data_9C0G
# 
_entry.id   9C0G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9C0G         pdb_00009c0g 10.2210/pdb9c0g/pdb 
WWPDB D_1000284481 ?            ?                   
EMDB  EMD-45083    ?            ?                   
# 
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 2025-02-12 ? 
2 'Structure model' 1 1 2025-02-19 ? 
3 'Structure model' 1 2 2025-03-19 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
3 3 'Structure model' 'Data collection'     
4 3 'Structure model' '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' em_admin 
3 3 'Structure model' citation 
4 3 'Structure model' em_admin 
# 
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.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_em_admin.last_update'             
5 3 'Structure model' '_citation.journal_volume'          
6 3 'Structure model' '_citation.page_first'              
7 3 'Structure model' '_citation.page_last'               
8 3 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C0G 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-25 
_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_database_related.db_name        EMDB 
_pdbx_database_related.details        'Phosphorylated human NKCC1 in complex with torsemide' 
_pdbx_database_related.db_id          EMD-45083 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              erhu.cao@biochem.utah.edu 
_pdbx_contact_author.name_first         Erhu 
_pdbx_contact_author.name_last          Cao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3102-5692 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhao, Y.X.' 1 ? 
'Cao, E.H.'  2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Embo J.' 
_citation.journal_id_ASTM           EMJODG 
_citation.journal_id_CSD            0897 
_citation.journal_id_ISSN           1460-2075 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            44 
_citation.language                  ? 
_citation.page_first                1540 
_citation.page_last                 1562 
_citation.title                     'Structural basis for human NKCC1 inhibition by loop diuretic drugs.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s44318-025-00368-6 
_citation.pdbx_database_id_PubMed   39875725 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhao, Y.'      1 ? 
primary 'Vidossich, P.' 2 ? 
primary 'Forbush, B.'   3 ? 
primary 'Ma, J.'        4 ? 
primary 'Rinehart, J.'  5 ? 
primary 'De Vivo, M.'   6 ? 
primary 'Cao, E.'       7 ? 
# 
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 'Solute carrier family 12 member 2'                                    131663.406 2 ? ? ? ? 
2 non-polymer syn '4-(3-methylanilino)-N-[(propan-2-yl)carbamoyl]pyridine-3-sulfonamide' 348.420    2 ? ? ? ? 
3 non-polymer nat 'CHLORIDE ION'                                                         35.453     2 ? ? ? ? 
4 non-polymer syn 'SODIUM ION'                                                           22.990     2 ? ? ? ? 
5 water       nat water                                                                  18.015     2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Basolateral Na-K-Cl symporter,Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MEPRPTAPSSGAPGLAGVGETPSAAALAAARVELPGTAVPSVPEDAAPASRDGGGVRDEGPAAAGDGLGRPLGPTPSQSR
FQVDLVSENAGRAAAAAAAAAAAAAAAGAGAGAKQTPADGEASGESEPAKGSEEAKGRFRVNFVDPAASSSAEDSLSDAA
GVGVDGPNVSFQNGGDTVLSEGSSLHSGGGGGSGHHQHYYYDTHTNTYYLRTFGHN(TPO)MDAVPRIDHYRHTAAQLGE
KLLRPSLAELHDELEKEPFEDGFANGEESTPTRDAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAG
IGLSVLVIMMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFANAVAVAMYVVGFAETVVELLK
EHSILMIDEINDIRIIGAITVVILLGISVAGMEWEAKAQIVLLVILLLAIGDFVIGTFIPLESKKPKGFFGYKSEIFNEN
FGPDFREEETFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTLVYVGIAVSVGSCVVRDATGNVNDTI
VTELTNCTSAACKLNFDFSSCESSPCSYGLMNNFQVMSMVSGFTPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYP
AFQMFAKGYGKNNEPLRGYILTFLIALGFILIAELNVIAPIISNFFLASYALINFSVFHASLAKSPGWRPAFKYYNMWIS
LLGAILCCIVMFVINWWAALLTYVIVLGLYIYVTYKKPDVNWGSSTQALTYLNALQHSIRLSGVEDHVKNFRPQCLVMTG
APNSRPALLHLVHDFTKNVGLMICGHVHMGPRRQAMKEMSIDQAKYQRWLIKNKMKAFYAPVHADDLREGAQYLMQAAGL
GRMKPNTLVLGFKKDWLQADMRDVDMYINLFHDAFDIQYGVVVIRLKEGLDISHLQGQEELLSSQEKSPGTKDVVVSVEY
SKKSDLDTSKPLSEKPITHKVEEEDGKTATQPLLKKESKGPIVPLNVADQKLLEASTQFQKKQGKNTIDVWWLFDDGGLT
LLIPYLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIIAFEEIIEPYRLHED
DKEQDIADKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGAVSSALYMAWLEALSKDLPP
ILLVRGNHQSVLTFYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEPRPTAPSSGAPGLAGVGETPSAAALAAARVELPGTAVPSVPEDAAPASRDGGGVRDEGPAAAGDGLGRPLGPTPSQSR
FQVDLVSENAGRAAAAAAAAAAAAAAAGAGAGAKQTPADGEASGESEPAKGSEEAKGRFRVNFVDPAASSSAEDSLSDAA
GVGVDGPNVSFQNGGDTVLSEGSSLHSGGGGGSGHHQHYYYDTHTNTYYLRTFGHNTMDAVPRIDHYRHTAAQLGEKLLR
PSLAELHDELEKEPFEDGFANGEESTPTRDAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAGIGLS
VLVIMMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFANAVAVAMYVVGFAETVVELLKEHSI
LMIDEINDIRIIGAITVVILLGISVAGMEWEAKAQIVLLVILLLAIGDFVIGTFIPLESKKPKGFFGYKSEIFNENFGPD
FREEETFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTLVYVGIAVSVGSCVVRDATGNVNDTIVTEL
TNCTSAACKLNFDFSSCESSPCSYGLMNNFQVMSMVSGFTPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYPAFQM
FAKGYGKNNEPLRGYILTFLIALGFILIAELNVIAPIISNFFLASYALINFSVFHASLAKSPGWRPAFKYYNMWISLLGA
ILCCIVMFVINWWAALLTYVIVLGLYIYVTYKKPDVNWGSSTQALTYLNALQHSIRLSGVEDHVKNFRPQCLVMTGAPNS
RPALLHLVHDFTKNVGLMICGHVHMGPRRQAMKEMSIDQAKYQRWLIKNKMKAFYAPVHADDLREGAQYLMQAAGLGRMK
PNTLVLGFKKDWLQADMRDVDMYINLFHDAFDIQYGVVVIRLKEGLDISHLQGQEELLSSQEKSPGTKDVVVSVEYSKKS
DLDTSKPLSEKPITHKVEEEDGKTATQPLLKKESKGPIVPLNVADQKLLEASTQFQKKQGKNTIDVWWLFDDGGLTLLIP
YLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIIAFEEIIEPYRLHEDDKEQ
DIADKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGAVSSALYMAWLEALSKDLPPILLV
RGNHQSVLTFYS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-(3-methylanilino)-N-[(propan-2-yl)carbamoyl]pyridine-3-sulfonamide' A1ATU 
3 'CHLORIDE ION'                                                         CL    
4 'SODIUM ION'                                                           NA    
5 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    GLU n 
1 3    PRO n 
1 4    ARG n 
1 5    PRO n 
1 6    THR n 
1 7    ALA n 
1 8    PRO n 
1 9    SER n 
1 10   SER n 
1 11   GLY n 
1 12   ALA n 
1 13   PRO n 
1 14   GLY n 
1 15   LEU n 
1 16   ALA n 
1 17   GLY n 
1 18   VAL n 
1 19   GLY n 
1 20   GLU n 
1 21   THR n 
1 22   PRO n 
1 23   SER n 
1 24   ALA n 
1 25   ALA n 
1 26   ALA n 
1 27   LEU n 
1 28   ALA n 
1 29   ALA n 
1 30   ALA n 
1 31   ARG n 
1 32   VAL n 
1 33   GLU n 
1 34   LEU n 
1 35   PRO n 
1 36   GLY n 
1 37   THR n 
1 38   ALA n 
1 39   VAL n 
1 40   PRO n 
1 41   SER n 
1 42   VAL n 
1 43   PRO n 
1 44   GLU n 
1 45   ASP n 
1 46   ALA n 
1 47   ALA n 
1 48   PRO n 
1 49   ALA n 
1 50   SER n 
1 51   ARG n 
1 52   ASP n 
1 53   GLY n 
1 54   GLY n 
1 55   GLY n 
1 56   VAL n 
1 57   ARG n 
1 58   ASP n 
1 59   GLU n 
1 60   GLY n 
1 61   PRO n 
1 62   ALA n 
1 63   ALA n 
1 64   ALA n 
1 65   GLY n 
1 66   ASP n 
1 67   GLY n 
1 68   LEU n 
1 69   GLY n 
1 70   ARG n 
1 71   PRO n 
1 72   LEU n 
1 73   GLY n 
1 74   PRO n 
1 75   THR n 
1 76   PRO n 
1 77   SER n 
1 78   GLN n 
1 79   SER n 
1 80   ARG n 
1 81   PHE n 
1 82   GLN n 
1 83   VAL n 
1 84   ASP n 
1 85   LEU n 
1 86   VAL n 
1 87   SER n 
1 88   GLU n 
1 89   ASN n 
1 90   ALA n 
1 91   GLY n 
1 92   ARG n 
1 93   ALA n 
1 94   ALA n 
1 95   ALA n 
1 96   ALA n 
1 97   ALA n 
1 98   ALA n 
1 99   ALA n 
1 100  ALA n 
1 101  ALA n 
1 102  ALA n 
1 103  ALA n 
1 104  ALA n 
1 105  ALA n 
1 106  ALA n 
1 107  ALA n 
1 108  GLY n 
1 109  ALA n 
1 110  GLY n 
1 111  ALA n 
1 112  GLY n 
1 113  ALA n 
1 114  LYS n 
1 115  GLN n 
1 116  THR n 
1 117  PRO n 
1 118  ALA n 
1 119  ASP n 
1 120  GLY n 
1 121  GLU n 
1 122  ALA n 
1 123  SER n 
1 124  GLY n 
1 125  GLU n 
1 126  SER n 
1 127  GLU n 
1 128  PRO n 
1 129  ALA n 
1 130  LYS n 
1 131  GLY n 
1 132  SER n 
1 133  GLU n 
1 134  GLU n 
1 135  ALA n 
1 136  LYS n 
1 137  GLY n 
1 138  ARG n 
1 139  PHE n 
1 140  ARG n 
1 141  VAL n 
1 142  ASN n 
1 143  PHE n 
1 144  VAL n 
1 145  ASP n 
1 146  PRO n 
1 147  ALA n 
1 148  ALA n 
1 149  SER n 
1 150  SER n 
1 151  SER n 
1 152  ALA n 
1 153  GLU n 
1 154  ASP n 
1 155  SER n 
1 156  LEU n 
1 157  SER n 
1 158  ASP n 
1 159  ALA n 
1 160  ALA n 
1 161  GLY n 
1 162  VAL n 
1 163  GLY n 
1 164  VAL n 
1 165  ASP n 
1 166  GLY n 
1 167  PRO n 
1 168  ASN n 
1 169  VAL n 
1 170  SER n 
1 171  PHE n 
1 172  GLN n 
1 173  ASN n 
1 174  GLY n 
1 175  GLY n 
1 176  ASP n 
1 177  THR n 
1 178  VAL n 
1 179  LEU n 
1 180  SER n 
1 181  GLU n 
1 182  GLY n 
1 183  SER n 
1 184  SER n 
1 185  LEU n 
1 186  HIS n 
1 187  SER n 
1 188  GLY n 
1 189  GLY n 
1 190  GLY n 
1 191  GLY n 
1 192  GLY n 
1 193  SER n 
1 194  GLY n 
1 195  HIS n 
1 196  HIS n 
1 197  GLN n 
1 198  HIS n 
1 199  TYR n 
1 200  TYR n 
1 201  TYR n 
1 202  ASP n 
1 203  THR n 
1 204  HIS n 
1 205  THR n 
1 206  ASN n 
1 207  THR n 
1 208  TYR n 
1 209  TYR n 
1 210  LEU n 
1 211  ARG n 
1 212  THR n 
1 213  PHE n 
1 214  GLY n 
1 215  HIS n 
1 216  ASN n 
1 217  TPO n 
1 218  MET n 
1 219  ASP n 
1 220  ALA n 
1 221  VAL n 
1 222  PRO n 
1 223  ARG n 
1 224  ILE n 
1 225  ASP n 
1 226  HIS n 
1 227  TYR n 
1 228  ARG n 
1 229  HIS n 
1 230  THR n 
1 231  ALA n 
1 232  ALA n 
1 233  GLN n 
1 234  LEU n 
1 235  GLY n 
1 236  GLU n 
1 237  LYS n 
1 238  LEU n 
1 239  LEU n 
1 240  ARG n 
1 241  PRO n 
1 242  SER n 
1 243  LEU n 
1 244  ALA n 
1 245  GLU n 
1 246  LEU n 
1 247  HIS n 
1 248  ASP n 
1 249  GLU n 
1 250  LEU n 
1 251  GLU n 
1 252  LYS n 
1 253  GLU n 
1 254  PRO n 
1 255  PHE n 
1 256  GLU n 
1 257  ASP n 
1 258  GLY n 
1 259  PHE n 
1 260  ALA n 
1 261  ASN n 
1 262  GLY n 
1 263  GLU n 
1 264  GLU n 
1 265  SER n 
1 266  THR n 
1 267  PRO n 
1 268  THR n 
1 269  ARG n 
1 270  ASP n 
1 271  ALA n 
1 272  VAL n 
1 273  VAL n 
1 274  THR n 
1 275  TYR n 
1 276  THR n 
1 277  ALA n 
1 278  GLU n 
1 279  SER n 
1 280  LYS n 
1 281  GLY n 
1 282  VAL n 
1 283  VAL n 
1 284  LYS n 
1 285  PHE n 
1 286  GLY n 
1 287  TRP n 
1 288  ILE n 
1 289  LYS n 
1 290  GLY n 
1 291  VAL n 
1 292  LEU n 
1 293  VAL n 
1 294  ARG n 
1 295  CYS n 
1 296  MET n 
1 297  LEU n 
1 298  ASN n 
1 299  ILE n 
1 300  TRP n 
1 301  GLY n 
1 302  VAL n 
1 303  MET n 
1 304  LEU n 
1 305  PHE n 
1 306  ILE n 
1 307  ARG n 
1 308  LEU n 
1 309  SER n 
1 310  TRP n 
1 311  ILE n 
1 312  VAL n 
1 313  GLY n 
1 314  GLN n 
1 315  ALA n 
1 316  GLY n 
1 317  ILE n 
1 318  GLY n 
1 319  LEU n 
1 320  SER n 
1 321  VAL n 
1 322  LEU n 
1 323  VAL n 
1 324  ILE n 
1 325  MET n 
1 326  MET n 
1 327  ALA n 
1 328  THR n 
1 329  VAL n 
1 330  VAL n 
1 331  THR n 
1 332  THR n 
1 333  ILE n 
1 334  THR n 
1 335  GLY n 
1 336  LEU n 
1 337  SER n 
1 338  THR n 
1 339  SER n 
1 340  ALA n 
1 341  ILE n 
1 342  ALA n 
1 343  THR n 
1 344  ASN n 
1 345  GLY n 
1 346  PHE n 
1 347  VAL n 
1 348  ARG n 
1 349  GLY n 
1 350  GLY n 
1 351  GLY n 
1 352  ALA n 
1 353  TYR n 
1 354  TYR n 
1 355  LEU n 
1 356  ILE n 
1 357  SER n 
1 358  ARG n 
1 359  SER n 
1 360  LEU n 
1 361  GLY n 
1 362  PRO n 
1 363  GLU n 
1 364  PHE n 
1 365  GLY n 
1 366  GLY n 
1 367  ALA n 
1 368  ILE n 
1 369  GLY n 
1 370  LEU n 
1 371  ILE n 
1 372  PHE n 
1 373  ALA n 
1 374  PHE n 
1 375  ALA n 
1 376  ASN n 
1 377  ALA n 
1 378  VAL n 
1 379  ALA n 
1 380  VAL n 
1 381  ALA n 
1 382  MET n 
1 383  TYR n 
1 384  VAL n 
1 385  VAL n 
1 386  GLY n 
1 387  PHE n 
1 388  ALA n 
1 389  GLU n 
1 390  THR n 
1 391  VAL n 
1 392  VAL n 
1 393  GLU n 
1 394  LEU n 
1 395  LEU n 
1 396  LYS n 
1 397  GLU n 
1 398  HIS n 
1 399  SER n 
1 400  ILE n 
1 401  LEU n 
1 402  MET n 
1 403  ILE n 
1 404  ASP n 
1 405  GLU n 
1 406  ILE n 
1 407  ASN n 
1 408  ASP n 
1 409  ILE n 
1 410  ARG n 
1 411  ILE n 
1 412  ILE n 
1 413  GLY n 
1 414  ALA n 
1 415  ILE n 
1 416  THR n 
1 417  VAL n 
1 418  VAL n 
1 419  ILE n 
1 420  LEU n 
1 421  LEU n 
1 422  GLY n 
1 423  ILE n 
1 424  SER n 
1 425  VAL n 
1 426  ALA n 
1 427  GLY n 
1 428  MET n 
1 429  GLU n 
1 430  TRP n 
1 431  GLU n 
1 432  ALA n 
1 433  LYS n 
1 434  ALA n 
1 435  GLN n 
1 436  ILE n 
1 437  VAL n 
1 438  LEU n 
1 439  LEU n 
1 440  VAL n 
1 441  ILE n 
1 442  LEU n 
1 443  LEU n 
1 444  LEU n 
1 445  ALA n 
1 446  ILE n 
1 447  GLY n 
1 448  ASP n 
1 449  PHE n 
1 450  VAL n 
1 451  ILE n 
1 452  GLY n 
1 453  THR n 
1 454  PHE n 
1 455  ILE n 
1 456  PRO n 
1 457  LEU n 
1 458  GLU n 
1 459  SER n 
1 460  LYS n 
1 461  LYS n 
1 462  PRO n 
1 463  LYS n 
1 464  GLY n 
1 465  PHE n 
1 466  PHE n 
1 467  GLY n 
1 468  TYR n 
1 469  LYS n 
1 470  SER n 
1 471  GLU n 
1 472  ILE n 
1 473  PHE n 
1 474  ASN n 
1 475  GLU n 
1 476  ASN n 
1 477  PHE n 
1 478  GLY n 
1 479  PRO n 
1 480  ASP n 
1 481  PHE n 
1 482  ARG n 
1 483  GLU n 
1 484  GLU n 
1 485  GLU n 
1 486  THR n 
1 487  PHE n 
1 488  PHE n 
1 489  SER n 
1 490  VAL n 
1 491  PHE n 
1 492  ALA n 
1 493  ILE n 
1 494  PHE n 
1 495  PHE n 
1 496  PRO n 
1 497  ALA n 
1 498  ALA n 
1 499  THR n 
1 500  GLY n 
1 501  ILE n 
1 502  LEU n 
1 503  ALA n 
1 504  GLY n 
1 505  ALA n 
1 506  ASN n 
1 507  ILE n 
1 508  SER n 
1 509  GLY n 
1 510  ASP n 
1 511  LEU n 
1 512  ALA n 
1 513  ASP n 
1 514  PRO n 
1 515  GLN n 
1 516  SER n 
1 517  ALA n 
1 518  ILE n 
1 519  PRO n 
1 520  LYS n 
1 521  GLY n 
1 522  THR n 
1 523  LEU n 
1 524  LEU n 
1 525  ALA n 
1 526  ILE n 
1 527  LEU n 
1 528  ILE n 
1 529  THR n 
1 530  THR n 
1 531  LEU n 
1 532  VAL n 
1 533  TYR n 
1 534  VAL n 
1 535  GLY n 
1 536  ILE n 
1 537  ALA n 
1 538  VAL n 
1 539  SER n 
1 540  VAL n 
1 541  GLY n 
1 542  SER n 
1 543  CYS n 
1 544  VAL n 
1 545  VAL n 
1 546  ARG n 
1 547  ASP n 
1 548  ALA n 
1 549  THR n 
1 550  GLY n 
1 551  ASN n 
1 552  VAL n 
1 553  ASN n 
1 554  ASP n 
1 555  THR n 
1 556  ILE n 
1 557  VAL n 
1 558  THR n 
1 559  GLU n 
1 560  LEU n 
1 561  THR n 
1 562  ASN n 
1 563  CYS n 
1 564  THR n 
1 565  SER n 
1 566  ALA n 
1 567  ALA n 
1 568  CYS n 
1 569  LYS n 
1 570  LEU n 
1 571  ASN n 
1 572  PHE n 
1 573  ASP n 
1 574  PHE n 
1 575  SER n 
1 576  SER n 
1 577  CYS n 
1 578  GLU n 
1 579  SER n 
1 580  SER n 
1 581  PRO n 
1 582  CYS n 
1 583  SER n 
1 584  TYR n 
1 585  GLY n 
1 586  LEU n 
1 587  MET n 
1 588  ASN n 
1 589  ASN n 
1 590  PHE n 
1 591  GLN n 
1 592  VAL n 
1 593  MET n 
1 594  SER n 
1 595  MET n 
1 596  VAL n 
1 597  SER n 
1 598  GLY n 
1 599  PHE n 
1 600  THR n 
1 601  PRO n 
1 602  LEU n 
1 603  ILE n 
1 604  SER n 
1 605  ALA n 
1 606  GLY n 
1 607  ILE n 
1 608  PHE n 
1 609  SER n 
1 610  ALA n 
1 611  THR n 
1 612  LEU n 
1 613  SER n 
1 614  SER n 
1 615  ALA n 
1 616  LEU n 
1 617  ALA n 
1 618  SER n 
1 619  LEU n 
1 620  VAL n 
1 621  SER n 
1 622  ALA n 
1 623  PRO n 
1 624  LYS n 
1 625  ILE n 
1 626  PHE n 
1 627  GLN n 
1 628  ALA n 
1 629  LEU n 
1 630  CYS n 
1 631  LYS n 
1 632  ASP n 
1 633  ASN n 
1 634  ILE n 
1 635  TYR n 
1 636  PRO n 
1 637  ALA n 
1 638  PHE n 
1 639  GLN n 
1 640  MET n 
1 641  PHE n 
1 642  ALA n 
1 643  LYS n 
1 644  GLY n 
1 645  TYR n 
1 646  GLY n 
1 647  LYS n 
1 648  ASN n 
1 649  ASN n 
1 650  GLU n 
1 651  PRO n 
1 652  LEU n 
1 653  ARG n 
1 654  GLY n 
1 655  TYR n 
1 656  ILE n 
1 657  LEU n 
1 658  THR n 
1 659  PHE n 
1 660  LEU n 
1 661  ILE n 
1 662  ALA n 
1 663  LEU n 
1 664  GLY n 
1 665  PHE n 
1 666  ILE n 
1 667  LEU n 
1 668  ILE n 
1 669  ALA n 
1 670  GLU n 
1 671  LEU n 
1 672  ASN n 
1 673  VAL n 
1 674  ILE n 
1 675  ALA n 
1 676  PRO n 
1 677  ILE n 
1 678  ILE n 
1 679  SER n 
1 680  ASN n 
1 681  PHE n 
1 682  PHE n 
1 683  LEU n 
1 684  ALA n 
1 685  SER n 
1 686  TYR n 
1 687  ALA n 
1 688  LEU n 
1 689  ILE n 
1 690  ASN n 
1 691  PHE n 
1 692  SER n 
1 693  VAL n 
1 694  PHE n 
1 695  HIS n 
1 696  ALA n 
1 697  SER n 
1 698  LEU n 
1 699  ALA n 
1 700  LYS n 
1 701  SER n 
1 702  PRO n 
1 703  GLY n 
1 704  TRP n 
1 705  ARG n 
1 706  PRO n 
1 707  ALA n 
1 708  PHE n 
1 709  LYS n 
1 710  TYR n 
1 711  TYR n 
1 712  ASN n 
1 713  MET n 
1 714  TRP n 
1 715  ILE n 
1 716  SER n 
1 717  LEU n 
1 718  LEU n 
1 719  GLY n 
1 720  ALA n 
1 721  ILE n 
1 722  LEU n 
1 723  CYS n 
1 724  CYS n 
1 725  ILE n 
1 726  VAL n 
1 727  MET n 
1 728  PHE n 
1 729  VAL n 
1 730  ILE n 
1 731  ASN n 
1 732  TRP n 
1 733  TRP n 
1 734  ALA n 
1 735  ALA n 
1 736  LEU n 
1 737  LEU n 
1 738  THR n 
1 739  TYR n 
1 740  VAL n 
1 741  ILE n 
1 742  VAL n 
1 743  LEU n 
1 744  GLY n 
1 745  LEU n 
1 746  TYR n 
1 747  ILE n 
1 748  TYR n 
1 749  VAL n 
1 750  THR n 
1 751  TYR n 
1 752  LYS n 
1 753  LYS n 
1 754  PRO n 
1 755  ASP n 
1 756  VAL n 
1 757  ASN n 
1 758  TRP n 
1 759  GLY n 
1 760  SER n 
1 761  SER n 
1 762  THR n 
1 763  GLN n 
1 764  ALA n 
1 765  LEU n 
1 766  THR n 
1 767  TYR n 
1 768  LEU n 
1 769  ASN n 
1 770  ALA n 
1 771  LEU n 
1 772  GLN n 
1 773  HIS n 
1 774  SER n 
1 775  ILE n 
1 776  ARG n 
1 777  LEU n 
1 778  SER n 
1 779  GLY n 
1 780  VAL n 
1 781  GLU n 
1 782  ASP n 
1 783  HIS n 
1 784  VAL n 
1 785  LYS n 
1 786  ASN n 
1 787  PHE n 
1 788  ARG n 
1 789  PRO n 
1 790  GLN n 
1 791  CYS n 
1 792  LEU n 
1 793  VAL n 
1 794  MET n 
1 795  THR n 
1 796  GLY n 
1 797  ALA n 
1 798  PRO n 
1 799  ASN n 
1 800  SER n 
1 801  ARG n 
1 802  PRO n 
1 803  ALA n 
1 804  LEU n 
1 805  LEU n 
1 806  HIS n 
1 807  LEU n 
1 808  VAL n 
1 809  HIS n 
1 810  ASP n 
1 811  PHE n 
1 812  THR n 
1 813  LYS n 
1 814  ASN n 
1 815  VAL n 
1 816  GLY n 
1 817  LEU n 
1 818  MET n 
1 819  ILE n 
1 820  CYS n 
1 821  GLY n 
1 822  HIS n 
1 823  VAL n 
1 824  HIS n 
1 825  MET n 
1 826  GLY n 
1 827  PRO n 
1 828  ARG n 
1 829  ARG n 
1 830  GLN n 
1 831  ALA n 
1 832  MET n 
1 833  LYS n 
1 834  GLU n 
1 835  MET n 
1 836  SER n 
1 837  ILE n 
1 838  ASP n 
1 839  GLN n 
1 840  ALA n 
1 841  LYS n 
1 842  TYR n 
1 843  GLN n 
1 844  ARG n 
1 845  TRP n 
1 846  LEU n 
1 847  ILE n 
1 848  LYS n 
1 849  ASN n 
1 850  LYS n 
1 851  MET n 
1 852  LYS n 
1 853  ALA n 
1 854  PHE n 
1 855  TYR n 
1 856  ALA n 
1 857  PRO n 
1 858  VAL n 
1 859  HIS n 
1 860  ALA n 
1 861  ASP n 
1 862  ASP n 
1 863  LEU n 
1 864  ARG n 
1 865  GLU n 
1 866  GLY n 
1 867  ALA n 
1 868  GLN n 
1 869  TYR n 
1 870  LEU n 
1 871  MET n 
1 872  GLN n 
1 873  ALA n 
1 874  ALA n 
1 875  GLY n 
1 876  LEU n 
1 877  GLY n 
1 878  ARG n 
1 879  MET n 
1 880  LYS n 
1 881  PRO n 
1 882  ASN n 
1 883  THR n 
1 884  LEU n 
1 885  VAL n 
1 886  LEU n 
1 887  GLY n 
1 888  PHE n 
1 889  LYS n 
1 890  LYS n 
1 891  ASP n 
1 892  TRP n 
1 893  LEU n 
1 894  GLN n 
1 895  ALA n 
1 896  ASP n 
1 897  MET n 
1 898  ARG n 
1 899  ASP n 
1 900  VAL n 
1 901  ASP n 
1 902  MET n 
1 903  TYR n 
1 904  ILE n 
1 905  ASN n 
1 906  LEU n 
1 907  PHE n 
1 908  HIS n 
1 909  ASP n 
1 910  ALA n 
1 911  PHE n 
1 912  ASP n 
1 913  ILE n 
1 914  GLN n 
1 915  TYR n 
1 916  GLY n 
1 917  VAL n 
1 918  VAL n 
1 919  VAL n 
1 920  ILE n 
1 921  ARG n 
1 922  LEU n 
1 923  LYS n 
1 924  GLU n 
1 925  GLY n 
1 926  LEU n 
1 927  ASP n 
1 928  ILE n 
1 929  SER n 
1 930  HIS n 
1 931  LEU n 
1 932  GLN n 
1 933  GLY n 
1 934  GLN n 
1 935  GLU n 
1 936  GLU n 
1 937  LEU n 
1 938  LEU n 
1 939  SER n 
1 940  SER n 
1 941  GLN n 
1 942  GLU n 
1 943  LYS n 
1 944  SER n 
1 945  PRO n 
1 946  GLY n 
1 947  THR n 
1 948  LYS n 
1 949  ASP n 
1 950  VAL n 
1 951  VAL n 
1 952  VAL n 
1 953  SER n 
1 954  VAL n 
1 955  GLU n 
1 956  TYR n 
1 957  SER n 
1 958  LYS n 
1 959  LYS n 
1 960  SER n 
1 961  ASP n 
1 962  LEU n 
1 963  ASP n 
1 964  THR n 
1 965  SER n 
1 966  LYS n 
1 967  PRO n 
1 968  LEU n 
1 969  SER n 
1 970  GLU n 
1 971  LYS n 
1 972  PRO n 
1 973  ILE n 
1 974  THR n 
1 975  HIS n 
1 976  LYS n 
1 977  VAL n 
1 978  GLU n 
1 979  GLU n 
1 980  GLU n 
1 981  ASP n 
1 982  GLY n 
1 983  LYS n 
1 984  THR n 
1 985  ALA n 
1 986  THR n 
1 987  GLN n 
1 988  PRO n 
1 989  LEU n 
1 990  LEU n 
1 991  LYS n 
1 992  LYS n 
1 993  GLU n 
1 994  SER n 
1 995  LYS n 
1 996  GLY n 
1 997  PRO n 
1 998  ILE n 
1 999  VAL n 
1 1000 PRO n 
1 1001 LEU n 
1 1002 ASN n 
1 1003 VAL n 
1 1004 ALA n 
1 1005 ASP n 
1 1006 GLN n 
1 1007 LYS n 
1 1008 LEU n 
1 1009 LEU n 
1 1010 GLU n 
1 1011 ALA n 
1 1012 SER n 
1 1013 THR n 
1 1014 GLN n 
1 1015 PHE n 
1 1016 GLN n 
1 1017 LYS n 
1 1018 LYS n 
1 1019 GLN n 
1 1020 GLY n 
1 1021 LYS n 
1 1022 ASN n 
1 1023 THR n 
1 1024 ILE n 
1 1025 ASP n 
1 1026 VAL n 
1 1027 TRP n 
1 1028 TRP n 
1 1029 LEU n 
1 1030 PHE n 
1 1031 ASP n 
1 1032 ASP n 
1 1033 GLY n 
1 1034 GLY n 
1 1035 LEU n 
1 1036 THR n 
1 1037 LEU n 
1 1038 LEU n 
1 1039 ILE n 
1 1040 PRO n 
1 1041 TYR n 
1 1042 LEU n 
1 1043 LEU n 
1 1044 THR n 
1 1045 THR n 
1 1046 LYS n 
1 1047 LYS n 
1 1048 LYS n 
1 1049 TRP n 
1 1050 LYS n 
1 1051 ASP n 
1 1052 CYS n 
1 1053 LYS n 
1 1054 ILE n 
1 1055 ARG n 
1 1056 VAL n 
1 1057 PHE n 
1 1058 ILE n 
1 1059 GLY n 
1 1060 GLY n 
1 1061 LYS n 
1 1062 ILE n 
1 1063 ASN n 
1 1064 ARG n 
1 1065 ILE n 
1 1066 ASP n 
1 1067 HIS n 
1 1068 ASP n 
1 1069 ARG n 
1 1070 ARG n 
1 1071 ALA n 
1 1072 MET n 
1 1073 ALA n 
1 1074 THR n 
1 1075 LEU n 
1 1076 LEU n 
1 1077 SER n 
1 1078 LYS n 
1 1079 PHE n 
1 1080 ARG n 
1 1081 ILE n 
1 1082 ASP n 
1 1083 PHE n 
1 1084 SER n 
1 1085 ASP n 
1 1086 ILE n 
1 1087 MET n 
1 1088 VAL n 
1 1089 LEU n 
1 1090 GLY n 
1 1091 ASP n 
1 1092 ILE n 
1 1093 ASN n 
1 1094 THR n 
1 1095 LYS n 
1 1096 PRO n 
1 1097 LYS n 
1 1098 LYS n 
1 1099 GLU n 
1 1100 ASN n 
1 1101 ILE n 
1 1102 ILE n 
1 1103 ALA n 
1 1104 PHE n 
1 1105 GLU n 
1 1106 GLU n 
1 1107 ILE n 
1 1108 ILE n 
1 1109 GLU n 
1 1110 PRO n 
1 1111 TYR n 
1 1112 ARG n 
1 1113 LEU n 
1 1114 HIS n 
1 1115 GLU n 
1 1116 ASP n 
1 1117 ASP n 
1 1118 LYS n 
1 1119 GLU n 
1 1120 GLN n 
1 1121 ASP n 
1 1122 ILE n 
1 1123 ALA n 
1 1124 ASP n 
1 1125 LYS n 
1 1126 MET n 
1 1127 LYS n 
1 1128 GLU n 
1 1129 ASP n 
1 1130 GLU n 
1 1131 PRO n 
1 1132 TRP n 
1 1133 ARG n 
1 1134 ILE n 
1 1135 THR n 
1 1136 ASP n 
1 1137 ASN n 
1 1138 GLU n 
1 1139 LEU n 
1 1140 GLU n 
1 1141 LEU n 
1 1142 TYR n 
1 1143 LYS n 
1 1144 THR n 
1 1145 LYS n 
1 1146 THR n 
1 1147 TYR n 
1 1148 ARG n 
1 1149 GLN n 
1 1150 ILE n 
1 1151 ARG n 
1 1152 LEU n 
1 1153 ASN n 
1 1154 GLU n 
1 1155 LEU n 
1 1156 LEU n 
1 1157 LYS n 
1 1158 GLU n 
1 1159 HIS n 
1 1160 SER n 
1 1161 SER n 
1 1162 THR n 
1 1163 ALA n 
1 1164 ASN n 
1 1165 ILE n 
1 1166 ILE n 
1 1167 VAL n 
1 1168 MET n 
1 1169 SER n 
1 1170 LEU n 
1 1171 PRO n 
1 1172 VAL n 
1 1173 ALA n 
1 1174 ARG n 
1 1175 LYS n 
1 1176 GLY n 
1 1177 ALA n 
1 1178 VAL n 
1 1179 SER n 
1 1180 SER n 
1 1181 ALA n 
1 1182 LEU n 
1 1183 TYR n 
1 1184 MET n 
1 1185 ALA n 
1 1186 TRP n 
1 1187 LEU n 
1 1188 GLU n 
1 1189 ALA n 
1 1190 LEU n 
1 1191 SER n 
1 1192 LYS n 
1 1193 ASP n 
1 1194 LEU n 
1 1195 PRO n 
1 1196 PRO n 
1 1197 ILE n 
1 1198 LEU n 
1 1199 LEU n 
1 1200 VAL n 
1 1201 ARG n 
1 1202 GLY n 
1 1203 ASN n 
1 1204 HIS n 
1 1205 GLN n 
1 1206 SER n 
1 1207 VAL n 
1 1208 LEU n 
1 1209 THR n 
1 1210 PHE n 
1 1211 TYR n 
1 1212 SER 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                   1212 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SLC12A2, NKCC1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ATU non-polymer         . '4-(3-methylanilino)-N-[(propan-2-yl)carbamoyl]pyridine-3-sulfonamide' ?                  
'C16 H20 N4 O3 S' 348.420 
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 
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 
NA    non-polymer         . 'SODIUM ION'                                                           ?                  'Na 1' 
22.990  
PHE   'L-peptide linking' y PHENYLALANINE                                                          ?                  
'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                ?                  'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                 ?                  'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                              ?                  'C4 H9 N O3' 
119.119 
TPO   'L-peptide linking' n PHOSPHOTHREONINE                                                       PHOSPHONOTHREONINE 
'C4 H10 N O6 P'   199.099 
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    1    ?    ?   ?   A . n 
A 1 2    GLU 2    2    ?    ?   ?   A . n 
A 1 3    PRO 3    3    ?    ?   ?   A . n 
A 1 4    ARG 4    4    ?    ?   ?   A . n 
A 1 5    PRO 5    5    ?    ?   ?   A . n 
A 1 6    THR 6    6    ?    ?   ?   A . n 
A 1 7    ALA 7    7    ?    ?   ?   A . n 
A 1 8    PRO 8    8    ?    ?   ?   A . n 
A 1 9    SER 9    9    ?    ?   ?   A . n 
A 1 10   SER 10   10   ?    ?   ?   A . n 
A 1 11   GLY 11   11   ?    ?   ?   A . n 
A 1 12   ALA 12   12   ?    ?   ?   A . n 
A 1 13   PRO 13   13   ?    ?   ?   A . n 
A 1 14   GLY 14   14   ?    ?   ?   A . n 
A 1 15   LEU 15   15   ?    ?   ?   A . n 
A 1 16   ALA 16   16   ?    ?   ?   A . n 
A 1 17   GLY 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   GLY 19   19   ?    ?   ?   A . n 
A 1 20   GLU 20   20   ?    ?   ?   A . n 
A 1 21   THR 21   21   ?    ?   ?   A . n 
A 1 22   PRO 22   22   ?    ?   ?   A . n 
A 1 23   SER 23   23   ?    ?   ?   A . n 
A 1 24   ALA 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ALA 26   26   ?    ?   ?   A . n 
A 1 27   LEU 27   27   ?    ?   ?   A . n 
A 1 28   ALA 28   28   ?    ?   ?   A . n 
A 1 29   ALA 29   29   ?    ?   ?   A . n 
A 1 30   ALA 30   30   ?    ?   ?   A . n 
A 1 31   ARG 31   31   ?    ?   ?   A . n 
A 1 32   VAL 32   32   ?    ?   ?   A . n 
A 1 33   GLU 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   PRO 35   35   ?    ?   ?   A . n 
A 1 36   GLY 36   36   ?    ?   ?   A . n 
A 1 37   THR 37   37   ?    ?   ?   A . n 
A 1 38   ALA 38   38   ?    ?   ?   A . n 
A 1 39   VAL 39   39   ?    ?   ?   A . n 
A 1 40   PRO 40   40   ?    ?   ?   A . n 
A 1 41   SER 41   41   ?    ?   ?   A . n 
A 1 42   VAL 42   42   ?    ?   ?   A . n 
A 1 43   PRO 43   43   ?    ?   ?   A . n 
A 1 44   GLU 44   44   ?    ?   ?   A . n 
A 1 45   ASP 45   45   ?    ?   ?   A . n 
A 1 46   ALA 46   46   ?    ?   ?   A . n 
A 1 47   ALA 47   47   ?    ?   ?   A . n 
A 1 48   PRO 48   48   ?    ?   ?   A . n 
A 1 49   ALA 49   49   ?    ?   ?   A . n 
A 1 50   SER 50   50   ?    ?   ?   A . n 
A 1 51   ARG 51   51   ?    ?   ?   A . n 
A 1 52   ASP 52   52   ?    ?   ?   A . n 
A 1 53   GLY 53   53   ?    ?   ?   A . n 
A 1 54   GLY 54   54   ?    ?   ?   A . n 
A 1 55   GLY 55   55   ?    ?   ?   A . n 
A 1 56   VAL 56   56   ?    ?   ?   A . n 
A 1 57   ARG 57   57   ?    ?   ?   A . n 
A 1 58   ASP 58   58   ?    ?   ?   A . n 
A 1 59   GLU 59   59   ?    ?   ?   A . n 
A 1 60   GLY 60   60   ?    ?   ?   A . n 
A 1 61   PRO 61   61   ?    ?   ?   A . n 
A 1 62   ALA 62   62   ?    ?   ?   A . n 
A 1 63   ALA 63   63   ?    ?   ?   A . n 
A 1 64   ALA 64   64   ?    ?   ?   A . n 
A 1 65   GLY 65   65   ?    ?   ?   A . n 
A 1 66   ASP 66   66   ?    ?   ?   A . n 
A 1 67   GLY 67   67   ?    ?   ?   A . n 
A 1 68   LEU 68   68   ?    ?   ?   A . n 
A 1 69   GLY 69   69   ?    ?   ?   A . n 
A 1 70   ARG 70   70   ?    ?   ?   A . n 
A 1 71   PRO 71   71   ?    ?   ?   A . n 
A 1 72   LEU 72   72   ?    ?   ?   A . n 
A 1 73   GLY 73   73   ?    ?   ?   A . n 
A 1 74   PRO 74   74   ?    ?   ?   A . n 
A 1 75   THR 75   75   ?    ?   ?   A . n 
A 1 76   PRO 76   76   ?    ?   ?   A . n 
A 1 77   SER 77   77   ?    ?   ?   A . n 
A 1 78   GLN 78   78   ?    ?   ?   A . n 
A 1 79   SER 79   79   ?    ?   ?   A . n 
A 1 80   ARG 80   80   ?    ?   ?   A . n 
A 1 81   PHE 81   81   ?    ?   ?   A . n 
A 1 82   GLN 82   82   ?    ?   ?   A . n 
A 1 83   VAL 83   83   ?    ?   ?   A . n 
A 1 84   ASP 84   84   ?    ?   ?   A . n 
A 1 85   LEU 85   85   ?    ?   ?   A . n 
A 1 86   VAL 86   86   ?    ?   ?   A . n 
A 1 87   SER 87   87   ?    ?   ?   A . n 
A 1 88   GLU 88   88   ?    ?   ?   A . n 
A 1 89   ASN 89   89   ?    ?   ?   A . n 
A 1 90   ALA 90   90   ?    ?   ?   A . n 
A 1 91   GLY 91   91   ?    ?   ?   A . n 
A 1 92   ARG 92   92   ?    ?   ?   A . n 
A 1 93   ALA 93   93   ?    ?   ?   A . n 
A 1 94   ALA 94   94   ?    ?   ?   A . n 
A 1 95   ALA 95   95   ?    ?   ?   A . n 
A 1 96   ALA 96   96   ?    ?   ?   A . n 
A 1 97   ALA 97   97   ?    ?   ?   A . n 
A 1 98   ALA 98   98   ?    ?   ?   A . n 
A 1 99   ALA 99   99   ?    ?   ?   A . n 
A 1 100  ALA 100  100  ?    ?   ?   A . n 
A 1 101  ALA 101  101  ?    ?   ?   A . n 
A 1 102  ALA 102  102  ?    ?   ?   A . n 
A 1 103  ALA 103  103  ?    ?   ?   A . n 
A 1 104  ALA 104  104  ?    ?   ?   A . n 
A 1 105  ALA 105  105  ?    ?   ?   A . n 
A 1 106  ALA 106  106  ?    ?   ?   A . n 
A 1 107  ALA 107  107  ?    ?   ?   A . n 
A 1 108  GLY 108  108  ?    ?   ?   A . n 
A 1 109  ALA 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  ALA 111  111  ?    ?   ?   A . n 
A 1 112  GLY 112  112  ?    ?   ?   A . n 
A 1 113  ALA 113  113  ?    ?   ?   A . n 
A 1 114  LYS 114  114  ?    ?   ?   A . n 
A 1 115  GLN 115  115  ?    ?   ?   A . n 
A 1 116  THR 116  116  ?    ?   ?   A . n 
A 1 117  PRO 117  117  ?    ?   ?   A . n 
A 1 118  ALA 118  118  ?    ?   ?   A . n 
A 1 119  ASP 119  119  ?    ?   ?   A . n 
A 1 120  GLY 120  120  ?    ?   ?   A . n 
A 1 121  GLU 121  121  ?    ?   ?   A . n 
A 1 122  ALA 122  122  ?    ?   ?   A . n 
A 1 123  SER 123  123  ?    ?   ?   A . n 
A 1 124  GLY 124  124  ?    ?   ?   A . n 
A 1 125  GLU 125  125  ?    ?   ?   A . n 
A 1 126  SER 126  126  ?    ?   ?   A . n 
A 1 127  GLU 127  127  ?    ?   ?   A . n 
A 1 128  PRO 128  128  ?    ?   ?   A . n 
A 1 129  ALA 129  129  ?    ?   ?   A . n 
A 1 130  LYS 130  130  ?    ?   ?   A . n 
A 1 131  GLY 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  GLU 133  133  ?    ?   ?   A . n 
A 1 134  GLU 134  134  ?    ?   ?   A . n 
A 1 135  ALA 135  135  ?    ?   ?   A . n 
A 1 136  LYS 136  136  ?    ?   ?   A . n 
A 1 137  GLY 137  137  ?    ?   ?   A . n 
A 1 138  ARG 138  138  ?    ?   ?   A . n 
A 1 139  PHE 139  139  ?    ?   ?   A . n 
A 1 140  ARG 140  140  ?    ?   ?   A . n 
A 1 141  VAL 141  141  ?    ?   ?   A . n 
A 1 142  ASN 142  142  ?    ?   ?   A . n 
A 1 143  PHE 143  143  ?    ?   ?   A . n 
A 1 144  VAL 144  144  ?    ?   ?   A . n 
A 1 145  ASP 145  145  ?    ?   ?   A . n 
A 1 146  PRO 146  146  ?    ?   ?   A . n 
A 1 147  ALA 147  147  ?    ?   ?   A . n 
A 1 148  ALA 148  148  ?    ?   ?   A . n 
A 1 149  SER 149  149  ?    ?   ?   A . n 
A 1 150  SER 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  ALA 152  152  ?    ?   ?   A . n 
A 1 153  GLU 153  153  ?    ?   ?   A . n 
A 1 154  ASP 154  154  ?    ?   ?   A . n 
A 1 155  SER 155  155  ?    ?   ?   A . n 
A 1 156  LEU 156  156  ?    ?   ?   A . n 
A 1 157  SER 157  157  ?    ?   ?   A . n 
A 1 158  ASP 158  158  ?    ?   ?   A . n 
A 1 159  ALA 159  159  ?    ?   ?   A . n 
A 1 160  ALA 160  160  ?    ?   ?   A . n 
A 1 161  GLY 161  161  ?    ?   ?   A . n 
A 1 162  VAL 162  162  ?    ?   ?   A . n 
A 1 163  GLY 163  163  ?    ?   ?   A . n 
A 1 164  VAL 164  164  ?    ?   ?   A . n 
A 1 165  ASP 165  165  ?    ?   ?   A . n 
A 1 166  GLY 166  166  ?    ?   ?   A . n 
A 1 167  PRO 167  167  ?    ?   ?   A . n 
A 1 168  ASN 168  168  ?    ?   ?   A . n 
A 1 169  VAL 169  169  ?    ?   ?   A . n 
A 1 170  SER 170  170  ?    ?   ?   A . n 
A 1 171  PHE 171  171  ?    ?   ?   A . n 
A 1 172  GLN 172  172  ?    ?   ?   A . n 
A 1 173  ASN 173  173  ?    ?   ?   A . n 
A 1 174  GLY 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  THR 177  177  ?    ?   ?   A . n 
A 1 178  VAL 178  178  ?    ?   ?   A . n 
A 1 179  LEU 179  179  ?    ?   ?   A . n 
A 1 180  SER 180  180  ?    ?   ?   A . n 
A 1 181  GLU 181  181  ?    ?   ?   A . n 
A 1 182  GLY 182  182  ?    ?   ?   A . n 
A 1 183  SER 183  183  ?    ?   ?   A . n 
A 1 184  SER 184  184  ?    ?   ?   A . n 
A 1 185  LEU 185  185  ?    ?   ?   A . n 
A 1 186  HIS 186  186  ?    ?   ?   A . n 
A 1 187  SER 187  187  ?    ?   ?   A . n 
A 1 188  GLY 188  188  ?    ?   ?   A . n 
A 1 189  GLY 189  189  ?    ?   ?   A . n 
A 1 190  GLY 190  190  ?    ?   ?   A . n 
A 1 191  GLY 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  SER 193  193  ?    ?   ?   A . n 
A 1 194  GLY 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  HIS 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  HIS 198  198  ?    ?   ?   A . n 
A 1 199  TYR 199  199  ?    ?   ?   A . n 
A 1 200  TYR 200  200  ?    ?   ?   A . n 
A 1 201  TYR 201  201  ?    ?   ?   A . n 
A 1 202  ASP 202  202  ?    ?   ?   A . n 
A 1 203  THR 203  203  ?    ?   ?   A . n 
A 1 204  HIS 204  204  ?    ?   ?   A . n 
A 1 205  THR 205  205  ?    ?   ?   A . n 
A 1 206  ASN 206  206  ?    ?   ?   A . n 
A 1 207  THR 207  207  ?    ?   ?   A . n 
A 1 208  TYR 208  208  ?    ?   ?   A . n 
A 1 209  TYR 209  209  ?    ?   ?   A . n 
A 1 210  LEU 210  210  ?    ?   ?   A . n 
A 1 211  ARG 211  211  ?    ?   ?   A . n 
A 1 212  THR 212  212  ?    ?   ?   A . n 
A 1 213  PHE 213  213  ?    ?   ?   A . n 
A 1 214  GLY 214  214  ?    ?   ?   A . n 
A 1 215  HIS 215  215  ?    ?   ?   A . n 
A 1 216  ASN 216  216  ?    ?   ?   A . n 
A 1 217  TPO 217  217  217  TPO TPO A . n 
A 1 218  MET 218  218  218  MET MET A . n 
A 1 219  ASP 219  219  219  ASP ASP A . n 
A 1 220  ALA 220  220  220  ALA ALA A . n 
A 1 221  VAL 221  221  221  VAL VAL A . n 
A 1 222  PRO 222  222  222  PRO PRO A . n 
A 1 223  ARG 223  223  223  ARG ARG A . n 
A 1 224  ILE 224  224  224  ILE ILE A . n 
A 1 225  ASP 225  225  225  ASP ASP A . n 
A 1 226  HIS 226  226  226  HIS HIS A . n 
A 1 227  TYR 227  227  227  TYR TYR A . n 
A 1 228  ARG 228  228  228  ARG ARG A . n 
A 1 229  HIS 229  229  229  HIS HIS A . n 
A 1 230  THR 230  230  230  THR THR A . n 
A 1 231  ALA 231  231  231  ALA ALA A . n 
A 1 232  ALA 232  232  232  ALA ALA A . n 
A 1 233  GLN 233  233  233  GLN GLN A . n 
A 1 234  LEU 234  234  234  LEU LEU A . n 
A 1 235  GLY 235  235  235  GLY GLY A . n 
A 1 236  GLU 236  236  236  GLU GLU A . n 
A 1 237  LYS 237  237  237  LYS LYS A . n 
A 1 238  LEU 238  238  238  LEU LEU A . n 
A 1 239  LEU 239  239  239  LEU LEU A . n 
A 1 240  ARG 240  240  240  ARG ARG A . n 
A 1 241  PRO 241  241  241  PRO PRO A . n 
A 1 242  SER 242  242  242  SER SER A . n 
A 1 243  LEU 243  243  243  LEU LEU A . n 
A 1 244  ALA 244  244  244  ALA ALA A . n 
A 1 245  GLU 245  245  245  GLU GLU A . n 
A 1 246  LEU 246  246  246  LEU LEU A . n 
A 1 247  HIS 247  247  247  HIS HIS A . n 
A 1 248  ASP 248  248  248  ASP ASP A . n 
A 1 249  GLU 249  249  249  GLU GLU A . n 
A 1 250  LEU 250  250  250  LEU LEU A . n 
A 1 251  GLU 251  251  ?    ?   ?   A . n 
A 1 252  LYS 252  252  ?    ?   ?   A . n 
A 1 253  GLU 253  253  ?    ?   ?   A . n 
A 1 254  PRO 254  254  ?    ?   ?   A . n 
A 1 255  PHE 255  255  ?    ?   ?   A . n 
A 1 256  GLU 256  256  ?    ?   ?   A . n 
A 1 257  ASP 257  257  ?    ?   ?   A . n 
A 1 258  GLY 258  258  ?    ?   ?   A . n 
A 1 259  PHE 259  259  ?    ?   ?   A . n 
A 1 260  ALA 260  260  ?    ?   ?   A . n 
A 1 261  ASN 261  261  ?    ?   ?   A . n 
A 1 262  GLY 262  262  ?    ?   ?   A . n 
A 1 263  GLU 263  263  ?    ?   ?   A . n 
A 1 264  GLU 264  264  ?    ?   ?   A . n 
A 1 265  SER 265  265  ?    ?   ?   A . n 
A 1 266  THR 266  266  ?    ?   ?   A . n 
A 1 267  PRO 267  267  ?    ?   ?   A . n 
A 1 268  THR 268  268  ?    ?   ?   A . n 
A 1 269  ARG 269  269  ?    ?   ?   A . n 
A 1 270  ASP 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  VAL 272  272  ?    ?   ?   A . n 
A 1 273  VAL 273  273  ?    ?   ?   A . n 
A 1 274  THR 274  274  ?    ?   ?   A . n 
A 1 275  TYR 275  275  ?    ?   ?   A . n 
A 1 276  THR 276  276  ?    ?   ?   A . n 
A 1 277  ALA 277  277  ?    ?   ?   A . n 
A 1 278  GLU 278  278  ?    ?   ?   A . n 
A 1 279  SER 279  279  ?    ?   ?   A . n 
A 1 280  LYS 280  280  ?    ?   ?   A . n 
A 1 281  GLY 281  281  ?    ?   ?   A . n 
A 1 282  VAL 282  282  282  VAL VAL A . n 
A 1 283  VAL 283  283  283  VAL VAL A . n 
A 1 284  LYS 284  284  284  LYS LYS A . n 
A 1 285  PHE 285  285  285  PHE PHE A . n 
A 1 286  GLY 286  286  286  GLY GLY A . n 
A 1 287  TRP 287  287  287  TRP TRP A . n 
A 1 288  ILE 288  288  288  ILE ILE A . n 
A 1 289  LYS 289  289  289  LYS LYS A . n 
A 1 290  GLY 290  290  290  GLY GLY A . n 
A 1 291  VAL 291  291  291  VAL VAL A . n 
A 1 292  LEU 292  292  292  LEU LEU A . n 
A 1 293  VAL 293  293  293  VAL VAL A . n 
A 1 294  ARG 294  294  294  ARG ARG A . n 
A 1 295  CYS 295  295  295  CYS CYS A . n 
A 1 296  MET 296  296  296  MET MET A . n 
A 1 297  LEU 297  297  297  LEU LEU A . n 
A 1 298  ASN 298  298  298  ASN ASN A . n 
A 1 299  ILE 299  299  299  ILE ILE A . n 
A 1 300  TRP 300  300  300  TRP TRP A . n 
A 1 301  GLY 301  301  301  GLY GLY A . n 
A 1 302  VAL 302  302  302  VAL VAL A . n 
A 1 303  MET 303  303  303  MET MET A . n 
A 1 304  LEU 304  304  304  LEU LEU A . n 
A 1 305  PHE 305  305  305  PHE PHE A . n 
A 1 306  ILE 306  306  306  ILE ILE A . n 
A 1 307  ARG 307  307  307  ARG ARG A . n 
A 1 308  LEU 308  308  308  LEU LEU A . n 
A 1 309  SER 309  309  309  SER SER A . n 
A 1 310  TRP 310  310  310  TRP TRP A . n 
A 1 311  ILE 311  311  311  ILE ILE A . n 
A 1 312  VAL 312  312  312  VAL VAL A . n 
A 1 313  GLY 313  313  313  GLY GLY A . n 
A 1 314  GLN 314  314  314  GLN GLN A . n 
A 1 315  ALA 315  315  315  ALA ALA A . n 
A 1 316  GLY 316  316  316  GLY GLY A . n 
A 1 317  ILE 317  317  317  ILE ILE A . n 
A 1 318  GLY 318  318  318  GLY GLY A . n 
A 1 319  LEU 319  319  319  LEU LEU A . n 
A 1 320  SER 320  320  320  SER SER A . n 
A 1 321  VAL 321  321  321  VAL VAL A . n 
A 1 322  LEU 322  322  322  LEU LEU A . n 
A 1 323  VAL 323  323  323  VAL VAL A . n 
A 1 324  ILE 324  324  324  ILE ILE A . n 
A 1 325  MET 325  325  325  MET MET A . n 
A 1 326  MET 326  326  326  MET MET A . n 
A 1 327  ALA 327  327  327  ALA ALA A . n 
A 1 328  THR 328  328  328  THR THR A . n 
A 1 329  VAL 329  329  329  VAL VAL A . n 
A 1 330  VAL 330  330  330  VAL VAL A . n 
A 1 331  THR 331  331  331  THR THR A . n 
A 1 332  THR 332  332  332  THR THR A . n 
A 1 333  ILE 333  333  333  ILE ILE A . n 
A 1 334  THR 334  334  334  THR THR A . n 
A 1 335  GLY 335  335  335  GLY GLY A . n 
A 1 336  LEU 336  336  336  LEU LEU A . n 
A 1 337  SER 337  337  337  SER SER A . n 
A 1 338  THR 338  338  338  THR THR A . n 
A 1 339  SER 339  339  339  SER SER A . n 
A 1 340  ALA 340  340  340  ALA ALA A . n 
A 1 341  ILE 341  341  341  ILE ILE A . n 
A 1 342  ALA 342  342  342  ALA ALA A . n 
A 1 343  THR 343  343  343  THR THR A . n 
A 1 344  ASN 344  344  344  ASN ASN A . n 
A 1 345  GLY 345  345  345  GLY GLY A . n 
A 1 346  PHE 346  346  346  PHE PHE A . n 
A 1 347  VAL 347  347  347  VAL VAL A . n 
A 1 348  ARG 348  348  348  ARG ARG A . n 
A 1 349  GLY 349  349  349  GLY GLY A . n 
A 1 350  GLY 350  350  350  GLY GLY A . n 
A 1 351  GLY 351  351  351  GLY GLY A . n 
A 1 352  ALA 352  352  352  ALA ALA A . n 
A 1 353  TYR 353  353  353  TYR TYR A . n 
A 1 354  TYR 354  354  354  TYR TYR A . n 
A 1 355  LEU 355  355  355  LEU LEU A . n 
A 1 356  ILE 356  356  356  ILE ILE A . n 
A 1 357  SER 357  357  357  SER SER A . n 
A 1 358  ARG 358  358  358  ARG ARG A . n 
A 1 359  SER 359  359  359  SER SER A . n 
A 1 360  LEU 360  360  360  LEU LEU A . n 
A 1 361  GLY 361  361  361  GLY GLY A . n 
A 1 362  PRO 362  362  362  PRO PRO A . n 
A 1 363  GLU 363  363  363  GLU GLU A . n 
A 1 364  PHE 364  364  364  PHE PHE A . n 
A 1 365  GLY 365  365  365  GLY GLY A . n 
A 1 366  GLY 366  366  366  GLY GLY A . n 
A 1 367  ALA 367  367  367  ALA ALA A . n 
A 1 368  ILE 368  368  368  ILE ILE A . n 
A 1 369  GLY 369  369  369  GLY GLY A . n 
A 1 370  LEU 370  370  370  LEU LEU A . n 
A 1 371  ILE 371  371  371  ILE ILE A . n 
A 1 372  PHE 372  372  372  PHE PHE A . n 
A 1 373  ALA 373  373  373  ALA ALA A . n 
A 1 374  PHE 374  374  374  PHE PHE A . n 
A 1 375  ALA 375  375  375  ALA ALA A . n 
A 1 376  ASN 376  376  376  ASN ASN A . n 
A 1 377  ALA 377  377  377  ALA ALA A . n 
A 1 378  VAL 378  378  378  VAL VAL A . n 
A 1 379  ALA 379  379  379  ALA ALA A . n 
A 1 380  VAL 380  380  380  VAL VAL A . n 
A 1 381  ALA 381  381  381  ALA ALA A . n 
A 1 382  MET 382  382  382  MET MET A . n 
A 1 383  TYR 383  383  383  TYR TYR A . n 
A 1 384  VAL 384  384  384  VAL VAL A . n 
A 1 385  VAL 385  385  385  VAL VAL A . n 
A 1 386  GLY 386  386  386  GLY GLY A . n 
A 1 387  PHE 387  387  387  PHE PHE A . n 
A 1 388  ALA 388  388  388  ALA ALA A . n 
A 1 389  GLU 389  389  389  GLU GLU A . n 
A 1 390  THR 390  390  390  THR THR A . n 
A 1 391  VAL 391  391  391  VAL VAL A . n 
A 1 392  VAL 392  392  392  VAL VAL A . n 
A 1 393  GLU 393  393  393  GLU GLU A . n 
A 1 394  LEU 394  394  394  LEU LEU A . n 
A 1 395  LEU 395  395  395  LEU LEU A . n 
A 1 396  LYS 396  396  396  LYS LYS A . n 
A 1 397  GLU 397  397  397  GLU GLU A . n 
A 1 398  HIS 398  398  398  HIS HIS A . n 
A 1 399  SER 399  399  399  SER SER A . n 
A 1 400  ILE 400  400  400  ILE ILE A . n 
A 1 401  LEU 401  401  401  LEU LEU A . n 
A 1 402  MET 402  402  402  MET MET A . n 
A 1 403  ILE 403  403  403  ILE ILE A . n 
A 1 404  ASP 404  404  404  ASP ASP A . n 
A 1 405  GLU 405  405  405  GLU GLU A . n 
A 1 406  ILE 406  406  406  ILE ILE A . n 
A 1 407  ASN 407  407  407  ASN ASN A . n 
A 1 408  ASP 408  408  408  ASP ASP A . n 
A 1 409  ILE 409  409  409  ILE ILE A . n 
A 1 410  ARG 410  410  410  ARG ARG A . n 
A 1 411  ILE 411  411  411  ILE ILE A . n 
A 1 412  ILE 412  412  412  ILE ILE A . n 
A 1 413  GLY 413  413  413  GLY GLY A . n 
A 1 414  ALA 414  414  414  ALA ALA A . n 
A 1 415  ILE 415  415  415  ILE ILE A . n 
A 1 416  THR 416  416  416  THR THR A . n 
A 1 417  VAL 417  417  417  VAL VAL A . n 
A 1 418  VAL 418  418  418  VAL VAL A . n 
A 1 419  ILE 419  419  419  ILE ILE A . n 
A 1 420  LEU 420  420  420  LEU LEU A . n 
A 1 421  LEU 421  421  421  LEU LEU A . n 
A 1 422  GLY 422  422  422  GLY GLY A . n 
A 1 423  ILE 423  423  423  ILE ILE A . n 
A 1 424  SER 424  424  424  SER SER A . n 
A 1 425  VAL 425  425  425  VAL VAL A . n 
A 1 426  ALA 426  426  426  ALA ALA A . n 
A 1 427  GLY 427  427  427  GLY GLY A . n 
A 1 428  MET 428  428  428  MET MET A . n 
A 1 429  GLU 429  429  429  GLU GLU A . n 
A 1 430  TRP 430  430  430  TRP TRP A . n 
A 1 431  GLU 431  431  431  GLU GLU A . n 
A 1 432  ALA 432  432  432  ALA ALA A . n 
A 1 433  LYS 433  433  433  LYS LYS A . n 
A 1 434  ALA 434  434  434  ALA ALA A . n 
A 1 435  GLN 435  435  435  GLN GLN A . n 
A 1 436  ILE 436  436  436  ILE ILE A . n 
A 1 437  VAL 437  437  437  VAL VAL A . n 
A 1 438  LEU 438  438  438  LEU LEU A . n 
A 1 439  LEU 439  439  439  LEU LEU A . n 
A 1 440  VAL 440  440  440  VAL VAL A . n 
A 1 441  ILE 441  441  441  ILE ILE A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  LEU 443  443  443  LEU LEU A . n 
A 1 444  LEU 444  444  444  LEU LEU A . n 
A 1 445  ALA 445  445  445  ALA ALA A . n 
A 1 446  ILE 446  446  446  ILE ILE A . n 
A 1 447  GLY 447  447  447  GLY GLY A . n 
A 1 448  ASP 448  448  448  ASP ASP A . n 
A 1 449  PHE 449  449  449  PHE PHE A . n 
A 1 450  VAL 450  450  450  VAL VAL A . n 
A 1 451  ILE 451  451  451  ILE ILE A . n 
A 1 452  GLY 452  452  452  GLY GLY A . n 
A 1 453  THR 453  453  453  THR THR A . n 
A 1 454  PHE 454  454  454  PHE PHE A . n 
A 1 455  ILE 455  455  455  ILE ILE A . n 
A 1 456  PRO 456  456  456  PRO PRO A . n 
A 1 457  LEU 457  457  457  LEU LEU A . n 
A 1 458  GLU 458  458  458  GLU GLU A . n 
A 1 459  SER 459  459  459  SER SER A . n 
A 1 460  LYS 460  460  460  LYS LYS A . n 
A 1 461  LYS 461  461  461  LYS LYS A . n 
A 1 462  PRO 462  462  462  PRO PRO A . n 
A 1 463  LYS 463  463  463  LYS LYS A . n 
A 1 464  GLY 464  464  464  GLY GLY A . n 
A 1 465  PHE 465  465  465  PHE PHE A . n 
A 1 466  PHE 466  466  466  PHE PHE A . n 
A 1 467  GLY 467  467  467  GLY GLY A . n 
A 1 468  TYR 468  468  468  TYR TYR A . n 
A 1 469  LYS 469  469  469  LYS LYS A . n 
A 1 470  SER 470  470  470  SER SER A . n 
A 1 471  GLU 471  471  471  GLU GLU A . n 
A 1 472  ILE 472  472  472  ILE ILE A . n 
A 1 473  PHE 473  473  473  PHE PHE A . n 
A 1 474  ASN 474  474  474  ASN ASN A . n 
A 1 475  GLU 475  475  475  GLU GLU A . n 
A 1 476  ASN 476  476  476  ASN ASN A . n 
A 1 477  PHE 477  477  477  PHE PHE A . n 
A 1 478  GLY 478  478  478  GLY GLY A . n 
A 1 479  PRO 479  479  479  PRO PRO A . n 
A 1 480  ASP 480  480  480  ASP ASP A . n 
A 1 481  PHE 481  481  481  PHE PHE A . n 
A 1 482  ARG 482  482  482  ARG ARG A . n 
A 1 483  GLU 483  483  483  GLU GLU A . n 
A 1 484  GLU 484  484  484  GLU GLU A . n 
A 1 485  GLU 485  485  485  GLU GLU A . n 
A 1 486  THR 486  486  486  THR THR A . n 
A 1 487  PHE 487  487  487  PHE PHE A . n 
A 1 488  PHE 488  488  488  PHE PHE A . n 
A 1 489  SER 489  489  489  SER SER A . n 
A 1 490  VAL 490  490  490  VAL VAL A . n 
A 1 491  PHE 491  491  491  PHE PHE A . n 
A 1 492  ALA 492  492  492  ALA ALA A . n 
A 1 493  ILE 493  493  493  ILE ILE A . n 
A 1 494  PHE 494  494  494  PHE PHE A . n 
A 1 495  PHE 495  495  495  PHE PHE A . n 
A 1 496  PRO 496  496  496  PRO PRO A . n 
A 1 497  ALA 497  497  497  ALA ALA A . n 
A 1 498  ALA 498  498  498  ALA ALA A . n 
A 1 499  THR 499  499  499  THR THR A . n 
A 1 500  GLY 500  500  500  GLY GLY A . n 
A 1 501  ILE 501  501  501  ILE ILE A . n 
A 1 502  LEU 502  502  502  LEU LEU A . n 
A 1 503  ALA 503  503  503  ALA ALA A . n 
A 1 504  GLY 504  504  504  GLY GLY A . n 
A 1 505  ALA 505  505  505  ALA ALA A . n 
A 1 506  ASN 506  506  506  ASN ASN A . n 
A 1 507  ILE 507  507  507  ILE ILE A . n 
A 1 508  SER 508  508  508  SER SER A . n 
A 1 509  GLY 509  509  509  GLY GLY A . n 
A 1 510  ASP 510  510  510  ASP ASP A . n 
A 1 511  LEU 511  511  511  LEU LEU A . n 
A 1 512  ALA 512  512  512  ALA ALA A . n 
A 1 513  ASP 513  513  513  ASP ASP A . n 
A 1 514  PRO 514  514  514  PRO PRO A . n 
A 1 515  GLN 515  515  515  GLN GLN A . n 
A 1 516  SER 516  516  516  SER SER A . n 
A 1 517  ALA 517  517  517  ALA ALA A . n 
A 1 518  ILE 518  518  518  ILE ILE A . n 
A 1 519  PRO 519  519  519  PRO PRO A . n 
A 1 520  LYS 520  520  520  LYS LYS A . n 
A 1 521  GLY 521  521  521  GLY GLY A . n 
A 1 522  THR 522  522  522  THR THR A . n 
A 1 523  LEU 523  523  523  LEU LEU A . n 
A 1 524  LEU 524  524  524  LEU LEU A . n 
A 1 525  ALA 525  525  525  ALA ALA A . n 
A 1 526  ILE 526  526  526  ILE ILE A . n 
A 1 527  LEU 527  527  527  LEU LEU A . n 
A 1 528  ILE 528  528  528  ILE ILE A . n 
A 1 529  THR 529  529  529  THR THR A . n 
A 1 530  THR 530  530  530  THR THR A . n 
A 1 531  LEU 531  531  531  LEU LEU A . n 
A 1 532  VAL 532  532  532  VAL VAL A . n 
A 1 533  TYR 533  533  533  TYR TYR A . n 
A 1 534  VAL 534  534  534  VAL VAL A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  ILE 536  536  536  ILE ILE A . n 
A 1 537  ALA 537  537  537  ALA ALA A . n 
A 1 538  VAL 538  538  538  VAL VAL A . n 
A 1 539  SER 539  539  539  SER SER A . n 
A 1 540  VAL 540  540  540  VAL VAL A . n 
A 1 541  GLY 541  541  541  GLY GLY A . n 
A 1 542  SER 542  542  542  SER SER A . n 
A 1 543  CYS 543  543  543  CYS CYS A . n 
A 1 544  VAL 544  544  544  VAL VAL A . n 
A 1 545  VAL 545  545  545  VAL VAL A . n 
A 1 546  ARG 546  546  546  ARG ARG A . n 
A 1 547  ASP 547  547  547  ASP ASP A . n 
A 1 548  ALA 548  548  548  ALA ALA A . n 
A 1 549  THR 549  549  549  THR THR A . n 
A 1 550  GLY 550  550  550  GLY GLY A . n 
A 1 551  ASN 551  551  551  ASN ASN A . n 
A 1 552  VAL 552  552  552  VAL VAL A . n 
A 1 553  ASN 553  553  553  ASN ASN A . n 
A 1 554  ASP 554  554  554  ASP ASP A . n 
A 1 555  THR 555  555  555  THR THR A . n 
A 1 556  ILE 556  556  556  ILE ILE A . n 
A 1 557  VAL 557  557  557  VAL VAL A . n 
A 1 558  THR 558  558  558  THR THR A . n 
A 1 559  GLU 559  559  559  GLU GLU A . n 
A 1 560  LEU 560  560  560  LEU LEU A . n 
A 1 561  THR 561  561  561  THR THR A . n 
A 1 562  ASN 562  562  562  ASN ASN A . n 
A 1 563  CYS 563  563  563  CYS CYS A . n 
A 1 564  THR 564  564  564  THR THR A . n 
A 1 565  SER 565  565  565  SER SER A . n 
A 1 566  ALA 566  566  566  ALA ALA A . n 
A 1 567  ALA 567  567  567  ALA ALA A . n 
A 1 568  CYS 568  568  568  CYS CYS A . n 
A 1 569  LYS 569  569  569  LYS LYS A . n 
A 1 570  LEU 570  570  570  LEU LEU A . n 
A 1 571  ASN 571  571  571  ASN ASN A . n 
A 1 572  PHE 572  572  572  PHE PHE A . n 
A 1 573  ASP 573  573  573  ASP ASP A . n 
A 1 574  PHE 574  574  574  PHE PHE A . n 
A 1 575  SER 575  575  575  SER SER A . n 
A 1 576  SER 576  576  576  SER SER A . n 
A 1 577  CYS 577  577  577  CYS CYS A . n 
A 1 578  GLU 578  578  578  GLU GLU A . n 
A 1 579  SER 579  579  579  SER SER A . n 
A 1 580  SER 580  580  580  SER SER A . n 
A 1 581  PRO 581  581  581  PRO PRO A . n 
A 1 582  CYS 582  582  582  CYS CYS A . n 
A 1 583  SER 583  583  583  SER SER A . n 
A 1 584  TYR 584  584  584  TYR TYR A . n 
A 1 585  GLY 585  585  585  GLY GLY A . n 
A 1 586  LEU 586  586  586  LEU LEU A . n 
A 1 587  MET 587  587  587  MET MET A . n 
A 1 588  ASN 588  588  588  ASN ASN A . n 
A 1 589  ASN 589  589  589  ASN ASN A . n 
A 1 590  PHE 590  590  590  PHE PHE A . n 
A 1 591  GLN 591  591  591  GLN GLN A . n 
A 1 592  VAL 592  592  592  VAL VAL A . n 
A 1 593  MET 593  593  593  MET MET A . n 
A 1 594  SER 594  594  594  SER SER A . n 
A 1 595  MET 595  595  595  MET MET A . n 
A 1 596  VAL 596  596  596  VAL VAL A . n 
A 1 597  SER 597  597  597  SER SER A . n 
A 1 598  GLY 598  598  598  GLY GLY A . n 
A 1 599  PHE 599  599  599  PHE PHE A . n 
A 1 600  THR 600  600  600  THR THR A . n 
A 1 601  PRO 601  601  601  PRO PRO A . n 
A 1 602  LEU 602  602  602  LEU LEU A . n 
A 1 603  ILE 603  603  603  ILE ILE A . n 
A 1 604  SER 604  604  604  SER SER A . n 
A 1 605  ALA 605  605  605  ALA ALA A . n 
A 1 606  GLY 606  606  606  GLY GLY A . n 
A 1 607  ILE 607  607  607  ILE ILE A . n 
A 1 608  PHE 608  608  608  PHE PHE A . n 
A 1 609  SER 609  609  609  SER SER A . n 
A 1 610  ALA 610  610  610  ALA ALA A . n 
A 1 611  THR 611  611  611  THR THR A . n 
A 1 612  LEU 612  612  612  LEU LEU A . n 
A 1 613  SER 613  613  613  SER SER A . n 
A 1 614  SER 614  614  614  SER SER A . n 
A 1 615  ALA 615  615  615  ALA ALA A . n 
A 1 616  LEU 616  616  616  LEU LEU A . n 
A 1 617  ALA 617  617  617  ALA ALA A . n 
A 1 618  SER 618  618  618  SER SER A . n 
A 1 619  LEU 619  619  619  LEU LEU A . n 
A 1 620  VAL 620  620  620  VAL VAL A . n 
A 1 621  SER 621  621  621  SER SER A . n 
A 1 622  ALA 622  622  622  ALA ALA A . n 
A 1 623  PRO 623  623  623  PRO PRO A . n 
A 1 624  LYS 624  624  624  LYS LYS A . n 
A 1 625  ILE 625  625  625  ILE ILE A . n 
A 1 626  PHE 626  626  626  PHE PHE A . n 
A 1 627  GLN 627  627  627  GLN GLN A . n 
A 1 628  ALA 628  628  628  ALA ALA A . n 
A 1 629  LEU 629  629  629  LEU LEU A . n 
A 1 630  CYS 630  630  630  CYS CYS A . n 
A 1 631  LYS 631  631  631  LYS LYS A . n 
A 1 632  ASP 632  632  632  ASP ASP A . n 
A 1 633  ASN 633  633  633  ASN ASN A . n 
A 1 634  ILE 634  634  634  ILE ILE A . n 
A 1 635  TYR 635  635  635  TYR TYR A . n 
A 1 636  PRO 636  636  636  PRO PRO A . n 
A 1 637  ALA 637  637  637  ALA ALA A . n 
A 1 638  PHE 638  638  638  PHE PHE A . n 
A 1 639  GLN 639  639  639  GLN GLN A . n 
A 1 640  MET 640  640  640  MET MET A . n 
A 1 641  PHE 641  641  641  PHE PHE A . n 
A 1 642  ALA 642  642  642  ALA ALA A . n 
A 1 643  LYS 643  643  643  LYS LYS A . n 
A 1 644  GLY 644  644  644  GLY GLY A . n 
A 1 645  TYR 645  645  645  TYR TYR A . n 
A 1 646  GLY 646  646  646  GLY GLY A . n 
A 1 647  LYS 647  647  647  LYS LYS A . n 
A 1 648  ASN 648  648  648  ASN ASN A . n 
A 1 649  ASN 649  649  649  ASN ASN A . n 
A 1 650  GLU 650  650  650  GLU GLU A . n 
A 1 651  PRO 651  651  651  PRO PRO A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ARG 653  653  653  ARG ARG A . n 
A 1 654  GLY 654  654  654  GLY GLY A . n 
A 1 655  TYR 655  655  655  TYR TYR A . n 
A 1 656  ILE 656  656  656  ILE ILE A . n 
A 1 657  LEU 657  657  657  LEU LEU A . n 
A 1 658  THR 658  658  658  THR THR A . n 
A 1 659  PHE 659  659  659  PHE PHE A . n 
A 1 660  LEU 660  660  660  LEU LEU A . n 
A 1 661  ILE 661  661  661  ILE ILE A . n 
A 1 662  ALA 662  662  662  ALA ALA A . n 
A 1 663  LEU 663  663  663  LEU LEU A . n 
A 1 664  GLY 664  664  664  GLY GLY A . n 
A 1 665  PHE 665  665  665  PHE PHE A . n 
A 1 666  ILE 666  666  666  ILE ILE A . n 
A 1 667  LEU 667  667  667  LEU LEU A . n 
A 1 668  ILE 668  668  668  ILE ILE A . n 
A 1 669  ALA 669  669  669  ALA ALA A . n 
A 1 670  GLU 670  670  670  GLU GLU A . n 
A 1 671  LEU 671  671  671  LEU LEU A . n 
A 1 672  ASN 672  672  672  ASN ASN A . n 
A 1 673  VAL 673  673  673  VAL VAL A . n 
A 1 674  ILE 674  674  674  ILE ILE A . n 
A 1 675  ALA 675  675  675  ALA ALA A . n 
A 1 676  PRO 676  676  676  PRO PRO A . n 
A 1 677  ILE 677  677  677  ILE ILE A . n 
A 1 678  ILE 678  678  678  ILE ILE A . n 
A 1 679  SER 679  679  679  SER SER A . n 
A 1 680  ASN 680  680  680  ASN ASN A . n 
A 1 681  PHE 681  681  681  PHE PHE A . n 
A 1 682  PHE 682  682  682  PHE PHE A . n 
A 1 683  LEU 683  683  683  LEU LEU A . n 
A 1 684  ALA 684  684  684  ALA ALA A . n 
A 1 685  SER 685  685  685  SER SER A . n 
A 1 686  TYR 686  686  686  TYR TYR A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  LEU 688  688  688  LEU LEU A . n 
A 1 689  ILE 689  689  689  ILE ILE A . n 
A 1 690  ASN 690  690  690  ASN ASN A . n 
A 1 691  PHE 691  691  691  PHE PHE A . n 
A 1 692  SER 692  692  692  SER SER A . n 
A 1 693  VAL 693  693  693  VAL VAL A . n 
A 1 694  PHE 694  694  694  PHE PHE A . n 
A 1 695  HIS 695  695  695  HIS HIS A . n 
A 1 696  ALA 696  696  696  ALA ALA A . n 
A 1 697  SER 697  697  697  SER SER A . n 
A 1 698  LEU 698  698  698  LEU LEU A . n 
A 1 699  ALA 699  699  699  ALA ALA A . n 
A 1 700  LYS 700  700  700  LYS LYS A . n 
A 1 701  SER 701  701  701  SER SER A . n 
A 1 702  PRO 702  702  702  PRO PRO A . n 
A 1 703  GLY 703  703  703  GLY GLY A . n 
A 1 704  TRP 704  704  704  TRP TRP A . n 
A 1 705  ARG 705  705  705  ARG ARG A . n 
A 1 706  PRO 706  706  706  PRO PRO A . n 
A 1 707  ALA 707  707  707  ALA ALA A . n 
A 1 708  PHE 708  708  708  PHE PHE A . n 
A 1 709  LYS 709  709  709  LYS LYS A . n 
A 1 710  TYR 710  710  710  TYR TYR A . n 
A 1 711  TYR 711  711  711  TYR TYR A . n 
A 1 712  ASN 712  712  712  ASN ASN A . n 
A 1 713  MET 713  713  713  MET MET A . n 
A 1 714  TRP 714  714  714  TRP TRP A . n 
A 1 715  ILE 715  715  715  ILE ILE A . n 
A 1 716  SER 716  716  716  SER SER A . n 
A 1 717  LEU 717  717  717  LEU LEU A . n 
A 1 718  LEU 718  718  718  LEU LEU A . n 
A 1 719  GLY 719  719  719  GLY GLY A . n 
A 1 720  ALA 720  720  720  ALA ALA A . n 
A 1 721  ILE 721  721  721  ILE ILE A . n 
A 1 722  LEU 722  722  722  LEU LEU A . n 
A 1 723  CYS 723  723  723  CYS CYS A . n 
A 1 724  CYS 724  724  724  CYS CYS A . n 
A 1 725  ILE 725  725  725  ILE ILE A . n 
A 1 726  VAL 726  726  726  VAL VAL A . n 
A 1 727  MET 727  727  727  MET MET A . n 
A 1 728  PHE 728  728  728  PHE PHE A . n 
A 1 729  VAL 729  729  729  VAL VAL A . n 
A 1 730  ILE 730  730  730  ILE ILE A . n 
A 1 731  ASN 731  731  731  ASN ASN A . n 
A 1 732  TRP 732  732  732  TRP TRP A . n 
A 1 733  TRP 733  733  733  TRP TRP A . n 
A 1 734  ALA 734  734  734  ALA ALA A . n 
A 1 735  ALA 735  735  735  ALA ALA A . n 
A 1 736  LEU 736  736  736  LEU LEU A . n 
A 1 737  LEU 737  737  737  LEU LEU A . n 
A 1 738  THR 738  738  738  THR THR A . n 
A 1 739  TYR 739  739  739  TYR TYR A . n 
A 1 740  VAL 740  740  740  VAL VAL A . n 
A 1 741  ILE 741  741  741  ILE ILE A . n 
A 1 742  VAL 742  742  742  VAL VAL A . n 
A 1 743  LEU 743  743  743  LEU LEU A . n 
A 1 744  GLY 744  744  744  GLY GLY A . n 
A 1 745  LEU 745  745  745  LEU LEU A . n 
A 1 746  TYR 746  746  746  TYR TYR A . n 
A 1 747  ILE 747  747  747  ILE ILE A . n 
A 1 748  TYR 748  748  748  TYR TYR A . n 
A 1 749  VAL 749  749  749  VAL VAL A . n 
A 1 750  THR 750  750  750  THR THR A . n 
A 1 751  TYR 751  751  751  TYR TYR A . n 
A 1 752  LYS 752  752  752  LYS LYS A . n 
A 1 753  LYS 753  753  753  LYS LYS A . n 
A 1 754  PRO 754  754  754  PRO PRO A . n 
A 1 755  ASP 755  755  755  ASP ASP A . n 
A 1 756  VAL 756  756  756  VAL VAL A . n 
A 1 757  ASN 757  757  757  ASN ASN A . n 
A 1 758  TRP 758  758  758  TRP TRP A . n 
A 1 759  GLY 759  759  759  GLY GLY A . n 
A 1 760  SER 760  760  760  SER SER A . n 
A 1 761  SER 761  761  761  SER SER A . n 
A 1 762  THR 762  762  762  THR THR A . n 
A 1 763  GLN 763  763  763  GLN GLN A . n 
A 1 764  ALA 764  764  764  ALA ALA A . n 
A 1 765  LEU 765  765  765  LEU LEU A . n 
A 1 766  THR 766  766  766  THR THR A . n 
A 1 767  TYR 767  767  767  TYR TYR A . n 
A 1 768  LEU 768  768  768  LEU LEU A . n 
A 1 769  ASN 769  769  769  ASN ASN A . n 
A 1 770  ALA 770  770  770  ALA ALA A . n 
A 1 771  LEU 771  771  771  LEU LEU A . n 
A 1 772  GLN 772  772  772  GLN GLN A . n 
A 1 773  HIS 773  773  773  HIS HIS A . n 
A 1 774  SER 774  774  774  SER SER A . n 
A 1 775  ILE 775  775  775  ILE ILE A . n 
A 1 776  ARG 776  776  776  ARG ARG A . n 
A 1 777  LEU 777  777  777  LEU LEU A . n 
A 1 778  SER 778  778  778  SER SER A . n 
A 1 779  GLY 779  779  779  GLY GLY A . n 
A 1 780  VAL 780  780  780  VAL VAL A . n 
A 1 781  GLU 781  781  781  GLU GLU A . n 
A 1 782  ASP 782  782  782  ASP ASP A . n 
A 1 783  HIS 783  783  783  HIS HIS A . n 
A 1 784  VAL 784  784  784  VAL VAL A . n 
A 1 785  LYS 785  785  785  LYS LYS A . n 
A 1 786  ASN 786  786  786  ASN ASN A . n 
A 1 787  PHE 787  787  787  PHE PHE A . n 
A 1 788  ARG 788  788  788  ARG ARG A . n 
A 1 789  PRO 789  789  789  PRO PRO A . n 
A 1 790  GLN 790  790  790  GLN GLN A . n 
A 1 791  CYS 791  791  791  CYS CYS A . n 
A 1 792  LEU 792  792  792  LEU LEU A . n 
A 1 793  VAL 793  793  793  VAL VAL A . n 
A 1 794  MET 794  794  794  MET MET A . n 
A 1 795  THR 795  795  795  THR THR A . n 
A 1 796  GLY 796  796  796  GLY GLY A . n 
A 1 797  ALA 797  797  797  ALA ALA A . n 
A 1 798  PRO 798  798  798  PRO PRO A . n 
A 1 799  ASN 799  799  799  ASN ASN A . n 
A 1 800  SER 800  800  800  SER SER A . n 
A 1 801  ARG 801  801  801  ARG ARG A . n 
A 1 802  PRO 802  802  802  PRO PRO A . n 
A 1 803  ALA 803  803  803  ALA ALA A . n 
A 1 804  LEU 804  804  804  LEU LEU A . n 
A 1 805  LEU 805  805  805  LEU LEU A . n 
A 1 806  HIS 806  806  806  HIS HIS A . n 
A 1 807  LEU 807  807  807  LEU LEU A . n 
A 1 808  VAL 808  808  808  VAL VAL A . n 
A 1 809  HIS 809  809  809  HIS HIS A . n 
A 1 810  ASP 810  810  810  ASP ASP A . n 
A 1 811  PHE 811  811  811  PHE PHE A . n 
A 1 812  THR 812  812  812  THR THR A . n 
A 1 813  LYS 813  813  813  LYS LYS A . n 
A 1 814  ASN 814  814  814  ASN ASN A . n 
A 1 815  VAL 815  815  815  VAL VAL A . n 
A 1 816  GLY 816  816  816  GLY GLY A . n 
A 1 817  LEU 817  817  817  LEU LEU A . n 
A 1 818  MET 818  818  818  MET MET A . n 
A 1 819  ILE 819  819  819  ILE ILE A . n 
A 1 820  CYS 820  820  820  CYS CYS A . n 
A 1 821  GLY 821  821  821  GLY GLY A . n 
A 1 822  HIS 822  822  822  HIS HIS A . n 
A 1 823  VAL 823  823  823  VAL VAL A . n 
A 1 824  HIS 824  824  824  HIS HIS A . n 
A 1 825  MET 825  825  825  MET MET A . n 
A 1 826  GLY 826  826  826  GLY GLY A . n 
A 1 827  PRO 827  827  827  PRO PRO A . n 
A 1 828  ARG 828  828  828  ARG ARG A . n 
A 1 829  ARG 829  829  829  ARG ARG A . n 
A 1 830  GLN 830  830  830  GLN GLN A . n 
A 1 831  ALA 831  831  831  ALA ALA A . n 
A 1 832  MET 832  832  832  MET MET A . n 
A 1 833  LYS 833  833  833  LYS LYS A . n 
A 1 834  GLU 834  834  834  GLU GLU A . n 
A 1 835  MET 835  835  835  MET MET A . n 
A 1 836  SER 836  836  836  SER SER A . n 
A 1 837  ILE 837  837  837  ILE ILE A . n 
A 1 838  ASP 838  838  838  ASP ASP A . n 
A 1 839  GLN 839  839  839  GLN GLN A . n 
A 1 840  ALA 840  840  840  ALA ALA A . n 
A 1 841  LYS 841  841  841  LYS LYS A . n 
A 1 842  TYR 842  842  842  TYR TYR A . n 
A 1 843  GLN 843  843  843  GLN GLN A . n 
A 1 844  ARG 844  844  844  ARG ARG A . n 
A 1 845  TRP 845  845  845  TRP TRP A . n 
A 1 846  LEU 846  846  846  LEU LEU A . n 
A 1 847  ILE 847  847  847  ILE ILE A . n 
A 1 848  LYS 848  848  848  LYS LYS A . n 
A 1 849  ASN 849  849  849  ASN ASN A . n 
A 1 850  LYS 850  850  850  LYS LYS A . n 
A 1 851  MET 851  851  851  MET MET A . n 
A 1 852  LYS 852  852  852  LYS LYS A . n 
A 1 853  ALA 853  853  853  ALA ALA A . n 
A 1 854  PHE 854  854  854  PHE PHE A . n 
A 1 855  TYR 855  855  855  TYR TYR A . n 
A 1 856  ALA 856  856  856  ALA ALA A . n 
A 1 857  PRO 857  857  857  PRO PRO A . n 
A 1 858  VAL 858  858  858  VAL VAL A . n 
A 1 859  HIS 859  859  859  HIS HIS A . n 
A 1 860  ALA 860  860  860  ALA ALA A . n 
A 1 861  ASP 861  861  861  ASP ASP A . n 
A 1 862  ASP 862  862  862  ASP ASP A . n 
A 1 863  LEU 863  863  863  LEU LEU A . n 
A 1 864  ARG 864  864  864  ARG ARG A . n 
A 1 865  GLU 865  865  865  GLU GLU A . n 
A 1 866  GLY 866  866  866  GLY GLY A . n 
A 1 867  ALA 867  867  867  ALA ALA A . n 
A 1 868  GLN 868  868  868  GLN GLN A . n 
A 1 869  TYR 869  869  869  TYR TYR A . n 
A 1 870  LEU 870  870  870  LEU LEU A . n 
A 1 871  MET 871  871  871  MET MET A . n 
A 1 872  GLN 872  872  872  GLN GLN A . n 
A 1 873  ALA 873  873  873  ALA ALA A . n 
A 1 874  ALA 874  874  874  ALA ALA A . n 
A 1 875  GLY 875  875  875  GLY GLY A . n 
A 1 876  LEU 876  876  876  LEU LEU A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  ARG 878  878  878  ARG ARG A . n 
A 1 879  MET 879  879  879  MET MET A . n 
A 1 880  LYS 880  880  880  LYS LYS A . n 
A 1 881  PRO 881  881  881  PRO PRO A . n 
A 1 882  ASN 882  882  882  ASN ASN A . n 
A 1 883  THR 883  883  883  THR THR A . n 
A 1 884  LEU 884  884  884  LEU LEU A . n 
A 1 885  VAL 885  885  885  VAL VAL A . n 
A 1 886  LEU 886  886  886  LEU LEU A . n 
A 1 887  GLY 887  887  887  GLY GLY A . n 
A 1 888  PHE 888  888  888  PHE PHE A . n 
A 1 889  LYS 889  889  889  LYS LYS A . n 
A 1 890  LYS 890  890  890  LYS LYS A . n 
A 1 891  ASP 891  891  891  ASP ASP A . n 
A 1 892  TRP 892  892  892  TRP TRP A . n 
A 1 893  LEU 893  893  893  LEU LEU A . n 
A 1 894  GLN 894  894  894  GLN GLN A . n 
A 1 895  ALA 895  895  895  ALA ALA A . n 
A 1 896  ASP 896  896  896  ASP ASP A . n 
A 1 897  MET 897  897  897  MET MET A . n 
A 1 898  ARG 898  898  898  ARG ARG A . n 
A 1 899  ASP 899  899  899  ASP ASP A . n 
A 1 900  VAL 900  900  900  VAL VAL A . n 
A 1 901  ASP 901  901  901  ASP ASP A . n 
A 1 902  MET 902  902  902  MET MET A . n 
A 1 903  TYR 903  903  903  TYR TYR A . n 
A 1 904  ILE 904  904  904  ILE ILE A . n 
A 1 905  ASN 905  905  905  ASN ASN A . n 
A 1 906  LEU 906  906  906  LEU LEU A . n 
A 1 907  PHE 907  907  907  PHE PHE A . n 
A 1 908  HIS 908  908  908  HIS HIS A . n 
A 1 909  ASP 909  909  909  ASP ASP A . n 
A 1 910  ALA 910  910  910  ALA ALA A . n 
A 1 911  PHE 911  911  911  PHE PHE A . n 
A 1 912  ASP 912  912  912  ASP ASP A . n 
A 1 913  ILE 913  913  913  ILE ILE A . n 
A 1 914  GLN 914  914  914  GLN GLN A . n 
A 1 915  TYR 915  915  915  TYR TYR A . n 
A 1 916  GLY 916  916  916  GLY GLY A . n 
A 1 917  VAL 917  917  917  VAL VAL A . n 
A 1 918  VAL 918  918  918  VAL VAL A . n 
A 1 919  VAL 919  919  919  VAL VAL A . n 
A 1 920  ILE 920  920  920  ILE ILE A . n 
A 1 921  ARG 921  921  921  ARG ARG A . n 
A 1 922  LEU 922  922  922  LEU LEU A . n 
A 1 923  LYS 923  923  923  LYS LYS A . n 
A 1 924  GLU 924  924  924  GLU GLU A . n 
A 1 925  GLY 925  925  925  GLY GLY A . n 
A 1 926  LEU 926  926  926  LEU LEU A . n 
A 1 927  ASP 927  927  ?    ?   ?   A . n 
A 1 928  ILE 928  928  ?    ?   ?   A . n 
A 1 929  SER 929  929  ?    ?   ?   A . n 
A 1 930  HIS 930  930  ?    ?   ?   A . n 
A 1 931  LEU 931  931  ?    ?   ?   A . n 
A 1 932  GLN 932  932  ?    ?   ?   A . n 
A 1 933  GLY 933  933  ?    ?   ?   A . n 
A 1 934  GLN 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  GLU 936  936  ?    ?   ?   A . n 
A 1 937  LEU 937  937  ?    ?   ?   A . n 
