   A OG1   1 
ATOM   2154 C  CG2   . THR   A 1 400  ? 32.018  -5.265  -80.711 1.00 57.68  ? 549  THR   A CG2   1 
ATOM   2155 N  N     . SER   A 1 401  ? 30.846  -5.657  -85.433 1.00 57.18  ? 550  SER   A N     1 
ATOM   2156 C  CA    . SER   A 1 401  ? 30.642  -5.091  -86.797 1.00 58.23  ? 550  SER   A CA    1 
ATOM   2157 C  C     . SER   A 1 401  ? 29.190  -4.619  -86.959 1.00 53.81  ? 550  SER   A C     1 
ATOM   2158 O  O     . SER   A 1 401  ? 28.973  -3.561  -87.601 1.00 57.77  ? 550  SER   A O     1 
ATOM   2159 C  CB    . SER   A 1 401  ? 31.047  -6.077  -87.874 1.00 56.77  ? 550  SER   A CB    1 
ATOM   2160 O  OG    . SER   A 1 401  ? 30.327  -7.286  -87.742 1.00 61.30  ? 550  SER   A OG    1 
ATOM   2161 N  N     . MET   A 1 402  ? 28.231  -5.339  -86.367 1.00 51.97  ? 551  MET   A N     1 
ATOM   2162 C  CA    . MET   A 1 402  ? 26.779  -5.017  -86.459 1.00 53.04  ? 551  MET   A CA    1 
ATOM   2163 C  C     . MET   A 1 402  ? 26.533  -3.624  -85.852 1.00 54.98  ? 551  MET   A C     1 
ATOM   2164 O  O     . MET   A 1 402  ? 25.863  -2.780  -86.516 1.00 55.47  ? 551  MET   A O     1 
ATOM   2165 C  CB    . MET   A 1 402  ? 25.964  -6.098  -85.740 1.00 62.13  ? 551  MET   A CB    1 
ATOM   2166 C  CG    . MET   A 1 402  ? 24.454  -5.952  -85.847 1.00 66.92  ? 551  MET   A CG    1 
ATOM   2167 S  SD    . MET   A 1 402  ? 23.576  -7.154  -84.798 1.00 77.40  ? 551  MET   A SD    1 
ATOM   2168 C  CE    . MET   A 1 402  ? 24.453  -6.994  -83.242 1.00 73.16  ? 551  MET   A CE    1 
ATOM   2169 N  N     . PHE   A 1 403  ? 27.099  -3.353  -84.670 1.00 47.09  ? 552  PHE   A N     1 
ATOM   2170 C  CA    . PHE   A 1 403  ? 26.976  -2.046  -83.967 1.00 46.92  ? 552  PHE   A CA    1 
ATOM   2171 C  C     . PHE   A 1 403  ? 27.779  -0.976  -84.703 1.00 45.37  ? 552  PHE   A C     1 
ATOM   2172 O  O     . PHE   A 1 403  ? 27.318  0.155   -84.853 1.00 47.56  ? 552  PHE   A O     1 
ATOM   2173 C  CB    . PHE   A 1 403  ? 27.513  -2.148  -82.542 1.00 44.58  ? 552  PHE   A CB    1 
ATOM   2174 C  CG    . PHE   A 1 403  ? 26.707  -3.044  -81.656 1.00 42.67  ? 552  PHE   A CG    1 
ATOM   2175 C  CD1   . PHE   A 1 403  ? 25.521  -2.590  -81.100 1.00 41.93  ? 552  PHE   A CD1   1 
ATOM   2176 C  CD2   . PHE   A 1 403  ? 27.116  -4.341  -81.407 1.00 43.02  ? 552  PHE   A CD2   1 
ATOM   2177 C  CE1   . PHE   A 1 403  ? 24.777  -3.413  -80.275 1.00 42.62  ? 552  PHE   A CE1   1 
ATOM   2178 C  CE2   . PHE   A 1 403  ? 26.361  -5.164  -80.590 1.00 46.19  ? 552  PHE   A CE2   1 
ATOM   2179 C  CZ    . PHE   A 1 403  ? 25.196  -4.698  -80.027 1.00 44.90  ? 552  PHE   A CZ    1 
ATOM   2180 N  N     . CYS   A 1 404  ? 28.987  -1.345  -85.107 1.00 44.91  ? 553  CYS   A N     1 
ATOM   2181 C  CA    . CYS   A 1 404  ? 29.934  -0.480  -85.842 1.00 49.64  ? 553  CYS   A CA    1 
ATOM   2182 C  C     . CYS   A 1 404  ? 29.219  0.098   -87.064 1.00 50.12  ? 553  CYS   A C     1 
ATOM   2183 O  O     . CYS   A 1 404  ? 29.177  1.331   -87.172 1.00 55.45  ? 553  CYS   A O     1 
ATOM   2184 C  CB    . CYS   A 1 404  ? 31.173  -1.283  -86.227 1.00 54.53  ? 553  CYS   A CB    1 
ATOM   2185 S  SG    . CYS   A 1 404  ? 32.362  -0.320  -87.182 1.00 58.76  ? 553  CYS   A SG    1 
ATOM   2186 N  N     . GLU   A 1 405  ? 28.632  -0.768  -87.902 1.00 51.46  ? 554  GLU   A N     1 
ATOM   2187 C  CA    . GLU   A 1 405  ? 27.908  -0.392  -89.148 1.00 53.90  ? 554  GLU   A CA    1 
ATOM   2188 C  C     . GLU   A 1 405  ? 26.678  0.442   -88.798 1.00 50.93  ? 554  GLU   A C     1 
ATOM   2189 O  O     . GLU   A 1 405  ? 26.390  1.402   -89.530 1.00 47.26  ? 554  GLU   A O     1 
ATOM   2190 C  CB    . GLU   A 1 405  ? 27.465  -1.624  -89.942 1.00 60.61  ? 554  GLU   A CB    1 
ATOM   2191 C  CG    . GLU   A 1 405  ? 28.585  -2.271  -90.734 1.00 69.44  ? 554  GLU   A CG    1 
ATOM   2192 C  CD    . GLU   A 1 405  ? 28.350  -3.733  -91.083 1.00 81.47  ? 554  GLU   A CD    1 
ATOM   2193 O  OE1   . GLU   A 1 405  ? 29.332  -4.510  -91.059 1.00 85.65  ? 554  GLU   A OE1   1 
ATOM   2194 O  OE2   . GLU   A 1 405  ? 27.186  -4.094  -91.373 1.00 84.32  ? 554  GLU   A OE2   1 
ATOM   2195 N  N     . TYR   A 1 406  ? 25.960  0.067   -87.736 1.00 51.01  ? 555  TYR   A N     1 
ATOM   2196 C  CA    . TYR   A 1 406  ? 24.730  0.770   -87.297 1.00 50.41  ? 555  TYR   A CA    1 
ATOM   2197 C  C     . TYR   A 1 406  ? 25.091  2.230   -87.015 1.00 51.01  ? 555  TYR   A C     1 
ATOM   2198 O  O     . TYR   A 1 406  ? 24.324  3.119   -87.396 1.00 49.61  ? 555  TYR   A O     1 
ATOM   2199 C  CB    . TYR   A 1 406  ? 24.107  0.059   -86.097 1.00 52.87  ? 555  TYR   A CB    1 
ATOM   2200 C  CG    . TYR   A 1 406  ? 22.739  0.545   -85.693 1.00 51.02  ? 555  TYR   A CG    1 
ATOM   2201 C  CD1   . TYR   A 1 406  ? 21.598  0.067   -86.312 1.00 49.23  ? 555  TYR   A CD1   1 
ATOM   2202 C  CD2   . TYR   A 1 406  ? 22.580  1.454   -84.662 1.00 52.05  ? 555  TYR   A CD2   1 
ATOM   2203 C  CE1   . TYR   A 1 406  ? 20.337  0.500   -85.936 1.00 53.27  ? 555  TYR   A CE1   1 
ATOM   2204 C  CE2   . TYR   A 1 406  ? 21.326  1.887   -84.258 1.00 51.37  ? 555  TYR   A CE2   1 
ATOM   2205 C  CZ    . TYR   A 1 406  ? 20.199  1.407   -84.898 1.00 54.89  ? 555  TYR   A CZ    1 
ATOM   2206 O  OH    . TYR   A 1 406  ? 18.962  1.821   -84.501 1.00 51.27  ? 555  TYR   A OH    1 
ATOM   2207 N  N     . PHE   A 1 407  ? 26.258  2.474   -86.409 1.00 54.19  ? 556  PHE   A N     1 
ATOM   2208 C  CA    . PHE   A 1 407  ? 26.735  3.839   -86.050 1.00 55.61  ? 556  PHE   A CA    1 
ATOM   2209 C  C     . PHE   A 1 407  ? 27.751  4.346   -87.084 1.00 58.75  ? 556  PHE   A C     1 
ATOM   2210 O  O     . PHE   A 1 407  ? 28.779  4.926   -86.684 1.00 57.63  ? 556  PHE   A O     1 
ATOM   2211 C  CB    . PHE   A 1 407  ? 27.267  3.833   -84.614 1.00 52.47  ? 556  PHE   A CB    1 
ATOM   2212 C  CG    . PHE   A 1 407  ? 26.184  3.858   -83.574 1.00 46.90  ? 556  PHE   A CG    1 
ATOM   2213 C  CD1   . PHE   A 1 407  ? 25.564  5.052   -83.241 1.00 41.59  ? 556  PHE   A CD1   1 
ATOM   2214 C  CD2   . PHE   A 1 407  ? 25.775  2.688   -82.942 1.00 44.29  ? 556  PHE   A CD2   1 
ATOM   2215 C  CE1   . PHE   A 1 407  ? 24.543  5.077   -82.304 1.00 41.36  ? 556  PHE   A CE1   1 
ATOM   2216 C  CE2   . PHE   A 1 407  ? 24.769  2.723   -81.989 1.00 43.41  ? 556  PHE   A CE2   1 
ATOM   2217 C  CZ    . PHE   A 1 407  ? 24.147  3.914   -81.680 1.00 40.68  ? 556  PHE   A CZ    1 
ATOM   2218 N  N     . PHE   A 1 408  ? 27.466  4.136   -88.378 1.00 69.05  ? 557  PHE   A N     1 
ATOM   2219 C  CA    . PHE   A 1 408  ? 28.143  4.796   -89.531 1.00 69.36  ? 557  PHE   A CA    1 
ATOM   2220 C  C     . PHE   A 1 408  ? 29.641  4.449   -89.557 1.00 64.68  ? 557  PHE   A C     1 
ATOM   2221 O  O     . PHE   A 1 408  ? 30.475  5.352   -89.748 1.00 72.92  ? 557  PHE   A O     1 
ATOM   2222 C  CB    . PHE   A 1 408  ? 27.910  6.311   -89.457 1.00 73.01  ? 557  PHE   A CB    1 
ATOM   2223 C  CG    . PHE   A 1 408  ? 26.491  6.711   -89.135 1.00 76.13  ? 557  PHE   A CG    1 
ATOM   2224 C  CD1   . PHE   A 1 408  ? 25.437  6.290   -89.937 1.00 77.48  ? 557  PHE   A CD1   1 
ATOM   2225 C  CD2   . PHE   A 1 408  ? 26.207  7.491   -88.021 1.00 77.80  ? 557  PHE   A CD2   1 
ATOM   2226 C  CE1   . PHE   A 1 408  ? 24.130  6.651   -89.640 1.00 79.35  ? 557  PHE   A CE1   1 
ATOM   2227 C  CE2   . PHE   A 1 408  ? 24.902  7.855   -87.726 1.00 78.96  ? 557  PHE   A CE2   1 
ATOM   2228 C  CZ    . PHE   A 1 408  ? 23.866  7.438   -88.539 1.00 83.36  ? 557  PHE   A CZ    1 
ATOM   2229 N  N     . ASN   A 1 409  ? 29.975  3.172   -89.375 1.00 65.00  ? 558  ASN   A N     1 
ATOM   2230 C  CA    . ASN   A 1 409  ? 31.374  2.655   -89.310 1.00 72.59  ? 558  ASN   A CA    1 
ATOM   2231 C  C     . ASN   A 1 409  ? 32.215  3.565   -88.409 1.00 68.77  ? 558  ASN   A C     1 
ATOM   2232 O  O     . ASN   A 1 409  ? 33.172  4.197   -88.902 1.00 70.73  ? 558  ASN   A O     1 
ATOM   2233 C  CB    . ASN   A 1 409  ? 31.979  2.485   -90.705 1.00 70.35  ? 558  ASN   A CB    1 
ATOM   2234 C  CG    . ASN   A 1 409  ? 31.167  1.509   -91.526 1.00 73.83  ? 558  ASN   A CG    1 
ATOM   2235 O  OD1   . ASN   A 1 409  ? 31.191  0.304   -91.267 1.00 77.56  ? 558  ASN   A OD1   1 
ATOM   2236 N  ND2   . ASN   A 1 409  ? 30.403  2.031   -92.472 1.00 68.50  ? 558  ASN   A ND2   1 
ATOM   2237 N  N     . CYS   A 1 410  ? 31.842  3.631   -87.133 1.00 61.12  ? 559  CYS   A N     1 
ATOM   2238 C  CA    . CYS   A 1 410  ? 32.576  4.356   -86.071 1.00 57.51  ? 559  CYS   A CA    1 
ATOM   2239 C  C     . CYS   A 1 410  ? 33.828  3.562   -85.712 1.00 55.18  ? 559  CYS   A C     1 
ATOM   2240 O  O     . CYS   A 1 410  ? 33.878  2.351   -85.908 1.00 57.58  ? 559  CYS   A O     1 
ATOM   2241 C  CB    . CYS   A 1 410  ? 31.695  4.541   -84.843 1.00 58.42  ? 559  CYS   A CB    1 
ATOM   2242 S  SG    . CYS   A 1 410  ? 31.334  2.976   -84.014 1.00 55.79  ? 559  CYS   A SG    1 
ATOM   2243 N  N     . PRO   A 1 411  ? 34.893  4.207   -85.188 1.00 54.75  ? 560  PRO   A N     1 
ATOM   2244 C  CA    . PRO   A 1 411  ? 36.095  3.479   -84.785 1.00 49.84  ? 560  PRO   A CA    1 
ATOM   2245 C  C     . PRO   A 1 411  ? 35.867  2.466   -83.655 1.00 49.39  ? 560  PRO   A C     1 
ATOM   2246 O  O     . PRO   A 1 411  ? 34.997  2.657   -82.834 1.00 51.44  ? 560  PRO   A O     1 
ATOM   2247 C  CB    . PRO   A 1 411  ? 37.020  4.593   -84.287 1.00 54.40  ? 560  PRO   A CB    1 
ATOM   2248 C  CG    . PRO   A 1 411  ? 36.519  5.836   -84.997 1.00 54.84  ? 560  PRO   A CG    1 
ATOM   2249 C  CD    . PRO   A 1 411  ? 35.020  5.660   -85.001 1.00 54.95  ? 560  PRO   A CD    1 
ATOM   2250 N  N     . ILE   A 1 412  ? 36.687  1.423   -83.627 1.00 51.14  ? 561  ILE   A N     1 
ATOM   2251 C  CA    . ILE   A 1 412  ? 36.707  0.396   -82.549 1.00 51.40  ? 561  ILE   A CA    1 
ATOM   2252 C  C     . ILE   A 1 412  ? 38.084  0.430   -81.878 1.00 54.15  ? 561  ILE   A C     1 
ATOM   2253 O  O     . ILE   A 1 412  ? 39.070  0.039   -82.532 1.00 52.34  ? 561  ILE   A O     1 
ATOM   2254 C  CB    . ILE   A 1 412  ? 36.410  -0.990  -83.131 1.00 50.36  ? 561  ILE   A CB    1 
ATOM   2255 C  CG1   . ILE   A 1 412  ? 35.116  -0.988  -83.955 1.00 54.06  ? 561  ILE   A CG1   1 
ATOM   2256 C  CG2   . ILE   A 1 412  ? 36.418  -2.034  -82.025 1.00 51.80  ? 561  ILE   A CG2   1 
ATOM   2257 C  CD1   . ILE   A 1 412  ? 34.849  -2.294  -84.690 1.00 52.82  ? 561  ILE   A CD1   1 
ATOM   2258 N  N     . ILE   A 1 413  ? 38.145  0.852   -80.615 1.00 51.34  ? 562  ILE   A N     1 
ATOM   2259 C  CA    . ILE   A 1 413  ? 39.399  0.835   -79.818 1.00 48.43  ? 562  ILE   A CA    1 
ATOM   2260 C  C     . ILE   A 1 413  ? 39.478  -0.517  -79.121 1.00 51.11  ? 562  ILE   A C     1 
ATOM   2261 O  O     . ILE   A 1 413  ? 38.641  -0.778  -78.230 1.00 50.85  ? 562  ILE   A O     1 
ATOM   2262 C  CB    . ILE   A 1 413  ? 39.442  2.011   -78.832 1.00 52.15  ? 562  ILE   A CB    1 
ATOM   2263 C  CG1   . ILE   A 1 413  ? 39.025  3.325   -79.497 1.00 55.91  ? 562  ILE   A CG1   1 
ATOM   2264 C  CG2   . ILE   A 1 413  ? 40.815  2.113   -78.199 1.00 53.46  ? 562  ILE   A CG2   1 
ATOM   2265 C  CD1   . ILE   A 1 413  ? 39.648  3.551   -80.860 1.00 61.61  ? 562  ILE   A CD1   1 
ATOM   2266 N  N     . GLU   A 1 414  ? 40.429  -1.353  -79.536 1.00 53.50  ? 563  GLU   A N     1 
ATOM   2267 C  CA    . GLU   A 1 414  ? 40.687  -2.677  -78.911 1.00 56.97  ? 563  GLU   A CA    1 
ATOM   2268 C  C     . GLU   A 1 414  ? 41.469  -2.461  -77.609 1.00 58.46  ? 563  GLU   A C     1 
ATOM   2269 O  O     . GLU   A 1 414  ? 42.391  -1.611  -77.586 1.00 69.99  ? 563  GLU   A O     1 
ATOM   2270 C  CB    . GLU   A 1 414  ? 41.444  -3.613  -79.859 1.00 57.78  ? 563  GLU   A CB    1 
ATOM   2271 C  CG    . GLU   A 1 414  ? 40.744  -3.850  -81.195 1.00 59.87  ? 563  GLU   A CG    1 
ATOM   2272 C  CD    . GLU   A 1 414  ? 39.478  -4.698  -81.147 1.00 62.27  ? 563  GLU   A CD    1 
ATOM   2273 O  OE1   . GLU   A 1 414  ? 39.132  -5.192  -80.045 1.00 52.98  ? 563  GLU   A OE1   1 
ATOM   2274 O  OE2   . GLU   A 1 414  ? 38.839  -4.875  -82.215 1.00 65.51  ? 563  GLU   A OE2   1 
ATOM   2275 N  N     . VAL   A 1 415  ? 41.113  -3.221  -76.575 1.00 52.16  ? 564  VAL   A N     1 
ATOM   2276 C  CA    . VAL   A 1 415  ? 41.676  -3.137  -75.204 1.00 53.71  ? 564  VAL   A CA    1 
ATOM   2277 C  C     . VAL   A 1 415  ? 41.902  -4.583  -74.741 1.00 59.08  ? 564  VAL   A C     1 
ATOM   2278 O  O     . VAL   A 1 415  ? 40.989  -5.405  -74.916 1.00 54.85  ? 564  VAL   A O     1 
ATOM   2279 C  CB    . VAL   A 1 415  ? 40.710  -2.326  -74.318 1.00 57.55  ? 564  VAL   A CB    1 
ATOM   2280 C  CG1   . VAL   A 1 415  ? 40.809  -2.677  -72.842 1.00 62.18  ? 564  VAL   A CG1   1 
ATOM   2281 C  CG2   . VAL   A 1 415  ? 40.868  -0.829  -74.548 1.00 50.65  ? 564  VAL   A CG2   1 
ATOM   2282 N  N     . TYR   A 1 416  ? 43.105  -4.898  -74.249 1.00 57.95  ? 565  TYR   A N     1 
ATOM   2283 C  CA    . TYR   A 1 416  ? 43.537  -6.266  -73.858 1.00 59.50  ? 565  TYR   A CA    1 
ATOM   2284 C  C     . TYR   A 1 416  ? 44.651  -6.166  -72.814 1.00 62.49  ? 565  TYR   A C     1 
ATOM   2285 O  O     . TYR   A 1 416  ? 45.320  -5.104  -72.728 1.00 58.67  ? 565  TYR   A O     1 
ATOM   2286 C  CB    . TYR   A 1 416  ? 44.069  -7.028  -75.075 1.00 61.62  ? 565  TYR   A CB    1 
ATOM   2287 C  CG    . TYR   A 1 416  ? 45.013  -6.195  -75.906 1.00 64.88  ? 565  TYR   A CG    1 
ATOM   2288 C  CD1   . TYR   A 1 416  ? 46.368  -6.120  -75.606 1.00 65.29  ? 565  TYR   A CD1   1 
ATOM   2289 C  CD2   . TYR   A 1 416  ? 44.530  -5.406  -76.936 1.00 58.49  ? 565  TYR   A CD2   1 
ATOM   2290 C  CE1   . TYR   A 1 416  ? 47.224  -5.316  -76.345 1.00 68.97  ? 565  TYR   A CE1   1 
ATOM   2291 C  CE2   . TYR   A 1 416  ? 45.368  -4.595  -77.679 1.00 63.00  ? 565  TYR   A CE2   1 
ATOM   2292 C  CZ    . TYR   A 1 416  ? 46.720  -4.549  -77.386 1.00 68.12  ? 565  TYR   A CZ    1 
ATOM   2293 O  OH    . TYR   A 1 416  ? 47.531  -3.732  -78.123 1.00 63.78  ? 565  TYR   A OH    1 
ATOM   2294 N  N     . GLY   A 1 417  ? 44.846  -7.257  -72.070 1.00 63.31  ? 566  GLY   A N     1 
ATOM   2295 C  CA    . GLY   A 1 417  ? 45.994  -7.476  -71.174 1.00 65.83  ? 566  GLY   A CA    1 
ATOM   2296 C  C     . GLY   A 1 417  ? 46.312  -8.952  -71.073 1.00 65.58  ? 566  GLY   A C     1 
ATOM   2297 O  O     . GLY   A 1 417  ? 45.827  -9.719  -71.908 1.00 52.88  ? 566  GLY   A O     1 
ATOM   2298 N  N     . ARG   A 1 418  ? 47.078  -9.342  -70.059 1.00 75.21  ? 567  ARG   A N     1 
ATOM   2299 C  CA    . ARG   A 1 418  ? 47.472  -10.753 -69.827 1.00 76.78  ? 567  ARG   A CA    1 
ATOM   2300 C  C     . ARG   A 1 418  ? 46.216  -11.622 -69.713 1.00 70.77  ? 567  ARG   A C     1 
ATOM   2301 O  O     . ARG   A 1 418  ? 45.259  -11.211 -69.043 1.00 78.21  ? 567  ARG   A O     1 
ATOM   2302 C  CB    . ARG   A 1 418  ? 48.317  -10.875 -68.554 1.00 84.98  ? 567  ARG   A CB    1 
ATOM   2303 C  CG    . ARG   A 1 418  ? 48.919  -12.255 -68.325 1.00 88.34  ? 567  ARG   A CG    1 
ATOM   2304 C  CD    . ARG   A 1 418  ? 50.325  -12.126 -67.762 1.00 95.93  ? 567  ARG   A CD    1 
ATOM   2305 N  NE    . ARG   A 1 418  ? 51.104  -13.352 -67.652 1.00 83.68  ? 567  ARG   A NE    1 
ATOM   2306 C  CZ    . ARG   A 1 418  ? 51.422  -14.141 -68.663 1.00 83.22  ? 567  ARG   A CZ    1 
ATOM   2307 N  NH1   . ARG   A 1 418  ? 51.004  -13.868 -69.888 1.00 91.59  ? 567  ARG   A NH1   1 
ATOM   2308 N  NH2   . ARG   A 1 418  ? 52.144  -15.223 -68.441 1.00 85.94  ? 567  ARG   A NH2   1 
ATOM   2309 N  N     . THR   A 1 419  ? 46.233  -12.772 -70.379 1.00 69.43  ? 568  THR   A N     1 
ATOM   2310 C  CA    . THR   A 1 419  ? 45.327  -13.917 -70.140 1.00 74.06  ? 568  THR   A CA    1 
ATOM   2311 C  C     . THR   A 1 419  ? 46.199  -15.175 -70.148 1.00 79.46  ? 568  THR   A C     1 
ATOM   2312 O  O     . THR   A 1 419  ? 47.249  -15.146 -70.815 1.00 78.91  ? 568  THR   A O     1 
ATOM   2313 C  CB    . THR   A 1 419  ? 44.191  -13.947 -71.172 1.00 82.07  ? 568  THR   A CB    1 
ATOM   2314 O  OG1   . THR   A 1 419  ? 44.750  -13.707 -72.465 1.00 78.81  ? 568  THR   A OG1   1 
ATOM   2315 C  CG2   . THR   A 1 419  ? 43.106  -12.928 -70.882 1.00 80.82  ? 568  THR   A CG2   1 
ATOM   2316 N  N     . TYR   A 1 420  ? 45.803  -16.203 -69.397 1.00 76.24  ? 569  TYR   A N     1 
ATOM   2317 C  CA    . TYR   A 1 420  ? 46.477  -17.526 -69.335 1.00 75.10  ? 569  TYR   A CA    1 
ATOM   2318 C  C     . TYR   A 1 420  ? 45.579  -18.550 -70.021 1.00 71.81  ? 569  TYR   A C     1 
ATOM   2319 O  O     . TYR   A 1 420  ? 44.367  -18.383 -70.069 1.00 79.82  ? 569  TYR   A O     1 
ATOM   2320 C  CB    . TYR   A 1 420  ? 46.785  -17.901 -67.880 1.00 74.10  ? 569  TYR   A CB    1 
ATOM   2321 C  CG    . TYR   A 1 420  ? 47.501  -16.827 -67.103 1.00 67.95  ? 569  TYR   A CG    1 
ATOM   2322 C  CD1   . TYR   A 1 420  ? 46.801  -15.799 -66.505 1.00 64.96  ? 569  TYR   A CD1   1 
ATOM   2323 C  CD2   . TYR   A 1 420  ? 48.884  -16.829 -66.975 1.00 70.60  ? 569  TYR   A CD2   1 
ATOM   2324 C  CE1   . TYR   A 1 420  ? 47.452  -14.797 -65.802 1.00 70.37  ? 569  TYR   A CE1   1 
ATOM   2325 C  CE2   . TYR   A 1 420  ? 49.551  -15.834 -66.275 1.00 65.89  ? 569  TYR   A CE2   1 
ATOM   2326 C  CZ    . TYR   A 1 420  ? 48.832  -14.811 -65.687 1.00 67.71  ? 569  TYR   A CZ    1 
ATOM   2327 O  OH    . TYR   A 1 420  ? 49.468  -13.811 -65.005 1.00 64.68  ? 569  TYR   A OH    1 
ATOM   2328 N  N     . PRO   A 1 421  ? 46.129  -19.635 -70.599 1.00 75.18  ? 570  PRO   A N     1 
ATOM   2329 C  CA    . PRO   A 1 421  ? 45.286  -20.701 -71.136 1.00 72.61  ? 570  PRO   A CA    1 
ATOM   2330 C  C     . PRO   A 1 421  ? 44.461  -21.380 -70.028 1.00 66.58  ? 570  PRO   A C     1 
ATOM   2331 O  O     . PRO   A 1 421  ? 44.865  -21.388 -68.875 1.00 62.51  ? 570  PRO   A O     1 
ATOM   2332 C  CB    . PRO   A 1 421  ? 46.290  -21.670 -71.783 1.00 81.02  ? 570  PRO   A CB    1 
ATOM   2333 C  CG    . PRO   A 1 421  ? 47.614  -21.369 -71.097 1.00 81.72  ? 570  PRO   A CG    1 
ATOM   2334 C  CD    . PRO   A 1 421  ? 47.566  -19.886 -70.790 1.00 82.64  ? 570  PRO   A CD    1 
ATOM   2335 N  N     . VAL   A 1 422  ? 43.310  -21.928 -70.399 1.00 58.65  ? 571  VAL   A N     1 
ATOM   2336 C  CA    . VAL   A 1 422  ? 42.383  -22.599 -69.448 1.00 63.63  ? 571  VAL   A CA    1 
ATOM   2337 C  C     . VAL   A 1 422  ? 42.076  -23.974 -70.031 1.00 67.61  ? 571  VAL   A C     1 
ATOM   2338 O  O     . VAL   A 1 422  ? 41.578  -24.031 -71.175 1.00 64.59  ? 571  VAL   A O     1 
ATOM   2339 C  CB    . VAL   A 1 422  ? 41.099  -21.775 -69.191 1.00 59.42  ? 571  VAL   A CB    1 
ATOM   2340 C  CG1   . VAL   A 1 422  ? 40.150  -22.455 -68.207 1.00 59.84  ? 571  VAL   A CG1   1 
ATOM   2341 C  CG2   . VAL   A 1 422  ? 41.414  -20.366 -68.719 1.00 55.66  ? 571  VAL   A CG2   1 
ATOM   2342 N  N     . GLN   A 1 423  ? 42.399  -25.031 -69.280 1.00 74.48  ? 572  GLN   A N     1 
ATOM   2343 C  CA    . GLN   A 1 423  ? 42.027  -26.425 -69.640 1.00 78.37  ? 572  GLN   A CA    1 
ATOM   2344 C  C     . GLN   A 1 423  ? 40.510  -26.550 -69.447 1.00 66.50  ? 572  GLN   A C     1 
ATOM   2345 O  O     . GLN   A 1 423  ? 40.024  -26.219 -68.346 1.00 73.45  ? 572  GLN   A O     1 
ATOM   2346 C  CB    . GLN   A 1 423  ? 42.859  -27.428 -68.831 1.00 80.45  ? 572  GLN   A CB    1 
ATOM   2347 C  CG    . GLN   A 1 423  ? 42.576  -28.886 -69.181 1.00 90.95  ? 572  GLN   A CG    1 
ATOM   2348 C  CD    . GLN   A 1 423  ? 42.730  -29.218 -70.649 1.00 93.36  ? 572  GLN   A CD    1 
ATOM   2349 O  OE1   . GLN   A 1 423  ? 41.815  -29.745 -71.283 1.00 89.25  ? 572  GLN   A OE1   1 
ATOM   2350 N  NE2   . GLN   A 1 423  ? 43.894  -28.915 -71.203 1.00 89.21  ? 572  GLN   A NE2   1 
ATOM   2351 N  N     . GLU   A 1 424  ? 39.776  -26.931 -70.496 1.00 65.48  ? 573  GLU   A N     1 
ATOM   2352 C  CA    . GLU   A 1 424  ? 38.298  -27.059 -70.431 1.00 68.12  ? 573  GLU   A CA    1 
ATOM   2353 C  C     . GLU   A 1 424  ? 37.938  -28.543 -70.483 1.00 62.07  ? 573  GLU   A C     1 
ATOM   2354 O  O     . GLU   A 1 424  ? 38.600  -29.299 -71.208 1.00 57.33  ? 573  GLU   A O     1 
ATOM   2355 C  CB    . GLU   A 1 424  ? 37.602  -26.163 -71.461 1.00 76.04  ? 573  GLU   A CB    1 
ATOM   2356 C  CG    . GLU   A 1 424  ? 37.601  -26.637 -72.902 1.00 91.48  ? 573  GLU   A CG    1 
ATOM   2357 C  CD    . GLU   A 1 424  ? 36.850  -25.688 -73.838 1.00 98.69  ? 573  GLU   A CD    1 
ATOM   2358 O  OE1   . GLU   A 1 424  ? 35.722  -25.247 -73.476 1.00 87.90  ? 573  GLU   A OE1   1 
ATOM   2359 O  OE2   . GLU   A 1 424  ? 37.397  -25.366 -74.919 1.00 97.07  ? 573  GLU   A OE2   1 
ATOM   2360 N  N     . TYR   A 1 425  ? 36.966  -28.928 -69.658 1.00 58.86  ? 574  TYR   A N     1 
ATOM   2361 C  CA    . TYR   A 1 425  ? 36.487  -30.318 -69.447 1.00 62.58  ? 574  TYR   A CA    1 
ATOM   2362 C  C     . TYR   A 1 425  ? 34.972  -30.334 -69.667 1.00 60.52  ? 574  TYR   A C     1 
ATOM   2363 O  O     . TYR   A 1 425  ? 34.321  -29.280 -69.462 1.00 65.68  ? 574  TYR   A O     1 
ATOM   2364 C  CB    . TYR   A 1 425  ? 36.834  -30.804 -68.033 1.00 65.91  ? 574  TYR   A CB    1 
ATOM   2365 C  CG    . TYR   A 1 425  ? 38.307  -30.915 -67.709 1.00 68.95  ? 574  TYR   A CG    1 
ATOM   2366 C  CD1   . TYR   A 1 425  ? 39.150  -31.756 -68.425 1.00 69.07  ? 574  TYR   A CD1   1 
ATOM   2367 C  CD2   . TYR   A 1 425  ? 38.852  -30.214 -66.643 1.00 72.16  ? 574  TYR   A CD2   1 
ATOM   2368 C  CE1   . TYR   A 1 425  ? 40.495  -31.881 -68.108 1.00 70.91  ? 574  TYR   A CE1   1 
ATOM   2369 C  CE2   . TYR   A 1 425  ? 40.194  -30.330 -66.311 1.00 78.26  ? 574  TYR   A CE2   1 
ATOM   2370 C  CZ    . TYR   A 1 425  ? 41.019  -31.170 -67.042 1.00 75.12  ? 574  TYR   A CZ    1 
ATOM   2371 O  OH    . TYR   A 1 425  ? 42.343  -31.263 -66.717 1.00 74.36  ? 574  TYR   A OH    1 
ATOM   2372 N  N     . PHE   A 1 426  ? 34.417  -31.474 -70.071 1.00 52.76  ? 575  PHE   A N     1 
ATOM   2373 C  CA    . PHE   A 1 426  ? 32.952  -31.641 -70.252 1.00 56.04  ? 575  PHE   A CA    1 
ATOM   2374 C  C     . PHE   A 1 426  ? 32.437  -32.697 -69.268 1.00 56.34  ? 575  PHE   A C     1 
ATOM   2375 O  O     . PHE   A 1 426  ? 33.248  -33.275 -68.514 1.00 55.00  ? 575  PHE   A O     1 
ATOM   2376 C  CB    . PHE   A 1 426  ? 32.642  -31.865 -71.734 1.00 61.04  ? 575  PHE   A CB    1 
ATOM   2377 C  CG    . PHE   A 1 426  ? 32.855  -30.616 -72.557 1.00 61.93  ? 575  PHE   A CG    1 
ATOM   2378 C  CD1   . PHE   A 1 426  ? 31.855  -29.660 -72.670 1.00 60.52  ? 575  PHE   A CD1   1 
ATOM   2379 C  CD2   . PHE   A 1 426  ? 34.079  -30.361 -73.159 1.00 62.19  ? 575  PHE   A CD2   1 
ATOM   2380 C  CE1   . PHE   A 1 426  ? 32.067  -28.494 -73.390 1.00 59.95  ? 575  PHE   A CE1   1 
ATOM   2381 C  CE2   . PHE   A 1 426  ? 34.282  -29.197 -73.891 1.00 65.26  ? 575  PHE   A CE2   1 
ATOM   2382 C  CZ    . PHE   A 1 426  ? 33.277  -28.265 -74.001 1.00 58.98  ? 575  PHE   A CZ    1 
ATOM   2383 N  N     . LEU   A 1 427  ? 31.114  -32.883 -69.218 1.00 55.04  ? 576  LEU   A N     1 
ATOM   2384 C  CA    . LEU   A 1 427  ? 30.437  -33.698 -68.177 1.00 55.01  ? 576  LEU   A CA    1 
ATOM   2385 C  C     . LEU   A 1 427  ? 31.160  -35.044 -68.019 1.00 65.30  ? 576  LEU   A C     1 
ATOM   2386 O  O     . LEU   A 1 427  ? 31.389  -35.454 -66.857 1.00 68.66  ? 576  LEU   A O     1 
ATOM   2387 C  CB    . LEU   A 1 427  ? 28.971  -33.877 -68.569 1.00 50.69  ? 576  LEU   A CB    1 
ATOM   2388 C  CG    . LEU   A 1 427  ? 28.103  -34.707 -67.619 1.00 52.86  ? 576  LEU   A CG    1 
ATOM   2389 C  CD1   . LEU   A 1 427  ? 28.452  -34.469 -66.150 1.00 49.18  ? 576  LEU   A CD1   1 
ATOM   2390 C  CD2   . LEU   A 1 427  ? 26.622  -34.419 -67.869 1.00 52.18  ? 576  LEU   A CD2   1 
ATOM   2391 N  N     . GLU   A 1 428  ? 31.509  -35.693 -69.139 1.00 69.23  ? 577  GLU   A N     1 
ATOM   2392 C  CA    . GLU   A 1 428  ? 32.147  -37.036 -69.157 1.00 72.34  ? 577  GLU   A CA    1 
ATOM   2393 C  C     . GLU   A 1 428  ? 33.557  -36.921 -68.566 1.00 71.86  ? 577  GLU   A C     1 
ATOM   2394 O  O     . GLU   A 1 428  ? 33.918  -37.827 -67.791 1.00 70.59  ? 577  GLU   A O     1 
ATOM   2395 C  CB    . GLU   A 1 428  ? 32.160  -37.696 -70.547 1.00 76.14  ? 577  GLU   A CB    1 
ATOM   2396 C  CG    . GLU   A 1 428  ? 32.560  -36.796 -71.715 1.00 82.10  ? 577  GLU   A CG    1 
ATOM   2397 C  CD    . GLU   A 1 428  ? 31.390  -36.270 -72.541 1.00 76.41  ? 577  GLU   A CD    1 
ATOM   2398 O  OE1   . GLU   A 1 428  ? 30.466  -35.679 -71.941 1.00 61.98  ? 577  GLU   A OE1   1 
ATOM   2399 O  OE2   . GLU   A 1 428  ? 31.392  -36.474 -73.775 1.00 71.50  ? 577  GLU   A OE2   1 
ATOM   2400 N  N     . ASP   A 1 429  ? 34.315  -35.868 -68.902 1.00 68.52  ? 578  ASP   A N     1 
ATOM   2401 C  CA    . ASP   A 1 429  ? 35.646  -35.604 -68.286 1.00 63.04  ? 578  ASP   A CA    1 
ATOM   2402 C  C     . ASP   A 1 429  ? 35.488  -35.503 -66.766 1.00 62.06  ? 578  ASP   A C     1 
ATOM   2403 O  O     . ASP   A 1 429  ? 36.308  -36.100 -66.046 1.00 61.14  ? 578  ASP   A O     1 
ATOM   2404 C  CB    . ASP   A 1 429  ? 36.289  -34.322 -68.807 1.00 64.23  ? 578  ASP   A CB    1 
ATOM   2405 C  CG    . ASP   A 1 429  ? 36.826  -34.446 -70.215 1.00 73.71  ? 578  ASP   A CG    1 
ATOM   2406 O  OD1   . ASP   A 1 429  ? 36.902  -35.579 -70.703 1.00 76.81  ? 578  ASP   A OD1   1 
ATOM   2407 O  OD2   . ASP   A 1 429  ? 37.196  -33.405 -70.798 1.00 84.61  ? 578  ASP   A OD2   1 
ATOM   2408 N  N     . CYS   A 1 430  ? 34.468  -34.776 -66.306 1.00 64.05  ? 579  CYS   A N     1 
ATOM   2409 C  CA    . CYS   A 1 430  ? 34.180  -34.521 -64.868 1.00 66.31  ? 579  CYS   A CA    1 
ATOM   2410 C  C     . CYS   A 1 430  ? 33.884  -35.846 -64.151 1.00 68.43  ? 579  CYS   A C     1 
ATOM   2411 O  O     . CYS   A 1 430  ? 34.373  -36.030 -63.009 1.00 71.27  ? 579  CYS   A O     1 
ATOM   2412 C  CB    . CYS   A 1 430  ? 33.019  -33.543 -64.697 1.00 63.54  ? 579  CYS   A CB    1 
ATOM   2413 S  SG    . CYS   A 1 430  ? 33.415  -31.853 -65.233 1.00 62.73  ? 579  CYS   A SG    1 
ATOM   2414 N  N     . ILE   A 1 431  ? 33.132  -36.742 -64.791 1.00 63.75  ? 580  ILE   A N     1 
ATOM   2415 C  CA    . ILE   A 1 431  ? 32.700  -38.020 -64.158 1.00 67.87  ? 580  ILE   A CA    1 
ATOM   2416 C  C     . ILE   A 1 431  ? 33.941  -38.905 -63.991 1.00 66.23  ? 580  ILE   A C     1 
ATOM   2417 O  O     . ILE   A 1 431  ? 34.112  -39.456 -62.889 1.00 62.67  ? 580  ILE   A O     1 
ATOM   2418 C  CB    . ILE   A 1 431  ? 31.553  -38.683 -64.947 1.00 71.20  ? 580  ILE   A CB    1 
ATOM   2419 C  CG1   . ILE   A 1 431  ? 30.262  -37.870 -64.799 1.00 73.34  ? 580  ILE   A CG1   1 
ATOM   2420 C  CG2   . ILE   A 1 431  ? 31.349  -40.132 -64.516 1.00 69.90  ? 580  ILE   A CG2   1 
ATOM   2421 C  CD1   . ILE   A 1 431  ? 29.163  -38.241 -65.777 1.00 72.17  ? 580  ILE   A CD1   1 
ATOM   2422 N  N     . GLN   A 1 432  ? 34.816  -38.951 -64.999 1.00 64.35  ? 581  GLN   A N     1 
ATOM   2423 C  CA    . GLN   A 1 432  ? 36.022  -39.822 -65.009 1.00 71.84  ? 581  GLN   A CA    1 
ATOM   2424 C  C     . GLN   A 1 432  ? 37.013  -39.428 -63.895 1.00 72.56  ? 581  GLN   A C     1 
ATOM   2425 O  O     . GLN   A 1 432  ? 37.458  -40.340 -63.156 1.00 70.13  ? 581  GLN   A O     1 
ATOM   2426 C  CB    . GLN   A 1 432  ? 36.707  -39.795 -66.376 1.00 71.68  ? 581  GLN   A CB    1 
ATOM   2427 C  CG    . GLN   A 1 432  ? 37.536  -41.046 -66.644 1.00 74.36  ? 581  GLN   A CG    1 
ATOM   2428 C  CD    . GLN   A 1 432  ? 37.827  -41.229 -68.110 1.00 76.24  ? 581  GLN   A CD    1 
ATOM   2429 O  OE1   . GLN   A 1 432  ? 37.152  -41.993 -68.797 1.00 70.38  ? 581  GLN   A OE1   1 
ATOM   2430 N  NE2   . GLN   A 1 432  ? 38.819  -40.499 -68.600 1.00 78.57  ? 581  GLN   A NE2   1 
ATOM   2431 N  N     . MET   A 1 433  ? 37.380  -38.146 -63.784 1.00 66.95  ? 582  MET   A N     1 
ATOM   2432 C  CA    . MET   A 1 433  ? 38.487  -37.712 -62.889 1.00 70.06  ? 582  MET   A CA    1 
ATOM   2433 C  C     . MET   A 1 433  ? 38.042  -37.688 -61.409 1.00 65.37  ? 582  MET   A C     1 
ATOM   2434 O  O     . MET   A 1 433  ? 38.938  -37.692 -60.555 1.00 70.27  ? 582  MET   A O     1 
ATOM   2435 C  CB    . MET   A 1 433  ? 39.106  -36.376 -63.323 1.00 72.93  ? 582  MET   A CB    1 
ATOM   2436 C  CG    . MET   A 1 433  ? 38.135  -35.236 -63.617 1.00 86.60  ? 582  MET   A CG    1 
ATOM   2437 S  SD    . MET   A 1 433  ? 38.940  -33.737 -64.336 1.00 93.41  ? 582  MET   A SD    1 
ATOM   2438 C  CE    . MET   A 1 433  ? 40.142  -34.463 -65.453 1.00 98.96  ? 582  MET   A CE    1 
ATOM   2439 N  N     . THR   A 1 434  ? 36.738  -37.752 -61.107 1.00 58.60  ? 583  THR   A N     1 
ATOM   2440 C  CA    . THR   A 1 434  ? 36.174  -37.836 -59.728 1.00 56.05  ? 583  THR   A CA    1 
ATOM   2441 C  C     . THR   A 1 434  ? 35.606  -39.229 -59.397 1.00 55.38  ? 583  THR   A C     1 
ATOM   2442 O  O     . THR   A 1 434  ? 35.159  -39.416 -58.244 1.00 53.41  ? 583  THR   A O     1 
ATOM   2443 C  CB    . THR   A 1 434  ? 35.004  -36.864 -59.528 1.00 60.55  ? 583  THR   A CB    1 
ATOM   2444 O  OG1   . THR   A 1 434  ? 33.907  -37.287 -60.347 1.00 60.25  ? 583  THR   A OG1   1 
ATOM   2445 C  CG2   . THR   A 1 434  ? 35.372  -35.429 -59.831 1.00 62.34  ? 583  THR   A CG2   1 
ATOM   2446 N  N     . HIS   A 1 435  ? 35.530  -40.139 -60.374 1.00 56.17  ? 584  HIS   A N     1 
ATOM   2447 C  CA    . HIS   A 1 435  ? 34.998  -41.521 -60.217 1.00 59.33  ? 584  HIS   A CA    1 
ATOM   2448 C  C     . HIS   A 1 435  ? 33.538  -41.451 -59.743 1.00 59.84  ? 584  HIS   A C     1 
ATOM   2449 O  O     . HIS   A 1 435  ? 33.075  -42.392 -59.045 1.00 57.80  ? 584  HIS   A O     1 
ATOM   2450 C  CB    . HIS   A 1 435  ? 35.941  -42.330 -59.304 1.00 58.83  ? 584  HIS   A CB    1 
ATOM   2451 C  CG    . HIS   A 1 435  ? 37.375  -42.228 -59.724 1.00 61.75  ? 584  HIS   A CG    1 
ATOM   2452 N  ND1   . HIS   A 1 435  ? 37.851  -42.801 -60.892 1.00 66.95  ? 584  HIS   A ND1   1 
ATOM   2453 C  CD2   . HIS   A 1 435  ? 38.432  -41.599 -59.163 1.00 65.26  ? 584  HIS   A CD2   1 
ATOM   2454 C  CE1   . HIS   A 1 435  ? 39.137  -42.536 -61.029 1.00 68.55  ? 584  HIS   A CE1   1 
ATOM   2455 N  NE2   . HIS   A 1 435  ? 39.517  -41.799 -59.982 1.00 70.13  ? 584  HIS   A NE2   1 
ATOM   2456 N  N     . PHE   A 1 436  ? 32.829  -40.371 -60.096 1.00 55.99  ? 585  PHE   A N     1 
ATOM   2457 C  CA    . PHE   A 1 436  ? 31.505  -40.055 -59.501 1.00 56.96  ? 585  PHE   A CA    1 
ATOM   2458 C  C     . PHE   A 1 436  ? 30.475  -41.018 -60.101 1.00 60.19  ? 585  PHE   A C     1 
ATOM   2459 O  O     . PHE   A 1 436  ? 30.631  -41.440 -61.263 1.00 62.37  ? 585  PHE   A O     1 
ATOM   2460 C  CB    . PHE   A 1 436  ? 31.139  -38.576 -59.691 1.00 58.95  ? 585  PHE   A CB    1 
ATOM   2461 C  CG    . PHE   A 1 436  ? 29.678  -38.282 -59.449 1.00 57.69  ? 585  PHE   A CG    1 
ATOM   2462 C  CD1   . PHE   A 1 436  ? 29.201  -38.065 -58.164 1.00 56.32  ? 585  PHE   A CD1   1 
ATOM   2463 C  CD2   . PHE   A 1 436  ? 28.769  -38.275 -60.498 1.00 55.83  ? 585  PHE   A CD2   1 
ATOM   2464 C  CE1   . PHE   A 1 436  ? 27.856  -37.817 -57.931 1.00 55.51  ? 585  PHE   A CE1   1 
ATOM   2465 C  CE2   . PHE   A 1 436  ? 27.419  -38.053 -60.261 1.00 56.42  ? 585  PHE   A CE2   1 
ATOM   2466 C  CZ    . PHE   A 1 436  ? 26.965  -37.818 -58.979 1.00 57.81  ? 585  PHE   A CZ    1 
ATOM   2467 N  N     . VAL   A 1 437  ? 29.461  -41.364 -59.311 1.00 61.57  ? 586  VAL   A N     1 
ATOM   2468 C  CA    . VAL   A 1 437  ? 28.406  -42.350 -59.676 1.00 65.92  ? 586  VAL   A CA    1 
ATOM   2469 C  C     . VAL   A 1 437  ? 27.062  -41.771 -59.245 1.00 65.29  ? 586  VAL   A C     1 
ATOM   2470 O  O     . VAL   A 1 437  ? 26.830  -41.546 -58.064 1.00 63.05  ? 586  VAL   A O     1 
ATOM   2471 C  CB    . VAL   A 1 437  ? 28.679  -43.728 -59.042 1.00 69.18  ? 586  VAL   A CB    1 
ATOM   2472 C  CG1   . VAL   A 1 437  ? 27.600  -44.741 -59.401 1.00 71.30  ? 586  VAL   A CG1   1 
ATOM   2473 C  CG2   . VAL   A 1 437  ? 30.058  -44.257 -59.426 1.00 68.04  ? 586  VAL   A CG2   1 
ATOM   2474 N  N     . PRO   A 1 438  ? 26.164  -41.442 -60.197 1.00 66.81  ? 587  PRO   A N     1 
ATOM   2475 C  CA    . PRO   A 1 438  ? 24.841  -40.924 -59.867 1.00 67.61  ? 587  PRO   A CA    1 
ATOM   2476 C  C     . PRO   A 1 438  ? 24.048  -41.840 -58.950 1.00 72.92  ? 587  PRO   A C     1 
ATOM   2477 O  O     . PRO   A 1 438  ? 24.234  -43.053 -58.974 1.00 79.28  ? 587  PRO   A O     1 
ATOM   2478 C  CB    . PRO   A 1 438  ? 24.133  -40.846 -61.224 1.00 72.50  ? 587  PRO   A CB    1 
ATOM   2479 C  CG    . PRO   A 1 438  ? 25.260  -40.651 -62.208 1.00 78.91  ? 587  PRO   A CG    1 
ATOM   2480 C  CD    . PRO   A 1 438  ? 26.418  -41.452 -61.645 1.00 78.26  ? 587  PRO   A CD    1 
ATOM   2481 N  N     . PRO   A 1 439  ? 23.143  -41.284 -58.116 1.00 79.50  ? 588  PRO   A N     1 
ATOM   2482 C  CA    . PRO   A 1 439  ? 22.140  -42.097 -57.429 1.00 89.05  ? 588  PRO   A CA    1 
ATOM   2483 C  C     . PRO   A 1 439  ? 21.434  -43.057 -58.392 1.00 106.07 ? 588  PRO   A C     1 
ATOM   2484 O  O     . PRO   A 1 439  ? 21.558  -42.930 -59.612 1.00 108.63 ? 588  PRO   A O     1 
ATOM   2485 C  CB    . PRO   A 1 439  ? 21.186  -41.040 -56.843 1.00 89.70  ? 588  PRO   A CB    1 
ATOM   2486 C  CG    . PRO   A 1 439  ? 22.050  -39.802 -56.648 1.00 85.35  ? 588  PRO   A CG    1 
ATOM   2487 C  CD    . PRO   A 1 439  ? 23.066  -39.854 -57.771 1.00 82.13  ? 588  PRO   A CD    1 
ATOM   2488 N  N     . PRO   A 1 440  ? 20.691  -44.070 -57.884 1.00 125.00 ? 589  PRO   A N     1 
ATOM   2489 C  CA    . PRO   A 1 440  ? 19.927  -44.991 -58.729 1.00 120.77 ? 589  PRO   A CA    1 
ATOM   2490 C  C     . PRO   A 1 440  ? 19.595  -44.476 -60.144 1.00 114.59 ? 589  PRO   A C     1 
ATOM   2491 O  O     . PRO   A 1 440  ? 18.431  -44.237 -60.425 1.00 97.61  ? 589  PRO   A O     1 
ATOM   2492 C  CB    . PRO   A 1 440  ? 18.692  -45.155 -57.829 1.00 124.89 ? 589  PRO   A CB    1 
ATOM   2493 C  CG    . PRO   A 1 440  ? 19.279  -45.248 -56.423 1.00 128.52 ? 589  PRO   A CG    1 
ATOM   2494 C  CD    . PRO   A 1 440  ? 20.531  -44.390 -56.454 1.00 128.84 ? 589  PRO   A CD    1 
ATOM   2495 N  N     . ALA   A 1 458  ? 16.040  -34.541 -77.784 1.00 88.34  ? 607  ALA   A N     1 
ATOM   2496 C  CA    . ALA   A 1 458  ? 16.812  -35.770 -77.479 1.00 88.62  ? 607  ALA   A CA    1 
ATOM   2497 C  C     . ALA   A 1 458  ? 17.768  -35.492 -76.310 1.00 86.24  ? 607  ALA   A C     1 
ATOM   2498 O  O     . ALA   A 1 458  ? 17.722  -34.373 -75.767 1.00 82.03  ? 607  ALA   A O     1 
ATOM   2499 C  CB    . ALA   A 1 458  ? 17.552  -36.258 -78.705 1.00 83.04  ? 607  ALA   A CB    1 
ATOM   2500 N  N     . ASN   A 1 459  ? 18.615  -36.473 -75.986 1.00 79.15  ? 608  ASN   A N     1 
ATOM   2501 C  CA    . ASN   A 1 459  ? 19.346  -36.623 -74.699 1.00 74.19  ? 608  ASN   A CA    1 
ATOM   2502 C  C     . ASN   A 1 459  ? 20.822  -36.932 -74.988 1.00 70.61  ? 608  ASN   A C     1 
ATOM   2503 O  O     . ASN   A 1 459  ? 21.121  -38.095 -75.331 1.00 67.86  ? 608  ASN   A O     1 
ATOM   2504 C  CB    . ASN   A 1 459  ? 18.692  -37.731 -73.868 1.00 74.26  ? 608  ASN   A CB    1 
ATOM   2505 C  CG    . ASN   A 1 459  ? 19.431  -38.057 -72.586 1.00 78.68  ? 608  ASN   A CG    1 
ATOM   2506 O  OD1   . ASN   A 1 459  ? 20.519  -37.541 -72.324 1.00 81.96  ? 608  ASN   A OD1   1 
ATOM   2507 N  ND2   . ASN   A 1 459  ? 18.834  -38.909 -71.770 1.00 72.12  ? 608  ASN   A ND2   1 
ATOM   2508 N  N     . CYS   A 1 460  ? 21.720  -35.954 -74.824 1.00 67.19  ? 609  CYS   A N     1 
ATOM   2509 C  CA    . CYS   A 1 460  ? 23.146  -36.065 -75.246 1.00 70.34  ? 609  CYS   A CA    1 
ATOM   2510 C  C     . CYS   A 1 460  ? 24.010  -36.665 -74.123 1.00 72.30  ? 609  CYS   A C     1 
ATOM   2511 O  O     . CYS   A 1 460  ? 25.261  -36.707 -74.303 1.00 62.42  ? 609  CYS   A O     1 
ATOM   2512 C  CB    . CYS   A 1 460  ? 23.683  -34.713 -75.695 1.00 75.02  ? 609  CYS   A CB    1 
ATOM   2513 S  SG    . CYS   A 1 460  ? 22.604  -33.891 -76.896 1.00 74.02  ? 609  CYS   A SG    1 
ATOM   2514 N  N     . ASN   A 1 461  ? 23.377  -37.149 -73.040 1.00 68.76  ? 610  ASN   A N     1 
ATOM   2515 C  CA    . ASN   A 1 461  ? 24.039  -37.908 -71.937 1.00 73.85  ? 610  ASN   A CA    1 
ATOM   2516 C  C     . ASN   A 1 461  ? 24.116  -39.415 -72.279 1.00 79.25  ? 610  ASN   A C     1 
ATOM   2517 O  O     . ASN   A 1 461  ? 24.920  -40.138 -71.626 1.00 72.95  ? 610  ASN   A O     1 
ATOM   2518 C  CB    . ASN   A 1 461  ? 23.341  -37.664 -70.590 1.00 66.68  ? 610  ASN   A CB    1 
ATOM   2519 C  CG    . ASN   A 1 461  ? 23.620  -36.301 -69.976 1.00 59.02  ? 610  ASN   A CG    1 
ATOM   2520 O  OD1   . ASN   A 1 461  ? 24.424  -35.523 -70.487 1.00 51.90  ? 610  ASN   A OD1   1 
ATOM   2521 N  ND2   . ASN   A 1 461  ? 22.966  -36.008 -68.860 1.00 50.48  ? 610  ASN   A ND2   1 
ATOM   2522 N  N     . LEU   A 1 462  ? 23.330  -39.886 -73.259 1.00 76.73  ? 611  LEU   A N     1 
ATOM   2523 C  CA    . LEU   A 1 462  ? 23.415  -41.271 -73.805 1.00 74.80  ? 611  LEU   A CA    1 
ATOM   2524 C  C     . LEU   A 1 462  ? 24.494  -41.343 -74.896 1.00 71.72  ? 611  LEU   A C     1 
ATOM   2525 O  O     . LEU   A 1 462  ? 24.781  -42.460 -75.363 1.00 73.92  ? 611  LEU   A O     1 
ATOM   2526 C  CB    . LEU   A 1 462  ? 22.052  -41.696 -74.360 1.00 72.95  ? 611  LEU   A CB    1 
ATOM   2527 C  CG    . LEU   A 1 462  ? 20.861  -41.499 -73.424 1.00 76.04  ? 611  LEU   A CG    1 
ATOM   2528 C  CD1   . LEU   A 1 462  ? 19.582  -41.985 -74.084 1.00 74.11  ? 611  LEU   A CD1   1 
ATOM   2529 C  CD2   . LEU   A 1 462  ? 21.076  -42.200 -72.090 1.00 75.44  ? 611  LEU   A CD2   1 
ATOM   2530 N  N     . ILE   A 1 463  ? 25.067  -40.204 -75.294 1.00 70.32  ? 612  ILE   A N     1 
ATOM   2531 C  CA    . ILE   A 1 463  ? 26.136  -40.124 -76.333 1.00 73.07  ? 612  ILE   A CA    1 
ATOM   2532 C  C     . ILE   A 1 463  ? 27.435  -39.776 -75.612 1.00 76.22  ? 612  ILE   A C     1 
ATOM   2533 O  O     . ILE   A 1 463  ? 27.487  -38.700 -74.986 1.00 87.48  ? 612  ILE   A O     1 
ATOM   2534 C  CB    . ILE   A 1 463  ? 25.802  -39.086 -77.431 1.00 74.53  ? 612  ILE   A CB    1 
ATOM   2535 C  CG1   . ILE   A 1 463  ? 24.680  -39.560 -78.361 1.00 78.74  ? 612  ILE   A CG1   1 
ATOM   2536 C  CG2   . ILE   A 1 463  ? 27.056  -38.706 -78.217 1.00 74.69  ? 612  ILE   A CG2   1 
ATOM   2537 C  CD1   . ILE   A 1 463  ? 23.282  -39.447 -77.781 1.00 83.62  ? 612  ILE   A CD1   1 
ATOM   2538 N  N     . CYS   A 1 464  ? 28.436  -40.647 -75.710 1.00 79.42  ? 613  CYS   A N     1 
ATOM   2539 C  CA    . CYS   A 1 464  ? 29.799  -40.431 -75.163 1.00 80.58  ? 613  CYS   A CA    1 
ATOM   2540 C  C     . CYS   A 1 464  ? 30.807  -41.133 -76.075 1.00 74.34  ? 613  CYS   A C     1 
ATOM   2541 O  O     . CYS   A 1 464  ? 30.562  -42.303 -76.389 1.00 76.97  ? 613  CYS   A O     1 
ATOM   2542 C  CB    . CYS   A 1 464  ? 29.894  -40.952 -73.730 1.00 85.51  ? 613  CYS   A CB    1 
ATOM   2543 S  SG    . CYS   A 1 464  ? 31.452  -40.541 -72.890 1.00 88.80  ? 613  CYS   A SG    1 
ATOM   2544 N  N     . GLY   A 1 465  ? 31.896  -40.447 -76.448 1.00 79.55  ? 614  GLY   A N     1 
ATOM   2545 C  CA    . GLY   A 1 465  ? 32.980  -40.965 -77.310 1.00 87.03  ? 614  GLY   A CA    1 
ATOM   2546 C  C     . GLY   A 1 465  ? 33.534  -42.314 -76.850 1.00 97.45  ? 614  GLY   A C     1 
ATOM   2547 O  O     . GLY   A 1 465  ? 33.436  -42.640 -75.639 1.00 85.23  ? 614  GLY   A O     1 
ATOM   2548 N  N     . ASP   A 1 466  ? 34.110  -43.076 -77.788 1.00 104.05 ? 615  ASP   A N     1 
ATOM   2549 C  CA    . ASP   A 1 466  ? 34.701  -44.423 -77.554 1.00 107.21 ? 615  ASP   A CA    1 
ATOM   2550 C  C     . ASP   A 1 466  ? 35.782  -44.347 -76.467 1.00 104.19 ? 615  ASP   A C     1 
ATOM   2551 O  O     . ASP   A 1 466  ? 35.852  -45.288 -75.658 1.00 93.37  ? 615  ASP   A O     1 
ATOM   2552 C  CB    . ASP   A 1 466  ? 35.289  -45.012 -78.843 1.00 113.26 ? 615  ASP   A CB    1 
ATOM   2553 C  CG    . ASP   A 1 466  ? 34.283  -45.750 -79.711 1.00 116.09 ? 615  ASP   A CG    1 
ATOM   2554 O  OD1   . ASP   A 1 466  ? 33.462  -46.501 -79.147 1.00 116.23 ? 615  ASP   A OD1   1 
ATOM   2555 O  OD2   . ASP   A 1 466  ? 34.334  -45.577 -80.945 1.00 116.37 ? 615  ASP   A OD2   1 
ATOM   2556 N  N     . GLU   A 1 467  ? 36.573  -43.266 -76.437 1.00 100.65 ? 616  GLU   A N     1 
ATOM   2557 C  CA    . GLU   A 1 467  ? 37.839  -43.174 -75.655 1.00 97.38  ? 616  GLU   A CA    1 
ATOM   2558 C  C     . GLU   A 1 467  ? 37.565  -42.996 -74.147 1.00 94.05  ? 616  GLU   A C     1 
ATOM   2559 O  O     . GLU   A 1 467  ? 38.546  -42.862 -73.401 1.00 90.11  ? 616  GLU   A O     1 
ATOM   2560 C  CB    . GLU   A 1 467  ? 38.743  -42.078 -76.236 1.00 97.80  ? 616  GLU   A CB    1 
ATOM   2561 C  CG    . GLU   A 1 467  ? 38.308  -40.646 -75.945 1.00 100.18 ? 616  GLU   A CG    1 
ATOM   2562 C  CD    . GLU   A 1 467  ? 37.336  -40.030 -76.942 1.00 103.41 ? 616  GLU   A CD    1 
ATOM   2563 O  OE1   . GLU   A 1 467  ? 36.130  -40.362 -76.885 1.00 96.57  ? 616  GLU   A OE1   1 
ATOM   2564 O  OE2   . GLU   A 1 467  ? 37.788  -39.222 -77.780 1.00 100.45 ? 616  GLU   A OE2   1 
ATOM   2565 N  N     . TYR   A 1 468  ? 36.305  -43.016 -73.695 1.00 93.62  ? 617  TYR   A N     1 
ATOM   2566 C  CA    . TYR   A 1 468  ? 35.924  -42.961 -72.253 1.00 94.30  ? 617  TYR   A CA    1 
ATOM   2567 C  C     . TYR   A 1 468  ? 35.645  -44.381 -71.746 1.00 93.32  ? 617  TYR   A C     1 
ATOM   2568 O  O     . TYR   A 1 468  ? 35.341  -45.265 -72.570 1.00 93.16  ? 617  TYR   A O     1 
ATOM   2569 C  CB    . TYR   A 1 468  ? 34.736  -42.014 -72.026 1.00 94.53  ? 617  TYR   A CB    1 
ATOM   2570 C  CG    . TYR   A 1 468  ? 35.084  -40.563 -72.253 1.00 98.64  ? 617  TYR   A CG    1 
ATOM   2571 C  CD1   . TYR   A 1 468  ? 35.663  -39.799 -71.251 1.00 92.57  ? 617  TYR   A CD1   1 
ATOM   2572 C  CD2   . TYR   A 1 468  ? 34.889  -39.965 -73.491 1.00 100.58 ? 617  TYR   A CD2   1 
ATOM   2573 C  CE1   . TYR   A 1 468  ? 36.025  -38.479 -71.468 1.00 93.38  ? 617  TYR   A CE1   1 
ATOM   2574 C  CE2   . TYR   A 1 468  ? 35.248  -38.647 -73.726 1.00 97.47  ? 617  TYR   A CE2   1 
ATOM   2575 C  CZ    . TYR   A 1 468  ? 35.818  -37.900 -72.710 1.00 94.17  ? 617  TYR   A CZ    1 
ATOM   2576 O  OH    . TYR   A 1 468  ? 36.165  -36.602 -72.944 1.00 81.67  ? 617  TYR   A OH    1 
ATOM   2577 N  N     . GLY   A 1 469  ? 35.760  -44.587 -70.430 1.00 84.82  ? 618  GLY   A N     1 
ATOM   2578 C  CA    . GLY   A 1 469  ? 35.485  -45.877 -69.774 1.00 86.84  ? 618  GLY   A CA    1 
ATOM   2579 C  C     . GLY   A 1 469  ? 34.014  -46.265 -69.903 1.00 88.92  ? 618  GLY   A C     1 
ATOM   2580 O  O     . GLY   A 1 469  ? 33.174  -45.409 -70.169 1.00 87.78  ? 618  GLY   A O     1 
ATOM   2581 N  N     . PRO   A 1 470  ? 33.665  -47.564 -69.743 1.00 98.16  ? 619  PRO   A N     1 
ATOM   2582 C  CA    . PRO   A 1 470  ? 32.266  -48.006 -69.702 1.00 97.43  ? 619  PRO   A CA    1 
ATOM   2583 C  C     . PRO   A 1 470  ? 31.467  -47.538 -68.471 1.00 91.03  ? 619  PRO   A C     1 
ATOM   2584 O  O     . PRO   A 1 470  ? 30.239  -47.516 -68.546 1.00 78.25  ? 619  PRO   A O     1 
ATOM   2585 C  CB    . PRO   A 1 470  ? 32.340  -49.547 -69.669 1.00 97.99  ? 619  PRO   A CB    1 
ATOM   2586 C  CG    . PRO   A 1 470  ? 33.769  -49.884 -70.062 1.00 101.98 ? 619  PRO   A CG    1 
ATOM   2587 C  CD    . PRO   A 1 470  ? 34.607  -48.692 -69.648 1.00 102.15 ? 619  PRO   A CD    1 
ATOM   2588 N  N     . GLU   A 1 471  ? 32.155  -47.218 -67.366 1.00 91.62  ? 620  GLU   A N     1 
ATOM   2589 C  CA    . GLU   A 1 471  ? 31.520  -46.682 -66.128 1.00 91.01  ? 620  GLU   A CA    1 
ATOM   2590 C  C     . GLU   A 1 471  ? 31.162  -45.203 -66.338 1.00 82.73  ? 620  GLU   A C     1 
ATOM   2591 O  O     . GLU   A 1 471  ? 30.048  -44.819 -65.920 1.00 79.51  ? 620  GLU   A O     1 
ATOM   2592 C  CB    . GLU   A 1 471  ? 32.414  -46.864 -64.900 1.00 93.61  ? 620  GLU   A CB    1 
ATOM   2593 C  CG    . GLU   A 1 471  ? 31.678  -46.597 -63.596 1.00 96.25  ? 620  GLU   A CG    1 
ATOM   2594 C  CD    . GLU   A 1 471  ? 32.535  -46.580 -62.340 1.00 98.33  ? 620  GLU   A CD    1 
ATOM   2595 O  OE1   . GLU   A 1 471  ? 32.239  -47.368 -61.413 1.00 103.41 ? 620  GLU   A OE1   1 
ATOM   2596 O  OE2   . GLU   A 1 471  ? 33.478  -45.767 -62.280 1.00 87.58  ? 620  GLU   A OE2   1 
ATOM   2597 N  N     . THR   A 1 472  ? 32.053  -44.414 -66.962 1.00 75.15  ? 621  THR   A N     1 
ATOM   2598 C  CA    . THR   A 1 472  ? 31.809  -42.993 -67.341 1.00 77.36  ? 621  THR   A CA    1 
ATOM   2599 C  C     . THR   A 1 472  ? 30.502  -42.906 -68.152 1.00 82.18  ? 621  THR   A C     1 
ATOM   2600 O  O     . THR   A 1 472  ? 29.559  -42.206 -67.685 1.00 70.77  ? 621  THR   A O     1 
ATOM   2601 C  CB    . THR   A 1 472  ? 32.996  -42.390 -68.107 1.00 79.22  ? 621  THR   A CB    1 
ATOM   2602 O  OG1   . THR   A 1 472  ? 34.232  -42.673 -67.448 1.00 70.39  ? 621  THR   A OG1   1 
ATOM   2603 C  CG2   . THR   A 1 472  ? 32.875  -40.889 -68.260 1.00 80.85  ? 621  THR   A CG2   1 
ATOM   2604 N  N     . ARG   A 1 473  ? 30.452  -43.605 -69.298 1.00 80.27  ? 622  ARG   A N     1 
ATOM   2605 C  CA    . ARG   A 1 473  ? 29.276  -43.718 -70.209 1.00 85.24  ? 622  ARG   A CA    1 
ATOM   2606 C  C     . ARG   A 1 473  ? 28.023  -44.090 -69.410 1.00 84.95  ? 622  ARG   A C     1 
ATOM   2607 O  O     . ARG   A 1 473  ? 26.977  -43.444 -69.609 1.00 78.61  ? 622  ARG   A O     1 
ATOM   2608 C  CB    . ARG   A 1 473  ? 29.503  -44.790 -71.283 1.00 97.57  ? 622  ARG   A CB    1 
ATOM   2609 C  CG    . ARG   A 1 473  ? 29.553  -44.260 -72.708 1.00 107.25 ? 622  ARG   A CG    1 
ATOM   2610 C  CD    . ARG   A 1 473  ? 29.522  -45.357 -73.761 1.00 109.27 ? 622  ARG   A CD    1 
ATOM   2611 N  NE    . ARG   A 1 473  ? 30.703  -46.215 -73.704 1.00 112.75 ? 622  ARG   A NE    1 
ATOM   2612 C  CZ    . ARG   A 1 473  ? 31.914  -45.902 -74.173 1.00 114.92 ? 622  ARG   A CZ    1 
ATOM   2613 N  NH1   . ARG   A 1 473  ? 32.141  -44.730 -74.747 1.00 109.43 ? 622  ARG   A NH1   1 
ATOM   2614 N  NH2   . ARG   A 1 473  ? 32.903  -46.773 -74.062 1.00 111.28 ? 622  ARG   A NH2   1 
ATOM   2615 N  N     . MET   A 1 474  ? 28.129  -45.121 -68.569 1.00 87.98  ? 623  MET   A N     1 
ATOM   2616 C  CA    . MET   A 1 474  ? 26.998  -45.675 -67.778 1.00 86.73  ? 623  MET   A CA    1 
ATOM   2617 C  C     . MET   A 1 474  ? 26.530  -44.618 -66.768 1.00 77.59  ? 623  MET   A C     1 
ATOM   2618 O  O     . MET   A 1 474  ? 25.311  -44.413 -66.646 1.00 76.04  ? 623  MET   A O     1 
ATOM   2619 C  CB    . MET   A 1 474  ? 27.421  -46.966 -67.063 1.00 91.36  ? 623  MET   A CB    1 
ATOM   2620 C  CG    . MET   A 1 474  ? 26.332  -47.608 -66.199 1.00 102.34 ? 623  MET   A CG    1 
ATOM   2621 S  SD    . MET   A 1 474  ? 24.769  -47.963 -67.071 1.00 110.72 ? 623  MET   A SD    1 
ATOM   2622 C  CE    . MET   A 1 474  ? 23.795  -48.666 -65.740 1.00 106.28 ? 623  MET   A CE    1 
ATOM   2623 N  N     . SER   A 1 475  ? 27.467  -43.970 -66.072 1.00 75.12  ? 624  SER   A N     1 
ATOM   2624 C  CA    . SER   A 1 475  ? 27.187  -42.926 -65.049 1.00 76.38  ? 624  SER   A CA    1 
ATOM   2625 C  C     . SER   A 1 475  ? 26.544  -41.703 -65.727 1.00 70.49  ? 624  SER   A C     1 
ATOM   2626 O  O     . SER   A 1 475  ? 25.448  -41.291 -65.278 1.00 62.78  ? 624  SER   A O     1 
ATOM   2627 C  CB    . SER   A 1 475  ? 28.439  -42.555 -64.272 1.00 78.00  ? 624  SER   A CB    1 
ATOM   2628 O  OG    . SER   A 1 475  ? 29.004  -43.678 -63.602 1.00 75.36  ? 624  SER   A OG    1 
ATOM   2629 N  N     . MET   A 1 476  ? 27.170  -41.169 -66.788 1.00 63.52  ? 625  MET   A N     1 
ATOM   2630 C  CA    . MET   A 1 476  ? 26.650  -39.986 -67.532 1.00 68.19  ? 625  MET   A CA    1 
ATOM   2631 C  C     . MET   A 1 476  ? 25.197  -40.263 -67.939 1.00 68.57  ? 625  MET   A C     1 
ATOM   2632 O  O     . MET   A 1 476  ? 24.312  -39.414 -67.639 1.00 61.23  ? 625  MET   A O     1 
ATOM   2633 C  CB    . MET   A 1 476  ? 27.476  -39.651 -68.780 1.00 63.51  ? 625  MET   A CB    1 
ATOM   2634 C  CG    . MET   A 1 476  ? 27.064  -38.327 -69.411 1.00 60.41  ? 625  MET   A CG    1 
ATOM   2635 S  SD    . MET   A 1 476  ? 28.413  -37.468 -70.260 1.00 71.13  ? 625  MET   A SD    1 
ATOM   2636 C  CE    . MET   A 1 476  ? 28.353  -38.232 -71.877 1.00 68.52  ? 625  MET   A CE    1 
ATOM   2637 N  N     . ALA   A 1 477  ? 24.960  -41.446 -68.515 1.00 65.46  ? 626  ALA   A N     1 
ATOM   2638 C  CA    . ALA   A 1 477  ? 23.655  -41.883 -69.060 1.00 68.03  ? 626  ALA   A CA    1 
ATOM   2639 C  C     . ALA   A 1 477  ? 22.568  -41.886 -67.976 1.00 68.10  ? 626  ALA   A C     1 
ATOM   2640 O  O     . ALA   A 1 477  ? 21.393  -41.984 -68.356 1.00 70.40  ? 626  ALA   A O     1 
ATOM   2641 C  CB    . ALA   A 1 477  ? 23.793  -43.242 -69.701 1.00 68.46  ? 626  ALA   A CB    1 
ATOM   2642 N  N     . GLN   A 1 478  ? 22.916  -41.769 -66.689 1.00 71.04  ? 627  GLN   A N     1 
ATOM   2643 C  CA    . GLN   A 1 478  ? 21.920  -41.801 -65.577 1.00 75.66  ? 627  GLN   A CA    1 
ATOM   2644 C  C     . GLN   A 1 478  ? 21.465  -40.377 -65.211 1.00 73.03  ? 627  GLN   A C     1 
ATOM   2645 O  O     . GLN   A 1 478  ? 20.455  -40.271 -64.488 1.00 62.81  ? 627  GLN   A O     1 
ATOM   2646 C  CB    . GLN   A 1 478  ? 22.509  -42.537 -64.373 1.00 81.34  ? 627  GLN   A CB    1 
ATOM   2647 C  CG    . GLN   A 1 478  ? 22.940  -43.968 -64.685 1.00 83.66  ? 627  GLN   A CG    1 
ATOM   2648 C  CD    . GLN   A 1 478  ? 21.843  -44.976 -64.441 1.00 94.31  ? 627  GLN   A CD    1 
ATOM   2649 O  OE1   . GLN   A 1 478  ? 20.981  -44.799 -63.579 1.00 104.36 ? 627  GLN   A OE1   1 
ATOM   2650 N  NE2   . GLN   A 1 478  ? 21.877  -46.061 -65.197 1.00 100.00 ? 627  GLN   A NE2   1 
ATOM   2651 N  N     . LEU   A 1 479  ? 22.146  -39.338 -65.729 1.00 71.29  ? 628  LEU   A N     1 
ATOM   2652 C  CA    . LEU   A 1 479  ? 21.961  -37.908 -65.342 1.00 72.11  ? 628  LEU   A CA    1 
ATOM   2653 C  C     . LEU   A 1 479  ? 20.926  -37.239 -66.249 1.00 71.37  ? 628  LEU   A C     1 
ATOM   2654 O  O     . LEU   A 1 479  ? 21.165  -37.146 -67.468 1.00 70.21  ? 628  LEU   A O     1 
ATOM   2655 C  CB    . LEU   A 1 479  ? 23.300  -37.169 -65.440 1.00 71.18  ? 628  LEU   A CB    1 
ATOM   2656 C  CG    . LEU   A 1 479  ? 24.366  -37.605 -64.439 1.00 72.67  ? 628  LEU   A CG    1 
ATOM   2657 C  CD1   . LEU   A 1 479  ? 25.745  -37.126 -64.863 1.00 72.71  ? 628  LEU   A CD1   1 
ATOM   2658 C  CD2   . LEU   A 1 479  ? 24.022  -37.099 -63.045 1.00 75.71  ? 628  LEU   A CD2   1 
ATOM   2659 N  N     . ASN   A 1 480  ? 19.843  -36.743 -65.659 1.00 70.10  ? 629  ASN   A N     1 
ATOM   2660 C  CA    . ASN   A 1 480  ? 18.810  -35.942 -66.363 1.00 73.99  ? 629  ASN   A CA    1 
ATOM   2661 C  C     . ASN   A 1 480  ? 19.421  -34.576 -66.722 1.00 73.04  ? 629  ASN   A C     1 
ATOM   2662 O  O     . ASN   A 1 480  ? 19.811  -33.838 -65.797 1.00 73.97  ? 629  ASN   A O     1 
ATOM   2663 C  CB    . ASN   A 1 480  ? 17.542  -35.845 -65.508 1.00 71.77  ? 629  ASN   A CB    1 
ATOM   2664 C  CG    . ASN   A 1 480  ? 16.331  -35.370 -66.280 1.00 79.49  ? 629  ASN   A CG    1 
ATOM   2665 O  OD1   . ASN   A 1 480  ? 16.397  -35.184 -67.493 1.00 81.28  ? 629  ASN   A OD1   1 
ATOM   2666 N  ND2   . ASN   A 1 480  ? 15.221  -35.166 -65.584 1.00 85.39  ? 629  ASN   A ND2   1 
ATOM   2667 N  N     . GLU   A 1 481  ? 19.505  -34.251 -68.015 1.00 67.89  ? 630  GLU   A N     1 
ATOM   2668 C  CA    . GLU   A 1 481  ? 20.083  -32.977 -68.527 1.00 69.70  ? 630  GLU   A CA    1 
ATOM   2669 C  C     . GLU   A 1 481  ? 19.320  -31.745 -68.000 1.00 67.71  ? 630  GLU   A C     1 
ATOM   2670 O  O     . GLU   A 1 481  ? 19.906  -30.659 -68.028 1.00 64.29  ? 630  GLU   A O     1 
ATOM   2671 C  CB    . GLU   A 1 481  ? 20.091  -32.974 -70.056 1.00 68.24  ? 630  GLU   A CB    1 
ATOM   2672 C  CG    . GLU   A 1 481  ? 21.390  -33.476 -70.658 1.00 68.35  ? 630  GLU   A CG    1 
ATOM   2673 C  CD    . GLU   A 1 481  ? 21.444  -33.314 -72.165 1.00 67.50  ? 630  GLU   A CD    1 
ATOM   2674 O  OE1   . GLU   A 1 481  ? 20.453  -33.686 -72.825 1.00 73.64  ? 630  GLU   A OE1   1 
ATOM   2675 O  OE2   . GLU   A 1 481  ? 22.457  -32.796 -72.672 1.00 66.10  ? 630  GLU   A OE2   1 
ATOM   2676 N  N     . LYS   A 1 482  ? 18.074  -31.896 -67.541 1.00 68.67  ? 631  LYS   A N     1 
ATOM   2677 C  CA    . LYS   A 1 482  ? 17.207  -30.778 -67.064 1.00 73.35  ? 631  LYS   A CA    1 
ATOM   2678 C  C     . LYS   A 1 482  ? 17.524  -30.444 -65.600 1.00 71.49  ? 631  LYS   A C     1 
ATOM   2679 O  O     . LYS   A 1 482  ? 17.097  -29.374 -65.135 1.00 67.94  ? 631  LYS   A O     1 
ATOM   2680 C  CB    . LYS   A 1 482  ? 15.720  -31.124 -67.223 1.00 75.35  ? 631  LYS   A CB    1 
ATOM   2681 C  CG    . LYS   A 1 482  ? 15.376  -31.880 -68.503 1.00 85.82  ? 631  LYS   A CG    1 
ATOM   2682 C  CD    . LYS   A 1 482  ? 14.153  -31.389 -69.256 1.00 91.91  ? 631  LYS   A CD    1 
ATOM   2683 C  CE    . LYS   A 1 482  ? 13.999  -32.083 -70.598 1.00 98.98  ? 631  LYS   A CE    1 
ATOM   2684 N  NZ    . LYS   A 1 482  ? 13.224  -31.276 -71.571 1.00 99.58  ? 631  LYS   A NZ    1 
ATOM   2685 N  N     . GLU   A 1 483  ? 18.214  -31.338 -64.890 1.00 74.92  ? 632  GLU   A N     1 
ATOM   2686 C  CA    . GLU   A 1 483  ? 18.695  -31.103 -63.503 1.00 75.62  ? 632  GLU   A CA    1 
ATOM   2687 C  C     . GLU   A 1 483  ? 20.163  -30.664 -63.579 1.00 71.13  ? 632  GLU   A C     1 
ATOM   2688 O  O     . GLU   A 1 483  ? 20.854  -31.043 -64.552 1.00 70.00  ? 632  GLU   A O     1 
ATOM   2689 C  CB    . GLU   A 1 483  ? 18.552  -32.370 -62.652 1.00 80.05  ? 632  GLU   A CB    1 
ATOM   2690 C  CG    . GLU   A 1 483  ? 17.116  -32.763 -62.337 1.00 82.09  ? 632  GLU   A CG    1 
ATOM   2691 C  CD    . GLU   A 1 483  ? 16.974  -34.049 -61.529 1.00 85.09  ? 632  GLU   A CD    1 
ATOM   2692 O  OE1   . GLU   A 1 483  ? 16.022  -34.140 -60.714 1.00 80.73  ? 632  GLU   A OE1   1 
ATOM   2693 O  OE2   . GLU   A 1 483  ? 17.826  -34.955 -61.702 1.00 75.38  ? 632  GLU   A OE2   1 
ATOM   2694 N  N     . THR   A 1 484  ? 20.625  -29.877 -62.606 1.00 68.31  ? 633  THR   A N     1 
ATOM   2695 C  CA    . THR   A 1 484  ? 22.076  -29.634 -62.386 1.00 67.59  ? 633  THR   A CA    1 
ATOM   2696 C  C     . THR   A 1 484  ? 22.548  -30.611 -61.308 1.00 59.79  ? 633  THR   A C     1 
ATOM   2697 O  O     . THR   A 1 484  ? 21.880  -30.836 -60.295 1.00 52.44  ? 633  THR   A O     1 
ATOM   2698 C  CB    . THR   A 1 484  ? 22.366  -28.150 -62.127 1.00 74.10  ? 633  THR   A CB    1 
ATOM   2699 O  OG1   . THR   A 1 484  ? 22.193  -27.461 -63.373 1.00 74.07  ? 633  THR   A OG1   1 
ATOM   2700 C  CG2   . THR   A 1 484  ? 23.759  -27.920 -61.579 1.00 71.51  ? 633  THR   A CG2   1 
ATOM   2701 N  N     . PRO   A 1 485  ? 23.686  -31.293 -61.535 1.00 54.50  ? 634  PRO   A N     1 
ATOM   2702 C  CA    . PRO   A 1 485  ? 24.112  -32.366 -60.643 1.00 55.35  ? 634  PRO   A CA    1 
ATOM   2703 C  C     . PRO   A 1 485  ? 24.916  -31.792 -59.457 1.00 54.20  ? 634  PRO   A C     1 
ATOM   2704 O  O     . PRO   A 1 485  ? 26.134  -31.645 -59.558 1.00 44.99  ? 634  PRO   A O     1 
ATOM   2705 C  CB    . PRO   A 1 485  ? 24.904  -33.249 -61.624 1.00 57.14  ? 634  PRO   A CB    1 
ATOM   2706 C  CG    . PRO   A 1 485  ? 25.563  -32.264 -62.584 1.00 57.00  ? 634  PRO   A CG    1 
ATOM   2707 C  CD    . PRO   A 1 485  ? 24.616  -31.080 -62.660 1.00 54.66  ? 634  PRO   A CD    1 
ATOM   2708 N  N     . PHE   A 1 486  ? 24.204  -31.438 -58.384 1.00 55.27  ? 635  PHE   A N     1 
ATOM   2709 C  CA    . PHE   A 1 486  ? 24.753  -30.833 -57.143 1.00 64.66  ? 635  PHE   A CA    1 
ATOM   2710 C  C     . PHE   A 1 486  ? 25.875  -31.726 -56.594 1.00 69.98  ? 635  PHE   A C     1 
ATOM   2711 O  O     . PHE   A 1 486  ? 26.955  -31.192 -56.268 1.00 65.02  ? 635  PHE   A O     1 
ATOM   2712 C  CB    . PHE   A 1 486  ? 23.635  -30.620 -56.120 1.00 72.41  ? 635  PHE   A CB    1 
ATOM   2713 C  CG    . PHE   A 1 486  ? 22.551  -29.679 -56.580 1.00 84.14  ? 635  PHE   A CG    1 
ATOM   2714 C  CD1   . PHE   A 1 486  ? 22.772  -28.310 -56.630 1.00 86.07  ? 635  PHE   A CD1   1 
ATOM   2715 C  CD2   . PHE   A 1 486  ? 21.312  -30.162 -56.976 1.00 94.87  ? 635  PHE   A CD2   1 
ATOM   2716 C  CE1   . PHE   A 1 486  ? 21.776  -27.444 -57.054 1.00 92.76  ? 635  PHE   A CE1   1 
ATOM   2717 C  CE2   . PHE   A 1 486  ? 20.316  -29.295 -57.405 1.00 99.85  ? 635  PHE   A CE2   1 
ATOM   2718 C  CZ    . PHE   A 1 486  ? 20.550  -27.938 -57.440 1.00 102.24 ? 635  PHE   A CZ    1 
ATOM   2719 N  N     . GLU   A 1 487  ? 25.649  -33.047 -56.562 1.00 69.25  ? 636  GLU   A N     1 
ATOM   2720 C  CA    . GLU   A 1 487  ? 26.577  -34.041 -55.956 1.00 64.66  ? 636  GLU   A CA    1 
ATOM   2721 C  C     . GLU   A 1 487  ? 27.863  -34.097 -56.787 1.00 61.08  ? 636  GLU   A C     1 
ATOM   2722 O  O     . GLU   A 1 487  ? 28.951  -34.292 -56.188 1.00 63.44  ? 636  GLU   A O     1 
ATOM   2723 C  CB    . GLU   A 1 487  ? 25.893  -35.405 -55.803 1.00 72.60  ? 636  GLU   A CB    1 
ATOM   2724 C  CG    . GLU   A 1 487  ? 24.755  -35.416 -54.785 1.00 76.13  ? 636  GLU   A CG    1 
ATOM   2725 C  CD    . GLU   A 1 487  ? 23.405  -34.916 -55.288 1.00 88.03  ? 636  GLU   A CD    1 
ATOM   2726 O  OE1   . GLU   A 1 487  ? 22.462  -34.794 -54.459 1.00 90.60  ? 636  GLU   A OE1   1 
ATOM   2727 O  OE2   . GLU   A 1 487  ? 23.292  -34.636 -56.507 1.00 81.92  ? 636  GLU   A OE2   1 
ATOM   2728 N  N     . LEU   A 1 488  ? 27.781  -33.880 -58.104 1.00 59.66  ? 637  LEU   A N     1 
ATOM   2729 C  CA    . LEU   A 1 488  ? 28.991  -33.859 -58.975 1.00 56.08  ? 637  LEU   A CA    1 
ATOM   2730 C  C     . LEU   A 1 488  ? 29.827  -32.613 -58.657 1.00 51.66  ? 637  LEU   A C     1 
ATOM   2731 O  O     . LEU   A 1 488  ? 31.090  -32.696 -58.682 1.00 46.29  ? 637  LEU   A O     1 
ATOM   2732 C  CB    . LEU   A 1 488  ? 28.586  -33.896 -60.451 1.00 56.67  ? 637  LEU   A CB    1 
ATOM   2733 C  CG    . LEU   A 1 488  ? 29.752  -33.867 -61.440 1.00 60.45  ? 637  LEU   A CG    1 
ATOM   2734 C  CD1   . LEU   A 1 488  ? 30.829  -34.860 -61.032 1.00 61.20  ? 637  LEU   A CD1   1 
ATOM   2735 C  CD2   . LEU   A 1 488  ? 29.279  -34.139 -62.865 1.00 61.74  ? 637  LEU   A CD2   1 
ATOM   2736 N  N     . ILE   A 1 489  ? 29.158  -31.504 -58.337 1.00 52.40  ? 638  ILE   A N     1 
ATOM   2737 C  CA    . ILE   A 1 489  ? 29.835  -30.209 -58.030 1.00 54.73  ? 638  ILE   A CA    1 
ATOM   2738 C  C     . ILE   A 1 489  ? 30.629  -30.377 -56.725 1.00 52.06  ? 638  ILE   A C     1 
ATOM   2739 O  O     . ILE   A 1 489  ? 31.850  -30.063 -56.730 1.00 50.89  ? 638  ILE   A O     1 
ATOM   2740 C  CB    . ILE   A 1 489  ? 28.820  -29.050 -57.991 1.00 53.01  ? 638  ILE   A CB    1 
ATOM   2741 C  CG1   . ILE   A 1 489  ? 28.101  -28.911 -59.336 1.00 52.91  ? 638  ILE   A CG1   1 
ATOM   2742 C  CG2   . ILE   A 1 489  ? 29.512  -27.758 -57.581 1.00 53.85  ? 638  ILE   A CG2   1 
ATOM   2743 C  CD1   . ILE   A 1 489  ? 27.108  -27.771 -59.405 1.00 53.82  ? 638  ILE   A CD1   1 
ATOM   2744 N  N     . GLU   A 1 490  ? 29.974  -30.901 -55.680 1.00 54.87  ? 639  GLU   A N     1 
ATOM   2745 C  CA    . GLU   A 1 490  ? 30.599  -31.347 -54.401 1.00 59.80  ? 639  GLU   A CA    1 
ATOM   2746 C  C     . GLU   A 1 490  ? 31.877  -32.136 -54.713 1.00 57.87  ? 639  GLU   A C     1 
ATOM   2747 O  O     . GLU   A 1 490  ? 32.962  -31.736 -54.245 1.00 58.55  ? 639  GLU   A O     1 
ATOM   2748 C  CB    . GLU   A 1 490  ? 29.608  -32.185 -53.595 1.00 63.41  ? 639  GLU   A CB    1 
ATOM   2749 C  CG    . GLU   A 1 490  ? 30.046  -32.446 -52.165 1.00 74.25  ? 639  GLU   A CG    1 
ATOM   2750 C  CD    . GLU   A 1 490  ? 29.004  -33.141 -51.299 1.00 75.64  ? 639  GLU   A CD    1 
ATOM   2751 O  OE1   . GLU   A 1 490  ? 28.041  -33.709 -51.859 1.00 83.05  ? 639  GLU   A OE1   1 
ATOM   2752 O  OE2   . GLU   A 1 490  ? 29.155  -33.119 -50.066 1.00 73.49  ? 639  GLU   A OE2   1 
ATOM   2753 N  N     . ALA   A 1 491  ? 31.762  -33.176 -55.539 1.00 56.71  ? 640  ALA   A N     1 
ATOM   2754 C  CA    . ALA   A 1 491  ? 32.884  -34.064 -55.919 1.00 56.56  ? 640  ALA   A CA    1 
ATOM   2755 C  C     . ALA   A 1 491  ? 33.937  -33.296 -56.730 1.00 55.48  ? 640  ALA   A C     1 
ATOM   2756 O  O     . ALA   A 1 491  ? 35.102  -33.691 -56.689 1.00 58.26  ? 640  ALA   A O     1 
ATOM   2757 C  CB    . ALA   A 1 491  ? 32.358  -35.265 -56.669 1.00 61.68  ? 640  ALA   A CB    1 
ATOM   2758 N  N     . LEU   A 1 492  ? 33.567  -32.234 -57.443 1.00 57.93  ? 641  LEU   A N     1 
ATOM   2759 C  CA    . LEU   A 1 492  ? 34.544  -31.455 -58.254 1.00 59.55  ? 641  LEU   A CA    1 
ATOM   2760 C  C     . LEU   A 1 492  ? 35.358  -30.518 -57.350 1.00 56.23  ? 641  LEU   A C     1 
ATOM   2761 O  O     . LEU   A 1 492  ? 36.554  -30.330 -57.637 1.00 54.17  ? 641  LEU   A O     1 
ATOM   2762 C  CB    . LEU   A 1 492  ? 33.805  -30.684 -59.353 1.00 64.76  ? 641  LEU   A CB    1 
ATOM   2763 C  CG    . LEU   A 1 492  ? 33.453  -31.504 -60.596 1.00 64.95  ? 641  LEU   A CG    1 
ATOM   2764 C  CD1   . LEU   A 1 492  ? 32.311  -30.858 -61.358 1.00 65.88  ? 641  LEU   A CD1   1 
ATOM   2765 C  CD2   . LEU   A 1 492  ? 34.667  -31.689 -61.497 1.00 60.87  ? 641  LEU   A CD2   1 
ATOM   2766 N  N     . LEU   A 1 493  ? 34.738  -29.931 -56.322 1.00 53.91  ? 642  LEU   A N     1 
ATOM   2767 C  CA    . LEU   A 1 493  ? 35.438  -29.082 -55.319 1.00 59.14  ? 642  LEU   A CA    1 
ATOM   2768 C  C     . LEU   A 1 493  ? 36.521  -29.928 -54.627 1.00 66.01  ? 642  LEU   A C     1 
ATOM   2769 O  O     . LEU   A 1 493  ? 37.632  -29.402 -54.444 1.00 74.87  ? 642  LEU   A O     1 
ATOM   2770 C  CB    . LEU   A 1 493  ? 34.433  -28.516 -54.308 1.00 56.28  ? 642  LEU   A CB    1 
ATOM   2771 C  CG    . LEU   A 1 493  ? 33.332  -27.629 -54.888 1.00 55.25  ? 642  LEU   A CG    1 
ATOM   2772 C  CD1   . LEU   A 1 493  ? 32.321  -27.232 -53.825 1.00 57.08  ? 642  LEU   A CD1   1 
ATOM   2773 C  CD2   . LEU   A 1 493  ? 33.916  -26.392 -55.547 1.00 55.82  ? 642  LEU   A CD2   1 
ATOM   2774 N  N     . LYS   A 1 494  ? 36.228  -31.198 -54.298 1.00 67.25  ? 643  LYS   A N     1 
ATOM   2775 C  CA    . LYS   A 1 494  ? 37.188  -32.126 -53.632 1.00 61.59  ? 643  LYS   A CA    1 
ATOM   2776 C  C     . LYS   A 1 494  ? 38.330  -32.451 -54.600 1.00 60.46  ? 643  LYS   A C     1 
ATOM   2777 O  O     . LYS   A 1 494  ? 39.506  -32.406 -54.163 1.00 61.44  ? 643  LYS   A O     1 
ATOM   2778 C  CB    . LYS   A 1 494  ? 36.494  -33.403 -53.145 1.00 60.26  ? 643  LYS   A CB    1 
ATOM   2779 C  CG    . LYS   A 1 494  ? 35.536  -33.205 -51.978 1.00 62.40  ? 643  LYS   A CG    1 
ATOM   2780 C  CD    . LYS   A 1 494  ? 34.697  -34.422 -51.656 1.00 62.61  ? 643  LYS   A CD    1 
ATOM   2781 C  CE    . LYS   A 1 494  ? 33.576  -34.106 -50.689 1.00 67.54  ? 643  LYS   A CE    1 
ATOM   2782 N  NZ    . LYS   A 1 494  ? 32.673  -35.264 -50.479 1.00 68.65  ? 643  LYS   A NZ    1 
ATOM   2783 N  N     . TYR   A 1 495  ? 38.019  -32.736 -55.868 1.00 55.51  ? 644  TYR   A N     1 
ATOM   2784 C  CA    . TYR   A 1 495  ? 39.044  -32.949 -56.925 1.00 56.16  ? 644  TYR   A CA    1 
ATOM   2785 C  C     . TYR   A 1 495  ? 39.985  -31.735 -57.015 1.00 54.49  ? 644  TYR   A C     1 
ATOM   2786 O  O     . TYR   A 1 495  ? 41.188  -31.906 -57.276 1.00 58.30  ? 644  TYR   A O     1 
ATOM   2787 C  CB    . TYR   A 1 495  ? 38.409  -33.206 -58.291 1.00 57.13  ? 644  TYR   A CB    1 
ATOM   2788 C  CG    . TYR   A 1 495  ? 39.425  -33.326 -59.403 1.00 60.41  ? 644  TYR   A CG    1 
ATOM   2789 C  CD1   . TYR   A 1 495  ? 40.140  -34.502 -59.583 1.00 59.01  ? 644  TYR   A CD1   1 
ATOM   2790 C  CD2   . TYR   A 1 495  ? 39.704  -32.261 -60.249 1.00 57.87  ? 644  TYR   A CD2   1 
ATOM   2791 C  CE1   . TYR   A 1 495  ? 41.084  -34.628 -60.593 1.00 63.30  ? 644  TYR   A CE1   1 
ATOM   2792 C  CE2   . TYR   A 1 495  ? 40.649  -32.369 -61.259 1.00 59.32  ? 644  TYR   A CE2   1 
ATOM   2793 C  CZ    . TYR   A 1 495  ? 41.333  -33.562 -61.437 1.00 60.36  ? 644  TYR   A CZ    1 
ATOM   2794 O  OH    . TYR   A 1 495  ? 42.254  -33.700 -62.428 1.00 62.39  ? 644  TYR   A OH    1 
ATOM   2795 N  N     . ILE   A 1 496  ? 39.457  -30.527 -56.822 1.00 51.91  ? 645  ILE   A N     1 
ATOM   2796 C  CA    . ILE   A 1 496  ? 40.242  -29.266 -56.969 1.00 57.47  ? 645  ILE   A CA    1 