A 1 938  LEU 938  938  ?    ?   ?   A . n 
A 1 939  SER 939  939  ?    ?   ?   A . n 
A 1 940  SER 940  940  ?    ?   ?   A . n 
A 1 941  GLN 941  941  ?    ?   ?   A . n 
A 1 942  GLU 942  942  ?    ?   ?   A . n 
A 1 943  LYS 943  943  ?    ?   ?   A . n 
A 1 944  SER 944  944  ?    ?   ?   A . n 
A 1 945  PRO 945  945  ?    ?   ?   A . n 
A 1 946  GLY 946  946  ?    ?   ?   A . n 
A 1 947  THR 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  ASP 949  949  ?    ?   ?   A . n 
A 1 950  VAL 950  950  ?    ?   ?   A . n 
A 1 951  VAL 951  951  ?    ?   ?   A . n 
A 1 952  VAL 952  952  ?    ?   ?   A . n 
A 1 953  SER 953  953  ?    ?   ?   A . n 
A 1 954  VAL 954  954  ?    ?   ?   A . n 
A 1 955  GLU 955  955  ?    ?   ?   A . n 
A 1 956  TYR 956  956  ?    ?   ?   A . n 
A 1 957  SER 957  957  ?    ?   ?   A . n 
A 1 958  LYS 958  958  ?    ?   ?   A . n 
A 1 959  LYS 959  959  ?    ?   ?   A . n 
A 1 960  SER 960  960  ?    ?   ?   A . n 
A 1 961  ASP 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ASP 963  963  ?    ?   ?   A . n 
A 1 964  THR 964  964  ?    ?   ?   A . n 
A 1 965  SER 965  965  ?    ?   ?   A . n 
A 1 966  LYS 966  966  ?    ?   ?   A . n 
A 1 967  PRO 967  967  ?    ?   ?   A . n 
A 1 968  LEU 968  968  ?    ?   ?   A . n 
A 1 969  SER 969  969  ?    ?   ?   A . n 
A 1 970  GLU 970  970  ?    ?   ?   A . n 
A 1 971  LYS 971  971  ?    ?   ?   A . n 
A 1 972  PRO 972  972  ?    ?   ?   A . n 
A 1 973  ILE 973  973  ?    ?   ?   A . n 
A 1 974  THR 974  974  ?    ?   ?   A . n 
A 1 975  HIS 975  975  ?    ?   ?   A . n 
A 1 976  LYS 976  976  ?    ?   ?   A . n 
A 1 977  VAL 977  977  ?    ?   ?   A . n 
A 1 978  GLU 978  978  ?    ?   ?   A . n 
A 1 979  GLU 979  979  ?    ?   ?   A . n 
A 1 980  GLU 980  980  ?    ?   ?   A . n 
A 1 981  ASP 981  981  ?    ?   ?   A . n 
A 1 982  GLY 982  982  ?    ?   ?   A . n 
A 1 983  LYS 983  983  ?    ?   ?   A . n 
A 1 984  THR 984  984  ?    ?   ?   A . n 
A 1 985  ALA 985  985  ?    ?   ?   A . n 
A 1 986  THR 986  986  ?    ?   ?   A . n 
A 1 987  GLN 987  987  ?    ?   ?   A . n 
A 1 988  PRO 988  988  ?    ?   ?   A . n 
A 1 989  LEU 989  989  ?    ?   ?   A . n 
A 1 990  LEU 990  990  ?    ?   ?   A . n 
A 1 991  LYS 991  991  ?    ?   ?   A . n 
A 1 992  LYS 992  992  ?    ?   ?   A . n 
A 1 993  GLU 993  993  ?    ?   ?   A . n 
A 1 994  SER 994  994  ?    ?   ?   A . n 
A 1 995  LYS 995  995  ?    ?   ?   A . n 
A 1 996  GLY 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ILE 998  998  ?    ?   ?   A . n 
A 1 999  VAL 999  999  ?    ?   ?   A . n 
A 1 1000 PRO 1000 1000 ?    ?   ?   A . n 
A 1 1001 LEU 1001 1001 ?    ?   ?   A . n 
A 1 1002 ASN 1002 1002 ?    ?   ?   A . n 
A 1 1003 VAL 1003 1003 ?    ?   ?   A . n 
A 1 1004 ALA 1004 1004 ?    ?   ?   A . n 
A 1 1005 ASP 1005 1005 ?    ?   ?   A . n 
A 1 1006 GLN 1006 1006 ?    ?   ?   A . n 
A 1 1007 LYS 1007 1007 ?    ?   ?   A . n 
A 1 1008 LEU 1008 1008 ?    ?   ?   A . n 
A 1 1009 LEU 1009 1009 ?    ?   ?   A . n 
A 1 1010 GLU 1010 1010 ?    ?   ?   A . n 
A 1 1011 ALA 1011 1011 ?    ?   ?   A . n 
A 1 1012 SER 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLN 1014 1014 ?    ?   ?   A . n 
A 1 1015 PHE 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLN 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 LYS 1018 1018 ?    ?   ?   A . n 
A 1 1019 GLN 1019 1019 ?    ?   ?   A . n 
A 1 1020 GLY 1020 1020 ?    ?   ?   A . n 
A 1 1021 LYS 1021 1021 ?    ?   ?   A . n 
A 1 1022 ASN 1022 1022 1022 ASN ASN A . n 
A 1 1023 THR 1023 1023 1023 THR THR A . n 
A 1 1024 ILE 1024 1024 1024 ILE ILE A . n 
A 1 1025 ASP 1025 1025 1025 ASP ASP A . n 
A 1 1026 VAL 1026 1026 1026 VAL VAL A . n 
A 1 1027 TRP 1027 1027 1027 TRP TRP A . n 
A 1 1028 TRP 1028 1028 1028 TRP TRP A . n 
A 1 1029 LEU 1029 1029 1029 LEU LEU A . n 
A 1 1030 PHE 1030 1030 1030 PHE PHE A . n 
A 1 1031 ASP 1031 1031 1031 ASP ASP A . n 
A 1 1032 ASP 1032 1032 1032 ASP ASP A . n 
A 1 1033 GLY 1033 1033 1033 GLY GLY A . n 
A 1 1034 GLY 1034 1034 1034 GLY GLY A . n 
A 1 1035 LEU 1035 1035 1035 LEU LEU A . n 
A 1 1036 THR 1036 1036 1036 THR THR A . n 
A 1 1037 LEU 1037 1037 1037 LEU LEU A . n 
A 1 1038 LEU 1038 1038 1038 LEU LEU A . n 
A 1 1039 ILE 1039 1039 1039 ILE ILE A . n 
A 1 1040 PRO 1040 1040 1040 PRO PRO A . n 
A 1 1041 TYR 1041 1041 1041 TYR TYR A . n 
A 1 1042 LEU 1042 1042 1042 LEU LEU A . n 
A 1 1043 LEU 1043 1043 1043 LEU LEU A . n 
A 1 1044 THR 1044 1044 1044 THR THR A . n 
A 1 1045 THR 1045 1045 1045 THR THR A . n 
A 1 1046 LYS 1046 1046 1046 LYS LYS A . n 
A 1 1047 LYS 1047 1047 1047 LYS LYS A . n 
A 1 1048 LYS 1048 1048 1048 LYS LYS A . n 
A 1 1049 TRP 1049 1049 1049 TRP TRP A . n 
A 1 1050 LYS 1050 1050 1050 LYS LYS A . n 
A 1 1051 ASP 1051 1051 1051 ASP ASP A . n 
A 1 1052 CYS 1052 1052 1052 CYS CYS A . n 
A 1 1053 LYS 1053 1053 1053 LYS LYS A . n 
A 1 1054 ILE 1054 1054 1054 ILE ILE A . n 
A 1 1055 ARG 1055 1055 1055 ARG ARG A . n 
A 1 1056 VAL 1056 1056 1056 VAL VAL A . n 
A 1 1057 PHE 1057 1057 1057 PHE PHE A . n 
A 1 1058 ILE 1058 1058 1058 ILE ILE A . n 
A 1 1059 GLY 1059 1059 1059 GLY GLY A . n 
A 1 1060 GLY 1060 1060 1060 GLY GLY A . n 
A 1 1061 LYS 1061 1061 1061 LYS LYS A . n 
A 1 1062 ILE 1062 1062 1062 ILE ILE A . n 
A 1 1063 ASN 1063 1063 1063 ASN ASN A . n 
A 1 1064 ARG 1064 1064 1064 ARG ARG A . n 
A 1 1065 ILE 1065 1065 1065 ILE ILE A . n 
A 1 1066 ASP 1066 1066 1066 ASP ASP A . n 
A 1 1067 HIS 1067 1067 1067 HIS HIS A . n 
A 1 1068 ASP 1068 1068 1068 ASP ASP A . n 
A 1 1069 ARG 1069 1069 1069 ARG ARG A . n 
A 1 1070 ARG 1070 1070 1070 ARG ARG A . n 
A 1 1071 ALA 1071 1071 1071 ALA ALA A . n 
A 1 1072 MET 1072 1072 1072 MET MET A . n 
A 1 1073 ALA 1073 1073 1073 ALA ALA A . n 
A 1 1074 THR 1074 1074 1074 THR THR A . n 
A 1 1075 LEU 1075 1075 1075 LEU LEU A . n 
A 1 1076 LEU 1076 1076 1076 LEU LEU A . n 
A 1 1077 SER 1077 1077 1077 SER SER A . n 
A 1 1078 LYS 1078 1078 1078 LYS LYS A . n 
A 1 1079 PHE 1079 1079 1079 PHE PHE A . n 
A 1 1080 ARG 1080 1080 1080 ARG ARG A . n 
A 1 1081 ILE 1081 1081 1081 ILE ILE A . n 
A 1 1082 ASP 1082 1082 1082 ASP ASP A . n 
A 1 1083 PHE 1083 1083 1083 PHE PHE A . n 
A 1 1084 SER 1084 1084 1084 SER SER A . n 
A 1 1085 ASP 1085 1085 1085 ASP ASP A . n 
A 1 1086 ILE 1086 1086 1086 ILE ILE A . n 
A 1 1087 MET 1087 1087 1087 MET MET A . n 
A 1 1088 VAL 1088 1088 1088 VAL VAL A . n 
A 1 1089 LEU 1089 1089 1089 LEU LEU A . n 
A 1 1090 GLY 1090 1090 1090 GLY GLY A . n 
A 1 1091 ASP 1091 1091 1091 ASP ASP A . n 
A 1 1092 ILE 1092 1092 1092 ILE ILE A . n 
A 1 1093 ASN 1093 1093 1093 ASN ASN A . n 
A 1 1094 THR 1094 1094 1094 THR THR A . n 
A 1 1095 LYS 1095 1095 1095 LYS LYS A . n 
A 1 1096 PRO 1096 1096 1096 PRO PRO A . n 
A 1 1097 LYS 1097 1097 1097 LYS LYS A . n 
A 1 1098 LYS 1098 1098 1098 LYS LYS A . n 
A 1 1099 GLU 1099 1099 1099 GLU GLU A . n 
A 1 1100 ASN 1100 1100 1100 ASN ASN A . n 
A 1 1101 ILE 1101 1101 1101 ILE ILE A . n 
A 1 1102 ILE 1102 1102 1102 ILE ILE A . n 
A 1 1103 ALA 1103 1103 1103 ALA ALA A . n 
A 1 1104 PHE 1104 1104 1104 PHE PHE A . n 
A 1 1105 GLU 1105 1105 1105 GLU GLU A . n 
A 1 1106 GLU 1106 1106 1106 GLU GLU A . n 
A 1 1107 ILE 1107 1107 1107 ILE ILE A . n 
A 1 1108 ILE 1108 1108 1108 ILE ILE A . n 
A 1 1109 GLU 1109 1109 1109 GLU GLU A . n 
A 1 1110 PRO 1110 1110 1110 PRO PRO A . n 
A 1 1111 TYR 1111 1111 1111 TYR TYR A . n 
A 1 1112 ARG 1112 1112 1112 ARG ARG A . n 
A 1 1113 LEU 1113 1113 1113 LEU LEU A . n 
A 1 1114 HIS 1114 1114 1114 HIS HIS A . n 
A 1 1115 GLU 1115 1115 1115 GLU GLU A . n 
A 1 1116 ASP 1116 1116 1116 ASP ASP A . n 
A 1 1117 ASP 1117 1117 1117 ASP ASP A . n 
A 1 1118 LYS 1118 1118 1118 LYS LYS A . n 
A 1 1119 GLU 1119 1119 1119 GLU GLU A . n 
A 1 1120 GLN 1120 1120 1120 GLN GLN A . n 
A 1 1121 ASP 1121 1121 1121 ASP ASP A . n 
A 1 1122 ILE 1122 1122 1122 ILE ILE A . n 
A 1 1123 ALA 1123 1123 1123 ALA ALA A . n 
A 1 1124 ASP 1124 1124 1124 ASP ASP A . n 
A 1 1125 LYS 1125 1125 1125 LYS LYS A . n 
A 1 1126 MET 1126 1126 1126 MET MET A . n 
A 1 1127 LYS 1127 1127 1127 LYS LYS A . n 
A 1 1128 GLU 1128 1128 1128 GLU GLU A . n 
A 1 1129 ASP 1129 1129 1129 ASP ASP A . n 
A 1 1130 GLU 1130 1130 1130 GLU ALA A . n 
A 1 1131 PRO 1131 1131 1131 PRO PRO A . n 
A 1 1132 TRP 1132 1132 1132 TRP TRP A . n 
A 1 1133 ARG 1133 1133 1133 ARG ARG A . n 
A 1 1134 ILE 1134 1134 1134 ILE ILE A . n 
A 1 1135 THR 1135 1135 1135 THR THR A . n 
A 1 1136 ASP 1136 1136 1136 ASP ASP A . n 
A 1 1137 ASN 1137 1137 1137 ASN ASN A . n 
A 1 1138 GLU 1138 1138 1138 GLU GLU A . n 
A 1 1139 LEU 1139 1139 1139 LEU LEU A . n 
A 1 1140 GLU 1140 1140 1140 GLU GLU A . n 
A 1 1141 LEU 1141 1141 1141 LEU LEU A . n 
A 1 1142 TYR 1142 1142 1142 TYR TYR A . n 
A 1 1143 LYS 1143 1143 1143 LYS LYS A . n 
A 1 1144 THR 1144 1144 1144 THR THR A . n 
A 1 1145 LYS 1145 1145 1145 LYS LYS A . n 
A 1 1146 THR 1146 1146 1146 THR THR A . n 
A 1 1147 TYR 1147 1147 1147 TYR TYR A . n 
A 1 1148 ARG 1148 1148 1148 ARG ARG A . n 
A 1 1149 GLN 1149 1149 1149 GLN GLN A . n 
A 1 1150 ILE 1150 1150 1150 ILE ILE A . n 
A 1 1151 ARG 1151 1151 1151 ARG ARG A . n 
A 1 1152 LEU 1152 1152 1152 LEU LEU A . n 
A 1 1153 ASN 1153 1153 1153 ASN ASN A . n 
A 1 1154 GLU 1154 1154 1154 GLU GLU A . n 
A 1 1155 LEU 1155 1155 1155 LEU LEU A . n 
A 1 1156 LEU 1156 1156 1156 LEU LEU A . n 
A 1 1157 LYS 1157 1157 1157 LYS LYS A . n 
A 1 1158 GLU 1158 1158 1158 GLU GLU A . n 
A 1 1159 HIS 1159 1159 1159 HIS HIS A . n 
A 1 1160 SER 1160 1160 1160 SER SER A . n 
A 1 1161 SER 1161 1161 1161 SER SER A . n 
A 1 1162 THR 1162 1162 1162 THR THR A . n 
A 1 1163 ALA 1163 1163 1163 ALA ALA A . n 
A 1 1164 ASN 1164 1164 1164 ASN ASN A . n 
A 1 1165 ILE 1165 1165 1165 ILE ILE A . n 
A 1 1166 ILE 1166 1166 1166 ILE ILE A . n 
A 1 1167 VAL 1167 1167 1167 VAL VAL A . n 
A 1 1168 MET 1168 1168 1168 MET MET A . n 
A 1 1169 SER 1169 1169 1169 SER SER A . n 
A 1 1170 LEU 1170 1170 1170 LEU LEU A . n 
A 1 1171 PRO 1171 1171 1171 PRO PRO A . n 
A 1 1172 VAL 1172 1172 1172 VAL VAL A . n 
A 1 1173 ALA 1173 1173 1173 ALA ALA A . n 
A 1 1174 ARG 1174 1174 1174 ARG ARG A . n 
A 1 1175 LYS 1175 1175 1175 LYS LYS A . n 
A 1 1176 GLY 1176 1176 1176 GLY GLY A . n 
A 1 1177 ALA 1177 1177 1177 ALA ALA A . n 
A 1 1178 VAL 1178 1178 1178 VAL VAL A . n 
A 1 1179 SER 1179 1179 1179 SER SER A . n 
A 1 1180 SER 1180 1180 1180 SER SER A . n 
A 1 1181 ALA 1181 1181 1181 ALA ALA A . n 
A 1 1182 LEU 1182 1182 1182 LEU LEU A . n 
A 1 1183 TYR 1183 1183 1183 TYR TYR A . n 
A 1 1184 MET 1184 1184 1184 MET MET A . n 
A 1 1185 ALA 1185 1185 1185 ALA ALA A . n 
A 1 1186 TRP 1186 1186 1186 TRP TRP A . n 
A 1 1187 LEU 1187 1187 1187 LEU LEU A . n 
A 1 1188 GLU 1188 1188 1188 GLU GLU A . n 
A 1 1189 ALA 1189 1189 1189 ALA ALA A . n 
A 1 1190 LEU 1190 1190 1190 LEU LEU A . n 
A 1 1191 SER 1191 1191 1191 SER SER A . n 
A 1 1192 LYS 1192 1192 1192 LYS LYS A . n 
A 1 1193 ASP 1193 1193 1193 ASP ASP A . n 
A 1 1194 LEU 1194 1194 1194 LEU LEU A . n 
A 1 1195 PRO 1195 1195 1195 PRO PRO A . n 
A 1 1196 PRO 1196 1196 1196 PRO PRO A . n 
A 1 1197 ILE 1197 1197 1197 ILE ILE A . n 
A 1 1198 LEU 1198 1198 1198 LEU LEU A . n 
A 1 1199 LEU 1199 1199 1199 LEU LEU A . n 
A 1 1200 VAL 1200 1200 1200 VAL VAL A . n 
A 1 1201 ARG 1201 1201 1201 ARG ARG A . n 
A 1 1202 GLY 1202 1202 1202 GLY GLY A . n 
A 1 1203 ASN 1203 1203 1203 ASN ASN A . n 
A 1 1204 HIS 1204 1204 1204 HIS HIS A . n 
A 1 1205 GLN 1205 1205 1205 GLN GLN A . n 
A 1 1206 SER 1206 1206 1206 SER SER A . n 
A 1 1207 VAL 1207 1207 1207 VAL VAL A . n 
A 1 1208 LEU 1208 1208 1208 LEU LEU A . n 
A 1 1209 THR 1209 1209 1209 THR THR A . n 
A 1 1210 PHE 1210 1210 1210 PHE PHE A . n 
A 1 1211 TYR 1211 1211 1211 TYR TYR A . n 
A 1 1212 SER 1212 1212 1212 SER SER A . n 
B 1 1    MET 1    1    ?    ?   ?   B . n 
B 1 2    GLU 2    2    ?    ?   ?   B . n 
B 1 3    PRO 3    3    ?    ?   ?   B . n 
B 1 4    ARG 4    4    ?    ?   ?   B . n 
B 1 5    PRO 5    5    ?    ?   ?   B . n 
B 1 6    THR 6    6    ?    ?   ?   B . n 
B 1 7    ALA 7    7    ?    ?   ?   B . n 
B 1 8    PRO 8    8    ?    ?   ?   B . n 
B 1 9    SER 9    9    ?    ?   ?   B . n 
B 1 10   SER 10   10   ?    ?   ?   B . n 
B 1 11   GLY 11   11   ?    ?   ?   B . n 
B 1 12   ALA 12   12   ?    ?   ?   B . n 
B 1 13   PRO 13   13   ?    ?   ?   B . n 
B 1 14   GLY 14   14   ?    ?   ?   B . n 
B 1 15   LEU 15   15   ?    ?   ?   B . n 
B 1 16   ALA 16   16   ?    ?   ?   B . n 
B 1 17   GLY 17   17   ?    ?   ?   B . n 
B 1 18   VAL 18   18   ?    ?   ?   B . n 
B 1 19   GLY 19   19   ?    ?   ?   B . n 
B 1 20   GLU 20   20   ?    ?   ?   B . n 
B 1 21   THR 21   21   ?    ?   ?   B . n 
B 1 22   PRO 22   22   ?    ?   ?   B . n 
B 1 23   SER 23   23   ?    ?   ?   B . n 
B 1 24   ALA 24   24   ?    ?   ?   B . n 
B 1 25   ALA 25   25   ?    ?   ?   B . n 
B 1 26   ALA 26   26   ?    ?   ?   B . n 
B 1 27   LEU 27   27   ?    ?   ?   B . n 
B 1 28   ALA 28   28   ?    ?   ?   B . n 
B 1 29   ALA 29   29   ?    ?   ?   B . n 
B 1 30   ALA 30   30   ?    ?   ?   B . n 
B 1 31   ARG 31   31   ?    ?   ?   B . n 
B 1 32   VAL 32   32   ?    ?   ?   B . n 
B 1 33   GLU 33   33   ?    ?   ?   B . n 
B 1 34   LEU 34   34   ?    ?   ?   B . n 
B 1 35   PRO 35   35   ?    ?   ?   B . n 
B 1 36   GLY 36   36   ?    ?   ?   B . n 
B 1 37   THR 37   37   ?    ?   ?   B . n 
B 1 38   ALA 38   38   ?    ?   ?   B . n 
B 1 39   VAL 39   39   ?    ?   ?   B . n 
B 1 40   PRO 40   40   ?    ?   ?   B . n 
B 1 41   SER 41   41   ?    ?   ?   B . n 
B 1 42   VAL 42   42   ?    ?   ?   B . n 
B 1 43   PRO 43   43   ?    ?   ?   B . n 
B 1 44   GLU 44   44   ?    ?   ?   B . n 
B 1 45   ASP 45   45   ?    ?   ?   B . n 
B 1 46   ALA 46   46   ?    ?   ?   B . n 
B 1 47   ALA 47   47   ?    ?   ?   B . n 
B 1 48   PRO 48   48   ?    ?   ?   B . n 
B 1 49   ALA 49   49   ?    ?   ?   B . n 
B 1 50   SER 50   50   ?    ?   ?   B . n 
B 1 51   ARG 51   51   ?    ?   ?   B . n 
B 1 52   ASP 52   52   ?    ?   ?   B . n 
B 1 53   GLY 53   53   ?    ?   ?   B . n 
B 1 54   GLY 54   54   ?    ?   ?   B . n 
B 1 55   GLY 55   55   ?    ?   ?   B . n 
B 1 56   VAL 56   56   ?    ?   ?   B . n 
B 1 57   ARG 57   57   ?    ?   ?   B . n 
B 1 58   ASP 58   58   ?    ?   ?   B . n 
B 1 59   GLU 59   59   ?    ?   ?   B . n 
B 1 60   GLY 60   60   ?    ?   ?   B . n 
B 1 61   PRO 61   61   ?    ?   ?   B . n 
B 1 62   ALA 62   62   ?    ?   ?   B . n 
B 1 63   ALA 63   63   ?    ?   ?   B . n 
B 1 64   ALA 64   64   ?    ?   ?   B . n 
B 1 65   GLY 65   65   ?    ?   ?   B . n 
B 1 66   ASP 66   66   ?    ?   ?   B . n 
B 1 67   GLY 67   67   ?    ?   ?   B . n 
B 1 68   LEU 68   68   ?    ?   ?   B . n 
B 1 69   GLY 69   69   ?    ?   ?   B . n 
B 1 70   ARG 70   70   ?    ?   ?   B . n 
B 1 71   PRO 71   71   ?    ?   ?   B . n 
B 1 72   LEU 72   72   ?    ?   ?   B . n 
B 1 73   GLY 73   73   ?    ?   ?   B . n 
B 1 74   PRO 74   74   ?    ?   ?   B . n 
B 1 75   THR 75   75   ?    ?   ?   B . n 
B 1 76   PRO 76   76   ?    ?   ?   B . n 
B 1 77   SER 77   77   ?    ?   ?   B . n 
B 1 78   GLN 78   78   ?    ?   ?   B . n 
B 1 79   SER 79   79   ?    ?   ?   B . n 
B 1 80   ARG 80   80   ?    ?   ?   B . n 
B 1 81   PHE 81   81   ?    ?   ?   B . n 
B 1 82   GLN 82   82   ?    ?   ?   B . n 
B 1 83   VAL 83   83   ?    ?   ?   B . n 
B 1 84   ASP 84   84   ?    ?   ?   B . n 
B 1 85   LEU 85   85   ?    ?   ?   B . n 
B 1 86   VAL 86   86   ?    ?   ?   B . n 
B 1 87   SER 87   87   ?    ?   ?   B . n 
B 1 88   GLU 88   88   ?    ?   ?   B . n 
B 1 89   ASN 89   89   ?    ?   ?   B . n 
B 1 90   ALA 90   90   ?    ?   ?   B . n 
B 1 91   GLY 91   91   ?    ?   ?   B . n 
B 1 92   ARG 92   92   ?    ?   ?   B . n 
B 1 93   ALA 93   93   ?    ?   ?   B . n 
B 1 94   ALA 94   94   ?    ?   ?   B . n 
B 1 95   ALA 95   95   ?    ?   ?   B . n 
B 1 96   ALA 96   96   ?    ?   ?   B . n 
B 1 97   ALA 97   97   ?    ?   ?   B . n 
B 1 98   ALA 98   98   ?    ?   ?   B . n 
B 1 99   ALA 99   99   ?    ?   ?   B . n 
B 1 100  ALA 100  100  ?    ?   ?   B . n 
B 1 101  ALA 101  101  ?    ?   ?   B . n 
B 1 102  ALA 102  102  ?    ?   ?   B . n 
B 1 103  ALA 103  103  ?    ?   ?   B . n 
B 1 104  ALA 104  104  ?    ?   ?   B . n 
B 1 105  ALA 105  105  ?    ?   ?   B . n 
B 1 106  ALA 106  106  ?    ?   ?   B . n 
B 1 107  ALA 107  107  ?    ?   ?   B . n 
B 1 108  GLY 108  108  ?    ?   ?   B . n 
B 1 109  ALA 109  109  ?    ?   ?   B . n 
B 1 110  GLY 110  110  ?    ?   ?   B . n 
B 1 111  ALA 111  111  ?    ?   ?   B . n 
B 1 112  GLY 112  112  ?    ?   ?   B . n 
B 1 113  ALA 113  113  ?    ?   ?   B . n 
B 1 114  LYS 114  114  ?    ?   ?   B . n 
B 1 115  GLN 115  115  ?    ?   ?   B . n 
B 1 116  THR 116  116  ?    ?   ?   B . n 
B 1 117  PRO 117  117  ?    ?   ?   B . n 
B 1 118  ALA 118  118  ?    ?   ?   B . n 
B 1 119  ASP 119  119  ?    ?   ?   B . n 
B 1 120  GLY 120  120  ?    ?   ?   B . n 
B 1 121  GLU 121  121  ?    ?   ?   B . n 
B 1 122  ALA 122  122  ?    ?   ?   B . n 
B 1 123  SER 123  123  ?    ?   ?   B . n 
B 1 124  GLY 124  124  ?    ?   ?   B . n 
B 1 125  GLU 125  125  ?    ?   ?   B . n 
B 1 126  SER 126  126  ?    ?   ?   B . n 
B 1 127  GLU 127  127  ?    ?   ?   B . n 
B 1 128  PRO 128  128  ?    ?   ?   B . n 
B 1 129  ALA 129  129  ?    ?   ?   B . n 
B 1 130  LYS 130  130  ?    ?   ?   B . n 
B 1 131  GLY 131  131  ?    ?   ?   B . n 
B 1 132  SER 132  132  ?    ?   ?   B . n 
B 1 133  GLU 133  133  ?    ?   ?   B . n 
B 1 134  GLU 134  134  ?    ?   ?   B . n 
B 1 135  ALA 135  135  ?    ?   ?   B . n 
B 1 136  LYS 136  136  ?    ?   ?   B . n 
B 1 137  GLY 137  137  ?    ?   ?   B . n 
B 1 138  ARG 138  138  ?    ?   ?   B . n 
B 1 139  PHE 139  139  ?    ?   ?   B . n 
B 1 140  ARG 140  140  ?    ?   ?   B . n 
B 1 141  VAL 141  141  ?    ?   ?   B . n 
B 1 142  ASN 142  142  ?    ?   ?   B . n 
B 1 143  PHE 143  143  ?    ?   ?   B . n 
B 1 144  VAL 144  144  ?    ?   ?   B . n 
B 1 145  ASP 145  145  ?    ?   ?   B . n 
B 1 146  PRO 146  146  ?    ?   ?   B . n 
B 1 147  ALA 147  147  ?    ?   ?   B . n 
B 1 148  ALA 148  148  ?    ?   ?   B . n 
B 1 149  SER 149  149  ?    ?   ?   B . n 
B 1 150  SER 150  150  ?    ?   ?   B . n 
B 1 151  SER 151  151  ?    ?   ?   B . n 
B 1 152  ALA 152  152  ?    ?   ?   B . n 
B 1 153  GLU 153  153  ?    ?   ?   B . n 
B 1 154  ASP 154  154  ?    ?   ?   B . n 
B 1 155  SER 155  155  ?    ?   ?   B . n 
B 1 156  LEU 156  156  ?    ?   ?   B . n 
B 1 157  SER 157  157  ?    ?   ?   B . n 
B 1 158  ASP 158  158  ?    ?   ?   B . n 
B 1 159  ALA 159  159  ?    ?   ?   B . n 
B 1 160  ALA 160  160  ?    ?   ?   B . n 
B 1 161  GLY 161  161  ?    ?   ?   B . n 
B 1 162  VAL 162  162  ?    ?   ?   B . n 
B 1 163  GLY 163  163  ?    ?   ?   B . n 
B 1 164  VAL 164  164  ?    ?   ?   B . n 
B 1 165  ASP 165  165  ?    ?   ?   B . n 
B 1 166  GLY 166  166  ?    ?   ?   B . n 
B 1 167  PRO 167  167  ?    ?   ?   B . n 
B 1 168  ASN 168  168  ?    ?   ?   B . n 
B 1 169  VAL 169  169  ?    ?   ?   B . n 
B 1 170  SER 170  170  ?    ?   ?   B . n 
B 1 171  PHE 171  171  ?    ?   ?   B . n 
B 1 172  GLN 172  172  ?    ?   ?   B . n 
B 1 173  ASN 173  173  ?    ?   ?   B . n 
B 1 174  GLY 174  174  ?    ?   ?   B . n 
B 1 175  GLY 175  175  ?    ?   ?   B . n 
B 1 176  ASP 176  176  ?    ?   ?   B . n 
B 1 177  THR 177  177  ?    ?   ?   B . n 
B 1 178  VAL 178  178  ?    ?   ?   B . n 
B 1 179  LEU 179  179  ?    ?   ?   B . n 
B 1 180  SER 180  180  ?    ?   ?   B . n 
B 1 181  GLU 181  181  ?    ?   ?   B . n 
B 1 182  GLY 182  182  ?    ?   ?   B . n 
B 1 183  SER 183  183  ?    ?   ?   B . n 
B 1 184  SER 184  184  ?    ?   ?   B . n 
B 1 185  LEU 185  185  ?    ?   ?   B . n 
B 1 186  HIS 186  186  ?    ?   ?   B . n 
B 1 187  SER 187  187  ?    ?   ?   B . n 
B 1 188  GLY 188  188  ?    ?   ?   B . n 
B 1 189  GLY 189  189  ?    ?   ?   B . n 
B 1 190  GLY 190  190  ?    ?   ?   B . n 
B 1 191  GLY 191  191  ?    ?   ?   B . n 
B 1 192  GLY 192  192  ?    ?   ?   B . n 
B 1 193  SER 193  193  ?    ?   ?   B . n 
B 1 194  GLY 194  194  ?    ?   ?   B . n 
B 1 195  HIS 195  195  ?    ?   ?   B . n 
B 1 196  HIS 196  196  ?    ?   ?   B . n 
B 1 197  GLN 197  197  ?    ?   ?   B . n 
B 1 198  HIS 198  198  ?    ?   ?   B . n 
B 1 199  TYR 199  199  ?    ?   ?   B . n 
B 1 200  TYR 200  200  ?    ?   ?   B . n 
B 1 201  TYR 201  201  ?    ?   ?   B . n 
B 1 202  ASP 202  202  ?    ?   ?   B . n 
B 1 203  THR 203  203  ?    ?   ?   B . n 
B 1 204  HIS 204  204  ?    ?   ?   B . n 
B 1 205  THR 205  205  ?    ?   ?   B . n 
B 1 206  ASN 206  206  ?    ?   ?   B . n 
B 1 207  THR 207  207  ?    ?   ?   B . n 
B 1 208  TYR 208  208  ?    ?   ?   B . n 
B 1 209  TYR 209  209  ?    ?   ?   B . n 
B 1 210  LEU 210  210  ?    ?   ?   B . n 
B 1 211  ARG 211  211  ?    ?   ?   B . n 
B 1 212  THR 212  212  ?    ?   ?   B . n 
B 1 213  PHE 213  213  ?    ?   ?   B . n 
B 1 214  GLY 214  214  ?    ?   ?   B . n 
B 1 215  HIS 215  215  ?    ?   ?   B . n 
B 1 216  ASN 216  216  ?    ?   ?   B . n 
B 1 217  TPO 217  217  217  TPO TPO B . n 
B 1 218  MET 218  218  218  MET MET B . n 
B 1 219  ASP 219  219  219  ASP ASP B . n 
B 1 220  ALA 220  220  220  ALA ALA B . n 
B 1 221  VAL 221  221  221  VAL VAL B . n 
B 1 222  PRO 222  222  222  PRO PRO B . n 
B 1 223  ARG 223  223  223  ARG ARG B . n 
B 1 224  ILE 224  224  224  ILE ILE B . n 
B 1 225  ASP 225  225  225  ASP ASP B . n 
B 1 226  HIS 226  226  226  HIS HIS B . n 
B 1 227  TYR 227  227  227  TYR TYR B . n 
B 1 228  ARG 228  228  228  ARG ARG B . n 
B 1 229  HIS 229  229  229  HIS HIS B . n 
B 1 230  THR 230  230  230  THR THR B . n 
B 1 231  ALA 231  231  231  ALA ALA B . n 
B 1 232  ALA 232  232  232  ALA ALA B . n 
B 1 233  GLN 233  233  233  GLN GLN B . n 
B 1 234  LEU 234  234  234  LEU LEU B . n 
B 1 235  GLY 235  235  235  GLY GLY B . n 
B 1 236  GLU 236  236  236  GLU GLU B . n 
B 1 237  LYS 237  237  237  LYS LYS B . n 
B 1 238  LEU 238  238  238  LEU LEU B . n 
B 1 239  LEU 239  239  239  LEU LEU B . n 
B 1 240  ARG 240  240  240  ARG ARG B . n 
B 1 241  PRO 241  241  241  PRO PRO B . n 
B 1 242  SER 242  242  242  SER SER B . n 
B 1 243  LEU 243  243  243  LEU LEU B . n 
B 1 244  ALA 244  244  244  ALA ALA B . n 
B 1 245  GLU 245  245  245  GLU GLU B . n 
B 1 246  LEU 246  246  246  LEU LEU B . n 
B 1 247  HIS 247  247  247  HIS HIS B . n 
B 1 248  ASP 248  248  248  ASP ASP B . n 
B 1 249  GLU 249  249  249  GLU GLU B . n 
B 1 250  LEU 250  250  250  LEU LEU B . n 
B 1 251  GLU 251  251  ?    ?   ?   B . n 
B 1 252  LYS 252  252  ?    ?   ?   B . n 
B 1 253  GLU 253  253  ?    ?   ?   B . n 
B 1 254  PRO 254  254  ?    ?   ?   B . n 
B 1 255  PHE 255  255  ?    ?   ?   B . n 
B 1 256  GLU 256  256  ?    ?   ?   B . n 
B 1 257  ASP 257  257  ?    ?   ?   B . n 
B 1 258  GLY 258  258  ?    ?   ?   B . n 
B 1 259  PHE 259  259  ?    ?   ?   B . n 
B 1 260  ALA 260  260  ?    ?   ?   B . n 
B 1 261  ASN 261  261  ?    ?   ?   B . n 
B 1 262  GLY 262  262  ?    ?   ?   B . n 
B 1 263  GLU 263  263  ?    ?   ?   B . n 
B 1 264  GLU 264  264  ?    ?   ?   B . n 
B 1 265  SER 265  265  ?    ?   ?   B . n 
B 1 266  THR 266  266  ?    ?   ?   B . n 
B 1 267  PRO 267  267  ?    ?   ?   B . n 
B 1 268  THR 268  268  ?    ?   ?   B . n 
B 1 269  ARG 269  269  ?    ?   ?   B . n 
B 1 270  ASP 270  270  ?    ?   ?   B . n 
B 1 271  ALA 271  271  ?    ?   ?   B . n 
B 1 272  VAL 272  272  ?    ?   ?   B . n 
B 1 273  VAL 273  273  ?    ?   ?   B . n 
B 1 274  THR 274  274  ?    ?   ?   B . n 
B 1 275  TYR 275  275  ?    ?   ?   B . n 
B 1 276  THR 276  276  ?    ?   ?   B . n 
B 1 277  ALA 277  277  ?    ?   ?   B . n 
B 1 278  GLU 278  278  ?    ?   ?   B . n 
B 1 279  SER 279  279  ?    ?   ?   B . n 
B 1 280  LYS 280  280  ?    ?   ?   B . n 
B 1 281  GLY 281  281  ?    ?   ?   B . n 
B 1 282  VAL 282  282  282  VAL VAL B . n 
B 1 283  VAL 283  283  283  VAL VAL B . n 
B 1 284  LYS 284  284  284  LYS LYS B . n 
B 1 285  PHE 285  285  285  PHE PHE B . n 
B 1 286  GLY 286  286  286  GLY GLY B . n 
B 1 287  TRP 287  287  287  TRP TRP B . n 
B 1 288  ILE 288  288  288  ILE ILE B . n 
B 1 289  LYS 289  289  289  LYS LYS B . n 
B 1 290  GLY 290  290  290  GLY GLY B . n 
B 1 291  VAL 291  291  291  VAL VAL B . n 
B 1 292  LEU 292  292  292  LEU LEU B . n 
B 1 293  VAL 293  293  293  VAL VAL B . n 
B 1 294  ARG 294  294  294  ARG ARG B . n 
B 1 295  CYS 295  295  295  CYS CYS B . n 
B 1 296  MET 296  296  296  MET MET B . n 
B 1 297  LEU 297  297  297  LEU LEU B . n 
B 1 298  ASN 298  298  298  ASN ASN B . n 
B 1 299  ILE 299  299  299  ILE ILE B . n 
B 1 300  TRP 300  300  300  TRP TRP B . n 
B 1 301  GLY 301  301  301  GLY GLY B . n 
B 1 302  VAL 302  302  302  VAL VAL B . n 
B 1 303  MET 303  303  303  MET MET B . n 
B 1 304  LEU 304  304  304  LEU LEU B . n 
B 1 305  PHE 305  305  305  PHE PHE B . n 
B 1 306  ILE 306  306  306  ILE ILE B . n 
B 1 307  ARG 307  307  307  ARG ARG B . n 
B 1 308  LEU 308  308  308  LEU LEU B . n 
B 1 309  SER 309  309  309  SER SER B . n 
B 1 310  TRP 310  310  310  TRP TRP B . n 
B 1 311  ILE 311  311  311  ILE ILE B . n 
B 1 312  VAL 312  312  312  VAL VAL B . n 
B 1 313  GLY 313  313  313  GLY GLY B . n 
B 1 314  GLN 314  314  314  GLN GLN B . n 
B 1 315  ALA 315  315  315  ALA ALA B . n 
B 1 316  GLY 316  316  316  GLY GLY B . n 
B 1 317  ILE 317  317  317  ILE ILE B . n 
B 1 318  GLY 318  318  318  GLY GLY B . n 
B 1 319  LEU 319  319  319  LEU LEU B . n 
B 1 320  SER 320  320  320  SER SER B . n 
B 1 321  VAL 321  321  321  VAL VAL B . n 
B 1 322  LEU 322  322  322  LEU LEU B . n 
B 1 323  VAL 323  323  323  VAL VAL B . n 
B 1 324  ILE 324  324  324  ILE ILE B . n 
B 1 325  MET 325  325  325  MET MET B . n 
B 1 326  MET 326  326  326  MET MET B . n 
B 1 327  ALA 327  327  327  ALA ALA B . n 
B 1 328  THR 328  328  328  THR THR B . n 
B 1 329  VAL 329  329  329  VAL VAL B . n 
B 1 330  VAL 330  330  330  VAL VAL B . n 
B 1 331  THR 331  331  331  THR THR B . n 
B 1 332  THR 332  332  332  THR THR B . n 
B 1 333  ILE 333  333  333  ILE ILE B . n 
B 1 334  THR 334  334  334  THR THR B . n 
B 1 335  GLY 335  335  335  GLY GLY B . n 
B 1 336  LEU 336  336  336  LEU LEU B . n 
B 1 337  SER 337  337  337  SER SER B . n 
B 1 338  THR 338  338  338  THR THR B . n 
B 1 339  SER 339  339  339  SER SER B . n 
B 1 340  ALA 340  340  340  ALA ALA B . n 
B 1 341  ILE 341  341  341  ILE ILE B . n 
B 1 342  ALA 342  342  342  ALA ALA B . n 
B 1 343  THR 343  343  343  THR THR B . n 
B 1 344  ASN 344  344  344  ASN ASN B . n 
B 1 345  GLY 345  345  345  GLY GLY B . n 
B 1 346  PHE 346  346  346  PHE PHE B . n 
B 1 347  VAL 347  347  347  VAL VAL B . n 
B 1 348  ARG 348  348  348  ARG ARG B . n 
B 1 349  GLY 349  349  349  GLY GLY B . n 
B 1 350  GLY 350  350  350  GLY GLY B . n 
B 1 351  GLY 351  351  351  GLY GLY B . n 
B 1 352  ALA 352  352  352  ALA ALA B . n 
B 1 353  TYR 353  353  353  TYR TYR B . n 
B 1 354  TYR 354  354  354  TYR TYR B . n 
B 1 355  LEU 355  355  355  LEU LEU B . n 
B 1 356  ILE 356  356  356  ILE ILE B . n 
B 1 357  SER 357  357  357  SER SER B . n 
B 1 358  ARG 358  358  358  ARG ARG B . n 
B 1 359  SER 359  359  359  SER SER B . n 
B 1 360  LEU 360  360  360  LEU LEU B . n 
B 1 361  GLY 361  361  361  GLY GLY B . n 
B 1 362  PRO 362  362  362  PRO PRO B . n 
B 1 363  GLU 363  363  363  GLU GLU B . n 
B 1 364  PHE 364  364  364  PHE PHE B . n 
B 1 365  GLY 365  365  365  GLY GLY B . n 
B 1 366  GLY 366  366  366  GLY GLY B . n 
B 1 367  ALA 367  367  367  ALA ALA B . n 
B 1 368  ILE 368  368  368  ILE ILE B . n 
B 1 369  GLY 369  369  369  GLY GLY B . n 
B 1 370  LEU 370  370  370  LEU LEU B . n 
B 1 371  ILE 371  371  371  ILE ILE B . n 
B 1 372  PHE 372  372  372  PHE PHE B . n 
B 1 373  ALA 373  373  373  ALA ALA B . n 
B 1 374  PHE 374  374  374  PHE PHE B . n 
B 1 375  ALA 375  375  375  ALA ALA B . n 
B 1 376  ASN 376  376  376  ASN ASN B . n 
B 1 377  ALA 377  377  377  ALA ALA B . n 
B 1 378  VAL 378  378  378  VAL VAL B . n 
B 1 379  ALA 379  379  379  ALA ALA B . n 
B 1 380  VAL 380  380  380  VAL VAL B . n 
B 1 381  ALA 381  381  381  ALA ALA B . n 
B 1 382  MET 382  382  382  MET MET B . n 
B 1 383  TYR 383  383  383  TYR TYR B . n 
B 1 384  VAL 384  384  384  VAL VAL B . n 
B 1 385  VAL 385  385  385  VAL VAL B . n 
B 1 386  GLY 386  386  386  GLY GLY B . n 
B 1 387  PHE 387  387  387  PHE PHE B . n 
B 1 388  ALA 388  388  388  ALA ALA B . n 
B 1 389  GLU 389  389  389  GLU GLU B . n 
B 1 390  THR 390  390  390  THR THR B . n 
B 1 391  VAL 391  391  391  VAL VAL B . n 
B 1 392  VAL 392  392  392  VAL VAL B . n 
B 1 393  GLU 393  393  393  GLU GLU B . n 
B 1 394  LEU 394  394  394  LEU LEU B . n 
B 1 395  LEU 395  395  395  LEU LEU B . n 
B 1 396  LYS 396  396  396  LYS LYS B . n 
B 1 397  GLU 397  397  397  GLU GLU B . n 
B 1 398  HIS 398  398  398  HIS HIS B . n 
B 1 399  SER 399  399  399  SER SER B . n 
B 1 400  ILE 400  400  400  ILE ILE B . n 
B 1 401  LEU 401  401  401  LEU LEU B . n 
B 1 402  MET 402  402  402  MET MET B . n 
B 1 403  ILE 403  403  403  ILE ILE B . n 
B 1 404  ASP 404  404  404  ASP ASP B . n 
B 1 405  GLU 405  405  405  GLU GLU B . n 
B 1 406  ILE 406  406  406  ILE ILE B . n 
B 1 407  ASN 407  407  407  ASN ASN B . n 
B 1 408  ASP 408  408  408  ASP ASP B . n 
B 1 409  ILE 409  409  409  ILE ILE B . n 
B 1 410  ARG 410  410  410  ARG ARG B . n 
B 1 411  ILE 411  411  411  ILE ILE B . n 
B 1 412  ILE 412  412  412  ILE ILE B . n 
B 1 413  GLY 413  413  413  GLY GLY B . n 
B 1 414  ALA 414  414  414  ALA ALA B . n 
B 1 415  ILE 415  415  415  ILE ILE B . n 
B 1 416  THR 416  416  416  THR THR B . n 
B 1 417  VAL 417  417  417  VAL VAL B . n 
B 1 418  VAL 418  418  418  VAL VAL B . n 
B 1 419  ILE 419  419  419  ILE ILE B . n 
B 1 420  LEU 420  420  420  LEU LEU B . n 
B 1 421  LEU 421  421  421  LEU LEU B . n 
B 1 422  GLY 422  422  422  GLY GLY B . n 
B 1 423  ILE 423  423  423  ILE ILE B . n 
B 1 424  SER 424  424  424  SER SER B . n 
B 1 425  VAL 425  425  425  VAL VAL B . n 
B 1 426  ALA 426  426  426  ALA ALA B . n 
B 1 427  GLY 427  427  427  GLY GLY B . n 
B 1 428  MET 428  428  428  MET MET B . n 
B 1 429  GLU 429  429  429  GLU GLU B . n 
B 1 430  TRP 430  430  430  TRP TRP B . n 
B 1 431  GLU 431  431  431  GLU GLU B . n 
B 1 432  ALA 432  432  432  ALA ALA B . n 
B 1 433  LYS 433  433  433  LYS LYS B . n 
B 1 434  ALA 434  434  434  ALA ALA B . n 
B 1 435  GLN 435  435  435  GLN GLN B . n 
B 1 436  ILE 436  436  436  ILE ILE B . n 
B 1 437  VAL 437  437  437  VAL VAL B . n 
B 1 438  LEU 438  438  438  LEU LEU B . n 
B 1 439  LEU 439  439  439  LEU LEU B . n 
B 1 440  VAL 440  440  440  VAL VAL B . n 
B 1 441  ILE 441  441  441  ILE ILE B . n 
B 1 442  LEU 442  442  442  LEU LEU B . n 
B 1 443  LEU 443  443  443  LEU LEU B . n 
B 1 444  LEU 444  444  444  LEU LEU B . n 
B 1 445  ALA 445  445  445  ALA ALA B . n 
B 1 446  ILE 446  446  446  ILE ILE B . n 
B 1 447  GLY 447  447  447  GLY GLY B . n 
B 1 448  ASP 448  448  448  ASP ASP B . n 
B 1 449  PHE 449  449  449  PHE PHE B . n 
B 1 450  VAL 450  450  450  VAL VAL B . n 
B 1 451  ILE 451  451  451  ILE ILE B . n 
B 1 452  GLY 452  452  452  GLY GLY B . n 
B 1 453  THR 453  453  453  THR THR B . n 
B 1 454  PHE 454  454  454  PHE PHE B . n 
B 1 455  ILE 455  455  455  ILE ILE B . n 
B 1 456  PRO 456  456  456  PRO PRO B . n 
B 1 457  LEU 457  457  457  LEU LEU B . n 
B 1 458  GLU 458  458  458  GLU GLU B . n 
B 1 459  SER 459  459  459  SER SER B . n 
B 1 460  LYS 460  460  460  LYS LYS B . n 
B 1 461  LYS 461  461  461  LYS LYS B . n 
B 1 462  PRO 462  462  462  PRO PRO B . n 
B 1 463  LYS 463  463  463  LYS LYS B . n 
B 1 464  GLY 464  464  464  GLY GLY B . n 
B 1 465  PHE 465  465  465  PHE PHE B . n 
B 1 466  PHE 466  466  466  PHE PHE B . n 
B 1 467  GLY 467  467  467  GLY GLY B . n 
B 1 468  TYR 468  468  468  TYR TYR B . n 
B 1 469  LYS 469  469  469  LYS LYS B . n 
B 1 470  SER 470  470  470  SER SER B . n 
B 1 471  GLU 471  471  471  GLU GLU B . n 
B 1 472  ILE 472  472  472  ILE ILE B . n 
B 1 473  PHE 473  473  473  PHE PHE B . n 
B 1 474  ASN 474  474  474  ASN ASN B . n 
B 1 475  GLU 475  475  475  GLU GLU B . n 
B 1 476  ASN 476  476  476  ASN ASN B . n 
B 1 477  PHE 477  477  477  PHE PHE B . n 
B 1 478  GLY 478  478  478  GLY GLY B . n 
B 1 479  PRO 479  479  479  PRO PRO B . n 
B 1 480  ASP 480  480  480  ASP ASP B . n 
B 1 481  PHE 481  481  481  PHE PHE B . n 
B 1 482  ARG 482  482  482  ARG ARG B . n 
B 1 483  GLU 483  483  483  GLU GLU B . n 
B 1 484  GLU 484  484  484  GLU GLU B . n 
B 1 485  GLU 485  485  485  GLU GLU B . n 
B 1 486  THR 486  486  486  THR THR B . n 
B 1 487  PHE 487  487  487  PHE PHE B . n 
B 1 488  PHE 488  488  488  PHE PHE B . n 
B 1 489  SER 489  489  489  SER SER B . n 
B 1 490  VAL 490  490  490  VAL VAL B . n 
B 1 491  PHE 491  491  491  PHE PHE B . n 
B 1 492  ALA 492  492  492  ALA ALA B . n 
B 1 493  ILE 493  493  493  ILE ILE B . n 
B 1 494  PHE 494  494  494  PHE PHE B . n 
B 1 495  PHE 495  495  495  PHE PHE B . n 
B 1 496  PRO 496  496  496  PRO PRO B . n 
B 1 497  ALA 497  497  497  ALA ALA B . n 
B 1 498  ALA 498  498  498  ALA ALA B . n 
B 1 499  THR 499  499  499  THR THR B . n 
B 1 500  GLY 500  500  500  GLY GLY B . n 
B 1 501  ILE 501  501  501  ILE ILE B . n 
B 1 502  LEU 502  502  502  LEU LEU B . n 
B 1 503  ALA 503  503  503  ALA ALA B . n 
B 1 504  GLY 504  504  504  GLY GLY B . n 
B 1 505  ALA 505  505  505  ALA ALA B . n 
B 1 506  ASN 506  506  506  ASN ASN B . n 
B 1 507  ILE 507  507  507  ILE ILE B . n 
B 1 508  SER 508  508  508  SER SER B . n 
B 1 509  GLY 509  509  509  GLY GLY B . n 
B 1 510  ASP 510  510  510  ASP ASP B . n 
B 1 511  LEU 511  511  511  LEU LEU B . n 
B 1 512  ALA 512  512  512  ALA ALA B . n 
B 1 513  ASP 513  513  513  ASP ASP B . n 
B 1 514  PRO 514  514  514  PRO PRO B . n 
B 1 515  GLN 515  515  515  GLN GLN B . n 
B 1 516  SER 516  516  516  SER SER B . n 
B 1 517  ALA 517  517  517  ALA ALA B . n 
B 1 518  ILE 518  518  518  ILE ILE B . n 
B 1 519  PRO 519  519  519  PRO PRO B . n 
B 1 520  LYS 520  520  520  LYS LYS B . n 
B 1 521  GLY 521  521  521  GLY GLY B . n 
B 1 522  THR 522  522  522  THR THR B . n 
B 1 523  LEU 523  523  523  LEU LEU B . n 
B 1 524  LEU 524  524  524  LEU LEU B . n 
B 1 525  ALA 525  525  525  ALA ALA B . n 
B 1 526  ILE 526  526  526  ILE ILE B . n 
B 1 527  LEU 527  527  527  LEU LEU B . n 
B 1 528  ILE 528  528  528  ILE ILE B . n 
B 1 529  THR 529  529  529  THR THR B . n 
B 1 530  THR 530  530  530  THR THR B . n 
B 1 531  LEU 531  531  531  LEU LEU B . n 
B 1 532  VAL 532  532  532  VAL VAL B . n 
B 1 533  TYR 533  533  533  TYR TYR B . n 
B 1 534  VAL 534  534  534  VAL VAL B . n 
B 1 535  GLY 535  535  535  GLY GLY B . n 
B 1 536  ILE 536  536  536  ILE ILE B . n 
B 1 537  ALA 537  537  537  ALA ALA B . n 
B 1 538  VAL 538  538  538  VAL VAL B . n 
B 1 539  SER 539  539  539  SER SER B . n 
B 1 540  VAL 540  540  540  VAL VAL B . n 
B 1 541  GLY 541  541  541  GLY GLY B . n 
B 1 542  SER 542  542  542  SER SER B . n 
B 1 543  CYS 543  543  543  CYS CYS B . n 
B 1 544  VAL 544  544  544  VAL VAL B . n 
B 1 545  VAL 545  545  545  VAL VAL B . n 
B 1 546  ARG 546  546  546  ARG ARG B . n 
B 1 547  ASP 547  547  547  ASP ASP B . n 
B 1 548  ALA 548  548  548  ALA ALA B . n 
B 1 549  THR 549  549  549  THR THR B . n 
B 1 550  GLY 550  550  550  GLY GLY B . n 
B 1 551  ASN 551  551  551  ASN ASN B . n 
B 1 552  VAL 552  552  552  VAL VAL B . n 
B 1 553  ASN 553  553  553  ASN ASN B . n 
B 1 554  ASP 554  554  554  ASP ASP B . n 
B 1 555  THR 555  555  555  THR THR B . n 
B 1 556  ILE 556  556  556  ILE ILE B . n 
B 1 557  VAL 557  557  557  VAL VAL B . n 
B 1 558  THR 558  558  558  THR THR B . n 
B 1 559  GLU 559  559  559  GLU GLU B . n 
B 1 560  LEU 560  560  560  LEU LEU B . n 
B 1 561  THR 561  561  561  THR THR B . n 
B 1 562  ASN 562  562  562  ASN ASN B . n 
B 1 563  CYS 563  563  563  CYS CYS B . n 
B 1 564  THR 564  564  564  THR THR B . n 
B 1 565  SER 565  565  565  SER SER B . n 
B 1 566  ALA 566  566  566  ALA ALA B . n 
B 1 567  ALA 567  567  567  ALA ALA B . n 
B 1 568  CYS 568  568  568  CYS CYS B . n 
B 1 569  LYS 569  569  569  LYS LYS B . n 
B 1 570  LEU 570  570  570  LEU LEU B . n 
B 1 571  ASN 571  571  571  ASN ASN B . n 
B 1 572  PHE 572  572  572  PHE PHE B . n 
B 1 573  ASP 573  573  573  ASP ASP B . n 
B 1 574  PHE 574  574  574  PHE PHE B . n 
B 1 575  SER 575  575  575  SER SER B . n 
B 1 576  SER 576  576  576  SER SER B . n 
B 1 577  CYS 577  577  577  CYS CYS B . n 
B 1 578  GLU 578  578  578  GLU GLU B . n 
B 1 579  SER 579  579  579  SER SER B . n 
B 1 580  SER 580  580  580  SER SER B . n 
B 1 581  PRO 581  581  581  PRO PRO B . n 
B 1 582  CYS 582  582  582  CYS CYS B . n 
B 1 583  SER 583  583  583  SER SER B . n 
B 1 584  TYR 584  584  584  TYR TYR B . n 
B 1 585  GLY 585  585  585  GLY GLY B . n 
B 1 586  LEU 586  586  586  LEU LEU B . n 
B 1 587  MET 587  587  587  MET MET B . n 
B 1 588  ASN 588  588  588  ASN ASN B . n 
B 1 589  ASN 589  589  589  ASN ASN B . n 
B 1 590  PHE 590  590  590  PHE PHE B . n 
B 1 591  GLN 591  591  591  GLN GLN B . n 
B 1 592  VAL 592  592  592  VAL VAL B . n 
B 1 593  MET 593  593  593  MET MET B . n 
B 1 594  SER 594  594  594  SER SER B . n 
B 1 595  MET 595  595  595  MET MET B . n 
B 1 596  VAL 596  596  596  VAL VAL B . n 
B 1 597  SER 597  597  597  SER SER B . n 
B 1 598  GLY 598  598  598  GLY GLY B . n 
B 1 599  PHE 599  599  599  PHE PHE B . n 
B 1 600  THR 600  600  600  THR THR B . n 
B 1 601  PRO 601  601  601  PRO PRO B . n 
B 1 602  LEU 602  602  602  LEU LEU B . n 
B 1 603  ILE 603  603  603  ILE ILE B . n 
B 1 604  SER 604  604  604  SER SER B . n 
B 1 605  ALA 605  605  605  ALA ALA B . n 
B 1 606  GLY 606  606  606  GLY GLY B . n 
B 1 607  ILE 607  607  607  ILE ILE B . n 
B 1 608  PHE 608  608  608  PHE PHE B . n 
B 1 609  SER 609  609  609  SER SER B . n 
B 1 610  ALA 610  610  610  ALA ALA B . n 
B 1 611  THR 611  611  611  THR THR B . n 
B 1 612  LEU 612  612  612  LEU LEU B . n 
B 1 613  SER 613  613  613  SER SER B . n 
B 1 614  SER 614  614  614  SER SER B . n 
B 1 615  ALA 615  615  615  ALA ALA B . n 
B 1 616  LEU 616  616  616  LEU LEU B . n 
B 1 617  ALA 617  617  617  ALA ALA B . n 
B 1 618  SER 618  618  618  SER SER B . n 
B 1 619  LEU 619  619  619  LEU LEU B . n 
B 1 620  VAL 620  620  620  VAL VAL B . n 
B 1 621  SER 621  621  621  SER SER B . n 
B 1 622  ALA 622  622  622  ALA ALA B . n 
B 1 623  PRO 623  623  623  PRO PRO B . n 
B 1 624  LYS 624  624  624  LYS LYS B . n 
B 1 625  ILE 625  625  625  ILE ILE B . n 
B 1 626  PHE 626  626  626  PHE PHE B . n 
B 1 627  GLN 627  627  627  GLN GLN B . n 
B 1 628  ALA 628  628  628  ALA ALA B . n 
B 1 629  LEU 629  629  629  LEU LEU B . n 
B 1 630  CYS 630  630  630  CYS CYS B . n 
B 1 631  LYS 631  631  631  LYS LYS B . n 
B 1 632  ASP 632  632  632  ASP ASP B . n 
B 1 633  ASN 633  633  633  ASN ASN B . n 
B 1 634  ILE 634  634  634  ILE ILE B . n 
B 1 635  TYR 635  635  635  TYR TYR B . n 
B 1 636  PRO 636  636  636  PRO PRO B . n 
B 1 637  ALA 637  637  637  ALA ALA B . n 
B 1 638  PHE 638  638  638  PHE PHE B . n 
B 1 639  GLN 639  639  639  GLN GLN B . n 
B 1 640  MET 640  640  640  MET MET B . n 
B 1 641  PHE 641  641  641  PHE PHE B . n 
B 1 642  ALA 642  642  642  ALA ALA B . n 
B 1 643  LYS 643  643  643  LYS LYS B . n 
B 1 644  GLY 644  644  644  GLY GLY B . n 
B 1 645  TYR 645  645  645  TYR TYR B . n 
B 1 646  GLY 646  646  646  GLY GLY B . n 
B 1 647  LYS 647  647  647  LYS LYS B . n 
B 1 648  ASN 648  648  648  ASN ASN B . n 
B 1 649  ASN 649  649  649  ASN ASN B . n 
B 1 650  GLU 650  650  650  GLU GLU B . n 
B 1 651  PRO 651  651  651  PRO PRO B . n 
B 1 652  LEU 652  652  652  LEU LEU B . n 
B 1 653  ARG 653  653  653  ARG ARG B . n 
B 1 654  GLY 654  654  654  GLY GLY B . n 
B 1 655  TYR 655  655  655  TYR TYR B . n 
B 1 656  ILE 656  656  656  ILE ILE B . n 
B 1 657  LEU 657  657  657  LEU LEU B . n 
B 1 658  THR 658  658  658  THR THR B . n 
B 1 659  PHE 659  659  659  PHE PHE B . n 
B 1 660  LEU 660  660  660  LEU LEU B . n 
B 1 661  ILE 661  661  661  ILE ILE B . n 
B 1 662  ALA 662  662  662  ALA ALA B . n 
B 1 663  LEU 663  663  663  LEU LEU B . n 
B 1 664  GLY 664  664  664  GLY GLY B . n 
B 1 665  PHE 665  665  665  PHE PHE B . n 
B 1 666  ILE 666  666  666  ILE ILE B . n 
B 1 667  LEU 667  667  667  LEU LEU B . n 
B 1 668  ILE 668  668  668  ILE ILE B . n 
B 1 669  ALA 669  669  669  ALA ALA B . n 
B 1 670  GLU 670  670  670  GLU GLU B . n 
B 1 671  LEU 671  671  671  LEU LEU B . n 
B 1 672  ASN 672  672  672  ASN ASN B . n 
B 1 673  VAL 673  673  673  VAL VAL B . n 
B 1 674  ILE 674  674  674  ILE ILE B . n 
B 1 675  ALA 675  675  675  ALA ALA B . n 
B 1 676  PRO 676  676  676  PRO PRO B . n 
B 1 677  ILE 677  677  677  ILE ILE B . n 
B 1 678  ILE 678  678  678  ILE ILE B . n 
B 1 679  SER 679  679  679  SER SER B . n 
B 1 680  ASN 680  680  680  ASN ASN B . n 
B 1 681  PHE 681  681  681  PHE PHE B . n 
B 1 682  PHE 682  682  682  PHE PHE B . n 
B 1 683  LEU 683  683  683  LEU LEU B . n 
B 1 684  ALA 684  684  684  ALA ALA B . n 
B 1 685  SER 685  685  685  SER SER B . n 
B 1 686  TYR 686  686  686  TYR TYR B . n 
B 1 687  ALA 687  687  687  ALA ALA B . n 
B 1 688  LEU 688  688  688  LEU LEU B . n 
B 1 689  ILE 689  689  689  ILE ILE B . n 
B 1 690  ASN 690  690  690  ASN ASN B . n 
B 1 691  PHE 691  691  691  PHE PHE B . n 
B 1 692  SER 692  692  692  SER SER B . n 
B 1 693  VAL 693  693  693  VAL VAL B . n 
B 1 694  PHE 694  694  694  PHE PHE B . n 
B 1 695  HIS 695  695  695  HIS HIS B . n 
B 1 696  ALA 696  696  696  ALA ALA B . n 
B 1 697  SER 697  697  697  SER SER B . n 
B 1 698  LEU 698  698  698  LEU LEU B . n 
B 1 699  ALA 699  699  699  ALA ALA B . n 
B 1 700  LYS 700  700  700  LYS LYS B . n 
B 1 701  SER 701  701  701  SER SER B . n 
B 1 702  PRO 702  702  702  PRO PRO B . n 
B 1 703  GLY 703  703  703  GLY GLY B . n 
B 1 704  TRP 704  704  704  TRP TRP B . n 
B 1 705  ARG 705  705  705  ARG ARG B . n 
B 1 706  PRO 706  706  706  PRO PRO B . n 
B 1 707  ALA 707  707  707  ALA ALA B . n 
B 1 708  PHE 708  708  708  PHE PHE B . n 
B 1 709  LYS 709  709  709  LYS LYS B . n 
B 1 710  TYR 710  710  710  TYR TYR B . n 
B 1 711  TYR 711  711  711  TYR TYR B . n 
B 1 712  ASN 712  712  712  ASN ASN B . n 
B 1 713  MET 713  713  713  MET MET B . n 
B 1 714  TRP 714  714  714  TRP TRP B . n 
B 1 715  ILE 715  715  715  ILE ILE B . n 
B 1 716  SER 716  716  716  SER SER B . n 
B 1 717  LEU 717  717  717  LEU LEU B . n 
B 1 718  LEU 718  718  718  LEU LEU B . n 
B 1 719  GLY 719  719  719  GLY GLY B . n 
B 1 720  ALA 720  720  720  ALA ALA B . n 
B 1 721  ILE 721  721  721  ILE ILE B . n 
B 1 722  LEU 722  722  722  LEU LEU B . n 
B 1 723  CYS 723  723  723  CYS CYS B . n 
B 1 724  CYS 724  724  724  CYS CYS B . n 
B 1 725  ILE 725  725  725  ILE ILE B . n 
B 1 726  VAL 726  726  726  VAL VAL B . n 
B 1 727  MET 727  727  727  MET MET B . n 
B 1 728  PHE 728  728  728  PHE PHE B . n 
B 1 729  VAL 729  729  729  VAL VAL B . n 
B 1 730  ILE 730  730  730  ILE ILE B . n 
B 1 731  ASN 731  731  731  ASN ASN B . n 
B 1 732  TRP 732  732  732  TRP TRP B . n 
B 1 733  TRP 733  733  733  TRP TRP B . n 
B 1 734  ALA 734  734  734  ALA ALA B . n 
B 1 735  ALA 735  735  735  ALA ALA B . n 
B 1 736  LEU 736  736  736  LEU LEU B . n 
B 1 737  LEU 737  737  737  LEU LEU B . n 
B 1 738  THR 738  738  738  THR THR B . n 
B 1 739  TYR 739  739  739  TYR TYR B . n 
B 1 740  VAL 740  740  740  VAL VAL B . n 
B 1 741  ILE 741  741  741  ILE ILE B . n 
B 1 742  VAL 742  742  742  VAL VAL B . n 
B 1 743  LEU 743  743  743  LEU LEU B . n 
B 1 744  GLY 744  744  744  GLY GLY B . n 
B 1 745  LEU 745  745  745  LEU LEU B . n 
B 1 746  TYR 746  746  746  TYR TYR B . n 
B 1 747  ILE 747  747  747  ILE ILE B . n 
B 1 748  TYR 748  748  748  TYR TYR B . n 
B 1 749  VAL 749  749  749  VAL VAL B . n 
B 1 750  THR 750  750  750  THR THR B . n 
B 1 751  TYR 751  751  751  TYR TYR B . n 
B 1 752  LYS 752  752  752  LYS LYS B . n 
B 1 753  LYS 753  753  753  LYS LYS B . n 
B 1 754  PRO 754  754  754  PRO PRO B . n 
B 1 755  ASP 755  755  755  ASP ASP B . n 
B 1 756  VAL 756  756  756  VAL VAL B . n 
B 1 757  ASN 757  757  757  ASN ASN B . n 
B 1 758  TRP 758  758  758  TRP TRP B . n 
B 1 759  GLY 759  759  759  GLY GLY B . n 
B 1 760  SER 760  760  760  SER SER B . n 
B 1 761  SER 761  761  761  SER SER B . n 
B 1 762  THR 762  762  762  THR THR B . n 
B 1 763  GLN 763  763  763  GLN GLN B . n 
B 1 764  ALA 764  764  764  ALA ALA B . n 
B 1 765  LEU 765  765  765  LEU LEU B . n 
B 1 766  THR 766  766  766  THR THR B . n 
B 1 767  TYR 767  767  767  TYR TYR B . n 
B 1 768  LEU 768  768  768  LEU LEU B . n 
B 1 769  ASN 769  769  769  ASN ASN B . n 
B 1 770  ALA 770  770  770  ALA ALA B . n 
B 1 771  LEU 771  771  771  LEU LEU B . n 
B 1 772  GLN 772  772  772  GLN GLN B . n 
B 1 773  HIS 773  773  773  HIS HIS B . n 
B 1 774  SER 774  774  774  SER SER B . n 
B 1 775  ILE 775  775  775  ILE ILE B . n 
B 1 776  ARG 776  776  776  ARG ARG B . n 
B 1 777  LEU 777  777  777  LEU LEU B . n 
B 1 778  SER 778  778  778  SER SER B . n 
B 1 779  GLY 779  779  779  GLY GLY B . n 
B 1 780  VAL 780  780  780  VAL VAL B . n 
B 1 781  GLU 781  781  781  GLU GLU B . n 
B 1 782  ASP 782  782  782  ASP ASP B . n 
B 1 783  HIS 783  783  783  HIS HIS B . n 
B 1 784  VAL 784  784  784  VAL VAL B . n 
B 1 785  LYS 785  785  785  LYS LYS B . n 
B 1 786  ASN 786  786  786  ASN ASN B . n 
B 1 787  PHE 787  787  787  PHE PHE B . n 
B 1 788  ARG 788  788  788  ARG ARG B . n 
B 1 789  PRO 789  789  789  PRO PRO B . n 
B 1 790  GLN 790  790  790  GLN GLN B . n 
B 1 791  CYS 791  791  791  CYS CYS B . n 
B 1 792  LEU 792  792  792  LEU LEU B . n 
B 1 793  VAL 793  793  793  VAL VAL B . n 
B 1 794  MET 794  794  794  MET MET B . n 
B 1 795  THR 795  795  795  THR THR B . n 
B 1 796  GLY 796  796  796  GLY GLY B . n 
B 1 797  ALA 797  797  797  ALA ALA B . n 
B 1 798  PRO 798  798  798  PRO PRO B . n 
B 1 799  ASN 799  799  799  ASN ASN B . n 
B 1 800  SER 800  800  800  SER SER B . n 
B 1 801  ARG 801  801  801  ARG ARG B . n 
B 1 802  PRO 802  802  802  PRO PRO B . n 
B 1 803  ALA 803  803  803  ALA ALA B . n 
B 1 804  LEU 804  804  804  LEU LEU B . n 
B 1 805  LEU 805  805  805  LEU LEU B . n 
B 1 806  HIS 806  806  806  HIS HIS B . n 
B 1 807  LEU 807  807  807  LEU LEU B . n 
B 1 808  VAL 808  808  808  VAL VAL B . n 
B 1 809  HIS 809  809  809  HIS HIS B . n 
B 1 810  ASP 810  810  810  ASP ASP B . n 
B 1 811  PHE 811  811  811  PHE PHE B . n 
B 1 812  THR 812  812  812  THR THR B . n 
B 1 813  LYS 813  813  813  LYS LYS B . n 
B 1 814  ASN 814  814  814  ASN ASN B . n 
B 1 815  VAL 815  815  815  VAL VAL B . n 
B 1 816  GLY 816  816  816  GLY GLY B . n 
B 1 817  LEU 817  817  817  LEU LEU B . n 
B 1 818  MET 818  818  818  MET MET B . n 
B 1 819  ILE 819  819  819  ILE ILE B . n 
B 1 820  CYS 820  820  820  CYS CYS B . n 
B 1 821  GLY 821  821  821  GLY GLY B . n 
B 1 822  HIS 822  822  822  HIS HIS B . n 
B 1 823  VAL 823  823  823  VAL VAL B . n 
B 1 824  HIS 824  824  824  HIS HIS B . n 
B 1 825  MET 825  825  825  MET MET B . n 
B 1 826  GLY 826  826  826  GLY GLY B . n 
B 1 827  PRO 827  827  827  PRO PRO B . n 
B 1 828  ARG 828  828  828  ARG ARG B . n 
B 1 829  ARG 829  829  829  ARG ARG B . n 
B 1 830  GLN 830  830  830  GLN GLN B . n 
B 1 831  ALA 831  831  831  ALA ALA B . n 
B 1 832  MET 832  832  832  MET MET B . n 
B 1 833  LYS 833  833  833  LYS LYS B . n 
B 1 834  GLU 834  834  834  GLU GLU B . n 
B 1 835  MET 835  835  835  MET MET B . n 
B 1 836  SER 836  836  836  SER SER B . n 
B 1 837  ILE 837  837  837  ILE ILE B . n 
B 1 838  ASP 838  838  838  ASP ASP B . n 
B 1 839  GLN 839  839  839  GLN GLN B . n 
B 1 840  ALA 840  840  840  ALA ALA B . n 
B 1 841  LYS 841  841  841  LYS LYS B . n 
B 1 842  TYR 842  842  842  TYR TYR B . n 
B 1 843  GLN 843  843  843  GLN GLN B . n 
B 1 844  ARG 844  844  844  ARG ARG B . n 
B 1 845  TRP 845  845  845  TRP TRP B . n 
B 1 846  LEU 846  846  846  LEU LEU B . n 
B 1 847  ILE 847  847  847  ILE ILE B . n 
B 1 848  LYS 848  848  848  LYS LYS B . n 
B 1 849  ASN 849  849  849  ASN ASN B . n 
B 1 850  LYS 850  850  850  LYS LYS B . n 
B 1 851  MET 851  851  851  MET MET B . n 
B 1 852  LYS 852  852  852  LYS LYS B . n 
B 1 853  ALA 853  853  853  ALA ALA B . n 
B 1 854  PHE 854  854  854  PHE PHE B . n 
B 1 855  TYR 855  855  855  TYR TYR B . n 
B 1 856  ALA 856  856  856  ALA ALA B . n 
B 1 857  PRO 857  857  857  PRO PRO B . n 
B 1 858  VAL 858  858  858  VAL VAL B . n 
B 1 859  HIS 859  859  859  HIS HIS B . n 
B 1 860  ALA 860  860  860  ALA ALA B . n 
B 1 861  ASP 861  861  861  ASP ASP B . n 
B 1 862  ASP 862  862  862  ASP ASP B . n 
B 1 863  LEU 863  863  863  LEU LEU B . n 
B 1 864  ARG 864  864  864  ARG ARG B . n 
B 1 865  GLU 865  865  865  GLU GLU B . n 
B 1 866  GLY 866  866  866  GLY GLY B . n 
B 1 867  ALA 867  867  867  ALA ALA B . n 
B 1 868  GLN 868  868  868  GLN GLN B . n 
B 1 869  TYR 869  869  869  TYR TYR B . n 
B 1 870  LEU 870  870  870  LEU LEU B . n 
B 1 871  MET 871  871  871  MET MET B . n 
B 1 872  GLN 872  872  872  GLN GLN B . n 
B 1 873  ALA 873  873  873  ALA ALA B . n 
B 1 874  ALA 874  874  874  ALA ALA B . n 
B 1 875  GLY 875  875  875  GLY GLY B . n 
B 1 876  LEU 876  876  876  LEU LEU B . n 
B 1 877  GLY 877  877  877  GLY GLY B . n 
B 1 878  ARG 878  878  878  ARG ARG B . n 
B 1 879  MET 879  879  879  MET MET B . n 
B 1 880  LYS 880  880  880  LYS LYS B . n 
B 1 881  PRO 881  881  881  PRO PRO B . n 
B 1 882  ASN 882  882  882  ASN ASN B . n 
B 1 883  THR 883  883  883  THR THR B . n 
B 1 884  LEU 884  884  884  LEU LEU B . n 
B 1 885  VAL 885  885  885  VAL VAL B . n 
B 1 886  LEU 886  886  886  LEU LEU B . n 
B 1 887  GLY 887  887  887  GLY GLY B . n 
B 1 888  PHE 888  888  888  PHE PHE B . n 
B 1 889  LYS 889  889  889  LYS LYS B . n 
B 1 890  LYS 890  890  890  LYS LYS B . n 
B 1 891  ASP 891  891  891  ASP ASP B . n 
B 1 892  TRP 892  892  892  TRP TRP B . n 
B 1 893  LEU 893  893  893  LEU LEU B . n 
B 1 894  GLN 894  894  894  GLN GLN B . n 
B 1 895  ALA 895  895  895  ALA ALA B . n 
B 1 896  ASP 896  896  896  ASP ASP B . n 
B 1 897  MET 897  897  897  MET MET B . n 
B 1 898  ARG 898  898  898  ARG ARG B . n 
B 1 899  ASP 899  899  899  ASP ASP B . n 
B 1 900  VAL 900  900  900  VAL VAL B . n 
B 1 901  ASP 901  901  901  ASP ASP B . n 
B 1 902  MET 902  902  902  MET MET B . n 
B 1 903  TYR 903  903  903  TYR TYR B . n 
B 1 904  ILE 904  904  904  ILE ILE B . n 
B 1 905  ASN 905  905  905  ASN ASN B . n 
B 1 906  LEU 906  906  906  LEU LEU B . n 
B 1 907  PHE 907  907  907  PHE PHE B . n 
B 1 908  HIS 908  908  908  HIS HIS B . n 
B 1 909  ASP 909  909  909  ASP ASP B . n 
B 1 910  ALA 910  910  910  ALA ALA B . n 
B 1 911  PHE 911  911  911  PHE PHE B . n 
B 1 912  ASP 912  912  912  ASP ASP B . n 
B 1 913  ILE 913  913  913  ILE ILE B . n 
B 1 914  GLN 914  914  914  GLN GLN B . n 
B 1 915  TYR 915  915  915  TYR TYR B . n 
B 1 916  GLY 916  916  916  GLY GLY B . n 
B 1 917  VAL 917  917  917  VAL VAL B . n 
B 1 918  VAL 918  918  918  VAL VAL B . n 
B 1 919  VAL 919  919  919  VAL VAL B . n 
B 1 920  ILE 920  920  920  ILE ILE B . n 
B 1 921  ARG 921  921  921  ARG ARG B . n 
B 1 922  LEU 922  922  922  LEU LEU B . n 
B 1 923  LYS 923  923  923  LYS LYS B . n 
B 1 924  GLU 924  924  924  GLU GLU B . n 
B 1 925  GLY 925  925  925  GLY GLY B . n 
B 1 926  LEU 926  926  926  LEU LEU B . n 
B 1 927  ASP 927  927  ?    ?   ?   B . n 
B 1 928  ILE 928  928  ?    ?   ?   B . n 
B 1 929  SER 929  929  ?    ?   ?   B . n 
B 1 930  HIS 930  930  ?    ?   ?   B . n 
B 1 931  LEU 931  931  ?    ?   ?   B . n 
B 1 932  GLN 932  932  ?    ?   ?   B . n 
B 1 933  GLY 933  933  ?    ?   ?   B . n 
B 1 934  GLN 934  934  ?    ?   ?   B . n 
B 1 935  GLU 935  935  ?    ?   ?   B . n 
B 1 936  GLU 936  936  ?    ?   ?   B . n 
B 1 937  LEU 937  937  ?    ?   ?   B . n 
B 1 938  LEU 938  938  ?    ?   ?   B . n 
B 1 939  SER 939  939  ?    ?   ?   B . n 
B 1 940  SER 940  940  ?    ?   ?   B . n 
B 1 941  GLN 941  941  ?    ?   ?   B . n 
B 1 942  GLU 942  942  ?    ?   ?   B . n 
B 1 943  LYS 943  943  ?    ?   ?   B . n 
B 1 944  SER 944  944  ?    ?   ?   B . n 
B 1 945  PRO 945  945  ?    ?   ?   B . n 
B 1 946  GLY 946  946  ?    ?   ?   B . n 
B 1 947  THR 947  947  ?    ?   ?   B . n 
B 1 948  LYS 948  948  ?    ?   ?   B . n 
B 1 949  ASP 949  949  ?    ?   ?   B . n 
B 1 950  VAL 950  950  ?    ?   ?   B . n 
B 1 951  VAL 951  951  ?    ?   ?   B . n 
B 1 952  VAL 952  952  ?    ?   ?   B . n 
B 1 953  SER 953  953  ?    ?   ?   B . n 
B 1 954  VAL 954  954  ?    ?   ?   B . n 
B 1 955  GLU 955  955  ?    ?   ?   B . n 
B 1 956  TYR 956  956  ?    ?   ?   B . n 
B 1 957  SER 957  957  ?    ?   ?   B . n 
B 1 958  LYS 958  958  ?    ?   ?   B . n 
B 1 959  LYS 959  959  ?    ?   ?   B . n 
B 1 960  SER 960  960  ?    ?   ?   B . n 
B 1 961  ASP 961  961  ?    ?   ?   B . n 
B 1 962  LEU 962  962  ?    ?   ?   B . n 
B 1 963  ASP 963  963  ?    ?   ?   B . n 
B 1 964  THR 964  964  ?    ?   ?   B . n 
B 1 965  SER 965  965  ?    ?   ?   B . n 
B 1 966  LYS 966  966  ?    ?   ?   B . n 
B 1 967  PRO 967  967  ?    ?   ?   B . n 
B 1 968  LEU 968  968  ?    ?   ?   B . n 
B 1 969  SER 969  969  ?    ?   ?   B . n 
B 1 970  GLU 970  970  ?    ?   ?   B . n 
B 1 971  LYS 971  971  ?    ?   ?   B . n 
B 1 972  PRO 972  972  ?    ?   ?   B . n 
B 1 973  ILE 973  973  ?    ?   ?   B . n 
B 1 974  THR 974  974  ?    ?   ?   B . n 
B 1 975  HIS 975  975  ?    ?   ?   B . n 
B 1 976  LYS 976  976  ?    ?   ?   B . n 
B 1 977  VAL 977  977  ?    ?   ?   B . n 
B 1 978  GLU 978  978  ?    ?   ?   B . n 
B 1 979  GLU 979  979  ?    ?   ?   B . n 
B 1 980  GLU 980  980  ?    ?   ?   B . n 
B 1 981  ASP 981  981  ?    ?   ?   B . n 
B 1 982  GLY 982  982  ?    ?   ?   B . n 
B 1 983  LYS 983  983  ?    ?   ?   B . n 
B 1 984  THR 984  984  ?    ?   ?   B . n 
B 1 985  ALA 985  985  ?    ?   ?   B . n 
B 1 986  THR 986  986  ?    ?   ?   B . n 
B 1 987  GLN 987  987  ?    ?   ?   B . n 
B 1 988  PRO 988  988  ?    ?   ?   B . n 
B 1 989  LEU 989  989  ?    ?   ?   B . n 
B 1 990  LEU 990  990  ?    ?   ?   B . n 
B 1 991  LYS 991  991  ?    ?   ?   B . n 
B 1 992  LYS 992  992  ?    ?   ?   B . n 
B 1 993  GLU 993  993  ?    ?   ?   B . n 
B 1 994  SER 994  994  ?    ?   ?   B . n 
B 1 995  LYS 995  995  ?    ?   ?   B . n 
B 1 996  GLY 996  996  ?    ?   ?   B . n 
B 1 997  PRO 997  997  ?    ?   ?   B . n 
B 1 998  ILE 998  998  ?    ?   ?   B . n 
B 1 999  VAL 999  999  ?    ?   ?   B . n 
B 1 1000 PRO 1000 1000 ?    ?   ?   B . n 
B 1 1001 LEU 1001 1001 ?    ?   ?   B . n 
B 1 1002 ASN 1002 1002 ?    ?   ?   B . n 
B 1 1003 VAL 1003 1003 ?    ?   ?   B . n 
B 1 1004 ALA 1004 1004 ?    ?   ?   B . n 
B 1 1005 ASP 1005 1005 ?    ?   ?   B . n 
B 1 1006 GLN 1006 1006 ?    ?   ?   B . n 
B 1 1007 LYS 1007 1007 ?    ?   ?   B . n 
B 1 1008 LEU 1008 1008 ?    ?   ?   B . n 
B 1 1009 LEU 1009 1009 ?    ?   ?   B . n 
B 1 1010 GLU 1010 1010 ?    ?   ?   B . n 
B 1 1011 ALA 1011 1011 ?    ?   ?   B . n 
B 1 1012 SER 1012 1012 ?    ?   ?   B . n 
B 1 1013 THR 1013 1013 ?    ?   ?   B . n 
B 1 1014 GLN 1014 1014 ?    ?   ?   B . n 
B 1 1015 PHE 1015 1015 ?    ?   ?   B . n 
B 1 1016 GLN 1016 1016 ?    ?   ?   B . n 
B 1 1017 LYS 1017 1017 ?    ?   ?   B . n 
B 1 1018 LYS 1018 1018 ?    ?   ?   B . n 
B 1 1019 GLN 1019 1019 ?    ?   ?   B . n 
B 1 1020 GLY 1020 1020 ?    ?   ?   B . n 
B 1 1021 LYS 1021 1021 ?    ?   ?   B . n 
B 1 1022 ASN 1022 1022 1022 ASN ASN B . n 
B 1 1023 THR 1023 1023 1023 THR THR B . n 
B 1 1024 ILE 1024 1024 1024 ILE ILE B . n 
B 1 1025 ASP 1025 1025 1025 ASP ASP B . n 
B 1 1026 VAL 1026 1026 1026 VAL VAL B . n 
B 1 1027 TRP 1027 1027 1027 TRP TRP B . n 
B 1 1028 TRP 1028 1028 1028 TRP TRP B . n 
B 1 1029 LEU 1029 1029 1029 LEU LEU B . n 
B 1 1030 PHE 1030 1030 1030 PHE PHE B . n 
B 1 1031 ASP 1031 1031 1031 ASP ASP B . n 
B 1 1032 ASP 1032 1032 1032 ASP ASP B . n 
B 1 1033 GLY 1033 1033 1033 GLY GLY B . n 
B 1 1034 GLY 1034 1034 1034 GLY GLY B . n 
B 1 1035 LEU 1035 1035 1035 LEU LEU B . n 
B 1 1036 THR 1036 1036 1036 THR THR B . n 
B 1 1037 LEU 1037 1037 1037 LEU LEU B . n 
B 1 1038 LEU 1038 1038 1038 LEU LEU B . n 
B 1 1039 ILE 1039 1039 1039 ILE ILE B . n 
B 1 1040 PRO 1040 1040 1040 PRO PRO B . n 
B 1 1041 TYR 1041 1041 1041 TYR TYR B . n 
B 1 1042 LEU 1042 1042 1042 LEU LEU B . n 
B 1 1043 LEU 1043 1043 1043 LEU LEU B . n 
B 1 1044 THR 1044 1044 1044 THR THR B . n 
B 1 1045 THR 1045 1045 1045 THR THR B . n 
B 1 1046 LYS 1046 1046 1046 LYS LYS B . n 
B 1 1047 LYS 1047 1047 1047 LYS LYS B . n 
B 1 1048 LYS 1048 1048 1048 LYS LYS B . n 
B 1 1049 TRP 1049 1049 1049 TRP TRP B . n 
B 1 1050 LYS 1050 1050 1050 LYS LYS B . n 
B 1 1051 ASP 1051 1051 1051 ASP ASP B . n 
B 1 1052 CYS 1052 1052 1052 CYS CYS B . n 
B 1 1053 LYS 1053 1053 1053 LYS LYS B . n 
B 1 1054 ILE 1054 1054 1054 ILE ILE B . n 
B 1 1055 ARG 1055 1055 1055 ARG ARG B . n 
B 1 1056 VAL 1056 1056 1056 VAL VAL B . n 
B 1 1057 PHE 1057 1057 1057 PHE PHE B . n 
B 1 1058 ILE 1058 1058 1058 ILE ILE B . n 
B 1 1059 GLY 1059 1059 1059 GLY GLY B . n 
B 1 1060 GLY 1060 1060 1060 GLY GLY B . n 
B 1 1061 LYS 1061 1061 1061 LYS LYS B . n 
B 1 1062 ILE 1062 1062 1062 ILE ILE B . n 
B 1 1063 ASN 1063 1063 1063 ASN ASN B . n 
B 1 1064 ARG 1064 1064 1064 ARG ARG B . n 
B 1 1065 ILE 1065 1065 1065 ILE ILE B . n 
B 1 1066 ASP 1066 1066 1066 ASP ASP B . n 
B 1 1067 HIS 1067 1067 1067 HIS HIS B . n 
B 1 1068 ASP 1068 1068 1068 ASP ASP B . n 
B 1 1069 ARG 1069 1069 1069 ARG ARG B . n 
B 1 1070 ARG 1070 1070 1070 ARG ARG B . n 
B 1 1071 ALA 1071 1071 1071 ALA ALA B . n 
B 1 1072 MET 1072 1072 1072 MET MET B . n 
B 1 1073 ALA 1073 1073 1073 ALA ALA B . n 
B 1 1074 THR 1074 1074 1074 THR THR B . n 
B 1 1075 LEU 1075 1075 1075 LEU LEU B . n 
B 1 1076 LEU 1076 1076 1076 LEU LEU B . n 
B 1 1077 SER 1077 1077 1077 SER SER B . n 
B 1 1078 LYS 1078 1078 1078 LYS LYS B . n 
B 1 1079 PHE 1079 1079 1079 PHE PHE B . n 
B 1 1080 ARG 1080 1080 1080 ARG ARG B . n 
B 1 1081 ILE 1081 1081 1081 ILE ILE B . n 
B 1 1082 ASP 1082 1082 1082 ASP ASP B . n 
B 1 1083 PHE 1083 1083 1083 PHE PHE B . n 
B 1 1084 SER 1084 1084 1084 SER SER B . n 
B 1 1085 ASP 1085 1085 1085 ASP ASP B . n 
B 1 1086 ILE 1086 1086 1086 ILE ILE B . n 
B 1 1087 MET 1087 1087 1087 MET MET B . n 
B 1 1088 VAL 1088 1088 1088 VAL VAL B . n 
B 1 1089 LEU 1089 1089 1089 LEU LEU B . n 
B 1 1090 GLY 1090 1090 1090 GLY GLY B . n 
B 1 1091 ASP 1091 1091 1091 ASP ASP B . n 
B 1 1092 ILE 1092 1092 1092 ILE ILE B . n 
B 1 1093 ASN 1093 1093 1093 ASN ASN B . n 
B 1 1094 THR 1094 1094 1094 THR THR B . n 
B 1 1095 LYS 1095 1095 1095 LYS LYS B . n 
B 1 1096 PRO 1096 1096 1096 PRO PRO B . n 
B 1 1097 LYS 1097 1097 1097 LYS LYS B . n 
B 1 1098 LYS 1098 1098 1098 LYS LYS B . n 
B 1 1099 GLU 1099 1099 1099 GLU GLU B . n 
B 1 1100 ASN 1100 1100 1100 ASN ASN B . n 
B 1 1101 ILE 1101 1101 1101 ILE ILE B . n 
B 1 1102 ILE 1102 1102 1102 ILE ILE B . n 
B 1 1103 ALA 1103 1103 1103 ALA ALA B . n 
B 1 1104 PHE 1104 1104 1104 PHE PHE B . n 
B 1 1105 GLU 1105 1105 1105 GLU GLU B . n 
B 1 1106 GLU 1106 1106 1106 GLU GLU B . n 
B 1 1107 ILE 1107 1107 1107 ILE ILE B . n 
B 1 1108 ILE 1108 1108 1108 ILE ILE B . n 
B 1 1109 GLU 1109 1109 1109 GLU GLU B . n 
B 1 1110 PRO 1110 1110 1110 PRO PRO B . n 
B 1 1111 TYR 1111 1111 1111 TYR TYR B . n 
B 1 1112 ARG 1112 1112 1112 ARG ARG B . n 
B 1 1113 LEU 1113 1113 1113 LEU LEU B . n 
B 1 1114 HIS 1114 1114 1114 HIS HIS B . n 
B 1 1115 GLU 1115 1115 1115 GLU GLU B . n 
B 1 1116 ASP 1116 1116 1116 ASP ASP B . n 
B 1 1117 ASP 1117 1117 1117 ASP ASP B . n 
B 1 1118 LYS 1118 1118 1118 LYS LYS B . n 
B 1 1119 GLU 1119 1119 1119 GLU GLU B . n 
B 1 1120 GLN 1120 1120 1120 GLN GLN B . n 
B 1 1121 ASP 1121 1121 1121 ASP ASP B . n 
B 1 1122 ILE 1122 1122 1122 ILE ILE B . n 
B 1 1123 ALA 1123 1123 1123 ALA ALA B . n 
B 1 1124 ASP 1124 1124 1124 ASP ASP B . n 
B 1 1125 LYS 1125 1125 1125 LYS LYS B . n 
B 1 1126 MET 1126 1126 1126 MET MET B . n 
B 1 1127 LYS 1127 1127 1127 LYS LYS B . n 
B 1 1128 GLU 1128 1128 1128 GLU GLU B . n 
B 1 1129 ASP 1129 1129 1129 ASP ASP B . n 
B 1 1130 GLU 1130 1130 1130 GLU ALA B . n 
B 1 1131 PRO 1131 1131 1131 PRO PRO B . n 
B 1 1132 TRP 1132 1132 1132 TRP TRP B . n 
B 1 1133 ARG 1133 1133 1133 ARG ARG B . n 
B 1 1134 ILE 1134 1134 1134 ILE ILE B . n 
B 1 1135 THR 1135 1135 1135 THR THR B . n 
B 1 1136 ASP 1136 1136 1136 ASP ASP B . n 
B 1 1137 ASN 1137 1137 1137 ASN ASN B . n 
B 1 1138 GLU 1138 1138 1138 GLU GLU B . n 
B 1 1139 LEU 1139 1139 1139 LEU LEU B . n 
B 1 1140 GLU 1140 1140 1140 GLU GLU B . n 
B 1 1141 LEU 1141 1141 1141 LEU LEU B . n 
B 1 1142 TYR 1142 1142 1142 TYR TYR B . n 
B 1 1143 LYS 1143 1143 1143 LYS LYS B . n 
B 1 1144 THR 1144 1144 1144 THR THR B . n 
B 1 1145 LYS 1145 1145 1145 LYS LYS B . n 
B 1 1146 THR 1146 1146 1146 THR THR B . n 
B 1 1147 TYR 1147 1147 1147 TYR TYR B . n 
B 1 1148 ARG 1148 1148 1148 ARG ARG B . n 
B 1 1149 GLN 1149 1149 1149 GLN GLN B . n 
B 1 1150 ILE 1150 1150 1150 ILE ILE B . n 
B 1 1151 ARG 1151 1151 1151 ARG ARG B . n 
B 1 1152 LEU 1152 1152 1152 LEU LEU B . n 
B 1 1153 ASN 1153 1153 1153 ASN ASN B . n 
B 1 1154 GLU 1154 1154 1154 GLU GLU B . n 
B 1 1155 LEU 1155 1155 1155 LEU LEU B . n 
B 1 1156 LEU 1156 1156 1156 LEU LEU B . n 
B 1 1157 LYS 1157 1157 1157 LYS LYS B . n 
B 1 1158 GLU 1158 1158 1158 GLU GLU B . n 
B 1 1159 HIS 1159 1159 1159 HIS HIS B . n 
B 1 1160 SER 1160 1160 1160 SER SER B . n 
B 1 1161 SER 1161 1161 1161 SER SER B . n 
B 1 1162 THR 1162 1162 1162 THR THR B . n 
B 1 1163 ALA 1163 1163 1163 ALA ALA B . n 
B 1 1164 ASN 1164 1164 1164 ASN ASN B . n 
B 1 1165 ILE 1165 1165 1165 ILE ILE B . n 
B 1 1166 ILE 1166 1166 1166 ILE ILE B . n 
B 1 1167 VAL 1167 1167 1167 VAL VAL B . n 
B 1 1168 MET 1168 1168 1168 MET MET B . n 
B 1 1169 SER 1169 1169 1169 SER SER B . n 
B 1 1170 LEU 1170 1170 1170 LEU LEU B . n 
B 1 1171 PRO 1171 1171 1171 PRO PRO B . n 
B 1 1172 VAL 1172 1172 1172 VAL VAL B . n 
B 1 1173 ALA 1173 1173 1173 ALA ALA B . n 
B 1 1174 ARG 1174 1174 1174 ARG ARG B . n 
B 1 1175 LYS 1175 1175 1175 LYS LYS B . n 
B 1 1176 GLY 1176 1176 1176 GLY GLY B . n 
B 1 1177 ALA 1177 1177 1177 ALA ALA B . n 
B 1 1178 VAL 1178 1178 1178 VAL VAL B . n 
B 1 1179 SER 1179 1179 1179 SER SER B . n 
B 1 1180 SER 1180 1180 1180 SER SER B . n 
B 1 1181 ALA 1181 1181 1181 ALA ALA B . n 
B 1 1182 LEU 1182 1182 1182 LEU LEU B . n 
B 1 1183 TYR 1183 1183 1183 TYR TYR B . n 
B 1 1184 MET 1184 1184 1184 MET MET B . n 
B 1 1185 ALA 1185 1185 1185 ALA ALA B . n 
B 1 1186 TRP 1186 1186 1186 TRP TRP B . n 
B 1 1187 LEU 1187 1187 1187 LEU LEU B . n 
B 1 1188 GLU 1188 1188 1188 GLU GLU B . n 
B 1 1189 ALA 1189 1189 1189 ALA ALA B . n 
B 1 1190 LEU 1190 1190 1190 LEU LEU B . n 
B 1 1191 SER 1191 1191 1191 SER SER B . n 
B 1 1192 LYS 1192 1192 1192 LYS LYS B . n 
B 1 1193 ASP 1193 1193 1193 ASP ASP B . n 
B 1 1194 LEU 1194 1194 1194 LEU LEU B . n 
B 1 1195 PRO 1195 1195 1195 PRO PRO B . n 
B 1 1196 PRO 1196 1196 1196 PRO PRO B . n 
B 1 1197 ILE 1197 1197 1197 ILE ILE B . n 
B 1 1198 LEU 1198 1198 1198 LEU LEU B . n 
B 1 1199 LEU 1199 1199 1199 LEU LEU B . n 
B 1 1200 VAL 1200 1200 1200 VAL VAL B . n 
B 1 1201 ARG 1201 1201 1201 ARG ARG B . n 
B 1 1202 GLY 1202 1202 1202 GLY GLY B . n 
B 1 1203 ASN 1203 1203 1203 ASN ASN B . n 
B 1 1204 HIS 1204 1204 1204 HIS HIS B . n 
B 1 1205 GLN 1205 1205 1205 GLN GLN B . n 
B 1 1206 SER 1206 1206 1206 SER SER B . n 
B 1 1207 VAL 1207 1207 1207 VAL VAL B . n 
B 1 1208 LEU 1208 1208 1208 LEU LEU B . n 
B 1 1209 THR 1209 1209 1209 THR THR B . n 
B 1 1210 PHE 1210 1210 1210 PHE PHE B . n 
B 1 1211 TYR 1211 1211 1211 TYR TYR B . n 
B 1 1212 SER 1212 1212 1212 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ATU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ATU 
_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 
C 2 A1ATU 1 1301 1301 A1ATU LIG A . 
D 3 CL    1 1302 1304 CL    CL  A . 
E 4 NA    1 1303 1305 NA    NA  A . 
F 2 A1ATU 1 1301 1301 A1ATU LIG B . 
G 3 CL    1 1302 1304 CL    CL  B . 
H 4 NA    1 1303 1305 NA    NA  B . 
I 5 HOH   1 1401 1303 HOH   HOH A . 
J 5 HOH   1 1401 1303 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A HIS 229  ? CB  ? A HIS 229  CB  
2   1 Y 1 A HIS 229  ? CG  ? A HIS 229  CG  
3   1 Y 1 A HIS 229  ? ND1 ? A HIS 229  ND1 
4   1 Y 1 A HIS 229  ? CD2 ? A HIS 229  CD2 
5   1 Y 1 A HIS 229  ? CE1 ? A HIS 229  CE1 
6   1 Y 1 A HIS 229  ? NE2 ? A HIS 229  NE2 
7   1 Y 1 A ALA 231  ? CB  ? A ALA 231  CB  
8   1 Y 1 A GLN 233  ? CG  ? A GLN 233  CG  
9   1 Y 1 A GLN 233  ? CD  ? A GLN 233  CD  
10  1 Y 1 A GLN 233  ? OE1 ? A GLN 233  OE1 
11  1 Y 1 A GLN 233  ? NE2 ? A GLN 233  NE2 
12  1 Y 1 A LEU 234  ? CB  ? A LEU 234  CB  
13  1 Y 1 A LEU 234  ? CG  ? A LEU 234  CG  
14  1 Y 1 A LEU 234  ? CD1 ? A LEU 234  CD1 
15  1 Y 1 A LEU 234  ? CD2 ? A LEU 234  CD2 
16  1 Y 1 A GLU 236  ? CB  ? A GLU 236  CB  
17  1 Y 1 A GLU 236  ? CG  ? A GLU 236  CG  
18  1 Y 1 A GLU 236  ? CD  ? A GLU 236  CD  
19  1 Y 1 A GLU 236  ? OE1 ? A GLU 236  OE1 
20  1 Y 1 A GLU 236  ? OE2 ? A GLU 236  OE2 
21  1 Y 1 A LYS 237  ? CB  ? A LYS 237  CB  
22  1 Y 1 A LYS 237  ? CG  ? A LYS 237  CG  
23  1 Y 1 A LYS 237  ? CD  ? A LYS 237  CD  
24  1 Y 1 A LYS 237  ? CE  ? A LYS 237  CE  
25  1 Y 1 A LYS 237  ? NZ  ? A LYS 237  NZ  
26  1 Y 1 A LEU 238  ? CB  ? A LEU 238  CB  
27  1 Y 1 A LEU 238  ? CG  ? A LEU 238  CG  
28  1 Y 1 A LEU 238  ? CD1 ? A LEU 238  CD1 
29  1 Y 1 A LEU 238  ? CD2 ? A LEU 238  CD2 
30  1 Y 1 A LEU 250  ? CG  ? A LEU 250  CG  
31  1 Y 1 A LEU 250  ? CD1 ? A LEU 250  CD1 
32  1 Y 1 A LEU 250  ? CD2 ? A LEU 250  CD2 
33  1 Y 1 A MET 325  ? CG  ? A MET 325  CG  
34  1 Y 1 A MET 325  ? SD  ? A MET 325  SD  
35  1 Y 1 A MET 325  ? CE  ? A MET 325  CE  
36  1 Y 1 A GLU 393  ? CG  ? A GLU 393  CG  
37  1 Y 1 A GLU 393  ? CD  ? A GLU 393  CD  
38  1 Y 1 A GLU 393  ? OE1 ? A GLU 393  OE1 
39  1 Y 1 A GLU 393  ? OE2 ? A GLU 393  OE2 
40  1 Y 1 A LYS 396  ? CG  ? A LYS 396  CG  
41  1 Y 1 A LYS 396  ? CD  ? A LYS 396  CD  
42  1 Y 1 A LYS 396  ? CE  ? A LYS 396  CE  
43  1 Y 1 A LYS 396  ? NZ  ? A LYS 396  NZ  
44  1 Y 1 A GLU 397  ? CG  ? A GLU 397  CG  
45  1 Y 1 A GLU 397  ? CD  ? A GLU 397  CD  
46  1 Y 1 A GLU 397  ? OE1 ? A GLU 397  OE1 
47  1 Y 1 A GLU 397  ? OE2 ? A GLU 397  OE2 
48  1 Y 1 A ILE 400  ? CG1 ? A ILE 400  CG1 
49  1 Y 1 A ILE 400  ? CG2 ? A ILE 400  CG2 
50  1 Y 1 A ILE 400  ? CD1 ? A ILE 400  CD1 
51  1 Y 1 A LEU 401  ? CG  ? A LEU 401  CG  
52  1 Y 1 A LEU 401  ? CD1 ? A LEU 401  CD1 
53  1 Y 1 A LEU 401  ? CD2 ? A LEU 401  CD2 
54  1 Y 1 A MET 402  ? CG  ? A MET 402  CG  
55  1 Y 1 A MET 402  ? SD  ? A MET 402  SD  
56  1 Y 1 A MET 402  ? CE  ? A MET 402  CE  
57  1 Y 1 A ILE 403  ? CG1 ? A ILE 403  CG1 
58  1 Y 1 A ILE 403  ? CG2 ? A ILE 403  CG2 
59  1 Y 1 A ILE 403  ? CD1 ? A ILE 403  CD1 
60  1 Y 1 A ASP 404  ? CG  ? A ASP 404  CG  
61  1 Y 1 A ASP 404  ? OD1 ? A ASP 404  OD1 
62  1 Y 1 A ASP 404  ? OD2 ? A ASP 404  OD2 
63  1 Y 1 A GLU 405  ? CG  ? A GLU 405  CG  
64  1 Y 1 A GLU 405  ? CD  ? A GLU 405  CD  
65  1 Y 1 A GLU 405  ? OE1 ? A GLU 405  OE1 
66  1 Y 1 A GLU 405  ? OE2 ? A GLU 405  OE2 
67  1 Y 1 A ILE 406  ? CG1 ? A ILE 406  CG1 
68  1 Y 1 A ILE 406  ? CG2 ? A ILE 406  CG2 
69  1 Y 1 A ILE 406  ? CD1 ? A ILE 406  CD1 
70  1 Y 1 A ASP 408  ? CG  ? A ASP 408  CG  
71  1 Y 1 A ASP 408  ? OD1 ? A ASP 408  OD1 
72  1 Y 1 A ASP 408  ? OD2 ? A ASP 408  OD2 
73  1 Y 1 A GLU 429  ? CG  ? A GLU 429  CG  
74  1 Y 1 A GLU 429  ? CD  ? A GLU 429  CD  
75  1 Y 1 A GLU 429  ? OE1 ? A GLU 429  OE1 
76  1 Y 1 A GLU 429  ? OE2 ? A GLU 429  OE2 
77  1 Y 1 A ILE 451  ? CG1 ? A ILE 451  CG1 
78  1 Y 1 A ILE 451  ? CG2 ? A ILE 451  CG2 
79  1 Y 1 A ILE 451  ? CD1 ? A ILE 451  CD1 
80  1 Y 1 A ILE 455  ? CG1 ? A ILE 455  CG1 
81  1 Y 1 A ILE 455  ? CG2 ? A ILE 455  CG2 
82  1 Y 1 A ILE 455  ? CD1 ? A ILE 455  CD1 
83  1 Y 1 A LEU 457  ? CG  ? A LEU 457  CG  
84  1 Y 1 A LEU 457  ? CD1 ? A LEU 457  CD1 
85  1 Y 1 A LEU 457  ? CD2 ? A LEU 457  CD2 
86  1 Y 1 A GLU 458  ? CG  ? A GLU 458  CG  
87  1 Y 1 A GLU 458  ? CD  ? A GLU 458  CD  
88  1 Y 1 A GLU 458  ? OE1 ? A GLU 458  OE1 
89  1 Y 1 A GLU 458  ? OE2 ? A GLU 458  OE2 
90  1 Y 1 A LYS 461  ? CG  ? A LYS 461  CG  
91  1 Y 1 A LYS 461  ? CD  ? A LYS 461  CD  
92  1 Y 1 A LYS 461  ? CE  ? A LYS 461  CE  
93  1 Y 1 A LYS 461  ? NZ  ? A LYS 461  NZ  
94  1 Y 1 A GLU 475  ? CG  ? A GLU 475  CG  
95  1 Y 1 A GLU 475  ? CD  ? A GLU 475  CD  
96  1 Y 1 A GLU 475  ? OE1 ? A GLU 475  OE1 
97  1 Y 1 A GLU 475  ? OE2 ? A GLU 475  OE2 
98  1 Y 1 A GLU 483  ? CG  ? A GLU 483  CG  
99  1 Y 1 A GLU 483  ? CD  ? A GLU 483  CD  
100 1 Y 1 A GLU 483  ? OE1 ? A GLU 483  OE1 
101 1 Y 1 A GLU 483  ? OE2 ? A GLU 483  OE2 
102 1 Y 1 A GLU 484  ? CG  ? A GLU 484  CG  
103 1 Y 1 A GLU 484  ? CD  ? A GLU 484  CD  
104 1 Y 1 A GLU 484  ? OE1 ? A GLU 484  OE1 
105 1 Y 1 A GLU 484  ? OE2 ? A GLU 484  OE2 
106 1 Y 1 A ASP 547  ? CG  ? A ASP 547  CG  
107 1 Y 1 A ASP 547  ? OD1 ? A ASP 547  OD1 
108 1 Y 1 A ASP 547  ? OD2 ? A ASP 547  OD2 
109 1 Y 1 A THR 549  ? OG1 ? A THR 549  OG1 
110 1 Y 1 A THR 549  ? CG2 ? A THR 549  CG2 
111 1 Y 1 A ASN 551  ? CB  ? A ASN 551  CB  
112 1 Y 1 A ASN 551  ? CG  ? A ASN 551  CG  
113 1 Y 1 A ASN 551  ? OD1 ? A ASN 551  OD1 
114 1 Y 1 A ASN 551  ? ND2 ? A ASN 551  ND2 
115 1 Y 1 A VAL 552  ? CB  ? A VAL 552  CB  
116 1 Y 1 A VAL 552  ? CG1 ? A VAL 552  CG1 
117 1 Y 1 A VAL 552  ? CG2 ? A VAL 552  CG2 
118 1 Y 1 A ASP 554  ? CB  ? A ASP 554  CB  
119 1 Y 1 A ASP 554  ? CG  ? A ASP 554  CG  
120 1 Y 1 A ASP 554  ? OD1 ? A ASP 554  OD1 
121 1 Y 1 A ASP 554  ? OD2 ? A ASP 554  OD2 
122 1 Y 1 A THR 555  ? CB  ? A THR 555  CB  
123 1 Y 1 A THR 555  ? OG1 ? A THR 555  OG1 
124 1 Y 1 A THR 555  ? CG2 ? A THR 555  CG2 
125 1 Y 1 A ILE 556  ? CB  ? A ILE 556  CB  
126 1 Y 1 A ILE 556  ? CG1 ? A ILE 556  CG1 
127 1 Y 1 A ILE 556  ? CG2 ? A ILE 556  CG2 
128 1 Y 1 A ILE 556  ? CD1 ? A ILE 556  CD1 
129 1 Y 1 A VAL 557  ? CB  ? A VAL 557  CB  
130 1 Y 1 A VAL 557  ? CG1 ? A VAL 557  CG1 
131 1 Y 1 A VAL 557  ? CG2 ? A VAL 557  CG2 
132 1 Y 1 A THR 558  ? CB  ? A THR 558  CB  
133 1 Y 1 A THR 558  ? OG1 ? A THR 558  OG1 
134 1 Y 1 A THR 558  ? CG2 ? A THR 558  CG2 
135 1 Y 1 A GLU 559  ? CB  ? A GLU 559  CB  
136 1 Y 1 A GLU 559  ? CG  ? A GLU 559  CG  
137 1 Y 1 A GLU 559  ? CD  ? A GLU 559  CD  
138 1 Y 1 A GLU 559  ? OE1 ? A GLU 559  OE1 
139 1 Y 1 A GLU 559  ? OE2 ? A GLU 559  OE2 
140 1 Y 1 A LEU 560  ? CB  ? A LEU 560  CB  
141 1 Y 1 A LEU 560  ? CG  ? A LEU 560  CG  
142 1 Y 1 A LEU 560  ? CD1 ? A LEU 560  CD1 
143 1 Y 1 A LEU 560  ? CD2 ? A LEU 560  CD2 
144 1 Y 1 A THR 561  ? CB  ? A THR 561  CB  
145 1 Y 1 A THR 561  ? OG1 ? A THR 561  OG1 
146 1 Y 1 A THR 561  ? CG2 ? A THR 561  CG2 
147 1 Y 1 A THR 564  ? CB  ? A THR 564  CB  
148 1 Y 1 A THR 564  ? OG1 ? A THR 564  OG1 
149 1 Y 1 A THR 564  ? CG2 ? A THR 564  CG2 
150 1 Y 1 A SER 565  ? CB  ? A SER 565  CB  
151 1 Y 1 A SER 565  ? OG  ? A SER 565  OG  
152 1 Y 1 A ALA 566  ? CB  ? A ALA 566  CB  
153 1 Y 1 A LYS 569  ? CB  ? A LYS 569  CB  
154 1 Y 1 A LYS 569  ? CG  ? A LYS 569  CG  
155 1 Y 1 A LYS 569  ? CD  ? A LYS 569  CD  
156 1 Y 1 A LYS 569  ? CE  ? A LYS 569  CE  
157 1 Y 1 A LYS 569  ? NZ  ? A LYS 569  NZ  
158 1 Y 1 A LEU 570  ? CB  ? A LEU 570  CB  
159 1 Y 1 A LEU 570  ? CG  ? A LEU 570  CG  
160 1 Y 1 A LEU 570  ? CD1 ? A LEU 570  CD1 
161 1 Y 1 A LEU 570  ? CD2 ? A LEU 570  CD2 
162 1 Y 1 A ASN 571  ? CB  ? A ASN 571  CB  
163 1 Y 1 A ASN 571  ? CG  ? A ASN 571  CG  
164 1 Y 1 A ASN 571  ? OD1 ? A ASN 571  OD1 
165 1 Y 1 A ASN 571  ? ND2 ? A ASN 571  ND2 
166 1 Y 1 A PHE 572  ? CB  ? A PHE 572  CB  
167 1 Y 1 A PHE 572  ? CG  ? A PHE 572  CG  
168 1 Y 1 A PHE 572  ? CD1 ? A PHE 572  CD1 
169 1 Y 1 A PHE 572  ? CD2 ? A PHE 572  CD2 
170 1 Y 1 A PHE 572  ? CE1 ? A PHE 572  CE1 
171 1 Y 1 A PHE 572  ? CE2 ? A PHE 572  CE2 
172 1 Y 1 A PHE 572  ? CZ  ? A PHE 572  CZ  
173 1 Y 1 A ASP 573  ? CB  ? A ASP 573  CB  
174 1 Y 1 A ASP 573  ? CG  ? A ASP 573  CG  
175 1 Y 1 A ASP 573  ? OD1 ? A ASP 573  OD1 
176 1 Y 1 A ASP 573  ? OD2 ? A ASP 573  OD2 
177 1 Y 1 A PHE 574  ? CG  ? A PHE 574  CG  
178 1 Y 1 A PHE 574  ? CD1 ? A PHE 574  CD1 
179 1 Y 1 A PHE 574  ? CD2 ? A PHE 574  CD2 
180 1 Y 1 A PHE 574  ? CE1 ? A PHE 574  CE1 
181 1 Y 1 A PHE 574  ? CE2 ? A PHE 574  CE2 
182 1 Y 1 A PHE 574  ? CZ  ? A PHE 574  CZ  
183 1 Y 1 A SER 576  ? OG  ? A SER 576  OG  
184 1 Y 1 A GLU 578  ? CG  ? A GLU 578  CG  
185 1 Y 1 A GLU 578  ? CD  ? A GLU 578  CD  
186 1 Y 1 A GLU 578  ? OE1 ? A GLU 578  OE1 
187 1 Y 1 A GLU 578  ? OE2 ? A GLU 578  OE2 
188 1 Y 1 A SER 579  ? CB  ? A SER 579  CB  
189 1 Y 1 A SER 579  ? OG  ? A SER 579  OG  
190 1 Y 1 A SER 580  ? CB  ? A SER 580  CB  
191 1 Y 1 A SER 580  ? OG  ? A SER 580  OG  
192 1 Y 1 A SER 583  ? CB  ? A SER 583  CB  
193 1 Y 1 A SER 583  ? OG  ? A SER 583  OG  
194 1 Y 1 A ASN 588  ? CG  ? A ASN 588  CG  
195 1 Y 1 A ASN 588  ? OD1 ? A ASN 588  OD1 
196 1 Y 1 A ASN 588  ? ND2 ? A ASN 588  ND2 
197 1 Y 1 A SER 594  ? OG  ? A SER 594  OG  
198 1 Y 1 A THR 600  ? OG1 ? A THR 600  OG1 
199 1 Y 1 A THR 600  ? CG2 ? A THR 600  CG2 
200 1 Y 1 A LYS 631  ? CG  ? A LYS 631  CG  
201 1 Y 1 A LYS 631  ? CD  ? A LYS 631  CD  
202 1 Y 1 A LYS 631  ? CE  ? A LYS 631  CE  
203 1 Y 1 A LYS 631  ? NZ  ? A LYS 631  NZ  
204 1 Y 1 A ASN 633  ? CG  ? A ASN 633  CG  
205 1 Y 1 A ASN 633  ? OD1 ? A ASN 633  OD1 
206 1 Y 1 A ASN 633  ? ND2 ? A ASN 633  ND2 
207 1 Y 1 A GLN 639  ? CG  ? A GLN 639  CG  
208 1 Y 1 A GLN 639  ? CD  ? A GLN 639  CD  
209 1 Y 1 A GLN 639  ? OE1 ? A GLN 639  OE1 
210 1 Y 1 A GLN 639  ? NE2 ? A GLN 639  NE2 
211 1 Y 1 A LYS 647  ? CG  ? A LYS 647  CG  
212 1 Y 1 A LYS 647  ? CD  ? A LYS 647  CD  
213 1 Y 1 A LYS 647  ? CE  ? A LYS 647  CE  
214 1 Y 1 A LYS 647  ? NZ  ? A LYS 647  NZ  
215 1 Y 1 A ASN 648  ? CG  ? A ASN 648  CG  
216 1 Y 1 A ASN 648  ? OD1 ? A ASN 648  OD1 
217 1 Y 1 A ASN 648  ? ND2 ? A ASN 648  ND2 
218 1 Y 1 A ASN 649  ? CG  ? A ASN 649  CG  
219 1 Y 1 A ASN 649  ? OD1 ? A ASN 649  OD1 
220 1 Y 1 A ASN 649  ? ND2 ? A ASN 649  ND2 
221 1 Y 1 A GLU 670  ? CG  ? A GLU 670  CG  
222 1 Y 1 A GLU 670  ? CD  ? A GLU 670  CD  
223 1 Y 1 A GLU 670  ? OE1 ? A GLU 670  OE1 
224 1 Y 1 A GLU 670  ? OE2 ? A GLU 670  OE2 
225 1 Y 1 A LYS 709  ? CG  ? A LYS 709  CG  
226 1 Y 1 A LYS 709  ? CD  ? A LYS 709  CD  
227 1 Y 1 A LYS 709  ? CE  ? A LYS 709  CE  
228 1 Y 1 A LYS 709  ? NZ  ? A LYS 709  NZ  
229 1 Y 1 A ASP 755  ? CG  ? A ASP 755  CG  
230 1 Y 1 A ASP 755  ? OD1 ? A ASP 755  OD1 
231 1 Y 1 A ASP 755  ? OD2 ? A ASP 755  OD2 
232 1 Y 1 A GLU 781  ? CG  ? A GLU 781  CG  
233 1 Y 1 A GLU 781  ? CD  ? A GLU 781  CD  
234 1 Y 1 A GLU 781  ? OE1 ? A GLU 781  OE1 
235 1 Y 1 A GLU 781  ? OE2 ? A GLU 781  OE2 
236 1 Y 1 A ARG 829  ? CG  ? A ARG 829  CG  
237 1 Y 1 A ARG 829  ? CD  ? A ARG 829  CD  
238 1 Y 1 A ARG 829  ? NE  ? A ARG 829  NE  
239 1 Y 1 A ARG 829  ? CZ  ? A ARG 829  CZ  
240 1 Y 1 A ARG 829  ? NH1 ? A ARG 829  NH1 
241 1 Y 1 A ARG 829  ? NH2 ? A ARG 829  NH2 
242 1 Y 1 A GLN 830  ? CG  ? A GLN 830  CG  
243 1 Y 1 A GLN 830  ? CD  ? A GLN 830  CD  
244 1 Y 1 A GLN 830  ? OE1 ? A GLN 830  OE1 
245 1 Y 1 A GLN 830  ? NE2 ? A GLN 830  NE2 
246 1 Y 1 A LYS 833  ? CG  ? A LYS 833  CG  
247 1 Y 1 A LYS 833  ? CD  ? A LYS 833  CD  
248 1 Y 1 A LYS 833  ? CE  ? A LYS 833  CE  
249 1 Y 1 A LYS 833  ? NZ  ? A LYS 833  NZ  
250 1 Y 1 A ARG 844  ? CG  ? A ARG 844  CG  
251 1 Y 1 A ARG 844  ? CD  ? A ARG 844  CD  
252 1 Y 1 A ARG 844  ? NE  ? A ARG 844  NE  
253 1 Y 1 A ARG 844  ? CZ  ? A ARG 844  CZ  
254 1 Y 1 A ARG 844  ? NH1 ? A ARG 844  NH1 
255 1 Y 1 A ARG 844  ? NH2 ? A ARG 844  NH2 
256 1 Y 1 A LYS 848  ? CG  ? A LYS 848  CG  
257 1 Y 1 A LYS 848  ? CD  ? A LYS 848  CD  
258 1 Y 1 A LYS 848  ? CE  ? A LYS 848  CE  
259 1 Y 1 A LYS 848  ? NZ  ? A LYS 848  NZ  
260 1 Y 1 A GLN 894  ? CG  ? A GLN 894  CG  
261 1 Y 1 A GLN 894  ? CD  ? A GLN 894  CD  
262 1 Y 1 A GLN 894  ? OE1 ? A GLN 894  OE1 
263 1 Y 1 A GLN 894  ? NE2 ? A GLN 894  NE2 
264 1 Y 1 A ASP 896  ? CG  ? A ASP 896  CG  
265 1 Y 1 A ASP 896  ? OD1 ? A ASP 896  OD1 
266 1 Y 1 A ASP 896  ? OD2 ? A ASP 896  OD2 
267 1 Y 1 A ASP 899  ? CG  ? A ASP 899  CG  
268 1 Y 1 A ASP 899  ? OD1 ? A ASP 899  OD1 
269 1 Y 1 A ASP 899  ? OD2 ? A ASP 899  OD2 
270 1 Y 1 A LYS 923  ? CG  ? A LYS 923  CG  
271 1 Y 1 A LYS 923  ? CD  ? A LYS 923  CD  
272 1 Y 1 A LYS 923  ? CE  ? A LYS 923  CE  
273 1 Y 1 A LYS 923  ? NZ  ? A LYS 923  NZ  
274 1 Y 1 A LEU 926  ? CG  ? A LEU 926  CG  
275 1 Y 1 A LEU 926  ? CD1 ? A LEU 926  CD1 
276 1 Y 1 A LEU 926  ? CD2 ? A LEU 926  CD2 
277 1 Y 1 A ASN 1022 ? CG  ? A ASN 1022 CG  
278 1 Y 1 A ASN 1022 ? OD1 ? A ASN 1022 OD1 
279 1 Y 1 A ASN 1022 ? ND2 ? A ASN 1022 ND2 
280 1 Y 1 A LYS 1047 ? CG  ? A LYS 1047 CG  
281 1 Y 1 A LYS 1047 ? CD  ? A LYS 1047 CD  
282 1 Y 1 A LYS 1047 ? CE  ? A LYS 1047 CE  
283 1 Y 1 A LYS 1047 ? NZ  ? A LYS 1047 NZ  
284 1 Y 1 A ASP 1051 ? CG  ? A ASP 1051 CG  
285 1 Y 1 A ASP 1051 ? OD1 ? A ASP 1051 OD1 
286 1 Y 1 A ASP 1051 ? OD2 ? A ASP 1051 OD2 
287 1 Y 1 A ASN 1063 ? CG  ? A ASN 1063 CG  
288 1 Y 1 A ASN 1063 ? OD1 ? A ASN 1063 OD1 
289 1 Y 1 A ASN 1063 ? ND2 ? A ASN 1063 ND2 
290 1 Y 1 A ASP 1082 ? CG  ? A ASP 1082 CG  
291 1 Y 1 A ASP 1082 ? OD1 ? A ASP 1082 OD1 
292 1 Y 1 A ASP 1082 ? OD2 ? A ASP 1082 OD2 
293 1 Y 1 A ASP 1085 ? CG  ? A ASP 1085 CG  
294 1 Y 1 A ASP 1085 ? OD1 ? A ASP 1085 OD1 
295 1 Y 1 A ASP 1085 ? OD2 ? A ASP 1085 OD2 
296 1 Y 1 A ASP 1091 ? CG  ? A ASP 1091 CG  
297 1 Y 1 A ASP 1091 ? OD1 ? A ASP 1091 OD1 
298 1 Y 1 A ASP 1091 ? OD2 ? A ASP 1091 OD2 
299 1 Y 1 A LYS 1098 ? CG  ? A LYS 1098 CG  
300 1 Y 1 A LYS 1098 ? CD  ? A LYS 1098 CD  
301 1 Y 1 A LYS 1098 ? CE  ? A LYS 1098 CE  
302 1 Y 1 A LYS 1098 ? NZ  ? A LYS 1098 NZ  
303 1 Y 1 A GLU 1099 ? CG  ? A GLU 1099 CG  
304 1 Y 1 A GLU 1099 ? CD  ? A GLU 1099 CD  
305 1 Y 1 A GLU 1099 ? OE1 ? A GLU 1099 OE1 
306 1 Y 1 A GLU 1099 ? OE2 ? A GLU 1099 OE2 
307 1 Y 1 A GLU 1105 ? CG  ? A GLU 1105 CG  
308 1 Y 1 A GLU 1105 ? CD  ? A GLU 1105 CD  
309 1 Y 1 A GLU 1105 ? OE1 ? A GLU 1105 OE1 
310 1 Y 1 A GLU 1105 ? OE2 ? A GLU 1105 OE2 
311 1 Y 1 A GLU 1106 ? CG  ? A GLU 1106 CG  
312 1 Y 1 A GLU 1106 ? CD  ? A GLU 1106 CD  
313 1 Y 1 A GLU 1106 ? OE1 ? A GLU 1106 OE1 
314 1 Y 1 A GLU 1106 ? OE2 ? A GLU 1106 OE2 
315 1 Y 1 A GLU 1109 ? CG  ? A GLU 1109 CG  
316 1 Y 1 A GLU 1109 ? CD  ? A GLU 1109 CD  
317 1 Y 1 A GLU 1109 ? OE1 ? A GLU 1109 OE1 
318 1 Y 1 A GLU 1109 ? OE2 ? A GLU 1109 OE2 
319 1 Y 1 A ASP 1116 ? CG  ? A ASP 1116 CG  
320 1 Y 1 A ASP 1116 ? OD1 ? A ASP 1116 OD1 
321 1 Y 1 A ASP 1116 ? OD2 ? A ASP 1116 OD2 
322 1 Y 1 A ASP 1117 ? CG  ? A ASP 1117 CG  
323 1 Y 1 A ASP 1117 ? OD1 ? A ASP 1117 OD1 
324 1 Y 1 A ASP 1117 ? OD2 ? A ASP 1117 OD2 
325 1 Y 1 A GLU 1119 ? CG  ? A GLU 1119 CG  
326 1 Y 1 A GLU 1119 ? CD  ? A GLU 1119 CD  
327 1 Y 1 A GLU 1119 ? OE1 ? A GLU 1119 OE1 
328 1 Y 1 A GLU 1119 ? OE2 ? A GLU 1119 OE2 
329 1 Y 1 A GLN 1120 ? CG  ? A GLN 1120 CG  
330 1 Y 1 A GLN 1120 ? CD  ? A GLN 1120 CD  
331 1 Y 1 A GLN 1120 ? OE1 ? A GLN 1120 OE1 
332 1 Y 1 A GLN 1120 ? NE2 ? A GLN 1120 NE2 
333 1 Y 1 A ILE 1122 ? CG1 ? A ILE 1122 CG1 
334 1 Y 1 A ILE 1122 ? CG2 ? A ILE 1122 CG2 
335 1 Y 1 A ILE 1122 ? CD1 ? A ILE 1122 CD1 
336 1 Y 1 A ASP 1124 ? CG  ? A ASP 1124 CG  
337 1 Y 1 A ASP 1124 ? OD1 ? A ASP 1124 OD1 
338 1 Y 1 A ASP 1124 ? OD2 ? A ASP 1124 OD2 
339 1 Y 1 A LYS 1127 ? CG  ? A LYS 1127 CG  
340 1 Y 1 A LYS 1127 ? CD  ? A LYS 1127 CD  
341 1 Y 1 A LYS 1127 ? CE  ? A LYS 1127 CE  
342 1 Y 1 A LYS 1127 ? NZ  ? A LYS 1127 NZ  
343 1 Y 1 A GLU 1128 ? CG  ? A GLU 1128 CG  
344 1 Y 1 A GLU 1128 ? CD  ? A GLU 1128 CD  
345 1 Y 1 A GLU 1128 ? OE1 ? A GLU 1128 OE1 
346 1 Y 1 A GLU 1128 ? OE2 ? A GLU 1128 OE2 
347 1 Y 1 A GLU 1130 ? CG  ? A GLU 1130 CG  
348 1 Y 1 A GLU 1130 ? CD  ? A GLU 1130 CD  
349 1 Y 1 A GLU 1130 ? OE1 ? A GLU 1130 OE1 
350 1 Y 1 A GLU 1130 ? OE2 ? A GLU 1130 OE2 
351 1 Y 1 A ASP 1136 ? CG  ? A ASP 1136 CG  
352 1 Y 1 A ASP 1136 ? OD1 ? A ASP 1136 OD1 
353 1 Y 1 A ASP 1136 ? OD2 ? A ASP 1136 OD2 
354 1 Y 1 A ASN 1137 ? CG  ? A ASN 1137 CG  
355 1 Y 1 A ASN 1137 ? OD1 ? A ASN 1137 OD1 
356 1 Y 1 A ASN 1137 ? ND2 ? A ASN 1137 ND2 
357 1 Y 1 A LEU 1139 ? CG  ? A LEU 1139 CG  
358 1 Y 1 A LEU 1139 ? CD1 ? A LEU 1139 CD1 
359 1 Y 1 A LEU 1139 ? CD2 ? A LEU 1139 CD2 
360 1 Y 1 A GLU 1140 ? CG  ? A GLU 1140 CG  
361 1 Y 1 A GLU 1140 ? CD  ? A GLU 1140 CD  
362 1 Y 1 A GLU 1140 ? OE1 ? A GLU 1140 OE1 
363 1 Y 1 A GLU 1140 ? OE2 ? A GLU 1140 OE2 
364 1 Y 1 A LYS 1143 ? CG  ? A LYS 1143 CG  
365 1 Y 1 A LYS 1143 ? CD  ? A LYS 1143 CD  
366 1 Y 1 A LYS 1143 ? CE  ? A LYS 1143 CE  
367 1 Y 1 A LYS 1143 ? NZ  ? A LYS 1143 NZ  
368 1 Y 1 B HIS 229  ? CB  ? B HIS 229  CB  
369 1 Y 1 B HIS 229  ? CG  ? B HIS 229  CG  
370 1 Y 1 B HIS 229  ? ND1 ? B HIS 229  ND1 
371 1 Y 1 B HIS 229  ? CD2 ? B HIS 229  CD2 
372 1 Y 1 B HIS 229  ? CE1 ? B HIS 229  CE1 
373 1 Y 1 B HIS 229  ? NE2 ? B HIS 229  NE2 
374 1 Y 1 B ALA 231  ? CB  ? B ALA 231  CB  
375 1 Y 1 B GLN 233  ? CG  ? B GLN 233  CG  
376 1 Y 1 B GLN 233  ? CD  ? B GLN 233  CD  
377 1 Y 1 B GLN 233  ? OE1 ? B GLN 233  OE1 
378 1 Y 1 B GLN 233  ? NE2 ? B GLN 233  NE2 
379 1 Y 1 B LEU 234  ? CB  ? B LEU 234  CB  
380 1 Y 1 B LEU 234  ? CG  ? B LEU 234  CG  
381 1 Y 1 B LEU 234  ? CD1 ? B LEU 234  CD1 
382 1 Y 1 B LEU 234  ? CD2 ? B LEU 234  CD2 
383 1 Y 1 B GLU 236  ? CB  ? B GLU 236  CB  
384 1 Y 1 B GLU 236  ? CG  ? B GLU 236  CG  
385 1 Y 1 B GLU 236  ? CD  ? B GLU 236  CD  
386 1 Y 1 B GLU 236  ? OE1 ? B GLU 236  OE1 
387 1 Y 1 B GLU 236  ? OE2 ? B GLU 236  OE2 
388 1 Y 1 B LYS 237  ? CB  ? B LYS 237  CB  
389 1 Y 1 B LYS 237  ? CG  ? B LYS 237  CG  
390 1 Y 1 B LYS 237  ? CD  ? B LYS 237  CD  
391 1 Y 1 B LYS 237  ? CE  ? B LYS 237  CE  
392 1 Y 1 B LYS 237  ? NZ  ? B LYS 237  NZ  
393 1 Y 1 B LEU 238  ? CB  ? B LEU 238  CB  
394 1 Y 1 B LEU 238  ? CG  ? B LEU 238  CG  
395 1 Y 1 B LEU 238  ? CD1 ? B LEU 238  CD1 
396 1 Y 1 B LEU 238  ? CD2 ? B LEU 238  CD2 
397 1 Y 1 B LEU 250  ? CG  ? B LEU 250  CG  
398 1 Y 1 B LEU 250  ? CD1 ? B LEU 250  CD1 
399 1 Y 1 B LEU 250  ? CD2 ? B LEU 250  CD2 
400 1 Y 1 B MET 325  ? CG  ? B MET 325  CG  
401 1 Y 1 B MET 325  ? SD  ? B MET 325  SD  
402 1 Y 1 B MET 325  ? CE  ? B MET 325  CE  
403 1 Y 1 B GLU 393  ? CG  ? B GLU 393  CG  
404 1 Y 1 B GLU 393  ? CD  ? B GLU 393  CD  
405 1 Y 1 B GLU 393  ? OE1 ? B GLU 393  OE1 
406 1 Y 1 B GLU 393  ? OE2 ? B GLU 393  OE2 
407 1 Y 1 B LYS 396  ? CG  ? B LYS 396  CG  
408 1 Y 1 B LYS 396  ? CD  ? B LYS 396  CD  
409 1 Y 1 B LYS 396  ? CE  ? B LYS 396  CE  
410 1 Y 1 B LYS 396  ? NZ  ? B LYS 396  NZ  
411 1 Y 1 B GLU 397  ? CG  ? B GLU 397  CG  
412 1 Y 1 B GLU 397  ? CD  ? B GLU 397  CD  
413 1 Y 1 B GLU 397  ? OE1 ? B GLU 397  OE1 
414 1 Y 1 B GLU 397  ? OE2 ? B GLU 397  OE2 
415 1 Y 1 B ILE 400  ? CG1 ? B ILE 400  CG1 
416 1 Y 1 B ILE 400  ? CG2 ? B ILE 400  CG2 
417 1 Y 1 B ILE 400  ? CD1 ? B ILE 400  CD1 
418 1 Y 1 B LEU 401  ? CG  ? B LEU 401  CG  
419 1 Y 1 B LEU 401  ? CD1 ? B LEU 401  CD1 
420 1 Y 1 B LEU 401  ? CD2 ? B LEU 401  CD2 
421 1 Y 1 B MET 402  ? CG  ? B MET 402  CG  
422 1 Y 1 B MET 402  ? SD  ? B MET 402  SD  
423 1 Y 1 B MET 402  ? CE  ? B MET 402  CE  
424 1 Y 1 B ILE 403  ? CG1 ? B ILE 403  CG1 
425 1 Y 1 B ILE 403  ? CG2 ? B ILE 403  CG2 
426 1 Y 1 B ILE 403  ? CD1 ? B ILE 403  CD1 
427 1 Y 1 B ASP 404  ? CG  ? B ASP 404  CG  
428 1 Y 1 B ASP 404  ? OD1 ? B ASP 404  OD1 
429 1 Y 1 B ASP 404  ? OD2 ? B ASP 404  OD2 
430 1 Y 1 B GLU 405  ? CG  ? B GLU 405  CG  
431 1 Y 1 B GLU 405  ? CD  ? B GLU 405  CD  
432 1 Y 1 B GLU 405  ? OE1 ? B GLU 405  OE1 
433 1 Y 1 B GLU 405  ? OE2 ? B GLU 405  OE2 
434 1 Y 1 B ILE 406  ? CG1 ? B ILE 406  CG1 
435 1 Y 1 B ILE 406  ? CG2 ? B ILE 406  CG2 
436 1 Y 1 B ILE 406  ? CD1 ? B ILE 406  CD1 
437 1 Y 1 B ASP 408  ? CG  ? B ASP 408  CG  
438 1 Y 1 B ASP 408  ? OD1 ? B ASP 408  OD1 
439 1 Y 1 B ASP 408  ? OD2 ? B ASP 408  OD2 
440 1 Y 1 B GLU 429  ? CG  ? B GLU 429  CG  
441 1 Y 1 B GLU 429  ? CD  ? B GLU 429  CD  
442 1 Y 1 B GLU 429  ? OE1 ? B GLU 429  OE1 
443 1 Y 1 B GLU 429  ? OE2 ? B GLU 429  OE2 
444 1 Y 1 B ILE 451  ? CG1 ? B ILE 451  CG1 
445 1 Y 1 B ILE 451  ? CG2 ? B ILE 451  CG2 
446 1 Y 1 B ILE 451  ? CD1 ? B ILE 451  CD1 
447 1 Y 1 B ILE 455  ? CG1 ? B ILE 455  CG1 
448 1 Y 1 B ILE 455  ? CG2 ? B ILE 455  CG2 
449 1 Y 1 B ILE 455  ? CD1 ? B ILE 455  CD1 
450 1 Y 1 B LEU 457  ? CG  ? B LEU 457  CG  
451 1 Y 1 B LEU 457  ? CD1 ? B LEU 457  CD1 
452 1 Y 1 B LEU 457  ? CD2 ? B LEU 457  CD2 
453 1 Y 1 B GLU 458  ? CG  ? B GLU 458  CG  
454 1 Y 1 B GLU 458  ? CD  ? B GLU 458  CD  
455 1 Y 1 B GLU 458  ? OE1 ? B GLU 458  OE1 
456 1 Y 1 B GLU 458  ? OE2 ? B GLU 458  OE2 
457 1 Y 1 B LYS 461  ? CG  ? B LYS 461  CG  
458 1 Y 1 B LYS 461  ? CD  ? B LYS 461  CD  
459 1 Y 1 B LYS 461  ? CE  ? B LYS 461  CE  
460 1 Y 1 B LYS 461  ? NZ  ? B LYS 461  NZ  
461 1 Y 1 B GLU 475  ? CG  ? B GLU 475  CG  
462 1 Y 1 B GLU 475  ? CD  ? B GLU 475  CD  
463 1 Y 1 B GLU 475  ? OE1 ? B GLU 475  OE1 
464 1 Y 1 B GLU 475  ? OE2 ? B GLU 475  OE2 
465 1 Y 1 B GLU 483  ? CG  ? B GLU 483  CG  
466 1 Y 1 B GLU 483  ? CD  ? B GLU 483  CD  
467 1 Y 1 B GLU 483  ? OE1 ? B GLU 483  OE1 
468 1 Y 1 B GLU 483  ? OE2 ? B GLU 483  OE2 
469 1 Y 1 B GLU 484  ? CG  ? B GLU 484  CG  
470 1 Y 1 B GLU 484  ? CD  ? B GLU 484  CD  
471 1 Y 1 B GLU 484  ? OE1 ? B GLU 484  OE1 
472 1 Y 1 B GLU 484  ? OE2 ? B GLU 484  OE2 
473 1 Y 1 B ASP 547  ? CG  ? B ASP 547  CG  
474 1 Y 1 B ASP 547  ? OD1 ? B ASP 547  OD1 
475 1 Y 1 B ASP 547  ? OD2 ? B ASP 547  OD2 
476 1 Y 1 B THR 549  ? OG1 ? B THR 549  OG1 
477 1 Y 1 B THR 549  ? CG2 ? B THR 549  CG2 
478 1 Y 1 B ASN 551  ? CB  ? B ASN 551  CB  
479 1 Y 1 B ASN 551  ? CG  ? B ASN 551  CG  
480 1 Y 1 B ASN 551  ? OD1 ? B ASN 551  OD1 
481 1 Y 1 B ASN 551  ? ND2 ? B ASN 551  ND2 
482 1 Y 1 B VAL 552  ? CB  ? B VAL 552  CB  
483 1 Y 1 B VAL 552  ? CG1 ? B VAL 552  CG1 
484 1 Y 1 B VAL 552  ? CG2 ? B VAL 552  CG2 
485 1 Y 1 B ASP 554  ? CB  ? B ASP 554  CB  
486 1 Y 1 B ASP 554  ? CG  ? B ASP 554  CG  
487 1 Y 1 B ASP 554  ? OD1 ? B ASP 554  OD1 
488 1 Y 1 B ASP 554  ? OD2 ? B ASP 554  OD2 
489 1 Y 1 B THR 555  ? CB  ? B THR 555  CB  
490 1 Y 1 B THR 555  ? OG1 ? B THR 555  OG1 
491 1 Y 1 B THR 555  ? CG2 ? B THR 555  CG2 
492 1 Y 1 B ILE 556  ? CB  ? B ILE 556  CB  
493 1 Y 1 B ILE 556  ? CG1 ? B ILE 556  CG1 
494 1 Y 1 B ILE 556  ? CG2 ? B ILE 556  CG2 
495 1 Y 1 B ILE 556  ? CD1 ? B ILE 556  CD1 
496 1 Y 1 B VAL 557  ? CB  ? B VAL 557  CB  
497 1 Y 1 B VAL 557  ? CG1 ? B VAL 557  CG1 
498 1 Y 1 B VAL 557  ? CG2 ? B VAL 557  CG2 
499 1 Y 1 B THR 558  ? CB  ? B THR 558  CB  
500 1 Y 1 B THR 558  ? OG1 ? B THR 558  OG1 
501 1 Y 1 B THR 558  ? CG2 ? B THR 558  CG2 
502 1 Y 1 B GLU 559  ? CB  ? B GLU 559  CB  
503 1 Y 1 B GLU 559  ? CG  ? B GLU 559  CG  
504 1 Y 1 B GLU 559  ? CD  ? B GLU 559  CD  
505 1 Y 1 B GLU 559  ? OE1 ? B GLU 559  OE1 
506 1 Y 1 B GLU 559  ? OE2 ? B GLU 559  OE2 
507 1 Y 1 B LEU 560  ? CB  ? B LEU 560  CB  
508 1 Y 1 B LEU 560  ? CG  ? B LEU 560  CG  
509 1 Y 1 B LEU 560  ? CD1 ? B LEU 560  CD1 
510 1 Y 1 B LEU 560  ? CD2 ? B LEU 560  CD2 
511 1 Y 1 B THR 561  ? CB  ? B THR 561  CB  
512 1 Y 1 B THR 561  ? OG1 ? B THR 561  OG1 
513 1 Y 1 B THR 561  ? CG2 ? B THR 561  CG2 
514 1 Y 1 B THR 564  ? CB  ? B THR 564  CB  
515 1 Y 1 B THR 564  ? OG1 ? B THR 564  OG1 
516 1 Y 1 B THR 564  ? CG2 ? B THR 564  CG2 
517 1 Y 1 B SER 565  ? CB  ? B SER 565  CB  
518 1 Y 1 B SER 565  ? OG  ? B SER 565  OG  
519 1 Y 1 B ALA 566  ? CB  ? B ALA 566  CB  
520 1 Y 1 B LYS 569  ? CB  ? B LYS 569  CB  
521 1 Y 1 B LYS 569  ? CG  ? B LYS 569  CG  
522 1 Y 1 B LYS 569  ? CD  ? B LYS 569  CD  
523 1 Y 1 B LYS 569  ? CE  ? B LYS 569  CE  
524 1 Y 1 B LYS 569  ? NZ  ? B LYS 569  NZ  
525 1 Y 1 B LEU 570  ? CB  ? B LEU 570  CB  
526 1 Y 1 B LEU 570  ? CG  ? B LEU 570  CG  
527 1 Y 1 B LEU 570  ? CD1 ? B LEU 570  CD1 
528 1 Y 1 B LEU 570  ? CD2 ? B LEU 570  CD2 
529 1 Y 1 B ASN 571  ? CB  ? B ASN 571  CB  
530 1 Y 1 B ASN 571  ? CG  ? B ASN 571  CG  
531 1 Y 1 B ASN 571  ? OD1 ? B ASN 571  OD1 
532 1 Y 1 B ASN 571  ? ND2 ? B ASN 571  ND2 
533 1 Y 1 B PHE 572  ? CB  ? B PHE 572  CB  
534 1 Y 1 B PHE 572  ? CG  ? B PHE 572  CG  
535 1 Y 1 B PHE 572  ? CD1 ? B PHE 572  CD1 
536 1 Y 1 B PHE 572  ? CD2 ? B PHE 572  CD2 
537 1 Y 1 B PHE 572  ? CE1 ? B PHE 572  CE1 
538 1 Y 1 B PHE 572  ? CE2 ? B PHE 572  CE2 
539 1 Y 1 B PHE 572  ? CZ  ? B PHE 572  CZ  
540 1 Y 1 B ASP 573  ? CB  ? B ASP 573  CB  
541 1 Y 1 B ASP 573  ? CG  ? B ASP 573  CG  
542 1 Y 1 B ASP 573  ? OD1 ? B ASP 573  OD1 
543 1 Y 1 B ASP 573  ? OD2 ? B ASP 573  OD2 
544 1 Y 1 B PHE 574  ? CG  ? B PHE 574  CG  
545 1 Y 1 B PHE 574  ? CD1 ? B PHE 574  CD1 
546 1 Y 1 B PHE 574  ? CD2 ? B PHE 574  CD2 
547 1 Y 1 B PHE 574  ? CE1 ? B PHE 574  CE1 
548 1 Y 1 B PHE 574  ? CE2 ? B PHE 574  CE2 
549 1 Y 1 B PHE 574  ? CZ  ? B PHE 574  CZ  
550 1 Y 1 B SER 576  ? OG  ? B SER 576  OG  
551 1 Y 1 B GLU 578  ? CG  ? B GLU 578  CG  
552 1 Y 1 B GLU 578  ? CD  ? B GLU 578  CD  
553 1 Y 1 B GLU 578  ? OE1 ? B GLU 578  OE1 
554 1 Y 1 B GLU 578  ? OE2 ? B GLU 578  OE2 
555 1 Y 1 B SER 579  ? CB  ? B SER 579  CB  
556 1 Y 1 B SER 579  ? OG  ? B SER 579  OG  
557 1 Y 1 B SER 580  ? CB  ? B SER 580  CB  
558 1 Y 1 B SER 580  ? OG  ? B SER 580  OG  
559 1 Y 1 B SER 583  ? CB  ? B SER 583  CB  
560 1 Y 1 B SER 583  ? OG  ? B SER 583  OG  
561 1 Y 1 B ASN 588  ? CG  ? B ASN 588  CG  
562 1 Y 1 B ASN 588  ? OD1 ? B ASN 588  OD1 
563 1 Y 1 B ASN 588  ? ND2 ? B ASN 588  ND2 
564 1 Y 1 B SER 594  ? OG  ? B SER 594  OG  
565 1 Y 1 B THR 600  ? OG1 ? B THR 600  OG1 
566 1 Y 1 B THR 600  ? CG2 ? B THR 600  CG2 
567 1 Y 1 B LYS 631  ? CG  ? B LYS 631  CG  
568 1 Y 1 B LYS 631  ? CD  ? B LYS 631  CD  
569 1 Y 1 B LYS 631  ? CE  ? B LYS 631  CE  
570 1 Y 1 B LYS 631  ? NZ  ? B LYS 631  NZ  
571 1 Y 1 B ASN 633  ? CG  ? B ASN 633  CG  
572 1 Y 1 B ASN 633  ? OD1 ? B ASN 633  OD1 
573 1 Y 1 B ASN 633  ? ND2 ? B ASN 633  ND2 
574 1 Y 1 B GLN 639  ? CG  ? B GLN 639  CG  
575 1 Y 1 B GLN 639  ? CD  ? B GLN 639  CD  
576 1 Y 1 B GLN 639  ? OE1 ? B GLN 639  OE1 
577 1 Y 1 B GLN 639  ? NE2 ? B GLN 639  NE2 
578 1 Y 1 B LYS 647  ? CG  ? B LYS 647  CG  
579 1 Y 1 B LYS 647  ? CD  ? B LYS 647  CD  
580 1 Y 1 B LYS 647  ? CE  ? B LYS 647  CE  
581 1 Y 1 B LYS 647  ? NZ  ? B LYS 647  NZ  
582 1 Y 1 B ASN 648  ? CG  ? B ASN 648  CG  
583 1 Y 1 B ASN 648  ? OD1 ? B ASN 648  OD1 
584 1 Y 1 B ASN 648  ? ND2 ? B ASN 648  ND2 
585 1 Y 1 B ASN 649  ? CG  ? B ASN 649  CG  
586 1 Y 1 B ASN 649  ? OD1 ? B ASN 649  OD1 
587 1 Y 1 B ASN 649  ? ND2 ? B ASN 649  ND2 
588 1 Y 1 B GLU 670  ? CG  ? B GLU 670  CG  
589 1 Y 1 B GLU 670  ? CD  ? B GLU 670  CD  
590 1 Y 1 B GLU 670  ? OE1 ? B GLU 670  OE1 
591 1 Y 1 B GLU 670  ? OE2 ? B GLU 670  OE2 
592 1 Y 1 B LYS 709  ? CG  ? B LYS 709  CG  
593 1 Y 1 B LYS 709  ? CD  ? B LYS 709  CD  
594 1 Y 1 B LYS 709  ? CE  ? B LYS 709  CE  
595 1 Y 1 B LYS 709  ? NZ  ? B LYS 709  NZ  
596 1 Y 1 B ASP 755  ? CG  ? B ASP 755  CG  
597 1 Y 1 B ASP 755  ? OD1 ? B ASP 755  OD1 
598 1 Y 1 B ASP 755  ? OD2 ? B ASP 755  OD2 
599 1 Y 1 B GLU 781  ? CG  ? B GLU 781  CG  
600 1 Y 1 B GLU 781  ? CD  ? B GLU 781  CD  
601 1 Y 1 B GLU 781  ? OE1 ? B GLU 781  OE1 
602 1 Y 1 B GLU 781  ? OE2 ? B GLU 781  OE2 
603 1 Y 1 B ARG 829  ? CG  ? B ARG 829  CG  
604 1 Y 1 B ARG 829  ? CD  ? B ARG 829  CD  
605 1 Y 1 B ARG 829  ? NE  ? B ARG 829  NE  
606 1 Y 1 B ARG 829  ? CZ  ? B ARG 829  CZ  
607 1 Y 1 B ARG 829  ? NH1 ? B ARG 829  NH1 
608 1 Y 1 B ARG 829  ? NH2 ? B ARG 829  NH2 
609 1 Y 1 B GLN 830  ? CG  ? B GLN 830  CG  
610 1 Y 1 B GLN 830  ? CD  ? B GLN 830  CD  
611 1 Y 1 B GLN 830  ? OE1 ? B GLN 830  OE1 
612 1 Y 1 B GLN 830  ? NE2 ? B GLN 830  NE2 
613 1 Y 1 B LYS 833  ? CG  ? B LYS 833  CG  
614 1 Y 1 B LYS 833  ? CD  ? B LYS 833  CD  
615 1 Y 1 B LYS 833  ? CE  ? B LYS 833  CE  
616 1 Y 1 B LYS 833  ? NZ  ? B LYS 833  NZ  
617 1 Y 1 B ARG 844  ? CG  ? B ARG 844  CG  
618 1 Y 1 B ARG 844  ? CD  ? B ARG 844  CD  
619 1 Y 1 B ARG 844  ? NE  ? B ARG 844  NE  
620 1 Y 1 B ARG 844  ? CZ  ? B ARG 844  CZ  
621 1 Y 1 B ARG 844  ? NH1 ? B ARG 844  NH1 
622 1 Y 1 B ARG 844  ? NH2 ? B ARG 844  NH2 
623 1 Y 1 B LYS 848  ? CG  ? B LYS 848  CG  
624 1 Y 1 B LYS 848  ? CD  ? B LYS 848  CD  
625 1 Y 1 B LYS 848  ? CE  ? B LYS 848  CE  
626 1 Y 1 B LYS 848  ? NZ  ? B LYS 848  NZ  
627 1 Y 1 B GLN 894  ? CG  ? B GLN 894  CG  
628 1 Y 1 B GLN 894  ? CD  ? B GLN 894  CD  
629 1 Y 1 B GLN 894  ? OE1 ? B GLN 894  OE1 
630 1 Y 1 B GLN 894  ? NE2 ? B GLN 894  NE2 
631 1 Y 1 B ASP 896  ? CG  ? B ASP 896  CG  
632 1 Y 1 B ASP 896  ? OD1 ? B ASP 896  OD1 
633 1 Y 1 B ASP 896  ? OD2 ? B ASP 896  OD2 
634 1 Y 1 B ASP 899  ? CG  ? B ASP 899  CG  
635 1 Y 1 B ASP 899  ? OD1 ? B ASP 899  OD1 
636 1 Y 1 B ASP 899  ? OD2 ? B ASP 899  OD2 
637 1 Y 1 B LYS 923  ? CG  ? B LYS 923  CG  
638 1 Y 1 B LYS 923  ? CD  ? B LYS 923  CD  
639 1 Y 1 B LYS 923  ? CE  ? B LYS 923  CE  
640 1 Y 1 B LYS 923  ? NZ  ? B LYS 923  NZ  
641 1 Y 1 B LEU 926  ? CG  ? B LEU 926  CG  
642 1 Y 1 B LEU 926  ? CD1 ? B LEU 926  CD1 
643 1 Y 1 B LEU 926  ? CD2 ? B LEU 926  CD2 
644 1 Y 1 B ASN 1022 ? CG  ? B ASN 1022 CG  
645 1 Y 1 B ASN 1022 ? OD1 ? B ASN 1022 OD1 
646 1 Y 1 B ASN 1022 ? ND2 ? B ASN 1022 ND2 
647 1 Y 1 B LYS 1047 ? CG  ? B LYS 1047 CG  
648 1 Y 1 B LYS 1047 ? CD  ? B LYS 1047 CD  
649 1 Y 1 B LYS 1047 ? CE  ? B LYS 1047 CE  
650 1 Y 1 B LYS 1047 ? NZ  ? B LYS 1047 NZ  
651 1 Y 1 B ASP 1051 ? CG  ? B ASP 1051 CG  
652 1 Y 1 B ASP 1051 ? OD1 ? B ASP 1051 OD1 
653 1 Y 1 B ASP 1051 ? OD2 ? B ASP 1051 OD2 
654 1 Y 1 B ASN 1063 ? CG  ? B ASN 1063 CG  
655 1 Y 1 B ASN 1063 ? OD1 ? B ASN 1063 OD1 
656 1 Y 1 B ASN 1063 ? ND2 ? B ASN 1063 ND2 
657 1 Y 1 B ASP 1082 ? CG  ? B ASP 1082 CG  
658 1 Y 1 B ASP 1082 ? OD1 ? B ASP 1082 OD1 
659 1 Y 1 B ASP 1082 ? OD2 ? B ASP 1082 OD2 
660 1 Y 1 B ASP 1085 ? CG  ? B ASP 1085 CG  
661 1 Y 1 B ASP 1085 ? OD1 ? B ASP 1085 OD1 
662 1 Y 1 B ASP 1085 ? OD2 ? B ASP 1085 OD2 
663 1 Y 1 B ASP 1091 ? CG  ? B ASP 1091 CG  
664 1 Y 1 B ASP 1091 ? OD1 ? B ASP 1091 OD1 
665 1 Y 1 B ASP 1091 ? OD2 ? B ASP 1091 OD2 
666 1 Y 1 B LYS 1098 ? CG  ? B LYS 1098 CG  
667 1 Y 1 B LYS 1098 ? CD  ? B LYS 1098 CD  
668 1 Y 1 B LYS 1098 ? CE  ? B LYS 1098 CE  
669 1 Y 1 B LYS 1098 ? NZ  ? B LYS 1098 NZ  
670 1 Y 1 B GLU 1099 ? CG  ? B GLU 1099 CG  
671 1 Y 1 B GLU 1099 ? CD  ? B GLU 1099 CD  
672 1 Y 1 B GLU 1099 ? OE1 ? B GLU 1099 OE1 
673 1 Y 1 B GLU 1099 ? OE2 ? B GLU 1099 OE2 
674 1 Y 1 B GLU 1105 ? CG  ? B GLU 1105 CG  
675 1 Y 1 B GLU 1105 ? CD  ? B GLU 1105 CD  
676 1 Y 1 B GLU 1105 ? OE1 ? B GLU 1105 OE1 
677 1 Y 1 B GLU 1105 ? OE2 ? B GLU 1105 OE2 
678 1 Y 1 B GLU 1106 ? CG  ? B GLU 1106 CG  
679 1 Y 1 B GLU 1106 ? CD  ? B GLU 1106 CD  
680 1 Y 1 B GLU 1106 ? OE1 ? B GLU 1106 OE1 
681 1 Y 1 B GLU 1106 ? OE2 ? B GLU 1106 OE2 
682 1 Y 1 B GLU 1109 ? CG  ? B GLU 1109 CG  
683 1 Y 1 B GLU 1109 ? CD  ? B GLU 1109 CD  
684 1 Y 1 B GLU 1109 ? OE1 ? B GLU 1109 OE1 
685 1 Y 1 B GLU 1109 ? OE2 ? B GLU 1109 OE2 
686 1 Y 1 B ASP 1116 ? CG  ? B ASP 1116 CG  
687 1 Y 1 B ASP 1116 ? OD1 ? B ASP 1116 OD1 
688 1 Y 1 B ASP 1116 ? OD2 ? B ASP 1116 OD2 
689 1 Y 1 B ASP 1117 ? CG  ? B ASP 1117 CG  
690 1 Y 1 B ASP 1117 ? OD1 ? B ASP 1117 OD1 
691 1 Y 1 B ASP 1117 ? OD2 ? B ASP 1117 OD2 
692 1 Y 1 B GLU 1119 ? CG  ? B GLU 1119 CG  
693 1 Y 1 B GLU 1119 ? CD  ? B GLU 1119 CD  
694 1 Y 1 B GLU 1119 ? OE1 ? B GLU 1119 OE1 
695 1 Y 1 B GLU 1119 ? OE2 ? B GLU 1119 OE2 
696 1 Y 1 B GLN 1120 ? CG  ? B GLN 1120 CG  
697 1 Y 1 B GLN 1120 ? CD  ? B GLN 1120 CD  
698 1 Y 1 B GLN 1120 ? OE1 ? B GLN 1120 OE1 
699 1 Y 1 B GLN 1120 ? NE2 ? B GLN 1120 NE2 
700 1 Y 1 B ILE 1122 ? CG1 ? B ILE 1122 CG1 
701 1 Y 1 B ILE 1122 ? CG2 ? B ILE 1122 CG2 
702 1 Y 1 B ILE 1122 ? CD1 ? B ILE 1122 CD1 
703 1 Y 1 B ASP 1124 ? CG  ? B ASP 1124 CG  
704 1 Y 1 B ASP 1124 ? OD1 ? B ASP 1124 OD1 
705 1 Y 1 B ASP 1124 ? OD2 ? B ASP 1124 OD2 
706 1 Y 1 B LYS 1127 ? CG  ? B LYS 1127 CG  
707 1 Y 1 B LYS 1127 ? CD  ? B LYS 1127 CD  
708 1 Y 1 B LYS 1127 ? CE  ? B LYS 1127 CE  
709 1 Y 1 B LYS 1127 ? NZ  ? B LYS 1127 NZ  
710 1 Y 1 B GLU 1128 ? CG  ? B GLU 1128 CG  
711 1 Y 1 B GLU 1128 ? CD  ? B GLU 1128 CD  
712 1 Y 1 B GLU 1128 ? OE1 ? B GLU 1128 OE1 
713 1 Y 1 B GLU 1128 ? OE2 ? B GLU 1128 OE2 
714 1 Y 1 B GLU 1130 ? CG  ? B GLU 1130 CG  
715 1 Y 1 B GLU 1130 ? CD  ? B GLU 1130 CD  
716 1 Y 1 B GLU 1130 ? OE1 ? B GLU 1130 OE1 
717 1 Y 1 B GLU 1130 ? OE2 ? B GLU 1130 OE2 
718 1 Y 1 B ASP 1136 ? CG  ? B ASP 1136 CG  
719 1 Y 1 B ASP 1136 ? OD1 ? B ASP 1136 OD1 
720 1 Y 1 B ASP 1136 ? OD2 ? B ASP 1136 OD2 
721 1 Y 1 B ASN 1137 ? CG  ? B ASN 1137 CG  
722 1 Y 1 B ASN 1137 ? OD1 ? B ASN 1137 OD1 
723 1 Y 1 B ASN 1137 ? ND2 ? B ASN 1137 ND2 
724 1 Y 1 B LEU 1139 ? CG  ? B LEU 1139 CG  
725 1 Y 1 B LEU 1139 ? CD1 ? B LEU 1139 CD1 
726 1 Y 1 B LEU 1139 ? CD2 ? B LEU 1139 CD2 
727 1 Y 1 B GLU 1140 ? CG  ? B GLU 1140 CG  
728 1 Y 1 B GLU 1140 ? CD  ? B GLU 1140 CD  
729 1 Y 1 B GLU 1140 ? OE1 ? B GLU 1140 OE1 
730 1 Y 1 B GLU 1140 ? OE2 ? B GLU 1140 OE2 
731 1 Y 1 B LYS 1143 ? CG  ? B LYS 1143 CG  
732 1 Y 1 B LYS 1143 ? CD  ? B LYS 1143 CD  
733 1 Y 1 B LYS 1143 ? CE  ? B LYS 1143 CE  
734 1 Y 1 B LYS 1143 ? NZ  ? B LYS 1143 NZ  
# 
_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                     9C0G 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9C0G 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9C0G 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9C0G 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003 ? 13246 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.496 ? 18016 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.629 ? 1898  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.038 ? 2084  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 2246  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9C0G 
_struct.title                        'Phosphorylated human NKCC1 in complex with torsemide' 
_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        9C0G 
_struct_keywords.text            
'Phosphorylation, sodium potassium chloride cotransporter, outward-open, torsemide, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    S12A2_HUMAN 
_struct_ref.pdbx_db_accession          P55011 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEPRPTAPSSGAPGLAGVGETPSAAALAAARVELPGTAVPSVPEDAAPASRDGGGVRDEGPAAAGDGLGRPLGPTPSQSR
FQVDLVSENAGRAAAAAAAAAAAAAAAGAGAGAKQTPADGEASGESEPAKGSEEAKGRFRVNFVDPAASSSAEDSLSDAA
GVGVDGPNVSFQNGGDTVLSEGSSLHSGGGGGSGHHQHYYYDTHTNTYYLRTFGHNTMDAVPRIDHYRHTAAQLGEKLLR
PSLAELHDELEKEPFEDGFANGEESTPTRDAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAGIGLS
VLVIMMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFANAVAVAMYVVGFAETVVELLKEHSI
LMIDEINDIRIIGAITVVILLGISVAGMEWEAKAQIVLLVILLLAIGDFVIGTFIPLESKKPKGFFGYKSEIFNENFGPD
FREEETFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTLVYVGIAVSVGSCVVRDATGNVNDTIVTEL
TNCTSAACKLNFDFSSCESSPCSYGLMNNFQVMSMVSGFTPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYPAFQM
FAKGYGKNNEPLRGYILTFLIALGFILIAELNVIAPIISNFFLASYALINFSVFHASLAKSPGWRPAFKYYNMWISLLGA
ILCCIVMFVINWWAALLTYVIVLGLYIYVTYKKPDVNWGSSTQALTYLNALQHSIRLSGVEDHVKNFRPQCLVMTGAPNS
RPALLHLVHDFTKNVGLMICGHVHMGPRRQAMKEMSIDQAKYQRWLIKNKMKAFYAPVHADDLREGAQYLMQAAGLGRMK
PNTLVLGFKKDWLQADMRDVDMYINLFHDAFDIQYGVVVIRLKEGLDISHLQGQEELLSSQEKSPGTKDVVVSVEYSKKS
DLDTSKPLSEKPITHKVEEEDGKTATQPLLKKESKGPIVPLNVADQKLLEASTQFQKKQGKNTIDVWWLFDDGGLTLLIP
YLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIIAFEEIIEPYRLHEDDKEQ
DIADKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGAVSSALYMAWLEALSKDLPPILLV
RGNHQSVLTFYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9C0G A 1 ? 1212 ? P55011 1 ? 1212 ? 1 1212 
2 1 9C0G B 1 ? 1212 ? P55011 1 ? 1212 ? 1 1212 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ARG A 223  ? ARG A 228  ? ARG A 223  ARG A 228  1 ? 6  
HELX_P HELX_P2  AA2 SER A 242  ? ASP A 248  ? SER A 242  ASP A 248  1 ? 7  
HELX_P HELX_P3  AA3 GLY A 286  ? VAL A 291  ? GLY A 286  VAL A 291  1 ? 6  
HELX_P HELX_P4  AA4 VAL A 291  ? TRP A 300  ? VAL A 291  TRP A 300  1 ? 10 
HELX_P HELX_P5  AA5 GLY A 301  ? PHE A 305  ? GLY A 301  PHE A 305  5 ? 5  
HELX_P HELX_P6  AA6 ILE A 306  ? ALA A 315  ? ILE A 306  ALA A 315  1 ? 10 
HELX_P HELX_P7  AA7 GLY A 316  ? THR A 343  ? GLY A 316  THR A 343  1 ? 28 
HELX_P HELX_P8  AA8 GLY A 351  ? GLU A 397  ? GLY A 351  GLU A 397  1 ? 47 
HELX_P HELX_P9  AA9 ASP A 404  ? GLY A 427  ? ASP A 404  GLY A 427  1 ? 24 
HELX_P HELX_P10 AB1 GLY A 427  ? THR A 453  ? GLY A 427  THR A 453  1 ? 27 
HELX_P HELX_P11 AB2 LEU A 457  ? LYS A 461  ? LEU A 457  LYS A 461  5 ? 5  
HELX_P HELX_P12 AB3 LYS A 469  ? PHE A 477  ? LYS A 469  PHE A 477  1 ? 9  
HELX_P HELX_P13 AB4 THR A 486  ? PHE A 495  ? THR A 486  PHE A 495  1 ? 10 
HELX_P HELX_P14 AB5 PRO A 496  ? THR A 499  ? PRO A 496  THR A 499  5 ? 4  
HELX_P HELX_P15 AB6 ALA A 503  ? LEU A 511  ? ALA A 503  LEU A 511  5 ? 9  
HELX_P HELX_P16 AB7 SER A 516  ? SER A 542  ? SER A 516  SER A 542  1 ? 27 
HELX_P HELX_P17 AB8 ALA A 566  ? LEU A 570  ? ALA A 566  LEU A 570  5 ? 5  
HELX_P HELX_P18 AB9 GLN A 591  ? SER A 597  ? GLN A 591  SER A 597  1 ? 7  
HELX_P HELX_P19 AC1 PHE A 599  ? ASP A 632  ? PHE A 599  ASP A 632  1 ? 34 
HELX_P HELX_P20 AC2 TYR A 635  ? GLN A 639  ? TYR A 635  GLN A 639  5 ? 5  
HELX_P HELX_P21 AC3 PRO A 651  ? ALA A 669  ? PRO A 651  ALA A 669  1 ? 19 
HELX_P HELX_P22 AC4 ILE A 674  ? ALA A 699  ? ILE A 674  ALA A 699  1 ? 26 
HELX_P HELX_P23 AC5 ASN A 712  ? ILE A 730  ? ASN A 712  ILE A 730  1 ? 19 
HELX_P HELX_P24 AC6 ASN A 731  ? LYS A 753  ? ASN A 731  LYS A 753  1 ? 23 
HELX_P HELX_P25 AC7 SER A 760  ? SER A 778  ? SER A 760  SER A 778  1 ? 19 
HELX_P HELX_P26 AC8 HIS A 783  ? PHE A 787  ? HIS A 783  PHE A 787  5 ? 5  
HELX_P HELX_P27 AC9 ARG A 801  ? PHE A 811  ? ARG A 801  PHE A 811  1 ? 11 
HELX_P HELX_P28 AD1 PRO A 827  ? LYS A 848  ? PRO A 827  LYS A 848  1 ? 22 
HELX_P HELX_P29 AD2 ASP A 862  ? ALA A 874  ? ASP A 862  ALA A 874  1 ? 13 
HELX_P HELX_P30 AD3 ASP A 896  ? ILE A 913  ? ASP A 896  ILE A 913  1 ? 18 
HELX_P HELX_P31 AD4 GLY A 1034 ? THR A 1045 ? GLY A 1034 THR A 1045 1 ? 12 
HELX_P HELX_P32 AD5 ARG A 1064 ? ARG A 1080 ? ARG A 1064 ARG A 1080 1 ? 17 
HELX_P HELX_P33 AD6 LYS A 1097 ? GLU A 1109 ? LYS A 1097 GLU A 1109 1 ? 13 
HELX_P HELX_P34 AD7 PRO A 1110 ? ARG A 1112 ? PRO A 1110 ARG A 1112 5 ? 3  
HELX_P HELX_P35 AD8 GLU A 1119 ? LYS A 1125 ? GLU A 1119 LYS A 1125 5 ? 7  
HELX_P HELX_P36 AD9 THR A 1135 ? TYR A 1142 ? THR A 1135 TYR A 1142 1 ? 8  
HELX_P HELX_P37 AE1 TYR A 1142 ? SER A 1160 ? TYR A 1142 SER A 1160 1 ? 19 
HELX_P HELX_P38 AE2 SER A 1179 ? LYS A 1192 ? SER A 1179 LYS A 1192 1 ? 14 
HELX_P HELX_P39 AE3 ARG B 223  ? ARG B 228  ? ARG B 223  ARG B 228  1 ? 6  
HELX_P HELX_P40 AE4 SER B 242  ? ASP B 248  ? SER B 242  ASP B 248  1 ? 7  
HELX_P HELX_P41 AE5 GLY B 286  ? VAL B 291  ? GLY B 286  VAL B 291  1 ? 6  
HELX_P HELX_P42 AE6 VAL B 291  ? TRP B 300  ? VAL B 291  TRP B 300  1 ? 10 
HELX_P HELX_P43 AE7 GLY B 301  ? PHE B 305  ? GLY B 301  PHE B 305  5 ? 5  
HELX_P HELX_P44 AE8 ARG B 307  ? ALA B 315  ? ARG B 307  ALA B 315  1 ? 9  
HELX_P HELX_P45 AE9 GLY B 316  ? THR B 343  ? GLY B 316  THR B 343  1 ? 28 
HELX_P HELX_P46 AF1 GLY B 351  ? GLU B 397  ? GLY B 351  GLU B 397  1 ? 47 
HELX_P HELX_P47 AF2 GLU B 405  ? ALA B 426  ? GLU B 405  ALA B 426  1 ? 22 
HELX_P HELX_P48 AF3 GLY B 427  ? THR B 453  ? GLY B 427  THR B 453  1 ? 27 
HELX_P HELX_P49 AF4 LEU B 457  ? LYS B 461  ? LEU B 457  LYS B 461  5 ? 5  
HELX_P HELX_P50 AF5 LYS B 469  ? PHE B 477  ? LYS B 469  PHE B 477  1 ? 9  
HELX_P HELX_P51 AF6 THR B 486  ? PHE B 495  ? THR B 486  PHE B 495  1 ? 10 
HELX_P HELX_P52 AF7 PRO B 496  ? THR B 499  ? PRO B 496  THR B 499  5 ? 4  
HELX_P HELX_P53 AF8 GLY B 504  ? LEU B 511  ? GLY B 504  LEU B 511  5 ? 8  
HELX_P HELX_P54 AF9 SER B 516  ? SER B 542  ? SER B 516  SER B 542  1 ? 27 
HELX_P HELX_P55 AG1 SER B 565  ? LEU B 570  ? SER B 565  LEU B 570  5 ? 6  
HELX_P HELX_P56 AG2 GLN B 591  ? SER B 597  ? GLN B 591  SER B 597  1 ? 7  
HELX_P HELX_P57 AG3 PHE B 599  ? ASP B 632  ? PHE B 599  ASP B 632  1 ? 34 
HELX_P HELX_P58 AG4 TYR B 635  ? GLN B 639  ? TYR B 635  GLN B 639  5 ? 5  
HELX_P HELX_P59 AG5 PRO B 651  ? ALA B 669  ? PRO B 651  ALA B 669  1 ? 19 
HELX_P HELX_P60 AG6 ILE B 674  ? ALA B 699  ? ILE B 674  ALA B 699  1 ? 26 
HELX_P HELX_P61 AG7 ASN B 712  ? ILE B 730  ? ASN B 712  ILE B 730  1 ? 19 
HELX_P HELX_P62 AG8 ASN B 731  ? LYS B 753  ? ASN B 731  LYS B 753  1 ? 23 
HELX_P HELX_P63 AG9 SER B 760  ? SER B 778  ? SER B 760  SER B 778  1 ? 19 
HELX_P HELX_P64 AH1 HIS B 783  ? PHE B 787  ? HIS B 783  PHE B 787  5 ? 5  
HELX_P HELX_P65 AH2 ARG B 801  ? PHE B 811  ? ARG B 801  PHE B 811  1 ? 11 
HELX_P HELX_P66 AH3 PRO B 827  ? ASN B 849  ? PRO B 827  ASN B 849  1 ? 23 
HELX_P HELX_P67 AH4 ASP B 862  ? ALA B 874  ? ASP B 862  ALA B 874  1 ? 13 
HELX_P HELX_P68 AH5 ASP B 896  ? ILE B 913  ? ASP B 896  ILE B 913  1 ? 18 
HELX_P HELX_P69 AH6 GLY B 1034 ? THR B 1045 ? GLY B 1034 THR B 1045 1 ? 12 
HELX_P HELX_P70 AH7 LYS B 1046 ? LYS B 1050 ? LYS B 1046 LYS B 1050 5 ? 5  
HELX_P HELX_P71 AH8 ARG B 1064 ? ARG B 1080 ? ARG B 1064 ARG B 1080 1 ? 17 
HELX_P HELX_P72 AH9 LYS B 1097 ? GLU B 1109 ? LYS B 1097 GLU B 1109 1 ? 13 
HELX_P HELX_P73 AI1 PRO B 1110 ? ARG B 1112 ? PRO B 1110 ARG B 1112 5 ? 3  
HELX_P HELX_P74 AI2 ASP B 1121 ? ASP B 1129 ? ASP B 1121 ASP B 1129 1 ? 9  
HELX_P HELX_P75 AI3 THR B 1135 ? TYR B 1142 ? THR B 1135 TYR B 1142 1 ? 8  
HELX_P HELX_P76 AI4 TYR B 1142 ? SER B 1160 ? TYR B 1142 SER B 1160 1 ? 19 
HELX_P HELX_P77 AI5 SER B 1161 ? ALA B 1163 ? SER B 1161 ALA B 1163 5 ? 3  
HELX_P HELX_P78 AI6 SER B 1179 ? SER B 1191 ? SER B 1179 SER B 1191 1 ? 13 
# 
_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 
disulf1  disulf ?    ? A CYS 563  SG  ? ? ? 1_555 A CYS 568  SG  ? ? A CYS 563  A CYS 568  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf2  disulf ?    ? A CYS 577  SG  ? ? ? 1_555 A CYS 582  SG  ? ? A CYS 577  A CYS 582  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf3  disulf ?    ? B CYS 563  SG  ? ? ? 1_555 B CYS 568  SG  ? ? B CYS 563  B CYS 568  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf4  disulf ?    ? B CYS 577  SG  ? ? ? 1_555 B CYS 582  SG  ? ? B CYS 577  B CYS 582  1_555 ? ? ? ? ? ? ? 2.035 ? ? 
covale1  covale both ? A TPO 217  C   ? ? ? 1_555 A MET 218  N   ? ? A TPO 217  A MET 218  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale2  covale none ? A TPO 217  O1P ? ? ? 1_555 B ARG 1148 NH2 ? ? A TPO 217  B ARG 1148 1_555 ? ? ? ? ? ? ? 1.298 ? ? 
covale3  covale none ? A ARG 1148 NH2 ? ? ? 1_555 B TPO 217  O1P ? ? A ARG 1148 B TPO 217  1_555 ? ? ? ? ? ? ? 1.296 ? ? 
covale4  covale both ? B TPO 217  C   ? ? ? 1_555 B MET 218  N   ? ? B TPO 217  B MET 218  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
metalc1  metalc ?    ? A LEU 297  O   ? ? ? 1_555 E NA  .    NA  ? ? A LEU 297  A NA  1303 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc2  metalc ?    ? A TRP 300  O   ? ? ? 1_555 E NA  .    NA  ? ? A TRP 300  A NA  1303 1_555 ? ? ? ? ? ? ? 2.566 ? ? 
metalc3  metalc ?    ? A ALA 610  O   ? ? ? 1_555 E NA  .    NA  ? ? A ALA 610  A NA  1303 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc4  metalc ?    ? A SER 613  OG  ? ? ? 1_555 E NA  .    NA  ? ? A SER 613  A NA  1303 1_555 ? ? ? ? ? ? ? 3.028 ? ? 
metalc5  metalc ?    ? A SER 614  OG  ? ? ? 1_555 E NA  .    NA  ? ? A SER 614  A NA  1303 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc6  metalc ?    ? B LEU 297  O   ? ? ? 1_555 H NA  .    NA  ? ? B LEU 297  B NA  1303 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc7  metalc ?    ? B TRP 300  O   ? ? ? 1_555 H NA  .    NA  ? ? B TRP 300  B NA  1303 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc8  metalc ?    ? B ALA 610  O   ? ? ? 1_555 H NA  .    NA  ? ? B ALA 610  B NA  1303 1_555 ? ? ? ? ? ? ? 2.493 ? ? 
metalc9  metalc ?    ? B SER 613  OG  ? ? ? 1_555 H NA  .    NA  ? ? B SER 613  B NA  1303 1_555 ? ? ? ? ? ? ? 2.913 ? ? 
metalc10 metalc ?    ? B SER 614  OG  ? ? ? 1_555 H NA  .    NA  ? ? B SER 614  B NA  1303 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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  O  ? A LEU 297 ? A LEU 297 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 O  ? A TRP 300 ? A TRP 300 ? 1_555 74.2  ? 
2  O  ? A LEU 297 ? A LEU 297 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 O  ? A ALA 610 ? A ALA 610 ? 1_555 160.3 ? 
3  O  ? A TRP 300 ? A TRP 300 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 O  ? A ALA 610 ? A ALA 610 ? 1_555 110.6 ? 
4  O  ? A LEU 297 ? A LEU 297 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 613 ? A SER 613 ? 1_555 93.8  ? 
5  O  ? A TRP 300 ? A TRP 300 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 613 ? A SER 613 ? 1_555 138.6 ? 
6  O  ? A ALA 610 ? A ALA 610 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 613 ? A SER 613 ? 1_555 69.7  ? 
7  O  ? A LEU 297 ? A LEU 297 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 614 ? A SER 614 ? 1_555 97.6  ? 
8  O  ? A TRP 300 ? A TRP 300 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 614 ? A SER 614 ? 1_555 95.6  ? 
9  O  ? A ALA 610 ? A ALA 610 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 614 ? A SER 614 ? 1_555 100.9 ? 
10 OG ? A SER 613 ? A SER 613 ? 1_555 NA ? E NA . ? A NA 1303 ? 1_555 OG ? A SER 614 ? A SER 614 ? 1_555 125.5 ? 
11 O  ? B LEU 297 ? B LEU 297 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 O  ? B TRP 300 ? B TRP 300 ? 1_555 79.9  ? 
12 O  ? B LEU 297 ? B LEU 297 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 O  ? B ALA 610 ? B ALA 610 ? 1_555 165.4 ? 
13 O  ? B TRP 300 ? B TRP 300 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 O  ? B ALA 610 ? B ALA 610 ? 1_555 110.5 ? 