ATOM   2797 C  C     . ILE   A 1 496  ? 41.270  -29.156 -55.827 1.00 53.80  ? 645  ILE   A C     1 
ATOM   2798 O  O     . ILE   A 1 496  ? 42.416  -28.766 -56.103 1.00 60.06  ? 645  ILE   A O     1 
ATOM   2799 C  CB    . ILE   A 1 496  ? 39.269  -28.072 -57.066 1.00 56.78  ? 645  ILE   A CB    1 
ATOM   2800 C  CG1   . ILE   A 1 496  ? 38.570  -28.070 -58.430 1.00 51.92  ? 645  ILE   A CG1   1 
ATOM   2801 C  CG2   . ILE   A 1 496  ? 39.976  -26.753 -56.785 1.00 57.70  ? 645  ILE   A CG2   1 
ATOM   2802 C  CD1   . ILE   A 1 496  ? 37.259  -27.334 -58.458 1.00 53.43  ? 645  ILE   A CD1   1 
ATOM   2803 N  N     . GLU   A 1 497  ? 40.869  -29.497 -54.602 1.00 57.80  ? 646  GLU   A N     1 
ATOM   2804 C  CA    . GLU   A 1 497  ? 41.742  -29.620 -53.397 1.00 66.13  ? 646  GLU   A CA    1 
ATOM   2805 C  C     . GLU   A 1 497  ? 43.005  -30.439 -53.723 1.00 66.67  ? 646  GLU   A C     1 
ATOM   2806 O  O     . GLU   A 1 497  ? 44.096  -29.997 -53.342 1.00 74.11  ? 646  GLU   A O     1 
ATOM   2807 C  CB    . GLU   A 1 497  ? 40.988  -30.278 -52.230 1.00 67.16  ? 646  GLU   A CB    1 
ATOM   2808 C  CG    . GLU   A 1 497  ? 39.810  -29.471 -51.683 1.00 63.14  ? 646  GLU   A CG    1 
ATOM   2809 C  CD    . GLU   A 1 497  ? 39.090  -30.095 -50.488 1.00 68.41  ? 646  GLU   A CD    1 
ATOM   2810 O  OE1   . GLU   A 1 497  ? 37.850  -29.910 -50.379 1.00 68.02  ? 646  GLU   A OE1   1 
ATOM   2811 O  OE2   . GLU   A 1 497  ? 39.760  -30.763 -49.659 1.00 65.74  ? 646  GLU   A OE2   1 
ATOM   2812 N  N     . THR   A 1 498  ? 42.871  -31.570 -54.427 1.00 66.24  ? 647  THR   A N     1 
ATOM   2813 C  CA    . THR   A 1 498  ? 43.972  -32.535 -54.707 1.00 65.07  ? 647  THR   A CA    1 
ATOM   2814 C  C     . THR   A 1 498  ? 45.008  -31.931 -55.663 1.00 66.33  ? 647  THR   A C     1 
ATOM   2815 O  O     . THR   A 1 498  ? 46.114  -32.486 -55.724 1.00 73.55  ? 647  THR   A O     1 
ATOM   2816 C  CB    . THR   A 1 498  ? 43.483  -33.867 -55.304 1.00 71.83  ? 647  THR   A CB    1 
ATOM   2817 O  OG1   . THR   A 1 498  ? 43.343  -33.739 -56.721 1.00 66.22  ? 647  THR   A OG1   1 
ATOM   2818 C  CG2   . THR   A 1 498  ? 42.187  -34.372 -54.702 1.00 70.03  ? 647  THR   A CG2   1 
ATOM   2819 N  N     . LEU   A 1 499  ? 44.678  -30.861 -56.392 1.00 71.24  ? 648  LEU   A N     1 
ATOM   2820 C  CA    . LEU   A 1 499  ? 45.584  -30.261 -57.411 1.00 74.46  ? 648  LEU   A CA    1 
ATOM   2821 C  C     . LEU   A 1 499  ? 46.642  -29.406 -56.713 1.00 76.67  ? 648  LEU   A C     1 
ATOM   2822 O  O     . LEU   A 1 499  ? 47.653  -29.081 -57.379 1.00 82.14  ? 648  LEU   A O     1 
ATOM   2823 C  CB    . LEU   A 1 499  ? 44.775  -29.419 -58.404 1.00 78.63  ? 648  LEU   A CB    1 
ATOM   2824 C  CG    . LEU   A 1 499  ? 43.718  -30.181 -59.203 1.00 84.61  ? 648  LEU   A CG    1 
ATOM   2825 C  CD1   . LEU   A 1 499  ? 42.764  -29.219 -59.902 1.00 85.85  ? 648  LEU   A CD1   1 
ATOM   2826 C  CD2   . LEU   A 1 499  ? 44.365  -31.132 -60.206 1.00 81.29  ? 648  LEU   A CD2   1 
ATOM   2827 N  N     . ASN   A 1 500  ? 46.389  -29.036 -55.450 1.00 74.52  ? 649  ASN   A N     1 
ATOM   2828 C  CA    . ASN   A 1 500  ? 47.288  -28.210 -54.600 1.00 82.58  ? 649  ASN   A CA    1 
ATOM   2829 C  C     . ASN   A 1 500  ? 47.801  -27.040 -55.442 1.00 82.93  ? 649  ASN   A C     1 
ATOM   2830 O  O     . ASN   A 1 500  ? 49.027  -26.959 -55.700 1.00 88.85  ? 649  ASN   A O     1 
ATOM   2831 C  CB    . ASN   A 1 500  ? 48.426  -29.029 -53.979 1.00 89.36  ? 649  ASN   A CB    1 
ATOM   2832 C  CG    . ASN   A 1 500  ? 47.953  -30.084 -52.997 1.00 98.28  ? 649  ASN   A CG    1 
ATOM   2833 O  OD1   . ASN   A 1 500  ? 46.757  -30.237 -52.757 1.00 97.33  ? 649  ASN   A OD1   1 
ATOM   2834 N  ND2   . ASN   A 1 500  ? 48.886  -30.829 -52.424 1.00 102.38 ? 649  ASN   A ND2   1 
ATOM   2835 N  N     . VAL   A 1 501  ? 46.865  -26.213 -55.910 1.00 84.09  ? 650  VAL   A N     1 
ATOM   2836 C  CA    . VAL   A 1 501  ? 47.115  -24.822 -56.383 1.00 81.80  ? 650  VAL   A CA    1 
ATOM   2837 C  C     . VAL   A 1 501  ? 46.027  -23.929 -55.788 1.00 79.13  ? 650  VAL   A C     1 
ATOM   2838 O  O     . VAL   A 1 501  ? 44.851  -24.074 -56.109 1.00 74.07  ? 650  VAL   A O     1 
ATOM   2839 C  CB    . VAL   A 1 501  ? 47.186  -24.738 -57.919 1.00 81.32  ? 650  VAL   A CB    1 
ATOM   2840 C  CG1   . VAL   A 1 501  ? 47.531  -23.330 -58.379 1.00 80.91  ? 650  VAL   A CG1   1 
ATOM   2841 C  CG2   . VAL   A 1 501  ? 48.176  -25.748 -58.489 1.00 81.13  ? 650  VAL   A CG2   1 
ATOM   2842 N  N     . PRO   A 1 502  ? 46.375  -23.017 -54.852 1.00 81.76  ? 651  PRO   A N     1 
ATOM   2843 C  CA    . PRO   A 1 502  ? 45.404  -22.083 -54.288 1.00 79.29  ? 651  PRO   A CA    1 
ATOM   2844 C  C     . PRO   A 1 502  ? 44.710  -21.235 -55.364 1.00 72.79  ? 651  PRO   A C     1 
ATOM   2845 O  O     . PRO   A 1 502  ? 45.350  -20.821 -56.313 1.00 69.30  ? 651  PRO   A O     1 
ATOM   2846 C  CB    . PRO   A 1 502  ? 46.240  -21.188 -53.364 1.00 81.96  ? 651  PRO   A CB    1 
ATOM   2847 C  CG    . PRO   A 1 502  ? 47.430  -22.042 -53.014 1.00 87.59  ? 651  PRO   A CG    1 
ATOM   2848 C  CD    . PRO   A 1 502  ? 47.713  -22.853 -54.261 1.00 87.39  ? 651  PRO   A CD    1 
ATOM   2849 N  N     . GLY   A 1 503  ? 43.419  -20.984 -55.163 1.00 66.67  ? 652  GLY   A N     1 
ATOM   2850 C  CA    . GLY   A 1 503  ? 42.558  -20.292 -56.137 1.00 66.48  ? 652  GLY   A CA    1 
ATOM   2851 C  C     . GLY   A 1 503  ? 41.094  -20.404 -55.768 1.00 62.19  ? 652  GLY   A C     1 
ATOM   2852 O  O     . GLY   A 1 503  ? 40.675  -21.476 -55.243 1.00 67.13  ? 652  GLY   A O     1 
ATOM   2853 N  N     . ALA   A 1 504  ? 40.335  -19.345 -56.046 1.00 58.22  ? 653  ALA   A N     1 
ATOM   2854 C  CA    . ALA   A 1 504  ? 38.870  -19.287 -55.834 1.00 56.15  ? 653  ALA   A CA    1 
ATOM   2855 C  C     . ALA   A 1 504  ? 38.173  -20.084 -56.941 1.00 52.03  ? 653  ALA   A C     1 
ATOM   2856 O  O     . ALA   A 1 504  ? 38.745  -20.202 -58.052 1.00 48.22  ? 653  ALA   A O     1 
ATOM   2857 C  CB    . ALA   A 1 504  ? 38.395  -17.854 -55.788 1.00 57.99  ? 653  ALA   A CB    1 
ATOM   2858 N  N     . VAL   A 1 505  ? 37.007  -20.640 -56.601 1.00 52.09  ? 654  VAL   A N     1 
ATOM   2859 C  CA    . VAL   A 1 505  ? 36.095  -21.395 -57.503 1.00 53.52  ? 654  VAL   A CA    1 
ATOM   2860 C  C     . VAL   A 1 505  ? 34.853  -20.538 -57.746 1.00 52.25  ? 654  VAL   A C     1 
ATOM   2861 O  O     . VAL   A 1 505  ? 34.153  -20.192 -56.763 1.00 57.88  ? 654  VAL   A O     1 
ATOM   2862 C  CB    . VAL   A 1 505  ? 35.685  -22.764 -56.932 1.00 58.00  ? 654  VAL   A CB    1 
ATOM   2863 C  CG1   . VAL   A 1 505  ? 35.138  -23.664 -58.036 1.00 58.47  ? 654  VAL   A CG1   1 
ATOM   2864 C  CG2   . VAL   A 1 505  ? 36.821  -23.445 -56.181 1.00 57.46  ? 654  VAL   A CG2   1 
ATOM   2865 N  N     . LEU   A 1 506  ? 34.610  -20.205 -59.012 1.00 48.90  ? 655  LEU   A N     1 
ATOM   2866 C  CA    . LEU   A 1 506  ? 33.376  -19.539 -59.492 1.00 49.73  ? 655  LEU   A CA    1 
ATOM   2867 C  C     . LEU   A 1 506  ? 32.451  -20.613 -60.092 1.00 48.25  ? 655  LEU   A C     1 
ATOM   2868 O  O     . LEU   A 1 506  ? 32.864  -21.301 -61.039 1.00 45.93  ? 655  LEU   A O     1 
ATOM   2869 C  CB    . LEU   A 1 506  ? 33.801  -18.474 -60.505 1.00 49.51  ? 655  LEU   A CB    1 
ATOM   2870 C  CG    . LEU   A 1 506  ? 32.680  -17.638 -61.115 1.00 49.20  ? 655  LEU   A CG    1 
ATOM   2871 C  CD1   . LEU   A 1 506  ? 31.886  -16.919 -60.033 1.00 50.79  ? 655  LEU   A CD1   1 
ATOM   2872 C  CD2   . LEU   A 1 506  ? 33.264  -16.660 -62.112 1.00 49.85  ? 655  LEU   A CD2   1 
ATOM   2873 N  N     . VAL   A 1 507  ? 31.279  -20.803 -59.494 1.00 48.14  ? 656  VAL   A N     1 
ATOM   2874 C  CA    . VAL   A 1 507  ? 30.251  -21.790 -59.934 1.00 52.19  ? 656  VAL   A CA    1 
ATOM   2875 C  C     . VAL   A 1 507  ? 29.094  -20.999 -60.559 1.00 51.17  ? 656  VAL   A C     1 
ATOM   2876 O  O     . VAL   A 1 507  ? 28.500  -20.149 -59.854 1.00 46.07  ? 656  VAL   A O     1 
ATOM   2877 C  CB    . VAL   A 1 507  ? 29.760  -22.698 -58.783 1.00 53.24  ? 656  VAL   A CB    1 
ATOM   2878 C  CG1   . VAL   A 1 507  ? 28.960  -23.877 -59.324 1.00 53.87  ? 656  VAL   A CG1   1 
ATOM   2879 C  CG2   . VAL   A 1 507  ? 30.898  -23.203 -57.902 1.00 49.66  ? 656  VAL   A CG2   1 
ATOM   2880 N  N     . PHE   A 1 508  ? 28.794  -21.251 -61.837 1.00 49.26  ? 657  PHE   A N     1 
ATOM   2881 C  CA    . PHE   A 1 508  ? 27.676  -20.596 -62.569 1.00 41.79  ? 657  PHE   A CA    1 
ATOM   2882 C  C     . PHE   A 1 508  ? 26.441  -21.480 -62.469 1.00 43.68  ? 657  PHE   A C     1 
ATOM   2883 O  O     . PHE   A 1 508  ? 26.448  -22.597 -63.017 1.00 44.68  ? 657  PHE   A O     1 
ATOM   2884 C  CB    . PHE   A 1 508  ? 28.068  -20.322 -64.016 1.00 41.17  ? 657  PHE   A CB    1 
ATOM   2885 C  CG    . PHE   A 1 508  ? 29.089  -19.227 -64.215 1.00 37.80  ? 657  PHE   A CG    1 
ATOM   2886 C  CD1   . PHE   A 1 508  ? 28.720  -17.897 -64.148 1.00 39.77  ? 657  PHE   A CD1   1 
ATOM   2887 C  CD2   . PHE   A 1 508  ? 30.411  -19.523 -64.483 1.00 40.92  ? 657  PHE   A CD2   1 
ATOM   2888 C  CE1   . PHE   A 1 508  ? 29.646  -16.884 -64.350 1.00 40.94  ? 657  PHE   A CE1   1 
ATOM   2889 C  CE2   . PHE   A 1 508  ? 31.338  -18.511 -64.707 1.00 46.07  ? 657  PHE   A CE2   1 
ATOM   2890 C  CZ    . PHE   A 1 508  ? 30.959  -17.192 -64.633 1.00 43.60  ? 657  PHE   A CZ    1 
ATOM   2891 N  N     . LEU   A 1 509  ? 25.435  -20.979 -61.754 1.00 47.89  ? 658  LEU   A N     1 
ATOM   2892 C  CA    . LEU   A 1 509  ? 24.101  -21.589 -61.555 1.00 49.49  ? 658  LEU   A CA    1 
ATOM   2893 C  C     . LEU   A 1 509  ? 23.039  -20.632 -62.094 1.00 53.70  ? 658  LEU   A C     1 
ATOM   2894 O  O     . LEU   A 1 509  ? 23.135  -19.426 -61.901 1.00 50.60  ? 658  LEU   A O     1 
ATOM   2895 C  CB    . LEU   A 1 509  ? 23.912  -21.861 -60.058 1.00 51.26  ? 658  LEU   A CB    1 
ATOM   2896 C  CG    . LEU   A 1 509  ? 24.820  -22.933 -59.445 1.00 53.15  ? 658  LEU   A CG    1 
ATOM   2897 C  CD1   . LEU   A 1 509  ? 24.392  -23.252 -58.015 1.00 54.39  ? 658  LEU   A CD1   1 
ATOM   2898 C  CD2   . LEU   A 1 509  ? 24.810  -24.202 -60.287 1.00 56.62  ? 658  LEU   A CD2   1 
ATOM   2899 N  N     . PRO   A 1 510  ? 21.977  -21.136 -62.761 1.00 60.76  ? 659  PRO   A N     1 
ATOM   2900 C  CA    . PRO   A 1 510  ? 21.016  -20.275 -63.444 1.00 61.66  ? 659  PRO   A CA    1 
ATOM   2901 C  C     . PRO   A 1 510  ? 20.505  -19.124 -62.573 1.00 61.99  ? 659  PRO   A C     1 
ATOM   2902 O  O     . PRO   A 1 510  ? 20.691  -17.991 -62.987 1.00 70.55  ? 659  PRO   A O     1 
ATOM   2903 C  CB    . PRO   A 1 510  ? 19.845  -21.203 -63.785 1.00 60.56  ? 659  PRO   A CB    1 
ATOM   2904 C  CG    . PRO   A 1 510  ? 20.465  -22.583 -63.848 1.00 60.43  ? 659  PRO   A CG    1 
ATOM   2905 C  CD    . PRO   A 1 510  ? 21.628  -22.559 -62.879 1.00 59.95  ? 659  PRO   A CD    1 
ATOM   2906 N  N     . GLY   A 1 511  ? 19.869  -19.442 -61.439 1.00 58.17  ? 660  GLY   A N     1 
ATOM   2907 C  CA    . GLY   A 1 511  ? 19.167  -18.464 -60.581 1.00 58.67  ? 660  GLY   A CA    1 
ATOM   2908 C  C     . GLY   A 1 511  ? 19.301  -18.759 -59.091 1.00 62.05  ? 660  GLY   A C     1 
ATOM   2909 O  O     . GLY   A 1 511  ? 19.926  -19.779 -58.730 1.00 60.31  ? 660  GLY   A O     1 
ATOM   2910 N  N     . TRP   A 1 512  ? 18.715  -17.892 -58.252 1.00 67.66  ? 661  TRP   A N     1 
ATOM   2911 C  CA    . TRP   A 1 512  ? 18.825  -17.916 -56.769 1.00 72.80  ? 661  TRP   A CA    1 
ATOM   2912 C  C     . TRP   A 1 512  ? 18.337  -19.261 -56.215 1.00 75.18  ? 661  TRP   A C     1 
ATOM   2913 O  O     . TRP   A 1 512  ? 18.931  -19.734 -55.230 1.00 73.16  ? 661  TRP   A O     1 
ATOM   2914 C  CB    . TRP   A 1 512  ? 18.111  -16.706 -56.134 1.00 86.03  ? 661  TRP   A CB    1 
ATOM   2915 C  CG    . TRP   A 1 512  ? 16.620  -16.630 -56.291 1.00 108.25 ? 661  TRP   A CG    1 
ATOM   2916 C  CD1   . TRP   A 1 512  ? 15.929  -15.908 -57.224 1.00 111.03 ? 661  TRP   A CD1   1 
ATOM   2917 C  CD2   . TRP   A 1 512  ? 15.625  -17.246 -55.447 1.00 124.66 ? 661  TRP   A CD2   1 
ATOM   2918 N  NE1   . TRP   A 1 512  ? 14.580  -16.060 -57.042 1.00 113.85 ? 661  TRP   A NE1   1 
ATOM   2919 C  CE2   . TRP   A 1 512  ? 14.361  -16.875 -55.962 1.00 122.59 ? 661  TRP   A CE2   1 
ATOM   2920 C  CE3   . TRP   A 1 512  ? 15.674  -18.084 -54.324 1.00 127.70 ? 661  TRP   A CE3   1 
ATOM   2921 C  CZ2   . TRP   A 1 512  ? 13.167  -17.314 -55.387 1.00 127.17 ? 661  TRP   A CZ2   1 
ATOM   2922 C  CZ3   . TRP   A 1 512  ? 14.494  -18.519 -53.759 1.00 128.30 ? 661  TRP   A CZ3   1 
ATOM   2923 C  CH2   . TRP   A 1 512  ? 13.258  -18.138 -54.287 1.00 129.49 ? 661  TRP   A CH2   1 
ATOM   2924 N  N     . ASN   A 1 513  ? 17.330  -19.871 -56.850 1.00 83.12  ? 662  ASN   A N     1 
ATOM   2925 C  CA    . ASN   A 1 513  ? 16.693  -21.141 -56.405 1.00 81.08  ? 662  ASN   A CA    1 
ATOM   2926 C  C     . ASN   A 1 513  ? 17.754  -22.246 -56.322 1.00 73.21  ? 662  ASN   A C     1 
ATOM   2927 O  O     . ASN   A 1 513  ? 17.756  -22.972 -55.298 1.00 74.60  ? 662  ASN   A O     1 
ATOM   2928 C  CB    . ASN   A 1 513  ? 15.514  -21.544 -57.298 1.00 88.86  ? 662  ASN   A CB    1 
ATOM   2929 C  CG    . ASN   A 1 513  ? 14.252  -21.830 -56.507 1.00 97.37  ? 662  ASN   A CG    1 
ATOM   2930 O  OD1   . ASN   A 1 513  ? 13.700  -20.937 -55.854 1.00 93.06  ? 662  ASN   A OD1   1 
ATOM   2931 N  ND2   . ASN   A 1 513  ? 13.787  -23.069 -56.565 1.00 97.09  ? 662  ASN   A ND2   1 
ATOM   2932 N  N     . LEU   A 1 514  ? 18.622  -22.366 -57.334 1.00 66.18  ? 663  LEU   A N     1 
ATOM   2933 C  CA    . LEU   A 1 514  ? 19.677  -23.421 -57.390 1.00 63.72  ? 663  LEU   A CA    1 
ATOM   2934 C  C     . LEU   A 1 514  ? 20.911  -22.987 -56.587 1.00 64.81  ? 663  LEU   A C     1 
ATOM   2935 O  O     . LEU   A 1 514  ? 21.704  -23.866 -56.211 1.00 67.83  ? 663  LEU   A O     1 
ATOM   2936 C  CB    . LEU   A 1 514  ? 20.080  -23.721 -58.837 1.00 62.69  ? 663  LEU   A CB    1 
ATOM   2937 C  CG    . LEU   A 1 514  ? 19.012  -24.293 -59.778 1.00 70.80  ? 663  LEU   A CG    1 
ATOM   2938 C  CD1   . LEU   A 1 514  ? 19.652  -25.262 -60.771 1.00 65.27  ? 663  LEU   A CD1   1 
ATOM   2939 C  CD2   . LEU   A 1 514  ? 17.875  -24.980 -59.031 1.00 76.12  ? 663  LEU   A CD2   1 
ATOM   2940 N  N     . ILE   A 1 515  ? 21.099  -21.691 -56.342 1.00 64.37  ? 664  ILE   A N     1 
ATOM   2941 C  CA    . ILE   A 1 515  ? 22.221  -21.206 -55.484 1.00 61.22  ? 664  ILE   A CA    1 
ATOM   2942 C  C     . ILE   A 1 515  ? 21.911  -21.588 -54.029 1.00 63.17  ? 664  ILE   A C     1 
ATOM   2943 O  O     . ILE   A 1 515  ? 22.776  -22.227 -53.391 1.00 60.47  ? 664  ILE   A O     1 
ATOM   2944 C  CB    . ILE   A 1 515  ? 22.474  -19.703 -55.692 1.00 54.55  ? 664  ILE   A CB    1 
ATOM   2945 C  CG1   . ILE   A 1 515  ? 23.094  -19.457 -57.071 1.00 55.68  ? 664  ILE   A CG1   1 
ATOM   2946 C  CG2   . ILE   A 1 515  ? 23.331  -19.120 -54.569 1.00 59.26  ? 664  ILE   A CG2   1 
ATOM   2947 C  CD1   . ILE   A 1 515  ? 22.781  -18.092 -57.669 1.00 50.36  ? 664  ILE   A CD1   1 
ATOM   2948 N  N     . TYR   A 1 516  ? 20.716  -21.244 -53.542 1.00 69.42  ? 665  TYR   A N     1 
ATOM   2949 C  CA    . TYR   A 1 516  ? 20.195  -21.646 -52.211 1.00 78.39  ? 665  TYR   A CA    1 
ATOM   2950 C  C     . TYR   A 1 516  ? 20.351  -23.164 -52.049 1.00 78.40  ? 665  TYR   A C     1 
ATOM   2951 O  O     . TYR   A 1 516  ? 20.924  -23.596 -51.039 1.00 80.17  ? 665  TYR   A O     1 
ATOM   2952 C  CB    . TYR   A 1 516  ? 18.740  -21.199 -52.058 1.00 90.01  ? 665  TYR   A CB    1 
ATOM   2953 C  CG    . TYR   A 1 516  ? 18.124  -21.440 -50.702 1.00 98.56  ? 665  TYR   A CG    1 
ATOM   2954 C  CD1   . TYR   A 1 516  ? 18.257  -20.515 -49.675 1.00 99.53  ? 665  TYR   A CD1   1 
ATOM   2955 C  CD2   . TYR   A 1 516  ? 17.378  -22.584 -50.456 1.00 101.67 ? 665  TYR   A CD2   1 
ATOM   2956 C  CE1   . TYR   A 1 516  ? 17.673  -20.727 -48.436 1.00 105.69 ? 665  TYR   A CE1   1 
ATOM   2957 C  CE2   . TYR   A 1 516  ? 16.790  -22.812 -49.223 1.00 106.40 ? 665  TYR   A CE2   1 
ATOM   2958 C  CZ    . TYR   A 1 516  ? 16.937  -21.880 -48.210 1.00 110.59 ? 665  TYR   A CZ    1 
ATOM   2959 O  OH    . TYR   A 1 516  ? 16.361  -22.120 -46.997 1.00 109.85 ? 665  TYR   A OH    1 
ATOM   2960 N  N     . THR   A 1 517  ? 19.898  -23.942 -53.036 1.00 75.89  ? 666  THR   A N     1 
ATOM   2961 C  CA    . THR   A 1 517  ? 19.890  -25.429 -52.994 1.00 76.18  ? 666  THR   A CA    1 
ATOM   2962 C  C     . THR   A 1 517  ? 21.323  -25.950 -52.904 1.00 72.92  ? 666  THR   A C     1 
ATOM   2963 O  O     . THR   A 1 517  ? 21.556  -26.855 -52.076 1.00 81.52  ? 666  THR   A O     1 
ATOM   2964 C  CB    . THR   A 1 517  ? 19.172  -26.039 -54.205 1.00 85.06  ? 666  THR   A CB    1 
ATOM   2965 O  OG1   . THR   A 1 517  ? 17.776  -25.773 -54.068 1.00 84.54  ? 666  THR   A OG1   1 
ATOM   2966 C  CG2   . THR   A 1 517  ? 19.386  -27.532 -54.339 1.00 85.20  ? 666  THR   A CG2   1 
ATOM   2967 N  N     . MET   A 1 518  ? 22.237  -25.423 -53.724 1.00 63.15  ? 667  MET   A N     1 
ATOM   2968 C  CA    . MET   A 1 518  ? 23.665  -25.849 -53.719 1.00 60.63  ? 667  MET   A CA    1 
ATOM   2969 C  C     . MET   A 1 518  ? 24.320  -25.489 -52.379 1.00 63.22  ? 667  MET   A C     1 
ATOM   2970 O  O     . MET   A 1 518  ? 25.177  -26.261 -51.898 1.00 62.92  ? 667  MET   A O     1 
ATOM   2971 C  CB    . MET   A 1 518  ? 24.458  -25.182 -54.843 1.00 58.65  ? 667  MET   A CB    1 
ATOM   2972 C  CG    . MET   A 1 518  ? 25.889  -25.673 -54.946 1.00 57.40  ? 667  MET   A CG    1 
ATOM   2973 S  SD    . MET   A 1 518  ? 25.914  -27.439 -55.343 1.00 61.56  ? 667  MET   A SD    1 
ATOM   2974 C  CE    . MET   A 1 518  ? 27.580  -27.886 -54.856 1.00 68.88  ? 667  MET   A CE    1 
ATOM   2975 N  N     . GLN   A 1 519  ? 23.947  -24.349 -51.808 1.00 63.21  ? 668  GLN   A N     1 
ATOM   2976 C  CA    . GLN   A 1 519  ? 24.540  -23.840 -50.547 1.00 74.33  ? 668  GLN   A CA    1 
ATOM   2977 C  C     . GLN   A 1 519  ? 24.149  -24.779 -49.398 1.00 73.88  ? 668  GLN   A C     1 
ATOM   2978 O  O     . GLN   A 1 519  ? 25.067  -25.299 -48.739 1.00 69.75  ? 668  GLN   A O     1 
ATOM   2979 C  CB    . GLN   A 1 519  ? 24.074  -22.404 -50.323 1.00 81.39  ? 668  GLN   A CB    1 
ATOM   2980 C  CG    . GLN   A 1 519  ? 24.906  -21.648 -49.308 1.00 88.89  ? 668  GLN   A CG    1 
ATOM   2981 C  CD    . GLN   A 1 519  ? 24.652  -20.165 -49.409 1.00 96.87  ? 668  GLN   A CD    1 
ATOM   2982 O  OE1   . GLN   A 1 519  ? 23.665  -19.718 -50.012 1.00 83.84  ? 668  GLN   A OE1   1 
ATOM   2983 N  NE2   . GLN   A 1 519  ? 25.561  -19.399 -48.823 1.00 95.60  ? 668  GLN   A NE2   1 
ATOM   2984 N  N     . LYS   A 1 520  ? 22.839  -24.994 -49.200 1.00 82.39  ? 669  LYS   A N     1 
ATOM   2985 C  CA    . LYS   A 1 520  ? 22.260  -25.898 -48.164 1.00 87.33  ? 669  LYS   A CA    1 
ATOM   2986 C  C     . LYS   A 1 520  ? 22.916  -27.275 -48.305 1.00 81.10  ? 669  LYS   A C     1 
ATOM   2987 O  O     . LYS   A 1 520  ? 23.406  -27.803 -47.298 1.00 82.88  ? 669  LYS   A O     1 
ATOM   2988 C  CB    . LYS   A 1 520  ? 20.730  -25.988 -48.260 1.00 93.20  ? 669  LYS   A CB    1 
ATOM   2989 C  CG    . LYS   A 1 520  ? 19.956  -25.217 -47.190 1.00 104.26 ? 669  LYS   A CG    1 
ATOM   2990 C  CD    . LYS   A 1 520  ? 19.969  -23.699 -47.354 1.00 110.36 ? 669  LYS   A CD    1 
ATOM   2991 C  CE    . LYS   A 1 520  ? 21.080  -22.997 -46.593 1.00 112.25 ? 669  LYS   A CE    1 
ATOM   2992 N  NZ    . LYS   A 1 520  ? 21.318  -21.619 -47.092 1.00 108.04 ? 669  LYS   A NZ    1 
ATOM   2993 N  N     . HIS   A 1 521  ? 22.976  -27.801 -49.524 1.00 76.43  ? 670  HIS   A N     1 
ATOM   2994 C  CA    . HIS   A 1 521  ? 23.623  -29.102 -49.824 1.00 74.04  ? 670  HIS   A CA    1 
ATOM   2995 C  C     . HIS   A 1 521  ? 25.042  -29.134 -49.233 1.00 75.41  ? 670  HIS   A C     1 
ATOM   2996 O  O     . HIS   A 1 521  ? 25.380  -30.150 -48.593 1.00 80.69  ? 670  HIS   A O     1 
ATOM   2997 C  CB    . HIS   A 1 521  ? 23.605  -29.389 -51.331 1.00 72.23  ? 670  HIS   A CB    1 
ATOM   2998 C  CG    . HIS   A 1 521  ? 24.295  -30.662 -51.667 1.00 66.72  ? 670  HIS   A CG    1 
ATOM   2999 N  ND1   . HIS   A 1 521  ? 23.623  -31.863 -51.710 1.00 67.14  ? 670  HIS   A ND1   1 
ATOM   3000 C  CD2   . HIS   A 1 521  ? 25.599  -30.929 -51.906 1.00 63.88  ? 670  HIS   A CD2   1 
ATOM   3001 C  CE1   . HIS   A 1 521  ? 24.481  -32.824 -51.986 1.00 73.81  ? 670  HIS   A CE1   1 
ATOM   3002 N  NE2   . HIS   A 1 521  ? 25.706  -32.273 -52.116 1.00 72.52  ? 670  HIS   A NE2   1 
ATOM   3003 N  N     . LEU   A 1 522  ? 25.843  -28.081 -49.427 1.00 67.72  ? 671  LEU   A N     1 
ATOM   3004 C  CA    . LEU   A 1 522  ? 27.258  -28.058 -48.964 1.00 69.12  ? 671  LEU   A CA    1 
ATOM   3005 C  C     . LEU   A 1 522  ? 27.329  -27.981 -47.431 1.00 75.51  ? 671  LEU   A C     1 
ATOM   3006 O  O     . LEU   A 1 522  ? 28.144  -28.722 -46.846 1.00 75.97  ? 671  LEU   A O     1 
ATOM   3007 C  CB    . LEU   A 1 522  ? 28.011  -26.890 -49.609 1.00 66.89  ? 671  LEU   A CB    1 
ATOM   3008 C  CG    . LEU   A 1 522  ? 28.435  -27.103 -51.060 1.00 68.38  ? 671  LEU   A CG    1 
ATOM   3009 C  CD1   . LEU   A 1 522  ? 29.369  -25.989 -51.519 1.00 68.62  ? 671  LEU   A CD1   1 
ATOM   3010 C  CD2   . LEU   A 1 522  ? 29.095  -28.460 -51.253 1.00 63.44  ? 671  LEU   A CD2   1 
ATOM   3011 N  N     . GLU   A 1 523  ? 26.538  -27.120 -46.786 1.00 84.82  ? 672  GLU   A N     1 
ATOM   3012 C  CA    . GLU   A 1 523  ? 26.668  -26.893 -45.318 1.00 95.38  ? 672  GLU   A CA    1 
ATOM   3013 C  C     . GLU   A 1 523  ? 26.074  -28.099 -44.564 1.00 99.67  ? 672  GLU   A C     1 
ATOM   3014 O  O     . GLU   A 1 523  ? 26.252  -28.142 -43.329 1.00 91.21  ? 672  GLU   A O     1 
ATOM   3015 C  CB    . GLU   A 1 523  ? 26.121  -25.516 -44.908 1.00 95.43  ? 672  GLU   A CB    1 
ATOM   3016 C  CG    . GLU   A 1 523  ? 24.615  -25.336 -45.035 1.00 100.52 ? 672  GLU   A CG    1 
ATOM   3017 C  CD    . GLU   A 1 523  ? 24.110  -23.912 -44.803 1.00 106.36 ? 672  GLU   A CD    1 
ATOM   3018 O  OE1   . GLU   A 1 523  ? 24.812  -22.951 -45.208 1.00 108.20 ? 672  GLU   A OE1   1 
ATOM   3019 O  OE2   . GLU   A 1 523  ? 23.008  -23.760 -44.222 1.00 101.28 ? 672  GLU   A OE2   1 
ATOM   3020 N  N     . MET   A 1 524  ? 25.454  -29.061 -45.271 1.00 96.99  ? 673  MET   A N     1 
ATOM   3021 C  CA    . MET   A 1 524  ? 25.098  -30.406 -44.730 1.00 95.99  ? 673  MET   A CA    1 
ATOM   3022 C  C     . MET   A 1 524  ? 26.388  -31.189 -44.439 1.00 88.49  ? 673  MET   A C     1 
ATOM   3023 O  O     . MET   A 1 524  ? 26.482  -31.768 -43.345 1.00 96.30  ? 673  MET   A O     1 
ATOM   3024 C  CB    . MET   A 1 524  ? 24.226  -31.232 -45.688 1.00 100.97 ? 673  MET   A CB    1 
ATOM   3025 C  CG    . MET   A 1 524  ? 22.837  -30.651 -45.978 1.00 111.17 ? 673  MET   A CG    1 
ATOM   3026 S  SD    . MET   A 1 524  ? 21.814  -30.242 -44.519 1.00 119.16 ? 673  MET   A SD    1 
ATOM   3027 C  CE    . MET   A 1 524  ? 22.055  -28.469 -44.386 1.00 112.32 ? 673  MET   A CE    1 
ATOM   3028 N  N     . ASN   A 1 525  ? 27.334  -31.224 -45.382 1.00 75.17  ? 674  ASN   A N     1 
ATOM   3029 C  CA    . ASN   A 1 525  ? 28.669  -31.862 -45.211 1.00 74.38  ? 674  ASN   A CA    1 
ATOM   3030 C  C     . ASN   A 1 525  ? 29.530  -30.900 -44.385 1.00 80.88  ? 674  ASN   A C     1 
ATOM   3031 O  O     . ASN   A 1 525  ? 29.673  -29.733 -44.752 1.00 76.94  ? 674  ASN   A O     1 
ATOM   3032 C  CB    . ASN   A 1 525  ? 29.264  -32.251 -46.569 1.00 70.61  ? 674  ASN   A CB    1 
ATOM   3033 C  CG    . ASN   A 1 525  ? 30.504  -33.121 -46.494 1.00 80.16  ? 674  ASN   A CG    1 
ATOM   3034 O  OD1   . ASN   A 1 525  ? 31.283  -33.043 -45.548 1.00 77.67  ? 674  ASN   A OD1   1 
ATOM   3035 N  ND2   . ASN   A 1 525  ? 30.717  -33.944 -47.511 1.00 84.12  ? 674  ASN   A ND2   1 
ATOM   3036 N  N     . PRO   A 1 526  ? 30.052  -31.316 -43.200 1.00 87.86  ? 675  PRO   A N     1 
ATOM   3037 C  CA    . PRO   A 1 526  ? 30.923  -30.461 -42.383 1.00 80.53  ? 675  PRO   A CA    1 
ATOM   3038 C  C     . PRO   A 1 526  ? 32.338  -30.227 -42.936 1.00 73.04  ? 675  PRO   A C     1 
ATOM   3039 O  O     . PRO   A 1 526  ? 33.054  -29.415 -42.380 1.00 77.14  ? 675  PRO   A O     1 
ATOM   3040 C  CB    . PRO   A 1 526  ? 31.032  -31.209 -41.042 1.00 78.89  ? 675  PRO   A CB    1 
ATOM   3041 C  CG    . PRO   A 1 526  ? 29.871  -32.180 -41.055 1.00 83.94  ? 675  PRO   A CG    1 
ATOM   3042 C  CD    . PRO   A 1 526  ? 29.735  -32.578 -42.509 1.00 87.39  ? 675  PRO   A CD    1 
ATOM   3043 N  N     . HIS   A 1 527  ? 32.722  -30.943 -43.994 1.00 71.44  ? 676  HIS   A N     1 
ATOM   3044 C  CA    . HIS   A 1 527  ? 34.004  -30.738 -44.722 1.00 72.26  ? 676  HIS   A CA    1 
ATOM   3045 C  C     . HIS   A 1 527  ? 34.048  -29.313 -45.298 1.00 70.09  ? 676  HIS   A C     1 
ATOM   3046 O  O     . HIS   A 1 527  ? 35.169  -28.764 -45.372 1.00 67.30  ? 676  HIS   A O     1 
ATOM   3047 C  CB    . HIS   A 1 527  ? 34.204  -31.818 -45.802 1.00 72.69  ? 676  HIS   A CB    1 
ATOM   3048 C  CG    . HIS   A 1 527  ? 35.396  -31.575 -46.668 1.00 79.17  ? 676  HIS   A CG    1 
ATOM   3049 N  ND1   . HIS   A 1 527  ? 36.612  -31.161 -46.153 1.00 88.52  ? 676  HIS   A ND1   1 
ATOM   3050 C  CD2   . HIS   A 1 527  ? 35.564  -31.670 -48.004 1.00 82.97  ? 676  HIS   A CD2   1 
ATOM   3051 C  CE1   . HIS   A 1 527  ? 37.479  -31.021 -47.138 1.00 92.05  ? 676  HIS   A CE1   1 
ATOM   3052 N  NE2   . HIS   A 1 527  ? 36.859  -31.328 -48.284 1.00 83.64  ? 676  HIS   A NE2   1 
ATOM   3053 N  N     . PHE   A 1 528  ? 32.884  -28.743 -45.663 1.00 65.07  ? 677  PHE   A N     1 
ATOM   3054 C  CA    . PHE   A 1 528  ? 32.732  -27.413 -46.322 1.00 69.29  ? 677  PHE   A CA    1 
ATOM   3055 C  C     . PHE   A 1 528  ? 32.415  -26.320 -45.286 1.00 71.60  ? 677  PHE   A C     1 
ATOM   3056 O  O     . PHE   A 1 528  ? 31.685  -25.354 -45.620 1.00 69.66  ? 677  PHE   A O     1 
ATOM   3057 C  CB    . PHE   A 1 528  ? 31.678  -27.491 -47.439 1.00 66.77  ? 677  PHE   A CB    1 
ATOM   3058 C  CG    . PHE   A 1 528  ? 32.078  -28.386 -48.584 1.00 61.18  ? 677  PHE   A CG    1 
ATOM   3059 C  CD1   . PHE   A 1 528  ? 33.086  -28.008 -49.459 1.00 61.33  ? 677  PHE   A CD1   1 
ATOM   3060 C  CD2   . PHE   A 1 528  ? 31.497  -29.633 -48.750 1.00 59.81  ? 677  PHE   A CD2   1 
ATOM   3061 C  CE1   . PHE   A 1 528  ? 33.481  -28.839 -50.499 1.00 58.26  ? 677  PHE   A CE1   1 
ATOM   3062 C  CE2   . PHE   A 1 528  ? 31.900  -30.467 -49.782 1.00 62.89  ? 677  PHE   A CE2   1 
ATOM   3063 C  CZ    . PHE   A 1 528  ? 32.892  -30.069 -50.654 1.00 60.58  ? 677  PHE   A CZ    1 
ATOM   3064 N  N     . GLY   A 1 529  ? 32.985  -26.436 -44.079 1.00 76.82  ? 678  GLY   A N     1 
ATOM   3065 C  CA    . GLY   A 1 529  ? 32.853  -25.446 -42.988 1.00 70.52  ? 678  GLY   A CA    1 
ATOM   3066 C  C     . GLY   A 1 529  ? 33.959  -24.406 -43.043 1.00 71.42  ? 678  GLY   A C     1 
ATOM   3067 O  O     . GLY   A 1 529  ? 34.885  -24.561 -43.881 1.00 72.16  ? 678  GLY   A O     1 
ATOM   3068 N  N     . SER   A 1 530  ? 33.889  -23.405 -42.160 1.00 67.13  ? 679  SER   A N     1 
ATOM   3069 C  CA    . SER   A 1 530  ? 34.739  -22.183 -42.158 1.00 71.66  ? 679  SER   A CA    1 
ATOM   3070 C  C     . SER   A 1 530  ? 36.232  -22.534 -42.131 1.00 76.14  ? 679  SER   A C     1 
ATOM   3071 O  O     . SER   A 1 530  ? 37.031  -21.748 -42.691 1.00 78.33  ? 679  SER   A O     1 
ATOM   3072 C  CB    . SER   A 1 530  ? 34.384  -21.300 -41.000 1.00 74.16  ? 679  SER   A CB    1 
ATOM   3073 O  OG    . SER   A 1 530  ? 33.005  -21.410 -40.716 1.00 74.90  ? 679  SER   A OG    1 
ATOM   3074 N  N     . HIS   A 1 531  ? 36.607  -23.640 -41.482 1.00 73.73  ? 680  HIS   A N     1 
ATOM   3075 C  CA    . HIS   A 1 531  ? 38.023  -24.082 -41.353 1.00 79.41  ? 680  HIS   A CA    1 
ATOM   3076 C  C     . HIS   A 1 531  ? 38.680  -24.195 -42.742 1.00 80.11  ? 680  HIS   A C     1 
ATOM   3077 O  O     . HIS   A 1 531  ? 39.915  -23.959 -42.834 1.00 73.10  ? 680  HIS   A O     1 
ATOM   3078 C  CB    . HIS   A 1 531  ? 38.128  -25.377 -40.522 1.00 81.06  ? 680  HIS   A CB    1 
ATOM   3079 C  CG    . HIS   A 1 531  ? 37.372  -26.551 -41.052 1.00 85.83  ? 680  HIS   A CG    1 
ATOM   3080 N  ND1   . HIS   A 1 531  ? 36.043  -26.788 -40.715 1.00 91.35  ? 680  HIS   A ND1   1 
ATOM   3081 C  CD2   . HIS   A 1 531  ? 37.756  -27.579 -41.847 1.00 87.84  ? 680  HIS   A CD2   1 
ATOM   3082 C  CE1   . HIS   A 1 531  ? 35.637  -27.899 -41.303 1.00 96.61  ? 680  HIS   A CE1   1 
ATOM   3083 N  NE2   . HIS   A 1 531  ? 36.672  -28.404 -42.009 1.00 94.21  ? 680  HIS   A NE2   1 
ATOM   3084 N  N     . ARG   A 1 532  ? 37.895  -24.527 -43.778 1.00 82.09  ? 681  ARG   A N     1 
ATOM   3085 C  CA    . ARG   A 1 532  ? 38.403  -24.882 -45.135 1.00 79.69  ? 681  ARG   A CA    1 
ATOM   3086 C  C     . ARG   A 1 532  ? 37.754  -24.020 -46.237 1.00 70.76  ? 681  ARG   A C     1 
ATOM   3087 O  O     . ARG   A 1 532  ? 38.425  -23.797 -47.262 1.00 68.79  ? 681  ARG   A O     1 
ATOM   3088 C  CB    . ARG   A 1 532  ? 38.173  -26.383 -45.366 1.00 79.02  ? 681  ARG   A CB    1 
ATOM   3089 C  CG    . ARG   A 1 532  ? 38.922  -26.978 -46.553 1.00 82.95  ? 681  ARG   A CG    1 
ATOM   3090 C  CD    . ARG   A 1 532  ? 40.438  -26.864 -46.481 1.00 83.04  ? 681  ARG   A CD    1 
ATOM   3091 N  NE    . ARG   A 1 532  ? 41.082  -27.176 -47.754 1.00 82.78  ? 681  ARG   A NE    1 
ATOM   3092 C  CZ    . ARG   A 1 532  ? 41.084  -26.386 -48.828 1.00 81.21  ? 681  ARG   A CZ    1 
ATOM   3093 N  NH1   . ARG   A 1 532  ? 40.464  -25.217 -48.811 1.00 77.14  ? 681  ARG   A NH1   1 
ATOM   3094 N  NH2   . ARG   A 1 532  ? 41.706  -26.777 -49.927 1.00 77.84  ? 681  ARG   A NH2   1 
ATOM   3095 N  N     . TYR   A 1 533  ? 36.518  -23.542 -46.059 1.00 64.99  ? 682  TYR   A N     1 
ATOM   3096 C  CA    . TYR   A 1 533  ? 35.670  -23.048 -47.178 1.00 65.11  ? 682  TYR   A CA    1 
ATOM   3097 C  C     . TYR   A 1 533  ? 34.910  -21.767 -46.820 1.00 61.86  ? 682  TYR   A C     1 
ATOM   3098 O  O     . TYR   A 1 533  ? 34.182  -21.744 -45.806 1.00 61.84  ? 682  TYR   A O     1 
ATOM   3099 C  CB    . TYR   A 1 533  ? 34.675  -24.131 -47.591 1.00 61.46  ? 682  TYR   A CB    1 
ATOM   3100 C  CG    . TYR   A 1 533  ? 35.222  -25.101 -48.602 1.00 60.30  ? 682  TYR   A CG    1 
ATOM   3101 C  CD1   . TYR   A 1 533  ? 35.280  -24.768 -49.945 1.00 62.38  ? 682  TYR   A CD1   1 
ATOM   3102 C  CD2   . TYR   A 1 533  ? 35.668  -26.352 -48.224 1.00 59.47  ? 682  TYR   A CD2   1 
ATOM   3103 C  CE1   . TYR   A 1 533  ? 35.775  -25.652 -50.889 1.00 63.47  ? 682  TYR   A CE1   1 
ATOM   3104 C  CE2   . TYR   A 1 533  ? 36.167  -27.251 -49.154 1.00 65.01  ? 682  TYR   A CE2   1 
ATOM   3105 C  CZ    . TYR   A 1 533  ? 36.221  -26.899 -50.492 1.00 66.93  ? 682  TYR   A CZ    1 
ATOM   3106 O  OH    . TYR   A 1 533  ? 36.711  -27.778 -51.414 1.00 63.63  ? 682  TYR   A OH    1 
ATOM   3107 N  N     . GLN   A 1 534  ? 35.049  -20.748 -47.674 1.00 63.00  ? 683  GLN   A N     1 
ATOM   3108 C  CA    . GLN   A 1 534  ? 34.190  -19.535 -47.690 1.00 62.84  ? 683  GLN   A CA    1 
ATOM   3109 C  C     . GLN   A 1 534  ? 33.298  -19.628 -48.941 1.00 63.19  ? 683  GLN   A C     1 
ATOM   3110 O  O     . GLN   A 1 534  ? 33.808  -19.447 -50.070 1.00 59.84  ? 683  GLN   A O     1 
ATOM   3111 C  CB    . GLN   A 1 534  ? 35.063  -18.277 -47.594 1.00 67.50  ? 683  GLN   A CB    1 
ATOM   3112 C  CG    . GLN   A 1 534  ? 34.302  -16.965 -47.423 1.00 71.29  ? 683  GLN   A CG    1 
ATOM   3113 C  CD    . GLN   A 1 534  ? 33.352  -16.922 -46.245 1.00 78.95  ? 683  GLN   A CD    1 
ATOM   3114 O  OE1   . GLN   A 1 534  ? 32.885  -17.942 -45.744 1.00 86.94  ? 683  GLN   A OE1   1 
ATOM   3115 N  NE2   . GLN   A 1 534  ? 33.016  -15.720 -45.806 1.00 80.08  ? 683  GLN   A NE2   1 
ATOM   3116 N  N     . ILE   A 1 535  ? 32.022  -19.967 -48.730 1.00 58.28  ? 684  ILE   A N     1 
ATOM   3117 C  CA    . ILE   A 1 535  ? 31.006  -20.258 -49.781 1.00 57.65  ? 684  ILE   A CA    1 
ATOM   3118 C  C     . ILE   A 1 535  ? 30.036  -19.086 -49.776 1.00 55.56  ? 684  ILE   A C     1 
ATOM   3119 O  O     . ILE   A 1 535  ? 29.322  -18.959 -48.775 1.00 53.63  ? 684  ILE   A O     1 
ATOM   3120 C  CB    . ILE   A 1 535  ? 30.306  -21.610 -49.511 1.00 60.18  ? 684  ILE   A CB    1 
ATOM   3121 C  CG1   . ILE   A 1 535  ? 31.253  -22.790 -49.758 1.00 62.94  ? 684  ILE   A CG1   1 
ATOM   3122 C  CG2   . ILE   A 1 535  ? 29.027  -21.756 -50.323 1.00 60.67  ? 684  ILE   A CG2   1 
ATOM   3123 C  CD1   . ILE   A 1 535  ? 30.885  -24.036 -48.994 1.00 62.61  ? 684  ILE   A CD1   1 
ATOM   3124 N  N     . LEU   A 1 536  ? 30.049  -18.257 -50.828 1.00 57.01  ? 685  LEU   A N     1 
ATOM   3125 C  CA    . LEU   A 1 536  ? 29.307  -16.966 -50.874 1.00 56.91  ? 685  LEU   A CA    1 
ATOM   3126 C  C     . LEU   A 1 536  ? 28.346  -16.975 -52.053 1.00 56.64  ? 685  LEU   A C     1 
ATOM   3127 O  O     . LEU   A 1 536  ? 28.740  -17.261 -53.182 1.00 54.35  ? 685  LEU   A O     1 
ATOM   3128 C  CB    . LEU   A 1 536  ? 30.303  -15.807 -50.977 1.00 59.11  ? 685  LEU   A CB    1 
ATOM   3129 C  CG    . LEU   A 1 536  ? 31.274  -15.680 -49.799 1.00 57.55  ? 685  LEU   A CG    1 
ATOM   3130 C  CD1   . LEU   A 1 536  ? 32.441  -14.753 -50.128 1.00 52.65  ? 685  LEU   A CD1   1 
ATOM   3131 C  CD2   . LEU   A 1 536  ? 30.541  -15.208 -48.552 1.00 58.65  ? 685  LEU   A CD2   1 
ATOM   3132 N  N     . PRO   A 1 537  ? 27.053  -16.662 -51.822 1.00 59.08  ? 686  PRO   A N     1 
ATOM   3133 C  CA    . PRO   A 1 537  ? 26.079  -16.574 -52.905 1.00 57.24  ? 686  PRO   A CA    1 
ATOM   3134 C  C     . PRO   A 1 537  ? 26.258  -15.221 -53.605 1.00 56.90  ? 686  PRO   A C     1 
ATOM   3135 O  O     . PRO   A 1 537  ? 26.536  -14.269 -52.901 1.00 62.31  ? 686  PRO   A O     1 
ATOM   3136 C  CB    . PRO   A 1 537  ? 24.753  -16.651 -52.146 1.00 61.58  ? 686  PRO   A CB    1 
ATOM   3137 C  CG    . PRO   A 1 537  ? 25.051  -15.897 -50.858 1.00 59.30  ? 686  PRO   A CG    1 
ATOM   3138 C  CD    . PRO   A 1 537  ? 26.470  -16.301 -50.520 1.00 60.15  ? 686  PRO   A CD    1 
ATOM   3139 N  N     . LEU   A 1 538  ? 26.145  -15.177 -54.937 1.00 54.62  ? 687  LEU   A N     1 
ATOM   3140 C  CA    . LEU   A 1 538  ? 26.132  -13.913 -55.734 1.00 54.68  ? 687  LEU   A CA    1 
ATOM   3141 C  C     . LEU   A 1 538  ? 24.925  -13.924 -56.684 1.00 55.09  ? 687  LEU   A C     1 
ATOM   3142 O  O     . LEU   A 1 538  ? 24.968  -14.613 -57.710 1.00 58.98  ? 687  LEU   A O     1 
ATOM   3143 C  CB    . LEU   A 1 538  ? 27.456  -13.776 -56.488 1.00 47.75  ? 687  LEU   A CB    1 
ATOM   3144 C  CG    . LEU   A 1 538  ? 27.597  -12.526 -57.352 1.00 52.01  ? 687  LEU   A CG    1 
ATOM   3145 C  CD1   . LEU   A 1 538  ? 27.043  -11.292 -56.663 1.00 51.75  ? 687  LEU   A CD1   1 
ATOM   3146 C  CD2   . LEU   A 1 538  ? 29.048  -12.302 -57.736 1.00 54.56  ? 687  LEU   A CD2   1 
ATOM   3147 N  N     . HIS   A 1 539  ? 23.850  -13.253 -56.294 1.00 58.58  ? 688  HIS   A N     1 
ATOM   3148 C  CA    . HIS   A 1 539  ? 22.687  -12.940 -57.158 1.00 64.80  ? 688  HIS   A CA    1 
ATOM   3149 C  C     . HIS   A 1 539  ? 22.185  -11.538 -56.799 1.00 69.94  ? 688  HIS   A C     1 
ATOM   3150 O  O     . HIS   A 1 539  ? 22.696  -10.946 -55.841 1.00 66.95  ? 688  HIS   A O     1 
ATOM   3151 C  CB    . HIS   A 1 539  ? 21.626  -14.039 -57.073 1.00 61.23  ? 688  HIS   A CB    1 
ATOM   3152 C  CG    . HIS   A 1 539  ? 21.194  -14.415 -55.697 1.00 63.60  ? 688  HIS   A CG    1 
ATOM   3153 N  ND1   . HIS   A 1 539  ? 20.205  -13.726 -55.020 1.00 68.40  ? 688  HIS   A ND1   1 
ATOM   3154 C  CD2   . HIS   A 1 539  ? 21.550  -15.451 -54.901 1.00 67.26  ? 688  HIS   A CD2   1 
ATOM   3155 C  CE1   . HIS   A 1 539  ? 19.983  -14.313 -53.856 1.00 71.37  ? 688  HIS   A CE1   1 
ATOM   3156 N  NE2   . HIS   A 1 539  ? 20.802  -15.374 -53.756 1.00 70.37  ? 688  HIS   A NE2   1 
ATOM   3157 N  N     . SER   A 1 540  ? 21.247  -11.006 -57.575 1.00 82.00  ? 689  SER   A N     1 
ATOM   3158 C  CA    . SER   A 1 540  ? 20.866  -9.572  -57.543 1.00 85.09  ? 689  SER   A CA    1 
ATOM   3159 C  C     . SER   A 1 540  ? 20.095  -9.250  -56.257 1.00 81.81  ? 689  SER   A C     1 
ATOM   3160 O  O     . SER   A 1 540  ? 19.997  -8.052  -55.936 1.00 80.16  ? 689  SER   A O     1 
ATOM   3161 C  CB    . SER   A 1 540  ? 20.080  -9.197  -58.782 1.00 85.13  ? 689  SER   A CB    1 
ATOM   3162 O  OG    . SER   A 1 540  ? 18.895  -9.972  -58.881 1.00 84.60  ? 689  SER   A OG    1 
ATOM   3163 N  N     . GLN   A 1 541  ? 19.594  -10.270 -55.548 1.00 78.02  ? 690  GLN   A N     1 
ATOM   3164 C  CA    . GLN   A 1 541  ? 18.668  -10.104 -54.394 1.00 81.52  ? 690  GLN   A CA    1 
ATOM   3165 C  C     . GLN   A 1 541  ? 19.387  -10.275 -53.044 1.00 79.34  ? 690  GLN   A C     1 
ATOM   3166 O  O     . GLN   A 1 541  ? 18.763  -9.949  -52.020 1.00 73.90  ? 690  GLN   A O     1 
ATOM   3167 C  CB    . GLN   A 1 541  ? 17.480  -11.056 -54.545 1.00 83.99  ? 690  GLN   A CB    1 
ATOM   3168 C  CG    . GLN   A 1 541  ? 16.691  -10.830 -55.836 1.00 91.06  ? 690  GLN   A CG    1 
ATOM   3169 C  CD    . GLN   A 1 541  ? 16.214  -9.405  -56.016 1.00 92.43  ? 690  GLN   A CD    1 
ATOM   3170 O  OE1   . GLN   A 1 541  ? 16.149  -8.617  -55.073 1.00 97.97  ? 690  GLN   A OE1   1 
ATOM   3171 N  NE2   . GLN   A 1 541  ? 15.863  -9.054  -57.242 1.00 92.37  ? 690  GLN   A NE2   1 
ATOM   3172 N  N     . ILE   A 1 542  ? 20.646  -10.715 -53.012 1.00 74.66  ? 691  ILE   A N     1 
ATOM   3173 C  CA    . ILE   A 1 542  ? 21.434  -10.707 -51.744 1.00 81.13  ? 691  ILE   A CA    1 
ATOM   3174 C  C     . ILE   A 1 542  ? 21.839  -9.265  -51.442 1.00 83.06  ? 691  ILE   A C     1 
ATOM   3175 O  O     . ILE   A 1 542  ? 22.136  -8.505  -52.363 1.00 70.81  ? 691  ILE   A O     1 
ATOM   3176 C  CB    . ILE   A 1 542  ? 22.652  -11.653 -51.779 1.00 83.17  ? 691  ILE   A CB    1 
ATOM   3177 C  CG1   . ILE   A 1 542  ? 23.758  -11.170 -52.719 1.00 85.13  ? 691  ILE   A CG1   1 
ATOM   3178 C  CG2   . ILE   A 1 542  ? 22.236  -13.084 -52.087 1.00 82.80  ? 691  ILE   A CG2   1 
ATOM   3179 C  CD1   . ILE   A 1 542  ? 25.147  -11.520 -52.233 1.00 88.28  ? 691  ILE   A CD1   1 
ATOM   3180 N  N     . PRO   A 1 543  ? 21.880  -8.858  -50.148 1.00 85.75  ? 692  PRO   A N     1 
ATOM   3181 C  CA    . PRO   A 1 543  ? 22.174  -7.475  -49.769 1.00 85.10  ? 692  PRO   A CA    1 
ATOM   3182 C  C     . PRO   A 1 543  ? 23.584  -7.047  -50.199 1.00 80.84  ? 692  PRO   A C     1 
ATOM   3183 O  O     . PRO   A 1 543  ? 24.453  -7.901  -50.297 1.00 77.61  ? 692  PRO   A O     1 
ATOM   3184 C  CB    . PRO   A 1 543  ? 22.072  -7.453  -48.233 1.00 90.57  ? 692  PRO   A CB    1 
ATOM   3185 C  CG    . PRO   A 1 543  ? 21.355  -8.740  -47.859 1.00 89.01  ? 692  PRO   A CG    1 
ATOM   3186 C  CD    . PRO   A 1 543  ? 21.672  -9.718  -48.971 1.00 88.58  ? 692  PRO   A CD    1 
ATOM   3187 N  N     . ARG   A 1 544  ? 23.781  -5.747  -50.433 1.00 77.72  ? 693  ARG   A N     1 
ATOM   3188 C  CA    . ARG   A 1 544  ? 25.017  -5.206  -51.062 1.00 81.17  ? 693  ARG   A CA    1 
ATOM   3189 C  C     . ARG   A 1 544  ? 26.207  -5.415  -50.122 1.00 80.83  ? 693  ARG   A C     1 
ATOM   3190 O  O     . ARG   A 1 544  ? 27.331  -5.646  -50.628 1.00 80.87  ? 693  ARG   A O     1 
ATOM   3191 C  CB    . ARG   A 1 544  ? 24.822  -3.741  -51.467 1.00 82.74  ? 693  ARG   A CB    1 
ATOM   3192 C  CG    . ARG   A 1 544  ? 23.909  -3.577  -52.673 1.00 81.54  ? 693  ARG   A CG    1 
ATOM   3193 C  CD    . ARG   A 1 544  ? 24.331  -2.438  -53.568 1.00 78.79  ? 693  ARG   A CD    1 
ATOM   3194 N  NE    . ARG   A 1 544  ? 24.334  -1.178  -52.837 1.00 87.31  ? 693  ARG   A NE    1 
ATOM   3195 C  CZ    . ARG   A 1 544  ? 23.248  -0.487  -52.459 1.00 84.62  ? 693  ARG   A CZ    1 
ATOM   3196 N  NH1   . ARG   A 1 544  ? 23.394  0.660   -51.807 1.00 72.59  ? 693  ARG   A NH1   1 
ATOM   3197 N  NH2   . ARG   A 1 544  ? 22.028  -0.928  -52.738 1.00 80.25  ? 693  ARG   A NH2   1 
ATOM   3198 N  N     . GLU   A 1 545  ? 25.966  -5.363  -48.812 1.00 86.72  ? 694  GLU   A N     1 
ATOM   3199 C  CA    . GLU   A 1 545  ? 26.946  -5.792  -47.779 1.00 92.09  ? 694  GLU   A CA    1 
ATOM   3200 C  C     . GLU   A 1 545  ? 27.515  -7.169  -48.179 1.00 85.86  ? 694  GLU   A C     1 
ATOM   3201 O  O     . GLU   A 1 545  ? 28.753  -7.292  -48.306 1.00 80.41  ? 694  GLU   A O     1 
ATOM   3202 C  CB    . GLU   A 1 545  ? 26.266  -5.784  -46.407 1.00 100.52 ? 694  GLU   A CB    1 
ATOM   3203 C  CG    . GLU   A 1 545  ? 27.234  -5.897  -45.243 1.00 112.05 ? 694  GLU   A CG    1 
ATOM   3204 C  CD    . GLU   A 1 545  ? 26.564  -6.150  -43.903 1.00 118.84 ? 694  GLU   A CD    1 
ATOM   3205 O  OE1   . GLU   A 1 545  ? 25.566  -5.463  -43.604 1.00 124.79 ? 694  GLU   A OE1   1 
ATOM   3206 O  OE2   . GLU   A 1 545  ? 27.036  -7.039  -43.165 1.00 116.55 ? 694  GLU   A OE2   1 
ATOM   3207 N  N     . GLU   A 1 546  ? 26.642  -8.156  -48.417 1.00 81.78  ? 695  GLU   A N     1 
ATOM   3208 C  CA    . GLU   A 1 546  ? 27.011  -9.564  -48.746 1.00 76.66  ? 695  GLU   A CA    1 
ATOM   3209 C  C     . GLU   A 1 546  ? 27.653  -9.651  -50.138 1.00 73.45  ? 695  GLU   A C     1 
ATOM   3210 O  O     . GLU   A 1 546  ? 28.529  -10.509 -50.324 1.00 69.49  ? 695  GLU   A O     1 
ATOM   3211 C  CB    . GLU   A 1 546  ? 25.778  -10.464 -48.684 1.00 83.36  ? 695  GLU   A CB    1 
ATOM   3212 C  CG    . GLU   A 1 546  ? 25.113  -10.512 -47.320 1.00 90.35  ? 695  GLU   A CG    1 
ATOM   3213 C  CD    . GLU   A 1 546  ? 25.507  -11.711 -46.477 1.00 103.86 ? 695  GLU   A CD    1 
ATOM   3214 O  OE1   . GLU   A 1 546  ? 24.733  -12.700 -46.472 1.00 111.76 ? 695  GLU   A OE1   1 
ATOM   3215 O  OE2   . GLU   A 1 546  ? 26.585  -11.654 -45.831 1.00 98.18  ? 695  GLU   A OE2   1 
ATOM   3216 N  N     . GLN   A 1 547  ? 27.228  -8.813  -51.089 1.00 77.40  ? 696  GLN   A N     1 
ATOM   3217 C  CA    . GLN   A 1 547  ? 27.739  -8.819  -52.490 1.00 74.04  ? 696  GLN   A CA    1 
ATOM   3218 C  C     . GLN   A 1 547  ? 29.229  -8.479  -52.509 1.00 70.04  ? 696  GLN   A C     1 
ATOM   3219 O  O     . GLN   A 1 547  ? 29.973  -9.155  -53.258 1.00 62.11  ? 696  GLN   A O     1 
ATOM   3220 C  CB    . GLN   A 1 547  ? 26.974  -7.829  -53.368 1.00 80.06  ? 696  GLN   A CB    1 
ATOM   3221 C  CG    . GLN   A 1 547  ? 25.811  -8.458  -54.126 1.00 88.68  ? 696  GLN   A CG    1 
ATOM   3222 C  CD    . GLN   A 1 547  ? 24.663  -7.503  -54.351 1.00 92.82  ? 696  GLN   A CD    1 
ATOM   3223 O  OE1   . GLN   A 1 547  ? 24.805  -6.289  -54.208 1.00 95.02  ? 696  GLN   A OE1   1 
ATOM   3224 N  NE2   . GLN   A 1 547  ? 23.506  -8.050  -54.692 1.00 91.41  ? 696  GLN   A NE2   1 
ATOM   3225 N  N     . ARG   A 1 548  ? 29.636  -7.462  -51.743 1.00 70.62  ? 697  ARG   A N     1 
ATOM   3226 C  CA    . ARG   A 1 548  ? 31.036  -6.953  -51.708 1.00 72.32  ? 697  ARG   A CA    1 
ATOM   3227 C  C     . ARG   A 1 548  ? 31.984  -8.068  -51.246 1.00 68.31  ? 697  ARG   A C     1 
ATOM   3228 O  O     . ARG   A 1 548  ? 33.117  -8.100  -51.750 1.00 60.48  ? 697  ARG   A O     1 
ATOM   3229 C  CB    . ARG   A 1 548  ? 31.158  -5.722  -50.801 1.00 80.03  ? 697  ARG   A CB    1 
ATOM   3230 C  CG    . ARG   A 1 548  ? 30.558  -4.447  -51.382 1.00 85.93  ? 697  ARG   A CG    1 
ATOM   3231 C  CD    . ARG   A 1 548  ? 30.741  -3.228  -50.486 1.00 87.45  ? 697  ARG   A CD    1 
ATOM   3232 N  NE    . ARG   A 1 548  ? 29.564  -2.910  -49.682 1.00 84.26  ? 697  ARG   A NE    1 
ATOM   3233 C  CZ    . ARG   A 1 548  ? 28.530  -2.164  -50.085 1.00 92.03  ? 697  ARG   A CZ    1 
ATOM   3234 N  NH1   . ARG   A 1 548  ? 27.513  -1.935  -49.266 1.00 90.50  ? 697  ARG   A NH1   1 
ATOM   3235 N  NH2   . ARG   A 1 548  ? 28.510  -1.645  -51.301 1.00 95.60  ? 697  ARG   A NH2   1 
ATOM   3236 N  N     . LYS   A 1 549  ? 31.521  -8.964  -50.362 1.00 71.22  ? 698  LYS   A N     1 
ATOM   3237 C  CA    . LYS   A 1 549  ? 32.337  -10.041 -49.726 1.00 77.72  ? 698  LYS   A CA    1 
ATOM   3238 C  C     . LYS   A 1 549  ? 32.949  -11.004 -50.760 1.00 81.10  ? 698  LYS   A C     1 
ATOM   3239 O  O     . LYS   A 1 549  ? 33.891  -11.745 -50.375 1.00 75.84  ? 698  LYS   A O     1 
ATOM   3240 C  CB    . LYS   A 1 549  ? 31.500  -10.854 -48.730 1.00 81.71  ? 698  LYS   A CB    1 
ATOM   3241 C  CG    . LYS   A 1 549  ? 31.138  -10.144 -47.432 1.00 87.69  ? 698  LYS   A CG    1 
ATOM   3242 C  CD    . LYS   A 1 549  ? 30.292  -11.000 -46.515 1.00 89.55  ? 698  LYS   A CD    1 
ATOM   3243 C  CE    . LYS   A 1 549  ? 30.066  -10.374 -45.157 1.00 94.63  ? 698  LYS   A CE    1 
ATOM   3244 N  NZ    . LYS   A 1 549  ? 28.962  -11.053 -44.443 1.00 97.65  ? 698  LYS   A NZ    1 
ATOM   3245 N  N     . VAL   A 1 550  ? 32.446  -11.040 -52.004 1.00 72.31  ? 699  VAL   A N     1 
ATOM   3246 C  CA    . VAL   A 1 550  ? 32.989  -11.941 -53.067 1.00 68.72  ? 699  VAL   A CA    1 
ATOM   3247 C  C     . VAL   A 1 550  ? 34.337  -11.385 -53.543 1.00 65.55  ? 699  VAL   A C     1 
ATOM   3248 O  O     . VAL   A 1 550  ? 35.062  -12.121 -54.234 1.00 63.82  ? 699  VAL   A O     1 
ATOM   3249 C  CB    . VAL   A 1 550  ? 32.005  -12.146 -54.240 1.00 69.60  ? 699  VAL   A CB    1 
ATOM   3250 C  CG1   . VAL   A 1 550  ? 30.614  -12.534 -53.751 1.00 68.67  ? 699  VAL   A CG1   1 
ATOM   3251 C  CG2   . VAL   A 1 550  ? 31.944  -10.939 -55.168 1.00 66.95  ? 699  VAL   A CG2   1 
ATOM   3252 N  N     . PHE   A 1 551  ? 34.667  -10.141 -53.181 1.00 68.34  ? 700  PHE   A N     1 
ATOM   3253 C  CA    . PHE   A 1 551  ? 35.923  -9.450  -53.581 1.00 72.48  ? 700  PHE   A CA    1 
ATOM   3254 C  C     . PHE   A 1 551  ? 36.997  -9.592  -52.490 1.00 71.84  ? 700  PHE   A C     1 
ATOM   3255 O  O     . PHE   A 1 551  ? 38.195  -9.551  -52.861 1.00 69.53  ? 700  PHE   A O     1 
ATOM   3256 C  CB    . PHE   A 1 551  ? 35.638  -7.983  -53.911 1.00 67.43  ? 700  PHE   A CB    1 
ATOM   3257 C  CG    . PHE   A 1 551  ? 34.879  -7.788  -55.195 1.00 64.16  ? 700  PHE   A CG    1 
ATOM   3258 C  CD1   . PHE   A 1 551  ? 35.486  -8.051  -56.415 1.00 60.01  ? 700  PHE   A CD1   1 
ATOM   3259 C  CD2   . PHE   A 1 551  ? 33.559  -7.355  -55.187 1.00 60.63  ? 700  PHE   A CD2   1 
ATOM   3260 C  CE1   . PHE   A 1 551  ? 34.790  -7.874  -57.602 1.00 57.46  ? 700  PHE   A CE1   1 
ATOM   3261 C  CE2   . PHE   A 1 551  ? 32.863  -7.180  -56.377 1.00 54.55  ? 700  PHE   A CE2   1 
ATOM   3262 C  CZ    . PHE   A 1 551  ? 33.480  -7.446  -57.581 1.00 56.01  ? 700  PHE   A CZ    1 
ATOM   3263 N  N     . ASP   A 1 552  ? 36.591  -9.752  -51.221 1.00 71.01  ? 701  ASP   A N     1 
ATOM   3264 C  CA    . ASP   A 1 552  ? 37.497  -9.893  -50.041 1.00 81.31  ? 701  ASP   A CA    1 
ATOM   3265 C  C     . ASP   A 1 552  ? 38.508  -11.014 -50.253 1.00 87.21  ? 701  ASP   A C     1 
ATOM   3266 O  O     . ASP   A 1 552  ? 38.150  -12.095 -50.722 1.00 83.69  ? 701  ASP   A O     1 
ATOM   3267 C  CB    . ASP   A 1 552  ? 36.747  -10.255 -48.756 1.00 79.33  ? 701  ASP   A CB    1 
ATOM   3268 C  CG    . ASP   A 1 552  ? 35.920  -9.123  -48.177 1.00 79.81  ? 701  ASP   A CG    1 
ATOM   3269 O  OD1   . ASP   A 1 552  ? 36.202  -7.953  -48.523 1.00 68.01  ? 701  ASP   A OD1   1 
ATOM   3270 O  OD2   . ASP   A 1 552  ? 35.001  -9.426  -47.377 1.00 83.59  ? 701  ASP   A OD2   1 
ATOM   3271 N  N     . PRO   A 1 553  ? 39.798  -10.795 -49.904 1.00 99.86  ? 702  PRO   A N     1 
ATOM   3272 C  CA    . PRO   A 1 553  ? 40.742  -11.900 -49.716 1.00 96.03  ? 702  PRO   A CA    1 
ATOM   3273 C  C     . PRO   A 1 553  ? 40.308  -12.846 -48.584 1.00 83.64  ? 702  PRO   A C     1 
ATOM   3274 O  O     . PRO   A 1 553  ? 39.415  -12.510 -47.809 1.00 69.81  ? 702  PRO   A O     1 
ATOM   3275 C  CB    . PRO   A 1 553  ? 42.075  -11.203 -49.393 1.00 100.98 ? 702  PRO   A CB    1 
ATOM   3276 C  CG    . PRO   A 1 553  ? 41.910  -9.805  -49.970 1.00 106.40 ? 702  PRO   A CG    1 
ATOM   3277 C  CD    . PRO   A 1 553  ? 40.444  -9.479  -49.765 1.00 103.69 ? 702  PRO   A CD    1 
ATOM   3278 N  N     . VAL   A 1 554  ? 40.966  -14.001 -48.497 1.00 78.97  ? 703  VAL   A N     1 
ATOM   3279 C  CA    . VAL   A 1 554  ? 40.490  -15.151 -47.677 1.00 83.14  ? 703  VAL   A CA    1 
ATOM   3280 C  C     . VAL   A 1 554  ? 41.649  -15.706 -46.830 1.00 79.48  ? 703  VAL   A C     1 
ATOM   3281 O  O     . VAL   A 1 554  ? 42.788  -15.750 -47.298 1.00 78.34  ? 703  VAL   A O     1 
ATOM   3282 C  CB    . VAL   A 1 554  ? 39.828  -16.161 -48.645 1.00 83.98  ? 703  VAL   A CB    1 
ATOM   3283 C  CG1   . VAL   A 1 554  ? 40.816  -17.112 -49.309 1.00 80.31  ? 703  VAL   A CG1   1 
ATOM   3284 C  CG2   . VAL   A 1 554  ? 38.686  -16.923 -47.992 1.00 83.34  ? 703  VAL   A CG2   1 
ATOM   3285 N  N     . PRO   A 1 555  ? 41.420  -16.120 -45.550 1.00 77.67  ? 704  PRO   A N     1 
ATOM   3286 C  CA    . PRO   A 1 555  ? 42.459  -16.759 -44.734 1.00 77.93  ? 704  PRO   A CA    1 
ATOM   3287 C  C     . PRO   A 1 555  ? 43.204  -17.872 -45.485 1.00 83.03  ? 704  PRO   A C     1 
ATOM   3288 O  O     . PRO   A 1 555  ? 42.541  -18.709 -46.084 1.00 83.41  ? 704  PRO   A O     1 
ATOM   3289 C  CB    . PRO   A 1 555  ? 41.703  -17.390 -43.550 1.00 73.71  ? 704  PRO   A CB    1 
ATOM   3290 C  CG    . PRO   A 1 555  ? 40.409  -16.596 -43.439 1.00 74.65  ? 704  PRO   A CG    1 
ATOM   3291 C  CD    . PRO   A 1 555  ? 40.146  -16.007 -44.815 1.00 79.87  ? 704  PRO   A CD    1 
ATOM   3292 N  N     . SER   A 1 556  ? 44.541  -17.864 -45.443 1.00 85.41  ? 705  SER   A N     1 
ATOM   3293 C  CA    . SER   A 1 556  ? 45.411  -18.870 -46.115 1.00 89.99  ? 705  SER   A CA    1 
ATOM   3294 C  C     . SER   A 1 556  ? 44.925  -20.284 -45.752 1.00 86.79  ? 705  SER   A C     1 
ATOM   3295 O  O     . SER   A 1 556  ? 44.637  -20.514 -44.558 1.00 71.23  ? 705  SER   A O     1 
ATOM   3296 C  CB    . SER   A 1 556  ? 46.865  -18.668 -45.756 1.00 92.56  ? 705  SER   A CB    1 
ATOM   3297 O  OG    . SER   A 1 556  ? 47.707  -19.421 -46.620 1.00 92.71  ? 705  SER   A OG    1 
ATOM   3298 N  N     . GLY   A 1 557  ? 44.780  -21.167 -46.752 1.00 79.64  ? 706  GLY   A N     1 
ATOM   3299 C  CA    . GLY   A 1 557  ? 44.294  -22.555 -46.582 1.00 75.75  ? 706  GLY   A CA    1 
ATOM   3300 C  C     . GLY   A 1 557  ? 42.773  -22.652 -46.543 1.00 78.94  ? 706  GLY   A C     1 
ATOM   3301 O  O     . GLY   A 1 557  ? 42.262  -23.760 -46.275 1.00 76.51  ? 706  GLY   A O     1 
ATOM   3302 N  N     . VAL   A 1 558  ? 42.067  -21.538 -46.770 1.00 78.22  ? 707  VAL   A N     1 
ATOM   3303 C  CA    . VAL   A 1 558  ? 40.597  -21.513 -47.030 1.00 75.54  ? 707  VAL   A CA    1 
ATOM   3304 C  C     . VAL   A 1 558  ? 40.381  -21.245 -48.525 1.00 72.04  ? 707  VAL   A C     1 
ATOM   3305 O  O     . VAL   A 1 558  ? 41.170  -20.482 -49.128 1.00 65.28  ? 707  VAL   A O     1 
ATOM   3306 C  CB    . VAL   A 1 558  ? 39.864  -20.493 -46.138 1.00 74.14  ? 707  VAL   A CB    1 
ATOM   3307 C  CG1   . VAL   A 1 558  ? 38.433  -20.229 -46.602 1.00 72.54  ? 707  VAL   A CG1   1 
ATOM   3308 C  CG2   . VAL   A 1 558  ? 39.873  -20.943 -44.687 1.00 75.55  ? 707  VAL   A CG2   1 
ATOM   3309 N  N     . THR   A 1 559  ? 39.363  -21.892 -49.096 1.00 70.03  ? 708  THR   A N     1 
ATOM   3310 C  CA    . THR   A 1 559  ? 38.959  -21.767 -50.520 1.00 69.04  ? 708  THR   A CA    1 
ATOM   3311 C  C     . THR   A 1 559  ? 37.699  -20.909 -50.583 1.00 62.56  ? 708  THR   A C     1 
ATOM   3312 O  O     . THR   A 1 559  ? 36.728  -21.260 -49.867 1.00 63.10  ? 708  THR   A O     1 
ATOM   3313 C  CB    . THR   A 1 559  ? 38.749  -23.147 -51.153 1.00 68.28  ? 708  THR   A CB    1 
ATOM   3314 O  OG1   . THR   A 1 559  ? 40.047  -23.730 -51.236 1.00 68.30  ? 708  THR   A OG1   1 
ATOM   3315 C  CG2   . THR   A 1 559  ? 38.124  -23.096 -52.529 1.00 70.07  ? 708  THR   A CG2   1 
ATOM   3316 N  N     . LYS   A 1 560  ? 37.753  -19.813 -51.350 1.00 56.67  ? 709  LYS   A N     1 
ATOM   3317 C  CA    . LYS   A 1 560  ? 36.581  -18.950 -51.687 1.00 56.43  ? 709  LYS   A CA    1 
ATOM   3318 C  C     . LYS   A 1 560  ? 35.768  -19.633 -52.796 1.00 50.88  ? 709  LYS   A C     1 
ATOM   3319 O  O     . LYS   A 1 560  ? 36.325  -19.928 -53.869 1.00 47.62  ? 709  LYS   A O     1 
ATOM   3320 C  CB    . LYS   A 1 560  ? 37.022  -17.560 -52.161 1.00 56.34  ? 709  LYS   A CB    1 
ATOM   3321 C  CG    . LYS   A 1 560  ? 35.915  -16.508 -52.164 1.00 56.99  ? 709  LYS   A CG    1 
ATOM   3322 C  CD    . LYS   A 1 560  ? 36.361  -15.112 -52.581 1.00 61.77  ? 709  LYS   A CD    1 
ATOM   3323 C  CE    . LYS   A 1 560  ? 37.261  -15.086 -53.802 1.00 65.38  ? 709  LYS   A CE    1 
ATOM   3324 N  NZ    . LYS   A 1 560  ? 37.624  -13.701 -54.196 1.00 67.56  ? 709  LYS   A NZ    1 
ATOM   3325 N  N     . VAL   A 1 561  ? 34.499  -19.916 -52.553 1.00 51.60  ? 710  VAL   A N     1 
ATOM   3326 C  CA    . VAL   A 1 561  ? 33.611  -20.454 -53.618 1.00 52.81  ? 710  VAL   A CA    1 
ATOM   3327 C  C     . VAL   A 1 561  ? 32.454  -19.475 -53.811 1.00 51.64  ? 710  VAL   A C     1 
ATOM   3328 O  O     . VAL   A 1 561  ? 31.697  -19.257 -52.844 1.00 47.64  ? 710  VAL   A O     1 
ATOM   3329 C  CB    . VAL   A 1 561  ? 33.130  -21.873 -53.294 1.00 51.08  ? 710  VAL   A CB    1 
ATOM   3330 C  CG1   . VAL   A 1 561  ? 32.237  -22.416 -54.397 1.00 52.37  ? 710  VAL   A CG1   1 
ATOM   3331 C  CG2   . VAL   A 1 561  ? 34.316  -22.793 -53.053 1.00 52.64  ? 710  VAL   A CG2   1 
ATOM   3332 N  N     . ILE   A 1 562  ? 32.351  -18.914 -55.019 1.00 49.58  ? 711  ILE   A N     1 
ATOM   3333 C  CA    . ILE   A 1 562  ? 31.231  -18.023 -55.436 1.00 54.47  ? 711  ILE   A CA    1 
ATOM   3334 C  C     . ILE   A 1 562  ? 30.196  -18.855 -56.203 1.00 48.27  ? 711  ILE   A C     1 
ATOM   3335 O  O     . ILE   A 1 562  ? 30.506  -19.309 -57.325 1.00 47.07  ? 711  ILE   A O     1 
ATOM   3336 C  CB    . ILE   A 1 562  ? 31.729  -16.841 -56.294 1.00 60.28  ? 711  ILE   A CB    1 
ATOM   3337 C  CG1   . ILE   A 1 562  ? 33.123  -16.361 -55.876 1.00 61.53  ? 711  ILE   A CG1   1 
ATOM   3338 C  CG2   . ILE   A 1 562  ? 30.695  -15.717 -56.282 1.00 53.37  ? 711  ILE   A CG2   1 
ATOM   3339 C  CD1   . ILE   A 1 562  ? 33.190  -15.851 -54.452 1.00 65.87  ? 711  ILE   A CD1   1 
ATOM   3340 N  N     . LEU   A 1 563  ? 29.017  -19.024 -55.614 1.00 44.06  ? 712  LEU   A N     1 
ATOM   3341 C  CA    . LEU   A 1 563  ? 27.816  -19.579 -56.281 1.00 43.60  ? 712  LEU   A CA    1 
ATOM   3342 C  C     . LEU   A 1 563  ? 27.076  -18.394 -56.900 1.00 49.36  ? 712  LEU   A C     1 
ATOM   3343 O  O     . LEU   A 1 563  ? 26.355  -17.691 -56.169 1.00 52.79  ? 712  LEU   A O     1 
ATOM   3344 C  CB    . LEU   A 1 563  ? 26.967  -20.344 -55.262 1.00 43.22  ? 712  LEU   A CB    1 
ATOM   3345 C  CG    . LEU   A 1 563  ? 27.718  -21.389 -54.427 1.00 44.95  ? 712  LEU   A CG    1 
ATOM   3346 C  CD1   . LEU   A 1 563  ? 26.752  -22.152 -53.529 1.00 47.74  ? 712  LEU   A CD1   1 
ATOM   3347 C  CD2   . LEU   A 1 563  ? 28.489  -22.368 -55.310 1.00 44.80  ? 712  LEU   A CD2   1 
ATOM   3348 N  N     . SER   A 1 564  ? 27.299  -18.177 -58.198 1.00 50.46  ? 713  SER   A N     1 
ATOM   3349 C  CA    . SER   A 1 564  ? 26.967  -16.942 -58.951 1.00 54.78  ? 713  SER   A CA    1 
ATOM   3350 C  C     . SER   A 1 564  ? 25.930  -17.194 -60.063 1.00 54.26  ? 713  SER   A C     1 
ATOM   3351 O  O     . SER   A 1 564  ? 25.996  -18.240 -60.712 1.00 56.52  ? 713  SER   A O     1 
ATOM   3352 C  CB    . SER   A 1 564  ? 28.231  -16.392 -59.537 1.00 54.74  ? 713  SER   A CB    1 
ATOM   3353 O  OG    . SER   A 1 564  ? 27.968  -15.183 -60.213 1.00 57.10  ? 713  SER   A OG    1 
ATOM   3354 N  N     . THR   A 1 565  ? 25.040  -16.232 -60.309 1.00 52.29  ? 714  THR   A N     1 
ATOM   3355 C  CA    . THR   A 1 565  ? 24.293  -16.078 -61.589 1.00 49.23  ? 714  THR   A CA    1 
ATOM   3356 C  C     . THR   A 1 565  ? 25.263  -15.562 -62.670 1.00 48.10  ? 714  THR   A C     1 
ATOM   3357 O  O     . THR   A 1 565  ? 26.455  -15.387 -62.387 1.00 48.89  ? 714  THR   A O     1 
ATOM   3358 C  CB    . THR   A 1 565  ? 23.063  -15.165 -61.425 1.00 54.15  ? 714  THR   A CB    1 
ATOM   3359 O  OG1   . THR   A 1 565  ? 23.470  -13.839 -61.073 1.00 46.75  ? 714  THR   A OG1   1 
ATOM   3360 C  CG2   . THR   A 1 565  ? 22.070  -15.680 -60.402 1.00 49.38  ? 714  THR   A CG2   1 
ATOM   3361 N  N     . ASN   A 1 566  ? 24.776  -15.341 -63.885 1.00 47.60  ? 715  ASN   A N     1 
ATOM   3362 C  CA    . ASN   A 1 566  ? 25.593  -14.895 -65.040 1.00 46.94  ? 715  ASN   A CA    1 
ATOM   3363 C  C     . ASN   A 1 566  ? 25.984  -13.415 -64.914 1.00 45.75  ? 715  ASN   A C     1 
ATOM   3364 O  O     . ASN   A 1 566  ? 26.606  -12.927 -65.866 1.00 44.38  ? 715  ASN   A O     1 
ATOM   3365 C  CB    . ASN   A 1 566  ? 24.846  -15.113 -66.350 1.00 48.18  ? 715  ASN   A CB    1 
ATOM   3366 C  CG    . ASN   A 1 566  ? 23.595  -14.264 -66.430 1.00 55.36  ? 715  ASN   A CG    1 
ATOM   3367 O  OD1   . ASN   A 1 566  ? 23.233  -13.563 -65.477 1.00 54.20  ? 715  ASN   A OD1   1 
ATOM   3368 N  ND2   . ASN   A 1 566  ? 22.927  -14.320 -67.565 1.00 52.61  ? 715  ASN   A ND2   1 
ATOM   3369 N  N     . ILE   A 1 567  ? 25.628  -12.724 -63.823 1.00 47.09  ? 716  ILE   A N     1 
ATOM   3370 C  CA    . ILE   A 1 567  ? 26.247  -11.420 -63.410 1.00 54.62  ? 716  ILE   A CA    1 
ATOM   3371 C  C     . ILE   A 1 567  ? 27.779  -11.522 -63.535 1.00 53.54  ? 716  ILE   A C     1 
ATOM   3372 O  O     . ILE   A 1 567  ? 28.422  -10.555 -63.996 1.00 51.59  ? 716  ILE   A O     1 
ATOM   3373 C  CB    . ILE   A 1 567  ? 25.812  -11.023 -61.978 1.00 60.51  ? 716  ILE   A CB    1 
ATOM   3374 C  CG1   . ILE   A 1 567  ? 26.290  -9.628  -61.577 1.00 68.14  ? 716  ILE   A CG1   1 
ATOM   3375 C  CG2   . ILE   A 1 567  ? 26.290  -12.042 -60.962 1.00 66.63  ? 716  ILE   A CG2   1 
ATOM   3376 C  CD1   . ILE   A 1 567  ? 25.631  -8.507  -62.334 1.00 75.72  ? 716  ILE   A CD1   1 
ATOM   3377 N  N     . ALA   A 1 568  ? 28.364  -12.659 -63.160 1.00 53.73  ? 717  ALA   A N     1 
ATOM   3378 C  CA    . ALA   A 1 568  ? 29.835  -12.842 -63.107 1.00 55.82  ? 717  ALA   A CA    1 
ATOM   3379 C  C     . ALA   A 1 568  ? 30.371  -13.367 -64.446 1.00 51.11  ? 717  ALA   A C     1 
ATOM   3380 O  O     . ALA   A 1 568  ? 31.533  -13.806 -64.482 1.00 50.47  ? 717  ALA   A O     1 
ATOM   3381 C  CB    . ALA   A 1 568  ? 30.195  -13.761 -61.959 1.00 54.07  ? 717  ALA   A CB    1 
ATOM   3382 N  N     . GLU   A 1 569  ? 29.559  -13.330 -65.504 1.00 52.70  ? 718  GLU   A N     1 
ATOM   3383 C  CA    . GLU   A 1 569  ? 29.956  -13.758 -66.875 1.00 52.69  ? 718  GLU   A CA    1 
ATOM   3384 C  C     . GLU   A 1 569  ? 30.769  -12.638 -67.546 1.00 47.83  ? 718  GLU   A C     1 
ATOM   3385 O  O     . GLU   A 1 569  ? 31.886  -12.920 -68.020 1.00 52.25  ? 718  GLU   A O     1 
ATOM   3386 C  CB    . GLU   A 1 569  ? 28.708  -14.133 -67.680 1.00 55.97  ? 718  GLU   A CB    1 
ATOM   3387 C  CG    . GLU   A 1 569  ? 29.003  -14.827 -68.997 1.00 58.67  ? 718  GLU   A CG    1 
ATOM   3388 C  CD    . GLU   A 1 569  ? 27.799  -15.409 -69.731 1.00 62.16  ? 718  GLU   A CD    1 
ATOM   3389 O  OE1   . GLU   A 1 569  ? 26.995  -16.137 -69.108 1.00 57.90  ? 718  GLU   A OE1   1 
ATOM   3390 O  OE2   . GLU   A 1 569  ? 27.684  -15.149 -70.948 1.00 69.14  ? 718  GLU   A OE2   1 
ATOM   3391 N  N     . THR   A 1 570  ? 30.228  -11.416 -67.604 1.00 46.51  ? 719  THR   A N     1 
ATOM   3392 C  CA    . THR   A 1 570  ? 30.853  -10.257 -68.307 1.00 45.02  ? 719  THR   A CA    1 
ATOM   3393 C  C     . THR   A 1 570  ? 30.709  -8.932  -67.544 1.00 42.74  ? 719  THR   A C     1 
ATOM   3394 O  O     . THR   A 1 570  ? 31.384  -7.979  -67.951 1.00 49.99  ? 719  THR   A O     1 
ATOM   3395 C  CB    . THR   A 1 570  ? 30.236  -10.057 -69.688 1.00 46.69  ? 719  THR   A CB    1 
ATOM   3396 O  OG1   . THR   A 1 570  ? 28.863  -9.724  -69.462 1.00 51.27  ? 719  THR   A OG1   1 
ATOM   3397 C  CG2   . THR   A 1 570  ? 30.363  -11.278 -70.572 1.00 47.63  ? 719  THR   A CG2   1 
ATOM   3398 N  N     . SER   A 1 571  ? 29.859  -8.817  -66.527 1.00 42.99  ? 720  SER   A N     1 
ATOM   3399 C  CA    . SER   A 1 571  ? 29.578  -7.499  -65.898 1.00 53.10  ? 720  SER   A CA    1 
ATOM   3400 C  C     . SER   A 1 571  ? 30.520  -7.257  -64.700 1.00 54.27  ? 720  SER   A C     1 
ATOM   3401 O  O     . SER   A 1 571  ? 30.940  -6.098  -64.500 1.00 55.20  ? 720  SER   A O     1 
ATOM   3402 C  CB    . SER   A 1 571  ? 28.114  -7.332  -65.567 1.00 54.45  ? 720  SER   A CB    1 
ATOM   3403 O  OG    . SER   A 1 571  ? 27.856  -7.655  -64.214 1.00 64.82  ? 720  SER   A OG    1 
ATOM   3404 N  N     . ILE   A 1 572  ? 30.905  -8.287  -63.950 1.00 53.71  ? 721  ILE   A N     1 
ATOM   3405 C  CA    . ILE   A 1 572  ? 31.925  -8.121  -62.866 1.00 59.61  ? 721  ILE   A CA    1 
ATOM   3406 C  C     . ILE   A 1 572  ? 33.015  -9.191  -62.973 1.00 56.31  ? 721  ILE   A C     1 
ATOM   3407 O  O     . ILE   A 1 572  ? 32.773  -10.257 -63.554 1.00 64.18  ? 721  ILE   A O     1 
ATOM   3408 C  CB    . ILE   A 1 572  ? 31.286  -8.128  -61.466 1.00 60.07  ? 721  ILE   A CB    1 
ATOM   3409 C  CG1   . ILE   A 1 572  ? 31.043  -9.551  -60.965 1.00 61.85  ? 721  ILE   A CG1   1 
ATOM   3410 C  CG2   . ILE   A 1 572  ? 30.018  -7.292  -61.434 1.00 61.50  ? 721  ILE   A CG2   1 
ATOM   3411 C  CD1   . ILE   A 1 572  ? 30.591  -9.606  -59.528 1.00 69.14  ? 721  ILE   A CD1   1 
ATOM   3412 N  N     . THR   A 1 573  ? 34.173  -8.905  -62.385 1.00 55.99  ? 722  THR   A N     1 
ATOM   3413 C  CA    . THR   A 1 573  ? 35.354  -9.792  -62.380 1.00 57.84  ? 722  THR   A CA    1 
ATOM   3414 C  C     . THR   A 1 573  ? 35.753  -10.072 -60.935 1.00 60.54  ? 722  THR   A C     1 
ATOM   3415 O  O     . THR   A 1 573  ? 36.284  -9.168  -60.278 1.00 61.97  ? 722  THR   A O     1 
ATOM   3416 C  CB    . THR   A 1 573  ? 36.511  -9.154  -63.150 1.00 64.51  ? 722  THR   A CB    1 
ATOM   3417 O  OG1   . THR   A 1 573  ? 36.089  -8.954  -64.498 1.00 63.37  ? 722  THR   A OG1   1 
ATOM   3418 C  CG2   . THR   A 1 573  ? 37.764  -9.999  -63.103 1.00 64.67  ? 722  THR   A CG2   1 
ATOM   3419 N  N     . ILE   A 1 574  ? 35.515  -11.287 -60.463 1.00 64.56  ? 723  ILE   A N     1 
ATOM   3420 C  CA    . ILE   A 1 574  ? 35.998  -11.729 -59.127 1.00 66.00  ? 723  ILE   A CA    1 
ATOM   3421 C  C     . ILE   A 1 574  ? 37.492  -12.034 -59.253 1.00 66.68  ? 723  ILE   A C     1 
ATOM   3422 O  O     . ILE   A 1 574  ? 37.875  -12.715 -60.207 1.00 63.45  ? 723  ILE   A O     1 
ATOM   3423 C  CB    . ILE   A 1 574  ? 35.159  -12.924 -58.648 1.00 69.25  ? 723  ILE   A CB    1 
ATOM   3424 C  CG1   . ILE   A 1 574  ? 33.680  -12.536 -58.547 1.00 63.93  ? 723  ILE   A CG1   1 
ATOM   3425 C  CG2   . ILE   A 1 574  ? 35.697  -13.478 -57.334 1.00 71.92  ? 723  ILE   A CG2   1 
ATOM   3426 C  CD1   . ILE   A 1 574  ? 32.745  -13.703 -58.709 1.00 65.63  ? 723  ILE   A CD1   1 
ATOM   3427 N  N     . ASN   A 1 575  ? 38.327  -11.509 -58.354 1.00 83.28  ? 724  ASN   A N     1 
ATOM   3428 C  CA    . ASN   A 1 575  ? 39.794  -11.764 -58.402 1.00 86.52  ? 724  ASN   A CA    1 
ATOM   3429 C  C     . ASN   A 1 575  ? 40.092  -13.095 -57.688 1.00 82.33  ? 724  ASN   A C     1 
ATOM   3430 O  O     . ASN   A 1 575  ? 39.223  -13.575 -56.909 1.00 70.14  ? 724  ASN   A O     1 
ATOM   3431 C  CB    . ASN   A 1 575  ? 40.588  -10.557 -57.889 1.00 93.48  ? 724  ASN   A CB    1 
ATOM   3432 C  CG    . ASN   A 1 575  ? 40.883  -9.534  -58.972 1.00 101.43 ? 724  ASN   A CG    1 
ATOM   3433 O  OD1   . ASN   A 1 575  ? 40.239  -9.509  -60.026 1.00 81.87  ? 724  ASN   A OD1   1 
ATOM   3434 N  ND2   . ASN   A 1 575  ? 41.868  -8.683  -58.724 1.00 100.31 ? 724  ASN   A ND2   1 
ATOM   3435 N  N     . ASP   A 1 576  ? 41.252  -13.692 -57.992 1.00 80.64  ? 725  ASP   A N     1 
ATOM   3436 C  CA    . ASP   A 1 576  ? 41.767  -14.937 -57.358 1.00 82.40  ? 725  ASP   A CA    1 
ATOM   3437 C  C     . ASP   A 1 576  ? 41.103  -16.167 -58.009 1.00 75.10  ? 725  ASP   A C     1 
ATOM   3438 O  O     . ASP   A 1 576  ? 41.347  -17.289 -57.517 1.00 76.25  ? 725  ASP   A O     1 
ATOM   3439 C  CB    . ASP   A 1 576  ? 41.573  -14.878 -55.831 1.00 93.36  ? 725  ASP   A CB    1 