14 O  ? B LEU 297 ? B LEU 297 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 613 ? B SER 613 ? 1_555 93.7  ? 
15 O  ? B TRP 300 ? B TRP 300 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 613 ? B SER 613 ? 1_555 143.6 ? 
16 O  ? B ALA 610 ? B ALA 610 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 613 ? B SER 613 ? 1_555 71.8  ? 
17 O  ? B LEU 297 ? B LEU 297 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 614 ? B SER 614 ? 1_555 105.8 ? 
18 O  ? B TRP 300 ? B TRP 300 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 614 ? B SER 614 ? 1_555 103.0 ? 
19 O  ? B ALA 610 ? B ALA 610 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 614 ? B SER 614 ? 1_555 82.4  ? 
20 OG ? B SER 613 ? B SER 613 ? 1_555 NA ? H NA . ? B NA 1303 ? 1_555 OG ? B SER 614 ? B SER 614 ? 1_555 113.2 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 TPO A 217  ? .   . .    . TPO A 217  ? 1_555 .   . .    . .     .   .   THR 1 TPO Phosphorylation 'Named protein modification' 
2 TPO B 217  ? .   . .    . TPO B 217  ? 1_555 .   . .    . .     .   .   THR 1 TPO Phosphorylation 'Named protein modification' 
3 CYS A 563  ? CYS A 568  ? CYS A 563  ? 1_555 CYS A 568  ? 1_555 SG  SG  .   . .   None            'Disulfide bridge'           
4 CYS A 577  ? CYS A 582  ? CYS A 577  ? 1_555 CYS A 582  ? 1_555 SG  SG  .   . .   None            'Disulfide bridge'           
5 CYS B 563  ? CYS B 568  ? CYS B 563  ? 1_555 CYS B 568  ? 1_555 SG  SG  .   . .   None            'Disulfide bridge'           
6 CYS B 577  ? CYS B 582  ? CYS B 577  ? 1_555 CYS B 582  ? 1_555 SG  SG  .   . .   None            'Disulfide bridge'           
7 TPO A 217  ? ARG B 1148 ? TPO A 217  ? 1_555 ARG B 1148 ? 1_555 O1P NH2 .   . .   None            'Non-standard linkage'       
8 ARG A 1148 ? TPO B 217  ? ARG A 1148 ? 1_555 TPO B 217  ? 1_555 NH2 O1P .   . .   None            'Non-standard linkage'       
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 1130 A . ? GLU 1130 A PRO 1131 A ? PRO 1131 A 1 4.44 
2 GLU 1130 B . ? GLU 1130 B PRO 1131 B ? PRO 1131 B 1 7.35 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 10 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? anti-parallel 
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA1 9 10 ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? parallel      
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? parallel      
AA2 7 8  ? parallel      
AA2 8 9  ? parallel      
AA2 9 10 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 854  ? HIS A 859  ? PHE A 854  HIS A 859  
AA1 2  MET A 818  ? HIS A 824  ? MET A 818  HIS A 824  
AA1 3  CYS A 791  ? MET A 794  ? CYS A 791  MET A 794  
AA1 4  THR A 883  ? GLY A 887  ? THR A 883  GLY A 887  
AA1 5  GLY A 916  ? ARG A 921  ? GLY A 916  ARG A 921  
AA1 6  ILE A 1197 ? ARG A 1201 ? ILE A 1197 ARG A 1201 
AA1 7  ILE A 1165 ? SER A 1169 ? ILE A 1165 SER A 1169 
AA1 8  THR A 1023 ? TRP A 1027 ? THR A 1023 TRP A 1027 
AA1 9  LYS A 1053 ? GLY A 1059 ? LYS A 1053 GLY A 1059 
AA1 10 ASP A 1085 ? LEU A 1089 ? ASP A 1085 LEU A 1089 
AA2 1  PHE B 854  ? HIS B 859  ? PHE B 854  HIS B 859  
AA2 2  MET B 818  ? HIS B 824  ? MET B 818  HIS B 824  
AA2 3  CYS B 791  ? MET B 794  ? CYS B 791  MET B 794  
AA2 4  THR B 883  ? GLY B 887  ? THR B 883  GLY B 887  
AA2 5  GLY B 916  ? ARG B 921  ? GLY B 916  ARG B 921  
AA2 6  ILE B 1197 ? ARG B 1201 ? ILE B 1197 ARG B 1201 
AA2 7  ILE B 1165 ? SER B 1169 ? ILE B 1165 SER B 1169 
AA2 8  THR B 1023 ? TRP B 1027 ? THR B 1023 TRP B 1027 
AA2 9  LYS B 1053 ? GLY B 1059 ? LYS B 1053 GLY B 1059 
AA2 10 ASP B 1085 ? LEU B 1089 ? ASP B 1085 LEU B 1089 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O VAL A 858  ? O VAL A 858  N HIS A 824  ? N HIS A 824  
AA1 2 3  O ILE A 819  ? O ILE A 819  N CYS A 791  ? N CYS A 791  
AA1 3 4  N LEU A 792  ? N LEU A 792  O VAL A 885  ? O VAL A 885  
AA1 4 5  N LEU A 886  ? N LEU A 886  O ILE A 920  ? O ILE A 920  
AA1 5 6  N VAL A 919  ? N VAL A 919  O LEU A 1199 ? O LEU A 1199 
AA1 6 7  O LEU A 1198 ? O LEU A 1198 N MET A 1168 ? N MET A 1168 
AA1 7 8  O VAL A 1167 ? O VAL A 1167 N TRP A 1027 ? N TRP A 1027 
AA1 8 9  N VAL A 1026 ? N VAL A 1026 O PHE A 1057 ? O PHE A 1057 
AA1 9 10 N ILE A 1058 ? N ILE A 1058 O MET A 1087 ? O MET A 1087 
AA2 1 2  O ALA B 856  ? O ALA B 856  N CYS B 820  ? N CYS B 820  
AA2 2 3  O GLY B 821  ? O GLY B 821  N VAL B 793  ? N VAL B 793  
AA2 3 4  N LEU B 792  ? N LEU B 792  O VAL B 885  ? O VAL B 885  
AA2 4 5  N LEU B 886  ? N LEU B 886  O VAL B 918  ? O VAL B 918  
AA2 5 6  N ARG B 921  ? N ARG B 921  O ILE B 1197 ? O ILE B 1197 
AA2 6 7  O VAL B 1200 ? O VAL B 1200 N MET B 1168 ? N MET B 1168 
AA2 7 8  O VAL B 1167 ? O VAL B 1167 N TRP B 1027 ? N TRP B 1027 
AA2 8 9  N ILE B 1024 ? N ILE B 1024 O LYS B 1053 ? O LYS B 1053 
AA2 9 10 N ILE B 1058 ? N ILE B 1058 O MET B 1087 ? O MET B 1087 
# 
_pdbx_entry_details.entry_id                   9C0G 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A VAL 808  ? ? OG1 A THR 812  ? ? 1.97 
2  1 ND2 A ASN 1100 ? ? OE2 A GLU 1154 ? ? 2.04 
3  1 O   B PHE 572  ? ? OG  B SER 575  ? ? 2.06 
4  1 ND2 B ASN 1100 ? ? OE2 B GLU 1154 ? ? 2.08 
5  1 O   B VAL 808  ? ? OG1 B THR 812  ? ? 2.08 
6  1 OD2 B ASP 1032 ? ? OG1 B THR 1036 ? ? 2.12 
7  1 O1P A TPO 217  ? ? CZ  B ARG 1148 ? ? 2.12 
8  1 OD1 A ASP 1031 ? ? OH  B TYR 227  ? ? 2.14 
9  1 OD2 A ASP 513  ? ? OG  A SER 516  ? ? 2.15 
10 1 OH  B TYR 353  ? ? OD2 B ASP 632  ? ? 2.15 
11 1 OD2 A ASP 1032 ? ? OG1 A THR 1036 ? ? 2.17 
12 1 O   B GLY 887  ? ? OH  B TYR 903  ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA B PRO 462 ? ? N  B PRO 462 ? ? CD B PRO 462 ? ? 103.14 111.70 -8.56  1.40 N 
2 1 CA B PRO 462 ? ? CB B PRO 462 ? ? CG B PRO 462 ? ? 88.88  104.80 -15.92 1.90 N 
3 1 N  B PRO 462 ? ? CD B PRO 462 ? ? CG B PRO 462 ? ? 87.19  103.20 -16.01 1.50 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 MET A 218  ? ? 76.29   -17.68  
2  1 ALA A 232  ? ? -170.74 -179.43 
3  1 ILE A 306  ? ? -123.13 -59.60  
4  1 LEU A 401  ? ? -173.20 147.39  
5  1 TYR A 468  ? ? 64.71   62.13   
6  1 THR A 499  ? ? -79.31  -168.20 
7  1 GLN A 515  ? ? 76.33   -8.75   
8  1 SER A 516  ? ? -131.06 -38.85  
9  1 CYS A 563  ? ? 39.17   64.50   
10 1 SER A 576  ? ? 60.23   63.91   
11 1 PHE A 599  ? ? -59.92  108.46  
12 1 MET A 640  ? ? 77.30   179.26  
13 1 ALA A 669  ? ? 73.43   -4.96   
14 1 ARG A 705  ? ? 30.48   62.92   
15 1 LYS A 753  ? ? 53.25   72.00   
16 1 ASN A 814  ? ? 74.40   -6.69   
17 1 ALA A 895  ? ? -174.20 149.98  
18 1 TRP A 1027 ? ? -100.95 75.46   
19 1 ASN A 1063 ? ? 77.52   -1.48   
20 1 PRO A 1131 ? ? -80.32  33.94   
21 1 PRO A 1195 ? ? -56.52  172.23  
22 1 THR B 343  ? ? -98.43  34.02   
23 1 ASP B 404  ? ? 69.67   -162.38 
24 1 ILE B 455  ? ? -116.34 75.20   
25 1 GLU B 483  ? ? 49.19   -154.92 
26 1 ASP B 513  ? ? -156.04 82.16   
27 1 GLN B 515  ? ? 76.16   -5.94   
28 1 SER B 516  ? ? -131.64 -31.40  
29 1 CYS B 563  ? ? 39.64   61.62   
30 1 PHE B 574  ? ? 60.14   61.05   
31 1 SER B 576  ? ? 72.82   37.61   
32 1 ALA B 669  ? ? 73.45   -5.13   
33 1 LYS B 700  ? ? -98.35  36.55   
34 1 ARG B 705  ? ? 33.52   59.89   
35 1 LYS B 753  ? ? 53.31   71.41   
36 1 ASN B 814  ? ? 73.16   -10.32  
37 1 MET B 879  ? ? -90.99  55.65   
38 1 ALA B 895  ? ? -174.91 149.62  
39 1 ASN B 1063 ? ? 80.96   -6.34   
40 1 PRO B 1110 ? ? -80.11  42.23   
41 1 GLU B 1119 ? ? -122.97 -167.04 
42 1 PRO B 1131 ? ? -82.90  40.09   
43 1 LYS B 1192 ? ? -173.14 147.28  
44 1 PRO B 1195 ? ? -67.10  -179.18 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A TPO 217 A TPO 217 ? THR 'modified residue' 
2 B TPO 217 B TPO 217 ? THR 'modified residue' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9C0G 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9C0G 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.6 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               2360417 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Phosphorylated human NKCC1 in complex with torsemide' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9C0G 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI MORGAGNI' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             700 
_em_imaging.nominal_defocus_max             3500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9C0G 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9C0G 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1    ? A MET 1    
2   1 Y 1 A GLU 2    ? A GLU 2    
3   1 Y 1 A PRO 3    ? A PRO 3    
4   1 Y 1 A ARG 4    ? A ARG 4    
5   1 Y 1 A PRO 5    ? A PRO 5    
6   1 Y 1 A THR 6    ? A THR 6    
7   1 Y 1 A ALA 7    ? A ALA 7    
8   1 Y 1 A PRO 8    ? A PRO 8    
9   1 Y 1 A SER 9    ? A SER 9    
10  1 Y 1 A SER 10   ? A SER 10   
11  1 Y 1 A GLY 11   ? A GLY 11   
12  1 Y 1 A ALA 12   ? A ALA 12   
13  1 Y 1 A PRO 13   ? A PRO 13   
14  1 Y 1 A GLY 14   ? A GLY 14   
15  1 Y 1 A LEU 15   ? A LEU 15   
16  1 Y 1 A ALA 16   ? A ALA 16   
17  1 Y 1 A GLY 17   ? A GLY 17   
18  1 Y 1 A VAL 18   ? A VAL 18   
19  1 Y 1 A GLY 19   ? A GLY 19   
20  1 Y 1 A GLU 20   ? A GLU 20   
21  1 Y 1 A THR 21   ? A THR 21   
22  1 Y 1 A PRO 22   ? A PRO 22   
23  1 Y 1 A SER 23   ? A SER 23   
24  1 Y 1 A ALA 24   ? A ALA 24   
25  1 Y 1 A ALA 25   ? A ALA 25   
26  1 Y 1 A ALA 26   ? A ALA 26   
27  1 Y 1 A LEU 27   ? A LEU 27   
28  1 Y 1 A ALA 28   ? A ALA 28   
29  1 Y 1 A ALA 29   ? A ALA 29   
30  1 Y 1 A ALA 30   ? A ALA 30   
31  1 Y 1 A ARG 31   ? A ARG 31   
32  1 Y 1 A VAL 32   ? A VAL 32   
33  1 Y 1 A GLU 33   ? A GLU 33   
34  1 Y 1 A LEU 34   ? A LEU 34   
35  1 Y 1 A PRO 35   ? A PRO 35   
36  1 Y 1 A GLY 36   ? A GLY 36   
37  1 Y 1 A THR 37   ? A THR 37   
38  1 Y 1 A ALA 38   ? A ALA 38   
39  1 Y 1 A VAL 39   ? A VAL 39   
40  1 Y 1 A PRO 40   ? A PRO 40   
41  1 Y 1 A SER 41   ? A SER 41   
42  1 Y 1 A VAL 42   ? A VAL 42   
43  1 Y 1 A PRO 43   ? A PRO 43   
44  1 Y 1 A GLU 44   ? A GLU 44   
45  1 Y 1 A ASP 45   ? A ASP 45   
46  1 Y 1 A ALA 46   ? A ALA 46   
47  1 Y 1 A ALA 47   ? A ALA 47   
48  1 Y 1 A PRO 48   ? A PRO 48   
49  1 Y 1 A ALA 49   ? A ALA 49   
50  1 Y 1 A SER 50   ? A SER 50   
51  1 Y 1 A ARG 51   ? A ARG 51   
52  1 Y 1 A ASP 52   ? A ASP 52   
53  1 Y 1 A GLY 53   ? A GLY 53   
54  1 Y 1 A GLY 54   ? A GLY 54   
55  1 Y 1 A GLY 55   ? A GLY 55   
56  1 Y 1 A VAL 56   ? A VAL 56   
57  1 Y 1 A ARG 57   ? A ARG 57   
58  1 Y 1 A ASP 58   ? A ASP 58   
59  1 Y 1 A GLU 59   ? A GLU 59   
60  1 Y 1 A GLY 60   ? A GLY 60   
61  1 Y 1 A PRO 61   ? A PRO 61   
62  1 Y 1 A ALA 62   ? A ALA 62   
63  1 Y 1 A ALA 63   ? A ALA 63   
64  1 Y 1 A ALA 64   ? A ALA 64   
65  1 Y 1 A GLY 65   ? A GLY 65   
66  1 Y 1 A ASP 66   ? A ASP 66   
67  1 Y 1 A GLY 67   ? A GLY 67   
68  1 Y 1 A LEU 68   ? A LEU 68   
69  1 Y 1 A GLY 69   ? A GLY 69   
70  1 Y 1 A ARG 70   ? A ARG 70   
71  1 Y 1 A PRO 71   ? A PRO 71   
72  1 Y 1 A LEU 72   ? A LEU 72   
73  1 Y 1 A GLY 73   ? A GLY 73   
74  1 Y 1 A PRO 74   ? A PRO 74   
75  1 Y 1 A THR 75   ? A THR 75   
76  1 Y 1 A PRO 76   ? A PRO 76   
77  1 Y 1 A SER 77   ? A SER 77   
78  1 Y 1 A GLN 78   ? A GLN 78   
79  1 Y 1 A SER 79   ? A SER 79   
80  1 Y 1 A ARG 80   ? A ARG 80   
81  1 Y 1 A PHE 81   ? A PHE 81   
82  1 Y 1 A GLN 82   ? A GLN 82   
83  1 Y 1 A VAL 83   ? A VAL 83   
84  1 Y 1 A ASP 84   ? A ASP 84   
85  1 Y 1 A LEU 85   ? A LEU 85   
86  1 Y 1 A VAL 86   ? A VAL 86   
87  1 Y 1 A SER 87   ? A SER 87   
88  1 Y 1 A GLU 88   ? A GLU 88   
89  1 Y 1 A ASN 89   ? A ASN 89   
90  1 Y 1 A ALA 90   ? A ALA 90   
91  1 Y 1 A GLY 91   ? A GLY 91   
92  1 Y 1 A ARG 92   ? A ARG 92   
93  1 Y 1 A ALA 93   ? A ALA 93   
94  1 Y 1 A ALA 94   ? A ALA 94   
95  1 Y 1 A ALA 95   ? A ALA 95   
96  1 Y 1 A ALA 96   ? A ALA 96   
97  1 Y 1 A ALA 97   ? A ALA 97   
98  1 Y 1 A ALA 98   ? A ALA 98   
99  1 Y 1 A ALA 99   ? A ALA 99   
100 1 Y 1 A ALA 100  ? A ALA 100  
101 1 Y 1 A ALA 101  ? A ALA 101  
102 1 Y 1 A ALA 102  ? A ALA 102  
103 1 Y 1 A ALA 103  ? A ALA 103  
104 1 Y 1 A ALA 104  ? A ALA 104  
105 1 Y 1 A ALA 105  ? A ALA 105  
106 1 Y 1 A ALA 106  ? A ALA 106  
107 1 Y 1 A ALA 107  ? A ALA 107  
108 1 Y 1 A GLY 108  ? A GLY 108  
109 1 Y 1 A ALA 109  ? A ALA 109  
110 1 Y 1 A GLY 110  ? A GLY 110  
111 1 Y 1 A ALA 111  ? A ALA 111  
112 1 Y 1 A GLY 112  ? A GLY 112  
113 1 Y 1 A ALA 113  ? A ALA 113  
114 1 Y 1 A LYS 114  ? A LYS 114  
115 1 Y 1 A GLN 115  ? A GLN 115  
116 1 Y 1 A THR 116  ? A THR 116  
117 1 Y 1 A PRO 117  ? A PRO 117  
118 1 Y 1 A ALA 118  ? A ALA 118  
119 1 Y 1 A ASP 119  ? A ASP 119  
120 1 Y 1 A GLY 120  ? A GLY 120  
121 1 Y 1 A GLU 121  ? A GLU 121  
122 1 Y 1 A ALA 122  ? A ALA 122  
123 1 Y 1 A SER 123  ? A SER 123  
124 1 Y 1 A GLY 124  ? A GLY 124  
125 1 Y 1 A GLU 125  ? A GLU 125  
126 1 Y 1 A SER 126  ? A SER 126  
127 1 Y 1 A GLU 127  ? A GLU 127  
128 1 Y 1 A PRO 128  ? A PRO 128  
129 1 Y 1 A ALA 129  ? A ALA 129  
130 1 Y 1 A LYS 130  ? A LYS 130  
131 1 Y 1 A GLY 131  ? A GLY 131  
132 1 Y 1 A SER 132  ? A SER 132  
133 1 Y 1 A GLU 133  ? A GLU 133  
134 1 Y 1 A GLU 134  ? A GLU 134  
135 1 Y 1 A ALA 135  ? A ALA 135  
136 1 Y 1 A LYS 136  ? A LYS 136  
137 1 Y 1 A GLY 137  ? A GLY 137  
138 1 Y 1 A ARG 138  ? A ARG 138  
139 1 Y 1 A PHE 139  ? A PHE 139  
140 1 Y 1 A ARG 140  ? A ARG 140  
141 1 Y 1 A VAL 141  ? A VAL 141  
142 1 Y 1 A ASN 142  ? A ASN 142  
143 1 Y 1 A PHE 143  ? A PHE 143  
144 1 Y 1 A VAL 144  ? A VAL 144  
145 1 Y 1 A ASP 145  ? A ASP 145  
146 1 Y 1 A PRO 146  ? A PRO 146  
147 1 Y 1 A ALA 147  ? A ALA 147  
148 1 Y 1 A ALA 148  ? A ALA 148  
149 1 Y 1 A SER 149  ? A SER 149  
150 1 Y 1 A SER 150  ? A SER 150  
151 1 Y 1 A SER 151  ? A SER 151  
152 1 Y 1 A ALA 152  ? A ALA 152  
153 1 Y 1 A GLU 153  ? A GLU 153  
154 1 Y 1 A ASP 154  ? A ASP 154  
155 1 Y 1 A SER 155  ? A SER 155  
156 1 Y 1 A LEU 156  ? A LEU 156  
157 1 Y 1 A SER 157  ? A SER 157  
158 1 Y 1 A ASP 158  ? A ASP 158  
159 1 Y 1 A ALA 159  ? A ALA 159  
160 1 Y 1 A ALA 160  ? A ALA 160  
161 1 Y 1 A GLY 161  ? A GLY 161  
162 1 Y 1 A VAL 162  ? A VAL 162  
163 1 Y 1 A GLY 163  ? A GLY 163  
164 1 Y 1 A VAL 164  ? A VAL 164  
165 1 Y 1 A ASP 165  ? A ASP 165  
166 1 Y 1 A GLY 166  ? A GLY 166  
167 1 Y 1 A PRO 167  ? A PRO 167  
168 1 Y 1 A ASN 168  ? A ASN 168  
169 1 Y 1 A VAL 169  ? A VAL 169  
170 1 Y 1 A SER 170  ? A SER 170  
171 1 Y 1 A PHE 171  ? A PHE 171  
172 1 Y 1 A GLN 172  ? A GLN 172  
173 1 Y 1 A ASN 173  ? A ASN 173  
174 1 Y 1 A GLY 174  ? A GLY 174  
175 1 Y 1 A GLY 175  ? A GLY 175  
176 1 Y 1 A ASP 176  ? A ASP 176  
177 1 Y 1 A THR 177  ? A THR 177  
178 1 Y 1 A VAL 178  ? A VAL 178  
179 1 Y 1 A LEU 179  ? A LEU 179  
180 1 Y 1 A SER 180  ? A SER 180  
181 1 Y 1 A GLU 181  ? A GLU 181  
182 1 Y 1 A GLY 182  ? A GLY 182  
183 1 Y 1 A SER 183  ? A SER 183  
184 1 Y 1 A SER 184  ? A SER 184  
185 1 Y 1 A LEU 185  ? A LEU 185  
186 1 Y 1 A HIS 186  ? A HIS 186  
187 1 Y 1 A SER 187  ? A SER 187  
188 1 Y 1 A GLY 188  ? A GLY 188  
189 1 Y 1 A GLY 189  ? A GLY 189  
190 1 Y 1 A GLY 190  ? A GLY 190  
191 1 Y 1 A GLY 191  ? A GLY 191  
192 1 Y 1 A GLY 192  ? A GLY 192  
193 1 Y 1 A SER 193  ? A SER 193  
194 1 Y 1 A GLY 194  ? A GLY 194  
195 1 Y 1 A HIS 195  ? A HIS 195  
196 1 Y 1 A HIS 196  ? A HIS 196  
197 1 Y 1 A GLN 197  ? A GLN 197  
198 1 Y 1 A HIS 198  ? A HIS 198  
199 1 Y 1 A TYR 199  ? A TYR 199  
200 1 Y 1 A TYR 200  ? A TYR 200  
201 1 Y 1 A TYR 201  ? A TYR 201  
202 1 Y 1 A ASP 202  ? A ASP 202  
203 1 Y 1 A THR 203  ? A THR 203  
204 1 Y 1 A HIS 204  ? A HIS 204  
205 1 Y 1 A THR 205  ? A THR 205  
206 1 Y 1 A ASN 206  ? A ASN 206  
207 1 Y 1 A THR 207  ? A THR 207  
208 1 Y 1 A TYR 208  ? A TYR 208  
209 1 Y 1 A TYR 209  ? A TYR 209  
210 1 Y 1 A LEU 210  ? A LEU 210  
211 1 Y 1 A ARG 211  ? A ARG 211  
212 1 Y 1 A THR 212  ? A THR 212  
213 1 Y 1 A PHE 213  ? A PHE 213  
214 1 Y 1 A GLY 214  ? A GLY 214  
215 1 Y 1 A HIS 215  ? A HIS 215  
216 1 Y 1 A ASN 216  ? A ASN 216  
217 1 Y 1 A GLU 251  ? A GLU 251  
218 1 Y 1 A LYS 252  ? A LYS 252  
219 1 Y 1 A GLU 253  ? A GLU 253  
220 1 Y 1 A PRO 254  ? A PRO 254  
221 1 Y 1 A PHE 255  ? A PHE 255  
222 1 Y 1 A GLU 256  ? A GLU 256  
223 1 Y 1 A ASP 257  ? A ASP 257  
224 1 Y 1 A GLY 258  ? A GLY 258  
225 1 Y 1 A PHE 259  ? A PHE 259  
226 1 Y 1 A ALA 260  ? A ALA 260  
227 1 Y 1 A ASN 261  ? A ASN 261  
228 1 Y 1 A GLY 262  ? A GLY 262  
229 1 Y 1 A GLU 263  ? A GLU 263  
230 1 Y 1 A GLU 264  ? A GLU 264  
231 1 Y 1 A SER 265  ? A SER 265  
232 1 Y 1 A THR 266  ? A THR 266  
233 1 Y 1 A PRO 267  ? A PRO 267  
234 1 Y 1 A THR 268  ? A THR 268  
235 1 Y 1 A ARG 269  ? A ARG 269  
236 1 Y 1 A ASP 270  ? A ASP 270  
237 1 Y 1 A ALA 271  ? A ALA 271  
238 1 Y 1 A VAL 272  ? A VAL 272  
239 1 Y 1 A VAL 273  ? A VAL 273  
240 1 Y 1 A THR 274  ? A THR 274  
241 1 Y 1 A TYR 275  ? A TYR 275  
242 1 Y 1 A THR 276  ? A THR 276  
243 1 Y 1 A ALA 277  ? A ALA 277  
244 1 Y 1 A GLU 278  ? A GLU 278  
245 1 Y 1 A SER 279  ? A SER 279  
246 1 Y 1 A LYS 280  ? A LYS 280  
247 1 Y 1 A GLY 281  ? A GLY 281  
248 1 Y 1 A ASP 927  ? A ASP 927  
249 1 Y 1 A ILE 928  ? A ILE 928  
250 1 Y 1 A SER 929  ? A SER 929  
251 1 Y 1 A HIS 930  ? A HIS 930  
252 1 Y 1 A LEU 931  ? A LEU 931  
253 1 Y 1 A GLN 932  ? A GLN 932  
254 1 Y 1 A GLY 933  ? A GLY 933  
255 1 Y 1 A GLN 934  ? A GLN 934  
256 1 Y 1 A GLU 935  ? A GLU 935  
257 1 Y 1 A GLU 936  ? A GLU 936  
258 1 Y 1 A LEU 937  ? A LEU 937  
259 1 Y 1 A LEU 938  ? A LEU 938  
260 1 Y 1 A SER 939  ? A SER 939  
261 1 Y 1 A SER 940  ? A SER 940  
262 1 Y 1 A GLN 941  ? A GLN 941  
263 1 Y 1 A GLU 942  ? A GLU 942  
264 1 Y 1 A LYS 943  ? A LYS 943  
265 1 Y 1 A SER 944  ? A SER 944  
266 1 Y 1 A PRO 945  ? A PRO 945  
267 1 Y 1 A GLY 946  ? A GLY 946  
268 1 Y 1 A THR 947  ? A THR 947  
269 1 Y 1 A LYS 948  ? A LYS 948  
270 1 Y 1 A ASP 949  ? A ASP 949  
271 1 Y 1 A VAL 950  ? A VAL 950  
272 1 Y 1 A VAL 951  ? A VAL 951  
273 1 Y 1 A VAL 952  ? A VAL 952  
274 1 Y 1 A SER 953  ? A SER 953  
275 1 Y 1 A VAL 954  ? A VAL 954  
276 1 Y 1 A GLU 955  ? A GLU 955  
277 1 Y 1 A TYR 956  ? A TYR 956  
278 1 Y 1 A SER 957  ? A SER 957  
279 1 Y 1 A LYS 958  ? A LYS 958  
280 1 Y 1 A LYS 959  ? A LYS 959  
281 1 Y 1 A SER 960  ? A SER 960  
282 1 Y 1 A ASP 961  ? A ASP 961  
283 1 Y 1 A LEU 962  ? A LEU 962  
284 1 Y 1 A ASP 963  ? A ASP 963  
285 1 Y 1 A THR 964  ? A THR 964  
286 1 Y 1 A SER 965  ? A SER 965  
287 1 Y 1 A LYS 966  ? A LYS 966  
288 1 Y 1 A PRO 967  ? A PRO 967  
289 1 Y 1 A LEU 968  ? A LEU 968  
290 1 Y 1 A SER 969  ? A SER 969  
291 1 Y 1 A GLU 970  ? A GLU 970  
292 1 Y 1 A LYS 971  ? A LYS 971  
293 1 Y 1 A PRO 972  ? A PRO 972  
294 1 Y 1 A ILE 973  ? A ILE 973  
295 1 Y 1 A THR 974  ? A THR 974  
296 1 Y 1 A HIS 975  ? A HIS 975  
297 1 Y 1 A LYS 976  ? A LYS 976  
298 1 Y 1 A VAL 977  ? A VAL 977  
299 1 Y 1 A GLU 978  ? A GLU 978  
300 1 Y 1 A GLU 979  ? A GLU 979  
301 1 Y 1 A GLU 980  ? A GLU 980  
302 1 Y 1 A ASP 981  ? A ASP 981  
303 1 Y 1 A GLY 982  ? A GLY 982  
304 1 Y 1 A LYS 983  ? A LYS 983  
305 1 Y 1 A THR 984  ? A THR 984  
306 1 Y 1 A ALA 985  ? A ALA 985  
307 1 Y 1 A THR 986  ? A THR 986  
308 1 Y 1 A GLN 987  ? A GLN 987  
309 1 Y 1 A PRO 988  ? A PRO 988  
310 1 Y 1 A LEU 989  ? A LEU 989  
311 1 Y 1 A LEU 990  ? A LEU 990  
312 1 Y 1 A LYS 991  ? A LYS 991  
313 1 Y 1 A LYS 992  ? A LYS 992  
314 1 Y 1 A GLU 993  ? A GLU 993  
315 1 Y 1 A SER 994  ? A SER 994  
316 1 Y 1 A LYS 995  ? A LYS 995  
317 1 Y 1 A GLY 996  ? A GLY 996  
318 1 Y 1 A PRO 997  ? A PRO 997  
319 1 Y 1 A ILE 998  ? A ILE 998  
320 1 Y 1 A VAL 999  ? A VAL 999  
321 1 Y 1 A PRO 1000 ? A PRO 1000 
322 1 Y 1 A LEU 1001 ? A LEU 1001 
323 1 Y 1 A ASN 1002 ? A ASN 1002 
324 1 Y 1 A VAL 1003 ? A VAL 1003 
325 1 Y 1 A ALA 1004 ? A ALA 1004 
326 1 Y 1 A ASP 1005 ? A ASP 1005 
327 1 Y 1 A GLN 1006 ? A GLN 1006 
328 1 Y 1 A LYS 1007 ? A LYS 1007 
329 1 Y 1 A LEU 1008 ? A LEU 1008 
330 1 Y 1 A LEU 1009 ? A LEU 1009 
331 1 Y 1 A GLU 1010 ? A GLU 1010 
332 1 Y 1 A ALA 1011 ? A ALA 1011 
333 1 Y 1 A SER 1012 ? A SER 1012 
334 1 Y 1 A THR 1013 ? A THR 1013 
335 1 Y 1 A GLN 1014 ? A GLN 1014 
336 1 Y 1 A PHE 1015 ? A PHE 1015 
337 1 Y 1 A GLN 1016 ? A GLN 1016 
338 1 Y 1 A LYS 1017 ? A LYS 1017 
339 1 Y 1 A LYS 1018 ? A LYS 1018 
340 1 Y 1 A GLN 1019 ? A GLN 1019 
341 1 Y 1 A GLY 1020 ? A GLY 1020 
342 1 Y 1 A LYS 1021 ? A LYS 1021 
343 1 Y 1 B MET 1    ? B MET 1    
344 1 Y 1 B GLU 2    ? B GLU 2    
345 1 Y 1 B PRO 3    ? B PRO 3    
346 1 Y 1 B ARG 4    ? B ARG 4    
347 1 Y 1 B PRO 5    ? B PRO 5    
348 1 Y 1 B THR 6    ? B THR 6    
349 1 Y 1 B ALA 7    ? B ALA 7    
350 1 Y 1 B PRO 8    ? B PRO 8    
351 1 Y 1 B SER 9    ? B SER 9    
352 1 Y 1 B SER 10   ? B SER 10   
353 1 Y 1 B GLY 11   ? B GLY 11   
354 1 Y 1 B ALA 12   ? B ALA 12   
355 1 Y 1 B PRO 13   ? B PRO 13   
356 1 Y 1 B GLY 14   ? B GLY 14   
357 1 Y 1 B LEU 15   ? B LEU 15   
358 1 Y 1 B ALA 16   ? B ALA 16   
359 1 Y 1 B GLY 17   ? B GLY 17   
360 1 Y 1 B VAL 18   ? B VAL 18   
361 1 Y 1 B GLY 19   ? B GLY 19   
362 1 Y 1 B GLU 20   ? B GLU 20   
363 1 Y 1 B THR 21   ? B THR 21   
364 1 Y 1 B PRO 22   ? B PRO 22   
365 1 Y 1 B SER 23   ? B SER 23   
366 1 Y 1 B ALA 24   ? B ALA 24   
367 1 Y 1 B ALA 25   ? B ALA 25   
368 1 Y 1 B ALA 26   ? B ALA 26   
369 1 Y 1 B LEU 27   ? B LEU 27   
370 1 Y 1 B ALA 28   ? B ALA 28   
371 1 Y 1 B ALA 29   ? B ALA 29   
372 1 Y 1 B ALA 30   ? B ALA 30   
373 1 Y 1 B ARG 31   ? B ARG 31   
374 1 Y 1 B VAL 32   ? B VAL 32   
375 1 Y 1 B GLU 33   ? B GLU 33   
376 1 Y 1 B LEU 34   ? B LEU 34   
377 1 Y 1 B PRO 35   ? B PRO 35   
378 1 Y 1 B GLY 36   ? B GLY 36   
379 1 Y 1 B THR 37   ? B THR 37   
380 1 Y 1 B ALA 38   ? B ALA 38   
381 1 Y 1 B VAL 39   ? B VAL 39   
382 1 Y 1 B PRO 40   ? B PRO 40   
383 1 Y 1 B SER 41   ? B SER 41   
384 1 Y 1 B VAL 42   ? B VAL 42   
385 1 Y 1 B PRO 43   ? B PRO 43   
386 1 Y 1 B GLU 44   ? B GLU 44   
387 1 Y 1 B ASP 45   ? B ASP 45   
388 1 Y 1 B ALA 46   ? B ALA 46   
389 1 Y 1 B ALA 47   ? B ALA 47   
390 1 Y 1 B PRO 48   ? B PRO 48   
391 1 Y 1 B ALA 49   ? B ALA 49   
392 1 Y 1 B SER 50   ? B SER 50   
393 1 Y 1 B ARG 51   ? B ARG 51   
394 1 Y 1 B ASP 52   ? B ASP 52   
395 1 Y 1 B GLY 53   ? B GLY 53   
396 1 Y 1 B GLY 54   ? B GLY 54   
397 1 Y 1 B GLY 55   ? B GLY 55   
398 1 Y 1 B VAL 56   ? B VAL 56   
399 1 Y 1 B ARG 57   ? B ARG 57   
400 1 Y 1 B ASP 58   ? B ASP 58   
401 1 Y 1 B GLU 59   ? B GLU 59   
402 1 Y 1 B GLY 60   ? B GLY 60   
403 1 Y 1 B PRO 61   ? B PRO 61   
404 1 Y 1 B ALA 62   ? B ALA 62   
405 1 Y 1 B ALA 63   ? B ALA 63   
406 1 Y 1 B ALA 64   ? B ALA 64   
407 1 Y 1 B GLY 65   ? B GLY 65   
408 1 Y 1 B ASP 66   ? B ASP 66   
409 1 Y 1 B GLY 67   ? B GLY 67   
410 1 Y 1 B LEU 68   ? B LEU 68   
411 1 Y 1 B GLY 69   ? B GLY 69   
412 1 Y 1 B ARG 70   ? B ARG 70   
413 1 Y 1 B PRO 71   ? B PRO 71   
414 1 Y 1 B LEU 72   ? B LEU 72   
415 1 Y 1 B GLY 73   ? B GLY 73   
416 1 Y 1 B PRO 74   ? B PRO 74   
417 1 Y 1 B THR 75   ? B THR 75   
418 1 Y 1 B PRO 76   ? B PRO 76   
419 1 Y 1 B SER 77   ? B SER 77   
420 1 Y 1 B GLN 78   ? B GLN 78   
421 1 Y 1 B SER 79   ? B SER 79   
422 1 Y 1 B ARG 80   ? B ARG 80   
423 1 Y 1 B PHE 81   ? B PHE 81   
424 1 Y 1 B GLN 82   ? B GLN 82   
425 1 Y 1 B VAL 83   ? B VAL 83   
426 1 Y 1 B ASP 84   ? B ASP 84   
427 1 Y 1 B LEU 85   ? B LEU 85   
428 1 Y 1 B VAL 86   ? B VAL 86   
429 1 Y 1 B SER 87   ? B SER 87   
430 1 Y 1 B GLU 88   ? B GLU 88   
431 1 Y 1 B ASN 89   ? B ASN 89   
432 1 Y 1 B ALA 90   ? B ALA 90   
433 1 Y 1 B GLY 91   ? B GLY 91   
434 1 Y 1 B ARG 92   ? B ARG 92   
435 1 Y 1 B ALA 93   ? B ALA 93   
436 1 Y 1 B ALA 94   ? B ALA 94   
437 1 Y 1 B ALA 95   ? B ALA 95   
438 1 Y 1 B ALA 96   ? B ALA 96   
439 1 Y 1 B ALA 97   ? B ALA 97   
440 1 Y 1 B ALA 98   ? B ALA 98   
441 1 Y 1 B ALA 99   ? B ALA 99   
442 1 Y 1 B ALA 100  ? B ALA 100  
443 1 Y 1 B ALA 101  ? B ALA 101  
444 1 Y 1 B ALA 102  ? B ALA 102  
445 1 Y 1 B ALA 103  ? B ALA 103  
446 1 Y 1 B ALA 104  ? B ALA 104  
447 1 Y 1 B ALA 105  ? B ALA 105  
448 1 Y 1 B ALA 106  ? B ALA 106  
449 1 Y 1 B ALA 107  ? B ALA 107  
450 1 Y 1 B GLY 108  ? B GLY 108  
451 1 Y 1 B ALA 109  ? B ALA 109  
452 1 Y 1 B GLY 110  ? B GLY 110  
453 1 Y 1 B ALA 111  ? B ALA 111  
454 1 Y 1 B GLY 112  ? B GLY 112  
455 1 Y 1 B ALA 113  ? B ALA 113  
456 1 Y 1 B LYS 114  ? B LYS 114  
457 1 Y 1 B GLN 115  ? B GLN 115  
458 1 Y 1 B THR 116  ? B THR 116  
459 1 Y 1 B PRO 117  ? B PRO 117  
460 1 Y 1 B ALA 118  ? B ALA 118  
461 1 Y 1 B ASP 119  ? B ASP 119  
462 1 Y 1 B GLY 120  ? B GLY 120  
463 1 Y 1 B GLU 121  ? B GLU 121  
464 1 Y 1 B ALA 122  ? B ALA 122  
465 1 Y 1 B SER 123  ? B SER 123  
466 1 Y 1 B GLY 124  ? B GLY 124  
467 1 Y 1 B GLU 125  ? B GLU 125  
468 1 Y 1 B SER 126  ? B SER 126  
469 1 Y 1 B GLU 127  ? B GLU 127  
470 1 Y 1 B PRO 128  ? B PRO 128  
471 1 Y 1 B ALA 129  ? B ALA 129  
472 1 Y 1 B LYS 130  ? B LYS 130  
473 1 Y 1 B GLY 131  ? B GLY 131  
474 1 Y 1 B SER 132  ? B SER 132  
475 1 Y 1 B GLU 133  ? B GLU 133  
476 1 Y 1 B GLU 134  ? B GLU 134  
477 1 Y 1 B ALA 135  ? B ALA 135  
478 1 Y 1 B LYS 136  ? B LYS 136  
479 1 Y 1 B GLY 137  ? B GLY 137  
480 1 Y 1 B ARG 138  ? B ARG 138  
481 1 Y 1 B PHE 139  ? B PHE 139  
482 1 Y 1 B ARG 140  ? B ARG 140  
483 1 Y 1 B VAL 141  ? B VAL 141  
484 1 Y 1 B ASN 142  ? B ASN 142  
485 1 Y 1 B PHE 143  ? B PHE 143  
486 1 Y 1 B VAL 144  ? B VAL 144  
487 1 Y 1 B ASP 145  ? B ASP 145  
488 1 Y 1 B PRO 146  ? B PRO 146  
489 1 Y 1 B ALA 147  ? B ALA 147  
490 1 Y 1 B ALA 148  ? B ALA 148  
491 1 Y 1 B SER 149  ? B SER 149  
492 1 Y 1 B SER 150  ? B SER 150  
493 1 Y 1 B SER 151  ? B SER 151  
494 1 Y 1 B ALA 152  ? B ALA 152  
495 1 Y 1 B GLU 153  ? B GLU 153  
496 1 Y 1 B ASP 154  ? B ASP 154  
497 1 Y 1 B SER 155  ? B SER 155  
498 1 Y 1 B LEU 156  ? B LEU 156  
499 1 Y 1 B SER 157  ? B SER 157  
500 1 Y 1 B ASP 158  ? B ASP 158  
501 1 Y 1 B ALA 159  ? B ALA 159  
502 1 Y 1 B ALA 160  ? B ALA 160  
503 1 Y 1 B GLY 161  ? B GLY 161  
504 1 Y 1 B VAL 162  ? B VAL 162  
505 1 Y 1 B GLY 163  ? B GLY 163  
506 1 Y 1 B VAL 164  ? B VAL 164  
507 1 Y 1 B ASP 165  ? B ASP 165  
508 1 Y 1 B GLY 166  ? B GLY 166  
509 1 Y 1 B PRO 167  ? B PRO 167  
510 1 Y 1 B ASN 168  ? B ASN 168  
511 1 Y 1 B VAL 169  ? B VAL 169  
512 1 Y 1 B SER 170  ? B SER 170  
513 1 Y 1 B PHE 171  ? B PHE 171  
514 1 Y 1 B GLN 172  ? B GLN 172  
515 1 Y 1 B ASN 173  ? B ASN 173  
516 1 Y 1 B GLY 174  ? B GLY 174  
517 1 Y 1 B GLY 175  ? B GLY 175  
518 1 Y 1 B ASP 176  ? B ASP 176  
519 1 Y 1 B THR 177  ? B THR 177  
520 1 Y 1 B VAL 178  ? B VAL 178  
521 1 Y 1 B LEU 179  ? B LEU 179  
522 1 Y 1 B SER 180  ? B SER 180  
523 1 Y 1 B GLU 181  ? B GLU 181  
524 1 Y 1 B GLY 182  ? B GLY 182  
525 1 Y 1 B SER 183  ? B SER 183  
526 1 Y 1 B SER 184  ? B SER 184  
527 1 Y 1 B LEU 185  ? B LEU 185  
528 1 Y 1 B HIS 186  ? B HIS 186  
529 1 Y 1 B SER 187  ? B SER 187  
530 1 Y 1 B GLY 188  ? B GLY 188  
531 1 Y 1 B GLY 189  ? B GLY 189  
532 1 Y 1 B GLY 190  ? B GLY 190  
533 1 Y 1 B GLY 191  ? B GLY 191  
534 1 Y 1 B GLY 192  ? B GLY 192  
535 1 Y 1 B SER 193  ? B SER 193  
536 1 Y 1 B GLY 194  ? B GLY 194  
537 1 Y 1 B HIS 195  ? B HIS 195  
538 1 Y 1 B HIS 196  ? B HIS 196  
539 1 Y 1 B GLN 197  ? B GLN 197  
540 1 Y 1 B HIS 198  ? B HIS 198  
541 1 Y 1 B TYR 199  ? B TYR 199  
542 1 Y 1 B TYR 200  ? B TYR 200  
543 1 Y 1 B TYR 201  ? B TYR 201  
544 1 Y 1 B ASP 202  ? B ASP 202  
545 1 Y 1 B THR 203  ? B THR 203  
546 1 Y 1 B HIS 204  ? B HIS 204  
547 1 Y 1 B THR 205  ? B THR 205  
548 1 Y 1 B ASN 206  ? B ASN 206  
549 1 Y 1 B THR 207  ? B THR 207  
550 1 Y 1 B TYR 208  ? B TYR 208  
551 1 Y 1 B TYR 209  ? B TYR 209  
552 1 Y 1 B LEU 210  ? B LEU 210  
553 1 Y 1 B ARG 211  ? B ARG 211  
554 1 Y 1 B THR 212  ? B THR 212  
555 1 Y 1 B PHE 213  ? B PHE 213  
556 1 Y 1 B GLY 214  ? B GLY 214  
557 1 Y 1 B HIS 215  ? B HIS 215  
558 1 Y 1 B ASN 216  ? B ASN 216  
559 1 Y 1 B GLU 251  ? B GLU 251  
560 1 Y 1 B LYS 252  ? B LYS 252  
561 1 Y 1 B GLU 253  ? B GLU 253  
562 1 Y 1 B PRO 254  ? B PRO 254  
563 1 Y 1 B PHE 255  ? B PHE 255  
564 1 Y 1 B GLU 256  ? B GLU 256  
565 1 Y 1 B ASP 257  ? B ASP 257  
566 1 Y 1 B GLY 258  ? B GLY 258  
567 1 Y 1 B PHE 259  ? B PHE 259  
568 1 Y 1 B ALA 260  ? B ALA 260  
569 1 Y 1 B ASN 261  ? B ASN 261  
570 1 Y 1 B GLY 262  ? B GLY 262  
571 1 Y 1 B GLU 263  ? B GLU 263  
572 1 Y 1 B GLU 264  ? B GLU 264  
573 1 Y 1 B SER 265  ? B SER 265  
574 1 Y 1 B THR 266  ? B THR 266  
575 1 Y 1 B PRO 267  ? B PRO 267  
576 1 Y 1 B THR 268  ? B THR 268  
577 1 Y 1 B ARG 269  ? B ARG 269  
578 1 Y 1 B ASP 270  ? B ASP 270  
579 1 Y 1 B ALA 271  ? B ALA 271  
580 1 Y 1 B VAL 272  ? B VAL 272  
581 1 Y 1 B VAL 273  ? B VAL 273  
582 1 Y 1 B THR 274  ? B THR 274  
583 1 Y 1 B TYR 275  ? B TYR 275  
584 1 Y 1 B THR 276  ? B THR 276  
585 1 Y 1 B ALA 277  ? B ALA 277  
586 1 Y 1 B GLU 278  ? B GLU 278  
587 1 Y 1 B SER 279  ? B SER 279  
588 1 Y 1 B LYS 280  ? B LYS 280  
589 1 Y 1 B GLY 281  ? B GLY 281  
590 1 Y 1 B ASP 927  ? B ASP 927  
591 1 Y 1 B ILE 928  ? B ILE 928  
592 1 Y 1 B SER 929  ? B SER 929  
593 1 Y 1 B HIS 930  ? B HIS 930  
594 1 Y 1 B LEU 931  ? B LEU 931  
595 1 Y 1 B GLN 932  ? B GLN 932  
596 1 Y 1 B GLY 933  ? B GLY 933  
597 1 Y 1 B GLN 934  ? B GLN 934  
598 1 Y 1 B GLU 935  ? B GLU 935  
599 1 Y 1 B GLU 936  ? B GLU 936  
600 1 Y 1 B LEU 937  ? B LEU 937  
601 1 Y 1 B LEU 938  ? B LEU 938  
602 1 Y 1 B SER 939  ? B SER 939  
603 1 Y 1 B SER 940  ? B SER 940  
604 1 Y 1 B GLN 941  ? B GLN 941  
605 1 Y 1 B GLU 942  ? B GLU 942  
606 1 Y 1 B LYS 943  ? B LYS 943  
607 1 Y 1 B SER 944  ? B SER 944  
608 1 Y 1 B PRO 945  ? B PRO 945  
609 1 Y 1 B GLY 946  ? B GLY 946  
610 1 Y 1 B THR 947  ? B THR 947  
611 1 Y 1 B LYS 948  ? B LYS 948  
612 1 Y 1 B ASP 949  ? B ASP 949  
613 1 Y 1 B VAL 950  ? B VAL 950  
614 1 Y 1 B VAL 951  ? B VAL 951  
615 1 Y 1 B VAL 952  ? B VAL 952  
616 1 Y 1 B SER 953  ? B SER 953  
617 1 Y 1 B VAL 954  ? B VAL 954  
618 1 Y 1 B GLU 955  ? B GLU 955  
619 1 Y 1 B TYR 956  ? B TYR 956  
620 1 Y 1 B SER 957  ? B SER 957  
621 1 Y 1 B LYS 958  ? B LYS 958  
622 1 Y 1 B LYS 959  ? B LYS 959  
623 1 Y 1 B SER 960  ? B SER 960  
624 1 Y 1 B ASP 961  ? B ASP 961  
625 1 Y 1 B LEU 962  ? B LEU 962  
626 1 Y 1 B ASP 963  ? B ASP 963  
627 1 Y 1 B THR 964  ? B THR 964  
628 1 Y 1 B SER 965  ? B SER 965  
629 1 Y 1 B LYS 966  ? B LYS 966  
630 1 Y 1 B PRO 967  ? B PRO 967  
631 1 Y 1 B LEU 968  ? B LEU 968  
632 1 Y 1 B SER 969  ? B SER 969  
633 1 Y 1 B GLU 970  ? B GLU 970  
634 1 Y 1 B LYS 971  ? B LYS 971  
635 1 Y 1 B PRO 972  ? B PRO 972  
636 1 Y 1 B ILE 973  ? B ILE 973  
637 1 Y 1 B THR 974  ? B THR 974  
638 1 Y 1 B HIS 975  ? B HIS 975  
639 1 Y 1 B LYS 976  ? B LYS 976  
640 1 Y 1 B VAL 977  ? B VAL 977  
641 1 Y 1 B GLU 978  ? B GLU 978  
642 1 Y 1 B GLU 979  ? B GLU 979  
643 1 Y 1 B GLU 980  ? B GLU 980  
644 1 Y 1 B ASP 981  ? B ASP 981  
645 1 Y 1 B GLY 982  ? B GLY 982  
646 1 Y 1 B LYS 983  ? B LYS 983  
647 1 Y 1 B THR 984  ? B THR 984  
648 1 Y 1 B ALA 985  ? B ALA 985  
649 1 Y 1 B THR 986  ? B THR 986  
650 1 Y 1 B GLN 987  ? B GLN 987  
651 1 Y 1 B PRO 988  ? B PRO 988  
652 1 Y 1 B LEU 989  ? B LEU 989  
653 1 Y 1 B LEU 990  ? B LEU 990  
654 1 Y 1 B LYS 991  ? B LYS 991  
655 1 Y 1 B LYS 992  ? B LYS 992  
656 1 Y 1 B GLU 993  ? B GLU 993  
657 1 Y 1 B SER 994  ? B SER 994  
658 1 Y 1 B LYS 995  ? B LYS 995  
659 1 Y 1 B GLY 996  ? B GLY 996  
660 1 Y 1 B PRO 997  ? B PRO 997  
661 1 Y 1 B ILE 998  ? B ILE 998  
662 1 Y 1 B VAL 999  ? B VAL 999  
663 1 Y 1 B PRO 1000 ? B PRO 1000 
664 1 Y 1 B LEU 1001 ? B LEU 1001 
665 1 Y 1 B ASN 1002 ? B ASN 1002 
666 1 Y 1 B VAL 1003 ? B VAL 1003 
667 1 Y 1 B ALA 1004 ? B ALA 1004 
668 1 Y 1 B ASP 1005 ? B ASP 1005 
669 1 Y 1 B GLN 1006 ? B GLN 1006 
670 1 Y 1 B LYS 1007 ? B LYS 1007 
671 1 Y 1 B LEU 1008 ? B LEU 1008 
672 1 Y 1 B LEU 1009 ? B LEU 1009 
673 1 Y 1 B GLU 1010 ? B GLU 1010 
674 1 Y 1 B ALA 1011 ? B ALA 1011 
675 1 Y 1 B SER 1012 ? B SER 1012 
676 1 Y 1 B THR 1013 ? B THR 1013 
677 1 Y 1 B GLN 1014 ? B GLN 1014 
678 1 Y 1 B PHE 1015 ? B PHE 1015 
679 1 Y 1 B GLN 1016 ? B GLN 1016 
680 1 Y 1 B LYS 1017 ? B LYS 1017 
681 1 Y 1 B LYS 1018 ? B LYS 1018 
682 1 Y 1 B GLN 1019 ? B GLN 1019 
683 1 Y 1 B GLY 1020 ? B GLY 1020 
684 1 Y 1 B LYS 1021 ? B LYS 1021 
# 
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 
A1ATU N1    N  N N 1   
A1ATU N3    N  N N 2   
A1ATU C4    C  Y N 3   
A1ATU C5    C  Y N 4   
A1ATU C6    C  N N 5   
A1ATU C10   C  Y N 6   
A1ATU C15   C  N N 7   
A1ATU C1    C  N N 8   
A1ATU "C1'" C  Y N 9   
A1ATU C11   C  Y N 10  
A1ATU C12   C  Y N 11  
A1ATU C16   C  N N 12  
A1ATU C2    C  N N 13  
A1ATU "C2'" C  Y N 14  
A1ATU "C3'" C  Y N 15  
A1ATU "C4'" C  Y N 16  
A1ATU "C5'" C  Y N 17  
A1ATU C9    C  Y N 18  
A1ATU N7    N  Y N 19  
A1ATU N9    N  N N 20  
A1ATU O6    O  N N 21  
A1ATU OP1   O  N N 22  
A1ATU OP3   O  N N 23  
A1ATU S1    S  N N 24  
A1ATU H13   H  N N 25  
A1ATU H12   H  N N 26  
A1ATU H5    H  N N 27  
A1ATU H9    H  N N 28  
A1ATU H17   H  N N 29  
A1ATU H16   H  N N 30  
A1ATU H15   H  N N 31  
A1ATU H3    H  N N 32  
A1ATU H1    H  N N 33  
A1ATU H2    H  N N 34  
A1ATU H10   H  N N 35  
A1ATU H11   H  N N 36  
A1ATU H20   H  N N 37  
A1ATU H19   H  N N 38  
A1ATU H18   H  N N 39  
A1ATU H14   H  N N 40  
A1ATU H4    H  N N 41  
A1ATU H7    H  N N 42  
A1ATU H6    H  N N 43  
A1ATU H8    H  N N 44  
ALA   N     N  N N 45  
ALA   CA    C  N S 46  
ALA   C     C  N N 47  
ALA   O     O  N N 48  
ALA   CB    C  N N 49  
ALA   OXT   O  N N 50  
ALA   H     H  N N 51  
ALA   H2    H  N N 52  
ALA   HA    H  N N 53  
ALA   HB1   H  N N 54  
ALA   HB2   H  N N 55  
ALA   HB3   H  N N 56  
ALA   HXT   H  N N 57  
ARG   N     N  N N 58  
ARG   CA    C  N S 59  
ARG   C     C  N N 60  
ARG   O     O  N N 61  
ARG   CB    C  N N 62  
ARG   CG    C  N N 63  
ARG   CD    C  N N 64  
ARG   NE    N  N N 65  
ARG   CZ    C  N N 66  
ARG   NH1   N  N N 67  
ARG   NH2   N  N N 68  
ARG   OXT   O  N N 69  
ARG   H     H  N N 70  
ARG   H2    H  N N 71  
ARG   HA    H  N N 72  
ARG   HB2   H  N N 73  
ARG   HB3   H  N N 74  
ARG   HG2   H  N N 75  
ARG   HG3   H  N N 76  
ARG   HD2   H  N N 77  
ARG   HD3   H  N N 78  
ARG   HE    H  N N 79  
ARG   HH11  H  N N 80  
ARG   HH12  H  N N 81  
ARG   HH21  H  N N 82  
ARG   HH22  H  N N 83  
ARG   HXT   H  N N 84  
ASN   N     N  N N 85  
ASN   CA    C  N S 86  
ASN   C     C  N N 87  
ASN   O     O  N N 88  
ASN   CB    C  N N 89  
ASN   CG    C  N N 90  
ASN   OD1   O  N N 91  
ASN   ND2   N  N N 92  
ASN   OXT   O  N N 93  
ASN   H     H  N N 94  
ASN   H2    H  N N 95  
ASN   HA    H  N N 96  
ASN   HB2   H  N N 97  
ASN   HB3   H  N N 98  
ASN   HD21  H  N N 99  
ASN   HD22  H  N N 100 
ASN   HXT   H  N N 101 
ASP   N     N  N N 102 
ASP   CA    C  N S 103 
ASP   C     C  N N 104 
ASP   O     O  N N 105 
ASP   CB    C  N N 106 
ASP   CG    C  N N 107 
ASP   OD1   O  N N 108 
ASP   OD2   O  N N 109 
ASP   OXT   O  N N 110 
ASP   H     H  N N 111 
ASP   H2    H  N N 112 
ASP   HA    H  N N 113 
ASP   HB2   H  N N 114 
ASP   HB3   H  N N 115 
ASP   HD2   H  N N 116 
ASP   HXT   H  N N 117 
CL    CL    CL N N 118 
CYS   N     N  N N 119 
CYS   CA    C  N R 120 
CYS   C     C  N N 121 
CYS   O     O  N N 122 
CYS   CB    C  N N 123 
CYS   SG    S  N N 124 
CYS   OXT   O  N N 125 
CYS   H     H  N N 126 
CYS   H2    H  N N 127 
CYS   HA    H  N N 128 
CYS   HB2   H  N N 129 
CYS   HB3   H  N N 130 
CYS   HG    H  N N 131 
CYS   HXT   H  N N 132 
GLN   N     N  N N 133 
GLN   CA    C  N S 134 
GLN   C     C  N N 135 
GLN   O     O  N N 136 
GLN   CB    C  N N 137 
GLN   CG    C  N N 138 
GLN   CD    C  N N 139 
GLN   OE1   O  N N 140 
GLN   NE2   N  N N 141 
GLN   OXT   O  N N 142 
GLN   H     H  N N 143 
GLN   H2    H  N N 144 
GLN   HA    H  N N 145 
GLN   HB2   H  N N 146 
GLN   HB3   H  N N 147 
GLN   HG2   H  N N 148 
GLN   HG3   H  N N 149 
GLN   HE21  H  N N 150 
GLN   HE22  H  N N 151 
GLN   HXT   H  N N 152 
GLU   N     N  N N 153 
GLU   CA    C  N S 154 
GLU   C     C  N N 155 
GLU   O     O  N N 156 
GLU   CB    C  N N 157 
GLU   CG    C  N N 158 
GLU   CD    C  N N 159 
GLU   OE1   O  N N 160 
GLU   OE2   O  N N 161 
GLU   OXT   O  N N 162 
GLU   H     H  N N 163 
GLU   H2    H  N N 164 
GLU   HA    H  N N 165 
GLU   HB2   H  N N 166 
GLU   HB3   H  N N 167 
GLU   HG2   H  N N 168 
GLU   HG3   H  N N 169 
GLU   HE2   H  N N 170 
GLU   HXT   H  N N 171 
GLY   N     N  N N 172 
GLY   CA    C  N N 173 
GLY   C     C  N N 174 
GLY   O     O  N N 175 
GLY   OXT   O  N N 176 
GLY   H     H  N N 177 
GLY   H2    H  N N 178 
GLY   HA2   H  N N 179 
GLY   HA3   H  N N 180 
GLY   HXT   H  N N 181 
HIS   N     N  N N 182 
HIS   CA    C  N S 183 
HIS   C     C  N N 184 
HIS   O     O  N N 185 
HIS   CB    C  N N 186 
HIS   CG    C  Y N 187 
HIS   ND1   N  Y N 188 
HIS   CD2   C  Y N 189 
HIS   CE1   C  Y N 190 
HIS   NE2   N  Y N 191 
HIS   OXT   O  N N 192 
HIS   H     H  N N 193 
HIS   H2    H  N N 194 
HIS   HA    H  N N 195 
HIS   HB2   H  N N 196 
HIS   HB3   H  N N 197 
HIS   HD1   H  N N 198 
HIS   HD2   H  N N 199 
HIS   HE1   H  N N 200 
HIS   HE2   H  N N 201 
HIS   HXT   H  N N 202 
HOH   O     O  N N 203 
HOH   H1    H  N N 204 
HOH   H2    H  N N 205 
ILE   N     N  N N 206 
ILE   CA    C  N S 207 
ILE   C     C  N N 208 
ILE   O     O  N N 209 
ILE   CB    C  N S 210 
ILE   CG1   C  N N 211 
ILE   CG2   C  N N 212 
ILE   CD1   C  N N 213 
ILE   OXT   O  N N 214 
ILE   H     H  N N 215 
ILE   H2    H  N N 216 
ILE   HA    H  N N 217 
ILE   HB    H  N N 218 
ILE   HG12  H  N N 219 
ILE   HG13  H  N N 220 
ILE   HG21  H  N N 221 
ILE   HG22  H  N N 222 
ILE   HG23  H  N N 223 
ILE   HD11  H  N N 224 
ILE   HD12  H  N N 225 
ILE   HD13  H  N N 226 
ILE   HXT   H  N N 227 
LEU   N     N  N N 228 
LEU   CA    C  N S 229 
LEU   C     C  N N 230 
LEU   O     O  N N 231 
LEU   CB    C  N N 232 
LEU   CG    C  N N 233 
LEU   CD1   C  N N 234 
LEU   CD2   C  N N 235 
LEU   OXT   O  N N 236 
LEU   H     H  N N 237 
LEU   H2    H  N N 238 
LEU   HA    H  N N 239 
LEU   HB2   H  N N 240 
LEU   HB3   H  N N 241 
LEU   HG    H  N N 242 
LEU   HD11  H  N N 243 
LEU   HD12  H  N N 244 
LEU   HD13  H  N N 245 
LEU   HD21  H  N N 246 
LEU   HD22  H  N N 247 
LEU   HD23  H  N N 248 
LEU   HXT   H  N N 249 
LYS   N     N  N N 250 
LYS   CA    C  N S 251 
LYS   C     C  N N 252 
LYS   O     O  N N 253 
LYS   CB    C  N N 254 
LYS   CG    C  N N 255 
LYS   CD    C  N N 256 
LYS   CE    C  N N 257 
LYS   NZ    N  N N 258 
LYS   OXT   O  N N 259 
LYS   H     H  N N 260 
LYS   H2    H  N N 261 
LYS   HA    H  N N 262 
LYS   HB2   H  N N 263 
LYS   HB3   H  N N 264 
LYS   HG2   H  N N 265 
LYS   HG3   H  N N 266 
LYS   HD2   H  N N 267 
LYS   HD3   H  N N 268 
LYS   HE2   H  N N 269 
LYS   HE3   H  N N 270 
LYS   HZ1   H  N N 271 
LYS   HZ2   H  N N 272 
LYS   HZ3   H  N N 273 
LYS   HXT   H  N N 274 
MET   N     N  N N 275 
MET   CA    C  N S 276 
MET   C     C  N N 277 
MET   O     O  N N 278 
MET   CB    C  N N 279 
MET   CG    C  N N 280 
MET   SD    S  N N 281 
MET   CE    C  N N 282 
MET   OXT   O  N N 283 
MET   H     H  N N 284 
MET   H2    H  N N 285 
MET   HA    H  N N 286 
MET   HB2   H  N N 287 
MET   HB3   H  N N 288 
MET   HG2   H  N N 289 
MET   HG3   H  N N 290 
MET   HE1   H  N N 291 
MET   HE2   H  N N 292 
MET   HE3   H  N N 293 
MET   HXT   H  N N 294 
NA    NA    NA N N 295 
PHE   N     N  N N 296 
PHE   CA    C  N S 297 
PHE   C     C  N N 298 
PHE   O     O  N N 299 
PHE   CB    C  N N 300 
PHE   CG    C  Y N 301 
PHE   CD1   C  Y N 302 
PHE   CD2   C  Y N 303 
PHE   CE1   C  Y N 304 
PHE   CE2   C  Y N 305 
PHE   CZ    C  Y N 306 
PHE   OXT   O  N N 307 
PHE   H     H  N N 308 
PHE   H2    H  N N 309 
PHE   HA    H  N N 310 
PHE   HB2   H  N N 311 
PHE   HB3   H  N N 312 
PHE   HD1   H  N N 313 
PHE   HD2   H  N N 314 
PHE   HE1   H  N N 315 
PHE   HE2   H  N N 316 
PHE   HZ    H  N N 317 
PHE   HXT   H  N N 318 
PRO   N     N  N N 319 
PRO   CA    C  N S 320 
PRO   C     C  N N 321 
PRO   O     O  N N 322 
PRO   CB    C  N N 323 
PRO   CG    C  N N 324 
PRO   CD    C  N N 325 
PRO   OXT   O  N N 326 
PRO   H     H  N N 327 
PRO   HA    H  N N 328 
PRO   HB2   H  N N 329 
PRO   HB3   H  N N 330 
PRO   HG2   H  N N 331 
PRO   HG3   H  N N 332 
PRO   HD2   H  N N 333 
PRO   HD3   H  N N 334 
PRO   HXT   H  N N 335 
SER   N     N  N N 336 
SER   CA    C  N S 337 
SER   C     C  N N 338 
SER   O     O  N N 339 
SER   CB    C  N N 340 
SER   OG    O  N N 341 
SER   OXT   O  N N 342 
SER   H     H  N N 343 
SER   H2    H  N N 344 
SER   HA    H  N N 345 
SER   HB2   H  N N 346 
SER   HB3   H  N N 347 
SER   HG    H  N N 348 
SER   HXT   H  N N 349 
THR   N     N  N N 350 
THR   CA    C  N S 351 
THR   C     C  N N 352 
THR   O     O  N N 353 
THR   CB    C  N R 354 
THR   OG1   O  N N 355 
THR   CG2   C  N N 356 
THR   OXT   O  N N 357 
THR   H     H  N N 358 
THR   H2    H  N N 359 
THR   HA    H  N N 360 
THR   HB    H  N N 361 
THR   HG1   H  N N 362 
THR   HG21  H  N N 363 
THR   HG22  H  N N 364 
THR   HG23  H  N N 365 
THR   HXT   H  N N 366 
TPO   N     N  N N 367 
TPO   CA    C  N S 368 
TPO   CB    C  N R 369 
TPO   CG2   C  N N 370 
TPO   OG1   O  N N 371 
TPO   P     P  N N 372 
TPO   O1P   O  N N 373 
TPO   O2P   O  N N 374 
TPO   O3P   O  N N 375 
TPO   C     C  N N 376 
TPO   O     O  N N 377 
TPO   OXT   O  N N 378 
TPO   H     H  N N 379 
TPO   H2    H  N N 380 
TPO   HA    H  N N 381 
TPO   HB    H  N N 382 
TPO   HG21  H  N N 383 
TPO   HG22  H  N N 384 
TPO   HG23  H  N N 385 
TPO   HOP2  H  N N 386 
TPO   HOP3  H  N N 387 
TPO   HXT   H  N N 388 
TRP   N     N  N N 389 
TRP   CA    C  N S 390 
TRP   C     C  N N 391 
TRP   O     O  N N 392 
TRP   CB    C  N N 393 
TRP   CG    C  Y N 394 
TRP   CD1   C  Y N 395 
TRP   CD2   C  Y N 396 
TRP   NE1   N  Y N 397 
TRP   CE2   C  Y N 398 
TRP   CE3   C  Y N 399 
TRP   CZ2   C  Y N 400 
TRP   CZ3   C  Y N 401 
TRP   CH2   C  Y N 402 
TRP   OXT   O  N N 403 
TRP   H     H  N N 404 
TRP   H2    H  N N 405 
TRP   HA    H  N N 406 
TRP   HB2   H  N N 407 
TRP   HB3   H  N N 408 
TRP   HD1   H  N N 409 
TRP   HE1   H  N N 410 
TRP   HE3   H  N N 411 
TRP   HZ2   H  N N 412 
TRP   HZ3   H  N N 413 
TRP   HH2   H  N N 414 
TRP   HXT   H  N N 415 
TYR   N     N  N N 416 
TYR   CA    C  N S 417 
TYR   C     C  N N 418 
TYR   O     O  N N 419 
TYR   CB    C  N N 420 
TYR   CG    C  Y N 421 
TYR   CD1   C  Y N 422 
TYR   CD2   C  Y N 423 
TYR   CE1   C  Y N 424 
TYR   CE2   C  Y N 425 
TYR   CZ    C  Y N 426 
TYR   OH    O  N N 427 
TYR   OXT   O  N N 428 
TYR   H     H  N N 429 
TYR   H2    H  N N 430 
TYR   HA    H  N N 431 
TYR   HB2   H  N N 432 
TYR   HB3   H  N N 433 
TYR   HD1   H  N N 434 
TYR   HD2   H  N N 435 
TYR   HE1   H  N N 436 
TYR   HE2   H  N N 437 
TYR   HH    H  N N 438 
TYR   HXT   H  N N 439 
VAL   N     N  N N 440 
VAL   CA    C  N S 441 
VAL   C     C  N N 442 
VAL   O     O  N N 443 
VAL   CB    C  N N 444 
VAL   CG1   C  N N 445 
VAL   CG2   C  N N 446 
VAL   OXT   O  N N 447 
VAL   H     H  N N 448 
VAL   H2    H  N N 449 
VAL   HA    H  N N 450 
VAL   HB    H  N N 451 
VAL   HG11  H  N N 452 
VAL   HG12  H  N N 453 
VAL   HG13  H  N N 454 
VAL   HG21  H  N N 455 
VAL   HG22  H  N N 456 
VAL   HG23  H  N N 457 
VAL   HXT   H  N N 458 
# 
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 
A1ATU C11   N7    doub Y N 1   
A1ATU C11   C12   sing Y N 2   
A1ATU C1    "C3'" sing N N 3   
A1ATU N7    C10   sing Y N 4   
A1ATU C12   C4    doub Y N 5   
A1ATU "C3'" "C2'" doub Y N 6   
A1ATU "C3'" "C4'" sing Y N 7   
A1ATU "C2'" "C1'" sing Y N 8   
A1ATU "C4'" "C5'" doub Y N 9   
A1ATU C10   C9    doub Y N 10  
A1ATU C4    C9    sing Y N 11  
A1ATU C4    N9    sing N N 12  
A1ATU "C1'" N9    sing N N 13  
A1ATU "C1'" C5    doub Y N 14  
A1ATU "C5'" C5    sing Y N 15  
A1ATU C9    S1    sing N N 16  
A1ATU C15   C2    sing N N 17  
A1ATU S1    N3    sing N N 18  
A1ATU S1    OP3   doub N N 19  
A1ATU S1    OP1   doub N N 20  
A1ATU N1    C2    sing N N 21  
A1ATU N1    C6    sing N N 22  
A1ATU N3    C6    sing N N 23  
A1ATU C2    C16   sing N N 24  
A1ATU C6    O6    doub N N 25  
A1ATU N1    H13   sing N N 26  
A1ATU N3    H12   sing N N 27  
A1ATU C5    H5    sing N N 28  
A1ATU C10   H9    sing N N 29  
A1ATU C15   H17   sing N N 30  
A1ATU C15   H16   sing N N 31  
A1ATU C15   H15   sing N N 32  
A1ATU C1    H3    sing N N 33  
A1ATU C1    H1    sing N N 34  
A1ATU C1    H2    sing N N 35  
A1ATU C11   H10   sing N N 36  
A1ATU C12   H11   sing N N 37  
A1ATU C16   H20   sing N N 38  
A1ATU C16   H19   sing N N 39  
A1ATU C16   H18   sing N N 40  
A1ATU C2    H14   sing N N 41  
A1ATU "C2'" H4    sing N N 42  
A1ATU "C4'" H7    sing N N 43  
A1ATU "C5'" H6    sing N N 44  
A1ATU N9    H8    sing N N 45  
ALA   N     CA    sing N N 46  
ALA   N     H     sing N N 47  
ALA   N     H2    sing N N 48  
ALA   CA    C     sing N N 49  
ALA   CA    CB    sing N N 50  
ALA   CA    HA    sing N N 51  
ALA   C     O     doub N N 52  
ALA   C     OXT   sing N N 53  
ALA   CB    HB1   sing N N 54  
ALA   CB    HB2   sing N N 55  
ALA   CB    HB3   sing N N 56  
ALA   OXT   HXT   sing N N 57  
ARG   N     CA    sing N N 58  
ARG   N     H     sing N N 59  
ARG   N     H2    sing N N 60  
ARG   CA    C     sing N N 61  
ARG   CA    CB    sing N N 62  
ARG   CA    HA    sing N N 63  
ARG   C     O     doub N N 64  
ARG   C     OXT   sing N N 65  
ARG   CB    CG    sing N N 66  
ARG   CB    HB2   sing N N 67  
ARG   CB    HB3   sing N N 68  
ARG   CG    CD    sing N N 69  
ARG   CG    HG2   sing N N 70  
ARG   CG    HG3   sing N N 71  
ARG   CD    NE    sing N N 72  
ARG   CD    HD2   sing N N 73  
ARG   CD    HD3   sing N N 74  
ARG   NE    CZ    sing N N 75  
ARG   NE    HE    sing N N 76  
ARG   CZ    NH1   sing N N 77  
ARG   CZ    NH2   doub N N 78  
ARG   NH1   HH11  sing N N 79  
ARG   NH1   HH12  sing N N 80  
ARG   NH2   HH21  sing N N 81  
ARG   NH2   HH22  sing N N 82  
ARG   OXT   HXT   sing N N 83  
ASN   N     CA    sing N N 84  
ASN   N     H     sing N N 85  
ASN   N     H2    sing N N 86  
ASN   CA    C     sing N N 87  
ASN   CA    CB    sing N N 88  
ASN   CA    HA    sing N N 89  
ASN   C     O     doub N N 90  
ASN   C     OXT   sing N N 91  
ASN   CB    CG    sing N N 92  
ASN   CB    HB2   sing N N 93  
ASN   CB    HB3   sing N N 94  
ASN   CG    OD1   doub N N 95  
ASN   CG    ND2   sing N N 96  
ASN   ND2   HD21  sing N N 97  
ASN   ND2   HD22  sing N N 98  
ASN   OXT   HXT   sing N N 99  
ASP   N     CA    sing N N 100 
ASP   N     H     sing N N 101 
ASP   N     H2    sing N N 102 
ASP   CA    C     sing N N 103 
ASP   CA    CB    sing N N 104 
ASP   CA    HA    sing N N 105 
ASP   C     O     doub N N 106 
ASP   C     OXT   sing N N 107 
ASP   CB    CG    sing N N 108 
ASP   CB    HB2   sing N N 109 
ASP   CB    HB3   sing N N 110 
ASP   CG    OD1   doub N N 111 
ASP   CG    OD2   sing N N 112 
ASP   OD2   HD2   sing N N 113 
ASP   OXT   HXT   sing N N 114 
CYS   N     CA    sing N N 115 
CYS   N     H     sing N N 116 
CYS   N     H2    sing N N 117 
CYS   CA    C     sing N N 118 
CYS   CA    CB    sing N N 119 
CYS   CA    HA    sing N N 120 
CYS   C     O     doub N N 121 
CYS   C     OXT   sing N N 122 
CYS   CB    SG    sing N N 123 
CYS   CB    HB2   sing N N 124 
CYS   CB    HB3   sing N N 125 
CYS   SG    HG    sing N N 126 
CYS   OXT   HXT   sing N N 127 
GLN   N     CA    sing N N 128 
GLN   N     H     sing N N 129 
GLN   N     H2    sing N N 130 
GLN   CA    C     sing N N 131 
GLN   CA    CB    sing N N 132 
GLN   CA    HA    sing N N 133 
GLN   C     O     doub N N 134 
GLN   C     OXT   sing N N 135 
GLN   CB    CG    sing N N 136 
GLN   CB    HB2   sing N N 137 
GLN   CB    HB3   sing N N 138 
GLN   CG    CD    sing N N 139 
GLN   CG    HG2   sing N N 140 
GLN   CG    HG3   sing N N 141 
GLN   CD    OE1   doub N N 142 
GLN   CD    NE2   sing N N 143 
GLN   NE2   HE21  sing N N 144 
GLN   NE2   HE22  sing N N 145 
GLN   OXT   HXT   sing N N 146 
GLU   N     CA    sing N N 147 
GLU   N     H     sing N N 148 
GLU   N     H2    sing N N 149 
GLU   CA    C     sing N N 150 
GLU   CA    CB    sing N N 151 
GLU   CA    HA    sing N N 152 
GLU   C     O     doub N N 153 
GLU   C     OXT   sing N N 154 
GLU   CB    CG    sing N N 155 
GLU   CB    HB2   sing N N 156 
GLU   CB    HB3   sing N N 157 
GLU   CG    CD    sing N N 158 
GLU   CG    HG2   sing N N 159 
GLU   CG    HG3   sing N N 160 
GLU   CD    OE1   doub N N 161 
GLU   CD    OE2   sing N N 162 
GLU   OE2   HE2   sing N N 163 
GLU   OXT   HXT   sing N N 164 
GLY   N     CA    sing N N 165 
GLY   N     H     sing N N 166 
GLY   N     H2    sing N N 167 
GLY   CA    C     sing N N 168 
GLY   CA    HA2   sing N N 169 
GLY   CA    HA3   sing N N 170 
GLY   C     O     doub N N 171 
GLY   C     OXT   sing N N 172 
GLY   OXT   HXT   sing N N 173 
HIS   N     CA    sing N N 174 
HIS   N     H     sing N N 175 
HIS   N     H2    sing N N 176 
HIS   CA    C     sing N N 177 
HIS   CA    CB    sing N N 178 
HIS   CA    HA    sing N N 179 
HIS   C     O     doub N N 180 
HIS   C     OXT   sing N N 181 
HIS   CB    CG    sing N N 182 
HIS   CB    HB2   sing N N 183 
HIS   CB    HB3   sing N N 184 
HIS   CG    ND1   sing Y N 185 
HIS   CG    CD2   doub Y N 186 
HIS   ND1   CE1   doub Y N 187 
HIS   ND1   HD1   sing N N 188 
HIS   CD2   NE2   sing Y N 189 
HIS   CD2   HD2   sing N N 190 
HIS   CE1   NE2   sing Y N 191 
HIS   CE1   HE1   sing N N 192 
HIS   NE2   HE2   sing N N 193 
HIS   OXT   HXT   sing N N 194 
HOH   O     H1    sing N N 195 
HOH   O     H2    sing N N 196 
ILE   N     CA    sing N N 197 
ILE   N     H     sing N N 198 
ILE   N     H2    sing N N 199 
ILE   CA    C     sing N N 200 
ILE   CA    CB    sing N N 201 
ILE   CA    HA    sing N N 202 
ILE   C     O     doub N N 203 
ILE   C     OXT   sing N N 204 
ILE   CB    CG1   sing N N 205 
ILE   CB    CG2   sing N N 206 
ILE   CB    HB    sing N N 207 
ILE   CG1   CD1   sing N N 208 
ILE   CG1   HG12  sing N N 209 
ILE   CG1   HG13  sing N N 210 
ILE   CG2   HG21  sing N N 211 
ILE   CG2   HG22  sing N N 212 
ILE   CG2   HG23  sing N N 213 
ILE   CD1   HD11  sing N N 214 
ILE   CD1   HD12  sing N N 215 
ILE   CD1   HD13  sing N N 216 
ILE   OXT   HXT   sing N N 217 
LEU   N     CA    sing N N 218 
LEU   N     H     sing N N 219 
LEU   N     H2    sing N N 220 
LEU   CA    C     sing N N 221 
LEU   CA    CB    sing N N 222 
LEU   CA    HA    sing N N 223 
LEU   C     O     doub N N 224 
LEU   C     OXT   sing N N 225 
LEU   CB    CG    sing N N 226 
LEU   CB    HB2   sing N N 227 
LEU   CB    HB3   sing N N 228 
LEU   CG    CD1   sing N N 229 
LEU   CG    CD2   sing N N 230 
LEU   CG    HG    sing N N 231 
LEU   CD1   HD11  sing N N 232 
LEU   CD1   HD12  sing N N 233 
LEU   CD1   HD13  sing N N 234 
LEU   CD2   HD21  sing N N 235 
LEU   CD2   HD22  sing N N 236 
LEU   CD2   HD23  sing N N 237 
LEU   OXT   HXT   sing N N 238 
LYS   N     CA    sing N N 239 
LYS   N     H     sing N N 240 
LYS   N     H2    sing N N 241 
LYS   CA    C     sing N N 242 
LYS   CA    CB    sing N N 243 
LYS   CA    HA    sing N N 244 
LYS   C     O     doub N N 245 
LYS   C     OXT   sing N N 246 
LYS   CB    CG    sing N N 247 
LYS   CB    HB2   sing N N 248 
LYS   CB    HB3   sing N N 249 
LYS   CG    CD    sing N N 250 
LYS   CG    HG2   sing N N 251 
LYS   CG    HG3   sing N N 252 
LYS   CD    CE    sing N N 253 
LYS   CD    HD2   sing N N 254 
LYS   CD    HD3   sing N N 255 
LYS   CE    NZ    sing N N 256 
LYS   CE    HE2   sing N N 257 
LYS   CE    HE3   sing N N 258 
LYS   NZ    HZ1   sing N N 259 
LYS   NZ    HZ2   sing N N 260 
LYS   NZ    HZ3   sing N N 261 
LYS   OXT   HXT   sing N N 262 
MET   N     CA    sing N N 263 
MET   N     H     sing N N 264 
MET   N     H2    sing N N 265 
MET   CA    C     sing N N 266 
MET   CA    CB    sing N N 267 
MET   CA    HA    sing N N 268 
MET   C     O     doub N N 269 
MET   C     OXT   sing N N 270 
MET   CB    CG    sing N N 271 
MET   CB    HB2   sing N N 272 
MET   CB    HB3   sing N N 273 
MET   CG    SD    sing N N 274 
MET   CG    HG2   sing N N 275 
MET   CG    HG3   sing N N 276 
MET   SD    CE    sing N N 277 
MET   CE    HE1   sing N N 278 
MET   CE    HE2   sing N N 279 
MET   CE    HE3   sing N N 280 
MET   OXT   HXT   sing N N 281 
PHE   N     CA    sing N N 282 
PHE   N     H     sing N N 283 
PHE   N     H2    sing N N 284 
PHE   CA    C     sing N N 285 
PHE   CA    CB    sing N N 286 
PHE   CA    HA    sing N N 287 
PHE   C     O     doub N N 288 
PHE   C     OXT   sing N N 289 
PHE   CB    CG    sing N N 290 
PHE   CB    HB2   sing N N 291 
PHE   CB    HB3   sing N N 292 
PHE   CG    CD1   doub Y N 293 
PHE   CG    CD2   sing Y N 294 
PHE   CD1   CE1   sing Y N 295 
PHE   CD1   HD1   sing N N 296 
PHE   CD2   CE2   doub Y N 297 
PHE   CD2   HD2   sing N N 298 
PHE   CE1   CZ    doub Y N 299 
PHE   CE1   HE1   sing N N 300 
PHE   CE2   CZ    sing Y N 301 
PHE   CE2   HE2   sing N N 302 
PHE   CZ    HZ    sing N N 303 
PHE   OXT   HXT   sing N N 304 
PRO   N     CA    sing N N 305 
PRO   N     CD    sing N N 306 
PRO   N     H     sing N N 307 
PRO   CA    C     sing N N 308 
PRO   CA    CB    sing N N 309 
PRO   CA    HA    sing N N 310 
PRO   C     O     doub N N 311 
PRO   C     OXT   sing N N 312 
PRO   CB    CG    sing N N 313 
PRO   CB    HB2   sing N N 314 
PRO   CB    HB3   sing N N 315 
PRO   CG    CD    sing N N 316 
PRO   CG    HG2   sing N N 317 
PRO   CG    HG3   sing N N 318 
PRO   CD    HD2   sing N N 319 
PRO   CD    HD3   sing N N 320 
PRO   OXT   HXT   sing N N 321 
SER   N     CA    sing N N 322 
SER   N     H     sing N N 323 
SER   N     H2    sing N N 324 
SER   CA    C     sing N N 325 
SER   CA    CB    sing N N 326 
SER   CA    HA    sing N N 327 
SER   C     O     doub N N 328 
SER   C     OXT   sing N N 329 
SER   CB    OG    sing N N 330 
SER   CB    HB2   sing N N 331 
SER   CB    HB3   sing N N 332 
SER   OG    HG    sing N N 333 
SER   OXT   HXT   sing N N 334 
THR   N     CA    sing N N 335 
THR   N     H     sing N N 336 
THR   N     H2    sing N N 337 
THR   CA    C     sing N N 338 
THR   CA    CB    sing N N 339 
THR   CA    HA    sing N N 340 
THR   C     O     doub N N 341 
THR   C     OXT   sing N N 342 
THR   CB    OG1   sing N N 343 
THR   CB    CG2   sing N N 344 
THR   CB    HB    sing N N 345 
THR   OG1   HG1   sing N N 346 
THR   CG2   HG21  sing N N 347 
THR   CG2   HG22  sing N N 348 
THR   CG2   HG23  sing N N 349 
THR   OXT   HXT   sing N N 350 
TPO   N     CA    sing N N 351 
TPO   N     H     sing N N 352 
TPO   N     H2    sing N N 353 
TPO   CA    CB    sing N N 354 
TPO   CA    C     sing N N 355 
TPO   CA    HA    sing N N 356 
TPO   CB    CG2   sing N N 357 
TPO   CB    OG1   sing N N 358 
TPO   CB    HB    sing N N 359 
TPO   CG2   HG21  sing N N 360 
TPO   CG2   HG22  sing N N 361 
TPO   CG2   HG23  sing N N 362 
TPO   OG1   P     sing N N 363 
TPO   P     O1P   doub N N 364 
TPO   P     O2P   sing N N 365 
TPO   P     O3P   sing N N 366 
TPO   O2P   HOP2  sing N N 367 
TPO   O3P   HOP3  sing N N 368 
TPO   C     O     doub N N 369 
TPO   C     OXT   sing N N 370 
TPO   OXT   HXT   sing N N 371 
TRP   N     CA    sing N N 372 
TRP   N     H     sing N N 373 
TRP   N     H2    sing N N 374 
TRP   CA    C     sing N N 375 
TRP   CA    CB    sing N N 376 
TRP   CA    HA    sing N N 377 
TRP   C     O     doub N N 378 
TRP   C     OXT   sing N N 379 
TRP   CB    CG    sing N N 380 
TRP   CB    HB2   sing N N 381 
TRP   CB    HB3   sing N N 382 
TRP   CG    CD1   doub Y N 383 
TRP   CG    CD2   sing Y N 384 
TRP   CD1   NE1   sing Y N 385 
TRP   CD1   HD1   sing N N 386 
TRP   CD2   CE2   doub Y N 387 
TRP   CD2   CE3   sing Y N 388 
TRP   NE1   CE2   sing Y N 389 
TRP   NE1   HE1   sing N N 390 
TRP   CE2   CZ2   sing Y N 391 
TRP   CE3   CZ3   doub Y N 392 
TRP   CE3   HE3   sing N N 393 
TRP   CZ2   CH2   doub Y N 394 
TRP   CZ2   HZ2   sing N N 395 
TRP   CZ3   CH2   sing Y N 396 
TRP   CZ3   HZ3   sing N N 397 
TRP   CH2   HH2   sing N N 398 
TRP   OXT   HXT   sing N N 399 
TYR   N     CA    sing N N 400 
TYR   N     H     sing N N 401 
TYR   N     H2    sing N N 402 
TYR   CA    C     sing N N 403 
TYR   CA    CB    sing N N 404 
TYR   CA    HA    sing N N 405 
TYR   C     O     doub N N 406 
TYR   C     OXT   sing N N 407 
TYR   CB    CG    sing N N 408 
TYR   CB    HB2   sing N N 409 
TYR   CB    HB3   sing N N 410 
TYR   CG    CD1   doub Y N 411 
TYR   CG    CD2   sing Y N 412 
TYR   CD1   CE1   sing Y N 413 
TYR   CD1   HD1   sing N N 414 
TYR   CD2   CE2   doub Y N 415 
TYR   CD2   HD2   sing N N 416 
TYR   CE1   CZ    doub Y N 417 
TYR   CE1   HE1   sing N N 418 
TYR   CE2   CZ    sing Y N 419 
TYR   CE2   HE2   sing N N 420 
TYR   CZ    OH    sing N N 421 
TYR   OH    HH    sing N N 422 
TYR   OXT   HXT   sing N N 423 
VAL   N     CA    sing N N 424 
VAL   N     H     sing N N 425 
VAL   N     H2    sing N N 426 
VAL   CA    C     sing N N 427 
VAL   CA    CB    sing N N 428 
VAL   CA    HA    sing N N 429 
VAL   C     O     doub N N 430 
VAL   C     OXT   sing N N 431 
VAL   CB    CG1   sing N N 432 
VAL   CB    CG2   sing N N 433 
VAL   CB    HB    sing N N 434 
VAL   CG1   HG11  sing N N 435 
VAL   CG1   HG12  sing N N 436 
VAL   CG1   HG13  sing N N 437 
VAL   CG2   HG21  sing N N 438 
VAL   CG2   HG22  sing N N 439 
VAL   CG2   HG23  sing N N 440 
VAL   OXT   HXT   sing N N 441 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-25 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9C0G 
_em_admin.last_update        2025-03-19 
_em_admin.map_release_date   2025-02-12 
_em_admin.title              'Phosphorylated human NKCC1 in complex with torsemide' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         42 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           5R01DK128592 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9C0G 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
NA 
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 
HETATM 1     N  N     . TPO   A 1 217  ? 123.380 168.250 107.854 1.00 119.09 ? 217  TPO   A N     1 
HETATM 2     C  CA    . TPO   A 1 217  ? 124.824 168.424 107.748 1.00 121.44 ? 217  TPO   A CA    1 
HETATM 3     C  CB    . TPO   A 1 217  ? 125.284 169.599 108.606 1.00 121.95 ? 217  TPO   A CB    1 
HETATM 4     C  CG2   . TPO   A 1 217  ? 124.293 169.799 109.754 1.00 120.48 ? 217  TPO   A CG2   1 
HETATM 5     O  OG1   . TPO   A 1 217  ? 126.597 169.354 109.121 1.00 123.94 ? 217  TPO   A OG1   1 
HETATM 6     P  P     . TPO   A 1 217  ? 127.615 170.304 108.318 1.00 127.59 ? 217  TPO   A P     1 
HETATM 7     O  O1P   . TPO   A 1 217  ? 127.002 171.641 108.153 1.00 122.55 ? 217  TPO   A O1P   1 
HETATM 8     O  O2P   . TPO   A 1 217  ? 128.987 170.432 109.146 1.00 123.63 ? 217  TPO   A O2P   1 
HETATM 9     O  O3P   . TPO   A 1 217  ? 127.927 169.667 106.877 1.00 120.68 ? 217  TPO   A O3P   1 
HETATM 10    C  C     . TPO   A 1 217  ? 125.561 167.154 108.151 1.00 122.32 ? 217  TPO   A C     1 
HETATM 11    O  O     . TPO   A 1 217  ? 126.780 167.064 108.013 1.00 122.36 ? 217  TPO   A O     1 
ATOM   12    N  N     . MET   A 1 218  ? 124.809 166.185 108.665 1.00 109.99 ? 218  MET   A N     1 
ATOM   13    C  CA    . MET   A 1 218  ? 125.354 164.891 109.077 1.00 108.25 ? 218  MET   A CA    1 
ATOM   14    C  C     . MET   A 1 218  ? 126.098 164.981 110.409 1.00 108.34 ? 218  MET   A C     1 
ATOM   15    O  O     . MET   A 1 218  ? 126.345 163.966 111.060 1.00 107.20 ? 218  MET   A O     1 
ATOM   16    C  CB    . MET   A 1 218  ? 126.282 164.329 107.996 1.00 108.23 ? 218  MET   A CB    1 
ATOM   17    C  CG    . MET   A 1 218  ? 127.005 163.046 108.387 1.00 108.34 ? 218  MET   A CG    1 
ATOM   18    S  SD    . MET   A 1 218  ? 126.137 161.560 107.850 1.00 110.83 ? 218  MET   A SD    1 
ATOM   19    C  CE    . MET   A 1 218  ? 125.324 161.080 109.370 1.00 107.47 ? 218  MET   A CE    1 
ATOM   20    N  N     . ASP   A 1 219  ? 126.461 166.198 110.804 1.00 105.52 ? 219  ASP   A N     1 
ATOM   21    C  CA    . ASP   A 1 219  ? 127.107 166.441 112.087 1.00 103.24 ? 219  ASP   A CA    1 
ATOM   22    C  C     . ASP   A 1 219  ? 126.032 166.656 113.146 1.00 104.33 ? 219  ASP   A C     1 
ATOM   23    O  O     . ASP   A 1 219  ? 125.244 167.604 113.053 1.00 105.39 ? 219  ASP   A O     1 
ATOM   24    C  CB    . ASP   A 1 219  ? 128.037 167.651 112.007 1.00 103.85 ? 219  ASP   A CB    1 
ATOM   25    C  CG    . ASP   A 1 219  ? 129.393 167.390 112.640 1.00 105.76 ? 219  ASP   A CG    1 
ATOM   26    O  OD1   . ASP   A 1 219  ? 130.420 167.693 111.998 1.00 107.52 ? 219  ASP   A OD1   1 
ATOM   27    O  OD2   . ASP   A 1 219  ? 129.433 166.881 113.779 1.00 103.79 ? 219  ASP   A OD2   1 
ATOM   28    N  N     . ALA   A 1 220  ? 126.002 165.782 114.148 1.00 95.89  ? 220  ALA   A N     1 
ATOM   29    C  CA    . ALA   A 1 220  ? 124.978 165.850 115.179 1.00 95.85  ? 220  ALA   A CA    1 
ATOM   30    C  C     . ALA   A 1 220  ? 125.313 166.923 116.206 1.00 96.57  ? 220  ALA   A C     1 
ATOM   31    O  O     . ALA   A 1 220  ? 126.476 167.113 116.572 1.00 97.49  ? 220  ALA   A O     1 
ATOM   32    C  CB    . ALA   A 1 220  ? 124.824 164.496 115.871 1.00 94.82  ? 220  ALA   A CB    1 
ATOM   33    N  N     . VAL   A 1 221  ? 124.283 167.623 116.670 1.00 90.11  ? 221  VAL   A N     1 
ATOM   34    C  CA    . VAL   A 1 221  ? 124.435 168.643 117.704 1.00 87.37  ? 221  VAL   A CA    1 
ATOM   35    C  C     . VAL   A 1 221  ? 124.576 167.950 119.053 1.00 87.02  ? 221  VAL   A C     1 
ATOM   36    O  O     . VAL   A 1 221  ? 124.185 166.782 119.192 1.00 84.79  ? 221  VAL   A O     1 
ATOM   37    C  CB    . VAL   A 1 221  ? 123.250 169.622 117.706 1.00 85.82  ? 221  VAL   A CB    1 
ATOM   38    C  CG1   . VAL   A 1 221  ? 123.055 170.222 116.324 1.00 87.30  ? 221  VAL   A CG1   1 
ATOM   39    C  CG2   . VAL   A 1 221  ? 121.985 168.921 118.172 1.00 85.06  ? 221  VAL   A CG2   1 
ATOM   40    N  N     . PRO   A 1 222  ? 125.134 168.613 120.063 1.00 89.36  ? 222  PRO   A N     1 
ATOM   41    C  CA    . PRO   A 1 222  ? 125.237 167.986 121.386 1.00 86.45  ? 222  PRO   A CA    1 
ATOM   42    C  C     . PRO   A 1 222  ? 123.869 167.560 121.896 1.00 89.50  ? 222  PRO   A C     1 
ATOM   43    O  O     . PRO   A 1 222  ? 122.907 168.331 121.863 1.00 90.36  ? 222  PRO   A O     1 
ATOM   44    C  CB    . PRO   A 1 222  ? 125.845 169.094 122.251 1.00 86.44  ? 222  PRO   A CB    1 
ATOM   45    C  CG    . PRO   A 1 222  ? 126.608 169.938 121.284 1.00 86.15  ? 222  PRO   A CG    1 
ATOM   46    C  CD    . PRO   A 1 222  ? 125.804 169.924 120.015 1.00 88.75  ? 222  PRO   A CD    1 
ATOM   47    N  N     . ARG   A 1 223  ? 123.787 166.319 122.374 1.00 88.30  ? 223  ARG   A N     1 
ATOM   48    C  CA    . ARG   A 1 223  ? 122.524 165.765 122.838 1.00 85.99  ? 223  ARG   A CA    1 
ATOM   49    C  C     . ARG   A 1 223  ? 122.791 164.760 123.949 1.00 85.70  ? 223  ARG   A C     1 
ATOM   50    O  O     . ARG   A 1 223  ? 123.724 163.958 123.860 1.00 88.72  ? 223  ARG   A O     1 
ATOM   51    C  CB    . ARG   A 1 223  ? 121.755 165.103 121.690 1.00 88.39  ? 223  ARG   A CB    1 
ATOM   52    C  CG    . ARG   A 1 223  ? 120.520 164.336 122.121 1.00 88.96  ? 223  ARG   A CG    1 
ATOM   53    C  CD    . ARG   A 1 223  ? 120.004 163.462 120.992 1.00 89.76  ? 223  ARG   A CD    1 
ATOM   54    N  NE    . ARG   A 1 223  ? 119.815 164.225 119.764 1.00 91.12  ? 223  ARG   A NE    1 
ATOM   55    C  CZ    . ARG   A 1 223  ? 118.771 165.004 119.518 1.00 91.17  ? 223  ARG   A CZ    1 
ATOM   56    N  NH1   . ARG   A 1 223  ? 117.793 165.148 120.398 1.00 90.54  ? 223  ARG   A NH1   1 
ATOM   57    N  NH2   . ARG   A 1 223  ? 118.707 165.657 118.361 1.00 89.98  ? 223  ARG   A NH2   1 
ATOM   58    N  N     . ILE   A 1 224  ? 121.954 164.804 124.989 1.00 80.61  ? 224  ILE   A N     1 
ATOM   59    C  CA    . ILE   A 1 224  ? 122.142 163.926 126.140 1.00 80.97  ? 224  ILE   A CA    1 
ATOM   60    C  C     . ILE   A 1 224  ? 122.093 162.461 125.728 1.00 82.07  ? 224  ILE   A C     1 
ATOM   61    O  O     . ILE   A 1 224  ? 122.755 161.614 126.339 1.00 84.07  ? 224  ILE   A O     1 
ATOM   62    C  CB    . ILE   A 1 224  ? 121.093 164.240 127.224 1.00 82.20  ? 224  ILE   A CB    1 
ATOM   63    C  CG1   . ILE   A 1 224  ? 121.413 163.484 128.514 1.00 81.10  ? 224  ILE   A CG1   1 
ATOM   64    C  CG2   . ILE   A 1 224  ? 119.700 163.885 126.734 1.00 82.26  ? 224  ILE   A CG2   1 
ATOM   65    C  CD1   . ILE   A 1 224  ? 121.220 164.306 129.768 1.00 79.93  ? 224  ILE   A CD1   1 
ATOM   66    N  N     . ASP   A 1 225  ? 121.316 162.135 124.692 1.00 88.61  ? 225  ASP   A N     1 
ATOM   67    C  CA    . ASP   A 1 225  ? 121.194 160.743 124.273 1.00 86.19  ? 225  ASP   A CA    1 
ATOM   68    C  C     . ASP   A 1 225  ? 122.530 160.168 123.824 1.00 87.92  ? 225  ASP   A C     1 
ATOM   69    O  O     . ASP   A 1 225  ? 122.765 158.962 123.965 1.00 90.02  ? 225  ASP   A O     1 
ATOM   70    C  CB    . ASP   A 1 225  ? 120.160 160.620 123.153 1.00 89.02  ? 225  ASP   A CB    1 
ATOM   71    C  CG    . ASP   A 1 225  ? 118.888 161.388 123.449 1.00 91.61  ? 225  ASP   A CG    1 
ATOM   72    O  OD1   . ASP   A 1 225  ? 118.763 161.924 124.570 1.00 91.00  ? 225  ASP   A OD1   1 
ATOM   73    O  OD2   . ASP   A 1 225  ? 118.010 161.453 122.563 1.00 92.84  ? 225  ASP   A OD2   1 
ATOM   74    N  N     . HIS   A 1 226  ? 123.416 161.005 123.280 1.00 84.16  ? 226  HIS   A N     1 
ATOM   75    C  CA    . HIS   A 1 226  ? 124.713 160.511 122.829 1.00 81.76  ? 226  HIS   A CA    1 
ATOM   76    C  C     . HIS   A 1 226  ? 125.519 159.934 123.985 1.00 83.92  ? 226  HIS   A C     1 
ATOM   77    O  O     . HIS   A 1 226  ? 126.136 158.871 123.853 1.00 84.66  ? 226  HIS   A O     1 
ATOM   78    C  CB    . HIS   A 1 226  ? 125.494 161.632 122.143 1.00 80.81  ? 226  HIS   A CB    1 
ATOM   79    C  CG    . HIS   A 1 226  ? 124.808 162.202 120.943 1.00 80.80  ? 226  HIS   A CG    1 
ATOM   80    N  ND1   . HIS   A 1 226  ? 125.121 163.441 120.426 1.00 80.31  ? 226  HIS   A ND1   1 
ATOM   81    C  CD2   . HIS   A 1 226  ? 123.826 161.703 120.155 1.00 82.76  ? 226  HIS   A CD2   1 
ATOM   82    C  CE1   . HIS   A 1 226  ? 124.362 163.680 119.372 1.00 81.79  ? 226  HIS   A CE1   1 
ATOM   83    N  NE2   . HIS   A 1 226  ? 123.567 162.642 119.187 1.00 84.06  ? 226  HIS   A NE2   1 
ATOM   84    N  N     . TYR   A 1 227  ? 125.530 160.623 125.126 1.00 82.82  ? 227  TYR   A N     1 
ATOM   85    C  CA    . TYR   A 1 227  ? 126.342 160.211 126.262 1.00 79.41  ? 227  TYR   A CA    1 
ATOM   86    C  C     . TYR   A 1 227  ? 125.626 159.253 127.203 1.00 79.92  ? 227  TYR   A C     1 
ATOM   87    O  O     . TYR   A 1 227  ? 126.277 158.659 128.070 1.00 80.40  ? 227  TYR   A O     1 
ATOM   88    C  CB    . TYR   A 1 227  ? 126.803 161.441 127.048 1.00 78.75  ? 227  TYR   A CB    1 
ATOM   89    C  CG    . TYR   A 1 227  ? 127.540 162.458 126.208 1.00 80.68  ? 227  TYR   A CG    1 
ATOM   90    C  CD1   . TYR   A 1 227  ? 126.849 163.422 125.487 1.00 78.71  ? 227  TYR   A CD1   1 
ATOM   91    C  CD2   . TYR   A 1 227  ? 128.927 162.454 126.136 1.00 78.40  ? 227  TYR   A CD2   1 
ATOM   92    C  CE1   . TYR   A 1 227  ? 127.517 164.353 124.719 1.00 79.54  ? 227  TYR   A CE1   1 
ATOM   93    C  CE2   . TYR   A 1 227  ? 129.605 163.383 125.370 1.00 77.91  ? 227  TYR   A CE2   1 
ATOM   94    C  CZ    . TYR   A 1 227  ? 128.895 164.330 124.665 1.00 80.54  ? 227  TYR   A CZ    1 
ATOM   95    O  OH    . TYR   A 1 227  ? 129.561 165.257 123.900 1.00 81.05  ? 227  TYR   A OH    1 
ATOM   96    N  N     . ARG   A 1 228  ? 124.315 159.086 127.056 1.00 90.76  ? 228  ARG   A N     1 
ATOM   97    C  CA    . ARG   A 1 228  ? 123.541 158.204 127.928 1.00 89.93  ? 228  ARG   A CA    1 
ATOM   98    C  C     . ARG   A 1 228  ? 123.570 156.799 127.341 1.00 90.44  ? 228  ARG   A C     1 
ATOM   99    O  O     . ARG   A 1 228  ? 122.815 156.481 126.421 1.00 94.52  ? 228  ARG   A O     1 
ATOM   100   C  CB    . ARG   A 1 228  ? 122.114 158.719 128.074 1.00 88.69  ? 228  ARG   A CB    1 
ATOM   101   C  CG    . ARG   A 1 228  ? 121.092 157.645 128.398 1.00 90.49  ? 228  ARG   A CG    1 
ATOM   102   C  CD    . ARG   A 1 228  ? 119.694 158.230 128.509 1.00 91.37  ? 228  ARG   A CD    1 
ATOM   103   N  NE    . ARG   A 1 228  ? 119.607 159.267 129.530 1.00 92.36  ? 228  ARG   A NE    1 
ATOM   104   C  CZ    . ARG   A 1 228  ? 119.763 159.058 130.830 1.00 94.14  ? 228  ARG   A CZ    1 
ATOM   105   N  NH1   . ARG   A 1 228  ? 120.028 157.854 131.310 1.00 93.01  ? 228  ARG   A NH1   1 
ATOM   106   N  NH2   . ARG   A 1 228  ? 119.649 160.082 131.670 1.00 92.60  ? 228  ARG   A NH2   1 
ATOM   107   N  N     . HIS   A 1 229  ? 124.454 155.947 127.870 1.00 90.18  ? 229  HIS   A N     1 
ATOM   108   C  CA    . HIS   A 1 229  ? 124.579 154.591 127.352 1.00 93.35  ? 229  HIS   A CA    1 
ATOM   109   C  C     . HIS   A 1 229  ? 124.771 153.529 128.428 1.00 93.98  ? 229  HIS   A C     1 
ATOM   110   O  O     . HIS   A 1 229  ? 125.176 152.407 128.098 1.00 94.66  ? 229  HIS   A O     1 
ATOM   111   N  N     . THR   A 1 230  ? 124.496 153.829 129.688 1.00 99.87  ? 230  THR   A N     1 
ATOM   112   C  CA    . THR   A 1 230  ? 124.634 152.814 130.728 1.00 101.53 ? 230  THR   A CA    1 
ATOM   113   C  C     . THR   A 1 230  ? 123.381 152.659 131.575 1.00 101.88 ? 230  THR   A C     1 
ATOM   114   O  O     . THR   A 1 230  ? 123.077 151.547 132.013 1.00 101.06 ? 230  THR   A O     1 
ATOM   115   C  CB    . THR   A 1 230  ? 125.832 153.135 131.636 1.00 99.29  ? 230  THR   A CB    1 
ATOM   116   O  OG1   . THR   A 1 230  ? 125.535 154.286 132.434 1.00 97.88  ? 230  THR   A OG1   1 
ATOM   117   C  CG2   . THR   A 1 230  ? 127.071 153.413 130.801 1.00 97.01  ? 230  THR   A CG2   1 