ATOM   3440 C  CG    . ASP   A 1 576  ? 42.354  -15.892 -54.994 1.00 102.95 ? 725  ASP   A CG    1 
ATOM   3441 O  OD1   . ASP   A 1 576  ? 43.454  -16.322 -55.434 1.00 90.75  ? 725  ASP   A OD1   1 
ATOM   3442 O  OD2   . ASP   A 1 576  ? 41.850  -16.250 -53.892 1.00 104.28 ? 725  ASP   A OD2   1 
ATOM   3443 N  N     . VAL   A 1 577  ? 40.338  -16.004 -59.099 1.00 68.37  ? 726  VAL   A N     1 
ATOM   3444 C  CA    . VAL   A 1 577  ? 39.575  -17.136 -59.714 1.00 57.78  ? 726  VAL   A CA    1 
ATOM   3445 C  C     . VAL   A 1 577  ? 40.523  -17.949 -60.596 1.00 53.07  ? 726  VAL   A C     1 
ATOM   3446 O  O     . VAL   A 1 577  ? 41.178  -17.368 -61.500 1.00 53.68  ? 726  VAL   A O     1 
ATOM   3447 C  CB    . VAL   A 1 577  ? 38.316  -16.691 -60.482 1.00 56.01  ? 726  VAL   A CB    1 
ATOM   3448 C  CG1   . VAL   A 1 577  ? 37.517  -17.888 -60.970 1.00 54.49  ? 726  VAL   A CG1   1 
ATOM   3449 C  CG2   . VAL   A 1 577  ? 37.426  -15.806 -59.628 1.00 57.21  ? 726  VAL   A CG2   1 
ATOM   3450 N  N     . VAL   A 1 578  ? 40.613  -19.248 -60.301 1.00 53.56  ? 727  VAL   A N     1 
ATOM   3451 C  CA    . VAL   A 1 578  ? 41.477  -20.224 -61.032 1.00 53.49  ? 727  VAL   A CA    1 
ATOM   3452 C  C     . VAL   A 1 578  ? 40.595  -21.360 -61.554 1.00 51.22  ? 727  VAL   A C     1 
ATOM   3453 O  O     . VAL   A 1 578  ? 41.016  -22.032 -62.505 1.00 54.15  ? 727  VAL   A O     1 
ATOM   3454 C  CB    . VAL   A 1 578  ? 42.613  -20.737 -60.116 1.00 56.26  ? 727  VAL   A CB    1 
ATOM   3455 C  CG1   . VAL   A 1 578  ? 43.557  -21.715 -60.817 1.00 54.53  ? 727  VAL   A CG1   1 
ATOM   3456 C  CG2   . VAL   A 1 578  ? 43.402  -19.576 -59.532 1.00 55.34  ? 727  VAL   A CG2   1 
ATOM   3457 N  N     . TYR   A 1 579  ? 39.417  -21.549 -60.955 1.00 55.85  ? 728  TYR   A N     1 
ATOM   3458 C  CA    . TYR   A 1 579  ? 38.496  -22.687 -61.208 1.00 59.39  ? 728  TYR   A CA    1 
ATOM   3459 C  C     . TYR   A 1 579  ? 37.090  -22.141 -61.448 1.00 56.19  ? 728  TYR   A C     1 
ATOM   3460 O  O     . TYR   A 1 579  ? 36.621  -21.321 -60.626 1.00 51.93  ? 728  TYR   A O     1 
ATOM   3461 C  CB    . TYR   A 1 579  ? 38.514  -23.684 -60.040 1.00 63.00  ? 728  TYR   A CB    1 
ATOM   3462 C  CG    . TYR   A 1 579  ? 39.900  -24.107 -59.619 1.00 64.31  ? 728  TYR   A CG    1 
ATOM   3463 C  CD1   . TYR   A 1 579  ? 40.585  -25.116 -60.283 1.00 64.90  ? 728  TYR   A CD1   1 
ATOM   3464 C  CD2   . TYR   A 1 579  ? 40.547  -23.464 -58.578 1.00 65.15  ? 728  TYR   A CD2   1 
ATOM   3465 C  CE1   . TYR   A 1 579  ? 41.863  -25.496 -59.898 1.00 67.72  ? 728  TYR   A CE1   1 
ATOM   3466 C  CE2   . TYR   A 1 579  ? 41.826  -23.824 -58.186 1.00 68.07  ? 728  TYR   A CE2   1 
ATOM   3467 C  CZ    . TYR   A 1 579  ? 42.489  -24.841 -58.849 1.00 67.45  ? 728  TYR   A CZ    1 
ATOM   3468 O  OH    . TYR   A 1 579  ? 43.755  -25.169 -58.460 1.00 64.15  ? 728  TYR   A OH    1 
ATOM   3469 N  N     . VAL   A 1 580  ? 36.487  -22.567 -62.564 1.00 51.27  ? 729  VAL   A N     1 
ATOM   3470 C  CA    . VAL   A 1 580  ? 35.070  -22.325 -62.955 1.00 49.08  ? 729  VAL   A CA    1 
ATOM   3471 C  C     . VAL   A 1 580  ? 34.372  -23.684 -63.083 1.00 48.54  ? 729  VAL   A C     1 
ATOM   3472 O  O     . VAL   A 1 580  ? 34.886  -24.545 -63.811 1.00 50.56  ? 729  VAL   A O     1 
ATOM   3473 C  CB    . VAL   A 1 580  ? 34.992  -21.549 -64.284 1.00 51.30  ? 729  VAL   A CB    1 
ATOM   3474 C  CG1   . VAL   A 1 580  ? 33.592  -21.605 -64.883 1.00 49.97  ? 729  VAL   A CG1   1 
ATOM   3475 C  CG2   . VAL   A 1 580  ? 35.457  -20.110 -64.129 1.00 49.96  ? 729  VAL   A CG2   1 
ATOM   3476 N  N     . ILE   A 1 581  ? 33.257  -23.871 -62.385 1.00 47.20  ? 730  ILE   A N     1 
ATOM   3477 C  CA    . ILE   A 1 581  ? 32.272  -24.962 -62.643 1.00 54.54  ? 730  ILE   A CA    1 
ATOM   3478 C  C     . ILE   A 1 581  ? 31.056  -24.282 -63.283 1.00 52.53  ? 730  ILE   A C     1 
ATOM   3479 O  O     . ILE   A 1 581  ? 30.485  -23.372 -62.650 1.00 55.47  ? 730  ILE   A O     1 
ATOM   3480 C  CB    . ILE   A 1 581  ? 31.912  -25.750 -61.358 1.00 54.10  ? 730  ILE   A CB    1 
ATOM   3481 C  CG1   . ILE   A 1 581  ? 33.155  -26.272 -60.634 1.00 56.04  ? 730  ILE   A CG1   1 
ATOM   3482 C  CG2   . ILE   A 1 581  ? 30.958  -26.896 -61.665 1.00 55.79  ? 730  ILE   A CG2   1 
ATOM   3483 C  CD1   . ILE   A 1 581  ? 32.871  -26.812 -59.248 1.00 57.26  ? 730  ILE   A CD1   1 
ATOM   3484 N  N     . ASP   A 1 582  ? 30.728  -24.683 -64.511 1.00 55.32  ? 731  ASP   A N     1 
ATOM   3485 C  CA    . ASP   A 1 582  ? 29.694  -24.071 -65.389 1.00 53.10  ? 731  ASP   A CA    1 
ATOM   3486 C  C     . ASP   A 1 582  ? 28.550  -25.071 -65.560 1.00 48.71  ? 731  ASP   A C     1 
ATOM   3487 O  O     . ASP   A 1 582  ? 28.772  -26.092 -66.218 1.00 48.75  ? 731  ASP   A O     1 
ATOM   3488 C  CB    . ASP   A 1 582  ? 30.307  -23.729 -66.747 1.00 56.06  ? 731  ASP   A CB    1 
ATOM   3489 C  CG    . ASP   A 1 582  ? 29.350  -23.142 -67.774 1.00 63.01  ? 731  ASP   A CG    1 
ATOM   3490 O  OD1   . ASP   A 1 582  ? 28.201  -22.812 -67.399 1.00 61.36  ? 731  ASP   A OD1   1 
ATOM   3491 O  OD2   . ASP   A 1 582  ? 29.772  -23.010 -68.948 1.00 61.28  ? 731  ASP   A OD2   1 
ATOM   3492 N  N     . SER   A 1 583  ? 27.379  -24.768 -65.005 1.00 45.67  ? 732  SER   A N     1 
ATOM   3493 C  CA    . SER   A 1 583  ? 26.136  -25.557 -65.179 1.00 47.48  ? 732  SER   A CA    1 
ATOM   3494 C  C     . SER   A 1 583  ? 25.736  -25.623 -66.664 1.00 54.62  ? 732  SER   A C     1 
ATOM   3495 O  O     . SER   A 1 583  ? 24.978  -26.563 -67.029 1.00 52.79  ? 732  SER   A O     1 
ATOM   3496 C  CB    . SER   A 1 583  ? 25.032  -24.978 -64.351 1.00 49.83  ? 732  SER   A CB    1 
ATOM   3497 O  OG    . SER   A 1 583  ? 24.581  -23.758 -64.913 1.00 54.29  ? 732  SER   A OG    1 
ATOM   3498 N  N     . CYS   A 1 584  ? 26.214  -24.661 -67.472 1.00 54.37  ? 733  CYS   A N     1 
ATOM   3499 C  CA    . CYS   A 1 584  ? 25.958  -24.517 -68.930 1.00 55.81  ? 733  CYS   A CA    1 
ATOM   3500 C  C     . CYS   A 1 584  ? 24.509  -24.057 -69.181 1.00 51.56  ? 733  CYS   A C     1 
ATOM   3501 O  O     . CYS   A 1 584  ? 24.005  -24.279 -70.288 1.00 54.92  ? 733  CYS   A O     1 
ATOM   3502 C  CB    . CYS   A 1 584  ? 26.272  -25.821 -69.650 1.00 52.09  ? 733  CYS   A CB    1 
ATOM   3503 S  SG    . CYS   A 1 584  ? 28.053  -26.107 -69.806 1.00 59.93  ? 733  CYS   A SG    1 
ATOM   3504 N  N     . LYS   A 1 585  ? 23.873  -23.432 -68.188 1.00 48.97  ? 734  LYS   A N     1 
ATOM   3505 C  CA    . LYS   A 1 585  ? 22.446  -23.012 -68.209 1.00 52.19  ? 734  LYS   A CA    1 
ATOM   3506 C  C     . LYS   A 1 585  ? 22.349  -21.484 -68.142 1.00 52.38  ? 734  LYS   A C     1 
ATOM   3507 O  O     . LYS   A 1 585  ? 23.341  -20.840 -67.746 1.00 46.72  ? 734  LYS   A O     1 
ATOM   3508 C  CB    . LYS   A 1 585  ? 21.679  -23.623 -67.033 1.00 59.29  ? 734  LYS   A CB    1 
ATOM   3509 C  CG    . LYS   A 1 585  ? 21.704  -25.149 -66.923 1.00 61.43  ? 734  LYS   A CG    1 
ATOM   3510 C  CD    . LYS   A 1 585  ? 21.382  -25.893 -68.211 1.00 60.49  ? 734  LYS   A CD    1 
ATOM   3511 C  CE    . LYS   A 1 585  ? 21.327  -27.400 -68.046 1.00 62.41  ? 734  LYS   A CE    1 
ATOM   3512 N  NZ    . LYS   A 1 585  ? 20.194  -27.826 -67.184 1.00 70.07  ? 734  LYS   A NZ    1 
ATOM   3513 N  N     . GLN   A 1 586  ? 21.206  -20.932 -68.558 1.00 50.70  ? 735  GLN   A N     1 
ATOM   3514 C  CA    . GLN   A 1 586  ? 20.813  -19.519 -68.311 1.00 51.74  ? 735  GLN   A CA    1 
ATOM   3515 C  C     . GLN   A 1 586  ? 19.418  -19.533 -67.697 1.00 49.93  ? 735  GLN   A C     1 
ATOM   3516 O  O     . GLN   A 1 586  ? 18.695  -20.509 -67.948 1.00 54.14  ? 735  GLN   A O     1 
ATOM   3517 C  CB    . GLN   A 1 586  ? 20.768  -18.702 -69.604 1.00 56.63  ? 735  GLN   A CB    1 
ATOM   3518 C  CG    . GLN   A 1 586  ? 22.120  -18.491 -70.264 1.00 55.12  ? 735  GLN   A CG    1 
ATOM   3519 C  CD    . GLN   A 1 586  ? 22.880  -17.348 -69.649 1.00 65.88  ? 735  GLN   A CD    1 
ATOM   3520 O  OE1   . GLN   A 1 586  ? 22.505  -16.823 -68.599 1.00 68.37  ? 735  GLN   A OE1   1 
ATOM   3521 N  NE2   . GLN   A 1 586  ? 23.970  -16.964 -70.298 1.00 68.68  ? 735  GLN   A NE2   1 
ATOM   3522 N  N     . LYS   A 1 587  ? 19.071  -18.511 -66.918 1.00 52.48  ? 736  LYS   A N     1 
ATOM   3523 C  CA    . LYS   A 1 587  ? 17.667  -18.225 -66.526 1.00 56.36  ? 736  LYS   A CA    1 
ATOM   3524 C  C     . LYS   A 1 587  ? 17.162  -17.115 -67.447 1.00 52.37  ? 736  LYS   A C     1 
ATOM   3525 O  O     . LYS   A 1 587  ? 17.905  -16.156 -67.660 1.00 55.67  ? 736  LYS   A O     1 
ATOM   3526 C  CB    . LYS   A 1 587  ? 17.545  -17.826 -65.051 1.00 59.83  ? 736  LYS   A CB    1 
ATOM   3527 C  CG    . LYS   A 1 587  ? 16.140  -17.951 -64.475 1.00 70.11  ? 736  LYS   A CG    1 
ATOM   3528 C  CD    . LYS   A 1 587  ? 16.061  -17.865 -62.961 1.00 78.80  ? 736  LYS   A CD    1 
ATOM   3529 C  CE    . LYS   A 1 587  ? 16.387  -16.493 -62.405 1.00 84.75  ? 736  LYS   A CE    1 
ATOM   3530 N  NZ    . LYS   A 1 587  ? 15.991  -16.380 -60.978 1.00 87.03  ? 736  LYS   A NZ    1 
ATOM   3531 N  N     . VAL   A 1 588  ? 15.957  -17.269 -67.992 1.00 57.69  ? 737  VAL   A N     1 
ATOM   3532 C  CA    . VAL   A 1 588  ? 15.302  -16.281 -68.899 1.00 60.25  ? 737  VAL   A CA    1 
ATOM   3533 C  C     . VAL   A 1 588  ? 13.828  -16.210 -68.506 1.00 60.89  ? 737  VAL   A C     1 
ATOM   3534 O  O     . VAL   A 1 588  ? 13.244  -17.262 -68.176 1.00 58.66  ? 737  VAL   A O     1 
ATOM   3535 C  CB    . VAL   A 1 588  ? 15.479  -16.655 -70.385 1.00 64.96  ? 737  VAL   A CB    1 
ATOM   3536 C  CG1   . VAL   A 1 588  ? 16.936  -16.947 -70.729 1.00 65.78  ? 737  VAL   A CG1   1 
ATOM   3537 C  CG2   . VAL   A 1 588  ? 14.597  -17.829 -70.786 1.00 66.71  ? 737  VAL   A CG2   1 
ATOM   3538 N  N     . LYS   A 1 589  ? 13.268  -15.006 -68.495 1.00 63.30  ? 738  LYS   A N     1 
ATOM   3539 C  CA    . LYS   A 1 589  ? 11.808  -14.794 -68.373 1.00 67.78  ? 738  LYS   A CA    1 
ATOM   3540 C  C     . LYS   A 1 589  ? 11.202  -14.960 -69.769 1.00 57.52  ? 738  LYS   A C     1 
ATOM   3541 O  O     . LYS   A 1 589  ? 11.545  -14.170 -70.639 1.00 67.17  ? 738  LYS   A O     1 
ATOM   3542 C  CB    . LYS   A 1 589  ? 11.517  -13.418 -67.765 1.00 76.31  ? 738  LYS   A CB    1 
ATOM   3543 C  CG    . LYS   A 1 589  ? 10.222  -13.353 -66.970 1.00 85.16  ? 738  LYS   A CG    1 
ATOM   3544 C  CD    . LYS   A 1 589  ? 9.917   -12.002 -66.377 1.00 85.56  ? 738  LYS   A CD    1 
ATOM   3545 C  CE    . LYS   A 1 589  ? 8.522   -11.955 -65.793 1.00 87.18  ? 738  LYS   A CE    1 
ATOM   3546 N  NZ    . LYS   A 1 589  ? 8.377   -10.839 -64.833 1.00 92.53  ? 738  LYS   A NZ    1 
ATOM   3547 N  N     . LEU   A 1 590  ? 10.394  -15.997 -69.978 1.00 57.71  ? 739  LEU   A N     1 
ATOM   3548 C  CA    . LEU   A 1 590  ? 9.569   -16.184 -71.198 1.00 61.54  ? 739  LEU   A CA    1 
ATOM   3549 C  C     . LEU   A 1 590  ? 8.111   -15.915 -70.826 1.00 63.44  ? 739  LEU   A C     1 
ATOM   3550 O  O     . LEU   A 1 590  ? 7.581   -16.628 -69.972 1.00 67.80  ? 739  LEU   A O     1 
ATOM   3551 C  CB    . LEU   A 1 590  ? 9.726   -17.605 -71.752 1.00 66.91  ? 739  LEU   A CB    1 
ATOM   3552 C  CG    . LEU   A 1 590  ? 11.113  -17.987 -72.286 1.00 76.12  ? 739  LEU   A CG    1 
ATOM   3553 C  CD1   . LEU   A 1 590  ? 11.065  -19.337 -72.995 1.00 75.32  ? 739  LEU   A CD1   1 
ATOM   3554 C  CD2   . LEU   A 1 590  ? 11.693  -16.921 -73.219 1.00 75.29  ? 739  LEU   A CD2   1 
ATOM   3555 N  N     . PHE   A 1 591  ? 7.498   -14.914 -71.451 1.00 64.20  ? 740  PHE   A N     1 
ATOM   3556 C  CA    . PHE   A 1 591  ? 6.051   -14.626 -71.336 1.00 62.92  ? 740  PHE   A CA    1 
ATOM   3557 C  C     . PHE   A 1 591  ? 5.363   -15.089 -72.621 1.00 63.30  ? 740  PHE   A C     1 
ATOM   3558 O  O     . PHE   A 1 591  ? 5.924   -14.868 -73.699 1.00 70.88  ? 740  PHE   A O     1 
ATOM   3559 C  CB    . PHE   A 1 591  ? 5.815   -13.135 -71.079 1.00 63.11  ? 740  PHE   A CB    1 
ATOM   3560 C  CG    . PHE   A 1 591  ? 4.380   -12.810 -70.751 1.00 65.26  ? 740  PHE   A CG    1 
ATOM   3561 C  CD1   . PHE   A 1 591  ? 3.798   -13.282 -69.581 1.00 62.10  ? 740  PHE   A CD1   1 
ATOM   3562 C  CD2   . PHE   A 1 591  ? 3.598   -12.075 -71.636 1.00 63.17  ? 740  PHE   A CD2   1 
ATOM   3563 C  CE1   . PHE   A 1 591  ? 2.471   -13.000 -69.293 1.00 64.16  ? 740  PHE   A CE1   1 
ATOM   3564 C  CE2   . PHE   A 1 591  ? 2.272   -11.794 -71.348 1.00 59.68  ? 740  PHE   A CE2   1 
ATOM   3565 C  CZ    . PHE   A 1 591  ? 1.714   -12.253 -70.177 1.00 66.33  ? 740  PHE   A CZ    1 
ATOM   3566 N  N     . THR   A 1 592  ? 4.185   -15.702 -72.500 1.00 58.76  ? 741  THR   A N     1 
ATOM   3567 C  CA    . THR   A 1 592  ? 3.300   -16.056 -73.640 1.00 63.05  ? 741  THR   A CA    1 
ATOM   3568 C  C     . THR   A 1 592  ? 1.936   -15.404 -73.394 1.00 61.65  ? 741  THR   A C     1 
ATOM   3569 O  O     . THR   A 1 592  ? 1.231   -15.831 -72.443 1.00 60.42  ? 741  THR   A O     1 
ATOM   3570 C  CB    . THR   A 1 592  ? 3.275   -17.576 -73.881 1.00 66.39  ? 741  THR   A CB    1 
ATOM   3571 O  OG1   . THR   A 1 592  ? 2.957   -18.263 -72.667 1.00 60.65  ? 741  THR   A OG1   1 
ATOM   3572 C  CG2   . THR   A 1 592  ? 4.595   -18.094 -74.421 1.00 63.79  ? 741  THR   A CG2   1 
ATOM   3573 N  N     . ALA   A 1 593  ? 1.614   -14.392 -74.212 1.00 64.00  ? 742  ALA   A N     1 
ATOM   3574 C  CA    . ALA   A 1 593  ? 0.440   -13.494 -74.095 1.00 65.79  ? 742  ALA   A CA    1 
ATOM   3575 C  C     . ALA   A 1 593  ? -0.856  -14.305 -74.154 1.00 70.79  ? 742  ALA   A C     1 
ATOM   3576 O  O     . ALA   A 1 593  ? -1.769  -14.011 -73.343 1.00 68.01  ? 742  ALA   A O     1 
ATOM   3577 C  CB    . ALA   A 1 593  ? 0.473   -12.456 -75.190 1.00 69.40  ? 742  ALA   A CB    1 
ATOM   3578 N  N     . HIS   A 1 594  ? -0.915  -15.289 -75.060 1.00 71.75  ? 743  HIS   A N     1 
ATOM   3579 C  CA    . HIS   A 1 594  ? -2.135  -16.064 -75.412 1.00 76.03  ? 743  HIS   A CA    1 
ATOM   3580 C  C     . HIS   A 1 594  ? -2.705  -16.787 -74.174 1.00 78.12  ? 743  HIS   A C     1 
ATOM   3581 O  O     . HIS   A 1 594  ? -3.938  -16.760 -74.013 1.00 81.22  ? 743  HIS   A O     1 
ATOM   3582 C  CB    . HIS   A 1 594  ? -1.850  -16.987 -76.614 1.00 81.24  ? 743  HIS   A CB    1 
ATOM   3583 C  CG    . HIS   A 1 594  ? -1.063  -18.221 -76.305 1.00 81.09  ? 743  HIS   A CG    1 
ATOM   3584 N  ND1   . HIS   A 1 594  ? -1.671  -19.403 -75.903 1.00 77.73  ? 743  HIS   A ND1   1 
ATOM   3585 C  CD2   . HIS   A 1 594  ? 0.265   -18.473 -76.363 1.00 77.50  ? 743  HIS   A CD2   1 
ATOM   3586 C  CE1   . HIS   A 1 594  ? -0.744  -20.327 -75.718 1.00 79.17  ? 743  HIS   A CE1   1 
ATOM   3587 N  NE2   . HIS   A 1 594  ? 0.453   -19.780 -75.995 1.00 78.49  ? 743  HIS   A NE2   1 
ATOM   3588 N  N     . ASN   A 1 595  ? -1.869  -17.385 -73.312 1.00 74.81  ? 744  ASN   A N     1 
ATOM   3589 C  CA    . ASN   A 1 595  ? -2.331  -18.074 -72.070 1.00 74.58  ? 744  ASN   A CA    1 
ATOM   3590 C  C     . ASN   A 1 595  ? -1.773  -17.370 -70.818 1.00 72.88  ? 744  ASN   A C     1 
ATOM   3591 O  O     . ASN   A 1 595  ? -1.910  -17.941 -69.718 1.00 70.95  ? 744  ASN   A O     1 
ATOM   3592 C  CB    . ASN   A 1 595  ? -2.002  -19.573 -72.086 1.00 71.31  ? 744  ASN   A CB    1 
ATOM   3593 C  CG    . ASN   A 1 595  ? -0.531  -19.882 -72.282 1.00 75.51  ? 744  ASN   A CG    1 
ATOM   3594 O  OD1   . ASN   A 1 595  ? 0.280   -18.987 -72.533 1.00 78.46  ? 744  ASN   A OD1   1 
ATOM   3595 N  ND2   . ASN   A 1 595  ? -0.177  -21.154 -72.175 1.00 76.03  ? 744  ASN   A ND2   1 
ATOM   3596 N  N     . ASN   A 1 596  ? -1.160  -16.193 -70.988 1.00 70.35  ? 745  ASN   A N     1 
ATOM   3597 C  CA    . ASN   A 1 596  ? -0.664  -15.300 -69.903 1.00 72.65  ? 745  ASN   A CA    1 
ATOM   3598 C  C     . ASN   A 1 596  ? 0.270   -16.089 -68.970 1.00 69.44  ? 745  ASN   A C     1 
ATOM   3599 O  O     . ASN   A 1 596  ? 0.184   -15.919 -67.747 1.00 69.87  ? 745  ASN   A O     1 
ATOM   3600 C  CB    . ASN   A 1 596  ? -1.833  -14.630 -69.171 1.00 67.99  ? 745  ASN   A CB    1 
ATOM   3601 C  CG    . ASN   A 1 596  ? -1.454  -13.291 -68.575 1.00 68.39  ? 745  ASN   A CG    1 
ATOM   3602 O  OD1   . ASN   A 1 596  ? -1.140  -12.356 -69.307 1.00 76.72  ? 745  ASN   A OD1   1 
ATOM   3603 N  ND2   . ASN   A 1 596  ? -1.481  -13.181 -67.255 1.00 59.95  ? 745  ASN   A ND2   1 
ATOM   3604 N  N     . MET   A 1 597  ? 1.143   -16.915 -69.548 1.00 76.56  ? 746  MET   A N     1 
ATOM   3605 C  CA    . MET   A 1 597  ? 2.035   -17.859 -68.822 1.00 74.95  ? 746  MET   A CA    1 
ATOM   3606 C  C     . MET   A 1 597  ? 3.425   -17.232 -68.701 1.00 70.24  ? 746  MET   A C     1 
ATOM   3607 O  O     . MET   A 1 597  ? 3.999   -16.871 -69.743 1.00 70.66  ? 746  MET   A O     1 
ATOM   3608 C  CB    . MET   A 1 597  ? 2.154   -19.198 -69.564 1.00 75.62  ? 746  MET   A CB    1 
ATOM   3609 C  CG    . MET   A 1 597  ? 2.800   -20.312 -68.751 1.00 73.04  ? 746  MET   A CG    1 
ATOM   3610 S  SD    . MET   A 1 597  ? 1.699   -20.963 -67.464 1.00 70.54  ? 746  MET   A SD    1 
ATOM   3611 C  CE    . MET   A 1 597  ? 0.584   -21.929 -68.487 1.00 71.09  ? 746  MET   A CE    1 
ATOM   3612 N  N     . THR   A 1 598  ? 3.920   -17.098 -67.467 1.00 70.57  ? 747  THR   A N     1 
ATOM   3613 C  CA    . THR   A 1 598  ? 5.330   -16.762 -67.155 1.00 70.42  ? 747  THR   A CA    1 
ATOM   3614 C  C     . THR   A 1 598  ? 6.085   -18.079 -66.960 1.00 69.19  ? 747  THR   A C     1 
ATOM   3615 O  O     . THR   A 1 598  ? 5.605   -18.949 -66.217 1.00 68.23  ? 747  THR   A O     1 
ATOM   3616 C  CB    . THR   A 1 598  ? 5.440   -15.841 -65.934 1.00 70.12  ? 747  THR   A CB    1 
ATOM   3617 O  OG1   . THR   A 1 598  ? 4.438   -14.828 -66.046 1.00 71.62  ? 747  THR   A OG1   1 
ATOM   3618 C  CG2   . THR   A 1 598  ? 6.817   -15.224 -65.802 1.00 67.21  ? 747  THR   A CG2   1 
ATOM   3619 N  N     . ASN   A 1 599  ? 7.200   -18.236 -67.658 1.00 70.83  ? 748  ASN   A N     1 
ATOM   3620 C  CA    . ASN   A 1 599  ? 8.139   -19.369 -67.482 1.00 75.27  ? 748  ASN   A CA    1 
ATOM   3621 C  C     . ASN   A 1 599  ? 9.486   -18.763 -67.075 1.00 72.85  ? 748  ASN   A C     1 
ATOM   3622 O  O     . ASN   A 1 599  ? 10.131  -18.123 -67.942 1.00 66.80  ? 748  ASN   A O     1 
ATOM   3623 C  CB    . ASN   A 1 599  ? 8.207   -20.228 -68.750 1.00 77.29  ? 748  ASN   A CB    1 
ATOM   3624 C  CG    . ASN   A 1 599  ? 8.989   -21.518 -68.588 1.00 79.73  ? 748  ASN   A CG    1 
ATOM   3625 O  OD1   . ASN   A 1 599  ? 9.855   -21.639 -67.718 1.00 69.95  ? 748  ASN   A OD1   1 
ATOM   3626 N  ND2   . ASN   A 1 599  ? 8.699   -22.486 -69.444 1.00 81.18  ? 748  ASN   A ND2   1 
ATOM   3627 N  N     . TYR   A 1 600  ? 9.863   -18.895 -65.798 1.00 60.76  ? 749  TYR   A N     1 
ATOM   3628 C  CA    . TYR   A 1 600  ? 11.259  -18.683 -65.360 1.00 63.72  ? 749  TYR   A CA    1 
ATOM   3629 C  C     . TYR   A 1 600  ? 11.980  -19.960 -65.779 1.00 64.53  ? 749  TYR   A C     1 
ATOM   3630 O  O     . TYR   A 1 600  ? 12.128  -20.886 -64.959 1.00 73.00  ? 749  TYR   A O     1 
ATOM   3631 C  CB    . TYR   A 1 600  ? 11.344  -18.328 -63.875 1.00 63.52  ? 749  TYR   A CB    1 
ATOM   3632 C  CG    . TYR   A 1 600  ? 10.649  -17.041 -63.512 1.00 69.45  ? 749  TYR   A CG    1 
ATOM   3633 C  CD1   . TYR   A 1 600  ? 11.254  -15.803 -63.710 1.00 68.65  ? 749  TYR   A CD1   1 
ATOM   3634 C  CD2   . TYR   A 1 600  ? 9.371   -17.066 -62.975 1.00 71.80  ? 749  TYR   A CD2   1 
ATOM   3635 C  CE1   . TYR   A 1 600  ? 10.606  -14.622 -63.379 1.00 64.81  ? 749  TYR   A CE1   1 
ATOM   3636 C  CE2   . TYR   A 1 600  ? 8.710   -15.897 -62.638 1.00 73.34  ? 749  TYR   A CE2   1 
ATOM   3637 C  CZ    . TYR   A 1 600  ? 9.327   -14.674 -62.843 1.00 75.41  ? 749  TYR   A CZ    1 
ATOM   3638 O  OH    . TYR   A 1 600  ? 8.637   -13.546 -62.504 1.00 79.24  ? 749  TYR   A OH    1 
ATOM   3639 N  N     . ALA   A 1 601  ? 12.309  -20.033 -67.066 1.00 56.99  ? 750  ALA   A N     1 
ATOM   3640 C  CA    . ALA   A 1 601  ? 12.805  -21.255 -67.723 1.00 59.30  ? 750  ALA   A CA    1 
ATOM   3641 C  C     . ALA   A 1 601  ? 14.309  -21.339 -67.497 1.00 62.95  ? 750  ALA   A C     1 
ATOM   3642 O  O     . ALA   A 1 601  ? 14.987  -20.297 -67.562 1.00 61.38  ? 750  ALA   A O     1 
ATOM   3643 C  CB    . ALA   A 1 601  ? 12.473  -21.258 -69.190 1.00 57.01  ? 750  ALA   A CB    1 
ATOM   3644 N  N     . THR   A 1 602  ? 14.784  -22.548 -67.217 1.00 61.04  ? 751  THR   A N     1 
ATOM   3645 C  CA    . THR   A 1 602  ? 16.213  -22.917 -67.257 1.00 59.77  ? 751  THR   A CA    1 
ATOM   3646 C  C     . THR   A 1 602  ? 16.494  -23.417 -68.672 1.00 59.96  ? 751  THR   A C     1 
ATOM   3647 O  O     . THR   A 1 602  ? 15.837  -24.401 -69.072 1.00 68.01  ? 751  THR   A O     1 
ATOM   3648 C  CB    . THR   A 1 602  ? 16.528  -23.943 -66.163 1.00 58.87  ? 751  THR   A CB    1 
ATOM   3649 O  OG1   . THR   A 1 602  ? 16.010  -23.419 -64.939 1.00 62.03  ? 751  THR   A OG1   1 
ATOM   3650 C  CG2   . THR   A 1 602  ? 18.007  -24.224 -66.037 1.00 59.82  ? 751  THR   A CG2   1 
ATOM   3651 N  N     . VAL   A 1 603  ? 17.419  -22.767 -69.387 1.00 53.13  ? 752  VAL   A N     1 
ATOM   3652 C  CA    . VAL   A 1 603  ? 17.727  -23.068 -70.814 1.00 54.83  ? 752  VAL   A CA    1 
ATOM   3653 C  C     . VAL   A 1 603  ? 19.232  -23.240 -70.990 1.00 56.79  ? 752  VAL   A C     1 
ATOM   3654 O  O     . VAL   A 1 603  ? 19.994  -22.741 -70.138 1.00 60.78  ? 752  VAL   A O     1 
ATOM   3655 C  CB    . VAL   A 1 603  ? 17.189  -21.966 -71.746 1.00 52.70  ? 752  VAL   A CB    1 
ATOM   3656 C  CG1   . VAL   A 1 603  ? 15.666  -21.944 -71.741 1.00 51.47  ? 752  VAL   A CG1   1 
ATOM   3657 C  CG2   . VAL   A 1 603  ? 17.758  -20.602 -71.388 1.00 53.17  ? 752  VAL   A CG2   1 
ATOM   3658 N  N     . TRP   A 1 604  ? 19.626  -23.907 -72.074 1.00 54.13  ? 753  TRP   A N     1 
ATOM   3659 C  CA    . TRP   A 1 604  ? 21.043  -24.039 -72.489 1.00 59.04  ? 753  TRP   A CA    1 
ATOM   3660 C  C     . TRP   A 1 604  ? 21.614  -22.647 -72.721 1.00 53.06  ? 753  TRP   A C     1 
ATOM   3661 O  O     . TRP   A 1 604  ? 20.886  -21.780 -73.167 1.00 58.78  ? 753  TRP   A O     1 
ATOM   3662 C  CB    . TRP   A 1 604  ? 21.179  -24.950 -73.714 1.00 62.41  ? 753  TRP   A CB    1 
ATOM   3663 C  CG    . TRP   A 1 604  ? 20.750  -26.344 -73.383 1.00 69.42  ? 753  TRP   A CG    1 
ATOM   3664 C  CD1   . TRP   A 1 604  ? 19.604  -26.981 -73.762 1.00 69.81  ? 753  TRP   A CD1   1 
ATOM   3665 C  CD2   . TRP   A 1 604  ? 21.427  -27.236 -72.481 1.00 71.85  ? 753  TRP   A CD2   1 
ATOM   3666 N  NE1   . TRP   A 1 604  ? 19.550  -28.227 -73.198 1.00 71.91  ? 753  TRP   A NE1   1 
ATOM   3667 C  CE2   . TRP   A 1 604  ? 20.650  -28.408 -72.403 1.00 73.69  ? 753  TRP   A CE2   1 
ATOM   3668 C  CE3   . TRP   A 1 604  ? 22.615  -27.160 -71.748 1.00 67.45  ? 753  TRP   A CE3   1 
ATOM   3669 C  CZ2   . TRP   A 1 604  ? 21.036  -29.494 -71.619 1.00 80.94  ? 753  TRP   A CZ2   1 
ATOM   3670 C  CZ3   . TRP   A 1 604  ? 22.996  -28.235 -70.976 1.00 67.76  ? 753  TRP   A CZ3   1 
ATOM   3671 C  CH2   . TRP   A 1 604  ? 22.212  -29.384 -70.910 1.00 71.57  ? 753  TRP   A CH2   1 
ATOM   3672 N  N     . ALA   A 1 605  ? 22.855  -22.442 -72.309 1.00 59.37  ? 754  ALA   A N     1 
ATOM   3673 C  CA    . ALA   A 1 605  ? 23.651  -21.246 -72.635 1.00 53.88  ? 754  ALA   A CA    1 
ATOM   3674 C  C     . ALA   A 1 605  ? 24.117  -21.395 -74.077 1.00 48.78  ? 754  ALA   A C     1 
ATOM   3675 O  O     . ALA   A 1 605  ? 23.949  -22.474 -74.624 1.00 52.00  ? 754  ALA   A O     1 
ATOM   3676 C  CB    . ALA   A 1 605  ? 24.814  -21.136 -71.688 1.00 51.51  ? 754  ALA   A CB    1 
ATOM   3677 N  N     . SER   A 1 606  ? 24.723  -20.355 -74.631 1.00 46.28  ? 755  SER   A N     1 
ATOM   3678 C  CA    . SER   A 1 606  ? 25.323  -20.342 -75.985 1.00 47.64  ? 755  SER   A CA    1 
ATOM   3679 C  C     . SER   A 1 606  ? 26.788  -20.803 -75.914 1.00 54.80  ? 755  SER   A C     1 
ATOM   3680 O  O     . SER   A 1 606  ? 27.408  -20.719 -74.824 1.00 60.21  ? 755  SER   A O     1 
ATOM   3681 C  CB    . SER   A 1 606  ? 25.206  -18.953 -76.564 1.00 44.01  ? 755  SER   A CB    1 
ATOM   3682 O  OG    . SER   A 1 606  ? 26.086  -18.040 -75.910 1.00 45.03  ? 755  SER   A OG    1 
ATOM   3683 N  N     . LYS   A 1 607  ? 27.363  -21.215 -77.041 1.00 55.27  ? 756  LYS   A N     1 
ATOM   3684 C  CA    . LYS   A 1 607  ? 28.834  -21.399 -77.151 1.00 56.08  ? 756  LYS   A CA    1 
ATOM   3685 C  C     . LYS   A 1 607  ? 29.543  -20.136 -76.651 1.00 51.81  ? 756  LYS   A C     1 
ATOM   3686 O  O     . LYS   A 1 607  ? 30.578  -20.276 -75.983 1.00 60.72  ? 756  LYS   A O     1 
ATOM   3687 C  CB    . LYS   A 1 607  ? 29.247  -21.724 -78.587 1.00 56.51  ? 756  LYS   A CB    1 
ATOM   3688 C  CG    . LYS   A 1 607  ? 28.952  -23.149 -79.032 1.00 57.07  ? 756  LYS   A CG    1 
ATOM   3689 C  CD    . LYS   A 1 607  ? 29.508  -23.450 -80.408 1.00 66.36  ? 756  LYS   A CD    1 
ATOM   3690 C  CE    . LYS   A 1 607  ? 29.366  -24.901 -80.830 1.00 73.86  ? 756  LYS   A CE    1 
ATOM   3691 N  NZ    . LYS   A 1 607  ? 27.949  -25.291 -81.029 1.00 77.17  ? 756  LYS   A NZ    1 
ATOM   3692 N  N     . THR   A 1 608  ? 29.022  -18.949 -76.957 1.00 50.53  ? 757  THR   A N     1 
ATOM   3693 C  CA    . THR   A 1 608  ? 29.670  -17.655 -76.602 1.00 50.59  ? 757  THR   A CA    1 
ATOM   3694 C  C     . THR   A 1 608  ? 29.638  -17.463 -75.078 1.00 49.48  ? 757  THR   A C     1 
ATOM   3695 O  O     . THR   A 1 608  ? 30.633  -16.953 -74.531 1.00 52.77  ? 757  THR   A O     1 
ATOM   3696 C  CB    . THR   A 1 608  ? 29.025  -16.464 -77.324 1.00 51.97  ? 757  THR   A CB    1 
ATOM   3697 O  OG1   . THR   A 1 608  ? 29.406  -16.550 -78.696 1.00 54.12  ? 757  THR   A OG1   1 
ATOM   3698 C  CG2   . THR   A 1 608  ? 29.457  -15.121 -76.772 1.00 52.05  ? 757  THR   A CG2   1 
ATOM   3699 N  N     . ASN   A 1 609  ? 28.558  -17.866 -74.414 1.00 46.12  ? 758  ASN   A N     1 
ATOM   3700 C  CA    . ASN   A 1 609  ? 28.492  -17.847 -72.930 1.00 51.21  ? 758  ASN   A CA    1 
ATOM   3701 C  C     . ASN   A 1 609  ? 29.531  -18.807 -72.331 1.00 54.71  ? 758  ASN   A C     1 
ATOM   3702 O  O     . ASN   A 1 609  ? 30.221  -18.384 -71.379 1.00 57.71  ? 758  ASN   A O     1 
ATOM   3703 C  CB    . ASN   A 1 609  ? 27.115  -18.232 -72.405 1.00 48.24  ? 758  ASN   A CB    1 
ATOM   3704 C  CG    . ASN   A 1 609  ? 26.032  -17.286 -72.853 1.00 44.33  ? 758  ASN   A CG    1 
ATOM   3705 O  OD1   . ASN   A 1 609  ? 24.948  -17.717 -73.241 1.00 51.92  ? 758  ASN   A OD1   1 
ATOM   3706 N  ND2   . ASN   A 1 609  ? 26.308  -16.000 -72.776 1.00 44.11  ? 758  ASN   A ND2   1 
ATOM   3707 N  N     . LEU   A 1 610  ? 29.609  -20.049 -72.827 1.00 51.72  ? 759  LEU   A N     1 
ATOM   3708 C  CA    . LEU   A 1 610  ? 30.577  -21.065 -72.331 1.00 51.45  ? 759  LEU   A CA    1 
ATOM   3709 C  C     . LEU   A 1 610  ? 32.003  -20.519 -72.498 1.00 52.27  ? 759  LEU   A C     1 
ATOM   3710 O  O     . LEU   A 1 610  ? 32.779  -20.628 -71.533 1.00 55.24  ? 759  LEU   A O     1 
ATOM   3711 C  CB    . LEU   A 1 610  ? 30.382  -22.410 -73.045 1.00 52.53  ? 759  LEU   A CB    1 
ATOM   3712 C  CG    . LEU   A 1 610  ? 29.529  -23.435 -72.292 1.00 51.27  ? 759  LEU   A CG    1 
ATOM   3713 C  CD1   . LEU   A 1 610  ? 28.088  -22.974 -72.147 1.00 54.96  ? 759  LEU   A CD1   1 
ATOM   3714 C  CD2   . LEU   A 1 610  ? 29.548  -24.776 -72.983 1.00 52.99  ? 759  LEU   A CD2   1 
ATOM   3715 N  N     . GLU   A 1 611  ? 32.333  -19.902 -73.635 1.00 50.73  ? 760  GLU   A N     1 
ATOM   3716 C  CA    . GLU   A 1 611  ? 33.692  -19.325 -73.867 1.00 53.44  ? 760  GLU   A CA    1 
ATOM   3717 C  C     . GLU   A 1 611  ? 33.965  -18.209 -72.844 1.00 53.06  ? 760  GLU   A C     1 
ATOM   3718 O  O     . GLU   A 1 611  ? 35.093  -18.128 -72.332 1.00 65.65  ? 760  GLU   A O     1 
ATOM   3719 C  CB    . GLU   A 1 611  ? 33.835  -18.811 -75.303 1.00 54.22  ? 760  GLU   A CB    1 
ATOM   3720 C  CG    . GLU   A 1 611  ? 35.218  -18.275 -75.646 1.00 61.58  ? 760  GLU   A CG    1 
ATOM   3721 C  CD    . GLU   A 1 611  ? 36.353  -19.296 -75.686 1.00 80.08  ? 760  GLU   A CD    1 
ATOM   3722 O  OE1   . GLU   A 1 611  ? 36.088  -20.486 -76.017 1.00 87.28  ? 760  GLU   A OE1   1 
ATOM   3723 O  OE2   . GLU   A 1 611  ? 37.516  -18.902 -75.397 1.00 79.50  ? 760  GLU   A OE2   1 
ATOM   3724 N  N     . GLN   A 1 612  ? 32.981  -17.364 -72.560 1.00 53.11  ? 761  GLN   A N     1 
ATOM   3725 C  CA    . GLN   A 1 612  ? 33.136  -16.218 -71.623 1.00 57.57  ? 761  GLN   A CA    1 
ATOM   3726 C  C     . GLN   A 1 612  ? 33.298  -16.747 -70.188 1.00 53.49  ? 761  GLN   A C     1 
ATOM   3727 O  O     . GLN   A 1 612  ? 34.172  -16.241 -69.482 1.00 55.05  ? 761  GLN   A O     1 
ATOM   3728 C  CB    . GLN   A 1 612  ? 31.945  -15.266 -71.758 1.00 60.24  ? 761  GLN   A CB    1 
ATOM   3729 C  CG    . GLN   A 1 612  ? 32.006  -14.381 -72.998 1.00 64.84  ? 761  GLN   A CG    1 
ATOM   3730 C  CD    . GLN   A 1 612  ? 30.708  -13.641 -73.243 1.00 72.71  ? 761  GLN   A CD    1 
ATOM   3731 O  OE1   . GLN   A 1 612  ? 29.641  -13.998 -72.735 1.00 72.88  ? 761  GLN   A OE1   1 
ATOM   3732 N  NE2   . GLN   A 1 612  ? 30.787  -12.584 -74.034 1.00 78.13  ? 761  GLN   A NE2   1 
ATOM   3733 N  N     . ARG   A 1 613  ? 32.483  -17.723 -69.788 1.00 48.16  ? 762  ARG   A N     1 
ATOM   3734 C  CA    . ARG   A 1 613  ? 32.561  -18.401 -68.470 1.00 52.54  ? 762  ARG   A CA    1 
ATOM   3735 C  C     . ARG   A 1 613  ? 33.931  -19.088 -68.331 1.00 54.69  ? 762  ARG   A C     1 
ATOM   3736 O  O     . ARG   A 1 613  ? 34.581  -18.902 -67.295 1.00 63.13  ? 762  ARG   A O     1 
ATOM   3737 C  CB    . ARG   A 1 613  ? 31.369  -19.352 -68.310 1.00 50.92  ? 762  ARG   A CB    1 
ATOM   3738 C  CG    . ARG   A 1 613  ? 30.017  -18.657 -68.230 1.00 50.57  ? 762  ARG   A CG    1 
ATOM   3739 C  CD    . ARG   A 1 613  ? 28.840  -19.621 -68.257 1.00 52.17  ? 762  ARG   A CD    1 
ATOM   3740 N  NE    . ARG   A 1 613  ? 27.558  -18.924 -68.208 1.00 53.17  ? 762  ARG   A NE    1 
ATOM   3741 C  CZ    . ARG   A 1 613  ? 26.377  -19.480 -67.930 1.00 54.69  ? 762  ARG   A CZ    1 
ATOM   3742 N  NH1   . ARG   A 1 613  ? 26.279  -20.771 -67.673 1.00 57.13  ? 762  ARG   A NH1   1 
ATOM   3743 N  NH2   . ARG   A 1 613  ? 25.283  -18.737 -67.922 1.00 52.68  ? 762  ARG   A NH2   1 
ATOM   3744 N  N     . LYS   A 1 614  ? 34.383  -19.819 -69.351 1.00 58.07  ? 763  LYS   A N     1 
ATOM   3745 C  CA    . LYS   A 1 614  ? 35.728  -20.455 -69.375 1.00 57.75  ? 763  LYS   A CA    1 
ATOM   3746 C  C     . LYS   A 1 614  ? 36.793  -19.392 -69.055 1.00 60.45  ? 763  LYS   A C     1 
ATOM   3747 O  O     . LYS   A 1 614  ? 37.680  -19.678 -68.212 1.00 56.35  ? 763  LYS   A O     1 
ATOM   3748 C  CB    . LYS   A 1 614  ? 35.966  -21.146 -70.721 1.00 59.41  ? 763  LYS   A CB    1 
ATOM   3749 C  CG    . LYS   A 1 614  ? 37.386  -21.648 -70.969 1.00 65.35  ? 763  LYS   A CG    1 
ATOM   3750 C  CD    . LYS   A 1 614  ? 37.621  -22.074 -72.413 1.00 71.39  ? 763  LYS   A CD    1 
ATOM   3751 C  CE    . LYS   A 1 614  ? 39.085  -22.139 -72.795 1.00 77.15  ? 763  LYS   A CE    1 
ATOM   3752 N  NZ    . LYS   A 1 614  ? 39.392  -21.273 -73.960 1.00 82.54  ? 763  LYS   A NZ    1 
ATOM   3753 N  N     . GLY   A 1 615  ? 36.689  -18.204 -69.662 1.00 55.85  ? 764  GLY   A N     1 
ATOM   3754 C  CA    . GLY   A 1 615  ? 37.706  -17.137 -69.570 1.00 51.76  ? 764  GLY   A CA    1 
ATOM   3755 C  C     . GLY   A 1 615  ? 37.761  -16.480 -68.203 1.00 50.43  ? 764  GLY   A C     1 
ATOM   3756 O  O     . GLY   A 1 615  ? 38.766  -15.823 -67.933 1.00 50.45  ? 764  GLY   A O     1 
ATOM   3757 N  N     . ARG   A 1 616  ? 36.744  -16.645 -67.346 1.00 55.67  ? 765  ARG   A N     1 
ATOM   3758 C  CA    . ARG   A 1 616  ? 36.797  -16.108 -65.952 1.00 56.82  ? 765  ARG   A CA    1 
ATOM   3759 C  C     . ARG   A 1 616  ? 37.830  -16.872 -65.105 1.00 51.01  ? 765  ARG   A C     1 
ATOM   3760 O  O     . ARG   A 1 616  ? 38.159  -16.364 -64.025 1.00 58.73  ? 765  ARG   A O     1 
ATOM   3761 C  CB    . ARG   A 1 616  ? 35.451  -16.160 -65.220 1.00 57.69  ? 765  ARG   A CB    1 
ATOM   3762 C  CG    . ARG   A 1 616  ? 34.239  -15.705 -66.013 1.00 64.39  ? 765  ARG   A CG    1 
ATOM   3763 C  CD    . ARG   A 1 616  ? 34.428  -14.512 -66.922 1.00 65.75  ? 765  ARG   A CD    1 
ATOM   3764 N  NE    . ARG   A 1 616  ? 34.890  -13.348 -66.201 1.00 64.22  ? 765  ARG   A NE    1 
ATOM   3765 C  CZ    . ARG   A 1 616  ? 35.930  -12.609 -66.558 1.00 71.78  ? 765  ARG   A CZ    1 
ATOM   3766 N  NH1   . ARG   A 1 616  ? 36.640  -12.909 -67.637 1.00 70.33  ? 765  ARG   A NH1   1 
ATOM   3767 N  NH2   . ARG   A 1 616  ? 36.256  -11.563 -65.823 1.00 78.94  ? 765  ARG   A NH2   1 
ATOM   3768 N  N     . ALA   A 1 617  ? 38.329  -18.030 -65.554 1.00 54.92  ? 766  ALA   A N     1 
ATOM   3769 C  CA    . ALA   A 1 617  ? 39.338  -18.859 -64.841 1.00 62.88  ? 766  ALA   A CA    1 
ATOM   3770 C  C     . ALA   A 1 617  ? 40.782  -18.475 -65.212 1.00 65.93  ? 766  ALA   A C     1 
ATOM   3771 O  O     . ALA   A 1 617  ? 41.704  -19.049 -64.573 1.00 65.90  ? 766  ALA   A O     1 
ATOM   3772 C  CB    . ALA   A 1 617  ? 39.098  -20.327 -65.126 1.00 64.94  ? 766  ALA   A CB    1 
ATOM   3773 N  N     . GLY   A 1 618  ? 40.988  -17.549 -66.165 1.00 59.86  ? 767  GLY   A N     1 
ATOM   3774 C  CA    . GLY   A 1 618  ? 42.303  -17.304 -66.797 1.00 57.81  ? 767  GLY   A CA    1 
ATOM   3775 C  C     . GLY   A 1 618  ? 42.766  -15.854 -66.738 1.00 58.02  ? 767  GLY   A C     1 
ATOM   3776 O  O     . GLY   A 1 618  ? 43.379  -15.395 -67.712 1.00 61.90  ? 767  GLY   A O     1 
ATOM   3777 N  N     . ARG   A 1 619  ? 42.532  -15.159 -65.630 1.00 62.09  ? 768  ARG   A N     1 
ATOM   3778 C  CA    A ARG   A 1 619  ? 43.061  -13.780 -65.475 0.50 67.47  ? 768  ARG   A CA    1 
ATOM   3779 C  CA    B ARG   A 1 619  ? 42.978  -13.764 -65.356 0.50 65.51  ? 768  ARG   A CA    1 
ATOM   3780 C  C     . ARG   A 1 619  ? 44.218  -13.773 -64.457 1.00 69.71  ? 768  ARG   A C     1 
ATOM   3781 O  O     . ARG   A 1 619  ? 45.072  -12.866 -64.590 1.00 66.60  ? 768  ARG   A O     1 
ATOM   3782 C  CB    A ARG   A 1 619  ? 41.902  -12.810 -65.208 0.50 71.91  ? 768  ARG   A CB    1 
ATOM   3783 C  CB    B ARG   A 1 619  ? 41.900  -12.984 -64.596 0.50 66.43  ? 768  ARG   A CB    1 
ATOM   3784 C  CG    A ARG   A 1 619  ? 40.931  -12.705 -66.382 0.50 72.50  ? 768  ARG   A CG    1 
ATOM   3785 C  CG    B ARG   A 1 619  ? 41.019  -12.102 -65.466 0.50 65.93  ? 768  ARG   A CG    1 
ATOM   3786 C  CD    A ARG   A 1 619  ? 40.390  -11.313 -66.694 0.50 72.54  ? 768  ARG   A CD    1 
ATOM   3787 C  CD    B ARG   A 1 619  ? 40.295  -11.067 -64.631 0.50 62.84  ? 768  ARG   A CD    1 
ATOM   3788 N  NE    A ARG   A 1 619  ? 41.387  -10.343 -67.146 0.50 70.59  ? 768  ARG   A NE    1 
ATOM   3789 N  NE    B ARG   A 1 619  ? 40.944  -9.763  -64.595 0.50 59.99  ? 768  ARG   A NE    1 
ATOM   3790 C  CZ    A ARG   A 1 619  ? 41.749  -10.152 -68.413 0.50 69.90  ? 768  ARG   A CZ    1 
ATOM   3791 C  CZ    B ARG   A 1 619  ? 41.623  -9.283  -63.563 0.50 62.81  ? 768  ARG   A CZ    1 
ATOM   3792 N  NH1   A ARG   A 1 619  ? 41.209  -10.874 -69.380 0.50 70.14  ? 768  ARG   A NH1   1 
ATOM   3793 N  NH1   B ARG   A 1 619  ? 41.769  -10.008 -62.467 0.50 62.78  ? 768  ARG   A NH1   1 
ATOM   3794 N  NH2   A ARG   A 1 619  ? 42.659  -9.242  -68.710 0.50 68.14  ? 768  ARG   A NH2   1 
ATOM   3795 N  NH2   B ARG   A 1 619  ? 42.160  -8.077  -63.632 0.50 62.33  ? 768  ARG   A NH2   1 
ATOM   3796 N  N     . VAL   A 1 620  ? 44.290  -14.752 -63.545 1.00 72.92  ? 769  VAL   A N     1 
ATOM   3797 C  CA    . VAL   A 1 620  ? 45.294  -14.772 -62.435 1.00 79.74  ? 769  VAL   A CA    1 
ATOM   3798 C  C     . VAL   A 1 620  ? 46.512  -15.636 -62.811 1.00 80.41  ? 769  VAL   A C     1 
ATOM   3799 O  O     . VAL   A 1 620  ? 47.633  -15.095 -62.800 1.00 73.44  ? 769  VAL   A O     1 
ATOM   3800 C  CB    . VAL   A 1 620  ? 44.632  -15.233 -61.124 1.00 80.27  ? 769  VAL   A CB    1 
ATOM   3801 C  CG1   . VAL   A 1 620  ? 45.657  -15.416 -60.014 1.00 81.55  ? 769  VAL   A CG1   1 
ATOM   3802 C  CG2   . VAL   A 1 620  ? 43.523  -14.276 -60.692 1.00 79.35  ? 769  VAL   A CG2   1 
ATOM   3803 N  N     . ARG   A 1 621  ? 46.288  -16.920 -63.110 1.00 80.00  ? 770  ARG   A N     1 
ATOM   3804 C  CA    . ARG   A 1 621  ? 47.306  -17.920 -63.542 1.00 75.45  ? 770  ARG   A CA    1 
ATOM   3805 C  C     . ARG   A 1 621  ? 46.614  -18.902 -64.487 1.00 69.81  ? 770  ARG   A C     1 
ATOM   3806 O  O     . ARG   A 1 621  ? 45.409  -18.796 -64.678 1.00 69.81  ? 770  ARG   A O     1 
ATOM   3807 C  CB    . ARG   A 1 621  ? 47.895  -18.629 -62.315 1.00 80.26  ? 770  ARG   A CB    1 
ATOM   3808 C  CG    . ARG   A 1 621  ? 47.223  -19.951 -61.956 1.00 84.45  ? 770  ARG   A CG    1 
ATOM   3809 C  CD    . ARG   A 1 621  ? 47.625  -20.510 -60.606 1.00 87.47  ? 770  ARG   A CD    1 
ATOM   3810 N  NE    . ARG   A 1 621  ? 47.045  -19.714 -59.528 1.00 91.60  ? 770  ARG   A NE    1 
ATOM   3811 C  CZ    . ARG   A 1 621  ? 47.713  -18.897 -58.712 1.00 92.28  ? 770  ARG   A CZ    1 
ATOM   3812 N  NH1   . ARG   A 1 621  ? 49.024  -18.749 -58.821 1.00 89.97  ? 770  ARG   A NH1   1 
ATOM   3813 N  NH2   . ARG   A 1 621  ? 47.056  -18.231 -57.775 1.00 89.49  ? 770  ARG   A NH2   1 
ATOM   3814 N  N     . PRO   A 1 622  ? 47.316  -19.900 -65.078 1.00 70.65  ? 771  PRO   A N     1 
ATOM   3815 C  CA    . PRO   A 1 622  ? 46.656  -20.937 -65.876 1.00 73.40  ? 771  PRO   A CA    1 
ATOM   3816 C  C     . PRO   A 1 622  ? 45.530  -21.622 -65.085 1.00 68.91  ? 771  PRO   A C     1 
ATOM   3817 O  O     . PRO   A 1 622  ? 45.723  -21.858 -63.917 1.00 69.91  ? 771  PRO   A O     1 
ATOM   3818 C  CB    . PRO   A 1 622  ? 47.779  -21.936 -66.197 1.00 75.72  ? 771  PRO   A CB    1 
ATOM   3819 C  CG    . PRO   A 1 622  ? 49.045  -21.111 -66.105 1.00 77.09  ? 771  PRO   A CG    1 
ATOM   3820 C  CD    . PRO   A 1 622  ? 48.773  -20.100 -65.009 1.00 75.96  ? 771  PRO   A CD    1 
ATOM   3821 N  N     . GLY   A 1 623  ? 44.395  -21.920 -65.728 1.00 67.21  ? 772  GLY   A N     1 
ATOM   3822 C  CA    . GLY   A 1 623  ? 43.136  -22.237 -65.021 1.00 63.84  ? 772  GLY   A CA    1 
ATOM   3823 C  C     . GLY   A 1 623  ? 42.426  -23.464 -65.557 1.00 55.90  ? 772  GLY   A C     1 
ATOM   3824 O  O     . GLY   A 1 623  ? 42.888  -24.046 -66.551 1.00 56.90  ? 772  GLY   A O     1 
ATOM   3825 N  N     . PHE   A 1 624  ? 41.310  -23.825 -64.923 1.00 57.74  ? 773  PHE   A N     1 
ATOM   3826 C  CA    . PHE   A 1 624  ? 40.458  -24.986 -65.297 1.00 66.00  ? 773  PHE   A CA    1 
ATOM   3827 C  C     . PHE   A 1 624  ? 38.996  -24.530 -65.378 1.00 61.47  ? 773  PHE   A C     1 
ATOM   3828 O  O     . PHE   A 1 624  ? 38.564  -23.784 -64.476 1.00 57.84  ? 773  PHE   A O     1 
ATOM   3829 C  CB    . PHE   A 1 624  ? 40.663  -26.144 -64.309 1.00 69.80  ? 773  PHE   A CB    1 
ATOM   3830 C  CG    . PHE   A 1 624  ? 42.093  -26.614 -64.195 1.00 73.81  ? 773  PHE   A CG    1 
ATOM   3831 C  CD1   . PHE   A 1 624  ? 42.956  -26.047 -63.266 1.00 73.89  ? 773  PHE   A CD1   1 
ATOM   3832 C  CD2   . PHE   A 1 624  ? 42.585  -27.603 -65.037 1.00 78.26  ? 773  PHE   A CD2   1 
ATOM   3833 C  CE1   . PHE   A 1 624  ? 44.274  -26.469 -63.175 1.00 81.23  ? 773  PHE   A CE1   1 
ATOM   3834 C  CE2   . PHE   A 1 624  ? 43.904  -28.020 -64.947 1.00 78.48  ? 773  PHE   A CE2   1 
ATOM   3835 C  CZ    . PHE   A 1 624  ? 44.746  -27.453 -64.017 1.00 82.90  ? 773  PHE   A CZ    1 
ATOM   3836 N  N     . CYS   A 1 625  ? 38.280  -24.958 -66.429 1.00 60.39  ? 774  CYS   A N     1 
ATOM   3837 C  CA    . CYS   A 1 625  ? 36.808  -24.793 -66.588 1.00 59.15  ? 774  CYS   A CA    1 
ATOM   3838 C  C     . CYS   A 1 625  ? 36.140  -26.162 -66.716 1.00 53.32  ? 774  CYS   A C     1 
ATOM   3839 O  O     . CYS   A 1 625  ? 36.438  -26.866 -67.692 1.00 50.62  ? 774  CYS   A O     1 
ATOM   3840 C  CB    . CYS   A 1 625  ? 36.449  -23.969 -67.821 1.00 65.72  ? 774  CYS   A CB    1 
ATOM   3841 S  SG    . CYS   A 1 625  ? 34.701  -23.491 -67.857 1.00 65.68  ? 774  CYS   A SG    1 
ATOM   3842 N  N     . PHE   A 1 626  ? 35.258  -26.497 -65.774 1.00 52.44  ? 775  PHE   A N     1 
ATOM   3843 C  CA    . PHE   A 1 626  ? 34.489  -27.768 -65.730 1.00 59.65  ? 775  PHE   A CA    1 
ATOM   3844 C  C     . PHE   A 1 626  ? 33.041  -27.503 -66.177 1.00 57.54  ? 775  PHE   A C     1 
ATOM   3845 O  O     . PHE   A 1 626  ? 32.180  -27.217 -65.323 1.00 56.73  ? 775  PHE   A O     1 
ATOM   3846 C  CB    . PHE   A 1 626  ? 34.530  -28.394 -64.327 1.00 62.16  ? 775  PHE   A CB    1 
ATOM   3847 C  CG    . PHE   A 1 626  ? 35.904  -28.665 -63.765 1.00 60.07  ? 775  PHE   A CG    1 
ATOM   3848 C  CD1   . PHE   A 1 626  ? 36.577  -27.692 -63.043 1.00 56.53  ? 775  PHE   A CD1   1 
ATOM   3849 C  CD2   . PHE   A 1 626  ? 36.520  -29.897 -63.946 1.00 60.70  ? 775  PHE   A CD2   1 
ATOM   3850 C  CE1   . PHE   A 1 626  ? 37.838  -27.941 -62.525 1.00 60.12  ? 775  PHE   A CE1   1 
ATOM   3851 C  CE2   . PHE   A 1 626  ? 37.787  -30.140 -63.431 1.00 59.11  ? 775  PHE   A CE2   1 
ATOM   3852 C  CZ    . PHE   A 1 626  ? 38.441  -29.165 -62.717 1.00 58.90  ? 775  PHE   A CZ    1 
ATOM   3853 N  N     . HIS   A 1 627  ? 32.788  -27.610 -67.485 1.00 61.18  ? 776  HIS   A N     1 
ATOM   3854 C  CA    . HIS   A 1 627  ? 31.442  -27.538 -68.115 1.00 56.76  ? 776  HIS   A CA    1 
ATOM   3855 C  C     . HIS   A 1 627  ? 30.684  -28.813 -67.754 1.00 55.23  ? 776  HIS   A C     1 
ATOM   3856 O  O     . HIS   A 1 627  ? 31.226  -29.899 -68.026 1.00 52.58  ? 776  HIS   A O     1 
ATOM   3857 C  CB    . HIS   A 1 627  ? 31.548  -27.388 -69.645 1.00 55.69  ? 776  HIS   A CB    1 
ATOM   3858 C  CG    . HIS   A 1 627  ? 32.253  -26.158 -70.119 1.00 55.74  ? 776  HIS   A CG    1 
ATOM   3859 N  ND1   . HIS   A 1 627  ? 31.788  -24.884 -69.847 1.00 54.84  ? 776  HIS   A ND1   1 
ATOM   3860 C  CD2   . HIS   A 1 627  ? 33.346  -26.002 -70.900 1.00 57.97  ? 776  HIS   A CD2   1 
ATOM   3861 C  CE1   . HIS   A 1 627  ? 32.582  -23.998 -70.423 1.00 56.85  ? 776  HIS   A CE1   1 
ATOM   3862 N  NE2   . HIS   A 1 627  ? 33.557  -24.658 -71.070 1.00 57.23  ? 776  HIS   A NE2   1 
ATOM   3863 N  N     . LEU   A 1 628  ? 29.488  -28.683 -67.183 1.00 47.68  ? 777  LEU   A N     1 
ATOM   3864 C  CA    . LEU   A 1 628  ? 28.628  -29.830 -66.800 1.00 51.40  ? 777  LEU   A CA    1 
ATOM   3865 C  C     . LEU   A 1 628  ? 27.638  -30.216 -67.915 1.00 56.44  ? 777  LEU   A C     1 
ATOM   3866 O  O     . LEU   A 1 628  ? 26.550  -30.718 -67.588 1.00 58.11  ? 777  LEU   A O     1 
ATOM   3867 C  CB    . LEU   A 1 628  ? 27.875  -29.451 -65.525 1.00 53.22  ? 777  LEU   A CB    1 
ATOM   3868 C  CG    . LEU   A 1 628  ? 28.760  -29.114 -64.329 1.00 54.23  ? 777  LEU   A CG    1 
ATOM   3869 C  CD1   . LEU   A 1 628  ? 27.900  -28.703 -63.136 1.00 51.34  ? 777  LEU   A CD1   1 
ATOM   3870 C  CD2   . LEU   A 1 628  ? 29.665  -30.292 -63.980 1.00 49.93  ? 777  LEU   A CD2   1 
ATOM   3871 N  N     . CYS   A 1 629  ? 27.986  -30.049 -69.189 1.00 57.43  ? 778  CYS   A N     1 
ATOM   3872 C  CA    . CYS   A 1 629  ? 27.200  -30.631 -70.310 1.00 58.09  ? 778  CYS   A CA    1 
ATOM   3873 C  C     . CYS   A 1 629  ? 28.094  -31.614 -71.081 1.00 58.04  ? 778  CYS   A C     1 
ATOM   3874 O  O     . CYS   A 1 629  ? 29.340  -31.387 -71.112 1.00 57.46  ? 778  CYS   A O     1 
ATOM   3875 C  CB    . CYS   A 1 629  ? 26.616  -29.538 -71.206 1.00 53.69  ? 778  CYS   A CB    1 
ATOM   3876 S  SG    . CYS   A 1 629  ? 27.851  -28.650 -72.192 1.00 54.93  ? 778  CYS   A SG    1 
ATOM   3877 N  N     . SER   A 1 630  ? 27.488  -32.660 -71.664 1.00 62.00  ? 779  SER   A N     1 
ATOM   3878 C  CA    . SER   A 1 630  ? 28.126  -33.631 -72.602 1.00 57.06  ? 779  SER   A CA    1 
ATOM   3879 C  C     . SER   A 1 630  ? 28.870  -32.877 -73.710 1.00 58.56  ? 779  SER   A C     1 
ATOM   3880 O  O     . SER   A 1 630  ? 28.534  -31.697 -73.940 1.00 62.79  ? 779  SER   A O     1 
ATOM   3881 C  CB    . SER   A 1 630  ? 27.104  -34.557 -73.198 1.00 58.73  ? 779  SER   A CB    1 
ATOM   3882 O  OG    . SER   A 1 630  ? 26.174  -34.988 -72.218 1.00 66.61  ? 779  SER   A OG    1 
ATOM   3883 N  N     . ARG   A 1 631  ? 29.839  -33.524 -74.366 1.00 61.84  ? 780  ARG   A N     1 
ATOM   3884 C  CA    . ARG   A 1 631  ? 30.522  -32.984 -75.578 1.00 72.64  ? 780  ARG   A CA    1 
ATOM   3885 C  C     . ARG   A 1 631  ? 29.519  -32.961 -76.745 1.00 71.46  ? 780  ARG   A C     1 
ATOM   3886 O  O     . ARG   A 1 631  ? 29.742  -32.193 -77.698 1.00 73.73  ? 780  ARG   A O     1 
ATOM   3887 C  CB    . ARG   A 1 631  ? 31.777  -33.801 -75.918 1.00 69.91  ? 780  ARG   A CB    1 
ATOM   3888 C  CG    . ARG   A 1 631  ? 32.876  -33.697 -74.869 1.00 72.62  ? 780  ARG   A CG    1 
ATOM   3889 C  CD    . ARG   A 1 631  ? 34.156  -34.460 -75.155 1.00 70.39  ? 780  ARG   A CD    1 
ATOM   3890 N  NE    . ARG   A 1 631  ? 35.229  -34.014 -74.262 1.00 72.79  ? 780  ARG   A NE    1 
ATOM   3891 C  CZ    . ARG   A 1 631  ? 36.131  -33.058 -74.529 1.00 79.43  ? 780  ARG   A CZ    1 
ATOM   3892 N  NH1   . ARG   A 1 631  ? 36.120  -32.411 -75.686 1.00 80.70  ? 780  ARG   A NH1   1 
ATOM   3893 N  NH2   . ARG   A 1 631  ? 37.053  -32.748 -73.627 1.00 72.10  ? 780  ARG   A NH2   1 
ATOM   3894 N  N     . ALA   A 1 632  ? 28.449  -33.758 -76.653 1.00 66.04  ? 781  ALA   A N     1 
ATOM   3895 C  CA    . ALA   A 1 632  ? 27.422  -33.947 -77.701 1.00 73.01  ? 781  ALA   A CA    1 
ATOM   3896 C  C     . ALA   A 1 632  ? 26.282  -32.939 -77.505 1.00 76.90  ? 781  ALA   A C     1 
ATOM   3897 O  O     . ALA   A 1 632  ? 25.562  -32.649 -78.483 1.00 77.91  ? 781  ALA   A O     1 
ATOM   3898 C  CB    . ALA   A 1 632  ? 26.924  -35.371 -77.670 1.00 69.39  ? 781  ALA   A CB    1 
ATOM   3899 N  N     . ARG   A 1 633  ? 26.107  -32.431 -76.285 1.00 70.40  ? 782  ARG   A N     1 
ATOM   3900 C  CA    . ARG   A 1 633  ? 25.188  -31.298 -76.023 1.00 66.87  ? 782  ARG   A CA    1 
ATOM   3901 C  C     . ARG   A 1 633  ? 25.887  -30.017 -76.485 1.00 69.78  ? 782  ARG   A C     1 
ATOM   3902 O  O     . ARG   A 1 633  ? 25.214  -29.181 -77.120 1.00 74.85  ? 782  ARG   A O     1 
ATOM   3903 C  CB    . ARG   A 1 633  ? 24.758  -31.243 -74.554 1.00 67.40  ? 782  ARG   A CB    1 
ATOM   3904 C  CG    . ARG   A 1 633  ? 23.912  -30.029 -74.194 1.00 68.10  ? 782  ARG   A CG    1 
ATOM   3905 C  CD    . ARG   A 1 633  ? 22.747  -29.800 -75.134 1.00 65.55  ? 782  ARG   A CD    1 
ATOM   3906 N  NE    . ARG   A 1 633  ? 21.705  -30.787 -74.911 1.00 70.13  ? 782  ARG   A NE    1 
ATOM   3907 C  CZ    . ARG   A 1 633  ? 20.686  -31.040 -75.732 1.00 68.58  ? 782  ARG   A CZ    1 
ATOM   3908 N  NH1   . ARG   A 1 633  ? 20.559  -30.394 -76.881 1.00 65.96  ? 782  ARG   A NH1   1 
ATOM   3909 N  NH2   . ARG   A 1 633  ? 19.789  -31.947 -75.386 1.00 68.71  ? 782  ARG   A NH2   1 
ATOM   3910 N  N     . PHE   A 1 634  ? 27.189  -29.875 -76.222 1.00 63.68  ? 783  PHE   A N     1 
ATOM   3911 C  CA    . PHE   A 1 634  ? 27.970  -28.701 -76.688 1.00 66.91  ? 783  PHE   A CA    1 
ATOM   3912 C  C     . PHE   A 1 634  ? 27.709  -28.513 -78.187 1.00 70.72  ? 783  PHE   A C     1 
ATOM   3913 O  O     . PHE   A 1 634  ? 27.388  -27.387 -78.586 1.00 76.46  ? 783  PHE   A O     1 
ATOM   3914 C  CB    . PHE   A 1 634  ? 29.465  -28.830 -76.395 1.00 59.68  ? 783  PHE   A CB    1 
ATOM   3915 C  CG    . PHE   A 1 634  ? 30.291  -27.659 -76.874 1.00 60.33  ? 783  PHE   A CG    1 
ATOM   3916 C  CD1   . PHE   A 1 634  ? 30.365  -26.487 -76.135 1.00 58.97  ? 783  PHE   A CD1   1 
ATOM   3917 C  CD2   . PHE   A 1 634  ? 30.991  -27.722 -78.070 1.00 61.33  ? 783  PHE   A CD2   1 
ATOM   3918 C  CE1   . PHE   A 1 634  ? 31.128  -25.411 -76.571 1.00 58.81  ? 783  PHE   A CE1   1 
ATOM   3919 C  CE2   . PHE   A 1 634  ? 31.754  -26.646 -78.507 1.00 60.95  ? 783  PHE   A CE2   1 
ATOM   3920 C  CZ    . PHE   A 1 634  ? 31.818  -25.488 -77.759 1.00 61.06  ? 783  PHE   A CZ    1 
ATOM   3921 N  N     . GLU   A 1 635  ? 27.807  -29.586 -78.978 1.00 74.89  ? 784  GLU   A N     1 
ATOM   3922 C  CA    . GLU   A 1 635  ? 27.728  -29.529 -80.466 1.00 75.91  ? 784  GLU   A CA    1 
ATOM   3923 C  C     . GLU   A 1 635  ? 26.405  -28.875 -80.901 1.00 76.18  ? 784  GLU   A C     1 
ATOM   3924 O  O     . GLU   A 1 635  ? 26.428  -28.092 -81.874 1.00 73.79  ? 784  GLU   A O     1 
ATOM   3925 C  CB    . GLU   A 1 635  ? 27.907  -30.927 -81.068 1.00 78.11  ? 784  GLU   A CB    1 
ATOM   3926 C  CG    . GLU   A 1 635  ? 29.346  -31.434 -81.044 1.00 79.96  ? 784  GLU   A CG    1 
ATOM   3927 C  CD    . GLU   A 1 635  ? 30.392  -30.448 -81.545 1.00 91.85  ? 784  GLU   A CD    1 
ATOM   3928 O  OE1   . GLU   A 1 635  ? 30.069  -29.633 -82.440 1.00 100.20 ? 784  GLU   A OE1   1 
ATOM   3929 O  OE2   . GLU   A 1 635  ? 31.532  -30.485 -81.035 1.00 95.83  ? 784  GLU   A OE2   1 
ATOM   3930 N  N     . ARG   A 1 636  ? 25.316  -29.149 -80.176 1.00 72.07  ? 785  ARG   A N     1 
ATOM   3931 C  CA    . ARG   A 1 636  ? 23.934  -28.692 -80.481 1.00 72.19  ? 785  ARG   A CA    1 
ATOM   3932 C  C     . ARG   A 1 636  ? 23.626  -27.290 -79.926 1.00 73.15  ? 785  ARG   A C     1 
ATOM   3933 O  O     . ARG   A 1 636  ? 22.498  -26.820 -80.144 1.00 71.45  ? 785  ARG   A O     1 
ATOM   3934 C  CB    . ARG   A 1 636  ? 22.930  -29.653 -79.847 1.00 73.35  ? 785  ARG   A CB    1 
ATOM   3935 C  CG    . ARG   A 1 636  ? 22.985  -31.074 -80.379 1.00 75.03  ? 785  ARG   A CG    1 
ATOM   3936 C  CD    . ARG   A 1 636  ? 21.675  -31.710 -79.981 1.00 79.93  ? 785  ARG   A CD    1 
ATOM   3937 N  NE    . ARG   A 1 636  ? 21.598  -33.128 -80.275 1.00 90.82  ? 785  ARG   A NE    1 
ATOM   3938 C  CZ    . ARG   A 1 636  ? 20.505  -33.861 -80.097 1.00 97.62  ? 785  ARG   A CZ    1 
ATOM   3939 N  NH1   . ARG   A 1 636  ? 20.526  -35.151 -80.394 1.00 90.83  ? 785  ARG   A NH1   1 
ATOM   3940 N  NH2   . ARG   A 1 636  ? 19.399  -33.301 -79.628 1.00 103.47 ? 785  ARG   A NH2   1 
ATOM   3941 N  N     . LEU   A 1 637  ? 24.553  -26.655 -79.203 1.00 74.11  ? 786  LEU   A N     1 
ATOM   3942 C  CA    . LEU   A 1 637  ? 24.334  -25.303 -78.613 1.00 72.32  ? 786  LEU   A CA    1 
ATOM   3943 C  C     . LEU   A 1 637  ? 24.327  -24.269 -79.740 1.00 62.63  ? 786  LEU   A C     1 
ATOM   3944 O  O     . LEU   A 1 637  ? 25.249  -24.313 -80.563 1.00 63.83  ? 786  LEU   A O     1 
ATOM   3945 C  CB    . LEU   A 1 637  ? 25.436  -24.953 -77.598 1.00 66.57  ? 786  LEU   A CB    1 
ATOM   3946 C  CG    . LEU   A 1 637  ? 25.537  -25.818 -76.339 1.00 63.69  ? 786  LEU   A CG    1 
ATOM   3947 C  CD1   . LEU   A 1 637  ? 26.650  -25.298 -75.447 1.00 60.46  ? 786  LEU   A CD1   1 
ATOM   3948 C  CD2   . LEU   A 1 637  ? 24.221  -25.891 -75.569 1.00 57.54  ? 786  LEU   A CD2   1 
ATOM   3949 N  N     . GLU   A 1 638  ? 23.359  -23.347 -79.727 1.00 59.95  ? 787  GLU   A N     1 
ATOM   3950 C  CA    . GLU   A 1 638  ? 23.383  -22.096 -80.534 1.00 56.78  ? 787  GLU   A CA    1 
ATOM   3951 C  C     . GLU   A 1 638  ? 24.677  -21.328 -80.240 1.00 55.99  ? 787  GLU   A C     1 
ATOM   3952 O  O     . GLU   A 1 638  ? 25.271  -21.558 -79.176 1.00 57.29  ? 787  GLU   A O     1 
ATOM   3953 C  CB    . GLU   A 1 638  ? 22.118  -21.278 -80.266 1.00 58.82  ? 787  GLU   A CB    1 
ATOM   3954 C  CG    . GLU   A 1 638  ? 20.882  -21.827 -80.968 1.00 71.00  ? 787  GLU   A CG    1 
ATOM   3955 C  CD    . GLU   A 1 638  ? 21.064  -22.238 -82.431 1.00 80.86  ? 787  GLU   A CD    1 
ATOM   3956 O  OE1   . GLU   A 1 638  ? 21.597  -21.424 -83.243 1.00 76.18  ? 787  GLU   A OE1   1 
ATOM   3957 O  OE2   . GLU   A 1 638  ? 20.702  -23.390 -82.756 1.00 83.95  ? 787  GLU   A OE2   1 
ATOM   3958 N  N     . THR   A 1 639  ? 25.123  -20.476 -81.167 1.00 54.73  ? 788  THR   A N     1 
ATOM   3959 C  CA    . THR   A 1 639  ? 26.381  -19.696 -81.046 1.00 50.57  ? 788  THR   A CA    1 
ATOM   3960 C  C     . THR   A 1 639  ? 26.136  -18.489 -80.138 1.00 57.06  ? 788  THR   A C     1 
ATOM   3961 O  O     . THR   A 1 639  ? 27.070  -18.089 -79.383 1.00 57.19  ? 788  THR   A O     1 
ATOM   3962 C  CB    . THR   A 1 639  ? 26.912  -19.316 -82.433 1.00 55.29  ? 788  THR   A CB    1 
ATOM   3963 O  OG1   . THR   A 1 639  ? 27.348  -20.517 -83.075 1.00 65.85  ? 788  THR   A OG1   1 
ATOM   3964 C  CG2   . THR   A 1 639  ? 28.075  -18.352 -82.398 1.00 56.43  ? 788  THR   A CG2   1 
ATOM   3965 N  N     . HIS   A 1 640  ? 24.939  -17.909 -80.219 1.00 64.41  ? 789  HIS   A N     1 
ATOM   3966 C  CA    . HIS   A 1 640  ? 24.512  -16.749 -79.390 1.00 64.14  ? 789  HIS   A CA    1 
ATOM   3967 C  C     . HIS   A 1 640  ? 23.107  -17.005 -78.845 1.00 56.67  ? 789  HIS   A C     1 
ATOM   3968 O  O     . HIS   A 1 640  ? 22.360  -17.774 -79.470 1.00 56.24  ? 789  HIS   A O     1 
ATOM   3969 C  CB    . HIS   A 1 640  ? 24.512  -15.429 -80.178 1.00 62.79  ? 789  HIS   A CB    1 
ATOM   3970 C  CG    . HIS   A 1 640  ? 25.711  -15.159 -81.026 1.00 71.13  ? 789  HIS   A CG    1 
ATOM   3971 N  ND1   . HIS   A 1 640  ? 26.801  -14.443 -80.558 1.00 73.00  ? 789  HIS   A ND1   1 
ATOM   3972 C  CD2   . HIS   A 1 640  ? 25.958  -15.419 -82.331 1.00 71.65  ? 789  HIS   A CD2   1 
ATOM   3973 C  CE1   . HIS   A 1 640  ? 27.676  -14.294 -81.533 1.00 71.81  ? 789  HIS   A CE1   1 
ATOM   3974 N  NE2   . HIS   A 1 640  ? 27.183  -14.888 -82.632 1.00 72.35  ? 789  HIS   A NE2   1 
ATOM   3975 N  N     . MET   A 1 641  ? 22.777  -16.363 -77.726 1.00 57.12  ? 790  MET   A N     1 
ATOM   3976 C  CA    . MET   A 1 641  ? 21.400  -16.276 -77.179 1.00 58.89  ? 790  MET   A CA    1 
ATOM   3977 C  C     . MET   A 1 641  ? 20.566  -15.429 -78.155 1.00 56.14  ? 790  MET   A C     1 
ATOM   3978 O  O     . MET   A 1 641  ? 21.102  -14.496 -78.777 1.00 46.57  ? 790  MET   A O     1 
ATOM   3979 C  CB    . MET   A 1 641  ? 21.352  -15.608 -75.791 1.00 64.29  ? 790  MET   A CB    1 
ATOM   3980 C  CG    . MET   A 1 641  ? 22.164  -16.289 -74.688 1.00 66.37  ? 790  MET   A CG    1 
ATOM   3981 S  SD    . MET   A 1 641  ? 21.556  -17.933 -74.242 1.00 72.70  ? 790  MET   A SD    1 
ATOM   3982 C  CE    . MET   A 1 641  ? 19.937  -17.520 -73.590 1.00 74.84  ? 790  MET   A CE    1 
ATOM   3983 N  N     . THR   A 1 642  ? 19.288  -15.755 -78.269 1.00 51.57  ? 791  THR   A N     1 
ATOM   3984 C  CA    . THR   A 1 642  ? 18.235  -14.862 -78.781 1.00 51.67  ? 791  THR   A CA    1 
ATOM   3985 C  C     . THR   A 1 642  ? 18.320  -13.540 -78.026 1.00 53.15  ? 791  THR   A C     1 
ATOM   3986 O  O     . THR   A 1 642  ? 18.161  -13.535 -76.809 1.00 51.63  ? 791  THR   A O     1 
ATOM   3987 C  CB    . THR   A 1 642  ? 16.898  -15.573 -78.594 1.00 51.62  ? 791  THR   A CB    1 
ATOM   3988 O  OG1   . THR   A 1 642  ? 17.053  -16.813 -79.291 1.00 58.70  ? 791  THR   A OG1   1 
ATOM   3989 C  CG2   . THR   A 1 642  ? 15.723  -14.786 -79.118 1.00 56.54  ? 791  THR   A CG2   1 
ATOM   3990 N  N     . PRO   A 1 643  ? 18.571  -12.389 -78.702 1.00 47.89  ? 792  PRO   A N     1 
ATOM   3991 C  CA    . PRO   A 1 643  ? 18.443  -11.082 -78.061 1.00 44.62  ? 792  PRO   A CA    1 
ATOM   3992 C  C     . PRO   A 1 643  ? 17.043  -10.896 -77.454 1.00 47.11  ? 792  PRO   A C     1 
ATOM   3993 O  O     . PRO   A 1 643  ? 16.103  -11.547 -77.933 1.00 48.02  ? 792  PRO   A O     1 
ATOM   3994 C  CB    . PRO   A 1 643  ? 18.700  -10.085 -79.197 1.00 47.31  ? 792  PRO   A CB    1 
ATOM   3995 C  CG    . PRO   A 1 643  ? 18.549  -10.880 -80.459 1.00 46.95  ? 792  PRO   A CG    1 
ATOM   3996 C  CD    . PRO   A 1 643  ? 18.990  -12.280 -80.105 1.00 46.10  ? 792  PRO   A CD    1 
ATOM   3997 N  N     . GLU   A 1 644  ? 16.921  -10.060 -76.417 1.00 40.19  ? 793  GLU   A N     1 
ATOM   3998 C  CA    . GLU   A 1 644  ? 15.654  -9.911  -75.636 1.00 44.56  ? 793  GLU   A CA    1 
ATOM   3999 C  C     . GLU   A 1 644  ? 14.589  -9.249  -76.506 1.00 38.70  ? 793  GLU   A C     1 
ATOM   4000 O  O     . GLU   A 1 644  ? 13.412  -9.454  -76.230 1.00 37.33  ? 793  GLU   A O     1 
ATOM   4001 C  CB    . GLU   A 1 644  ? 15.828  -9.065  -74.373 1.00 45.92  ? 793  GLU   A CB    1 
ATOM   4002 C  CG    . GLU   A 1 644  ? 16.739  -9.706  -73.349 1.00 51.25  ? 793  GLU   A CG    1 
ATOM   4003 C  CD    . GLU   A 1 644  ? 16.947  -8.921  -72.062 1.00 54.81  ? 793  GLU   A CD    1 
ATOM   4004 O  OE1   . GLU   A 1 644  ? 17.610  -9.469  -71.148 1.00 65.81  ? 793  GLU   A OE1   1 
ATOM   4005 O  OE2   . GLU   A 1 644  ? 16.458  -7.774  -71.967 1.00 55.33  ? 793  GLU   A OE2   1 
ATOM   4006 N  N     . MET   A 1 645  ? 15.012  -8.460  -77.491 1.00 40.26  ? 794  MET   A N     1 
ATOM   4007 C  CA    . MET   A 1 645  ? 14.118  -7.737  -78.432 1.00 42.08  ? 794  MET   A CA    1 
ATOM   4008 C  C     . MET   A 1 645  ? 13.244  -8.754  -79.197 1.00 40.66  ? 794  MET   A C     1 
ATOM   4009 O  O     . MET   A 1 645  ? 12.130  -8.394  -79.576 1.00 36.85  ? 794  MET   A O     1 
ATOM   4010 C  CB    . MET   A 1 645  ? 14.975  -6.908  -79.392 1.00 42.82  ? 794  MET   A CB    1 
ATOM   4011 C  CG    . MET   A 1 645  ? 14.188  -6.057  -80.370 1.00 44.87  ? 794  MET   A CG    1 
ATOM   4012 S  SD    . MET   A 1 645  ? 13.347  -4.650  -79.635 1.00 45.18  ? 794  MET   A SD    1 
ATOM   4013 C  CE    . MET   A 1 645  ? 14.751  -3.597  -79.276 1.00 48.96  ? 794  MET   A CE    1 
ATOM   4014 N  N     . PHE   A 1 646  ? 13.718  -9.992  -79.380 1.00 40.06  ? 795  PHE   A N     1 
ATOM   4015 C  CA    . PHE   A 1 646  ? 13.008  -11.077 -80.104 1.00 42.20  ? 795  PHE   A CA    1 
ATOM   4016 C  C     . PHE   A 1 646  ? 11.995  -11.783 -79.194 1.00 44.54  ? 795  PHE   A C     1 
ATOM   4017 O  O     . PHE   A 1 646  ? 11.172  -12.528 -79.734 1.00 47.75  ? 795  PHE   A O     1 
ATOM   4018 C  CB    . PHE   A 1 646  ? 13.979  -12.124 -80.656 1.00 38.77  ? 795  PHE   A CB    1 
ATOM   4019 C  CG    . PHE   A 1 646  ? 14.886  -11.672 -81.772 1.00 44.88  ? 795  PHE   A CG    1 
ATOM   4020 C  CD1   . PHE   A 1 646  ? 14.907  -10.353 -82.213 1.00 47.30  ? 795  PHE   A CD1   1 
ATOM   4021 C  CD2   . PHE   A 1 646  ? 15.746  -12.577 -82.379 1.00 49.09  ? 795  PHE   A CD2   1 
ATOM   4022 C  CE1   . PHE   A 1 646  ? 15.764  -9.956  -83.228 1.00 49.02  ? 795  PHE   A CE1   1 
ATOM   4023 C  CE2   . PHE   A 1 646  ? 16.603  -12.177 -83.397 1.00 51.44  ? 795  PHE   A CE2   1 
ATOM   4024 C  CZ    . PHE   A 1 646  ? 16.611  -10.867 -83.820 1.00 50.49  ? 795  PHE   A CZ    1 
ATOM   4025 N  N     . ARG   A 1 647  ? 12.041  -11.600 -77.876 1.00 44.88  ? 796  ARG   A N     1 
ATOM   4026 C  CA    . ARG   A 1 647  ? 11.301  -12.516 -76.959 1.00 46.45  ? 796  ARG   A CA    1 
ATOM   4027 C  C     . ARG   A 1 647  ? 10.821  -11.793 -75.701 1.00 44.57  ? 796  ARG   A C     1 
ATOM   4028 O  O     . ARG   A 1 647  ? 10.703  -12.464 -74.681 1.00 43.21  ? 796  ARG   A O     1 
ATOM   4029 C  CB    . ARG   A 1 647  ? 12.179  -13.710 -76.569 1.00 47.59  ? 796  ARG   A CB    1 
ATOM   4030 C  CG    . ARG   A 1 647  ? 13.497  -13.345 -75.897 1.00 51.33  ? 796  ARG   A CG    1 
ATOM   4031 C  CD    . ARG   A 1 647  ? 14.300  -14.573 -75.485 1.00 52.32  ? 796  ARG   A CD    1 
ATOM   4032 N  NE    . ARG   A 1 647  ? 15.700  -14.284 -75.171 1.00 53.80  ? 796  ARG   A NE    1 
ATOM   4033 C  CZ    . ARG   A 1 647  ? 16.143  -13.743 -74.031 1.00 57.57  ? 796  ARG   A CZ    1 
ATOM   4034 N  NH1   . ARG   A 1 647  ? 15.306  -13.399 -73.063 1.00 54.31  ? 796  ARG   A NH1   1 
ATOM   4035 N  NH2   . ARG   A 1 647  ? 17.437  -13.544 -73.867 1.00 56.75  ? 796  ARG   A NH2   1 
ATOM   4036 N  N     . THR   A 1 648  ? 10.524  -10.496 -75.787 1.00 41.95  ? 797  THR   A N     1 
ATOM   4037 C  CA    . THR   A 1 648  ? 10.039  -9.679  -74.646 1.00 43.55  ? 797  THR   A CA    1 
ATOM   4038 C  C     . THR   A 1 648  ? 8.816   -8.885  -75.091 1.00 39.39  ? 797  THR   A C     1 
ATOM   4039 O  O     . THR   A 1 648  ? 8.791   -8.354  -76.183 1.00 42.14  ? 797  THR   A O     1 
ATOM   4040 C  CB    . THR   A 1 648  ? 11.137  -8.736  -74.117 1.00 47.70  ? 797  THR   A CB    1 
ATOM   4041 O  OG1   . THR   A 1 648  ? 12.339  -9.462  -73.860 1.00 46.68  ? 797  THR   A OG1   1 
ATOM   4042 C  CG2   . THR   A 1 648  ? 10.733  -8.012  -72.852 1.00 48.99  ? 797  THR   A CG2   1 
ATOM   4043 N  N     . PRO   A 1 649  ? 7.779   -8.745  -74.249 1.00 42.77  ? 798  PRO   A N     1 
ATOM   4044 C  CA    . PRO   A 1 649  ? 6.673   -7.839  -74.541 1.00 40.89  ? 798  PRO   A CA    1 
ATOM   4045 C  C     . PRO   A 1 649  ? 7.155   -6.397  -74.743 1.00 41.23  ? 798  PRO   A C     1 
ATOM   4046 O  O     . PRO   A 1 649  ? 8.119   -6.012  -74.105 1.00 39.76  ? 798  PRO   A O     1 
ATOM   4047 C  CB    . PRO   A 1 649  ? 5.802   -7.934  -73.281 1.00 46.93  ? 798  PRO   A CB    1 
ATOM   4048 C  CG    . PRO   A 1 649  ? 6.146   -9.287  -72.677 1.00 45.50  ? 798  PRO   A CG    1 
ATOM   4049 C  CD    . PRO   A 1 649  ? 7.619   -9.445  -72.962 1.00 45.08  ? 798  PRO   A CD    1 
ATOM   4050 N  N     . LEU   A 1 650  ? 6.478   -5.640  -75.616 1.00 41.21  ? 799  LEU   A N     1 
ATOM   4051 C  CA    . LEU   A 1 650  ? 6.956   -4.321  -76.102 1.00 38.47  ? 799  LEU   A CA    1 
ATOM   4052 C  C     . LEU   A 1 650  ? 6.003   -3.197  -75.698 1.00 37.05  ? 799  LEU   A C     1 
ATOM   4053 O  O     . LEU   A 1 650  ? 6.251   -2.064  -76.137 1.00 36.27  ? 799  LEU   A O     1 
ATOM   4054 C  CB    . LEU   A 1 650  ? 7.094   -4.347  -77.624 1.00 41.66  ? 799  LEU   A CB    1 
ATOM   4055 C  CG    . LEU   A 1 650  ? 8.009   -5.412  -78.222 1.00 41.01  ? 799  LEU   A CG    1 
ATOM   4056 C  CD1   . LEU   A 1 650  ? 7.920   -5.355  -79.736 1.00 43.95  ? 799  LEU   A CD1   1 
ATOM   4057 C  CD2   . LEU   A 1 650  ? 9.444   -5.213  -77.790 1.00 41.66  ? 799  LEU   A CD2   1 
ATOM   4058 N  N     . HIS   A 1 651  ? 4.978   -3.453  -74.884 1.00 38.30  ? 800  HIS   A N     1 
ATOM   4059 C  CA    . HIS   A 1 651  ? 3.987   -2.408  -74.520 1.00 40.25  ? 800  HIS   A CA    1 
ATOM   4060 C  C     . HIS   A 1 651  ? 4.667   -1.265  -73.757 1.00 41.01  ? 800  HIS   A C     1 
ATOM   4061 O  O     . HIS   A 1 651  ? 4.315   -0.097  -74.047 1.00 45.16  ? 800  HIS   A O     1 
ATOM   4062 C  CB    . HIS   A 1 651  ? 2.740   -2.978  -73.846 1.00 44.22  ? 800  HIS   A CB    1 
ATOM   4063 C  CG    . HIS   A 1 651  ? 3.023   -3.976  -72.793 1.00 46.26  ? 800  HIS   A CG    1 
ATOM   4064 N  ND1   . HIS   A 1 651  ? 3.268   -5.292  -73.093 1.00 50.83  ? 800  HIS   A ND1   1 
ATOM   4065 C  CD2   . HIS   A 1 651  ? 3.079   -3.855  -71.453 1.00 51.48  ? 800  HIS   A CD2   1 
ATOM   4066 C  CE1   . HIS   A 1 651  ? 3.497   -5.947  -71.975 1.00 57.07  ? 800  HIS   A CE1   1 
ATOM   4067 N  NE2   . HIS   A 1 651  ? 3.386   -5.083  -70.954 1.00 58.67  ? 800  HIS   A NE2   1 
ATOM   4068 N  N     . GLU   A 1 652  ? 5.658   -1.527  -72.903 1.00 42.74  ? 801  GLU   A N     1 
ATOM   4069 C  CA    . GLU   A 1 652  ? 6.329   -0.438  -72.130 1.00 44.34  ? 801  GLU   A CA    1 
ATOM   4070 C  C     . GLU   A 1 652  ? 7.213   0.369   -73.076 1.00 42.00  ? 801  GLU   A C     1 
ATOM   4071 O  O     . GLU   A 1 652  ? 7.188   1.612   -72.995 1.00 47.91  ? 801  GLU   A O     1 
ATOM   4072 C  CB    . GLU   A 1 652  ? 7.114   -0.985  -70.936 1.00 49.81  ? 801  GLU   A CB    1 
ATOM   4073 C  CG    . GLU   A 1 652  ? 6.187   -1.505  -69.847 1.00 59.37  ? 801  GLU   A CG    1 
ATOM   4074 C  CD    . GLU   A 1 652  ? 6.855   -2.164  -68.654 1.00 65.01  ? 801  GLU   A CD    1 
ATOM   4075 O  OE1   . GLU   A 1 652  ? 7.871   -2.864  -68.854 1.00 74.24  ? 801  GLU   A OE1   1 
ATOM   4076 O  OE2   . GLU   A 1 652  ? 6.354   -1.974  -67.527 1.00 75.29  ? 801  GLU   A OE2   1 
ATOM   4077 N  N     . ILE   A 1 653  ? 7.973   -0.302  -73.936 1.00 38.29  ? 802  ILE   A N     1 
ATOM   4078 C  CA    . ILE   A 1 653  ? 8.751   0.394   -75.000 1.00 40.71  ? 802  ILE   A CA    1 
ATOM   4079 C  C     . ILE   A 1 653  ? 7.782   1.210   -75.877 1.00 39.17  ? 802  ILE   A C     1 
ATOM   4080 O  O     . ILE   A 1 653  ? 8.089   2.374   -76.140 1.00 40.08  ? 802  ILE   A O     1 
ATOM   4081 C  CB    . ILE   A 1 653  ? 9.609   -0.608  -75.786 1.00 41.66  ? 802  ILE   A CB    1 
ATOM   4082 C  CG1   . ILE   A 1 653  ? 10.838  -0.984  -74.960 1.00 45.26  ? 802  ILE   A CG1   1 
ATOM   4083 C  CG2   . ILE   A 1 653  ? 9.998   -0.070  -77.149 1.00 43.95  ? 802  ILE   A CG2   1 
ATOM   4084 C  CD1   . ILE   A 1 653  ? 11.616  -2.143  -75.512 1.00 46.70  ? 802  ILE   A CD1   1 
ATOM   4085 N  N     . ALA   A 1 654  ? 6.635   0.659   -76.278 1.00 37.71  ? 803  ALA   A N     1 
ATOM   4086 C  CA    . ALA   A 1 654  ? 5.654   1.381   -77.119 1.00 39.23  ? 803  ALA   A CA    1 
ATOM   4087 C  C     . ALA   A 1 654  ? 5.247   2.678   -76.407 1.00 38.50  ? 803  ALA   A C     1 
ATOM   4088 O  O     . ALA   A 1 654  ? 5.276   3.722   -77.060 1.00 44.89  ? 803  ALA   A O     1 
ATOM   4089 C  CB    . ALA   A 1 654  ? 4.459   0.520   -77.485 1.00 37.95  ? 803  ALA   A CB    1 
ATOM   4090 N  N     . LEU   A 1 655  ? 4.901   2.645   -75.122 1.00 41.06  ? 804  LEU   A N     1 
ATOM   4091 C  CA    . LEU   A 1 655  ? 4.501   3.878   -74.380 1.00 40.58  ? 804  LEU   A CA    1 
ATOM   4092 C  C     . LEU   A 1 655  ? 5.642   4.886   -74.387 1.00 38.28  ? 804  LEU   A C     1 
ATOM   4093 O  O     . LEU   A 1 655  ? 5.363   6.085   -74.491 1.00 41.81  ? 804  LEU   A O     1 
ATOM   4094 C  CB    . LEU   A 1 655  ? 4.130   3.560   -72.936 1.00 37.11  ? 804  LEU   A CB    1 
ATOM   4095 C  CG    . LEU   A 1 655  ? 2.812   2.822   -72.755 1.00 39.91  ? 804  LEU   A CG    1 
ATOM   4096 C  CD1   . LEU   A 1 655  ? 2.519   2.653   -71.283 1.00 40.76  ? 804  LEU   A CD1   1 
ATOM   4097 C  CD2   . LEU   A 1 655  ? 1.666   3.549   -73.428 1.00 41.06  ? 804  LEU   A CD2   1 
ATOM   4098 N  N     . SER   A 1 656  ? 6.878   4.435   -74.230 1.00 39.00  ? 805  SER   A N     1 
ATOM   4099 C  CA    . SER   A 1 656  ? 8.052   5.349   -74.186 1.00 38.60  ? 805  SER   A CA    1 
ATOM   4100 C  C     . SER   A 1 656  ? 8.191   6.054   -75.546 1.00 39.57  ? 805  SER   A C     1 
ATOM   4101 O  O     . SER   A 1 656  ? 8.381   7.299   -75.565 1.00 38.72  ? 805  SER   A O     1 
ATOM   4102 C  CB    . SER   A 1 656  ? 9.300   4.599   -73.771 1.00 41.16  ? 805  SER   A CB    1 
ATOM   4103 O  OG    . SER   A 1 656  ? 10.461  5.352   -74.082 1.00 48.16  ? 805  SER   A OG    1 
ATOM   4104 N  N     . ILE   A 1 657  ? 8.052   5.300   -76.648 1.00 38.87  ? 806  ILE   A N     1 
ATOM   4105 C  CA    . ILE   A 1 657  ? 8.120   5.842   -78.038 1.00 41.43  ? 806  ILE   A CA    1 
ATOM   4106 C  C     . ILE   A 1 657  ? 7.100   6.975   -78.201 1.00 38.69  ? 806  ILE   A C     1 
ATOM   4107 O  O     . ILE   A 1 657  ? 7.449   7.973   -78.833 1.00 39.91  ? 806  ILE   A O     1 
ATOM   4108 C  CB    . ILE   A 1 657  ? 7.902   4.747   -79.099 1.00 40.58  ? 806  ILE   A CB    1 
ATOM   4109 C  CG1   . ILE   A 1 657  ? 9.155   3.906   -79.323 1.00 40.44  ? 806  ILE   A CG1   1 
ATOM   4110 C  CG2   . ILE   A 1 657  ? 7.430   5.382   -80.399 1.00 41.47  ? 806  ILE   A CG2   1 
ATOM   4111 C  CD1   . ILE   A 1 657  ? 8.871   2.545   -79.929 1.00 45.47  ? 806  ILE   A CD1   1 
ATOM   4112 N  N     . LYS   A 1 658  ? 5.889   6.797   -77.673 1.00 39.52  ? 807  LYS   A N     1 
ATOM   4113 C  CA    . LYS   A 1 658  ? 4.745   7.738   -77.800 1.00 42.16  ? 807  LYS   A CA    1 
ATOM   4114 C  C     . LYS   A 1 658  ? 4.938   8.941   -76.879 1.00 41.00  ? 807  LYS   A C     1 
ATOM   4115 O  O     . LYS   A 1 658  ? 4.707   10.065  -77.331 1.00 45.81  ? 807  LYS   A O     1 
ATOM   4116 C  CB    . LYS   A 1 658  ? 3.426   7.018   -77.501 1.00 48.00  ? 807  LYS   A CB    1 
ATOM   4117 C  CG    . LYS   A 1 658  ? 2.960   6.047   -78.583 1.00 50.83  ? 807  LYS   A CG    1 
ATOM   4118 C  CD    . LYS   A 1 658  ? 2.479   6.775   -79.819 1.00 55.81  ? 807  LYS   A CD    1 
ATOM   4119 C  CE    . LYS   A 1 658  ? 2.478   5.908   -81.053 1.00 65.67  ? 807  LYS   A CE    1 
ATOM   4120 N  NZ    . LYS   A 1 658  ? 1.859   6.624   -82.193 1.00 69.52  ? 807  LYS   A NZ    1 
ATOM   4121 N  N     . LEU   A 1 659  ? 5.353   8.719   -75.639 1.00 43.84  ? 808  LEU   A N     1 
ATOM   4122 C  CA    . LEU   A 1 659  ? 5.587   9.821   -74.672 1.00 46.51  ? 808  LEU   A CA    1 
ATOM   4123 C  C     . LEU   A 1 659  ? 6.697   10.719  -75.211 1.00 47.52  ? 808  LEU   A C     1 
ATOM   4124 O  O     . LEU   A 1 659  ? 6.568   11.941  -75.031 1.00 46.86  ? 808  LEU   A O     1 
ATOM   4125 C  CB    . LEU   A 1 659  ? 5.969   9.266   -73.296 1.00 47.38  ? 808  LEU   A CB    1 
ATOM   4126 C  CG    . LEU   A 1 659  ? 6.361   10.325  -72.270 1.00 47.38  ? 808  LEU   A CG    1 
ATOM   4127 C  CD1   . LEU   A 1 659  ? 5.171   11.195  -71.920 1.00 47.73  ? 808  LEU   A CD1   1 
ATOM   4128 C  CD2   . LEU   A 1 659  ? 6.950   9.688   -71.027 1.00 47.80  ? 808  LEU   A CD2   1 
ATOM   4129 N  N     . LEU   A 1 660  ? 7.743   10.132  -75.817 1.00 47.37  ? 809  LEU   A N     1 
ATOM   4130 C  CA    . LEU   A 1 660  ? 8.926   10.882  -76.340 1.00 43.82  ? 809  LEU   A CA    1 
ATOM   4131 C  C     . LEU   A 1 660  ? 8.665   11.428  -77.749 1.00 43.06  ? 809  LEU   A C     1 
ATOM   4132 O  O     . LEU   A 1 660  ? 9.564   12.126  -78.263 1.00 43.75  ? 809  LEU   A O     1 
ATOM   4133 C  CB    . LEU   A 1 660  ? 10.156  9.973   -76.330 1.00 44.33  ? 809  LEU   A CB    1 
ATOM   4134 C  CG    . LEU   A 1 660  ? 10.666  9.591   -74.939 1.00 47.79  ? 809  LEU   A CG    1 
ATOM   4135 C  CD1   . LEU   A 1 660  ? 11.940  8.764   -75.016 1.00 47.04  ? 809  LEU   A CD1   1 
ATOM   4136 C  CD2   . LEU   A 1 660  ? 10.893  10.831  -74.093 1.00 49.59  ? 809  LEU   A CD2   1 
ATOM   4137 N  N     . ARG   A 1 661  ? 7.506   11.121  -78.350 1.00 45.06  ? 810  ARG   A N     1 
ATOM   4138 C  CA    . ARG   A 1 661  ? 7.076   11.637  -79.683 1.00 50.47  ? 810  ARG   A CA    1 
ATOM   4139 C  C     . ARG   A 1 661  ? 8.091   11.211  -80.756 1.00 46.55  ? 810  ARG   A C     1 
ATOM   4140 O  O     . ARG   A 1 661  ? 8.527   12.051  -81.562 1.00 46.74  ? 810  ARG   A O     1 
ATOM   4141 C  CB    . ARG   A 1 661  ? 6.919   13.162  -79.647 1.00 57.69  ? 810  ARG   A CB    1 
ATOM   4142 C  CG    . ARG   A 1 661  ? 6.262   13.700  -78.384 1.00 69.34  ? 810  ARG   A CG    1 
ATOM   4143 C  CD    . ARG   A 1 661  ? 5.859   15.158  -78.492 1.00 78.01  ? 810  ARG   A CD    1 
ATOM   4144 N  NE    . ARG   A 1 661  ? 4.595   15.290  -79.206 1.00 92.27  ? 810  ARG   A NE    1 
ATOM   4145 C  CZ    . ARG   A 1 661  ? 3.392   15.014  -78.696 1.00 97.59  ? 810  ARG   A CZ    1 
ATOM   4146 N  NH1   . ARG   A 1 661  ? 3.273   14.591  -77.447 1.00 97.01  ? 810  ARG   A NH1   1 
ATOM   4147 N  NH2   . ARG   A 1 661  ? 2.308   15.157  -79.444 1.00 92.05  ? 810  ARG   A NH2   1 
ATOM   4148 N  N     . LEU   A 1 662  ? 8.472   9.941   -80.769 1.00 42.64  ? 811  LEU   A N     1 
ATOM   4149 C  CA    . LEU   A 1 662  ? 9.508   9.441   -81.693 1.00 43.70  ? 811  LEU   A CA    1 
ATOM   4150 C  C     . LEU   A 1 662  ? 8.840   8.894   -82.954 1.00 46.24  ? 811  LEU   A C     1 
ATOM   4151 O  O     . LEU   A 1 662  ? 9.569   8.557   -83.897 1.00 57.85  ? 811  LEU   A O     1 
ATOM   4152 C  CB    . LEU   A 1 662  ? 10.342  8.408   -80.936 1.00 46.45  ? 811  LEU   A CB    1 
ATOM   4153 C  CG    . LEU   A 1 662  ? 11.103  9.000   -79.755 1.00 46.35  ? 811  LEU   A CG    1 
ATOM   4154 C  CD1   . LEU   A 1 662  ? 11.838  7.929   -78.972 1.00 50.60  ? 811  LEU   A CD1   1 
ATOM   4155 C  CD2   . LEU   A 1 662  ? 12.063  10.078  -80.235 1.00 47.20  ? 811  LEU   A CD2   1 
ATOM   4156 N  N     . GLY   A 1 663  ? 7.506   8.876   -82.980 1.00 49.41  ? 812  GLY   A N     1 
ATOM   4157 C  CA    . GLY   A 1 663  ? 6.695   8.534   -84.161 1.00 48.06  ? 812  GLY   A CA    1 
ATOM   4158 C  C     . GLY   A 1 663  ? 5.876   7.278   -83.932 1.00 46.05  ? 812  GLY   A C     1 
ATOM   4159 O  O     . GLY   A 1 663  ? 5.456   7.032   -82.770 1.00 41.36  ? 812  GLY   A O     1 
ATOM   4160 N  N     . GLY   A 1 664  ? 5.637   6.524   -85.011 1.00 46.50  ? 813  GLY   A N     1 
ATOM   4161 C  CA    . GLY   A 1 664  ? 4.873   5.262   -84.990 1.00 41.10  ? 813  GLY   A CA    1 
ATOM   4162 C  C     . GLY   A 1 664  ? 5.640   4.192   -84.247 1.00 38.36  ? 813  GLY   A C     1 
ATOM   4163 O  O     . GLY   A 1 664  ? 6.863   4.189   -84.323 1.00 38.90  ? 813  GLY   A O     1 
ATOM   4164 N  N     . ILE   A 1 665  ? 4.941   3.296   -83.569 1.00 36.74  ? 814  ILE   A N     1 
ATOM   4165 C  CA    . ILE   A 1 665  ? 5.571   2.196   -82.785 1.00 41.28  ? 814  ILE   A CA    1 
ATOM   4166 C  C     . ILE   A 1 665  ? 6.299   1.242   -83.732 1.00 39.86  ? 814  ILE   A C     1 
ATOM   4167 O  O     . ILE   A 1 665  ? 7.495   0.971   -83.521 1.00 40.44  ? 814  ILE   A O     1 
ATOM   4168 C  CB    . ILE   A 1 665  ? 4.492   1.491   -81.947 1.00 41.57  ? 814  ILE   A CB    1 
ATOM   4169 C  CG1   . ILE   A 1 665  ? 4.010   2.410   -80.823 1.00 42.31  ? 814  ILE   A CG1   1 
ATOM   4170 C  CG2   . ILE   A 1 665  ? 4.999   0.152   -81.445 1.00 39.69  ? 814  ILE   A CG2   1 
ATOM   4171 C  CD1   . ILE   A 1 665  ? 2.658   2.029   -80.248 1.00 44.74  ? 814  ILE   A CD1   1 
ATOM   4172 N  N     . GLY   A 1 666  ? 5.595   0.737   -84.742 1.00 40.98  ? 815  GLY   A N     1 
ATOM   4173 C  CA    . GLY   A 1 666  ? 6.182   -0.187  -85.727 1.00 38.83  ? 815  GLY   A CA    1 
ATOM   4174 C  C     . GLY   A 1 666  ? 7.251   0.512   -86.534 1.00 38.63  ? 815  GLY   A C     1 
ATOM   4175 O  O     . GLY   A 1 666  ? 8.319   -0.096  -86.771 1.00 37.60  ? 815  GLY   A O     1 
ATOM   4176 N  N     . GLN   A 1 667  ? 7.019   1.769   -86.900 1.00 41.58  ? 816  GLN   A N     1 
ATOM   4177 C  CA    . GLN   A 1 667  ? 8.005   2.524   -87.721 1.00 46.69  ? 816  GLN   A CA    1 
ATOM   4178 C  C     . GLN   A 1 667  ? 9.302   2.743   -86.923 1.00 43.12  ? 816  GLN   A C     1 
ATOM   4179 O  O     . GLN   A 1 667  ? 10.397  2.579   -87.477 1.00 40.01  ? 816  GLN   A O     1 
ATOM   4180 C  CB    . GLN   A 1 667  ? 7.405   3.831   -88.217 1.00 52.46  ? 816  GLN   A CB    1 
ATOM   4181 C  CG    . GLN   A 1 667  ? 8.342   4.549   -89.172 1.00 72.03  ? 816  GLN   A CG    1 
ATOM   4182 C  CD    . GLN   A 1 667  ? 7.685   5.650   -89.971 1.00 90.45  ? 816  GLN   A CD    1 
ATOM   4183 O  OE1   . GLN   A 1 667  ? 6.460   5.733   -90.083 1.00 97.84  ? 816  GLN   A OE1   1 
ATOM   4184 N  NE2   . GLN   A 1 667  ? 8.516   6.502   -90.555 1.00 95.98  ? 816  GLN   A NE2   1 
ATOM   4185 N  N     . PHE   A 1 668  ? 9.216   3.083   -85.646 1.00 45.19  ? 817  PHE   A N     1 
ATOM   4186 C  CA    . PHE   A 1 668  ? 10.433  3.319   -84.830 1.00 44.48  ? 817  PHE   A CA    1 
ATOM   4187 C  C     . PHE   A 1 668  ? 11.172  1.985   -84.616 1.00 42.37  ? 817  PHE   A C     1 
ATOM   4188 O  O     . PHE   A 1 668  ? 12.399  1.966   -84.811 1.00 40.20  ? 817  PHE   A O     1 
ATOM   4189 C  CB    . PHE   A 1 668  ? 10.090  4.011   -83.511 1.00 47.67  ? 817  PHE   A CB    1 
ATOM   4190 C  CG    . PHE   A 1 668  ? 11.319  4.419   -82.750 1.00 47.43  ? 817  PHE   A CG    1 
ATOM   4191 C  CD1   . PHE   A 1 668  ? 11.941  5.625   -83.023 1.00 47.87  ? 817  PHE   A CD1   1 
ATOM   4192 C  CD2   . PHE   A 1 668  ? 11.882  3.572   -81.818 1.00 41.74  ? 817  PHE   A CD2   1 
ATOM   4193 C  CE1   . PHE   A 1 668  ? 13.083  5.995   -82.336 1.00 50.47  ? 817  PHE   A CE1   1 
ATOM   4194 C  CE2   . PHE   A 1 668  ? 13.023  3.949   -81.128 1.00 45.69  ? 817  PHE   A CE2   1 
ATOM   4195 C  CZ    . PHE   A 1 668  ? 13.618  5.158   -81.386 1.00 46.00  ? 817  PHE   A CZ    1 
ATOM   4196 N  N     . LEU   A 1 669  ? 10.461  0.900   -84.275 1.00 36.59  ? 818  LEU   A N     1 
ATOM   4197 C  CA    . LEU   A 1 669  ? 11.105  -0.409  -83.968 1.00 36.90  ? 818  LEU   A CA    1 
ATOM   4198 C  C     . LEU   A 1 669  ? 11.702  -1.032  -85.234 1.00 35.76  ? 818  LEU   A C     1 
ATOM   4199 O  O     . LEU   A 1 669  ? 12.692  -1.780  -85.083 1.00 40.09  ? 818  LEU   A O     1 
ATOM   4200 C  CB    . LEU   A 1 669  ? 10.130  -1.328  -83.224 1.00 36.06  ? 818  LEU   A CB    1 
ATOM   4201 C  CG    . LEU   A 1 669  ? 9.779   -0.806  -81.824 1.00 39.53  ? 818  LEU   A CG    1 
ATOM   4202 C  CD1   . LEU   A 1 669  ? 8.736   -1.665  -81.131 1.00 43.01  ? 818  LEU   A CD1   1 
ATOM   4203 C  CD2   . LEU   A 1 669  ? 11.019  -0.712  -80.954 1.00 37.81  ? 818  LEU   A CD2   1 
ATOM   4204 N  N     . ALA   A 1 670  ? 11.235  -0.655  -86.427 1.00 35.81  ? 819  ALA   A N     1 
ATOM   4205 C  CA    . ALA   A 1 670  ? 11.826  -1.084  -87.721 1.00 39.60  ? 819  ALA   A CA    1 
ATOM   4206 C  C     . ALA   A 1 670  ? 13.250  -0.533  -87.877 1.00 42.60  ? 819  ALA   A C     1 
ATOM   4207 O  O     . ALA   A 1 670  ? 14.052  -1.114  -88.637 1.00 43.31  ? 819  ALA   A O     1 
ATOM   4208 C  CB    . ALA   A 1 670  ? 10.961  -0.635  -88.870 1.00 43.18  ? 819  ALA   A CB    1 
ATOM   4209 N  N     . LYS   A 1 671  ? 13.581  0.554   -87.190 1.00 45.12  ? 820  LYS   A N     1 
ATOM   4210 C  CA    . LYS   A 1 671  ? 14.939  1.145   -87.292 1.00 43.24  ? 820  LYS   A CA    1 
ATOM   4211 C  C     . LYS   A 1 671  ? 15.880  0.521   -86.261 1.00 38.44  ? 820  LYS   A C     1 
ATOM   4212 O  O     . LYS   A 1 671  ? 17.048  0.874   -86.288 1.00 43.37  ? 820  LYS   A O     1 
ATOM   4213 C  CB    . LYS   A 1 671  ? 14.869  2.662   -87.125 1.00 45.33  ? 820  LYS   A CB    1 
ATOM   4214 C  CG    . LYS   A 1 671  ? 13.962  3.352   -88.126 1.00 50.02  ? 820  LYS   A CG    1 
ATOM   4215 C  CD    . LYS   A 1 671  ? 13.943  4.850   -88.012 1.00 57.69  ? 820  LYS   A CD    1 
ATOM   4216 C  CE    . LYS   A 1 671  ? 14.351  5.358   -86.646 1.00 61.41  ? 820  LYS   A CE    1 
ATOM   4217 N  NZ    . LYS   A 1 671  ? 14.173  6.821   -86.555 1.00 69.34  ? 820  LYS   A NZ    1 
ATOM   4218 N  N     . ALA   A 1 672  ? 15.406  -0.343  -85.363 1.00 40.62  ? 821  ALA   A N     1 
ATOM   4219 C  CA    . ALA   A 1 672  ? 16.271  -1.035  -84.369 1.00 40.37  ? 821  ALA   A CA    1 
ATOM   4220 C  C     . ALA   A 1 672  ? 17.365  -1.851  -85.077 1.00 45.94  ? 821  ALA   A C     1 
ATOM   4221 O  O     . ALA   A 1 672  ? 17.167  -2.248  -86.244 1.00 50.35  ? 821  ALA   A O     1 
ATOM   4222 C  CB    . ALA   A 1 672  ? 15.452  -1.913  -83.472 1.00 40.79  ? 821  ALA   A CB    1 
ATOM   4223 N  N     . ILE   A 1 673  ? 18.495  -2.064  -84.395 1.00 46.30  ? 822  ILE   A N     1 
ATOM   4224 C  CA    . ILE   A 1 673  ? 19.687  -2.764  -84.941 1.00 47.43  ? 822  ILE   A CA    1 
ATOM   4225 C  C     . ILE   A 1 673  ? 19.255  -4.170  -85.378 1.00 51.21  ? 822  ILE   A C     1 
ATOM   4226 O  O     . ILE   A 1 673  ? 19.799  -4.658  -86.382 1.00 46.83  ? 822  ILE   A O     1 
ATOM   4227 C  CB    . ILE   A 1 673  ? 20.850  -2.783  -83.924 1.00 54.23  ? 822  ILE   A CB    1 
ATOM   4228 C  CG1   . ILE   A 1 673  ? 22.118  -3.369  -84.541 1.00 54.24  ? 822  ILE   A CG1   1 
ATOM   4229 C  CG2   . ILE   A 1 673  ? 20.494  -3.539  -82.651 1.00 59.38  ? 822  ILE   A CG2   1 
ATOM   4230 C  CD1   . ILE   A 1 673  ? 23.353  -3.157  -83.699 1.00 59.24  ? 822  ILE   A CD1   1 
ATOM   4231 N  N     . GLU   A 1 674  ? 18.367  -4.806  -84.603 1.00 49.94  ? 823  GLU   A N     1 
ATOM   4232 C  CA    . GLU   A 1 674  ? 17.706  -6.093  -84.930 1.00 45.57  ? 823  GLU   A CA    1 
ATOM   4233 C  C     . GLU   A 1 674  ? 16.248  -5.952  -84.530 1.00 42.71  ? 823  GLU   A C     1 
ATOM   4234 O  O     . GLU   A 1 674  ? 15.905  -6.082  -83.361 1.00 45.20  ? 823  GLU   A O     1 
ATOM   4235 C  CB    . GLU   A 1 674  ? 18.364  -7.278  -84.224 1.00 50.00  ? 823  GLU   A CB    1 
ATOM   4236 C  CG    . GLU   A 1 674  ? 19.646  -7.732  -84.904 1.00 50.72  ? 823  GLU   A CG    1 
ATOM   4237 C  CD    . GLU   A 1 674  ? 20.290  -8.993  -84.345 1.00 53.51  ? 823  GLU   A CD    1 
ATOM   4238 O  OE1   . GLU   A 1 674  ? 20.196  -9.249  -83.122 1.00 54.19  ? 823  GLU   A OE1   1 
ATOM   4239 O  OE2   . GLU   A 1 674  ? 20.891  -9.721  -85.142 1.00 62.28  ? 823  GLU   A OE2   1 
ATOM   4240 N  N     . PRO   A 1 675  ? 15.360  -5.614  -85.485 1.00 41.72  ? 824  PRO   A N     1 
ATOM   4241 C  CA    . PRO   A 1 675  ? 13.980  -5.284  -85.141 1.00 36.56  ? 824  PRO   A CA    1 
ATOM   4242 C  C     . PRO   A 1 675  ? 13.261  -6.463  -84.513 1.00 36.62  ? 824  PRO   A C     1 
ATOM   4243 O  O     . PRO   A 1 675  ? 13.539  -7.603  -84.865 1.00 37.53  ? 824  PRO   A O     1 
ATOM   4244 C  CB    . PRO   A 1 675  ? 13.344  -4.892  -86.482 1.00 36.80  ? 824  PRO   A CB    1 
ATOM   4245 C  CG    . PRO   A 1 675  ? 14.536  -4.514  -87.362 1.00 38.01  ? 824  PRO   A CG    1 
ATOM   4246 C  CD    . PRO   A 1 675  ? 15.652  -5.438  -86.926 1.00 37.31  ? 824  PRO   A CD    1 
ATOM   4247 N  N     . PRO   A 1 676  ? 12.290  -6.211  -83.602 1.00 35.83  ? 825  PRO   A N     1 
ATOM   4248 C  CA    . PRO   A 1 676  ? 11.510  -7.279  -82.997 1.00 36.96  ? 825  PRO   A CA    1 
ATOM   4249 C  C     . PRO   A 1 676  ? 10.546  -7.868  -84.022 1.00 42.21  ? 825  PRO   A C     1 
ATOM   4250 O  O     . PRO   A 1 676  ? 10.294  -7.271  -85.083 1.00 38.28  ? 825  PRO   A O     1 
ATOM   4251 C  CB    . PRO   A 1 676  ? 10.755  -6.556  -81.887 1.00 38.05  ? 825  PRO   A CB    1 
ATOM   4252 C  CG    . PRO   A 1 676  ? 10.541  -5.176  -82.444 1.00 35.54  ? 825  PRO   A CG    1 
ATOM   4253 C  CD    . PRO   A 1 676  ? 11.809  -4.883  -83.212 1.00 33.80  ? 825  PRO   A CD    1 
ATOM   4254 N  N     . PRO   A 1 677  ? 10.017  -9.078  -83.743 1.00 42.70  ? 826  PRO   A N     1 
ATOM   4255 C  CA    . PRO   A 1 677  ? 9.115   -9.756  -84.664 1.00 41.74  ? 826  PRO   A CA    1 
ATOM   4256 C  C     . PRO   A 1 677  ? 7.782   -9.016  -84.726 1.00 41.62  ? 826  PRO   A C     1 
ATOM   4257 O  O     . PRO   A 1 677  ? 7.369   -8.437  -83.729 1.00 38.72  ? 826  PRO   A O     1 
ATOM   4258 C  CB    . PRO   A 1 677  ? 8.936   -11.162 -84.076 1.00 42.29  ? 826  PRO   A CB    1 
ATOM   4259 C  CG    . PRO   A 1 677  ? 9.263   -10.996 -82.607 1.00 45.73  ? 826  PRO   A CG    1 
ATOM   4260 C  CD    . PRO   A 1 677  ? 10.295  -9.886  -82.548 1.00 47.09  ? 826  PRO   A CD    1 
ATOM   4261 N  N     . LEU   A 1 678  ? 7.135   -9.101  -85.886 1.00 42.37  ? 827  LEU   A N     1 
ATOM   4262 C  CA    . LEU   A 1 678  ? 5.848   -8.419  -86.183 1.00 42.63  ? 827  LEU   A CA    1 
ATOM   4263 C  C     . LEU   A 1 678  ? 4.803   -8.730  -85.100 1.00 37.06  ? 827  LEU   A C     1 
ATOM   4264 O  O     . LEU   A 1 678  ? 4.141   -7.809  -84.677 1.00 36.76  ? 827  LEU   A O     1 
ATOM   4265 C  CB    . LEU   A 1 678  ? 5.392   -8.873  -87.570 1.00 40.56  ? 827  LEU   A CB    1 
ATOM   4266 C  CG    . LEU   A 1 678  ? 4.033   -8.365  -88.029 1.00 42.00  ? 827  LEU   A CG    1 
ATOM   4267 C  CD1   . LEU   A 1 678  ? 3.996   -6.843  -88.070 1.00 39.55  ? 827  LEU   A CD1   1 
ATOM   4268 C  CD2   . LEU   A 1 678  ? 3.719   -8.961  -89.395 1.00 44.26  ? 827  LEU   A CD2   1 
ATOM   4269 N  N     . ASP   A 1 679  ? 4.660   -9.978  -84.660 1.00 39.88  ? 828  ASP   A N     1 
ATOM   4270 C  CA    . ASP   A 1 679  ? 3.562   -10.371 -83.729 1.00 47.18  ? 828  ASP   A CA    1 
ATOM   4271 C  C     . ASP   A 1 679  ? 3.702   -9.604  -82.397 1.00 42.82  ? 828  ASP   A C     1 
ATOM   4272 O  O     . ASP   A 1 679  ? 2.654   -9.227  -81.838 1.00 41.65  ? 828  ASP   A O     1 
ATOM   4273 C  CB    . ASP   A 1 679  ? 3.445   -11.898 -83.570 1.00 49.93  ? 828  ASP   A CB    1 
ATOM   4274 C  CG    . ASP   A 1 679  ? 4.622   -12.595 -82.907 1.00 60.56  ? 828  ASP   A CG    1 
ATOM   4275 O  OD1   . ASP   A 1 679  ? 5.493   -11.904 -82.343 1.00 68.90  ? 828  ASP   A OD1   1 
ATOM   4276 O  OD2   . ASP   A 1 679  ? 4.662   -13.845 -82.960 1.00 75.40  ? 828  ASP   A OD2   1 
ATOM   4277 N  N     . ALA   A 1 680  ? 4.932   -9.350  -81.927 1.00 37.05  ? 829  ALA   A N     1 
ATOM   4278 C  CA    . ALA   A 1 680  ? 5.205   -8.642  -80.655 1.00 37.72  ? 829  ALA   A CA    1 
ATOM   4279 C  C     . ALA   A 1 680  ? 4.713   -7.200  -80.771 1.00 35.28  ? 829  ALA   A C     1 
ATOM   4280 O  O     . ALA   A 1 680  ? 3.974   -6.761  -79.892 1.00 37.71  ? 829  ALA   A O     1 
ATOM   4281 C  CB    . ALA   A 1 680  ? 6.668   -8.711  -80.310 1.00 43.12  ? 829  ALA   A CB    1 
ATOM   4282 N  N     . VAL   A 1 681  ? 5.042   -6.513  -81.860 1.00 34.50  ? 830  VAL   A N     1 
ATOM   4283 C  CA    . VAL   A 1 681  ? 4.544   -5.135  -82.128 1.00 36.15  ? 830  VAL   A CA    1 
ATOM   4284 C  C     . VAL   A 1 681  ? 3.010   -5.133  -82.143 1.00 39.22  ? 830  VAL   A C     1 
ATOM   4285 O  O     . VAL   A 1 681  ? 2.390   -4.213  -81.556 1.00 38.89  ? 830  VAL   A O     1 
ATOM   4286 C  CB    . VAL   A 1 681  ? 5.110   -4.580  -83.442 1.00 33.05  ? 830  VAL   A CB    1 
ATOM   4287 C  CG1   . VAL   A 1 681  ? 4.609   -3.169  -83.708 1.00 34.26  ? 830  VAL   A CG1   1 
ATOM   4288 C  CG2   . VAL   A 1 681  ? 6.617   -4.616  -83.437 1.00 33.09  ? 830  VAL   A CG2   1 
ATOM   4289 N  N     . ILE   A 1 682  ? 2.417   -6.091  -82.845 1.00 40.97  ? 831  ILE   A N     1 
ATOM   4290 C  CA    . ILE   A 1 682  ? 0.936   -6.190  -82.999 1.00 39.71  ? 831  ILE   A CA    1 
ATOM   4291 C  C     . ILE   A 1 682  ? 0.326   -6.416  -81.620 1.00 35.89  ? 831  ILE   A C     1 
ATOM   4292 O  O     . ILE   A 1 682  ? -0.709  -5.830  -81.354 1.00 36.73  ? 831  ILE   A O     1 
ATOM   4293 C  CB    . ILE   A 1 682  ? 0.553   -7.325  -83.976 1.00 37.98  ? 831  ILE   A CB    1 
ATOM   4294 C  CG1   . ILE   A 1 682  ? 0.971   -6.984  -85.410 1.00 36.65  ? 831  ILE   A CG1   1 
ATOM   4295 C  CG2   . ILE   A 1 682  ? -0.929  -7.662  -83.863 1.00 38.84  ? 831  ILE   A CG2   1 
ATOM   4296 C  CD1   . ILE   A 1 682  ? 0.384   -5.721  -85.960 1.00 36.78  ? 831  ILE   A CD1   1 
ATOM   4297 N  N     . GLU   A 1 683  ? 0.938   -7.262  -80.795 1.00 37.11  ? 832  GLU   A N     1 
ATOM   4298 C  CA    . GLU   A 1 683  ? 0.416   -7.577  -79.442 1.00 41.95  ? 832  GLU   A CA    1 
ATOM   4299 C  C     . GLU   A 1 683  ? 0.534   -6.331  -78.533 1.00 41.19  ? 832  GLU   A C     1 
ATOM   4300 O  O     . GLU   A 1 683  ? -0.383  -6.106  -77.748 1.00 39.75  ? 832  GLU   A O     1 
ATOM   4301 C  CB    . GLU   A 1 683  ? 1.143   -8.810  -78.920 1.00 52.70  ? 832  GLU   A CB    1 
ATOM   4302 C  CG    . GLU   A 1 683  ? 0.593   -9.313  -77.603 1.00 65.82  ? 832  GLU   A CG    1 
ATOM   4303 C  CD    . GLU   A 1 683  ? -0.756  -9.994  -77.722 1.00 76.06  ? 832  GLU   A CD    1 
ATOM   4304 O  OE1   . GLU   A 1 683  ? -1.669  -9.623  -76.943 1.00 89.58  ? 832  GLU   A OE1   1 
ATOM   4305 O  OE2   . GLU   A 1 683  ? -0.890  -10.897 -78.591 1.00 84.61  ? 832  GLU   A OE2   1 
ATOM   4306 N  N     . ALA   A 1 684  ? 1.601   -5.531  -78.635 1.00 38.33  ? 833  ALA   A N     1 
ATOM   4307 C  CA    . ALA   A 1 684  ? 1.796   -4.314  -77.808 1.00 41.17  ? 833  ALA   A CA    1 
ATOM   4308 C  C     . ALA   A 1 684  ? 0.711   -3.297  -78.155 1.00 43.23  ? 833  ALA   A C     1 
ATOM   4309 O  O     . ALA   A 1 684  ? 0.052   -2.780  -77.238 1.00 44.78  ? 833  ALA   A O     1 
ATOM   4310 C  CB    . ALA   A 1 684  ? 3.167   -3.709  -78.014 1.00 38.81  ? 833  ALA   A CB    1 
ATOM   4311 N  N     . GLU   A 1 685  ? 0.534   -3.016  -79.441 1.00 45.20  ? 834  GLU   A N     1 
ATOM   4312 C  CA    . GLU   A 1 685  ? -0.479  -2.039  -79.903 1.00 44.01  ? 834  GLU   A CA    1 
ATOM   4313 C  C     . GLU   A 1 685  ? -1.845  -2.503  -79.412 1.00 40.34  ? 834  GLU   A C     1 
ATOM   4314 O  O     . GLU   A 1 685  ? -2.590  -1.656  -78.929 1.00 44.81  ? 834  GLU   A O     1 
ATOM   4315 C  CB    . GLU   A 1 685  ? -0.462  -1.894  -81.421 1.00 47.39  ? 834  GLU   A CB    1 
ATOM   4316 C  CG    . GLU   A 1 685  ? 0.838   -1.318  -81.968 1.00 52.82  ? 834  GLU   A CG    1 
ATOM   4317 C  CD    . GLU   A 1 685  ? 0.989   -1.384  -83.486 1.00 58.92  ? 834  GLU   A CD    1 
ATOM   4318 O  OE1   . GLU   A 1 685  ? 0.548   -2.406  -84.094 1.00 57.55  ? 834  GLU   A OE1   1 
ATOM   4319 O  OE2   . GLU   A 1 685  ? 1.530   -0.405  -84.065 1.00 57.21  ? 834  GLU   A OE2   1 
ATOM   4320 N  N     . HIS   A 1 686  ? -2.161  -3.791  -79.538 1.00 41.45  ? 835  HIS   A N     1 
ATOM   4321 C  CA    . HIS   A 1 686  ? -3.471  -4.369  -79.125 1.00 46.02  ? 835  HIS   A CA    1 
ATOM   4322 C  C     . HIS   A 1 686  ? -3.677  -4.150  -77.609 1.00 46.78  ? 835  HIS   A C     1 
ATOM   4323 O  O     . HIS   A 1 686  ? -4.754  -3.656  -77.212 1.00 45.81  ? 835  HIS   A O     1 
ATOM   4324 C  CB    . HIS   A 1 686  ? -3.567  -5.840  -79.557 1.00 51.69  ? 835  HIS   A CB    1 
ATOM   4325 C  CG    . HIS   A 1 686  ? -4.735  -6.570  -78.981 1.00 66.02  ? 835  HIS   A CG    1 
ATOM   4326 N  ND1   . HIS   A 1 686  ? -6.037  -6.343  -79.404 1.00 68.70  ? 835  HIS   A ND1   1 
ATOM   4327 C  CD2   . HIS   A 1 686  ? -4.805  -7.525  -78.023 1.00 70.18  ? 835  HIS   A CD2   1 
ATOM   4328 C  CE1   . HIS   A 1 686  ? -6.853  -7.126  -78.726 1.00 71.99  ? 835  HIS   A CE1   1 
ATOM   4329 N  NE2   . HIS   A 1 686  ? -6.123  -7.863  -77.869 1.00 67.89  ? 835  HIS   A NE2   1 
ATOM   4330 N  N     . THR   A 1 687  ? -2.673  -4.484  -76.798 1.00 39.58  ? 836  THR   A N     1 
ATOM   4331 C  CA    . THR   A 1 687  ? -2.651  -4.281  -75.330 1.00 43.35  ? 836  THR   A CA    1 
ATOM   4332 C  C     . THR   A 1 687  ? -2.908  -2.812  -74.991 1.00 40.98  ? 836  THR   A C     1 
ATOM   4333 O  O     . THR   A 1 687  ? -3.768  -2.558  -74.148 1.00 41.08  ? 836  THR   A O     1 
ATOM   4334 C  CB    . THR   A 1 687  ? -1.329  -4.783  -74.742 1.00 45.36  ? 836  THR   A CB    1 
ATOM   4335 O  OG1   . THR   A 1 687  ? -1.430  -6.203  -74.808 1.00 58.47  ? 836  THR   A OG1   1 
ATOM   4336 C  CG2   . THR   A 1 687  ? -1.066  -4.321  -73.331 1.00 45.72  ? 836  THR   A CG2   1 
ATOM   4337 N  N     . LEU   A 1 688  ? -2.192  -1.868  -75.596 1.00 39.08  ? 837  LEU   A N     1 
ATOM   4338 C  CA    . LEU   A 1 688  ? -2.357  -0.443  -75.218 1.00 40.43  ? 837  LEU   A CA    1 
ATOM   4339 C  C     . LEU   A 1 688  ? -3.712  0.085   -75.707 1.00 43.54  ? 837  LEU   A C     1 
ATOM   4340 O  O     . LEU   A 1 688  ? -4.181  1.084   -75.133 1.00 46.26  ? 837  LEU   A O     1 
ATOM   4341 C  CB    . LEU   A 1 688  ? -1.195  0.375   -75.775 1.00 39.43  ? 837  LEU   A CB    1 
ATOM   4342 C  CG    . LEU   A 1 688  ? 0.185   -0.030  -75.268 1.00 40.98  ? 837  LEU   A CG    1 
ATOM   4343 C  CD1   . LEU   A 1 688  ? 1.261   0.864   -75.867 1.00 41.51  ? 837  LEU   A CD1   1 
ATOM   4344 C  CD2   . LEU   A 1 688  ? 0.235   -0.012  -73.751 1.00 40.69  ? 837  LEU   A CD2   1 
ATOM   4345 N  N     . ARG   A 1 689  ? -4.321  -0.547  -76.717 1.00 47.90  ? 838  ARG   A N     1 
ATOM   4346 C  CA    . ARG   A 1 689  ? -5.659  -0.149  -77.254 1.00 49.44  ? 838  ARG   A CA    1 
ATOM   4347 C  C     . ARG   A 1 689  ? -6.762  -0.697  -76.346 1.00 44.90  ? 838  ARG   A C     1 
ATOM   4348 O  O     . ARG   A 1 689  ? -7.666  0.058   -76.054 1.00 44.08  ? 838  ARG   A O     1 
ATOM   4349 C  CB    . ARG   A 1 689  ? -5.865  -0.591  -78.709 1.00 50.79  ? 838  ARG   A CB    1 
ATOM   4350 C  CG    . ARG   A 1 689  ? -5.260  0.363   -79.737 1.00 54.62  ? 838  ARG   A CG    1 
ATOM   4351 C  CD    . ARG   A 1 689  ? -5.783  0.140   -81.152 1.00 58.49  ? 838  ARG   A CD    1 
ATOM   4352 N  NE    . ARG   A 1 689  ? -5.529  -1.240  -81.538 1.00 64.08  ? 838  ARG   A NE    1 
ATOM   4353 C  CZ    . ARG   A 1 689  ? -4.508  -1.664  -82.284 1.00 61.84  ? 838  ARG   A CZ    1 
ATOM   4354 N  NH1   . ARG   A 1 689  ? -4.386  -2.965  -82.507 1.00 56.64  ? 838  ARG   A NH1   1 
ATOM   4355 N  NH2   . ARG   A 1 689  ? -3.633  -0.803  -82.798 1.00 59.36  ? 838  ARG   A NH2   1 
ATOM   4356 N  N     . GLU   A 1 690  ? -6.685  -1.948  -75.897 1.00 45.53  ? 839  GLU   A N     1 
ATOM   4357 C  CA    . GLU   A 1 690  ? -7.635  -2.487  -74.884 1.00 50.23  ? 839  GLU   A CA    1 
ATOM   4358 C  C     . GLU   A 1 690  ? -7.641  -1.576  -73.642 1.00 48.06  ? 839  GLU   A C     1 
ATOM   4359 O  O     . GLU   A 1 690  ? -8.694  -1.365  -73.088 1.00 47.30  ? 839  GLU   A O     1 
ATOM   4360 C  CB    . GLU   A 1 690  ? -7.271  -3.916  -74.485 1.00 55.31  ? 839  GLU   A CB    1 
ATOM   4361 C  CG    . GLU   A 1 690  ? -7.526  -4.948  -75.569 1.00 72.69  ? 839  GLU   A CG    1 
ATOM   4362 C  CD    . GLU   A 1 690  ? -8.972  -5.397  -75.747 1.00 88.78  ? 839  GLU   A CD    1 
ATOM   4363 O  OE1   . GLU   A 1 690  ? -9.616  -5.765  -74.727 1.00 97.09  ? 839  GLU   A OE1   1 
ATOM   4364 O  OE2   . GLU   A 1 690  ? -9.451  -5.389  -76.910 1.00 85.59  ? 839  GLU   A OE2   1 
ATOM   4365 N  N     . LEU   A 1 691  ? -6.490  -1.050  -73.222 1.00 46.27  ? 840  LEU   A N     1 
ATOM   4366 C  CA    . LEU   A 1 691  ? -6.354  -0.264  -71.973 1.00 44.93  ? 840  LEU   A CA    1 
ATOM   4367 C  C     . LEU   A 1 691  ? -6.878  1.151   -72.175 1.00 43.45  ? 840  LEU   A C     1 
ATOM   4368 O  O     . LEU   A 1 691  ? -7.054  1.830   -71.148 1.00 40.53  ? 840  LEU   A O     1 
ATOM   4369 C  CB    . LEU   A 1 691  ? -4.877  -0.209  -71.571 1.00 45.66  ? 840  LEU   A CB    1 
ATOM   4370 C  CG    . LEU   A 1 691  ? -4.354  -1.452  -70.882 1.00 48.17  ? 840  LEU   A CG    1 
ATOM   4371 C  CD1   . LEU   A 1 691  ? -2.861  -1.296  -70.628 1.00 52.44  ? 840  LEU   A CD1   1 
ATOM   4372 C  CD2   . LEU   A 1 691  ? -5.136  -1.715  -69.591 1.00 48.75  ? 840  LEU   A CD2   1 
ATOM   4373 N  N     . ASP   A 1 692  ? -7.017  1.585   -73.436 1.00 46.71  ? 841  ASP   A N     1 
ATOM   4374 C  CA    . ASP   A 1 692  ? -7.403  2.961   -73.842 1.00 46.77  ? 841  ASP   A CA    1 
ATOM   4375 C  C     . ASP   A 1 692  ? -6.220  3.887   -73.570 1.00 49.03  ? 841  ASP   A C     1 
ATOM   4376 O  O     . ASP   A 1 692  ? -6.448  5.089   -73.302 1.00 48.66  ? 841  ASP   A O     1 
ATOM   4377 C  CB    . ASP   A 1 692  ? -8.683  3.417   -73.129 1.00 58.62  ? 841  ASP   A CB    1 
ATOM   4378 C  CG    . ASP   A 1 692  ? -9.937  3.279   -73.980 1.00 68.72  ? 841  ASP   A CG    1 
ATOM   4379 O  OD1   . ASP   A 1 692  ? -9.918  3.750   -75.151 1.00 69.38  ? 841  ASP   A OD1   1 
ATOM   4380 O  OD2   . ASP   A 1 692  ? -10.927 2.713   -73.469 1.00 76.81  ? 841  ASP   A OD2   1 
ATOM   4381 N  N     . ALA   A 1 693  ? -4.998  3.345   -73.637 1.00 45.44  ? 842  ALA   A N     1 
ATOM   4382 C  CA    . ALA   A 1 693  ? -3.754  4.142   -73.636 1.00 43.91  ? 842  ALA   A CA    1 
ATOM   4383 C  C     . ALA   A 1 693  ? -3.519  4.711   -75.042 1.00 44.05  ? 842  ALA   A C     1 
ATOM   4384 O  O     . ALA   A 1 693  ? -2.913  5.790   -75.147 1.00 44.65  ? 842  ALA   A O     1 
ATOM   4385 C  CB    . ALA   A 1 693  ? -2.603  3.302   -73.147 1.00 46.34  ? 842  ALA   A CB    1 
ATOM   4386 N  N     . LEU   A 1 694  ? -3.969  4.018   -76.093 1.00 46.93  ? 843  LEU   A N     1 
ATOM   4387 C  CA    . LEU   A 1 694  ? -3.978  4.567   -77.479 1.00 51.48  ? 843  LEU   A CA    1 
ATOM   4388 C  C     . LEU   A 1 694  ? -5.428  4.660   -77.973 1.00 53.94  ? 843  LEU   A C     1 
ATOM   4389 O  O     . LEU   A 1 694  ? -6.215  3.728   -77.699 1.00 55.27  ? 843  LEU   A O     1 
ATOM   4390 C  CB    . LEU   A 1 694  ? -3.147  3.681   -78.412 1.00 50.83  ? 843  LEU   A CB    1 
ATOM   4391 C  CG    . LEU   A 1 694  ? -1.740  3.337   -77.936 1.00 55.90  ? 843  LEU   A CG    1 
ATOM   4392 C  CD1   . LEU   A 1 694  ? -1.056  2.422   -78.936 1.00 63.61  ? 843  LEU   A CD1   1 
ATOM   4393 C  CD2   . LEU   A 1 694  ? -0.908  4.588   -77.704 1.00 54.93  ? 843  LEU   A CD2   1 
ATOM   4394 N  N     . ASP   A 1 695  ? -5.760  5.737   -78.686 1.00 59.61  ? 844  ASP   A N     1 
ATOM   4395 C  CA    . ASP   A 1 695  ? -7.095  5.956   -79.303 1.00 66.86  ? 844  ASP   A CA    1 
ATOM   4396 C  C     . ASP   A 1 695  ? -7.172  5.138   -80.605 1.00 73.10  ? 844  ASP   A C     1 
ATOM   4397 O  O     . ASP   A 1 695  ? -6.363  4.200   -80.770 1.00 74.74  ? 844  ASP   A O     1 
ATOM   4398 C  CB    . ASP   A 1 695  ? -7.355  7.455   -79.482 1.00 67.52  ? 844  ASP   A CB    1 
ATOM   4399 C  CG    . ASP   A 1 695  ? -6.380  8.140   -80.427 1.00 70.39  ? 844  ASP   A CG    1 
ATOM   4400 O  OD1   . ASP   A 1 695  ? -5.827  7.439   -81.313 1.00 65.65  ? 844  ASP   A OD1   1 
ATOM   4401 O  OD2   . ASP   A 1 695  ? -6.163  9.361   -80.252 1.00 67.12  ? 844  ASP   A OD2   1 
ATOM   4402 N  N     . ALA   A 1 696  ? -8.134  5.449   -81.480 1.00 82.94  ? 845  ALA   A N     1 
ATOM   4403 C  CA    . ALA   A 1 696  ? -8.314  4.802   -82.803 1.00 88.31  ? 845  ALA   A CA    1 
ATOM   4404 C  C     . ALA   A 1 696  ? -7.098  5.087   -83.698 1.00 83.19  ? 845  ALA   A C     1 
ATOM   4405 O  O     . ALA   A 1 696  ? -6.641  4.145   -84.362 1.00 80.56  ? 845  ALA   A O     1 
ATOM   4406 C  CB    . ALA   A 1 696  ? -9.597  5.280   -83.439 1.00 92.76  ? 845  ALA   A CB    1 
ATOM   4407 N  N     . ASN   A 1 697  ? -6.583  6.326   -83.672 1.00 83.78  ? 846  ASN   A N     1 
ATOM   4408 C  CA    . ASN   A 1 697  ? -5.440  6.823   -84.492 1.00 87.46  ? 846  ASN   A CA    1 
ATOM   4409 C  C     . ASN   A 1 697  ? -4.086  6.332   -83.944 1.00 83.00  ? 846  ASN   A C     1 
ATOM   4410 O  O     . ASN   A 1 697  ? -3.050  6.730   -84.521 1.00 81.66  ? 846  ASN   A O     1 
ATOM   4411 C  CB    . ASN   A 1 697  ? -5.389  8.359   -84.553 1.00 95.04  ? 846  ASN   A CB    1 
ATOM   4412 C  CG    . ASN   A 1 697  ? -6.650  9.011   -85.083 1.00 101.31 ? 846  ASN   A CG    1 
ATOM   4413 O  OD1   . ASN   A 1 697  ? -7.274  8.510   -86.014 1.00 103.96 ? 846  ASN   A OD1   1 
ATOM   4414 N  ND2   . ASN   A 1 697  ? -7.027  10.140  -84.505 1.00 105.49 ? 846  ASN   A ND2   1 
ATOM   4415 N  N     . ASP   A 1 698  ? -4.077  5.541   -82.862 1.00 82.86  ? 847  ASP   A N     1 
ATOM   4416 C  CA    . ASP   A 1 698  ? -2.859  4.998   -82.189 1.00 73.96  ? 847  ASP   A CA    1 
ATOM   4417 C  C     . ASP   A 1 698  ? -2.011  6.156   -81.611 1.00 62.11  ? 847  ASP   A C     1 
ATOM   4418 O  O     . ASP   A 1 698  ? -0.773  6.035   -81.550 1.00 60.38  ? 847  ASP   A O     1 
ATOM   4419 C  CB    . ASP   A 1 698  ? -2.118  4.026   -83.122 1.00 68.85  ? 847  ASP   A CB    1 
ATOM   4420 C  CG    . ASP   A 1 698  ? -2.746  2.639   -83.151 1.00 75.02  ? 847  ASP   A CG    1 
ATOM   4421 O  OD1   . ASP   A 1 698  ? -3.913  2.519   -82.714 1.00 78.87  ? 847  ASP   A OD1   1 
ATOM   4422 O  OD2   . ASP   A 1 698  ? -2.069  1.682   -83.598 1.00 70.99  ? 847  ASP   A OD2   1 
ATOM   4423 N  N     . GLU   A 1 699  ? -2.658  7.238   -81.182 1.00 59.59  ? 848  GLU   A N     1 
ATOM   4424 C  CA    . GLU   A 1 699  ? -2.018  8.389   -80.491 1.00 65.59  ? 848  GLU   A CA    1 
ATOM   4425 C  C     . GLU   A 1 699  ? -2.280  8.275   -78.984 1.00 62.14  ? 848  GLU   A C     1 
ATOM   4426 O  O     . GLU   A 1 699  ? -3.299  7.673   -78.586 1.00 56.63  ? 848  GLU   A O     1 
ATOM   4427 C  CB    . GLU   A 1 699  ? -2.547  9.729   -81.010 1.00 67.17  ? 848  GLU   A CB    1 
ATOM   4428 C  CG    . GLU   A 1 699  ? -2.173  10.019  -82.458 1.00 75.10  ? 848  GLU   A CG    1 
ATOM   4429 C  CD    . GLU   A 1 699  ? -0.701  9.842   -82.789 1.00 78.31  ? 848  GLU   A CD    1 
ATOM   4430 O  OE1   . GLU   A 1 699  ? 0.135   10.562  -82.186 1.00 72.68  ? 848  GLU   A OE1   1 
ATOM   4431 O  OE2   . GLU   A 1 699  ? -0.392  8.963   -83.634 1.00 81.43  ? 848  GLU   A OE2   1 
ATOM   4432 N  N     . LEU   A 1 700  ? -1.391  8.868   -78.195 1.00 55.82  ? 849  LEU   A N     1 
ATOM   4433 C  CA    . LEU   A 1 700  ? -1.381  8.778   -76.719 1.00 54.98  ? 849  LEU   A CA    1 
ATOM   4434 C  C     . LEU   A 1 700  ? -2.644  9.464   -76.190 1.00 56.31  ? 849  LEU   A C     1 
ATOM   4435 O  O     . LEU   A 1 700  ? -2.847  10.647  -76.503 1.00 63.91  ? 849  LEU   A O     1 
ATOM   4436 C  CB    . LEU   A 1 700  ? -0.082  9.427   -76.210 1.00 52.47  ? 849  LEU   A CB    1 
ATOM   4437 C  CG    . LEU   A 1 700  ? 0.500   8.845   -74.921 1.00 51.35  ? 849  LEU   A CG    1 
ATOM   4438 C  CD1   . LEU   A 1 700  ? 0.561   7.328   -74.980 1.00 46.50  ? 849  LEU   A CD1   1 
ATOM   4439 C  CD2   . LEU   A 1 700  ? 1.874   9.426   -74.639 1.00 52.71  ? 849  LEU   A CD2   1 
ATOM   4440 N  N     . THR   A 1 701  ? -3.488  8.738   -75.453 1.00 53.94  ? 850  THR   A N     1 
ATOM   4441 C  CA    . THR   A 1 701  ? -4.597  9.339   -74.665 1.00 53.79  ? 850  THR   A CA    1 
ATOM   4442 C  C     . THR   A 1 701  ? -3.982  10.026  -73.452 1.00 52.40  ? 850  THR   A C     1 
ATOM   4443 O  O     . THR   A 1 701  ? -2.810  9.816   -73.158 1.00 47.81  ? 850  THR   A O     1 
ATOM   4444 C  CB    . THR   A 1 701  ? -5.632  8.288   -74.242 1.00 55.16  ? 850  THR   A CB    1 
ATOM   4445 O  OG1   . THR   A 1 701  ? -4.993  7.336   -73.386 1.00 48.89  ? 850  THR   A OG1   1 
ATOM   4446 C  CG2   . THR   A 1 701  ? -6.280  7.599   -75.425 1.00 50.49  ? 850  THR   A CG2   1 
ATOM   4447 N  N     . PRO   A 1 702  ? -4.713  10.903  -72.733 1.00 56.49  ? 851  PRO   A N     1 
ATOM   4448 C  CA    . PRO   A 1 702  ? -4.268  11.353  -71.408 1.00 54.96  ? 851  PRO   A CA    1 
ATOM   4449 C  C     . PRO   A 1 702  ? -4.044  10.200  -70.401 1.00 51.90  ? 851  PRO   A C     1 
ATOM   4450 O  O     . PRO   A 1 702  ? -3.166  10.302  -69.553 1.00 47.77  ? 851  PRO   A O     1 
ATOM   4451 C  CB    . PRO   A 1 702  ? -5.402  12.302  -70.975 1.00 53.69  ? 851  PRO   A CB    1 
ATOM   4452 C  CG    . PRO   A 1 702  ? -5.978  12.805  -72.289 1.00 56.05  ? 851  PRO   A CG    1 
ATOM   4453 C  CD    . PRO   A 1 702  ? -5.919  11.604  -73.208 1.00 55.44  ? 851  PRO   A CD    1 
ATOM   4454 N  N     . LEU   A 1 703  ? -4.816  9.120   -70.512 1.00 46.82  ? 852  LEU   A N     1 
ATOM   4455 C  CA    . LEU   A 1 703  ? -4.576  7.875   -69.728 1.00 50.00  ? 852  LEU   A CA    1 
ATOM   4456 C  C     . LEU   A 1 703  ? -3.194  7.303   -70.111 1.00 48.14  ? 852  LEU   A C     1 
ATOM   4457 O  O     . LEU   A 1 703  ? -2.384  7.015   -69.195 1.00 44.36  ? 852  LEU   A O     1 
ATOM   4458 C  CB    . LEU   A 1 703  ? -5.721  6.890   -69.991 1.00 48.67  ? 852  LEU   A CB    1 
ATOM   4459 C  CG    . LEU   A 1 703  ? -5.531  5.478   -69.441 1.00 54.95  ? 852  LEU   A CG    1 
ATOM   4460 C  CD1   . LEU   A 1 703  ? -5.228  5.505   -67.953 1.00 55.77  ? 852  LEU   A CD1   1 
ATOM   4461 C  CD2   . LEU   A 1 703  ? -6.761  4.626   -69.706 1.00 58.48  ? 852  LEU   A CD2   1 
ATOM   4462 N  N     . GLY   A 1 704  ? -2.920  7.181   -71.415 1.00 45.51  ? 853  GLY   A N     1 
ATOM   4463 C  CA    . GLY   A 1 704  ? -1.640  6.694   -71.966 1.00 44.72  ? 853  GLY   A CA    1 
ATOM   4464 C  C     . GLY   A 1 704  ? -0.453  7.420   -71.368 1.00 45.51  ? 853  GLY   A C     1 
ATOM   4465 O  O     . GLY   A 1 704  ? 0.511   6.737   -70.956 1.00 50.33  ? 853  GLY   A O     1 
ATOM   4466 N  N     . ARG   A 1 705  ? -0.545  8.751   -71.308 1.00 44.52  ? 854  ARG   A N     1 
ATOM   4467 C  CA    . ARG   A 1 705  ? 0.508   9.688   -70.834 1.00 44.26  ? 854  ARG   A CA    1 
ATOM   4468 C  C     . ARG   A 1 705  ? 0.838   9.373   -69.372 1.00 48.59  ? 854  ARG   A C     1 
ATOM   4469 O  O     . ARG   A 1 705  ? 2.036   9.190   -69.060 1.00 50.16  ? 854  ARG   A O     1 
ATOM   4470 C  CB    . ARG   A 1 705  ? 0.006   11.121  -71.001 1.00 47.37  ? 854  ARG   A CB    1 
ATOM   4471 C  CG    . ARG   A 1 705  ? 1.047   12.204  -70.759 1.00 56.84  ? 854  ARG   A CG    1 
ATOM   4472 C  CD    . ARG   A 1 705  ? 0.529   13.557  -71.235 1.00 63.79  ? 854  ARG   A CD    1 
ATOM   4473 N  NE    . ARG   A 1 705  ? 0.260   13.519  -72.667 1.00 66.17  ? 854  ARG   A NE    1 
ATOM   4474 C  CZ    . ARG   A 1 705  ? 1.192   13.573  -73.616 1.00 69.20  ? 854  ARG   A CZ    1 
ATOM   4475 N  NH1   . ARG   A 1 705  ? 0.834   13.512  -74.889 1.00 69.02  ? 854  ARG   A NH1   1 
ATOM   4476 N  NH2   . ARG   A 1 705  ? 2.474   13.688  -73.300 1.00 66.27  ? 854  ARG   A NH2   1 
ATOM   4477 N  N     . ILE   A 1 706  ? -0.183  9.275   -68.517 1.00 42.50  ? 855  ILE   A N     1 
ATOM   4478 C  CA    . ILE   A 1 706  ? 0.001   8.847   -67.103 1.00 45.44  ? 855  ILE   A CA    1 
ATOM   4479 C  C     . ILE   A 1 706  ? 0.674   7.464   -67.067 1.00 41.59  ? 855  ILE   A C     1 
ATOM   4480 O  O     . ILE   A 1 706  ? 1.671   7.311   -66.334 1.00 42.04  ? 855  ILE   A O     1 
ATOM   4481 C  CB    . ILE   A 1 706  ? -1.335  8.873   -66.331 1.00 47.38  ? 855  ILE   A CB    1 
ATOM   4482 C  CG1   . ILE   A 1 706  ? -1.914  10.288  -66.255 1.00 45.62  ? 855  ILE   A CG1   1 
ATOM   4483 C  CG2   . ILE   A 1 706  ? -1.163  8.265   -64.942 1.00 46.97  ? 855  ILE   A CG2   1 
ATOM   4484 C  CD1   . ILE   A 1 706  ? -3.396  10.305  -66.033 1.00 47.37  ? 855  ILE   A CD1   1 
ATOM   4485 N  N     . LEU   A 1 707  ? 0.157   6.476   -67.799 1.00 43.01  ? 856  LEU   A N     1 
ATOM   4486 C  CA    . LEU   A 1 707  ? 0.708   5.093   -67.744 1.00 45.49  ? 856  LEU   A CA    1 
ATOM   4487 C  C     . LEU   A 1 707  ? 2.174   5.109   -68.202 1.00 43.50  ? 856  LEU   A C     1 
ATOM   4488 O  O     . LEU   A 1 707  ? 2.969   4.358   -67.630 1.00 45.09  ? 856  LEU   A O     1 
ATOM   4489 C  CB    . LEU   A 1 707  ? -0.121  4.132   -68.604 1.00 43.43  ? 856  LEU   A CB    1 
ATOM   4490 C  CG    . LEU   A 1 707  ? -1.588  3.965   -68.216 1.00 42.24  ? 856  LEU   A CG    1 
ATOM   4491 C  CD1   . LEU   A 1 707  ? -2.215  2.834   -69.018 1.00 44.71  ? 856  LEU   A CD1   1 
ATOM   4492 C  CD2   . LEU   A 1 707  ? -1.743  3.683   -66.740 1.00 42.21  ? 856  LEU   A CD2   1 
ATOM   4493 N  N     . ALA   A 1 708  ? 2.517   5.939   -69.187 1.00 42.32  ? 857  ALA   A N     1 
ATOM   4494 C  CA    . ALA   A 1 708  ? 3.886   6.051   -69.740 1.00 40.60  ? 857  ALA   A CA    1 
ATOM   4495 C  C     . ALA   A 1 708  ? 4.827   6.620   -68.679 1.00 42.60  ? 857  ALA   A C     1 
ATOM   4496 O  O     . ALA   A 1 708  ? 6.000   6.212   -68.676 1.00 40.93  ? 857  ALA   A O     1 
ATOM   4497 C  CB    . ALA   A 1 708  ? 3.872   6.919   -70.967 1.00 43.02  ? 857  ALA   A CB    1 
ATOM   4498 N  N     . LYS   A 1 709  ? 4.322   7.519   -67.821 1.00 40.66  ? 858  LYS   A N     1 
ATOM   4499 C  CA    . LYS   A 1 709  ? 5.107   8.222   -66.775 1.00 42.65  ? 858  LYS   A CA    1 
ATOM   4500 C  C     . LYS   A 1 709  ? 5.257   7.376   -65.501 1.00 45.90  ? 858  LYS   A C     1 
ATOM   4501 O  O     . LYS   A 1 709  ? 6.107   7.732   -64.664 1.00 50.74  ? 858  LYS   A O     1 
ATOM   4502 C  CB    . LYS   A 1 709  ? 4.427   9.541   -66.414 1.00 48.09  ? 858  LYS   A CB    1 
ATOM   4503 C  CG    . LYS   A 1 709  ? 4.583   10.650  -67.439 1.00 52.94  ? 858  LYS   A CG    1 
ATOM   4504 C  CD    . LYS   A 1 709  ? 3.621   11.801  -67.240 1.00 54.85  ? 858  LYS   A CD    1 
ATOM   4505 C  CE    . LYS   A 1 709  ? 3.994   13.007  -68.072 1.00 62.96  ? 858  LYS   A CE    1 
ATOM   4506 N  NZ    . LYS   A 1 709  ? 3.570   14.266  -67.416 1.00 74.64  ? 858  LYS   A NZ    1 
ATOM   4507 N  N     . LEU   A 1 710  ? 4.423   6.352   -65.300 1.00 49.89  ? 859  LEU   A N     1 
ATOM   4508 C  CA    . LEU   A 1 710  ? 4.512   5.447   -64.121 1.00 44.66  ? 859  LEU   A CA    1 
ATOM   4509 C  C     . LEU   A 1 710  ? 5.425   4.273   -64.461 1.00 41.44  ? 859  LEU   A C     1 
ATOM   4510 O  O     . LEU   A 1 710  ? 5.141   3.533   -65.385 1.00 40.25  ? 859  LEU   A O     1 
ATOM   4511 C  CB    . LEU   A 1 710  ? 3.114   4.940   -63.768 1.00 48.40  ? 859  LEU   A CB    1 
ATOM   4512 C  CG    . LEU   A 1 710  ? 2.140   5.977   -63.226 1.00 48.91  ? 859  LEU   A CG    1 
ATOM   4513 C  CD1   . LEU   A 1 710  ? 0.731   5.401   -63.224 1.00 46.52  ? 859  LEU   A CD1   1 
ATOM   4514 C  CD2   . LEU   A 1 710  ? 2.554   6.427   -61.826 1.00 48.77  ? 859  LEU   A CD2   1 
ATOM   4515 N  N     . PRO   A 1 711  ? 6.530   4.020   -63.730 1.00 42.08  ? 860  PRO   A N     1 
ATOM   4516 C  CA    . PRO   A 1 711  ? 7.375   2.858   -64.025 1.00 42.09  ? 860  PRO   A CA    1 
ATOM   4517 C  C     . PRO   A 1 711  ? 6.903   1.521   -63.408 1.00 45.06  ? 860  PRO   A C     1 
ATOM   4518 O  O     . PRO   A 1 711  ? 7.658   0.932   -62.635 1.00 43.26  ? 860  PRO   A O     1 
ATOM   4519 C  CB    . PRO   A 1 711  ? 8.697   3.323   -63.410 1.00 40.78  ? 860  PRO   A CB    1 
ATOM   4520 C  CG    . PRO   A 1 711  ? 8.248   4.048   -62.157 1.00 45.12  ? 860  PRO   A CG    1 
ATOM   4521 C  CD    . PRO   A 1 711  ? 7.020   4.817   -62.595 1.00 41.89  ? 860  PRO   A CD    1 
ATOM   4522 N  N     . ILE   A 1 712  ? 5.700   1.059   -63.787 1.00 44.22  ? 861  ILE   A N     1 
ATOM   4523 C  CA    . ILE   A 1 712  ? 5.101   -0.278  -63.451 1.00 46.98  ? 861  ILE   A CA    1 
ATOM   4524 C  C     . ILE   A 1 712  ? 4.295   -0.754  -64.670 1.00 42.37  ? 861  ILE   A C     1 
ATOM   4525 O  O     . ILE   A 1 712  ? 4.015   0.069   -65.533 1.00 39.75  ? 861  ILE   A O     1 
ATOM   4526 C  CB    . ILE   A 1 712  ? 4.201   -0.239  -62.190 1.00 47.72  ? 861  ILE   A CB    1 
ATOM   4527 C  CG1   . ILE   A 1 712  ? 3.484   1.094   -62.032 1.00 51.32  ? 861  ILE   A CG1   1 
ATOM   4528 C  CG2   . ILE   A 1 712  ? 4.966   -0.571  -60.925 1.00 54.28  ? 861  ILE   A CG2   1 
ATOM   4529 C  CD1   . ILE   A 1 712  ? 2.395   1.301   -63.024 1.00 54.22  ? 861  ILE   A CD1   1 
ATOM   4530 N  N     . GLU   A 1 713  ? 3.892   -2.020  -64.710 1.00 42.86  ? 862  GLU   A N     1 
ATOM   4531 C  CA    . GLU   A 1 713  ? 3.013   -2.564  -65.781 1.00 47.21  ? 862  GLU   A CA    1 
ATOM   4532 C  C     . GLU   A 1 713  ? 1.849   -1.594  -65.994 1.00 45.93  ? 862  GLU   A C     1 
ATOM   4533 O  O     . GLU   A 1 713  ? 1.220   -1.168  -65.028 1.00 38.57  ? 862  GLU   A O     1 
ATOM   4534 C  CB    . GLU   A 1 713  ? 2.537   -3.975  -65.416 1.00 53.07  ? 862  GLU   A CB    1 
ATOM   4535 C  CG    . GLU   A 1 713  ? 3.564   -5.055  -65.735 1.00 64.55  ? 862  GLU   A CG    1 
ATOM   4536 C  CD    . GLU   A 1 713  ? 3.750   -5.318  -67.224 1.00 77.62  ? 862  GLU   A CD    1 
ATOM   4537 O  OE1   . GLU   A 1 713  ? 2.810   -4.996  -68.002 1.00 77.53  ? 862  GLU   A OE1   1 
ATOM   4538 O  OE2   . GLU   A 1 713  ? 4.838   -5.825  -67.616 1.00 80.29  ? 862  GLU   A OE2   1 
ATOM   4539 N  N     . PRO   A 1 714  ? 1.577   -1.152  -67.248 1.00 45.14  ? 863  PRO   A N     1 
ATOM   4540 C  CA    . PRO   A 1 714  ? 0.443   -0.275  -67.549 1.00 42.35  ? 863  PRO   A CA    1 
ATOM   4541 C  C     . PRO   A 1 714  ? -0.882  -0.689  -66.899 1.00 39.80  ? 863  PRO   A C     1 
ATOM   4542 O  O     . PRO   A 1 714  ? -1.592  0.165   -66.397 1.00 36.03  ? 863  PRO   A O     1 
ATOM   4543 C  CB    . PRO   A 1 714  ? 0.344   -0.410  -69.068 1.00 42.89  ? 863  PRO   A CB    1 
ATOM   4544 C  CG    . PRO   A 1 714  ? 1.780   -0.471  -69.465 1.00 45.38  ? 863  PRO   A CG    1 
ATOM   4545 C  CD    . PRO   A 1 714  ? 2.407   -1.391  -68.438 1.00 43.07  ? 863  PRO   A CD    1 
ATOM   4546 N  N     . ARG   A 1 715  ? -1.162  -1.988  -66.884 1.00 38.19  ? 864  ARG   A N     1 
ATOM   4547 C  CA    . ARG   A 1 715  ? -2.422  -2.505  -66.301 1.00 40.44  ? 864  ARG   A CA    1 
ATOM   4548 C  C     . ARG   A 1 715  ? -2.480  -2.089  -64.823 1.00 40.94  ? 864  ARG   A C     1 
ATOM   4549 O  O     . ARG   A 1 715  ? -3.566  -1.696  -64.364 1.00 45.16  ? 864  ARG   A O     1 
ATOM   4550 C  CB    . ARG   A 1 715  ? -2.544  -4.011  -66.535 1.00 39.88  ? 864  ARG   A CB    1 
ATOM   4551 C  CG    . ARG   A 1 715  ? -3.970  -4.494  -66.359 1.00 42.34  ? 864  ARG   A CG    1 
ATOM   4552 C  CD    . ARG   A 1 715  ? -4.263  -5.923  -66.739 1.00 41.41  ? 864  ARG   A CD    1 
ATOM   4553 N  NE    . ARG   A 1 715  ? -5.692  -6.048  -66.531 1.00 44.57  ? 864  ARG   A NE    1 
ATOM   4554 C  CZ    . ARG   A 1 715  ? -6.622  -5.638  -67.385 1.00 46.46  ? 864  ARG   A CZ    1 
ATOM   4555 N  NH1   . ARG   A 1 715  ? -7.897  -5.767  -67.070 1.00 50.52  ? 864  ARG   A NH1   1 
ATOM   4556 N  NH2   . ARG   A 1 715  ? -6.288  -5.141  -68.559 1.00 43.90  ? 864  ARG   A NH2   1 
ATOM   4557 N  N     . PHE   A 1 716  ? -1.343  -2.115  -64.122 1.00 40.12  ? 865  PHE   A N     1 
ATOM   4558 C  CA    . PHE   A 1 716  ? -1.230  -1.698  -62.700 1.00 43.83  ? 865  PHE   A CA    1 
ATOM   4559 C  C     . PHE   A 1 716  ? -1.335  -0.177  -62.585 1.00 39.73  ? 865  PHE   A C     1 
ATOM   4560 O  O     . PHE   A 1 716  ? -1.937  0.306   -61.628 1.00 40.39  ? 865  PHE   A O     1 
ATOM   4561 C  CB    . PHE   A 1 716  ? 0.032   -2.286  -62.063 1.00 44.34  ? 865  PHE   A CB    1 
ATOM   4562 C  CG    . PHE   A 1 716  ? -0.180  -3.703  -61.604 1.00 49.53  ? 865  PHE   A CG    1 
ATOM   4563 C  CD1   . PHE   A 1 716  ? -0.064  -4.763  -62.483 1.00 57.48  ? 865  PHE   A CD1   1 
ATOM   4564 C  CD2   . PHE   A 1 716  ? -0.550  -3.973  -60.303 1.00 56.51  ? 865  PHE   A CD2   1 
ATOM   4565 C  CE1   . PHE   A 1 716  ? -0.266  -6.066  -62.062 1.00 56.86  ? 865  PHE   A CE1   1 
ATOM   4566 C  CE2   . PHE   A 1 716  ? -0.753  -5.278  -59.880 1.00 62.37  ? 865  PHE   A CE2   1 
ATOM   4567 C  CZ    . PHE   A 1 716  ? -0.612  -6.322  -60.762 1.00 59.76  ? 865  PHE   A CZ    1 
ATOM   4568 N  N     . GLY   A 1 717  ? -0.767  0.560   -63.531 1.00 42.75  ? 866  GLY   A N     1 
ATOM   4569 C  CA    . GLY   A 1 717  ? -0.957  2.021   -63.631 1.00 43.34  ? 866  GLY   A CA    1 
ATOM   4570 C  C     . GLY   A 1 717  ? -2.434  2.385   -63.687 1.00 40.73  ? 866  GLY   A C     1 
ATOM   4571 O  O     . GLY   A 1 717  ? -2.872  3.255   -62.911 1.00 41.15  ? 866  GLY   A O     1 
ATOM   4572 N  N     . LYS   A 1 718  ? -3.196  1.698   -64.533 1.00 38.16  ? 867  LYS   A N     1 
ATOM   4573 C  CA    . LYS   A 1 718  ? -4.644  1.954   -64.678 1.00 37.27  ? 867  LYS   A CA    1 
ATOM   4574 C  C     . LYS   A 1 718  ? -5.358  1.561   -63.380 1.00 38.47  ? 867  LYS   A C     1 
ATOM   4575 O  O     . LYS   A 1 718  ? -6.285  2.292   -62.991 1.00 39.78  ? 867  LYS   A O     1 
ATOM   4576 C  CB    . LYS   A 1 718  ? -5.198  1.210   -65.888 1.00 37.52  ? 867  LYS   A CB    1 
ATOM   4577 C  CG    . LYS   A 1 718  ? -6.637  1.567   -66.203 1.00 37.53  ? 867  LYS   A CG    1 
ATOM   4578 C  CD    . LYS   A 1 718  ? -7.115  1.075   -67.525 1.00 38.67  ? 867  LYS   A CD    1 
ATOM   4579 C  CE    . LYS   A 1 718  ? -8.520  1.542   -67.826 1.00 42.89  ? 867  LYS   A CE    1 
ATOM   4580 N  NZ    . LYS   A 1 718  ? -8.772  1.497   -69.281 1.00 47.15  ? 867  LYS   A NZ    1 
ATOM   4581 N  N     . MET   A 1 719  ? -4.947  0.462   -62.732 1.00 38.43  ? 868  MET   A N     1 
ATOM   4582 C  CA    . MET   A 1 719  ? -5.527  0.026   -61.434 1.00 39.08  ? 868  MET   A CA    1 
ATOM   4583 C  C     . MET   A 1 719  ? -5.318  1.126   -60.374 1.00 38.17  ? 868  MET   A C     1 
ATOM   4584 O  O     . MET   A 1 719  ? -6.228  1.335   -59.544 1.00 34.84  ? 868  MET   A O     1 
ATOM   4585 C  CB    . MET   A 1 719  ? -4.888  -1.280  -60.958 1.00 42.90  ? 868  MET   A CB    1 
ATOM   4586 C  CG    . MET   A 1 719  ? -5.416  -1.777  -59.620 1.00 41.50  ? 868  MET   A CG    1 
ATOM   4587 S  SD    . MET   A 1 719  ? -4.590  -3.310  -59.116 1.00 40.85  ? 868  MET   A SD    1 
ATOM   4588 C  CE    . MET   A 1 719  ? -3.020  -2.649  -58.563 1.00 45.48  ? 868  MET   A CE    1 
ATOM   4589 N  N     . MET   A 1 720  ? -4.175  1.809   -60.387 1.00 37.39  ? 869  MET   A N     1 
ATOM   4590 C  CA    . MET   A 1 720  ? -3.863  2.895   -59.416 1.00 41.10  ? 869  MET   A CA    1 
ATOM   4591 C  C     . MET   A 1 720  ? -4.757  4.107   -59.715 1.00 40.81  ? 869  MET   A C     1 
ATOM   4592 O  O     . MET   A 1 720  ? -5.213  4.704   -58.764 1.00 43.02  ? 869  MET   A O     1 
ATOM   4593 C  CB    . MET   A 1 720  ? -2.384  3.308   -59.436 1.00 39.27  ? 869  MET   A CB    1 
ATOM   4594 C  CG    . MET   A 1 720  ? -1.457  2.237   -58.859 1.00 43.28  ? 869  MET   A CG    1 
ATOM   4595 S  SD    . MET   A 1 720  ? 0.255   2.319   -59.499 1.00 51.24  ? 869  MET   A SD    1 
ATOM   4596 C  CE    . MET   A 1 720  ? 0.753   3.865   -58.762 1.00 46.89  ? 869  MET   A CE    1 
ATOM   4597 N  N     . ILE   A 1 721  ? -5.039  4.444   -60.978 1.00 44.08  ? 870  ILE   A N     1 
ATOM   4598 C  CA    . ILE   A 1 721  ? -5.957  5.581   -61.306 1.00 42.63  ? 870  ILE   A CA    1 
ATOM   4599 C  C     . ILE   A 1 721  ? -7.335  5.266   -60.714 1.00 39.11  ? 870  ILE   A C     1 
ATOM   4600 O  O     . ILE   A 1 721  ? -7.859  6.094   -59.973 1.00 38.98  ? 870  ILE   A O     1 
ATOM   4601 C  CB    . ILE   A 1 721  ? -6.003  5.834   -62.823 1.00 45.37  ? 870  ILE   A CB    1 
ATOM   4602 C  CG1   . ILE   A 1 721  ? -4.672  6.404   -63.309 1.00 44.98  ? 870  ILE   A CG1   1 
ATOM   4603 C  CG2   . ILE   A 1 721  ? -7.187  6.724   -63.212 1.00 44.30  ? 870  ILE   A CG2   1 
ATOM   4604 C  CD1   . ILE   A 1 721  ? -4.435  6.192   -64.780 1.00 47.35  ? 870  ILE   A CD1   1 
ATOM   4605 N  N     . MET   A 1 722  ? -7.849  4.061   -60.962 1.00 40.13  ? 871  MET   A N     1 
ATOM   4606 C  CA    . MET   A 1 722  ? -9.134  3.575   -60.391 1.00 41.87  ? 871  MET   A CA    1 
ATOM   4607 C  C     . MET   A 1 722  ? -9.084  3.633   -58.851 1.00 41.30  ? 871  MET   A C     1 
ATOM   4608 O  O     . MET   A 1 722  ? -10.073 4.039   -58.221 1.00 37.50  ? 871  MET   A O     1 
ATOM   4609 C  CB    . MET   A 1 722  ? -9.409  2.149   -60.881 1.00 44.10  ? 871  MET   A CB    1 
ATOM   4610 C  CG    . MET   A 1 722  ? -9.633  2.092   -62.396 1.00 48.17  ? 871  MET   A CG    1 
ATOM   4611 S  SD    . MET   A 1 722  ? -9.823  0.427   -63.096 1.00 46.40  ? 871  MET   A SD    1 
ATOM   4612 C  CE    . MET   A 1 722  ? -11.445 0.030   -62.469 1.00 45.22  ? 871  MET   A CE    1 
ATOM   4613 N  N     . GLY   A 1 723  ? -7.966  3.257   -58.238 1.00 41.39  ? 872  GLY   A N     1 
ATOM   4614 C  CA    . GLY   A 1 723  ? -7.803  3.352   -56.777 1.00 39.33  ? 872  GLY   A CA    1 
ATOM   4615 C  C     . GLY   A 1 723  ? -7.991  4.782   -56.322 1.00 35.65  ? 872  GLY   A C     1 
ATOM   4616 O  O     . GLY   A 1 723  ? -8.703  4.988   -55.347 1.00 38.89  ? 872  GLY   A O     1 
ATOM   4617 N  N     . CYS   A 1 724  ? -7.406  5.736   -57.038 1.00 35.36  ? 873  CYS   A N     1 
ATOM   4618 C  CA    . CYS   A 1 724  ? -7.506  7.192   -56.749 1.00 40.96  ? 873  CYS   A CA    1 
ATOM   4619 C  C     . CYS   A 1 724  ? -8.979  7.623   -56.814 1.00 43.32  ? 873  CYS   A C     1 
ATOM   4620 O  O     . CYS   A 1 724  ? -9.428  8.346   -55.925 1.00 39.58  ? 873  CYS   A O     1 
ATOM   4621 C  CB    . CYS   A 1 724  ? -6.664  8.002   -57.729 1.00 41.51  ? 873  CYS   A CB    1 
ATOM   4622 S  SG    . CYS   A 1 724  ? -4.882  7.864   -57.414 1.00 43.19  ? 873  CYS   A SG    1 
ATOM   4623 N  N     . ILE   A 1 725  ? -9.713  7.176   -57.833 1.00 42.22  ? 874  ILE   A N     1 
ATOM   4624 C  CA    . ILE   A 1 725  ? -11.142 7.548   -58.022 1.00 40.20  ? 874  ILE   A CA    1 
ATOM   4625 C  C     . ILE   A 1 725  ? -11.943 7.055   -56.818 1.00 40.02  ? 874  ILE   A C     1 
ATOM   4626 O  O     . ILE   A 1 725  ? -12.845 7.767   -56.414 1.00 43.36  ? 874  ILE   A O     1 
ATOM   4627 C  CB    . ILE   A 1 725  ? -11.682 7.011   -59.361 1.00 41.48  ? 874  ILE   A CB    1 
ATOM   4628 C  CG1   . ILE   A 1 725  ? -11.021 7.730   -60.539 1.00 37.41  ? 874  ILE   A CG1   1 
ATOM   4629 C  CG2   . ILE   A 1 725  ? -13.202 7.103   -59.411 1.00 41.86  ? 874  ILE   A CG2   1 
ATOM   4630 C  CD1   . ILE   A 1 725  ? -11.190 7.036   -61.857 1.00 38.81  ? 874  ILE   A CD1   1 
ATOM   4631 N  N     . PHE   A 1 726  ? -11.608 5.895   -56.253 1.00 42.01  ? 875  PHE   A N     1 
ATOM   4632 C  CA    . PHE   A 1 726  ? -12.318 5.290   -55.092 1.00 40.92  ? 875  PHE   A CA    1 
ATOM   4633 C  C     . PHE   A 1 726  ? -11.705 5.736   -53.753 1.00 42.09  ? 875  PHE   A C     1 
ATOM   4634 O  O     . PHE   A 1 726  ? -12.123 5.206   -52.700 1.00 44.81  ? 875  PHE   A O     1 
ATOM   4635 C  CB    . PHE   A 1 726  ? -12.294 3.761   -55.183 1.00 41.33  ? 875  PHE   A CB    1 
ATOM   4636 C  CG    . PHE   A 1 726  ? -13.301 3.134   -56.117 1.00 40.78  ? 875  PHE   A CG    1 
ATOM   4637 C  CD1   . PHE   A 1 726  ? -14.620 2.966   -55.727 1.00 41.24  ? 875  PHE   A CD1   1 
ATOM   4638 C  CD2   . PHE   A 1 726  ? -12.911 2.639   -57.349 1.00 37.34  ? 875  PHE   A CD2   1 
ATOM   4639 C  CE1   . PHE   A 1 726  ? -15.537 2.349   -56.566 1.00 42.12  ? 875  PHE   A CE1   1 
ATOM   4640 C  CE2   . PHE   A 1 726  ? -13.829 2.050   -58.194 1.00 40.56  ? 875  PHE   A CE2   1 
ATOM   4641 C  CZ    . PHE   A 1 726  ? -15.138 1.897   -57.799 1.00 44.24  ? 875  PHE   A CZ    1 
ATOM   4642 N  N     . TYR   A 1 727  ? -10.712 6.629   -53.761 1.00 42.53  ? 876  TYR   A N     1 
ATOM   4643 C  CA    . TYR   A 1 727  ? -10.040 7.124   -52.532 1.00 44.02  ? 876  TYR   A CA    1 
ATOM   4644 C  C     . TYR   A 1 727  ? -9.426  5.959   -51.742 1.00 45.12  ? 876  TYR   A C     1 
ATOM   4645 O  O     . TYR   A 1 727  ? -9.456  5.984   -50.488 1.00 46.51  ? 876  TYR   A O     1 
ATOM   4646 C  CB    . TYR   A 1 727  ? -11.034 7.921   -51.676 1.00 44.58  ? 876  TYR   A CB    1 
ATOM   4647 C  CG    . TYR   A 1 727  ? -11.200 9.343   -52.142 1.00 47.18  ? 876  TYR   A CG    1 
ATOM   4648 C  CD1   . TYR   A 1 727  ? -11.865 9.635   -53.323 1.00 47.85  ? 876  TYR   A CD1   1 
ATOM   4649 C  CD2   . TYR   A 1 727  ? -10.659 10.395  -51.422 1.00 47.70  ? 876  TYR   A CD2   1 
ATOM   4650 C  CE1   . TYR   A 1 727  ? -11.991 10.941  -53.768 1.00 53.05  ? 876  TYR   A CE1   1 
ATOM   4651 C  CE2   . TYR   A 1 727  ? -10.793 11.706  -51.842 1.00 47.27  ? 876  TYR   A CE2   1 
ATOM   4652 C  CZ    . TYR   A 1 727  ? -11.459 11.980  -53.021 1.00 50.69  ? 876  TYR   A CZ    1 
ATOM   4653 O  OH    . TYR   A 1 727  ? -11.571 13.268  -53.448 1.00 56.66  ? 876  TYR   A OH    1 
ATOM   4654 N  N     . VAL   A 1 728  ? -8.885  4.962   -52.439 1.00 40.60  ? 877  VAL   A N     1 
ATOM   4655 C  CA    . VAL   A 1 728  ? -7.988  3.943   -51.823 1.00 39.30  ? 877  VAL   A CA    1 
ATOM   4656 C  C     . VAL   A 1 728  ? -6.644  3.959   -52.562 1.00 34.57  ? 877  VAL   A C     1 
ATOM   4657 O  O     . VAL   A 1 728  ? -5.984  2.935   -52.607 1.00 39.84  ? 877  VAL   A O     1 
ATOM   4658 C  CB    . VAL   A 1 728  ? -8.663  2.563   -51.804 1.00 39.07  ? 877  VAL   A CB    1 
ATOM   4659 C  CG1   . VAL   A 1 728  ? -9.944  2.625   -50.988 1.00 42.55  ? 877  VAL   A CG1   1 
ATOM   4660 C  CG2   . VAL   A 1 728  ? -8.940  2.016   -53.202 1.00 39.06  ? 877  VAL   A CG2   1 
ATOM   4661 N  N     . GLY   A 1 729  ? -6.263  5.099   -53.123 1.00 36.11  ? 878  GLY   A N     1 
ATOM   4662 C  CA    . GLY   A 1 729  ? -4.976  5.276   -53.827 1.00 40.93  ? 878  GLY   A CA    1 
ATOM   4663 C  C     . GLY   A 1 729  ? -3.792  4.644   -53.101 1.00 38.74  ? 878  GLY   A C     1 
ATOM   4664 O  O     . GLY   A 1 729  ? -2.968  3.999   -53.759 1.00 40.67  ? 878  GLY   A O     1 
ATOM   4665 N  N     . ASP   A 1 730  ? -3.658  4.858   -51.796 1.00 40.64  ? 879  ASP   A N     1 
ATOM   4666 C  CA    . ASP   A 1 730  ? -2.412  4.490   -51.071 1.00 42.88  ? 879  ASP   A CA    1 
ATOM   4667 C  C     . ASP   A 1 730  ? -2.260  2.964   -51.090 1.00 42.35  ? 879  ASP   A C     1 
ATOM   4668 O  O     . ASP   A 1 730  ? -1.128  2.458   -51.334 1.00 39.10  ? 879  ASP   A O     1 
ATOM   4669 C  CB    . ASP   A 1 730  ? -2.367  5.062   -49.652 1.00 41.06  ? 879  ASP   A CB    1 
ATOM   4670 C  CG    . ASP   A 1 730  ? -1.205  4.516   -48.836 1.00 44.62  ? 879  ASP   A CG    1 
ATOM   4671 O  OD1   . ASP   A 1 730  ? -0.074  5.043   -48.994 1.00 44.69  ? 879  ASP   A OD1   1 
ATOM   4672 O  OD2   . ASP   A 1 730  ? -1.429  3.546   -48.060 1.00 46.65  ? 879  ASP   A OD2   1 
ATOM   4673 N  N     . ALA   A 1 731  ? -3.348  2.245   -50.847 1.00 36.67  ? 880  ALA   A N     1 
ATOM   4674 C  CA    . ALA   A 1 731  ? -3.316  0.772   -50.774 1.00 36.61  ? 880  ALA   A CA    1 
ATOM   4675 C  C     . ALA   A 1 731  ? -2.990  0.190   -52.162 1.00 36.80  ? 880  ALA   A C     1 
ATOM   4676 O  O     . ALA   A 1 731  ? -2.223  -0.794  -52.241 1.00 37.04  ? 880  ALA   A O     1 
ATOM   4677 C  CB    . ALA   A 1 731  ? -4.632  0.274   -50.225 1.00 35.65  ? 880  ALA   A CB    1 
ATOM   4678 N  N     . VAL   A 1 732  ? -3.535  0.756   -53.239 1.00 36.65  ? 881  VAL   A N     1 
ATOM   4679 C  CA    A VAL   A 1 732  ? -3.338  0.208   -54.611 0.50 36.53  ? 881  VAL   A CA    1 
ATOM   4680 C  CA    B VAL   A 1 732  ? -3.328  0.199   -54.611 0.50 36.76  ? 881  VAL   A CA    1 
ATOM   4681 C  C     . VAL   A 1 732  ? -1.903  0.528   -55.063 1.00 36.14  ? 881  VAL   A C     1 
ATOM   4682 O  O     . VAL   A 1 732  ? -1.314  -0.309  -55.764 1.00 39.71  ? 881  VAL   A O     1 
ATOM   4683 C  CB    A VAL   A 1 732  ? -4.427  0.734   -55.566 0.50 34.96  ? 881  VAL   A CB    1 
ATOM   4684 C  CB    B VAL   A 1 732  ? -4.363  0.680   -55.645 0.50 35.50  ? 881  VAL   A CB    1 
ATOM   4685 C  CG1   A VAL   A 1 732  ? -4.292  0.187   -56.971 0.50 34.58  ? 881  VAL   A CG1   1 
ATOM   4686 C  CG1   B VAL   A 1 732  ? -5.764  0.245   -55.269 0.50 35.62  ? 881  VAL   A CG1   1 
ATOM   4687 C  CG2   A VAL   A 1 732  ? -5.808  0.405   -55.034 0.50 35.82  ? 881  VAL   A CG2   1 
ATOM   4688 C  CG2   B VAL   A 1 732  ? -4.299  2.178   -55.882 0.50 36.17  ? 881  VAL   A CG2   1 
ATOM   4689 N  N     . CYS   A 1 733  ? -1.374  1.682   -54.655 1.00 36.49  ? 882  CYS   A N     1 
ATOM   4690 C  CA    . CYS   A 1 733  ? 0.043   2.070   -54.875 1.00 36.60  ? 882  CYS   A CA    1 
ATOM   4691 C  C     . CYS   A 1 733  ? 0.972   1.101   -54.139 1.00 38.64  ? 882  CYS   A C     1 
ATOM   4692 O  O     . CYS   A 1 733  ? 2.084   0.834   -54.663 1.00 42.03  ? 882  CYS   A O     1 
ATOM   4693 C  CB    . CYS   A 1 733  ? 0.327   3.492   -54.416 1.00 40.26  ? 882  CYS   A CB    1 
ATOM   4694 S  SG    . CYS   A 1 733  ? -0.199  4.766   -55.595 1.00 41.44  ? 882  CYS   A SG    1 
ATOM   4695 N  N     . THR   A 1 734  ? 0.559   0.589   -52.977 1.00 39.67  ? 883  THR   A N     1 
ATOM   4696 C  CA    . THR   A 1 734  ? 1.380   -0.345  -52.156 1.00 40.84  ? 883  THR   A CA    1 
ATOM   4697 C  C     . THR   A 1 734  ? 1.465   -1.687  -52.879 1.00 42.65  ? 883  THR   A C     1 
ATOM   4698 O  O     . THR   A 1 734  ? 2.589   -2.196  -53.043 1.00 45.21  ? 883  THR   A O     1 
ATOM   4699 C  CB    . THR   A 1 734  ? 0.838   -0.500  -50.734 1.00 42.13  ? 883  THR   A CB    1 
ATOM   4700 O  OG1   . THR   A 1 734  ? 0.927   0.769   -50.084 1.00 43.87  ? 883  THR   A OG1   1 
ATOM   4701 C  CG2   . THR   A 1 734  ? 1.609   -1.520  -49.931 1.00 44.45  ? 883  THR   A CG2   1 
ATOM   4702 N  N     . ILE   A 1 735  ? 0.325   -2.194  -53.349 1.00 40.69  ? 884  ILE   A N     1 
ATOM   4703 C  CA    . ILE   A 1 735  ? 0.234   -3.467  -54.114 1.00 38.38  ? 884  ILE   A CA    1 
ATOM   4704 C  C     . ILE   A 1 735  ? 1.082   -3.352  -55.380 1.00 38.13  ? 884  ILE   A C     1 
ATOM   4705 O  O     . ILE   A 1 735  ? 1.855   -4.278  -55.661 1.00 36.06  ? 884  ILE   A O     1 
ATOM   4706 C  CB    . ILE   A 1 735  ? -1.241  -3.826  -54.395 1.00 42.32  ? 884  ILE   A CB    1 
ATOM   4707 C  CG1   . ILE   A 1 735  ? -1.887  -4.431  -53.149 1.00 41.62  ? 884  ILE   A CG1   1 
ATOM   4708 C  CG2   . ILE   A 1 735  ? -1.391  -4.765  -55.592 1.00 43.72  ? 884  ILE   A CG2   1 
ATOM   4709 C  CD1   . ILE   A 1 735  ? -3.317  -4.031  -52.972 1.00 45.07  ? 884  ILE   A CD1   1 
ATOM   4710 N  N     . SER   A 1 736  ? 0.972   -2.254  -56.114 1.00 37.40  ? 885  SER   A N     1 
ATOM   4711 C  CA    . SER   A 1 736  ? 1.750   -2.057  -57.362 1.00 37.14  ? 885  SER   A CA    1 
ATOM   4712 C  C     . SER   A 1 736  ? 3.260   -2.076  -57.061 1.00 38.89  ? 885  SER   A C     1 
ATOM   4713 O  O     . SER   A 1 736  ? 4.002   -2.829  -57.745 1.00 40.19  ? 885  SER   A O     1 
ATOM   4714 C  CB    . SER   A 1 736  ? 1.328   -0.801  -58.042 1.00 38.90  ? 885  SER   A CB    1 
ATOM   4715 O  OG    . SER   A 1 736  ? -0.060  -0.825  -58.318 1.00 37.17  ? 885  SER   A OG    1 
ATOM   4716 N  N     . ALA   A 1 737  ? 3.712   -1.318  -56.058 1.00 38.42  ? 886  ALA   A N     1 
ATOM   4717 C  CA    . ALA   A 1 737  ? 5.146   -1.216  -55.698 1.00 38.36  ? 886  ALA   A CA    1 
ATOM   4718 C  C     . ALA   A 1 737  ? 5.670   -2.608  -55.306 1.00 36.93  ? 886  ALA   A C     1 
ATOM   4719 O  O     . ALA   A 1 737  ? 6.750   -2.980  -55.771 1.00 39.44  ? 886  ALA   A O     1 
ATOM   4720 C  CB    . ALA   A 1 737  ? 5.363   -0.193  -54.607 1.00 37.20  ? 886  ALA   A CB    1 
ATOM   4721 N  N     . ALA   A 1 738  ? 4.912   -3.375  -54.532 1.00 38.28  ? 887  ALA   A N     1 
ATOM   4722 C  CA    . ALA   A 1 738  ? 5.315   -4.716  -54.035 1.00 42.52  ? 887  ALA   A CA    1 
ATOM   4723 C  C     . ALA   A 1 738  ? 5.620   -5.683  -55.190 1.00 41.70  ? 887  ALA   A C     1 
ATOM   4724 O  O     . ALA   A 1 738  ? 6.423   -6.591  -54.968 1.00 50.86  ? 887  ALA   A O     1 
ATOM   4725 C  CB    . ALA   A 1 738  ? 4.272   -5.291  -53.103 1.00 40.00  ? 887  ALA   A CB    1 