ATOM   118   N  N     . ALA   A 1 231  ? 122.648 153.744 131.818 1.00 105.64 ? 231  ALA   A N     1 
ATOM   119   C  CA    . ALA   A 1 231  ? 121.411 153.703 132.583 1.00 103.32 ? 231  ALA   A CA    1 
ATOM   120   C  C     . ALA   A 1 231  ? 120.171 153.840 131.709 1.00 105.22 ? 231  ALA   A C     1 
ATOM   121   O  O     . ALA   A 1 231  ? 119.072 154.038 132.237 1.00 103.29 ? 231  ALA   A O     1 
ATOM   122   N  N     . ALA   A 1 232  ? 120.321 153.739 130.394 1.00 116.56 ? 232  ALA   A N     1 
ATOM   123   C  CA    . ALA   A 1 232  ? 119.201 153.866 129.467 1.00 116.88 ? 232  ALA   A CA    1 
ATOM   124   C  C     . ALA   A 1 232  ? 119.692 153.469 128.080 1.00 116.30 ? 232  ALA   A C     1 
ATOM   125   O  O     . ALA   A 1 232  ? 120.857 153.105 127.892 1.00 113.07 ? 232  ALA   A O     1 
ATOM   126   C  CB    . ALA   A 1 232  ? 118.623 155.283 129.476 1.00 115.64 ? 232  ALA   A CB    1 
ATOM   127   N  N     . GLN   A 1 233  ? 118.789 153.541 127.107 1.00 127.51 ? 233  GLN   A N     1 
ATOM   128   C  CA    . GLN   A 1 233  ? 119.082 153.194 125.723 1.00 128.07 ? 233  GLN   A CA    1 
ATOM   129   C  C     . GLN   A 1 233  ? 119.066 154.453 124.869 1.00 128.20 ? 233  GLN   A C     1 
ATOM   130   O  O     . GLN   A 1 233  ? 118.082 155.200 124.875 1.00 127.44 ? 233  GLN   A O     1 
ATOM   131   C  CB    . GLN   A 1 233  ? 118.071 152.178 125.187 1.00 125.37 ? 233  GLN   A CB    1 
ATOM   132   N  N     . LEU   A 1 234  ? 120.157 154.685 124.135 1.00 127.75 ? 234  LEU   A N     1 
ATOM   133   C  CA    . LEU   A 1 234  ? 120.232 155.863 123.277 1.00 126.80 ? 234  LEU   A CA    1 
ATOM   134   C  C     . LEU   A 1 234  ? 119.165 155.823 122.191 1.00 127.23 ? 234  LEU   A C     1 
ATOM   135   O  O     . LEU   A 1 234  ? 118.534 156.843 121.891 1.00 126.20 ? 234  LEU   A O     1 
ATOM   136   N  N     . GLY   A 1 235  ? 118.951 154.655 121.588 1.00 128.54 ? 235  GLY   A N     1 
ATOM   137   C  CA    . GLY   A 1 235  ? 117.940 154.507 120.563 1.00 128.45 ? 235  GLY   A CA    1 
ATOM   138   C  C     . GLY   A 1 235  ? 118.365 155.094 119.231 1.00 128.90 ? 235  GLY   A C     1 
ATOM   139   O  O     . GLY   A 1 235  ? 119.478 155.591 119.048 1.00 128.48 ? 235  GLY   A O     1 
ATOM   140   N  N     . GLU   A 1 236  ? 117.436 155.032 118.275 1.00 130.50 ? 236  GLU   A N     1 
ATOM   141   C  CA    . GLU   A 1 236  ? 117.709 155.564 116.944 1.00 130.52 ? 236  GLU   A CA    1 
ATOM   142   C  C     . GLU   A 1 236  ? 117.684 157.087 116.927 1.00 131.63 ? 236  GLU   A C     1 
ATOM   143   O  O     . GLU   A 1 236  ? 118.386 157.708 116.121 1.00 129.92 ? 236  GLU   A O     1 
ATOM   144   N  N     . LYS   A 1 237  ? 116.886 157.704 117.801 1.00 129.63 ? 237  LYS   A N     1 
ATOM   145   C  CA    . LYS   A 1 237  ? 116.786 159.158 117.838 1.00 128.21 ? 237  LYS   A CA    1 
ATOM   146   C  C     . LYS   A 1 237  ? 118.035 159.829 118.390 1.00 127.77 ? 237  LYS   A C     1 
ATOM   147   O  O     . LYS   A 1 237  ? 118.144 161.057 118.303 1.00 126.39 ? 237  LYS   A O     1 
ATOM   148   N  N     . LEU   A 1 238  ? 118.972 159.067 118.951 1.00 118.07 ? 238  LEU   A N     1 
ATOM   149   C  CA    . LEU   A 1 238  ? 120.194 159.628 119.524 1.00 115.28 ? 238  LEU   A CA    1 
ATOM   150   C  C     . LEU   A 1 238  ? 121.349 158.698 119.184 1.00 115.90 ? 238  LEU   A C     1 
ATOM   151   O  O     . LEU   A 1 238  ? 121.470 157.616 119.766 1.00 114.71 ? 238  LEU   A O     1 
ATOM   152   N  N     . LEU   A 1 239  ? 122.192 159.117 118.242 1.00 105.14 ? 239  LEU   A N     1 
ATOM   153   C  CA    . LEU   A 1 239  ? 123.383 158.351 117.883 1.00 103.64 ? 239  LEU   A CA    1 
ATOM   154   C  C     . LEU   A 1 239  ? 124.378 159.313 117.249 1.00 101.02 ? 239  LEU   A C     1 
ATOM   155   O  O     . LEU   A 1 239  ? 124.172 159.753 116.114 1.00 101.38 ? 239  LEU   A O     1 
ATOM   156   C  CB    . LEU   A 1 239  ? 123.033 157.209 116.936 1.00 102.51 ? 239  LEU   A CB    1 
ATOM   157   C  CG    . LEU   A 1 239  ? 122.889 155.827 117.576 1.00 103.58 ? 239  LEU   A CG    1 
ATOM   158   C  CD1   . LEU   A 1 239  ? 122.767 154.749 116.510 1.00 100.66 ? 239  LEU   A CD1   1 
ATOM   159   C  CD2   . LEU   A 1 239  ? 124.058 155.538 118.507 1.00 101.17 ? 239  LEU   A CD2   1 
ATOM   160   N  N     . ARG   A 1 240  ? 125.417 159.665 118.008 1.00 85.33  ? 240  ARG   A N     1 
ATOM   161   C  CA    . ARG   A 1 240  ? 126.456 160.590 117.494 1.00 85.55  ? 240  ARG   A CA    1 
ATOM   162   C  C     . ARG   A 1 240  ? 127.146 159.905 116.326 1.00 87.06  ? 240  ARG   A C     1 
ATOM   163   O  O     . ARG   A 1 240  ? 127.510 158.725 116.470 1.00 86.35  ? 240  ARG   A O     1 
ATOM   164   C  CB    . ARG   A 1 240  ? 127.482 160.904 118.584 1.00 84.13  ? 240  ARG   A CB    1 
ATOM   165   C  CG    . ARG   A 1 240  ? 128.815 161.439 118.080 1.00 81.41  ? 240  ARG   A CG    1 
ATOM   166   C  CD    . ARG   A 1 240  ? 129.915 161.006 119.030 1.00 82.03  ? 240  ARG   A CD    1 
ATOM   167   N  NE    . ARG   A 1 240  ? 129.458 161.136 120.406 1.00 85.06  ? 240  ARG   A NE    1 
ATOM   168   C  CZ    . ARG   A 1 240  ? 130.066 160.620 121.465 1.00 84.20  ? 240  ARG   A CZ    1 
ATOM   169   N  NH1   . ARG   A 1 240  ? 131.171 159.913 121.315 1.00 84.04  ? 240  ARG   A NH1   1 
ATOM   170   N  NH2   . ARG   A 1 240  ? 129.558 160.805 122.670 1.00 82.65  ? 240  ARG   A NH2   1 
ATOM   171   N  N     . PRO   A 1 241  ? 127.324 160.571 115.171 1.00 86.70  ? 241  PRO   A N     1 
ATOM   172   C  CA    . PRO   A 1 241  ? 128.089 159.980 114.069 1.00 83.85  ? 241  PRO   A CA    1 
ATOM   173   C  C     . PRO   A 1 241  ? 129.551 159.799 114.445 1.00 83.93  ? 241  PRO   A C     1 
ATOM   174   O  O     . PRO   A 1 241  ? 130.135 160.614 115.163 1.00 84.19  ? 241  PRO   A O     1 
ATOM   175   C  CB    . PRO   A 1 241  ? 127.917 161.004 112.941 1.00 84.19  ? 241  PRO   A CB    1 
ATOM   176   C  CG    . PRO   A 1 241  ? 127.708 162.294 113.674 1.00 84.23  ? 241  PRO   A CG    1 
ATOM   177   C  CD    . PRO   A 1 241  ? 126.809 161.903 114.814 1.00 85.30  ? 241  PRO   A CD    1 
ATOM   178   N  N     . SER   A 1 242  ? 130.141 158.714 113.952 1.00 80.24  ? 242  SER   A N     1 
ATOM   179   C  CA    . SER   A 1 242  ? 131.554 158.466 114.178 1.00 78.71  ? 242  SER   A CA    1 
ATOM   180   C  C     . SER   A 1 242  ? 132.399 159.373 113.289 1.00 79.06  ? 242  SER   A C     1 
ATOM   181   O  O     . SER   A 1 242  ? 131.945 159.879 112.260 1.00 82.02  ? 242  SER   A O     1 
ATOM   182   C  CB    . SER   A 1 242  ? 131.898 157.000 113.915 1.00 79.69  ? 242  SER   A CB    1 
ATOM   183   O  OG    . SER   A 1 242  ? 132.030 156.746 112.528 1.00 83.68  ? 242  SER   A OG    1 
ATOM   184   N  N     . LEU   A 1 243  ? 133.651 159.576 113.703 1.00 76.99  ? 243  LEU   A N     1 
ATOM   185   C  CA    . LEU   A 1 243  ? 134.544 160.438 112.938 1.00 75.95  ? 243  LEU   A CA    1 
ATOM   186   C  C     . LEU   A 1 243  ? 134.814 159.876 111.548 1.00 78.85  ? 243  LEU   A C     1 
ATOM   187   O  O     . LEU   A 1 243  ? 135.016 160.642 110.600 1.00 81.23  ? 243  LEU   A O     1 
ATOM   188   C  CB    . LEU   A 1 243  ? 135.855 160.640 113.698 1.00 76.56  ? 243  LEU   A CB    1 
ATOM   189   C  CG    . LEU   A 1 243  ? 136.942 161.464 113.008 1.00 76.80  ? 243  LEU   A CG    1 
ATOM   190   C  CD1   . LEU   A 1 243  ? 136.645 162.950 113.127 1.00 72.14  ? 243  LEU   A CD1   1 
ATOM   191   C  CD2   . LEU   A 1 243  ? 138.309 161.137 113.591 1.00 80.02  ? 243  LEU   A CD2   1 
ATOM   192   N  N     . ALA   A 1 244  ? 134.818 158.548 111.406 1.00 82.02  ? 244  ALA   A N     1 
ATOM   193   C  CA    . ALA   A 1 244  ? 135.063 157.946 110.100 1.00 79.63  ? 244  ALA   A CA    1 
ATOM   194   C  C     . ALA   A 1 244  ? 133.979 158.329 109.101 1.00 81.88  ? 244  ALA   A C     1 
ATOM   195   O  O     . ALA   A 1 244  ? 134.274 158.616 107.934 1.00 86.26  ? 244  ALA   A O     1 
ATOM   196   C  CB    . ALA   A 1 244  ? 135.158 156.426 110.233 1.00 78.69  ? 244  ALA   A CB    1 
ATOM   197   N  N     . GLU   A 1 245  ? 132.718 158.340 109.537 1.00 79.50  ? 245  GLU   A N     1 
ATOM   198   C  CA    . GLU   A 1 245  ? 131.629 158.691 108.631 1.00 80.73  ? 245  GLU   A CA    1 
ATOM   199   C  C     . GLU   A 1 245  ? 131.779 160.116 108.116 1.00 82.22  ? 245  GLU   A C     1 
ATOM   200   O  O     . GLU   A 1 245  ? 131.513 160.392 106.940 1.00 85.78  ? 245  GLU   A O     1 
ATOM   201   C  CB    . GLU   A 1 245  ? 130.282 158.514 109.331 1.00 79.78  ? 245  GLU   A CB    1 
ATOM   202   C  CG    . GLU   A 1 245  ? 130.262 157.402 110.365 1.00 83.47  ? 245  GLU   A CG    1 
ATOM   203   C  CD    . GLU   A 1 245  ? 128.856 157.024 110.791 1.00 85.52  ? 245  GLU   A CD    1 
ATOM   204   O  OE1   . GLU   A 1 245  ? 127.984 156.876 109.909 1.00 85.41  ? 245  GLU   A OE1   1 
ATOM   205   O  OE2   . GLU   A 1 245  ? 128.622 156.878 112.009 1.00 83.63  ? 245  GLU   A OE2   1 
ATOM   206   N  N     . LEU   A 1 246  ? 132.199 161.038 108.983 1.00 78.02  ? 246  LEU   A N     1 
ATOM   207   C  CA    . LEU   A 1 246  ? 132.406 162.414 108.547 1.00 80.94  ? 246  LEU   A CA    1 
ATOM   208   C  C     . LEU   A 1 246  ? 133.668 162.554 107.707 1.00 82.26  ? 246  LEU   A C     1 
ATOM   209   O  O     . LEU   A 1 246  ? 133.755 163.459 106.869 1.00 83.41  ? 246  LEU   A O     1 
ATOM   210   C  CB    . LEU   A 1 246  ? 132.471 163.343 109.759 1.00 83.37  ? 246  LEU   A CB    1 
ATOM   211   C  CG    . LEU   A 1 246  ? 131.150 163.631 110.475 1.00 81.75  ? 246  LEU   A CG    1 
ATOM   212   C  CD1   . LEU   A 1 246  ? 131.160 165.022 111.085 1.00 82.35  ? 246  LEU   A CD1   1 
ATOM   213   C  CD2   . LEU   A 1 246  ? 129.976 163.468 109.526 1.00 82.75  ? 246  LEU   A CD2   1 
ATOM   214   N  N     . HIS   A 1 247  ? 134.652 161.679 107.914 1.00 81.48  ? 247  HIS   A N     1 
ATOM   215   C  CA    . HIS   A 1 247  ? 135.932 161.765 107.217 1.00 79.50  ? 247  HIS   A CA    1 
ATOM   216   C  C     . HIS   A 1 247  ? 136.027 160.801 106.039 1.00 80.38  ? 247  HIS   A C     1 
ATOM   217   O  O     . HIS   A 1 247  ? 136.289 161.223 104.909 1.00 80.33  ? 247  HIS   A O     1 
ATOM   218   C  CB    . HIS   A 1 247  ? 137.084 161.500 108.194 1.00 79.93  ? 247  HIS   A CB    1 
ATOM   219   C  CG    . HIS   A 1 247  ? 138.400 162.034 107.726 1.00 78.60  ? 247  HIS   A CG    1 
ATOM   220   N  ND1   . HIS   A 1 247  ? 139.606 161.538 108.171 1.00 80.67  ? 247  HIS   A ND1   1 
ATOM   221   C  CD2   . HIS   A 1 247  ? 138.700 163.024 106.853 1.00 78.90  ? 247  HIS   A CD2   1 
ATOM   222   C  CE1   . HIS   A 1 247  ? 140.592 162.195 107.587 1.00 80.87  ? 247  HIS   A CE1   1 
ATOM   223   N  NE2   . HIS   A 1 247  ? 140.069 163.104 106.785 1.00 77.89  ? 247  HIS   A NE2   1 
ATOM   224   N  N     . ASP   A 1 248  ? 135.825 159.510 106.287 1.00 88.04  ? 248  ASP   A N     1 
ATOM   225   C  CA    . ASP   A 1 248  ? 136.112 158.502 105.275 1.00 89.22  ? 248  ASP   A CA    1 
ATOM   226   C  C     . ASP   A 1 248  ? 135.326 158.767 103.998 1.00 91.78  ? 248  ASP   A C     1 
ATOM   227   O  O     . ASP   A 1 248  ? 134.132 159.078 104.032 1.00 93.02  ? 248  ASP   A O     1 
ATOM   228   C  CB    . ASP   A 1 248  ? 135.794 157.107 105.813 1.00 89.97  ? 248  ASP   A CB    1 
ATOM   229   C  CG    . ASP   A 1 248  ? 137.020 156.402 106.359 1.00 90.62  ? 248  ASP   A CG    1 
ATOM   230   O  OD1   . ASP   A 1 248  ? 138.112 156.572 105.777 1.00 90.19  ? 248  ASP   A OD1   1 
ATOM   231   O  OD2   . ASP   A 1 248  ? 136.893 155.678 107.368 1.00 93.17  ? 248  ASP   A OD2   1 
ATOM   232   N  N     . GLU   A 1 249  ? 136.010 158.639 102.864 1.00 101.30 ? 249  GLU   A N     1 
ATOM   233   C  CA    . GLU   A 1 249  ? 135.400 158.870 101.562 1.00 101.96 ? 249  GLU   A CA    1 
ATOM   234   C  C     . GLU   A 1 249  ? 134.636 157.624 101.131 1.00 103.48 ? 249  GLU   A C     1 
ATOM   235   O  O     . GLU   A 1 249  ? 135.203 156.527 101.081 1.00 103.30 ? 249  GLU   A O     1 
ATOM   236   C  CB    . GLU   A 1 249  ? 136.469 159.230 100.533 1.00 101.84 ? 249  GLU   A CB    1 
ATOM   237   C  CG    . GLU   A 1 249  ? 135.923 159.567 99.155  1.00 104.99 ? 249  GLU   A CG    1 
ATOM   238   C  CD    . GLU   A 1 249  ? 135.145 160.868 99.138  1.00 105.85 ? 249  GLU   A CD    1 
ATOM   239   O  OE1   . GLU   A 1 249  ? 135.252 161.639 100.114 1.00 107.34 ? 249  GLU   A OE1   1 
ATOM   240   O  OE2   . GLU   A 1 249  ? 134.429 161.121 98.147  1.00 105.02 ? 249  GLU   A OE2   1 
ATOM   241   N  N     . LEU   A 1 250  ? 133.355 157.791 100.824 1.00 100.76 ? 250  LEU   A N     1 
ATOM   242   C  CA    . LEU   A 1 250  ? 132.523 156.676 100.389 1.00 100.66 ? 250  LEU   A CA    1 
ATOM   243   C  C     . LEU   A 1 250  ? 132.048 156.882 98.956  1.00 100.14 ? 250  LEU   A C     1 
ATOM   244   O  O     . LEU   A 1 250  ? 132.212 157.962 98.388  1.00 98.72  ? 250  LEU   A O     1 
ATOM   245   C  CB    . LEU   A 1 250  ? 131.324 156.504 101.324 1.00 99.39  ? 250  LEU   A CB    1 
ATOM   246   N  N     . VAL   A 1 282  ? 108.745 150.258 141.470 1.00 64.15  ? 282  VAL   A N     1 
ATOM   247   C  CA    . VAL   A 1 282  ? 109.952 150.896 141.976 1.00 65.90  ? 282  VAL   A CA    1 
ATOM   248   C  C     . VAL   A 1 282  ? 109.583 152.001 142.958 1.00 66.99  ? 282  VAL   A C     1 
ATOM   249   O  O     . VAL   A 1 282  ? 108.651 152.769 142.722 1.00 67.22  ? 282  VAL   A O     1 
ATOM   250   C  CB    . VAL   A 1 282  ? 110.814 151.445 140.825 1.00 62.80  ? 282  VAL   A CB    1 
ATOM   251   C  CG1   . VAL   A 1 282  ? 110.320 152.818 140.393 1.00 62.26  ? 282  VAL   A CG1   1 
ATOM   252   C  CG2   . VAL   A 1 282  ? 112.276 151.500 141.237 1.00 60.42  ? 282  VAL   A CG2   1 
ATOM   253   N  N     . VAL   A 1 283  ? 110.316 152.072 144.066 1.00 62.36  ? 283  VAL   A N     1 
ATOM   254   C  CA    . VAL   A 1 283  ? 110.066 153.045 145.122 1.00 60.37  ? 283  VAL   A CA    1 
ATOM   255   C  C     . VAL   A 1 283  ? 111.270 153.969 145.223 1.00 58.45  ? 283  VAL   A C     1 
ATOM   256   O  O     . VAL   A 1 283  ? 112.404 153.503 145.387 1.00 58.62  ? 283  VAL   A O     1 
ATOM   257   C  CB    . VAL   A 1 283  ? 109.791 152.360 146.473 1.00 63.40  ? 283  VAL   A CB    1 
ATOM   258   C  CG1   . VAL   A 1 283  ? 109.565 153.399 147.556 1.00 62.81  ? 283  VAL   A CG1   1 
ATOM   259   C  CG2   . VAL   A 1 283  ? 108.593 151.434 146.359 1.00 63.94  ? 283  VAL   A CG2   1 
ATOM   260   N  N     . LYS   A 1 284  ? 111.022 155.272 145.126 1.00 51.33  ? 284  LYS   A N     1 
ATOM   261   C  CA    . LYS   A 1 284  ? 112.053 156.293 145.252 1.00 52.24  ? 284  LYS   A CA    1 
ATOM   262   C  C     . LYS   A 1 284  ? 111.637 157.286 146.326 1.00 51.22  ? 284  LYS   A C     1 
ATOM   263   O  O     . LYS   A 1 284  ? 110.508 157.789 146.307 1.00 56.49  ? 284  LYS   A O     1 
ATOM   264   C  CB    . LYS   A 1 284  ? 112.281 157.017 143.922 1.00 50.83  ? 284  LYS   A CB    1 
ATOM   265   C  CG    . LYS   A 1 284  ? 113.454 156.495 143.109 1.00 47.98  ? 284  LYS   A CG    1 
ATOM   266   C  CD    . LYS   A 1 284  ? 113.563 154.985 143.186 1.00 49.09  ? 284  LYS   A CD    1 
ATOM   267   C  CE    . LYS   A 1 284  ? 114.618 154.462 142.229 1.00 50.19  ? 284  LYS   A CE    1 
ATOM   268   N  NZ    . LYS   A 1 284  ? 115.243 153.208 142.729 1.00 51.58  ? 284  LYS   A NZ    1 
ATOM   269   N  N     . PHE   A 1 285  ? 112.545 157.574 147.251 1.00 37.36  ? 285  PHE   A N     1 
ATOM   270   C  CA    . PHE   A 1 285  ? 112.266 158.473 148.360 1.00 35.38  ? 285  PHE   A CA    1 
ATOM   271   C  C     . PHE   A 1 285  ? 112.912 159.832 148.126 1.00 35.48  ? 285  PHE   A C     1 
ATOM   272   O  O     . PHE   A 1 285  ? 113.914 159.952 147.418 1.00 47.03  ? 285  PHE   A O     1 
ATOM   273   C  CB    . PHE   A 1 285  ? 112.767 157.883 149.679 1.00 41.17  ? 285  PHE   A CB    1 
ATOM   274   C  CG    . PHE   A 1 285  ? 112.080 156.609 150.073 1.00 45.99  ? 285  PHE   A CG    1 
ATOM   275   C  CD1   . PHE   A 1 285  ? 110.845 156.637 150.694 1.00 47.63  ? 285  PHE   A CD1   1 
ATOM   276   C  CD2   . PHE   A 1 285  ? 112.669 155.383 149.822 1.00 46.40  ? 285  PHE   A CD2   1 
ATOM   277   C  CE1   . PHE   A 1 285  ? 110.211 155.467 151.057 1.00 45.97  ? 285  PHE   A CE1   1 
ATOM   278   C  CE2   . PHE   A 1 285  ? 112.039 154.211 150.184 1.00 45.34  ? 285  PHE   A CE2   1 
ATOM   279   C  CZ    . PHE   A 1 285  ? 110.809 154.253 150.801 1.00 44.56  ? 285  PHE   A CZ    1 
ATOM   280   N  N     . GLY   A 1 286  ? 112.321 160.861 148.731 1.00 35.09  ? 286  GLY   A N     1 
ATOM   281   C  CA    . GLY   A 1 286  ? 112.884 162.191 148.688 1.00 33.39  ? 286  GLY   A CA    1 
ATOM   282   C  C     . GLY   A 1 286  ? 114.020 162.363 149.677 1.00 39.14  ? 286  GLY   A C     1 
ATOM   283   O  O     . GLY   A 1 286  ? 114.405 161.449 150.406 1.00 46.10  ? 286  GLY   A O     1 
ATOM   284   N  N     . TRP   A 1 287  ? 114.569 163.579 149.700 1.00 31.97  ? 287  TRP   A N     1 
ATOM   285   C  CA    . TRP   A 1 287  ? 115.708 163.851 150.570 1.00 22.34  ? 287  TRP   A CA    1 
ATOM   286   C  C     . TRP   A 1 287  ? 115.299 163.918 152.036 1.00 34.14  ? 287  TRP   A C     1 
ATOM   287   O  O     . TRP   A 1 287  ? 116.120 163.641 152.918 1.00 40.94  ? 287  TRP   A O     1 
ATOM   288   C  CB    . TRP   A 1 287  ? 116.389 165.154 150.156 1.00 34.70  ? 287  TRP   A CB    1 
ATOM   289   C  CG    . TRP   A 1 287  ? 115.570 166.371 150.434 1.00 33.20  ? 287  TRP   A CG    1 
ATOM   290   C  CD1   . TRP   A 1 287  ? 114.567 166.876 149.664 1.00 33.23  ? 287  TRP   A CD1   1 
ATOM   291   C  CD2   . TRP   A 1 287  ? 115.688 167.244 151.563 1.00 29.79  ? 287  TRP   A CD2   1 
ATOM   292   N  NE1   . TRP   A 1 287  ? 114.050 168.008 150.242 1.00 41.39  ? 287  TRP   A NE1   1 
ATOM   293   C  CE2   . TRP   A 1 287  ? 114.722 168.255 151.410 1.00 35.03  ? 287  TRP   A CE2   1 
ATOM   294   C  CE3   . TRP   A 1 287  ? 116.517 167.267 152.688 1.00 30.78  ? 287  TRP   A CE3   1 
ATOM   295   C  CZ2   . TRP   A 1 287  ? 114.561 169.279 152.339 1.00 41.12  ? 287  TRP   A CZ2   1 
ATOM   296   C  CZ3   . TRP   A 1 287  ? 116.355 168.284 153.609 1.00 31.14  ? 287  TRP   A CZ3   1 
ATOM   297   C  CH2   . TRP   A 1 287  ? 115.385 169.275 153.429 1.00 39.88  ? 287  TRP   A CH2   1 
ATOM   298   N  N     . ILE   A 1 288  ? 114.048 164.281 152.316 1.00 41.52  ? 288  ILE   A N     1 
ATOM   299   C  CA    . ILE   A 1 288  ? 113.597 164.418 153.698 1.00 38.35  ? 288  ILE   A CA    1 
ATOM   300   C  C     . ILE   A 1 288  ? 113.291 163.054 154.303 1.00 39.62  ? 288  ILE   A C     1 
ATOM   301   O  O     . ILE   A 1 288  ? 113.849 162.674 155.339 1.00 41.84  ? 288  ILE   A O     1 
ATOM   302   C  CB    . ILE   A 1 288  ? 112.375 165.350 153.776 1.00 30.95  ? 288  ILE   A CB    1 
ATOM   303   C  CG1   . ILE   A 1 288  ? 112.827 166.808 153.831 1.00 39.18  ? 288  ILE   A CG1   1 
ATOM   304   C  CG2   . ILE   A 1 288  ? 111.533 165.019 154.993 1.00 36.11  ? 288  ILE   A CG2   1 
ATOM   305   C  CD1   . ILE   A 1 288  ? 111.693 167.796 153.924 1.00 42.75  ? 288  ILE   A CD1   1 
ATOM   306   N  N     . LYS   A 1 289  ? 112.398 162.298 153.666 1.00 44.94  ? 289  LYS   A N     1 
ATOM   307   C  CA    . LYS   A 1 289  ? 112.005 160.994 154.181 1.00 42.74  ? 289  LYS   A CA    1 
ATOM   308   C  C     . LYS   A 1 289  ? 113.011 159.899 153.859 1.00 40.08  ? 289  LYS   A C     1 
ATOM   309   O  O     . LYS   A 1 289  ? 112.859 158.777 154.355 1.00 46.19  ? 289  LYS   A O     1 
ATOM   310   C  CB    . LYS   A 1 289  ? 110.633 160.604 153.627 1.00 44.77  ? 289  LYS   A CB    1 
ATOM   311   C  CG    . LYS   A 1 289  ? 109.990 159.432 154.345 1.00 39.71  ? 289  LYS   A CG    1 
ATOM   312   C  CD    . LYS   A 1 289  ? 109.239 158.538 153.379 1.00 42.52  ? 289  LYS   A CD    1 
ATOM   313   C  CE    . LYS   A 1 289  ? 107.819 158.282 153.851 1.00 49.53  ? 289  LYS   A CE    1 
ATOM   314   N  NZ    . LYS   A 1 289  ? 107.087 157.369 152.931 1.00 50.29  ? 289  LYS   A NZ    1 
ATOM   315   N  N     . GLY   A 1 290  ? 114.026 160.190 153.052 1.00 31.88  ? 290  GLY   A N     1 
ATOM   316   C  CA    . GLY   A 1 290  ? 114.980 159.174 152.658 1.00 34.16  ? 290  GLY   A CA    1 
ATOM   317   C  C     . GLY   A 1 290  ? 116.353 159.329 153.277 1.00 32.93  ? 290  GLY   A C     1 
ATOM   318   O  O     . GLY   A 1 290  ? 117.045 158.335 153.512 1.00 35.61  ? 290  GLY   A O     1 
ATOM   319   N  N     . VAL   A 1 291  ? 116.763 160.568 153.547 1.00 36.12  ? 291  VAL   A N     1 
ATOM   320   C  CA    . VAL   A 1 291  ? 118.088 160.866 154.075 1.00 40.64  ? 291  VAL   A CA    1 
ATOM   321   C  C     . VAL   A 1 291  ? 118.008 161.561 155.429 1.00 37.19  ? 291  VAL   A C     1 
ATOM   322   O  O     . VAL   A 1 291  ? 118.662 161.148 156.391 1.00 45.18  ? 291  VAL   A O     1 
ATOM   323   C  CB    . VAL   A 1 291  ? 118.914 161.709 153.077 1.00 37.25  ? 291  VAL   A CB    1 
ATOM   324   C  CG1   . VAL   A 1 291  ? 120.343 161.863 153.567 1.00 27.34  ? 291  VAL   A CG1   1 
ATOM   325   C  CG2   . VAL   A 1 291  ? 118.886 161.076 151.695 1.00 32.00  ? 291  VAL   A CG2   1 
ATOM   326   N  N     . LEU   A 1 292  ? 117.206 162.623 155.523 1.00 24.71  ? 292  LEU   A N     1 
ATOM   327   C  CA    . LEU   A 1 292  ? 117.140 163.391 156.763 1.00 32.16  ? 292  LEU   A CA    1 
ATOM   328   C  C     . LEU   A 1 292  ? 116.658 162.528 157.922 1.00 27.90  ? 292  LEU   A C     1 
ATOM   329   O  O     . LEU   A 1 292  ? 117.311 162.449 158.970 1.00 38.58  ? 292  LEU   A O     1 
ATOM   330   C  CB    . LEU   A 1 292  ? 116.224 164.601 156.577 1.00 35.47  ? 292  LEU   A CB    1 
ATOM   331   C  CG    . LEU   A 1 292  ? 116.099 165.559 157.762 1.00 31.98  ? 292  LEU   A CG    1 
ATOM   332   C  CD1   . LEU   A 1 292  ? 117.461 166.105 158.154 1.00 30.18  ? 292  LEU   A CD1   1 
ATOM   333   C  CD2   . LEU   A 1 292  ? 115.137 166.691 157.443 1.00 36.10  ? 292  LEU   A CD2   1 
ATOM   334   N  N     . VAL   A 1 293  ? 115.515 161.862 157.746 1.00 31.82  ? 293  VAL   A N     1 
ATOM   335   C  CA    . VAL   A 1 293  ? 114.932 161.084 158.833 1.00 40.22  ? 293  VAL   A CA    1 
ATOM   336   C  C     . VAL   A 1 293  ? 115.838 159.920 159.208 1.00 37.68  ? 293  VAL   A C     1 
ATOM   337   O  O     . VAL   A 1 293  ? 116.078 159.661 160.393 1.00 36.33  ? 293  VAL   A O     1 
ATOM   338   C  CB    . VAL   A 1 293  ? 113.521 160.603 158.448 1.00 37.56  ? 293  VAL   A CB    1 
ATOM   339   C  CG1   . VAL   A 1 293  ? 113.089 159.445 159.336 1.00 34.54  ? 293  VAL   A CG1   1 
ATOM   340   C  CG2   . VAL   A 1 293  ? 112.527 161.748 158.532 1.00 33.33  ? 293  VAL   A CG2   1 
ATOM   341   N  N     . ARG   A 1 294  ? 116.347 159.194 158.211 1.00 32.59  ? 294  ARG   A N     1 
ATOM   342   C  CA    . ARG   A 1 294  ? 117.199 158.046 158.502 1.00 32.82  ? 294  ARG   A CA    1 
ATOM   343   C  C     . ARG   A 1 294  ? 118.472 158.472 159.221 1.00 38.19  ? 294  ARG   A C     1 
ATOM   344   O  O     . ARG   A 1 294  ? 118.879 157.843 160.204 1.00 45.84  ? 294  ARG   A O     1 
ATOM   345   C  CB    . ARG   A 1 294  ? 117.533 157.301 157.210 1.00 34.72  ? 294  ARG   A CB    1 
ATOM   346   C  CG    . ARG   A 1 294  ? 116.353 156.569 156.598 1.00 38.18  ? 294  ARG   A CG    1 
ATOM   347   C  CD    . ARG   A 1 294  ? 116.804 155.612 155.513 1.00 37.02  ? 294  ARG   A CD    1 
ATOM   348   N  NE    . ARG   A 1 294  ? 117.761 154.635 156.015 1.00 44.86  ? 294  ARG   A NE    1 
ATOM   349   C  CZ    . ARG   A 1 294  ? 117.459 153.383 156.328 1.00 45.27  ? 294  ARG   A CZ    1 
ATOM   350   N  NH1   . ARG   A 1 294  ? 116.225 152.920 156.212 1.00 38.72  ? 294  ARG   A NH1   1 
ATOM   351   N  NH2   . ARG   A 1 294  ? 118.419 152.575 156.767 1.00 46.99  ? 294  ARG   A NH2   1 
ATOM   352   N  N     . CYS   A 1 295  ? 119.115 159.541 158.747 1.00 42.48  ? 295  CYS   A N     1 
ATOM   353   C  CA    . CYS   A 1 295  ? 120.331 160.017 159.398 1.00 37.68  ? 295  CYS   A CA    1 
ATOM   354   C  C     . CYS   A 1 295  ? 120.053 160.457 160.829 1.00 34.18  ? 295  CYS   A C     1 
ATOM   355   O  O     . CYS   A 1 295  ? 120.805 160.114 161.750 1.00 38.04  ? 295  CYS   A O     1 
ATOM   356   C  CB    . CYS   A 1 295  ? 120.941 161.164 158.593 1.00 37.60  ? 295  CYS   A CB    1 
ATOM   357   S  SG    . CYS   A 1 295  ? 121.830 160.646 157.108 1.00 51.71  ? 295  CYS   A SG    1 
ATOM   358   N  N     . MET   A 1 296  ? 118.972 161.213 161.039 1.00 39.04  ? 296  MET   A N     1 
ATOM   359   C  CA    . MET   A 1 296  ? 118.654 161.683 162.383 1.00 35.97  ? 296  MET   A CA    1 
ATOM   360   C  C     . MET   A 1 296  ? 118.352 160.521 163.320 1.00 36.75  ? 296  MET   A C     1 
ATOM   361   O  O     . MET   A 1 296  ? 118.777 160.525 164.481 1.00 42.32  ? 296  MET   A O     1 
ATOM   362   C  CB    . MET   A 1 296  ? 117.477 162.656 162.335 1.00 34.27  ? 296  MET   A CB    1 
ATOM   363   C  CG    . MET   A 1 296  ? 117.843 164.037 161.819 1.00 42.12  ? 296  MET   A CG    1 
ATOM   364   S  SD    . MET   A 1 296  ? 116.462 165.191 161.859 1.00 61.17  ? 296  MET   A SD    1 
ATOM   365   C  CE    . MET   A 1 296  ? 115.081 164.056 161.894 1.00 44.39  ? 296  MET   A CE    1 
ATOM   366   N  N     . LEU   A 1 297  ? 117.616 159.518 162.838 1.00 36.63  ? 297  LEU   A N     1 
ATOM   367   C  CA    . LEU   A 1 297  ? 117.259 158.395 163.696 1.00 27.55  ? 297  LEU   A CA    1 
ATOM   368   C  C     . LEU   A 1 297  ? 118.455 157.501 163.987 1.00 29.51  ? 297  LEU   A C     1 
ATOM   369   O  O     . LEU   A 1 297  ? 118.561 156.954 165.091 1.00 43.28  ? 297  LEU   A O     1 
ATOM   370   C  CB    . LEU   A 1 297  ? 116.131 157.585 163.059 1.00 32.66  ? 297  LEU   A CB    1 
ATOM   371   C  CG    . LEU   A 1 297  ? 114.748 158.231 163.144 1.00 36.24  ? 297  LEU   A CG    1 
ATOM   372   C  CD1   . LEU   A 1 297  ? 113.686 157.325 162.548 1.00 38.42  ? 297  LEU   A CD1   1 
ATOM   373   C  CD2   . LEU   A 1 297  ? 114.414 158.576 164.584 1.00 36.27  ? 297  LEU   A CD2   1 
ATOM   374   N  N     . ASN   A 1 298  ? 119.359 157.332 163.021 1.00 31.71  ? 298  ASN   A N     1 
ATOM   375   C  CA    . ASN   A 1 298  ? 120.540 156.512 163.265 1.00 30.67  ? 298  ASN   A CA    1 
ATOM   376   C  C     . ASN   A 1 298  ? 121.513 157.215 164.202 1.00 27.10  ? 298  ASN   A C     1 
ATOM   377   O  O     . ASN   A 1 298  ? 122.133 156.573 165.056 1.00 33.99  ? 298  ASN   A O     1 
ATOM   378   C  CB    . ASN   A 1 298  ? 121.217 156.164 161.940 1.00 38.31  ? 298  ASN   A CB    1 
ATOM   379   C  CG    . ASN   A 1 298  ? 122.008 154.874 162.010 1.00 39.91  ? 298  ASN   A CG    1 
ATOM   380   O  OD1   . ASN   A 1 298  ? 121.651 153.951 162.741 1.00 33.84  ? 298  ASN   A OD1   1 
ATOM   381   N  ND2   . ASN   A 1 298  ? 123.088 154.800 161.242 1.00 43.40  ? 298  ASN   A ND2   1 
ATOM   382   N  N     . ILE   A 1 299  ? 121.659 158.534 164.057 1.00 22.05  ? 299  ILE   A N     1 
ATOM   383   C  CA    . ILE   A 1 299  ? 122.569 159.280 164.922 1.00 21.85  ? 299  ILE   A CA    1 
ATOM   384   C  C     . ILE   A 1 299  ? 122.101 159.225 166.370 1.00 37.31  ? 299  ILE   A C     1 
ATOM   385   O  O     . ILE   A 1 299  ? 122.904 159.026 167.291 1.00 48.33  ? 299  ILE   A O     1 
ATOM   386   C  CB    . ILE   A 1 299  ? 122.705 160.732 164.425 1.00 36.41  ? 299  ILE   A CB    1 
ATOM   387   C  CG1   . ILE   A 1 299  ? 123.700 160.806 163.265 1.00 33.64  ? 299  ILE   A CG1   1 
ATOM   388   C  CG2   . ILE   A 1 299  ? 123.129 161.647 165.561 1.00 35.83  ? 299  ILE   A CG2   1 
ATOM   389   C  CD1   . ILE   A 1 299  ? 123.522 162.018 162.378 1.00 26.96  ? 299  ILE   A CD1   1 
ATOM   390   N  N     . TRP   A 1 300  ? 120.803 159.399 166.597 1.00 40.96  ? 300  TRP   A N     1 
ATOM   391   C  CA    . TRP   A 1 300  ? 120.271 159.447 167.951 1.00 30.51  ? 300  TRP   A CA    1 
ATOM   392   C  C     . TRP   A 1 300  ? 120.134 158.048 168.535 1.00 36.94  ? 300  TRP   A C     1 
ATOM   393   O  O     . TRP   A 1 300  ? 119.758 157.099 167.841 1.00 36.65  ? 300  TRP   A O     1 
ATOM   394   C  CB    . TRP   A 1 300  ? 118.919 160.154 167.967 1.00 25.57  ? 300  TRP   A CB    1 
ATOM   395   C  CG    . TRP   A 1 300  ? 119.035 161.638 168.071 1.00 34.40  ? 300  TRP   A CG    1 
ATOM   396   C  CD1   . TRP   A 1 300  ? 120.086 162.342 168.578 1.00 36.59  ? 300  TRP   A CD1   1 
ATOM   397   C  CD2   . TRP   A 1 300  ? 118.068 162.605 167.651 1.00 33.39  ? 300  TRP   A CD2   1 
ATOM   398   N  NE1   . TRP   A 1 300  ? 119.833 163.689 168.503 1.00 43.49  ? 300  TRP   A NE1   1 
ATOM   399   C  CE2   . TRP   A 1 300  ? 118.600 163.877 167.937 1.00 36.67  ? 300  TRP   A CE2   1 
ATOM   400   C  CE3   . TRP   A 1 300  ? 116.805 162.520 167.060 1.00 30.12  ? 300  TRP   A CE3   1 
ATOM   401   C  CZ2   . TRP   A 1 300  ? 117.913 165.052 167.654 1.00 32.74  ? 300  TRP   A CZ2   1 
ATOM   402   C  CZ3   . TRP   A 1 300  ? 116.125 163.687 166.781 1.00 39.31  ? 300  TRP   A CZ3   1 
ATOM   403   C  CH2   . TRP   A 1 300  ? 116.680 164.937 167.078 1.00 39.84  ? 300  TRP   A CH2   1 
ATOM   404   N  N     . GLY   A 1 301  ? 120.441 157.929 169.824 1.00 45.12  ? 301  GLY   A N     1 
ATOM   405   C  CA    . GLY   A 1 301  ? 120.340 156.667 170.526 1.00 38.60  ? 301  GLY   A CA    1 
ATOM   406   C  C     . GLY   A 1 301  ? 120.056 156.849 172.002 1.00 43.58  ? 301  GLY   A C     1 
ATOM   407   O  O     . GLY   A 1 301  ? 119.503 157.873 172.413 1.00 44.98  ? 301  GLY   A O     1 
ATOM   408   N  N     . VAL   A 1 302  ? 120.429 155.856 172.812 1.00 49.84  ? 302  VAL   A N     1 
ATOM   409   C  CA    . VAL   A 1 302  ? 120.198 155.923 174.250 1.00 44.37  ? 302  VAL   A CA    1 
ATOM   410   C  C     . VAL   A 1 302  ? 121.057 156.965 174.947 1.00 44.65  ? 302  VAL   A C     1 
ATOM   411   O  O     . VAL   A 1 302  ? 120.849 157.224 176.137 1.00 52.06  ? 302  VAL   A O     1 
ATOM   412   C  CB    . VAL   A 1 302  ? 120.439 154.548 174.903 1.00 44.27  ? 302  VAL   A CB    1 
ATOM   413   C  CG1   . VAL   A 1 302  ? 119.722 153.458 174.126 1.00 43.18  ? 302  VAL   A CG1   1 
ATOM   414   C  CG2   . VAL   A 1 302  ? 121.930 154.261 174.986 1.00 45.29  ? 302  VAL   A CG2   1 
ATOM   415   N  N     . MET   A 1 303  ? 122.020 157.569 174.247 1.00 44.16  ? 303  MET   A N     1 
ATOM   416   C  CA    . MET   A 1 303  ? 122.871 158.565 174.889 1.00 44.23  ? 303  MET   A CA    1 
ATOM   417   C  C     . MET   A 1 303  ? 122.073 159.775 175.358 1.00 46.46  ? 303  MET   A C     1 
ATOM   418   O  O     . MET   A 1 303  ? 122.449 160.415 176.347 1.00 54.86  ? 303  MET   A O     1 
ATOM   419   C  CB    . MET   A 1 303  ? 123.983 159.004 173.937 1.00 41.69  ? 303  MET   A CB    1 
ATOM   420   C  CG    . MET   A 1 303  ? 124.763 160.215 174.421 1.00 40.37  ? 303  MET   A CG    1 
ATOM   421   S  SD    . MET   A 1 303  ? 126.140 159.789 175.503 1.00 59.33  ? 303  MET   A SD    1 
ATOM   422   C  CE    . MET   A 1 303  ? 126.448 158.095 175.016 1.00 48.79  ? 303  MET   A CE    1 
ATOM   423   N  N     . LEU   A 1 304  ? 120.975 160.101 174.676 1.00 41.78  ? 304  LEU   A N     1 
ATOM   424   C  CA    . LEU   A 1 304  ? 120.172 161.256 175.059 1.00 36.93  ? 304  LEU   A CA    1 
ATOM   425   C  C     . LEU   A 1 304  ? 119.385 161.034 176.342 1.00 43.79  ? 304  LEU   A C     1 
ATOM   426   O  O     . LEU   A 1 304  ? 118.834 161.999 176.881 1.00 51.14  ? 304  LEU   A O     1 
ATOM   427   C  CB    . LEU   A 1 304  ? 119.209 161.626 173.930 1.00 44.87  ? 304  LEU   A CB    1 
ATOM   428   C  CG    . LEU   A 1 304  ? 119.709 162.633 172.893 1.00 51.47  ? 304  LEU   A CG    1 
ATOM   429   C  CD1   . LEU   A 1 304  ? 118.728 162.746 171.737 1.00 44.93  ? 304  LEU   A CD1   1 
ATOM   430   C  CD2   . LEU   A 1 304  ? 119.944 163.991 173.534 1.00 46.74  ? 304  LEU   A CD2   1 
ATOM   431   N  N     . PHE   A 1 305  ? 119.318 159.800 176.844 1.00 50.67  ? 305  PHE   A N     1 
ATOM   432   C  CA    . PHE   A 1 305  ? 118.513 159.491 178.016 1.00 47.30  ? 305  PHE   A CA    1 
ATOM   433   C  C     . PHE   A 1 305  ? 119.241 158.691 179.085 1.00 46.08  ? 305  PHE   A C     1 
ATOM   434   O  O     . PHE   A 1 305  ? 118.671 158.485 180.161 1.00 49.98  ? 305  PHE   A O     1 
ATOM   435   C  CB    . PHE   A 1 305  ? 117.250 158.719 177.605 1.00 46.06  ? 305  PHE   A CB    1 
ATOM   436   C  CG    . PHE   A 1 305  ? 116.402 159.437 176.596 1.00 55.17  ? 305  PHE   A CG    1 
ATOM   437   C  CD1   . PHE   A 1 305  ? 116.050 160.762 176.786 1.00 52.62  ? 305  PHE   A CD1   1 
ATOM   438   C  CD2   . PHE   A 1 305  ? 115.964 158.789 175.454 1.00 53.37  ? 305  PHE   A CD2   1 
ATOM   439   C  CE1   . PHE   A 1 305  ? 115.272 161.425 175.857 1.00 50.90  ? 305  PHE   A CE1   1 
ATOM   440   C  CE2   . PHE   A 1 305  ? 115.187 159.446 174.523 1.00 48.58  ? 305  PHE   A CE2   1 
ATOM   441   C  CZ    . PHE   A 1 305  ? 114.841 160.766 174.724 1.00 47.96  ? 305  PHE   A CZ    1 
ATOM   442   N  N     . ILE   A 1 306  ? 120.466 158.234 178.834 1.00 48.15  ? 306  ILE   A N     1 
ATOM   443   C  CA    . ILE   A 1 306  ? 121.157 157.365 179.778 1.00 49.97  ? 306  ILE   A CA    1 
ATOM   444   C  C     . ILE   A 1 306  ? 122.492 157.977 180.182 1.00 56.55  ? 306  ILE   A C     1 
ATOM   445   O  O     . ILE   A 1 306  ? 122.730 158.247 181.365 1.00 61.07  ? 306  ILE   A O     1 
ATOM   446   C  CB    . ILE   A 1 306  ? 121.354 155.958 179.187 1.00 51.69  ? 306  ILE   A CB    1 
ATOM   447   C  CG1   . ILE   A 1 306  ? 120.031 155.192 179.189 1.00 48.99  ? 306  ILE   A CG1   1 
ATOM   448   C  CG2   . ILE   A 1 306  ? 122.399 155.192 179.977 1.00 55.78  ? 306  ILE   A CG2   1 
ATOM   449   C  CD1   . ILE   A 1 306  ? 120.095 153.858 178.486 1.00 46.60  ? 306  ILE   A CD1   1 
ATOM   450   N  N     . ARG   A 1 307  ? 123.369 158.208 179.205 1.00 48.63  ? 307  ARG   A N     1 
ATOM   451   C  CA    . ARG   A 1 307  ? 124.738 158.614 179.491 1.00 50.97  ? 307  ARG   A CA    1 
ATOM   452   C  C     . ARG   A 1 307  ? 124.981 160.110 179.353 1.00 50.39  ? 307  ARG   A C     1 
ATOM   453   O  O     . ARG   A 1 307  ? 126.003 160.599 179.847 1.00 61.29  ? 307  ARG   A O     1 
ATOM   454   C  CB    . ARG   A 1 307  ? 125.714 157.868 178.573 1.00 55.61  ? 307  ARG   A CB    1 
ATOM   455   C  CG    . ARG   A 1 307  ? 125.398 156.392 178.402 1.00 57.56  ? 307  ARG   A CG    1 
ATOM   456   C  CD    . ARG   A 1 307  ? 125.512 155.656 179.725 1.00 58.86  ? 307  ARG   A CD    1 
ATOM   457   N  NE    . ARG   A 1 307  ? 126.894 155.532 180.171 1.00 63.38  ? 307  ARG   A NE    1 
ATOM   458   C  CZ    . ARG   A 1 307  ? 127.692 154.518 179.865 1.00 65.29  ? 307  ARG   A CZ    1 
ATOM   459   N  NH1   . ARG   A 1 307  ? 127.279 153.520 179.102 1.00 64.44  ? 307  ARG   A NH1   1 
ATOM   460   N  NH2   . ARG   A 1 307  ? 128.934 154.505 180.339 1.00 62.09  ? 307  ARG   A NH2   1 
ATOM   461   N  N     . LEU   A 1 308  ? 124.082 160.848 178.702 1.00 39.70  ? 308  LEU   A N     1 
ATOM   462   C  CA    . LEU   A 1 308  ? 124.312 162.278 178.527 1.00 49.34  ? 308  LEU   A CA    1 
ATOM   463   C  C     . LEU   A 1 308  ? 124.374 162.992 179.871 1.00 52.98  ? 308  LEU   A C     1 
ATOM   464   O  O     . LEU   A 1 308  ? 125.252 163.833 180.096 1.00 51.86  ? 308  LEU   A O     1 
ATOM   465   C  CB    . LEU   A 1 308  ? 123.223 162.885 177.642 1.00 50.53  ? 308  LEU   A CB    1 
ATOM   466   C  CG    . LEU   A 1 308  ? 123.654 164.081 176.793 1.00 44.67  ? 308  LEU   A CG    1 
ATOM   467   C  CD1   . LEU   A 1 308  ? 123.159 165.376 177.408 1.00 50.52  ? 308  LEU   A CD1   1 
ATOM   468   C  CD2   . LEU   A 1 308  ? 125.163 164.109 176.643 1.00 42.40  ? 308  LEU   A CD2   1 
ATOM   469   N  N     . SER   A 1 309  ? 123.455 162.664 180.781 1.00 53.49  ? 309  SER   A N     1 
ATOM   470   C  CA    . SER   A 1 309  ? 123.499 163.258 182.112 1.00 46.90  ? 309  SER   A CA    1 
ATOM   471   C  C     . SER   A 1 309  ? 124.782 162.877 182.838 1.00 44.13  ? 309  SER   A C     1 
ATOM   472   O  O     . SER   A 1 309  ? 125.438 163.731 183.445 1.00 46.06  ? 309  SER   A O     1 
ATOM   473   C  CB    . SER   A 1 309  ? 122.276 162.826 182.920 1.00 47.66  ? 309  SER   A CB    1 
ATOM   474   O  OG    . SER   A 1 309  ? 121.958 161.468 182.675 1.00 50.33  ? 309  SER   A OG    1 
ATOM   475   N  N     . TRP   A 1 310  ? 125.159 161.598 182.782 1.00 47.04  ? 310  TRP   A N     1 
ATOM   476   C  CA    . TRP   A 1 310  ? 126.378 161.165 183.454 1.00 49.13  ? 310  TRP   A CA    1 
ATOM   477   C  C     . TRP   A 1 310  ? 127.605 161.833 182.851 1.00 49.12  ? 310  TRP   A C     1 
ATOM   478   O  O     . TRP   A 1 310  ? 128.539 162.200 183.571 1.00 52.76  ? 310  TRP   A O     1 
ATOM   479   C  CB    . TRP   A 1 310  ? 126.511 159.645 183.383 1.00 48.14  ? 310  TRP   A CB    1 
ATOM   480   C  CG    . TRP   A 1 310  ? 127.786 159.144 183.982 1.00 52.39  ? 310  TRP   A CG    1 
ATOM   481   C  CD1   . TRP   A 1 310  ? 128.019 158.872 185.298 1.00 53.26  ? 310  TRP   A CD1   1 
ATOM   482   C  CD2   . TRP   A 1 310  ? 129.011 158.873 183.293 1.00 52.25  ? 310  TRP   A CD2   1 
ATOM   483   N  NE1   . TRP   A 1 310  ? 129.310 158.438 185.470 1.00 56.21  ? 310  TRP   A NE1   1 
ATOM   484   C  CE2   . TRP   A 1 310  ? 129.941 158.430 184.254 1.00 52.74  ? 310  TRP   A CE2   1 
ATOM   485   C  CE3   . TRP   A 1 310  ? 129.412 158.957 181.957 1.00 48.90  ? 310  TRP   A CE3   1 
ATOM   486   C  CZ2   . TRP   A 1 310  ? 131.245 158.073 183.922 1.00 48.69  ? 310  TRP   A CZ2   1 
ATOM   487   C  CZ3   . TRP   A 1 310  ? 130.706 158.603 181.629 1.00 47.87  ? 310  TRP   A CZ3   1 
ATOM   488   C  CH2   . TRP   A 1 310  ? 131.607 158.166 182.607 1.00 50.57  ? 310  TRP   A CH2   1 
ATOM   489   N  N     . ILE   A 1 311  ? 127.632 161.980 181.526 1.00 45.89  ? 311  ILE   A N     1 
ATOM   490   C  CA    . ILE   A 1 311  ? 128.762 162.638 180.876 1.00 43.27  ? 311  ILE   A CA    1 
ATOM   491   C  C     . ILE   A 1 311  ? 128.847 164.094 181.314 1.00 48.64  ? 311  ILE   A C     1 
ATOM   492   O  O     . ILE   A 1 311  ? 129.926 164.599 181.647 1.00 49.91  ? 311  ILE   A O     1 
ATOM   493   C  CB    . ILE   A 1 311  ? 128.648 162.511 179.347 1.00 49.99  ? 311  ILE   A CB    1 
ATOM   494   C  CG1   . ILE   A 1 311  ? 128.795 161.047 178.929 1.00 48.85  ? 311  ILE   A CG1   1 
ATOM   495   C  CG2   . ILE   A 1 311  ? 129.688 163.381 178.659 1.00 44.88  ? 311  ILE   A CG2   1 
ATOM   496   C  CD1   . ILE   A 1 311  ? 129.438 160.858 177.580 1.00 46.33  ? 311  ILE   A CD1   1 
ATOM   497   N  N     . VAL   A 1 312  ? 127.709 164.791 181.325 1.00 51.26  ? 312  VAL   A N     1 
ATOM   498   C  CA    . VAL   A 1 312  ? 127.710 166.195 181.723 1.00 50.48  ? 312  VAL   A CA    1 
ATOM   499   C  C     . VAL   A 1 312  ? 128.094 166.341 183.189 1.00 55.79  ? 312  VAL   A C     1 
ATOM   500   O  O     . VAL   A 1 312  ? 128.663 167.363 183.590 1.00 56.40  ? 312  VAL   A O     1 
ATOM   501   C  CB    . VAL   A 1 312  ? 126.342 166.839 181.435 1.00 54.00  ? 312  VAL   A CB    1 
ATOM   502   C  CG1   . VAL   A 1 312  ? 126.078 167.975 182.407 1.00 52.36  ? 312  VAL   A CG1   1 
ATOM   503   C  CG2   . VAL   A 1 312  ? 126.286 167.338 180.002 1.00 55.87  ? 312  VAL   A CG2   1 
ATOM   504   N  N     . GLY   A 1 313  ? 127.779 165.342 184.013 1.00 56.28  ? 313  GLY   A N     1 
ATOM   505   C  CA    . GLY   A 1 313  ? 128.179 165.403 185.409 1.00 52.21  ? 313  GLY   A CA    1 
ATOM   506   C  C     . GLY   A 1 313  ? 129.666 165.167 185.596 1.00 52.37  ? 313  GLY   A C     1 
ATOM   507   O  O     . GLY   A 1 313  ? 130.367 165.984 186.199 1.00 55.37  ? 313  GLY   A O     1 
ATOM   508   N  N     . GLN   A 1 314  ? 130.169 164.044 185.078 1.00 52.85  ? 314  GLN   A N     1 
ATOM   509   C  CA    . GLN   A 1 314  ? 131.584 163.721 185.231 1.00 47.24  ? 314  GLN   A CA    1 
ATOM   510   C  C     . GLN   A 1 314  ? 132.461 164.839 184.684 1.00 46.74  ? 314  GLN   A C     1 
ATOM   511   O  O     . GLN   A 1 314  ? 133.360 165.333 185.373 1.00 60.70  ? 314  GLN   A O     1 
ATOM   512   C  CB    . GLN   A 1 314  ? 131.896 162.398 184.532 1.00 49.83  ? 314  GLN   A CB    1 
ATOM   513   C  CG    . GLN   A 1 314  ? 131.442 161.173 185.300 1.00 55.37  ? 314  GLN   A CG    1 
ATOM   514   C  CD    . GLN   A 1 314  ? 132.530 160.616 186.193 1.00 61.11  ? 314  GLN   A CD    1 
ATOM   515   O  OE1   . GLN   A 1 314  ? 133.529 161.282 186.461 1.00 64.03  ? 314  GLN   A OE1   1 
ATOM   516   N  NE2   . GLN   A 1 314  ? 132.342 159.388 186.661 1.00 58.70  ? 314  GLN   A NE2   1 
ATOM   517   N  N     . ALA   A 1 315  ? 132.211 165.253 183.449 1.00 45.02  ? 315  ALA   A N     1 
ATOM   518   C  CA    . ALA   A 1 315  ? 132.880 166.413 182.890 1.00 47.26  ? 315  ALA   A CA    1 
ATOM   519   C  C     . ALA   A 1 315  ? 132.109 167.678 183.254 1.00 50.64  ? 315  ALA   A C     1 
ATOM   520   O  O     . ALA   A 1 315  ? 131.092 167.639 183.949 1.00 49.52  ? 315  ALA   A O     1 
ATOM   521   C  CB    . ALA   A 1 315  ? 133.015 166.276 181.374 1.00 50.64  ? 315  ALA   A CB    1 
ATOM   522   N  N     . GLY   A 1 316  ? 132.610 168.814 182.786 1.00 47.07  ? 316  GLY   A N     1 
ATOM   523   C  CA    . GLY   A 1 316  ? 131.911 170.062 182.995 1.00 50.10  ? 316  GLY   A CA    1 
ATOM   524   C  C     . GLY   A 1 316  ? 130.927 170.358 181.884 1.00 55.47  ? 316  GLY   A C     1 
ATOM   525   O  O     . GLY   A 1 316  ? 130.904 169.704 180.842 1.00 64.28  ? 316  GLY   A O     1 
ATOM   526   N  N     . ILE   A 1 317  ? 130.088 171.367 182.119 1.00 48.79  ? 317  ILE   A N     1 
ATOM   527   C  CA    . ILE   A 1 317  ? 129.202 171.841 181.059 1.00 46.17  ? 317  ILE   A CA    1 
ATOM   528   C  C     . ILE   A 1 317  ? 130.026 172.281 179.857 1.00 51.45  ? 317  ILE   A C     1 
ATOM   529   O  O     . ILE   A 1 317  ? 129.771 171.872 178.716 1.00 60.66  ? 317  ILE   A O     1 
ATOM   530   C  CB    . ILE   A 1 317  ? 128.305 172.980 181.575 1.00 47.73  ? 317  ILE   A CB    1 
ATOM   531   C  CG1   . ILE   A 1 317  ? 127.027 172.418 182.198 1.00 55.90  ? 317  ILE   A CG1   1 
ATOM   532   C  CG2   . ILE   A 1 317  ? 127.966 173.940 180.446 1.00 45.38  ? 317  ILE   A CG2   1 
ATOM   533   C  CD1   . ILE   A 1 317  ? 126.119 173.478 182.784 1.00 52.44  ? 317  ILE   A CD1   1 
ATOM   534   N  N     . GLY   A 1 318  ? 131.046 173.104 180.103 1.00 47.37  ? 318  GLY   A N     1 
ATOM   535   C  CA    . GLY   A 1 318  ? 131.907 173.542 179.019 1.00 53.67  ? 318  GLY   A CA    1 
ATOM   536   C  C     . GLY   A 1 318  ? 132.674 172.399 178.383 1.00 52.48  ? 318  GLY   A C     1 
ATOM   537   O  O     . GLY   A 1 318  ? 132.778 172.317 177.158 1.00 55.38  ? 318  GLY   A O     1 
ATOM   538   N  N     . LEU   A 1 319  ? 133.218 171.499 179.204 1.00 49.68  ? 319  LEU   A N     1 
ATOM   539   C  CA    . LEU   A 1 319  ? 133.978 170.380 178.658 1.00 50.11  ? 319  LEU   A CA    1 
ATOM   540   C  C     . LEU   A 1 319  ? 133.074 169.408 177.911 1.00 51.73  ? 319  LEU   A C     1 
ATOM   541   O  O     . LEU   A 1 319  ? 133.467 168.856 176.877 1.00 58.83  ? 319  LEU   A O     1 
ATOM   542   C  CB    . LEU   A 1 319  ? 134.741 169.665 179.771 1.00 49.37  ? 319  LEU   A CB    1 
ATOM   543   C  CG    . LEU   A 1 319  ? 136.028 170.354 180.230 1.00 47.80  ? 319  LEU   A CG    1 
ATOM   544   C  CD1   . LEU   A 1 319  ? 136.880 169.411 181.064 1.00 49.47  ? 319  LEU   A CD1   1 
ATOM   545   C  CD2   . LEU   A 1 319  ? 136.811 170.880 179.038 1.00 43.14  ? 319  LEU   A CD2   1 
ATOM   546   N  N     . SER   A 1 320  ? 131.860 169.182 178.416 1.00 49.32  ? 320  SER   A N     1 
ATOM   547   C  CA    . SER   A 1 320  ? 130.915 168.338 177.692 1.00 52.87  ? 320  SER   A CA    1 
ATOM   548   C  C     . SER   A 1 320  ? 130.555 168.954 176.346 1.00 52.55  ? 320  SER   A C     1 
ATOM   549   O  O     . SER   A 1 320  ? 130.500 168.255 175.324 1.00 55.29  ? 320  SER   A O     1 
ATOM   550   C  CB    . SER   A 1 320  ? 129.661 168.111 178.535 1.00 52.07  ? 320  SER   A CB    1 
ATOM   551   O  OG    . SER   A 1 320  ? 128.681 169.098 178.265 1.00 56.09  ? 320  SER   A OG    1 
ATOM   552   N  N     . VAL   A 1 321  ? 130.280 170.256 176.345 1.00 46.12  ? 321  VAL   A N     1 
ATOM   553   C  CA    . VAL   A 1 321  ? 129.961 170.945 175.066 1.00 45.10  ? 321  VAL   A CA    1 
ATOM   554   C  C     . VAL   A 1 321  ? 131.151 170.747 174.128 1.00 48.97  ? 321  VAL   A C     1 
ATOM   555   O  O     . VAL   A 1 321  ? 130.917 170.411 172.969 1.00 57.60  ? 321  VAL   A O     1 
ATOM   556   C  CB    . VAL   A 1 321  ? 129.619 172.431 175.269 1.00 44.22  ? 321  VAL   A CB    1 
ATOM   557   C  CG1   . VAL   A 1 321  ? 129.637 173.202 173.960 1.00 48.81  ? 321  VAL   A CG1   1 
ATOM   558   C  CG2   . VAL   A 1 321  ? 128.283 172.604 175.973 1.00 47.99  ? 321  VAL   A CG2   1 
ATOM   559   N  N     . LEU   A 1 322  ? 132.373 170.889 174.637 1.00 47.60  ? 322  LEU   A N     1 
ATOM   560   C  CA    . LEU   A 1 322  ? 133.588 170.739 173.793 1.00 45.60  ? 322  LEU   A CA    1 
ATOM   561   C  C     . LEU   A 1 322  ? 133.638 169.319 173.218 1.00 49.58  ? 322  LEU   A C     1 
ATOM   562   O  O     . LEU   A 1 322  ? 133.963 169.181 172.031 1.00 61.92  ? 322  LEU   A O     1 
ATOM   563   C  CB    . LEU   A 1 322  ? 134.831 171.031 174.635 1.00 45.93  ? 322  LEU   A CB    1 
ATOM   564   C  CG    . LEU   A 1 322  ? 136.167 170.752 173.951 1.00 52.47  ? 322  LEU   A CG    1 
ATOM   565   C  CD1   . LEU   A 1 322  ? 136.363 171.666 172.752 1.00 56.06  ? 322  LEU   A CD1   1 
ATOM   566   C  CD2   . LEU   A 1 322  ? 137.320 170.904 174.929 1.00 56.19  ? 322  LEU   A CD2   1 
ATOM   567   N  N     . VAL   A 1 323  ? 133.343 168.307 174.032 1.00 39.30  ? 323  VAL   A N     1 
ATOM   568   C  CA    . VAL   A 1 323  ? 133.415 166.900 173.551 1.00 44.11  ? 323  VAL   A CA    1 
ATOM   569   C  C     . VAL   A 1 323  ? 132.433 166.764 172.389 1.00 52.48  ? 323  VAL   A C     1 
ATOM   570   O  O     . VAL   A 1 323  ? 132.831 166.241 171.301 1.00 56.16  ? 323  VAL   A O     1 
ATOM   571   C  CB    . VAL   A 1 323  ? 133.082 165.909 174.680 1.00 44.22  ? 323  VAL   A CB    1 
ATOM   572   C  CG1   . VAL   A 1 323  ? 132.773 164.520 174.147 1.00 49.70  ? 323  VAL   A CG1   1 
ATOM   573   C  CG2   . VAL   A 1 323  ? 134.185 165.850 175.723 1.00 46.68  ? 323  VAL   A CG2   1 
ATOM   574   N  N     . ILE   A 1 324  ? 131.212 167.258 172.597 1.00 42.48  ? 324  ILE   A N     1 
ATOM   575   C  CA    . ILE   A 1 324  ? 130.170 167.146 171.543 1.00 38.93  ? 324  ILE   A CA    1 
ATOM   576   C  C     . ILE   A 1 324  ? 130.714 167.825 170.292 1.00 42.97  ? 324  ILE   A C     1 
ATOM   577   O  O     . ILE   A 1 324  ? 130.710 167.184 169.254 1.00 45.56  ? 324  ILE   A O     1 
ATOM   578   C  CB    . ILE   A 1 324  ? 128.853 167.792 172.013 1.00 38.59  ? 324  ILE   A CB    1 
ATOM   579   C  CG1   . ILE   A 1 324  ? 128.362 167.189 173.330 1.00 44.82  ? 324  ILE   A CG1   1 
ATOM   580   C  CG2   . ILE   A 1 324  ? 127.791 167.709 170.929 1.00 35.62  ? 324  ILE   A CG2   1 
ATOM   581   C  CD1   . ILE   A 1 324  ? 127.083 167.801 173.845 1.00 45.82  ? 324  ILE   A CD1   1 
ATOM   582   N  N     . MET   A 1 325  ? 131.226 169.043 170.422 1.00 43.38  ? 325  MET   A N     1 
ATOM   583   C  CA    . MET   A 1 325  ? 131.699 169.831 169.259 1.00 41.64  ? 325  MET   A CA    1 
ATOM   584   C  C     . MET   A 1 325  ? 132.820 169.101 168.511 1.00 47.59  ? 325  MET   A C     1 
ATOM   585   O  O     . MET   A 1 325  ? 132.831 169.191 167.292 1.00 56.05  ? 325  MET   A O     1 
ATOM   586   C  CB    . MET   A 1 325  ? 132.194 171.203 169.723 1.00 41.63  ? 325  MET   A CB    1 
ATOM   587   N  N     . MET   A 1 326  ? 133.744 168.447 169.212 1.00 36.01  ? 326  MET   A N     1 
ATOM   588   C  CA    . MET   A 1 326  ? 134.885 167.752 168.553 1.00 42.52  ? 326  MET   A CA    1 
ATOM   589   C  C     . MET   A 1 326  ? 134.387 166.494 167.828 1.00 51.44  ? 326  MET   A C     1 
ATOM   590   O  O     . MET   A 1 326  ? 134.858 166.197 166.677 1.00 48.14  ? 326  MET   A O     1 
ATOM   591   C  CB    . MET   A 1 326  ? 135.946 167.373 169.588 1.00 30.00  ? 326  MET   A CB    1 
ATOM   592   C  CG    . MET   A 1 326  ? 136.677 168.571 170.157 1.00 30.00  ? 326  MET   A CG    1 
ATOM   593   S  SD    . MET   A 1 326  ? 138.019 168.101 171.275 1.00 30.00  ? 326  MET   A SD    1 
ATOM   594   C  CE    . MET   A 1 326  ? 137.093 167.286 172.573 1.00 30.00  ? 326  MET   A CE    1 
ATOM   595   N  N     . ALA   A 1 327  ? 133.459 165.776 168.458 1.00 42.95  ? 327  ALA   A N     1 
ATOM   596   C  CA    . ALA   A 1 327  ? 132.879 164.620 167.747 1.00 38.24  ? 327  ALA   A CA    1 
ATOM   597   C  C     . ALA   A 1 327  ? 132.181 165.150 166.494 1.00 42.00  ? 327  ALA   A C     1 
ATOM   598   O  O     . ALA   A 1 327  ? 132.230 164.484 165.424 1.00 42.77  ? 327  ALA   A O     1 
ATOM   599   C  CB    . ALA   A 1 327  ? 131.923 163.911 168.662 1.00 39.16  ? 327  ALA   A CB    1 
ATOM   600   N  N     . THR   A 1 328  ? 131.579 166.329 166.618 1.00 39.47  ? 328  THR   A N     1 
ATOM   601   C  CA    . THR   A 1 328  ? 130.820 166.910 165.491 1.00 43.63  ? 328  THR   A CA    1 
ATOM   602   C  C     . THR   A 1 328  ? 131.804 167.292 164.393 1.00 40.43  ? 328  THR   A C     1 
ATOM   603   O  O     . THR   A 1 328  ? 131.455 167.116 163.260 1.00 45.09  ? 328  THR   A O     1 
ATOM   604   C  CB    . THR   A 1 328  ? 129.959 168.074 165.980 1.00 39.91  ? 328  THR   A CB    1 
ATOM   605   O  OG1   . THR   A 1 328  ? 129.095 167.516 166.966 1.00 49.91  ? 328  THR   A OG1   1 
ATOM   606   C  CG2   . THR   A 1 328  ? 129.160 168.730 164.876 1.00 44.24  ? 328  THR   A CG2   1 
ATOM   607   N  N     . VAL   A 1 329  ? 132.967 167.823 164.738 1.00 33.75  ? 329  VAL   A N     1 
ATOM   608   C  CA    . VAL   A 1 329  ? 134.015 168.120 163.730 1.00 41.12  ? 329  VAL   A CA    1 
ATOM   609   C  C     . VAL   A 1 329  ? 134.292 166.816 162.998 1.00 39.15  ? 329  VAL   A C     1 
ATOM   610   O  O     . VAL   A 1 329  ? 134.149 166.786 161.765 1.00 47.81  ? 329  VAL   A O     1 
ATOM   611   C  CB    . VAL   A 1 329  ? 135.289 168.656 164.404 1.00 40.99  ? 329  VAL   A CB    1 
ATOM   612   C  CG1   . VAL   A 1 329  ? 136.501 168.569 163.491 1.00 35.85  ? 329  VAL   A CG1   1 
ATOM   613   C  CG2   . VAL   A 1 329  ? 135.100 170.073 164.919 1.00 45.96  ? 329  VAL   A CG2   1 
ATOM   614   N  N     . VAL   A 1 330  ? 134.600 165.761 163.747 1.00 35.25  ? 330  VAL   A N     1 
ATOM   615   C  CA    . VAL   A 1 330  ? 134.967 164.515 163.019 1.00 32.19  ? 330  VAL   A CA    1 
ATOM   616   C  C     . VAL   A 1 330  ? 133.826 164.123 162.076 1.00 35.83  ? 330  VAL   A C     1 
ATOM   617   O  O     . VAL   A 1 330  ? 134.131 163.755 160.944 1.00 38.36  ? 330  VAL   A O     1 
ATOM   618   C  CB    . VAL   A 1 330  ? 135.326 163.371 163.981 1.00 39.74  ? 330  VAL   A CB    1 
ATOM   619   C  CG1   . VAL   A 1 330  ? 135.619 162.075 163.242 1.00 35.11  ? 330  VAL   A CG1   1 
ATOM   620   C  CG2   . VAL   A 1 330  ? 136.497 163.747 164.874 1.00 40.07  ? 330  VAL   A CG2   1 
ATOM   621   N  N     . THR   A 1 331  ? 132.568 164.224 162.508 1.00 42.35  ? 331  THR   A N     1 
ATOM   622   C  CA    . THR   A 1 331  ? 131.444 163.727 161.660 1.00 30.53  ? 331  THR   A CA    1 
ATOM   623   C  C     . THR   A 1 331  ? 131.160 164.651 160.469 1.00 25.39  ? 331  THR   A C     1 
ATOM   624   O  O     . THR   A 1 331  ? 130.817 164.128 159.406 1.00 30.87  ? 331  THR   A O     1 
ATOM   625   C  CB    . THR   A 1 331  ? 130.219 163.463 162.540 1.00 33.80  ? 331  THR   A CB    1 
ATOM   626   O  OG1   . THR   A 1 331  ? 129.887 164.675 163.214 1.00 43.19  ? 331  THR   A OG1   1 
ATOM   627   C  CG2   . THR   A 1 331  ? 130.474 162.356 163.537 1.00 34.85  ? 331  THR   A CG2   1 
ATOM   628   N  N     . THR   A 1 332  ? 131.282 165.961 160.643 1.00 28.21  ? 332  THR   A N     1 
ATOM   629   C  CA    . THR   A 1 332  ? 131.002 166.957 159.587 1.00 27.87  ? 332  THR   A CA    1 
ATOM   630   C  C     . THR   A 1 332  ? 132.090 166.846 158.535 1.00 29.02  ? 332  THR   A C     1 
ATOM   631   O  O     . THR   A 1 332  ? 131.770 166.840 157.334 1.00 35.97  ? 332  THR   A O     1 
ATOM   632   C  CB    . THR   A 1 332  ? 131.000 168.373 160.168 1.00 27.08  ? 332  THR   A CB    1 
ATOM   633   O  OG1   . THR   A 1 332  ? 130.160 168.372 161.322 1.00 46.34  ? 332  THR   A OG1   1 
ATOM   634   C  CG2   . THR   A 1 332  ? 130.525 169.419 159.184 1.00 31.11  ? 332  THR   A CG2   1 
ATOM   635   N  N     . ILE   A 1 333  ? 133.339 166.761 158.977 1.00 30.08  ? 333  ILE   A N     1 
ATOM   636   C  CA    . ILE   A 1 333  ? 134.349 166.543 157.945 1.00 28.38  ? 333  ILE   A CA    1 
ATOM   637   C  C     . ILE   A 1 333  ? 134.010 165.297 157.138 1.00 31.02  ? 333  ILE   A C     1 
ATOM   638   O  O     . ILE   A 1 333  ? 134.080 165.297 155.898 1.00 35.09  ? 333  ILE   A O     1 
ATOM   639   C  CB    . ILE   A 1 333  ? 135.751 166.449 158.573 1.00 29.64  ? 333  ILE   A CB    1 
ATOM   640   C  CG1   . ILE   A 1 333  ? 136.253 167.839 158.967 1.00 33.85  ? 333  ILE   A CG1   1 
ATOM   641   C  CG2   . ILE   A 1 333  ? 136.721 165.788 157.607 1.00 30.12  ? 333  ILE   A CG2   1 
ATOM   642   C  CD1   . ILE   A 1 333  ? 137.324 167.822 160.034 1.00 33.72  ? 333  ILE   A CD1   1 
ATOM   643   N  N     . THR   A 1 334  ? 133.628 164.217 157.825 1.00 34.85  ? 334  THR   A N     1 
ATOM   644   C  CA    . THR   A 1 334  ? 133.247 163.001 157.113 1.00 25.02  ? 334  THR   A CA    1 
ATOM   645   C  C     . THR   A 1 334  ? 132.057 163.249 156.193 1.00 28.81  ? 334  THR   A C     1 
ATOM   646   O  O     . THR   A 1 334  ? 132.021 162.748 155.063 1.00 39.87  ? 334  THR   A O     1 
ATOM   647   C  CB    . THR   A 1 334  ? 132.933 161.883 158.107 1.00 33.25  ? 334  THR   A CB    1 
ATOM   648   O  OG1   . THR   A 1 334  ? 134.004 161.770 159.052 1.00 37.53  ? 334  THR   A OG1   1 
ATOM   649   C  CG2   . THR   A 1 334  ? 132.762 160.558 157.382 1.00 28.51  ? 334  THR   A CG2   1 
ATOM   650   N  N     . GLY   A 1 335  ? 131.073 164.019 156.659 1.00 29.67  ? 335  GLY   A N     1 
ATOM   651   C  CA    . GLY   A 1 335  ? 129.907 164.298 155.838 1.00 26.04  ? 335  GLY   A CA    1 
ATOM   652   C  C     . GLY   A 1 335  ? 130.228 165.150 154.626 1.00 30.62  ? 335  GLY   A C     1 
ATOM   653   O  O     . GLY   A 1 335  ? 129.679 164.935 153.543 1.00 38.63  ? 335  GLY   A O     1 
ATOM   654   N  N     . LEU   A 1 336  ? 131.106 166.140 154.793 1.00 24.84  ? 336  LEU   A N     1 
ATOM   655   C  CA    . LEU   A 1 336  ? 131.534 166.936 153.649 1.00 21.31  ? 336  LEU   A CA    1 
ATOM   656   C  C     . LEU   A 1 336  ? 132.234 166.063 152.617 1.00 23.05  ? 336  LEU   A C     1 
ATOM   657   O  O     . LEU   A 1 336  ? 131.976 166.181 151.411 1.00 36.30  ? 336  LEU   A O     1 
ATOM   658   C  CB    . LEU   A 1 336  ? 132.455 168.068 154.104 1.00 26.97  ? 336  LEU   A CB    1 
ATOM   659   C  CG    . LEU   A 1 336  ? 131.836 169.173 154.960 1.00 26.62  ? 336  LEU   A CG    1 
ATOM   660   C  CD1   . LEU   A 1 336  ? 132.881 170.211 155.326 1.00 25.87  ? 336  LEU   A CD1   1 
ATOM   661   C  CD2   . LEU   A 1 336  ? 130.668 169.819 154.241 1.00 24.10  ? 336  LEU   A CD2   1 
ATOM   662   N  N     . SER   A 1 337  ? 133.115 165.170 153.072 1.00 27.85  ? 337  SER   A N     1 
ATOM   663   C  CA    . SER   A 1 337  ? 133.778 164.266 152.138 1.00 23.23  ? 337  SER   A CA    1 
ATOM   664   C  C     . SER   A 1 337  ? 132.769 163.359 151.441 1.00 23.90  ? 337  SER   A C     1 
ATOM   665   O  O     . SER   A 1 337  ? 132.879 163.101 150.236 1.00 36.17  ? 337  SER   A O     1 
ATOM   666   C  CB    . SER   A 1 337  ? 134.835 163.439 152.869 1.00 28.55  ? 337  SER   A CB    1 
ATOM   667   O  OG    . SER   A 1 337  ? 135.999 164.207 153.119 1.00 30.85  ? 337  SER   A OG    1 
ATOM   668   N  N     . THR   A 1 338  ? 131.775 162.866 152.184 1.00 25.89  ? 338  THR   A N     1 
ATOM   669   C  CA    . THR   A 1 338  ? 130.763 162.000 151.588 1.00 28.91  ? 338  THR   A CA    1 
ATOM   670   C  C     . THR   A 1 338  ? 129.954 162.739 150.529 1.00 25.83  ? 338  THR   A C     1 
ATOM   671   O  O     . THR   A 1 338  ? 129.676 162.192 149.458 1.00 36.71  ? 338  THR   A O     1 
ATOM   672   C  CB    . THR   A 1 338  ? 129.839 161.444 152.671 1.00 24.95  ? 338  THR   A CB    1 
ATOM   673   O  OG1   . THR   A 1 338  ? 130.613 161.082 153.821 1.00 34.39  ? 338  THR   A OG1   1 
ATOM   674   C  CG2   . THR   A 1 338  ? 129.096 160.220 152.162 1.00 20.27  ? 338  THR   A CG2   1 
ATOM   675   N  N     . SER   A 1 339  ? 129.563 163.982 150.812 1.00 28.04  ? 339  SER   A N     1 
ATOM   676   C  CA    . SER   A 1 339  ? 128.816 164.758 149.828 1.00 31.00  ? 339  SER   A CA    1 
ATOM   677   C  C     . SER   A 1 339  ? 129.662 165.033 148.591 1.00 19.63  ? 339  SER   A C     1 
ATOM   678   O  O     . SER   A 1 339  ? 129.168 164.961 147.458 1.00 28.29  ? 339  SER   A O     1 
ATOM   679   C  CB    . SER   A 1 339  ? 128.325 166.065 150.451 1.00 25.33  ? 339  SER   A CB    1 
ATOM   680   O  OG    . SER   A 1 339  ? 129.378 166.743 151.109 1.00 31.78  ? 339  SER   A OG    1 
ATOM   681   N  N     . ALA   A 1 340  ? 130.947 165.340 148.789 1.00 20.89  ? 340  ALA   A N     1 
ATOM   682   C  CA    . ALA   A 1 340  ? 131.832 165.551 147.650 1.00 26.08  ? 340  ALA   A CA    1 
ATOM   683   C  C     . ALA   A 1 340  ? 131.933 164.297 146.792 1.00 31.15  ? 340  ALA   A C     1 
ATOM   684   O  O     . ALA   A 1 340  ? 131.897 164.375 145.558 1.00 35.91  ? 340  ALA   A O     1 
ATOM   685   C  CB    . ALA   A 1 340  ? 133.215 165.985 148.132 1.00 24.28  ? 340  ALA   A CB    1 
ATOM   686   N  N     . ILE   A 1 341  ? 132.060 163.129 147.425 1.00 31.88  ? 341  ILE   A N     1 
ATOM   687   C  CA    . ILE   A 1 341  ? 132.175 161.890 146.664 1.00 21.71  ? 341  ILE   A CA    1 
ATOM   688   C  C     . ILE   A 1 341  ? 130.843 161.471 146.058 1.00 24.55  ? 341  ILE   A C     1 
ATOM   689   O  O     . ILE   A 1 341  ? 130.820 160.701 145.091 1.00 35.46  ? 341  ILE   A O     1 
ATOM   690   C  CB    . ILE   A 1 341  ? 132.745 160.770 147.555 1.00 23.67  ? 341  ILE   A CB    1 
ATOM   691   C  CG1   . ILE   A 1 341  ? 134.227 161.017 147.835 1.00 33.53  ? 341  ILE   A CG1   1 
ATOM   692   C  CG2   . ILE   A 1 341  ? 132.560 159.414 146.900 1.00 32.71  ? 341  ILE   A CG2   1 
ATOM   693   C  CD1   . ILE   A 1 341  ? 135.157 160.387 146.824 1.00 39.28  ? 341  ILE   A CD1   1 
ATOM   694   N  N     . ALA   A 1 342  ? 129.728 161.963 146.591 1.00 24.55  ? 342  ALA   A N     1 
ATOM   695   C  CA    . ALA   A 1 342  ? 128.416 161.595 146.082 1.00 21.40  ? 342  ALA   A CA    1 
ATOM   696   C  C     . ALA   A 1 342  ? 127.903 162.541 145.007 1.00 26.78  ? 342  ALA   A C     1 
ATOM   697   O  O     . ALA   A 1 342  ? 126.959 162.187 144.294 1.00 37.51  ? 342  ALA   A O     1 
ATOM   698   C  CB    . ALA   A 1 342  ? 127.404 161.534 147.230 1.00 27.98  ? 342  ALA   A CB    1 
ATOM   699   N  N     . THR   A 1 343  ? 128.497 163.725 144.868 1.00 29.85  ? 343  THR   A N     1 
ATOM   700   C  CA    . THR   A 1 343  ? 128.108 164.661 143.823 1.00 27.69  ? 343  THR   A CA    1 
ATOM   701   C  C     . THR   A 1 343  ? 128.969 164.528 142.571 1.00 30.38  ? 343  THR   A C     1 
ATOM   702   O  O     . THR   A 1 343  ? 129.114 165.497 141.819 1.00 29.50  ? 343  THR   A O     1 
ATOM   703   C  CB    . THR   A 1 343  ? 128.156 166.096 144.349 1.00 31.54  ? 343  THR   A CB    1 
ATOM   704   O  OG1   . THR   A 1 343  ? 129.378 166.309 145.065 1.00 36.00  ? 343  THR   A OG1   1 
ATOM   705   C  CG2   . THR   A 1 343  ? 126.980 166.358 145.271 1.00 28.59  ? 343  THR   A CG2   1 
ATOM   706   N  N     . ASN   A 1 344  ? 129.540 163.346 142.334 1.00 33.87  ? 344  ASN   A N     1 
ATOM   707   C  CA    . ASN   A 1 344  ? 130.366 163.130 141.150 1.00 28.86  ? 344  ASN   A CA    1 
ATOM   708   C  C     . ASN   A 1 344  ? 129.540 162.640 139.968 1.00 30.95  ? 344  ASN   A C     1 
ATOM   709   O  O     . ASN   A 1 344  ? 129.428 163.323 138.947 1.00 44.86  ? 344  ASN   A O     1 
ATOM   710   C  CB    . ASN   A 1 344  ? 131.480 162.131 141.471 1.00 38.60  ? 344  ASN   A CB    1 
ATOM   711   C  CG    . ASN   A 1 344  ? 132.636 162.223 140.505 1.00 38.75  ? 344  ASN   A CG    1 
ATOM   712   O  OD1   . ASN   A 1 344  ? 133.240 163.275 140.350 1.00 26.20  ? 344  ASN   A OD1   1 
ATOM   713   N  ND2   . ASN   A 1 344  ? 132.958 161.112 139.857 1.00 41.48  ? 344  ASN   A ND2   1 
ATOM   714   N  N     . GLY   A 1 345  ? 128.947 161.461 140.094 1.00 38.55  ? 345  GLY   A N     1 
ATOM   715   C  CA    . GLY   A 1 345  ? 128.143 160.907 139.026 1.00 35.63  ? 345  GLY   A CA    1 
ATOM   716   C  C     . GLY   A 1 345  ? 126.889 160.258 139.563 1.00 36.61  ? 345  GLY   A C     1 
ATOM   717   O  O     . GLY   A 1 345  ? 126.545 160.443 140.733 1.00 46.46  ? 345  GLY   A O     1 
ATOM   718   N  N     . PHE   A 1 346  ? 126.195 159.495 138.726 1.00 42.81  ? 346  PHE   A N     1 
ATOM   719   C  CA    . PHE   A 1 346  ? 125.014 158.788 139.192 1.00 47.15  ? 346  PHE   A CA    1 
ATOM   720   C  C     . PHE   A 1 346  ? 125.435 157.597 140.043 1.00 54.60  ? 346  PHE   A C     1 
ATOM   721   O  O     . PHE   A 1 346  ? 126.209 156.745 139.596 1.00 56.57  ? 346  PHE   A O     1 
ATOM   722   C  CB    . PHE   A 1 346  ? 124.167 158.324 138.010 1.00 42.70  ? 346  PHE   A CB    1 
ATOM   723   C  CG    . PHE   A 1 346  ? 123.022 157.437 138.402 1.00 54.48  ? 346  PHE   A CG    1 
ATOM   724   C  CD1   . PHE   A 1 346  ? 121.935 157.953 139.087 1.00 52.79  ? 346  PHE   A CD1   1 
ATOM   725   C  CD2   . PHE   A 1 346  ? 123.037 156.085 138.103 1.00 54.33  ? 346  PHE   A CD2   1 
ATOM   726   C  CE1   . PHE   A 1 346  ? 120.882 157.142 139.456 1.00 51.60  ? 346  PHE   A CE1   1 
ATOM   727   C  CE2   . PHE   A 1 346  ? 121.986 155.269 138.472 1.00 55.92  ? 346  PHE   A CE2   1 
ATOM   728   C  CZ    . PHE   A 1 346  ? 120.907 155.799 139.149 1.00 55.52  ? 346  PHE   A CZ    1 
ATOM   729   N  N     . VAL   A 1 347  ? 124.924 157.535 141.268 1.00 48.93  ? 347  VAL   A N     1 
ATOM   730   C  CA    . VAL   A 1 347  ? 125.237 156.442 142.181 1.00 46.80  ? 347  VAL   A CA    1 
ATOM   731   C  C     . VAL   A 1 347  ? 124.187 155.356 141.969 1.00 49.02  ? 347  VAL   A C     1 
ATOM   732   O  O     . VAL   A 1 347  ? 123.005 155.548 142.262 1.00 55.57  ? 347  VAL   A O     1 
ATOM   733   C  CB    . VAL   A 1 347  ? 125.294 156.918 143.639 1.00 47.30  ? 347  VAL   A CB    1 
ATOM   734   C  CG1   . VAL   A 1 347  ? 126.087 158.210 143.736 1.00 46.45  ? 347  VAL   A CG1   1 
ATOM   735   C  CG2   . VAL   A 1 347  ? 123.903 157.122 144.213 1.00 49.29  ? 347  VAL   A CG2   1 
ATOM   736   N  N     . ARG   A 1 348  ? 124.620 154.218 141.426 1.00 59.05  ? 348  ARG   A N     1 
ATOM   737   C  CA    . ARG   A 1 348  ? 123.669 153.190 141.020 1.00 62.02  ? 348  ARG   A CA    1 
ATOM   738   C  C     . ARG   A 1 348  ? 122.924 152.622 142.219 1.00 68.65  ? 348  ARG   A C     1 
ATOM   739   O  O     . ARG   A 1 348  ? 121.705 152.419 142.164 1.00 68.63  ? 348  ARG   A O     1 
ATOM   740   C  CB    . ARG   A 1 348  ? 124.394 152.081 140.259 1.00 55.94  ? 348  ARG   A CB    1 
ATOM   741   C  CG    . ARG   A 1 348  ? 124.645 152.408 138.796 1.00 60.59  ? 348  ARG   A CG    1 
ATOM   742   C  CD    . ARG   A 1 348  ? 123.503 151.954 137.902 1.00 61.18  ? 348  ARG   A CD    1 
ATOM   743   N  NE    . ARG   A 1 348  ? 123.479 152.689 136.642 1.00 64.42  ? 348  ARG   A NE    1 
ATOM   744   C  CZ    . ARG   A 1 348  ? 124.477 152.719 135.769 1.00 68.97  ? 348  ARG   A CZ    1 
ATOM   745   N  NH1   . ARG   A 1 348  ? 125.601 152.053 135.980 1.00 66.93  ? 348  ARG   A NH1   1 
ATOM   746   N  NH2   . ARG   A 1 348  ? 124.345 153.436 134.657 1.00 69.99  ? 348  ARG   A NH2   1 
ATOM   747   N  N     . GLY   A 1 349  ? 123.635 152.368 143.313 1.00 46.80  ? 349  GLY   A N     1 
ATOM   748   C  CA    . GLY   A 1 349  ? 123.027 151.784 144.491 1.00 40.63  ? 349  GLY   A CA    1 
ATOM   749   C  C     . GLY   A 1 349  ? 124.016 151.592 145.619 1.00 51.13  ? 349  GLY   A C     1 
ATOM   750   O  O     . GLY   A 1 349  ? 124.821 152.483 145.905 1.00 63.07  ? 349  GLY   A O     1 
ATOM   751   N  N     . GLY   A 1 350  ? 123.968 150.432 146.268 1.00 51.31  ? 350  GLY   A N     1 
ATOM   752   C  CA    . GLY   A 1 350  ? 124.873 150.146 147.362 1.00 46.61  ? 350  GLY   A CA    1 
ATOM   753   C  C     . GLY   A 1 350  ? 124.776 151.145 148.494 1.00 50.43  ? 350  GLY   A C     1 
ATOM   754   O  O     . GLY   A 1 350  ? 123.756 151.213 149.186 1.00 65.85  ? 350  GLY   A O     1 
ATOM   755   N  N     . GLY   A 1 351  ? 125.832 151.926 148.694 1.00 32.86  ? 351  GLY   A N     1 
ATOM   756   C  CA    . GLY   A 1 351  ? 125.863 152.908 149.758 1.00 36.21  ? 351  GLY   A CA    1 
ATOM   757   C  C     . GLY   A 1 351  ? 127.202 153.606 149.837 1.00 40.63  ? 351  GLY   A C     1 
ATOM   758   O  O     . GLY   A 1 351  ? 127.736 154.046 148.814 1.00 45.88  ? 351  GLY   A O     1 
ATOM   759   N  N     . ALA   A 1 352  ? 127.755 153.728 151.045 1.00 45.18  ? 352  ALA   A N     1 
ATOM   760   C  CA    . ALA   A 1 352  ? 129.115 154.236 151.169 1.00 42.85  ? 352  ALA   A CA    1 
ATOM   761   C  C     . ALA   A 1 352  ? 130.106 153.323 150.464 1.00 39.71  ? 352  ALA   A C     1 
ATOM   762   O  O     . ALA   A 1 352  ? 131.156 153.783 149.998 1.00 41.23  ? 352  ALA   A O     1 
ATOM   763   C  CB    . ALA   A 1 352  ? 129.488 154.396 152.642 1.00 37.20  ? 352  ALA   A CB    1 
ATOM   764   N  N     . TYR   A 1 353  ? 129.787 152.029 150.367 1.00 40.00  ? 353  TYR   A N     1 
ATOM   765   C  CA    . TYR   A 1 353  ? 130.650 151.112 149.634 1.00 38.74  ? 353  TYR   A CA    1 
ATOM   766   C  C     . TYR   A 1 353  ? 130.730 151.491 148.163 1.00 39.07  ? 353  TYR   A C     1 
ATOM   767   O  O     . TYR   A 1 353  ? 131.813 151.478 147.571 1.00 44.81  ? 353  TYR   A O     1 
ATOM   768   C  CB    . TYR   A 1 353  ? 130.150 149.677 149.771 1.00 38.03  ? 353  TYR   A CB    1 
ATOM   769   C  CG    . TYR   A 1 353  ? 130.481 148.830 148.563 1.00 31.61  ? 353  TYR   A CG    1 
ATOM   770   C  CD1   . TYR   A 1 353  ? 131.769 148.355 148.357 1.00 39.78  ? 353  TYR   A CD1   1 
ATOM   771   C  CD2   . TYR   A 1 353  ? 129.513 148.527 147.616 1.00 38.07  ? 353  TYR   A CD2   1 
ATOM   772   C  CE1   . TYR   A 1 353  ? 132.080 147.591 147.251 1.00 32.36  ? 353  TYR   A CE1   1 
ATOM   773   C  CE2   . TYR   A 1 353  ? 129.815 147.763 146.505 1.00 39.44  ? 353  TYR   A CE2   1 
ATOM   774   C  CZ    . TYR   A 1 353  ? 131.100 147.297 146.328 1.00 34.11  ? 353  TYR   A CZ    1 
ATOM   775   O  OH    . TYR   A 1 353  ? 131.406 146.536 145.225 1.00 38.63  ? 353  TYR   A OH    1 
ATOM   776   N  N     . TYR   A 1 354  ? 129.590 151.816 147.551 1.00 28.41  ? 354  TYR   A N     1 
ATOM   777   C  CA    . TYR   A 1 354  ? 129.598 152.195 146.143 1.00 27.56  ? 354  TYR   A CA    1 
ATOM   778   C  C     . TYR   A 1 354  ? 130.452 153.436 145.922 1.00 39.45  ? 354  TYR   A C     1 
ATOM   779   O  O     . TYR   A 1 354  ? 131.271 153.487 144.997 1.00 40.78  ? 354  TYR   A O     1 
ATOM   780   C  CB    . TYR   A 1 354  ? 128.167 152.426 145.653 1.00 27.38  ? 354  TYR   A CB    1 
ATOM   781   C  CG    . TYR   A 1 354  ? 128.040 152.483 144.148 1.00 38.19  ? 354  TYR   A CG    1 
ATOM   782   C  CD1   . TYR   A 1 354  ? 127.866 151.327 143.400 1.00 40.35  ? 354  TYR   A CD1   1 
ATOM   783   C  CD2   . TYR   A 1 354  ? 128.097 153.695 143.475 1.00 36.37  ? 354  TYR   A CD2   1 
ATOM   784   C  CE1   . TYR   A 1 354  ? 127.753 151.377 142.026 1.00 32.29  ? 354  TYR   A CE1   1 
ATOM   785   C  CE2   . TYR   A 1 354  ? 127.984 153.755 142.103 1.00 35.67  ? 354  TYR   A CE2   1 
ATOM   786   C  CZ    . TYR   A 1 354  ? 127.813 152.594 141.383 1.00 36.34  ? 354  TYR   A CZ    1 
ATOM   787   O  OH    . TYR   A 1 354  ? 127.700 152.651 140.014 1.00 50.70  ? 354  TYR   A OH    1 
ATOM   788   N  N     . LEU   A 1 355  ? 130.289 154.441 146.783 1.00 36.78  ? 355  LEU   A N     1 
ATOM   789   C  CA    . LEU   A 1 355  ? 131.075 155.661 146.650 1.00 35.00  ? 355  LEU   A CA    1 
ATOM   790   C  C     . LEU   A 1 355  ? 132.563 155.371 146.799 1.00 32.69  ? 355  LEU   A C     1 
ATOM   791   O  O     . LEU   A 1 355  ? 133.375 155.793 145.969 1.00 46.84  ? 355  LEU   A O     1 
ATOM   792   C  CB    . LEU   A 1 355  ? 130.617 156.690 147.683 1.00 31.60  ? 355  LEU   A CB    1 
ATOM   793   C  CG    . LEU   A 1 355  ? 129.142 157.085 147.619 1.00 28.37  ? 355  LEU   A CG    1 
ATOM   794   C  CD1   . LEU   A 1 355  ? 128.730 157.825 148.878 1.00 36.29  ? 355  LEU   A CD1   1 
ATOM   795   C  CD2   . LEU   A 1 355  ? 128.870 157.934 146.390 1.00 30.63  ? 355  LEU   A CD2   1 
ATOM   796   N  N     . ILE   A 1 356  ? 132.936 154.624 147.840 1.00 24.55  ? 356  ILE   A N     1 
ATOM   797   C  CA    . ILE   A 1 356  ? 134.351 154.364 148.091 1.00 33.12  ? 356  ILE   A CA    1 
ATOM   798   C  C     . ILE   A 1 356  ? 134.962 153.563 146.948 1.00 37.44  ? 356  ILE   A C     1 
ATOM   799   O  O     . ILE   A 1 356  ? 136.078 153.852 146.493 1.00 37.23  ? 356  ILE   A O     1 
ATOM   800   C  CB    . ILE   A 1 356  ? 134.534 153.650 149.443 1.00 34.30  ? 356  ILE   A CB    1 
ATOM   801   C  CG1   . ILE   A 1 356  ? 134.570 154.670 150.583 1.00 38.28  ? 356  ILE   A CG1   1 
ATOM   802   C  CG2   . ILE   A 1 356  ? 135.802 152.810 149.437 1.00 31.51  ? 356  ILE   A CG2   1 
ATOM   803   C  CD1   . ILE   A 1 356  ? 134.196 154.094 151.930 1.00 40.29  ? 356  ILE   A CD1   1 
ATOM   804   N  N     . SER   A 1 357  ? 134.255 152.533 146.478 1.00 34.74  ? 357  SER   A N     1 
ATOM   805   C  CA    . SER   A 1 357  ? 134.781 151.711 145.396 1.00 31.65  ? 357  SER   A CA    1 
ATOM   806   C  C     . SER   A 1 357  ? 134.939 152.525 144.121 1.00 33.08  ? 357  SER   A C     1 
ATOM   807   O  O     . SER   A 1 357  ? 136.031 152.583 143.545 1.00 39.41  ? 357  SER   A O     1 
ATOM   808   C  CB    . SER   A 1 357  ? 133.872 150.503 145.166 1.00 34.83  ? 357  SER   A CB    1 
ATOM   809   O  OG    . SER   A 1 357  ? 132.712 150.862 144.438 1.00 37.38  ? 357  SER   A OG    1 
ATOM   810   N  N     . ARG   A 1 358  ? 133.874 153.207 143.690 1.00 36.70  ? 358  ARG   A N     1 