ATOM   4726 N  N     . THR   A 1 739  ? 5.070   -5.474  -56.383 1.00 41.37  ? 888  THR   A N     1 
ATOM   4727 C  CA    . THR   A 1 739  ? 5.271   -6.374  -57.548 1.00 45.49  ? 888  THR   A CA    1 
ATOM   4728 C  C     . THR   A 1 739  ? 6.666   -6.166  -58.136 1.00 45.55  ? 888  THR   A C     1 
ATOM   4729 O  O     . THR   A 1 739  ? 7.064   -6.966  -59.008 1.00 49.61  ? 888  THR   A O     1 
ATOM   4730 C  CB    . THR   A 1 739  ? 4.217   -6.188  -58.655 1.00 46.74  ? 888  THR   A CB    1 
ATOM   4731 O  OG1   . THR   A 1 739  ? 4.396   -4.911  -59.270 1.00 44.25  ? 888  THR   A OG1   1 
ATOM   4732 C  CG2   . THR   A 1 739  ? 2.797   -6.334  -58.147 1.00 47.82  ? 888  THR   A CG2   1 
ATOM   4733 N  N     . CYS   A 1 740  ? 7.383   -5.134  -57.703 1.00 48.72  ? 889  CYS   A N     1 
ATOM   4734 C  CA    . CYS   A 1 740  ? 8.717   -4.798  -58.256 1.00 48.32  ? 889  CYS   A CA    1 
ATOM   4735 C  C     . CYS   A 1 740  ? 9.824   -5.392  -57.384 1.00 50.08  ? 889  CYS   A C     1 
ATOM   4736 O  O     . CYS   A 1 740  ? 11.000  -5.206  -57.749 1.00 55.79  ? 889  CYS   A O     1 
ATOM   4737 C  CB    . CYS   A 1 740  ? 8.877   -3.295  -58.371 1.00 48.07  ? 889  CYS   A CB    1 
ATOM   4738 S  SG    . CYS   A 1 740  ? 7.736   -2.574  -59.577 1.00 52.31  ? 889  CYS   A SG    1 
ATOM   4739 N  N     . PHE   A 1 741  ? 9.463   -6.068  -56.286 1.00 44.17  ? 890  PHE   A N     1 
ATOM   4740 C  CA    . PHE   A 1 741  ? 10.413  -6.512  -55.236 1.00 44.88  ? 890  PHE   A CA    1 
ATOM   4741 C  C     . PHE   A 1 741  ? 10.071  -7.935  -54.823 1.00 47.91  ? 890  PHE   A C     1 
ATOM   4742 O  O     . PHE   A 1 741  ? 8.941   -8.389  -54.953 1.00 51.59  ? 890  PHE   A O     1 
ATOM   4743 C  CB    . PHE   A 1 741  ? 10.418  -5.555  -54.032 1.00 40.62  ? 890  PHE   A CB    1 
ATOM   4744 C  CG    . PHE   A 1 741  ? 10.834  -4.144  -54.364 1.00 40.62  ? 890  PHE   A CG    1 
ATOM   4745 C  CD1   . PHE   A 1 741  ? 12.163  -3.825  -54.573 1.00 40.95  ? 890  PHE   A CD1   1 
ATOM   4746 C  CD2   . PHE   A 1 741  ? 9.886   -3.149  -54.559 1.00 40.75  ? 890  PHE   A CD2   1 
ATOM   4747 C  CE1   . PHE   A 1 741  ? 12.540  -2.537  -54.927 1.00 41.47  ? 890  PHE   A CE1   1 
ATOM   4748 C  CE2   . PHE   A 1 741  ? 10.264  -1.867  -54.927 1.00 40.86  ? 890  PHE   A CE2   1 
ATOM   4749 C  CZ    . PHE   A 1 741  ? 11.592  -1.556  -55.088 1.00 39.67  ? 890  PHE   A CZ    1 
ATOM   4750 N  N     . PRO   A 1 742  ? 11.046  -8.682  -54.286 1.00 53.36  ? 891  PRO   A N     1 
ATOM   4751 C  CA    . PRO   A 1 742  ? 10.750  -10.003 -53.741 1.00 55.91  ? 891  PRO   A CA    1 
ATOM   4752 C  C     . PRO   A 1 742  ? 9.742   -9.901  -52.587 1.00 58.43  ? 891  PRO   A C     1 
ATOM   4753 O  O     . PRO   A 1 742  ? 9.604   -8.832  -52.002 1.00 51.28  ? 891  PRO   A O     1 
ATOM   4754 C  CB    . PRO   A 1 742  ? 12.120  -10.536 -53.296 1.00 56.42  ? 891  PRO   A CB    1 
ATOM   4755 C  CG    . PRO   A 1 742  ? 13.004  -9.298  -53.184 1.00 58.06  ? 891  PRO   A CG    1 
ATOM   4756 C  CD    . PRO   A 1 742  ? 12.466  -8.309  -54.195 1.00 52.11  ? 891  PRO   A CD    1 
ATOM   4757 N  N     . GLU   A 1 743  ? 9.051   -11.006 -52.305 1.00 53.24  ? 892  GLU   A N     1 
ATOM   4758 C  CA    . GLU   A 1 743  ? 8.105   -11.110 -51.169 1.00 58.84  ? 892  GLU   A CA    1 
ATOM   4759 C  C     . GLU   A 1 743  ? 8.840   -10.680 -49.897 1.00 56.23  ? 892  GLU   A C     1 
ATOM   4760 O  O     . GLU   A 1 743  ? 9.952   -11.113 -49.656 1.00 54.10  ? 892  GLU   A O     1 
ATOM   4761 C  CB    . GLU   A 1 743  ? 7.592   -12.551 -51.031 1.00 66.84  ? 892  GLU   A CB    1 
ATOM   4762 C  CG    . GLU   A 1 743  ? 6.899   -13.109 -52.272 1.00 71.52  ? 892  GLU   A CG    1 
ATOM   4763 C  CD    . GLU   A 1 743  ? 5.465   -12.655 -52.505 1.00 83.08  ? 892  GLU   A CD    1 
ATOM   4764 O  OE1   . GLU   A 1 743  ? 4.858   -12.062 -51.584 1.00 80.93  ? 892  GLU   A OE1   1 
ATOM   4765 O  OE2   . GLU   A 1 743  ? 4.945   -12.903 -53.617 1.00 96.75  ? 892  GLU   A OE2   1 
ATOM   4766 N  N     . PRO   A 1 744  ? 8.267   -9.834  -49.018 1.00 56.07  ? 893  PRO   A N     1 
ATOM   4767 C  CA    . PRO   A 1 744  ? 8.893   -9.552  -47.725 1.00 56.22  ? 893  PRO   A CA    1 
ATOM   4768 C  C     . PRO   A 1 744  ? 8.958   -10.732 -46.742 1.00 55.92  ? 893  PRO   A C     1 
ATOM   4769 O  O     . PRO   A 1 744  ? 9.759   -10.692 -45.819 1.00 46.46  ? 893  PRO   A O     1 
ATOM   4770 C  CB    . PRO   A 1 744  ? 8.006   -8.446  -47.133 1.00 57.27  ? 893  PRO   A CB    1 
ATOM   4771 C  CG    . PRO   A 1 744  ? 6.679   -8.613  -47.832 1.00 54.11  ? 893  PRO   A CG    1 
ATOM   4772 C  CD    . PRO   A 1 744  ? 7.033   -9.067  -49.230 1.00 55.44  ? 893  PRO   A CD    1 
ATOM   4773 N  N     . PHE   A 1 745  ? 8.100   -11.736 -46.911 1.00 56.20  ? 894  PHE   A N     1 
ATOM   4774 C  CA    . PHE   A 1 745  ? 8.080   -12.927 -46.023 1.00 54.81  ? 894  PHE   A CA    1 
ATOM   4775 C  C     . PHE   A 1 745  ? 9.359   -13.746 -46.242 1.00 54.73  ? 894  PHE   A C     1 
ATOM   4776 O  O     . PHE   A 1 745  ? 9.681   -14.045 -47.395 1.00 54.45  ? 894  PHE   A O     1 
ATOM   4777 C  CB    . PHE   A 1 745  ? 6.846   -13.789 -46.291 1.00 53.25  ? 894  PHE   A CB    1 
ATOM   4778 C  CG    . PHE   A 1 745  ? 5.534   -13.265 -45.768 1.00 51.54  ? 894  PHE   A CG    1 
ATOM   4779 C  CD1   . PHE   A 1 745  ? 5.478   -12.353 -44.732 1.00 53.25  ? 894  PHE   A CD1   1 
ATOM   4780 C  CD2   . PHE   A 1 745  ? 4.340   -13.734 -46.293 1.00 55.58  ? 894  PHE   A CD2   1 
ATOM   4781 C  CE1   . PHE   A 1 745  ? 4.259   -11.909 -44.244 1.00 55.88  ? 894  PHE   A CE1   1 
ATOM   4782 C  CE2   . PHE   A 1 745  ? 3.120   -13.308 -45.793 1.00 58.65  ? 894  PHE   A CE2   1 
ATOM   4783 C  CZ    . PHE   A 1 745  ? 3.083   -12.387 -44.772 1.00 62.18  ? 894  PHE   A CZ    1 
ATOM   4784 N  N     . ILE   A 1 746  ? 10.068  -14.097 -45.168 1.00 58.93  ? 895  ILE   A N     1 
ATOM   4785 C  CA    . ILE   A 1 746  ? 11.237  -15.024 -45.224 1.00 62.26  ? 895  ILE   A CA    1 
ATOM   4786 C  C     . ILE   A 1 746  ? 10.721  -16.437 -44.921 1.00 60.83  ? 895  ILE   A C     1 
ATOM   4787 O  O     . ILE   A 1 746  ? 10.618  -16.813 -43.748 1.00 56.32  ? 895  ILE   A O     1 
ATOM   4788 C  CB    . ILE   A 1 746  ? 12.366  -14.562 -44.280 1.00 65.83  ? 895  ILE   A CB    1 
ATOM   4789 C  CG1   . ILE   A 1 746  ? 12.719  -13.092 -44.532 1.00 62.71  ? 895  ILE   A CG1   1 
ATOM   4790 C  CG2   . ILE   A 1 746  ? 13.586  -15.479 -44.409 1.00 63.39  ? 895  ILE   A CG2   1 
ATOM   4791 C  CD1   . ILE   A 1 746  ? 13.708  -12.504 -43.549 1.00 62.49  ? 895  ILE   A CD1   1 
ATOM   4792 N  N     . SER   A 1 747  ? 10.347  -17.168 -45.968 1.00 63.86  ? 896  SER   A N     1 
ATOM   4793 C  CA    . SER   A 1 747  ? 9.684   -18.490 -45.867 1.00 72.93  ? 896  SER   A CA    1 
ATOM   4794 C  C     . SER   A 1 747  ? 10.699  -19.606 -46.143 1.00 77.34  ? 896  SER   A C     1 
ATOM   4795 O  O     . SER   A 1 747  ? 10.546  -20.677 -45.540 1.00 84.20  ? 896  SER   A O     1 
ATOM   4796 C  CB    . SER   A 1 747  ? 8.483   -18.557 -46.780 1.00 68.23  ? 896  SER   A CB    1 
ATOM   4797 O  OG    . SER   A 1 747  ? 8.738   -17.882 -47.995 1.00 63.78  ? 896  SER   A OG    1 
ATOM   4798 N  N     . GLU   A 1 748  ? 11.696  -19.357 -47.001 1.00 83.78  ? 897  GLU   A N     1 
ATOM   4799 C  CA    . GLU   A 1 748  ? 12.795  -20.310 -47.325 1.00 91.93  ? 897  GLU   A CA    1 
ATOM   4800 C  C     . GLU   A 1 748  ? 12.234  -21.448 -48.203 1.00 94.56  ? 897  GLU   A C     1 
ATOM   4801 O  O     . GLU   A 1 748  ? 12.698  -22.602 -48.058 1.00 79.59  ? 897  GLU   A O     1 
ATOM   4802 C  CB    . GLU   A 1 748  ? 13.448  -20.807 -46.027 1.00 95.63  ? 897  GLU   A CB    1 
ATOM   4803 C  CG    . GLU   A 1 748  ? 13.953  -19.685 -45.126 1.00 101.19 ? 897  GLU   A CG    1 
ATOM   4804 C  CD    . GLU   A 1 748  ? 14.227  -20.054 -43.674 1.00 100.97 ? 897  GLU   A CD    1 
ATOM   4805 O  OE1   . GLU   A 1 748  ? 13.665  -21.059 -43.200 1.00 100.35 ? 897  GLU   A OE1   1 
ATOM   4806 O  OE2   . GLU   A 1 748  ? 14.999  -19.324 -43.013 1.00 97.67  ? 897  GLU   A OE2   1 
ATOM   4807 N  N     . GLY   A 1 749  ? 11.266  -21.132 -49.078 1.00 94.99  ? 898  GLY   A N     1 
ATOM   4808 C  CA    . GLY   A 1 749  ? 10.647  -22.067 -50.044 1.00 96.52  ? 898  GLY   A CA    1 
ATOM   4809 C  C     . GLY   A 1 749  ? 9.772   -23.128 -49.383 1.00 92.68  ? 898  GLY   A C     1 
ATOM   4810 O  O     . GLY   A 1 749  ? 9.410   -24.118 -50.067 1.00 89.58  ? 898  GLY   A O     1 
ATOM   4811 N  N     . LYS   A 1 750  ? 9.444   -22.948 -48.101 1.00 88.98  ? 899  LYS   A N     1 
ATOM   4812 C  CA    . LYS   A 1 750  ? 8.527   -23.838 -47.344 1.00 89.73  ? 899  LYS   A CA    1 
ATOM   4813 C  C     . LYS   A 1 750  ? 7.163   -23.144 -47.240 1.00 84.57  ? 899  LYS   A C     1 
ATOM   4814 O  O     . LYS   A 1 750  ? 7.071   -21.938 -47.557 1.00 87.23  ? 899  LYS   A O     1 
ATOM   4815 C  CB    . LYS   A 1 750  ? 9.102   -24.189 -45.964 1.00 92.66  ? 899  LYS   A CB    1 
ATOM   4816 C  CG    . LYS   A 1 750  ? 10.615  -24.376 -45.906 1.00 103.26 ? 899  LYS   A CG    1 
ATOM   4817 C  CD    . LYS   A 1 750  ? 11.089  -25.556 -45.067 1.00 112.07 ? 899  LYS   A CD    1 
ATOM   4818 C  CE    . LYS   A 1 750  ? 10.430  -25.658 -43.705 1.00 119.92 ? 899  LYS   A CE    1 
ATOM   4819 N  NZ    . LYS   A 1 750  ? 10.442  -24.365 -42.980 1.00 122.15 ? 899  LYS   A NZ    1 
ATOM   4820 N  N     . ARG   A 1 751  ? 6.138   -23.903 -46.853 1.00 84.50  ? 900  ARG   A N     1 
ATOM   4821 C  CA    . ARG   A 1 751  ? 4.797   -23.401 -46.470 1.00 79.66  ? 900  ARG   A CA    1 
ATOM   4822 C  C     . ARG   A 1 751  ? 4.966   -22.346 -45.379 1.00 75.41  ? 900  ARG   A C     1 
ATOM   4823 O  O     . ARG   A 1 751  ? 5.769   -22.568 -44.440 1.00 74.47  ? 900  ARG   A O     1 
ATOM   4824 C  CB    . ARG   A 1 751  ? 3.918   -24.550 -45.970 1.00 80.85  ? 900  ARG   A CB    1 
ATOM   4825 C  CG    . ARG   A 1 751  ? 3.428   -25.464 -47.081 1.00 92.19  ? 900  ARG   A CG    1 
ATOM   4826 C  CD    . ARG   A 1 751  ? 2.702   -26.674 -46.532 1.00 98.67  ? 900  ARG   A CD    1 
ATOM   4827 N  NE    . ARG   A 1 751  ? 2.199   -27.507 -47.615 1.00 102.41 ? 900  ARG   A NE    1 
ATOM   4828 C  CZ    . ARG   A 1 751  ? 2.928   -28.374 -48.314 1.00 104.44 ? 900  ARG   A CZ    1 
ATOM   4829 N  NH1   . ARG   A 1 751  ? 4.214   -28.540 -48.052 1.00 105.04 ? 900  ARG   A NH1   1 
ATOM   4830 N  NH2   . ARG   A 1 751  ? 2.364   -29.073 -49.284 1.00 103.92 ? 900  ARG   A NH2   1 
ATOM   4831 N  N     . LEU   A 1 752  ? 4.222   -21.248 -45.495 1.00 66.12  ? 901  LEU   A N     1 
ATOM   4832 C  CA    . LEU   A 1 752  ? 4.137   -20.216 -44.436 1.00 62.05  ? 901  LEU   A CA    1 
ATOM   4833 C  C     . LEU   A 1 752  ? 3.758   -20.938 -43.141 1.00 56.84  ? 901  LEU   A C     1 
ATOM   4834 O  O     . LEU   A 1 752  ? 3.006   -21.916 -43.215 1.00 52.04  ? 901  LEU   A O     1 
ATOM   4835 C  CB    . LEU   A 1 752  ? 3.101   -19.143 -44.806 1.00 61.28  ? 901  LEU   A CB    1 
ATOM   4836 C  CG    . LEU   A 1 752  ? 3.258   -18.488 -46.180 1.00 59.38  ? 901  LEU   A CG    1 
ATOM   4837 C  CD1   . LEU   A 1 752  ? 2.090   -17.555 -46.486 1.00 59.01  ? 901  LEU   A CD1   1 
ATOM   4838 C  CD2   . LEU   A 1 752  ? 4.582   -17.755 -46.291 1.00 58.28  ? 901  LEU   A CD2   1 
ATOM   4839 N  N     . GLY   A 1 753  ? 4.290   -20.478 -42.012 1.00 54.59  ? 902  GLY   A N     1 
ATOM   4840 C  CA    . GLY   A 1 753  ? 3.856   -20.873 -40.662 1.00 53.40  ? 902  GLY   A CA    1 
ATOM   4841 C  C     . GLY   A 1 753  ? 2.802   -19.920 -40.140 1.00 56.04  ? 902  GLY   A C     1 
ATOM   4842 O  O     . GLY   A 1 753  ? 2.234   -19.146 -40.960 1.00 59.87  ? 902  GLY   A O     1 
ATOM   4843 N  N     . TYR   A 1 754  ? 2.561   -19.969 -38.831 1.00 54.25  ? 903  TYR   A N     1 
ATOM   4844 C  CA    . TYR   A 1 754  ? 1.402   -19.335 -38.154 1.00 62.01  ? 903  TYR   A CA    1 
ATOM   4845 C  C     . TYR   A 1 754  ? 1.488   -17.806 -38.251 1.00 62.63  ? 903  TYR   A C     1 
ATOM   4846 O  O     . TYR   A 1 754  ? 0.457   -17.158 -38.551 1.00 63.29  ? 903  TYR   A O     1 
ATOM   4847 C  CB    . TYR   A 1 754  ? 1.319   -19.787 -36.695 1.00 60.42  ? 903  TYR   A CB    1 
ATOM   4848 C  CG    . TYR   A 1 754  ? 0.270   -19.077 -35.879 1.00 69.76  ? 903  TYR   A CG    1 
ATOM   4849 C  CD1   . TYR   A 1 754  ? -1.079  -19.377 -36.033 1.00 74.90  ? 903  TYR   A CD1   1 
ATOM   4850 C  CD2   . TYR   A 1 754  ? 0.620   -18.104 -34.951 1.00 67.27  ? 903  TYR   A CD2   1 
ATOM   4851 C  CE1   . TYR   A 1 754  ? -2.057  -18.734 -35.285 1.00 73.01  ? 903  TYR   A CE1   1 
ATOM   4852 C  CE2   . TYR   A 1 754  ? -0.345  -17.450 -34.199 1.00 72.68  ? 903  TYR   A CE2   1 
ATOM   4853 C  CZ    . TYR   A 1 754  ? -1.690  -17.765 -34.362 1.00 76.30  ? 903  TYR   A CZ    1 
ATOM   4854 O  OH    . TYR   A 1 754  ? -2.647  -17.129 -33.610 1.00 66.88  ? 903  TYR   A OH    1 
ATOM   4855 N  N     . VAL   A 1 755  ? 2.656   -17.224 -37.982 1.00 55.54  ? 904  VAL   A N     1 
ATOM   4856 C  CA    . VAL   A 1 755  ? 2.751   -15.749 -37.800 1.00 57.84  ? 904  VAL   A CA    1 
ATOM   4857 C  C     . VAL   A 1 755  ? 2.474   -15.109 -39.162 1.00 54.87  ? 904  VAL   A C     1 
ATOM   4858 O  O     . VAL   A 1 755  ? 1.597   -14.221 -39.222 1.00 56.44  ? 904  VAL   A O     1 
ATOM   4859 C  CB    . VAL   A 1 755  ? 4.088   -15.290 -37.186 1.00 61.28  ? 904  VAL   A CB    1 
ATOM   4860 C  CG1   . VAL   A 1 755  ? 4.082   -13.786 -36.936 1.00 59.29  ? 904  VAL   A CG1   1 
ATOM   4861 C  CG2   . VAL   A 1 755  ? 4.388   -16.028 -35.889 1.00 64.11  ? 904  VAL   A CG2   1 
ATOM   4862 N  N     . HIS   A 1 756  ? 3.160   -15.579 -40.206 1.00 48.96  ? 905  HIS   A N     1 
ATOM   4863 C  CA    . HIS   A 1 756  ? 2.962   -15.134 -41.607 1.00 48.48  ? 905  HIS   A CA    1 
ATOM   4864 C  C     . HIS   A 1 756  ? 1.487   -15.306 -42.014 1.00 50.35  ? 905  HIS   A C     1 
ATOM   4865 O  O     . HIS   A 1 756  ? 0.934   -14.343 -42.599 1.00 52.04  ? 905  HIS   A O     1 
ATOM   4866 C  CB    . HIS   A 1 756  ? 3.961   -15.827 -42.536 1.00 47.69  ? 905  HIS   A CB    1 
ATOM   4867 C  CG    . HIS   A 1 756  ? 5.365   -15.337 -42.386 1.00 51.25  ? 905  HIS   A CG    1 
ATOM   4868 N  ND1   . HIS   A 1 756  ? 6.445   -15.984 -42.969 1.00 51.43  ? 905  HIS   A ND1   1 
ATOM   4869 C  CD2   . HIS   A 1 756  ? 5.877   -14.278 -41.721 1.00 52.01  ? 905  HIS   A CD2   1 
ATOM   4870 C  CE1   . HIS   A 1 756  ? 7.552   -15.330 -42.683 1.00 53.46  ? 905  HIS   A CE1   1 
ATOM   4871 N  NE2   . HIS   A 1 756  ? 7.230   -14.270 -41.929 1.00 51.95  ? 905  HIS   A NE2   1 
ATOM   4872 N  N     . ARG   A 1 757  ? 0.839   -16.430 -41.686 1.00 47.27  ? 906  ARG   A N     1 
ATOM   4873 C  CA    . ARG   A 1 757  ? -0.587  -16.677 -42.067 1.00 49.04  ? 906  ARG   A CA    1 
ATOM   4874 C  C     . ARG   A 1 757  ? -1.501  -15.689 -41.331 1.00 47.39  ? 906  ARG   A C     1 
ATOM   4875 O  O     . ARG   A 1 757  ? -2.479  -15.233 -41.945 1.00 51.15  ? 906  ARG   A O     1 
ATOM   4876 C  CB    . ARG   A 1 757  ? -1.014  -18.124 -41.793 1.00 51.05  ? 906  ARG   A CB    1 
ATOM   4877 C  CG    . ARG   A 1 757  ? -0.490  -19.116 -42.822 1.00 53.04  ? 906  ARG   A CG    1 
ATOM   4878 C  CD    . ARG   A 1 757  ? -0.614  -20.570 -42.407 1.00 53.68  ? 906  ARG   A CD    1 
ATOM   4879 N  NE    . ARG   A 1 757  ? 0.169   -21.431 -43.288 1.00 51.13  ? 906  ARG   A NE    1 
ATOM   4880 C  CZ    . ARG   A 1 757  ? -0.284  -22.033 -44.399 1.00 54.21  ? 906  ARG   A CZ    1 
ATOM   4881 N  NH1   . ARG   A 1 757  ? 0.549   -22.765 -45.133 1.00 48.93  ? 906  ARG   A NH1   1 
ATOM   4882 N  NH2   . ARG   A 1 757  ? -1.553  -21.909 -44.772 1.00 49.49  ? 906  ARG   A NH2   1 
ATOM   4883 N  N     . ASN   A 1 758  ? -1.183  -15.333 -40.087 1.00 48.16  ? 907  ASN   A N     1 
ATOM   4884 C  CA    . ASN   A 1 758  ? -2.019  -14.416 -39.266 1.00 54.00  ? 907  ASN   A CA    1 
ATOM   4885 C  C     . ASN   A 1 758  ? -2.182  -13.054 -39.952 1.00 55.30  ? 907  ASN   A C     1 
ATOM   4886 O  O     . ASN   A 1 758  ? -3.209  -12.398 -39.706 1.00 59.07  ? 907  ASN   A O     1 
ATOM   4887 C  CB    . ASN   A 1 758  ? -1.482  -14.223 -37.850 1.00 58.29  ? 907  ASN   A CB    1 
ATOM   4888 C  CG    . ASN   A 1 758  ? -2.293  -14.999 -36.841 1.00 69.17  ? 907  ASN   A CG    1 
ATOM   4889 O  OD1   . ASN   A 1 758  ? -2.881  -16.036 -37.164 1.00 72.99  ? 907  ASN   A OD1   1 
ATOM   4890 N  ND2   . ASN   A 1 758  ? -2.346  -14.485 -35.624 1.00 76.91  ? 907  ASN   A ND2   1 
ATOM   4891 N  N     . PHE   A 1 759  ? -1.243  -12.647 -40.801 1.00 48.59  ? 908  PHE   A N     1 
ATOM   4892 C  CA    . PHE   A 1 759  ? -1.316  -11.338 -41.496 1.00 50.92  ? 908  PHE   A CA    1 
ATOM   4893 C  C     . PHE   A 1 759  ? -2.495  -11.316 -42.476 1.00 48.24  ? 908  PHE   A C     1 
ATOM   4894 O  O     . PHE   A 1 759  ? -2.954  -10.225 -42.807 1.00 41.63  ? 908  PHE   A O     1 
ATOM   4895 C  CB    . PHE   A 1 759  ? 0.028   -11.021 -42.149 1.00 50.13  ? 908  PHE   A CB    1 
ATOM   4896 C  CG    . PHE   A 1 759  ? 1.058   -10.539 -41.164 1.00 46.69  ? 908  PHE   A CG    1 
ATOM   4897 C  CD1   . PHE   A 1 759  ? 0.899   -9.319  -40.522 1.00 49.97  ? 908  PHE   A CD1   1 
ATOM   4898 C  CD2   . PHE   A 1 759  ? 2.167   -11.313 -40.854 1.00 46.43  ? 908  PHE   A CD2   1 
ATOM   4899 C  CE1   . PHE   A 1 759  ? 1.844   -8.873  -39.604 1.00 49.62  ? 908  PHE   A CE1   1 
ATOM   4900 C  CE2   . PHE   A 1 759  ? 3.120   -10.852 -39.952 1.00 52.45  ? 908  PHE   A CE2   1 
ATOM   4901 C  CZ    . PHE   A 1 759  ? 2.961   -9.631  -39.331 1.00 47.62  ? 908  PHE   A CZ    1 
ATOM   4902 N  N     . ALA   A 1 760  ? -2.985  -12.489 -42.878 1.00 48.34  ? 909  ALA   A N     1 
ATOM   4903 C  CA    . ALA   A 1 760  ? -4.042  -12.672 -43.893 1.00 46.47  ? 909  ALA   A CA    1 
ATOM   4904 C  C     . ALA   A 1 760  ? -5.425  -12.314 -43.330 1.00 41.14  ? 909  ALA   A C     1 
ATOM   4905 O  O     . ALA   A 1 760  ? -6.304  -11.965 -44.125 1.00 43.16  ? 909  ALA   A O     1 
ATOM   4906 C  CB    . ALA   A 1 760  ? -4.006  -14.099 -44.383 1.00 47.75  ? 909  ALA   A CB    1 
ATOM   4907 N  N     . GLY   A 1 761  ? -5.623  -12.432 -42.019 1.00 43.27  ? 910  GLY   A N     1 
ATOM   4908 C  CA    . GLY   A 1 761  ? -6.954  -12.326 -41.393 1.00 40.85  ? 910  GLY   A CA    1 
ATOM   4909 C  C     . GLY   A 1 761  ? -7.859  -13.410 -41.940 1.00 44.15  ? 910  GLY   A C     1 
ATOM   4910 O  O     . GLY   A 1 761  ? -7.375  -14.546 -42.133 1.00 39.57  ? 910  GLY   A O     1 
ATOM   4911 N  N     . ASN   A 1 762  ? -9.103  -13.062 -42.264 1.00 43.20  ? 911  ASN   A N     1 
ATOM   4912 C  CA    . ASN   A 1 762  ? -10.124 -14.043 -42.692 1.00 45.57  ? 911  ASN   A CA    1 
ATOM   4913 C  C     . ASN   A 1 762  ? -10.385 -13.894 -44.202 1.00 43.25  ? 911  ASN   A C     1 
ATOM   4914 O  O     . ASN   A 1 762  ? -11.383 -14.454 -44.669 1.00 37.76  ? 911  ASN   A O     1 
ATOM   4915 C  CB    . ASN   A 1 762  ? -11.375 -13.913 -41.806 1.00 51.01  ? 911  ASN   A CB    1 
ATOM   4916 C  CG    . ASN   A 1 762  ? -12.061 -12.561 -41.889 1.00 53.88  ? 911  ASN   A CG    1 
ATOM   4917 O  OD1   . ASN   A 1 762  ? -11.788 -11.751 -42.777 1.00 56.23  ? 911  ASN   A OD1   1 
ATOM   4918 N  ND2   . ASN   A 1 762  ? -12.952 -12.299 -40.951 1.00 55.26  ? 911  ASN   A ND2   1 
ATOM   4919 N  N     . ARG   A 1 763  ? -9.502  -13.220 -44.951 1.00 44.59  ? 912  ARG   A N     1 
ATOM   4920 C  CA    . ARG   A 1 763  ? -9.748  -12.801 -46.360 1.00 38.45  ? 912  ARG   A CA    1 
ATOM   4921 C  C     . ARG   A 1 763  ? -9.168  -13.788 -47.381 1.00 40.09  ? 912  ARG   A C     1 
ATOM   4922 O  O     . ARG   A 1 763  ? -9.410  -13.578 -48.570 1.00 38.56  ? 912  ARG   A O     1 
ATOM   4923 C  CB    . ARG   A 1 763  ? -9.138  -11.427 -46.606 1.00 41.89  ? 912  ARG   A CB    1 
ATOM   4924 C  CG    . ARG   A 1 763  ? -9.910  -10.288 -45.958 1.00 43.93  ? 912  ARG   A CG    1 
ATOM   4925 C  CD    . ARG   A 1 763  ? -11.061 -9.843  -46.830 1.00 40.41  ? 912  ARG   A CD    1 
ATOM   4926 N  NE    . ARG   A 1 763  ? -11.596 -8.604  -46.322 1.00 40.48  ? 912  ARG   A NE    1 
ATOM   4927 C  CZ    . ARG   A 1 763  ? -12.457 -7.818  -46.960 1.00 44.42  ? 912  ARG   A CZ    1 
ATOM   4928 N  NH1   . ARG   A 1 763  ? -12.917 -8.143  -48.163 1.00 42.84  ? 912  ARG   A NH1   1 
ATOM   4929 N  NH2   . ARG   A 1 763  ? -12.846 -6.695  -46.379 1.00 43.92  ? 912  ARG   A NH2   1 
ATOM   4930 N  N     . PHE   A 1 764  ? -8.457  -14.841 -46.971 1.00 41.22  ? 913  PHE   A N     1 
ATOM   4931 C  CA    . PHE   A 1 764  ? -7.938  -15.867 -47.915 1.00 39.99  ? 913  PHE   A CA    1 
ATOM   4932 C  C     . PHE   A 1 764  ? -7.170  -15.158 -49.040 1.00 42.54  ? 913  PHE   A C     1 
ATOM   4933 O  O     . PHE   A 1 764  ? -7.449  -15.402 -50.222 1.00 39.24  ? 913  PHE   A O     1 
ATOM   4934 C  CB    . PHE   A 1 764  ? -9.099  -16.690 -48.477 1.00 41.72  ? 913  PHE   A CB    1 
ATOM   4935 C  CG    . PHE   A 1 764  ? -9.850  -17.489 -47.446 1.00 42.97  ? 913  PHE   A CG    1 
ATOM   4936 C  CD1   . PHE   A 1 764  ? -9.355  -18.702 -46.986 1.00 46.68  ? 913  PHE   A CD1   1 
ATOM   4937 C  CD2   . PHE   A 1 764  ? -11.051 -17.030 -46.933 1.00 44.78  ? 913  PHE   A CD2   1 
ATOM   4938 C  CE1   . PHE   A 1 764  ? -10.038 -19.423 -46.015 1.00 49.91  ? 913  PHE   A CE1   1 
ATOM   4939 C  CE2   . PHE   A 1 764  ? -11.730 -17.751 -45.959 1.00 45.72  ? 913  PHE   A CE2   1 
ATOM   4940 C  CZ    . PHE   A 1 764  ? -11.232 -18.953 -45.515 1.00 46.11  ? 913  PHE   A CZ    1 
ATOM   4941 N  N     . SER   A 1 765  ? -6.241  -14.268 -48.685 1.00 41.71  ? 914  SER   A N     1 
ATOM   4942 C  CA    . SER   A 1 765  ? -5.611  -13.311 -49.628 1.00 39.42  ? 914  SER   A CA    1 
ATOM   4943 C  C     . SER   A 1 765  ? -4.170  -13.012 -49.230 1.00 40.24  ? 914  SER   A C     1 
ATOM   4944 O  O     . SER   A 1 765  ? -3.980  -12.408 -48.168 1.00 41.66  ? 914  SER   A O     1 
ATOM   4945 C  CB    . SER   A 1 765  ? -6.388  -12.030 -49.677 1.00 39.90  ? 914  SER   A CB    1 
ATOM   4946 O  OG    . SER   A 1 765  ? -5.710  -11.081 -50.491 1.00 41.72  ? 914  SER   A OG    1 
ATOM   4947 N  N     . ASP   A 1 766  ? -3.227  -13.329 -50.120 1.00 40.89  ? 915  ASP   A N     1 
ATOM   4948 C  CA    . ASP   A 1 766  ? -1.785  -12.988 -50.003 1.00 40.47  ? 915  ASP   A CA    1 
ATOM   4949 C  C     . ASP   A 1 766  ? -1.611  -11.475 -50.100 1.00 39.40  ? 915  ASP   A C     1 
ATOM   4950 O  O     . ASP   A 1 766  ? -0.770  -10.943 -49.397 1.00 41.04  ? 915  ASP   A O     1 
ATOM   4951 C  CB    . ASP   A 1 766  ? -0.968  -13.687 -51.088 1.00 41.48  ? 915  ASP   A CB    1 
ATOM   4952 C  CG    . ASP   A 1 766  ? -0.847  -15.188 -50.862 1.00 45.41  ? 915  ASP   A CG    1 
ATOM   4953 O  OD1   . ASP   A 1 766  ? -0.657  -15.586 -49.682 1.00 43.86  ? 915  ASP   A OD1   1 
ATOM   4954 O  OD2   . ASP   A 1 766  ? -0.961  -15.949 -51.867 1.00 43.75  ? 915  ASP   A OD2   1 
ATOM   4955 N  N     . HIS   A 1 767  ? -2.385  -10.818 -50.958 1.00 38.42  ? 916  HIS   A N     1 
ATOM   4956 C  CA    . HIS   A 1 767  ? -2.362  -9.349  -51.141 1.00 36.72  ? 916  HIS   A CA    1 
ATOM   4957 C  C     . HIS   A 1 767  ? -2.819  -8.639  -49.854 1.00 38.23  ? 916  HIS   A C     1 
ATOM   4958 O  O     . HIS   A 1 767  ? -2.231  -7.611  -49.540 1.00 37.69  ? 916  HIS   A O     1 
ATOM   4959 C  CB    . HIS   A 1 767  ? -3.197  -8.979  -52.363 1.00 37.37  ? 916  HIS   A CB    1 
ATOM   4960 C  CG    . HIS   A 1 767  ? -2.573  -9.427  -53.636 1.00 39.44  ? 916  HIS   A CG    1 
ATOM   4961 N  ND1   . HIS   A 1 767  ? -2.969  -10.581 -54.282 1.00 40.10  ? 916  HIS   A ND1   1 
ATOM   4962 C  CD2   . HIS   A 1 767  ? -1.570  -8.897  -54.367 1.00 40.36  ? 916  HIS   A CD2   1 
ATOM   4963 C  CE1   . HIS   A 1 767  ? -2.248  -10.729 -55.375 1.00 41.46  ? 916  HIS   A CE1   1 
ATOM   4964 N  NE2   . HIS   A 1 767  ? -1.372  -9.719  -55.450 1.00 42.07  ? 916  HIS   A NE2   1 
ATOM   4965 N  N     . VAL   A 1 768  ? -3.814  -9.164  -49.130 1.00 37.25  ? 917  VAL   A N     1 
ATOM   4966 C  CA    . VAL   A 1 768  ? -4.239  -8.598  -47.816 1.00 39.61  ? 917  VAL   A CA    1 
ATOM   4967 C  C     . VAL   A 1 768  ? -3.132  -8.863  -46.776 1.00 41.96  ? 917  VAL   A C     1 
ATOM   4968 O  O     . VAL   A 1 768  ? -2.923  -8.007  -45.884 1.00 41.00  ? 917  VAL   A O     1 
ATOM   4969 C  CB    . VAL   A 1 768  ? -5.599  -9.164  -47.373 1.00 38.66  ? 917  VAL   A CB    1 
ATOM   4970 C  CG1   . VAL   A 1 768  ? -5.855  -8.980  -45.883 1.00 38.84  ? 917  VAL   A CG1   1 
ATOM   4971 C  CG2   . VAL   A 1 768  ? -6.740  -8.575  -48.182 1.00 37.77  ? 917  VAL   A CG2   1 
ATOM   4972 N  N     . ALA   A 1 769  ? -2.473  -10.021 -46.847 1.00 40.47  ? 918  ALA   A N     1 
ATOM   4973 C  CA    . ALA   A 1 769  ? -1.355  -10.378 -45.945 1.00 43.61  ? 918  ALA   A CA    1 
ATOM   4974 C  C     . ALA   A 1 769  ? -0.275  -9.291  -46.071 1.00 41.97  ? 918  ALA   A C     1 
ATOM   4975 O  O     . ALA   A 1 769  ? 0.162   -8.755  -45.041 1.00 41.93  ? 918  ALA   A O     1 
ATOM   4976 C  CB    . ALA   A 1 769  ? -0.829  -11.761 -46.269 1.00 42.21  ? 918  ALA   A CB    1 
ATOM   4977 N  N     . LEU   A 1 770  ? 0.074   -8.937  -47.304 1.00 37.60  ? 919  LEU   A N     1 
ATOM   4978 C  CA    . LEU   A 1 770  ? 1.075   -7.896  -47.635 1.00 41.52  ? 919  LEU   A CA    1 
ATOM   4979 C  C     . LEU   A 1 770  ? 0.657   -6.532  -47.069 1.00 41.24  ? 919  LEU   A C     1 
ATOM   4980 O  O     . LEU   A 1 770  ? 1.487   -5.885  -46.422 1.00 40.94  ? 919  LEU   A O     1 
ATOM   4981 C  CB    . LEU   A 1 770  ? 1.198   -7.835  -49.153 1.00 46.20  ? 919  LEU   A CB    1 
ATOM   4982 C  CG    . LEU   A 1 770  ? 2.168   -6.781  -49.679 1.00 53.09  ? 919  LEU   A CG    1 
ATOM   4983 C  CD1   . LEU   A 1 770  ? 3.587   -7.327  -49.683 1.00 58.09  ? 919  LEU   A CD1   1 
ATOM   4984 C  CD2   . LEU   A 1 770  ? 1.757   -6.325  -51.069 1.00 53.22  ? 919  LEU   A CD2   1 
ATOM   4985 N  N     . LEU   A 1 771  ? -0.566  -6.077  -47.343 1.00 39.39  ? 920  LEU   A N     1 
ATOM   4986 C  CA    . LEU   A 1 771  ? -1.056  -4.782  -46.820 1.00 39.18  ? 920  LEU   A CA    1 
ATOM   4987 C  C     . LEU   A 1 771  ? -0.992  -4.792  -45.287 1.00 41.09  ? 920  LEU   A C     1 
ATOM   4988 O  O     . LEU   A 1 771  ? -0.560  -3.775  -44.725 1.00 46.31  ? 920  LEU   A O     1 
ATOM   4989 C  CB    . LEU   A 1 771  ? -2.469  -4.514  -47.338 1.00 40.08  ? 920  LEU   A CB    1 
ATOM   4990 C  CG    . LEU   A 1 771  ? -2.543  -4.133  -48.810 1.00 41.64  ? 920  LEU   A CG    1 
ATOM   4991 C  CD1   . LEU   A 1 771  ? -3.986  -3.897  -49.233 1.00 42.99  ? 920  LEU   A CD1   1 
ATOM   4992 C  CD2   . LEU   A 1 771  ? -1.690  -2.906  -49.086 1.00 41.08  ? 920  LEU   A CD2   1 
ATOM   4993 N  N     . SER   A 1 772  ? -1.393  -5.883  -44.629 1.00 39.82  ? 921  SER   A N     1 
ATOM   4994 C  CA    . SER   A 1 772  ? -1.352  -6.028  -43.147 1.00 38.49  ? 921  SER   A CA    1 
ATOM   4995 C  C     . SER   A 1 772  ? 0.104   -5.987  -42.629 1.00 38.68  ? 921  SER   A C     1 
ATOM   4996 O  O     . SER   A 1 772  ? 0.371   -5.278  -41.632 1.00 40.34  ? 921  SER   A O     1 
ATOM   4997 C  CB    . SER   A 1 772  ? -2.112  -7.258  -42.715 1.00 41.36  ? 921  SER   A CB    1 
ATOM   4998 O  OG    . SER   A 1 772  ? -3.449  -7.271  -43.265 1.00 40.79  ? 921  SER   A OG    1 
ATOM   4999 N  N     . VAL   A 1 773  ? 1.051   -6.607  -43.324 1.00 39.20  ? 922  VAL   A N     1 
ATOM   5000 C  CA    . VAL   A 1 773  ? 2.512   -6.502  -43.003 1.00 45.64  ? 922  VAL   A CA    1 
ATOM   5001 C  C     . VAL   A 1 773  ? 2.947   -5.033  -43.045 1.00 46.80  ? 922  VAL   A C     1 
ATOM   5002 O  O     . VAL   A 1 773  ? 3.591   -4.592  -42.071 1.00 48.62  ? 922  VAL   A O     1 
ATOM   5003 C  CB    . VAL   A 1 773  ? 3.371   -7.369  -43.945 1.00 45.33  ? 922  VAL   A CB    1 
ATOM   5004 C  CG1   . VAL   A 1 773  ? 4.821   -6.969  -43.941 1.00 45.51  ? 922  VAL   A CG1   1 
ATOM   5005 C  CG2   . VAL   A 1 773  ? 3.242   -8.828  -43.579 1.00 50.37  ? 922  VAL   A CG2   1 
ATOM   5006 N  N     . PHE   A 1 774  ? 2.626   -4.307  -44.120 1.00 46.40  ? 923  PHE   A N     1 
ATOM   5007 C  CA    . PHE   A 1 774  ? 3.027   -2.882  -44.284 1.00 49.64  ? 923  PHE   A CA    1 
ATOM   5008 C  C     . PHE   A 1 774  ? 2.402   -2.000  -43.206 1.00 43.85  ? 923  PHE   A C     1 
ATOM   5009 O  O     . PHE   A 1 774  ? 3.096   -1.110  -42.764 1.00 44.12  ? 923  PHE   A O     1 
ATOM   5010 C  CB    . PHE   A 1 774  ? 2.701   -2.325  -45.667 1.00 48.49  ? 923  PHE   A CB    1 
ATOM   5011 C  CG    . PHE   A 1 774  ? 3.818   -2.617  -46.619 1.00 46.12  ? 923  PHE   A CG    1 
ATOM   5012 C  CD1   . PHE   A 1 774  ? 4.964   -1.848  -46.603 1.00 48.43  ? 923  PHE   A CD1   1 
ATOM   5013 C  CD2   . PHE   A 1 774  ? 3.762   -3.724  -47.450 1.00 49.73  ? 923  PHE   A CD2   1 
ATOM   5014 C  CE1   . PHE   A 1 774  ? 6.023   -2.160  -47.443 1.00 51.19  ? 923  PHE   A CE1   1 
ATOM   5015 C  CE2   . PHE   A 1 774  ? 4.808   -4.022  -48.307 1.00 47.06  ? 923  PHE   A CE2   1 
ATOM   5016 C  CZ    . PHE   A 1 774  ? 5.938   -3.239  -48.297 1.00 52.11  ? 923  PHE   A CZ    1 
ATOM   5017 N  N     . GLN   A 1 775  ? 1.163   -2.246  -42.799 1.00 43.21  ? 924  GLN   A N     1 
ATOM   5018 C  CA    . GLN   A 1 775  ? 0.515   -1.456  -41.724 1.00 45.50  ? 924  GLN   A CA    1 
ATOM   5019 C  C     . GLN   A 1 775  ? 1.251   -1.720  -40.395 1.00 45.23  ? 924  GLN   A C     1 
ATOM   5020 O  O     . GLN   A 1 775  ? 1.621   -0.749  -39.748 1.00 45.99  ? 924  GLN   A O     1 
ATOM   5021 C  CB    . GLN   A 1 775  ? -0.967  -1.799  -41.646 1.00 45.89  ? 924  GLN   A CB    1 
ATOM   5022 C  CG    . GLN   A 1 775  ? -1.742  -0.983  -40.632 1.00 48.19  ? 924  GLN   A CG    1 
ATOM   5023 C  CD    . GLN   A 1 775  ? -3.225  -1.177  -40.843 1.00 55.59  ? 924  GLN   A CD    1 
ATOM   5024 O  OE1   . GLN   A 1 775  ? -3.902  -0.362  -41.471 1.00 63.94  ? 924  GLN   A OE1   1 
ATOM   5025 N  NE2   . GLN   A 1 775  ? -3.737  -2.290  -40.353 1.00 54.46  ? 924  GLN   A NE2   1 
ATOM   5026 N  N     . ALA   A 1 776  ? 1.515   -2.981  -40.037 1.00 42.14  ? 925  ALA   A N     1 
ATOM   5027 C  CA    . ALA   A 1 776  ? 2.169   -3.361  -38.761 1.00 41.54  ? 925  ALA   A CA    1 
ATOM   5028 C  C     . ALA   A 1 776  ? 3.600   -2.794  -38.714 1.00 41.94  ? 925  ALA   A C     1 
ATOM   5029 O  O     . ALA   A 1 776  ? 3.944   -2.151  -37.717 1.00 42.78  ? 925  ALA   A O     1 
ATOM   5030 C  CB    . ALA   A 1 776  ? 2.140   -4.856  -38.593 1.00 40.73  ? 925  ALA   A CB    1 
ATOM   5031 N  N     . TRP   A 1 777  ? 4.376   -2.985  -39.777 1.00 40.24  ? 926  TRP   A N     1 
ATOM   5032 C  CA    . TRP   A 1 777  ? 5.773   -2.501  -39.930 1.00 42.04  ? 926  TRP   A CA    1 
ATOM   5033 C  C     . TRP   A 1 777  ? 5.844   -0.977  -39.790 1.00 45.02  ? 926  TRP   A C     1 
ATOM   5034 O  O     . TRP   A 1 777  ? 6.712   -0.497  -39.060 1.00 47.89  ? 926  TRP   A O     1 
ATOM   5035 C  CB    . TRP   A 1 777  ? 6.333   -2.947  -41.279 1.00 41.48  ? 926  TRP   A CB    1 
ATOM   5036 C  CG    . TRP   A 1 777  ? 7.580   -2.236  -41.685 1.00 39.71  ? 926  TRP   A CG    1 
ATOM   5037 C  CD1   . TRP   A 1 777  ? 8.839   -2.497  -41.243 1.00 41.35  ? 926  TRP   A CD1   1 
ATOM   5038 C  CD2   . TRP   A 1 777  ? 7.718   -1.199  -42.672 1.00 42.09  ? 926  TRP   A CD2   1 
ATOM   5039 N  NE1   . TRP   A 1 777  ? 9.746   -1.677  -41.863 1.00 39.52  ? 926  TRP   A NE1   1 
ATOM   5040 C  CE2   . TRP   A 1 777  ? 9.091   -0.862  -42.736 1.00 39.49  ? 926  TRP   A CE2   1 
ATOM   5041 C  CE3   . TRP   A 1 777  ? 6.826   -0.508  -43.492 1.00 41.96  ? 926  TRP   A CE3   1 
ATOM   5042 C  CZ2   . TRP   A 1 777  ? 9.587   0.123   -43.584 1.00 39.24  ? 926  TRP   A CZ2   1 
ATOM   5043 C  CZ3   . TRP   A 1 777  ? 7.313   0.485   -44.313 1.00 40.08  ? 926  TRP   A CZ3   1 
ATOM   5044 C  CH2   . TRP   A 1 777  ? 8.673   0.800   -44.353 1.00 40.47  ? 926  TRP   A CH2   1 
ATOM   5045 N  N     . ASP   A 1 778  ? 4.966   -0.241  -40.465 1.00 48.17  ? 927  ASP   A N     1 
ATOM   5046 C  CA    . ASP   A 1 778  ? 4.927   1.244   -40.408 1.00 48.38  ? 927  ASP   A CA    1 
ATOM   5047 C  C     . ASP   A 1 778  ? 4.567   1.693   -38.976 1.00 46.21  ? 927  ASP   A C     1 
ATOM   5048 O  O     . ASP   A 1 778  ? 5.153   2.664   -38.516 1.00 47.37  ? 927  ASP   A O     1 
ATOM   5049 C  CB    . ASP   A 1 778  ? 3.986   1.795   -41.482 1.00 49.63  ? 927  ASP   A CB    1 
ATOM   5050 C  CG    . ASP   A 1 778  ? 4.142   3.281   -41.734 1.00 52.98  ? 927  ASP   A CG    1 
ATOM   5051 O  OD1   . ASP   A 1 778  ? 5.277   3.726   -41.960 1.00 51.05  ? 927  ASP   A OD1   1 
ATOM   5052 O  OD2   . ASP   A 1 778  ? 3.125   3.976   -41.708 1.00 67.21  ? 927  ASP   A OD2   1 
ATOM   5053 N  N     . ASP   A 1 779  ? 3.658   1.004   -38.284 1.00 45.36  ? 928  ASP   A N     1 
ATOM   5054 C  CA    . ASP   A 1 779  ? 3.386   1.208   -36.833 1.00 52.90  ? 928  ASP   A CA    1 
ATOM   5055 C  C     . ASP   A 1 779  ? 4.679   0.964   -36.006 1.00 54.51  ? 928  ASP   A C     1 
ATOM   5056 O  O     . ASP   A 1 779  ? 5.086   1.880   -35.272 1.00 55.66  ? 928  ASP   A O     1 
ATOM   5057 C  CB    . ASP   A 1 779  ? 2.165   0.379   -36.421 1.00 60.63  ? 928  ASP   A CB    1 
ATOM   5058 C  CG    . ASP   A 1 779  ? 1.811   0.424   -34.938 1.00 72.67  ? 928  ASP   A CG    1 
ATOM   5059 O  OD1   . ASP   A 1 779  ? 1.471   1.520   -34.441 1.00 78.80  ? 928  ASP   A OD1   1 
ATOM   5060 O  OD2   . ASP   A 1 779  ? 1.852   -0.650  -34.291 1.00 75.13  ? 928  ASP   A OD2   1 
ATOM   5061 N  N     . ALA   A 1 780  ? 5.357   -0.184  -36.125 1.00 52.99  ? 929  ALA   A N     1 
ATOM   5062 C  CA    . ALA   A 1 780  ? 6.552   -0.527  -35.302 1.00 54.06  ? 929  ALA   A CA    1 
ATOM   5063 C  C     . ALA   A 1 780  ? 7.725   0.428   -35.578 1.00 52.18  ? 929  ALA   A C     1 
ATOM   5064 O  O     . ALA   A 1 780  ? 8.537   0.586   -34.674 1.00 54.97  ? 929  ALA   A O     1 
ATOM   5065 C  CB    . ALA   A 1 780  ? 6.974   -1.958  -35.524 1.00 56.45  ? 929  ALA   A CB    1 
ATOM   5066 N  N     . ARG   A 1 781  ? 7.815   1.005   -36.779 1.00 51.02  ? 930  ARG   A N     1 
ATOM   5067 C  CA    . ARG   A 1 781  ? 8.840   2.003   -37.200 1.00 50.58  ? 930  ARG   A CA    1 
ATOM   5068 C  C     . ARG   A 1 781  ? 8.772   3.312   -36.390 1.00 49.55  ? 930  ARG   A C     1 
ATOM   5069 O  O     . ARG   A 1 781  ? 9.782   4.029   -36.369 1.00 47.61  ? 930  ARG   A O     1 
ATOM   5070 C  CB    . ARG   A 1 781  ? 8.618   2.421   -38.652 1.00 54.31  ? 930  ARG   A CB    1 
ATOM   5071 C  CG    . ARG   A 1 781  ? 9.326   1.552   -39.672 1.00 63.17  ? 930  ARG   A CG    1 
ATOM   5072 C  CD    . ARG   A 1 781  ? 9.557   2.326   -40.950 1.00 67.61  ? 930  ARG   A CD    1 
ATOM   5073 N  NE    . ARG   A 1 781  ? 8.401   3.080   -41.421 1.00 66.63  ? 930  ARG   A NE    1 
ATOM   5074 C  CZ    . ARG   A 1 781  ? 8.434   3.881   -42.482 1.00 68.64  ? 930  ARG   A CZ    1 
ATOM   5075 N  NH1   . ARG   A 1 781  ? 7.353   4.545   -42.849 1.00 66.23  ? 930  ARG   A NH1   1 
ATOM   5076 N  NH2   . ARG   A 1 781  ? 9.550   4.007   -43.183 1.00 67.94  ? 930  ARG   A NH2   1 
ATOM   5077 N  N     . MET   A 1 782  ? 7.633   3.665   -35.799 1.00 53.91  ? 931  MET   A N     1 
ATOM   5078 C  CA    . MET   A 1 782  ? 7.514   4.908   -34.975 1.00 64.14  ? 931  MET   A CA    1 
ATOM   5079 C  C     . MET   A 1 782  ? 8.524   4.856   -33.815 1.00 66.10  ? 931  MET   A C     1 
ATOM   5080 O  O     . MET   A 1 782  ? 9.107   5.918   -33.503 1.00 70.14  ? 931  MET   A O     1 
ATOM   5081 C  CB    . MET   A 1 782  ? 6.101   5.097   -34.414 1.00 70.03  ? 931  MET   A CB    1 
ATOM   5082 C  CG    . MET   A 1 782  ? 5.018   4.960   -35.472 1.00 79.65  ? 931  MET   A CG    1 
ATOM   5083 S  SD    . MET   A 1 782  ? 3.677   6.146   -35.296 1.00 91.53  ? 931  MET   A SD    1 
ATOM   5084 C  CE    . MET   A 1 782  ? 4.079   7.235   -36.663 1.00 91.65  ? 931  MET   A CE    1 
ATOM   5085 N  N     . GLY   A 1 783  ? 8.760   3.663   -33.246 1.00 58.49  ? 932  GLY   A N     1 
ATOM   5086 C  CA    . GLY   A 1 783  ? 9.715   3.411   -32.146 1.00 58.60  ? 932  GLY   A CA    1 
ATOM   5087 C  C     . GLY   A 1 783  ? 11.180  3.608   -32.533 1.00 55.28  ? 932  GLY   A C     1 
ATOM   5088 O  O     . GLY   A 1 783  ? 12.033  3.565   -31.635 1.00 61.78  ? 932  GLY   A O     1 
ATOM   5089 N  N     . GLY   A 1 784  ? 11.496  3.808   -33.808 1.00 50.61  ? 933  GLY   A N     1 
ATOM   5090 C  CA    . GLY   A 1 784  ? 12.889  4.016   -34.256 1.00 49.41  ? 933  GLY   A CA    1 
ATOM   5091 C  C     . GLY   A 1 784  ? 13.467  2.768   -34.899 1.00 49.94  ? 933  GLY   A C     1 
ATOM   5092 O  O     . GLY   A 1 784  ? 12.744  1.744   -34.983 1.00 47.94  ? 933  GLY   A O     1 
ATOM   5093 N  N     . GLU   A 1 785  ? 14.731  2.853   -35.317 1.00 51.46  ? 934  GLU   A N     1 
ATOM   5094 C  CA    . GLU   A 1 785  ? 15.453  1.827   -36.114 1.00 58.90  ? 934  GLU   A CA    1 
ATOM   5095 C  C     . GLU   A 1 785  ? 15.467  0.479   -35.381 1.00 62.83  ? 934  GLU   A C     1 
ATOM   5096 O  O     . GLU   A 1 785  ? 15.178  -0.550  -36.029 1.00 67.61  ? 934  GLU   A O     1 
ATOM   5097 C  CB    . GLU   A 1 785  ? 16.876  2.291   -36.417 1.00 63.58  ? 934  GLU   A CB    1 
ATOM   5098 C  CG    . GLU   A 1 785  ? 17.734  1.189   -36.996 1.00 73.09  ? 934  GLU   A CG    1 
ATOM   5099 C  CD    . GLU   A 1 785  ? 18.594  1.603   -38.167 1.00 75.98  ? 934  GLU   A CD    1 
ATOM   5100 O  OE1   . GLU   A 1 785  ? 19.805  1.294   -38.139 1.00 80.29  ? 934  GLU   A OE1   1 
ATOM   5101 O  OE2   . GLU   A 1 785  ? 18.038  2.211   -39.105 1.00 75.34  ? 934  GLU   A OE2   1 
ATOM   5102 N  N     . GLU   A 1 786  ? 15.801  0.465   -34.092 1.00 58.30  ? 935  GLU   A N     1 
ATOM   5103 C  CA    . GLU   A 1 786  ? 15.980  -0.803  -33.343 1.00 56.08  ? 935  GLU   A CA    1 
ATOM   5104 C  C     . GLU   A 1 786  ? 14.606  -1.470  -33.176 1.00 54.62  ? 935  GLU   A C     1 
ATOM   5105 O  O     . GLU   A 1 786  ? 14.542  -2.707  -33.302 1.00 50.68  ? 935  GLU   A O     1 
ATOM   5106 C  CB    . GLU   A 1 786  ? 16.715  -0.558  -32.024 1.00 59.72  ? 935  GLU   A CB    1 
ATOM   5107 C  CG    . GLU   A 1 786  ? 17.315  -1.811  -31.415 1.00 68.52  ? 935  GLU   A CG    1 
ATOM   5108 C  CD    . GLU   A 1 786  ? 18.407  -2.486  -32.232 1.00 72.16  ? 935  GLU   A CD    1 
ATOM   5109 O  OE1   . GLU   A 1 786  ? 19.088  -1.766  -33.011 1.00 70.86  ? 935  GLU   A OE1   1 
ATOM   5110 O  OE2   . GLU   A 1 786  ? 18.562  -3.735  -32.095 1.00 70.46  ? 935  GLU   A OE2   1 
ATOM   5111 N  N     . ALA   A 1 787  ? 13.539  -0.699  -32.937 1.00 48.78  ? 936  ALA   A N     1 
ATOM   5112 C  CA    . ALA   A 1 787  ? 12.164  -1.241  -32.834 1.00 48.62  ? 936  ALA   A CA    1 
ATOM   5113 C  C     . ALA   A 1 787  ? 11.780  -1.881  -34.180 1.00 50.86  ? 936  ALA   A C     1 
ATOM   5114 O  O     . ALA   A 1 787  ? 11.069  -2.901  -34.163 1.00 48.19  ? 936  ALA   A O     1 
ATOM   5115 C  CB    . ALA   A 1 787  ? 11.176  -0.168  -32.433 1.00 45.57  ? 936  ALA   A CB    1 
ATOM   5116 N  N     . GLU   A 1 788  ? 12.239  -1.294  -35.289 1.00 46.56  ? 937  GLU   A N     1 
ATOM   5117 C  CA    . GLU   A 1 788  ? 11.915  -1.736  -36.658 1.00 50.96  ? 937  GLU   A CA    1 
ATOM   5118 C  C     . GLU   A 1 788  ? 12.654  -3.052  -36.885 1.00 49.32  ? 937  GLU   A C     1 
ATOM   5119 O  O     . GLU   A 1 788  ? 12.012  -3.995  -37.352 1.00 48.42  ? 937  GLU   A O     1 
ATOM   5120 C  CB    . GLU   A 1 788  ? 12.294  -0.678  -37.704 1.00 50.83  ? 937  GLU   A CB    1 
ATOM   5121 C  CG    . GLU   A 1 788  ? 11.996  -1.101  -39.143 1.00 48.75  ? 937  GLU   A CG    1 
ATOM   5122 C  CD    . GLU   A 1 788  ? 12.505  -0.137  -40.209 1.00 52.63  ? 937  GLU   A CD    1 
ATOM   5123 O  OE1   . GLU   A 1 788  ? 13.107  0.913   -39.844 1.00 52.51  ? 937  GLU   A OE1   1 
ATOM   5124 O  OE2   . GLU   A 1 788  ? 12.331  -0.438  -41.407 1.00 45.38  ? 937  GLU   A OE2   1 
ATOM   5125 N  N     . ILE   A 1 789  ? 13.945  -3.098  -36.557 1.00 50.84  ? 938  ILE   A N     1 
ATOM   5126 C  CA    . ILE   A 1 789  ? 14.798  -4.303  -36.776 1.00 52.13  ? 938  ILE   A CA    1 
ATOM   5127 C  C     . ILE   A 1 789  ? 14.203  -5.464  -35.973 1.00 49.59  ? 938  ILE   A C     1 
ATOM   5128 O  O     . ILE   A 1 789  ? 14.061  -6.569  -36.537 1.00 47.63  ? 938  ILE   A O     1 
ATOM   5129 C  CB    . ILE   A 1 789  ? 16.276  -4.035  -36.425 1.00 51.23  ? 938  ILE   A CB    1 
ATOM   5130 C  CG1   . ILE   A 1 789  ? 16.904  -3.046  -37.415 1.00 48.40  ? 938  ILE   A CG1   1 
ATOM   5131 C  CG2   . ILE   A 1 789  ? 17.062  -5.347  -36.364 1.00 48.95  ? 938  ILE   A CG2   1 
ATOM   5132 C  CD1   . ILE   A 1 789  ? 18.198  -2.409  -36.939 1.00 47.79  ? 938  ILE   A CD1   1 
ATOM   5133 N  N     . ARG   A 1 790  ? 13.849  -5.213  -34.717 1.00 47.14  ? 939  ARG   A N     1 
ATOM   5134 C  CA    . ARG   A 1 790  ? 13.312  -6.254  -33.811 1.00 51.96  ? 939  ARG   A CA    1 
ATOM   5135 C  C     . ARG   A 1 790  ? 11.981  -6.765  -34.351 1.00 50.79  ? 939  ARG   A C     1 
ATOM   5136 O  O     . ARG   A 1 790  ? 11.746  -7.974  -34.281 1.00 54.12  ? 939  ARG   A O     1 
ATOM   5137 C  CB    . ARG   A 1 790  ? 13.169  -5.723  -32.386 1.00 54.57  ? 939  ARG   A CB    1 
ATOM   5138 C  CG    . ARG   A 1 790  ? 14.515  -5.484  -31.721 1.00 57.02  ? 939  ARG   A CG    1 
ATOM   5139 C  CD    . ARG   A 1 790  ? 14.430  -5.347  -30.212 1.00 58.07  ? 939  ARG   A CD    1 
ATOM   5140 N  NE    . ARG   A 1 790  ? 15.785  -5.277  -29.688 1.00 64.14  ? 939  ARG   A NE    1 
ATOM   5141 C  CZ    . ARG   A 1 790  ? 16.094  -5.161  -28.408 1.00 61.38  ? 939  ARG   A CZ    1 
ATOM   5142 N  NH1   . ARG   A 1 790  ? 15.134  -5.112  -27.501 1.00 57.58  ? 939  ARG   A NH1   1 
ATOM   5143 N  NH2   . ARG   A 1 790  ? 17.364  -5.104  -28.047 1.00 62.05  ? 939  ARG   A NH2   1 
ATOM   5144 N  N     . PHE   A 1 791  ? 11.142  -5.869  -34.856 1.00 51.93  ? 940  PHE   A N     1 
ATOM   5145 C  CA    . PHE   A 1 791  ? 9.831   -6.228  -35.439 1.00 46.44  ? 940  PHE   A CA    1 
ATOM   5146 C  C     . PHE   A 1 791  ? 10.074  -7.212  -36.589 1.00 42.11  ? 940  PHE   A C     1 
ATOM   5147 O  O     . PHE   A 1 791  ? 9.446   -8.247  -36.648 1.00 41.49  ? 940  PHE   A O     1 
ATOM   5148 C  CB    . PHE   A 1 791  ? 9.068   -4.986  -35.893 1.00 45.55  ? 940  PHE   A CB    1 
ATOM   5149 C  CG    . PHE   A 1 791  ? 7.761   -5.337  -36.550 1.00 46.01  ? 940  PHE   A CG    1 
ATOM   5150 C  CD1   . PHE   A 1 791  ? 6.681   -5.746  -35.781 1.00 46.52  ? 940  PHE   A CD1   1 
ATOM   5151 C  CD2   . PHE   A 1 791  ? 7.643   -5.334  -37.927 1.00 41.96  ? 940  PHE   A CD2   1 
ATOM   5152 C  CE1   . PHE   A 1 791  ? 5.492   -6.125  -36.382 1.00 44.30  ? 940  PHE   A CE1   1 
ATOM   5153 C  CE2   . PHE   A 1 791  ? 6.450   -5.699  -38.526 1.00 46.09  ? 940  PHE   A CE2   1 
ATOM   5154 C  CZ    . PHE   A 1 791  ? 5.379   -6.094  -37.754 1.00 45.76  ? 940  PHE   A CZ    1 
ATOM   5155 N  N     . CYS   A 1 792  ? 11.025  -6.907  -37.451 1.00 43.85  ? 941  CYS   A N     1 
ATOM   5156 C  CA    . CYS   A 1 792  ? 11.308  -7.674  -38.682 1.00 50.61  ? 941  CYS   A CA    1 
ATOM   5157 C  C     . CYS   A 1 792  ? 11.966  -9.025  -38.338 1.00 54.35  ? 941  CYS   A C     1 
ATOM   5158 O  O     . CYS   A 1 792  ? 11.739  -10.002 -39.078 1.00 53.33  ? 941  CYS   A O     1 
ATOM   5159 C  CB    . CYS   A 1 792  ? 12.146  -6.819  -39.622 1.00 49.16  ? 941  CYS   A CB    1 
ATOM   5160 S  SG    . CYS   A 1 792  ? 11.216  -5.427  -40.318 1.00 52.37  ? 941  CYS   A SG    1 
ATOM   5161 N  N     . GLU   A 1 793  ? 12.732  -9.097  -37.253 1.00 55.46  ? 942  GLU   A N     1 
ATOM   5162 C  CA    . GLU   A 1 793  ? 13.412  -10.346 -36.825 1.00 55.49  ? 942  GLU   A CA    1 
ATOM   5163 C  C     . GLU   A 1 793  ? 12.380  -11.284 -36.179 1.00 49.86  ? 942  GLU   A C     1 
ATOM   5164 O  O     . GLU   A 1 793  ? 12.371  -12.465 -36.524 1.00 47.99  ? 942  GLU   A O     1 
ATOM   5165 C  CB    . GLU   A 1 793  ? 14.591  -10.029 -35.896 1.00 61.50  ? 942  GLU   A CB    1 
ATOM   5166 C  CG    . GLU   A 1 793  ? 15.868  -9.640  -36.632 1.00 62.81  ? 942  GLU   A CG    1 
ATOM   5167 C  CD    . GLU   A 1 793  ? 17.055  -9.292  -35.737 1.00 68.86  ? 942  GLU   A CD    1 
ATOM   5168 O  OE1   . GLU   A 1 793  ? 16.929  -9.379  -34.492 1.00 62.89  ? 942  GLU   A OE1   1 
ATOM   5169 O  OE2   . GLU   A 1 793  ? 18.109  -8.918  -36.288 1.00 69.79  ? 942  GLU   A OE2   1 
ATOM   5170 N  N     A HIS   A 1 794  ? 11.517  -10.763 -35.304 0.50 47.66  ? 943  HIS   A N     1 
ATOM   5171 N  N     B HIS   A 1 794  ? 11.565  -10.761 -35.257 0.50 49.07  ? 943  HIS   A N     1 
ATOM   5172 C  CA    A HIS   A 1 794  ? 10.483  -11.542 -34.568 0.50 48.72  ? 943  HIS   A CA    1 
ATOM   5173 C  CA    B HIS   A 1 794  ? 10.469  -11.493 -34.567 0.50 51.10  ? 943  HIS   A CA    1 
ATOM   5174 C  C     A HIS   A 1 794  ? 9.410   -12.085 -35.522 0.50 51.56  ? 943  HIS   A C     1 
ATOM   5175 C  C     B HIS   A 1 794  ? 9.544   -12.143 -35.606 0.50 53.11  ? 943  HIS   A C     1 
ATOM   5176 O  O     A HIS   A 1 794  ? 8.810   -13.132 -35.185 0.50 52.47  ? 943  HIS   A O     1 
ATOM   5177 O  O     B HIS   A 1 794  ? 9.241   -13.342 -35.450 0.50 56.07  ? 943  HIS   A O     1 
ATOM   5178 C  CB    A HIS   A 1 794  ? 9.837   -10.698 -33.460 0.50 47.85  ? 943  HIS   A CB    1 
ATOM   5179 C  CB    B HIS   A 1 794  ? 9.654   -10.567 -33.646 0.50 51.28  ? 943  HIS   A CB    1 
ATOM   5180 C  CG    A HIS   A 1 794  ? 8.729   -11.390 -32.734 0.50 48.04  ? 943  HIS   A CG    1 
ATOM   5181 C  CG    B HIS   A 1 794  ? 10.236  -10.338 -32.287 0.50 55.33  ? 943  HIS   A CG    1 
ATOM   5182 N  ND1   A HIS   A 1 794  ? 7.623   -10.713 -32.256 0.50 51.66  ? 943  HIS   A ND1   1 
ATOM   5183 N  ND1   B HIS   A 1 794  ? 10.454  -11.363 -31.387 0.50 56.58  ? 943  HIS   A ND1   1 
ATOM   5184 C  CD2   A HIS   A 1 794  ? 8.547   -12.689 -32.404 0.50 50.43  ? 943  HIS   A CD2   1 
ATOM   5185 C  CD2   B HIS   A 1 794  ? 10.599  -9.200  -31.653 0.50 54.23  ? 943  HIS   A CD2   1 
ATOM   5186 C  CE1   A HIS   A 1 794  ? 6.806   -11.560 -31.655 0.50 50.68  ? 943  HIS   A CE1   1 
ATOM   5187 C  CE1   B HIS   A 1 794  ? 10.957  -10.864 -30.276 0.50 55.35  ? 943  HIS   A CE1   1 
ATOM   5188 N  NE2   A HIS   A 1 794  ? 7.348   -12.781 -31.739 0.50 52.81  ? 943  HIS   A NE2   1 
ATOM   5189 N  NE2   B HIS   A 1 794  ? 11.053  -9.541  -30.414 0.50 51.42  ? 943  HIS   A NE2   1 
ATOM   5190 N  N     . LYS   A 1 795  ? 9.130   -11.378 -36.622 1.00 50.18  ? 944  LYS   A N     1 
ATOM   5191 C  CA    . LYS   A 1 795  ? 8.097   -11.778 -37.613 1.00 50.95  ? 944  LYS   A CA    1 
ATOM   5192 C  C     . LYS   A 1 795  ? 8.741   -12.407 -38.854 1.00 47.67  ? 944  LYS   A C     1 
ATOM   5193 O  O     . LYS   A 1 795  ? 7.990   -12.725 -39.782 1.00 46.30  ? 944  LYS   A O     1 
ATOM   5194 C  CB    . LYS   A 1 795  ? 7.267   -10.560 -38.037 1.00 53.53  ? 944  LYS   A CB    1 
ATOM   5195 C  CG    . LYS   A 1 795  ? 6.560   -9.819  -36.912 1.00 53.93  ? 944  LYS   A CG    1 
ATOM   5196 C  CD    . LYS   A 1 795  ? 5.548   -10.654 -36.187 1.00 58.19  ? 944  LYS   A CD    1 
ATOM   5197 C  CE    . LYS   A 1 795  ? 5.057   -9.976  -34.932 1.00 63.65  ? 944  LYS   A CE    1 
ATOM   5198 N  NZ    . LYS   A 1 795  ? 3.747   -10.530 -34.533 1.00 70.97  ? 944  LYS   A NZ    1 
ATOM   5199 N  N     . ARG   A 1 796  ? 10.070  -12.517 -38.911 1.00 46.36  ? 945  ARG   A N     1 
ATOM   5200 C  CA    . ARG   A 1 796  ? 10.798  -13.127 -40.061 1.00 47.94  ? 945  ARG   A CA    1 
ATOM   5201 C  C     . ARG   A 1 796  ? 10.413  -12.366 -41.341 1.00 47.28  ? 945  ARG   A C     1 
ATOM   5202 O  O     . ARG   A 1 796  ? 9.778   -12.954 -42.241 1.00 52.31  ? 945  ARG   A O     1 
ATOM   5203 C  CB    . ARG   A 1 796  ? 10.511  -14.637 -40.097 1.00 53.47  ? 945  ARG   A CB    1 
ATOM   5204 C  CG    . ARG   A 1 796  ? 10.609  -15.303 -38.724 1.00 62.34  ? 945  ARG   A CG    1 
ATOM   5205 C  CD    . ARG   A 1 796  ? 10.962  -16.788 -38.727 1.00 76.73  ? 945  ARG   A CD    1 
ATOM   5206 N  NE    . ARG   A 1 796  ? 9.889   -17.705 -39.138 1.00 86.52  ? 945  ARG   A NE    1 
ATOM   5207 C  CZ    . ARG   A 1 796  ? 9.857   -18.445 -40.262 1.00 90.89  ? 945  ARG   A CZ    1 
ATOM   5208 N  NH1   . ARG   A 1 796  ? 10.842  -18.412 -41.152 1.00 89.84  ? 945  ARG   A NH1   1 
ATOM   5209 N  NH2   . ARG   A 1 796  ? 8.816   -19.231 -40.491 1.00 85.14  ? 945  ARG   A NH2   1 
ATOM   5210 N  N     . LEU   A 1 797  ? 10.765  -11.081 -41.388 1.00 42.50  ? 946  LEU   A N     1 
ATOM   5211 C  CA    . LEU   A 1 797  ? 10.491  -10.158 -42.516 1.00 43.90  ? 946  LEU   A CA    1 
ATOM   5212 C  C     . LEU   A 1 797  ? 11.803  -9.546  -42.996 1.00 43.69  ? 946  LEU   A C     1 
ATOM   5213 O  O     . LEU   A 1 797  ? 12.635  -9.199  -42.172 1.00 48.35  ? 946  LEU   A O     1 
ATOM   5214 C  CB    . LEU   A 1 797  ? 9.539   -9.052  -42.056 1.00 42.76  ? 946  LEU   A CB    1 
ATOM   5215 C  CG    . LEU   A 1 797  ? 8.206   -9.519  -41.484 1.00 43.64  ? 946  LEU   A CG    1 
ATOM   5216 C  CD1   . LEU   A 1 797  ? 7.497   -8.362  -40.806 1.00 47.80  ? 946  LEU   A CD1   1 
ATOM   5217 C  CD2   . LEU   A 1 797  ? 7.326   -10.104 -42.573 1.00 44.17  ? 946  LEU   A CD2   1 
ATOM   5218 N  N     . ASN   A 1 798  ? 11.938  -9.368  -44.297 1.00 44.90  ? 947  ASN   A N     1 
ATOM   5219 C  CA    . ASN   A 1 798  ? 13.102  -8.703  -44.917 1.00 46.25  ? 947  ASN   A CA    1 
ATOM   5220 C  C     . ASN   A 1 798  ? 12.880  -7.187  -44.868 1.00 48.69  ? 947  ASN   A C     1 
ATOM   5221 O  O     . ASN   A 1 798  ? 12.090  -6.687  -45.680 1.00 45.09  ? 947  ASN   A O     1 
ATOM   5222 C  CB    . ASN   A 1 798  ? 13.272  -9.218  -46.339 1.00 50.22  ? 947  ASN   A CB    1 
ATOM   5223 C  CG    . ASN   A 1 798  ? 14.501  -8.654  -47.001 1.00 52.68  ? 947  ASN   A CG    1 
ATOM   5224 O  OD1   . ASN   A 1 798  ? 14.874  -7.513  -46.745 1.00 54.47  ? 947  ASN   A OD1   1 
ATOM   5225 N  ND2   . ASN   A 1 798  ? 15.122  -9.451  -47.854 1.00 56.98  ? 947  ASN   A ND2   1 
ATOM   5226 N  N     . MET   A 1 799  ? 13.584  -6.491  -43.969 1.00 48.85  ? 948  MET   A N     1 
ATOM   5227 C  CA    . MET   A 1 799  ? 13.423  -5.038  -43.690 1.00 45.53  ? 948  MET   A CA    1 
ATOM   5228 C  C     . MET   A 1 799  ? 13.726  -4.217  -44.947 1.00 42.71  ? 948  MET   A C     1 
ATOM   5229 O  O     . MET   A 1 799  ? 12.958  -3.285  -45.246 1.00 41.91  ? 948  MET   A O     1 
ATOM   5230 C  CB    . MET   A 1 799  ? 14.362  -4.598  -42.568 1.00 47.86  ? 948  MET   A CB    1 
ATOM   5231 C  CG    . MET   A 1 799  ? 14.005  -3.259  -41.968 1.00 53.35  ? 948  MET   A CG    1 
ATOM   5232 S  SD    . MET   A 1 799  ? 15.009  -2.874  -40.514 1.00 53.45  ? 948  MET   A SD    1 
ATOM   5233 C  CE    . MET   A 1 799  ? 16.646  -2.892  -41.246 1.00 56.01  ? 948  MET   A CE    1 
ATOM   5234 N  N     . ALA   A 1 800  ? 14.819  -4.539  -45.633 1.00 41.88  ? 949  ALA   A N     1 
ATOM   5235 C  CA    . ALA   A 1 800  ? 15.290  -3.839  -46.847 1.00 43.32  ? 949  ALA   A CA    1 
ATOM   5236 C  C     . ALA   A 1 800  ? 14.190  -3.875  -47.912 1.00 43.04  ? 949  ALA   A C     1 
ATOM   5237 O  O     . ALA   A 1 800  ? 14.024  -2.860  -48.576 1.00 48.09  ? 949  ALA   A O     1 
ATOM   5238 C  CB    . ALA   A 1 800  ? 16.575  -4.447  -47.366 1.00 39.96  ? 949  ALA   A CB    1 
ATOM   5239 N  N     . THR   A 1 801  ? 13.483  -4.998  -48.068 1.00 42.06  ? 950  THR   A N     1 
ATOM   5240 C  CA    . THR   A 1 801  ? 12.355  -5.148  -49.025 1.00 42.68  ? 950  THR   A CA    1 
ATOM   5241 C  C     . THR   A 1 801  ? 11.197  -4.240  -48.608 1.00 39.14  ? 950  THR   A C     1 
ATOM   5242 O  O     . THR   A 1 801  ? 10.616  -3.568  -49.492 1.00 40.22  ? 950  THR   A O     1 
ATOM   5243 C  CB    . THR   A 1 801  ? 11.848  -6.592  -49.122 1.00 43.81  ? 950  THR   A CB    1 
ATOM   5244 O  OG1   . THR   A 1 801  ? 12.923  -7.402  -49.588 1.00 50.57  ? 950  THR   A OG1   1 
ATOM   5245 C  CG2   . THR   A 1 801  ? 10.689  -6.743  -50.080 1.00 44.78  ? 950  THR   A CG2   1 
ATOM   5246 N  N     . LEU   A 1 802  ? 10.839  -4.240  -47.328 1.00 37.31  ? 951  LEU   A N     1 
ATOM   5247 C  CA    . LEU   A 1 802  ? 9.747   -3.364  -46.824 1.00 42.06  ? 951  LEU   A CA    1 
ATOM   5248 C  C     . LEU   A 1 802  ? 10.120  -1.890  -47.083 1.00 43.34  ? 951  LEU   A C     1 
ATOM   5249 O  O     . LEU   A 1 802  ? 9.264   -1.146  -47.601 1.00 44.92  ? 951  LEU   A O     1 
ATOM   5250 C  CB    . LEU   A 1 802  ? 9.490   -3.654  -45.347 1.00 40.95  ? 951  LEU   A CB    1 
ATOM   5251 C  CG    . LEU   A 1 802  ? 8.929   -5.037  -45.036 1.00 42.69  ? 951  LEU   A CG    1 
ATOM   5252 C  CD1   . LEU   A 1 802  ? 8.782   -5.222  -43.535 1.00 44.09  ? 951  LEU   A CD1   1 
ATOM   5253 C  CD2   . LEU   A 1 802  ? 7.588   -5.264  -45.734 1.00 46.54  ? 951  LEU   A CD2   1 
ATOM   5254 N  N     . ARG   A 1 803  ? 11.375  -1.501  -46.863 1.00 39.81  ? 952  ARG   A N     1 
ATOM   5255 C  CA    . ARG   A 1 803  ? 11.812  -0.081  -47.000 1.00 41.05  ? 952  ARG   A CA    1 
ATOM   5256 C  C     . ARG   A 1 803  ? 11.846  0.351   -48.468 1.00 38.94  ? 952  ARG   A C     1 
ATOM   5257 O  O     . ARG   A 1 803  ? 11.384  1.468   -48.756 1.00 36.22  ? 952  ARG   A O     1 
ATOM   5258 C  CB    . ARG   A 1 803  ? 13.196  0.121   -46.381 1.00 45.09  ? 952  ARG   A CB    1 
ATOM   5259 C  CG    . ARG   A 1 803  ? 13.195  0.074   -44.864 1.00 47.87  ? 952  ARG   A CG    1 
ATOM   5260 C  CD    . ARG   A 1 803  ? 14.618  0.045   -44.349 1.00 50.23  ? 952  ARG   A CD    1 
ATOM   5261 N  NE    . ARG   A 1 803  ? 14.629  0.336   -42.925 1.00 55.26  ? 952  ARG   A NE    1 
ATOM   5262 C  CZ    . ARG   A 1 803  ? 15.721  0.582   -42.204 1.00 55.35  ? 952  ARG   A CZ    1 
ATOM   5263 N  NH1   . ARG   A 1 803  ? 16.913  0.532   -42.771 1.00 50.45  ? 952  ARG   A NH1   1 
ATOM   5264 N  NH2   . ARG   A 1 803  ? 15.614  0.873   -40.915 1.00 54.26  ? 952  ARG   A NH2   1 
ATOM   5265 N  N     . MET   A 1 804  ? 12.375  -0.489  -49.368 1.00 38.72  ? 953  MET   A N     1 
ATOM   5266 C  CA    . MET   A 1 804  ? 12.412  -0.199  -50.829 1.00 43.86  ? 953  MET   A CA    1 
ATOM   5267 C  C     . MET   A 1 804  ? 10.977  -0.125  -51.406 1.00 40.29  ? 953  MET   A C     1 
ATOM   5268 O  O     . MET   A 1 804  ? 10.709  0.775   -52.215 1.00 41.83  ? 953  MET   A O     1 
ATOM   5269 C  CB    . MET   A 1 804  ? 13.229  -1.255  -51.586 1.00 47.64  ? 953  MET   A CB    1 
ATOM   5270 C  CG    . MET   A 1 804  ? 14.713  -1.272  -51.246 1.00 51.18  ? 953  MET   A CG    1 
ATOM   5271 S  SD    . MET   A 1 804  ? 15.695  -2.402  -52.313 1.00 60.71  ? 953  MET   A SD    1 
ATOM   5272 C  CE    . MET   A 1 804  ? 14.912  -3.989  -52.041 1.00 62.85  ? 953  MET   A CE    1 
ATOM   5273 N  N     . THR   A 1 805  ? 10.082  -1.038  -51.034 1.00 37.99  ? 954  THR   A N     1 
ATOM   5274 C  CA    . THR   A 1 805  ? 8.655   -1.014  -51.461 1.00 40.68  ? 954  THR   A CA    1 
ATOM   5275 C  C     . THR   A 1 805  ? 7.999   0.307   -51.016 1.00 38.77  ? 954  THR   A C     1 
ATOM   5276 O  O     . THR   A 1 805  ? 7.312   0.960   -51.834 1.00 38.46  ? 954  THR   A O     1 
ATOM   5277 C  CB    . THR   A 1 805  ? 7.877   -2.199  -50.882 1.00 39.65  ? 954  THR   A CB    1 
ATOM   5278 O  OG1   . THR   A 1 805  ? 8.501   -3.420  -51.270 1.00 33.68  ? 954  THR   A OG1   1 
ATOM   5279 C  CG2   . THR   A 1 805  ? 6.431   -2.201  -51.324 1.00 41.81  ? 954  THR   A CG2   1 
ATOM   5280 N  N     . TRP   A 1 806  ? 8.202   0.714   -49.769 1.00 38.46  ? 955  TRP   A N     1 
ATOM   5281 C  CA    . TRP   A 1 806  ? 7.599   1.965   -49.237 1.00 40.49  ? 955  TRP   A CA    1 
ATOM   5282 C  C     . TRP   A 1 806  ? 8.093   3.146   -50.062 1.00 39.47  ? 955  TRP   A C     1 
ATOM   5283 O  O     . TRP   A 1 806  ? 7.266   3.934   -50.541 1.00 42.72  ? 955  TRP   A O     1 
ATOM   5284 C  CB    . TRP   A 1 806  ? 7.937   2.146   -47.767 1.00 43.34  ? 955  TRP   A CB    1 
ATOM   5285 C  CG    . TRP   A 1 806  ? 7.314   3.357   -47.162 1.00 43.23  ? 955  TRP   A CG    1 
ATOM   5286 C  CD1   . TRP   A 1 806  ? 7.855   4.602   -47.069 1.00 46.20  ? 955  TRP   A CD1   1 
ATOM   5287 C  CD2   . TRP   A 1 806  ? 6.029   3.423   -46.532 1.00 44.90  ? 955  TRP   A CD2   1 
ATOM   5288 N  NE1   . TRP   A 1 806  ? 6.985   5.445   -46.430 1.00 51.65  ? 955  TRP   A NE1   1 
ATOM   5289 C  CE2   . TRP   A 1 806  ? 5.864   4.745   -46.075 1.00 49.34  ? 955  TRP   A CE2   1 
ATOM   5290 C  CE3   . TRP   A 1 806  ? 5.011   2.494   -46.291 1.00 51.60  ? 955  TRP   A CE3   1 
ATOM   5291 C  CZ2   . TRP   A 1 806  ? 4.714   5.159   -45.396 1.00 56.84  ? 955  TRP   A CZ2   1 
ATOM   5292 C  CZ3   . TRP   A 1 806  ? 3.877   2.902   -45.617 1.00 55.21  ? 955  TRP   A CZ3   1 
ATOM   5293 C  CH2   . TRP   A 1 806  ? 3.730   4.220   -45.175 1.00 52.00  ? 955  TRP   A CH2   1 
ATOM   5294 N  N     . GLU   A 1 807  ? 9.404   3.225   -50.252 1.00 41.81  ? 956  GLU   A N     1 
ATOM   5295 C  CA    . GLU   A 1 807  ? 10.038  4.283   -51.070 1.00 42.77  ? 956  GLU   A CA    1 
ATOM   5296 C  C     . GLU   A 1 807  ? 9.426   4.289   -52.481 1.00 40.35  ? 956  GLU   A C     1 
ATOM   5297 O  O     . GLU   A 1 807  ? 9.143   5.393   -52.993 1.00 37.42  ? 956  GLU   A O     1 
ATOM   5298 C  CB    . GLU   A 1 807  ? 11.552  4.094   -51.080 1.00 48.38  ? 956  GLU   A CB    1 
ATOM   5299 C  CG    . GLU   A 1 807  ? 12.279  5.272   -51.695 1.00 59.51  ? 956  GLU   A CG    1 
ATOM   5300 C  CD    . GLU   A 1 807  ? 11.800  6.618   -51.168 1.00 63.01  ? 956  GLU   A CD    1 
ATOM   5301 O  OE1   . GLU   A 1 807  ? 11.717  6.745   -49.913 1.00 67.76  ? 956  GLU   A OE1   1 
ATOM   5302 O  OE2   . GLU   A 1 807  ? 11.481  7.515   -52.003 1.00 54.05  ? 956  GLU   A OE2   1 
ATOM   5303 N  N     . ALA   A 1 808  ? 9.242   3.112   -53.092 1.00 41.68  ? 957  ALA   A N     1 
ATOM   5304 C  CA    . ALA   A 1 808  ? 8.709   2.958   -54.465 1.00 39.78  ? 957  ALA   A CA    1 
ATOM   5305 C  C     . ALA   A 1 808  ? 7.289   3.508   -54.497 1.00 38.71  ? 957  ALA   A C     1 
ATOM   5306 O  O     . ALA   A 1 808  ? 6.996   4.331   -55.396 1.00 38.82  ? 957  ALA   A O     1 
ATOM   5307 C  CB    . ALA   A 1 808  ? 8.731   1.512   -54.888 1.00 44.47  ? 957  ALA   A CB    1 
ATOM   5308 N  N     . LYS   A 1 809  ? 6.484   3.121   -53.500 1.00 37.76  ? 958  LYS   A N     1 
ATOM   5309 C  CA    . LYS   A 1 809  ? 5.101   3.609   -53.280 1.00 37.37  ? 958  LYS   A CA    1 
ATOM   5310 C  C     . LYS   A 1 809  ? 5.056   5.134   -53.155 1.00 40.57  ? 958  LYS   A C     1 
ATOM   5311 O  O     . LYS   A 1 809  ? 4.135   5.741   -53.729 1.00 39.28  ? 958  LYS   A O     1 
ATOM   5312 C  CB    . LYS   A 1 809  ? 4.512   2.999   -52.014 1.00 37.62  ? 958  LYS   A CB    1 
ATOM   5313 C  CG    . LYS   A 1 809  ? 3.090   3.456   -51.730 1.00 41.19  ? 958  LYS   A CG    1 
ATOM   5314 C  CD    . LYS   A 1 809  ? 2.679   3.279   -50.292 1.00 48.29  ? 958  LYS   A CD    1 
ATOM   5315 C  CE    . LYS   A 1 809  ? 3.251   4.331   -49.372 1.00 46.49  ? 958  LYS   A CE    1 
ATOM   5316 N  NZ    . LYS   A 1 809  ? 2.464   4.406   -48.121 1.00 50.68  ? 958  LYS   A NZ    1 
ATOM   5317 N  N     . VAL   A 1 810  ? 5.991   5.727   -52.410 1.00 38.91  ? 959  VAL   A N     1 
ATOM   5318 C  CA    . VAL   A 1 810  ? 6.088   7.210   -52.244 1.00 42.63  ? 959  VAL   A CA    1 
ATOM   5319 C  C     . VAL   A 1 810  ? 6.303   7.843   -53.622 1.00 38.32  ? 959  VAL   A C     1 
ATOM   5320 O  O     . VAL   A 1 810  ? 5.648   8.841   -53.901 1.00 38.67  ? 959  VAL   A O     1 
ATOM   5321 C  CB    . VAL   A 1 810  ? 7.188   7.628   -51.232 1.00 42.85  ? 959  VAL   A CB    1 
ATOM   5322 C  CG1   . VAL   A 1 810  ? 7.597   9.088   -51.376 1.00 37.88  ? 959  VAL   A CG1   1 
ATOM   5323 C  CG2   . VAL   A 1 810  ? 6.756   7.331   -49.797 1.00 39.58  ? 959  VAL   A CG2   1 
ATOM   5324 N  N     . GLN   A 1 811  ? 7.172   7.271   -54.448 1.00 38.59  ? 960  GLN   A N     1 
ATOM   5325 C  CA    . GLN   A 1 811  ? 7.504   7.827   -55.784 1.00 41.89  ? 960  GLN   A CA    1 
ATOM   5326 C  C     . GLN   A 1 811  ? 6.315   7.664   -56.750 1.00 42.88  ? 960  GLN   A C     1 
ATOM   5327 O  O     . GLN   A 1 811  ? 6.077   8.582   -57.542 1.00 41.29  ? 960  GLN   A O     1 
ATOM   5328 C  CB    . GLN   A 1 811  ? 8.802   7.194   -56.284 1.00 43.45  ? 960  GLN   A CB    1 
ATOM   5329 C  CG    . GLN   A 1 811  ? 10.031  7.725   -55.561 1.00 46.28  ? 960  GLN   A CG    1 
ATOM   5330 C  CD    . GLN   A 1 811  ? 11.312  7.161   -56.116 1.00 53.47  ? 960  GLN   A CD    1 
ATOM   5331 O  OE1   . GLN   A 1 811  ? 11.469  6.991   -57.323 1.00 60.10  ? 960  GLN   A OE1   1 
ATOM   5332 N  NE2   . GLN   A 1 811  ? 12.242  6.863   -55.230 1.00 59.59  ? 960  GLN   A NE2   1 
ATOM   5333 N  N     . LEU   A 1 812  ? 5.583   6.550   -56.696 1.00 42.10  ? 961  LEU   A N     1 
ATOM   5334 C  CA    . LEU   A 1 812  ? 4.406   6.328   -57.577 1.00 42.49  ? 961  LEU   A CA    1 
ATOM   5335 C  C     . LEU   A 1 812  ? 3.381   7.409   -57.265 1.00 42.02  ? 961  LEU   A C     1 
ATOM   5336 O  O     . LEU   A 1 812  ? 2.884   8.043   -58.192 1.00 42.02  ? 961  LEU   A O     1 
ATOM   5337 C  CB    . LEU   A 1 812  ? 3.800   4.940   -57.349 1.00 41.46  ? 961  LEU   A CB    1 
ATOM   5338 C  CG    . LEU   A 1 812  ? 4.695   3.772   -57.738 1.00 42.85  ? 961  LEU   A CG    1 
ATOM   5339 C  CD1   . LEU   A 1 812  ? 4.061   2.459   -57.331 1.00 44.64  ? 961  LEU   A CD1   1 
ATOM   5340 C  CD2   . LEU   A 1 812  ? 4.989   3.809   -59.220 1.00 43.48  ? 961  LEU   A CD2   1 
ATOM   5341 N  N     . LYS   A 1 813  ? 3.098   7.599   -55.986 1.00 40.80  ? 962  LYS   A N     1 
ATOM   5342 C  CA    . LYS   A 1 813  ? 2.126   8.605   -55.502 1.00 41.67  ? 962  LYS   A CA    1 
ATOM   5343 C  C     . LYS   A 1 813  ? 2.558   10.002  -55.971 1.00 40.94  ? 962  LYS   A C     1 
ATOM   5344 O  O     . LYS   A 1 813  ? 1.710   10.741  -56.467 1.00 46.22  ? 962  LYS   A O     1 
ATOM   5345 C  CB    . LYS   A 1 813  ? 2.008   8.438   -53.991 1.00 43.31  ? 962  LYS   A CB    1 
ATOM   5346 C  CG    . LYS   A 1 813  ? 1.209   9.507   -53.263 1.00 51.56  ? 962  LYS   A CG    1 
ATOM   5347 C  CD    . LYS   A 1 813  ? 1.189   9.278   -51.763 1.00 52.33  ? 962  LYS   A CD    1 
ATOM   5348 C  CE    . LYS   A 1 813  ? 0.861   7.843   -51.388 1.00 49.42  ? 962  LYS   A CE    1 
ATOM   5349 N  NZ    . LYS   A 1 813  ? 0.262   7.771   -50.040 1.00 51.20  ? 962  LYS   A NZ    1 
ATOM   5350 N  N     . GLU   A 1 814  ? 3.834   10.348  -55.864 1.00 45.22  ? 963  GLU   A N     1 
ATOM   5351 C  CA    . GLU   A 1 814  ? 4.368   11.669  -56.301 1.00 48.52  ? 963  GLU   A CA    1 
ATOM   5352 C  C     . GLU   A 1 814  ? 4.014   11.885  -57.786 1.00 47.91  ? 963  GLU   A C     1 
ATOM   5353 O  O     . GLU   A 1 814  ? 3.619   13.013  -58.145 1.00 44.96  ? 963  GLU   A O     1 
ATOM   5354 C  CB    . GLU   A 1 814  ? 5.869   11.727  -55.993 1.00 52.30  ? 963  GLU   A CB    1 
ATOM   5355 C  CG    . GLU   A 1 814  ? 6.606   12.955  -56.530 1.00 64.01  ? 963  GLU   A CG    1 
ATOM   5356 C  CD    . GLU   A 1 814  ? 8.130   12.911  -56.382 1.00 74.42  ? 963  GLU   A CD    1 
ATOM   5357 O  OE1   . GLU   A 1 814  ? 8.669   11.879  -55.883 1.00 70.49  ? 963  GLU   A OE1   1 
ATOM   5358 O  OE2   . GLU   A 1 814  ? 8.789   13.904  -56.775 1.00 81.57  ? 963  GLU   A OE2   1 
ATOM   5359 N  N     . ILE   A 1 815  ? 4.115   10.846  -58.625 1.00 43.22  ? 964  ILE   A N     1 
ATOM   5360 C  CA    . ILE   A 1 815  ? 3.861   10.979  -60.093 1.00 44.35  ? 964  ILE   A CA    1 
ATOM   5361 C  C     . ILE   A 1 815  ? 2.366   11.237  -60.356 1.00 43.61  ? 964  ILE   A C     1 
ATOM   5362 O  O     . ILE   A 1 815  ? 2.049   12.031  -61.272 1.00 44.80  ? 964  ILE   A O     1 
ATOM   5363 C  CB    . ILE   A 1 815  ? 4.423   9.778   -60.868 1.00 42.67  ? 964  ILE   A CB    1 
ATOM   5364 C  CG1   . ILE   A 1 815  ? 5.952   9.809   -60.900 1.00 41.24  ? 964  ILE   A CG1   1 
ATOM   5365 C  CG2   . ILE   A 1 815  ? 3.861   9.736   -62.275 1.00 46.60  ? 964  ILE   A CG2   1 
ATOM   5366 C  CD1   . ILE   A 1 815  ? 6.591   8.458   -61.158 1.00 44.39  ? 964  ILE   A CD1   1 
ATOM   5367 N  N     . LEU   A 1 816  ? 1.470   10.638  -59.577 1.00 43.58  ? 965  LEU   A N     1 
ATOM   5368 C  CA    . LEU   A 1 816  ? 0.007   10.885  -59.687 1.00 44.20  ? 965  LEU   A CA    1 
ATOM   5369 C  C     . LEU   A 1 816  ? -0.301  12.312  -59.210 1.00 46.74  ? 965  LEU   A C     1 
ATOM   5370 O  O     . LEU   A 1 816  ? -1.098  12.984  -59.875 1.00 46.75  ? 965  LEU   A O     1 
ATOM   5371 C  CB    . LEU   A 1 816  ? -0.755  9.834   -58.873 1.00 42.30  ? 965  LEU   A CB    1 
ATOM   5372 C  CG    . LEU   A 1 816  ? -0.592  8.391   -59.351 1.00 40.71  ? 965  LEU   A CG    1 
ATOM   5373 C  CD1   . LEU   A 1 816  ? -1.310  7.422   -58.427 1.00 45.54  ? 965  LEU   A CD1   1 
ATOM   5374 C  CD2   . LEU   A 1 816  ? -1.106  8.227   -60.759 1.00 40.96  ? 965  LEU   A CD2   1 
ATOM   5375 N  N     . ILE   A 1 817  ? 0.302   12.763  -58.101 1.00 48.76  ? 966  ILE   A N     1 
ATOM   5376 C  CA    . ILE   A 1 817  ? 0.168   14.164  -57.591 1.00 46.57  ? 966  ILE   A CA    1 
ATOM   5377 C  C     . ILE   A 1 817  ? 0.519   15.117  -58.743 1.00 45.54  ? 966  ILE   A C     1 
ATOM   5378 O  O     . ILE   A 1 817  ? -0.276  15.994  -59.020 1.00 49.85  ? 966  ILE   A O     1 
ATOM   5379 C  CB    . ILE   A 1 817  ? 1.068   14.436  -56.359 1.00 50.59  ? 966  ILE   A CB    1 
ATOM   5380 C  CG1   . ILE   A 1 817  ? 0.741   13.544  -55.154 1.00 49.56  ? 966  ILE   A CG1   1 
ATOM   5381 C  CG2   . ILE   A 1 817  ? 1.022   15.909  -55.985 1.00 47.34  ? 966  ILE   A CG2   1 
ATOM   5382 C  CD1   . ILE   A 1 817  ? -0.710  13.504  -54.796 1.00 50.77  ? 966  ILE   A CD1   1 
ATOM   5383 N  N     . ASN   A 1 818  ? 1.655   14.903  -59.412 1.00 50.65  ? 967  ASN   A N     1 
ATOM   5384 C  CA    . ASN   A 1 818  ? 2.181   15.777  -60.497 1.00 57.48  ? 967  ASN   A CA    1 
ATOM   5385 C  C     . ASN   A 1 818  ? 1.341   15.649  -61.776 1.00 55.45  ? 967  ASN   A C     1 
ATOM   5386 O  O     . ASN   A 1 818  ? 1.561   16.474  -62.676 1.00 56.84  ? 967  ASN   A O     1 
ATOM   5387 C  CB    . ASN   A 1 818  ? 3.657   15.494  -60.828 1.00 56.99  ? 967  ASN   A CB    1 
ATOM   5388 C  CG    . ASN   A 1 818  ? 4.608   15.944  -59.741 1.00 59.56  ? 967  ASN   A CG    1 
ATOM   5389 O  OD1   . ASN   A 1 818  ? 4.249   16.750  -58.881 1.00 57.15  ? 967  ASN   A OD1   1 
ATOM   5390 N  ND2   . ASN   A 1 818  ? 5.821   15.411  -59.754 1.00 61.66  ? 967  ASN   A ND2   1 
ATOM   5391 N  N     . SER   A 1 819  ? 0.468   14.641  -61.889 1.00 53.23  ? 968  SER   A N     1 
ATOM   5392 C  CA    . SER   A 1 819  ? -0.495  14.486  -63.016 1.00 50.79  ? 968  SER   A CA    1 
ATOM   5393 C  C     . SER   A 1 819  ? -1.843  15.128  -62.651 1.00 48.99  ? 968  SER   A C     1 
ATOM   5394 O  O     . SER   A 1 819  ? -2.774  15.097  -63.492 1.00 47.44  ? 968  SER   A O     1 
ATOM   5395 C  CB    . SER   A 1 819  ? -0.637  13.037  -63.412 1.00 53.38  ? 968  SER   A CB    1 
ATOM   5396 O  OG    . SER   A 1 819  ? 0.505   12.615  -64.144 1.00 54.06  ? 968  SER   A OG    1 
ATOM   5397 N  N     . GLY   A 1 820  ? -1.935  15.719  -61.453 1.00 49.08  ? 969  GLY   A N     1 
ATOM   5398 C  CA    . GLY   A 1 820  ? -3.091  16.507  -60.991 1.00 43.66  ? 969  GLY   A CA    1 
ATOM   5399 C  C     . GLY   A 1 820  ? -4.005  15.726  -60.066 1.00 43.57  ? 969  GLY   A C     1 
ATOM   5400 O  O     . GLY   A 1 820  ? -5.091  16.247  -59.738 1.00 46.55  ? 969  GLY   A O     1 
ATOM   5401 N  N     . PHE   A 1 821  ? -3.619  14.531  -59.616 1.00 45.76  ? 970  PHE   A N     1 
ATOM   5402 C  CA    . PHE   A 1 821  ? -4.478  13.737  -58.696 1.00 46.55  ? 970  PHE   A CA    1 
ATOM   5403 C  C     . PHE   A 1 821  ? -4.430  14.429  -57.335 1.00 49.12  ? 970  PHE   A C     1 
ATOM   5404 O  O     . PHE   A 1 821  ? -3.374  14.895  -56.909 1.00 53.24  ? 970  PHE   A O     1 
ATOM   5405 C  CB    . PHE   A 1 821  ? -4.094  12.249  -58.683 1.00 47.27  ? 970  PHE   A CB    1 
ATOM   5406 C  CG    . PHE   A 1 821  ? -4.570  11.462  -59.882 1.00 44.78  ? 970  PHE   A CG    1 
ATOM   5407 C  CD1   . PHE   A 1 821  ? -3.837  11.435  -61.059 1.00 48.41  ? 970  PHE   A CD1   1 
ATOM   5408 C  CD2   . PHE   A 1 821  ? -5.758  10.758  -59.841 1.00 43.82  ? 970  PHE   A CD2   1 
ATOM   5409 C  CE1   . PHE   A 1 821  ? -4.275  10.720  -62.162 1.00 49.21  ? 970  PHE   A CE1   1 
ATOM   5410 C  CE2   . PHE   A 1 821  ? -6.193  10.042  -60.944 1.00 44.67  ? 970  PHE   A CE2   1 
ATOM   5411 C  CZ    . PHE   A 1 821  ? -5.459  10.033  -62.105 1.00 45.56  ? 970  PHE   A CZ    1 
ATOM   5412 N  N     . PRO   A 1 822  ? -5.579  14.575  -56.636 1.00 50.08  ? 971  PRO   A N     1 
ATOM   5413 C  CA    . PRO   A 1 822  ? -5.608  15.258  -55.345 1.00 49.17  ? 971  PRO   A CA    1 
ATOM   5414 C  C     . PRO   A 1 822  ? -4.980  14.431  -54.214 1.00 51.36  ? 971  PRO   A C     1 
ATOM   5415 O  O     . PRO   A 1 822  ? -5.188  13.232  -54.172 1.00 55.42  ? 971  PRO   A O     1 
ATOM   5416 C  CB    . PRO   A 1 822  ? -7.099  15.512  -55.085 1.00 49.32  ? 971  PRO   A CB    1 
ATOM   5417 C  CG    . PRO   A 1 822  ? -7.827  14.494  -55.927 1.00 48.90  ? 971  PRO   A CG    1 
ATOM   5418 C  CD    . PRO   A 1 822  ? -6.908  14.142  -57.080 1.00 49.90  ? 971  PRO   A CD    1 
ATOM   5419 N  N     . GLU   A 1 823  ? -4.246  15.106  -53.327 1.00 50.33  ? 972  GLU   A N     1 
ATOM   5420 C  CA    . GLU   A 1 823  ? -3.550  14.514  -52.157 1.00 54.16  ? 972  GLU   A CA    1 
ATOM   5421 C  C     . GLU   A 1 823  ? -4.492  13.549  -51.426 1.00 53.24  ? 972  GLU   A C     1 
ATOM   5422 O  O     . GLU   A 1 823  ? -4.039  12.466  -51.041 1.00 55.55  ? 972  GLU   A O     1 
ATOM   5423 C  CB    . GLU   A 1 823  ? -3.090  15.603  -51.181 1.00 61.58  ? 972  GLU   A CB    1 
ATOM   5424 C  CG    . GLU   A 1 823  ? -2.037  16.549  -51.742 1.00 69.92  ? 972  GLU   A CG    1 
ATOM   5425 C  CD    . GLU   A 1 823  ? -0.620  15.996  -51.796 1.00 83.18  ? 972  GLU   A CD    1 
ATOM   5426 O  OE1   . GLU   A 1 823  ? 0.235   16.637  -52.454 1.00 83.63  ? 972  GLU   A OE1   1 
ATOM   5427 O  OE2   . GLU   A 1 823  ? -0.365  14.931  -51.175 1.00 89.30  ? 972  GLU   A OE2   1 
ATOM   5428 N  N     . ASP   A 1 824  ? -5.750  13.930  -51.225 1.00 48.67  ? 973  ASP   A N     1 
ATOM   5429 C  CA    . ASP   A 1 824  ? -6.637  13.269  -50.233 1.00 56.62  ? 973  ASP   A CA    1 
ATOM   5430 C  C     . ASP   A 1 824  ? -7.226  11.958  -50.785 1.00 51.27  ? 973  ASP   A C     1 
ATOM   5431 O  O     . ASP   A 1 824  ? -7.878  11.265  -50.002 1.00 48.76  ? 973  ASP   A O     1 
ATOM   5432 C  CB    . ASP   A 1 824  ? -7.689  14.247  -49.690 1.00 67.86  ? 973  ASP   A CB    1 
ATOM   5433 C  CG    . ASP   A 1 824  ? -8.663  14.837  -50.700 1.00 73.57  ? 973  ASP   A CG    1 
ATOM   5434 O  OD1   . ASP   A 1 824  ? -8.711  14.353  -51.850 1.00 77.48  ? 973  ASP   A OD1   1 
ATOM   5435 O  OD2   . ASP   A 1 824  ? -9.386  15.784  -50.315 1.00 87.29  ? 973  ASP   A OD2   1 
ATOM   5436 N  N     . CYS   A 1 825  ? -6.982  11.592  -52.050 1.00 47.31  ? 974  CYS   A N     1 
ATOM   5437 C  CA    . CYS   A 1 825  ? -7.350  10.251  -52.593 1.00 47.37  ? 974  CYS   A CA    1 
ATOM   5438 C  C     . CYS   A 1 825  ? -6.181  9.272   -52.425 1.00 43.16  ? 974  CYS   A C     1 
ATOM   5439 O  O     . CYS   A 1 825  ? -6.343  8.117   -52.810 1.00 46.92  ? 974  CYS   A O     1 
ATOM   5440 C  CB    . CYS   A 1 825  ? -7.809  10.313  -54.049 1.00 45.55  ? 974  CYS   A CB    1 
ATOM   5441 S  SG    . CYS   A 1 825  ? -6.494  10.577  -55.269 1.00 46.41  ? 974  CYS   A SG    1 
ATOM   5442 N  N     . LEU   A 1 826  ? -5.070  9.703   -51.822 1.00 44.17  ? 975  LEU   A N     1 
ATOM   5443 C  CA    . LEU   A 1 826  ? -3.828  8.904   -51.685 1.00 42.31  ? 975  LEU   A CA    1 
ATOM   5444 C  C     . LEU   A 1 826  ? -3.328  8.878   -50.234 1.00 40.60  ? 975  LEU   A C     1 
ATOM   5445 O  O     . LEU   A 1 826  ? -2.155  8.520   -50.046 1.00 42.37  ? 975  LEU   A O     1 
ATOM   5446 C  CB    . LEU   A 1 826  ? -2.785  9.498   -52.634 1.00 40.32  ? 975  LEU   A CB    1 
ATOM   5447 C  CG    . LEU   A 1 826  ? -3.009  9.195   -54.113 1.00 40.59  ? 975  LEU   A CG    1 
ATOM   5448 C  CD1   . LEU   A 1 826  ? -2.383  10.271  -54.988 1.00 39.90  ? 975  LEU   A CD1   1 
ATOM   5449 C  CD2   . LEU   A 1 826  ? -2.436  7.834   -54.476 1.00 44.35  ? 975  LEU   A CD2   1 
ATOM   5450 N  N     . LEU   A 1 827  ? -4.174  9.153   -49.237 1.00 43.81  ? 976  LEU   A N     1 
ATOM   5451 C  CA    . LEU   A 1 827  ? -3.766  9.082   -47.798 1.00 45.26  ? 976  LEU   A CA    1 
ATOM   5452 C  C     . LEU   A 1 827  ? -3.738  7.621   -47.328 1.00 42.48  ? 976  LEU   A C     1 
ATOM   5453 O  O     . LEU   A 1 827  ? -4.566  6.818   -47.815 1.00 42.63  ? 976  LEU   A O     1 
ATOM   5454 C  CB    . LEU   A 1 827  ? -4.729  9.895   -46.930 1.00 46.07  ? 976  LEU   A CB    1 
ATOM   5455 C  CG    . LEU   A 1 827  ? -4.868  11.372  -47.304 1.00 49.48  ? 976  LEU   A CG    1 
ATOM   5456 C  CD1   . LEU   A 1 827  ? -5.999  12.012  -46.513 1.00 46.55  ? 976  LEU   A CD1   1 
ATOM   5457 C  CD2   . LEU   A 1 827  ? -3.560  12.136  -47.109 1.00 47.20  ? 976  LEU   A CD2   1 
ATOM   5458 N  N     . THR   A 1 828  ? -2.809  7.290   -46.431 1.00 39.61  ? 977  THR   A N     1 
ATOM   5459 C  CA    . THR   A 1 828  ? -2.783  5.993   -45.725 1.00 46.07  ? 977  THR   A CA    1 
ATOM   5460 C  C     . THR   A 1 828  ? -4.102  5.888   -44.962 1.00 44.56  ? 977  THR   A C     1 
ATOM   5461 O  O     . THR   A 1 828  ? -4.541  6.895   -44.389 1.00 51.38  ? 977  THR   A O     1 
ATOM   5462 C  CB    . THR   A 1 828  ? -1.560  5.809   -44.810 1.00 50.17  ? 977  THR   A CB    1 
ATOM   5463 O  OG1   . THR   A 1 828  ? -1.611  6.825   -43.820 1.00 60.86  ? 977  THR   A OG1   1 
ATOM   5464 C  CG2   . THR   A 1 828  ? -0.227  5.882   -45.526 1.00 50.61  ? 977  THR   A CG2   1 
ATOM   5465 N  N     . GLN   A 1 829  ? -4.735  4.724   -45.014 1.00 43.57  ? 978  GLN   A N     1 
ATOM   5466 C  CA    . GLN   A 1 829  ? -6.034  4.470   -44.363 1.00 47.97  ? 978  GLN   A CA    1 
ATOM   5467 C  C     . GLN   A 1 829  ? -5.889  3.206   -43.544 1.00 49.18  ? 978  GLN   A C     1 
ATOM   5468 O  O     . GLN   A 1 829  ? -5.526  2.158   -44.100 1.00 55.10  ? 978  GLN   A O     1 
ATOM   5469 C  CB    . GLN   A 1 829  ? -7.151  4.431   -45.399 1.00 52.71  ? 978  GLN   A CB    1 
ATOM   5470 C  CG    . GLN   A 1 829  ? -7.568  5.838   -45.802 1.00 57.24  ? 978  GLN   A CG    1 
ATOM   5471 C  CD    . GLN   A 1 829  ? -8.377  5.874   -47.069 1.00 62.46  ? 978  GLN   A CD    1 
ATOM   5472 O  OE1   . GLN   A 1 829  ? -8.675  4.835   -47.675 1.00 61.82  ? 978  GLN   A OE1   1 
ATOM   5473 N  NE2   . GLN   A 1 829  ? -8.739  7.086   -47.463 1.00 59.77  ? 978  GLN   A NE2   1 
ATOM   5474 N  N     . VAL   A 1 830  ? -6.097  3.347   -42.242 1.00 53.62  ? 979  VAL   A N     1 
ATOM   5475 C  CA    . VAL   A 1 830  ? -6.104  2.189   -41.327 1.00 52.77  ? 979  VAL   A CA    1 
ATOM   5476 C  C     . VAL   A 1 830  ? -7.217  1.276   -41.836 1.00 48.81  ? 979  VAL   A C     1 
ATOM   5477 O  O     . VAL   A 1 830  ? -8.259  1.786   -42.264 1.00 45.25  ? 979  VAL   A O     1 
ATOM   5478 C  CB    . VAL   A 1 830  ? -6.278  2.623   -39.860 1.00 59.18  ? 979  VAL   A CB    1 
ATOM   5479 C  CG1   . VAL   A 1 830  ? -7.688  3.118   -39.561 1.00 58.61  ? 979  VAL   A CG1   1 
ATOM   5480 C  CG2   . VAL   A 1 830  ? -5.893  1.490   -38.919 1.00 66.04  ? 979  VAL   A CG2   1 
ATOM   5481 N  N     . PHE   A 1 831  ? -6.971  -0.027  -41.844 1.00 47.81  ? 980  PHE   A N     1 
ATOM   5482 C  CA    . PHE   A 1 831  ? -7.993  -1.053  -42.140 1.00 42.72  ? 980  PHE   A CA    1 
ATOM   5483 C  C     . PHE   A 1 831  ? -7.837  -2.207  -41.173 1.00 42.96  ? 980  PHE   A C     1 
ATOM   5484 O  O     . PHE   A 1 831  ? -6.747  -2.388  -40.602 1.00 43.42  ? 980  PHE   A O     1 
ATOM   5485 C  CB    . PHE   A 1 831  ? -7.830  -1.587  -43.561 1.00 44.21  ? 980  PHE   A CB    1 
ATOM   5486 C  CG    . PHE   A 1 831  ? -6.586  -2.395  -43.794 1.00 45.75  ? 980  PHE   A CG    1 
ATOM   5487 C  CD1   . PHE   A 1 831  ? -5.372  -1.779  -44.055 1.00 46.92  ? 980  PHE   A CD1   1 
ATOM   5488 C  CD2   . PHE   A 1 831  ? -6.636  -3.781  -43.783 1.00 50.02  ? 980  PHE   A CD2   1 
ATOM   5489 C  CE1   . PHE   A 1 831  ? -4.235  -2.539  -44.290 1.00 51.61  ? 980  PHE   A CE1   1 
ATOM   5490 C  CE2   . PHE   A 1 831  ? -5.499  -4.536  -44.026 1.00 50.71  ? 980  PHE   A CE2   1 
ATOM   5491 C  CZ    . PHE   A 1 831  ? -4.299  -3.916  -44.274 1.00 49.32  ? 980  PHE   A CZ    1 
ATOM   5492 N  N     . THR   A 1 832  ? -8.903  -2.989  -41.057 1.00 43.71  ? 981  THR   A N     1 
ATOM   5493 C  CA    . THR   A 1 832  ? -8.918  -4.288  -40.354 1.00 43.03  ? 981  THR   A CA    1 
ATOM   5494 C  C     . THR   A 1 832  ? -8.941  -5.390  -41.423 1.00 46.01  ? 981  THR   A C     1 
ATOM   5495 O  O     . THR   A 1 832  ? -9.605  -5.197  -42.466 1.00 44.31  ? 981  THR   A O     1 
ATOM   5496 C  CB    . THR   A 1 832  ? -10.111 -4.381  -39.396 1.00 42.86  ? 981  THR   A CB    1 
ATOM   5497 O  OG1   . THR   A 1 832  ? -10.204 -5.738  -38.960 1.00 46.35  ? 981  THR   A OG1   1 
ATOM   5498 C  CG2   . THR   A 1 832  ? -11.434 -4.007  -40.029 1.00 46.34  ? 981  THR   A CG2   1 
ATOM   5499 N  N     . ASN   A 1 833  ? -8.268  -6.513  -41.162 1.00 46.93  ? 982  ASN   A N     1 
ATOM   5500 C  CA    . ASN   A 1 833  ? -8.239  -7.684  -42.070 1.00 47.47  ? 982  ASN   A CA    1 
ATOM   5501 C  C     . ASN   A 1 833  ? -9.201  -8.769  -41.562 1.00 45.58  ? 982  ASN   A C     1 
ATOM   5502 O  O     . ASN   A 1 833  ? -9.159  -9.854  -42.135 1.00 46.81  ? 982  ASN   A O     1 
ATOM   5503 C  CB    . ASN   A 1 833  ? -6.801  -8.169  -42.288 1.00 47.36  ? 982  ASN   A CB    1 
ATOM   5504 C  CG    . ASN   A 1 833  ? -6.120  -8.681  -41.033 1.00 47.00  ? 982  ASN   A CG    1 
ATOM   5505 O  OD1   . ASN   A 1 833  ? -6.756  -8.907  -40.007 1.00 42.97  ? 982  ASN   A OD1   1 
ATOM   5506 N  ND2   . ASN   A 1 833  ? -4.820  -8.890  -41.124 1.00 43.38  ? 982  ASN   A ND2   1 
ATOM   5507 N  N     . THR   A 1 834  ? -10.055 -8.491  -40.565 1.00 49.27  ? 983  THR   A N     1 
ATOM   5508 C  CA    . THR   A 1 834  ? -11.069 -9.457  -40.031 1.00 50.10  ? 983  THR   A CA    1 
ATOM   5509 C  C     . THR   A 1 834  ? -12.481 -8.857  -40.014 1.00 46.98  ? 983  THR   A C     1 
ATOM   5510 O  O     . THR   A 1 834  ? -13.416 -9.578  -40.371 1.00 51.27  ? 983  THR   A O     1 
ATOM   5511 C  CB    . THR   A 1 834  ? -10.707 -9.961  -38.626 1.00 49.24  ? 983  THR   A CB    1 
ATOM   5512 O  OG1   . THR   A 1 834  ? -10.454 -8.836  -37.786 1.00 48.87  ? 983  THR   A OG1   1 
ATOM   5513 C  CG2   . THR   A 1 834  ? -9.500  -10.872 -38.627 1.00 50.83  ? 983  THR   A CG2   1 
ATOM   5514 N  N     . GLY   A 1 835  ? -12.636 -7.610  -39.575 1.00 49.65  ? 984  GLY   A N     1 
ATOM   5515 C  CA    . GLY   A 1 835  ? -13.936 -6.916  -39.505 1.00 48.85  ? 984  GLY   A CA    1 
ATOM   5516 C  C     . GLY   A 1 835  ? -14.395 -6.406  -40.868 1.00 53.07  ? 984  GLY   A C     1 
ATOM   5517 O  O     . GLY   A 1 835  ? -13.633 -6.415  -41.834 1.00 52.31  ? 984  GLY   A O     1 
ATOM   5518 N  N     . PRO   A 1 836  ? -15.665 -5.959  -40.989 1.00 56.89  ? 985  PRO   A N     1 
ATOM   5519 C  CA    . PRO   A 1 836  ? -16.133 -5.291  -42.206 1.00 56.40  ? 985  PRO   A CA    1 
ATOM   5520 C  C     . PRO   A 1 836  ? -15.211 -4.126  -42.591 1.00 55.88  ? 985  PRO   A C     1 
ATOM   5521 O  O     . PRO   A 1 836  ? -14.853 -3.366  -41.715 1.00 53.41  ? 985  PRO   A O     1 
ATOM   5522 C  CB    . PRO   A 1 836  ? -17.528 -4.761  -41.837 1.00 53.51  ? 985  PRO   A CB    1 
ATOM   5523 C  CG    . PRO   A 1 836  ? -17.988 -5.694  -40.712 1.00 56.10  ? 985  PRO   A CG    1 
ATOM   5524 C  CD    . PRO   A 1 836  ? -16.723 -6.085  -39.970 1.00 55.83  ? 985  PRO   A CD    1 
ATOM   5525 N  N     . ASP   A 1 837  ? -14.849 -4.018  -43.874 1.00 51.97  ? 986  ASP   A N     1 
ATOM   5526 C  CA    . ASP   A 1 837  ? -13.964 -2.934  -44.376 1.00 51.94  ? 986  ASP   A CA    1 
ATOM   5527 C  C     . ASP   A 1 837  ? -14.245 -2.732  -45.867 1.00 51.42  ? 986  ASP   A C     1 
ATOM   5528 O  O     . ASP   A 1 837  ? -13.682 -3.481  -46.686 1.00 50.79  ? 986  ASP   A O     1 
ATOM   5529 C  CB    . ASP   A 1 837  ? -12.489 -3.225  -44.064 1.00 49.14  ? 986  ASP   A CB    1 
ATOM   5530 C  CG    . ASP   A 1 837  ? -11.624 -1.981  -44.137 1.00 49.93  ? 986  ASP   A CG    1 
ATOM   5531 O  OD1   . ASP   A 1 837  ? -11.784 -1.227  -45.111 1.00 50.03  ? 986  ASP   A OD1   1 
ATOM   5532 O  OD2   . ASP   A 1 837  ? -10.838 -1.744  -43.186 1.00 55.25  ? 986  ASP   A OD2   1 
ATOM   5533 N  N     . ASN   A 1 838  ? -15.074 -1.741  -46.194 1.00 49.20  ? 987  ASN   A N     1 
ATOM   5534 C  CA    . ASN   A 1 838  ? -15.458 -1.451  -47.592 1.00 47.52  ? 987  ASN   A CA    1 
ATOM   5535 C  C     . ASN   A 1 838  ? -14.219 -1.001  -48.375 1.00 45.73  ? 987  ASN   A C     1 
ATOM   5536 O  O     . ASN   A 1 838  ? -14.124 -1.381  -49.558 1.00 45.78  ? 987  ASN   A O     1 
ATOM   5537 C  CB    . ASN   A 1 838  ? -16.626 -0.467  -47.711 1.00 48.20  ? 987  ASN   A CB    1 
ATOM   5538 C  CG    . ASN   A 1 838  ? -17.337 -0.613  -49.048 1.00 50.30  ? 987  ASN   A CG    1 
ATOM   5539 O  OD1   . ASN   A 1 838  ? -17.602 0.366   -49.739 1.00 52.60  ? 987  ASN   A OD1   1 
ATOM   5540 N  ND2   . ASN   A 1 838  ? -17.616 -1.844  -49.448 1.00 46.96  ? 987  ASN   A ND2   1 
ATOM   5541 N  N     . ASN   A 1 839  ? -13.300 -0.251  -47.759 1.00 44.55  ? 988  ASN   A N     1 
ATOM   5542 C  CA    . ASN   A 1 839  ? -12.043 0.182   -48.430 1.00 44.33  ? 988  ASN   A CA    1 
ATOM   5543 C  C     . ASN   A 1 839  ? -11.277 -1.057  -48.920 1.00 41.60  ? 988  ASN   A C     1 
ATOM   5544 O  O     . ASN   A 1 839  ? -10.870 -1.096  -50.092 1.00 38.05  ? 988  ASN   A O     1 
ATOM   5545 C  CB    . ASN   A 1 839  ? -11.161 1.048   -47.536 1.00 43.22  ? 988  ASN   A CB    1 
ATOM   5546 C  CG    . ASN   A 1 839  ? -11.665 2.470   -47.380 1.00 46.03  ? 988  ASN   A CG    1 
ATOM   5547 O  OD1   . ASN   A 1 839  ? -12.411 2.979   -48.209 1.00 43.36  ? 988  ASN   A OD1   1 
ATOM   5548 N  ND2   . ASN   A 1 839  ? -11.216 3.148   -46.341 1.00 44.99  ? 988  ASN   A ND2   1 
ATOM   5549 N  N     . LEU   A 1 840  ? -11.122 -2.058  -48.071 1.00 38.41  ? 989  LEU   A N     1 
ATOM   5550 C  CA    . LEU   A 1 840  ? -10.377 -3.288  -48.429 1.00 39.86  ? 989  LEU   A CA    1 
ATOM   5551 C  C     . LEU   A 1 840  ? -11.166 -4.074  -49.490 1.00 37.07  ? 989  LEU   A C     1 
ATOM   5552 O  O     . LEU   A 1 840  ? -10.528 -4.568  -50.431 1.00 34.99  ? 989  LEU   A O     1 
ATOM   5553 C  CB    . LEU   A 1 840  ? -10.119 -4.103  -47.158 1.00 40.57  ? 989  LEU   A CB    1 
ATOM   5554 C  CG    . LEU   A 1 840  ? -9.090  -5.219  -47.307 1.00 43.30  ? 989  LEU   A CG    1 
ATOM   5555 C  CD1   . LEU   A 1 840  ? -7.758  -4.670  -47.819 1.00 42.88  ? 989  LEU   A CD1   1 
ATOM   5556 C  CD2   . LEU   A 1 840  ? -8.913  -5.948  -45.983 1.00 45.08  ? 989  LEU   A CD2   1 
ATOM   5557 N  N     . ASP   A 1 841  ? -12.502 -4.134  -49.385 1.00 39.47  ? 990  ASP   A N     1 
ATOM   5558 C  CA    . ASP   A 1 841  ? -13.394 -4.782  -50.389 1.00 39.31  ? 990  ASP   A CA    1 
ATOM   5559 C  C     . ASP   A 1 841  ? -13.071 -4.202  -51.779 1.00 39.93  ? 990  ASP   A C     1 
ATOM   5560 O  O     . ASP   A 1 841  ? -12.905 -4.977  -52.745 1.00 35.00  ? 990  ASP   A O     1 
ATOM   5561 C  CB    . ASP   A 1 841  ? -14.883 -4.571  -50.089 1.00 46.48  ? 990  ASP   A CB    1 
ATOM   5562 C  CG    . ASP   A 1 841  ? -15.427 -5.081  -48.752 1.00 52.78  ? 990  ASP   A CG    1 
ATOM   5563 O  OD1   . ASP   A 1 841  ? -14.874 -6.051  -48.188 1.00 55.58  ? 990  ASP   A OD1   1 
ATOM   5564 O  OD2   . ASP   A 1 841  ? -16.423 -4.492  -48.275 1.00 59.31  ? 990  ASP   A OD2   1 
ATOM   5565 N  N     . VAL   A 1 842  ? -12.980 -2.876  -51.876 1.00 37.25  ? 991  VAL   A N     1 
ATOM   5566 C  CA    . VAL   A 1 842  ? -12.781 -2.160  -53.161 1.00 39.88  ? 991  VAL   A CA    1 
ATOM   5567 C  C     . VAL   A 1 842  ? -11.363 -2.452  -53.665 1.00 40.06  ? 991  VAL   A C     1 
ATOM   5568 O  O     . VAL   A 1 842  ? -11.207 -2.709  -54.880 1.00 34.75  ? 991  VAL   A O     1 
ATOM   5569 C  CB    . VAL   A 1 842  ? -13.048 -0.652  -53.015 1.00 39.55  ? 991  VAL   A CB    1 
ATOM   5570 C  CG1   . VAL   A 1 842  ? -12.683 0.085   -54.281 1.00 39.28  ? 991  VAL   A CG1   1 
ATOM   5571 C  CG2   . VAL   A 1 842  ? -14.489 -0.360  -52.654 1.00 42.19  ? 991  VAL   A CG2   1 
ATOM   5572 N  N     . VAL   A 1 843  ? -10.377 -2.466  -52.766 1.00 36.92  ? 992  VAL   A N     1 
ATOM   5573 C  CA    . VAL   A 1 843  ? -8.958  -2.731  -53.146 1.00 35.70  ? 992  VAL   A CA    1 
ATOM   5574 C  C     . VAL   A 1 843  ? -8.872  -4.102  -53.818 1.00 36.47  ? 992  VAL   A C     1 
ATOM   5575 O  O     . VAL   A 1 843  ? -8.194  -4.201  -54.868 1.00 34.21  ? 992  VAL   A O     1 
ATOM   5576 C  CB    . VAL   A 1 843  ? -8.004  -2.646  -51.950 1.00 36.87  ? 992  VAL   A CB    1 
ATOM   5577 C  CG1   . VAL   A 1 843  ? -6.639  -3.231  -52.302 1.00 39.04  ? 992  VAL   A CG1   1 
ATOM   5578 C  CG2   . VAL   A 1 843  ? -7.884  -1.214  -51.453 1.00 36.35  ? 992  VAL   A CG2   1 
ATOM   5579 N  N     . ILE   A 1 844  ? -9.522  -5.112  -53.238 1.00 35.12  ? 993  ILE   A N     1 
ATOM   5580 C  CA    . ILE   A 1 844  ? -9.555  -6.497  -53.794 1.00 38.91  ? 993  ILE   A CA    1 
ATOM   5581 C  C     . ILE   A 1 844  ? -10.310 -6.523  -55.139 1.00 42.06  ? 993  ILE   A C     1 
ATOM   5582 O  O     . ILE   A 1 844  ? -9.890  -7.276  -56.016 1.00 39.90  ? 993  ILE   A O     1 
ATOM   5583 C  CB    . ILE   A 1 844  ? -10.167 -7.463  -52.762 1.00 39.79  ? 993  ILE   A CB    1 
ATOM   5584 C  CG1   . ILE   A 1 844  ? -9.257  -7.602  -51.542 1.00 38.17  ? 993  ILE   A CG1   1 
ATOM   5585 C  CG2   . ILE   A 1 844  ? -10.465 -8.802  -53.411 1.00 38.12  ? 993  ILE   A CG2   1 
ATOM   5586 C  CD1   . ILE   A 1 844  ? -9.925  -8.193  -50.338 1.00 40.17  ? 993  ILE   A CD1   1 
ATOM   5587 N  N     . SER   A 1 845  ? -11.388 -5.748  -55.319 1.00 41.54  ? 994  SER   A N     1 
ATOM   5588 C  CA    . SER   A 1 845  ? -12.066 -5.609  -56.638 1.00 41.83  ? 994  SER   A CA    1 
ATOM   5589 C  C     . SER   A 1 845  ? -11.044 -5.091  -57.663 1.00 42.24  ? 994  SER   A C     1 
ATOM   5590 O  O     . SER   A 1 845  ? -10.949 -5.649  -58.771 1.00 41.05  ? 994  SER   A O     1 
ATOM   5591 C  CB    . SER   A 1 845  ? -13.273 -4.693  -56.569 1.00 41.97  ? 994  SER   A CB    1 
ATOM   5592 O  OG    . SER   A 1 845  ? -14.323 -5.272  -55.808 1.00 42.59  ? 994  SER   A OG    1 
ATOM   5593 N  N     . LEU   A 1 846  ? -10.318 -4.031  -57.308 1.00 40.52  ? 995  LEU   A N     1 
ATOM   5594 C  CA    . LEU   A 1 846  ? -9.352  -3.353  -58.205 1.00 39.34  ? 995  LEU   A CA    1 
ATOM   5595 C  C     . LEU   A 1 846  ? -8.172  -4.297  -58.503 1.00 40.36  ? 995  LEU   A C     1 
ATOM   5596 O  O     . LEU   A 1 846  ? -7.644  -4.266  -59.617 1.00 40.14  ? 995  LEU   A O     1 
ATOM   5597 C  CB    . LEU   A 1 846  ? -8.936  -2.040  -57.535 1.00 41.26  ? 995  LEU   A CB    1 
ATOM   5598 C  CG    . LEU   A 1 846  ? -10.042 -0.980  -57.428 1.00 39.55  ? 995  LEU   A CG    1 
ATOM   5599 C  CD1   . LEU   A 1 846  ? -9.467  0.334   -56.961 1.00 39.37  ? 995  LEU   A CD1   1 
ATOM   5600 C  CD2   . LEU   A 1 846  ? -10.743 -0.781  -58.760 1.00 40.35  ? 995  LEU   A CD2   1 
ATOM   5601 N  N     . LEU   A 1 847  ? -7.821  -5.185  -57.579 1.00 40.17  ? 996  LEU   A N     1 
ATOM   5602 C  CA    . LEU   A 1 847  ? -6.710  -6.139  -57.776 1.00 40.95  ? 996  LEU   A CA    1 
ATOM   5603 C  C     . LEU   A 1 847  ? -7.123  -7.167  -58.843 1.00 41.85  ? 996  LEU   A C     1 
ATOM   5604 O  O     . LEU   A 1 847  ? -6.279  -7.502  -59.695 1.00 42.91  ? 996  LEU   A O     1 
ATOM   5605 C  CB    . LEU   A 1 847  ? -6.357  -6.778  -56.427 1.00 43.35  ? 996  LEU   A CB    1 
ATOM   5606 C  CG    . LEU   A 1 847  ? -5.474  -8.012  -56.537 1.00 49.02  ? 996  LEU   A CG    1 
ATOM   5607 C  CD1   . LEU   A 1 847  ? -4.062  -7.609  -56.937 1.00 49.44  ? 996  LEU   A CD1   1 
ATOM   5608 C  CD2   . LEU   A 1 847  ? -5.483  -8.816  -55.249 1.00 50.98  ? 996  LEU   A CD2   1 
ATOM   5609 N  N     . ALA   A 1 848  ? -8.378  -7.634  -58.831 1.00 39.92  ? 997  ALA   A N     1 
ATOM   5610 C  CA    . ALA   A 1 848  ? -8.945  -8.508  -59.887 1.00 40.78  ? 997  ALA   A CA    1 
ATOM   5611 C  C     . ALA   A 1 848  ? -8.711  -7.865  -61.256 1.00 43.22  ? 997  ALA   A C     1 
ATOM   5612 O  O     . ALA   A 1 848  ? -8.200  -8.538  -62.166 1.00 46.05  ? 997  ALA   A O     1 
ATOM   5613 C  CB    . ALA   A 1 848  ? -10.409 -8.745  -59.658 1.00 43.46  ? 997  ALA   A CB    1 
ATOM   5614 N  N     . PHE   A 1 849  ? -9.045  -6.587  -61.392 1.00 40.93  ? 998  PHE   A N     1 
ATOM   5615 C  CA    . PHE   A 1 849  ? -8.789  -5.839  -62.644 1.00 41.94  ? 998  PHE   A CA    1 
ATOM   5616 C  C     . PHE   A 1 849  ? -7.290  -5.920  -62.974 1.00 39.04  ? 998  PHE   A C     1 
ATOM   5617 O  O     . PHE   A 1 849  ? -6.938  -6.356  -64.064 1.00 39.70  ? 998  PHE   A O     1 
ATOM   5618 C  CB    . PHE   A 1 849  ? -9.300  -4.403  -62.561 1.00 37.07  ? 998  PHE   A CB    1 
ATOM   5619 C  CG    . PHE   A 1 849  ? -8.832  -3.598  -63.731 1.00 39.39  ? 998  PHE   A CG    1 
ATOM   5620 C  CD1   . PHE   A 1 849  ? -7.574  -3.030  -63.723 1.00 41.26  ? 998  PHE   A CD1   1 
ATOM   5621 C  CD2   . PHE   A 1 849  ? -9.613  -3.485  -64.873 1.00 44.35  ? 998  PHE   A CD2   1 
ATOM   5622 C  CE1   . PHE   A 1 849  ? -7.119  -2.315  -64.817 1.00 42.26  ? 998  PHE   A CE1   1 
ATOM   5623 C  CE2   . PHE   A 1 849  ? -9.163  -2.767  -65.969 1.00 41.77  ? 998  PHE   A CE2   1 
ATOM   5624 C  CZ    . PHE   A 1 849  ? -7.917  -2.185  -65.937 1.00 47.80  ? 998  PHE   A CZ    1 
ATOM   5625 N  N     . GLY   A 1 850  ? -6.432  -5.567  -62.025 1.00 42.74  ? 999  GLY   A N     1 
ATOM   5626 C  CA    . GLY   A 1 850  ? -4.971  -5.464  -62.225 1.00 42.91  ? 999  GLY   A CA    1 
ATOM   5627 C  C     . GLY   A 1 850  ? -4.344  -6.730  -62.790 1.00 39.78  ? 999  GLY   A C     1 
ATOM   5628 O  O     . GLY   A 1 850  ? -3.543  -6.624  -63.726 1.00 38.52  ? 999  GLY   A O     1 
ATOM   5629 N  N     . VAL   A 1 851  ? -4.689  -7.889  -62.244 1.00 38.95  ? 1000 VAL   A N     1 
ATOM   5630 C  CA    . VAL   A 1 851  ? -3.988  -9.170  -62.533 1.00 41.56  ? 1000 VAL   A CA    1 
ATOM   5631 C  C     . VAL   A 1 851  ? -4.749  -9.974  -63.599 1.00 43.91  ? 1000 VAL   A C     1 
ATOM   5632 O  O     . VAL   A 1 851  ? -4.257  -11.058 -63.952 1.00 44.02  ? 1000 VAL   A O     1 
ATOM   5633 C  CB    . VAL   A 1 851  ? -3.775  -9.998  -61.250 1.00 42.15  ? 1000 VAL   A CB    1 
ATOM   5634 C  CG1   . VAL   A 1 851  ? -2.967  -9.242  -60.204 1.00 44.01  ? 1000 VAL   A CG1   1 
ATOM   5635 C  CG2   . VAL   A 1 851  ? -5.078  -10.481 -60.659 1.00 41.39  ? 1000 VAL   A CG2   1 
ATOM   5636 N  N     . TYR   A 1 852  ? -5.874  -9.475  -64.124 1.00 46.94  ? 1001 TYR   A N     1 
ATOM   5637 C  CA    . TYR   A 1 852  ? -6.577  -10.093 -65.280 1.00 46.11  ? 1001 TYR   A CA    1 
ATOM   5638 C  C     . TYR   A 1 852  ? -5.569  -10.260 -66.417 1.00 49.78  ? 1001 TYR   A C     1 
ATOM   5639 O  O     . TYR   A 1 852  ? -4.828  -9.324  -66.737 1.00 51.84  ? 1001 TYR   A O     1 
ATOM   5640 C  CB    . TYR   A 1 852  ? -7.794  -9.271  -65.715 1.00 52.23  ? 1001 TYR   A CB    1 
ATOM   5641 C  CG    . TYR   A 1 852  ? -8.593  -9.938  -66.804 1.00 56.35  ? 1001 TYR   A CG    1 
ATOM   5642 C  CD1   . TYR   A 1 852  ? -9.531  -10.910 -66.486 1.00 52.50  ? 1001 TYR   A CD1   1 
ATOM   5643 C  CD2   . TYR   A 1 852  ? -8.348  -9.670  -68.148 1.00 55.08  ? 1001 TYR   A CD2   1 
ATOM   5644 C  CE1   . TYR   A 1 852  ? -10.228 -11.582 -67.473 1.00 61.60  ? 1001 TYR   A CE1   1 
ATOM   5645 C  CE2   . TYR   A 1 852  ? -9.038  -10.336 -69.148 1.00 58.60  ? 1001 TYR   A CE2   1 
ATOM   5646 C  CZ    . TYR   A 1 852  ? -9.981  -11.294 -68.808 1.00 64.52  ? 1001 TYR   A CZ    1 
ATOM   5647 O  OH    . TYR   A 1 852  ? -10.688 -11.961 -69.765 1.00 68.70  ? 1001 TYR   A OH    1 
ATOM   5648 N  N     . PRO   A 1 853  ? -5.522  -11.430 -67.097 1.00 50.81  ? 1002 PRO   A N     1 
ATOM   5649 C  CA    . PRO   A 1 853  ? -6.536  -12.479 -66.965 1.00 52.42  ? 1002 PRO   A CA    1 
ATOM   5650 C  C     . PRO   A 1 853  ? -6.310  -13.610 -65.946 1.00 51.81  ? 1002 PRO   A C     1 
ATOM   5651 O  O     . PRO   A 1 853  ? -6.931  -14.645 -66.122 1.00 57.48  ? 1002 PRO   A O     1 
ATOM   5652 C  CB    . PRO   A 1 853  ? -6.512  -13.088 -68.384 1.00 49.68  ? 1002 PRO   A CB    1 
ATOM   5653 C  CG    . PRO   A 1 853  ? -5.058  -13.018 -68.791 1.00 50.81  ? 1002 PRO   A CG    1 
ATOM   5654 C  CD    . PRO   A 1 853  ? -4.511  -11.772 -68.111 1.00 51.92  ? 1002 PRO   A CD    1 
ATOM   5655 N  N     . ASN   A 1 854  ? -5.479  -13.415 -64.918 1.00 52.79  ? 1003 ASN   A N     1 
ATOM   5656 C  CA    . ASN   A 1 854  ? -5.163  -14.474 -63.914 1.00 48.31  ? 1003 ASN   A CA    1 
ATOM   5657 C  C     . ASN   A 1 854  ? -6.364  -14.663 -62.977 1.00 51.55  ? 1003 ASN   A C     1 
ATOM   5658 O  O     . ASN   A 1 854  ? -6.410  -13.996 -61.923 1.00 44.83  ? 1003 ASN   A O     1 
ATOM   5659 C  CB    . ASN   A 1 854  ? -3.909  -14.174 -63.103 1.00 45.89  ? 1003 ASN   A CB    1 
ATOM   5660 C  CG    . ASN   A 1 854  ? -2.640  -14.209 -63.927 1.00 48.35  ? 1003 ASN   A CG    1 
ATOM   5661 O  OD1   . ASN   A 1 854  ? -2.594  -14.787 -65.017 1.00 50.29  ? 1003 ASN   A OD1   1 
ATOM   5662 N  ND2   . ASN   A 1 854  ? -1.590  -13.620 -63.387 1.00 45.74  ? 1003 ASN   A ND2   1 
ATOM   5663 N  N     . VAL   A 1 855  ? -7.301  -15.531 -63.383 1.00 50.22  ? 1004 VAL   A N     1 
ATOM   5664 C  CA    . VAL   A 1 855  ? -8.449  -16.025 -62.576 1.00 51.56  ? 1004 VAL   A CA    1 
ATOM   5665 C  C     . VAL   A 1 855  ? -8.333  -17.540 -62.537 1.00 50.99  ? 1004 VAL   A C     1 
ATOM   5666 O  O     . VAL   A 1 855  ? -7.871  -18.109 -63.543 1.00 58.49  ? 1004 VAL   A O     1 
ATOM   5667 C  CB    . VAL   A 1 855  ? -9.815  -15.655 -63.177 1.00 56.88  ? 1004 VAL   A CB    1 
ATOM   5668 C  CG1   . VAL   A 1 855  ? -10.875 -15.584 -62.098 1.00 64.40  ? 1004 VAL   A CG1   1 
ATOM   5669 C  CG2   . VAL   A 1 855  ? -9.777  -14.373 -63.980 1.00 63.27  ? 1004 VAL   A CG2   1 
ATOM   5670 N  N     . CYS   A 1 856  ? -8.781  -18.164 -61.452 1.00 46.23  ? 1005 CYS   A N     1 
ATOM   5671 C  CA    . CYS   A 1 856  ? -8.818  -19.638 -61.328 1.00 51.42  ? 1005 CYS   A CA    1 
ATOM   5672 C  C     . CYS   A 1 856  ? -10.003 -20.074 -60.453 1.00 51.18  ? 1005 CYS   A C     1 
ATOM   5673 O  O     . CYS   A 1 856  ? -10.617 -19.217 -59.781 1.00 53.32  ? 1005 CYS   A O     1 
ATOM   5674 C  CB    . CYS   A 1 856  ? -7.486  -20.177 -60.829 1.00 54.74  ? 1005 CYS   A CB    1 
ATOM   5675 S  SG    . CYS   A 1 856  ? -7.231  -19.922 -59.061 1.00 56.85  ? 1005 CYS   A SG    1 
ATOM   5676 N  N     . TYR   A 1 857  ? -10.371 -21.352 -60.578 1.00 53.47  ? 1006 TYR   A N     1 
ATOM   5677 C  CA    . TYR   A 1 857  ? -11.486 -22.027 -59.868 1.00 56.78  ? 1006 TYR   A CA    1 
ATOM   5678 C  C     . TYR   A 1 857  ? -10.868 -23.154 -59.051 1.00 55.22  ? 1006 TYR   A C     1 
ATOM   5679 O  O     . TYR   A 1 857  ? -10.103 -23.927 -59.637 1.00 60.41  ? 1006 TYR   A O     1 
ATOM   5680 C  CB    . TYR   A 1 857  ? -12.511 -22.548 -60.881 1.00 59.94  ? 1006 TYR   A CB    1 
ATOM   5681 C  CG    . TYR   A 1 857  ? -13.726 -23.233 -60.302 1.00 63.17  ? 1006 TYR   A CG    1 
ATOM   5682 C  CD1   . TYR   A 1 857  ? -14.875 -22.524 -60.002 1.00 63.07  ? 1006 TYR   A CD1   1 
ATOM   5683 C  CD2   . TYR   A 1 857  ? -13.742 -24.604 -60.090 1.00 65.29  ? 1006 TYR   A CD2   1 
ATOM   5684 C  CE1   . TYR   A 1 857  ? -15.997 -23.147 -59.476 1.00 65.65  ? 1006 TYR   A CE1   1 
ATOM   5685 C  CE2   . TYR   A 1 857  ? -14.856 -25.245 -59.570 1.00 65.59  ? 1006 TYR   A CE2   1 
ATOM   5686 C  CZ    . TYR   A 1 857  ? -15.992 -24.516 -59.262 1.00 67.75  ? 1006 TYR   A CZ    1 
ATOM   5687 O  OH    . TYR   A 1 857  ? -17.096 -25.142 -58.748 1.00 62.93  ? 1006 TYR   A OH    1 
ATOM   5688 N  N     . HIS   A 1 858  ? -11.129 -23.201 -57.748 1.00 55.30  ? 1007 HIS   A N     1 
ATOM   5689 C  CA    . HIS   A 1 858  ? -10.582 -24.249 -56.844 1.00 60.69  ? 1007 HIS   A CA    1 
ATOM   5690 C  C     . HIS   A 1 858  ? -11.517 -25.472 -56.822 1.00 60.07  ? 1007 HIS   A C     1 
ATOM   5691 O  O     . HIS   A 1 858  ? -12.663 -25.327 -56.328 1.00 58.90  ? 1007 HIS   A O     1 
ATOM   5692 C  CB    . HIS   A 1 858  ? -10.355 -23.678 -55.436 1.00 58.30  ? 1007 HIS   A CB    1 
ATOM   5693 C  CG    . HIS   A 1 858  ? -10.054 -24.731 -54.423 1.00 61.63  ? 1007 HIS   A CG    1 
ATOM   5694 N  ND1   . HIS   A 1 858  ? -10.996 -25.163 -53.506 1.00 63.22  ? 1007 HIS   A ND1   1 
ATOM   5695 C  CD2   . HIS   A 1 858  ? -8.938  -25.463 -54.202 1.00 61.64  ? 1007 HIS   A CD2   1 
ATOM   5696 C  CE1   . HIS   A 1 858  ? -10.463 -26.104 -52.750 1.00 68.16  ? 1007 HIS   A CE1   1 
ATOM   5697 N  NE2   . HIS   A 1 858  ? -9.198  -26.307 -53.157 1.00 60.98  ? 1007 HIS   A NE2   1 
ATOM   5698 N  N     . LYS   A 1 859  ? -11.044 -26.640 -57.282 1.00 60.33  ? 1008 LYS   A N     1 
ATOM   5699 C  CA    . LYS   A 1 859  ? -11.791 -27.926 -57.134 1.00 70.38  ? 1008 LYS   A CA    1 
ATOM   5700 C  C     . LYS   A 1 859  ? -11.618 -28.450 -55.701 1.00 71.51  ? 1008 LYS   A C     1 
ATOM   5701 O  O     . LYS   A 1 859  ? -12.591 -28.366 -54.933 1.00 73.32  ? 1008 LYS   A O     1 
ATOM   5702 C  CB    . LYS   A 1 859  ? -11.407 -29.024 -58.135 1.00 74.23  ? 1008 LYS   A CB    1 
ATOM   5703 C  CG    . LYS   A 1 859  ? -10.250 -28.752 -59.082 1.00 84.09  ? 1008 LYS   A CG    1 
ATOM   5704 C  CD    . LYS   A 1 859  ? -10.628 -27.886 -60.265 1.00 93.03  ? 1008 LYS   A CD    1 
ATOM   5705 C  CE    . LYS   A 1 859  ? -11.650 -28.515 -61.195 1.00 94.75  ? 1008 LYS   A CE    1 
ATOM   5706 N  NZ    . LYS   A 1 859  ? -11.032 -29.481 -62.134 1.00 98.42  ? 1008 LYS   A NZ    1 
ATOM   5707 N  N     . GLU   A 1 860  ? -10.434 -28.968 -55.360 1.00 74.20  ? 1009 GLU   A N     1 
ATOM   5708 C  CA    . GLU   A 1 860  ? -10.136 -29.526 -54.011 1.00 78.83  ? 1009 GLU   A CA    1 
ATOM   5709 C  C     . GLU   A 1 860  ? -8.626  -29.467 -53.735 1.00 75.66  ? 1009 GLU   A C     1 
ATOM   5710 O  O     . GLU   A 1 860  ? -7.829  -29.442 -54.699 1.00 71.25  ? 1009 GLU   A O     1 
ATOM   5711 C  CB    . GLU   A 1 860  ? -10.702 -30.946 -53.877 1.00 85.69  ? 1009 GLU   A CB    1 
ATOM   5712 C  CG    . GLU   A 1 860  ? -9.790  -32.061 -54.378 1.00 86.84  ? 1009 GLU   A CG    1 
ATOM   5713 C  CD    . GLU   A 1 860  ? -10.054 -32.575 -55.783 1.00 93.47  ? 1009 GLU   A CD    1 
ATOM   5714 O  OE1   . GLU   A 1 860  ? -10.991 -32.087 -56.441 1.00 99.04  ? 1009 GLU   A OE1   1 
ATOM   5715 O  OE2   . GLU   A 1 860  ? -9.320  -33.479 -56.212 1.00 106.17 ? 1009 GLU   A OE2   1 
ATOM   5716 N  N     . LYS   A 1 861  ? -8.260  -29.454 -52.451 1.00 73.47  ? 1010 LYS   A N     1 
ATOM   5717 C  CA    . LYS   A 1 861  ? -6.858  -29.413 -51.971 1.00 71.66  ? 1010 LYS   A CA    1 
ATOM   5718 C  C     . LYS   A 1 861  ? -6.137  -28.264 -52.690 1.00 64.03  ? 1010 LYS   A C     1 
ATOM   5719 O  O     . LYS   A 1 861  ? -6.666  -27.131 -52.653 1.00 60.28  ? 1010 LYS   A O     1 
ATOM   5720 C  CB    . LYS   A 1 861  ? -6.224  -30.796 -52.165 1.00 80.39  ? 1010 LYS   A CB    1 
ATOM   5721 C  CG    . LYS   A 1 861  ? -6.976  -31.942 -51.501 1.00 89.94  ? 1010 LYS   A CG    1 
ATOM   5722 C  CD    . LYS   A 1 861  ? -6.075  -32.942 -50.791 1.00 95.48  ? 1010 LYS   A CD    1 
ATOM   5723 C  CE    . LYS   A 1 861  ? -6.842  -33.995 -50.018 1.00 96.67  ? 1010 LYS   A CE    1 
ATOM   5724 N  NZ    . LYS   A 1 861  ? -7.372  -35.050 -50.913 1.00 97.15  ? 1010 LYS   A NZ    1 
ATOM   5725 N  N     . ARG   A 1 862  ? -4.992  -28.544 -53.324 1.00 59.89  ? 1011 ARG   A N     1 
ATOM   5726 C  CA    . ARG   A 1 862  ? -4.136  -27.547 -54.025 1.00 63.32  ? 1011 ARG   A CA    1 
ATOM   5727 C  C     . ARG   A 1 862  ? -4.533  -27.436 -55.508 1.00 58.62  ? 1011 ARG   A C     1 
ATOM   5728 O  O     . ARG   A 1 862  ? -3.978  -26.566 -56.187 1.00 67.01  ? 1011 ARG   A O     1 
ATOM   5729 C  CB    . ARG   A 1 862  ? -2.654  -27.920 -53.881 1.00 59.19  ? 1011 ARG   A CB    1 
ATOM   5730 C  CG    . ARG   A 1 862  ? -2.075  -27.685 -52.493 1.00 57.14  ? 1011 ARG   A CG    1 
ATOM   5731 C  CD    . ARG   A 1 862  ? -0.574  -27.909 -52.436 1.00 58.83  ? 1011 ARG   A CD    1 
ATOM   5732 N  NE    . ARG   A 1 862  ? 0.131   -27.141 -53.451 1.00 60.94  ? 1011 ARG   A NE    1 
ATOM   5733 C  CZ    . ARG   A 1 862  ? 1.420   -27.261 -53.767 1.00 65.70  ? 1011 ARG   A CZ    1 
ATOM   5734 N  NH1   . ARG   A 1 862  ? 2.190   -28.136 -53.146 1.00 68.38  ? 1011 ARG   A NH1   1 
ATOM   5735 N  NH2   . ARG   A 1 862  ? 1.938   -26.499 -54.715 1.00 63.76  ? 1011 ARG   A NH2   1 
ATOM   5736 N  N     . LYS   A 1 863  ? -5.469  -28.256 -55.993 1.00 62.14  ? 1012 LYS   A N     1 
ATOM   5737 C  CA    . LYS   A 1 863  ? -5.863  -28.317 -57.427 1.00 62.86  ? 1012 LYS   A CA    1 
ATOM   5738 C  C     . LYS   A 1 863  ? -6.790  -27.142 -57.759 1.00 55.54  ? 1012 LYS   A C     1 
ATOM   5739 O  O     . LYS   A 1 863  ? -7.793  -26.945 -57.045 1.00 48.60  ? 1012 LYS   A O     1 
ATOM   5740 C  CB    . LYS   A 1 863  ? -6.544  -29.650 -57.755 1.00 74.16  ? 1012 LYS   A CB    1 
ATOM   5741 C  CG    . LYS   A 1 863  ? -6.868  -29.873 -59.230 1.00 87.91  ? 1012 LYS   A CG    1 
ATOM   5742 C  CD    . LYS   A 1 863  ? -7.242  -31.311 -59.586 1.00 97.90  ? 1012 LYS   A CD    1 
ATOM   5743 C  CE    . LYS   A 1 863  ? -8.198  -31.951 -58.595 1.00 101.75 ? 1012 LYS   A CE    1 
ATOM   5744 N  NZ    . LYS   A 1 863  ? -8.829  -33.182 -59.130 1.00 100.07 ? 1012 LYS   A NZ    1 
ATOM   5745 N  N     . ILE   A 1 864  ? -6.459  -26.403 -58.817 1.00 51.51  ? 1013 ILE   A N     1 
ATOM   5746 C  CA    . ILE   A 1 864  ? -7.262  -25.261 -59.351 1.00 55.67  ? 1013 ILE   A CA    1 
ATOM   5747 C  C     . ILE   A 1 864  ? -7.420  -25.455 -60.863 1.00 55.84  ? 1013 ILE   A C     1 
ATOM   5748 O  O     . ILE   A 1 864  ? -6.571  -26.147 -61.464 1.00 55.87  ? 1013 ILE   A O     1 
ATOM   5749 C  CB    . ILE   A 1 864  ? -6.587  -23.910 -59.001 1.00 56.50  ? 1013 ILE   A CB    1 
ATOM   5750 C  CG1   . ILE   A 1 864  ? -5.133  -23.850 -59.469 1.00 52.92  ? 1013 ILE   A CG1   1 
ATOM   5751 C  CG2   . ILE   A 1 864  ? -6.673  -23.631 -57.507 1.00 56.52  ? 1013 ILE   A CG2   1 
ATOM   5752 C  CD1   . ILE   A 1 864  ? -4.569  -22.458 -59.583 1.00 53.36  ? 1013 ILE   A CD1   1 
ATOM   5753 N  N     . LEU   A 1 865  ? -8.461  -24.867 -61.454 1.00 57.07  ? 1014 LEU   A N     1 
ATOM   5754 C  CA    . LEU   A 1 865  ? -8.666  -24.823 -62.924 1.00 61.49  ? 1014 LEU   A CA    1 
ATOM   5755 C  C     . LEU   A 1 865  ? -8.376  -23.396 -63.413 1.00 65.22  ? 1014 LEU   A C     1 
ATOM   5756 O  O     . LEU   A 1 865  ? -8.916  -22.438 -62.799 1.00 60.55  ? 1014 LEU   A O     1 
ATOM   5757 C  CB    . LEU   A 1 865  ? -10.105 -25.248 -63.220 1.00 68.71  ? 1014 LEU   A CB    1 
ATOM   5758 C  CG    . LEU   A 1 865  ? -10.420 -25.591 -64.677 1.00 82.25  ? 1014 LEU   A CG    1 
ATOM   5759 C  CD1   . LEU   A 1 865  ? -10.249 -27.083 -64.931 1.00 86.60  ? 1014 LEU   A CD1   1 
ATOM   5760 C  CD2   . LEU   A 1 865  ? -11.833 -25.148 -65.046 1.00 87.51  ? 1014 LEU   A CD2   1 
ATOM   5761 N  N     . THR   A 1 866  ? -7.549  -23.254 -64.459 1.00 63.53  ? 1015 THR   A N     1 
ATOM   5762 C  CA    . THR   A 1 866  ? -7.180  -21.951 -65.083 1.00 67.59  ? 1015 THR   A CA    1 
ATOM   5763 C  C     . THR   A 1 866  ? -8.135  -21.637 -66.252 1.00 73.95  ? 1015 THR   A C     1 
ATOM   5764 O  O     . THR   A 1 866  ? -9.026  -22.475 -66.554 1.00 77.45  ? 1015 THR   A O     1 
ATOM   5765 C  CB    . THR   A 1 866  ? -5.696  -21.945 -65.462 1.00 67.25  ? 1015 THR   A CB    1 
ATOM   5766 O  OG1   . THR   A 1 866  ? -5.486  -22.920 -66.480 1.00 73.24  ? 1015 THR   A OG1   1 
ATOM   5767 C  CG2   . THR   A 1 866  ? -4.790  -22.231 -64.287 1.00 68.08  ? 1015 THR   A CG2   1 
ATOM   5768 N  N     . THR   A 1 867  ? -7.990  -20.457 -66.867 1.00 76.05  ? 1016 THR   A N     1 
ATOM   5769 C  CA    . THR   A 1 867  ? -8.947  -19.889 -67.860 1.00 83.07  ? 1016 THR   A CA    1 
ATOM   5770 C  C     . THR   A 1 867  ? -8.866  -20.649 -69.193 1.00 85.34  ? 1016 THR   A C     1 
ATOM   5771 O  O     . THR   A 1 867  ? -9.728  -20.392 -70.056 1.00 87.41  ? 1016 THR   A O     1 
ATOM   5772 C  CB    . THR   A 1 867  ? -8.730  -18.382 -68.077 1.00 84.38  ? 1016 THR   A CB    1 
ATOM   5773 O  OG1   . THR   A 1 867  ? -7.340  -18.133 -68.274 1.00 91.28  ? 1016 THR   A OG1   1 
ATOM   5774 C  CG2   . THR   A 1 867  ? -9.225  -17.532 -66.927 1.00 84.50  ? 1016 THR   A CG2   1 
ATOM   5775 N  N     . GLU   A 1 868  ? -7.894  -21.555 -69.354 1.00 87.98  ? 1017 GLU   A N     1 
ATOM   5776 C  CA    . GLU   A 1 868  ? -7.729  -22.398 -70.571 1.00 96.48  ? 1017 GLU   A CA    1 
ATOM   5777 C  C     . GLU   A 1 868  ? -8.409  -23.753 -70.329 1.00 89.78  ? 1017 GLU   A C     1 
ATOM   5778 O  O     . GLU   A 1 868  ? -8.160  -24.681 -71.115 1.00 96.09  ? 1017 GLU   A O     1 
ATOM   5779 C  CB    . GLU   A 1 868  ? -6.250  -22.605 -70.925 1.00 104.20 ? 1017 GLU   A CB    1 
ATOM   5780 C  CG    . GLU   A 1 868  ? -5.335  -21.433 -70.598 1.00 114.76 ? 1017 GLU   A CG    1 
ATOM   5781 C  CD    . GLU   A 1 868  ? -4.742  -21.441 -69.191 1.00 123.52 ? 1017 GLU   A CD    1 
ATOM   5782 O  OE1   . GLU   A 1 868  ? -3.799  -22.230 -68.922 1.00 109.08 ? 1017 GLU   A OE1   1 
ATOM   5783 O  OE2   . GLU   A 1 868  ? -5.233  -20.660 -68.356 1.00 135.84 ? 1017 GLU   A OE2   1 
ATOM   5784 N  N     . GLY   A 1 869  ? -9.211  -23.866 -69.265 1.00 86.31  ? 1018 GLY   A N     1 
ATOM   5785 C  CA    . GLY   A 1 869  ? -9.838  -25.122 -68.809 1.00 81.80  ? 1018 GLY   A CA    1 
ATOM   5786 C  C     . GLY   A 1 869  ? -8.834  -26.103 -68.208 1.00 86.26  ? 1018 GLY   A C     1 
ATOM   5787 O  O     . GLY   A 1 869  ? -9.273  -27.193 -67.795 1.00 90.49  ? 1018 GLY   A O     1 
ATOM   5788 N  N     . ARG   A 1 870  ? -7.543  -25.750 -68.140 1.00 84.52  ? 1019 ARG   A N     1 
ATOM   5789 C  CA    . ARG   A 1 870  ? -6.436  -26.673 -67.754 1.00 86.93  ? 1019 ARG   A CA    1 
ATOM   5790 C  C     . ARG   A 1 870  ? -6.212  -26.629 -66.231 1.00 82.14  ? 1019 ARG   A C     1 
ATOM   5791 O  O     . ARG   A 1 870  ? -6.594  -25.630 -65.593 1.00 82.07  ? 1019 ARG   A O     1 
ATOM   5792 C  CB    . ARG   A 1 870  ? -5.165  -26.334 -68.543 1.00 95.74  ? 1019 ARG   A CB    1 
ATOM   5793 C  CG    . ARG   A 1 870  ? -5.186  -26.807 -69.992 1.00 107.14 ? 1019 ARG   A CG    1 
ATOM   5794 C  CD    . ARG   A 1 870  ? -3.828  -26.682 -70.663 1.00 122.06 ? 1019 ARG   A CD    1 
ATOM   5795 N  NE    . ARG   A 1 870  ? -3.363  -25.296 -70.707 1.00 136.30 ? 1019 ARG   A NE    1 
ATOM   5796 C  CZ    . ARG   A 1 870  ? -2.131  -24.900 -71.037 1.00 138.20 ? 1019 ARG   A CZ    1 
ATOM   5797 N  NH1   . ARG   A 1 870  ? -1.199  -25.784 -71.357 1.00 141.45 ? 1019 ARG   A NH1   1 
ATOM   5798 N  NH2   . ARG   A 1 870  ? -1.833  -23.611 -71.041 1.00 127.16 ? 1019 ARG   A NH2   1 
ATOM   5799 N  N     . ASN   A 1 871  ? -5.617  -27.691 -65.674 1.00 80.93  ? 1020 ASN   A N     1 
ATOM   5800 C  CA    . ASN   A 1 871  ? -5.422  -27.908 -64.212 1.00 81.16  ? 1020 ASN   A CA    1 
ATOM   5801 C  C     . ASN   A 1 871  ? -4.120  -27.251 -63.740 1.00 70.91  ? 1020 ASN   A C     1 
ATOM   5802 O  O     . ASN   A 1 871  ? -3.170  -27.135 -64.543 1.00 66.25  ? 1020 ASN   A O     1 
ATOM   5803 C  CB    . ASN   A 1 871  ? -5.440  -29.398 -63.848 1.00 83.92  ? 1020 ASN   A CB    1 
ATOM   5804 C  CG    . ASN   A 1 871  ? -6.842  -29.970 -63.769 1.00 90.33  ? 1020 ASN   A CG    1 
ATOM   5805 O  OD1   . ASN   A 1 871  ? -7.829  -29.233 -63.783 1.00 92.83  ? 1020 ASN   A OD1   1 
ATOM   5806 N  ND2   . ASN   A 1 871  ? -6.941  -31.285 -63.671 1.00 88.56  ? 1020 ASN   A ND2   1 
ATOM   5807 N  N     . ALA   A 1 872  ? -4.083  -26.844 -62.470 1.00 64.61  ? 1021 ALA   A N     1 
ATOM   5808 C  CA    . ALA   A 1 872  ? -2.932  -26.137 -61.864 1.00 67.31  ? 1021 ALA   A CA    1 
ATOM   5809 C  C     . ALA   A 1 872  ? -2.943  -26.289 -60.334 1.00 61.23  ? 1021 ALA   A C     1 
ATOM   5810 O  O     . ALA   A 1 872  ? -3.968  -26.751 -59.793 1.00 61.53  ? 1021 ALA   A O     1 
ATOM   5811 C  CB    . ALA   A 1 872  ? -2.977  -24.689 -62.305 1.00 68.34  ? 1021 ALA   A CB    1 
ATOM   5812 N  N     . LEU   A 1 873  ? -1.845  -25.891 -59.678 1.00 57.25  ? 1022 LEU   A N     1 
ATOM   5813 C  CA    . LEU   A 1 873  ? -1.627  -25.990 -58.206 1.00 59.69  ? 1022 LEU   A CA    1 
ATOM   5814 C  C     . LEU   A 1 873  ? -1.579  -24.592 -57.561 1.00 59.68  ? 1022 LEU   A C     1 
ATOM   5815 O  O     . LEU   A 1 873  ? -0.934  -23.664 -58.146 1.00 49.79  ? 1022 LEU   A O     1 
ATOM   5816 C  CB    . LEU   A 1 873  ? -0.305  -26.715 -57.929 1.00 62.39  ? 1022 LEU   A CB    1 
ATOM   5817 C  CG    . LEU   A 1 873  ? -0.182  -28.147 -58.451 1.00 66.89  ? 1022 LEU   A CG    1 
ATOM   5818 C  CD1   . LEU   A 1 873  ? 1.237   -28.673 -58.243 1.00 66.76  ? 1022 LEU   A CD1   1 
ATOM   5819 C  CD2   . LEU   A 1 873  ? -1.206  -29.063 -57.787 1.00 65.26  ? 1022 LEU   A CD2   1 
ATOM   5820 N  N     . ILE   A 1 874  ? -2.175  -24.469 -56.369 1.00 49.37  ? 1023 ILE   A N     1 
ATOM   5821 C  CA    . ILE   A 1 874  ? -1.951  -23.336 -55.428 1.00 51.26  ? 1023 ILE   A CA    1 
ATOM   5822 C  C     . ILE   A 1 874  ? -0.485  -23.402 -54.999 1.00 54.34  ? 1023 ILE   A C     1 
ATOM   5823 O  O     . ILE   A 1 874  ? -0.086  -24.476 -54.531 1.00 58.80  ? 1023 ILE   A O     1 
ATOM   5824 C  CB    . ILE   A 1 874  ? -2.913  -23.409 -54.227 1.00 50.29  ? 1023 ILE   A CB    1 
ATOM   5825 C  CG1   . ILE   A 1 874  ? -4.366  -23.201 -54.665 1.00 48.97  ? 1023 ILE   A CG1   1 
ATOM   5826 C  CG2   . ILE   A 1 874  ? -2.497  -22.430 -53.134 1.00 49.16  ? 1023 ILE   A CG2   1 
ATOM   5827 C  CD1   . ILE   A 1 874  ? -5.398  -23.510 -53.594 1.00 51.83  ? 1023 ILE   A CD1   1 
ATOM   5828 N  N     . HIS   A 1 875  ? 0.277   -22.318 -55.189 1.00 52.19  ? 1024 HIS   A N     1 
ATOM   5829 C  CA    . HIS   A 1 875  ? 1.733   -22.231 -54.887 1.00 57.28  ? 1024 HIS   A CA    1 
ATOM   5830 C  C     . HIS   A 1 875  ? 1.944   -22.464 -53.392 1.00 55.18  ? 1024 HIS   A C     1 
ATOM   5831 O  O     . HIS   A 1 875  ? 1.147   -21.902 -52.619 1.00 51.62  ? 1024 HIS   A O     1 
ATOM   5832 C  CB    . HIS   A 1 875  ? 2.322   -20.883 -55.352 1.00 62.75  ? 1024 HIS   A CB    1 
ATOM   5833 C  CG    . HIS   A 1 875  ? 3.815   -20.852 -55.417 1.00 64.28  ? 1024 HIS   A CG    1 
ATOM   5834 N  ND1   . HIS   A 1 875  ? 4.597   -20.582 -54.313 1.00 63.06  ? 1024 HIS   A ND1   1 
ATOM   5835 C  CD2   . HIS   A 1 875  ? 4.673   -21.064 -56.444 1.00 68.69  ? 1024 HIS   A CD2   1 
ATOM   5836 C  CE1   . HIS   A 1 875  ? 5.872   -20.636 -54.647 1.00 68.10  ? 1024 HIS   A CE1   1 
ATOM   5837 N  NE2   . HIS   A 1 875  ? 5.947   -20.923 -55.953 1.00 70.48  ? 1024 HIS   A NE2   1 
ATOM   5838 N  N     . LYS   A 1 876  ? 2.969   -23.251 -53.030 1.00 58.25  ? 1025 LYS   A N     1 
ATOM   5839 C  CA    . LYS   A 1 876  ? 3.330   -23.654 -51.638 1.00 67.38  ? 1025 LYS   A CA    1 
ATOM   5840 C  C     . LYS   A 1 876  ? 3.404   -22.432 -50.709 1.00 65.04  ? 1025 LYS   A C     1 
ATOM   5841 O  O     . LYS   A 1 876  ? 3.113   -22.598 -49.506 1.00 65.61  ? 1025 LYS   A O     1 
ATOM   5842 C  CB    . LYS   A 1 876  ? 4.708   -24.330 -51.591 1.00 76.94  ? 1025 LYS   A CB    1 
ATOM   5843 C  CG    . LYS   A 1 876  ? 4.783   -25.764 -52.098 1.00 88.21  ? 1025 LYS   A CG    1 
ATOM   5844 C  CD    . LYS   A 1 876  ? 6.212   -26.313 -52.143 1.00 98.04  ? 1025 LYS   A CD    1 
ATOM   5845 C  CE    . LYS   A 1 876  ? 6.465   -27.481 -51.209 1.00 101.79 ? 1025 LYS   A CE    1 
ATOM   5846 N  NZ    . LYS   A 1 876  ? 5.990   -28.763 -51.782 1.00 97.29  ? 1025 LYS   A NZ    1 
ATOM   5847 N  N     . SER   A 1 877  ? 3.834   -21.275 -51.236 1.00 60.06  ? 1026 SER   A N     1 
ATOM   5848 C  CA    . SER   A 1 877  ? 4.111   -20.019 -50.481 1.00 65.59  ? 1026 SER   A CA    1 
ATOM   5849 C  C     . SER   A 1 877  ? 2.815   -19.298 -50.073 1.00 57.69  ? 1026 SER   A C     1 
ATOM   5850 O  O     . SER   A 1 877  ? 2.895   -18.438 -49.195 1.00 53.88  ? 1026 SER   A O     1 
ATOM   5851 C  CB    . SER   A 1 877  ? 5.025   -19.093 -51.272 1.00 68.27  ? 1026 SER   A CB    1 
ATOM   5852 O  OG    . SER   A 1 877  ? 4.331   -18.443 -52.338 1.00 65.87  ? 1026 SER   A OG    1 
ATOM   5853 N  N     . SER   A 1 878  ? 1.672   -19.639 -50.677 1.00 51.67  ? 1027 SER   A N     1 
ATOM   5854 C  CA    . SER   A 1 878  ? 0.378   -18.933 -50.487 1.00 51.42  ? 1027 SER   A CA    1 
ATOM   5855 C  C     . SER   A 1 878  ? -0.178  -19.195 -49.084 1.00 51.52  ? 1027 SER   A C     1 
ATOM   5856 O  O     . SER   A 1 878  ? 0.009   -20.316 -48.581 1.00 51.08  ? 1027 SER   A O     1 
ATOM   5857 C  CB    . SER   A 1 878  ? -0.616  -19.344 -51.536 1.00 50.78  ? 1027 SER   A CB    1 
ATOM   5858 O  OG    . SER   A 1 878  ? -1.834  -18.636 -51.368 1.00 51.26  ? 1027 SER   A OG    1 
ATOM   5859 N  N     . VAL   A 1 879  ? -0.850  -18.197 -48.495 1.00 46.70  ? 1028 VAL   A N     1 
ATOM   5860 C  CA    . VAL   A 1 879  ? -1.723  -18.363 -47.290 1.00 48.69  ? 1028 VAL   A CA    1 
ATOM   5861 C  C     . VAL   A 1 879  ? -2.907  -19.282 -47.641 1.00 48.26  ? 1028 VAL   A C     1 
ATOM   5862 O  O     . VAL   A 1 879  ? -3.588  -19.785 -46.712 1.00 46.59  ? 1028 VAL   A O     1 
ATOM   5863 C  CB    . VAL   A 1 879  ? -2.228  -17.012 -46.733 1.00 43.98  ? 1028 VAL   A CB    1 
ATOM   5864 C  CG1   . VAL   A 1 879  ? -1.077  -16.078 -46.383 1.00 46.39  ? 1028 VAL   A CG1   1 
ATOM   5865 C  CG2   . VAL   A 1 879  ? -3.219  -16.342 -47.672 1.00 43.06  ? 1028 VAL   A CG2   1 
ATOM   5866 N  N     . ASN   A 1 880  ? -3.199  -19.444 -48.926 1.00 48.40  ? 1029 ASN   A N     1 
ATOM   5867 C  CA    . ASN   A 1 880  ? -4.311  -20.302 -49.395 1.00 52.13  ? 1029 ASN   A CA    1 
ATOM   5868 C  C     . ASN   A 1 880  ? -3.801  -21.737 -49.583 1.00 51.78  ? 1029 ASN   A C     1 
ATOM   5869 O  O     . ASN   A 1 880  ? -4.622  -22.606 -49.902 1.00 54.24  ? 1029 ASN   A O     1 
ATOM   5870 C  CB    . ASN   A 1 880  ? -4.955  -19.696 -50.640 1.00 51.84  ? 1029 ASN   A CB    1 
ATOM   5871 C  CG    . ASN   A 1 880  ? -5.655  -18.390 -50.338 1.00 52.85  ? 1029 ASN   A CG    1 
ATOM   5872 O  OD1   . ASN   A 1 880  ? -6.428  -18.303 -49.391 1.00 55.69  ? 1029 ASN   A OD1   1 
ATOM   5873 N  ND2   . ASN   A 1 880  ? -5.402  -17.370 -51.138 1.00 52.11  ? 1029 ASN   A ND2   1 
ATOM   5874 N  N     . CYS   A 1 881  ? -2.498  -21.986 -49.421 1.00 53.22  ? 1030 CYS   A N     1 
ATOM   5875 C  CA    . CYS   A 1 881  ? -1.947  -23.365 -49.425 1.00 55.62  ? 1030 CYS   A CA    1 
ATOM   5876 C  C     . CYS   A 1 881  ? -2.163  -24.004 -48.058 1.00 56.54  ? 1030 CYS   A C     1 
ATOM   5877 O  O     . CYS   A 1 881  ? -1.707  -23.475 -47.041 1.00 52.82  ? 1030 CYS   A O     1 
ATOM   5878 C  CB    . CYS   A 1 881  ? -0.471  -23.429 -49.776 1.00 59.75  ? 1030 CYS   A CB    1 
ATOM   5879 S  SG    . CYS   A 1 881  ? 0.047   -25.133 -50.101 1.00 53.81  ? 1030 CYS   A SG    1 
ATOM   5880 N  N     . PRO   A 1 882  ? -2.883  -25.149 -48.006 1.00 52.87  ? 1031 PRO   A N     1 
ATOM   5881 C  CA    . PRO   A 1 882  ? -3.090  -25.885 -46.754 1.00 54.12  ? 1031 PRO   A CA    1 
ATOM   5882 C  C     . PRO   A 1 882  ? -1.770  -26.253 -46.052 1.00 54.34  ? 1031 PRO   A C     1 
ATOM   5883 O  O     . PRO   A 1 882  ? -0.960  -26.926 -46.684 1.00 52.64  ? 1031 PRO   A O     1 
ATOM   5884 C  CB    . PRO   A 1 882  ? -3.812  -27.169 -47.188 1.00 53.89  ? 1031 PRO   A CB    1 
ATOM   5885 C  CG    . PRO   A 1 882  ? -4.398  -26.857 -48.554 1.00 54.80  ? 1031 PRO   A CG    1 
ATOM   5886 C  CD    . PRO   A 1 882  ? -3.498  -25.805 -49.168 1.00 51.25  ? 1031 PRO   A CD    1 
ATOM   5887 N  N     . PHE   A 1 883  ? -1.584  -25.812 -44.798 1.00 52.29  ? 1032 PHE   A N     1 
ATOM   5888 C  CA    . PHE   A 1 883  ? -0.363  -26.050 -43.972 1.00 59.09  ? 1032 PHE   A CA    1 
ATOM   5889 C  C     . PHE   A 1 883  ? -0.081  -27.560 -43.901 1.00 62.44  ? 1032 PHE   A C     1 
ATOM   5890 O  O     . PHE   A 1 883  ? 1.086   -27.955 -44.075 1.00 63.93  ? 1032 PHE   A O     1 
ATOM   5891 C  CB    . PHE   A 1 883  ? -0.493  -25.417 -42.581 1.00 56.39  ? 1032 PHE   A CB    1 
ATOM   5892 C  CG    . PHE   A 1 883  ? 0.698   -25.582 -41.663 1.00 63.92  ? 1032 PHE   A CG    1 
ATOM   5893 C  CD1   . PHE   A 1 883  ? 1.809   -24.749 -41.769 1.00 65.07  ? 1032 PHE   A CD1   1 
ATOM   5894 C  CD2   . PHE   A 1 883  ? 0.700   -26.545 -40.656 1.00 65.79  ? 1032 PHE   A CD2   1 
ATOM   5895 C  CE1   . PHE   A 1 883  ? 2.897   -24.880 -40.909 1.00 64.35  ? 1032 PHE   A CE1   1 
ATOM   5896 C  CE2   . PHE   A 1 883  ? 1.793   -26.684 -39.806 1.00 71.22  ? 1032 PHE   A CE2   1 
ATOM   5897 C  CZ    . PHE   A 1 883  ? 2.888   -25.847 -39.928 1.00 66.48  ? 1032 PHE   A CZ    1 
ATOM   5898 N  N     . SER   A 1 884  ? -1.120  -28.371 -43.692 1.00 59.58  ? 1033 SER   A N     1 
ATOM   5899 C  CA    . SER   A 1 884  ? -1.034  -29.849 -43.591 1.00 65.79  ? 1033 SER   A CA    1 
ATOM   5900 C  C     . SER   A 1 884  ? -2.222  -30.482 -44.333 1.00 70.09  ? 1033 SER   A C     1 
ATOM   5901 O  O     . SER   A 1 884  ? -2.397  -30.134 -45.522 1.00 80.21  ? 1033 SER   A O     1 
ATOM   5902 C  CB    . SER   A 1 884  ? -0.931  -30.260 -42.140 1.00 64.12  ? 1033 SER   A CB    1 
ATOM   5903 O  OG    . SER   A 1 884  ? -0.682  -31.649 -42.008 1.00 54.69  ? 1033 SER   A OG    1 
ATOM   5904 N  N     . SER   A 1 885  ? -3.014  -31.341 -43.673 1.00 67.06  ? 1034 SER   A N     1 
ATOM   5905 C  CA    . SER   A 1 885  ? -4.059  -32.201 -44.299 1.00 69.69  ? 1034 SER   A CA    1 
ATOM   5906 C  C     . SER   A 1 885  ? -5.475  -31.630 -44.090 1.00 69.04  ? 1034 SER   A C     1 
ATOM   5907 O  O     . SER   A 1 885  ? -6.361  -31.962 -44.898 1.00 81.11  ? 1034 SER   A O     1 
ATOM   5908 C  CB    . SER   A 1 885  ? -3.941  -33.623 -43.794 1.00 67.42  ? 1034 SER   A CB    1 
ATOM   5909 O  OG    . SER   A 1 885  ? -3.766  -33.655 -42.382 1.00 64.85  ? 1034 SER   A OG    1 
ATOM   5910 N  N     . GLN   A 1 886  ? -5.695  -30.837 -43.035 1.00 71.67  ? 1035 GLN   A N     1 
ATOM   5911 C  CA    . GLN   A 1 886  ? -6.922  -30.015 -42.824 1.00 68.74  ? 1035 GLN   A CA    1 
ATOM   5912 C  C     . GLN   A 1 886  ? -7.221  -29.235 -44.111 1.00 72.24  ? 1035 GLN   A C     1 
ATOM   5913 O  O     . GLN   A 1 886  ? -6.330  -28.477 -44.557 1.00 67.25  ? 1035 GLN   A O     1 
ATOM   5914 C  CB    . GLN   A 1 886  ? -6.716  -29.045 -41.659 1.00 72.50  ? 1035 GLN   A CB    1 
ATOM   5915 C  CG    . GLN   A 1 886  ? -7.906  -28.141 -41.370 1.00 76.57  ? 1035 GLN   A CG    1 
ATOM   5916 C  CD    . GLN   A 1 886  ? -9.128  -28.941 -40.993 1.00 80.71  ? 1035 GLN   A CD    1 
ATOM   5917 O  OE1   . GLN   A 1 886  ? -9.123  -29.691 -40.020 1.00 80.63  ? 1035 GLN   A OE1   1 
ATOM   5918 N  NE2   . GLN   A 1 886  ? -10.184 -28.802 -41.777 1.00 80.82  ? 1035 GLN   A NE2   1 
ATOM   5919 N  N     . ASP   A 1 887  ? -8.407  -29.435 -44.697 1.00 72.80  ? 1036 ASP   A N     1 
ATOM   5920 C  CA    . ASP   A 1 887  ? -8.836  -28.756 -45.950 1.00 75.43  ? 1036 ASP   A CA    1 
ATOM   5921 C  C     . ASP   A 1 887  ? -9.313  -27.352 -45.579 1.00 67.24  ? 1036 ASP   A C     1 
ATOM   5922 O  O     . ASP   A 1 887  ? -9.907  -27.199 -44.504 1.00 64.15  ? 1036 ASP   A O     1 
ATOM   5923 C  CB    . ASP   A 1 887  ? -9.938  -29.521 -46.696 1.00 81.53  ? 1036 ASP   A CB    1 
ATOM   5924 C  CG    . ASP   A 1 887  ? -9.478  -30.788 -47.405 1.00 87.91  ? 1036 ASP   A CG    1 
ATOM   5925 O  OD1   . ASP   A 1 887  ? -8.243  -30.945 -47.622 1.00 88.18  ? 1036 ASP   A OD1   1 
ATOM   5926 O  OD2   . ASP   A 1 887  ? -10.362 -31.614 -47.735 1.00 85.83  ? 1036 ASP   A OD2   1 
ATOM   5927 N  N     . MET   A 1 888  ? -9.053  -26.370 -46.439 1.00 67.15  ? 1037 MET   A N     1 
ATOM   5928 C  CA    . MET   A 1 888  ? -9.611  -25.007 -46.269 1.00 68.67  ? 1037 MET   A CA    1 
ATOM   5929 C  C     . MET   A 1 888  ? -11.068 -25.050 -46.750 1.00 71.73  ? 1037 MET   A C     1 
ATOM   5930 O  O     . MET   A 1 888  ? -11.374 -25.809 -47.713 1.00 61.50  ? 1037 MET   A O     1 
ATOM   5931 C  CB    . MET   A 1 888  ? -8.819  -23.949 -47.046 1.00 68.79  ? 1037 MET   A CB    1 
ATOM   5932 C  CG    . MET   A 1 888  ? -7.308  -24.175 -47.043 1.00 72.71  ? 1037 MET   A CG    1 
ATOM   5933 S  SD    . MET   A 1 888  ? -6.242  -22.789 -46.505 1.00 77.97  ? 1037 MET   A SD    1 
ATOM   5934 C  CE    . MET   A 1 888  ? -7.399  -21.449 -46.239 1.00 76.25  ? 1037 MET   A CE    1 
ATOM   5935 N  N     . LYS   A 1 889  ? -11.942 -24.322 -46.056 1.00 78.77  ? 1038 LYS   A N     1 
ATOM   5936 C  CA    . LYS   A 1 889  ? -13.360 -24.119 -46.448 1.00 83.65  ? 1038 LYS   A CA    1 
ATOM   5937 C  C     . LYS   A 1 889  ? -13.468 -22.698 -47.005 1.00 72.46  ? 1038 LYS   A C     1 
ATOM   5938 O  O     . LYS   A 1 889  ? -13.760 -21.754 -46.228 1.00 66.37  ? 1038 LYS   A O     1 
ATOM   5939 C  CB    . LYS   A 1 889  ? -14.295 -24.406 -45.267 1.00 97.33  ? 1038 LYS   A CB    1 
ATOM   5940 C  CG    . LYS   A 1 889  ? -14.757 -25.855 -45.175 1.00 108.19 ? 1038 LYS   A CG    1 
ATOM   5941 C  CD    . LYS   A 1 889  ? -15.310 -26.249 -43.823 1.00 113.34 ? 1038 LYS   A CD    1 
ATOM   5942 C  CE    . LYS   A 1 889  ? -15.992 -27.600 -43.851 1.00 114.45 ? 1038 LYS   A CE    1 
ATOM   5943 N  NZ    . LYS   A 1 889  ? -16.351 -28.052 -42.488 1.00 113.50 ? 1038 LYS   A NZ    1 
ATOM   5944 N  N     . TYR   A 1 890  ? -13.171 -22.557 -48.298 1.00 59.83  ? 1039 TYR   A N     1 
ATOM   5945 C  CA    . TYR   A 1 890  ? -13.277 -21.280 -49.042 1.00 55.28  ? 1039 TYR   A CA    1 
ATOM   5946 C  C     . TYR   A 1 890  ? -14.753 -20.933 -49.200 1.00 49.98  ? 1039 TYR   A C     1 
ATOM   5947 O  O     . TYR   A 1 890  ? -15.524 -21.764 -49.652 1.00 51.65  ? 1039 TYR   A O     1 
ATOM   5948 C  CB    . TYR   A 1 890  ? -12.604 -21.400 -50.406 1.00 52.75  ? 1039 TYR   A CB    1 
ATOM   5949 C  CG    . TYR   A 1 890  ? -11.155 -21.791 -50.377 1.00 48.39  ? 1039 TYR   A CG    1 
ATOM   5950 C  CD1   . TYR   A 1 890  ? -10.226 -21.066 -49.652 1.00 52.56  ? 1039 TYR   A CD1   1 
ATOM   5951 C  CD2   . TYR   A 1 890  ? -10.701 -22.847 -51.136 1.00 56.15  ? 1039 TYR   A CD2   1 
ATOM   5952 C  CE1   . TYR   A 1 890  ? -8.882  -21.396 -49.664 1.00 53.92  ? 1039 TYR   A CE1   1 
ATOM   5953 C  CE2   . TYR   A 1 890  ? -9.362  -23.205 -51.148 1.00 58.00  ? 1039 TYR   A CE2   1 
ATOM   5954 C  CZ    . TYR   A 1 890  ? -8.448  -22.477 -50.411 1.00 55.65  ? 1039 TYR   A CZ    1 
ATOM   5955 O  OH    . TYR   A 1 890  ? -7.135  -22.849 -50.434 1.00 59.17  ? 1039 TYR   A OH    1 
ATOM   5956 N  N     . PRO   A 1 891  ? -15.201 -19.722 -48.804 1.00 47.67  ? 1040 PRO   A N     1 
ATOM   5957 C  CA    . PRO   A 1 891  ? -16.584 -19.302 -49.020 1.00 50.14  ? 1040 PRO   A CA    1 
ATOM   5958 C  C     . PRO   A 1 891  ? -16.886 -18.915 -50.475 1.00 51.12  ? 1040 PRO   A C     1 
ATOM   5959 O  O     . PRO   A 1 891  ? -18.003 -18.548 -50.760 1.00 54.14  ? 1040 PRO   A O     1 
ATOM   5960 C  CB    . PRO   A 1 891  ? -16.716 -18.080 -48.105 1.00 52.96  ? 1040 PRO   A CB    1 
ATOM   5961 C  CG    . PRO   A 1 891  ? -15.315 -17.504 -48.063 1.00 53.68  ? 1040 PRO   A CG    1 
ATOM   5962 C  CD    . PRO   A 1 891  ? -14.409 -18.713 -48.086 1.00 49.86  ? 1040 PRO   A CD    1 
ATOM   5963 N  N     . SER   A 1 892  ? -15.868 -18.949 -51.332 1.00 48.27  ? 1041 SER   A N     1 
ATOM   5964 C  CA    . SER   A 1 892  ? -15.975 -18.787 -52.802 1.00 49.00  ? 1041 SER   A CA    1 
ATOM   5965 C  C     . SER   A 1 892  ? -14.866 -19.619 -53.417 1.00 46.66  ? 1041 SER   A C     1 
ATOM   5966 O  O     . SER   A 1 892  ? -13.796 -19.715 -52.837 1.00 49.21  ? 1041 SER   A O     1 
ATOM   5967 C  CB    . SER   A 1 892  ? -15.875 -17.339 -53.244 1.00 47.85  ? 1041 SER   A CB    1 
ATOM   5968 O  OG    . SER   A 1 892  ? -15.479 -17.244 -54.611 1.00 47.45  ? 1041 SER   A OG    1 
ATOM   5969 N  N     . PRO   A 1 893  ? -15.099 -20.269 -54.569 1.00 41.86  ? 1042 PRO   A N     1 
ATOM   5970 C  CA    . PRO   A 1 893  ? -14.042 -20.999 -55.254 1.00 43.06  ? 1042 PRO   A CA    1 
ATOM   5971 C  C     . PRO   A 1 893  ? -13.192 -20.147 -56.208 1.00 42.82  ? 1042 PRO   A C     1 
ATOM   5972 O  O     . PRO   A 1 893  ? -12.262 -20.701 -56.762 1.00 48.11  ? 1042 PRO   A O     1 
ATOM   5973 C  CB    . PRO   A 1 893  ? -14.871 -22.027 -56.034 1.00 44.47  ? 1042 PRO   A CB    1 
ATOM   5974 C  CG    . PRO   A 1 893  ? -16.072 -21.220 -56.479 1.00 47.88  ? 1042 PRO   A CG    1 
ATOM   5975 C  CD    . PRO   A 1 893  ? -16.398 -20.378 -55.255 1.00 48.08  ? 1042 PRO   A CD    1 
ATOM   5976 N  N     . PHE   A 1 894  ? -13.508 -18.857 -56.381 1.00 42.88  ? 1043 PHE   A N     1 
ATOM   5977 C  CA    . PHE   A 1 894  ? -12.846 -17.954 -57.366 1.00 44.23  ? 1043 PHE   A CA    1 
ATOM   5978 C  C     . PHE   A 1 894  ? -11.669 -17.217 -56.705 1.00 46.19  ? 1043 PHE   A C     1 
ATOM   5979 O  O     . PHE   A 1 894  ? -11.785 -16.762 -55.545 1.00 45.50  ? 1043 PHE   A O     1 
ATOM   5980 C  CB    . PHE   A 1 894  ? -13.888 -17.031 -58.009 1.00 45.70  ? 1043 PHE   A CB    1 
ATOM   5981 C  CG    . PHE   A 1 894  ? -14.920 -17.789 -58.810 1.00 47.00  ? 1043 PHE   A CG    1 
ATOM   5982 C  CD1   . PHE   A 1 894  ? -14.546 -18.517 -59.931 1.00 54.33  ? 1043 PHE   A CD1   1 
ATOM   5983 C  CD2   . PHE   A 1 894  ? -16.242 -17.853 -58.407 1.00 49.16  ? 1043 PHE   A CD2   1 
ATOM   5984 C  CE1   . PHE   A 1 894  ? -15.478 -19.251 -60.649 1.00 53.02  ? 1043 PHE   A CE1   1 
ATOM   5985 C  CE2   . PHE   A 1 894  ? -17.176 -18.579 -59.133 1.00 49.37  ? 1043 PHE   A CE2   1 
ATOM   5986 C  CZ    . PHE   A 1 894  ? -16.792 -19.288 -60.245 1.00 48.01  ? 1043 PHE   A CZ    1 
ATOM   5987 N  N     . PHE   A 1 895  ? -10.543 -17.146 -57.421 1.00 43.40  ? 1044 PHE   A N     1 
ATOM   5988 C  CA    . PHE   A 1 895  ? -9.269  -16.548 -56.952 1.00 44.97  ? 1044 PHE   A CA    1 
ATOM   5989 C  C     . PHE   A 1 895  ? -8.590  -15.820 -58.116 1.00 46.06  ? 1044 PHE   A C     1 
ATOM   5990 O  O     . PHE   A 1 895  ? -8.582  -16.384 -59.217 1.00 43.03  ? 1044 PHE   A O     1 
ATOM   5991 C  CB    . PHE   A 1 895  ? -8.312  -17.620 -56.422 1.00 47.39  ? 1044 PHE   A CB    1 
ATOM   5992 C  CG    . PHE   A 1 895  ? -8.660  -18.218 -55.081 1.00 46.29  ? 1044 PHE   A CG    1 
ATOM   5993 C  CD1   . PHE   A 1 895  ? -8.177  -17.664 -53.907 1.00 46.31  ? 1044 PHE   A CD1   1 
ATOM   5994 C  CD2   . PHE   A 1 895  ? -9.454  -19.347 -54.993 1.00 50.20  ? 1044 PHE   A CD2   1 
ATOM   5995 C  CE1   . PHE   A 1 895  ? -8.486  -18.218 -52.678 1.00 47.37  ? 1044 PHE   A CE1   1 
ATOM   5996 C  CE2   . PHE   A 1 895  ? -9.757  -19.906 -53.760 1.00 52.91  ? 1044 PHE   A CE2   1 
ATOM   5997 C  CZ    . PHE   A 1 895  ? -9.279  -19.337 -52.603 1.00 48.85  ? 1044 PHE   A CZ    1 
ATOM   5998 N  N     . VAL   A 1 896  ? -8.033  -14.627 -57.859 1.00 41.37  ? 1045 VAL   A N     1 
ATOM   5999 C  CA    . VAL   A 1 896  ? -7.104  -13.897 -58.769 1.00 39.11  ? 1045 VAL   A CA    1 
ATOM   6000 C  C     . VAL   A 1 896  ? -5.686  -14.069 -58.202 1.00 41.29  ? 1045 VAL   A C     1 
ATOM   6001 O  O     . VAL   A 1 896  ? -5.585  -14.384 -57.028 1.00 42.13  ? 1045 VAL   A O     1 
ATOM   6002 C  CB    . VAL   A 1 896  ? -7.517  -12.425 -58.937 1.00 39.98  ? 1045 VAL   A CB    1 
ATOM   6003 C  CG1   . VAL   A 1 896  ? -8.941  -12.308 -59.452 1.00 37.81  ? 1045 VAL   A CG1   1 
ATOM   6004 C  CG2   . VAL   A 1 896  ? -7.357  -11.634 -57.642 1.00 40.14  ? 1045 VAL   A CG2   1 
ATOM   6005 N  N     . PHE   A 1 897  ? -4.637  -13.961 -59.026 1.00 42.80  ? 1046 PHE   A N     1 
ATOM   6006 C  CA    . PHE   A 1 897  ? -3.237  -14.212 -58.603 1.00 41.17  ? 1046 PHE   A CA    1 
ATOM   6007 C  C     . PHE   A 1 897  ? -2.253  -13.380 -59.427 1.00 40.26  ? 1046 PHE   A C     1 
ATOM   6008 O  O     . PHE   A 1 897  ? -2.571  -12.987 -60.548 1.00 44.37  ? 1046 PHE   A O     1 
ATOM   6009 C  CB    . PHE   A 1 897  ? -2.920  -15.709 -58.647 1.00 43.37  ? 1046 PHE   A CB    1 
ATOM   6010 C  CG    . PHE   A 1 897  ? -3.230  -16.422 -59.939 1.00 44.95  ? 1046 PHE   A CG    1 
ATOM   6011 C  CD1   . PHE   A 1 897  ? -4.527  -16.815 -60.244 1.00 45.13  ? 1046 PHE   A CD1   1 