ATOM   811   C  CA    . ARG   A 1 358  ? 133.952 153.986 142.462 1.00 23.45  ? 358  ARG   A CA    1 
ATOM   812   C  C     . ARG   A 1 358  ? 134.933 155.143 142.583 1.00 30.58  ? 358  ARG   A C     1 
ATOM   813   O  O     . ARG   A 1 358  ? 135.355 155.690 141.560 1.00 45.12  ? 358  ARG   A O     1 
ATOM   814   C  CB    . ARG   A 1 358  ? 132.567 154.508 142.079 1.00 30.90  ? 358  ARG   A CB    1 
ATOM   815   C  CG    . ARG   A 1 358  ? 131.752 153.547 141.221 1.00 33.25  ? 358  ARG   A CG    1 
ATOM   816   C  CD    . ARG   A 1 358  ? 131.788 152.145 141.805 1.00 34.08  ? 358  ARG   A CD    1 
ATOM   817   N  NE    . ARG   A 1 358  ? 131.215 151.143 140.915 1.00 34.50  ? 358  ARG   A NE    1 
ATOM   818   C  CZ    . ARG   A 1 358  ? 130.820 149.940 141.308 1.00 39.27  ? 358  ARG   A CZ    1 
ATOM   819   N  NH1   . ARG   A 1 358  ? 130.947 149.548 142.565 1.00 32.84  ? 358  ARG   A NH1   1 
ATOM   820   N  NH2   . ARG   A 1 358  ? 130.287 149.108 140.418 1.00 40.60  ? 358  ARG   A NH2   1 
ATOM   821   N  N     . SER   A 1 359  ? 135.299 155.531 143.806 1.00 30.95  ? 359  SER   A N     1 
ATOM   822   C  CA    . SER   A 1 359  ? 136.297 156.578 143.984 1.00 26.65  ? 359  SER   A CA    1 
ATOM   823   C  C     . SER   A 1 359  ? 137.713 156.027 143.857 1.00 36.87  ? 359  SER   A C     1 
ATOM   824   O  O     . SER   A 1 359  ? 138.489 156.475 143.007 1.00 45.72  ? 359  SER   A O     1 
ATOM   825   C  CB    . SER   A 1 359  ? 136.107 157.259 145.341 1.00 34.79  ? 359  SER   A CB    1 
ATOM   826   O  OG    . SER   A 1 359  ? 134.787 157.750 145.483 1.00 47.08  ? 359  SER   A OG    1 
ATOM   827   N  N     . LEU   A 1 360  ? 138.071 155.051 144.691 1.00 34.94  ? 360  LEU   A N     1 
ATOM   828   C  CA    . LEU   A 1 360  ? 139.459 154.595 144.765 1.00 39.88  ? 360  LEU   A CA    1 
ATOM   829   C  C     . LEU   A 1 360  ? 139.565 153.073 144.722 1.00 39.04  ? 360  LEU   A C     1 
ATOM   830   O  O     . LEU   A 1 360  ? 140.235 152.451 145.548 1.00 53.27  ? 360  LEU   A O     1 
ATOM   831   C  CB    . LEU   A 1 360  ? 140.163 155.141 146.005 1.00 45.27  ? 360  LEU   A CB    1 
ATOM   832   C  CG    . LEU   A 1 360  ? 139.465 155.137 147.363 1.00 36.11  ? 360  LEU   A CG    1 
ATOM   833   C  CD1   . LEU   A 1 360  ? 139.346 153.730 147.913 1.00 41.79  ? 360  LEU   A CD1   1 
ATOM   834   C  CD2   . LEU   A 1 360  ? 140.252 156.013 148.322 1.00 40.08  ? 360  LEU   A CD2   1 
ATOM   835   N  N     . GLY   A 1 361  ? 138.914 152.445 143.748 1.00 32.26  ? 361  GLY   A N     1 
ATOM   836   C  CA    . GLY   A 1 361  ? 139.313 151.122 143.334 1.00 33.74  ? 361  GLY   A CA    1 
ATOM   837   C  C     . GLY   A 1 361  ? 138.703 149.966 144.100 1.00 36.57  ? 361  GLY   A C     1 
ATOM   838   O  O     . GLY   A 1 361  ? 138.304 150.076 145.268 1.00 41.96  ? 361  GLY   A O     1 
ATOM   839   N  N     . PRO   A 1 362  ? 138.660 148.806 143.440 1.00 38.41  ? 362  PRO   A N     1 
ATOM   840   C  CA    . PRO   A 1 362  ? 138.016 147.634 144.047 1.00 44.53  ? 362  PRO   A CA    1 
ATOM   841   C  C     . PRO   A 1 362  ? 138.683 147.142 145.317 1.00 46.15  ? 362  PRO   A C     1 
ATOM   842   O  O     . PRO   A 1 362  ? 137.996 146.565 146.161 1.00 55.65  ? 362  PRO   A O     1 
ATOM   843   C  CB    . PRO   A 1 362  ? 138.093 146.592 142.924 1.00 42.19  ? 362  PRO   A CB    1 
ATOM   844   C  CG    . PRO   A 1 362  ? 139.320 146.976 142.175 1.00 45.91  ? 362  PRO   A CG    1 
ATOM   845   C  CD    . PRO   A 1 362  ? 139.259 148.479 142.135 1.00 41.98  ? 362  PRO   A CD    1 
ATOM   846   N  N     . GLU   A 1 363  ? 139.986 147.348 145.495 1.00 49.89  ? 363  GLU   A N     1 
ATOM   847   C  CA    . GLU   A 1 363  ? 140.655 146.827 146.683 1.00 50.49  ? 363  GLU   A CA    1 
ATOM   848   C  C     . GLU   A 1 363  ? 140.064 147.436 147.950 1.00 54.00  ? 363  GLU   A C     1 
ATOM   849   O  O     . GLU   A 1 363  ? 139.445 146.739 148.772 1.00 59.99  ? 363  GLU   A O     1 
ATOM   850   C  CB    . GLU   A 1 363  ? 142.158 147.112 146.611 1.00 48.58  ? 363  GLU   A CB    1 
ATOM   851   C  CG    . GLU   A 1 363  ? 142.731 147.080 145.200 1.00 53.45  ? 363  GLU   A CG    1 
ATOM   852   C  CD    . GLU   A 1 363  ? 142.600 148.417 144.489 1.00 61.91  ? 363  GLU   A CD    1 
ATOM   853   O  OE1   . GLU   A 1 363  ? 142.061 149.363 145.101 1.00 63.70  ? 363  GLU   A OE1   1 
ATOM   854   O  OE2   . GLU   A 1 363  ? 143.028 148.521 143.320 1.00 58.83  ? 363  GLU   A OE2   1 
ATOM   855   N  N     . PHE   A 1 364  ? 140.247 148.750 148.099 1.00 48.96  ? 364  PHE   A N     1 
ATOM   856   C  CA    . PHE   A 1 364  ? 139.661 149.455 149.231 1.00 43.85  ? 364  PHE   A CA    1 
ATOM   857   C  C     . PHE   A 1 364  ? 138.146 149.334 149.221 1.00 46.33  ? 364  PHE   A C     1 
ATOM   858   O  O     . PHE   A 1 364  ? 137.519 149.231 150.282 1.00 48.70  ? 364  PHE   A O     1 
ATOM   859   C  CB    . PHE   A 1 364  ? 140.080 150.925 149.212 1.00 39.62  ? 364  PHE   A CB    1 
ATOM   860   C  CG    . PHE   A 1 364  ? 141.432 151.181 149.814 1.00 45.19  ? 364  PHE   A CG    1 
ATOM   861   C  CD1   . PHE   A 1 364  ? 141.760 150.673 151.059 1.00 50.65  ? 364  PHE   A CD1   1 
ATOM   862   C  CD2   . PHE   A 1 364  ? 142.373 151.936 149.136 1.00 47.72  ? 364  PHE   A CD2   1 
ATOM   863   C  CE1   . PHE   A 1 364  ? 143.003 150.912 151.615 1.00 50.28  ? 364  PHE   A CE1   1 
ATOM   864   C  CE2   . PHE   A 1 364  ? 143.617 152.177 149.687 1.00 47.78  ? 364  PHE   A CE2   1 
ATOM   865   C  CZ    . PHE   A 1 364  ? 143.932 151.664 150.927 1.00 47.97  ? 364  PHE   A CZ    1 
ATOM   866   N  N     . GLY   A 1 365  ? 137.535 149.338 148.033 1.00 41.66  ? 365  GLY   A N     1 
ATOM   867   C  CA    . GLY   A 1 365  ? 136.087 149.231 147.974 1.00 41.74  ? 365  GLY   A CA    1 
ATOM   868   C  C     . GLY   A 1 365  ? 135.575 147.962 148.626 1.00 40.16  ? 365  GLY   A C     1 
ATOM   869   O  O     . GLY   A 1 365  ? 134.679 148.003 149.468 1.00 45.31  ? 365  GLY   A O     1 
ATOM   870   N  N     . GLY   A 1 366  ? 136.161 146.820 148.267 1.00 40.67  ? 366  GLY   A N     1 
ATOM   871   C  CA    . GLY   A 1 366  ? 135.732 145.561 148.847 1.00 46.99  ? 366  GLY   A CA    1 
ATOM   872   C  C     . GLY   A 1 366  ? 136.070 145.451 150.319 1.00 49.70  ? 366  GLY   A C     1 
ATOM   873   O  O     . GLY   A 1 366  ? 135.258 144.969 151.117 1.00 55.84  ? 366  GLY   A O     1 
ATOM   874   N  N     . ALA   A 1 367  ? 137.269 145.897 150.707 1.00 37.34  ? 367  ALA   A N     1 
ATOM   875   C  CA    . ALA   A 1 367  ? 137.620 145.850 152.123 1.00 38.25  ? 367  ALA   A CA    1 
ATOM   876   C  C     . ALA   A 1 367  ? 136.607 146.625 152.958 1.00 41.70  ? 367  ALA   A C     1 
ATOM   877   O  O     . ALA   A 1 367  ? 136.012 146.087 153.906 1.00 46.28  ? 367  ALA   A O     1 
ATOM   878   C  CB    . ALA   A 1 367  ? 139.031 146.400 152.332 1.00 40.86  ? 367  ALA   A CB    1 
ATOM   879   N  N     . ILE   A 1 368  ? 136.370 147.888 152.593 1.00 41.43  ? 368  ILE   A N     1 
ATOM   880   C  CA    . ILE   A 1 368  ? 135.446 148.724 153.347 1.00 40.84  ? 368  ILE   A CA    1 
ATOM   881   C  C     . ILE   A 1 368  ? 134.023 148.198 153.249 1.00 41.39  ? 368  ILE   A C     1 
ATOM   882   O  O     . ILE   A 1 368  ? 133.261 148.296 154.213 1.00 50.94  ? 368  ILE   A O     1 
ATOM   883   C  CB    . ILE   A 1 368  ? 135.544 150.188 152.880 1.00 44.87  ? 368  ILE   A CB    1 
ATOM   884   C  CG1   . ILE   A 1 368  ? 135.258 151.136 154.048 1.00 47.95  ? 368  ILE   A CG1   1 
ATOM   885   C  CG2   . ILE   A 1 368  ? 134.592 150.450 151.723 1.00 43.98  ? 368  ILE   A CG2   1 
ATOM   886   C  CD1   . ILE   A 1 368  ? 136.320 151.127 155.125 1.00 42.19  ? 368  ILE   A CD1   1 
ATOM   887   N  N     . GLY   A 1 369  ? 133.630 147.641 152.102 1.00 34.99  ? 369  GLY   A N     1 
ATOM   888   C  CA    . GLY   A 1 369  ? 132.278 147.123 151.981 1.00 34.99  ? 369  GLY   A CA    1 
ATOM   889   C  C     . GLY   A 1 369  ? 132.024 145.958 152.914 1.00 48.78  ? 369  GLY   A C     1 
ATOM   890   O  O     . GLY   A 1 369  ? 131.007 145.914 153.611 1.00 53.15  ? 369  GLY   A O     1 
ATOM   891   N  N     . LEU   A 1 370  ? 132.953 145.001 152.951 1.00 41.69  ? 370  LEU   A N     1 
ATOM   892   C  CA    . LEU   A 1 370  ? 132.806 143.882 153.875 1.00 41.33  ? 370  LEU   A CA    1 
ATOM   893   C  C     . LEU   A 1 370  ? 132.788 144.371 155.318 1.00 44.45  ? 370  LEU   A C     1 
ATOM   894   O  O     . LEU   A 1 370  ? 131.933 143.962 156.118 1.00 49.35  ? 370  LEU   A O     1 
ATOM   895   C  CB    . LEU   A 1 370  ? 133.931 142.869 153.659 1.00 42.13  ? 370  LEU   A CB    1 
ATOM   896   C  CG    . LEU   A 1 370  ? 133.573 141.401 153.895 1.00 42.15  ? 370  LEU   A CG    1 
ATOM   897   C  CD1   . LEU   A 1 370  ? 132.219 141.075 153.292 1.00 43.31  ? 370  LEU   A CD1   1 
ATOM   898   C  CD2   . LEU   A 1 370  ? 134.646 140.486 153.331 1.00 46.34  ? 370  LEU   A CD2   1 
ATOM   899   N  N     . ILE   A 1 371  ? 133.713 145.272 155.664 1.00 43.93  ? 371  ILE   A N     1 
ATOM   900   C  CA    . ILE   A 1 371  ? 133.782 145.757 157.041 1.00 41.07  ? 371  ILE   A CA    1 
ATOM   901   C  C     . ILE   A 1 371  ? 132.480 146.449 157.427 1.00 39.95  ? 371  ILE   A C     1 
ATOM   902   O  O     . ILE   A 1 371  ? 131.923 146.206 158.503 1.00 43.13  ? 371  ILE   A O     1 
ATOM   903   C  CB    . ILE   A 1 371  ? 134.994 146.689 157.223 1.00 42.48  ? 371  ILE   A CB    1 
ATOM   904   C  CG1   . ILE   A 1 371  ? 136.270 145.870 157.423 1.00 41.69  ? 371  ILE   A CG1   1 
ATOM   905   C  CG2   . ILE   A 1 371  ? 134.773 147.625 158.398 1.00 39.53  ? 371  ILE   A CG2   1 
ATOM   906   C  CD1   . ILE   A 1 371  ? 136.170 144.847 158.530 1.00 42.70  ? 371  ILE   A CD1   1 
ATOM   907   N  N     . PHE   A 1 372  ? 131.973 147.318 156.550 1.00 35.84  ? 372  PHE   A N     1 
ATOM   908   C  CA    . PHE   A 1 372  ? 130.774 148.091 156.853 1.00 39.81  ? 372  PHE   A CA    1 
ATOM   909   C  C     . PHE   A 1 372  ? 129.542 147.199 156.942 1.00 39.37  ? 372  PHE   A C     1 
ATOM   910   O  O     . PHE   A 1 372  ? 128.690 147.391 157.820 1.00 44.87  ? 372  PHE   A O     1 
ATOM   911   C  CB    . PHE   A 1 372  ? 130.582 149.172 155.790 1.00 34.01  ? 372  PHE   A CB    1 
ATOM   912   C  CG    . PHE   A 1 372  ? 129.917 150.415 156.299 1.00 41.42  ? 372  PHE   A CG    1 
ATOM   913   C  CD1   . PHE   A 1 372  ? 130.266 150.947 157.527 1.00 45.94  ? 372  PHE   A CD1   1 
ATOM   914   C  CD2   . PHE   A 1 372  ? 128.956 151.062 155.545 1.00 38.68  ? 372  PHE   A CD2   1 
ATOM   915   C  CE1   . PHE   A 1 372  ? 129.661 152.093 157.997 1.00 42.09  ? 372  PHE   A CE1   1 
ATOM   916   C  CE2   . PHE   A 1 372  ? 128.349 152.210 156.011 1.00 42.90  ? 372  PHE   A CE2   1 
ATOM   917   C  CZ    . PHE   A 1 372  ? 128.703 152.726 157.238 1.00 42.80  ? 372  PHE   A CZ    1 
ATOM   918   N  N     . ALA   A 1 373  ? 129.421 146.225 156.036 1.00 29.70  ? 373  ALA   A N     1 
ATOM   919   C  CA    . ALA   A 1 373  ? 128.283 145.317 156.088 1.00 36.72  ? 373  ALA   A CA    1 
ATOM   920   C  C     . ALA   A 1 373  ? 128.283 144.523 157.386 1.00 39.43  ? 373  ALA   A C     1 
ATOM   921   O  O     . ALA   A 1 373  ? 127.244 144.385 158.045 1.00 42.01  ? 373  ALA   A O     1 
ATOM   922   C  CB    . ALA   A 1 373  ? 128.303 144.381 154.879 1.00 38.72  ? 373  ALA   A CB    1 
ATOM   923   N  N     . PHE   A 1 374  ? 129.449 144.005 157.783 1.00 35.02  ? 374  PHE   A N     1 
ATOM   924   C  CA    . PHE   A 1 374  ? 129.522 143.282 159.048 1.00 30.00  ? 374  PHE   A CA    1 
ATOM   925   C  C     . PHE   A 1 374  ? 129.207 144.201 160.222 1.00 35.16  ? 374  PHE   A C     1 
ATOM   926   O  O     . PHE   A 1 374  ? 128.518 143.802 161.171 1.00 42.38  ? 374  PHE   A O     1 
ATOM   927   C  CB    . PHE   A 1 374  ? 130.901 142.646 159.213 1.00 38.31  ? 374  PHE   A CB    1 
ATOM   928   C  CG    . PHE   A 1 374  ? 131.004 141.723 160.393 1.00 41.06  ? 374  PHE   A CG    1 
ATOM   929   C  CD1   . PHE   A 1 374  ? 130.243 140.569 160.453 1.00 37.74  ? 374  PHE   A CD1   1 
ATOM   930   C  CD2   . PHE   A 1 374  ? 131.860 142.009 161.443 1.00 44.12  ? 374  PHE   A CD2   1 
ATOM   931   C  CE1   . PHE   A 1 374  ? 130.334 139.718 161.536 1.00 44.54  ? 374  PHE   A CE1   1 
ATOM   932   C  CE2   . PHE   A 1 374  ? 131.955 141.160 162.528 1.00 44.33  ? 374  PHE   A CE2   1 
ATOM   933   C  CZ    . PHE   A 1 374  ? 131.191 140.014 162.575 1.00 43.15  ? 374  PHE   A CZ    1 
ATOM   934   N  N     . ALA   A 1 375  ? 129.701 145.440 160.173 1.00 39.19  ? 375  ALA   A N     1 
ATOM   935   C  CA    . ALA   A 1 375  ? 129.444 146.380 161.256 1.00 39.42  ? 375  ALA   A CA    1 
ATOM   936   C  C     . ALA   A 1 375  ? 127.953 146.640 161.418 1.00 41.62  ? 375  ALA   A C     1 
ATOM   937   O  O     . ALA   A 1 375  ? 127.443 146.666 162.541 1.00 45.96  ? 375  ALA   A O     1 
ATOM   938   C  CB    . ALA   A 1 375  ? 130.195 147.688 161.007 1.00 41.75  ? 375  ALA   A CB    1 
ATOM   939   N  N     . ASN   A 1 376  ? 127.235 146.832 160.310 1.00 37.86  ? 376  ASN   A N     1 
ATOM   940   C  CA    . ASN   A 1 376  ? 125.793 147.056 160.407 1.00 36.50  ? 376  ASN   A CA    1 
ATOM   941   C  C     . ASN   A 1 376  ? 125.063 145.803 160.878 1.00 33.24  ? 376  ASN   A C     1 
ATOM   942   O  O     . ASN   A 1 376  ? 124.127 145.884 161.691 1.00 37.81  ? 376  ASN   A O     1 
ATOM   943   C  CB    . ASN   A 1 376  ? 125.242 147.528 159.062 1.00 38.09  ? 376  ASN   A CB    1 
ATOM   944   C  CG    . ASN   A 1 376  ? 125.454 149.011 158.836 1.00 38.52  ? 376  ASN   A CG    1 
ATOM   945   O  OD1   . ASN   A 1 376  ? 124.521 149.805 158.941 1.00 43.56  ? 376  ASN   A OD1   1 
ATOM   946   N  ND2   . ASN   A 1 376  ? 126.687 149.393 158.527 1.00 33.35  ? 376  ASN   A ND2   1 
ATOM   947   N  N     . ALA   A 1 377  ? 125.474 144.633 160.378 1.00 41.05  ? 377  ALA   A N     1 
ATOM   948   C  CA    . ALA   A 1 377  ? 124.829 143.391 160.788 1.00 41.44  ? 377  ALA   A CA    1 
ATOM   949   C  C     . ALA   A 1 377  ? 125.002 143.135 162.278 1.00 47.94  ? 377  ALA   A C     1 
ATOM   950   O  O     . ALA   A 1 377  ? 124.140 142.509 162.903 1.00 46.66  ? 377  ALA   A O     1 
ATOM   951   C  CB    . ALA   A 1 377  ? 125.381 142.220 159.977 1.00 45.32  ? 377  ALA   A CB    1 
ATOM   952   N  N     . VAL   A 1 378  ? 126.112 143.590 162.860 1.00 43.85  ? 378  VAL   A N     1 
ATOM   953   C  CA    . VAL   A 1 378  ? 126.283 143.428 164.302 1.00 33.71  ? 378  VAL   A CA    1 
ATOM   954   C  C     . VAL   A 1 378  ? 125.626 144.573 165.069 1.00 35.47  ? 378  VAL   A C     1 
ATOM   955   O  O     . VAL   A 1 378  ? 125.181 144.389 166.210 1.00 49.38  ? 378  VAL   A O     1 
ATOM   956   C  CB    . VAL   A 1 378  ? 127.774 143.302 164.655 1.00 38.39  ? 378  VAL   A CB    1 
ATOM   957   C  CG1   . VAL   A 1 378  ? 127.939 142.933 166.118 1.00 40.02  ? 378  VAL   A CG1   1 
ATOM   958   C  CG2   . VAL   A 1 378  ? 128.440 142.266 163.767 1.00 40.94  ? 378  VAL   A CG2   1 
ATOM   959   N  N     . ALA   A 1 379  ? 125.552 145.762 164.469 1.00 36.16  ? 379  ALA   A N     1 
ATOM   960   C  CA    . ALA   A 1 379  ? 124.906 146.887 165.130 1.00 40.56  ? 379  ALA   A CA    1 
ATOM   961   C  C     . ALA   A 1 379  ? 123.424 146.622 165.335 1.00 41.08  ? 379  ALA   A C     1 
ATOM   962   O  O     . ALA   A 1 379  ? 122.846 147.039 166.344 1.00 48.16  ? 379  ALA   A O     1 
ATOM   963   C  CB    . ALA   A 1 379  ? 125.117 148.166 164.321 1.00 41.39  ? 379  ALA   A CB    1 
ATOM   964   N  N     . VAL   A 1 380  ? 122.783 145.943 164.382 1.00 43.10  ? 380  VAL   A N     1 
ATOM   965   C  CA    . VAL   A 1 380  ? 121.372 145.609 164.571 1.00 43.17  ? 380  VAL   A CA    1 
ATOM   966   C  C     . VAL   A 1 380  ? 121.195 144.768 165.830 1.00 38.44  ? 380  VAL   A C     1 
ATOM   967   O  O     . VAL   A 1 380  ? 120.308 145.029 166.656 1.00 39.61  ? 380  VAL   A O     1 
ATOM   968   C  CB    . VAL   A 1 380  ? 120.808 144.898 163.325 1.00 41.50  ? 380  VAL   A CB    1 
ATOM   969   C  CG1   . VAL   A 1 380  ? 121.892 144.106 162.625 1.00 43.42  ? 380  VAL   A CG1   1 
ATOM   970   C  CG2   . VAL   A 1 380  ? 119.646 143.993 163.708 1.00 38.60  ? 380  VAL   A CG2   1 
ATOM   971   N  N     . ALA   A 1 381  ? 122.051 143.760 166.009 1.00 45.77  ? 381  ALA   A N     1 
ATOM   972   C  CA    . ALA   A 1 381  ? 121.972 142.921 167.200 1.00 42.11  ? 381  ALA   A CA    1 
ATOM   973   C  C     . ALA   A 1 381  ? 122.257 143.725 168.462 1.00 40.36  ? 381  ALA   A C     1 
ATOM   974   O  O     . ALA   A 1 381  ? 121.603 143.529 169.491 1.00 51.71  ? 381  ALA   A O     1 
ATOM   975   C  CB    . ALA   A 1 381  ? 122.942 141.747 167.081 1.00 44.27  ? 381  ALA   A CB    1 
ATOM   976   N  N     . MET   A 1 382  ? 123.240 144.627 168.408 1.00 43.60  ? 382  MET   A N     1 
ATOM   977   C  CA    . MET   A 1 382  ? 123.550 145.437 169.584 1.00 40.04  ? 382  MET   A CA    1 
ATOM   978   C  C     . MET   A 1 382  ? 122.369 146.318 169.981 1.00 40.68  ? 382  MET   A C     1 
ATOM   979   O  O     . MET   A 1 382  ? 122.046 146.443 171.170 1.00 49.86  ? 382  MET   A O     1 
ATOM   980   C  CB    . MET   A 1 382  ? 124.792 146.288 169.327 1.00 42.49  ? 382  MET   A CB    1 
ATOM   981   C  CG    . MET   A 1 382  ? 126.088 145.499 169.292 1.00 49.08  ? 382  MET   A CG    1 
ATOM   982   S  SD    . MET   A 1 382  ? 127.542 146.562 169.315 1.00 73.70  ? 382  MET   A SD    1 
ATOM   983   C  CE    . MET   A 1 382  ? 128.840 145.342 169.491 1.00 55.25  ? 382  MET   A CE    1 
ATOM   984   N  N     . TYR   A 1 383  ? 121.714 146.942 169.001 1.00 41.99  ? 383  TYR   A N     1 
ATOM   985   C  CA    . TYR   A 1 383  ? 120.557 147.779 169.304 1.00 35.79  ? 383  TYR   A CA    1 
ATOM   986   C  C     . TYR   A 1 383  ? 119.404 146.947 169.855 1.00 37.19  ? 383  TYR   A C     1 
ATOM   987   O  O     . TYR   A 1 383  ? 118.698 147.381 170.775 1.00 40.18  ? 383  TYR   A O     1 
ATOM   988   C  CB    . TYR   A 1 383  ? 120.124 148.551 168.058 1.00 43.54  ? 383  TYR   A CB    1 
ATOM   989   C  CG    . TYR   A 1 383  ? 121.069 149.668 167.674 1.00 44.58  ? 383  TYR   A CG    1 
ATOM   990   C  CD1   . TYR   A 1 383  ? 121.240 150.772 168.497 1.00 44.18  ? 383  TYR   A CD1   1 
ATOM   991   C  CD2   . TYR   A 1 383  ? 121.788 149.620 166.488 1.00 41.69  ? 383  TYR   A CD2   1 
ATOM   992   C  CE1   . TYR   A 1 383  ? 122.104 151.793 168.150 1.00 46.27  ? 383  TYR   A CE1   1 
ATOM   993   C  CE2   . TYR   A 1 383  ? 122.654 150.633 166.134 1.00 44.45  ? 383  TYR   A CE2   1 
ATOM   994   C  CZ    . TYR   A 1 383  ? 122.808 151.718 166.968 1.00 45.03  ? 383  TYR   A CZ    1 
ATOM   995   O  OH    . TYR   A 1 383  ? 123.668 152.732 166.618 1.00 48.51  ? 383  TYR   A OH    1 
ATOM   996   N  N     . VAL   A 1 384  ? 119.195 145.748 169.307 1.00 48.39  ? 384  VAL   A N     1 
ATOM   997   C  CA    . VAL   A 1 384  ? 118.149 144.879 169.839 1.00 49.41  ? 384  VAL   A CA    1 
ATOM   998   C  C     . VAL   A 1 384  ? 118.465 144.489 171.277 1.00 45.19  ? 384  VAL   A C     1 
ATOM   999   O  O     . VAL   A 1 384  ? 117.570 144.398 172.126 1.00 47.56  ? 384  VAL   A O     1 
ATOM   1000  C  CB    . VAL   A 1 384  ? 117.968 143.642 168.941 1.00 49.38  ? 384  VAL   A CB    1 
ATOM   1001  C  CG1   . VAL   A 1 384  ? 117.333 142.511 169.727 1.00 49.78  ? 384  VAL   A CG1   1 
ATOM   1002  C  CG2   . VAL   A 1 384  ? 117.129 143.990 167.722 1.00 46.41  ? 384  VAL   A CG2   1 
ATOM   1003  N  N     . VAL   A 1 385  ? 119.744 144.250 171.574 1.00 46.98  ? 385  VAL   A N     1 
ATOM   1004  C  CA    . VAL   A 1 385  ? 120.146 143.922 172.939 1.00 42.96  ? 385  VAL   A CA    1 
ATOM   1005  C  C     . VAL   A 1 385  ? 119.881 145.098 173.868 1.00 44.48  ? 385  VAL   A C     1 
ATOM   1006  O  O     . VAL   A 1 385  ? 119.447 144.919 175.010 1.00 55.19  ? 385  VAL   A O     1 
ATOM   1007  C  CB    . VAL   A 1 385  ? 121.625 143.495 172.977 1.00 47.40  ? 385  VAL   A CB    1 
ATOM   1008  C  CG1   . VAL   A 1 385  ? 122.232 143.814 174.332 1.00 45.51  ? 385  VAL   A CG1   1 
ATOM   1009  C  CG2   . VAL   A 1 385  ? 121.753 142.013 172.672 1.00 49.06  ? 385  VAL   A CG2   1 
ATOM   1010  N  N     . GLY   A 1 386  ? 120.156 146.317 173.403 1.00 43.18  ? 386  GLY   A N     1 
ATOM   1011  C  CA    . GLY   A 1 386  ? 119.842 147.487 174.211 1.00 41.13  ? 386  GLY   A CA    1 
ATOM   1012  C  C     . GLY   A 1 386  ? 118.357 147.613 174.497 1.00 47.41  ? 386  GLY   A C     1 
ATOM   1013  O  O     . GLY   A 1 386  ? 117.951 147.926 175.622 1.00 54.89  ? 386  GLY   A O     1 
ATOM   1014  N  N     . PHE   A 1 387  ? 117.526 147.372 173.481 1.00 48.15  ? 387  PHE   A N     1 
ATOM   1015  C  CA    . PHE   A 1 387  ? 116.079 147.402 173.685 1.00 36.80  ? 387  PHE   A CA    1 
ATOM   1016  C  C     . PHE   A 1 387  ? 115.646 146.349 174.700 1.00 45.95  ? 387  PHE   A C     1 
ATOM   1017  O  O     . PHE   A 1 387  ? 114.826 146.624 175.588 1.00 50.04  ? 387  PHE   A O     1 
ATOM   1018  C  CB    . PHE   A 1 387  ? 115.366 147.191 172.348 1.00 42.86  ? 387  PHE   A CB    1 
ATOM   1019  C  CG    . PHE   A 1 387  ? 113.884 146.979 172.471 1.00 47.69  ? 387  PHE   A CG    1 
ATOM   1020  C  CD1   . PHE   A 1 387  ? 113.020 148.056 172.559 1.00 48.91  ? 387  PHE   A CD1   1 
ATOM   1021  C  CD2   . PHE   A 1 387  ? 113.352 145.700 172.484 1.00 44.65  ? 387  PHE   A CD2   1 
ATOM   1022  C  CE1   . PHE   A 1 387  ? 111.657 147.860 172.664 1.00 43.65  ? 387  PHE   A CE1   1 
ATOM   1023  C  CE2   . PHE   A 1 387  ? 111.991 145.500 172.591 1.00 43.61  ? 387  PHE   A CE2   1 
ATOM   1024  C  CZ    . PHE   A 1 387  ? 111.143 146.581 172.681 1.00 41.95  ? 387  PHE   A CZ    1 
ATOM   1025  N  N     . ALA   A 1 388  ? 116.191 145.137 174.583 1.00 56.22  ? 388  ALA   A N     1 
ATOM   1026  C  CA    . ALA   A 1 388  ? 115.859 144.083 175.534 1.00 50.71  ? 388  ALA   A CA    1 
ATOM   1027  C  C     . ALA   A 1 388  ? 116.299 144.456 176.943 1.00 48.46  ? 388  ALA   A C     1 
ATOM   1028  O  O     . ALA   A 1 388  ? 115.591 144.177 177.914 1.00 54.06  ? 388  ALA   A O     1 
ATOM   1029  C  CB    . ALA   A 1 388  ? 116.494 142.763 175.102 1.00 50.54  ? 388  ALA   A CB    1 
ATOM   1030  N  N     . GLU   A 1 389  ? 117.471 145.080 177.074 1.00 49.16  ? 389  GLU   A N     1 
ATOM   1031  C  CA    . GLU   A 1 389  ? 117.936 145.517 178.386 1.00 49.16  ? 389  GLU   A CA    1 
ATOM   1032  C  C     . GLU   A 1 389  ? 116.992 146.549 178.987 1.00 53.47  ? 389  GLU   A C     1 
ATOM   1033  O  O     . GLU   A 1 389  ? 116.672 146.489 180.180 1.00 57.54  ? 389  GLU   A O     1 
ATOM   1034  C  CB    . GLU   A 1 389  ? 119.349 146.091 178.282 1.00 48.60  ? 389  GLU   A CB    1 
ATOM   1035  C  CG    . GLU   A 1 389  ? 120.399 145.108 177.801 1.00 55.94  ? 389  GLU   A CG    1 
ATOM   1036  C  CD    . GLU   A 1 389  ? 121.762 145.754 177.636 1.00 59.22  ? 389  GLU   A CD    1 
ATOM   1037  O  OE1   . GLU   A 1 389  ? 121.852 146.793 176.949 1.00 58.65  ? 389  GLU   A OE1   1 
ATOM   1038  O  OE2   . GLU   A 1 389  ? 122.743 145.224 178.196 1.00 61.60  ? 389  GLU   A OE2   1 
ATOM   1039  N  N     . THR   A 1 390  ? 116.544 147.511 178.179 1.00 52.50  ? 390  THR   A N     1 
ATOM   1040  C  CA    . THR   A 1 390  ? 115.616 148.514 178.692 1.00 52.85  ? 390  THR   A CA    1 
ATOM   1041  C  C     . THR   A 1 390  ? 114.308 147.873 179.141 1.00 52.50  ? 390  THR   A C     1 
ATOM   1042  O  O     . THR   A 1 390  ? 113.775 148.210 180.206 1.00 56.35  ? 390  THR   A O     1 
ATOM   1043  C  CB    . THR   A 1 390  ? 115.352 149.587 177.636 1.00 55.95  ? 390  THR   A CB    1 
ATOM   1044  O  OG1   . THR   A 1 390  ? 116.455 150.500 177.596 1.00 61.04  ? 390  THR   A OG1   1 
ATOM   1045  C  CG2   . THR   A 1 390  ? 114.088 150.358 177.976 1.00 52.87  ? 390  THR   A CG2   1 
ATOM   1046  N  N     . VAL   A 1 391  ? 113.781 146.936 178.350 1.00 52.23  ? 391  VAL   A N     1 
ATOM   1047  C  CA    . VAL   A 1 391  ? 112.533 146.275 178.729 1.00 53.63  ? 391  VAL   A CA    1 
ATOM   1048  C  C     . VAL   A 1 391  ? 112.725 145.456 180.001 1.00 52.53  ? 391  VAL   A C     1 
ATOM   1049  O  O     . VAL   A 1 391  ? 111.853 145.428 180.881 1.00 57.99  ? 391  VAL   A O     1 
ATOM   1050  C  CB    . VAL   A 1 391  ? 112.009 145.406 177.571 1.00 56.29  ? 391  VAL   A CB    1 
ATOM   1051  C  CG1   . VAL   A 1 391  ? 111.091 144.317 178.104 1.00 55.61  ? 391  VAL   A CG1   1 
ATOM   1052  C  CG2   . VAL   A 1 391  ? 111.281 146.266 176.552 1.00 54.22  ? 391  VAL   A CG2   1 
ATOM   1053  N  N     . VAL   A 1 392  ? 113.864 144.770 180.115 1.00 53.02  ? 392  VAL   A N     1 
ATOM   1054  C  CA    . VAL   A 1 392  ? 114.136 143.963 181.299 1.00 53.27  ? 392  VAL   A CA    1 
ATOM   1055  C  C     . VAL   A 1 392  ? 114.218 144.845 182.535 1.00 55.96  ? 392  VAL   A C     1 
ATOM   1056  O  O     . VAL   A 1 392  ? 113.690 144.498 183.595 1.00 61.54  ? 392  VAL   A O     1 
ATOM   1057  C  CB    . VAL   A 1 392  ? 115.423 143.140 181.104 1.00 55.99  ? 392  VAL   A CB    1 
ATOM   1058  C  CG1   . VAL   A 1 392  ? 116.096 142.885 182.442 1.00 53.48  ? 392  VAL   A CG1   1 
ATOM   1059  C  CG2   . VAL   A 1 392  ? 115.112 141.829 180.399 1.00 57.95  ? 392  VAL   A CG2   1 
ATOM   1060  N  N     . GLU   A 1 393  ? 114.892 145.992 182.426 1.00 58.09  ? 393  GLU   A N     1 
ATOM   1061  C  CA    . GLU   A 1 393  ? 114.957 146.910 183.558 1.00 56.62  ? 393  GLU   A CA    1 
ATOM   1062  C  C     . GLU   A 1 393  ? 113.573 147.430 183.923 1.00 57.02  ? 393  GLU   A C     1 
ATOM   1063  O  O     . GLU   A 1 393  ? 113.226 147.524 185.107 1.00 58.63  ? 393  GLU   A O     1 
ATOM   1064  C  CB    . GLU   A 1 393  ? 115.902 148.069 183.244 1.00 56.85  ? 393  GLU   A CB    1 
ATOM   1065  N  N     . LEU   A 1 394  ? 112.762 147.764 182.916 1.00 59.85  ? 394  LEU   A N     1 
ATOM   1066  C  CA    . LEU   A 1 394  ? 111.416 148.255 183.192 1.00 59.55  ? 394  LEU   A CA    1 
ATOM   1067  C  C     . LEU   A 1 394  ? 110.592 147.217 183.942 1.00 60.56  ? 394  LEU   A C     1 
ATOM   1068  O  O     . LEU   A 1 394  ? 109.878 147.552 184.894 1.00 64.98  ? 394  LEU   A O     1 
ATOM   1069  C  CB    . LEU   A 1 394  ? 110.723 148.648 181.887 1.00 63.16  ? 394  LEU   A CB    1 
ATOM   1070  C  CG    . LEU   A 1 394  ? 109.557 149.632 181.998 1.00 61.74  ? 394  LEU   A CG    1 
ATOM   1071  C  CD1   . LEU   A 1 394  ? 108.311 148.929 182.507 1.00 61.42  ? 394  LEU   A CD1   1 
ATOM   1072  C  CD2   . LEU   A 1 394  ? 109.923 150.796 182.900 1.00 64.31  ? 394  LEU   A CD2   1 
ATOM   1073  N  N     . LEU   A 1 395  ? 110.674 145.950 183.528 1.00 65.84  ? 395  LEU   A N     1 
ATOM   1074  C  CA    . LEU   A 1 395  ? 109.887 144.922 184.204 1.00 64.20  ? 395  LEU   A CA    1 
ATOM   1075  C  C     . LEU   A 1 395  ? 110.472 144.561 185.565 1.00 67.46  ? 395  LEU   A C     1 
ATOM   1076  O  O     . LEU   A 1 395  ? 109.723 144.203 186.481 1.00 72.37  ? 395  LEU   A O     1 
ATOM   1077  C  CB    . LEU   A 1 395  ? 109.766 143.675 183.329 1.00 59.81  ? 395  LEU   A CB    1 
ATOM   1078  C  CG    . LEU   A 1 395  ? 111.043 143.058 182.762 1.00 66.33  ? 395  LEU   A CG    1 
ATOM   1079  C  CD1   . LEU   A 1 395  ? 111.698 142.150 183.787 1.00 67.86  ? 395  LEU   A CD1   1 
ATOM   1080  C  CD2   . LEU   A 1 395  ? 110.728 142.288 181.493 1.00 65.38  ? 395  LEU   A CD2   1 
ATOM   1081  N  N     . LYS   A 1 396  ? 111.796 144.638 185.718 1.00 65.40  ? 396  LYS   A N     1 
ATOM   1082  C  CA    . LYS   A 1 396  ? 112.413 144.353 187.008 1.00 65.11  ? 396  LYS   A CA    1 
ATOM   1083  C  C     . LYS   A 1 396  ? 112.096 145.435 188.028 1.00 67.57  ? 396  LYS   A C     1 
ATOM   1084  O  O     . LYS   A 1 396  ? 112.020 145.149 189.228 1.00 69.93  ? 396  LYS   A O     1 
ATOM   1085  C  CB    . LYS   A 1 396  ? 113.925 144.199 186.847 1.00 63.42  ? 396  LYS   A CB    1 
ATOM   1086  N  N     . GLU   A 1 397  ? 111.908 146.678 187.578 1.00 70.98  ? 397  GLU   A N     1 
ATOM   1087  C  CA    . GLU   A 1 397  ? 111.433 147.713 188.487 1.00 71.07  ? 397  GLU   A CA    1 
ATOM   1088  C  C     . GLU   A 1 397  ? 110.081 147.350 189.081 1.00 70.79  ? 397  GLU   A C     1 
ATOM   1089  O  O     . GLU   A 1 397  ? 109.711 147.883 190.133 1.00 71.89  ? 397  GLU   A O     1 
ATOM   1090  C  CB    . GLU   A 1 397  ? 111.346 149.058 187.765 1.00 72.93  ? 397  GLU   A CB    1 
ATOM   1091  N  N     . HIS   A 1 398  ? 109.342 146.459 188.430 1.00 71.18  ? 398  HIS   A N     1 
ATOM   1092  C  CA    . HIS   A 1 398  ? 108.128 145.862 188.954 1.00 70.93  ? 398  HIS   A CA    1 
ATOM   1093  C  C     . HIS   A 1 398  ? 108.400 144.391 189.263 1.00 73.58  ? 398  HIS   A C     1 
ATOM   1094  O  O     . HIS   A 1 398  ? 109.535 143.911 189.153 1.00 74.01  ? 398  HIS   A O     1 
ATOM   1095  C  CB    . HIS   A 1 398  ? 106.977 146.049 187.963 1.00 69.45  ? 398  HIS   A CB    1 
ATOM   1096  C  CG    . HIS   A 1 398  ? 106.622 147.482 187.717 1.00 72.82  ? 398  HIS   A CG    1 
ATOM   1097  N  ND1   . HIS   A 1 398  ? 106.242 148.339 188.727 1.00 78.17  ? 398  HIS   A ND1   1 
ATOM   1098  C  CD2   . HIS   A 1 398  ? 106.585 148.209 186.575 1.00 72.95  ? 398  HIS   A CD2   1 
ATOM   1099  C  CE1   . HIS   A 1 398  ? 105.991 149.532 188.220 1.00 74.12  ? 398  HIS   A CE1   1 
ATOM   1100  N  NE2   . HIS   A 1 398  ? 106.191 149.480 186.915 1.00 72.14  ? 398  HIS   A NE2   1 
ATOM   1101  N  N     . SER   A 1 399  ? 107.353 143.667 189.656 1.00 84.53  ? 399  SER   A N     1 
ATOM   1102  C  CA    . SER   A 1 399  ? 107.522 142.289 190.100 1.00 86.14  ? 399  SER   A CA    1 
ATOM   1103  C  C     . SER   A 1 399  ? 107.611 141.289 188.952 1.00 84.00  ? 399  SER   A C     1 
ATOM   1104  O  O     . SER   A 1 399  ? 108.025 140.147 189.179 1.00 82.52  ? 399  SER   A O     1 
ATOM   1105  C  CB    . SER   A 1 399  ? 106.371 141.896 191.029 1.00 88.21  ? 399  SER   A CB    1 
ATOM   1106  O  OG    . SER   A 1 399  ? 105.117 142.183 190.435 1.00 89.75  ? 399  SER   A OG    1 
ATOM   1107  N  N     . ILE   A 1 400  ? 107.242 141.685 187.734 1.00 76.14  ? 400  ILE   A N     1 
ATOM   1108  C  CA    . ILE   A 1 400  ? 107.165 140.735 186.631 1.00 75.52  ? 400  ILE   A CA    1 
ATOM   1109  C  C     . ILE   A 1 400  ? 108.560 140.265 186.239 1.00 79.17  ? 400  ILE   A C     1 
ATOM   1110  O  O     . ILE   A 1 400  ? 109.516 141.052 186.194 1.00 81.27  ? 400  ILE   A O     1 
ATOM   1111  C  CB    . ILE   A 1 400  ? 106.436 141.363 185.431 1.00 73.63  ? 400  ILE   A CB    1 
ATOM   1112  N  N     . LEU   A 1 401  ? 108.680 138.969 185.954 1.00 84.47  ? 401  LEU   A N     1 
ATOM   1113  C  CA    . LEU   A 1 401  ? 109.914 138.373 185.462 1.00 85.26  ? 401  LEU   A CA    1 
ATOM   1114  C  C     . LEU   A 1 401  ? 109.633 136.925 185.089 1.00 86.28  ? 401  LEU   A C     1 
ATOM   1115  O  O     . LEU   A 1 401  ? 108.796 136.274 185.718 1.00 87.39  ? 401  LEU   A O     1 
ATOM   1116  C  CB    . LEU   A 1 401  ? 111.033 138.448 186.509 1.00 81.94  ? 401  LEU   A CB    1 
ATOM   1117  N  N     . MET   A 1 402  ? 110.334 136.431 184.070 1.00 79.32  ? 402  MET   A N     1 
ATOM   1118  C  CA    . MET   A 1 402  ? 110.145 135.075 183.569 1.00 75.75  ? 402  MET   A CA    1 
ATOM   1119  C  C     . MET   A 1 402  ? 111.300 134.148 183.913 1.00 77.76  ? 402  MET   A C     1 
ATOM   1120  O  O     . MET   A 1 402  ? 111.082 133.058 184.450 1.00 82.37  ? 402  MET   A O     1 
ATOM   1121  C  CB    . MET   A 1 402  ? 109.940 135.104 182.047 1.00 72.58  ? 402  MET   A CB    1 
ATOM   1122  N  N     . ILE   A 1 403  ? 112.530 134.552 183.608 1.00 70.74  ? 403  ILE   A N     1 
ATOM   1123  C  CA    . ILE   A 1 403  ? 113.727 133.765 183.861 1.00 70.18  ? 403  ILE   A CA    1 
ATOM   1124  C  C     . ILE   A 1 403  ? 114.848 134.718 184.263 1.00 72.15  ? 403  ILE   A C     1 
ATOM   1125  O  O     . ILE   A 1 403  ? 114.656 135.933 184.347 1.00 75.92  ? 403  ILE   A O     1 
ATOM   1126  C  CB    . ILE   A 1 403  ? 114.141 132.917 182.641 1.00 65.15  ? 403  ILE   A CB    1 
ATOM   1127  N  N     . ASP   A 1 404  ? 116.024 134.152 184.534 1.00 68.23  ? 404  ASP   A N     1 
ATOM   1128  C  CA    . ASP   A 1 404  ? 117.189 134.965 184.852 1.00 68.73  ? 404  ASP   A CA    1 
ATOM   1129  C  C     . ASP   A 1 404  ? 117.330 136.100 183.846 1.00 73.35  ? 404  ASP   A C     1 
ATOM   1130  O  O     . ASP   A 1 404  ? 116.966 135.968 182.674 1.00 77.40  ? 404  ASP   A O     1 
ATOM   1131  C  CB    . ASP   A 1 404  ? 118.455 134.106 184.861 1.00 67.31  ? 404  ASP   A CB    1 
ATOM   1132  N  N     . GLU   A 1 405  ? 117.870 137.227 184.317 1.00 71.23  ? 405  GLU   A N     1 
ATOM   1133  C  CA    . GLU   A 1 405  ? 117.888 138.442 183.508 1.00 70.46  ? 405  GLU   A CA    1 
ATOM   1134  C  C     . GLU   A 1 405  ? 118.473 138.190 182.124 1.00 71.44  ? 405  GLU   A C     1 
ATOM   1135  O  O     . GLU   A 1 405  ? 117.962 138.703 181.122 1.00 71.61  ? 405  GLU   A O     1 
ATOM   1136  C  CB    . GLU   A 1 405  ? 118.674 139.538 184.230 1.00 62.36  ? 405  GLU   A CB    1 
ATOM   1137  N  N     . ILE   A 1 406  ? 119.542 137.396 182.045 1.00 67.77  ? 406  ILE   A N     1 
ATOM   1138  C  CA    . ILE   A 1 406  ? 120.178 137.134 180.756 1.00 68.58  ? 406  ILE   A CA    1 
ATOM   1139  C  C     . ILE   A 1 406  ? 119.214 136.412 179.820 1.00 73.39  ? 406  ILE   A C     1 
ATOM   1140  O  O     . ILE   A 1 406  ? 119.094 136.753 178.637 1.00 79.54  ? 406  ILE   A O     1 
ATOM   1141  C  CB    . ILE   A 1 406  ? 121.480 136.336 180.952 1.00 65.10  ? 406  ILE   A CB    1 
ATOM   1142  N  N     . ASN   A 1 407  ? 118.518 135.395 180.334 1.00 67.15  ? 407  ASN   A N     1 
ATOM   1143  C  CA    . ASN   A 1 407  ? 117.613 134.625 179.486 1.00 67.47  ? 407  ASN   A CA    1 
ATOM   1144  C  C     . ASN   A 1 407  ? 116.422 135.463 179.036 1.00 65.55  ? 407  ASN   A C     1 
ATOM   1145  O  O     . ASN   A 1 407  ? 115.978 135.355 177.886 1.00 73.05  ? 407  ASN   A O     1 
ATOM   1146  C  CB    . ASN   A 1 407  ? 117.148 133.371 180.222 1.00 69.68  ? 407  ASN   A CB    1 
ATOM   1147  C  CG    . ASN   A 1 407  ? 118.299 132.596 180.830 1.00 71.81  ? 407  ASN   A CG    1 
ATOM   1148  O  OD1   . ASN   A 1 407  ? 119.413 132.607 180.307 1.00 67.95  ? 407  ASN   A OD1   1 
ATOM   1149  N  ND2   . ASN   A 1 407  ? 118.034 131.914 181.938 1.00 72.78  ? 407  ASN   A ND2   1 
ATOM   1150  N  N     . ASP   A 1 408  ? 115.887 136.299 179.927 1.00 56.22  ? 408  ASP   A N     1 
ATOM   1151  C  CA    . ASP   A 1 408  ? 114.815 137.202 179.526 1.00 58.20  ? 408  ASP   A CA    1 
ATOM   1152  C  C     . ASP   A 1 408  ? 115.295 138.169 178.453 1.00 62.41  ? 408  ASP   A C     1 
ATOM   1153  O  O     . ASP   A 1 408  ? 114.574 138.447 177.485 1.00 66.57  ? 408  ASP   A O     1 
ATOM   1154  C  CB    . ASP   A 1 408  ? 114.288 137.963 180.742 1.00 61.63  ? 408  ASP   A CB    1 
ATOM   1155  N  N     . ILE   A 1 409  ? 116.513 138.690 178.608 1.00 59.49  ? 409  ILE   A N     1 
ATOM   1156  C  CA    . ILE   A 1 409  ? 117.084 139.567 177.591 1.00 57.26  ? 409  ILE   A CA    1 
ATOM   1157  C  C     . ILE   A 1 409  ? 117.146 138.843 176.255 1.00 59.32  ? 409  ILE   A C     1 
ATOM   1158  O  O     . ILE   A 1 409  ? 116.778 139.392 175.212 1.00 64.43  ? 409  ILE   A O     1 
ATOM   1159  C  CB    . ILE   A 1 409  ? 118.476 140.058 178.026 1.00 55.40  ? 409  ILE   A CB    1 
ATOM   1160  C  CG1   . ILE   A 1 409  ? 118.358 141.310 178.895 1.00 62.89  ? 409  ILE   A CG1   1 
ATOM   1161  C  CG2   . ILE   A 1 409  ? 119.346 140.333 176.809 1.00 53.88  ? 409  ILE   A CG2   1 
ATOM   1162  C  CD1   . ILE   A 1 409  ? 119.691 141.848 179.362 1.00 61.09  ? 409  ILE   A CD1   1 
ATOM   1163  N  N     . ARG   A 1 410  ? 117.617 137.595 176.270 1.00 57.01  ? 410  ARG   A N     1 
ATOM   1164  C  CA    . ARG   A 1 410  ? 117.727 136.833 175.031 1.00 53.75  ? 410  ARG   A CA    1 
ATOM   1165  C  C     . ARG   A 1 410  ? 116.364 136.622 174.386 1.00 55.27  ? 410  ARG   A C     1 
ATOM   1166  O  O     . ARG   A 1 410  ? 116.216 136.768 173.167 1.00 64.21  ? 410  ARG   A O     1 
ATOM   1167  C  CB    . ARG   A 1 410  ? 118.403 135.490 175.301 1.00 50.50  ? 410  ARG   A CB    1 
ATOM   1168  C  CG    . ARG   A 1 410  ? 119.834 135.606 175.786 1.00 53.22  ? 410  ARG   A CG    1 
ATOM   1169  C  CD    . ARG   A 1 410  ? 120.441 134.238 176.025 1.00 56.84  ? 410  ARG   A CD    1 
ATOM   1170  N  NE    . ARG   A 1 410  ? 121.495 134.285 177.030 1.00 58.49  ? 410  ARG   A NE    1 
ATOM   1171  C  CZ    . ARG   A 1 410  ? 122.632 133.608 176.955 1.00 59.69  ? 410  ARG   A CZ    1 
ATOM   1172  N  NH1   . ARG   A 1 410  ? 122.896 132.812 175.932 1.00 56.74  ? 410  ARG   A NH1   1 
ATOM   1173  N  NH2   . ARG   A 1 410  ? 123.527 133.733 177.930 1.00 58.19  ? 410  ARG   A NH2   1 
ATOM   1174  N  N     . ILE   A 1 411  ? 115.353 136.280 175.187 1.00 53.50  ? 411  ILE   A N     1 
ATOM   1175  C  CA    . ILE   A 1 411  ? 114.023 136.021 174.636 1.00 55.04  ? 411  ILE   A CA    1 
ATOM   1176  C  C     . ILE   A 1 411  ? 113.449 137.287 174.011 1.00 57.36  ? 411  ILE   A C     1 
ATOM   1177  O  O     . ILE   A 1 411  ? 112.945 137.275 172.876 1.00 57.86  ? 411  ILE   A O     1 
ATOM   1178  C  CB    . ILE   A 1 411  ? 113.092 135.458 175.725 1.00 55.82  ? 411  ILE   A CB    1 
ATOM   1179  C  CG1   . ILE   A 1 411  ? 113.514 134.039 176.109 1.00 58.51  ? 411  ILE   A CG1   1 
ATOM   1180  C  CG2   . ILE   A 1 411  ? 111.649 135.478 175.255 1.00 55.82  ? 411  ILE   A CG2   1 
ATOM   1181  C  CD1   . ILE   A 1 411  ? 112.861 133.531 177.374 1.00 56.93  ? 411  ILE   A CD1   1 
ATOM   1182  N  N     . ILE   A 1 412  ? 113.510 138.401 174.745 1.00 57.49  ? 412  ILE   A N     1 
ATOM   1183  C  CA    . ILE   A 1 412  ? 112.965 139.650 174.223 1.00 57.42  ? 412  ILE   A CA    1 
ATOM   1184  C  C     . ILE   A 1 412  ? 113.721 140.076 172.972 1.00 61.53  ? 412  ILE   A C     1 
ATOM   1185  O  O     . ILE   A 1 412  ? 113.121 140.545 171.998 1.00 64.09  ? 412  ILE   A O     1 
ATOM   1186  C  CB    . ILE   A 1 412  ? 112.984 140.750 175.301 1.00 59.75  ? 412  ILE   A CB    1 
ATOM   1187  C  CG1   . ILE   A 1 412  ? 111.950 140.460 176.393 1.00 60.18  ? 412  ILE   A CG1   1 
ATOM   1188  C  CG2   . ILE   A 1 412  ? 112.713 142.107 174.676 1.00 57.92  ? 412  ILE   A CG2   1 
ATOM   1189  C  CD1   . ILE   A 1 412  ? 112.539 140.284 177.775 1.00 58.30  ? 412  ILE   A CD1   1 
ATOM   1190  N  N     . GLY   A 1 413  ? 115.047 139.926 172.977 1.00 55.29  ? 413  GLY   A N     1 
ATOM   1191  C  CA    . GLY   A 1 413  ? 115.824 140.279 171.802 1.00 53.54  ? 413  GLY   A CA    1 
ATOM   1192  C  C     . GLY   A 1 413  ? 115.471 139.436 170.594 1.00 58.28  ? 413  GLY   A C     1 
ATOM   1193  O  O     . GLY   A 1 413  ? 115.391 139.945 169.475 1.00 65.32  ? 413  GLY   A O     1 
ATOM   1194  N  N     . ALA   A 1 414  ? 115.263 138.134 170.798 1.00 57.84  ? 414  ALA   A N     1 
ATOM   1195  C  CA    . ALA   A 1 414  ? 114.883 137.271 169.685 1.00 60.10  ? 414  ALA   A CA    1 
ATOM   1196  C  C     . ALA   A 1 414  ? 113.532 137.676 169.112 1.00 57.79  ? 414  ALA   A C     1 
ATOM   1197  O  O     . ALA   A 1 414  ? 113.366 137.759 167.887 1.00 62.36  ? 414  ALA   A O     1 
ATOM   1198  C  CB    . ALA   A 1 414  ? 114.863 135.811 170.134 1.00 60.63  ? 414  ALA   A CB    1 
ATOM   1199  N  N     . ILE   A 1 415  ? 112.552 137.940 169.979 1.00 52.69  ? 415  ILE   A N     1 
ATOM   1200  C  CA    . ILE   A 1 415  ? 111.242 138.360 169.483 1.00 53.71  ? 415  ILE   A CA    1 
ATOM   1201  C  C     . ILE   A 1 415  ? 111.359 139.679 168.727 1.00 58.42  ? 415  ILE   A C     1 
ATOM   1202  O  O     . ILE   A 1 415  ? 110.768 139.856 167.652 1.00 63.21  ? 415  ILE   A O     1 
ATOM   1203  C  CB    . ILE   A 1 415  ? 110.230 138.457 170.639 1.00 56.47  ? 415  ILE   A CB    1 
ATOM   1204  C  CG1   . ILE   A 1 415  ? 110.026 137.088 171.289 1.00 56.83  ? 415  ILE   A CG1   1 
ATOM   1205  C  CG2   . ILE   A 1 415  ? 108.903 139.006 170.136 1.00 54.22  ? 415  ILE   A CG2   1 
ATOM   1206  C  CD1   . ILE   A 1 415  ? 110.076 135.935 170.314 1.00 56.73  ? 415  ILE   A CD1   1 
ATOM   1207  N  N     . THR   A 1 416  ? 112.125 140.626 169.277 1.00 58.21  ? 416  THR   A N     1 
ATOM   1208  C  CA    . THR   A 1 416  ? 112.304 141.915 168.620 1.00 56.35  ? 416  THR   A CA    1 
ATOM   1209  C  C     . THR   A 1 416  ? 112.961 141.754 167.256 1.00 52.28  ? 416  THR   A C     1 
ATOM   1210  O  O     . THR   A 1 416  ? 112.563 142.408 166.287 1.00 53.13  ? 416  THR   A O     1 
ATOM   1211  C  CB    . THR   A 1 416  ? 113.134 142.846 169.503 1.00 58.46  ? 416  THR   A CB    1 
ATOM   1212  O  OG1   . THR   A 1 416  ? 112.780 142.648 170.877 1.00 59.15  ? 416  THR   A OG1   1 
ATOM   1213  C  CG2   . THR   A 1 416  ? 112.888 144.298 169.127 1.00 58.04  ? 416  THR   A CG2   1 
ATOM   1214  N  N     . VAL   A 1 417  ? 113.979 140.896 167.162 1.00 52.85  ? 417  VAL   A N     1 
ATOM   1215  C  CA    . VAL   A 1 417  ? 114.670 140.704 165.892 1.00 54.51  ? 417  VAL   A CA    1 
ATOM   1216  C  C     . VAL   A 1 417  ? 113.744 140.055 164.873 1.00 58.73  ? 417  VAL   A C     1 
ATOM   1217  O  O     . VAL   A 1 417  ? 113.765 140.405 163.688 1.00 62.28  ? 417  VAL   A O     1 
ATOM   1218  C  CB    . VAL   A 1 417  ? 115.959 139.886 166.098 1.00 49.43  ? 417  VAL   A CB    1 
ATOM   1219  C  CG1   . VAL   A 1 417  ? 115.655 138.400 166.129 1.00 52.07  ? 417  VAL   A CG1   1 
ATOM   1220  C  CG2   . VAL   A 1 417  ? 116.966 140.200 165.003 1.00 52.90  ? 417  VAL   A CG2   1 
ATOM   1221  N  N     . VAL   A 1 418  ? 112.913 139.105 165.309 1.00 53.33  ? 418  VAL   A N     1 
ATOM   1222  C  CA    . VAL   A 1 418  ? 111.959 138.487 164.390 1.00 48.62  ? 418  VAL   A CA    1 
ATOM   1223  C  C     . VAL   A 1 418  ? 110.990 139.535 163.855 1.00 49.32  ? 418  VAL   A C     1 
ATOM   1224  O  O     . VAL   A 1 418  ? 110.710 139.597 162.649 1.00 54.78  ? 418  VAL   A O     1 
ATOM   1225  C  CB    . VAL   A 1 418  ? 111.215 137.331 165.082 1.00 50.44  ? 418  VAL   A CB    1 
ATOM   1226  C  CG1   . VAL   A 1 418  ? 109.911 137.036 164.360 1.00 47.42  ? 418  VAL   A CG1   1 
ATOM   1227  C  CG2   . VAL   A 1 418  ? 112.093 136.091 165.136 1.00 51.00  ? 418  VAL   A CG2   1 
ATOM   1228  N  N     . ILE   A 1 419  ? 110.467 140.380 164.746 1.00 52.49  ? 419  ILE   A N     1 
ATOM   1229  C  CA    . ILE   A 1 419  ? 109.523 141.410 164.316 1.00 52.22  ? 419  ILE   A CA    1 
ATOM   1230  C  C     . ILE   A 1 419  ? 110.197 142.386 163.359 1.00 51.85  ? 419  ILE   A C     1 
ATOM   1231  O  O     . ILE   A 1 419  ? 109.607 142.803 162.354 1.00 54.63  ? 419  ILE   A O     1 
ATOM   1232  C  CB    . ILE   A 1 419  ? 108.925 142.134 165.535 1.00 55.51  ? 419  ILE   A CB    1 
ATOM   1233  C  CG1   . ILE   A 1 419  ? 107.993 141.196 166.304 1.00 53.82  ? 419  ILE   A CG1   1 
ATOM   1234  C  CG2   . ILE   A 1 419  ? 108.180 143.386 165.098 1.00 52.74  ? 419  ILE   A CG2   1 
ATOM   1235  C  CD1   . ILE   A 1 419  ? 107.295 140.180 165.431 1.00 53.30  ? 419  ILE   A CD1   1 
ATOM   1236  N  N     . LEU   A 1 420  ? 111.436 142.778 163.663 1.00 54.04  ? 420  LEU   A N     1 
ATOM   1237  C  CA    . LEU   A 1 420  ? 112.150 143.713 162.802 1.00 53.01  ? 420  LEU   A CA    1 
ATOM   1238  C  C     . LEU   A 1 420  ? 112.405 143.111 161.427 1.00 54.20  ? 420  LEU   A C     1 
ATOM   1239  O  O     . LEU   A 1 420  ? 112.276 143.798 160.408 1.00 59.51  ? 420  LEU   A O     1 
ATOM   1240  C  CB    . LEU   A 1 420  ? 113.465 144.130 163.458 1.00 51.70  ? 420  LEU   A CB    1 
ATOM   1241  C  CG    . LEU   A 1 420  ? 113.338 144.996 164.712 1.00 51.37  ? 420  LEU   A CG    1 
ATOM   1242  C  CD1   . LEU   A 1 420  ? 114.657 145.678 165.032 1.00 52.15  ? 420  LEU   A CD1   1 
ATOM   1243  C  CD2   . LEU   A 1 420  ? 112.231 146.021 164.537 1.00 49.18  ? 420  LEU   A CD2   1 
ATOM   1244  N  N     . LEU   A 1 421  ? 112.781 141.832 161.379 1.00 50.81  ? 421  LEU   A N     1 
ATOM   1245  C  CA    . LEU   A 1 421  ? 112.980 141.174 160.094 1.00 51.25  ? 421  LEU   A CA    1 
ATOM   1246  C  C     . LEU   A 1 421  ? 111.684 141.135 159.297 1.00 51.39  ? 421  LEU   A C     1 
ATOM   1247  O  O     . LEU   A 1 421  ? 111.684 141.377 158.084 1.00 56.37  ? 421  LEU   A O     1 
ATOM   1248  C  CB    . LEU   A 1 421  ? 113.523 139.761 160.302 1.00 51.65  ? 421  LEU   A CB    1 
ATOM   1249  C  CG    . LEU   A 1 421  ? 113.244 138.776 159.165 1.00 50.29  ? 421  LEU   A CG    1 
ATOM   1250  C  CD1   . LEU   A 1 421  ? 113.816 139.295 157.854 1.00 52.15  ? 421  LEU   A CD1   1 
ATOM   1251  C  CD2   . LEU   A 1 421  ? 113.798 137.399 159.491 1.00 50.60  ? 421  LEU   A CD2   1 
ATOM   1252  N  N     . GLY   A 1 422  ? 110.569 140.826 159.960 1.00 50.96  ? 422  GLY   A N     1 
ATOM   1253  C  CA    . GLY   A 1 422  ? 109.290 140.856 159.268 1.00 52.46  ? 422  GLY   A CA    1 
ATOM   1254  C  C     . GLY   A 1 422  ? 108.982 142.226 158.695 1.00 51.59  ? 422  GLY   A C     1 
ATOM   1255  O  O     . GLY   A 1 422  ? 108.589 142.358 157.532 1.00 52.70  ? 422  GLY   A O     1 
ATOM   1256  N  N     . ILE   A 1 423  ? 109.171 143.270 159.504 1.00 52.00  ? 423  ILE   A N     1 
ATOM   1257  C  CA    . ILE   A 1 423  ? 108.890 144.626 159.041 1.00 48.77  ? 423  ILE   A CA    1 
ATOM   1258  C  C     . ILE   A 1 423  ? 109.769 144.975 157.848 1.00 50.74  ? 423  ILE   A C     1 
ATOM   1259  O  O     . ILE   A 1 423  ? 109.300 145.546 156.856 1.00 48.85  ? 423  ILE   A O     1 
ATOM   1260  C  CB    . ILE   A 1 423  ? 109.074 145.635 160.189 1.00 47.38  ? 423  ILE   A CB    1 
ATOM   1261  C  CG1   . ILE   A 1 423  ? 107.965 145.471 161.229 1.00 54.67  ? 423  ILE   A CG1   1 
ATOM   1262  C  CG2   . ILE   A 1 423  ? 109.088 147.054 159.648 1.00 44.67  ? 423  ILE   A CG2   1 
ATOM   1263  C  CD1   . ILE   A 1 423  ? 108.357 145.938 162.612 1.00 49.25  ? 423  ILE   A CD1   1 
ATOM   1264  N  N     . SER   A 1 424  ? 111.060 144.644 157.926 1.00 50.43  ? 424  SER   A N     1 
ATOM   1265  C  CA    . SER   A 1 424  ? 111.972 144.967 156.835 1.00 47.16  ? 424  SER   A CA    1 
ATOM   1266  C  C     . SER   A 1 424  ? 111.585 144.236 155.558 1.00 52.55  ? 424  SER   A C     1 
ATOM   1267  O  O     . SER   A 1 424  ? 111.582 144.827 154.472 1.00 53.96  ? 424  SER   A O     1 
ATOM   1268  C  CB    . SER   A 1 424  ? 113.407 144.627 157.233 1.00 54.89  ? 424  SER   A CB    1 
ATOM   1269  O  OG    . SER   A 1 424  ? 113.713 143.280 156.921 1.00 66.31  ? 424  SER   A OG    1 
ATOM   1270  N  N     . VAL   A 1 425  ? 111.254 142.946 155.664 1.00 52.96  ? 425  VAL   A N     1 
ATOM   1271  C  CA    . VAL   A 1 425  ? 110.849 142.189 154.484 1.00 47.01  ? 425  VAL   A CA    1 
ATOM   1272  C  C     . VAL   A 1 425  ? 109.531 142.715 153.933 1.00 48.06  ? 425  VAL   A C     1 
ATOM   1273  O  O     . VAL   A 1 425  ? 109.242 142.560 152.740 1.00 46.07  ? 425  VAL   A O     1 
ATOM   1274  C  CB    . VAL   A 1 425  ? 110.766 140.686 154.815 1.00 47.89  ? 425  VAL   A CB    1 
ATOM   1275  C  CG1   . VAL   A 1 425  ? 109.729 140.004 153.940 1.00 49.77  ? 425  VAL   A CG1   1 
ATOM   1276  C  CG2   . VAL   A 1 425  ? 112.126 140.031 154.641 1.00 49.35  ? 425  VAL   A CG2   1 
ATOM   1277  N  N     . ALA   A 1 426  ? 108.714 143.344 154.781 1.00 54.76  ? 426  ALA   A N     1 
ATOM   1278  C  CA    . ALA   A 1 426  ? 107.431 143.863 154.317 1.00 50.49  ? 426  ALA   A CA    1 
ATOM   1279  C  C     . ALA   A 1 426  ? 107.596 144.810 153.136 1.00 53.04  ? 426  ALA   A C     1 
ATOM   1280  O  O     . ALA   A 1 426  ? 106.739 144.844 152.245 1.00 61.27  ? 426  ALA   A O     1 
ATOM   1281  C  CB    . ALA   A 1 426  ? 106.706 144.570 155.461 1.00 55.01  ? 426  ALA   A CB    1 
ATOM   1282  N  N     . GLY   A 1 427  ? 108.671 145.576 153.106 1.00 53.11  ? 427  GLY   A N     1 
ATOM   1283  C  CA    . GLY   A 1 427  ? 108.910 146.497 152.013 1.00 53.02  ? 427  GLY   A CA    1 
ATOM   1284  C  C     . GLY   A 1 427  ? 109.625 147.738 152.504 1.00 56.40  ? 427  GLY   A C     1 
ATOM   1285  O  O     . GLY   A 1 427  ? 109.833 147.938 153.697 1.00 62.50  ? 427  GLY   A O     1 
ATOM   1286  N  N     . MET   A 1 428  ? 110.002 148.576 151.539 1.00 51.94  ? 428  MET   A N     1 
ATOM   1287  C  CA    . MET   A 1 428  ? 110.737 149.801 151.818 1.00 50.96  ? 428  MET   A CA    1 
ATOM   1288  C  C     . MET   A 1 428  ? 109.842 150.963 152.231 1.00 52.45  ? 428  MET   A C     1 
ATOM   1289  O  O     . MET   A 1 428  ? 110.355 151.964 152.740 1.00 59.29  ? 428  MET   A O     1 
ATOM   1290  C  CB    . MET   A 1 428  ? 111.564 150.208 150.594 1.00 52.02  ? 428  MET   A CB    1 
ATOM   1291  C  CG    . MET   A 1 428  ? 112.726 151.133 150.911 1.00 49.70  ? 428  MET   A CG    1 
ATOM   1292  S  SD    . MET   A 1 428  ? 114.285 150.254 151.107 1.00 56.60  ? 428  MET   A SD    1 
ATOM   1293  C  CE    . MET   A 1 428  ? 114.259 149.912 152.865 1.00 52.40  ? 428  MET   A CE    1 
ATOM   1294  N  N     . GLU   A 1 429  ? 108.529 150.859 152.026 1.00 50.57  ? 429  GLU   A N     1 
ATOM   1295  C  CA    . GLU   A 1 429  ? 107.605 151.912 152.434 1.00 53.15  ? 429  GLU   A CA    1 
ATOM   1296  C  C     . GLU   A 1 429  ? 107.079 151.698 153.849 1.00 56.09  ? 429  GLU   A C     1 
ATOM   1297  O  O     . GLU   A 1 429  ? 106.948 152.660 154.616 1.00 63.74  ? 429  GLU   A O     1 
ATOM   1298  C  CB    . GLU   A 1 429  ? 106.437 151.999 151.448 1.00 51.23  ? 429  GLU   A CB    1 
ATOM   1299  N  N     . TRP   A 1 430  ? 106.776 150.449 154.208 1.00 53.60  ? 430  TRP   A N     1 
ATOM   1300  C  CA    . TRP   A 1 430  ? 106.381 150.147 155.579 1.00 54.85  ? 430  TRP   A CA    1 
ATOM   1301  C  C     . TRP   A 1 430  ? 107.488 150.525 156.553 1.00 58.92  ? 430  TRP   A C     1 
ATOM   1302  O  O     . TRP   A 1 430  ? 107.222 151.055 157.640 1.00 55.86  ? 430  TRP   A O     1 
ATOM   1303  C  CB    . TRP   A 1 430  ? 106.039 148.663 155.709 1.00 57.51  ? 430  TRP   A CB    1 
ATOM   1304  C  CG    . TRP   A 1 430  ? 104.873 148.231 154.875 1.00 58.68  ? 430  TRP   A CG    1 
ATOM   1305  C  CD1   . TRP   A 1 430  ? 104.785 147.101 154.117 1.00 58.32  ? 430  TRP   A CD1   1 
ATOM   1306  C  CD2   . TRP   A 1 430  ? 103.626 148.918 154.717 1.00 58.64  ? 430  TRP   A CD2   1 
ATOM   1307  N  NE1   . TRP   A 1 430  ? 103.563 147.042 153.494 1.00 58.12  ? 430  TRP   A NE1   1 
ATOM   1308  C  CE2   . TRP   A 1 430  ? 102.832 148.145 153.846 1.00 59.67  ? 430  TRP   A CE2   1 
ATOM   1309  C  CE3   . TRP   A 1 430  ? 103.103 150.110 155.227 1.00 58.65  ? 430  TRP   A CE3   1 
ATOM   1310  C  CZ2   . TRP   A 1 430  ? 101.546 148.526 153.474 1.00 61.59  ? 430  TRP   A CZ2   1 
ATOM   1311  C  CZ3   . TRP   A 1 430  ? 101.826 150.486 154.856 1.00 57.30  ? 430  TRP   A CZ3   1 
ATOM   1312  C  CH2   . TRP   A 1 430  ? 101.062 149.697 153.988 1.00 59.56  ? 430  TRP   A CH2   1 
ATOM   1313  N  N     . GLU   A 1 431  ? 108.739 150.249 156.181 1.00 55.95  ? 431  GLU   A N     1 
ATOM   1314  C  CA    . GLU   A 1 431  ? 109.864 150.642 157.019 1.00 50.47  ? 431  GLU   A CA    1 
ATOM   1315  C  C     . GLU   A 1 431  ? 109.916 152.153 157.192 1.00 52.98  ? 431  GLU   A C     1 
ATOM   1316  O  O     . GLU   A 1 431  ? 110.206 152.649 158.285 1.00 55.57  ? 431  GLU   A O     1 
ATOM   1317  C  CB    . GLU   A 1 431  ? 111.169 150.123 156.417 1.00 50.03  ? 431  GLU   A CB    1 
ATOM   1318  C  CG    . GLU   A 1 431  ? 112.360 150.195 157.358 1.00 58.97  ? 431  GLU   A CG    1 
ATOM   1319  C  CD    . GLU   A 1 431  ? 113.365 151.250 156.943 1.00 62.62  ? 431  GLU   A CD    1 
ATOM   1320  O  OE1   . GLU   A 1 431  ? 113.233 151.788 155.824 1.00 65.04  ? 431  GLU   A OE1   1 
ATOM   1321  O  OE2   . GLU   A 1 431  ? 114.288 151.540 157.733 1.00 59.89  ? 431  GLU   A OE2   1 
ATOM   1322  N  N     . ALA   A 1 432  ? 109.641 152.904 156.122 1.00 38.93  ? 432  ALA   A N     1 
ATOM   1323  C  CA    . ALA   A 1 432  ? 109.631 154.360 156.227 1.00 41.37  ? 432  ALA   A CA    1 
ATOM   1324  C  C     . ALA   A 1 432  ? 108.521 154.839 157.155 1.00 53.87  ? 432  ALA   A C     1 
ATOM   1325  O  O     . ALA   A 1 432  ? 108.722 155.763 157.952 1.00 56.11  ? 432  ALA   A O     1 
ATOM   1326  C  CB    . ALA   A 1 432  ? 109.485 154.984 154.841 1.00 45.26  ? 432  ALA   A CB    1 
ATOM   1327  N  N     . LYS   A 1 433  ? 107.339 154.227 157.060 1.00 56.07  ? 433  LYS   A N     1 
ATOM   1328  C  CA    . LYS   A 1 433  ? 106.249 154.586 157.963 1.00 54.09  ? 433  LYS   A CA    1 
ATOM   1329  C  C     . LYS   A 1 433  ? 106.634 154.321 159.415 1.00 53.36  ? 433  LYS   A C     1 
ATOM   1330  O  O     . LYS   A 1 433  ? 106.398 155.154 160.301 1.00 54.30  ? 433  LYS   A O     1 
ATOM   1331  C  CB    . LYS   A 1 433  ? 104.986 153.808 157.591 1.00 54.00  ? 433  LYS   A CB    1 
ATOM   1332  C  CG    . LYS   A 1 433  ? 103.989 154.595 156.759 1.00 52.81  ? 433  LYS   A CG    1 
ATOM   1333  C  CD    . LYS   A 1 433  ? 104.594 155.022 155.433 1.00 58.33  ? 433  LYS   A CD    1 
ATOM   1334  C  CE    . LYS   A 1 433  ? 103.529 155.161 154.359 1.00 58.23  ? 433  LYS   A CE    1 
ATOM   1335  N  NZ    . LYS   A 1 433  ? 102.429 156.070 154.784 1.00 56.44  ? 433  LYS   A NZ    1 
ATOM   1336  N  N     . ALA   A 1 434  ? 107.230 153.156 159.674 1.00 48.19  ? 434  ALA   A N     1 
ATOM   1337  C  CA    . ALA   A 1 434  ? 107.658 152.828 161.030 1.00 47.27  ? 434  ALA   A CA    1 
ATOM   1338  C  C     . ALA   A 1 434  ? 108.717 153.805 161.522 1.00 52.59  ? 434  ALA   A C     1 
ATOM   1339  O  O     . ALA   A 1 434  ? 108.704 154.213 162.690 1.00 61.00  ? 434  ALA   A O     1 
ATOM   1340  C  CB    . ALA   A 1 434  ? 108.182 151.394 161.083 1.00 49.04  ? 434  ALA   A CB    1 
ATOM   1341  N  N     . GLN   A 1 435  ? 109.651 154.184 160.647 1.00 48.42  ? 435  GLN   A N     1 
ATOM   1342  C  CA    . GLN   A 1 435  ? 110.670 155.156 161.023 1.00 50.39  ? 435  GLN   A CA    1 
ATOM   1343  C  C     . GLN   A 1 435  ? 110.043 156.498 161.373 1.00 52.11  ? 435  GLN   A C     1 
ATOM   1344  O  O     . GLN   A 1 435  ? 110.466 157.159 162.327 1.00 52.77  ? 435  GLN   A O     1 
ATOM   1345  C  CB    . GLN   A 1 435  ? 111.686 155.317 159.892 1.00 52.10  ? 435  GLN   A CB    1 
ATOM   1346  C  CG    . GLN   A 1 435  ? 112.475 154.058 159.577 1.00 52.41  ? 435  GLN   A CG    1 
ATOM   1347  C  CD    . GLN   A 1 435  ? 113.372 153.628 160.718 1.00 56.72  ? 435  GLN   A CD    1 
ATOM   1348  O  OE1   . GLN   A 1 435  ? 113.780 154.443 161.545 1.00 59.45  ? 435  GLN   A OE1   1 
ATOM   1349  N  NE2   . GLN   A 1 435  ? 113.686 152.340 160.769 1.00 57.24  ? 435  GLN   A NE2   1 
ATOM   1350  N  N     . ILE   A 1 436  ? 109.034 156.921 160.610 1.00 43.95  ? 436  ILE   A N     1 
ATOM   1351  C  CA    . ILE   A 1 436  ? 108.362 158.182 160.912 1.00 45.46  ? 436  ILE   A CA    1 
ATOM   1352  C  C     . ILE   A 1 436  ? 107.673 158.105 162.269 1.00 50.93  ? 436  ILE   A C     1 
ATOM   1353  O  O     . ILE   A 1 436  ? 107.739 159.045 163.072 1.00 55.61  ? 436  ILE   A O     1 
ATOM   1354  C  CB    . ILE   A 1 436  ? 107.370 158.544 159.792 1.00 41.32  ? 436  ILE   A CB    1 
ATOM   1355  C  CG1   . ILE   A 1 436  ? 108.087 159.286 158.663 1.00 45.30  ? 436  ILE   A CG1   1 
ATOM   1356  C  CG2   . ILE   A 1 436  ? 106.237 159.394 160.342 1.00 42.87  ? 436  ILE   A CG2   1 
ATOM   1357  C  CD1   . ILE   A 1 436  ? 108.692 160.606 159.084 1.00 46.74  ? 436  ILE   A CD1   1 
ATOM   1358  N  N     . VAL   A 1 437  ? 106.997 156.987 162.545 1.00 40.65  ? 437  VAL   A N     1 
ATOM   1359  C  CA    . VAL   A 1 437  ? 106.328 156.829 163.836 1.00 39.39  ? 437  VAL   A CA    1 
ATOM   1360  C  C     . VAL   A 1 437  ? 107.344 156.891 164.973 1.00 41.72  ? 437  VAL   A C     1 
ATOM   1361  O  O     . VAL   A 1 437  ? 107.135 157.570 165.988 1.00 43.29  ? 437  VAL   A O     1 
ATOM   1362  C  CB    . VAL   A 1 437  ? 105.524 155.517 163.872 1.00 39.31  ? 437  VAL   A CB    1 
ATOM   1363  C  CG1   . VAL   A 1 437  ? 104.675 155.451 165.129 1.00 38.99  ? 437  VAL   A CG1   1 
ATOM   1364  C  CG2   . VAL   A 1 437  ? 104.652 155.391 162.635 1.00 47.50  ? 437  VAL   A CG2   1 
ATOM   1365  N  N     . LEU   A 1 438  ? 108.460 156.175 164.819 1.00 37.50  ? 438  LEU   A N     1 
ATOM   1366  C  CA    . LEU   A 1 438  ? 109.481 156.162 165.861 1.00 34.40  ? 438  LEU   A CA    1 
ATOM   1367  C  C     . LEU   A 1 438  ? 110.081 157.547 166.064 1.00 37.78  ? 438  LEU   A C     1 
ATOM   1368  O  O     . LEU   A 1 438  ? 110.349 157.955 167.200 1.00 43.72  ? 438  LEU   A O     1 
ATOM   1369  C  CB    . LEU   A 1 438  ? 110.569 155.148 165.514 1.00 35.09  ? 438  LEU   A CB    1 
ATOM   1370  C  CG    . LEU   A 1 438  ? 110.103 153.697 165.383 1.00 38.11  ? 438  LEU   A CG    1 
ATOM   1371  C  CD1   . LEU   A 1 438  ? 111.274 152.776 165.090 1.00 42.25  ? 438  LEU   A CD1   1 
ATOM   1372  C  CD2   . LEU   A 1 438  ? 109.382 153.258 166.645 1.00 40.27  ? 438  LEU   A CD2   1 
ATOM   1373  N  N     . LEU   A 1 439  ? 110.310 158.282 164.974 1.00 38.89  ? 439  LEU   A N     1 
ATOM   1374  C  CA    . LEU   A 1 439  ? 110.836 159.636 165.096 1.00 43.47  ? 439  LEU   A CA    1 
ATOM   1375  C  C     . LEU   A 1 439  ? 109.857 160.539 165.831 1.00 42.30  ? 439  LEU   A C     1 
ATOM   1376  O  O     . LEU   A 1 439  ? 110.262 161.357 166.665 1.00 46.48  ? 439  LEU   A O     1 
ATOM   1377  C  CB    . LEU   A 1 439  ? 111.154 160.205 163.714 1.00 46.65  ? 439  LEU   A CB    1 
ATOM   1378  C  CG    . LEU   A 1 439  ? 111.643 161.655 163.703 1.00 45.57  ? 439  LEU   A CG    1 
ATOM   1379  C  CD1   . LEU   A 1 439  ? 113.154 161.714 163.569 1.00 44.40  ? 439  LEU   A CD1   1 
ATOM   1380  C  CD2   . LEU   A 1 439  ? 110.973 162.444 162.591 1.00 41.87  ? 439  LEU   A CD2   1 
ATOM   1381  N  N     . VAL   A 1 440  ? 108.563 160.411 165.532 1.00 39.14  ? 440  VAL   A N     1 
ATOM   1382  C  CA    . VAL   A 1 440  ? 107.566 161.211 166.238 1.00 42.91  ? 440  VAL   A CA    1 
ATOM   1383  C  C     . VAL   A 1 440  ? 107.591 160.890 167.726 1.00 42.87  ? 440  VAL   A C     1 
ATOM   1384  O  O     . VAL   A 1 440  ? 107.551 161.791 168.573 1.00 43.42  ? 440  VAL   A O     1 
ATOM   1385  C  CB    . VAL   A 1 440  ? 106.167 160.985 165.633 1.00 41.26  ? 440  VAL   A CB    1 
ATOM   1386  C  CG1   . VAL   A 1 440  ? 105.091 161.190 166.689 1.00 40.31  ? 440  VAL   A CG1   1 
ATOM   1387  C  CG2   . VAL   A 1 440  ? 105.943 161.914 164.452 1.00 45.98  ? 440  VAL   A CG2   1 
ATOM   1388  N  N     . ILE   A 1 441  ? 107.666 159.602 168.069 1.00 47.03  ? 441  ILE   A N     1 
ATOM   1389  C  CA    . ILE   A 1 441  ? 107.686 159.211 169.477 1.00 40.24  ? 441  ILE   A CA    1 
ATOM   1390  C  C     . ILE   A 1 441  ? 108.924 159.766 170.175 1.00 40.28  ? 441  ILE   A C     1 
ATOM   1391  O  O     . ILE   A 1 441  ? 108.849 160.269 171.303 1.00 39.76  ? 441  ILE   A O     1 
ATOM   1392  C  CB    . ILE   A 1 441  ? 107.601 157.680 169.609 1.00 40.68  ? 441  ILE   A CB    1 
ATOM   1393  C  CG1   . ILE   A 1 441  ? 106.177 157.201 169.322 1.00 39.43  ? 441  ILE   A CG1   1 
ATOM   1394  C  CG2   . ILE   A 1 441  ? 108.035 157.241 170.995 1.00 43.27  ? 441  ILE   A CG2   1 
ATOM   1395  C  CD1   . ILE   A 1 441  ? 106.089 155.747 168.917 1.00 41.40  ? 441  ILE   A CD1   1 
ATOM   1396  N  N     . LEU   A 1 442  ? 110.085 159.672 169.524 1.00 42.13  ? 442  LEU   A N     1 
ATOM   1397  C  CA    . LEU   A 1 442  ? 111.318 160.152 170.141 1.00 42.34  ? 442  LEU   A CA    1 
ATOM   1398  C  C     . LEU   A 1 442  ? 111.299 161.667 170.316 1.00 45.67  ? 442  LEU   A C     1 
ATOM   1399  O  O     . LEU   A 1 442  ? 111.760 162.188 171.342 1.00 50.83  ? 442  LEU   A O     1 
ATOM   1400  C  CB    . LEU   A 1 442  ? 112.523 159.713 169.308 1.00 43.65  ? 442  LEU   A CB    1 
ATOM   1401  C  CG    . LEU   A 1 442  ? 113.851 160.427 169.558 1.00 46.52  ? 442  LEU   A CG    1 
ATOM   1402  C  CD1   . LEU   A 1 442  ? 115.014 159.470 169.374 1.00 47.47  ? 442  LEU   A CD1   1 
ATOM   1403  C  CD2   . LEU   A 1 442  ? 114.000 161.620 168.632 1.00 48.30  ? 442  LEU   A CD2   1 
ATOM   1404  N  N     . LEU   A 1 443  ? 110.777 162.394 169.326 1.00 43.12  ? 443  LEU   A N     1 
ATOM   1405  C  CA    . LEU   A 1 443  ? 110.638 163.838 169.476 1.00 43.95  ? 443  LEU   A CA    1 
ATOM   1406  C  C     . LEU   A 1 443  ? 109.680 164.176 170.609 1.00 49.26  ? 443  LEU   A C     1 
ATOM   1407  O  O     . LEU   A 1 443  ? 109.904 165.135 171.358 1.00 52.98  ? 443  LEU   A O     1 
ATOM   1408  C  CB    . LEU   A 1 443  ? 110.168 164.465 168.164 1.00 44.53  ? 443  LEU   A CB    1 
ATOM   1409  C  CG    . LEU   A 1 443  ? 111.251 164.689 167.107 1.00 48.98  ? 443  LEU   A CG    1 
ATOM   1410  C  CD1   . LEU   A 1 443  ? 110.775 165.671 166.051 1.00 50.08  ? 443  LEU   A CD1   1 
ATOM   1411  C  CD2   . LEU   A 1 443  ? 112.536 165.179 167.753 1.00 47.85  ? 443  LEU   A CD2   1 
ATOM   1412  N  N     . LEU   A 1 444  ? 108.602 163.402 170.749 1.00 49.41  ? 444  LEU   A N     1 
ATOM   1413  C  CA    . LEU   A 1 444  ? 107.700 163.599 171.877 1.00 47.09  ? 444  LEU   A CA    1 
ATOM   1414  C  C     . LEU   A 1 444  ? 108.427 163.399 173.198 1.00 47.51  ? 444  LEU   A C     1 
ATOM   1415  O  O     . LEU   A 1 444  ? 108.217 164.155 174.149 1.00 54.12  ? 444  LEU   A O     1 
ATOM   1416  C  CB    . LEU   A 1 444  ? 106.508 162.649 171.775 1.00 44.75  ? 444  LEU   A CB    1 
ATOM   1417  C  CG    . LEU   A 1 444  ? 105.442 163.001 170.739 1.00 51.33  ? 444  LEU   A CG    1 
ATOM   1418  C  CD1   . LEU   A 1 444  ? 104.254 162.063 170.856 1.00 51.85  ? 444  LEU   A CD1   1 
ATOM   1419  C  CD2   . LEU   A 1 444  ? 105.003 164.444 170.900 1.00 50.68  ? 444  LEU   A CD2   1 
ATOM   1420  N  N     . ALA   A 1 445  ? 109.277 162.375 173.280 1.00 44.60  ? 445  ALA   A N     1 
ATOM   1421  C  CA    . ALA   A 1 445  ? 110.032 162.144 174.510 1.00 46.42  ? 445  ALA   A CA    1 
ATOM   1422  C  C     . ALA   A 1 445  ? 110.966 163.310 174.817 1.00 47.91  ? 445  ALA   A C     1 
ATOM   1423  O  O     . ALA   A 1 445  ? 111.071 163.751 175.971 1.00 55.01  ? 445  ALA   A O     1 
ATOM   1424  C  CB    . ALA   A 1 445  ? 110.819 160.839 174.404 1.00 49.01  ? 445  ALA   A CB    1 
ATOM   1425  N  N     . ILE   A 1 446  ? 111.661 163.818 173.798 1.00 51.61  ? 446  ILE   A N     1 
ATOM   1426  C  CA    . ILE   A 1 446  ? 112.571 164.942 174.011 1.00 51.80  ? 446  ILE   A CA    1 
ATOM   1427  C  C     . ILE   A 1 446  ? 111.796 166.163 174.494 1.00 54.50  ? 446  ILE   A C     1 
ATOM   1428  O  O     . ILE   A 1 446  ? 112.195 166.846 175.449 1.00 52.29  ? 446  ILE   A O     1 
ATOM   1429  C  CB    . ILE   A 1 446  ? 113.360 165.247 172.725 1.00 47.86  ? 446  ILE   A CB    1 
ATOM   1430  C  CG1   . ILE   A 1 446  ? 114.510 164.253 172.557 1.00 53.95  ? 446  ILE   A CG1   1 
ATOM   1431  C  CG2   . ILE   A 1 446  ? 113.894 166.670 172.754 1.00 49.77  ? 446  ILE   A CG2   1 
ATOM   1432  C  CD1   . ILE   A 1 446  ? 115.271 164.414 171.258 1.00 55.00  ? 446  ILE   A CD1   1 
ATOM   1433  N  N     . GLY   A 1 447  ? 110.674 166.458 173.835 1.00 58.57  ? 447  GLY   A N     1 
ATOM   1434  C  CA    . GLY   A 1 447  ? 109.852 167.575 174.260 1.00 57.09  ? 447  GLY   A CA    1 
ATOM   1435  C  C     . GLY   A 1 447  ? 109.289 167.394 175.653 1.00 58.97  ? 447  GLY   A C     1 
ATOM   1436  O  O     . GLY   A 1 447  ? 109.154 168.363 176.401 1.00 60.96  ? 447  GLY   A O     1 
ATOM   1437  N  N     . ASP   A 1 448  ? 108.952 166.158 176.021 1.00 59.20  ? 448  ASP   A N     1 
ATOM   1438  C  CA    . ASP   A 1 448  ? 108.472 165.886 177.370 1.00 51.27  ? 448  ASP   A CA    1 
ATOM   1439  C  C     . ASP   A 1 448  ? 109.553 166.180 178.399 1.00 53.32  ? 448  ASP   A C     1 
ATOM   1440  O  O     . ASP   A 1 448  ? 109.281 166.792 179.438 1.00 63.03  ? 448  ASP   A O     1 
ATOM   1441  C  CB    . ASP   A 1 448  ? 108.002 164.433 177.467 1.00 51.98  ? 448  ASP   A CB    1 
ATOM   1442  C  CG    . ASP   A 1 448  ? 108.033 163.894 178.884 1.00 62.09  ? 448  ASP   A CG    1 
ATOM   1443  O  OD1   . ASP   A 1 448  ? 107.789 164.667 179.834 1.00 70.96  ? 448  ASP   A OD1   1 
ATOM   1444  O  OD2   . ASP   A 1 448  ? 108.300 162.685 179.048 1.00 62.99  ? 448  ASP   A OD2   1 
ATOM   1445  N  N     . PHE   A 1 449  ? 110.787 165.753 178.128 1.00 52.95  ? 449  PHE   A N     1 
ATOM   1446  C  CA    . PHE   A 1 449  ? 111.875 166.073 179.048 1.00 53.27  ? 449  PHE   A CA    1 
ATOM   1447  C  C     . PHE   A 1 449  ? 112.056 167.580 179.174 1.00 47.33  ? 449  PHE   A C     1 
ATOM   1448  O  O     . PHE   A 1 449  ? 112.207 168.109 180.284 1.00 50.09  ? 449  PHE   A O     1 
ATOM   1449  C  CB    . PHE   A 1 449  ? 113.179 165.420 178.588 1.00 57.72  ? 449  PHE   A CB    1 
ATOM   1450  C  CG    . PHE   A 1 449  ? 114.403 165.975 179.265 1.00 52.47  ? 449  PHE   A CG    1 
ATOM   1451  C  CD1   . PHE   A 1 449  ? 114.807 165.490 180.497 1.00 47.52  ? 449  PHE   A CD1   1 
ATOM   1452  C  CD2   . PHE   A 1 449  ? 115.146 166.985 178.674 1.00 52.81  ? 449  PHE   A CD2   1 
ATOM   1453  C  CE1   . PHE   A 1 449  ? 115.928 165.998 181.124 1.00 53.26  ? 449  PHE   A CE1   1 
ATOM   1454  C  CE2   . PHE   A 1 449  ? 116.268 167.496 179.298 1.00 51.92  ? 449  PHE   A CE2   1 
ATOM   1455  C  CZ    . PHE   A 1 449  ? 116.659 167.001 180.523 1.00 51.33  ? 449  PHE   A CZ    1 
ATOM   1456  N  N     . VAL   A 1 450  ? 112.039 168.292 178.045 1.00 52.16  ? 450  VAL   A N     1 
ATOM   1457  C  CA    . VAL   A 1 450  ? 112.265 169.734 178.088 1.00 54.56  ? 450  VAL   A CA    1 
ATOM   1458  C  C     . VAL   A 1 450  ? 111.128 170.436 178.824 1.00 57.51  ? 450  VAL   A C     1 
ATOM   1459  O  O     . VAL   A 1 450  ? 111.350 171.415 179.545 1.00 59.72  ? 450  VAL   A O     1 
ATOM   1460  C  CB    . VAL   A 1 450  ? 112.454 170.294 176.667 1.00 56.17  ? 450  VAL   A CB    1 
ATOM   1461  C  CG1   . VAL   A 1 450  ? 112.064 171.762 176.622 1.00 55.16  ? 450  VAL   A CG1   1 
ATOM   1462  C  CG2   . VAL   A 1 450  ? 113.894 170.114 176.215 1.00 54.67  ? 450  VAL   A CG2   1 
ATOM   1463  N  N     . ILE   A 1 451  ? 109.895 169.958 178.650 1.00 55.27  ? 451  ILE   A N     1 
ATOM   1464  C  CA    . ILE   A 1 451  ? 108.758 170.561 179.336 1.00 47.97  ? 451  ILE   A CA    1 
ATOM   1465  C  C     . ILE   A 1 451  ? 108.837 170.300 180.834 1.00 51.41  ? 451  ILE   A C     1 
ATOM   1466  O  O     . ILE   A 1 451  ? 108.576 171.193 181.648 1.00 55.29  ? 451  ILE   A O     1 
ATOM   1467  C  CB    . ILE   A 1 451  ? 107.437 170.044 178.740 1.00 43.53  ? 451  ILE   A CB    1 
ATOM   1468  N  N     . GLY   A 1 452  ? 109.196 169.075 181.223 1.00 55.66  ? 452  GLY   A N     1 
ATOM   1469  C  CA    . GLY   A 1 452  ? 109.298 168.751 182.634 1.00 48.01  ? 452  GLY   A CA    1 
ATOM   1470  C  C     . GLY   A 1 452  ? 110.482 169.389 183.323 1.00 48.31  ? 452  GLY   A C     1 
ATOM   1471  O  O     . GLY   A 1 452  ? 110.496 169.472 184.556 1.00 56.02  ? 452  GLY   A O     1 
ATOM   1472  N  N     . THR   A 1 453  ? 111.478 169.842 182.559 1.00 49.48  ? 453  THR   A N     1 
ATOM   1473  C  CA    . THR   A 1 453  ? 112.578 170.578 183.170 1.00 48.06  ? 453  THR   A CA    1 
ATOM   1474  C  C     . THR   A 1 453  ? 112.173 171.992 183.568 1.00 52.22  ? 453  THR   A C     1 
ATOM   1475  O  O     . THR   A 1 453  ? 112.901 172.642 184.326 1.00 51.20  ? 453  THR   A O     1 
ATOM   1476  C  CB    . THR   A 1 453  ? 113.779 170.631 182.223 1.00 49.77  ? 453  THR   A CB    1 
ATOM   1477  O  OG1   . THR   A 1 453  ? 114.980 170.818 182.982 1.00 53.83  ? 453  THR   A OG1   1 
ATOM   1478  C  CG2   . THR   A 1 453  ? 113.635 171.780 181.245 1.00 49.27  ? 453  THR   A CG2   1 
ATOM   1479  N  N     . PHE   A 1 454  ? 111.033 172.480 183.080 1.00 55.97  ? 454  PHE   A N     1 
ATOM   1480  C  CA    . PHE   A 1 454  ? 110.533 173.806 183.418 1.00 53.82  ? 454  PHE   A CA    1 
ATOM   1481  C  C     . PHE   A 1 454  ? 109.492 173.788 184.528 1.00 54.88  ? 454  PHE   A C     1 
ATOM   1482  O  O     . PHE   A 1 454  ? 109.022 174.855 184.933 1.00 56.65  ? 454  PHE   A O     1 
ATOM   1483  C  CB    . PHE   A 1 454  ? 109.939 174.481 182.178 1.00 48.98  ? 454  PHE   A CB    1 
ATOM   1484  C  CG    . PHE   A 1 454  ? 110.922 175.316 181.409 1.00 53.12  ? 454  PHE   A CG    1 
ATOM   1485  C  CD1   . PHE   A 1 454  ? 111.094 176.655 181.709 1.00 53.19  ? 454  PHE   A CD1   1 
ATOM   1486  C  CD2   . PHE   A 1 454  ? 111.669 174.764 180.384 1.00 55.08  ? 454  PHE   A CD2   1 
ATOM   1487  C  CE1   . PHE   A 1 454  ? 111.993 177.426 181.003 1.00 56.99  ? 454  PHE   A CE1   1 
ATOM   1488  C  CE2   . PHE   A 1 454  ? 112.570 175.531 179.676 1.00 53.13  ? 454  PHE   A CE2   1 
ATOM   1489  C  CZ    . PHE   A 1 454  ? 112.733 176.863 179.985 1.00 55.73  ? 454  PHE   A CZ    1 
ATOM   1490  N  N     . ILE   A 1 455  ? 109.120 172.614 185.026 1.00 50.62  ? 455  ILE   A N     1 
ATOM   1491  C  CA    . ILE   A 1 455  ? 108.116 172.507 186.081 1.00 45.81  ? 455  ILE   A CA    1 
ATOM   1492  C  C     . ILE   A 1 455  ? 108.741 171.808 187.281 1.00 54.41  ? 455  ILE   A C     1 
ATOM   1493  O  O     . ILE   A 1 455  ? 108.732 170.571 187.351 1.00 53.92  ? 455  ILE   A O     1 
ATOM   1494  C  CB    . ILE   A 1 455  ? 106.867 171.761 185.591 1.00 39.09  ? 455  ILE   A CB    1 
ATOM   1495  N  N     . PRO   A 1 456  ? 109.290 172.549 188.243 1.00 63.36  ? 456  PRO   A N     1 
ATOM   1496  C  CA    . PRO   A 1 456  ? 109.922 171.923 189.412 1.00 61.38  ? 456  PRO   A CA    1 
ATOM   1497  C  C     . PRO   A 1 456  ? 108.889 171.558 190.465 1.00 62.23  ? 456  PRO   A C     1 
ATOM   1498  O  O     . PRO   A 1 456  ? 108.244 172.430 191.057 1.00 61.08  ? 456  PRO   A O     1 
ATOM   1499  C  CB    . PRO   A 1 456  ? 110.889 173.011 189.905 1.00 56.97  ? 456  PRO   A CB    1 
ATOM   1500  C  CG    . PRO   A 1 456  ? 110.454 174.303 189.213 1.00 60.18  ? 456  PRO   A CG    1 
ATOM   1501  C  CD    . PRO   A 1 456  ? 109.245 174.011 188.375 1.00 61.97  ? 456  PRO   A CD    1 
ATOM   1502  N  N     . LEU   A 1 457  ? 108.733 170.260 190.705 1.00 65.39  ? 457  LEU   A N     1 
ATOM   1503  C  CA    . LEU   A 1 457  ? 107.814 169.748 191.712 1.00 62.38  ? 457  LEU   A CA    1 
ATOM   1504  C  C     . LEU   A 1 457  ? 108.589 169.437 192.985 1.00 65.54  ? 457  LEU   A C     1 
ATOM   1505  O  O     . LEU   A 1 457  ? 109.638 168.787 192.935 1.00 69.01  ? 457  LEU   A O     1 
ATOM   1506  C  CB    . LEU   A 1 457  ? 107.091 168.498 191.209 1.00 57.76  ? 457  LEU   A CB    1 
ATOM   1507  N  N     . GLU   A 1 458  ? 108.069 169.905 194.123 1.00 70.96  ? 458  GLU   A N     1 
ATOM   1508  C  CA    . GLU   A 1 458  ? 108.776 169.730 195.387 1.00 68.09  ? 458  GLU   A CA    1 
ATOM   1509  C  C     . GLU   A 1 458  ? 109.036 168.261 195.692 1.00 69.23  ? 458  GLU   A C     1 
ATOM   1510  O  O     . GLU   A 1 458  ? 110.026 167.933 196.356 1.00 70.19  ? 458  GLU   A O     1 
ATOM   1511  C  CB    . GLU   A 1 458  ? 107.986 170.376 196.525 1.00 64.06  ? 458  GLU   A CB    1 
ATOM   1512  N  N     . SER   A 1 459  ? 108.168 167.364 195.218 1.00 71.44  ? 459  SER   A N     1 
ATOM   1513  C  CA    . SER   A 1 459  ? 108.365 165.943 195.484 1.00 71.78  ? 459  SER   A CA    1 
ATOM   1514  C  C     . SER   A 1 459  ? 109.695 165.448 194.933 1.00 72.45  ? 459  SER   A C     1 
ATOM   1515  O  O     . SER   A 1 459  ? 110.274 164.497 195.471 1.00 70.51  ? 459  SER   A O     1 
ATOM   1516  C  CB    . SER   A 1 459  ? 107.211 165.133 194.893 1.00 72.94  ? 459  SER   A CB    1 
ATOM   1517  O  OG    . SER   A 1 459  ? 107.635 163.829 194.536 1.00 73.80  ? 459  SER   A OG    1 
ATOM   1518  N  N     . LYS   A 1 460  ? 110.194 166.074 193.871 1.00 72.04  ? 460  LYS   A N     1 
ATOM   1519  C  CA    . LYS   A 1 460  ? 111.477 165.712 193.287 1.00 67.77  ? 460  LYS   A CA    1 
ATOM   1520  C  C     . LYS   A 1 460  ? 112.638 166.483 193.900 1.00 69.49  ? 460  LYS   A C     1 
ATOM   1521  O  O     . LYS   A 1 460  ? 113.784 166.283 193.485 1.00 70.38  ? 460  LYS   A O     1 
ATOM   1522  C  CB    . LYS   A 1 460  ? 111.445 165.930 191.770 1.00 68.45  ? 460  LYS   A CB    1 
ATOM   1523  C  CG    . LYS   A 1 460  ? 110.902 164.738 190.996 1.00 68.98  ? 460  LYS   A CG    1 
ATOM   1524  C  CD    . LYS   A 1 460  ? 110.798 165.030 189.509 1.00 65.25  ? 460  LYS   A CD    1 
ATOM   1525  C  CE    . LYS   A 1 460  ? 110.011 166.302 189.247 1.00 68.89  ? 460  LYS   A CE    1 
ATOM   1526  N  NZ    . LYS   A 1 460  ? 109.205 166.209 187.998 1.00 66.73  ? 460  LYS   A NZ    1 
ATOM   1527  N  N     . LYS   A 1 461  ? 112.369 167.353 194.873 1.00 66.99  ? 461  LYS   A N     1 
ATOM   1528  C  CA    . LYS   A 1 461  ? 113.451 168.048 195.564 1.00 59.04  ? 461  LYS   A CA    1 
ATOM   1529  C  C     . LYS   A 1 461  ? 114.453 167.102 196.213 1.00 60.55  ? 461  LYS   A C     1 
ATOM   1530  O  O     . LYS   A 1 461  ? 115.664 167.356 196.088 1.00 57.80  ? 461  LYS   A O     1 
ATOM   1531  C  CB    . LYS   A 1 461  ? 112.864 169.011 196.603 1.00 60.85  ? 461  LYS   A CB    1 
ATOM   1532  N  N     . PRO   A 1 462  ? 114.053 166.027 196.900 1.00 72.09  ? 462  PRO   A N     1 
ATOM   1533  C  CA    . PRO   A 1 462  ? 115.063 165.116 197.458 1.00 70.25  ? 462  PRO   A CA    1 
ATOM   1534  C  C     . PRO   A 1 462  ? 115.881 164.417 196.392 1.00 72.15  ? 462  PRO   A C     1 
ATOM   1535  O  O     . PRO   A 1 462  ? 116.959 163.893 196.700 1.00 70.81  ? 462  PRO   A O     1 
ATOM   1536  C  CB    . PRO   A 1 462  ? 114.232 164.133 198.289 1.00 70.15  ? 462  PRO   A CB    1 
ATOM   1537  C  CG    . PRO   A 1 462  ? 112.894 164.119 197.647 1.00 73.44  ? 462  PRO   A CG    1 
ATOM   1538  C  CD    . PRO   A 1 462  ? 112.719 165.401 196.864 1.00 74.57  ? 462  PRO   A CD    1 
ATOM   1539  N  N     . LYS   A 1 463  ? 115.400 164.382 195.154 1.00 77.44  ? 463  LYS   A N     1 
ATOM   1540  C  CA    . LYS   A 1 463  ? 116.240 164.023 194.026 1.00 73.52  ? 463  LYS   A CA    1 
ATOM   1541  C  C     . LYS   A 1 463  ? 117.180 165.185 193.708 1.00 69.97  ? 463  LYS   A C     1 
ATOM   1542  O  O     . LYS   A 1 463  ? 117.224 166.198 194.412 1.00 77.13  ? 463  LYS   A O     1 
ATOM   1543  C  CB    . LYS   A 1 463  ? 115.381 163.666 192.814 1.00 71.61  ? 463  LYS   A CB    1 
ATOM   1544  C  CG    . LYS   A 1 463  ? 114.084 162.937 193.141 1.00 72.34  ? 463  LYS   A CG    1 
ATOM   1545  C  CD    . LYS   A 1 463  ? 114.282 161.431 193.181 1.00 71.64  ? 463  LYS   A CD    1 
ATOM   1546  C  CE    . LYS   A 1 463  ? 112.955 160.696 193.282 1.00 73.86  ? 463  LYS   A CE    1 
ATOM   1547  N  NZ    . LYS   A 1 463  ? 113.145 159.220 193.351 1.00 72.36  ? 463  LYS   A NZ    1 
ATOM   1548  N  N     . GLY   A 1 464  ? 117.946 165.040 192.631 1.00 55.78  ? 464  GLY   A N     1 
ATOM   1549  C  CA    . GLY   A 1 464  ? 118.847 166.104 192.233 1.00 62.18  ? 464  GLY   A CA    1 
ATOM   1550  C  C     . GLY   A 1 464  ? 118.203 167.258 191.496 1.00 66.08  ? 464  GLY   A C     1 
ATOM   1551  O  O     . GLY   A 1 464  ? 118.871 168.266 191.252 1.00 70.16  ? 464  GLY   A O     1 
ATOM   1552  N  N     . PHE   A 1 465  ? 116.926 167.140 191.142 1.00 57.09  ? 465  PHE   A N     1 
ATOM   1553  C  CA    . PHE   A 1 465  ? 116.264 168.146 190.322 1.00 57.34  ? 465  PHE   A CA    1 
ATOM   1554  C  C     . PHE   A 1 465  ? 115.877 169.359 191.161 1.00 56.59  ? 465  PHE   A C     1 
ATOM   1555  O  O     . PHE   A 1 465  ? 115.305 169.218 192.246 1.00 58.39  ? 465  PHE   A O     1 
ATOM   1556  C  CB    . PHE   A 1 465  ? 115.028 167.547 189.652 1.00 56.61  ? 465  PHE   A CB    1 
ATOM   1557  C  CG    . PHE   A 1 465  ? 114.341 168.479 188.694 1.00 55.71  ? 465  PHE   A CG    1 
ATOM   1558  C  CD1   . PHE   A 1 465  ? 115.062 169.415 187.974 1.00 52.14  ? 465  PHE   A CD1   1 
ATOM   1559  C  CD2   . PHE   A 1 465  ? 112.971 168.417 188.515 1.00 53.88  ? 465  PHE   A CD2   1 
ATOM   1560  C  CE1   . PHE   A 1 465  ? 114.427 170.269 187.096 1.00 53.20  ? 465  PHE   A CE1   1 
ATOM   1561  C  CE2   . PHE   A 1 465  ? 112.334 169.269 187.638 1.00 52.43  ? 465  PHE   A CE2   1 
ATOM   1562  C  CZ    . PHE   A 1 465  ? 113.062 170.195 186.928 1.00 53.96  ? 465  PHE   A CZ    1 
ATOM   1563  N  N     . PHE   A 1 466  ? 116.189 170.553 190.653 1.00 64.35  ? 466  PHE   A N     1 
ATOM   1564  C  CA    . PHE   A 1 466  ? 115.827 171.800 191.318 1.00 61.32  ? 466  PHE   A CA    1 
ATOM   1565  C  C     . PHE   A 1 466  ? 115.157 172.828 190.416 1.00 65.04  ? 466  PHE   A C     1 
ATOM   1566  O  O     . PHE   A 1 466  ? 114.511 173.742 190.943 1.00 69.09  ? 466  PHE   A O     1 
ATOM   1567  C  CB    . PHE   A 1 466  ? 117.058 172.440 191.979 1.00 61.52  ? 466  PHE   A CB    1 
ATOM   1568  C  CG    . PHE   A 1 466  ? 117.411 171.831 193.308 1.00 66.15  ? 466  PHE   A CG    1 
ATOM   1569  C  CD1   . PHE   A 1 466  ? 116.520 171.890 194.365 1.00 65.03  ? 466  PHE   A CD1   1 
ATOM   1570  C  CD2   . PHE   A 1 466  ? 118.626 171.195 193.501 1.00 67.08  ? 466  PHE   A CD2   1 
ATOM   1571  C  CE1   . PHE   A 1 466  ? 116.833 171.331 195.587 1.00 65.94  ? 466  PHE   A CE1   1 
ATOM   1572  C  CE2   . PHE   A 1 466  ? 118.944 170.634 194.725 1.00 66.05  ? 466  PHE   A CE2   1 
ATOM   1573  C  CZ    . PHE   A 1 466  ? 118.046 170.702 195.768 1.00 64.77  ? 466  PHE   A CZ    1 
ATOM   1574  N  N     . GLY   A 1 467  ? 115.278 172.723 189.094 1.00 65.14  ? 467  GLY   A N     1 
ATOM   1575  C  CA    . GLY   A 1 467  ? 114.529 173.613 188.227 1.00 62.49  ? 467  GLY   A CA    1 
ATOM   1576  C  C     . GLY   A 1 467  ? 115.227 174.874 187.757 1.00 63.24  ? 467  GLY   A C     1 
ATOM   1577  O  O     . GLY   A 1 467  ? 114.721 175.979 187.971 1.00 69.04  ? 467  GLY   A O     1 
ATOM   1578  N  N     . TYR   A 1 468  ? 116.390 174.731 187.120 1.00 58.23  ? 468  TYR   A N     1 
ATOM   1579  C  CA    . TYR   A 1 468  ? 117.063 175.873 186.509 1.00 60.19  ? 468  TYR   A CA    1 
ATOM   1580  C  C     . TYR   A 1 468  ? 117.509 176.904 187.537 1.00 62.07  ? 468  TYR   A C     1 
ATOM   1581  O  O     . TYR   A 1 468  ? 117.054 178.052 187.508 1.00 66.60  ? 468  TYR   A O     1 
ATOM   1582  C  CB    . TYR   A 1 468  ? 116.142 176.544 185.484 1.00 61.04  ? 468  TYR   A CB    1 
ATOM   1583  C  CG    . TYR   A 1 468  ? 116.181 175.931 184.102 1.00 64.60  ? 468  TYR   A CG    1 
ATOM   1584  C  CD1   . TYR   A 1 468  ? 116.995 174.844 183.825 1.00 62.05  ? 468  TYR   A CD1   1 
ATOM   1585  C  CD2   . TYR   A 1 468  ? 115.394 176.437 183.077 1.00 63.13  ? 468  TYR   A CD2   1 
ATOM   1586  C  CE1   . TYR   A 1 468  ? 117.029 174.280 182.563 1.00 59.68  ? 468  TYR   A CE1   1 
ATOM   1587  C  CE2   . TYR   A 1 468  ? 115.420 175.880 181.813 1.00 61.49  ? 468  TYR   A CE2   1 
ATOM   1588  C  CZ    . TYR   A 1 468  ? 116.238 174.802 181.562 1.00 62.62  ? 468  TYR   A CZ    1 
ATOM   1589  O  OH    . TYR   A 1 468  ? 116.267 174.245 180.305 1.00 67.28  ? 468  TYR   A OH    1 
ATOM   1590  N  N     . LYS   A 1 469  ? 118.396 176.512 188.446 1.00 63.41  ? 469  LYS   A N     1 
ATOM   1591  C  CA    . LYS   A 1 469  ? 118.950 177.423 189.439 1.00 61.54  ? 469  LYS   A CA    1 
ATOM   1592  C  C     . LYS   A 1 469  ? 120.361 177.816 189.021 1.00 61.50  ? 469  LYS   A C     1 
ATOM   1593  O  O     . LYS   A 1 469  ? 121.209 176.948 188.789 1.00 62.66  ? 469  LYS   A O     1 
ATOM   1594  C  CB    . LYS   A 1 469  ? 118.948 176.783 190.826 1.00 63.21  ? 469  LYS   A CB    1 
ATOM   1595  C  CG    . LYS   A 1 469  ? 117.581 176.783 191.483 1.00 64.55  ? 469  LYS   A CG    1 
ATOM   1596  C  CD    . LYS   A 1 469  ? 116.711 177.895 190.921 1.00 62.84  ? 469  LYS   A CD    1 
ATOM   1597  C  CE    . LYS   A 1 469  ? 115.421 178.036 191.709 1.00 63.83  ? 469  LYS   A CE    1 
ATOM   1598  N  NZ    . LYS   A 1 469  ? 114.542 176.845 191.550 1.00 61.86  ? 469  LYS   A NZ    1 
ATOM   1599  N  N     . SER   A 1 470  ? 120.606 179.126 188.926 1.00 64.47  ? 470  SER   A N     1 
ATOM   1600  C  CA    . SER   A 1 470  ? 121.898 179.612 188.454 1.00 64.45  ? 470  SER   A CA    1 
ATOM   1601  C  C     . SER   A 1 470  ? 123.047 179.090 189.305 1.00 64.95  ? 470  SER   A C     1 
ATOM   1602  O  O     . SER   A 1 470  ? 124.164 178.924 188.803 1.00 68.67  ? 470  SER   A O     1 
ATOM   1603  C  CB    . SER   A 1 470  ? 121.907 181.141 188.433 1.00 64.08  ? 470  SER   A CB    1 
ATOM   1604  O  OG    . SER   A 1 470  ? 120.857 181.644 187.627 1.00 69.28  ? 470  SER   A OG    1 
ATOM   1605  N  N     . GLU   A 1 471  ? 122.803 178.837 190.592 1.00 65.84  ? 471  GLU   A N     1 
ATOM   1606  C  CA    . GLU   A 1 471  ? 123.851 178.280 191.441 1.00 70.61  ? 471  GLU   A CA    1 
ATOM   1607  C  C     . GLU   A 1 471  ? 124.276 176.902 190.951 1.00 73.75  ? 471  GLU   A C     1 
ATOM   1608  O  O     . GLU   A 1 471  ? 125.472 176.586 190.921 1.00 75.03  ? 471  GLU   A O     1 
ATOM   1609  C  CB    . GLU   A 1 471  ? 123.372 178.214 192.890 1.00 71.22  ? 471  GLU   A CB    1 
ATOM   1610  C  CG    . GLU   A 1 471  ? 122.928 179.552 193.456 1.00 72.87  ? 471  GLU   A CG    1 
ATOM   1611  C  CD    . GLU   A 1 471  ? 121.423 179.647 193.598 1.00 76.45  ? 471  GLU   A CD    1 
ATOM   1612  O  OE1   . GLU   A 1 471  ? 120.720 178.784 193.034 1.00 75.30  ? 471  GLU   A OE1   1 
ATOM   1613  O  OE2   . GLU   A 1 471  ? 120.944 180.584 194.270 1.00 75.30  ? 471  GLU   A OE2   1 
ATOM   1614  N  N     . ILE   A 1 472  ? 123.310 176.071 190.556 1.00 66.33  ? 472  ILE   A N     1 
ATOM   1615  C  CA    . ILE   A 1 472  ? 123.634 174.754 190.017 1.00 58.53  ? 472  ILE   A CA    1 
ATOM   1616  C  C     . ILE   A 1 472  ? 124.468 174.890 188.751 1.00 63.42  ? 472  ILE   A C     1 
ATOM   1617  O  O     . ILE   A 1 472  ? 125.452 174.166 188.555 1.00 63.75  ? 472  ILE   A O     1 
ATOM   1618  C  CB    . ILE   A 1 472  ? 122.344 173.951 189.765 1.00 56.59  ? 472  ILE   A CB    1 
ATOM   1619  C  CG1   . ILE   A 1 472  ? 121.723 173.508 191.090 1.00 58.48  ? 472  ILE   A CG1   1 
ATOM   1620  C  CG2   . ILE   A 1 472  ? 122.629 172.749 188.890 1.00 63.22  ? 472  ILE   A CG2   1 
ATOM   1621  C  CD1   . ILE   A 1 472  ? 120.211 173.554 191.098 1.00 61.36  ? 472  ILE   A CD1   1 
ATOM   1622  N  N     . PHE   A 1 473  ? 124.088 175.817 187.868 1.00 62.58  ? 473  PHE   A N     1 
ATOM   1623  C  CA    . PHE   A 1 473  ? 124.861 176.043 186.651 1.00 59.60  ? 473  PHE   A CA    1 
ATOM   1624  C  C     . PHE   A 1 473  ? 126.293 176.443 186.980 1.00 64.74  ? 473  PHE   A C     1 
ATOM   1625  O  O     . PHE   A 1 473  ? 127.250 175.874 186.442 1.00 66.07  ? 473  PHE   A O     1 
ATOM   1626  C  CB    . PHE   A 1 473  ? 124.182 177.112 185.791 1.00 58.21  ? 473  PHE   A CB    1 
ATOM   1627  C  CG    . PHE   A 1 473  ? 124.980 177.524 184.584 1.00 61.41  ? 473  PHE   A CG    1 
ATOM   1628  C  CD1   . PHE   A 1 473  ? 125.971 178.487 184.682 1.00 61.04  ? 473  PHE   A CD1   1 
ATOM   1629  C  CD2   . PHE   A 1 473  ? 124.741 176.944 183.350 1.00 65.14  ? 473  PHE   A CD2   1 
ATOM   1630  C  CE1   . PHE   A 1 473  ? 126.706 178.862 183.575 1.00 62.65  ? 473  PHE   A CE1   1 
ATOM   1631  C  CE2   . PHE   A 1 473  ? 125.473 177.317 182.239 1.00 64.82  ? 473  PHE   A CE2   1 
ATOM   1632  C  CZ    . PHE   A 1 473  ? 126.457 178.277 182.352 1.00 63.38  ? 473  PHE   A CZ    1 
ATOM   1633  N  N     . ASN   A 1 474  ? 126.461 177.426 187.868 1.00 68.16  ? 474  ASN   A N     1 
ATOM   1634  C  CA    . ASN   A 1 474  ? 127.802 177.880 188.219 1.00 62.14  ? 474  ASN   A CA    1 
ATOM   1635  C  C     . ASN   A 1 474  ? 128.616 176.770 188.869 1.00 62.00  ? 474  ASN   A C     1 
ATOM   1636  O  O     . ASN   A 1 474  ? 129.841 176.722 188.704 1.00 67.69  ? 474  ASN   A O     1 
ATOM   1637  C  CB    . ASN   A 1 474  ? 127.720 179.095 189.143 1.00 64.46  ? 474  ASN   A CB    1 
ATOM   1638  C  CG    . ASN   A 1 474  ? 127.099 180.301 188.465 1.00 68.40  ? 474  ASN   A CG    1 
ATOM   1639  O  OD1   . ASN   A 1 474  ? 126.049 180.791 188.880 1.00 70.18  ? 474  ASN   A OD1   1 
ATOM   1640  N  ND2   . ASN   A 1 474  ? 127.749 180.787 187.414 1.00 67.25  ? 474  ASN   A ND2   1 
ATOM   1641  N  N     . GLU   A 1 475  ? 127.962 175.872 189.604 1.00 59.00  ? 475  GLU   A N     1 
ATOM   1642  C  CA    . GLU   A 1 475  ? 128.667 174.764 190.233 1.00 63.11  ? 475  GLU   A CA    1 
ATOM   1643  C  C     . GLU   A 1 475  ? 128.962 173.624 189.268 1.00 67.54  ? 475  GLU   A C     1 
ATOM   1644  O  O     . GLU   A 1 475  ? 129.846 172.809 189.550 1.00 68.70  ? 475  GLU   A O     1 
ATOM   1645  C  CB    . GLU   A 1 475  ? 127.861 174.232 191.420 1.00 60.61  ? 475  GLU   A CB    1 
ATOM   1646  N  N     . ASN   A 1 476  ? 128.255 173.546 188.142 1.00 64.84  ? 476  ASN   A N     1 
ATOM   1647  C  CA    . ASN   A 1 476  ? 128.410 172.427 187.221 1.00 57.03  ? 476  ASN   A CA    1 
ATOM   1648  C  C     . ASN   A 1 476  ? 129.447 172.671 186.134 1.00 60.39  ? 476  ASN   A C     1 
ATOM   1649  O  O     . ASN   A 1 476  ? 129.694 171.769 185.326 1.00 70.26  ? 476  ASN   A O     1 
ATOM   1650  C  CB    . ASN   A 1 476  ? 127.066 172.071 186.583 1.00 56.01  ? 476  ASN   A CB    1 
ATOM   1651  C  CG    . ASN   A 1 476  ? 126.278 171.080 187.414 1.00 59.68  ? 476  ASN   A CG    1 
ATOM   1652  O  OD1   . ASN   A 1 476  ? 126.754 169.984 187.707 1.00 58.61  ? 476  ASN   A OD1   1 
ATOM   1653  N  ND2   . ASN   A 1 476  ? 125.070 171.462 187.801 1.00 61.38  ? 476  ASN   A ND2   1 
ATOM   1654  N  N     . PHE   A 1 477  ? 130.052 173.853 186.082 1.00 60.25  ? 477  PHE   A N     1 
ATOM   1655  C  CA    . PHE   A 1 477  ? 131.239 174.019 185.263 1.00 52.71  ? 477  PHE   A CA    1 
ATOM   1656  C  C     . PHE   A 1 477  ? 132.380 173.176 185.831 1.00 52.79  ? 477  PHE   A C     1 
ATOM   1657  O  O     . PHE   A 1 477  ? 132.287 172.604 186.920 1.00 60.89  ? 477  PHE   A O     1 
ATOM   1658  C  CB    . PHE   A 1 477  ? 131.641 175.492 185.192 1.00 55.64  ? 477  PHE   A CB    1 
ATOM   1659  C  CG    . PHE   A 1 477  ? 131.305 176.150 183.885 1.00 51.74  ? 477  PHE   A CG    1 
ATOM   1660  C  CD1   . PHE   A 1 477  ? 130.016 176.575 183.623 1.00 54.21  ? 477  PHE   A CD1   1 
ATOM   1661  C  CD2   . PHE   A 1 477  ? 132.281 176.354 182.925 1.00 54.75  ? 477  PHE   A CD2   1 
ATOM   1662  C  CE1   . PHE   A 1 477  ? 129.703 177.183 182.423 1.00 61.44  ? 477  PHE   A CE1   1 
ATOM   1663  C  CE2   . PHE   A 1 477  ? 131.973 176.963 181.723 1.00 56.77  ? 477  PHE   A CE2   1 
ATOM   1664  C  CZ    . PHE   A 1 477  ? 130.683 177.378 181.473 1.00 58.49  ? 477  PHE   A CZ    1 
ATOM   1665  N  N     . GLY   A 1 478  ? 133.464 173.089 185.071 1.00 42.91  ? 478  GLY   A N     1 
ATOM   1666  C  CA    . GLY   A 1 478  ? 134.644 172.392 185.521 1.00 49.28  ? 478  GLY   A CA    1 
ATOM   1667  C  C     . GLY   A 1 478  ? 134.496 170.885 185.493 1.00 48.18  ? 478  GLY   A C     1 
ATOM   1668  O  O     . GLY   A 1 478  ? 133.401 170.334 185.641 1.00 50.94  ? 478  GLY   A O     1 
ATOM   1669  N  N     . PRO   A 1 479  ? 135.616 170.188 185.311 1.00 51.37  ? 479  PRO   A N     1 
ATOM   1670  C  CA    . PRO   A 1 479  ? 135.643 168.712 185.200 1.00 55.52  ? 479  PRO   A CA    1 
ATOM   1671  C  C     . PRO   A 1 479  ? 135.750 167.971 186.534 1.00 57.66  ? 479  PRO   A C     1 
ATOM   1672  O  O     . PRO   A 1 479  ? 136.823 167.589 187.004 1.00 63.03  ? 479  PRO   A O     1 
ATOM   1673  C  CB    . PRO   A 1 479  ? 136.876 168.463 184.328 1.00 57.11  ? 479  PRO   A CB    1 
ATOM   1674  C  CG    . PRO   A 1 479  ? 137.684 169.753 184.355 1.00 60.32  ? 479  PRO   A CG    1 
ATOM   1675  C  CD    . PRO   A 1 479  ? 136.961 170.766 185.189 1.00 58.56  ? 479  PRO   A CD    1 
ATOM   1676  N  N     . ASP   A 1 480  ? 134.601 167.761 187.176 1.00 51.70  ? 480  ASP   A N     1 
ATOM   1677  C  CA    . ASP   A 1 480  ? 134.548 167.053 188.454 1.00 54.94  ? 480  ASP   A CA    1 
ATOM   1678  C  C     . ASP   A 1 480  ? 134.494 165.555 188.154 1.00 55.74  ? 480  ASP   A C     1 
ATOM   1679  O  O     . ASP   A 1 480  ? 133.441 164.914 188.178 1.00 63.57  ? 480  ASP   A O     1 
ATOM   1680  C  CB    . ASP   A 1 480  ? 133.350 167.526 189.271 1.00 60.20  ? 480  ASP   A CB    1 
ATOM   1681  C  CG    . ASP   A 1 480  ? 133.167 166.752 190.568 1.00 65.33  ? 480  ASP   A CG    1 
ATOM   1682  O  OD1   . ASP   A 1 480  ? 132.582 167.325 191.511 1.00 65.92  ? 480  ASP   A OD1   1 
ATOM   1683  O  OD2   . ASP   A 1 480  ? 133.616 165.593 190.665 1.00 62.85  ? 480  ASP   A OD2   1 
ATOM   1684  N  N     . PHE   A 1 481  ? 135.665 164.991 187.861 1.00 53.77  ? 481  PHE   A N     1 
ATOM   1685  C  CA    . PHE   A 1 481  ? 135.797 163.578 187.505 1.00 55.19  ? 481  PHE   A CA    1 
ATOM   1686  C  C     . PHE   A 1 481  ? 135.875 162.745 188.781 1.00 60.57  ? 481  PHE   A C     1 
ATOM   1687  O  O     . PHE   A 1 481  ? 136.937 162.633 189.398 1.00 65.88  ? 481  PHE   A O     1 
ATOM   1688  C  CB    . PHE   A 1 481  ? 137.027 163.358 186.631 1.00 58.27  ? 481  PHE   A CB    1 
ATOM   1689  C  CG    . PHE   A 1 481  ? 136.995 164.109 185.329 1.00 60.71  ? 481  PHE   A CG    1 
ATOM   1690  C  CD1   . PHE   A 1 481  ? 135.883 164.057 184.508 1.00 62.53  ? 481  PHE   A CD1   1 
ATOM   1691  C  CD2   . PHE   A 1 481  ? 138.084 164.858 184.921 1.00 60.94  ? 481  PHE   A CD2   1 
ATOM   1692  C  CE1   . PHE   A 1 481  ? 135.856 164.743 183.308 1.00 59.38  ? 481  PHE   A CE1   1 
ATOM   1693  C  CE2   . PHE   A 1 481  ? 138.063 165.544 183.723 1.00 60.75  ? 481  PHE   A CE2   1 
ATOM   1694  C  CZ    . PHE   A 1 481  ? 136.947 165.487 182.916 1.00 56.64  ? 481  PHE   A CZ    1 
ATOM   1695  N  N     . ARG   A 1 482  ? 134.753 162.152 189.177 1.00 62.91  ? 482  ARG   A N     1 
ATOM   1696  C  CA    . ARG   A 1 482  ? 134.700 161.308 190.373 1.00 68.88  ? 482  ARG   A CA    1 
ATOM   1697  C  C     . ARG   A 1 482  ? 134.845 159.831 190.008 1.00 68.72  ? 482  ARG   A C     1 
ATOM   1698  O  O     . ARG   A 1 482  ? 133.951 159.017 190.240 1.00 68.44  ? 482  ARG   A O     1 
ATOM   1699  C  CB    . ARG   A 1 482  ? 133.402 161.550 191.135 1.00 65.05  ? 482  ARG   A CB    1 
ATOM   1700  C  CG    . ARG   A 1 482  ? 133.139 162.989 191.519 1.00 62.34  ? 482  ARG   A CG    1 
ATOM   1701  C  CD    . ARG   A 1 482  ? 132.246 163.067 192.749 1.00 63.32  ? 482  ARG   A CD    1 
ATOM   1702  N  NE    . ARG   A 1 482  ? 130.944 162.446 192.524 1.00 67.71  ? 482  ARG   A NE    1 
ATOM   1703  C  CZ    . ARG   A 1 482  ? 130.686 161.157 192.698 1.00 68.85  ? 482  ARG   A CZ    1 
ATOM   1704  N  NH1   . ARG   A 1 482  ? 131.619 160.312 193.105 1.00 68.86  ? 482  ARG   A NH1   1 
ATOM   1705  N  NH2   . ARG   A 1 482  ? 129.458 160.703 192.461 1.00 70.52  ? 482  ARG   A NH2   1 
ATOM   1706  N  N     . GLU   A 1 483  ? 135.993 159.481 189.429 1.00 62.81  ? 483  GLU   A N     1 
ATOM   1707  C  CA    . GLU   A 1 483  ? 136.251 158.083 189.105 1.00 67.70  ? 483  GLU   A CA    1 
ATOM   1708  C  C     . GLU   A 1 483  ? 137.660 157.876 188.567 1.00 71.15  ? 483  GLU   A C     1 
ATOM   1709  O  O     . GLU   A 1 483  ? 138.420 158.836 188.403 1.00 72.17  ? 483  GLU   A O     1 
ATOM   1710  C  CB    . GLU   A 1 483  ? 135.226 157.573 188.090 1.00 70.51  ? 483  GLU   A CB    1 
ATOM   1711  N  N     . GLU   A 1 484  ? 138.014 156.621 188.291 1.00 74.09  ? 484  GLU   A N     1 
ATOM   1712  C  CA    . GLU   A 1 484  ? 139.282 156.312 187.645 1.00 74.89  ? 484  GLU   A CA    1 
ATOM   1713  C  C     . GLU   A 1 484  ? 139.154 156.539 186.146 1.00 76.72  ? 484  GLU   A C     1 
ATOM   1714  O  O     . GLU   A 1 484  ? 139.441 155.645 185.344 1.00 79.86  ? 484  GLU   A O     1 
ATOM   1715  C  CB    . GLU   A 1 484  ? 139.704 154.871 187.941 1.00 74.50  ? 484  GLU   A CB    1 
ATOM   1716  N  N     . GLU   A 1 485  ? 138.720 157.739 185.765 1.00 70.56  ? 485  GLU   A N     1 
ATOM   1717  C  CA    . GLU   A 1 485  ? 138.507 158.102 184.374 1.00 70.29  ? 485  GLU   A CA    1 
ATOM   1718  C  C     . GLU   A 1 485  ? 139.048 159.508 184.157 1.00 69.81  ? 485  GLU   A C     1 
ATOM   1719  O  O     . GLU   A 1 485  ? 139.483 160.180 185.098 1.00 71.49  ? 485  GLU   A O     1 
ATOM   1720  C  CB    . GLU   A 1 485  ? 137.023 157.984 183.998 1.00 67.05  ? 485  GLU   A CB    1 
ATOM   1721  C  CG    . GLU   A 1 485  ? 136.081 158.887 184.788 1.00 67.18  ? 485  GLU   A CG    1 
ATOM   1722  C  CD    . GLU   A 1 485  ? 136.173 160.347 184.389 1.00 71.39  ? 485  GLU   A CD    1 
ATOM   1723  O  OE1   . GLU   A 1 485  ? 136.636 160.634 183.266 1.00 71.48  ? 485  GLU   A OE1   1 
ATOM   1724  O  OE2   . GLU   A 1 485  ? 135.783 161.208 185.202 1.00 77.11  ? 485  GLU   A OE2   1 
ATOM   1725  N  N     . THR   A 1 486  ? 139.016 159.960 182.908 1.00 63.61  ? 486  THR   A N     1 
ATOM   1726  C  CA    . THR   A 1 486  ? 139.571 161.260 182.558 1.00 61.06  ? 486  THR   A CA    1 
ATOM   1727  C  C     . THR   A 1 486  ? 138.777 161.836 181.392 1.00 62.60  ? 486  THR   A C     1 
ATOM   1728  O  O     . THR   A 1 486  ? 137.786 161.257 180.939 1.00 65.41  ? 486  THR   A O     1 
ATOM   1729  C  CB    . THR   A 1 486  ? 141.059 161.153 182.217 1.00 66.56  ? 486  THR   A CB    1 
ATOM   1730  O  OG1   . THR   A 1 486  ? 141.521 162.404 181.693 1.00 67.55  ? 486  THR   A OG1   1 
ATOM   1731  C  CG2   . THR   A 1 486  ? 141.291 160.058 181.188 1.00 66.32  ? 486  THR   A CG2   1 
ATOM   1732  N  N     . PHE   A 1 487  ? 139.230 162.994 180.909 1.00 57.35  ? 487  PHE   A N     1 
ATOM   1733  C  CA    . PHE   A 1 487  ? 138.557 163.659 179.798 1.00 57.39  ? 487  PHE   A CA    1 
ATOM   1734  C  C     . PHE   A 1 487  ? 138.473 162.748 178.580 1.00 57.32  ? 487  PHE   A C     1 
ATOM   1735  O  O     . PHE   A 1 487  ? 137.414 162.625 177.952 1.00 58.64  ? 487  PHE   A O     1 
ATOM   1736  C  CB    . PHE   A 1 487  ? 139.292 164.955 179.456 1.00 54.54  ? 487  PHE   A CB    1 
ATOM   1737  C  CG    . PHE   A 1 487  ? 138.718 165.690 178.281 1.00 54.21  ? 487  PHE   A CG    1 
ATOM   1738  C  CD1   . PHE   A 1 487  ? 139.153 165.418 176.996 1.00 55.67  ? 487  PHE   A CD1   1 
ATOM   1739  C  CD2   . PHE   A 1 487  ? 137.748 166.659 178.463 1.00 57.68  ? 487  PHE   A CD2   1 
ATOM   1740  C  CE1   . PHE   A 1 487  ? 138.628 166.096 175.915 1.00 56.84  ? 487  PHE   A CE1   1 
ATOM   1741  C  CE2   . PHE   A 1 487  ? 137.220 167.340 177.385 1.00 58.69  ? 487  PHE   A CE2   1 
ATOM   1742  C  CZ    . PHE   A 1 487  ? 137.661 167.058 176.110 1.00 55.27  ? 487  PHE   A CZ    1 
ATOM   1743  N  N     . PHE   A 1 488  ? 139.587 162.105 178.225 1.00 58.22  ? 488  PHE   A N     1 
ATOM   1744  C  CA    . PHE   A 1 488  ? 139.594 161.248 177.045 1.00 57.26  ? 488  PHE   A CA    1 
ATOM   1745  C  C     . PHE   A 1 488  ? 138.652 160.065 177.206 1.00 59.18  ? 488  PHE   A C     1 
ATOM   1746  O  O     . PHE   A 1 488  ? 138.073 159.598 176.221 1.00 67.06  ? 488  PHE   A O     1 
ATOM   1747  C  CB    . PHE   A 1 488  ? 141.016 160.771 176.752 1.00 60.65  ? 488  PHE   A CB    1 
ATOM   1748  C  CG    . PHE   A 1 488  ? 141.882 161.819 176.115 1.00 65.56  ? 488  PHE   A CG    1 
ATOM   1749  C  CD1   . PHE   A 1 488  ? 141.334 163.015 175.682 1.00 62.37  ? 488  PHE   A CD1   1 
ATOM   1750  C  CD2   . PHE   A 1 488  ? 143.241 161.614 175.952 1.00 64.78  ? 488  PHE   A CD2   1 
ATOM   1751  C  CE1   . PHE   A 1 488  ? 142.123 163.985 175.097 1.00 60.98  ? 488  PHE   A CE1   1 
ATOM   1752  C  CE2   . PHE   A 1 488  ? 144.036 162.582 175.366 1.00 63.51  ? 488  PHE   A CE2   1 
ATOM   1753  C  CZ    . PHE   A 1 488  ? 143.476 163.769 174.939 1.00 63.89  ? 488  PHE   A CZ    1 
ATOM   1754  N  N     . SER   A 1 489  ? 138.477 159.568 178.432 1.00 49.04  ? 489  SER   A N     1 
ATOM   1755  C  CA    . SER   A 1 489  ? 137.509 158.499 178.652 1.00 53.64  ? 489  SER   A CA    1 
ATOM   1756  C  C     . SER   A 1 489  ? 136.092 158.973 178.350 1.00 57.08  ? 489  SER   A C     1 
ATOM   1757  O  O     . SER   A 1 489  ? 135.304 158.252 177.726 1.00 55.71  ? 489  SER   A O     1 
ATOM   1758  C  CB    . SER   A 1 489  ? 137.612 157.984 180.087 1.00 56.38  ? 489  SER   A CB    1 
ATOM   1759  O  OG    . SER   A 1 489  ? 137.683 156.570 180.116 1.00 59.15  ? 489  SER   A OG    1 
ATOM   1760  N  N     . VAL   A 1 490  ? 135.754 160.192 178.775 1.00 55.52  ? 490  VAL   A N     1 
ATOM   1761  C  CA    . VAL   A 1 490  ? 134.436 160.743 178.478 1.00 54.46  ? 490  VAL   A CA    1 
ATOM   1762  C  C     . VAL   A 1 490  ? 134.269 160.944 176.978 1.00 55.23  ? 490  VAL   A C     1 
ATOM   1763  O  O     . VAL   A 1 490  ? 133.203 160.666 176.414 1.00 54.18  ? 490  VAL   A O     1 
ATOM   1764  C  CB    . VAL   A 1 490  ? 134.220 162.055 179.254 1.00 52.91  ? 490  VAL   A CB    1 
ATOM   1765  C  CG1   . VAL   A 1 490  ? 132.857 162.645 178.930 1.00 48.32  ? 490  VAL   A CG1   1 
ATOM   1766  C  CG2   . VAL   A 1 490  ? 134.360 161.814 180.747 1.00 53.77  ? 490  VAL   A CG2   1 
ATOM   1767  N  N     . PHE   A 1 491  ? 135.312 161.441 176.310 1.00 52.65  ? 491  PHE   A N     1 
ATOM   1768  C  CA    . PHE   A 1 491  ? 135.243 161.603 174.862 1.00 50.24  ? 491  PHE   A CA    1 
ATOM   1769  C  C     . PHE   A 1 491  ? 135.013 160.266 174.171 1.00 51.31  ? 491  PHE   A C     1 
ATOM   1770  O  O     . PHE   A 1 491  ? 134.203 160.170 173.243 1.00 53.96  ? 491  PHE   A O     1 
ATOM   1771  C  CB    . PHE   A 1 491  ? 136.520 162.265 174.344 1.00 48.79  ? 491  PHE   A CB    1 
ATOM   1772  C  CG    . PHE   A 1 491  ? 136.485 162.584 172.876 1.00 54.52  ? 491  PHE   A CG    1 
ATOM   1773  C  CD1   . PHE   A 1 491  ? 136.821 161.623 171.937 1.00 55.09  ? 491  PHE   A CD1   1 
ATOM   1774  C  CD2   . PHE   A 1 491  ? 136.109 163.840 172.434 1.00 54.23  ? 491  PHE   A CD2   1 
ATOM   1775  C  CE1   . PHE   A 1 491  ? 136.788 161.911 170.587 1.00 52.66  ? 491  PHE   A CE1   1 
ATOM   1776  C  CE2   . PHE   A 1 491  ? 136.074 164.133 171.084 1.00 48.31  ? 491  PHE   A CE2   1 
ATOM   1777  C  CZ    . PHE   A 1 491  ? 136.414 163.168 170.160 1.00 48.51  ? 491  PHE   A CZ    1 
ATOM   1778  N  N     . ALA   A 1 492  ? 135.725 159.224 174.604 1.00 45.83  ? 492  ALA   A N     1 
ATOM   1779  C  CA    . ALA   A 1 492  ? 135.550 157.906 174.004 1.00 39.53  ? 492  ALA   A CA    1 
ATOM   1780  C  C     . ALA   A 1 492  ? 134.147 157.373 174.252 1.00 42.17  ? 492  ALA   A C     1 
ATOM   1781  O  O     . ALA   A 1 492  ? 133.556 156.728 173.379 1.00 52.95  ? 492  ALA   A O     1 
ATOM   1782  C  CB    . ALA   A 1 492  ? 136.597 156.938 174.553 1.00 41.04  ? 492  ALA   A CB    1 
ATOM   1783  N  N     . ILE   A 1 493  ? 133.599 157.627 175.441 1.00 44.04  ? 493  ILE   A N     1 
ATOM   1784  C  CA    . ILE   A 1 493  ? 132.251 157.160 175.744 1.00 44.58  ? 493  ILE   A CA    1 
ATOM   1785  C  C     . ILE   A 1 493  ? 131.229 157.871 174.866 1.00 49.38  ? 493  ILE   A C     1 
ATOM   1786  O  O     . ILE   A 1 493  ? 130.284 157.250 174.364 1.00 49.78  ? 493  ILE   A O     1 
ATOM   1787  C  CB    . ILE   A 1 493  ? 131.941 157.350 177.240 1.00 52.87  ? 493  ILE   A CB    1 
ATOM   1788  C  CG1   . ILE   A 1 493  ? 132.877 156.495 178.095 1.00 52.95  ? 493  ILE   A CG1   1 
ATOM   1789  C  CG2   . ILE   A 1 493  ? 130.489 157.003 177.533 1.00 47.44  ? 493  ILE   A CG2   1 
ATOM   1790  C  CD1   . ILE   A 1 493  ? 133.256 155.181 177.457 1.00 54.06  ? 493  ILE   A CD1   1 
ATOM   1791  N  N     . PHE   A 1 494  ? 131.397 159.179 174.666 1.00 43.35  ? 494  PHE   A N     1 
ATOM   1792  C  CA    . PHE   A 1 494  ? 130.377 159.950 173.963 1.00 36.05  ? 494  PHE   A CA    1 
ATOM   1793  C  C     . PHE   A 1 494  ? 130.473 159.807 172.447 1.00 42.78  ? 494  PHE   A C     1 
ATOM   1794  O  O     . PHE   A 1 494  ? 129.443 159.794 171.765 1.00 48.14  ? 494  PHE   A O     1 
ATOM   1795  C  CB    . PHE   A 1 494  ? 130.466 161.426 174.353 1.00 34.13  ? 494  PHE   A CB    1 
ATOM   1796  C  CG    . PHE   A 1 494  ? 129.609 162.323 173.506 1.00 41.08  ? 494  PHE   A CG    1 
ATOM   1797  C  CD1   . PHE   A 1 494  ? 128.278 162.531 173.820 1.00 42.95  ? 494  PHE   A CD1   1 
ATOM   1798  C  CD2   . PHE   A 1 494  ? 130.133 162.953 172.389 1.00 42.96  ? 494  PHE   A CD2   1 
ATOM   1799  C  CE1   . PHE   A 1 494  ? 127.487 163.351 173.039 1.00 40.36  ? 494  PHE   A CE1   1 
ATOM   1800  C  CE2   . PHE   A 1 494  ? 129.346 163.772 171.606 1.00 42.90  ? 494  PHE   A CE2   1 
ATOM   1801  C  CZ    . PHE   A 1 494  ? 128.022 163.972 171.932 1.00 39.76  ? 494  PHE   A CZ    1 
ATOM   1802  N  N     . PHE   A 1 495  ? 131.682 159.697 171.901 1.00 43.66  ? 495  PHE   A N     1 
ATOM   1803  C  CA    . PHE   A 1 495  ? 131.860 159.838 170.458 1.00 36.88  ? 495  PHE   A CA    1 
ATOM   1804  C  C     . PHE   A 1 495  ? 130.946 158.945 169.629 1.00 42.08  ? 495  PHE   A C     1 
ATOM   1805  O  O     . PHE   A 1 495  ? 130.394 159.436 168.631 1.00 42.62  ? 495  PHE   A O     1 
ATOM   1806  C  CB    . PHE   A 1 495  ? 133.327 159.579 170.086 1.00 35.89  ? 495  PHE   A CB    1 
ATOM   1807  C  CG    . PHE   A 1 495  ? 133.616 159.753 168.624 1.00 44.43  ? 495  PHE   A CG    1 
ATOM   1808  C  CD1   . PHE   A 1 495  ? 133.819 161.017 168.096 1.00 43.61  ? 495  PHE   A CD1   1 
ATOM   1809  C  CD2   . PHE   A 1 495  ? 133.672 158.662 167.775 1.00 42.21  ? 495  PHE   A CD2   1 
ATOM   1810  C  CE1   . PHE   A 1 495  ? 134.081 161.188 166.752 1.00 41.25  ? 495  PHE   A CE1   1 
ATOM   1811  C  CE2   . PHE   A 1 495  ? 133.933 158.828 166.429 1.00 41.42  ? 495  PHE   A CE2   1 
ATOM   1812  C  CZ    . PHE   A 1 495  ? 134.138 160.093 165.918 1.00 43.27  ? 495  PHE   A CZ    1 
ATOM   1813  N  N     . PRO   A 1 496  ? 130.746 157.665 169.955 1.00 44.87  ? 496  PRO   A N     1 
ATOM   1814  C  CA    . PRO   A 1 496  ? 129.857 156.831 169.133 1.00 40.06  ? 496  PRO   A CA    1 
ATOM   1815  C  C     . PRO   A 1 496  ? 128.475 157.440 168.948 1.00 37.05  ? 496  PRO   A C     1 
ATOM   1816  O  O     . PRO   A 1 496  ? 127.757 157.084 168.010 1.00 37.03  ? 496  PRO   A O     1 
ATOM   1817  C  CB    . PRO   A 1 496  ? 129.788 155.513 169.912 1.00 38.63  ? 496  PRO   A CB    1 
ATOM   1818  C  CG    . PRO   A 1 496  ? 131.024 155.484 170.728 1.00 39.55  ? 496  PRO   A CG    1 
ATOM   1819  C  CD    . PRO   A 1 496  ? 131.373 156.904 171.048 1.00 40.02  ? 496  PRO   A CD    1 
ATOM   1820  N  N     . ALA   A 1 497  ? 128.094 158.363 169.834 1.00 45.95  ? 497  ALA   A N     1 
ATOM   1821  C  CA    . ALA   A 1 497  ? 126.807 159.033 169.701 1.00 42.15  ? 497  ALA   A CA    1 
ATOM   1822  C  C     . ALA   A 1 497  ? 126.771 159.988 168.515 1.00 44.64  ? 497  ALA   A C     1 
ATOM   1823  O  O     . ALA   A 1 497  ? 125.683 160.383 168.086 1.00 48.31  ? 497  ALA   A O     1 
ATOM   1824  C  CB    . ALA   A 1 497  ? 126.470 159.786 170.988 1.00 41.03  ? 497  ALA   A CB    1 
ATOM   1825  N  N     . ALA   A 1 498  ? 127.930 160.369 167.982 1.00 39.21  ? 498  ALA   A N     1 
ATOM   1826  C  CA    . ALA   A 1 498  ? 127.993 161.231 166.811 1.00 31.90  ? 498  ALA   A CA    1 
ATOM   1827  C  C     . ALA   A 1 498  ? 127.999 160.457 165.500 1.00 38.94  ? 498  ALA   A C     1 
ATOM   1828  O  O     . ALA   A 1 498  ? 127.874 161.071 164.436 1.00 44.03  ? 498  ALA   A O     1 
ATOM   1829  C  CB    . ALA   A 1 498  ? 129.236 162.125 166.879 1.00 32.86  ? 498  ALA   A CB    1 
ATOM   1830  N  N     . THR   A 1 499  ? 128.132 159.135 165.550 1.00 38.49  ? 499  THR   A N     1 
ATOM   1831  C  CA    . THR   A 1 499  ? 128.205 158.319 164.346 1.00 35.22  ? 499  THR   A CA    1 
ATOM   1832  C  C     . THR   A 1 499  ? 126.800 158.110 163.782 1.00 43.08  ? 499  THR   A C     1 
ATOM   1833  O  O     . THR   A 1 499  ? 125.835 158.761 164.191 1.00 48.42  ? 499  THR   A O     1 
ATOM   1834  C  CB    . THR   A 1 499  ? 128.906 156.997 164.644 1.00 38.17  ? 499  THR   A CB    1 
ATOM   1835  O  OG1   . THR   A 1 499  ? 128.156 156.264 165.619 1.00 48.89  ? 499  THR   A OG1   1 
ATOM   1836  C  CG2   . THR   A 1 499  ? 130.308 157.247 165.173 1.00 40.79  ? 499  THR   A CG2   1 
ATOM   1837  N  N     . GLY   A 1 500  ? 126.673 157.191 162.828 1.00 46.64  ? 500  GLY   A N     1 
ATOM   1838  C  CA    . GLY   A 1 500  ? 125.402 156.966 162.168 1.00 44.39  ? 500  GLY   A CA    1 
ATOM   1839  C  C     . GLY   A 1 500  ? 125.038 158.001 161.131 1.00 39.98  ? 500  GLY   A C     1 
ATOM   1840  O  O     . GLY   A 1 500  ? 123.855 158.155 160.814 1.00 36.97  ? 500  GLY   A O     1 
ATOM   1841  N  N     . ILE   A 1 501  ? 126.024 158.718 160.585 1.00 35.58  ? 501  ILE   A N     1 
ATOM   1842  C  CA    . ILE   A 1 501  ? 125.748 159.793 159.635 1.00 31.33  ? 501  ILE   A CA    1 
ATOM   1843  C  C     . ILE   A 1 501  ? 125.597 159.309 158.203 1.00 36.94  ? 501  ILE   A C     1 
ATOM   1844  O  O     . ILE   A 1 501  ? 125.260 160.113 157.325 1.00 44.78  ? 501  ILE   A O     1 
ATOM   1845  C  CB    . ILE   A 1 501  ? 126.860 160.856 159.689 1.00 30.35  ? 501  ILE   A CB    1 
ATOM   1846  C  CG1   . ILE   A 1 501  ? 128.206 160.237 159.310 1.00 35.58  ? 501  ILE   A CG1   1 
ATOM   1847  C  CG2   . ILE   A 1 501  ? 126.933 161.475 161.073 1.00 37.50  ? 501  ILE   A CG2   1 
ATOM   1848  C  CD1   . ILE   A 1 501  ? 128.996 161.052 158.314 1.00 37.69  ? 501  ILE   A CD1   1 
ATOM   1849  N  N     . LEU   A 1 502  ? 125.835 158.026 157.937 1.00 32.41  ? 502  LEU   A N     1 
ATOM   1850  C  CA    . LEU   A 1 502  ? 125.752 157.478 156.590 1.00 36.90  ? 502  LEU   A CA    1 
ATOM   1851  C  C     . LEU   A 1 502  ? 124.483 156.669 156.356 1.00 36.98  ? 502  LEU   A C     1 
ATOM   1852  O  O     . LEU   A 1 502  ? 124.394 155.954 155.354 1.00 43.27  ? 502  LEU   A O     1 
ATOM   1853  C  CB    . LEU   A 1 502  ? 126.981 156.616 156.294 1.00 37.86  ? 502  LEU   A CB    1 
ATOM   1854  C  CG    . LEU   A 1 502  ? 128.333 157.330 156.290 1.00 34.84  ? 502  LEU   A CG    1 
ATOM   1855  C  CD1   . LEU   A 1 502  ? 129.461 156.344 156.044 1.00 34.59  ? 502  LEU   A CD1   1 
ATOM   1856  C  CD2   . LEU   A 1 502  ? 128.352 158.431 155.247 1.00 31.61  ? 502  LEU   A CD2   1 
ATOM   1857  N  N     . ALA   A 1 503  ? 123.499 156.765 157.253 1.00 42.65  ? 503  ALA   A N     1 
ATOM   1858  C  CA    . ALA   A 1 503  ? 122.275 155.987 157.090 1.00 39.20  ? 503  ALA   A CA    1 
ATOM   1859  C  C     . ALA   A 1 503  ? 121.540 156.363 155.809 1.00 42.90  ? 503  ALA   A C     1 
ATOM   1860  O  O     . ALA   A 1 503  ? 121.071 155.486 155.074 1.00 42.06  ? 503  ALA   A O     1 
ATOM   1861  C  CB    . ALA   A 1 503  ? 121.369 156.177 158.305 1.00 37.61  ? 503  ALA   A CB    1 
ATOM   1862  N  N     . GLY   A 1 504  ? 121.429 157.661 155.521 1.00 44.00  ? 504  GLY   A N     1 
ATOM   1863  C  CA    . GLY   A 1 504  ? 120.719 158.085 154.327 1.00 39.50  ? 504  GLY   A CA    1 
ATOM   1864  C  C     . GLY   A 1 504  ? 121.439 157.738 153.040 1.00 42.87  ? 504  GLY   A C     1 
ATOM   1865  O  O     . GLY   A 1 504  ? 120.799 157.507 152.010 1.00 46.82  ? 504  GLY   A O     1 
ATOM   1866  N  N     . ALA   A 1 505  ? 122.771 157.692 153.075 1.00 46.88  ? 505  ALA   A N     1 
ATOM   1867  C  CA    . ALA   A 1 505  ? 123.545 157.321 151.899 1.00 45.61  ? 505  ALA   A CA    1 
ATOM   1868  C  C     . ALA   A 1 505  ? 123.684 155.816 151.735 1.00 41.44  ? 505  ALA   A C     1 
ATOM   1869  O  O     . ALA   A 1 505  ? 124.246 155.367 150.731 1.00 47.55  ? 505  ALA   A O     1 
ATOM   1870  C  CB    . ALA   A 1 505  ? 124.935 157.958 151.958 1.00 41.99  ? 505  ALA   A CB    1 
ATOM   1871  N  N     . ASN   A 1 506  ? 123.192 155.030 152.691 1.00 37.34  ? 506  ASN   A N     1 
ATOM   1872  C  CA    . ASN   A 1 506  ? 123.253 153.580 152.589 1.00 38.17  ? 506  ASN   A CA    1 
ATOM   1873  C  C     . ASN   A 1 506  ? 122.142 153.008 151.722 1.00 40.86  ? 506  ASN   A C     1 
ATOM   1874  O  O     . ASN   A 1 506  ? 122.217 151.836 151.337 1.00 47.37  ? 506  ASN   A O     1 
ATOM   1875  C  CB    . ASN   A 1 506  ? 123.193 152.958 153.985 1.00 44.94  ? 506  ASN   A CB    1 
ATOM   1876  C  CG    . ASN   A 1 506  ? 124.565 152.751 154.587 1.00 52.38  ? 506  ASN   A CG    1 
ATOM   1877  O  OD1   . ASN   A 1 506  ? 125.440 153.608 154.472 1.00 49.28  ? 506  ASN   A OD1   1 
ATOM   1878  N  ND2   . ASN   A 1 506  ? 124.758 151.616 155.246 1.00 55.21  ? 506  ASN   A ND2   1 
ATOM   1879  N  N     . ILE   A 1 507  ? 121.126 153.806 151.402 1.00 41.05  ? 507  ILE   A N     1 
ATOM   1880  C  CA    . ILE   A 1 507  ? 120.013 153.368 150.568 1.00 44.21  ? 507  ILE   A CA    1 
ATOM   1881  C  C     . ILE   A 1 507  ? 120.002 154.193 149.289 1.00 45.69  ? 507  ILE   A C     1 
ATOM   1882  O  O     . ILE   A 1 507  ? 118.937 154.480 148.732 1.00 45.38  ? 507  ILE   A O     1 
ATOM   1883  C  CB    . ILE   A 1 507  ? 118.671 153.480 151.312 1.00 43.42  ? 507  ILE   A CB    1 
ATOM   1884  C  CG1   . ILE   A 1 507  ? 118.478 154.896 151.858 1.00 43.54  ? 507  ILE   A CG1   1 
ATOM   1885  C  CG2   . ILE   A 1 507  ? 118.602 152.461 152.437 1.00 42.83  ? 507  ILE   A CG2   1 
ATOM   1886  C  CD1   . ILE   A 1 507  ? 117.031 155.332 151.918 1.00 39.91  ? 507  ILE   A CD1   1 
ATOM   1887  N  N     . SER   A 1 508  ? 121.190 154.588 148.823 1.00 50.69  ? 508  SER   A N     1 
ATOM   1888  C  CA    . SER   A 1 508  ? 121.285 155.437 147.639 1.00 44.04  ? 508  SER   A CA    1 
ATOM   1889  C  C     . SER   A 1 508  ? 120.576 154.820 146.440 1.00 45.59  ? 508  SER   A C     1 
ATOM   1890  O  O     . SER   A 1 508  ? 120.093 155.547 145.565 1.00 56.04  ? 508  SER   A O     1 
ATOM   1891  C  CB    . SER   A 1 508  ? 122.752 155.708 147.307 1.00 47.96  ? 508  SER   A CB    1 
ATOM   1892  O  OG    . SER   A 1 508  ? 123.447 154.502 147.049 1.00 44.76  ? 508  SER   A OG    1 
ATOM   1893  N  N     . GLY   A 1 509  ? 120.502 153.493 146.378 1.00 46.83  ? 509  GLY   A N     1 
ATOM   1894  C  CA    . GLY   A 1 509  ? 119.808 152.830 145.293 1.00 40.07  ? 509  GLY   A CA    1 
ATOM   1895  C  C     . GLY   A 1 509  ? 118.301 152.929 145.346 1.00 45.14  ? 509  GLY   A C     1 
ATOM   1896  O  O     . GLY   A 1 509  ? 117.630 152.400 144.455 1.00 52.38  ? 509  GLY   A O     1 
ATOM   1897  N  N     . ASP   A 1 510  ? 117.750 153.593 146.362 1.00 49.71  ? 510  ASP   A N     1 
ATOM   1898  C  CA    . ASP   A 1 510  ? 116.313 153.789 146.483 1.00 41.48  ? 510  ASP   A CA    1 
ATOM   1899  C  C     . ASP   A 1 510  ? 115.921 155.254 146.599 1.00 40.45  ? 510  ASP   A C     1 
ATOM   1900  O  O     . ASP   A 1 510  ? 114.731 155.549 146.753 1.00 45.82  ? 510  ASP   A O     1 
ATOM   1901  C  CB    . ASP   A 1 510  ? 115.767 153.018 147.694 1.00 48.36  ? 510  ASP   A CB    1 
ATOM   1902  C  CG    . ASP   A 1 510  ? 115.929 151.516 147.554 1.00 55.30  ? 510  ASP   A CG    1 
ATOM   1903  O  OD1   . ASP   A 1 510  ? 117.049 151.063 147.243 1.00 54.17  ? 510  ASP   A OD1   1 
ATOM   1904  O  OD2   . ASP   A 1 510  ? 114.936 150.788 147.755 1.00 64.61  ? 510  ASP   A OD2   1 
ATOM   1905  N  N     . LEU   A 1 511  ? 116.876 156.176 146.532 1.00 38.69  ? 511  LEU   A N     1 
ATOM   1906  C  CA    . LEU   A 1 511  ? 116.562 157.595 146.570 1.00 43.53  ? 511  LEU   A CA    1 
ATOM   1907  C  C     . LEU   A 1 511  ? 116.021 158.061 145.226 1.00 43.13  ? 511  LEU   A C     1 
ATOM   1908  O  O     . LEU   A 1 511  ? 116.421 157.571 144.166 1.00 46.84  ? 511  LEU   A O     1 
ATOM   1909  C  CB    . LEU   A 1 511  ? 117.799 158.415 146.940 1.00 42.54  ? 511  LEU   A CB    1 
ATOM   1910  C  CG    . LEU   A 1 511  ? 118.443 158.122 148.295 1.00 43.35  ? 511  LEU   A CG    1 
ATOM   1911  C  CD1   . LEU   A 1 511  ? 119.567 159.107 148.573 1.00 41.25  ? 511  LEU   A CD1   1 
ATOM   1912  C  CD2   . LEU   A 1 511  ? 117.400 158.168 149.400 1.00 43.22  ? 511  LEU   A CD2   1 
ATOM   1913  N  N     . ALA   A 1 512  ? 115.098 159.022 145.278 1.00 46.82  ? 512  ALA   A N     1 
ATOM   1914  C  CA    . ALA   A 1 512  ? 114.559 159.586 144.047 1.00 46.99  ? 512  ALA   A CA    1 
ATOM   1915  C  C     . ALA   A 1 512  ? 115.659 160.231 143.216 1.00 51.34  ? 512  ALA   A C     1 
ATOM   1916  O  O     . ALA   A 1 512  ? 115.691 160.082 141.989 1.00 52.16  ? 512  ALA   A O     1 
ATOM   1917  C  CB    . ALA   A 1 512  ? 113.461 160.600 144.366 1.00 48.85  ? 512  ALA   A CB    1 
ATOM   1918  N  N     . ASP   A 1 513  ? 116.570 160.947 143.866 1.00 53.99  ? 513  ASP   A N     1 
ATOM   1919  C  CA    . ASP   A 1 513  ? 117.664 161.593 143.158 1.00 53.12  ? 513  ASP   A CA    1 
ATOM   1920  C  C     . ASP   A 1 513  ? 118.843 161.820 144.097 1.00 50.71  ? 513  ASP   A C     1 
ATOM   1921  O  O     . ASP   A 1 513  ? 118.895 162.842 144.792 1.00 52.12  ? 513  ASP   A O     1 
ATOM   1922  C  CB    . ASP   A 1 513  ? 117.200 162.920 142.551 1.00 59.09  ? 513  ASP   A CB    1 
ATOM   1923  C  CG    . ASP   A 1 513  ? 118.346 163.885 142.309 1.00 62.21  ? 513  ASP   A CG    1 
ATOM   1924  O  OD1   . ASP   A 1 513  ? 119.361 163.467 141.714 1.00 56.46  ? 513  ASP   A OD1   1 
ATOM   1925  O  OD2   . ASP   A 1 513  ? 118.236 165.058 142.722 1.00 62.51  ? 513  ASP   A OD2   1 
ATOM   1926  N  N     . PRO   A 1 514  ? 119.797 160.892 144.163 1.00 45.12  ? 514  PRO   A N     1 
ATOM   1927  C  CA    . PRO   A 1 514  ? 121.045 161.186 144.878 1.00 39.04  ? 514  PRO   A CA    1 
ATOM   1928  C  C     . PRO   A 1 514  ? 121.793 162.316 144.194 1.00 48.66  ? 514  PRO   A C     1 
ATOM   1929  O  O     . PRO   A 1 514  ? 121.359 162.802 143.145 1.00 56.79  ? 514  PRO   A O     1 
ATOM   1930  C  CB    . PRO   A 1 514  ? 121.813 159.857 144.820 1.00 38.29  ? 514  PRO   A CB    1 
ATOM   1931  C  CG    . PRO   A 1 514  ? 120.777 158.827 144.457 1.00 38.98  ? 514  PRO   A CG    1 
ATOM   1932  C  CD    . PRO   A 1 514  ? 119.812 159.545 143.576 1.00 43.54  ? 514  PRO   A CD    1 
ATOM   1933  N  N     . GLN   A 1 515  ? 122.911 162.746 144.769 1.00 39.49  ? 515  GLN   A N     1 
ATOM   1934  C  CA    . GLN   A 1 515  ? 123.668 163.930 144.390 1.00 44.67  ? 515  GLN   A CA    1 
ATOM   1935  C  C     . GLN   A 1 515  ? 122.992 165.205 144.882 1.00 44.73  ? 515  GLN   A C     1 
ATOM   1936  O  O     . GLN   A 1 515  ? 123.594 166.275 144.792 1.00 49.44  ? 515  GLN   A O     1 
ATOM   1937  C  CB    . GLN   A 1 515  ? 123.886 164.051 142.869 1.00 38.99  ? 515  GLN   A CB    1 
ATOM   1938  C  CG    . GLN   A 1 515  ? 125.006 163.200 142.306 1.00 45.85  ? 515  GLN   A CG    1 
ATOM   1939  C  CD    . GLN   A 1 515  ? 125.702 163.883 141.146 1.00 52.00  ? 515  GLN   A CD    1 
ATOM   1940  O  OE1   . GLN   A 1 515  ? 125.578 165.093 140.961 1.00 51.04  ? 515  GLN   A OE1   1 
ATOM   1941  N  NE2   . GLN   A 1 515  ? 126.435 163.110 140.356 1.00 46.49  ? 515  GLN   A NE2   1 
ATOM   1942  N  N     . SER   A 1 516  ? 121.781 165.132 145.403 1.00 42.27  ? 516  SER   A N     1 
ATOM   1943  C  CA    . SER   A 1 516  ? 121.111 166.264 146.032 1.00 37.46  ? 516  SER   A CA    1 
ATOM   1944  C  C     . SER   A 1 516  ? 120.528 165.914 147.391 1.00 41.40  ? 516  SER   A C     1 
ATOM   1945  O  O     . SER   A 1 516  ? 120.596 166.730 148.312 1.00 49.47  ? 516  SER   A O     1 
ATOM   1946  C  CB    . SER   A 1 516  ? 120.004 166.801 145.112 1.00 38.88  ? 516  SER   A CB    1 
ATOM   1947  O  OG    . SER   A 1 516  ? 119.368 165.748 144.410 1.00 41.63  ? 516  SER   A OG    1 
ATOM   1948  N  N     . ALA   A 1 517  ? 119.963 164.714 147.540 1.00 35.09  ? 517  ALA   A N     1 
ATOM   1949  C  CA    . ALA   A 1 517  ? 119.362 164.327 148.811 1.00 30.08  ? 517  ALA   A CA    1 
ATOM   1950  C  C     . ALA   A 1 517  ? 120.427 164.004 149.852 1.00 30.12  ? 517  ALA   A C     1 
ATOM   1951  O  O     . ALA   A 1 517  ? 120.313 164.404 151.016 1.00 42.95  ? 517  ALA   A O     1 
ATOM   1952  C  CB    . ALA   A 1 517  ? 118.428 163.136 148.604 1.00 34.33  ? 517  ALA   A CB    1 
ATOM   1953  N  N     . ILE   A 1 518  ? 121.472 163.277 149.451 1.00 20.98  ? 518  ILE   A N     1 
ATOM   1954  C  CA    . ILE   A 1 518  ? 122.488 162.851 150.414 1.00 36.48  ? 518  ILE   A CA    1 
ATOM   1955  C  C     . ILE   A 1 518  ? 123.192 164.036 151.063 1.00 37.26  ? 518  ILE   A C     1 
ATOM   1956  O  O     . ILE   A 1 518  ? 123.235 164.096 152.303 1.00 45.78  ? 518  ILE   A O     1 
ATOM   1957  C  CB    . ILE   A 1 518  ? 123.476 161.879 149.743 1.00 29.05  ? 518  ILE   A CB    1 
ATOM   1958  C  CG1   . ILE   A 1 518  ? 122.840 160.499 149.575 1.00 27.79  ? 518  ILE   A CG1   1 
ATOM   1959  C  CG2   . ILE   A 1 518  ? 124.758 161.778 150.553 1.00 26.02  ? 518  ILE   A CG2   1 
ATOM   1960  C  CD1   . ILE   A 1 518  ? 123.696 159.520 148.800 1.00 29.47  ? 518  ILE   A CD1   1 
ATOM   1961  N  N     . PRO   A 1 519  ? 123.743 164.995 150.322 1.00 31.90  ? 519  PRO   A N     1 
ATOM   1962  C  CA    . PRO   A 1 519  ? 124.515 166.069 150.964 1.00 36.66  ? 519  PRO   A CA    1 
ATOM   1963  C  C     . PRO   A 1 519  ? 123.704 166.885 151.958 1.00 33.92  ? 519  PRO   A C     1 
ATOM   1964  O  O     . PRO   A 1 519  ? 124.056 166.967 153.141 1.00 40.13  ? 519  PRO   A O     1 
ATOM   1965  C  CB    . PRO   A 1 519  ? 124.971 166.933 149.781 1.00 30.80  ? 519  PRO   A CB    1 
ATOM   1966  C  CG    . PRO   A 1 519  ? 124.877 166.054 148.592 1.00 32.94  ? 519  PRO   A CG    1 
ATOM   1967  C  CD    . PRO   A 1 519  ? 123.772 165.084 148.853 1.00 31.94  ? 519  PRO   A CD    1 
ATOM   1968  N  N     . LYS   A 1 520  ? 122.619 167.498 151.480 1.00 33.34  ? 520  LYS   A N     1 
ATOM   1969  C  CA    . LYS   A 1 520  ? 121.831 168.372 152.341 1.00 35.60  ? 520  LYS   A CA    1 
ATOM   1970  C  C     . LYS   A 1 520  ? 121.190 167.591 153.480 1.00 38.61  ? 520  LYS   A C     1 
ATOM   1971  O  O     . LYS   A 1 520  ? 121.176 168.056 154.624 1.00 48.41  ? 520  LYS   A O     1 
ATOM   1972  C  CB    . LYS   A 1 520  ? 120.767 169.106 151.523 1.00 31.32  ? 520  LYS   A CB    1 
ATOM   1973  C  CG    . LYS   A 1 520  ? 119.647 168.219 151.008 1.00 31.30  ? 520  LYS   A CG    1 
ATOM   1974  C  CD    . LYS   A 1 520  ? 118.455 169.043 150.554 1.00 36.76  ? 520  LYS   A CD    1 
ATOM   1975  C  CE    . LYS   A 1 520  ? 118.570 169.400 149.085 1.00 44.84  ? 520  LYS   A CE    1 
ATOM   1976  N  NZ    . LYS   A 1 520  ? 117.238 169.559 148.446 1.00 38.96  ? 520  LYS   A NZ    1 
ATOM   1977  N  N     . GLY   A 1 521  ? 120.662 166.401 153.190 1.00 28.06  ? 521  GLY   A N     1 
ATOM   1978  C  CA    . GLY   A 1 521  ? 120.053 165.607 154.243 1.00 25.85  ? 521  GLY   A CA    1 
ATOM   1979  C  C     . GLY   A 1 521  ? 121.036 165.243 155.338 1.00 33.52  ? 521  GLY   A C     1 
ATOM   1980  O  O     . GLY   A 1 521  ? 120.749 165.402 156.527 1.00 46.09  ? 521  GLY   A O     1 
ATOM   1981  N  N     . THR   A 1 522  ? 122.220 164.760 154.950 1.00 26.16  ? 522  THR   A N     1 
ATOM   1982  C  CA    . THR   A 1 522  ? 123.220 164.375 155.940 1.00 27.37  ? 522  THR   A CA    1 
ATOM   1983  C  C     . THR   A 1 522  ? 123.689 165.578 156.748 1.00 31.72  ? 522  THR   A C     1 
ATOM   1984  O  O     . THR   A 1 522  ? 123.814 165.501 157.978 1.00 38.49  ? 522  THR   A O     1 
ATOM   1985  C  CB    . THR   A 1 522  ? 124.405 163.698 155.252 1.00 24.97  ? 522  THR   A CB    1 
ATOM   1986  O  OG1   . THR   A 1 522  ? 123.936 162.584 154.483 1.00 34.65  ? 522  THR   A OG1   1 
ATOM   1987  C  CG2   . THR   A 1 522  ? 125.413 163.203 156.279 1.00 32.44  ? 522  THR   A CG2   1 
ATOM   1988  N  N     . LEU   A 1 523  ? 123.954 166.702 156.077 1.00 27.12  ? 523  LEU   A N     1 
ATOM   1989  C  CA    . LEU   A 1 523  ? 124.423 167.880 156.795 1.00 29.30  ? 523  LEU   A CA    1 
ATOM   1990  C  C     . LEU   A 1 523  ? 123.366 168.389 157.767 1.00 39.54  ? 523  LEU   A C     1 
ATOM   1991  O  O     . LEU   A 1 523  ? 123.680 168.746 158.911 1.00 44.23  ? 523  LEU   A O     1 
ATOM   1992  C  CB    . LEU   A 1 523  ? 124.819 168.973 155.803 1.00 33.09  ? 523  LEU   A CB    1 
ATOM   1993  C  CG    . LEU   A 1 523  ? 126.274 168.942 155.328 1.00 37.39  ? 523  LEU   A CG    1 
ATOM   1994  C  CD1   . LEU   A 1 523  ? 127.222 169.179 156.489 1.00 40.25  ? 523  LEU   A CD1   1 
ATOM   1995  C  CD2   . LEU   A 1 523  ? 126.591 167.628 154.641 1.00 37.28  ? 523  LEU   A CD2   1 
ATOM   1996  N  N     . LEU   A 1 524  ? 122.103 168.422 157.334 1.00 29.41  ? 524  LEU   A N     1 
ATOM   1997  C  CA    . LEU   A 1 524  ? 121.028 168.867 158.212 1.00 27.48  ? 524  LEU   A CA    1 
ATOM   1998  C  C     . LEU   A 1 524  ? 120.868 167.932 159.402 1.00 33.49  ? 524  LEU   A C     1 
ATOM   1999  O  O     . LEU   A 1 524  ? 120.648 168.384 160.531 1.00 43.63  ? 524  LEU   A O     1 
ATOM   2000  C  CB    . LEU   A 1 524  ? 119.721 168.967 157.427 1.00 29.52  ? 524  LEU   A CB    1 
ATOM   2001  C  CG    . LEU   A 1 524  ? 118.750 170.069 157.848 1.00 37.58  ? 524  LEU   A CG    1 
ATOM   2002  C  CD1   . LEU   A 1 524  ? 119.508 171.310 158.286 1.00 36.27  ? 524  LEU   A CD1   1 
ATOM   2003  C  CD2   . LEU   A 1 524  ? 117.792 170.396 156.717 1.00 40.39  ? 524  LEU   A CD2   1 
ATOM   2004  N  N     . ALA   A 1 525  ? 120.963 166.622 159.168 1.00 31.27  ? 525  ALA   A N     1 
ATOM   2005  C  CA    . ALA   A 1 525  ? 120.863 165.674 160.271 1.00 33.42  ? 525  ALA   A CA    1 
ATOM   2006  C  C     . ALA   A 1 525  ? 121.976 165.902 161.284 1.00 31.36  ? 525  ALA   A C     1 
ATOM   2007  O  O     . ALA   A 1 525  ? 121.734 165.924 162.497 1.00 33.87  ? 525  ALA   A O     1 
ATOM   2008  C  CB    . ALA   A 1 525  ? 120.900 164.243 159.738 1.00 28.57  ? 525  ALA   A CB    1 
ATOM   2009  N  N     . ILE   A 1 526  ? 123.207 166.084 160.801 1.00 29.37  ? 526  ILE   A N     1 
ATOM   2010  C  CA    . ILE   A 1 526  ? 124.327 166.316 161.711 1.00 28.80  ? 526  ILE   A CA    1 
ATOM   2011  C  C     . ILE   A 1 526  ? 124.087 167.579 162.525 1.00 34.61  ? 526  ILE   A C     1 
ATOM   2012  O  O     . ILE   A 1 526  ? 124.243 167.592 163.754 1.00 43.46  ? 526  ILE   A O     1 
ATOM   2013  C  CB    . ILE   A 1 526  ? 125.650 166.395 160.928 1.00 38.62  ? 526  ILE   A CB    1 
ATOM   2014  C  CG1   . ILE   A 1 526  ? 126.105 165.000 160.496 1.00 36.10  ? 526  ILE   A CG1   1 
ATOM   2015  C  CG2   . ILE   A 1 526  ? 126.727 167.067 161.766 1.00 30.86  ? 526  ILE   A CG2   1 
ATOM   2016  C  CD1   . ILE   A 1 526  ? 127.133 165.011 159.385 1.00 33.18  ? 526  ILE   A CD1   1 
ATOM   2017  N  N     . LEU   A 1 527  ? 123.690 168.661 161.851 1.00 32.83  ? 527  LEU   A N     1 
ATOM   2018  C  CA    . LEU   A 1 527  ? 123.474 169.928 162.541 1.00 32.50  ? 527  LEU   A CA    1 
ATOM   2019  C  C     . LEU   A 1 527  ? 122.398 169.794 163.611 1.00 36.15  ? 527  LEU   A C     1 
ATOM   2020  O  O     . LEU   A 1 527  ? 122.588 170.217 164.758 1.00 42.62  ? 527  LEU   A O     1 
ATOM   2021  C  CB    . LEU   A 1 527  ? 123.098 171.011 161.529 1.00 30.70  ? 527  LEU   A CB    1 
ATOM   2022  C  CG    . LEU   A 1 527  ? 122.782 172.399 162.088 1.00 36.37  ? 527  LEU   A CG    1 
ATOM   2023  C  CD1   . LEU   A 1 527  ? 124.057 173.142 162.455 1.00 36.39  ? 527  LEU   A CD1   1 
ATOM   2024  C  CD2   . LEU   A 1 527  ? 121.959 173.203 161.097 1.00 32.99  ? 527  LEU   A CD2   1 
ATOM   2025  N  N     . ILE   A 1 528  ? 121.257 169.201 163.253 1.00 32.84  ? 528  ILE   A N     1 
ATOM   2026  C  CA    . ILE   A 1 528  ? 120.143 169.103 164.190 1.00 28.26  ? 528  ILE   A CA    1 
ATOM   2027  C  C     . ILE   A 1 528  ? 120.516 168.227 165.378 1.00 33.79  ? 528  ILE   A C     1 
ATOM   2028  O  O     . ILE   A 1 528  ? 120.227 168.567 166.533 1.00 44.38  ? 528  ILE   A O     1 
ATOM   2029  C  CB    . ILE   A 1 528  ? 118.886 168.580 163.471 1.00 35.40  ? 528  ILE   A CB    1 
ATOM   2030  C  CG1   . ILE   A 1 528  ? 118.166 169.726 162.760 1.00 34.43  ? 528  ILE   A CG1   1 
ATOM   2031  C  CG2   . ILE   A 1 528  ? 117.956 167.886 164.456 1.00 35.22  ? 528  ILE   A CG2   1 
ATOM   2032  C  CD1   . ILE   A 1 528  ? 117.473 169.313 161.480 1.00 35.29  ? 528  ILE   A CD1   1 
ATOM   2033  N  N     . THR   A 1 529  ? 121.154 167.083 165.119 1.00 32.07  ? 529  THR   A N     1 
ATOM   2034  C  CA    . THR   A 1 529  ? 121.518 166.192 166.213 1.00 38.01  ? 529  THR   A CA    1 
ATOM   2035  C  C     . THR   A 1 529  ? 122.508 166.858 167.159 1.00 36.43  ? 529  THR   A C     1 
ATOM   2036  O  O     . THR   A 1 529  ? 122.374 166.751 168.384 1.00 31.86  ? 529  THR   A O     1 
ATOM   2037  C  CB    . THR   A 1 529  ? 122.093 164.887 165.664 1.00 38.97  ? 529  THR   A CB    1 
ATOM   2038  O  OG1   . THR   A 1 529  ? 122.992 165.177 164.587 1.00 48.60  ? 529  THR   A OG1   1 
ATOM   2039  C  CG2   . THR   A 1 529  ? 120.976 163.984 165.159 1.00 25.37  ? 529  THR   A CG2   1 
ATOM   2040  N  N     . THR   A 1 530  ? 123.510 167.555 166.615 1.00 36.93  ? 530  THR   A N     1 
ATOM   2041  C  CA    . THR   A 1 530  ? 124.479 168.225 167.477 1.00 36.46  ? 530  THR   A CA    1 
ATOM   2042  C  C     . THR   A 1 530  ? 123.818 169.328 168.293 1.00 40.04  ? 530  THR   A C     1 
ATOM   2043  O  O     . THR   A 1 530  ? 124.107 169.489 169.487 1.00 45.63  ? 530  THR   A O     1 
ATOM   2044  C  CB    . THR   A 1 530  ? 125.627 168.786 166.640 1.00 35.09  ? 530  THR   A CB    1 
ATOM   2045  O  OG1   . THR   A 1 530  ? 126.144 167.756 165.789 1.00 42.15  ? 530  THR   A OG1   1 
ATOM   2046  C  CG2   . THR   A 1 530  ? 126.742 169.297 167.539 1.00 34.04  ? 530  THR   A CG2   1 
ATOM   2047  N  N     . LEU   A 1 531  ? 122.923 170.097 167.668 1.00 39.08  ? 531  LEU   A N     1 
ATOM   2048  C  CA    . LEU   A 1 531  ? 122.227 171.149 168.400 1.00 35.80  ? 531  LEU   A CA    1 
ATOM   2049  C  C     . LEU   A 1 531  ? 121.406 170.566 169.541 1.00 32.90  ? 531  LEU   A C     1 
ATOM   2050  O  O     . LEU   A 1 531  ? 121.420 171.094 170.661 1.00 41.82  ? 531  LEU   A O     1 
ATOM   2051  C  CB    . LEU   A 1 531  ? 121.335 171.945 167.449 1.00 37.08  ? 531  LEU   A CB    1 
ATOM   2052  C  CG    . LEU   A 1 531  ? 122.035 172.997 166.591 1.00 43.47  ? 531  LEU   A CG    1 
ATOM   2053  C  CD1   . LEU   A 1 531  ? 121.027 173.979 166.016 1.00 42.93  ? 531  LEU   A CD1   1 
ATOM   2054  C  CD2   . LEU   A 1 531  ? 123.098 173.722 167.397 1.00 34.87  ? 531  LEU   A CD2   1 
ATOM   2055  N  N     . VAL   A 1 532  ? 120.687 169.473 169.278 1.00 34.27  ? 532  VAL   A N     1 
ATOM   2056  C  CA    . VAL   A 1 532  ? 119.865 168.861 170.317 1.00 37.93  ? 532  VAL   A CA    1 
ATOM   2057  C  C     . VAL   A 1 532  ? 120.742 168.321 171.438 1.00 38.06  ? 532  VAL   A C     1 
ATOM   2058  O  O     . VAL   A 1 532  ? 120.407 168.446 172.622 1.00 47.63  ? 532  VAL   A O     1 
ATOM   2059  C  CB    . VAL   A 1 532  ? 118.969 167.762 169.717 1.00 38.62  ? 532  VAL   A CB    1 
ATOM   2060  C  CG1   . VAL   A 1 532  ? 118.648 166.708 170.765 1.00 38.50  ? 532  VAL   A CG1   1 
ATOM   2061  C  CG2   . VAL   A 1 532  ? 117.694 168.366 169.154 1.00 31.25  ? 532  VAL   A CG2   1 
ATOM   2062  N  N     . TYR   A 1 533  ? 121.874 167.708 171.086 1.00 36.52  ? 533  TYR   A N     1 
ATOM   2063  C  CA    . TYR   A 1 533  ? 122.785 167.199 172.106 1.00 30.54  ? 533  TYR   A CA    1 
ATOM   2064  C  C     . TYR   A 1 533  ? 123.272 168.322 173.012 1.00 40.78  ? 533  TYR   A C     1 
ATOM   2065  O  O     . TYR   A 1 533  ? 123.258 168.195 174.242 1.00 49.88  ? 533  TYR   A O     1 
ATOM   2066  C  CB    . TYR   A 1 533  ? 123.969 166.491 171.448 1.00 35.79  ? 533  TYR   A CB    1 
ATOM   2067  C  CG    . TYR   A 1 533  ? 123.715 165.041 171.107 1.00 42.28  ? 533  TYR   A CG    1 
ATOM   2068  C  CD1   . TYR   A 1 533  ? 123.003 164.220 171.968 1.00 33.79  ? 533  TYR   A CD1   1 
ATOM   2069  C  CD2   . TYR   A 1 533  ? 124.196 164.492 169.925 1.00 45.47  ? 533  TYR   A CD2   1 
ATOM   2070  C  CE1   . TYR   A 1 533  ? 122.772 162.896 171.661 1.00 40.43  ? 533  TYR   A CE1   1 
ATOM   2071  C  CE2   . TYR   A 1 533  ? 123.969 163.168 169.609 1.00 41.69  ? 533  TYR   A CE2   1 
ATOM   2072  C  CZ    . TYR   A 1 533  ? 123.257 162.375 170.481 1.00 45.25  ? 533  TYR   A CZ    1 
ATOM   2073  O  OH    . TYR   A 1 533  ? 123.028 161.055 170.171 1.00 41.96  ? 533  TYR   A OH    1 
ATOM   2074  N  N     . VAL   A 1 534  ? 123.706 169.436 172.417 1.00 45.24  ? 534  VAL   A N     1 
ATOM   2075  C  CA    . VAL   A 1 534  ? 124.209 170.554 173.215 1.00 45.91  ? 534  VAL   A CA    1 
ATOM   2076  C  C     . VAL   A 1 534  ? 123.105 171.107 174.109 1.00 44.37  ? 534  VAL   A C     1 
ATOM   2077  O  O     . VAL   A 1 534  ? 123.315 171.374 175.302 1.00 46.77  ? 534  VAL   A O     1 
ATOM   2078  C  CB    . VAL   A 1 534  ? 124.794 171.645 172.302 1.00 42.36  ? 534  VAL   A CB    1 
ATOM   2079  C  CG1   . VAL   A 1 534  ? 124.868 172.968 173.042 1.00 43.53  ? 534  VAL   A CG1   1 
ATOM   2080  C  CG2   . VAL   A 1 534  ? 126.168 171.236 171.798 1.00 44.00  ? 534  VAL   A CG2   1 
ATOM   2081  N  N     . GLY   A 1 535  ? 121.912 171.296 173.541 1.00 38.11  ? 535  GLY   A N     1 
ATOM   2082  C  CA    . GLY   A 1 535  ? 120.810 171.825 174.326 1.00 35.59  ? 535  GLY   A CA    1 
ATOM   2083  C  C     . GLY   A 1 535  ? 120.466 170.942 175.509 1.00 40.78  ? 535  GLY   A C     1 
ATOM   2084  O  O     . GLY   A 1 535  ? 120.284 171.426 176.629 1.00 50.87  ? 535  GLY   A O     1 
ATOM   2085  N  N     . ILE   A 1 536  ? 120.379 169.631 175.279 1.00 41.06  ? 536  ILE   A N     1 
ATOM   2086  C  CA    . ILE   A 1 536  ? 120.016 168.718 176.356 1.00 40.68  ? 536  ILE   A CA    1 
ATOM   2087  C  C     . ILE   A 1 536  ? 121.118 168.661 177.405 1.00 42.95  ? 536  ILE   A C     1 
ATOM   2088  O  O     . ILE   A 1 536  ? 120.842 168.584 178.608 1.00 49.50  ? 536  ILE   A O     1 
ATOM   2089  C  CB    . ILE   A 1 536  ? 119.697 167.322 175.793 1.00 47.29  ? 536  ILE   A CB    1 
ATOM   2090  C  CG1   . ILE   A 1 536  ? 118.406 167.367 174.975 1.00 45.40  ? 536  ILE   A CG1   1 
ATOM   2091  C  CG2   . ILE   A 1 536  ? 119.585 166.307 176.918 1.00 44.11  ? 536  ILE   A CG2   1 
ATOM   2092  C  CD1   . ILE   A 1 536  ? 117.382 168.342 175.508 1.00 45.02  ? 536  ILE   A CD1   1 
ATOM   2093  N  N     . ALA   A 1 537  ? 122.380 168.691 176.974 1.00 48.58  ? 537  ALA   A N     1 
ATOM   2094  C  CA    . ALA   A 1 537  ? 123.479 168.701 177.933 1.00 48.04  ? 537  ALA   A CA    1 
ATOM   2095  C  C     . ALA   A 1 537  ? 123.387 169.914 178.848 1.00 50.03  ? 537  ALA   A C     1 
ATOM   2096  O  O     . ALA   A 1 537  ? 123.456 169.787 180.077 1.00 52.37  ? 537  ALA   A O     1 
ATOM   2097  C  CB    . ALA   A 1 537  ? 124.818 168.675 177.196 1.00 43.22  ? 537  ALA   A CB    1 
ATOM   2098  N  N     . VAL   A 1 538  ? 123.210 171.103 178.265 1.00 49.14  ? 538  VAL   A N     1 
ATOM   2099  C  CA    . VAL   A 1 538  ? 123.119 172.310 179.084 1.00 47.29  ? 538  VAL   A CA    1 
ATOM   2100  C  C     . VAL   A 1 538  ? 121.907 172.241 180.006 1.00 49.55  ? 538  VAL   A C     1 
ATOM   2101  O  O     . VAL   A 1 538  ? 121.992 172.568 181.198 1.00 48.75  ? 538  VAL   A O     1 
ATOM   2102  C  CB    . VAL   A 1 538  ? 123.084 173.564 178.192 1.00 43.41  ? 538  VAL   A CB    1 
ATOM   2103  C  CG1   . VAL   A 1 538  ? 122.392 174.708 178.915 1.00 45.38  ? 538  VAL   A CG1   1 
ATOM   2104  C  CG2   . VAL   A 1 538  ? 124.491 173.964 177.791 1.00 44.19  ? 538  VAL   A CG2   1 
ATOM   2105  N  N     . SER   A 1 539  ? 120.759 171.815 179.473 1.00 45.29  ? 539  SER   A N     1 
ATOM   2106  C  CA    . SER   A 1 539  ? 119.549 171.743 180.285 1.00 42.28  ? 539  SER   A CA    1 
ATOM   2107  C  C     . SER   A 1 539  ? 119.749 170.832 181.489 1.00 48.40  ? 539  SER   A C     1 
ATOM   2108  O  O     . SER   A 1 539  ? 119.442 171.210 182.625 1.00 54.12  ? 539  SER   A O     1 
ATOM   2109  C  CB    . SER   A 1 539  ? 118.376 171.263 179.430 1.00 50.33  ? 539  SER   A CB    1 
ATOM   2110  O  OG    . SER   A 1 539  ? 117.643 172.358 178.911 1.00 56.98  ? 539  SER   A OG    1 
ATOM   2111  N  N     . VAL   A 1 540  ? 120.267 169.623 181.261 1.00 50.78  ? 540  VAL   A N     1 
ATOM   2112  C  CA    . VAL   A 1 540  ? 120.485 168.698 182.368 1.00 49.55  ? 540  VAL   A CA    1 
ATOM   2113  C  C     . VAL   A 1 540  ? 121.519 169.252 183.337 1.00 57.90  ? 540  VAL   A C     1 
ATOM   2114  O  O     . VAL   A 1 540  ? 121.439 169.008 184.548 1.00 58.79  ? 540  VAL   A O     1 
ATOM   2115  C  CB    . VAL   A 1 540  ? 120.891 167.308 181.839 1.00 51.88  ? 540  VAL   A CB    1 
ATOM   2116  C  CG1   . VAL   A 1 540  ? 122.393 167.234 181.627 1.00 54.04  ? 540  VAL   A CG1   1 
ATOM   2117  C  CG2   . VAL   A 1 540  ? 120.426 166.222 182.793 1.00 46.59  ? 540  VAL   A CG2   1 
ATOM   2118  N  N     . GLY   A 1 541  ? 122.500 170.001 182.834 1.00 57.81  ? 541  GLY   A N     1 
ATOM   2119  C  CA    . GLY   A 1 541  ? 123.486 170.591 183.720 1.00 51.65  ? 541  GLY   A CA    1 
ATOM   2120  C  C     . GLY   A 1 541  ? 122.995 171.795 184.494 1.00 50.25  ? 541  GLY   A C     1 
ATOM   2121  O  O     . GLY   A 1 541  ? 123.678 172.227 185.429 1.00 51.88  ? 541  GLY   A O     1 
ATOM   2122  N  N     . SER   A 1 542  ? 121.837 172.347 184.130 1.00 56.69  ? 542  SER   A N     1 
ATOM   2123  C  CA    . SER   A 1 542  ? 121.273 173.497 184.826 1.00 53.98  ? 542  SER   A CA    1 
ATOM   2124  C  C     . SER   A 1 542  ? 120.061 173.135 185.681 1.00 54.29  ? 542  SER   A C     1 
ATOM   2125  O  O     . SER   A 1 542  ? 119.321 174.028 186.106 1.00 56.21  ? 542  SER   A O     1 
ATOM   2126  C  CB    . SER   A 1 542  ? 120.903 174.591 183.825 1.00 54.90  ? 542  SER   A CB    1 
ATOM   2127  O  OG    . SER   A 1 542  ? 122.060 175.195 183.274 1.00 55.78  ? 542  SER   A OG    1 
ATOM   2128  N  N     . CYS   A 1 543  ? 119.838 171.846 185.943 1.00 53.17  ? 543  CYS   A N     1 
ATOM   2129  C  CA    . CYS   A 1 543  ? 118.681 171.430 186.727 1.00 51.83  ? 543  CYS   A CA    1 
ATOM   2130  C  C     . CYS   A 1 543  ? 119.067 170.534 187.897 1.00 56.88  ? 543  CYS   A C     1 
ATOM   2131  O  O     . CYS   A 1 543  ? 118.487 170.636 188.982 1.00 63.47  ? 543  CYS   A O     1 
ATOM   2132  C  CB    . CYS   A 1 543  ? 117.670 170.692 185.846 1.00 57.43  ? 543  CYS   A CB    1 
ATOM   2133  S  SG    . CYS   A 1 543  ? 116.899 171.689 184.564 1.00 67.23  ? 543  CYS   A SG    1 
ATOM   2134  N  N     . VAL   A 1 544  ? 120.042 169.656 187.687 1.00 50.40  ? 544  VAL   A N     1 
ATOM   2135  C  CA    . VAL   A 1 544  ? 120.362 168.592 188.629 1.00 52.30  ? 544  VAL   A CA    1 
ATOM   2136  C  C     . VAL   A 1 544  ? 121.754 168.824 189.194 1.00 54.09  ? 544  VAL   A C     1 
ATOM   2137  O  O     . VAL   A 1 544  ? 122.661 169.269 188.482 1.00 53.84  ? 544  VAL   A O     1 
ATOM   2138  C  CB    . VAL   A 1 544  ? 120.271 167.203 187.963 1.00 53.20  ? 544  VAL   A CB    1 
ATOM   2139  C  CG1   . VAL   A 1 544  ? 120.853 166.135 188.874 1.00 52.01  ? 544  VAL   A CG1   1 
ATOM   2140  C  CG2   . VAL   A 1 544  ? 118.832 166.883 187.606 1.00 50.61  ? 544  VAL   A CG2   1 
ATOM   2141  N  N     . VAL   A 1 545  ? 121.916 168.524 190.477 1.00 52.51  ? 545  VAL   A N     1 
ATOM   2142  C  CA    . VAL   A 1 545  ? 123.208 168.610 191.136 1.00 54.00  ? 545  VAL   A CA    1 
ATOM   2143  C  C     . VAL   A 1 545  ? 123.921 167.270 191.001 1.00 54.69  ? 545  VAL   A C     1 
ATOM   2144  O  O     . VAL   A 1 545  ? 123.300 166.224 190.799 1.00 51.23  ? 545  VAL   A O     1 
ATOM   2145  C  CB    . VAL   A 1 545  ? 123.060 169.021 192.614 1.00 56.63  ? 545  VAL   A CB    1 
ATOM   2146  C  CG1   . VAL   A 1 545  ? 122.452 170.408 192.713 1.00 53.62  ? 545  VAL   A CG1   1 
ATOM   2147  C  CG2   . VAL   A 1 545  ? 122.203 168.012 193.361 1.00 54.88  ? 545  VAL   A CG2   1 
ATOM   2148  N  N     . ARG   A 1 546  ? 125.250 167.303 191.112 1.00 55.77  ? 546  ARG   A N     1 
ATOM   2149  C  CA    . ARG   A 1 546  ? 126.044 166.106 190.854 1.00 57.13  ? 546  ARG   A CA    1 
ATOM   2150  C  C     . ARG   A 1 546  ? 125.655 164.965 191.787 1.00 64.02  ? 546  ARG   A C     1 
ATOM   2151  O  O     . ARG   A 1 546  ? 125.445 163.830 191.344 1.00 63.90  ? 546  ARG   A O     1 
ATOM   2152  C  CB    . ARG   A 1 546  ? 127.532 166.423 190.994 1.00 56.63  ? 546  ARG   A CB    1 
ATOM   2153  C  CG    . ARG   A 1 546  ? 128.427 165.606 190.082 1.00 54.92  ? 546  ARG   A CG    1 
ATOM   2154  C  CD    . ARG   A 1 546  ? 129.359 166.516 189.314 1.00 57.82  ? 546  ARG   A CD    1 
ATOM   2155  N  NE    . ARG   A 1 546  ? 128.844 167.878 189.294 1.00 62.03  ? 546  ARG   A NE    1 
ATOM   2156  C  CZ    . ARG   A 1 546  ? 129.507 168.926 188.829 1.00 60.64  ? 546  ARG   A CZ    1 
ATOM   2157  N  NH1   . ARG   A 1 546  ? 130.719 168.804 188.312 1.00 53.91  ? 546  ARG   A NH1   1 
ATOM   2158  N  NH2   . ARG   A 1 546  ? 128.942 170.127 188.886 1.00 58.44  ? 546  ARG   A NH2   1 
ATOM   2159  N  N     . ASP   A 1 547  ? 125.550 165.248 193.082 1.00 64.15  ? 547  ASP   A N     1 
ATOM   2160  C  CA    . ASP   A 1 547  ? 125.281 164.228 194.083 1.00 58.37  ? 547  ASP   A CA    1 
ATOM   2161  C  C     . ASP   A 1 547  ? 123.966 164.524 194.790 1.00 60.17  ? 547  ASP   A C     1 
ATOM   2162  O  O     . ASP   A 1 547  ? 123.550 165.680 194.907 1.00 59.27  ? 547  ASP   A O     1 
ATOM   2163  C  CB    . ASP   A 1 547  ? 126.416 164.143 195.110 1.00 54.70  ? 547  ASP   A CB    1 
ATOM   2164  N  N     . ALA   A 1 548  ? 123.315 163.463 195.261 1.00 67.36  ? 548  ALA   A N     1 
ATOM   2165  C  CA    . ALA   A 1 548  ? 122.039 163.599 195.945 1.00 67.83  ? 548  ALA   A CA    1 
ATOM   2166  C  C     . ALA   A 1 548  ? 121.751 162.326 196.724 1.00 72.88  ? 548  ALA   A C     1 
ATOM   2167  O  O     . ALA   A 1 548  ? 122.096 161.229 196.281 1.00 74.14  ? 548  ALA   A O     1 
ATOM   2168  C  CB    . ALA   A 1 548  ? 120.903 163.884 194.956 1.00 69.88  ? 548  ALA   A CB    1 
ATOM   2169  N  N     . THR   A 1 549  ? 121.125 162.484 197.885 1.00 83.21  ? 549  THR   A N     1 
ATOM   2170  C  CA    . THR   A 1 549  ? 120.682 161.367 198.715 1.00 77.29  ? 549  THR   A CA    1 
ATOM   2171  C  C     . THR   A 1 549  ? 119.164 161.476 198.834 1.00 76.00  ? 549  THR   A C     1 
ATOM   2172  O  O     . THR   A 1 549  ? 118.641 162.076 199.774 1.00 79.35  ? 549  THR   A O     1 
ATOM   2173  C  CB    . THR   A 1 549  ? 121.357 161.386 200.084 1.00 72.70  ? 549  THR   A CB    1 
ATOM   2174  N  N     . GLY   A 1 550  ? 118.461 160.891 197.868 1.00 78.90  ? 550  GLY   A N     1 
ATOM   2175  C  CA    . GLY   A 1 550  ? 117.017 160.996 197.824 1.00 80.50  ? 550  GLY   A CA    1 
ATOM   2176  C  C     . GLY   A 1 550  ? 116.341 160.453 199.064 1.00 87.26  ? 550  GLY   A C     1 
ATOM   2177  O  O     . GLY   A 1 550  ? 116.294 159.238 199.278 1.00 89.25  ? 550  GLY   A O     1 
ATOM   2178  N  N     . ASN   A 1 551  ? 115.807 161.352 199.888 1.00 94.02  ? 551  ASN   A N     1 
ATOM   2179  C  CA    . ASN   A 1 551  ? 115.128 160.957 201.114 1.00 90.90  ? 551  ASN   A CA    1 
ATOM   2180  C  C     . ASN   A 1 551  ? 114.349 162.131 201.691 1.00 92.03  ? 551  ASN   A C     1 
ATOM   2181  O  O     . ASN   A 1 551  ? 114.902 163.221 201.869 1.00 90.59  ? 551  ASN   A O     1 
ATOM   2182  N  N     . VAL   A 1 552  ? 113.065 161.921 201.985 1.00 95.87  ? 552  VAL   A N     1 
ATOM   2183  C  CA    . VAL   A 1 552  ? 112.269 162.980 202.599 1.00 92.60  ? 552  VAL   A CA    1 
ATOM   2184  C  C     . VAL   A 1 552  ? 112.886 163.402 203.925 1.00 97.12  ? 552  VAL   A C     1 
ATOM   2185  O  O     . VAL   A 1 552  ? 112.925 164.593 204.260 1.00 96.22  ? 552  VAL   A O     1 
ATOM   2186  N  N     . ASN   A 1 553  ? 113.385 162.435 204.698 1.00 100.77 ? 553  ASN   A N     1 
ATOM   2187  C  CA    . ASN   A 1 553  ? 114.037 162.748 205.963 1.00 99.25  ? 553  ASN   A CA    1 
ATOM   2188  C  C     . ASN   A 1 553  ? 115.262 163.632 205.776 1.00 98.79  ? 553  ASN   A C     1 
ATOM   2189  O  O     . ASN   A 1 553  ? 115.689 164.289 206.731 1.00 97.92  ? 553  ASN   A O     1 
ATOM   2190  C  CB    . ASN   A 1 553  ? 114.429 161.457 206.684 1.00 99.61  ? 553  ASN   A CB    1 
ATOM   2191  C  CG    . ASN   A 1 553  ? 113.228 160.604 207.047 1.00 99.64  ? 553  ASN   A CG    1 
ATOM   2192  O  OD1   . ASN   A 1 553  ? 112.480 160.161 206.176 1.00 101.67 ? 553  ASN   A OD1   1 
ATOM   2193  N  ND2   . ASN   A 1 553  ? 113.039 160.370 208.340 1.00 97.23  ? 553  ASN   A ND2   1 
ATOM   2194  N  N     . ASP   A 1 554  ? 115.838 163.660 204.576 1.00 92.75  ? 554  ASP   A N     1 
ATOM   2195  C  CA    . ASP   A 1 554  ? 116.990 164.515 204.323 1.00 91.33  ? 554  ASP   A CA    1 
ATOM   2196  C  C     . ASP   A 1 554  ? 116.644 165.959 204.659 1.00 91.27  ? 554  ASP   A C     1 
ATOM   2197  O  O     . ASP   A 1 554  ? 115.577 166.458 204.289 1.00 90.36  ? 554  ASP   A O     1 