ATOM   6012 C  CD2   . PHE   A 1 897  ? -2.220  -16.736 -60.838 1.00 44.87  ? 1046 PHE   A CD2   1 
ATOM   6013 C  CE1   . PHE   A 1 897  ? -4.801  -17.494 -61.426 1.00 44.98  ? 1046 PHE   A CE1   1 
ATOM   6014 C  CE2   . PHE   A 1 897  ? -2.504  -17.400 -62.025 1.00 45.43  ? 1046 PHE   A CE2   1 
ATOM   6015 C  CZ    . PHE   A 1 897  ? -3.792  -17.780 -62.318 1.00 44.14  ? 1046 PHE   A CZ    1 
ATOM   6016 N  N     . GLY   A 1 898  ? -1.083  -13.116 -58.849 1.00 48.04  ? 1047 GLY   A N     1 
ATOM   6017 C  CA    . GLY   A 1 898  ? -0.023  -12.272 -59.430 1.00 54.07  ? 1047 GLY   A CA    1 
ATOM   6018 C  C     . GLY   A 1 898  ? 0.534   -12.854 -60.720 1.00 59.00  ? 1047 GLY   A C     1 
ATOM   6019 O  O     . GLY   A 1 898  ? 0.398   -12.205 -61.761 1.00 61.44  ? 1047 GLY   A O     1 
ATOM   6020 N  N     . GLU   A 1 899  ? 1.172   -14.022 -60.665 1.00 69.37  ? 1048 GLU   A N     1 
ATOM   6021 C  CA    . GLU   A 1 899  ? 1.838   -14.631 -61.849 1.00 72.08  ? 1048 GLU   A CA    1 
ATOM   6022 C  C     . GLU   A 1 899  ? 1.432   -16.100 -61.978 1.00 68.26  ? 1048 GLU   A C     1 
ATOM   6023 O  O     . GLU   A 1 899  ? 1.561   -16.846 -60.973 1.00 74.23  ? 1048 GLU   A O     1 
ATOM   6024 C  CB    . GLU   A 1 899  ? 3.363   -14.483 -61.788 1.00 81.81  ? 1048 GLU   A CB    1 
ATOM   6025 C  CG    . GLU   A 1 899  ? 3.941   -14.287 -60.391 1.00 82.38  ? 1048 GLU   A CG    1 
ATOM   6026 C  CD    . GLU   A 1 899  ? 5.454   -14.115 -60.356 1.00 84.78  ? 1048 GLU   A CD    1 
ATOM   6027 O  OE1   . GLU   A 1 899  ? 6.076   -14.063 -61.450 1.00 77.73  ? 1048 GLU   A OE1   1 
ATOM   6028 O  OE2   . GLU   A 1 899  ? 6.012   -14.035 -59.237 1.00 87.68  ? 1048 GLU   A OE2   1 
ATOM   6029 N  N     . LYS   A 1 900  ? 0.946   -16.467 -63.170 1.00 59.05  ? 1049 LYS   A N     1 
ATOM   6030 C  CA    . LYS   A 1 900  ? 0.737   -17.867 -63.626 1.00 63.16  ? 1049 LYS   A CA    1 
ATOM   6031 C  C     . LYS   A 1 900  ? 2.091   -18.437 -64.065 1.00 65.33  ? 1049 LYS   A C     1 
ATOM   6032 O  O     . LYS   A 1 900  ? 2.599   -18.016 -65.141 1.00 65.48  ? 1049 LYS   A O     1 
ATOM   6033 C  CB    . LYS   A 1 900  ? -0.284  -17.945 -64.772 1.00 65.70  ? 1049 LYS   A CB    1 
ATOM   6034 C  CG    . LYS   A 1 900  ? -0.925  -19.316 -64.957 1.00 61.49  ? 1049 LYS   A CG    1 
ATOM   6035 C  CD    . LYS   A 1 900  ? -1.444  -19.585 -66.350 1.00 61.84  ? 1049 LYS   A CD    1 
ATOM   6036 C  CE    . LYS   A 1 900  ? -2.932  -19.360 -66.489 1.00 63.07  ? 1049 LYS   A CE    1 
ATOM   6037 N  NZ    . LYS   A 1 900  ? -3.261  -18.707 -67.778 1.00 60.60  ? 1049 LYS   A NZ    1 
ATOM   6038 N  N     . ILE   A 1 901  ? 2.645   -19.364 -63.275 1.00 63.23  ? 1050 ILE   A N     1 
ATOM   6039 C  CA    . ILE   A 1 901  ? 4.034   -19.887 -63.449 1.00 71.59  ? 1050 ILE   A CA    1 
ATOM   6040 C  C     . ILE   A 1 901  ? 4.004   -21.300 -64.064 1.00 72.63  ? 1050 ILE   A C     1 
ATOM   6041 O  O     . ILE   A 1 901  ? 3.287   -22.184 -63.536 1.00 70.92  ? 1050 ILE   A O     1 
ATOM   6042 C  CB    . ILE   A 1 901  ? 4.785   -19.830 -62.105 1.00 69.34  ? 1050 ILE   A CB    1 
ATOM   6043 C  CG1   . ILE   A 1 901  ? 4.965   -18.383 -61.650 1.00 72.04  ? 1050 ILE   A CG1   1 
ATOM   6044 C  CG2   . ILE   A 1 901  ? 6.114   -20.563 -62.177 1.00 71.49  ? 1050 ILE   A CG2   1 
ATOM   6045 C  CD1   . ILE   A 1 901  ? 5.228   -18.251 -60.171 1.00 81.80  ? 1050 ILE   A CD1   1 
ATOM   6046 N  N     . ARG   A 1 902  ? 4.766   -21.488 -65.148 1.00 76.63  ? 1051 ARG   A N     1 
ATOM   6047 C  CA    . ARG   A 1 902  ? 5.094   -22.796 -65.779 1.00 77.47  ? 1051 ARG   A CA    1 
ATOM   6048 C  C     . ARG   A 1 902  ? 6.412   -23.302 -65.174 1.00 72.04  ? 1051 ARG   A C     1 
ATOM   6049 O  O     . ARG   A 1 902  ? 7.443   -22.633 -65.385 1.00 69.91  ? 1051 ARG   A O     1 
ATOM   6050 C  CB    . ARG   A 1 902  ? 5.194   -22.614 -67.302 1.00 84.28  ? 1051 ARG   A CB    1 
ATOM   6051 C  CG    . ARG   A 1 902  ? 5.194   -23.901 -68.118 1.00 93.74  ? 1051 ARG   A CG    1 
ATOM   6052 C  CD    . ARG   A 1 902  ? 3.848   -24.595 -68.044 1.00 102.00 ? 1051 ARG   A CD    1 
ATOM   6053 N  NE    . ARG   A 1 902  ? 3.766   -25.793 -68.867 1.00 106.34 ? 1051 ARG   A NE    1 
ATOM   6054 C  CZ    . ARG   A 1 902  ? 3.225   -26.955 -68.491 1.00 114.16 ? 1051 ARG   A CZ    1 
ATOM   6055 N  NH1   . ARG   A 1 902  ? 2.720   -27.119 -67.279 1.00 110.26 ? 1051 ARG   A NH1   1 
ATOM   6056 N  NH2   . ARG   A 1 902  ? 3.216   -27.973 -69.334 1.00 122.48 ? 1051 ARG   A NH2   1 
ATOM   6057 N  N     . THR   A 1 903  ? 6.376   -24.403 -64.408 1.00 79.42  ? 1052 THR   A N     1 
ATOM   6058 C  CA    . THR   A 1 903  ? 7.577   -25.191 -63.986 1.00 87.75  ? 1052 THR   A CA    1 
ATOM   6059 C  C     . THR   A 1 903  ? 7.454   -26.593 -64.603 1.00 87.61  ? 1052 THR   A C     1 
ATOM   6060 O  O     . THR   A 1 903  ? 7.685   -26.708 -65.815 1.00 87.61  ? 1052 THR   A O     1 
ATOM   6061 C  CB    . THR   A 1 903  ? 7.786   -25.209 -62.458 1.00 83.66  ? 1052 THR   A CB    1 
ATOM   6062 O  OG1   . THR   A 1 903  ? 6.632   -25.756 -61.813 1.00 80.68  ? 1052 THR   A OG1   1 
ATOM   6063 C  CG2   . THR   A 1 903  ? 8.110   -23.846 -61.880 1.00 79.11  ? 1052 THR   A CG2   1 
ATOM   6064 N  N     . ARG   A 1 904  ? 7.104   -27.605 -63.800 1.00 99.20  ? 1053 ARG   A N     1 
ATOM   6065 C  CA    . ARG   A 1 904  ? 6.679   -28.956 -64.259 1.00 102.12 ? 1053 ARG   A CA    1 
ATOM   6066 C  C     . ARG   A 1 904  ? 5.148   -28.961 -64.359 1.00 95.16  ? 1053 ARG   A C     1 
ATOM   6067 O  O     . ARG   A 1 904  ? 4.615   -29.487 -65.355 1.00 88.89  ? 1053 ARG   A O     1 
ATOM   6068 C  CB    . ARG   A 1 904  ? 7.217   -30.027 -63.302 1.00 112.94 ? 1053 ARG   A CB    1 
ATOM   6069 C  CG    . ARG   A 1 904  ? 8.737   -30.066 -63.221 1.00 124.27 ? 1053 ARG   A CG    1 
ATOM   6070 C  CD    . ARG   A 1 904  ? 9.277   -31.260 -62.454 1.00 129.30 ? 1053 ARG   A CD    1 
ATOM   6071 N  NE    . ARG   A 1 904  ? 8.971   -31.184 -61.030 1.00 135.33 ? 1053 ARG   A NE    1 
ATOM   6072 C  CZ    . ARG   A 1 904  ? 9.578   -30.391 -60.145 1.00 133.30 ? 1053 ARG   A CZ    1 
ATOM   6073 N  NH1   . ARG   A 1 904  ? 10.547  -29.571 -60.517 1.00 131.32 ? 1053 ARG   A NH1   1 
ATOM   6074 N  NH2   . ARG   A 1 904  ? 9.209   -30.424 -58.877 1.00 135.70 ? 1053 ARG   A NH2   1 
ATOM   6075 N  N     . ALA   A 1 905  ? 4.485   -28.368 -63.360 1.00 88.51  ? 1054 ALA   A N     1 
ATOM   6076 C  CA    . ALA   A 1 905  ? 3.032   -28.082 -63.320 1.00 82.44  ? 1054 ALA   A CA    1 
ATOM   6077 C  C     . ALA   A 1 905  ? 2.786   -26.576 -63.519 1.00 76.99  ? 1054 ALA   A C     1 
ATOM   6078 O  O     . ALA   A 1 905  ? 3.756   -25.791 -63.531 1.00 70.04  ? 1054 ALA   A O     1 
ATOM   6079 C  CB    . ALA   A 1 905  ? 2.474   -28.566 -62.004 1.00 81.72  ? 1054 ALA   A CB    1 
ATOM   6080 N  N     . ILE   A 1 906  ? 1.522   -26.185 -63.681 1.00 67.94  ? 1055 ILE   A N     1 
ATOM   6081 C  CA    . ILE   A 1 906  ? 1.094   -24.757 -63.711 1.00 71.36  ? 1055 ILE   A CA    1 
ATOM   6082 C  C     . ILE   A 1 906  ? 0.742   -24.364 -62.273 1.00 69.62  ? 1055 ILE   A C     1 
ATOM   6083 O  O     . ILE   A 1 906  ? -0.089  -25.070 -61.659 1.00 60.40  ? 1055 ILE   A O     1 
ATOM   6084 C  CB    . ILE   A 1 906  ? -0.076  -24.544 -64.697 1.00 76.04  ? 1055 ILE   A CB    1 
ATOM   6085 C  CG1   . ILE   A 1 906  ? 0.322   -24.951 -66.120 1.00 77.67  ? 1055 ILE   A CG1   1 
ATOM   6086 C  CG2   . ILE   A 1 906  ? -0.602  -23.108 -64.636 1.00 73.33  ? 1055 ILE   A CG2   1 
ATOM   6087 C  CD1   . ILE   A 1 906  ? -0.847  -25.253 -67.036 1.00 81.20  ? 1055 ILE   A CD1   1 
ATOM   6088 N  N     . SER   A 1 907  ? 1.372   -23.299 -61.763 1.00 68.90  ? 1056 SER   A N     1 
ATOM   6089 C  CA    . SER   A 1 907  ? 1.218   -22.784 -60.375 1.00 68.85  ? 1056 SER   A CA    1 
ATOM   6090 C  C     . SER   A 1 907  ? 0.636   -21.362 -60.394 1.00 64.18  ? 1056 SER   A C     1 
ATOM   6091 O  O     . SER   A 1 907  ? 1.084   -20.524 -61.220 1.00 62.45  ? 1056 SER   A O     1 
ATOM   6092 C  CB    . SER   A 1 907  ? 2.528   -22.829 -59.633 1.00 66.59  ? 1056 SER   A CB    1 
ATOM   6093 O  OG    . SER   A 1 907  ? 3.170   -24.072 -59.851 1.00 71.34  ? 1056 SER   A OG    1 
ATOM   6094 N  N     . ALA   A 1 908  ? -0.341  -21.105 -59.524 1.00 53.52  ? 1057 ALA   A N     1 
ATOM   6095 C  CA    . ALA   A 1 908  ? -0.845  -19.753 -59.208 1.00 47.10  ? 1057 ALA   A CA    1 
ATOM   6096 C  C     . ALA   A 1 908  ? -0.135  -19.238 -57.955 1.00 48.01  ? 1057 ALA   A C     1 
ATOM   6097 O  O     . ALA   A 1 908  ? -0.312  -19.864 -56.906 1.00 51.22  ? 1057 ALA   A O     1 
ATOM   6098 C  CB    . ALA   A 1 908  ? -2.330  -19.803 -59.027 1.00 47.00  ? 1057 ALA   A CB    1 
ATOM   6099 N  N     . LYS   A 1 909  ? 0.648   -18.158 -58.078 1.00 49.53  ? 1058 LYS   A N     1 
ATOM   6100 C  CA    . LYS   A 1 909  ? 1.419   -17.532 -56.964 1.00 50.17  ? 1058 LYS   A CA    1 
ATOM   6101 C  C     . LYS   A 1 909  ? 0.858   -16.143 -56.626 1.00 55.30  ? 1058 LYS   A C     1 
ATOM   6102 O  O     . LYS   A 1 909  ? 0.613   -15.326 -57.587 1.00 52.82  ? 1058 LYS   A O     1 
ATOM   6103 C  CB    . LYS   A 1 909  ? 2.895   -17.387 -57.333 1.00 52.45  ? 1058 LYS   A CB    1 
ATOM   6104 C  CG    . LYS   A 1 909  ? 3.823   -17.101 -56.164 1.00 58.31  ? 1058 LYS   A CG    1 
ATOM   6105 C  CD    . LYS   A 1 909  ? 5.288   -17.376 -56.481 1.00 64.84  ? 1058 LYS   A CD    1 
ATOM   6106 C  CE    . LYS   A 1 909  ? 6.137   -16.128 -56.560 1.00 67.04  ? 1058 LYS   A CE    1 
ATOM   6107 N  NZ    . LYS   A 1 909  ? 6.432   -15.603 -55.211 1.00 67.91  ? 1058 LYS   A NZ    1 
ATOM   6108 N  N     . GLY   A 1 910  ? 0.747   -15.859 -55.315 1.00 49.92  ? 1059 GLY   A N     1 
ATOM   6109 C  CA    . GLY   A 1 910  ? 0.119   -14.640 -54.773 1.00 48.67  ? 1059 GLY   A CA    1 
ATOM   6110 C  C     . GLY   A 1 910  ? -1.373  -14.612 -55.075 1.00 46.47  ? 1059 GLY   A C     1 
ATOM   6111 O  O     . GLY   A 1 910  ? -1.756  -13.932 -56.035 1.00 42.15  ? 1059 GLY   A O     1 
ATOM   6112 N  N     . MET   A 1 911  ? -2.180  -15.320 -54.277 1.00 44.66  ? 1060 MET   A N     1 
ATOM   6113 C  CA    . MET   A 1 911  ? -3.610  -15.606 -54.564 1.00 43.44  ? 1060 MET   A CA    1 
ATOM   6114 C  C     . MET   A 1 911  ? -4.520  -14.801 -53.648 1.00 40.40  ? 1060 MET   A C     1 
ATOM   6115 O  O     . MET   A 1 911  ? -4.253  -14.781 -52.441 1.00 38.35  ? 1060 MET   A O     1 
ATOM   6116 C  CB    . MET   A 1 911  ? -3.920  -17.082 -54.352 1.00 45.06  ? 1060 MET   A CB    1 
ATOM   6117 C  CG    . MET   A 1 911  ? -3.260  -17.940 -55.392 1.00 53.97  ? 1060 MET   A CG    1 
ATOM   6118 S  SD    . MET   A 1 911  ? -3.706  -19.658 -55.234 1.00 53.16  ? 1060 MET   A SD    1 
ATOM   6119 C  CE    . MET   A 1 911  ? -5.451  -19.597 -55.645 1.00 51.17  ? 1060 MET   A CE    1 
ATOM   6120 N  N     . THR   A 1 912  ? -5.597  -14.250 -54.209 1.00 38.63  ? 1061 THR   A N     1 
ATOM   6121 C  CA    . THR   A 1 912  ? -6.655  -13.535 -53.467 1.00 40.87  ? 1061 THR   A CA    1 
ATOM   6122 C  C     . THR   A 1 912  ? -8.019  -14.084 -53.885 1.00 41.44  ? 1061 THR   A C     1 
ATOM   6123 O  O     . THR   A 1 912  ? -8.351  -14.028 -55.081 1.00 39.49  ? 1061 THR   A O     1 
ATOM   6124 C  CB    . THR   A 1 912  ? -6.503  -12.021 -53.666 1.00 42.10  ? 1061 THR   A CB    1 
ATOM   6125 O  OG1   . THR   A 1 912  ? -5.306  -11.671 -52.964 1.00 39.86  ? 1061 THR   A OG1   1 
ATOM   6126 C  CG2   . THR   A 1 912  ? -7.699  -11.235 -53.171 1.00 39.27  ? 1061 THR   A CG2   1 
ATOM   6127 N  N     . LEU   A 1 913  ? -8.795  -14.542 -52.904 1.00 42.58  ? 1062 LEU   A N     1 
ATOM   6128 C  CA    . LEU   A 1 913  ? -10.217 -14.931 -53.069 1.00 44.14  ? 1062 LEU   A CA    1 
ATOM   6129 C  C     . LEU   A 1 913  ? -11.025 -13.724 -53.547 1.00 41.57  ? 1062 LEU   A C     1 
ATOM   6130 O  O     . LEU   A 1 913  ? -10.881 -12.627 -52.965 1.00 42.01  ? 1062 LEU   A O     1 
ATOM   6131 C  CB    . LEU   A 1 913  ? -10.759 -15.448 -51.733 1.00 46.25  ? 1062 LEU   A CB    1 
ATOM   6132 C  CG    . LEU   A 1 913  ? -12.189 -15.985 -51.770 1.00 48.72  ? 1062 LEU   A CG    1 
ATOM   6133 C  CD1   . LEU   A 1 913  ? -12.368 -17.090 -50.743 1.00 48.75  ? 1062 LEU   A CD1   1 
ATOM   6134 C  CD2   . LEU   A 1 913  ? -13.208 -14.869 -51.547 1.00 49.72  ? 1062 LEU   A CD2   1 
ATOM   6135 N  N     . VAL   A 1 914  ? -11.866 -13.932 -54.556 1.00 42.68  ? 1063 VAL   A N     1 
ATOM   6136 C  CA    . VAL   A 1 914  ? -12.870 -12.925 -54.998 1.00 46.24  ? 1063 VAL   A CA    1 
ATOM   6137 C  C     . VAL   A 1 914  ? -14.237 -13.609 -55.028 1.00 46.23  ? 1063 VAL   A C     1 
ATOM   6138 O  O     . VAL   A 1 914  ? -14.292 -14.856 -55.119 1.00 45.98  ? 1063 VAL   A O     1 
ATOM   6139 C  CB    . VAL   A 1 914  ? -12.497 -12.271 -56.340 1.00 45.31  ? 1063 VAL   A CB    1 
ATOM   6140 C  CG1   . VAL   A 1 914  ? -11.160 -11.562 -56.238 1.00 46.73  ? 1063 VAL   A CG1   1 
ATOM   6141 C  CG2   . VAL   A 1 914  ? -12.493 -13.248 -57.501 1.00 44.06  ? 1063 VAL   A CG2   1 
ATOM   6142 N  N     . THR   A 1 915  ? -15.300 -12.823 -54.900 1.00 44.86  ? 1064 THR   A N     1 
ATOM   6143 C  CA    . THR   A 1 915  ? -16.685 -13.321 -55.084 1.00 48.90  ? 1064 THR   A CA    1 
ATOM   6144 C  C     . THR   A 1 915  ? -16.997 -13.403 -56.576 1.00 46.93  ? 1064 THR   A C     1 
ATOM   6145 O  O     . THR   A 1 915  ? -16.311 -12.808 -57.403 1.00 46.33  ? 1064 THR   A O     1 
ATOM   6146 C  CB    . THR   A 1 915  ? -17.691 -12.435 -54.356 1.00 49.09  ? 1064 THR   A CB    1 
ATOM   6147 O  OG1   . THR   A 1 915  ? -17.826 -11.283 -55.186 1.00 45.41  ? 1064 THR   A OG1   1 
ATOM   6148 C  CG2   . THR   A 1 915  ? -17.246 -12.118 -52.945 1.00 50.63  ? 1064 THR   A CG2   1 
ATOM   6149 N  N     . PRO   A 1 916  ? -18.047 -14.157 -56.955 1.00 48.90  ? 1065 PRO   A N     1 
ATOM   6150 C  CA    . PRO   A 1 916  ? -18.556 -14.148 -58.328 1.00 45.64  ? 1065 PRO   A CA    1 
ATOM   6151 C  C     . PRO   A 1 916  ? -18.911 -12.752 -58.862 1.00 42.28  ? 1065 PRO   A C     1 
ATOM   6152 O  O     . PRO   A 1 916  ? -18.731 -12.536 -60.031 1.00 44.79  ? 1065 PRO   A O     1 
ATOM   6153 C  CB    . PRO   A 1 916  ? -19.826 -15.004 -58.254 1.00 49.11  ? 1065 PRO   A CB    1 
ATOM   6154 C  CG    . PRO   A 1 916  ? -19.594 -15.903 -57.051 1.00 54.41  ? 1065 PRO   A CG    1 
ATOM   6155 C  CD    . PRO   A 1 916  ? -18.811 -15.051 -56.070 1.00 51.60  ? 1065 PRO   A CD    1 
ATOM   6156 N  N     . LEU   A 1 917  ? -19.375 -11.830 -58.010 1.00 41.21  ? 1066 LEU   A N     1 
ATOM   6157 C  CA    . LEU   A 1 917  ? -19.697 -10.433 -58.420 1.00 39.60  ? 1066 LEU   A CA    1 
ATOM   6158 C  C     . LEU   A 1 917  ? -18.429 -9.698  -58.858 1.00 39.82  ? 1066 LEU   A C     1 
ATOM   6159 O  O     . LEU   A 1 917  ? -18.478 -8.943  -59.842 1.00 43.23  ? 1066 LEU   A O     1 
ATOM   6160 C  CB    . LEU   A 1 917  ? -20.368 -9.708  -57.259 1.00 44.01  ? 1066 LEU   A CB    1 
ATOM   6161 C  CG    . LEU   A 1 917  ? -21.649 -10.351 -56.735 1.00 43.38  ? 1066 LEU   A CG    1 
ATOM   6162 C  CD1   . LEU   A 1 917  ? -22.446 -9.332  -55.952 1.00 43.89  ? 1066 LEU   A CD1   1 
ATOM   6163 C  CD2   . LEU   A 1 917  ? -22.483 -10.918 -57.875 1.00 44.64  ? 1066 LEU   A CD2   1 
ATOM   6164 N  N     . GLN   A 1 918  ? -17.326 -9.882  -58.140 1.00 42.40  ? 1067 GLN   A N     1 
ATOM   6165 C  CA    . GLN   A 1 918  ? -16.044 -9.227  -58.482 1.00 40.26  ? 1067 GLN   A CA    1 
ATOM   6166 C  C     . GLN   A 1 918  ? -15.513 -9.865  -59.761 1.00 42.83  ? 1067 GLN   A C     1 
ATOM   6167 O  O     . GLN   A 1 918  ? -14.959 -9.130  -60.596 1.00 44.22  ? 1067 GLN   A O     1 
ATOM   6168 C  CB    . GLN   A 1 918  ? -15.066 -9.358  -57.328 1.00 40.96  ? 1067 GLN   A CB    1 
ATOM   6169 C  CG    . GLN   A 1 918  ? -15.389 -8.444  -56.167 1.00 41.83  ? 1067 GLN   A CG    1 
ATOM   6170 C  CD    . GLN   A 1 918  ? -14.611 -8.859  -54.940 1.00 43.95  ? 1067 GLN   A CD    1 
ATOM   6171 O  OE1   . GLN   A 1 918  ? -14.470 -10.049 -54.645 1.00 44.13  ? 1067 GLN   A OE1   1 
ATOM   6172 N  NE2   . GLN   A 1 918  ? -14.090 -7.877  -54.222 1.00 42.51  ? 1067 GLN   A NE2   1 
ATOM   6173 N  N     . LEU   A 1 919  ? -15.685 -11.182 -59.911 1.00 47.84  ? 1068 LEU   A N     1 
ATOM   6174 C  CA    . LEU   A 1 919  ? -15.345 -11.896 -61.170 1.00 50.73  ? 1068 LEU   A CA    1 
ATOM   6175 C  C     . LEU   A 1 919  ? -16.001 -11.162 -62.353 1.00 48.28  ? 1068 LEU   A C     1 
ATOM   6176 O  O     . LEU   A 1 919  ? -15.265 -10.703 -63.253 1.00 45.06  ? 1068 LEU   A O     1 
ATOM   6177 C  CB    . LEU   A 1 919  ? -15.801 -13.352 -61.069 1.00 53.56  ? 1068 LEU   A CB    1 
ATOM   6178 C  CG    . LEU   A 1 919  ? -15.563 -14.190 -62.322 1.00 64.05  ? 1068 LEU   A CG    1 
ATOM   6179 C  CD1   . LEU   A 1 919  ? -14.079 -14.287 -62.638 1.00 67.29  ? 1068 LEU   A CD1   1 
ATOM   6180 C  CD2   . LEU   A 1 919  ? -16.164 -15.579 -62.166 1.00 67.65  ? 1068 LEU   A CD2   1 
ATOM   6181 N  N     . LEU   A 1 920  ? -17.324 -10.987 -62.318 1.00 49.12  ? 1069 LEU   A N     1 
ATOM   6182 C  CA    . LEU   A 1 920  ? -18.112 -10.396 -63.437 1.00 53.40  ? 1069 LEU   A CA    1 
ATOM   6183 C  C     . LEU   A 1 920  ? -17.748 -8.921  -63.672 1.00 50.17  ? 1069 LEU   A C     1 
ATOM   6184 O  O     . LEU   A 1 920  ? -17.800 -8.468  -64.837 1.00 55.94  ? 1069 LEU   A O     1 
ATOM   6185 C  CB    . LEU   A 1 920  ? -19.601 -10.533 -63.123 1.00 49.81  ? 1069 LEU   A CB    1 
ATOM   6186 C  CG    . LEU   A 1 920  ? -20.174 -11.907 -63.431 1.00 50.40  ? 1069 LEU   A CG    1 
ATOM   6187 C  CD1   . LEU   A 1 920  ? -21.483 -12.116 -62.684 1.00 55.11  ? 1069 LEU   A CD1   1 
ATOM   6188 C  CD2   . LEU   A 1 920  ? -20.349 -12.074 -64.930 1.00 52.72  ? 1069 LEU   A CD2   1 
ATOM   6189 N  N     . LEU   A 1 921  ? -17.415 -8.191  -62.614 1.00 46.40  ? 1070 LEU   A N     1 
ATOM   6190 C  CA    . LEU   A 1 921  ? -17.183 -6.733  -62.700 1.00 43.08  ? 1070 LEU   A CA    1 
ATOM   6191 C  C     . LEU   A 1 921  ? -15.800 -6.460  -63.289 1.00 43.23  ? 1070 LEU   A C     1 
ATOM   6192 O  O     . LEU   A 1 921  ? -15.718 -5.563  -64.157 1.00 45.37  ? 1070 LEU   A O     1 
ATOM   6193 C  CB    . LEU   A 1 921  ? -17.289 -6.109  -61.311 1.00 43.20  ? 1070 LEU   A CB    1 
ATOM   6194 C  CG    . LEU   A 1 921  ? -17.092 -4.599  -61.292 1.00 43.71  ? 1070 LEU   A CG    1 
ATOM   6195 C  CD1   . LEU   A 1 921  ? -18.189 -3.928  -62.094 1.00 44.92  ? 1070 LEU   A CD1   1 
ATOM   6196 C  CD2   . LEU   A 1 921  ? -17.055 -4.068  -59.867 1.00 46.68  ? 1070 LEU   A CD2   1 
ATOM   6197 N  N     . PHE   A 1 922  ? -14.746 -7.124  -62.791 1.00 39.87  ? 1071 PHE   A N     1 
ATOM   6198 C  CA    . PHE   A 1 922  ? -13.350 -6.708  -63.093 1.00 43.72  ? 1071 PHE   A CA    1 
ATOM   6199 C  C     . PHE   A 1 922  ? -12.469 -7.829  -63.663 1.00 40.25  ? 1071 PHE   A C     1 
ATOM   6200 O  O     . PHE   A 1 922  ? -11.465 -7.456  -64.256 1.00 46.32  ? 1071 PHE   A O     1 
ATOM   6201 C  CB    . PHE   A 1 922  ? -12.744 -6.018  -61.867 1.00 44.18  ? 1071 PHE   A CB    1 
ATOM   6202 C  CG    . PHE   A 1 922  ? -13.206 -4.596  -61.638 1.00 41.60  ? 1071 PHE   A CG    1 
ATOM   6203 C  CD1   . PHE   A 1 922  ? -13.190 -3.665  -62.663 1.00 44.91  ? 1071 PHE   A CD1   1 
ATOM   6204 C  CD2   . PHE   A 1 922  ? -13.627 -4.184  -60.388 1.00 46.18  ? 1071 PHE   A CD2   1 
ATOM   6205 C  CE1   . PHE   A 1 922  ? -13.586 -2.357  -62.442 1.00 49.15  ? 1071 PHE   A CE1   1 
ATOM   6206 C  CE2   . PHE   A 1 922  ? -14.041 -2.879  -60.170 1.00 50.29  ? 1071 PHE   A CE2   1 
ATOM   6207 C  CZ    . PHE   A 1 922  ? -14.015 -1.964  -61.197 1.00 50.26  ? 1071 PHE   A CZ    1 
ATOM   6208 N  N     . ALA   A 1 923  ? -12.819 -9.110  -63.527 1.00 44.33  ? 1072 ALA   A N     1 
ATOM   6209 C  CA    . ALA   A 1 923  ? -12.011 -10.266 -63.985 1.00 44.48  ? 1072 ALA   A CA    1 
ATOM   6210 C  C     . ALA   A 1 923  ? -12.717 -11.042 -65.112 1.00 49.85  ? 1072 ALA   A C     1 
ATOM   6211 O  O     . ALA   A 1 923  ? -12.600 -12.281 -65.128 1.00 50.51  ? 1072 ALA   A O     1 
ATOM   6212 C  CB    . ALA   A 1 923  ? -11.733 -11.161 -62.806 1.00 46.34  ? 1072 ALA   A CB    1 
ATOM   6213 N  N     . SER   A 1 924  ? -13.360 -10.337 -66.050 1.00 50.36  ? 1073 SER   A N     1 
ATOM   6214 C  CA    . SER   A 1 924  ? -14.214 -10.890 -67.138 1.00 50.65  ? 1073 SER   A CA    1 
ATOM   6215 C  C     . SER   A 1 924  ? -14.140 -9.960  -68.348 1.00 53.81  ? 1073 SER   A C     1 
ATOM   6216 O  O     . SER   A 1 924  ? -14.566 -8.798  -68.203 1.00 60.41  ? 1073 SER   A O     1 
ATOM   6217 C  CB    . SER   A 1 924  ? -15.652 -11.009 -66.700 1.00 51.55  ? 1073 SER   A CB    1 
ATOM   6218 O  OG    . SER   A 1 924  ? -15.845 -12.099 -65.814 1.00 52.35  ? 1073 SER   A OG    1 
ATOM   6219 N  N     . LYS   A 1 925  ? -13.636 -10.433 -69.489 1.00 61.98  ? 1074 LYS   A N     1 
ATOM   6220 C  CA    . LYS   A 1 925  ? -13.614 -9.632  -70.745 1.00 67.19  ? 1074 LYS   A CA    1 
ATOM   6221 C  C     . LYS   A 1 925  ? -14.909 -9.864  -71.524 1.00 65.83  ? 1074 LYS   A C     1 
ATOM   6222 O  O     . LYS   A 1 925  ? -15.375 -8.896  -72.143 1.00 73.38  ? 1074 LYS   A O     1 
ATOM   6223 C  CB    . LYS   A 1 925  ? -12.409 -9.946  -71.636 1.00 69.51  ? 1074 LYS   A CB    1 
ATOM   6224 C  CG    . LYS   A 1 925  ? -12.132 -8.879  -72.691 1.00 77.76  ? 1074 LYS   A CG    1 
ATOM   6225 C  CD    . LYS   A 1 925  ? -11.249 -9.332  -73.842 1.00 83.36  ? 1074 LYS   A CD    1 
ATOM   6226 C  CE    . LYS   A 1 925  ? -9.768  -9.254  -73.541 1.00 85.71  ? 1074 LYS   A CE    1 
ATOM   6227 N  NZ    . LYS   A 1 925  ? -8.971  -9.268  -74.790 1.00 88.41  ? 1074 LYS   A NZ    1 
ATOM   6228 N  N     . LYS   A 1 926  ? -15.451 -11.088 -71.491 1.00 69.08  ? 1075 LYS   A N     1 
ATOM   6229 C  CA    . LYS   A 1 926  ? -16.596 -11.528 -72.334 1.00 64.99  ? 1075 LYS   A CA    1 
ATOM   6230 C  C     . LYS   A 1 926  ? -17.537 -12.424 -71.523 1.00 55.69  ? 1075 LYS   A C     1 
ATOM   6231 O  O     . LYS   A 1 926  ? -17.064 -13.345 -70.853 1.00 59.06  ? 1075 LYS   A O     1 
ATOM   6232 C  CB    . LYS   A 1 926  ? -16.083 -12.248 -73.583 1.00 70.62  ? 1075 LYS   A CB    1 
ATOM   6233 C  CG    . LYS   A 1 926  ? -17.134 -12.540 -74.650 1.00 81.53  ? 1075 LYS   A CG    1 
ATOM   6234 C  CD    . LYS   A 1 926  ? -16.566 -13.163 -75.920 1.00 83.78  ? 1075 LYS   A CD    1 
ATOM   6235 C  CE    . LYS   A 1 926  ? -16.133 -14.607 -75.751 1.00 88.31  ? 1075 LYS   A CE    1 
ATOM   6236 N  NZ    . LYS   A 1 926  ? -14.873 -14.890 -76.481 1.00 90.23  ? 1075 LYS   A NZ    1 
ATOM   6237 N  N     . VAL   A 1 927  ? -18.838 -12.166 -71.629 1.00 59.74  ? 1076 VAL   A N     1 
ATOM   6238 C  CA    . VAL   A 1 927  ? -19.932 -12.805 -70.843 1.00 57.61  ? 1076 VAL   A CA    1 
ATOM   6239 C  C     . VAL   A 1 927  ? -21.106 -13.040 -71.801 1.00 59.80  ? 1076 VAL   A C     1 
ATOM   6240 O  O     . VAL   A 1 927  ? -21.612 -12.040 -72.352 1.00 58.34  ? 1076 VAL   A O     1 
ATOM   6241 C  CB    . VAL   A 1 927  ? -20.352 -11.904 -69.666 1.00 58.52  ? 1076 VAL   A CB    1 
ATOM   6242 C  CG1   . VAL   A 1 927  ? -21.452 -12.538 -68.827 1.00 63.12  ? 1076 VAL   A CG1   1 
ATOM   6243 C  CG2   . VAL   A 1 927  ? -19.173 -11.515 -68.791 1.00 59.18  ? 1076 VAL   A CG2   1 
ATOM   6244 N  N     . GLN   A 1 928  ? -21.501 -14.302 -72.002 1.00 66.02  ? 1077 GLN   A N     1 
ATOM   6245 C  CA    . GLN   A 1 928  ? -22.693 -14.720 -72.793 1.00 66.13  ? 1077 GLN   A CA    1 
ATOM   6246 C  C     . GLN   A 1 928  ? -23.751 -15.251 -71.824 1.00 61.12  ? 1077 GLN   A C     1 
ATOM   6247 O  O     . GLN   A 1 928  ? -23.385 -16.070 -70.973 1.00 63.52  ? 1077 GLN   A O     1 
ATOM   6248 C  CB    . GLN   A 1 928  ? -22.362 -15.835 -73.788 1.00 73.37  ? 1077 GLN   A CB    1 
ATOM   6249 C  CG    . GLN   A 1 928  ? -21.243 -15.514 -74.770 1.00 81.37  ? 1077 GLN   A CG    1 
ATOM   6250 C  CD    . GLN   A 1 928  ? -20.860 -16.731 -75.581 1.00 90.21  ? 1077 GLN   A CD    1 
ATOM   6251 O  OE1   . GLN   A 1 928  ? -21.717 -17.504 -76.017 1.00 83.43  ? 1077 GLN   A OE1   1 
ATOM   6252 N  NE2   . GLN   A 1 928  ? -19.560 -16.921 -75.769 1.00 91.39  ? 1077 GLN   A NE2   1 
ATOM   6253 N  N     . SER   A 1 929  ? -25.002 -14.805 -71.954 1.00 59.84  ? 1078 SER   A N     1 
ATOM   6254 C  CA    . SER   A 1 929  ? -26.169 -15.295 -71.171 1.00 60.02  ? 1078 SER   A CA    1 
ATOM   6255 C  C     . SER   A 1 929  ? -27.138 -16.059 -72.085 1.00 63.51  ? 1078 SER   A C     1 
ATOM   6256 O  O     . SER   A 1 929  ? -27.351 -15.608 -73.236 1.00 58.05  ? 1078 SER   A O     1 
ATOM   6257 C  CB    . SER   A 1 929  ? -26.876 -14.171 -70.498 1.00 56.76  ? 1078 SER   A CB    1 
ATOM   6258 O  OG    . SER   A 1 929  ? -28.052 -14.635 -69.850 1.00 63.74  ? 1078 SER   A OG    1 
ATOM   6259 N  N     . ASP   A 1 930  ? -27.708 -17.156 -71.573 1.00 63.95  ? 1079 ASP   A N     1 
ATOM   6260 C  CA    . ASP   A 1 930  ? -28.761 -17.976 -72.237 1.00 65.04  ? 1079 ASP   A CA    1 
ATOM   6261 C  C     . ASP   A 1 930  ? -30.130 -17.707 -71.584 1.00 67.25  ? 1079 ASP   A C     1 
ATOM   6262 O  O     . ASP   A 1 930  ? -31.126 -18.312 -72.048 1.00 70.03  ? 1079 ASP   A O     1 
ATOM   6263 C  CB    . ASP   A 1 930  ? -28.386 -19.466 -72.236 1.00 60.92  ? 1079 ASP   A CB    1 
ATOM   6264 C  CG    . ASP   A 1 930  ? -28.580 -20.222 -70.932 1.00 63.85  ? 1079 ASP   A CG    1 
ATOM   6265 O  OD1   . ASP   A 1 930  ? -29.151 -19.645 -69.976 1.00 71.12  ? 1079 ASP   A OD1   1 
ATOM   6266 O  OD2   . ASP   A 1 930  ? -28.166 -21.401 -70.884 1.00 75.18  ? 1079 ASP   A OD2   1 
ATOM   6267 N  N     . GLY   A 1 931  ? -30.179 -16.836 -70.567 1.00 60.19  ? 1080 GLY   A N     1 
ATOM   6268 C  CA    . GLY   A 1 931  ? -31.383 -16.537 -69.767 1.00 62.01  ? 1080 GLY   A CA    1 
ATOM   6269 C  C     . GLY   A 1 931  ? -31.232 -17.000 -68.328 1.00 65.45  ? 1080 GLY   A C     1 
ATOM   6270 O  O     . GLY   A 1 931  ? -31.763 -16.308 -67.431 1.00 64.85  ? 1080 GLY   A O     1 
ATOM   6271 N  N     . GLN   A 1 932  ? -30.517 -18.112 -68.114 1.00 67.02  ? 1081 GLN   A N     1 
ATOM   6272 C  CA    . GLN   A 1 932  ? -30.394 -18.809 -66.802 1.00 73.32  ? 1081 GLN   A CA    1 
ATOM   6273 C  C     . GLN   A 1 932  ? -28.924 -18.869 -66.365 1.00 69.89  ? 1081 GLN   A C     1 
ATOM   6274 O  O     . GLN   A 1 932  ? -28.631 -18.630 -65.168 1.00 70.15  ? 1081 GLN   A O     1 
ATOM   6275 C  CB    . GLN   A 1 932  ? -30.926 -20.245 -66.910 1.00 83.28  ? 1081 GLN   A CB    1 
ATOM   6276 C  CG    . GLN   A 1 932  ? -32.443 -20.359 -67.004 1.00 90.35  ? 1081 GLN   A CG    1 
ATOM   6277 C  CD    . GLN   A 1 932  ? -33.130 -19.999 -65.708 1.00 99.42  ? 1081 GLN   A CD    1 
ATOM   6278 O  OE1   . GLN   A 1 932  ? -33.170 -18.836 -65.308 1.00 101.62 ? 1081 GLN   A OE1   1 
ATOM   6279 N  NE2   . GLN   A 1 932  ? -33.686 -21.000 -65.040 1.00 99.27  ? 1081 GLN   A NE2   1 
ATOM   6280 N  N     . ILE   A 1 933  ? -28.053 -19.243 -67.300 1.00 60.35  ? 1082 ILE   A N     1 
ATOM   6281 C  CA    . ILE   A 1 933  ? -26.608 -19.526 -67.092 1.00 61.53  ? 1082 ILE   A CA    1 
ATOM   6282 C  C     . ILE   A 1 933  ? -25.842 -18.476 -67.899 1.00 67.13  ? 1082 ILE   A C     1 
ATOM   6283 O  O     . ILE   A 1 933  ? -26.246 -18.233 -69.053 1.00 72.44  ? 1082 ILE   A O     1 
ATOM   6284 C  CB    . ILE   A 1 933  ? -26.290 -20.967 -67.555 1.00 61.94  ? 1082 ILE   A CB    1 
ATOM   6285 C  CG1   . ILE   A 1 933  ? -27.264 -22.000 -66.970 1.00 67.96  ? 1082 ILE   A CG1   1 
ATOM   6286 C  CG2   . ILE   A 1 933  ? -24.846 -21.347 -67.282 1.00 58.95  ? 1082 ILE   A CG2   1 
ATOM   6287 C  CD1   . ILE   A 1 933  ? -27.299 -22.058 -65.455 1.00 69.73  ? 1082 ILE   A CD1   1 
ATOM   6288 N  N     . VAL   A 1 934  ? -24.810 -17.846 -67.325 1.00 63.35  ? 1083 VAL   A N     1 
ATOM   6289 C  CA    . VAL   A 1 934  ? -23.874 -16.991 -68.114 1.00 58.97  ? 1083 VAL   A CA    1 
ATOM   6290 C  C     . VAL   A 1 934  ? -22.553 -17.750 -68.196 1.00 55.47  ? 1083 VAL   A C     1 
ATOM   6291 O  O     . VAL   A 1 934  ? -22.267 -18.532 -67.274 1.00 49.99  ? 1083 VAL   A O     1 
ATOM   6292 C  CB    . VAL   A 1 934  ? -23.707 -15.563 -67.553 1.00 58.66  ? 1083 VAL   A CB    1 
ATOM   6293 C  CG1   . VAL   A 1 934  ? -25.019 -15.002 -67.034 1.00 61.73  ? 1083 VAL   A CG1   1 
ATOM   6294 C  CG2   . VAL   A 1 934  ? -22.644 -15.472 -66.477 1.00 60.37  ? 1083 VAL   A CG2   1 
ATOM   6295 N  N     . LEU   A 1 935  ? -21.818 -17.543 -69.287 1.00 57.40  ? 1084 LEU   A N     1 
ATOM   6296 C  CA    . LEU   A 1 935  ? -20.523 -18.205 -69.580 1.00 59.87  ? 1084 LEU   A CA    1 
ATOM   6297 C  C     . LEU   A 1 935  ? -19.466 -17.108 -69.640 1.00 56.96  ? 1084 LEU   A C     1 
ATOM   6298 O  O     . LEU   A 1 935  ? -19.594 -16.180 -70.473 1.00 57.45  ? 1084 LEU   A O     1 
ATOM   6299 C  CB    . LEU   A 1 935  ? -20.587 -18.999 -70.892 1.00 62.58  ? 1084 LEU   A CB    1 
ATOM   6300 C  CG    . LEU   A 1 935  ? -19.268 -19.640 -71.339 1.00 65.65  ? 1084 LEU   A CG    1 
ATOM   6301 C  CD1   . LEU   A 1 935  ? -18.887 -20.805 -70.437 1.00 63.12  ? 1084 LEU   A CD1   1 
ATOM   6302 C  CD2   . LEU   A 1 935  ? -19.329 -20.086 -72.798 1.00 70.10  ? 1084 LEU   A CD2   1 
ATOM   6303 N  N     . VAL   A 1 936  ? -18.478 -17.218 -68.761 1.00 50.98  ? 1085 VAL   A N     1 
ATOM   6304 C  CA    . VAL   A 1 936  ? -17.469 -16.159 -68.534 1.00 50.44  ? 1085 VAL   A CA    1 
ATOM   6305 C  C     . VAL   A 1 936  ? -16.209 -16.578 -69.277 1.00 49.38  ? 1085 VAL   A C     1 
ATOM   6306 O  O     . VAL   A 1 936  ? -15.689 -17.652 -68.950 1.00 54.76  ? 1085 VAL   A O     1 
ATOM   6307 C  CB    . VAL   A 1 936  ? -17.231 -15.965 -67.031 1.00 49.28  ? 1085 VAL   A CB    1 
ATOM   6308 C  CG1   . VAL   A 1 936  ? -16.167 -14.915 -66.790 1.00 56.63  ? 1085 VAL   A CG1   1 
ATOM   6309 C  CG2   . VAL   A 1 936  ? -18.515 -15.604 -66.309 1.00 48.75  ? 1085 VAL   A CG2   1 
ATOM   6310 N  N     . ASP   A 1 937  ? -15.760 -15.768 -70.241 1.00 51.87  ? 1086 ASP   A N     1 
ATOM   6311 C  CA    . ASP   A 1 937  ? -14.508 -15.979 -71.022 1.00 57.63  ? 1086 ASP   A CA    1 
ATOM   6312 C  C     . ASP   A 1 937  ? -14.362 -17.464 -71.415 1.00 59.02  ? 1086 ASP   A C     1 
ATOM   6313 O  O     . ASP   A 1 937  ? -13.232 -17.972 -71.370 1.00 60.10  ? 1086 ASP   A O     1 
ATOM   6314 C  CB    . ASP   A 1 937  ? -13.289 -15.453 -70.245 1.00 60.60  ? 1086 ASP   A CB    1 
ATOM   6315 C  CG    . ASP   A 1 937  ? -13.231 -13.943 -70.026 1.00 62.33  ? 1086 ASP   A CG    1 
ATOM   6316 O  OD1   . ASP   A 1 937  ? -13.665 -13.174 -70.926 1.00 65.77  ? 1086 ASP   A OD1   1 
ATOM   6317 O  OD2   . ASP   A 1 937  ? -12.715 -13.538 -68.967 1.00 69.95  ? 1086 ASP   A OD2   1 
ATOM   6318 N  N     . ASP   A 1 938  ? -15.465 -18.134 -71.787 1.00 70.56  ? 1087 ASP   A N     1 
ATOM   6319 C  CA    . ASP   A 1 938  ? -15.511 -19.493 -72.412 1.00 74.15  ? 1087 ASP   A CA    1 
ATOM   6320 C  C     . ASP   A 1 938  ? -14.877 -20.584 -71.532 1.00 67.88  ? 1087 ASP   A C     1 
ATOM   6321 O  O     . ASP   A 1 938  ? -14.472 -21.604 -72.100 1.00 65.95  ? 1087 ASP   A O     1 
ATOM   6322 C  CB    . ASP   A 1 938  ? -14.831 -19.487 -73.788 1.00 75.56  ? 1087 ASP   A CB    1 
ATOM   6323 C  CG    . ASP   A 1 938  ? -15.647 -18.786 -74.861 1.00 85.64  ? 1087 ASP   A CG    1 
ATOM   6324 O  OD1   . ASP   A 1 938  ? -16.839 -19.155 -75.036 1.00 92.27  ? 1087 ASP   A OD1   1 
ATOM   6325 O  OD2   . ASP   A 1 938  ? -15.093 -17.867 -75.504 1.00 89.68  ? 1087 ASP   A OD2   1 
ATOM   6326 N  N     . TRP   A 1 939  ? -14.817 -20.412 -70.207 1.00 71.17  ? 1088 TRP   A N     1 
ATOM   6327 C  CA    . TRP   A 1 939  ? -14.137 -21.368 -69.287 1.00 68.60  ? 1088 TRP   A CA    1 
ATOM   6328 C  C     . TRP   A 1 939  ? -14.948 -21.643 -68.001 1.00 66.49  ? 1088 TRP   A C     1 
ATOM   6329 O  O     . TRP   A 1 939  ? -14.630 -22.656 -67.350 1.00 68.78  ? 1088 TRP   A O     1 
ATOM   6330 C  CB    . TRP   A 1 939  ? -12.718 -20.871 -68.965 1.00 76.12  ? 1088 TRP   A CB    1 
ATOM   6331 C  CG    . TRP   A 1 939  ? -12.666 -19.905 -67.821 1.00 83.13  ? 1088 TRP   A CG    1 
ATOM   6332 C  CD1   . TRP   A 1 939  ? -12.920 -18.564 -67.854 1.00 86.71  ? 1088 TRP   A CD1   1 
ATOM   6333 C  CD2   . TRP   A 1 939  ? -12.383 -20.222 -66.448 1.00 85.96  ? 1088 TRP   A CD2   1 
ATOM   6334 N  NE1   . TRP   A 1 939  ? -12.806 -18.023 -66.602 1.00 88.79  ? 1088 TRP   A NE1   1 
ATOM   6335 C  CE2   . TRP   A 1 939  ? -12.481 -19.016 -65.719 1.00 91.87  ? 1088 TRP   A CE2   1 
ATOM   6336 C  CE3   . TRP   A 1 939  ? -12.060 -21.404 -65.772 1.00 85.45  ? 1088 TRP   A CE3   1 
ATOM   6337 C  CZ2   . TRP   A 1 939  ? -12.262 -18.960 -64.344 1.00 94.76  ? 1088 TRP   A CZ2   1 
ATOM   6338 C  CZ3   . TRP   A 1 939  ? -11.832 -21.345 -64.417 1.00 85.36  ? 1088 TRP   A CZ3   1 
ATOM   6339 C  CH2   . TRP   A 1 939  ? -11.934 -20.141 -63.716 1.00 93.06  ? 1088 TRP   A CH2   1 
ATOM   6340 N  N     . ILE   A 1 940  ? -15.909 -20.800 -67.591 1.00 57.01  ? 1089 ILE   A N     1 
ATOM   6341 C  CA    . ILE   A 1 940  ? -16.646 -21.036 -66.312 1.00 58.41  ? 1089 ILE   A CA    1 
ATOM   6342 C  C     . ILE   A 1 940  ? -18.056 -20.446 -66.381 1.00 56.48  ? 1089 ILE   A C     1 
ATOM   6343 O  O     . ILE   A 1 940  ? -18.248 -19.394 -67.006 1.00 51.55  ? 1089 ILE   A O     1 
ATOM   6344 C  CB    . ILE   A 1 940  ? -15.870 -20.512 -65.083 1.00 66.88  ? 1089 ILE   A CB    1 
ATOM   6345 C  CG1   . ILE   A 1 940  ? -16.392 -21.127 -63.776 1.00 79.51  ? 1089 ILE   A CG1   1 
ATOM   6346 C  CG2   . ILE   A 1 940  ? -15.884 -18.992 -65.014 1.00 59.86  ? 1089 ILE   A CG2   1 
ATOM   6347 C  CD1   . ILE   A 1 940  ? -16.300 -22.649 -63.683 1.00 77.79  ? 1089 ILE   A CD1   1 
ATOM   6348 N  N     . ARG   A 1 941  ? -18.996 -21.111 -65.714 1.00 57.70  ? 1090 ARG   A N     1 
ATOM   6349 C  CA    . ARG   A 1 941  ? -20.449 -20.849 -65.845 1.00 65.52  ? 1090 ARG   A CA    1 
ATOM   6350 C  C     . ARG   A 1 941  ? -21.002 -20.469 -64.470 1.00 58.00  ? 1090 ARG   A C     1 
ATOM   6351 O  O     . ARG   A 1 941  ? -20.644 -21.143 -63.497 1.00 57.62  ? 1090 ARG   A O     1 
ATOM   6352 C  CB    . ARG   A 1 941  ? -21.128 -22.084 -66.451 1.00 73.75  ? 1090 ARG   A CB    1 
ATOM   6353 C  CG    . ARG   A 1 941  ? -20.337 -22.740 -67.579 1.00 78.67  ? 1090 ARG   A CG    1 
ATOM   6354 C  CD    . ARG   A 1 941  ? -21.223 -23.500 -68.543 1.00 81.90  ? 1090 ARG   A CD    1 
ATOM   6355 N  NE    . ARG   A 1 941  ? -21.921 -24.586 -67.872 1.00 90.78  ? 1090 ARG   A NE    1 
ATOM   6356 C  CZ    . ARG   A 1 941  ? -21.708 -25.886 -68.071 1.00 99.16  ? 1090 ARG   A CZ    1 
ATOM   6357 N  NH1   . ARG   A 1 941  ? -20.814 -26.303 -68.953 1.00 105.83 ? 1090 ARG   A NH1   1 
ATOM   6358 N  NH2   . ARG   A 1 941  ? -22.404 -26.776 -67.384 1.00 94.48  ? 1090 ARG   A NH2   1 
ATOM   6359 N  N     . LEU   A 1 942  ? -21.819 -19.413 -64.408 1.00 52.58  ? 1091 LEU   A N     1 
ATOM   6360 C  CA    . LEU   A 1 942  ? -22.541 -18.981 -63.188 1.00 51.54  ? 1091 LEU   A CA    1 
ATOM   6361 C  C     . LEU   A 1 942  ? -24.040 -19.139 -63.432 1.00 54.84  ? 1091 LEU   A C     1 
ATOM   6362 O  O     . LEU   A 1 942  ? -24.525 -18.687 -64.490 1.00 60.30  ? 1091 LEU   A O     1 
ATOM   6363 C  CB    . LEU   A 1 942  ? -22.215 -17.520 -62.852 1.00 51.25  ? 1091 LEU   A CB    1 
ATOM   6364 C  CG    . LEU   A 1 942  ? -20.755 -17.084 -62.989 1.00 52.92  ? 1091 LEU   A CG    1 
ATOM   6365 C  CD1   . LEU   A 1 942  ? -20.629 -15.606 -62.674 1.00 55.48  ? 1091 LEU   A CD1   1 
ATOM   6366 C  CD2   . LEU   A 1 942  ? -19.826 -17.897 -62.099 1.00 52.45  ? 1091 LEU   A CD2   1 
ATOM   6367 N  N     . GLN   A 1 943  ? -24.734 -19.752 -62.476 1.00 55.33  ? 1092 GLN   A N     1 
ATOM   6368 C  CA    . GLN   A 1 943  ? -26.205 -19.670 -62.334 1.00 58.84  ? 1092 GLN   A CA    1 
ATOM   6369 C  C     . GLN   A 1 943  ? -26.518 -18.340 -61.629 1.00 60.33  ? 1092 GLN   A C     1 
ATOM   6370 O  O     . GLN   A 1 943  ? -26.495 -18.284 -60.379 1.00 59.91  ? 1092 GLN   A O     1 
ATOM   6371 C  CB    . GLN   A 1 943  ? -26.712 -20.914 -61.605 1.00 64.90  ? 1092 GLN   A CB    1 
ATOM   6372 C  CG    . GLN   A 1 943  ? -28.202 -21.188 -61.774 1.00 74.15  ? 1092 GLN   A CG    1 
ATOM   6373 C  CD    . GLN   A 1 943  ? -28.620 -22.397 -60.965 1.00 79.38  ? 1092 GLN   A CD    1 
ATOM   6374 O  OE1   . GLN   A 1 943  ? -28.088 -23.495 -61.129 1.00 81.37  ? 1092 GLN   A OE1   1 
ATOM   6375 N  NE2   . GLN   A 1 943  ? -29.561 -22.201 -60.056 1.00 84.92  ? 1092 GLN   A NE2   1 
ATOM   6376 N  N     . ILE   A 1 944  ? -26.786 -17.298 -62.415 1.00 58.76  ? 1093 ILE   A N     1 
ATOM   6377 C  CA    . ILE   A 1 944  ? -27.103 -15.925 -61.924 1.00 59.49  ? 1093 ILE   A CA    1 
ATOM   6378 C  C     . ILE   A 1 944  ? -28.149 -15.305 -62.855 1.00 55.17  ? 1093 ILE   A C     1 
ATOM   6379 O  O     . ILE   A 1 944  ? -28.067 -15.540 -64.065 1.00 57.51  ? 1093 ILE   A O     1 
ATOM   6380 C  CB    . ILE   A 1 944  ? -25.810 -15.081 -61.865 1.00 59.52  ? 1093 ILE   A CB    1 
ATOM   6381 C  CG1   . ILE   A 1 944  ? -26.020 -13.712 -61.218 1.00 63.10  ? 1093 ILE   A CG1   1 
ATOM   6382 C  CG2   . ILE   A 1 944  ? -25.170 -14.948 -63.240 1.00 60.96  ? 1093 ILE   A CG2   1 
ATOM   6383 C  CD1   . ILE   A 1 944  ? -24.731 -12.912 -61.076 1.00 67.82  ? 1093 ILE   A CD1   1 
ATOM   6384 N  N     . SER   A 1 945  ? -29.083 -14.531 -62.307 1.00 56.66  ? 1094 SER   A N     1 
ATOM   6385 C  CA    . SER   A 1 945  ? -30.006 -13.652 -63.068 1.00 55.27  ? 1094 SER   A CA    1 
ATOM   6386 C  C     . SER   A 1 945  ? -29.284 -13.041 -64.277 1.00 58.89  ? 1094 SER   A C     1 
ATOM   6387 O  O     . SER   A 1 945  ? -28.119 -12.639 -64.130 1.00 62.09  ? 1094 SER   A O     1 
ATOM   6388 C  CB    . SER   A 1 945  ? -30.539 -12.583 -62.176 1.00 58.17  ? 1094 SER   A CB    1 
ATOM   6389 O  OG    . SER   A 1 945  ? -30.480 -11.319 -62.816 1.00 68.40  ? 1094 SER   A OG    1 
ATOM   6390 N  N     . HIS   A 1 946  ? -29.955 -12.963 -65.427 1.00 56.18  ? 1095 HIS   A N     1 
ATOM   6391 C  CA    . HIS   A 1 946  ? -29.455 -12.270 -66.638 1.00 56.09  ? 1095 HIS   A CA    1 
ATOM   6392 C  C     . HIS   A 1 946  ? -29.307 -10.772 -66.326 1.00 62.34  ? 1095 HIS   A C     1 
ATOM   6393 O  O     . HIS   A 1 946  ? -28.266 -10.175 -66.683 1.00 64.65  ? 1095 HIS   A O     1 
ATOM   6394 C  CB    . HIS   A 1 946  ? -30.381 -12.536 -67.840 1.00 56.64  ? 1095 HIS   A CB    1 
ATOM   6395 C  CG    . HIS   A 1 946  ? -30.025 -11.728 -69.045 1.00 56.53  ? 1095 HIS   A CG    1 
ATOM   6396 N  ND1   . HIS   A 1 946  ? -29.264 -12.242 -70.086 1.00 51.22  ? 1095 HIS   A ND1   1 
ATOM   6397 C  CD2   . HIS   A 1 946  ? -30.271 -10.432 -69.354 1.00 50.46  ? 1095 HIS   A CD2   1 
ATOM   6398 C  CE1   . HIS   A 1 946  ? -29.072 -11.300 -70.991 1.00 50.54  ? 1095 HIS   A CE1   1 
ATOM   6399 N  NE2   . HIS   A 1 946  ? -29.676 -10.176 -70.563 1.00 51.41  ? 1095 HIS   A NE2   1 
ATOM   6400 N  N     . GLU   A 1 947  ? -30.303 -10.179 -65.672 1.00 60.47  ? 1096 GLU   A N     1 
ATOM   6401 C  CA    . GLU   A 1 947  ? -30.349 -8.711  -65.450 1.00 61.80  ? 1096 GLU   A CA    1 
ATOM   6402 C  C     . GLU   A 1 947  ? -29.176 -8.306  -64.551 1.00 58.05  ? 1096 GLU   A C     1 
ATOM   6403 O  O     . GLU   A 1 947  ? -28.483 -7.325  -64.904 1.00 56.17  ? 1096 GLU   A O     1 
ATOM   6404 C  CB    . GLU   A 1 947  ? -31.712 -8.297  -64.900 1.00 67.78  ? 1096 GLU   A CB    1 
ATOM   6405 C  CG    . GLU   A 1 947  ? -32.850 -8.644  -65.851 1.00 73.87  ? 1096 GLU   A CG    1 
ATOM   6406 C  CD    . GLU   A 1 947  ? -33.357 -10.077 -65.768 1.00 77.91  ? 1096 GLU   A CD    1 
ATOM   6407 O  OE1   . GLU   A 1 947  ? -32.887 -10.821 -64.887 1.00 80.17  ? 1096 GLU   A OE1   1 
ATOM   6408 O  OE2   . GLU   A 1 947  ? -34.213 -10.452 -66.589 1.00 78.56  ? 1096 GLU   A OE2   1 
ATOM   6409 N  N     . ALA   A 1 948  ? -28.927 -9.054  -63.470 1.00 53.27  ? 1097 ALA   A N     1 
ATOM   6410 C  CA    . ALA   A 1 948  ? -27.800 -8.809  -62.540 1.00 51.77  ? 1097 ALA   A CA    1 
ATOM   6411 C  C     . ALA   A 1 948  ? -26.479 -8.807  -63.335 1.00 51.94  ? 1097 ALA   A C     1 
ATOM   6412 O  O     . ALA   A 1 948  ? -25.751 -7.804  -63.245 1.00 48.19  ? 1097 ALA   A O     1 
ATOM   6413 C  CB    . ALA   A 1 948  ? -27.795 -9.818  -61.422 1.00 47.93  ? 1097 ALA   A CB    1 
ATOM   6414 N  N     . ALA   A 1 949  ? -26.205 -9.848  -64.129 1.00 46.69  ? 1098 ALA   A N     1 
ATOM   6415 C  CA    . ALA   A 1 949  ? -24.958 -9.976  -64.920 1.00 51.01  ? 1098 ALA   A CA    1 
ATOM   6416 C  C     . ALA   A 1 949  ? -24.838 -8.834  -65.942 1.00 53.17  ? 1098 ALA   A C     1 
ATOM   6417 O  O     . ALA   A 1 949  ? -23.717 -8.301  -66.115 1.00 50.46  ? 1098 ALA   A O     1 
ATOM   6418 C  CB    . ALA   A 1 949  ? -24.893 -11.328 -65.585 1.00 52.83  ? 1098 ALA   A CB    1 
ATOM   6419 N  N     . ALA   A 1 950  ? -25.938 -8.444  -66.590 1.00 50.74  ? 1099 ALA   A N     1 
ATOM   6420 C  CA    . ALA   A 1 950  ? -25.940 -7.348  -67.585 1.00 49.55  ? 1099 ALA   A CA    1 
ATOM   6421 C  C     . ALA   A 1 950  ? -25.716 -6.006  -66.879 1.00 49.99  ? 1099 ALA   A C     1 
ATOM   6422 O  O     . ALA   A 1 950  ? -25.051 -5.139  -67.464 1.00 56.64  ? 1099 ALA   A O     1 
ATOM   6423 C  CB    . ALA   A 1 950  ? -27.237 -7.342  -68.351 1.00 52.18  ? 1099 ALA   A CB    1 
ATOM   6424 N  N     . CYS   A 1 951  ? -26.299 -5.832  -65.692 1.00 45.74  ? 1100 CYS   A N     1 
ATOM   6425 C  CA    . CYS   A 1 951  ? -26.180 -4.609  -64.860 1.00 48.65  ? 1100 CYS   A CA    1 
ATOM   6426 C  C     . CYS   A 1 951  ? -24.729 -4.458  -64.392 1.00 47.89  ? 1100 CYS   A C     1 
ATOM   6427 O  O     . CYS   A 1 951  ? -24.170 -3.347  -64.477 1.00 53.22  ? 1100 CYS   A O     1 
ATOM   6428 C  CB    . CYS   A 1 951  ? -27.129 -4.658  -63.668 1.00 55.07  ? 1100 CYS   A CB    1 
ATOM   6429 S  SG    . CYS   A 1 951  ? -28.828 -4.158  -64.072 1.00 56.68  ? 1100 CYS   A SG    1 
ATOM   6430 N  N     . ILE   A 1 952  ? -24.105 -5.556  -63.991 1.00 46.83  ? 1101 ILE   A N     1 
ATOM   6431 C  CA    . ILE   A 1 952  ? -22.691 -5.552  -63.521 1.00 48.74  ? 1101 ILE   A CA    1 
ATOM   6432 C  C     . ILE   A 1 952  ? -21.763 -5.235  -64.696 1.00 50.32  ? 1101 ILE   A C     1 
ATOM   6433 O  O     . ILE   A 1 952  ? -20.834 -4.437  -64.496 1.00 50.02  ? 1101 ILE   A O     1 
ATOM   6434 C  CB    . ILE   A 1 952  ? -22.361 -6.861  -62.789 1.00 47.22  ? 1101 ILE   A CB    1 
ATOM   6435 C  CG1   . ILE   A 1 952  ? -23.084 -6.862  -61.437 1.00 43.39  ? 1101 ILE   A CG1   1 
ATOM   6436 C  CG2   . ILE   A 1 952  ? -20.854 -7.025  -62.649 1.00 50.02  ? 1101 ILE   A CG2   1 
ATOM   6437 C  CD1   . ILE   A 1 952  ? -23.086 -8.183  -60.717 1.00 47.17  ? 1101 ILE   A CD1   1 
ATOM   6438 N  N     . THR   A 1 953  ? -22.052 -5.752  -65.889 1.00 49.73  ? 1102 THR   A N     1 
ATOM   6439 C  CA    . THR   A 1 953  ? -21.271 -5.458  -67.112 1.00 45.84  ? 1102 THR   A CA    1 
ATOM   6440 C  C     . THR   A 1 953  ? -21.419 -3.971  -67.464 1.00 50.28  ? 1102 THR   A C     1 
ATOM   6441 O  O     . THR   A 1 953  ? -20.426 -3.359  -67.944 1.00 51.66  ? 1102 THR   A O     1 
ATOM   6442 C  CB    . THR   A 1 953  ? -21.662 -6.411  -68.242 1.00 52.37  ? 1102 THR   A CB    1 
ATOM   6443 O  OG1   . THR   A 1 953  ? -21.423 -7.754  -67.814 1.00 56.81  ? 1102 THR   A OG1   1 
ATOM   6444 C  CG2   . THR   A 1 953  ? -20.884 -6.146  -69.511 1.00 55.81  ? 1102 THR   A CG2   1 
ATOM   6445 N  N     . ALA   A 1 954  ? -22.584 -3.367  -67.224 1.00 52.65  ? 1103 ALA   A N     1 
ATOM   6446 C  CA    . ALA   A 1 954  ? -22.815 -1.939  -67.556 1.00 49.09  ? 1103 ALA   A CA    1 
ATOM   6447 C  C     . ALA   A 1 954  ? -22.073 -1.066  -66.544 1.00 46.25  ? 1103 ALA   A C     1 
ATOM   6448 O  O     . ALA   A 1 954  ? -21.630 0.028   -66.939 1.00 49.99  ? 1103 ALA   A O     1 
ATOM   6449 C  CB    . ALA   A 1 954  ? -24.287 -1.612  -67.588 1.00 49.05  ? 1103 ALA   A CB    1 
ATOM   6450 N  N     . LEU   A 1 955  ? -21.968 -1.511  -65.283 1.00 43.40  ? 1104 LEU   A N     1 
ATOM   6451 C  CA    . LEU   A 1 955  ? -21.136 -0.813  -64.261 1.00 47.13  ? 1104 LEU   A CA    1 
ATOM   6452 C  C     . LEU   A 1 955  ? -19.677 -0.798  -64.736 1.00 45.28  ? 1104 LEU   A C     1 
ATOM   6453 O  O     . LEU   A 1 955  ? -19.068 0.284   -64.715 1.00 46.28  ? 1104 LEU   A O     1 
ATOM   6454 C  CB    . LEU   A 1 955  ? -21.252 -1.485  -62.894 1.00 46.47  ? 1104 LEU   A CB    1 
ATOM   6455 C  CG    . LEU   A 1 955  ? -22.562 -1.257  -62.149 1.00 45.85  ? 1104 LEU   A CG    1 
ATOM   6456 C  CD1   . LEU   A 1 955  ? -22.613 -2.137  -60.912 1.00 47.55  ? 1104 LEU   A CD1   1 
ATOM   6457 C  CD2   . LEU   A 1 955  ? -22.753 0.199   -61.784 1.00 41.70  ? 1104 LEU   A CD2   1 
ATOM   6458 N  N     . ARG   A 1 956  ? -19.150 -1.932  -65.204 1.00 43.13  ? 1105 ARG   A N     1 
ATOM   6459 C  CA    A ARG   A 1 956  ? -17.760 -1.976  -65.718 0.50 44.68  ? 1105 ARG   A CA    1 
ATOM   6460 C  CA    B ARG   A 1 956  ? -17.775 -2.016  -65.761 0.50 46.41  ? 1105 ARG   A CA    1 
ATOM   6461 C  C     . ARG   A 1 956  ? -17.592 -0.885  -66.788 1.00 47.90  ? 1105 ARG   A C     1 
ATOM   6462 O  O     . ARG   A 1 956  ? -16.580 -0.159  -66.701 1.00 47.38  ? 1105 ARG   A O     1 
ATOM   6463 C  CB    A ARG   A 1 956  ? -17.384 -3.361  -66.239 0.50 42.10  ? 1105 ARG   A CB    1 
ATOM   6464 C  CB    B ARG   A 1 956  ? -17.549 -3.406  -66.359 0.50 46.67  ? 1105 ARG   A CB    1 
ATOM   6465 C  CG    A ARG   A 1 956  ? -15.969 -3.432  -66.795 0.50 42.13  ? 1105 ARG   A CG    1 
ATOM   6466 C  CG    B ARG   A 1 956  ? -16.097 -3.735  -66.674 0.50 49.28  ? 1105 ARG   A CG    1 
ATOM   6467 C  CD    A ARG   A 1 956  ? -14.907 -2.786  -65.915 0.50 41.87  ? 1105 ARG   A CD    1 
ATOM   6468 C  CD    B ARG   A 1 956  ? -15.937 -5.193  -67.072 0.50 50.83  ? 1105 ARG   A CD    1 
ATOM   6469 N  NE    A ARG   A 1 956  ? -13.615 -2.804  -66.587 0.50 40.69  ? 1105 ARG   A NE    1 
ATOM   6470 N  NE    B ARG   A 1 956  ? -15.985 -5.383  -68.513 0.50 52.30  ? 1105 ARG   A NE    1 
ATOM   6471 C  CZ    A ARG   A 1 956  ? -12.894 -3.897  -66.795 0.50 39.35  ? 1105 ARG   A CZ    1 
ATOM   6472 C  CZ    B ARG   A 1 956  ? -16.445 -6.466  -69.126 0.50 54.39  ? 1105 ARG   A CZ    1 
ATOM   6473 N  NH1   A ARG   A 1 956  ? -13.312 -5.078  -66.370 0.50 40.27  ? 1105 ARG   A NH1   1 
ATOM   6474 N  NH1   B ARG   A 1 956  ? -16.949 -7.480  -68.436 0.50 51.33  ? 1105 ARG   A NH1   1 
ATOM   6475 N  NH2   A ARG   A 1 956  ? -11.750 -3.803  -67.433 0.50 39.62  ? 1105 ARG   A NH2   1 
ATOM   6476 N  NH2   B ARG   A 1 956  ? -16.411 -6.516  -70.445 0.50 58.67  ? 1105 ARG   A NH2   1 
ATOM   6477 N  N     . ALA   A 1 957  ? -18.558 -0.736  -67.707 1.00 45.79  ? 1106 ALA   A N     1 
ATOM   6478 C  CA    . ALA   A 1 957  ? -18.464 0.196   -68.862 1.00 45.52  ? 1106 ALA   A CA    1 
ATOM   6479 C  C     . ALA   A 1 957  ? -18.554 1.632   -68.362 1.00 42.40  ? 1106 ALA   A C     1 
ATOM   6480 O  O     . ALA   A 1 957  ? -17.789 2.470   -68.872 1.00 46.84  ? 1106 ALA   A O     1 
ATOM   6481 C  CB    . ALA   A 1 957  ? -19.532 -0.084  -69.907 1.00 46.05  ? 1106 ALA   A CB    1 
ATOM   6482 N  N     . ALA   A 1 958  ? -19.433 1.901   -67.394 1.00 39.62  ? 1107 ALA   A N     1 
ATOM   6483 C  CA    . ALA   A 1 958  ? -19.576 3.234   -66.768 1.00 43.61  ? 1107 ALA   A CA    1 
ATOM   6484 C  C     . ALA   A 1 958  ? -18.252 3.615   -66.093 1.00 44.65  ? 1107 ALA   A C     1 
ATOM   6485 O  O     . ALA   A 1 958  ? -17.781 4.780   -66.275 1.00 49.94  ? 1107 ALA   A O     1 
ATOM   6486 C  CB    . ALA   A 1 958  ? -20.732 3.225   -65.800 1.00 47.57  ? 1107 ALA   A CB    1 
ATOM   6487 N  N     . MET   A 1 959  ? -17.647 2.658   -65.386 1.00 45.22  ? 1108 MET   A N     1 
ATOM   6488 C  CA    . MET   A 1 959  ? -16.346 2.828   -64.687 1.00 47.37  ? 1108 MET   A CA    1 
ATOM   6489 C  C     . MET   A 1 959  ? -15.236 3.154   -65.703 1.00 47.40  ? 1108 MET   A C     1 
ATOM   6490 O  O     . MET   A 1 959  ? -14.432 4.092   -65.434 1.00 49.28  ? 1108 MET   A O     1 
ATOM   6491 C  CB    . MET   A 1 959  ? -15.998 1.567   -63.891 1.00 47.20  ? 1108 MET   A CB    1 
ATOM   6492 C  CG    . MET   A 1 959  ? -14.780 1.730   -63.007 1.00 45.49  ? 1108 MET   A CG    1 
ATOM   6493 S  SD    . MET   A 1 959  ? -15.040 2.923   -61.660 1.00 47.15  ? 1108 MET   A SD    1 
ATOM   6494 C  CE    . MET   A 1 959  ? -13.356 3.519   -61.516 1.00 45.65  ? 1108 MET   A CE    1 
ATOM   6495 N  N     . GLU   A 1 960  ? -15.201 2.456   -66.840 1.00 47.15  ? 1109 GLU   A N     1 
ATOM   6496 C  CA    . GLU   A 1 960  ? -14.218 2.712   -67.937 1.00 53.03  ? 1109 GLU   A CA    1 
ATOM   6497 C  C     . GLU   A 1 960  ? -14.373 4.139   -68.467 1.00 51.76  ? 1109 GLU   A C     1 
ATOM   6498 O  O     . GLU   A 1 960  ? -13.346 4.774   -68.749 1.00 51.41  ? 1109 GLU   A O     1 
ATOM   6499 C  CB    . GLU   A 1 960  ? -14.401 1.758   -69.120 1.00 56.27  ? 1109 GLU   A CB    1 
ATOM   6500 C  CG    . GLU   A 1 960  ? -13.957 0.337   -68.827 1.00 66.49  ? 1109 GLU   A CG    1 
ATOM   6501 C  CD    . GLU   A 1 960  ? -12.455 0.175   -68.671 1.00 72.69  ? 1109 GLU   A CD    1 
ATOM   6502 O  OE1   . GLU   A 1 960  ? -11.731 1.147   -68.984 1.00 70.97  ? 1109 GLU   A OE1   1 
ATOM   6503 O  OE2   . GLU   A 1 960  ? -12.016 -0.921  -68.237 1.00 76.51  ? 1109 GLU   A OE2   1 
ATOM   6504 N  N     . ALA   A 1 961  ? -15.613 4.613   -68.624 1.00 49.58  ? 1110 ALA   A N     1 
ATOM   6505 C  CA    . ALA   A 1 961  ? -15.919 5.934   -69.217 1.00 47.27  ? 1110 ALA   A CA    1 
ATOM   6506 C  C     . ALA   A 1 961  ? -15.566 7.033   -68.210 1.00 46.71  ? 1110 ALA   A C     1 
ATOM   6507 O  O     . ALA   A 1 961  ? -15.234 8.138   -68.650 1.00 52.32  ? 1110 ALA   A O     1 
ATOM   6508 C  CB    . ALA   A 1 961  ? -17.379 6.002   -69.639 1.00 49.26  ? 1110 ALA   A CB    1 
ATOM   6509 N  N     . LEU   A 1 962  ? -15.663 6.743   -66.910 1.00 45.58  ? 1111 LEU   A N     1 
ATOM   6510 C  CA    . LEU   A 1 962  ? -15.284 7.707   -65.848 1.00 46.67  ? 1111 LEU   A CA    1 
ATOM   6511 C  C     . LEU   A 1 962  ? -13.757 7.813   -65.794 1.00 46.26  ? 1111 LEU   A C     1 
ATOM   6512 O  O     . LEU   A 1 962  ? -13.245 8.925   -65.580 1.00 45.39  ? 1111 LEU   A O     1 
ATOM   6513 C  CB    . LEU   A 1 962  ? -15.859 7.261   -64.500 1.00 46.40  ? 1111 LEU   A CB    1 
ATOM   6514 C  CG    . LEU   A 1 962  ? -15.551 8.201   -63.333 1.00 47.41  ? 1111 LEU   A CG    1 
ATOM   6515 C  CD1   . LEU   A 1 962  ? -15.885 9.639   -63.690 1.00 46.77  ? 1111 LEU   A CD1   1 
ATOM   6516 C  CD2   . LEU   A 1 962  ? -16.303 7.777   -62.083 1.00 49.26  ? 1111 LEU   A CD2   1 
ATOM   6517 N  N     . VAL   A 1 963  ? -13.057 6.700   -66.002 1.00 45.35  ? 1112 VAL   A N     1 
ATOM   6518 C  CA    . VAL   A 1 963  ? -11.568 6.676   -65.984 1.00 44.20  ? 1112 VAL   A CA    1 
ATOM   6519 C  C     . VAL   A 1 963  ? -11.103 7.570   -67.124 1.00 48.46  ? 1112 VAL   A C     1 
ATOM   6520 O  O     . VAL   A 1 963  ? -10.188 8.389   -66.900 1.00 48.45  ? 1112 VAL   A O     1 
ATOM   6521 C  CB    . VAL   A 1 963  ? -11.002 5.246   -66.076 1.00 43.56  ? 1112 VAL   A CB    1 
ATOM   6522 C  CG1   . VAL   A 1 963  ? -9.517  5.233   -66.383 1.00 41.75  ? 1112 VAL   A CG1   1 
ATOM   6523 C  CG2   . VAL   A 1 963  ? -11.289 4.455   -64.805 1.00 42.96  ? 1112 VAL   A CG2   1 
ATOM   6524 N  N     . VAL   A 1 964  ? -11.751 7.470   -68.286 1.00 53.57  ? 1113 VAL   A N     1 
ATOM   6525 C  CA    . VAL   A 1 964  ? -11.416 8.339   -69.455 1.00 54.19  ? 1113 VAL   A CA    1 
ATOM   6526 C  C     . VAL   A 1 964  ? -11.612 9.806   -69.052 1.00 53.91  ? 1113 VAL   A C     1 
ATOM   6527 O  O     . VAL   A 1 964  ? -10.685 10.601  -69.266 1.00 56.83  ? 1113 VAL   A O     1 
ATOM   6528 C  CB    . VAL   A 1 964  ? -12.210 7.964   -70.719 1.00 51.13  ? 1113 VAL   A CB    1 
ATOM   6529 C  CG1   . VAL   A 1 964  ? -12.032 9.007   -71.813 1.00 50.88  ? 1113 VAL   A CG1   1 
ATOM   6530 C  CG2   . VAL   A 1 964  ? -11.798 6.594   -71.228 1.00 49.67  ? 1113 VAL   A CG2   1 
ATOM   6531 N  N     . GLU   A 1 965  ? -12.754 10.147  -68.454 1.00 57.40  ? 1114 GLU   A N     1 
ATOM   6532 C  CA    . GLU   A 1 965  ? -13.085 11.544  -68.058 1.00 57.59  ? 1114 GLU   A CA    1 
ATOM   6533 C  C     . GLU   A 1 965  ? -12.056 12.030  -67.030 1.00 55.98  ? 1114 GLU   A C     1 
ATOM   6534 O  O     . GLU   A 1 965  ? -11.502 13.132  -67.210 1.00 51.41  ? 1114 GLU   A O     1 
ATOM   6535 C  CB    . GLU   A 1 965  ? -14.523 11.619  -67.532 1.00 61.81  ? 1114 GLU   A CB    1 
ATOM   6536 C  CG    . GLU   A 1 965  ? -15.573 11.367  -68.603 1.00 69.60  ? 1114 GLU   A CG    1 
ATOM   6537 C  CD    . GLU   A 1 965  ? -15.496 12.326  -69.780 1.00 82.15  ? 1114 GLU   A CD    1 
ATOM   6538 O  OE1   . GLU   A 1 965  ? -15.863 13.512  -69.590 1.00 90.58  ? 1114 GLU   A OE1   1 
ATOM   6539 O  OE2   . GLU   A 1 965  ? -15.023 11.902  -70.870 1.00 78.72  ? 1114 GLU   A OE2   1 
ATOM   6540 N  N     . VAL   A 1 966  ? -11.778 11.205  -66.016 1.00 53.57  ? 1115 VAL   A N     1 
ATOM   6541 C  CA    . VAL   A 1 966  ? -10.880 11.552  -64.881 1.00 47.79  ? 1115 VAL   A CA    1 
ATOM   6542 C  C     . VAL   A 1 966  ? -9.464  11.799  -65.412 1.00 48.30  ? 1115 VAL   A C     1 
ATOM   6543 O  O     . VAL   A 1 966  ? -8.789  12.698  -64.883 1.00 47.53  ? 1115 VAL   A O     1 
ATOM   6544 C  CB    . VAL   A 1 966  ? -10.918 10.473  -63.783 1.00 49.82  ? 1115 VAL   A CB    1 
ATOM   6545 C  CG1   . VAL   A 1 966  ? -9.715  10.570  -62.857 1.00 48.64  ? 1115 VAL   A CG1   1 
ATOM   6546 C  CG2   . VAL   A 1 966  ? -12.218 10.529  -62.986 1.00 46.71  ? 1115 VAL   A CG2   1 
ATOM   6547 N  N     . THR   A 1 967  ? -8.997  11.041  -66.404 1.00 46.54  ? 1116 THR   A N     1 
ATOM   6548 C  CA    . THR   A 1 967  ? -7.616  11.217  -66.925 1.00 47.51  ? 1116 THR   A CA    1 
ATOM   6549 C  C     . THR   A 1 967  ? -7.505  12.539  -67.706 1.00 49.34  ? 1116 THR   A C     1 
ATOM   6550 O  O     . THR   A 1 967  ? -6.422  13.148  -67.646 1.00 53.50  ? 1116 THR   A O     1 
ATOM   6551 C  CB    . THR   A 1 967  ? -7.141  9.967   -67.667 1.00 48.30  ? 1116 THR   A CB    1 
ATOM   6552 O  OG1   . THR   A 1 967  ? -8.034  9.640   -68.732 1.00 48.08  ? 1116 THR   A OG1   1 
ATOM   6553 C  CG2   . THR   A 1 967  ? -7.009  8.800   -66.713 1.00 48.47  ? 1116 THR   A CG2   1 
ATOM   6554 N  N     . LYS   A 1 968  ? -8.569  13.018  -68.357 1.00 52.10  ? 1117 LYS   A N     1 
ATOM   6555 C  CA    . LYS   A 1 968  ? -8.548  14.356  -69.019 1.00 59.69  ? 1117 LYS   A CA    1 
ATOM   6556 C  C     . LYS   A 1 968  ? -8.437  15.451  -67.949 1.00 61.99  ? 1117 LYS   A C     1 
ATOM   6557 O  O     . LYS   A 1 968  ? -7.786  16.454  -68.234 1.00 63.97  ? 1117 LYS   A O     1 
ATOM   6558 C  CB    . LYS   A 1 968  ? -9.785  14.593  -69.891 1.00 63.14  ? 1117 LYS   A CB    1 
ATOM   6559 C  CG    . LYS   A 1 968  ? -9.892  13.726  -71.142 1.00 69.26  ? 1117 LYS   A CG    1 
ATOM   6560 C  CD    . LYS   A 1 968  ? -11.286 13.712  -71.752 1.00 71.20  ? 1117 LYS   A CD    1 
ATOM   6561 C  CE    . LYS   A 1 968  ? -11.409 12.772  -72.933 1.00 74.53  ? 1117 LYS   A CE    1 
ATOM   6562 N  NZ    . LYS   A 1 968  ? -12.822 12.426  -73.228 1.00 74.38  ? 1117 LYS   A NZ    1 
ATOM   6563 N  N     . GLN   A 1 969  ? -9.023  15.235  -66.762 1.00 62.83  ? 1118 GLN   A N     1 
ATOM   6564 C  CA    . GLN   A 1 969  ? -9.270  16.259  -65.709 1.00 62.36  ? 1118 GLN   A CA    1 
ATOM   6565 C  C     . GLN   A 1 969  ? -9.249  15.591  -64.326 1.00 59.17  ? 1118 GLN   A C     1 
ATOM   6566 O  O     . GLN   A 1 969  ? -10.291 15.384  -63.704 1.00 56.65  ? 1118 GLN   A O     1 
ATOM   6567 C  CB    . GLN   A 1 969  ? -10.612 16.935  -66.012 1.00 66.58  ? 1118 GLN   A CB    1 
ATOM   6568 C  CG    . GLN   A 1 969  ? -10.869 18.220  -65.233 1.00 76.05  ? 1118 GLN   A CG    1 
ATOM   6569 C  CD    . GLN   A 1 969  ? -11.986 19.039  -65.843 1.00 84.70  ? 1118 GLN   A CD    1 
ATOM   6570 O  OE1   . GLN   A 1 969  ? -12.999 18.514  -66.318 1.00 83.13  ? 1118 GLN   A OE1   1 
ATOM   6571 N  NE2   . GLN   A 1 969  ? -11.796 20.347  -65.857 1.00 85.52  ? 1118 GLN   A NE2   1 
ATOM   6572 N  N     . PRO   A 1 970  ? -8.067  15.209  -63.791 1.00 54.72  ? 1119 PRO   A N     1 
ATOM   6573 C  CA    . PRO   A 1 970  ? -8.007  14.401  -62.568 1.00 53.80  ? 1119 PRO   A CA    1 
ATOM   6574 C  C     . PRO   A 1 970  ? -8.671  15.006  -61.320 1.00 56.03  ? 1119 PRO   A C     1 
ATOM   6575 O  O     . PRO   A 1 970  ? -9.092  14.259  -60.455 1.00 50.61  ? 1119 PRO   A O     1 
ATOM   6576 C  CB    . PRO   A 1 970  ? -6.500  14.219  -62.354 1.00 53.83  ? 1119 PRO   A CB    1 
ATOM   6577 C  CG    . PRO   A 1 970  ? -5.916  14.348  -63.759 1.00 54.93  ? 1119 PRO   A CG    1 
ATOM   6578 C  CD    . PRO   A 1 970  ? -6.738  15.451  -64.383 1.00 53.71  ? 1119 PRO   A CD    1 
ATOM   6579 N  N     . ASN   A 1 971  ? -8.812  16.326  -61.261 1.00 59.34  ? 1120 ASN   A N     1 
ATOM   6580 C  CA    . ASN   A 1 971  ? -9.359  17.007  -60.057 1.00 67.03  ? 1120 ASN   A CA    1 
ATOM   6581 C  C     . ASN   A 1 971  ? -10.879 16.794  -59.955 1.00 61.83  ? 1120 ASN   A C     1 
ATOM   6582 O  O     . ASN   A 1 971  ? -11.414 17.173  -58.914 1.00 72.99  ? 1120 ASN   A O     1 
ATOM   6583 C  CB    . ASN   A 1 971  ? -8.952  18.483  -59.983 1.00 73.51  ? 1120 ASN   A CB    1 
ATOM   6584 C  CG    . ASN   A 1 971  ? -9.377  19.290  -61.192 1.00 82.21  ? 1120 ASN   A CG    1 
ATOM   6585 O  OD1   . ASN   A 1 971  ? -10.427 19.924  -61.174 1.00 87.60  ? 1120 ASN   A OD1   1 
ATOM   6586 N  ND2   . ASN   A 1 971  ? -8.580  19.259  -62.249 1.00 88.13  ? 1120 ASN   A ND2   1 
ATOM   6587 N  N     . ILE   A 1 972  ? -11.552 16.162  -60.928 1.00 58.73  ? 1121 ILE   A N     1 
ATOM   6588 C  CA    . ILE   A 1 972  ? -13.010 15.833  -60.809 1.00 61.22  ? 1121 ILE   A CA    1 
ATOM   6589 C  C     . ILE   A 1 972  ? -13.215 14.721  -59.767 1.00 62.73  ? 1121 ILE   A C     1 
ATOM   6590 O  O     . ILE   A 1 972  ? -14.362 14.532  -59.319 1.00 58.91  ? 1121 ILE   A O     1 
ATOM   6591 C  CB    . ILE   A 1 972  ? -13.678 15.477  -62.157 1.00 65.83  ? 1121 ILE   A CB    1 
ATOM   6592 C  CG1   . ILE   A 1 972  ? -13.359 14.064  -62.644 1.00 69.93  ? 1121 ILE   A CG1   1 
ATOM   6593 C  CG2   . ILE   A 1 972  ? -13.374 16.512  -63.227 1.00 67.67  ? 1121 ILE   A CG2   1 
ATOM   6594 C  CD1   . ILE   A 1 972  ? -13.942 13.772  -64.011 1.00 77.40  ? 1121 ILE   A CD1   1 
ATOM   6595 N  N     . ILE   A 1 973  ? -12.154 13.996  -59.405 1.00 62.72  ? 1122 ILE   A N     1 
ATOM   6596 C  CA    . ILE   A 1 973  ? -12.149 13.088  -58.223 1.00 60.29  ? 1122 ILE   A CA    1 
ATOM   6597 C  C     . ILE   A 1 973  ? -12.622 13.897  -57.004 1.00 61.25  ? 1122 ILE   A C     1 
ATOM   6598 O  O     . ILE   A 1 973  ? -13.538 13.414  -56.310 1.00 58.28  ? 1122 ILE   A O     1 
ATOM   6599 C  CB    . ILE   A 1 973  ? -10.755 12.440  -58.053 1.00 58.93  ? 1122 ILE   A CB    1 
ATOM   6600 C  CG1   . ILE   A 1 973  ? -10.474 11.463  -59.200 1.00 61.52  ? 1122 ILE   A CG1   1 
ATOM   6601 C  CG2   . ILE   A 1 973  ? -10.604 11.753  -56.712 1.00 56.27  ? 1122 ILE   A CG2   1 
ATOM   6602 C  CD1   . ILE   A 1 973  ? -9.020  11.095  -59.353 1.00 61.80  ? 1122 ILE   A CD1   1 
ATOM   6603 N  N     . SER   A 1 974  ? -12.070 15.103  -56.791 1.00 66.02  ? 1123 SER   A N     1 
ATOM   6604 C  CA    . SER   A 1 974  ? -12.407 16.020  -55.659 1.00 76.97  ? 1123 SER   A CA    1 
ATOM   6605 C  C     . SER   A 1 974  ? -13.908 16.350  -55.654 1.00 71.06  ? 1123 SER   A C     1 
ATOM   6606 O  O     . SER   A 1 974  ? -14.524 16.225  -54.585 1.00 68.85  ? 1123 SER   A O     1 
ATOM   6607 C  CB    . SER   A 1 974  ? -11.594 17.307  -55.683 1.00 77.39  ? 1123 SER   A CB    1 
ATOM   6608 O  OG    . SER   A 1 974  ? -10.292 17.118  -55.153 1.00 73.85  ? 1123 SER   A OG    1 
ATOM   6609 N  N     . GLN   A 1 975  ? -14.454 16.744  -56.810 1.00 75.53  ? 1124 GLN   A N     1 
ATOM   6610 C  CA    . GLN   A 1 975  ? -15.855 17.218  -57.000 1.00 81.80  ? 1124 GLN   A CA    1 
ATOM   6611 C  C     . GLN   A 1 975  ? -16.854 16.297  -56.305 1.00 82.95  ? 1124 GLN   A C     1 
ATOM   6612 O  O     . GLN   A 1 975  ? -17.842 16.831  -55.771 1.00 80.01  ? 1124 GLN   A O     1 
ATOM   6613 C  CB    . GLN   A 1 975  ? -16.245 17.245  -58.473 1.00 82.36  ? 1124 GLN   A CB    1 
ATOM   6614 C  CG    . GLN   A 1 975  ? -15.680 18.435  -59.227 1.00 91.03  ? 1124 GLN   A CG    1 
ATOM   6615 C  CD    . GLN   A 1 975  ? -16.142 18.429  -60.664 1.00 102.34 ? 1124 GLN   A CD    1 
ATOM   6616 O  OE1   . GLN   A 1 975  ? -17.038 17.672  -61.046 1.00 103.70 ? 1124 GLN   A OE1   1 
ATOM   6617 N  NE2   . GLN   A 1 975  ? -15.528 19.277  -61.474 1.00 101.06 ? 1124 GLN   A NE2   1 
ATOM   6618 N  N     . LEU   A 1 976  ? -16.609 14.981  -56.365 1.00 92.87  ? 1125 LEU   A N     1 
ATOM   6619 C  CA    . LEU   A 1 976  ? -17.524 13.898  -55.908 1.00 92.79  ? 1125 LEU   A CA    1 
ATOM   6620 C  C     . LEU   A 1 976  ? -18.913 14.172  -56.511 1.00 94.95  ? 1125 LEU   A C     1 
ATOM   6621 O  O     . LEU   A 1 976  ? -19.901 14.247  -55.737 1.00 93.69  ? 1125 LEU   A O     1 
ATOM   6622 C  CB    . LEU   A 1 976  ? -17.530 13.834  -54.371 1.00 94.87  ? 1125 LEU   A CB    1 
ATOM   6623 C  CG    . LEU   A 1 976  ? -16.197 13.461  -53.704 1.00 95.63  ? 1125 LEU   A CG    1 
ATOM   6624 C  CD1   . LEU   A 1 976  ? -16.004 14.208  -52.390 1.00 96.29  ? 1125 LEU   A CD1   1 
ATOM   6625 C  CD2   . LEU   A 1 976  ? -16.074 11.960  -53.473 1.00 87.31  ? 1125 LEU   A CD2   1 
ATOM   6626 N  N     . ASP   A 1 977  ? -18.962 14.336  -57.843 1.00 85.91  ? 1126 ASP   A N     1 
ATOM   6627 C  CA    . ASP   A 1 977  ? -20.188 14.611  -58.643 1.00 84.28  ? 1126 ASP   A CA    1 
ATOM   6628 C  C     . ASP   A 1 977  ? -21.255 13.552  -58.351 1.00 87.53  ? 1126 ASP   A C     1 
ATOM   6629 O  O     . ASP   A 1 977  ? -20.937 12.367  -58.292 1.00 82.08  ? 1126 ASP   A O     1 
ATOM   6630 C  CB    . ASP   A 1 977  ? -19.855 14.662  -60.135 1.00 84.62  ? 1126 ASP   A CB    1 
ATOM   6631 C  CG    . ASP   A 1 977  ? -21.075 14.819  -61.027 1.00 86.91  ? 1126 ASP   A CG    1 
ATOM   6632 O  OD1   . ASP   A 1 977  ? -21.908 13.897  -61.043 1.00 99.04  ? 1126 ASP   A OD1   1 
ATOM   6633 O  OD2   . ASP   A 1 977  ? -21.193 15.869  -61.683 1.00 89.86  ? 1126 ASP   A OD2   1 
ATOM   6634 N  N     . PRO   A 1 978  ? -22.552 13.930  -58.202 1.00 96.74  ? 1127 PRO   A N     1 
ATOM   6635 C  CA    . PRO   A 1 978  ? -23.596 12.994  -57.762 1.00 92.49  ? 1127 PRO   A CA    1 
ATOM   6636 C  C     . PRO   A 1 978  ? -23.870 11.776  -58.663 1.00 80.87  ? 1127 PRO   A C     1 
ATOM   6637 O  O     . PRO   A 1 978  ? -24.202 10.730  -58.141 1.00 72.93  ? 1127 PRO   A O     1 
ATOM   6638 C  CB    . PRO   A 1 978  ? -24.874 13.856  -57.735 1.00 96.98  ? 1127 PRO   A CB    1 
ATOM   6639 C  CG    . PRO   A 1 978  ? -24.374 15.280  -57.624 1.00 95.99  ? 1127 PRO   A CG    1 
ATOM   6640 C  CD    . PRO   A 1 978  ? -23.089 15.285  -58.423 1.00 97.50  ? 1127 PRO   A CD    1 
ATOM   6641 N  N     . VAL   A 1 979  ? -23.769 11.927  -59.983 1.00 75.45  ? 1128 VAL   A N     1 
ATOM   6642 C  CA    . VAL   A 1 979  ? -24.092 10.828  -60.947 1.00 82.17  ? 1128 VAL   A CA    1 
ATOM   6643 C  C     . VAL   A 1 979  ? -22.960 9.774   -60.924 1.00 73.92  ? 1128 VAL   A C     1 
ATOM   6644 O  O     . VAL   A 1 979  ? -23.236 8.551   -61.071 1.00 63.34  ? 1128 VAL   A O     1 
ATOM   6645 C  CB    . VAL   A 1 979  ? -24.401 11.387  -62.358 1.00 85.73  ? 1128 VAL   A CB    1 
ATOM   6646 C  CG1   . VAL   A 1 979  ? -23.225 12.114  -63.006 1.00 87.04  ? 1128 VAL   A CG1   1 
ATOM   6647 C  CG2   . VAL   A 1 979  ? -24.940 10.304  -63.286 1.00 81.56  ? 1128 VAL   A CG2   1 
ATOM   6648 N  N     . ASN   A 1 980  ? -21.717 10.208  -60.727 1.00 65.40  ? 1129 ASN   A N     1 
ATOM   6649 C  CA    . ASN   A 1 980  ? -20.552 9.296   -60.640 1.00 61.78  ? 1129 ASN   A CA    1 
ATOM   6650 C  C     . ASN   A 1 980  ? -20.649 8.559   -59.301 1.00 59.70  ? 1129 ASN   A C     1 
ATOM   6651 O  O     . ASN   A 1 980  ? -20.498 7.318   -59.287 1.00 56.47  ? 1129 ASN   A O     1 
ATOM   6652 C  CB    . ASN   A 1 980  ? -19.241 10.059  -60.842 1.00 67.61  ? 1129 ASN   A CB    1 
ATOM   6653 C  CG    . ASN   A 1 980  ? -19.114 10.674  -62.225 1.00 71.00  ? 1129 ASN   A CG    1 
ATOM   6654 O  OD1   . ASN   A 1 980  ? -19.566 10.105  -63.229 1.00 67.40  ? 1129 ASN   A OD1   1 
ATOM   6655 N  ND2   . ASN   A 1 980  ? -18.504 11.848  -62.286 1.00 69.94  ? 1129 ASN   A ND2   1 
ATOM   6656 N  N     . GLU   A 1 981  ? -20.954 9.303   -58.237 1.00 51.24  ? 1130 GLU   A N     1 
ATOM   6657 C  CA    . GLU   A 1 981  ? -20.990 8.814   -56.840 1.00 54.80  ? 1130 GLU   A CA    1 
ATOM   6658 C  C     . GLU   A 1 981  ? -21.996 7.655   -56.744 1.00 54.90  ? 1130 GLU   A C     1 
ATOM   6659 O  O     . GLU   A 1 981  ? -21.745 6.704   -55.996 1.00 57.00  ? 1130 GLU   A O     1 
ATOM   6660 C  CB    . GLU   A 1 981  ? -21.308 9.993   -55.910 1.00 59.74  ? 1130 GLU   A CB    1 
ATOM   6661 C  CG    . GLU   A 1 981  ? -20.413 10.096  -54.681 1.00 74.07  ? 1130 GLU   A CG    1 
ATOM   6662 C  CD    . GLU   A 1 981  ? -18.931 9.776   -54.873 1.00 79.28  ? 1130 GLU   A CD    1 
ATOM   6663 O  OE1   . GLU   A 1 981  ? -18.248 10.508  -55.636 1.00 83.87  ? 1130 GLU   A OE1   1 
ATOM   6664 O  OE2   . GLU   A 1 981  ? -18.459 8.783   -54.261 1.00 70.85  ? 1130 GLU   A OE2   1 
ATOM   6665 N  N     . HIS   A 1 982  ? -23.096 7.746   -57.482 1.00 53.06  ? 1131 HIS   A N     1 
ATOM   6666 C  CA    . HIS   A 1 982  ? -24.205 6.765   -57.524 1.00 55.17  ? 1131 HIS   A CA    1 
ATOM   6667 C  C     . HIS   A 1 982  ? -23.659 5.472   -58.138 1.00 52.05  ? 1131 HIS   A C     1 
ATOM   6668 O  O     . HIS   A 1 982  ? -23.960 4.379   -57.634 1.00 54.71  ? 1131 HIS   A O     1 
ATOM   6669 C  CB    . HIS   A 1 982  ? -25.369 7.387   -58.326 1.00 68.97  ? 1131 HIS   A CB    1 
ATOM   6670 C  CG    . HIS   A 1 982  ? -26.735 7.100   -57.805 1.00 80.12  ? 1131 HIS   A CG    1 
ATOM   6671 N  ND1   . HIS   A 1 982  ? -27.218 7.688   -56.646 1.00 90.63  ? 1131 HIS   A ND1   1 
ATOM   6672 C  CD2   . HIS   A 1 982  ? -27.729 6.322   -58.292 1.00 85.22  ? 1131 HIS   A CD2   1 
ATOM   6673 C  CE1   . HIS   A 1 982  ? -28.449 7.262   -56.431 1.00 100.34 ? 1131 HIS   A CE1   1 
ATOM   6674 N  NE2   . HIS   A 1 982  ? -28.783 6.415   -57.425 1.00 96.12  ? 1131 HIS   A NE2   1 
ATOM   6675 N  N     . MET   A 1 983  ? -22.882 5.598   -59.212 1.00 46.02  ? 1132 MET   A N     1 
ATOM   6676 C  CA    . MET   A 1 983  ? -22.237 4.457   -59.902 1.00 43.03  ? 1132 MET   A CA    1 
ATOM   6677 C  C     . MET   A 1 983  ? -21.167 3.862   -58.977 1.00 42.35  ? 1132 MET   A C     1 
ATOM   6678 O  O     . MET   A 1 983  ? -21.205 2.631   -58.730 1.00 44.29  ? 1132 MET   A O     1 
ATOM   6679 C  CB    . MET   A 1 983  ? -21.631 4.944   -61.220 1.00 47.36  ? 1132 MET   A CB    1 
ATOM   6680 C  CG    . MET   A 1 983  ? -21.121 3.842   -62.117 1.00 51.08  ? 1132 MET   A CG    1 
ATOM   6681 S  SD    . MET   A 1 983  ? -19.429 3.382   -61.659 1.00 51.42  ? 1132 MET   A SD    1 
ATOM   6682 C  CE    . MET   A 1 983  ? -18.539 4.834   -62.218 1.00 48.33  ? 1132 MET   A CE    1 
ATOM   6683 N  N     . LEU   A 1 984  ? -20.279 4.696   -58.432 1.00 39.52  ? 1133 LEU   A N     1 
ATOM   6684 C  CA    . LEU   A 1 984  ? -19.161 4.237   -57.566 1.00 42.82  ? 1133 LEU   A CA    1 
ATOM   6685 C  C     . LEU   A 1 984  ? -19.724 3.503   -56.343 1.00 44.12  ? 1133 LEU   A C     1 
ATOM   6686 O  O     . LEU   A 1 984  ? -19.145 2.456   -55.963 1.00 48.76  ? 1133 LEU   A O     1 
ATOM   6687 C  CB    . LEU   A 1 984  ? -18.278 5.425   -57.164 1.00 42.16  ? 1133 LEU   A CB    1 
ATOM   6688 C  CG    . LEU   A 1 984  ? -17.466 6.039   -58.305 1.00 41.08  ? 1133 LEU   A CG    1 
ATOM   6689 C  CD1   . LEU   A 1 984  ? -16.628 7.206   -57.825 1.00 39.74  ? 1133 LEU   A CD1   1 
ATOM   6690 C  CD2   . LEU   A 1 984  ? -16.586 4.995   -58.970 1.00 43.68  ? 1133 LEU   A CD2   1 
ATOM   6691 N  N     . ASN   A 1 985  ? -20.823 3.999   -55.768 1.00 43.66  ? 1134 ASN   A N     1 
ATOM   6692 C  CA    . ASN   A 1 985  ? -21.406 3.439   -54.521 1.00 42.10  ? 1134 ASN   A CA    1 
ATOM   6693 C  C     . ASN   A 1 985  ? -21.959 2.061   -54.826 1.00 37.68  ? 1134 ASN   A C     1 
ATOM   6694 O  O     . ASN   A 1 985  ? -21.848 1.188   -53.968 1.00 41.80  ? 1134 ASN   A O     1 
ATOM   6695 C  CB    . ASN   A 1 985  ? -22.475 4.332   -53.887 1.00 44.54  ? 1134 ASN   A CB    1 
ATOM   6696 C  CG    . ASN   A 1 985  ? -21.880 5.499   -53.121 1.00 52.03  ? 1134 ASN   A CG    1 
ATOM   6697 O  OD1   . ASN   A 1 985  ? -20.685 5.520   -52.805 1.00 46.48  ? 1134 ASN   A OD1   1 
ATOM   6698 N  ND2   . ASN   A 1 985  ? -22.703 6.506   -52.863 1.00 58.10  ? 1134 ASN   A ND2   1 
ATOM   6699 N  N     . MET   A 1 986  ? -22.493 1.862   -56.021 1.00 39.10  ? 1135 MET   A N     1 
ATOM   6700 C  CA    . MET   A 1 986  ? -23.007 0.532   -56.406 1.00 42.58  ? 1135 MET   A CA    1 
ATOM   6701 C  C     . MET   A 1 986  ? -21.816 -0.441  -56.563 1.00 44.54  ? 1135 MET   A C     1 
ATOM   6702 O  O     . MET   A 1 986  ? -21.903 -1.562  -56.028 1.00 44.10  ? 1135 MET   A O     1 
ATOM   6703 C  CB    . MET   A 1 986  ? -23.863 0.633   -57.674 1.00 44.75  ? 1135 MET   A CB    1 
ATOM   6704 C  CG    . MET   A 1 986  ? -24.637 -0.640  -58.010 1.00 48.85  ? 1135 MET   A CG    1 
ATOM   6705 S  SD    . MET   A 1 986  ? -25.769 -1.277  -56.721 1.00 53.71  ? 1135 MET   A SD    1 
ATOM   6706 C  CE    . MET   A 1 986  ? -26.186 0.192   -55.780 1.00 64.29  ? 1135 MET   A CE    1 
ATOM   6707 N  N     . ILE   A 1 987  ? -20.715 -0.035  -57.208 1.00 42.30  ? 1136 ILE   A N     1 
ATOM   6708 C  CA    . ILE   A 1 987  ? -19.479 -0.873  -57.262 1.00 43.92  ? 1136 ILE   A CA    1 
ATOM   6709 C  C     . ILE   A 1 987  ? -18.978 -1.117  -55.829 1.00 43.21  ? 1136 ILE   A C     1 
ATOM   6710 O  O     . ILE   A 1 987  ? -18.606 -2.276  -55.529 1.00 43.09  ? 1136 ILE   A O     1 
ATOM   6711 C  CB    . ILE   A 1 987  ? -18.382 -0.278  -58.168 1.00 42.71  ? 1136 ILE   A CB    1 
ATOM   6712 C  CG1   . ILE   A 1 987  ? -18.780 -0.337  -59.643 1.00 44.72  ? 1136 ILE   A CG1   1 
ATOM   6713 C  CG2   . ILE   A 1 987  ? -17.064 -0.997  -57.927 1.00 42.24  ? 1136 ILE   A CG2   1 
ATOM   6714 C  CD1   . ILE   A 1 987  ? -17.857 0.429   -60.569 1.00 47.60  ? 1136 ILE   A CD1   1 
ATOM   6715 N  N     . ARG   A 1 988  ? -18.963 -0.092  -54.970 1.00 40.46  ? 1137 ARG   A N     1 
ATOM   6716 C  CA    . ARG   A 1 988  ? -18.575 -0.267  -53.546 1.00 38.96  ? 1137 ARG   A CA    1 
ATOM   6717 C  C     . ARG   A 1 988  ? -19.435 -1.364  -52.929 1.00 41.96  ? 1137 ARG   A C     1 
ATOM   6718 O  O     . ARG   A 1 988  ? -18.880 -2.203  -52.207 1.00 43.17  ? 1137 ARG   A O     1 
ATOM   6719 C  CB    . ARG   A 1 988  ? -18.733 1.023   -52.745 1.00 41.24  ? 1137 ARG   A CB    1 
ATOM   6720 C  CG    . ARG   A 1 988  ? -17.589 2.004   -52.937 1.00 44.17  ? 1137 ARG   A CG    1 
ATOM   6721 C  CD    . ARG   A 1 988  ? -17.831 3.301   -52.186 1.00 44.80  ? 1137 ARG   A CD    1 
ATOM   6722 N  NE    . ARG   A 1 988  ? -16.720 4.223   -52.387 1.00 44.62  ? 1137 ARG   A NE    1 
ATOM   6723 C  CZ    . ARG   A 1 988  ? -16.735 5.337   -53.103 1.00 46.28  ? 1137 ARG   A CZ    1 
ATOM   6724 N  NH1   . ARG   A 1 988  ? -17.832 5.736   -53.715 1.00 51.13  ? 1137 ARG   A NH1   1 
ATOM   6725 N  NH2   . ARG   A 1 988  ? -15.633 6.064   -53.202 1.00 50.87  ? 1137 ARG   A NH2   1 
ATOM   6726 N  N     . GLN   A 1 989  ? -20.741 -1.363  -53.223 1.00 47.47  ? 1138 GLN   A N     1 
ATOM   6727 C  CA    . GLN   A 1 989  ? -21.727 -2.285  -52.597 1.00 43.46  ? 1138 GLN   A CA    1 
ATOM   6728 C  C     . GLN   A 1 989  ? -21.444 -3.706  -53.071 1.00 42.93  ? 1138 GLN   A C     1 
ATOM   6729 O  O     . GLN   A 1 989  ? -21.489 -4.592  -52.213 1.00 43.57  ? 1138 GLN   A O     1 
ATOM   6730 C  CB    . GLN   A 1 989  ? -23.183 -1.897  -52.887 1.00 48.60  ? 1138 GLN   A CB    1 
ATOM   6731 C  CG    . GLN   A 1 989  ? -23.709 -0.727  -52.063 1.00 58.43  ? 1138 GLN   A CG    1 
ATOM   6732 C  CD    . GLN   A 1 989  ? -23.485 -0.865  -50.574 1.00 68.47  ? 1138 GLN   A CD    1 
ATOM   6733 O  OE1   . GLN   A 1 989  ? -22.874 -0.005  -49.933 1.00 80.29  ? 1138 GLN   A OE1   1 
ATOM   6734 N  NE2   . GLN   A 1 989  ? -23.956 -1.967  -50.009 1.00 67.72  ? 1138 GLN   A NE2   1 
ATOM   6735 N  N     . ILE   A 1 990  ? -21.182 -3.926  -54.368 1.00 46.00  ? 1139 ILE   A N     1 
ATOM   6736 C  CA    . ILE   A 1 990  ? -21.004 -5.309  -54.923 1.00 48.24  ? 1139 ILE   A CA    1 
ATOM   6737 C  C     . ILE   A 1 990  ? -19.563 -5.787  -54.691 1.00 44.14  ? 1139 ILE   A C     1 
ATOM   6738 O  O     . ILE   A 1 990  ? -19.251 -6.931  -55.044 1.00 43.30  ? 1139 ILE   A O     1 
ATOM   6739 C  CB    . ILE   A 1 990  ? -21.425 -5.445  -56.403 1.00 50.09  ? 1139 ILE   A CB    1 
ATOM   6740 C  CG1   . ILE   A 1 990  ? -20.683 -4.489  -57.335 1.00 49.87  ? 1139 ILE   A CG1   1 
ATOM   6741 C  CG2   . ILE   A 1 990  ? -22.931 -5.305  -56.556 1.00 50.93  ? 1139 ILE   A CG2   1 
ATOM   6742 C  CD1   . ILE   A 1 990  ? -20.603 -5.008  -58.760 1.00 51.60  ? 1139 ILE   A CD1   1 
ATOM   6743 N  N     . SER   A 1 991  ? -18.719 -4.963  -54.080 1.00 41.14  ? 1140 SER   A N     1 
ATOM   6744 C  CA    . SER   A 1 991  ? -17.389 -5.397  -53.595 1.00 40.88  ? 1140 SER   A CA    1 
ATOM   6745 C  C     . SER   A 1 991  ? -17.528 -6.093  -52.232 1.00 42.47  ? 1140 SER   A C     1 
ATOM   6746 O  O     . SER   A 1 991  ? -16.594 -6.813  -51.855 1.00 41.63  ? 1140 SER   A O     1 
ATOM   6747 C  CB    . SER   A 1 991  ? -16.436 -4.244  -53.582 1.00 36.39  ? 1140 SER   A CB    1 
ATOM   6748 O  OG    . SER   A 1 991  ? -16.249 -3.788  -54.908 1.00 34.73  ? 1140 SER   A OG    1 
ATOM   6749 N  N     . ARG   A 1 992  ? -18.665 -5.935  -51.547 1.00 44.67  ? 1141 ARG   A N     1 
ATOM   6750 C  CA    . ARG   A 1 992  ? -18.876 -6.478  -50.178 1.00 46.76  ? 1141 ARG   A CA    1 
ATOM   6751 C  C     . ARG   A 1 992  ? -18.982 -7.997  -50.278 1.00 46.77  ? 1141 ARG   A C     1 
ATOM   6752 O  O     . ARG   A 1 992  ? -19.617 -8.513  -51.192 1.00 48.91  ? 1141 ARG   A O     1 
ATOM   6753 C  CB    . ARG   A 1 992  ? -20.107 -5.849  -49.512 1.00 50.68  ? 1141 ARG   A CB    1 
ATOM   6754 C  CG    . ARG   A 1 992  ? -19.945 -4.366  -49.199 1.00 53.37  ? 1141 ARG   A CG    1 
ATOM   6755 C  CD    . ARG   A 1 992  ? -21.137 -3.737  -48.508 1.00 58.19  ? 1141 ARG   A CD    1 
ATOM   6756 N  NE    . ARG   A 1 992  ? -21.319 -4.292  -47.174 1.00 71.77  ? 1141 ARG   A NE    1 
ATOM   6757 C  CZ    . ARG   A 1 992  ? -22.338 -4.026  -46.355 1.00 71.88  ? 1141 ARG   A CZ    1 
ATOM   6758 N  NH1   . ARG   A 1 992  ? -23.292 -3.184  -46.719 1.00 70.15  ? 1141 ARG   A NH1   1 
ATOM   6759 N  NH2   . ARG   A 1 992  ? -22.394 -4.605  -45.166 1.00 71.08  ? 1141 ARG   A NH2   1 
ATOM   6760 N  N     . PRO   A 1 993  ? -18.324 -8.769  -49.383 1.00 46.21  ? 1142 PRO   A N     1 
ATOM   6761 C  CA    . PRO   A 1 993  ? -18.545 -10.209 -49.326 1.00 45.76  ? 1142 PRO   A CA    1 
ATOM   6762 C  C     . PRO   A 1 993  ? -20.033 -10.544 -49.112 1.00 48.78  ? 1142 PRO   A C     1 
ATOM   6763 O  O     . PRO   A 1 993  ? -20.493 -11.521 -49.682 1.00 52.06  ? 1142 PRO   A O     1 
ATOM   6764 C  CB    . PRO   A 1 993  ? -17.699 -10.696 -48.140 1.00 48.00  ? 1142 PRO   A CB    1 
ATOM   6765 C  CG    . PRO   A 1 993  ? -16.726 -9.577  -47.834 1.00 46.78  ? 1142 PRO   A CG    1 
ATOM   6766 C  CD    . PRO   A 1 993  ? -17.318 -8.306  -48.413 1.00 46.76  ? 1142 PRO   A CD    1 
ATOM   6767 N  N     . SER   A 1 994  ? -20.744 -9.738  -48.316 1.00 49.75  ? 1143 SER   A N     1 
ATOM   6768 C  CA    . SER   A 1 994  ? -22.190 -9.904  -47.994 1.00 53.71  ? 1143 SER   A CA    1 
ATOM   6769 C  C     . SER   A 1 994  ? -23.042 -9.816  -49.274 1.00 52.18  ? 1143 SER   A C     1 
ATOM   6770 O  O     . SER   A 1 994  ? -24.039 -10.559 -49.370 1.00 56.48  ? 1143 SER   A O     1 
ATOM   6771 C  CB    . SER   A 1 994  ? -22.657 -8.913  -46.929 1.00 53.20  ? 1143 SER   A CB    1 
ATOM   6772 O  OG    . SER   A 1 994  ? -22.491 -7.563  -47.351 1.00 52.08  ? 1143 SER   A OG    1 
ATOM   6773 N  N     . ALA   A 1 995  ? -22.651 -8.991  -50.245 1.00 46.40  ? 1144 ALA   A N     1 
ATOM   6774 C  CA    . ALA   A 1 995  ? -23.362 -8.852  -51.535 1.00 48.94  ? 1144 ALA   A CA    1 
ATOM   6775 C  C     . ALA   A 1 995  ? -23.484 -10.215 -52.230 1.00 47.73  ? 1144 ALA   A C     1 
ATOM   6776 O  O     . ALA   A 1 995  ? -24.483 -10.399 -52.923 1.00 48.07  ? 1144 ALA   A O     1 
ATOM   6777 C  CB    . ALA   A 1 995  ? -22.683 -7.843  -52.429 1.00 51.52  ? 1144 ALA   A CB    1 
ATOM   6778 N  N     . ALA   A 1 996  ? -22.520 -11.127 -52.060 1.00 48.04  ? 1145 ALA   A N     1 
ATOM   6779 C  CA    . ALA   A 1 996  ? -22.547 -12.483 -52.658 1.00 47.26  ? 1145 ALA   A CA    1 
ATOM   6780 C  C     . ALA   A 1 996  ? -22.867 -13.559 -51.604 1.00 49.87  ? 1145 ALA   A C     1 
ATOM   6781 O  O     . ALA   A 1 996  ? -22.593 -14.741 -51.885 1.00 49.30  ? 1145 ALA   A O     1 
ATOM   6782 C  CB    . ALA   A 1 996  ? -21.249 -12.753 -53.367 1.00 45.38  ? 1145 ALA   A CB    1 
ATOM   6783 N  N     . GLY   A 1 997  ? -23.484 -13.184 -50.476 1.00 51.33  ? 1146 GLY   A N     1 
ATOM   6784 C  CA    . GLY   A 1 997  ? -24.021 -14.117 -49.460 1.00 56.45  ? 1146 GLY   A CA    1 
ATOM   6785 C  C     . GLY   A 1 997  ? -22.957 -14.654 -48.506 1.00 60.87  ? 1146 GLY   A C     1 
ATOM   6786 O  O     . GLY   A 1 997  ? -23.241 -15.633 -47.795 1.00 65.62  ? 1146 GLY   A O     1 
ATOM   6787 N  N     . ILE   A 1 998  ? -21.782 -14.020 -48.459 1.00 57.60  ? 1147 ILE   A N     1 
ATOM   6788 C  CA    . ILE   A 1 998  ? -20.589 -14.485 -47.695 1.00 51.89  ? 1147 ILE   A CA    1 
ATOM   6789 C  C     . ILE   A 1 998  ? -20.401 -13.592 -46.463 1.00 56.25  ? 1147 ILE   A C     1 
ATOM   6790 O  O     . ILE   A 1 998  ? -20.409 -12.348 -46.613 1.00 61.51  ? 1147 ILE   A O     1 
ATOM   6791 C  CB    . ILE   A 1 998  ? -19.343 -14.485 -48.601 1.00 51.50  ? 1147 ILE   A CB    1 
ATOM   6792 C  CG1   . ILE   A 1 998  ? -19.481 -15.487 -49.747 1.00 50.55  ? 1147 ILE   A CG1   1 
ATOM   6793 C  CG2   . ILE   A 1 998  ? -18.087 -14.745 -47.788 1.00 55.52  ? 1147 ILE   A CG2   1 
ATOM   6794 C  CD1   . ILE   A 1 998  ? -18.509 -15.250 -50.871 1.00 55.16  ? 1147 ILE   A CD1   1 
ATOM   6795 N  N     . ASN   A 1 999  ? -20.249 -14.209 -45.289 1.00 56.67  ? 1148 ASN   A N     1 
ATOM   6796 C  CA    . ASN   A 1 999  ? -19.731 -13.550 -44.063 1.00 61.46  ? 1148 ASN   A CA    1 
ATOM   6797 C  C     . ASN   A 1 999  ? -18.410 -14.237 -43.724 1.00 64.08  ? 1148 ASN   A C     1 
ATOM   6798 O  O     . ASN   A 1 999  ? -18.419 -15.456 -43.450 1.00 62.83  ? 1148 ASN   A O     1 
ATOM   6799 C  CB    . ASN   A 1 999  ? -20.727 -13.585 -42.900 1.00 61.27  ? 1148 ASN   A CB    1 
ATOM   6800 C  CG    . ASN   A 1 999  ? -20.263 -12.794 -41.688 1.00 61.97  ? 1148 ASN   A CG    1 
ATOM   6801 O  OD1   . ASN   A 1 999  ? -19.093 -12.404 -41.594 1.00 55.56  ? 1148 ASN   A OD1   1 
ATOM   6802 N  ND2   . ASN   A 1 999  ? -21.171 -12.559 -40.749 1.00 54.25  ? 1148 ASN   A ND2   1 
ATOM   6803 N  N     . LEU   A 1 1000 ? -17.315 -13.486 -43.797 1.00 63.87  ? 1149 LEU   A N     1 
ATOM   6804 C  CA    . LEU   A 1 1000 ? -15.934 -14.022 -43.643 1.00 62.11  ? 1149 LEU   A CA    1 
ATOM   6805 C  C     . LEU   A 1 1000 ? -15.617 -14.241 -42.153 1.00 60.84  ? 1149 LEU   A C     1 
ATOM   6806 O  O     . LEU   A 1 1000 ? -14.668 -15.002 -41.879 1.00 53.07  ? 1149 LEU   A O     1 
ATOM   6807 C  CB    . LEU   A 1 1000 ? -14.951 -13.047 -44.307 1.00 60.10  ? 1149 LEU   A CB    1 
ATOM   6808 C  CG    . LEU   A 1 1000 ? -14.985 -13.017 -45.838 1.00 56.02  ? 1149 LEU   A CG    1 
ATOM   6809 C  CD1   . LEU   A 1 1000 ? -14.145 -11.875 -46.373 1.00 58.64  ? 1149 LEU   A CD1   1 
ATOM   6810 C  CD2   . LEU   A 1 1000 ? -14.499 -14.334 -46.428 1.00 56.03  ? 1149 LEU   A CD2   1 
ATOM   6811 N  N     . MET   A 1 1001 ? -16.388 -13.624 -41.241 1.00 61.63  ? 1150 MET   A N     1 
ATOM   6812 C  CA    . MET   A 1 1001 ? -16.238 -13.756 -39.761 1.00 71.62  ? 1150 MET   A CA    1 
ATOM   6813 C  C     . MET   A 1 1001 ? -16.837 -15.086 -39.246 1.00 72.40  ? 1150 MET   A C     1 
ATOM   6814 O  O     . MET   A 1 1001 ? -16.332 -15.580 -38.215 1.00 72.56  ? 1150 MET   A O     1 
ATOM   6815 C  CB    . MET   A 1 1001 ? -16.855 -12.554 -39.027 1.00 73.69  ? 1150 MET   A CB    1 
ATOM   6816 C  CG    . MET   A 1 1001 ? -15.815 -11.591 -38.445 1.00 78.65  ? 1150 MET   A CG    1 
ATOM   6817 S  SD    . MET   A 1 1001 ? -16.457 -9.920  -38.087 1.00 90.23  ? 1150 MET   A SD    1 
ATOM   6818 C  CE    . MET   A 1 1001 ? -16.942 -10.069 -36.365 1.00 85.05  ? 1150 MET   A CE    1 
ATOM   6819 N  N     . ILE   A 1 1002 ? -17.838 -15.673 -39.923 1.00 84.80  ? 1151 ILE   A N     1 
ATOM   6820 C  CA    . ILE   A 1 1002 ? -18.391 -17.033 -39.603 1.00 95.62  ? 1151 ILE   A CA    1 
ATOM   6821 C  C     . ILE   A 1 1002 ? -17.412 -18.096 -40.130 1.00 98.31  ? 1151 ILE   A C     1 
ATOM   6822 O  O     . ILE   A 1 1002 ? -16.373 -17.704 -40.681 1.00 97.95  ? 1151 ILE   A O     1 
ATOM   6823 C  CB    . ILE   A 1 1002 ? -19.828 -17.260 -40.147 1.00 94.12  ? 1151 ILE   A CB    1 
ATOM   6824 C  CG1   . ILE   A 1 1002 ? -19.839 -17.665 -41.630 1.00 97.14  ? 1151 ILE   A CG1   1 
ATOM   6825 C  CG2   . ILE   A 1 1002 ? -20.726 -16.063 -39.848 1.00 90.91  ? 1151 ILE   A CG2   1 
ATOM   6826 C  CD1   . ILE   A 1 1002 ? -21.215 -17.736 -42.279 1.00 99.03  ? 1151 ILE   A CD1   1 
ATOM   6827 N  N     . ASP   A 1 1003 ? -17.730 -19.386 -39.950 1.00 109.33 ? 1152 ASP   A N     1 
ATOM   6828 C  CA    . ASP   A 1 1003 ? -16.899 -20.547 -40.383 1.00 109.68 ? 1152 ASP   A CA    1 
ATOM   6829 C  C     . ASP   A 1 1003 ? -17.765 -21.504 -41.212 1.00 99.09  ? 1152 ASP   A C     1 
ATOM   6830 O  O     . ASP   A 1 1003 ? -17.684 -21.529 -42.439 1.00 92.00  ? 1152 ASP   A O     1 
ATOM   6831 C  CB    . ASP   A 1 1003 ? -16.274 -21.274 -39.185 1.00 112.99 ? 1152 ASP   A CB    1 
ATOM   6832 C  CG    . ASP   A 1 1003 ? -15.217 -20.478 -38.426 1.00 113.70 ? 1152 ASP   A CG    1 
ATOM   6833 O  OD1   . ASP   A 1 1003 ? -15.463 -19.288 -38.126 1.00 105.87 ? 1152 ASP   A OD1   1 
ATOM   6834 O  OD2   . ASP   A 1 1003 ? -14.155 -21.060 -38.125 1.00 111.93 ? 1152 ASP   A OD2   1 
HETATM 6835 C  C4    . A1BKX B 2 .    ? 14.230  16.937  -58.086 1.00 51.94  ? 1201 A1BKX A C4    1 
HETATM 6836 C  C5    . A1BKX B 2 .    ? 14.283  16.541  -59.413 1.00 56.65  ? 1201 A1BKX A C5    1 
HETATM 6837 C  C7    . A1BKX B 2 .    ? 15.197  14.470  -58.850 1.00 50.06  ? 1201 A1BKX A C7    1 
HETATM 6838 C  C8    . A1BKX B 2 .    ? 15.664  13.173  -59.431 1.00 48.12  ? 1201 A1BKX A C8    1 
HETATM 6839 C  C13   . A1BKX B 2 .    ? 17.463  11.441  -62.231 1.00 40.20  ? 1201 A1BKX A C13   1 
HETATM 6840 C  C17   . A1BKX B 2 .    ? 19.099  10.862  -64.691 1.00 35.80  ? 1201 A1BKX A C17   1 
HETATM 6841 C  C20   . A1BKX B 2 .    ? 19.542  13.003  -66.371 1.00 37.15  ? 1201 A1BKX A C20   1 
HETATM 6842 C  C21   . A1BKX B 2 .    ? 18.827  13.170  -65.196 1.00 35.71  ? 1201 A1BKX A C21   1 
HETATM 6843 C  C26   . A1BKX B 2 .    ? 17.471  14.046  -68.575 1.00 42.52  ? 1201 A1BKX A C26   1 
HETATM 6844 C  C1    . A1BKX B 2 .    ? 15.601  13.900  -56.360 1.00 51.93  ? 1201 A1BKX A C1    1 
HETATM 6845 C  C2    . A1BKX B 2 .    ? 15.147  14.805  -57.481 1.00 50.08  ? 1201 A1BKX A C2    1 
HETATM 6846 C  C3    . A1BKX B 2 .    ? 14.663  16.050  -57.115 1.00 51.63  ? 1201 A1BKX A C3    1 
HETATM 6847 N  N6    . A1BKX B 2 .    ? 14.751  15.347  -59.743 1.00 55.23  ? 1201 A1BKX A N6    1 
HETATM 6848 C  C9    . A1BKX B 2 .    ? 15.380  11.951  -58.900 1.00 48.42  ? 1201 A1BKX A C9    1 
HETATM 6849 S  S10   . A1BKX B 2 .    ? 16.062  10.723  -59.882 1.00 54.56  ? 1201 A1BKX A S10   1 
HETATM 6850 C  C11   . A1BKX B 2 .    ? 16.700  11.861  -61.039 1.00 41.77  ? 1201 A1BKX A C11   1 
HETATM 6851 C  C12   . A1BKX B 2 .    ? 16.380  13.118  -60.621 1.00 41.31  ? 1201 A1BKX A C12   1 
HETATM 6852 O  O14   . A1BKX B 2 .    ? 17.751  10.262  -62.360 1.00 42.03  ? 1201 A1BKX A O14   1 
HETATM 6853 N  N15   . A1BKX B 2 .    ? 17.844  12.353  -63.146 1.00 38.42  ? 1201 A1BKX A N15   1 
HETATM 6854 C  C16   . A1BKX B 2 .    ? 18.588  12.103  -64.335 1.00 38.14  ? 1201 A1BKX A C16   1 
HETATM 6855 C  C18   . A1BKX B 2 .    ? 19.785  10.698  -65.877 1.00 36.97  ? 1201 A1BKX A C18   1 
HETATM 6856 C  C19   . A1BKX B 2 .    ? 20.054  11.769  -66.712 1.00 34.15  ? 1201 A1BKX A C19   1 
HETATM 6857 N  N22   . A1BKX B 2 .    ? 19.759  14.125  -67.158 1.00 40.99  ? 1201 A1BKX A N22   1 
HETATM 6858 S  S23   . A1BKX B 2 .    ? 19.253  14.219  -68.707 1.00 46.97  ? 1201 A1BKX A S23   1 
HETATM 6859 O  O24   . A1BKX B 2 .    ? 19.556  15.539  -69.149 1.00 44.10  ? 1201 A1BKX A O24   1 
HETATM 6860 O  O25   . A1BKX B 2 .    ? 19.857  13.107  -69.323 1.00 46.58  ? 1201 A1BKX A O25   1 
HETATM 6861 CL CL27  . A1BKX B 2 .    ? 20.348  9.090   -66.245 1.00 43.97  ? 1201 A1BKX A CL27  1 
HETATM 6862 P  PB    . ADP   C 3 .    ? 35.401  -4.349  -67.314 1.00 43.38  ? 1202 ADP   A PB    1 
HETATM 6863 O  O1B   . ADP   C 3 .    ? 36.302  -4.040  -68.461 1.00 41.07  ? 1202 ADP   A O1B   1 
HETATM 6864 O  O2B   . ADP   C 3 .    ? 35.036  -5.835  -67.242 1.00 41.72  ? 1202 ADP   A O2B   1 
HETATM 6865 O  O3B   . ADP   C 3 .    ? 34.184  -3.452  -67.274 1.00 40.48  ? 1202 ADP   A O3B   1 
HETATM 6866 P  PA    . ADP   C 3 .    ? 35.763  -3.380  -64.604 1.00 44.85  ? 1202 ADP   A PA    1 
HETATM 6867 O  O1A   . ADP   C 3 .    ? 35.922  -1.910  -64.802 1.00 42.32  ? 1202 ADP   A O1A   1 
HETATM 6868 O  O2A   . ADP   C 3 .    ? 34.401  -3.899  -64.319 1.00 43.86  ? 1202 ADP   A O2A   1 
HETATM 6869 O  O3A   . ADP   C 3 .    ? 36.279  -4.058  -65.966 1.00 46.47  ? 1202 ADP   A O3A   1 
HETATM 6870 O  "O5'" . ADP   C 3 .    ? 36.753  -3.959  -63.479 1.00 49.69  ? 1202 ADP   A "O5'" 1 
HETATM 6871 C  "C5'" . ADP   C 3 .    ? 38.156  -3.607  -63.437 1.00 52.76  ? 1202 ADP   A "C5'" 1 
HETATM 6872 C  "C4'" . ADP   C 3 .    ? 38.777  -4.177  -62.187 1.00 53.68  ? 1202 ADP   A "C4'" 1 
HETATM 6873 O  "O4'" . ADP   C 3 .    ? 38.104  -3.598  -61.038 1.00 56.81  ? 1202 ADP   A "O4'" 1 
HETATM 6874 C  "C3'" . ADP   C 3 .    ? 38.702  -5.707  -62.018 1.00 56.62  ? 1202 ADP   A "C3'" 1 
HETATM 6875 O  "O3'" . ADP   C 3 .    ? 39.927  -6.342  -61.665 1.00 54.48  ? 1202 ADP   A "O3'" 1 
HETATM 6876 C  "C2'" . ADP   C 3 .    ? 37.724  -5.878  -60.857 1.00 61.28  ? 1202 ADP   A "C2'" 1 
HETATM 6877 O  "O2'" . ADP   C 3 .    ? 37.972  -7.059  -60.125 1.00 68.03  ? 1202 ADP   A "O2'" 1 
HETATM 6878 C  "C1'" . ADP   C 3 .    ? 37.962  -4.596  -60.062 1.00 57.82  ? 1202 ADP   A "C1'" 1 
HETATM 6879 N  N9    . ADP   C 3 .    ? 36.837  -4.268  -59.204 1.00 54.80  ? 1202 ADP   A N9    1 
HETATM 6880 C  C8    . ADP   C 3 .    ? 35.616  -3.803  -59.622 1.00 57.74  ? 1202 ADP   A C8    1 
HETATM 6881 N  N7    . ADP   C 3 .    ? 34.750  -3.674  -58.651 1.00 54.43  ? 1202 ADP   A N7    1 
HETATM 6882 C  C5    . ADP   C 3 .    ? 35.447  -4.079  -57.523 1.00 51.12  ? 1202 ADP   A C5    1 
HETATM 6883 C  C6    . ADP   C 3 .    ? 35.070  -4.162  -56.171 1.00 54.84  ? 1202 ADP   A C6    1 
HETATM 6884 N  N6    . ADP   C 3 .    ? 33.844  -3.868  -55.737 1.00 56.71  ? 1202 ADP   A N6    1 
HETATM 6885 N  N1    . ADP   C 3 .    ? 35.995  -4.622  -55.293 1.00 57.07  ? 1202 ADP   A N1    1 
HETATM 6886 C  C2    . ADP   C 3 .    ? 37.216  -4.945  -55.754 1.00 61.29  ? 1202 ADP   A C2    1 
HETATM 6887 N  N3    . ADP   C 3 .    ? 37.686  -4.901  -57.003 1.00 61.68  ? 1202 ADP   A N3    1 
HETATM 6888 C  C4    . ADP   C 3 .    ? 36.735  -4.459  -57.851 1.00 55.89  ? 1202 ADP   A C4    1 
HETATM 6889 MG MG    . MG    D 4 .    ? 32.167  -3.740  -67.773 1.00 42.72  ? 1203 MG    A MG    1 
HETATM 6890 C  C1    . EDO   E 5 .    ? 32.331  -3.405  -61.367 1.00 75.36  ? 1204 EDO   A C1    1 
HETATM 6891 O  O1    . EDO   E 5 .    ? 33.254  -4.424  -61.710 1.00 79.21  ? 1204 EDO   A O1    1 
HETATM 6892 C  C2    . EDO   E 5 .    ? 31.526  -3.708  -60.146 1.00 78.65  ? 1204 EDO   A C2    1 
HETATM 6893 O  O2    . EDO   E 5 .    ? 31.901  -2.922  -59.028 1.00 74.28  ? 1204 EDO   A O2    1 
HETATM 6894 C  C1    . EDO   F 5 .    ? 5.372   12.227  -83.705 1.00 83.88  ? 1205 EDO   A C1    1 
HETATM 6895 O  O1    . EDO   F 5 .    ? 4.595   11.809  -84.806 1.00 86.08  ? 1205 EDO   A O1    1 
HETATM 6896 C  C2    . EDO   F 5 .    ? 4.547   12.916  -82.686 1.00 86.40  ? 1205 EDO   A C2    1 
HETATM 6897 O  O2    . EDO   F 5 .    ? 3.937   12.017  -81.768 1.00 78.58  ? 1205 EDO   A O2    1 
HETATM 6898 C  C1    . EDO   G 5 .    ? -6.924  -0.069  -47.236 1.00 69.47  ? 1206 EDO   A C1    1 
HETATM 6899 O  O1    . EDO   G 5 .    ? -5.609  0.015   -46.713 1.00 75.56  ? 1206 EDO   A O1    1 
HETATM 6900 C  C2    . EDO   G 5 .    ? -7.631  1.214   -47.087 1.00 73.83  ? 1206 EDO   A C2    1 
HETATM 6901 O  O2    . EDO   G 5 .    ? -7.739  1.957   -48.294 1.00 74.05  ? 1206 EDO   A O2    1 
HETATM 6902 C  C1    . EDO   H 5 .    ? 3.237   8.579   -49.130 1.00 66.06  ? 1207 EDO   A C1    1 
HETATM 6903 O  O1    . EDO   H 5 .    ? 3.770   9.880   -49.417 1.00 66.04  ? 1207 EDO   A O1    1 
HETATM 6904 C  C2    . EDO   H 5 .    ? 3.749   7.925   -47.897 1.00 66.77  ? 1207 EDO   A C2    1 
HETATM 6905 O  O2    . EDO   H 5 .    ? 2.722   7.503   -47.008 1.00 76.37  ? 1207 EDO   A O2    1 
HETATM 6906 C  C1    . EDO   I 5 .    ? 8.140   -27.543 -47.875 1.00 74.45  ? 1208 EDO   A C1    1 
HETATM 6907 O  O1    . EDO   I 5 .    ? 7.816   -28.694 -48.628 1.00 78.95  ? 1208 EDO   A O1    1 
HETATM 6908 C  C2    . EDO   I 5 .    ? 7.141   -27.239 -46.823 1.00 68.33  ? 1208 EDO   A C2    1 
HETATM 6909 O  O2    . EDO   I 5 .    ? 7.409   -27.839 -45.583 1.00 70.90  ? 1208 EDO   A O2    1 
HETATM 6910 C  C1    . EDO   J 5 .    ? -13.454 -10.800 -50.986 1.00 48.10  ? 1209 EDO   A C1    1 
HETATM 6911 O  O1    . EDO   J 5 .    ? -12.730 -10.672 -49.774 1.00 44.34  ? 1209 EDO   A O1    1 
HETATM 6912 C  C2    . EDO   J 5 .    ? -14.470 -9.716  -51.144 1.00 51.77  ? 1209 EDO   A C2    1 
HETATM 6913 O  O2    . EDO   J 5 .    ? -13.944 -8.386  -51.159 1.00 52.44  ? 1209 EDO   A O2    1 
HETATM 6914 C  C1    . EDO   K 5 .    ? -13.704 2.997   -51.017 1.00 66.18  ? 1210 EDO   A C1    1 
HETATM 6915 O  O1    . EDO   K 5 .    ? -14.202 3.505   -52.231 1.00 66.74  ? 1210 EDO   A O1    1 
HETATM 6916 C  C2    . EDO   K 5 .    ? -14.614 3.273   -49.893 1.00 70.83  ? 1210 EDO   A C2    1 
HETATM 6917 O  O2    . EDO   K 5 .    ? -15.242 2.110   -49.440 1.00 80.83  ? 1210 EDO   A O2    1 
HETATM 6918 S  S     . SO4   L 6 .    ? 18.241  -13.588 -59.747 1.00 109.04 ? 1211 SO4   A S     1 
HETATM 6919 O  O1    . SO4   L 6 .    ? 19.130  -13.130 -60.798 1.00 84.88  ? 1211 SO4   A O1    1 
HETATM 6920 O  O2    . SO4   L 6 .    ? 17.001  -12.862 -59.813 1.00 105.95 ? 1211 SO4   A O2    1 
HETATM 6921 O  O3    . SO4   L 6 .    ? 17.978  -14.995 -59.912 1.00 98.34  ? 1211 SO4   A O3    1 
HETATM 6922 O  O4    . SO4   L 6 .    ? 18.832  -13.363 -58.452 1.00 105.84 ? 1211 SO4   A O4    1 
HETATM 6923 S  S     . SO4   M 6 .    ? 14.639  0.219   -65.078 1.00 68.31  ? 1212 SO4   A S     1 
HETATM 6924 O  O1    . SO4   M 6 .    ? 15.203  -0.270  -66.333 1.00 75.12  ? 1212 SO4   A O1    1 
HETATM 6925 O  O2    . SO4   M 6 .    ? 13.207  0.266   -65.172 1.00 86.91  ? 1212 SO4   A O2    1 
HETATM 6926 O  O3    . SO4   M 6 .    ? 15.022  -0.677  -64.008 1.00 62.98  ? 1212 SO4   A O3    1 
HETATM 6927 O  O4    . SO4   M 6 .    ? 15.122  1.547   -64.835 1.00 70.00  ? 1212 SO4   A O4    1 
HETATM 6928 S  S     . SO4   N 6 .    ? -19.461 -7.411  -45.180 1.00 62.15  ? 1213 SO4   A S     1 
HETATM 6929 O  O1    . SO4   N 6 .    ? -20.309 -6.533  -45.936 1.00 59.11  ? 1213 SO4   A O1    1 
HETATM 6930 O  O2    . SO4   N 6 .    ? -20.152 -7.813  -43.993 1.00 68.80  ? 1213 SO4   A O2    1 
HETATM 6931 O  O3    . SO4   N 6 .    ? -19.150 -8.570  -45.980 1.00 64.47  ? 1213 SO4   A O3    1 
HETATM 6932 O  O4    . SO4   N 6 .    ? -18.237 -6.730  -44.806 1.00 66.35  ? 1213 SO4   A O4    1 
HETATM 6933 S  S     . SO4   O 6 .    ? 2.033   -2.033  -87.760 0.50 117.63 ? 1214 SO4   A S     1 
HETATM 6934 O  O1    . SO4   O 6 .    ? 2.103   -3.137  -88.683 0.50 106.55 ? 1214 SO4   A O1    1 
HETATM 6935 O  O2    . SO4   O 6 .    ? 0.792   -2.096  -87.034 0.50 117.60 ? 1214 SO4   A O2    1 
HETATM 6936 O  O3    . SO4   O 6 .    ? 3.137   -2.104  -86.837 0.50 106.55 ? 1214 SO4   A O3    1 
HETATM 6937 O  O4    . SO4   O 6 .    ? 2.097   -0.792  -88.486 0.50 117.71 ? 1214 SO4   A O4    1 
HETATM 6938 CL CL    . CL    P 7 .    ? -11.401 -6.940  -67.705 1.00 89.66  ? 1215 CL    A CL    1 
HETATM 6939 O  O     . HOH   Q 8 .    ? 21.146  -12.113 -60.876 1.00 55.53  ? 1301 HOH   A O     1 
HETATM 6940 O  O     . HOH   Q 8 .    ? -30.870 0.582   -69.544 1.00 69.68  ? 1302 HOH   A O     1 
HETATM 6941 O  O     . HOH   Q 8 .    ? 16.255  -0.567  -62.012 1.00 50.69  ? 1303 HOH   A O     1 
HETATM 6942 O  O     . HOH   Q 8 .    ? 20.525  -0.325  -34.195 1.00 66.76  ? 1304 HOH   A O     1 
HETATM 6943 O  O     . HOH   Q 8 .    ? 42.782  11.021  -68.187 1.00 45.46  ? 1305 HOH   A O     1 
HETATM 6944 O  O     . HOH   Q 8 .    ? -2.110  -12.128 -71.908 1.00 54.68  ? 1306 HOH   A O     1 
HETATM 6945 O  O     . HOH   Q 8 .    ? 15.859  6.788   -59.744 1.00 43.80  ? 1307 HOH   A O     1 
HETATM 6946 O  O     . HOH   Q 8 .    ? 14.461  9.418   -82.641 1.00 45.06  ? 1308 HOH   A O     1 
HETATM 6947 O  O     . HOH   Q 8 .    ? 12.180  5.480   -61.149 1.00 56.94  ? 1309 HOH   A O     1 
HETATM 6948 O  O     . HOH   Q 8 .    ? -14.681 -20.676 -44.258 1.00 55.17  ? 1310 HOH   A O     1 
HETATM 6949 O  O     . HOH   Q 8 .    ? -20.419 7.854   -63.843 1.00 55.24  ? 1311 HOH   A O     1 
HETATM 6950 O  O     . HOH   Q 8 .    ? 40.160  7.885   -58.984 1.00 46.96  ? 1312 HOH   A O     1 
HETATM 6951 O  O     . HOH   Q 8 .    ? 46.994  18.754  -44.476 1.00 55.06  ? 1313 HOH   A O     1 
HETATM 6952 O  O     . HOH   Q 8 .    ? 3.734   15.362  -65.178 1.00 51.61  ? 1314 HOH   A O     1 
HETATM 6953 O  O     . HOH   Q 8 .    ? -17.475 2.288   -71.358 1.00 49.74  ? 1315 HOH   A O     1 
HETATM 6954 O  O     . HOH   Q 8 .    ? 0.424   -4.264  -68.308 1.00 55.17  ? 1316 HOH   A O     1 
HETATM 6955 O  O     . HOH   Q 8 .    ? 28.750  -3.469  -65.928 1.00 47.97  ? 1317 HOH   A O     1 
HETATM 6956 O  O     . HOH   Q 8 .    ? -10.516 -11.696 -50.407 1.00 42.04  ? 1318 HOH   A O     1 
HETATM 6957 O  O     . HOH   Q 8 .    ? 29.689  -4.127  -63.511 1.00 47.94  ? 1319 HOH   A O     1 
HETATM 6958 O  O     . HOH   Q 8 .    ? 32.258  -4.094  -65.753 1.00 35.77  ? 1320 HOH   A O     1 
HETATM 6959 O  O     . HOH   Q 8 .    ? 34.495  -6.981  -64.675 1.00 57.57  ? 1321 HOH   A O     1 
HETATM 6960 O  O     . HOH   Q 8 .    ? 41.188  8.910   -64.500 1.00 42.58  ? 1322 HOH   A O     1 
HETATM 6961 O  O     . HOH   Q 8 .    ? -13.200 -16.331 -43.483 1.00 51.67  ? 1323 HOH   A O     1 
HETATM 6962 O  O     . HOH   Q 8 .    ? 36.662  17.326  -56.260 1.00 51.25  ? 1324 HOH   A O     1 
HETATM 6963 O  O     . HOH   Q 8 .    ? 7.133   -7.577  -52.714 1.00 38.28  ? 1325 HOH   A O     1 
HETATM 6964 O  O     . HOH   Q 8 .    ? -30.179 -18.385 -63.141 1.00 61.02  ? 1326 HOH   A O     1 
HETATM 6965 O  O     . HOH   Q 8 .    ? 38.861  11.991  -56.273 1.00 51.27  ? 1327 HOH   A O     1 
HETATM 6966 O  O     . HOH   Q 8 .    ? 27.358  -10.630 -66.726 1.00 46.10  ? 1328 HOH   A O     1 
HETATM 6967 O  O     . HOH   Q 8 .    ? 11.410  9.985   -52.705 1.00 41.59  ? 1329 HOH   A O     1 
HETATM 6968 O  O     . HOH   Q 8 .    ? 17.586  10.488  -54.343 1.00 55.51  ? 1330 HOH   A O     1 
HETATM 6969 O  O     . HOH   Q 8 .    ? 18.958  -6.177  -32.813 1.00 64.10  ? 1331 HOH   A O     1 
HETATM 6970 O  O     . HOH   Q 8 .    ? 39.206  21.706  -64.534 1.00 51.15  ? 1332 HOH   A O     1 
HETATM 6971 O  O     . HOH   Q 8 .    ? 40.678  18.530  -51.487 1.00 58.99  ? 1333 HOH   A O     1 
HETATM 6972 O  O     . HOH   Q 8 .    ? 38.159  29.962  -58.496 1.00 68.02  ? 1334 HOH   A O     1 
HETATM 6973 O  O     . HOH   Q 8 .    ? 38.061  5.758   -50.962 1.00 47.09  ? 1335 HOH   A O     1 
HETATM 6974 O  O     . HOH   Q 8 .    ? 32.596  -5.717  -68.299 1.00 34.10  ? 1336 HOH   A O     1 
HETATM 6975 O  O     . HOH   Q 8 .    ? 20.712  -16.390 -66.781 1.00 51.71  ? 1337 HOH   A O     1 
HETATM 6976 O  O     . HOH   Q 8 .    ? 30.937  10.673  -55.444 1.00 45.72  ? 1338 HOH   A O     1 
HETATM 6977 O  O     . HOH   Q 8 .    ? 1.842   -21.827 -47.383 1.00 49.82  ? 1339 HOH   A O     1 
HETATM 6978 O  O     . HOH   Q 8 .    ? -7.570  8.739   -49.497 1.00 49.68  ? 1340 HOH   A O     1 
HETATM 6979 O  O     . HOH   Q 8 .    ? 16.700  -1.872  -88.773 1.00 49.92  ? 1341 HOH   A O     1 
HETATM 6980 O  O     . HOH   Q 8 .    ? -1.493  12.336  -50.478 1.00 50.87  ? 1342 HOH   A O     1 
HETATM 6981 O  O     . HOH   Q 8 .    ? 47.092  15.494  -44.196 1.00 52.47  ? 1343 HOH   A O     1 
HETATM 6982 O  O     . HOH   Q 8 .    ? 42.883  6.982   -80.897 1.00 50.83  ? 1344 HOH   A O     1 
HETATM 6983 O  O     . HOH   Q 8 .    ? 33.237  -12.506 -75.227 1.00 54.69  ? 1345 HOH   A O     1 
HETATM 6984 O  O     . HOH   Q 8 .    ? 46.294  -21.125 -48.899 1.00 64.28  ? 1346 HOH   A O     1 
HETATM 6985 O  O     . HOH   Q 8 .    ? 3.207   -3.249  -35.440 1.00 49.23  ? 1347 HOH   A O     1 
HETATM 6986 O  O     . HOH   Q 8 .    ? 9.769   -9.090  -78.630 1.00 35.57  ? 1348 HOH   A O     1 
HETATM 6987 O  O     . HOH   Q 8 .    ? 38.008  -26.868 -53.529 1.00 58.18  ? 1349 HOH   A O     1 
HETATM 6988 O  O     . HOH   Q 8 .    ? -12.573 -8.264  -36.307 1.00 66.42  ? 1350 HOH   A O     1 
HETATM 6989 O  O     . HOH   Q 8 .    ? -15.509 -6.355  -45.632 1.00 46.65  ? 1351 HOH   A O     1 
HETATM 6990 O  O     . HOH   Q 8 .    ? 15.539  -4.233  -70.377 1.00 54.92  ? 1352 HOH   A O     1 
HETATM 6991 O  O     . HOH   Q 8 .    ? 22.595  -3.774  -76.356 1.00 38.50  ? 1353 HOH   A O     1 
HETATM 6992 O  O     . HOH   Q 8 .    ? 18.758  -1.135  -81.910 1.00 52.24  ? 1354 HOH   A O     1 
HETATM 6993 O  O     . HOH   Q 8 .    ? -5.748  3.402   -49.325 1.00 35.77  ? 1355 HOH   A O     1 
HETATM 6994 O  O     . HOH   Q 8 .    ? 31.825  -22.729 -45.037 1.00 58.22  ? 1356 HOH   A O     1 
HETATM 6995 O  O     . HOH   Q 8 .    ? 28.242  -2.600  -53.941 1.00 53.44  ? 1357 HOH   A O     1 
HETATM 6996 O  O     . HOH   Q 8 .    ? 43.279  3.112   -64.603 1.00 49.46  ? 1358 HOH   A O     1 
HETATM 6997 O  O     . HOH   Q 8 .    ? 26.240  21.616  -64.844 1.00 46.19  ? 1359 HOH   A O     1 
HETATM 6998 O  O     . HOH   Q 8 .    ? -5.841  5.941   -49.997 1.00 40.43  ? 1360 HOH   A O     1 
HETATM 6999 O  O     . HOH   Q 8 .    ? 27.323  -4.807  -54.715 1.00 57.15  ? 1361 HOH   A O     1 
HETATM 7000 O  O     . HOH   Q 8 .    ? 18.362  12.282  -86.614 1.00 51.82  ? 1362 HOH   A O     1 
HETATM 7001 O  O     . HOH   Q 8 .    ? 22.959  -20.218 -45.504 1.00 62.83  ? 1363 HOH   A O     1 
HETATM 7002 O  O     . HOH   Q 8 .    ? -19.094 11.483  -65.483 1.00 58.73  ? 1364 HOH   A O     1 
HETATM 7003 O  O     . HOH   Q 8 .    ? 44.225  -0.477  -79.184 1.00 53.55  ? 1365 HOH   A O     1 
HETATM 7004 O  O     . HOH   Q 8 .    ? -17.598 -23.840 -43.801 1.00 66.49  ? 1366 HOH   A O     1 
HETATM 7005 O  O     . HOH   Q 8 .    ? -12.588 -9.341  -43.646 1.00 41.43  ? 1367 HOH   A O     1 
HETATM 7006 O  O     . HOH   Q 8 .    ? 43.686  -26.084 -51.613 1.00 74.15  ? 1368 HOH   A O     1 
HETATM 7007 O  O     . HOH   Q 8 .    ? -34.772 3.785   -61.385 1.00 55.73  ? 1369 HOH   A O     1 
HETATM 7008 O  O     . HOH   Q 8 .    ? 18.717  23.759  -58.842 1.00 57.02  ? 1370 HOH   A O     1 
HETATM 7009 O  O     . HOH   Q 8 .    ? 18.642  17.809  -67.771 1.00 43.89  ? 1371 HOH   A O     1 
HETATM 7010 O  O     . HOH   Q 8 .    ? -4.511  -16.790 -66.351 1.00 61.95  ? 1372 HOH   A O     1 
HETATM 7011 O  O     . HOH   Q 8 .    ? 26.868  29.651  -63.283 1.00 54.91  ? 1373 HOH   A O     1 
HETATM 7012 O  O     . HOH   Q 8 .    ? 2.510   -6.566  -75.355 1.00 49.28  ? 1374 HOH   A O     1 
HETATM 7013 O  O     . HOH   Q 8 .    ? 22.563  17.302  -57.743 1.00 43.04  ? 1375 HOH   A O     1 
HETATM 7014 O  O     . HOH   Q 8 .    ? 25.117  -34.128 -80.705 1.00 65.92  ? 1376 HOH   A O     1 
HETATM 7015 O  O     . HOH   Q 8 .    ? 1.505   -17.275 -53.137 1.00 47.12  ? 1377 HOH   A O     1 
HETATM 7016 O  O     . HOH   Q 8 .    ? 45.000  -3.276  -60.313 1.00 56.99  ? 1378 HOH   A O     1 
HETATM 7017 O  O     . HOH   Q 8 .    ? 7.145   -3.252  -65.275 1.00 53.53  ? 1379 HOH   A O     1 
HETATM 7018 O  O     . HOH   Q 8 .    ? -13.430 -24.513 -52.513 1.00 60.35  ? 1380 HOH   A O     1 
HETATM 7019 O  O     . HOH   Q 8 .    ? -19.230 -9.426  -53.801 1.00 49.39  ? 1381 HOH   A O     1 
HETATM 7020 O  O     . HOH   Q 8 .    ? -11.643 -6.867  -43.620 1.00 39.33  ? 1382 HOH   A O     1 
HETATM 7021 O  O     . HOH   Q 8 .    ? 6.141   7.849   -87.811 1.00 65.99  ? 1383 HOH   A O     1 
HETATM 7022 O  O     . HOH   Q 8 .    ? 22.105  22.877  -71.657 1.00 50.37  ? 1384 HOH   A O     1 
HETATM 7023 O  O     . HOH   Q 8 .    ? -14.837 -25.936 -54.814 1.00 64.62  ? 1385 HOH   A O     1 
HETATM 7024 O  O     . HOH   Q 8 .    ? 17.595  -7.241  -77.313 1.00 41.71  ? 1386 HOH   A O     1 
HETATM 7025 O  O     . HOH   Q 8 .    ? 50.341  5.512   -50.005 1.00 57.28  ? 1387 HOH   A O     1 
HETATM 7026 O  O     . HOH   Q 8 .    ? -9.520  11.541  -47.844 1.00 58.47  ? 1388 HOH   A O     1 
HETATM 7027 O  O     . HOH   Q 8 .    ? 15.162  -8.802  -86.698 1.00 40.85  ? 1389 HOH   A O     1 
HETATM 7028 O  O     . HOH   Q 8 .    ? 12.761  14.769  -75.640 1.00 51.98  ? 1390 HOH   A O     1 
HETATM 7029 O  O     . HOH   Q 8 .    ? 49.786  0.260   -66.833 1.00 45.28  ? 1391 HOH   A O     1 
HETATM 7030 O  O     . HOH   Q 8 .    ? 43.548  -26.518 -55.043 1.00 58.14  ? 1392 HOH   A O     1 
HETATM 7031 O  O     . HOH   Q 8 .    ? 11.692  14.815  -79.361 1.00 67.03  ? 1393 HOH   A O     1 
HETATM 7032 O  O     . HOH   Q 8 .    ? -19.416 6.967   -66.206 1.00 51.00  ? 1394 HOH   A O     1 
HETATM 7033 O  O     . HOH   Q 8 .    ? 47.246  4.747   -75.171 1.00 55.59  ? 1395 HOH   A O     1 
HETATM 7034 O  O     . HOH   Q 8 .    ? -12.432 -14.872 -66.598 1.00 53.66  ? 1396 HOH   A O     1 
HETATM 7035 O  O     . HOH   Q 8 .    ? 23.475  -0.162  -70.975 1.00 37.51  ? 1397 HOH   A O     1 
HETATM 7036 O  O     . HOH   Q 8 .    ? -12.099 5.561   -49.064 1.00 57.76  ? 1398 HOH   A O     1 
HETATM 7037 O  O     . HOH   Q 8 .    ? 28.239  -7.762  -85.079 1.00 56.00  ? 1399 HOH   A O     1 
HETATM 7038 O  O     . HOH   Q 8 .    ? 32.263  -3.083  -69.737 1.00 43.64  ? 1400 HOH   A O     1 
HETATM 7039 O  O     . HOH   Q 8 .    ? 38.703  -10.517 -55.384 1.00 63.84  ? 1401 HOH   A O     1 
HETATM 7040 O  O     . HOH   Q 8 .    ? -20.923 -2.769  -72.614 1.00 60.11  ? 1402 HOH   A O     1 
HETATM 7041 O  O     . HOH   Q 8 .    ? 48.385  5.405   -70.183 1.00 65.03  ? 1403 HOH   A O     1 
HETATM 7042 O  O     . HOH   Q 8 .    ? -10.167 0.846   -44.278 1.00 43.19  ? 1404 HOH   A O     1 
HETATM 7043 O  O     . HOH   Q 8 .    ? -4.040  -18.202 -38.420 1.00 63.34  ? 1405 HOH   A O     1 
HETATM 7044 O  O     . HOH   Q 8 .    ? 40.108  -19.099 -52.600 1.00 54.07  ? 1406 HOH   A O     1 
HETATM 7045 O  O     . HOH   Q 8 .    ? 4.760   10.734  -52.083 1.00 54.36  ? 1407 HOH   A O     1 
HETATM 7046 O  O     . HOH   Q 8 .    ? -32.958 4.858   -68.233 1.00 63.45  ? 1408 HOH   A O     1 
HETATM 7047 O  O     A HOH   Q 8 .    ? 42.018  -6.960  -63.835 0.50 38.06  ? 1409 HOH   A O     1 
HETATM 7048 O  O     . HOH   Q 8 .    ? 3.411   14.819  -70.944 1.00 62.55  ? 1410 HOH   A O     1 
HETATM 7049 O  O     . HOH   Q 8 .    ? -25.724 -3.228  -45.380 1.00 64.63  ? 1411 HOH   A O     1 
HETATM 7050 O  O     . HOH   Q 8 .    ? 2.124   2.128   -66.204 1.00 50.98  ? 1412 HOH   A O     1 
HETATM 7051 O  O     . HOH   Q 8 .    ? 12.617  10.187  -60.270 1.00 50.80  ? 1413 HOH   A O     1 
HETATM 7052 O  O     . HOH   Q 8 .    ? 29.956  16.729  -75.933 1.00 39.78  ? 1414 HOH   A O     1 
HETATM 7053 O  O     . HOH   Q 8 .    ? 8.289   10.073  -58.329 1.00 47.56  ? 1415 HOH   A O     1 
HETATM 7054 O  O     . HOH   Q 8 .    ? -21.598 -5.952  -42.513 1.00 61.89  ? 1416 HOH   A O     1 
HETATM 7055 O  O     . HOH   Q 8 .    ? 7.220   -5.785  -50.514 1.00 42.83  ? 1417 HOH   A O     1 
HETATM 7056 O  O     . HOH   Q 8 .    ? -27.083 -10.220 -51.911 1.00 62.77  ? 1418 HOH   A O     1 
HETATM 7057 O  O     . HOH   Q 8 .    ? 11.376  7.135   -34.601 1.00 50.73  ? 1419 HOH   A O     1 
HETATM 7058 O  O     . HOH   Q 8 .    ? 6.011   -12.022 -86.017 1.00 43.23  ? 1420 HOH   A O     1 
HETATM 7059 O  O     . HOH   Q 8 .    ? -4.901  -4.486  -72.456 1.00 43.71  ? 1421 HOH   A O     1 
HETATM 7060 O  O     . HOH   Q 8 .    ? -18.275 -3.563  -69.739 1.00 63.44  ? 1422 HOH   A O     1 
HETATM 7061 O  O     . HOH   Q 8 .    ? 17.807  -21.224 -60.755 1.00 58.68  ? 1423 HOH   A O     1 
HETATM 7062 O  O     . HOH   Q 8 .    ? 23.521  17.399  -88.320 1.00 55.42  ? 1424 HOH   A O     1 
HETATM 7063 O  O     . HOH   Q 8 .    ? 24.194  -2.829  -88.780 1.00 58.66  ? 1425 HOH   A O     1 
HETATM 7064 O  O     . HOH   Q 8 .    ? 41.859  11.092  -60.503 1.00 48.93  ? 1426 HOH   A O     1 
HETATM 7065 O  O     . HOH   Q 8 .    ? 8.363   10.469  -67.570 1.00 48.04  ? 1427 HOH   A O     1 
HETATM 7066 O  O     . HOH   Q 8 .    ? 12.884  3.188   -38.194 1.00 53.62  ? 1428 HOH   A O     1 
HETATM 7067 O  O     . HOH   Q 8 .    ? 13.938  15.284  -62.448 1.00 53.76  ? 1429 HOH   A O     1 
HETATM 7068 O  O     . HOH   Q 8 .    ? 44.549  5.762   -63.844 1.00 44.79  ? 1430 HOH   A O     1 
HETATM 7069 O  O     . HOH   Q 8 .    ? 27.803  -13.228 -50.591 1.00 62.38  ? 1431 HOH   A O     1 
HETATM 7070 O  O     . HOH   Q 8 .    ? 15.735  15.220  -64.202 1.00 44.68  ? 1432 HOH   A O     1 
HETATM 7071 O  O     . HOH   Q 8 .    ? -13.263 15.019  -68.375 1.00 50.33  ? 1433 HOH   A O     1 
HETATM 7072 O  O     . HOH   Q 8 .    ? -25.862 3.836   -55.599 1.00 54.39  ? 1434 HOH   A O     1 
HETATM 7073 O  O     . HOH   Q 8 .    ? 32.902  9.339   -78.653 1.00 47.16  ? 1435 HOH   A O     1 
HETATM 7074 O  O     . HOH   Q 8 .    ? 35.511  -1.542  -53.145 1.00 50.26  ? 1436 HOH   A O     1 
HETATM 7075 O  O     . HOH   Q 8 .    ? 12.587  2.575   -42.090 1.00 52.29  ? 1437 HOH   A O     1 
HETATM 7076 O  O     . HOH   Q 8 .    ? 3.277   13.248  -63.533 1.00 58.93  ? 1438 HOH   A O     1 
HETATM 7077 O  O     . HOH   Q 8 .    ? -0.687  -1.117  -45.740 1.00 43.71  ? 1439 HOH   A O     1 
HETATM 7078 O  O     . HOH   Q 8 .    ? 4.460   -7.885  -69.549 1.00 60.18  ? 1440 HOH   A O     1 
HETATM 7079 O  O     . HOH   Q 8 .    ? 42.445  0.043   -81.341 1.00 55.74  ? 1441 HOH   A O     1 
HETATM 7080 O  O     . HOH   Q 8 .    ? -25.132 -5.083  -70.605 1.00 59.16  ? 1442 HOH   A O     1 
HETATM 7081 O  O     . HOH   Q 8 .    ? 13.398  19.618  -60.502 1.00 56.63  ? 1443 HOH   A O     1 
HETATM 7082 O  O     . HOH   Q 8 .    ? 41.906  -17.142 -70.838 1.00 58.07  ? 1444 HOH   A O     1 
HETATM 7083 O  O     . HOH   Q 8 .    ? 14.803  -12.292 -47.991 1.00 57.24  ? 1445 HOH   A O     1 
HETATM 7084 O  O     . HOH   Q 8 .    ? 31.644  8.481   -84.959 1.00 49.22  ? 1446 HOH   A O     1 
HETATM 7085 O  O     . HOH   Q 8 .    ? 15.339  2.603   -51.623 1.00 48.14  ? 1447 HOH   A O     1 
HETATM 7086 O  O     . HOH   Q 8 .    ? 19.605  -15.023 -62.911 1.00 63.26  ? 1448 HOH   A O     1 
HETATM 7087 O  O     . HOH   Q 8 .    ? -37.043 -1.326  -56.794 1.00 50.35  ? 1449 HOH   A O     1 
HETATM 7088 O  O     . HOH   Q 8 .    ? 17.430  -12.337 -70.950 1.00 54.61  ? 1450 HOH   A O     1 
HETATM 7089 O  O     . HOH   Q 8 .    ? 25.069  -15.219 -76.405 1.00 55.10  ? 1451 HOH   A O     1 
HETATM 7090 O  O     . HOH   Q 8 .    ? 17.564  -4.691  -81.454 1.00 42.50  ? 1452 HOH   A O     1 
HETATM 7091 O  O     . HOH   Q 8 .    ? 50.424  8.603   -74.165 1.00 66.31  ? 1453 HOH   A O     1 
HETATM 7092 O  O     . HOH   Q 8 .    ? 16.270  10.467  -80.802 1.00 40.90  ? 1454 HOH   A O     1 
HETATM 7093 O  O     . HOH   Q 8 .    ? 13.352  1.663   -53.332 1.00 40.55  ? 1455 HOH   A O     1 
HETATM 7094 O  O     . HOH   Q 8 .    ? -32.667 -1.704  -65.253 1.00 56.60  ? 1456 HOH   A O     1 
HETATM 7095 O  O     . HOH   Q 8 .    ? 4.244   2.498   -87.223 1.00 49.64  ? 1457 HOH   A O     1 
HETATM 7096 O  O     . HOH   Q 8 .    ? 10.803  12.435  -64.144 1.00 60.03  ? 1458 HOH   A O     1 
HETATM 7097 O  O     . HOH   Q 8 .    ? 43.789  8.437   -65.088 1.00 54.67  ? 1459 HOH   A O     1 
HETATM 7098 O  O     . HOH   Q 8 .    ? 1.216   -12.166 -37.226 1.00 50.32  ? 1460 HOH   A O     1 
HETATM 7099 O  O     . HOH   Q 8 .    ? -1.054  -7.330  -65.020 1.00 60.71  ? 1461 HOH   A O     1 
HETATM 7100 O  O     . HOH   Q 8 .    ? 21.476  -27.370 -77.494 1.00 59.70  ? 1462 HOH   A O     1 
HETATM 7101 O  O     . HOH   Q 8 .    ? -3.816  -5.456  -70.034 1.00 57.33  ? 1463 HOH   A O     1 
HETATM 7102 O  O     . HOH   Q 8 .    ? 29.541  -36.021 -53.940 1.00 47.56  ? 1464 HOH   A O     1 
HETATM 7103 O  O     . HOH   Q 8 .    ? 36.678  13.252  -57.507 1.00 47.76  ? 1465 HOH   A O     1 
HETATM 7104 O  O     . HOH   Q 8 .    ? -1.668  -10.494 -65.138 1.00 48.92  ? 1466 HOH   A O     1 
HETATM 7105 O  O     . HOH   Q 8 .    ? -14.740 6.364   -50.447 1.00 60.32  ? 1467 HOH   A O     1 
HETATM 7106 O  O     . HOH   Q 8 .    ? 47.827  6.115   -72.729 1.00 55.93  ? 1468 HOH   A O     1 
HETATM 7107 O  O     . HOH   Q 8 .    ? 31.700  11.566  -50.293 1.00 62.35  ? 1469 HOH   A O     1 
HETATM 7108 O  O     . HOH   Q 8 .    ? -9.778  -31.865 -43.832 1.00 56.31  ? 1470 HOH   A O     1 
HETATM 7109 O  O     . HOH   Q 8 .    ? 0.091   -9.660  -63.163 1.00 60.94  ? 1471 HOH   A O     1 
HETATM 7110 O  O     . HOH   Q 8 .    ? -7.323  -16.242 -44.513 1.00 49.01  ? 1472 HOH   A O     1 
HETATM 7111 O  O     . HOH   Q 8 .    ? 22.218  21.970  -79.033 1.00 61.18  ? 1473 HOH   A O     1 
HETATM 7112 O  O     . HOH   Q 8 .    ? 1.887   3.992   -83.470 1.00 47.72  ? 1474 HOH   A O     1 
HETATM 7113 O  O     . HOH   Q 8 .    ? 17.068  -2.586  -64.862 1.00 56.14  ? 1475 HOH   A O     1 
HETATM 7114 O  O     . HOH   Q 8 .    ? 33.292  -6.750  -70.784 1.00 54.94  ? 1476 HOH   A O     1 
HETATM 7115 O  O     . HOH   Q 8 .    ? 11.221  -8.190  -87.707 1.00 29.80  ? 1477 HOH   A O     1 
HETATM 7116 O  O     . HOH   Q 8 .    ? 4.586   -7.345  -77.072 1.00 32.95  ? 1478 HOH   A O     1 
HETATM 7117 O  O     . HOH   Q 8 .    ? -17.766 13.298  -64.730 1.00 60.23  ? 1479 HOH   A O     1 
HETATM 7118 O  O     . HOH   Q 8 .    ? 8.619   -3.192  -73.424 1.00 51.07  ? 1480 HOH   A O     1 
HETATM 7119 O  O     . HOH   Q 8 .    ? 20.889  -8.087  -69.203 1.00 68.58  ? 1481 HOH   A O     1 
HETATM 7120 O  O     . HOH   Q 8 .    ? -17.574 -10.534 -44.446 1.00 44.37  ? 1482 HOH   A O     1 
HETATM 7121 O  O     . HOH   Q 8 .    ? 14.987  17.740  -81.834 1.00 64.62  ? 1483 HOH   A O     1 
HETATM 7122 O  O     . HOH   Q 8 .    ? 22.135  -25.874 -83.488 1.00 72.08  ? 1484 HOH   A O     1 
HETATM 7123 O  O     . HOH   Q 8 .    ? 26.004  19.296  -82.211 1.00 50.36  ? 1485 HOH   A O     1 
HETATM 7124 O  O     . HOH   Q 8 .    ? 19.518  -5.647  -57.601 1.00 78.06  ? 1486 HOH   A O     1 
HETATM 7125 O  O     . HOH   Q 8 .    ? 15.684  5.543   -34.511 1.00 50.45  ? 1487 HOH   A O     1 
HETATM 7126 O  O     . HOH   Q 8 .    ? 7.831   4.326   -67.287 1.00 55.64  ? 1488 HOH   A O     1 
HETATM 7127 O  O     . HOH   Q 8 .    ? 5.395   -28.097 -54.620 1.00 65.22  ? 1489 HOH   A O     1 
HETATM 7128 O  O     . HOH   Q 8 .    ? -17.692 -16.242 -72.761 1.00 67.87  ? 1490 HOH   A O     1 
HETATM 7129 O  O     . HOH   Q 8 .    ? -6.431  6.107   -41.174 1.00 54.43  ? 1491 HOH   A O     1 
HETATM 7130 O  O     . HOH   Q 8 .    ? 44.660  0.242   -52.773 1.00 65.70  ? 1492 HOH   A O     1 
HETATM 7131 O  O     . HOH   Q 8 .    ? 10.997  -2.783  -71.652 1.00 52.60  ? 1493 HOH   A O     1 
HETATM 7132 O  O     . HOH   Q 8 .    ? -3.936  -29.625 -60.624 1.00 59.97  ? 1494 HOH   A O     1 
HETATM 7133 O  O     . HOH   Q 8 .    ? 20.972  -17.145 -51.348 1.00 58.13  ? 1495 HOH   A O     1 
HETATM 7134 O  O     . HOH   Q 8 .    ? 55.432  5.321   -55.374 1.00 61.52  ? 1496 HOH   A O     1 
HETATM 7135 O  O     . HOH   Q 8 .    ? 31.569  -24.118 -40.403 1.00 61.62  ? 1497 HOH   A O     1 
HETATM 7136 O  O     . HOH   Q 8 .    ? 18.049  -20.361 -45.249 1.00 60.37  ? 1498 HOH   A O     1 
HETATM 7137 O  O     . HOH   Q 8 .    ? 24.992  -9.512  -80.544 1.00 49.34  ? 1499 HOH   A O     1 
HETATM 7138 O  O     . HOH   Q 8 .    ? 44.686  -17.344 -52.883 1.00 57.04  ? 1500 HOH   A O     1 
HETATM 7139 O  O     . HOH   Q 8 .    ? 36.106  13.968  -74.787 1.00 47.43  ? 1501 HOH   A O     1 
HETATM 7140 O  O     . HOH   Q 8 .    ? -11.707 7.617   -47.451 1.00 53.70  ? 1502 HOH   A O     1 
HETATM 7141 O  O     . HOH   Q 8 .    ? -14.059 0.833   -44.994 1.00 54.34  ? 1503 HOH   A O     1 
HETATM 7142 O  O     . HOH   Q 8 .    ? -31.056 -7.183  -69.191 1.00 59.25  ? 1504 HOH   A O     1 
HETATM 7143 O  O     . HOH   Q 8 .    ? -18.813 -5.866  -77.529 1.00 60.57  ? 1505 HOH   A O     1 
HETATM 7144 O  O     . HOH   Q 8 .    ? 5.158   -18.826 -37.429 1.00 52.99  ? 1506 HOH   A O     1 
HETATM 7145 O  O     . HOH   Q 8 .    ? -9.220  -1.499  -69.381 1.00 64.03  ? 1507 HOH   A O     1 
HETATM 7146 O  O     . HOH   Q 8 .    ? 22.804  -4.626  -73.785 1.00 52.38  ? 1508 HOH   A O     1 
HETATM 7147 O  O     . HOH   Q 8 .    ? -3.804  -8.077  -69.312 1.00 67.89  ? 1509 HOH   A O     1 
HETATM 7148 O  O     . HOH   Q 8 .    ? 5.577   -12.392 -64.627 1.00 67.59  ? 1510 HOH   A O     1 
HETATM 7149 O  O     . HOH   Q 8 .    ? 17.347  -31.561 -77.158 1.00 66.86  ? 1511 HOH   A O     1 
HETATM 7150 O  O     . HOH   Q 8 .    ? 24.914  20.918  -67.219 1.00 50.47  ? 1512 HOH   A O     1 
HETATM 7151 O  O     . HOH   Q 8 .    ? -6.054  -6.071  -39.115 1.00 52.20  ? 1513 HOH   A O     1 
HETATM 7152 O  O     . HOH   Q 8 .    ? 33.013  27.871  -57.474 1.00 57.18  ? 1514 HOH   A O     1 
HETATM 7153 O  O     . HOH   Q 8 .    ? 11.686  -25.234 -56.102 1.00 70.97  ? 1515 HOH   A O     1 
HETATM 7154 O  O     . HOH   Q 8 .    ? -5.226  -30.439 -47.661 1.00 79.13  ? 1516 HOH   A O     1 
HETATM 7155 O  O     . HOH   Q 8 .    ? 29.292  21.025  -58.564 1.00 59.81  ? 1517 HOH   A O     1 
HETATM 7156 O  O     . HOH   Q 8 .    ? -16.752 -0.528  -43.937 1.00 47.71  ? 1518 HOH   A O     1 
HETATM 7157 O  O     . HOH   Q 8 .    ? 17.753  -4.982  -62.880 1.00 44.23  ? 1519 HOH   A O     1 
HETATM 7158 O  O     . HOH   Q 8 .    ? 15.102  -8.590  -40.446 1.00 65.93  ? 1520 HOH   A O     1 
HETATM 7159 O  O     . HOH   Q 8 .    ? -17.204 -18.469 -78.012 1.00 68.66  ? 1521 HOH   A O     1 
HETATM 7160 O  O     . HOH   Q 8 .    ? 19.025  7.141   -51.420 1.00 63.61  ? 1522 HOH   A O     1 
HETATM 7161 O  O     . HOH   Q 8 .    ? 8.566   -11.371 -78.544 1.00 49.41  ? 1523 HOH   A O     1 
HETATM 7162 O  O     . HOH   Q 8 .    ? 0.216   -31.330 -46.675 1.00 66.75  ? 1524 HOH   A O     1 
HETATM 7163 O  O     . HOH   Q 8 .    ? 23.355  -18.745 -83.029 1.00 59.81  ? 1525 HOH   A O     1 
HETATM 7164 O  O     . HOH   Q 8 .    ? 40.115  -39.300 -71.150 1.00 63.90  ? 1526 HOH   A O     1 
HETATM 7165 O  O     . HOH   Q 8 .    ? 48.884  8.516   -64.817 1.00 63.42  ? 1527 HOH   A O     1 
HETATM 7166 O  O     . HOH   Q 8 .    ? 47.401  2.212   -76.882 1.00 59.53  ? 1528 HOH   A O     1 
HETATM 7167 O  O     . HOH   Q 8 .    ? -18.088 -22.862 -48.268 1.00 65.28  ? 1529 HOH   A O     1 
HETATM 7168 O  O     . HOH   Q 8 .    ? 14.789  7.845   -57.690 1.00 47.31  ? 1530 HOH   A O     1 
HETATM 7169 O  O     . HOH   Q 8 .    ? 21.542  22.340  -57.652 1.00 46.04  ? 1531 HOH   A O     1 
HETATM 7170 O  O     . HOH   Q 8 .    ? 8.491   15.021  -75.361 1.00 67.77  ? 1532 HOH   A O     1 
HETATM 7171 O  O     . HOH   Q 8 .    ? 32.661  12.346  -85.758 1.00 59.33  ? 1533 HOH   A O     1 
HETATM 7172 O  O     . HOH   Q 8 .    ? -0.100  10.483  -48.513 1.00 46.13  ? 1534 HOH   A O     1 
HETATM 7173 O  O     . HOH   Q 8 .    ? 34.941  -11.345 -72.641 1.00 48.18  ? 1535 HOH   A O     1 
HETATM 7174 O  O     . HOH   Q 8 .    ? 30.773  -20.803 -45.975 1.00 55.26  ? 1536 HOH   A O     1 
HETATM 7175 O  O     . HOH   Q 8 .    ? 9.926   7.174   -71.521 1.00 55.09  ? 1537 HOH   A O     1 
HETATM 7176 O  O     . HOH   Q 8 .    ? 5.103   -9.283  -53.051 1.00 51.41  ? 1538 HOH   A O     1 
HETATM 7177 O  O     . HOH   Q 8 .    ? 42.032  -24.234 -54.530 1.00 47.56  ? 1539 HOH   A O     1 
HETATM 7178 O  O     B HOH   Q 8 .    ? 41.292  -8.812  -67.586 0.50 40.58  ? 1540 HOH   A O     1 
HETATM 7179 O  O     . HOH   Q 8 .    ? 20.081  -6.308  -61.042 1.00 45.16  ? 1541 HOH   A O     1 
HETATM 7180 O  O     . HOH   Q 8 .    ? 19.403  -7.228  -66.919 1.00 60.28  ? 1542 HOH   A O     1 
HETATM 7181 O  O     . HOH   Q 8 .    ? -25.671 5.636   -53.625 1.00 53.20  ? 1543 HOH   A O     1 
HETATM 7182 O  O     . HOH   Q 8 .    ? -37.408 -6.140  -61.281 1.00 54.08  ? 1544 HOH   A O     1 
HETATM 7183 O  O     . HOH   Q 8 .    ? -6.560  16.961  -51.794 1.00 50.20  ? 1545 HOH   A O     1 
HETATM 7184 O  O     . HOH   Q 8 .    ? -3.052  -31.021 -53.842 1.00 56.53  ? 1546 HOH   A O     1 
HETATM 7185 O  O     . HOH   Q 8 .    ? 14.353  25.567  -64.162 1.00 58.07  ? 1547 HOH   A O     1 
HETATM 7186 O  O     . HOH   Q 8 .    ? 16.027  -19.414 -59.751 1.00 63.26  ? 1548 HOH   A O     1 
HETATM 7187 O  O     . HOH   Q 8 .    ? -13.335 -29.498 -52.014 1.00 56.48  ? 1549 HOH   A O     1 
HETATM 7188 O  O     . HOH   Q 8 .    ? -16.886 12.047  -58.761 1.00 61.83  ? 1550 HOH   A O     1 
HETATM 7189 O  O     . HOH   Q 8 .    ? 3.953   -13.781 -76.360 1.00 55.33  ? 1551 HOH   A O     1 
HETATM 7190 O  O     . HOH   Q 8 .    ? 18.875  -26.952 -63.930 1.00 61.49  ? 1552 HOH   A O     1 
HETATM 7191 O  O     . HOH   Q 8 .    ? 16.046  7.685   -53.293 1.00 40.64  ? 1553 HOH   A O     1 
HETATM 7192 O  O     . HOH   Q 8 .    ? 50.599  -28.505 -50.956 1.00 61.99  ? 1554 HOH   A O     1 
HETATM 7193 O  O     . HOH   Q 8 .    ? 29.325  3.355   -50.557 1.00 60.46  ? 1555 HOH   A O     1 
HETATM 7194 O  O     . HOH   Q 8 .    ? 33.433  15.114  -84.537 1.00 59.30  ? 1556 HOH   A O     1 
HETATM 7195 O  O     . HOH   Q 8 .    ? -28.932 -14.943 -59.085 1.00 62.05  ? 1557 HOH   A O     1 
HETATM 7196 O  O     . HOH   Q 8 .    ? -20.835 -18.750 -49.165 1.00 66.11  ? 1558 HOH   A O     1 
HETATM 7197 O  O     . HOH   Q 8 .    ? -4.583  -29.986 -67.779 1.00 53.80  ? 1559 HOH   A O     1 
HETATM 7198 O  O     . HOH   Q 8 .    ? -6.078  -12.959 -38.148 1.00 57.74  ? 1560 HOH   A O     1 
HETATM 7199 O  O     . HOH   Q 8 .    ? 37.367  17.456  -58.384 1.00 54.04  ? 1561 HOH   A O     1 
HETATM 7200 O  O     . HOH   Q 8 .    ? 28.518  12.194  -50.450 1.00 54.83  ? 1562 HOH   A O     1 
HETATM 7201 O  O     . HOH   Q 8 .    ? 42.262  -3.265  -59.363 1.00 61.30  ? 1563 HOH   A O     1 
HETATM 7202 O  O     . HOH   Q 8 .    ? 28.819  -6.325  -56.731 1.00 57.91  ? 1564 HOH   A O     1 
HETATM 7203 O  O     . HOH   Q 8 .    ? -23.178 -3.266  -71.116 1.00 58.72  ? 1565 HOH   A O     1 
HETATM 7204 O  O     . HOH   Q 8 .    ? 46.881  22.354  -55.182 1.00 69.28  ? 1566 HOH   A O     1 
HETATM 7205 O  O     . HOH   Q 8 .    ? -5.487  -15.827 -71.159 1.00 53.58  ? 1567 HOH   A O     1 
HETATM 7206 O  O     . HOH   Q 8 .    ? 1.288   -9.460  -59.994 1.00 51.81  ? 1568 HOH   A O     1 
HETATM 7207 O  O     . HOH   Q 8 .    ? 15.320  21.436  -70.344 1.00 64.16  ? 1569 HOH   A O     1 
HETATM 7208 O  O     . HOH   Q 8 .    ? 20.941  -3.964  -53.804 1.00 57.62  ? 1570 HOH   A O     1 
HETATM 7209 O  O     . HOH   Q 8 .    ? 17.439  -27.645 -70.599 1.00 63.11  ? 1571 HOH   A O     1 
HETATM 7210 O  O     . HOH   Q 8 .    ? 17.920  -24.234 -74.996 1.00 55.42  ? 1572 HOH   A O     1 
HETATM 7211 O  O     . HOH   Q 8 .    ? -31.133 -0.074  -72.314 1.00 61.53  ? 1573 HOH   A O     1 
HETATM 7212 O  O     . HOH   Q 8 .    ? 6.874   -11.135 -76.635 1.00 53.26  ? 1574 HOH   A O     1 
HETATM 7213 O  O     . HOH   Q 8 .    ? 11.327  3.298   -69.642 1.00 54.67  ? 1575 HOH   A O     1 
HETATM 7214 O  O     . HOH   Q 8 .    ? 21.036  -8.904  -61.944 1.00 55.40  ? 1576 HOH   A O     1 
HETATM 7215 O  O     . HOH   Q 8 .    ? 43.253  26.417  -62.845 1.00 59.67  ? 1577 HOH   A O     1 
HETATM 7216 O  O     . HOH   Q 8 .    ? 33.768  -30.893 -77.663 1.00 63.18  ? 1578 HOH   A O     1 
HETATM 7217 O  O     . HOH   Q 8 .    ? 38.027  -32.582 -43.369 1.00 57.69  ? 1579 HOH   A O     1 
HETATM 7218 O  O     . HOH   Q 8 .    ? -35.082 -3.102  -53.602 1.00 64.94  ? 1580 HOH   A O     1 
HETATM 7219 O  O     . HOH   Q 8 .    ? -36.181 7.944   -67.266 1.00 62.90  ? 1581 HOH   A O     1 
HETATM 7220 O  O     . HOH   Q 8 .    ? 40.301  -18.722 -71.804 1.00 59.18  ? 1582 HOH   A O     1 
HETATM 7221 O  O     . HOH   Q 8 .    ? 26.898  -12.024 -73.761 1.00 57.51  ? 1583 HOH   A O     1 
HETATM 7222 O  O     . HOH   Q 8 .    ? 30.078  25.012  -68.896 1.00 63.15  ? 1584 HOH   A O     1 
HETATM 7223 O  O     . HOH   Q 8 .    ? 41.748  -12.846 -44.424 1.00 63.10  ? 1585 HOH   A O     1 
HETATM 7224 O  O     . HOH   Q 8 .    ? 21.407  30.784  -50.976 1.00 70.90  ? 1586 HOH   A O     1 
HETATM 7225 O  O     . HOH   Q 8 .    ? 18.532  -17.849 -52.311 1.00 82.04  ? 1587 HOH   A O     1 
HETATM 7226 O  O     . HOH   Q 8 .    ? 3.809   -11.961 -79.271 1.00 60.08  ? 1588 HOH   A O     1 
HETATM 7227 O  O     . HOH   Q 8 .    ? -9.711  -15.332 -69.518 1.00 70.56  ? 1589 HOH   A O     1 
HETATM 7228 O  O     . HOH   Q 8 .    ? -23.892 -7.132  -43.224 1.00 58.63  ? 1590 HOH   A O     1 
HETATM 7229 O  O     . HOH   Q 8 .    ? 43.882  13.109  -66.531 1.00 61.28  ? 1591 HOH   A O     1 
HETATM 7230 O  O     . HOH   Q 8 .    ? 39.644  -10.918 -79.866 1.00 68.84  ? 1592 HOH   A O     1 
HETATM 7231 O  O     . HOH   Q 8 .    ? -31.856 -4.221  -65.942 1.00 64.57  ? 1593 HOH   A O     1 
HETATM 7232 O  O     . HOH   Q 8 .    ? 11.678  13.582  -59.191 1.00 67.22  ? 1594 HOH   A O     1 
HETATM 7233 O  O     A HOH   Q 8 .    ? -17.384 -5.877  -67.345 0.50 46.64  ? 1595 HOH   A O     1 
HETATM 7234 O  O     . HOH   Q 8 .    ? 11.790  -15.914 -35.415 1.00 63.13  ? 1596 HOH   A O     1 
HETATM 7235 O  O     . HOH   Q 8 .    ? 3.527   -8.830  -54.955 1.00 55.21  ? 1597 HOH   A O     1 
HETATM 7236 O  O     . HOH   Q 8 .    ? -4.871  -7.165  -73.948 1.00 57.47  ? 1598 HOH   A O     1 
HETATM 7237 O  O     . HOH   Q 8 .    ? 13.109  -2.526  -59.142 1.00 55.95  ? 1599 HOH   A O     1 
HETATM 7238 O  O     . HOH   Q 8 .    ? 40.669  10.838  -58.496 1.00 48.68  ? 1600 HOH   A O     1 
HETATM 7239 O  O     . HOH   Q 8 .    ? -8.956  -14.502 -38.797 1.00 57.76  ? 1601 HOH   A O     1 
HETATM 7240 O  O     . HOH   Q 8 .    ? 25.504  -20.425 -86.285 1.00 60.94  ? 1602 HOH   A O     1 
HETATM 7241 O  O     . HOH   Q 8 .    ? 25.591  4.992   -51.730 1.00 60.05  ? 1603 HOH   A O     1 
HETATM 7242 O  O     . HOH   Q 8 .    ? 8.932   -6.636  -31.975 1.00 56.64  ? 1604 HOH   A O     1 
HETATM 7243 O  O     . HOH   Q 8 .    ? 33.042  -0.463  -53.672 1.00 48.48  ? 1605 HOH   A O     1 
HETATM 7244 O  O     . HOH   Q 8 .    ? 15.144  20.710  -57.903 1.00 59.16  ? 1606 HOH   A O     1 
HETATM 7245 O  O     . HOH   Q 8 .    ? 50.442  1.873   -68.616 1.00 54.23  ? 1607 HOH   A O     1 
HETATM 7246 O  O     . HOH   Q 8 .    ? 1.478   -11.305 -53.064 1.00 54.89  ? 1608 HOH   A O     1 
HETATM 7247 O  O     . HOH   Q 8 .    ? 17.680  -1.160  -46.081 1.00 67.38  ? 1609 HOH   A O     1 
HETATM 7248 O  O     . HOH   Q 8 .    ? -15.230 -9.037  -44.476 1.00 46.90  ? 1610 HOH   A O     1 
HETATM 7249 O  O     . HOH   Q 8 .    ? 20.349  23.490  -70.402 1.00 59.14  ? 1611 HOH   A O     1 
HETATM 7250 O  O     . HOH   Q 8 .    ? 9.054   -6.361  -70.412 1.00 70.29  ? 1612 HOH   A O     1 
HETATM 7251 O  O     . HOH   Q 8 .    ? -13.832 9.572   -75.582 1.00 65.35  ? 1613 HOH   A O     1 
HETATM 7252 O  O     . HOH   Q 8 .    ? -4.043  -32.772 -47.852 1.00 63.20  ? 1614 HOH   A O     1 
HETATM 7253 O  O     . HOH   Q 8 .    ? 11.083  1.398   -71.069 1.00 53.94  ? 1615 HOH   A O     1 
HETATM 7254 O  O     . HOH   Q 8 .    ? 14.686  -22.297 -52.366 1.00 72.92  ? 1616 HOH   A O     1 
HETATM 7255 O  O     . HOH   Q 8 .    ? -24.160 -19.936 -71.863 1.00 62.22  ? 1617 HOH   A O     1 
HETATM 7256 O  O     . HOH   Q 8 .    ? 39.103  16.401  -50.894 1.00 52.73  ? 1618 HOH   A O     1 
HETATM 7257 O  O     . HOH   Q 8 .    ? 13.159  -11.510 -85.010 1.00 59.90  ? 1619 HOH   A O     1 
HETATM 7258 O  O     . HOH   Q 8 .    ? 18.483  20.701  -84.891 1.00 69.65  ? 1620 HOH   A O     1 
HETATM 7259 O  O     . HOH   Q 8 .    ? -15.080 9.174   -50.776 1.00 60.13  ? 1621 HOH   A O     1 
HETATM 7260 O  O     . HOH   Q 8 .    ? 15.078  14.312  -88.201 1.00 65.80  ? 1622 HOH   A O     1 
HETATM 7261 O  O     . HOH   Q 8 .    ? -21.824 11.155  -66.387 1.00 63.34  ? 1623 HOH   A O     1 
HETATM 7262 O  O     . HOH   Q 8 .    ? 0.524   -31.708 -51.725 1.00 66.34  ? 1624 HOH   A O     1 
HETATM 7263 O  O     . HOH   Q 8 .    ? 9.777   -19.641 -55.961 1.00 60.35  ? 1625 HOH   A O     1 
HETATM 7264 O  O     . HOH   Q 8 .    ? 32.845  16.932  -75.482 1.00 54.12  ? 1626 HOH   A O     1 
HETATM 7265 O  O     . HOH   Q 8 .    ? 15.687  5.474   -51.567 1.00 64.71  ? 1627 HOH   A O     1 
HETATM 7266 O  O     . HOH   Q 8 .    ? 1.072   -8.532  -70.919 1.00 76.81  ? 1628 HOH   A O     1 
HETATM 7267 O  O     . HOH   Q 8 .    ? 9.254   9.902   -63.003 1.00 58.63  ? 1629 HOH   A O     1 
HETATM 7268 O  O     . HOH   Q 8 .    ? -11.448 -17.893 -42.232 1.00 55.79  ? 1630 HOH   A O     1 
HETATM 7269 O  O     . HOH   Q 8 .    ? -21.123 6.438   -68.247 1.00 50.69  ? 1631 HOH   A O     1 
HETATM 7270 O  O     . HOH   Q 8 .    ? -0.994  -5.607  -69.837 1.00 47.60  ? 1632 HOH   A O     1 
HETATM 7271 O  O     . HOH   Q 8 .    ? 15.260  -12.968 -54.179 1.00 67.27  ? 1633 HOH   A O     1 
HETATM 7272 O  O     . HOH   Q 8 .    ? 4.855   -9.938  -77.144 1.00 55.51  ? 1634 HOH   A O     1 
HETATM 7273 O  O     . HOH   Q 8 .    ? 42.253  29.976  -55.563 1.00 54.32  ? 1635 HOH   A O     1 
HETATM 7274 O  O     . HOH   Q 8 .    ? 11.692  15.257  -66.106 1.00 60.21  ? 1636 HOH   A O     1 
HETATM 7275 O  O     . HOH   Q 8 .    ? -19.243 3.315   -73.025 1.00 70.16  ? 1637 HOH   A O     1 
HETATM 7276 O  O     . HOH   Q 8 .    ? 36.924  -14.103 -44.248 1.00 60.67  ? 1638 HOH   A O     1 
HETATM 7277 O  O     . HOH   Q 8 .    ? 20.761  17.038  -55.825 1.00 58.50  ? 1639 HOH   A O     1 
HETATM 7278 O  O     . HOH   Q 8 .    ? 5.866   12.475  -63.747 1.00 50.70  ? 1640 HOH   A O     1 
HETATM 7279 O  O     . HOH   Q 8 .    ? -16.939 2.055   -75.646 1.00 57.06  ? 1641 HOH   A O     1 
HETATM 7280 O  O     . HOH   Q 8 .    ? 16.181  -39.068 -79.562 1.00 73.69  ? 1642 HOH   A O     1 
HETATM 7281 O  O     . HOH   Q 8 .    ? 16.502  -19.452 -75.176 1.00 59.47  ? 1643 HOH   A O     1 
HETATM 7282 O  O     . HOH   Q 8 .    ? 15.919  -5.372  -61.346 1.00 62.55  ? 1644 HOH   A O     1 
HETATM 7283 O  O     . HOH   Q 8 .    ? 50.938  -23.047 -52.789 1.00 65.12  ? 1645 HOH   A O     1 
HETATM 7284 O  O     . HOH   Q 8 .    ? 42.807  -39.198 -78.591 1.00 61.87  ? 1646 HOH   A O     1 
HETATM 7285 O  O     . HOH   Q 8 .    ? 16.607  8.619   -92.802 1.00 68.89  ? 1647 HOH   A O     1 
HETATM 7286 O  O     . HOH   Q 8 .    ? 53.666  -33.706 -52.932 1.00 71.60  ? 1648 HOH   A O     1 
HETATM 7287 O  O     . HOH   Q 8 .    ? -14.318 7.316   -74.985 1.00 61.33  ? 1649 HOH   A O     1 
HETATM 7288 O  O     . HOH   Q 8 .    ? -31.388 -23.112 -84.857 1.00 63.82  ? 1650 HOH   A O     1 
HETATM 7289 O  O     . HOH   Q 8 .    ? -20.859 7.699   -70.452 1.00 53.94  ? 1651 HOH   A O     1 
HETATM 7290 O  O     . HOH   Q 8 .    ? 15.084  -37.491 -54.872 1.00 65.45  ? 1652 HOH   A O     1 
HETATM 7291 O  O     . HOH   Q 8 .    ? -16.934 9.766   -81.747 1.00 69.51  ? 1653 HOH   A O     1 
HETATM 7292 O  O     . HOH   Q 8 .    ? 26.605  4.689   -37.247 1.00 68.74  ? 1654 HOH   A O     1 
HETATM 7293 O  O     . HOH   Q 8 .    ? -17.055 6.699   -77.406 1.00 51.01  ? 1655 HOH   A O     1 
HETATM 7294 O  O     . HOH   Q 8 .    ? 7.444   -42.141 -57.908 1.00 62.70  ? 1656 HOH   A O     1 
HETATM 7295 O  O     . HOH   Q 8 .    ? 9.215   -49.394 -55.004 1.00 64.87  ? 1657 HOH   A O     1 
HETATM 7296 O  O     . HOH   Q 8 .    ? 6.920   -55.350 -53.501 1.00 67.58  ? 1658 HOH   A O     1 
HETATM 7297 O  O     . HOH   Q 8 .    ? 1.658   -58.344 -52.236 1.00 61.49  ? 1659 HOH   A O     1 
# 