ATOM   2198  N  N     . THR   A 1 555  ? 117.551 166.628 205.365 1.00 92.99  ? 555  THR   A N     1 
ATOM   2199  C  CA    . THR   A 1 555  ? 117.291 167.982 205.835 1.00 94.70  ? 555  THR   A CA    1 
ATOM   2200  C  C     . THR   A 1 555  ? 116.992 168.901 204.659 1.00 95.15  ? 555  THR   A C     1 
ATOM   2201  O  O     . THR   A 1 555  ? 117.867 169.172 203.832 1.00 96.26  ? 555  THR   A O     1 
ATOM   2202  N  N     . ILE   A 1 556  ? 115.749 169.377 204.587 1.00 104.06 ? 556  ILE   A N     1 
ATOM   2203  C  CA    . ILE   A 1 556  ? 115.319 170.321 203.566 1.00 104.37 ? 556  ILE   A CA    1 
ATOM   2204  C  C     . ILE   A 1 556  ? 114.918 171.666 204.156 1.00 106.93 ? 556  ILE   A C     1 
ATOM   2205  O  O     . ILE   A 1 556  ? 114.359 172.506 203.450 1.00 106.12 ? 556  ILE   A O     1 
ATOM   2206  N  N     . VAL   A 1 557  ? 115.194 171.891 205.444 1.00 118.83 ? 557  VAL   A N     1 
ATOM   2207  C  CA    . VAL   A 1 557  ? 114.808 173.137 206.101 1.00 118.17 ? 557  VAL   A CA    1 
ATOM   2208  C  C     . VAL   A 1 557  ? 115.919 174.176 206.113 1.00 119.06 ? 557  VAL   A C     1 
ATOM   2209  O  O     . VAL   A 1 557  ? 115.650 175.351 206.409 1.00 120.00 ? 557  VAL   A O     1 
ATOM   2210  N  N     . THR   A 1 558  ? 117.156 173.789 205.803 1.00 119.36 ? 558  THR   A N     1 
ATOM   2211  C  CA    . THR   A 1 558  ? 118.288 174.712 205.781 1.00 119.11 ? 558  THR   A CA    1 
ATOM   2212  C  C     . THR   A 1 558  ? 118.505 175.362 207.150 1.00 122.98 ? 558  THR   A C     1 
ATOM   2213  O  O     . THR   A 1 558  ? 118.388 176.577 207.323 1.00 121.79 ? 558  THR   A O     1 
ATOM   2214  N  N     . GLU   A 1 559  ? 118.825 174.519 208.128 1.00 127.08 ? 559  GLU   A N     1 
ATOM   2215  C  CA    . GLU   A 1 559  ? 119.090 174.976 209.485 1.00 123.35 ? 559  GLU   A CA    1 
ATOM   2216  C  C     . GLU   A 1 559  ? 120.455 175.661 209.538 1.00 125.12 ? 559  GLU   A C     1 
ATOM   2217  O  O     . GLU   A 1 559  ? 121.124 175.853 208.519 1.00 124.81 ? 559  GLU   A O     1 
ATOM   2218  N  N     . LEU   A 1 560  ? 120.883 176.046 210.740 1.00 127.81 ? 560  LEU   A N     1 
ATOM   2219  C  CA    . LEU   A 1 560  ? 122.162 176.724 210.914 1.00 128.29 ? 560  LEU   A CA    1 
ATOM   2220  C  C     . LEU   A 1 560  ? 123.318 175.874 210.400 1.00 128.96 ? 560  LEU   A C     1 
ATOM   2221  O  O     . LEU   A 1 560  ? 123.608 174.807 210.951 1.00 127.91 ? 560  LEU   A O     1 
ATOM   2222  N  N     . THR   A 1 561  ? 123.980 176.340 209.345 1.00 128.67 ? 561  THR   A N     1 
ATOM   2223  C  CA    . THR   A 1 561  ? 125.135 175.665 208.764 1.00 126.64 ? 561  THR   A CA    1 
ATOM   2224  C  C     . THR   A 1 561  ? 125.624 176.528 207.607 1.00 127.07 ? 561  THR   A C     1 
ATOM   2225  O  O     . THR   A 1 561  ? 124.965 177.493 207.208 1.00 126.71 ? 561  THR   A O     1 
ATOM   2226  N  N     . ASN   A 1 562  ? 126.792 176.171 207.072 1.00 129.44 ? 562  ASN   A N     1 
ATOM   2227  C  CA    . ASN   A 1 562  ? 127.353 176.869 205.922 1.00 129.87 ? 562  ASN   A CA    1 
ATOM   2228  C  C     . ASN   A 1 562  ? 127.397 175.986 204.682 1.00 131.43 ? 562  ASN   A C     1 
ATOM   2229  O  O     . ASN   A 1 562  ? 126.779 176.324 203.668 1.00 131.22 ? 562  ASN   A O     1 
ATOM   2230  C  CB    . ASN   A 1 562  ? 128.756 177.393 206.259 1.00 129.12 ? 562  ASN   A CB    1 
ATOM   2231  C  CG    . ASN   A 1 562  ? 128.721 178.668 207.076 1.00 129.44 ? 562  ASN   A CG    1 
ATOM   2232  O  OD1   . ASN   A 1 562  ? 129.068 179.743 206.586 1.00 128.98 ? 562  ASN   A OD1   1 
ATOM   2233  N  ND2   . ASN   A 1 562  ? 128.298 178.557 208.330 1.00 130.07 ? 562  ASN   A ND2   1 
ATOM   2234  N  N     . CYS   A 1 563  ? 128.100 174.857 204.742 1.00 131.45 ? 563  CYS   A N     1 
ATOM   2235  C  CA    . CYS   A 1 563  ? 128.143 173.875 203.657 1.00 131.01 ? 563  CYS   A CA    1 
ATOM   2236  C  C     . CYS   A 1 563  ? 128.192 174.568 202.296 1.00 129.82 ? 563  CYS   A C     1 
ATOM   2237  O  O     . CYS   A 1 563  ? 127.284 174.460 201.471 1.00 130.40 ? 563  CYS   A O     1 
ATOM   2238  C  CB    . CYS   A 1 563  ? 126.971 172.897 203.749 1.00 131.14 ? 563  CYS   A CB    1 
ATOM   2239  S  SG    . CYS   A 1 563  ? 125.329 173.629 203.620 1.00 139.98 ? 563  CYS   A SG    1 
ATOM   2240  N  N     . THR   A 1 564  ? 129.288 175.290 202.068 1.00 115.53 ? 564  THR   A N     1 
ATOM   2241  C  CA    . THR   A 1 564  ? 129.358 176.204 200.936 1.00 114.81 ? 564  THR   A CA    1 
ATOM   2242  C  C     . THR   A 1 564  ? 129.423 175.445 199.617 1.00 115.29 ? 564  THR   A C     1 
ATOM   2243  O  O     . THR   A 1 564  ? 130.442 175.473 198.919 1.00 114.77 ? 564  THR   A O     1 
ATOM   2244  N  N     . SER   A 1 565  ? 128.331 174.768 199.276 1.00 105.68 ? 565  SER   A N     1 
ATOM   2245  C  CA    . SER   A 1 565  ? 128.163 174.085 198.005 1.00 104.78 ? 565  SER   A CA    1 
ATOM   2246  C  C     . SER   A 1 565  ? 126.919 174.624 197.310 1.00 105.80 ? 565  SER   A C     1 
ATOM   2247  O  O     . SER   A 1 565  ? 126.125 175.368 197.892 1.00 105.50 ? 565  SER   A O     1 
ATOM   2248  N  N     . ALA   A 1 566  ? 126.753 174.239 196.044 1.00 103.91 ? 566  ALA   A N     1 
ATOM   2249  C  CA    . ALA   A 1 566  ? 125.623 174.737 195.267 1.00 101.19 ? 566  ALA   A CA    1 
ATOM   2250  C  C     . ALA   A 1 566  ? 124.295 174.316 195.883 1.00 99.86  ? 566  ALA   A C     1 
ATOM   2251  O  O     . ALA   A 1 566  ? 123.362 175.123 195.977 1.00 102.11 ? 566  ALA   A O     1 
ATOM   2252  N  N     . ALA   A 1 567  ? 124.193 173.059 196.320 1.00 95.74  ? 567  ALA   A N     1 
ATOM   2253  C  CA    . ALA   A 1 567  ? 122.929 172.558 196.851 1.00 97.51  ? 567  ALA   A CA    1 
ATOM   2254  C  C     . ALA   A 1 567  ? 122.426 173.428 197.996 1.00 103.12 ? 567  ALA   A C     1 
ATOM   2255  O  O     . ALA   A 1 567  ? 121.268 173.860 198.002 1.00 103.48 ? 567  ALA   A O     1 
ATOM   2256  C  CB    . ALA   A 1 567  ? 123.092 171.107 197.307 1.00 97.27  ? 567  ALA   A CB    1 
ATOM   2257  N  N     . CYS   A 1 568  ? 123.296 173.714 198.968 1.00 102.04 ? 568  CYS   A N     1 
ATOM   2258  C  CA    . CYS   A 1 568  ? 122.895 174.516 200.118 1.00 96.64  ? 568  CYS   A CA    1 
ATOM   2259  C  C     . CYS   A 1 568  ? 122.399 175.899 199.723 1.00 96.30  ? 568  CYS   A C     1 
ATOM   2260  O  O     . CYS   A 1 568  ? 121.677 176.529 200.503 1.00 96.60  ? 568  CYS   A O     1 
ATOM   2261  C  CB    . CYS   A 1 568  ? 124.054 174.658 201.103 1.00 100.64 ? 568  CYS   A CB    1 
ATOM   2262  S  SG    . CYS   A 1 568  ? 124.695 173.110 201.762 1.00 111.66 ? 568  CYS   A SG    1 
ATOM   2263  N  N     . LYS   A 1 569  ? 122.766 176.388 198.538 1.00 92.11  ? 569  LYS   A N     1 
ATOM   2264  C  CA    . LYS   A 1 569  ? 122.362 177.732 198.146 1.00 90.09  ? 569  LYS   A CA    1 
ATOM   2265  C  C     . LYS   A 1 569  ? 120.849 177.881 198.066 1.00 91.31  ? 569  LYS   A C     1 
ATOM   2266  O  O     . LYS   A 1 569  ? 120.347 179.010 198.081 1.00 92.24  ? 569  LYS   A O     1 
ATOM   2267  N  N     . LEU   A 1 570  ? 120.111 176.774 197.985 1.00 87.69  ? 570  LEU   A N     1 
ATOM   2268  C  CA    . LEU   A 1 570  ? 118.657 176.837 197.917 1.00 87.44  ? 570  LEU   A CA    1 
ATOM   2269  C  C     . LEU   A 1 570  ? 118.016 175.982 199.003 1.00 87.86  ? 570  LEU   A C     1 
ATOM   2270  O  O     . LEU   A 1 570  ? 116.965 176.341 199.543 1.00 87.83  ? 570  LEU   A O     1 
ATOM   2271  N  N     . ASN   A 1 571  ? 118.637 174.852 199.328 1.00 89.33  ? 571  ASN   A N     1 
ATOM   2272  C  CA    . ASN   A 1 571  ? 118.105 173.948 200.340 1.00 89.13  ? 571  ASN   A CA    1 
ATOM   2273  C  C     . ASN   A 1 571  ? 119.158 172.893 200.643 1.00 89.28  ? 571  ASN   A C     1 
ATOM   2274  O  O     . ASN   A 1 571  ? 120.132 172.733 199.903 1.00 89.97  ? 571  ASN   A O     1 
ATOM   2275  N  N     . PHE   A 1 572  ? 118.947 172.173 201.740 1.00 91.04  ? 572  PHE   A N     1 
ATOM   2276  C  CA    . PHE   A 1 572  ? 119.865 171.126 202.163 1.00 90.86  ? 572  PHE   A CA    1 
ATOM   2277  C  C     . PHE   A 1 572  ? 119.497 169.753 201.619 1.00 89.30  ? 572  PHE   A C     1 
ATOM   2278  O  O     . PHE   A 1 572  ? 120.171 168.772 201.949 1.00 87.20  ? 572  PHE   A O     1 
ATOM   2279  N  N     . ASP   A 1 573  ? 118.447 169.656 200.807 1.00 90.40  ? 573  ASP   A N     1 
ATOM   2280  C  CA    . ASP   A 1 573  ? 118.038 168.369 200.262 1.00 91.49  ? 573  ASP   A CA    1 
ATOM   2281  C  C     . ASP   A 1 573  ? 119.161 167.779 199.418 1.00 98.34  ? 573  ASP   A C     1 
ATOM   2282  O  O     . ASP   A 1 573  ? 119.757 168.468 198.585 1.00 98.79  ? 573  ASP   A O     1 
ATOM   2283  N  N     . PHE   A 1 574  ? 119.445 166.495 199.633 1.00 87.68  ? 574  PHE   A N     1 
ATOM   2284  C  CA    . PHE   A 1 574  ? 120.522 165.805 198.927 1.00 80.86  ? 574  PHE   A CA    1 
ATOM   2285  C  C     . PHE   A 1 574  ? 121.858 166.512 199.165 1.00 82.05  ? 574  PHE   A C     1 
ATOM   2286  O  O     . PHE   A 1 574  ? 122.495 167.034 198.248 1.00 74.99  ? 574  PHE   A O     1 
ATOM   2287  C  CB    . PHE   A 1 574  ? 120.208 165.699 197.432 1.00 80.39  ? 574  PHE   A CB    1 
ATOM   2288  N  N     . SER   A 1 575  ? 122.267 166.526 200.431 1.00 94.83  ? 575  SER   A N     1 
ATOM   2289  C  CA    . SER   A 1 575  ? 123.444 167.262 200.864 1.00 93.20  ? 575  SER   A CA    1 
ATOM   2290  C  C     . SER   A 1 575  ? 124.357 166.361 201.681 1.00 92.01  ? 575  SER   A C     1 
ATOM   2291  O  O     . SER   A 1 575  ? 123.905 165.426 202.348 1.00 90.78  ? 575  SER   A O     1 
ATOM   2292  C  CB    . SER   A 1 575  ? 123.055 168.490 201.702 1.00 91.19  ? 575  SER   A CB    1 
ATOM   2293  O  OG    . SER   A 1 575  ? 122.906 169.642 200.891 1.00 91.00  ? 575  SER   A OG    1 
ATOM   2294  N  N     . SER   A 1 576  ? 125.654 166.659 201.622 1.00 91.18  ? 576  SER   A N     1 
ATOM   2295  C  CA    . SER   A 1 576  ? 126.658 166.018 202.469 1.00 90.46  ? 576  SER   A CA    1 
ATOM   2296  C  C     . SER   A 1 576  ? 126.705 164.504 202.246 1.00 92.45  ? 576  SER   A C     1 
ATOM   2297  O  O     . SER   A 1 576  ? 126.417 163.704 203.139 1.00 87.27  ? 576  SER   A O     1 
ATOM   2298  C  CB    . SER   A 1 576  ? 126.406 166.348 203.943 1.00 89.25  ? 576  SER   A CB    1 
ATOM   2299  N  N     . CYS   A 1 577  ? 127.080 164.119 201.023 1.00 108.48 ? 577  CYS   A N     1 
ATOM   2300  C  CA    . CYS   A 1 577  ? 127.428 162.732 200.733 1.00 108.15 ? 577  CYS   A CA    1 
ATOM   2301  C  C     . CYS   A 1 577  ? 128.820 162.643 200.117 1.00 106.48 ? 577  CYS   A C     1 
ATOM   2302  O  O     . CYS   A 1 577  ? 129.079 161.783 199.271 1.00 105.81 ? 577  CYS   A O     1 
ATOM   2303  C  CB    . CYS   A 1 577  ? 126.394 162.065 199.823 1.00 107.63 ? 577  CYS   A CB    1 
ATOM   2304  S  SG    . CYS   A 1 577  ? 126.251 162.717 198.140 1.00 118.73 ? 577  CYS   A SG    1 
ATOM   2305  N  N     . GLU   A 1 578  ? 129.726 163.531 200.533 1.00 95.14  ? 578  GLU   A N     1 
ATOM   2306  C  CA    . GLU   A 1 578  ? 131.100 163.498 200.049 1.00 92.61  ? 578  GLU   A CA    1 
ATOM   2307  C  C     . GLU   A 1 578  ? 131.898 162.338 200.628 1.00 94.55  ? 578  GLU   A C     1 
ATOM   2308  O  O     . GLU   A 1 578  ? 133.006 162.072 200.149 1.00 93.11  ? 578  GLU   A O     1 
ATOM   2309  C  CB    . GLU   A 1 578  ? 131.802 164.819 200.372 1.00 91.53  ? 578  GLU   A CB    1 
ATOM   2310  N  N     . SER   A 1 579  ? 131.369 161.648 201.636 1.00 100.49 ? 579  SER   A N     1 
ATOM   2311  C  CA    . SER   A 1 579  ? 132.019 160.487 202.228 1.00 100.09 ? 579  SER   A CA    1 
ATOM   2312  C  C     . SER   A 1 579  ? 131.243 159.201 201.993 1.00 98.98  ? 579  SER   A C     1 
ATOM   2313  O  O     . SER   A 1 579  ? 131.805 158.217 201.504 1.00 99.04  ? 579  SER   A O     1 
ATOM   2314  N  N     . SER   A 1 580  ? 129.957 159.184 202.331 1.00 99.49  ? 580  SER   A N     1 
ATOM   2315  C  CA    . SER   A 1 580  ? 129.134 158.021 202.056 1.00 100.88 ? 580  SER   A CA    1 
ATOM   2316  C  C     . SER   A 1 580  ? 128.686 158.034 200.595 1.00 103.29 ? 580  SER   A C     1 
ATOM   2317  O  O     . SER   A 1 580  ? 128.570 159.098 199.982 1.00 105.25 ? 580  SER   A O     1 
ATOM   2318  N  N     . PRO   A 1 581  ? 128.431 156.864 200.017 1.00 101.14 ? 581  PRO   A N     1 
ATOM   2319  C  CA    . PRO   A 1 581  ? 127.956 156.797 198.619 1.00 100.25 ? 581  PRO   A CA    1 
ATOM   2320  C  C     . PRO   A 1 581  ? 126.458 157.071 198.513 1.00 100.67 ? 581  PRO   A C     1 
ATOM   2321  O  O     . PRO   A 1 581  ? 125.614 156.176 198.463 1.00 100.40 ? 581  PRO   A O     1 
ATOM   2322  C  CB    . PRO   A 1 581  ? 128.313 155.364 198.208 1.00 99.78  ? 581  PRO   A CB    1 
ATOM   2323  C  CG    . PRO   A 1 581  ? 128.950 154.705 199.430 1.00 99.30  ? 581  PRO   A CG    1 
ATOM   2324  C  CD    . PRO   A 1 581  ? 128.572 155.528 200.608 1.00 99.15  ? 581  PRO   A CD    1 
ATOM   2325  N  N     . CYS   A 1 582  ? 126.110 158.355 198.478 1.00 102.01 ? 582  CYS   A N     1 
ATOM   2326  C  CA    . CYS   A 1 582  ? 124.708 158.738 198.429 1.00 102.04 ? 582  CYS   A CA    1 
ATOM   2327  C  C     . CYS   A 1 582  ? 124.036 158.154 197.187 1.00 101.24 ? 582  CYS   A C     1 
ATOM   2328  O  O     . CYS   A 1 582  ? 124.671 157.893 196.162 1.00 95.71  ? 582  CYS   A O     1 
ATOM   2329  C  CB    . CYS   A 1 582  ? 124.569 160.261 198.500 1.00 101.00 ? 582  CYS   A CB    1 
ATOM   2330  S  SG    . CYS   A 1 582  ? 125.288 161.221 197.151 1.00 113.37 ? 582  CYS   A SG    1 
ATOM   2331  N  N     . SER   A 1 583  ? 122.723 157.945 197.303 1.00 91.68  ? 583  SER   A N     1 
ATOM   2332  C  CA    . SER   A 1 583  ? 122.026 157.003 196.430 1.00 86.27  ? 583  SER   A CA    1 
ATOM   2333  C  C     . SER   A 1 583  ? 122.217 157.336 194.955 1.00 82.51  ? 583  SER   A C     1 
ATOM   2334  O  O     . SER   A 1 583  ? 122.591 156.468 194.158 1.00 85.76  ? 583  SER   A O     1 
ATOM   2335  N  N     . TYR   A 1 584  ? 121.962 158.580 194.569 1.00 75.03  ? 584  TYR   A N     1 
ATOM   2336  C  CA    . TYR   A 1 584  ? 121.922 158.900 193.148 1.00 77.35  ? 584  TYR   A CA    1 
ATOM   2337  C  C     . TYR   A 1 584  ? 122.250 160.380 192.958 1.00 76.59  ? 584  TYR   A C     1 
ATOM   2338  O  O     . TYR   A 1 584  ? 122.759 161.037 193.873 1.00 82.27  ? 584  TYR   A O     1 
ATOM   2339  C  CB    . TYR   A 1 584  ? 120.561 158.497 192.554 1.00 75.78  ? 584  TYR   A CB    1 
ATOM   2340  C  CG    . TYR   A 1 584  ? 119.353 159.062 193.272 1.00 74.27  ? 584  TYR   A CG    1 
ATOM   2341  C  CD1   . TYR   A 1 584  ? 118.344 158.224 193.727 1.00 74.39  ? 584  TYR   A CD1   1 
ATOM   2342  C  CD2   . TYR   A 1 584  ? 119.204 160.429 193.468 1.00 74.24  ? 584  TYR   A CD2   1 
ATOM   2343  C  CE1   . TYR   A 1 584  ? 117.235 158.726 194.376 1.00 74.81  ? 584  TYR   A CE1   1 
ATOM   2344  C  CE2   . TYR   A 1 584  ? 118.096 160.941 194.115 1.00 77.84  ? 584  TYR   A CE2   1 
ATOM   2345  C  CZ    . TYR   A 1 584  ? 117.114 160.084 194.566 1.00 79.50  ? 584  TYR   A CZ    1 
ATOM   2346  O  OH    . TYR   A 1 584  ? 116.009 160.587 195.211 1.00 83.95  ? 584  TYR   A OH    1 
ATOM   2347  N  N     . GLY   A 1 585  ? 121.976 160.892 191.768 1.00 65.81  ? 585  GLY   A N     1 
ATOM   2348  C  CA    . GLY   A 1 585  ? 122.285 162.249 191.391 1.00 62.17  ? 585  GLY   A CA    1 
ATOM   2349  C  C     . GLY   A 1 585  ? 122.828 162.284 189.980 1.00 66.13  ? 585  GLY   A C     1 
ATOM   2350  O  O     . GLY   A 1 585  ? 122.766 161.301 189.243 1.00 67.72  ? 585  GLY   A O     1 
ATOM   2351  N  N     . LEU   A 1 586  ? 123.374 163.441 189.604 1.00 60.60  ? 586  LEU   A N     1 
ATOM   2352  C  CA    . LEU   A 1 586  ? 123.886 163.614 188.250 1.00 52.44  ? 586  LEU   A CA    1 
ATOM   2353  C  C     . LEU   A 1 586  ? 125.094 162.730 187.968 1.00 53.54  ? 586  LEU   A C     1 
ATOM   2354  O  O     . LEU   A 1 586  ? 125.475 162.578 186.803 1.00 57.15  ? 586  LEU   A O     1 
ATOM   2355  C  CB    . LEU   A 1 586  ? 124.246 165.080 188.010 1.00 53.40  ? 586  LEU   A CB    1 
ATOM   2356  C  CG    . LEU   A 1 586  ? 124.228 165.553 186.557 1.00 46.26  ? 586  LEU   A CG    1 
ATOM   2357  C  CD1   . LEU   A 1 586  ? 122.828 165.436 185.975 1.00 54.37  ? 586  LEU   A CD1   1 
ATOM   2358  C  CD2   . LEU   A 1 586  ? 124.740 166.977 186.449 1.00 51.32  ? 586  LEU   A CD2   1 
ATOM   2359  N  N     . MET   A 1 587  ? 125.704 162.147 189.001 1.00 60.35  ? 587  MET   A N     1 
ATOM   2360  C  CA    . MET   A 1 587  ? 126.863 161.282 188.828 1.00 57.71  ? 587  MET   A CA    1 
ATOM   2361  C  C     . MET   A 1 587  ? 126.628 159.853 189.298 1.00 57.75  ? 587  MET   A C     1 
ATOM   2362  O  O     . MET   A 1 587  ? 127.536 159.023 189.179 1.00 62.53  ? 587  MET   A O     1 
ATOM   2363  C  CB    . MET   A 1 587  ? 128.078 161.863 189.565 1.00 53.94  ? 587  MET   A CB    1 
ATOM   2364  C  CG    . MET   A 1 587  ? 129.386 161.164 189.240 1.00 60.29  ? 587  MET   A CG    1 
ATOM   2365  S  SD    . MET   A 1 587  ? 130.804 162.273 189.241 1.00 73.01  ? 587  MET   A SD    1 
ATOM   2366  C  CE    . MET   A 1 587  ? 130.172 163.625 188.260 1.00 59.68  ? 587  MET   A CE    1 
ATOM   2367  N  N     . ASN   A 1 588  ? 125.445 159.537 189.821 1.00 55.94  ? 588  ASN   A N     1 
ATOM   2368  C  CA    . ASN   A 1 588  ? 125.170 158.203 190.339 1.00 61.17  ? 588  ASN   A CA    1 
ATOM   2369  C  C     . ASN   A 1 588  ? 123.877 157.586 189.831 1.00 61.01  ? 588  ASN   A C     1 
ATOM   2370  O  O     . ASN   A 1 588  ? 123.664 156.389 190.057 1.00 62.48  ? 588  ASN   A O     1 
ATOM   2371  C  CB    . ASN   A 1 588  ? 125.135 158.221 191.875 1.00 58.78  ? 588  ASN   A CB    1 
ATOM   2372  N  N     . ASN   A 1 589  ? 123.015 158.343 189.158 1.00 58.16  ? 589  ASN   A N     1 
ATOM   2373  C  CA    . ASN   A 1 589  ? 121.766 157.827 188.616 1.00 59.27  ? 589  ASN   A CA    1 
ATOM   2374  C  C     . ASN   A 1 589  ? 121.744 158.051 187.112 1.00 65.99  ? 589  ASN   A C     1 
ATOM   2375  O  O     . ASN   A 1 589  ? 122.049 159.152 186.640 1.00 68.35  ? 589  ASN   A O     1 
ATOM   2376  C  CB    . ASN   A 1 589  ? 120.561 158.504 189.272 1.00 60.15  ? 589  ASN   A CB    1 
ATOM   2377  C  CG    . ASN   A 1 589  ? 119.255 157.813 188.942 1.00 64.58  ? 589  ASN   A CG    1 
ATOM   2378  O  OD1   . ASN   A 1 589  ? 119.233 156.626 188.617 1.00 66.13  ? 589  ASN   A OD1   1 
ATOM   2379  N  ND2   . ASN   A 1 589  ? 118.157 158.554 189.024 1.00 60.84  ? 589  ASN   A ND2   1 
ATOM   2380  N  N     . PHE   A 1 590  ? 121.386 157.010 186.364 1.00 59.21  ? 590  PHE   A N     1 
ATOM   2381  C  CA    . PHE   A 1 590  ? 121.312 157.085 184.913 1.00 55.30  ? 590  PHE   A CA    1 
ATOM   2382  C  C     . PHE   A 1 590  ? 119.892 157.281 184.400 1.00 60.47  ? 590  PHE   A C     1 
ATOM   2383  O  O     . PHE   A 1 590  ? 119.678 157.250 183.185 1.00 70.89  ? 590  PHE   A O     1 
ATOM   2384  C  CB    . PHE   A 1 590  ? 121.923 155.827 184.287 1.00 54.50  ? 590  PHE   A CB    1 
ATOM   2385  C  CG    . PHE   A 1 590  ? 123.382 155.650 184.592 1.00 56.51  ? 590  PHE   A CG    1 
ATOM   2386  C  CD1   . PHE   A 1 590  ? 124.333 156.436 183.966 1.00 56.93  ? 590  PHE   A CD1   1 
ATOM   2387  C  CD2   . PHE   A 1 590  ? 123.804 154.704 185.510 1.00 59.90  ? 590  PHE   A CD2   1 
ATOM   2388  C  CE1   . PHE   A 1 590  ? 125.676 156.281 184.245 1.00 58.99  ? 590  PHE   A CE1   1 
ATOM   2389  C  CE2   . PHE   A 1 590  ? 125.146 154.545 185.793 1.00 61.46  ? 590  PHE   A CE2   1 
ATOM   2390  C  CZ    . PHE   A 1 590  ? 126.083 155.334 185.159 1.00 58.76  ? 590  PHE   A CZ    1 
ATOM   2391  N  N     . GLN   A 1 591  ? 118.921 157.481 185.291 1.00 49.53  ? 591  GLN   A N     1 
ATOM   2392  C  CA    . GLN   A 1 591  ? 117.541 157.749 184.910 1.00 52.70  ? 591  GLN   A CA    1 
ATOM   2393  C  C     . GLN   A 1 591  ? 117.152 159.198 185.184 1.00 55.86  ? 591  GLN   A C     1 
ATOM   2394  O  O     . GLN   A 1 591  ? 115.971 159.508 185.353 1.00 61.53  ? 591  GLN   A O     1 
ATOM   2395  C  CB    . GLN   A 1 591  ? 116.585 156.801 185.632 1.00 57.06  ? 591  GLN   A CB    1 
ATOM   2396  C  CG    . GLN   A 1 591  ? 117.165 155.434 185.928 1.00 57.99  ? 591  GLN   A CG    1 
ATOM   2397  C  CD    . GLN   A 1 591  ? 117.526 154.674 184.671 1.00 61.53  ? 591  GLN   A CD    1 
ATOM   2398  O  OE1   . GLN   A 1 591  ? 118.684 154.656 184.254 1.00 63.11  ? 591  GLN   A OE1   1 
ATOM   2399  N  NE2   . GLN   A 1 591  ? 116.534 154.043 184.055 1.00 62.60  ? 591  GLN   A NE2   1 
ATOM   2400  N  N     . VAL   A 1 592  ? 118.138 160.095 185.229 1.00 51.08  ? 592  VAL   A N     1 
ATOM   2401  C  CA    . VAL   A 1 592  ? 117.856 161.498 185.522 1.00 54.79  ? 592  VAL   A CA    1 
ATOM   2402  C  C     . VAL   A 1 592  ? 116.848 162.052 184.524 1.00 56.01  ? 592  VAL   A C     1 
ATOM   2403  O  O     . VAL   A 1 592  ? 115.880 162.725 184.899 1.00 59.18  ? 592  VAL   A O     1 
ATOM   2404  C  CB    . VAL   A 1 592  ? 119.159 162.317 185.525 1.00 54.92  ? 592  VAL   A CB    1 
ATOM   2405  C  CG1   . VAL   A 1 592  ? 118.862 163.793 185.739 1.00 55.75  ? 592  VAL   A CG1   1 
ATOM   2406  C  CG2   . VAL   A 1 592  ? 120.111 161.797 186.591 1.00 52.53  ? 592  VAL   A CG2   1 
ATOM   2407  N  N     . MET   A 1 593  ? 117.052 161.766 183.236 1.00 56.93  ? 593  MET   A N     1 
ATOM   2408  C  CA    . MET   A 1 593  ? 116.118 162.237 182.220 1.00 57.04  ? 593  MET   A CA    1 
ATOM   2409  C  C     . MET   A 1 593  ? 114.709 161.720 182.474 1.00 62.54  ? 593  MET   A C     1 
ATOM   2410  O  O     . MET   A 1 593  ? 113.731 162.424 182.198 1.00 66.56  ? 593  MET   A O     1 
ATOM   2411  C  CB    . MET   A 1 593  ? 116.596 161.817 180.830 1.00 59.80  ? 593  MET   A CB    1 
ATOM   2412  C  CG    . MET   A 1 593  ? 117.396 162.882 180.100 1.00 61.25  ? 593  MET   A CG    1 
ATOM   2413  S  SD    . MET   A 1 593  ? 118.875 163.377 181.000 1.00 71.62  ? 593  MET   A SD    1 
ATOM   2414  C  CE    . MET   A 1 593  ? 119.493 164.679 179.940 1.00 61.64  ? 593  MET   A CE    1 
ATOM   2415  N  N     . SER   A 1 594  ? 114.583 160.498 182.997 1.00 59.14  ? 594  SER   A N     1 
ATOM   2416  C  CA    . SER   A 1 594  ? 113.266 159.941 183.277 1.00 49.62  ? 594  SER   A CA    1 
ATOM   2417  C  C     . SER   A 1 594  ? 112.620 160.561 184.508 1.00 55.85  ? 594  SER   A C     1 
ATOM   2418  O  O     . SER   A 1 594  ? 111.413 160.389 184.711 1.00 65.35  ? 594  SER   A O     1 
ATOM   2419  C  CB    . SER   A 1 594  ? 113.363 158.425 183.451 1.00 50.29  ? 594  SER   A CB    1 
ATOM   2420  N  N     . MET   A 1 595  ? 113.387 161.276 185.332 1.00 57.29  ? 595  MET   A N     1 
ATOM   2421  C  CA    . MET   A 1 595  ? 112.831 161.907 186.523 1.00 52.96  ? 595  MET   A CA    1 
ATOM   2422  C  C     . MET   A 1 595  ? 112.575 163.394 186.321 1.00 52.34  ? 595  MET   A C     1 
ATOM   2423  O  O     . MET   A 1 595  ? 111.538 163.908 186.754 1.00 61.78  ? 595  MET   A O     1 
ATOM   2424  C  CB    . MET   A 1 595  ? 113.764 161.697 187.718 1.00 57.09  ? 595  MET   A CB    1 
ATOM   2425  C  CG    . MET   A 1 595  ? 113.436 162.563 188.922 1.00 56.72  ? 595  MET   A CG    1 
ATOM   2426  S  SD    . MET   A 1 595  ? 114.633 163.886 189.177 1.00 63.35  ? 595  MET   A SD    1 
ATOM   2427  C  CE    . MET   A 1 595  ? 116.158 162.951 189.237 1.00 54.91  ? 595  MET   A CE    1 
ATOM   2428  N  N     . VAL   A 1 596  ? 113.503 164.098 185.670 1.00 45.69  ? 596  VAL   A N     1 
ATOM   2429  C  CA    . VAL   A 1 596  ? 113.303 165.511 185.379 1.00 43.91  ? 596  VAL   A CA    1 
ATOM   2430  C  C     . VAL   A 1 596  ? 112.141 165.720 184.424 1.00 53.23  ? 596  VAL   A C     1 
ATOM   2431  O  O     . VAL   A 1 596  ? 111.601 166.827 184.334 1.00 57.29  ? 596  VAL   A O     1 
ATOM   2432  C  CB    . VAL   A 1 596  ? 114.596 166.126 184.807 1.00 47.53  ? 596  VAL   A CB    1 
ATOM   2433  C  CG1   . VAL   A 1 596  ? 114.450 167.631 184.668 1.00 55.41  ? 596  VAL   A CG1   1 
ATOM   2434  C  CG2   . VAL   A 1 596  ? 115.782 165.775 185.688 1.00 54.84  ? 596  VAL   A CG2   1 
ATOM   2435  N  N     . SER   A 1 597  ? 111.741 164.678 183.703 1.00 59.72  ? 597  SER   A N     1 
ATOM   2436  C  CA    . SER   A 1 597  ? 110.664 164.772 182.728 1.00 54.39  ? 597  SER   A CA    1 
ATOM   2437  C  C     . SER   A 1 597  ? 109.317 164.794 183.446 1.00 55.89  ? 597  SER   A C     1 
ATOM   2438  O  O     . SER   A 1 597  ? 109.234 164.885 184.674 1.00 65.25  ? 597  SER   A O     1 
ATOM   2439  C  CB    . SER   A 1 597  ? 110.754 163.620 181.733 1.00 60.60  ? 597  SER   A CB    1 
ATOM   2440  O  OG    . SER   A 1 597  ? 110.397 162.393 182.347 1.00 64.67  ? 597  SER   A OG    1 
ATOM   2441  N  N     . GLY   A 1 598  ? 108.241 164.715 182.671 1.00 48.79  ? 598  GLY   A N     1 
ATOM   2442  C  CA    . GLY   A 1 598  ? 106.906 164.595 183.217 1.00 52.41  ? 598  GLY   A CA    1 
ATOM   2443  C  C     . GLY   A 1 598  ? 106.448 163.153 183.176 1.00 59.53  ? 598  GLY   A C     1 
ATOM   2444  O  O     . GLY   A 1 598  ? 106.799 162.359 184.053 1.00 65.13  ? 598  GLY   A O     1 
ATOM   2445  N  N     . PHE   A 1 599  ? 105.657 162.802 182.165 1.00 56.07  ? 599  PHE   A N     1 
ATOM   2446  C  CA    . PHE   A 1 599  ? 105.228 161.422 181.983 1.00 53.51  ? 599  PHE   A CA    1 
ATOM   2447  C  C     . PHE   A 1 599  ? 106.441 160.516 181.797 1.00 59.44  ? 599  PHE   A C     1 
ATOM   2448  O  O     . PHE   A 1 599  ? 107.097 160.558 180.751 1.00 67.63  ? 599  PHE   A O     1 
ATOM   2449  C  CB    . PHE   A 1 599  ? 104.288 161.319 180.780 1.00 55.10  ? 599  PHE   A CB    1 
ATOM   2450  C  CG    . PHE   A 1 599  ? 103.164 160.343 180.965 1.00 56.10  ? 599  PHE   A CG    1 
ATOM   2451  C  CD1   . PHE   A 1 599  ? 103.221 159.377 181.952 1.00 56.47  ? 599  PHE   A CD1   1 
ATOM   2452  C  CD2   . PHE   A 1 599  ? 102.050 160.391 180.146 1.00 60.62  ? 599  PHE   A CD2   1 
ATOM   2453  C  CE1   . PHE   A 1 599  ? 102.187 158.478 182.121 1.00 60.94  ? 599  PHE   A CE1   1 
ATOM   2454  C  CE2   . PHE   A 1 599  ? 101.013 159.495 180.310 1.00 60.76  ? 599  PHE   A CE2   1 
ATOM   2455  C  CZ    . PHE   A 1 599  ? 101.082 158.537 181.299 1.00 63.75  ? 599  PHE   A CZ    1 
ATOM   2456  N  N     . THR   A 1 600  ? 106.748 159.694 182.803 1.00 56.79  ? 600  THR   A N     1 
ATOM   2457  C  CA    . THR   A 1 600  ? 107.904 158.801 182.713 1.00 57.73  ? 600  THR   A CA    1 
ATOM   2458  C  C     . THR   A 1 600  ? 107.770 157.777 181.593 1.00 64.77  ? 600  THR   A C     1 
ATOM   2459  O  O     . THR   A 1 600  ? 108.752 157.560 180.856 1.00 68.82  ? 600  THR   A O     1 
ATOM   2460  C  CB    . THR   A 1 600  ? 108.124 158.112 184.063 1.00 47.59  ? 600  THR   A CB    1 
ATOM   2461  N  N     . PRO   A 1 601  ? 106.628 157.112 181.412 1.00 54.87  ? 601  PRO   A N     1 
ATOM   2462  C  CA    . PRO   A 1 601  ? 106.502 156.187 180.277 1.00 57.80  ? 601  PRO   A CA    1 
ATOM   2463  C  C     . PRO   A 1 601  ? 106.725 156.856 178.937 1.00 59.04  ? 601  PRO   A C     1 
ATOM   2464  O  O     . PRO   A 1 601  ? 107.115 156.175 177.985 1.00 59.05  ? 601  PRO   A O     1 
ATOM   2465  C  CB    . PRO   A 1 601  ? 105.071 155.643 180.410 1.00 55.42  ? 601  PRO   A CB    1 
ATOM   2466  C  CG    . PRO   A 1 601  ? 104.645 155.973 181.796 1.00 56.59  ? 601  PRO   A CG    1 
ATOM   2467  C  CD    . PRO   A 1 601  ? 105.403 157.180 182.221 1.00 52.59  ? 601  PRO   A CD    1 
ATOM   2468  N  N     . LEU   A 1 602  ? 106.504 158.167 178.828 1.00 54.44  ? 602  LEU   A N     1 
ATOM   2469  C  CA    . LEU   A 1 602  ? 106.866 158.864 177.599 1.00 47.36  ? 602  LEU   A CA    1 
ATOM   2470  C  C     . LEU   A 1 602  ? 108.365 158.771 177.340 1.00 49.09  ? 602  LEU   A C     1 
ATOM   2471  O  O     . LEU   A 1 602  ? 108.792 158.503 176.212 1.00 60.06  ? 602  LEU   A O     1 
ATOM   2472  C  CB    . LEU   A 1 602  ? 106.420 160.323 177.668 1.00 53.20  ? 602  LEU   A CB    1 
ATOM   2473  C  CG    . LEU   A 1 602  ? 106.240 161.026 176.321 1.00 54.02  ? 602  LEU   A CG    1 
ATOM   2474  C  CD1   . LEU   A 1 602  ? 105.398 160.177 175.383 1.00 53.44  ? 602  LEU   A CD1   1 
ATOM   2475  C  CD2   . LEU   A 1 602  ? 105.621 162.401 176.508 1.00 55.63  ? 602  LEU   A CD2   1 
ATOM   2476  N  N     . ILE   A 1 603  ? 109.183 158.972 178.375 1.00 43.18  ? 603  ILE   A N     1 
ATOM   2477  C  CA    . ILE   A 1 603  ? 110.628 158.850 178.210 1.00 48.54  ? 603  ILE   A CA    1 
ATOM   2478  C  C     . ILE   A 1 603  ? 111.014 157.403 177.929 1.00 51.09  ? 603  ILE   A C     1 
ATOM   2479  O  O     . ILE   A 1 603  ? 111.924 157.128 177.134 1.00 56.12  ? 603  ILE   A O     1 
ATOM   2480  C  CB    . ILE   A 1 603  ? 111.357 159.401 179.448 1.00 51.41  ? 603  ILE   A CB    1 
ATOM   2481  C  CG1   . ILE   A 1 603  ? 111.165 160.915 179.549 1.00 52.39  ? 603  ILE   A CG1   1 
ATOM   2482  C  CG2   . ILE   A 1 603  ? 112.837 159.054 179.392 1.00 49.54  ? 603  ILE   A CG2   1 
ATOM   2483  C  CD1   . ILE   A 1 603  ? 112.162 161.714 178.741 1.00 48.43  ? 603  ILE   A CD1   1 
ATOM   2484  N  N     . SER   A 1 604  ? 110.340 156.454 178.582 1.00 54.17  ? 604  SER   A N     1 
ATOM   2485  C  CA    . SER   A 1 604  ? 110.626 155.048 178.310 1.00 51.27  ? 604  SER   A CA    1 
ATOM   2486  C  C     . SER   A 1 604  ? 110.343 154.703 176.851 1.00 54.34  ? 604  SER   A C     1 
ATOM   2487  O  O     . SER   A 1 604  ? 111.137 154.014 176.197 1.00 56.89  ? 604  SER   A O     1 
ATOM   2488  C  CB    . SER   A 1 604  ? 109.809 154.156 179.245 1.00 54.54  ? 604  SER   A CB    1 
ATOM   2489  O  OG    . SER   A 1 604  ? 110.271 154.260 180.580 1.00 60.95  ? 604  SER   A OG    1 
ATOM   2490  N  N     . ALA   A 1 605  ? 109.219 155.187 176.318 1.00 52.78  ? 605  ALA   A N     1 
ATOM   2491  C  CA    . ALA   A 1 605  ? 108.902 154.971 174.912 1.00 45.56  ? 605  ALA   A CA    1 
ATOM   2492  C  C     . ALA   A 1 605  ? 109.875 155.703 174.001 1.00 49.60  ? 605  ALA   A C     1 
ATOM   2493  O  O     . ALA   A 1 605  ? 110.176 155.221 172.905 1.00 53.73  ? 605  ALA   A O     1 
ATOM   2494  C  CB    . ALA   A 1 605  ? 107.468 155.410 174.620 1.00 47.41  ? 605  ALA   A CB    1 
ATOM   2495  N  N     . GLY   A 1 606  ? 110.362 156.870 174.421 1.00 49.98  ? 606  GLY   A N     1 
ATOM   2496  C  CA    . GLY   A 1 606  ? 111.388 157.546 173.646 1.00 47.16  ? 606  GLY   A CA    1 
ATOM   2497  C  C     . GLY   A 1 606  ? 112.650 156.716 173.522 1.00 49.62  ? 606  GLY   A C     1 
ATOM   2498  O  O     . GLY   A 1 606  ? 113.241 156.623 172.444 1.00 53.98  ? 606  GLY   A O     1 
ATOM   2499  N  N     . ILE   A 1 607  ? 113.072 156.089 174.622 1.00 47.30  ? 607  ILE   A N     1 
ATOM   2500  C  CA    . ILE   A 1 607  ? 114.232 155.200 174.569 1.00 48.11  ? 607  ILE   A CA    1 
ATOM   2501  C  C     . ILE   A 1 607  ? 113.941 153.998 173.676 1.00 51.70  ? 607  ILE   A C     1 
ATOM   2502  O  O     . ILE   A 1 607  ? 114.790 153.568 172.877 1.00 55.10  ? 607  ILE   A O     1 
ATOM   2503  C  CB    . ILE   A 1 607  ? 114.641 154.764 175.988 1.00 50.48  ? 607  ILE   A CB    1 
ATOM   2504  C  CG1   . ILE   A 1 607  ? 115.532 155.822 176.638 1.00 53.90  ? 607  ILE   A CG1   1 
ATOM   2505  C  CG2   . ILE   A 1 607  ? 115.355 153.425 175.946 1.00 48.44  ? 607  ILE   A CG2   1 
ATOM   2506  C  CD1   . ILE   A 1 607  ? 115.342 155.945 178.132 1.00 51.97  ? 607  ILE   A CD1   1 
ATOM   2507  N  N     . PHE   A 1 608  ? 112.741 153.428 173.810 1.00 48.75  ? 608  PHE   A N     1 
ATOM   2508  C  CA    . PHE   A 1 608  ? 112.345 152.311 172.958 1.00 43.28  ? 608  PHE   A CA    1 
ATOM   2509  C  C     . PHE   A 1 608  ? 112.469 152.680 171.485 1.00 46.59  ? 608  PHE   A C     1 
ATOM   2510  O  O     . PHE   A 1 608  ? 113.038 151.926 170.686 1.00 51.02  ? 608  PHE   A O     1 
ATOM   2511  C  CB    . PHE   A 1 608  ? 110.909 151.898 173.281 1.00 48.68  ? 608  PHE   A CB    1 
ATOM   2512  C  CG    . PHE   A 1 608  ? 110.775 151.094 174.539 1.00 51.07  ? 608  PHE   A CG    1 
ATOM   2513  C  CD1   . PHE   A 1 608  ? 111.777 150.229 174.935 1.00 53.95  ? 608  PHE   A CD1   1 
ATOM   2514  C  CD2   . PHE   A 1 608  ? 109.644 151.207 175.330 1.00 44.83  ? 608  PHE   A CD2   1 
ATOM   2515  C  CE1   . PHE   A 1 608  ? 111.653 149.488 176.091 1.00 54.55  ? 608  PHE   A CE1   1 
ATOM   2516  C  CE2   . PHE   A 1 608  ? 109.517 150.468 176.489 1.00 49.20  ? 608  PHE   A CE2   1 
ATOM   2517  C  CZ    . PHE   A 1 608  ? 110.523 149.608 176.870 1.00 48.92  ? 608  PHE   A CZ    1 
ATOM   2518  N  N     . SER   A 1 609  ? 111.929 153.840 171.109 1.00 51.52  ? 609  SER   A N     1 
ATOM   2519  C  CA    . SER   A 1 609  ? 111.988 154.280 169.720 1.00 46.33  ? 609  SER   A CA    1 
ATOM   2520  C  C     . SER   A 1 609  ? 113.422 154.539 169.286 1.00 41.63  ? 609  SER   A C     1 
ATOM   2521  O  O     . SER   A 1 609  ? 113.810 154.194 168.165 1.00 46.52  ? 609  SER   A O     1 
ATOM   2522  C  CB    . SER   A 1 609  ? 111.139 155.537 169.532 1.00 41.13  ? 609  SER   A CB    1 
ATOM   2523  O  OG    . SER   A 1 609  ? 111.320 156.438 170.609 1.00 52.34  ? 609  SER   A OG    1 
ATOM   2524  N  N     . ALA   A 1 610  ? 114.226 155.148 170.159 1.00 38.14  ? 610  ALA   A N     1 
ATOM   2525  C  CA    . ALA   A 1 610  ? 115.611 155.432 169.806 1.00 40.55  ? 610  ALA   A CA    1 
ATOM   2526  C  C     . ALA   A 1 610  ? 116.363 154.152 169.473 1.00 42.39  ? 610  ALA   A C     1 
ATOM   2527  O  O     . ALA   A 1 610  ? 117.141 154.112 168.513 1.00 48.59  ? 610  ALA   A O     1 
ATOM   2528  C  CB    . ALA   A 1 610  ? 116.299 156.181 170.946 1.00 35.75  ? 610  ALA   A CB    1 
ATOM   2529  N  N     . THR   A 1 611  ? 116.144 153.092 170.253 1.00 41.84  ? 611  THR   A N     1 
ATOM   2530  C  CA    . THR   A 1 611  ? 116.833 151.837 169.965 1.00 45.43  ? 611  THR   A CA    1 
ATOM   2531  C  C     . THR   A 1 611  ? 116.251 151.148 168.732 1.00 39.57  ? 611  THR   A C     1 
ATOM   2532  O  O     . THR   A 1 611  ? 116.999 150.643 167.881 1.00 40.82  ? 611  THR   A O     1 
ATOM   2533  C  CB    . THR   A 1 611  ? 116.778 150.912 171.184 1.00 47.78  ? 611  THR   A CB    1 
ATOM   2534  O  OG1   . THR   A 1 611  ? 117.495 149.703 170.905 1.00 58.18  ? 611  THR   A OG1   1 
ATOM   2535  C  CG2   . THR   A 1 611  ? 115.344 150.568 171.538 1.00 47.64  ? 611  THR   A CG2   1 
ATOM   2536  N  N     . LEU   A 1 612  ? 114.920 151.127 168.612 1.00 41.28  ? 612  LEU   A N     1 
ATOM   2537  C  CA    . LEU   A 1 612  ? 114.287 150.389 167.524 1.00 38.54  ? 612  LEU   A CA    1 
ATOM   2538  C  C     . LEU   A 1 612  ? 114.585 151.019 166.170 1.00 42.45  ? 612  LEU   A C     1 
ATOM   2539  O  O     . LEU   A 1 612  ? 114.783 150.304 165.181 1.00 49.73  ? 612  LEU   A O     1 
ATOM   2540  C  CB    . LEU   A 1 612  ? 112.779 150.302 167.758 1.00 39.34  ? 612  LEU   A CB    1 
ATOM   2541  C  CG    . LEU   A 1 612  ? 112.325 149.281 168.803 1.00 43.42  ? 612  LEU   A CG    1 
ATOM   2542  C  CD1   . LEU   A 1 612  ? 110.809 149.244 168.892 1.00 45.87  ? 612  LEU   A CD1   1 
ATOM   2543  C  CD2   . LEU   A 1 612  ? 112.880 147.902 168.488 1.00 40.70  ? 612  LEU   A CD2   1 
ATOM   2544  N  N     . SER   A 1 613  ? 114.610 152.352 166.096 1.00 41.83  ? 613  SER   A N     1 
ATOM   2545  C  CA    . SER   A 1 613  ? 114.897 153.009 164.826 1.00 39.69  ? 613  SER   A CA    1 
ATOM   2546  C  C     . SER   A 1 613  ? 116.303 152.683 164.345 1.00 43.14  ? 613  SER   A C     1 
ATOM   2547  O  O     . SER   A 1 613  ? 116.512 152.400 163.160 1.00 49.35  ? 613  SER   A O     1 
ATOM   2548  C  CB    . SER   A 1 613  ? 114.716 154.520 164.964 1.00 40.39  ? 613  SER   A CB    1 
ATOM   2549  O  OG    . SER   A 1 613  ? 115.263 154.987 166.184 1.00 48.53  ? 613  SER   A OG    1 
ATOM   2550  N  N     . SER   A 1 614  ? 117.282 152.716 165.251 1.00 37.51  ? 614  SER   A N     1 
ATOM   2551  C  CA    . SER   A 1 614  ? 118.646 152.363 164.874 1.00 36.34  ? 614  SER   A CA    1 
ATOM   2552  C  C     . SER   A 1 614  ? 118.736 150.907 164.439 1.00 38.80  ? 614  SER   A C     1 
ATOM   2553  O  O     . SER   A 1 614  ? 119.404 150.586 163.446 1.00 47.38  ? 614  SER   A O     1 
ATOM   2554  C  CB    . SER   A 1 614  ? 119.600 152.637 166.035 1.00 39.81  ? 614  SER   A CB    1 
ATOM   2555  O  OG    . SER   A 1 614  ? 119.697 154.026 166.297 1.00 39.82  ? 614  SER   A OG    1 
ATOM   2556  N  N     . ALA   A 1 615  ? 118.070 150.007 165.167 1.00 42.12  ? 615  ALA   A N     1 
ATOM   2557  C  CA    . ALA   A 1 615  ? 118.094 148.600 164.779 1.00 39.07  ? 615  ALA   A CA    1 
ATOM   2558  C  C     . ALA   A 1 615  ? 117.507 148.410 163.385 1.00 40.30  ? 615  ALA   A C     1 
ATOM   2559  O  O     . ALA   A 1 615  ? 118.079 147.703 162.545 1.00 46.92  ? 615  ALA   A O     1 
ATOM   2560  C  CB    . ALA   A 1 615  ? 117.334 147.758 165.803 1.00 40.60  ? 615  ALA   A CB    1 
ATOM   2561  N  N     . LEU   A 1 616  ? 116.364 149.046 163.119 1.00 37.38  ? 616  LEU   A N     1 
ATOM   2562  C  CA    . LEU   A 1 616  ? 115.728 148.920 161.812 1.00 35.53  ? 616  LEU   A CA    1 
ATOM   2563  C  C     . LEU   A 1 616  ? 116.610 149.494 160.713 1.00 45.99  ? 616  LEU   A C     1 
ATOM   2564  O  O     . LEU   A 1 616  ? 116.745 148.896 159.638 1.00 49.67  ? 616  LEU   A O     1 
ATOM   2565  C  CB    . LEU   A 1 616  ? 114.369 149.620 161.825 1.00 40.16  ? 616  LEU   A CB    1 
ATOM   2566  C  CG    . LEU   A 1 616  ? 113.117 148.757 161.663 1.00 48.54  ? 616  LEU   A CG    1 
ATOM   2567  C  CD1   . LEU   A 1 616  ? 111.916 149.625 161.318 1.00 42.88  ? 616  LEU   A CD1   1 
ATOM   2568  C  CD2   . LEU   A 1 616  ? 113.332 147.692 160.602 1.00 44.76  ? 616  LEU   A CD2   1 
ATOM   2569  N  N     . ALA   A 1 617  ? 117.217 150.656 160.960 1.00 45.97  ? 617  ALA   A N     1 
ATOM   2570  C  CA    . ALA   A 1 617  ? 118.070 151.273 159.952 1.00 40.37  ? 617  ALA   A CA    1 
ATOM   2571  C  C     . ALA   A 1 617  ? 119.256 150.379 159.620 1.00 44.24  ? 617  ALA   A C     1 
ATOM   2572  O  O     . ALA   A 1 617  ? 119.597 150.194 158.447 1.00 46.83  ? 617  ALA   A O     1 
ATOM   2573  C  CB    . ALA   A 1 617  ? 118.543 152.644 160.433 1.00 42.04  ? 617  ALA   A CB    1 
ATOM   2574  N  N     . SER   A 1 618  ? 119.901 149.815 160.644 1.00 36.76  ? 618  SER   A N     1 
ATOM   2575  C  CA    . SER   A 1 618  ? 121.036 148.933 160.391 1.00 36.41  ? 618  SER   A CA    1 
ATOM   2576  C  C     . SER   A 1 618  ? 120.604 147.681 159.636 1.00 44.30  ? 618  SER   A C     1 
ATOM   2577  O  O     . SER   A 1 618  ? 121.277 147.250 158.689 1.00 45.53  ? 618  SER   A O     1 
ATOM   2578  C  CB    . SER   A 1 618  ? 121.712 148.559 161.710 1.00 44.18  ? 618  SER   A CB    1 
ATOM   2579  O  OG    . SER   A 1 618  ? 121.992 149.711 162.486 1.00 52.97  ? 618  SER   A OG    1 
ATOM   2580  N  N     . LEU   A 1 619  ? 119.478 147.084 160.040 1.00 45.90  ? 619  LEU   A N     1 
ATOM   2581  C  CA    . LEU   A 1 619  ? 119.012 145.873 159.374 1.00 38.67  ? 619  LEU   A CA    1 
ATOM   2582  C  C     . LEU   A 1 619  ? 118.665 146.139 157.917 1.00 42.63  ? 619  LEU   A C     1 
ATOM   2583  O  O     . LEU   A 1 619  ? 118.859 145.266 157.065 1.00 56.72  ? 619  LEU   A O     1 
ATOM   2584  C  CB    . LEU   A 1 619  ? 117.804 145.300 160.115 1.00 42.49  ? 619  LEU   A CB    1 
ATOM   2585  C  CG    . LEU   A 1 619  ? 117.121 144.079 159.498 1.00 43.70  ? 619  LEU   A CG    1 
ATOM   2586  C  CD1   . LEU   A 1 619  ? 118.082 142.905 159.418 1.00 44.94  ? 619  LEU   A CD1   1 
ATOM   2587  C  CD2   . LEU   A 1 619  ? 115.884 143.706 160.294 1.00 38.51  ? 619  LEU   A CD2   1 
ATOM   2588  N  N     . VAL   A 1 620  ? 118.141 147.326 157.614 1.00 40.73  ? 620  VAL   A N     1 
ATOM   2589  C  CA    . VAL   A 1 620  ? 117.855 147.679 156.226 1.00 41.98  ? 620  VAL   A CA    1 
ATOM   2590  C  C     . VAL   A 1 620  ? 119.148 147.914 155.453 1.00 44.79  ? 620  VAL   A C     1 
ATOM   2591  O  O     . VAL   A 1 620  ? 119.312 147.437 154.325 1.00 46.59  ? 620  VAL   A O     1 
ATOM   2592  C  CB    . VAL   A 1 620  ? 116.932 148.909 156.163 1.00 38.82  ? 620  VAL   A CB    1 
ATOM   2593  C  CG1   . VAL   A 1 620  ? 116.893 149.467 154.751 1.00 35.61  ? 620  VAL   A CG1   1 
ATOM   2594  C  CG2   . VAL   A 1 620  ? 115.534 148.546 156.631 1.00 41.66  ? 620  VAL   A CG2   1 
ATOM   2595  N  N     . SER   A 1 621  ? 120.087 148.654 156.049 1.00 43.47  ? 621  SER   A N     1 
ATOM   2596  C  CA    . SER   A 1 621  ? 121.245 149.131 155.302 1.00 40.26  ? 621  SER   A CA    1 
ATOM   2597  C  C     . SER   A 1 621  ? 122.259 148.027 155.026 1.00 40.72  ? 621  SER   A C     1 
ATOM   2598  O  O     . SER   A 1 621  ? 122.845 147.987 153.938 1.00 49.60  ? 621  SER   A O     1 
ATOM   2599  C  CB    . SER   A 1 621  ? 121.913 150.284 156.054 1.00 38.56  ? 621  SER   A CB    1 
ATOM   2600  O  OG    . SER   A 1 621  ? 122.937 149.811 156.910 1.00 40.00  ? 621  SER   A OG    1 
ATOM   2601  N  N     . ALA   A 1 622  ? 122.490 147.128 155.984 1.00 41.61  ? 622  ALA   A N     1 
ATOM   2602  C  CA    . ALA   A 1 622  ? 123.531 146.119 155.790 1.00 37.80  ? 622  ALA   A CA    1 
ATOM   2603  C  C     . ALA   A 1 622  ? 123.290 145.253 154.561 1.00 43.45  ? 622  ALA   A C     1 
ATOM   2604  O  O     . ALA   A 1 622  ? 124.221 145.090 153.749 1.00 42.35  ? 622  ALA   A O     1 
ATOM   2605  C  CB    . ALA   A 1 622  ? 123.656 145.262 157.053 1.00 33.75  ? 622  ALA   A CB    1 
ATOM   2606  N  N     . PRO   A 1 623  ? 122.106 144.672 154.360 1.00 39.04  ? 623  PRO   A N     1 
ATOM   2607  C  CA    . PRO   A 1 623  ? 121.895 143.845 153.162 1.00 35.99  ? 623  PRO   A CA    1 
ATOM   2608  C  C     . PRO   A 1 623  ? 122.074 144.606 151.864 1.00 42.12  ? 623  PRO   A C     1 
ATOM   2609  O  O     . PRO   A 1 623  ? 122.521 144.017 150.875 1.00 49.66  ? 623  PRO   A O     1 
ATOM   2610  C  CB    . PRO   A 1 623  ? 120.455 143.340 153.329 1.00 38.48  ? 623  PRO   A CB    1 
ATOM   2611  C  CG    . PRO   A 1 623  ? 120.122 143.559 154.766 1.00 39.83  ? 623  PRO   A CG    1 
ATOM   2612  C  CD    . PRO   A 1 623  ? 120.900 144.752 155.196 1.00 39.02  ? 623  PRO   A CD    1 
ATOM   2613  N  N     . LYS   A 1 624  ? 121.734 145.896 151.826 1.00 41.49  ? 624  LYS   A N     1 
ATOM   2614  C  CA    . LYS   A 1 624  ? 121.928 146.672 150.606 1.00 36.45  ? 624  LYS   A CA    1 
ATOM   2615  C  C     . LYS   A 1 624  ? 123.405 146.752 150.241 1.00 37.44  ? 624  LYS   A C     1 
ATOM   2616  O  O     . LYS   A 1 624  ? 123.788 146.524 149.087 1.00 46.85  ? 624  LYS   A O     1 
ATOM   2617  C  CB    . LYS   A 1 624  ? 121.339 148.072 150.778 1.00 36.29  ? 624  LYS   A CB    1 
ATOM   2618  C  CG    . LYS   A 1 624  ? 119.886 148.078 151.213 1.00 37.44  ? 624  LYS   A CG    1 
ATOM   2619  C  CD    . LYS   A 1 624  ? 118.972 147.651 150.080 1.00 43.42  ? 624  LYS   A CD    1 
ATOM   2620  C  CE    . LYS   A 1 624  ? 117.582 148.240 150.237 1.00 42.48  ? 624  LYS   A CE    1 
ATOM   2621  N  NZ    . LYS   A 1 624  ? 117.609 149.724 150.261 1.00 42.65  ? 624  LYS   A NZ    1 
ATOM   2622  N  N     . ILE   A 1 625  ? 124.251 147.077 151.220 1.00 31.16  ? 625  ILE   A N     1 
ATOM   2623  C  CA    . ILE   A 1 625  ? 125.688 147.127 150.971 1.00 34.76  ? 625  ILE   A CA    1 
ATOM   2624  C  C     . ILE   A 1 625  ? 126.200 145.757 150.556 1.00 34.09  ? 625  ILE   A C     1 
ATOM   2625  O  O     . ILE   A 1 625  ? 127.025 145.638 149.640 1.00 40.71  ? 625  ILE   A O     1 
ATOM   2626  C  CB    . ILE   A 1 625  ? 126.435 147.652 152.210 1.00 32.35  ? 625  ILE   A CB    1 
ATOM   2627  C  CG1   . ILE   A 1 625  ? 125.919 149.033 152.606 1.00 38.03  ? 625  ILE   A CG1   1 
ATOM   2628  C  CG2   . ILE   A 1 625  ? 127.930 147.697 151.949 1.00 31.88  ? 625  ILE   A CG2   1 
ATOM   2629  C  CD1   . ILE   A 1 625  ? 126.387 149.477 153.968 1.00 37.98  ? 625  ILE   A CD1   1 
ATOM   2630  N  N     . PHE   A 1 626  ? 125.740 144.702 151.232 1.00 44.33  ? 626  PHE   A N     1 
ATOM   2631  C  CA    . PHE   A 1 626  ? 126.213 143.367 150.881 1.00 38.78  ? 626  PHE   A CA    1 
ATOM   2632  C  C     . PHE   A 1 626  ? 125.840 143.007 149.448 1.00 45.39  ? 626  PHE   A C     1 
ATOM   2633  O  O     . PHE   A 1 626  ? 126.665 142.469 148.703 1.00 53.23  ? 626  PHE   A O     1 
ATOM   2634  C  CB    . PHE   A 1 626  ? 125.659 142.327 151.851 1.00 46.33  ? 626  PHE   A CB    1 
ATOM   2635  C  CG    . PHE   A 1 626  ? 126.485 141.077 151.920 1.00 48.10  ? 626  PHE   A CG    1 
ATOM   2636  C  CD1   . PHE   A 1 626  ? 127.863 141.142 151.808 1.00 50.46  ? 626  PHE   A CD1   1 
ATOM   2637  C  CD2   . PHE   A 1 626  ? 125.890 139.839 152.075 1.00 46.63  ? 626  PHE   A CD2   1 
ATOM   2638  C  CE1   . PHE   A 1 626  ? 128.633 140.000 151.864 1.00 48.95  ? 626  PHE   A CE1   1 
ATOM   2639  C  CE2   . PHE   A 1 626  ? 126.657 138.692 152.130 1.00 52.20  ? 626  PHE   A CE2   1 
ATOM   2640  C  CZ    . PHE   A 1 626  ? 128.030 138.774 152.024 1.00 51.88  ? 626  PHE   A CZ    1 
ATOM   2641  N  N     . GLN   A 1 627  ? 124.602 143.295 149.043 1.00 39.76  ? 627  GLN   A N     1 
ATOM   2642  C  CA    . GLN   A 1 627  ? 124.174 142.976 147.685 1.00 34.14  ? 627  GLN   A CA    1 
ATOM   2643  C  C     . GLN   A 1 627  ? 124.935 143.802 146.657 1.00 40.06  ? 627  GLN   A C     1 
ATOM   2644  O  O     . GLN   A 1 627  ? 125.300 143.292 145.591 1.00 52.00  ? 627  GLN   A O     1 
ATOM   2645  C  CB    . GLN   A 1 627  ? 122.669 143.194 147.545 1.00 35.47  ? 627  GLN   A CB    1 
ATOM   2646  C  CG    . GLN   A 1 627  ? 122.233 143.606 146.152 1.00 38.73  ? 627  GLN   A CG    1 
ATOM   2647  C  CD    . GLN   A 1 627  ? 120.886 144.293 146.148 1.00 46.33  ? 627  GLN   A CD    1 
ATOM   2648  O  OE1   . GLN   A 1 627  ? 119.846 143.647 146.028 1.00 47.03  ? 627  GLN   A OE1   1 
ATOM   2649  N  NE2   . GLN   A 1 627  ? 120.896 145.613 146.287 1.00 51.60  ? 627  GLN   A NE2   1 
ATOM   2650  N  N     . ALA   A 1 628  ? 125.176 145.082 146.949 1.00 43.52  ? 628  ALA   A N     1 
ATOM   2651  C  CA    . ALA   A 1 628  ? 125.960 145.900 146.032 1.00 34.13  ? 628  ALA   A CA    1 
ATOM   2652  C  C     . ALA   A 1 628  ? 127.368 145.344 145.872 1.00 27.90  ? 628  ALA   A C     1 
ATOM   2653  O  O     . ALA   A 1 628  ? 127.883 145.246 144.752 1.00 33.25  ? 628  ALA   A O     1 
ATOM   2654  C  CB    . ALA   A 1 628  ? 126.007 147.345 146.522 1.00 37.56  ? 628  ALA   A CB    1 
ATOM   2655  N  N     . LEU   A 1 629  ? 128.006 144.968 146.982 1.00 44.18  ? 629  LEU   A N     1 
ATOM   2656  C  CA    . LEU   A 1 629  ? 129.349 144.406 146.908 1.00 34.78  ? 629  LEU   A CA    1 
ATOM   2657  C  C     . LEU   A 1 629  ? 129.354 143.054 146.209 1.00 40.36  ? 629  LEU   A C     1 
ATOM   2658  O  O     . LEU   A 1 629  ? 130.346 142.694 145.566 1.00 44.19  ? 629  LEU   A O     1 
ATOM   2659  C  CB    . LEU   A 1 629  ? 129.941 144.282 148.312 1.00 32.51  ? 629  LEU   A CB    1 
ATOM   2660  C  CG    . LEU   A 1 629  ? 131.243 143.492 148.446 1.00 43.31  ? 629  LEU   A CG    1 
ATOM   2661  C  CD1   . LEU   A 1 629  ? 132.438 144.429 148.412 1.00 46.29  ? 629  LEU   A CD1   1 
ATOM   2662  C  CD2   . LEU   A 1 629  ? 131.241 142.666 149.720 1.00 42.58  ? 629  LEU   A CD2   1 
ATOM   2663  N  N     . CYS   A 1 630  ? 128.265 142.294 146.326 1.00 49.51  ? 630  CYS   A N     1 
ATOM   2664  C  CA    . CYS   A 1 630  ? 128.192 140.981 145.699 1.00 49.51  ? 630  CYS   A CA    1 
ATOM   2665  C  C     . CYS   A 1 630  ? 127.952 141.078 144.199 1.00 49.58  ? 630  CYS   A C     1 
ATOM   2666  O  O     . CYS   A 1 630  ? 128.439 140.232 143.441 1.00 56.75  ? 630  CYS   A O     1 
ATOM   2667  C  CB    . CYS   A 1 630  ? 127.088 140.153 146.355 1.00 49.31  ? 630  CYS   A CB    1 
ATOM   2668  S  SG    . CYS   A 1 630  ? 127.636 139.162 147.760 1.00 64.54  ? 630  CYS   A SG    1 
ATOM   2669  N  N     . LYS   A 1 631  ? 127.211 142.094 143.754 1.00 41.94  ? 631  LYS   A N     1 
ATOM   2670  C  CA    . LYS   A 1 631  ? 126.949 142.256 142.330 1.00 42.86  ? 631  LYS   A CA    1 
ATOM   2671  C  C     . LYS   A 1 631  ? 128.209 142.559 141.530 1.00 45.37  ? 631  LYS   A C     1 
ATOM   2672  O  O     . LYS   A 1 631  ? 128.184 142.431 140.302 1.00 54.19  ? 631  LYS   A O     1 
ATOM   2673  C  CB    . LYS   A 1 631  ? 125.918 143.363 142.107 1.00 39.28  ? 631  LYS   A CB    1 
ATOM   2674  N  N     . ASP   A 1 632  ? 129.299 142.950 142.185 1.00 40.28  ? 632  ASP   A N     1 
ATOM   2675  C  CA    . ASP   A 1 632  ? 130.560 143.217 141.507 1.00 46.02  ? 632  ASP   A CA    1 
ATOM   2676  C  C     . ASP   A 1 632  ? 131.489 142.011 141.483 1.00 50.52  ? 632  ASP   A C     1 
ATOM   2677  O  O     . ASP   A 1 632  ? 132.564 142.087 140.879 1.00 52.77  ? 632  ASP   A O     1 
ATOM   2678  C  CB    . ASP   A 1 632  ? 131.276 144.400 142.167 1.00 47.34  ? 632  ASP   A CB    1 
ATOM   2679  C  CG    . ASP   A 1 632  ? 130.524 145.703 141.997 1.00 50.40  ? 632  ASP   A CG    1 
ATOM   2680  O  OD1   . ASP   A 1 632  ? 130.411 146.179 140.849 1.00 54.27  ? 632  ASP   A OD1   1 
ATOM   2681  O  OD2   . ASP   A 1 632  ? 130.050 146.255 143.012 1.00 53.92  ? 632  ASP   A OD2   1 
ATOM   2682  N  N     . ASN   A 1 633  ? 131.105 140.905 142.120 1.00 53.73  ? 633  ASN   A N     1 
ATOM   2683  C  CA    . ASN   A 1 633  ? 131.892 139.673 142.112 1.00 52.18  ? 633  ASN   A CA    1 
ATOM   2684  C  C     . ASN   A 1 633  ? 133.326 139.906 142.580 1.00 51.64  ? 633  ASN   A C     1 
ATOM   2685  O  O     . ASN   A 1 633  ? 134.259 139.260 142.098 1.00 54.60  ? 633  ASN   A O     1 
ATOM   2686  C  CB    . ASN   A 1 633  ? 131.885 139.023 140.726 1.00 51.67  ? 633  ASN   A CB    1 
ATOM   2687  N  N     . ILE   A 1 634  ? 133.518 140.828 143.525 1.00 52.85  ? 634  ILE   A N     1 
ATOM   2688  C  CA    . ILE   A 1 634  ? 134.851 141.032 144.083 1.00 48.33  ? 634  ILE   A CA    1 
ATOM   2689  C  C     . ILE   A 1 634  ? 135.286 139.805 144.873 1.00 49.70  ? 634  ILE   A C     1 
ATOM   2690  O  O     . ILE   A 1 634  ? 136.442 139.375 144.793 1.00 57.00  ? 634  ILE   A O     1 
ATOM   2691  C  CB    . ILE   A 1 634  ? 134.886 142.308 144.942 1.00 48.12  ? 634  ILE   A CB    1 
ATOM   2692  C  CG1   . ILE   A 1 634  ? 134.768 143.544 144.051 1.00 49.05  ? 634  ILE   A CG1   1 
ATOM   2693  C  CG2   . ILE   A 1 634  ? 136.164 142.362 145.757 1.00 50.44  ? 634  ILE   A CG2   1 
ATOM   2694  C  CD1   . ILE   A 1 634  ? 134.822 144.849 144.805 1.00 51.22  ? 634  ILE   A CD1   1 
ATOM   2695  N  N     . TYR   A 1 635  ? 134.371 139.225 145.646 1.00 53.56  ? 635  TYR   A N     1 
ATOM   2696  C  CA    . TYR   A 1 635  ? 134.596 137.937 146.295 1.00 54.22  ? 635  TYR   A CA    1 
ATOM   2697  C  C     . TYR   A 1 635  ? 133.729 136.900 145.595 1.00 57.62  ? 635  TYR   A C     1 
ATOM   2698  O  O     . TYR   A 1 635  ? 132.508 136.866 145.808 1.00 60.03  ? 635  TYR   A O     1 
ATOM   2699  C  CB    . TYR   A 1 635  ? 134.262 138.006 147.788 1.00 50.78  ? 635  TYR   A CB    1 
ATOM   2700  C  CG    . TYR   A 1 635  ? 134.920 139.160 148.511 1.00 51.26  ? 635  TYR   A CG    1 
ATOM   2701  C  CD1   . TYR   A 1 635  ? 136.245 139.085 148.915 1.00 53.83  ? 635  TYR   A CD1   1 
ATOM   2702  C  CD2   . TYR   A 1 635  ? 134.214 140.322 148.793 1.00 52.74  ? 635  TYR   A CD2   1 
ATOM   2703  C  CE1   . TYR   A 1 635  ? 136.851 140.136 149.577 1.00 54.96  ? 635  TYR   A CE1   1 
ATOM   2704  C  CE2   . TYR   A 1 635  ? 134.812 141.378 149.455 1.00 56.71  ? 635  TYR   A CE2   1 
ATOM   2705  C  CZ    . TYR   A 1 635  ? 136.129 141.279 149.845 1.00 55.86  ? 635  TYR   A CZ    1 
ATOM   2706  O  OH    . TYR   A 1 635  ? 136.725 142.329 150.503 1.00 49.63  ? 635  TYR   A OH    1 
ATOM   2707  N  N     . PRO   A 1 636  ? 134.302 136.038 144.754 1.00 56.71  ? 636  PRO   A N     1 
ATOM   2708  C  CA    . PRO   A 1 636  ? 133.461 135.142 143.941 1.00 51.56  ? 636  PRO   A CA    1 
ATOM   2709  C  C     . PRO   A 1 636  ? 132.605 134.193 144.761 1.00 57.87  ? 636  PRO   A C     1 
ATOM   2710  O  O     . PRO   A 1 636  ? 131.490 133.858 144.343 1.00 59.01  ? 636  PRO   A O     1 
ATOM   2711  C  CB    . PRO   A 1 636  ? 134.484 134.387 143.076 1.00 56.30  ? 636  PRO   A CB    1 
ATOM   2712  C  CG    . PRO   A 1 636  ? 135.812 135.068 143.311 1.00 57.96  ? 636  PRO   A CG    1 
ATOM   2713  C  CD    . PRO   A 1 636  ? 135.728 135.695 144.654 1.00 57.04  ? 636  PRO   A CD    1 
ATOM   2714  N  N     . ALA   A 1 637  ? 133.092 133.750 145.921 1.00 61.40  ? 637  ALA   A N     1 
ATOM   2715  C  CA    . ALA   A 1 637  ? 132.297 132.853 146.753 1.00 59.44  ? 637  ALA   A CA    1 
ATOM   2716  C  C     . ALA   A 1 637  ? 131.018 133.532 147.220 1.00 59.03  ? 637  ALA   A C     1 
ATOM   2717  O  O     . ALA   A 1 637  ? 130.000 132.869 147.452 1.00 61.36  ? 637  ALA   A O     1 
ATOM   2718  C  CB    . ALA   A 1 637  ? 133.119 132.374 147.948 1.00 57.70  ? 637  ALA   A CB    1 
ATOM   2719  N  N     . PHE   A 1 638  ? 131.050 134.856 147.361 1.00 63.20  ? 638  PHE   A N     1 
ATOM   2720  C  CA    . PHE   A 1 638  ? 129.886 135.601 147.820 1.00 62.10  ? 638  PHE   A CA    1 
ATOM   2721  C  C     . PHE   A 1 638  ? 128.831 135.785 146.743 1.00 61.29  ? 638  PHE   A C     1 
ATOM   2722  O  O     . PHE   A 1 638  ? 127.771 136.341 147.047 1.00 67.75  ? 638  PHE   A O     1 
ATOM   2723  C  CB    . PHE   A 1 638  ? 130.313 136.963 148.369 1.00 63.34  ? 638  PHE   A CB    1 
ATOM   2724  C  CG    . PHE   A 1 638  ? 130.902 136.900 149.747 1.00 61.84  ? 638  PHE   A CG    1 
ATOM   2725  C  CD1   . PHE   A 1 638  ? 131.178 135.680 150.340 1.00 62.77  ? 638  PHE   A CD1   1 
ATOM   2726  C  CD2   . PHE   A 1 638  ? 131.174 138.057 150.453 1.00 63.07  ? 638  PHE   A CD2   1 
ATOM   2727  C  CE1   . PHE   A 1 638  ? 131.717 135.616 151.609 1.00 63.77  ? 638  PHE   A CE1   1 
ATOM   2728  C  CE2   . PHE   A 1 638  ? 131.714 137.999 151.723 1.00 64.62  ? 638  PHE   A CE2   1 
ATOM   2729  C  CZ    . PHE   A 1 638  ? 131.986 136.777 152.301 1.00 64.81  ? 638  PHE   A CZ    1 
ATOM   2730  N  N     . GLN   A 1 639  ? 129.084 135.354 145.507 1.00 56.49  ? 639  GLN   A N     1 
ATOM   2731  C  CA    . GLN   A 1 639  ? 128.032 135.356 144.501 1.00 55.88  ? 639  GLN   A CA    1 
ATOM   2732  C  C     . GLN   A 1 639  ? 126.767 134.753 145.096 1.00 59.42  ? 639  GLN   A C     1 
ATOM   2733  O  O     . GLN   A 1 639  ? 126.826 133.871 145.956 1.00 61.60  ? 639  GLN   A O     1 
ATOM   2734  C  CB    . GLN   A 1 639  ? 128.469 134.571 143.263 1.00 57.72  ? 639  GLN   A CB    1 
ATOM   2735  N  N     . MET   A 1 640  ? 125.617 135.232 144.621 1.00 54.49  ? 640  MET   A N     1 
ATOM   2736  C  CA    . MET   A 1 640  ? 124.362 135.113 145.355 1.00 55.27  ? 640  MET   A CA    1 
ATOM   2737  C  C     . MET   A 1 640  ? 124.380 136.166 146.455 1.00 58.51  ? 640  MET   A C     1 
ATOM   2738  O  O     . MET   A 1 640  ? 125.359 136.908 146.581 1.00 66.26  ? 640  MET   A O     1 
ATOM   2739  C  CB    . MET   A 1 640  ? 124.161 133.704 145.922 1.00 52.71  ? 640  MET   A CB    1 
ATOM   2740  C  CG    . MET   A 1 640  ? 124.532 133.551 147.390 1.00 58.38  ? 640  MET   A CG    1 
ATOM   2741  S  SD    . MET   A 1 640  ? 124.532 131.833 147.936 1.00 69.93  ? 640  MET   A SD    1 
ATOM   2742  C  CE    . MET   A 1 640  ? 122.885 131.697 148.622 1.00 58.79  ? 640  MET   A CE    1 
ATOM   2743  N  N     . PHE   A 1 641  ? 123.318 136.255 147.252 1.00 52.68  ? 641  PHE   A N     1 
ATOM   2744  C  CA    . PHE   A 1 641  ? 123.160 137.372 148.185 1.00 54.17  ? 641  PHE   A CA    1 
ATOM   2745  C  C     . PHE   A 1 641  ? 123.086 138.697 147.434 1.00 55.99  ? 641  PHE   A C     1 
ATOM   2746  O  O     . PHE   A 1 641  ? 123.166 139.774 148.028 1.00 63.91  ? 641  PHE   A O     1 
ATOM   2747  C  CB    . PHE   A 1 641  ? 124.291 137.408 149.216 1.00 49.05  ? 641  PHE   A CB    1 
ATOM   2748  C  CG    . PHE   A 1 641  ? 124.257 136.277 150.202 1.00 48.40  ? 641  PHE   A CG    1 
ATOM   2749  C  CD1   . PHE   A 1 641  ? 123.095 135.971 150.886 1.00 52.55  ? 641  PHE   A CD1   1 
ATOM   2750  C  CD2   . PHE   A 1 641  ? 125.393 135.530 150.456 1.00 46.58  ? 641  PHE   A CD2   1 
ATOM   2751  C  CE1   . PHE   A 1 641  ? 123.064 134.934 151.798 1.00 51.91  ? 641  PHE   A CE1   1 
ATOM   2752  C  CE2   . PHE   A 1 641  ? 125.368 134.493 151.367 1.00 50.05  ? 641  PHE   A CE2   1 
ATOM   2753  C  CZ    . PHE   A 1 641  ? 124.202 134.195 152.038 1.00 52.75  ? 641  PHE   A CZ    1 
ATOM   2754  N  N     . ALA   A 1 642  ? 122.933 138.619 146.112 1.00 50.77  ? 642  ALA   A N     1 
ATOM   2755  C  CA    . ALA   A 1 642  ? 122.786 139.798 145.271 1.00 47.70  ? 642  ALA   A CA    1 
ATOM   2756  C  C     . ALA   A 1 642  ? 121.517 139.787 144.439 1.00 54.25  ? 642  ALA   A C     1 
ATOM   2757  O  O     . ALA   A 1 642  ? 121.223 140.798 143.795 1.00 57.86  ? 642  ALA   A O     1 
ATOM   2758  C  CB    . ALA   A 1 642  ? 123.994 139.946 144.336 1.00 45.66  ? 642  ALA   A CB    1 
ATOM   2759  N  N     . LYS   A 1 643  ? 120.761 138.693 144.423 1.00 63.89  ? 643  LYS   A N     1 
ATOM   2760  C  CA    . LYS   A 1 643  ? 119.514 138.636 143.676 1.00 62.82  ? 643  LYS   A CA    1 
ATOM   2761  C  C     . LYS   A 1 643  ? 118.445 139.455 144.385 1.00 66.03  ? 643  LYS   A C     1 
ATOM   2762  O  O     . LYS   A 1 643  ? 118.228 139.299 145.591 1.00 67.97  ? 643  LYS   A O     1 
ATOM   2763  C  CB    . LYS   A 1 643  ? 119.051 137.188 143.523 1.00 62.72  ? 643  LYS   A CB    1 
ATOM   2764  C  CG    . LYS   A 1 643  ? 117.700 137.043 142.846 1.00 68.73  ? 643  LYS   A CG    1 
ATOM   2765  C  CD    . LYS   A 1 643  ? 117.766 136.071 141.683 1.00 70.06  ? 643  LYS   A CD    1 
ATOM   2766  C  CE    . LYS   A 1 643  ? 118.250 134.705 142.137 1.00 70.99  ? 643  LYS   A CE    1 
ATOM   2767  N  NZ    . LYS   A 1 643  ? 118.246 133.723 141.020 1.00 67.24  ? 643  LYS   A NZ    1 
ATOM   2768  N  N     . GLY   A 1 644  ? 117.782 140.329 143.637 1.00 66.66  ? 644  GLY   A N     1 
ATOM   2769  C  CA    . GLY   A 1 644  ? 116.688 141.120 144.158 1.00 66.87  ? 644  GLY   A CA    1 
ATOM   2770  C  C     . GLY   A 1 644  ? 115.348 140.520 143.777 1.00 66.85  ? 644  GLY   A C     1 
ATOM   2771  O  O     . GLY   A 1 644  ? 115.205 139.898 142.727 1.00 72.83  ? 644  GLY   A O     1 
ATOM   2772  N  N     . TYR   A 1 645  ? 114.361 140.713 144.647 1.00 64.49  ? 645  TYR   A N     1 
ATOM   2773  C  CA    . TYR   A 1 645  ? 113.013 140.213 144.424 1.00 65.78  ? 645  TYR   A CA    1 
ATOM   2774  C  C     . TYR   A 1 645  ? 112.035 141.377 144.362 1.00 65.62  ? 645  TYR   A C     1 
ATOM   2775  O  O     . TYR   A 1 645  ? 112.276 142.446 144.929 1.00 66.10  ? 645  TYR   A O     1 
ATOM   2776  C  CB    . TYR   A 1 645  ? 112.567 139.231 145.524 1.00 66.86  ? 645  TYR   A CB    1 
ATOM   2777  C  CG    . TYR   A 1 645  ? 113.349 137.934 145.608 1.00 68.62  ? 645  TYR   A CG    1 
ATOM   2778  C  CD1   . TYR   A 1 645  ? 112.742 136.773 146.070 1.00 69.79  ? 645  TYR   A CD1   1 
ATOM   2779  C  CD2   . TYR   A 1 645  ? 114.685 137.867 145.240 1.00 67.64  ? 645  TYR   A CD2   1 
ATOM   2780  C  CE1   . TYR   A 1 645  ? 113.441 135.584 146.154 1.00 71.50  ? 645  TYR   A CE1   1 
ATOM   2781  C  CE2   . TYR   A 1 645  ? 115.393 136.683 145.322 1.00 71.15  ? 645  TYR   A CE2   1 
ATOM   2782  C  CZ    . TYR   A 1 645  ? 114.766 135.545 145.779 1.00 73.27  ? 645  TYR   A CZ    1 
ATOM   2783  O  OH    . TYR   A 1 645  ? 115.466 134.363 145.863 1.00 69.97  ? 645  TYR   A OH    1 
ATOM   2784  N  N     . GLY   A 1 646  ? 110.925 141.155 143.663 1.00 62.23  ? 646  GLY   A N     1 
ATOM   2785  C  CA    . GLY   A 1 646  ? 109.880 142.151 143.564 1.00 63.75  ? 646  GLY   A CA    1 
ATOM   2786  C  C     . GLY   A 1 646  ? 110.223 143.272 142.603 1.00 63.53  ? 646  GLY   A C     1 
ATOM   2787  O  O     . GLY   A 1 646  ? 111.263 143.288 141.942 1.00 59.32  ? 646  GLY   A O     1 
ATOM   2788  N  N     . LYS   A 1 647  ? 109.306 144.238 142.528 1.00 70.03  ? 647  LYS   A N     1 
ATOM   2789  C  CA    . LYS   A 1 647  ? 109.510 145.395 141.663 1.00 69.31  ? 647  LYS   A CA    1 
ATOM   2790  C  C     . LYS   A 1 647  ? 110.800 146.121 142.026 1.00 68.25  ? 647  LYS   A C     1 
ATOM   2791  O  O     . LYS   A 1 647  ? 111.725 146.219 141.213 1.00 68.83  ? 647  LYS   A O     1 
ATOM   2792  C  CB    . LYS   A 1 647  ? 108.308 146.335 141.759 1.00 66.37  ? 647  LYS   A CB    1 
ATOM   2793  N  N     . ASN   A 1 648  ? 110.876 146.638 143.249 1.00 66.64  ? 648  ASN   A N     1 
ATOM   2794  C  CA    . ASN   A 1 648  ? 112.109 147.227 143.754 1.00 64.29  ? 648  ASN   A CA    1 
ATOM   2795  C  C     . ASN   A 1 648  ? 113.017 146.113 144.257 1.00 63.13  ? 648  ASN   A C     1 
ATOM   2796  O  O     . ASN   A 1 648  ? 112.695 145.442 145.244 1.00 68.45  ? 648  ASN   A O     1 
ATOM   2797  C  CB    . ASN   A 1 648  ? 111.811 148.228 144.867 1.00 60.46  ? 648  ASN   A CB    1 
ATOM   2798  N  N     . ASN   A 1 649  ? 114.148 145.914 143.582 1.00 56.30  ? 649  ASN   A N     1 
ATOM   2799  C  CA    . ASN   A 1 649  ? 115.046 144.818 143.919 1.00 58.68  ? 649  ASN   A CA    1 
ATOM   2800  C  C     . ASN   A 1 649  ? 115.484 144.908 145.375 1.00 63.62  ? 649  ASN   A C     1 
ATOM   2801  O  O     . ASN   A 1 649  ? 116.215 145.827 145.756 1.00 69.22  ? 649  ASN   A O     1 
ATOM   2802  C  CB    . ASN   A 1 649  ? 116.265 144.821 142.995 1.00 56.05  ? 649  ASN   A CB    1 
ATOM   2803  N  N     . GLU   A 1 650  ? 115.041 143.957 146.193 1.00 62.44  ? 650  GLU   A N     1 
ATOM   2804  C  CA    . GLU   A 1 650  ? 115.373 143.914 147.603 1.00 57.20  ? 650  GLU   A CA    1 
ATOM   2805  C  C     . GLU   A 1 650  ? 116.148 142.639 147.905 1.00 54.88  ? 650  GLU   A C     1 
ATOM   2806  O  O     . GLU   A 1 650  ? 115.702 141.546 147.528 1.00 59.44  ? 650  GLU   A O     1 
ATOM   2807  C  CB    . GLU   A 1 650  ? 114.103 143.972 148.466 1.00 55.40  ? 650  GLU   A CB    1 
ATOM   2808  C  CG    . GLU   A 1 650  ? 113.267 145.226 148.267 1.00 60.11  ? 650  GLU   A CG    1 
ATOM   2809  C  CD    . GLU   A 1 650  ? 113.856 146.440 148.958 1.00 64.76  ? 650  GLU   A CD    1 
ATOM   2810  O  OE1   . GLU   A 1 650  ? 114.469 146.273 150.032 1.00 61.10  ? 650  GLU   A OE1   1 
ATOM   2811  O  OE2   . GLU   A 1 650  ? 113.705 147.561 148.428 1.00 65.59  ? 650  GLU   A OE2   1 
ATOM   2812  N  N     . PRO   A 1 651  ? 117.292 142.726 148.578 1.00 44.27  ? 651  PRO   A N     1 
ATOM   2813  C  CA    . PRO   A 1 651  ? 118.107 141.525 148.846 1.00 48.04  ? 651  PRO   A CA    1 
ATOM   2814  C  C     . PRO   A 1 651  ? 117.567 140.695 150.009 1.00 51.02  ? 651  PRO   A C     1 
ATOM   2815  O  O     . PRO   A 1 651  ? 117.995 140.789 151.159 1.00 57.58  ? 651  PRO   A O     1 
ATOM   2816  C  CB    . PRO   A 1 651  ? 119.486 142.116 149.144 1.00 50.03  ? 651  PRO   A CB    1 
ATOM   2817  C  CG    . PRO   A 1 651  ? 119.223 143.528 149.623 1.00 51.19  ? 651  PRO   A CG    1 
ATOM   2818  C  CD    . PRO   A 1 651  ? 117.798 143.903 149.301 1.00 46.77  ? 651  PRO   A CD    1 
ATOM   2819  N  N     . LEU   A 1 652  ? 116.587 139.846 149.694 1.00 45.58  ? 652  LEU   A N     1 
ATOM   2820  C  CA    . LEU   A 1 652  ? 115.978 139.010 150.722 1.00 47.59  ? 652  LEU   A CA    1 
ATOM   2821  C  C     . LEU   A 1 652  ? 116.996 138.056 151.334 1.00 55.50  ? 652  LEU   A C     1 
ATOM   2822  O  O     . LEU   A 1 652  ? 116.989 137.827 152.549 1.00 62.56  ? 652  LEU   A O     1 
ATOM   2823  C  CB    . LEU   A 1 652  ? 114.796 138.237 150.138 1.00 48.01  ? 652  LEU   A CB    1 
ATOM   2824  C  CG    . LEU   A 1 652  ? 113.443 138.949 150.213 1.00 52.15  ? 652  LEU   A CG    1 
ATOM   2825  C  CD1   . LEU   A 1 652  ? 113.489 140.280 149.482 1.00 51.55  ? 652  LEU   A CD1   1 
ATOM   2826  C  CD2   . LEU   A 1 652  ? 112.337 138.070 149.657 1.00 57.10  ? 652  LEU   A CD2   1 
ATOM   2827  N  N     . ARG   A 1 653  ? 117.876 137.484 150.511 1.00 49.33  ? 653  ARG   A N     1 
ATOM   2828  C  CA    . ARG   A 1 653  ? 118.909 136.604 151.046 1.00 52.20  ? 653  ARG   A CA    1 
ATOM   2829  C  C     . ARG   A 1 653  ? 119.827 137.357 152.001 1.00 53.57  ? 653  ARG   A C     1 
ATOM   2830  O  O     . ARG   A 1 653  ? 120.181 136.846 153.070 1.00 59.05  ? 653  ARG   A O     1 
ATOM   2831  C  CB    . ARG   A 1 653  ? 119.709 135.981 149.904 1.00 49.38  ? 653  ARG   A CB    1 
ATOM   2832  C  CG    . ARG   A 1 653  ? 118.852 135.481 148.756 1.00 52.23  ? 653  ARG   A CG    1 
ATOM   2833  C  CD    . ARG   A 1 653  ? 119.529 134.336 148.023 1.00 54.30  ? 653  ARG   A CD    1 
ATOM   2834  N  NE    . ARG   A 1 653  ? 118.670 133.766 146.992 1.00 57.13  ? 653  ARG   A NE    1 
ATOM   2835  C  CZ    . ARG   A 1 653  ? 119.111 133.215 145.870 1.00 59.86  ? 653  ARG   A CZ    1 
ATOM   2836  N  NH1   . ARG   A 1 653  ? 120.403 133.137 145.599 1.00 59.48  ? 653  ARG   A NH1   1 
ATOM   2837  N  NH2   . ARG   A 1 653  ? 118.233 132.728 144.998 1.00 59.64  ? 653  ARG   A NH2   1 
ATOM   2838  N  N     . GLY   A 1 654  ? 120.217 138.578 151.635 1.00 51.11  ? 654  GLY   A N     1 
ATOM   2839  C  CA    . GLY   A 1 654  ? 121.000 139.392 152.547 1.00 49.88  ? 654  GLY   A CA    1 
ATOM   2840  C  C     . GLY   A 1 654  ? 120.232 139.747 153.805 1.00 51.99  ? 654  GLY   A C     1 
ATOM   2841  O  O     . GLY   A 1 654  ? 120.803 139.812 154.896 1.00 56.68  ? 654  GLY   A O     1 
ATOM   2842  N  N     . TYR   A 1 655  ? 118.924 139.975 153.670 1.00 50.12  ? 655  TYR   A N     1 
ATOM   2843  C  CA    . TYR   A 1 655  ? 118.094 140.239 154.840 1.00 44.77  ? 655  TYR   A CA    1 
ATOM   2844  C  C     . TYR   A 1 655  ? 118.130 139.060 155.803 1.00 52.09  ? 655  TYR   A C     1 
ATOM   2845  O  O     . TYR   A 1 655  ? 118.297 139.234 157.015 1.00 59.70  ? 655  TYR   A O     1 
ATOM   2846  C  CB    . TYR   A 1 655  ? 116.658 140.529 154.401 1.00 46.95  ? 655  TYR   A CB    1 
ATOM   2847  C  CG    . TYR   A 1 655  ? 116.376 141.985 154.108 1.00 51.00  ? 655  TYR   A CG    1 
ATOM   2848  C  CD1   . TYR   A 1 655  ? 116.878 142.989 154.924 1.00 54.01  ? 655  TYR   A CD1   1 
ATOM   2849  C  CD2   . TYR   A 1 655  ? 115.615 142.354 153.009 1.00 47.19  ? 655  TYR   A CD2   1 
ATOM   2850  C  CE1   . TYR   A 1 655  ? 116.623 144.319 154.656 1.00 50.28  ? 655  TYR   A CE1   1 
ATOM   2851  C  CE2   . TYR   A 1 655  ? 115.356 143.680 152.732 1.00 53.42  ? 655  TYR   A CE2   1 
ATOM   2852  C  CZ    . TYR   A 1 655  ? 115.862 144.658 153.558 1.00 55.01  ? 655  TYR   A CZ    1 
ATOM   2853  O  OH    . TYR   A 1 655  ? 115.605 145.982 153.285 1.00 56.46  ? 655  TYR   A OH    1 
ATOM   2854  N  N     . ILE   A 1 656  ? 117.991 137.844 155.271 1.00 49.42  ? 656  ILE   A N     1 
ATOM   2855  C  CA    . ILE   A 1 656  ? 118.007 136.653 156.115 1.00 46.24  ? 656  ILE   A CA    1 
ATOM   2856  C  C     . ILE   A 1 656  ? 119.381 136.457 156.742 1.00 47.76  ? 656  ILE   A C     1 
ATOM   2857  O  O     . ILE   A 1 656  ? 119.497 136.062 157.908 1.00 57.44  ? 656  ILE   A O     1 
ATOM   2858  C  CB    . ILE   A 1 656  ? 117.571 135.419 155.306 1.00 44.61  ? 656  ILE   A CB    1 
ATOM   2859  C  CG1   . ILE   A 1 656  ? 116.046 135.299 155.293 1.00 45.66  ? 656  ILE   A CG1   1 
ATOM   2860  C  CG2   . ILE   A 1 656  ? 118.206 134.161 155.869 1.00 49.89  ? 656  ILE   A CG2   1 
ATOM   2861  C  CD1   . ILE   A 1 656  ? 115.357 136.337 154.438 1.00 49.02  ? 656  ILE   A CD1   1 
ATOM   2862  N  N     . LEU   A 1 657  ? 120.445 136.707 155.977 1.00 40.74  ? 657  LEU   A N     1 
ATOM   2863  C  CA    . LEU   A 1 657  ? 121.790 136.561 156.525 1.00 41.40  ? 657  LEU   A CA    1 
ATOM   2864  C  C     . LEU   A 1 657  ? 122.032 137.545 157.665 1.00 50.11  ? 657  LEU   A C     1 
ATOM   2865  O  O     . LEU   A 1 657  ? 122.598 137.181 158.706 1.00 55.63  ? 657  LEU   A O     1 
ATOM   2866  C  CB    . LEU   A 1 657  ? 122.827 136.748 155.417 1.00 42.70  ? 657  LEU   A CB    1 
ATOM   2867  C  CG    . LEU   A 1 657  ? 124.291 136.809 155.849 1.00 42.83  ? 657  LEU   A CG    1 
ATOM   2868  C  CD1   . LEU   A 1 657  ? 124.804 135.416 156.175 1.00 47.39  ? 657  LEU   A CD1   1 
ATOM   2869  C  CD2   . LEU   A 1 657  ? 125.141 137.458 154.770 1.00 42.34  ? 657  LEU   A CD2   1 
ATOM   2870  N  N     . THR   A 1 658  ? 121.609 138.799 157.487 1.00 53.73  ? 658  THR   A N     1 
ATOM   2871  C  CA    . THR   A 1 658  ? 121.740 139.784 158.555 1.00 56.66  ? 658  THR   A CA    1 
ATOM   2872  C  C     . THR   A 1 658  ? 120.905 139.389 159.765 1.00 53.51  ? 658  THR   A C     1 
ATOM   2873  O  O     . THR   A 1 658  ? 121.344 139.546 160.911 1.00 55.10  ? 658  THR   A O     1 
ATOM   2874  C  CB    . THR   A 1 658  ? 121.333 141.168 158.050 1.00 52.26  ? 658  THR   A CB    1 
ATOM   2875  O  OG1   . THR   A 1 658  ? 121.761 141.325 156.692 1.00 50.74  ? 658  THR   A OG1   1 
ATOM   2876  C  CG2   . THR   A 1 658  ? 121.969 142.256 158.899 1.00 51.02  ? 658  THR   A CG2   1 
ATOM   2877  N  N     . PHE   A 1 659  ? 119.694 138.879 159.530 1.00 51.74  ? 659  PHE   A N     1 
ATOM   2878  C  CA    . PHE   A 1 659  ? 118.872 138.392 160.631 1.00 51.26  ? 659  PHE   A CA    1 
ATOM   2879  C  C     . PHE   A 1 659  ? 119.584 137.292 161.403 1.00 55.19  ? 659  PHE   A C     1 
ATOM   2880  O  O     . PHE   A 1 659  ? 119.583 137.292 162.637 1.00 59.85  ? 659  PHE   A O     1 
ATOM   2881  C  CB    . PHE   A 1 659  ? 117.529 137.890 160.099 1.00 53.33  ? 659  PHE   A CB    1 
ATOM   2882  C  CG    . PHE   A 1 659  ? 116.780 137.013 161.064 1.00 56.04  ? 659  PHE   A CG    1 
ATOM   2883  C  CD1   . PHE   A 1 659  ? 115.916 137.561 161.995 1.00 59.65  ? 659  PHE   A CD1   1 
ATOM   2884  C  CD2   . PHE   A 1 659  ? 116.933 135.637 161.031 1.00 56.06  ? 659  PHE   A CD2   1 
ATOM   2885  C  CE1   . PHE   A 1 659  ? 115.225 136.755 162.879 1.00 57.84  ? 659  PHE   A CE1   1 
ATOM   2886  C  CE2   . PHE   A 1 659  ? 116.245 134.827 161.913 1.00 59.23  ? 659  PHE   A CE2   1 
ATOM   2887  C  CZ    . PHE   A 1 659  ? 115.390 135.386 162.837 1.00 57.66  ? 659  PHE   A CZ    1 
ATOM   2888  N  N     . LEU   A 1 660  ? 120.191 136.340 160.693 1.00 53.45  ? 660  LEU   A N     1 
ATOM   2889  C  CA    . LEU   A 1 660  ? 120.883 135.245 161.366 1.00 50.49  ? 660  LEU   A CA    1 
ATOM   2890  C  C     . LEU   A 1 660  ? 122.067 135.754 162.179 1.00 52.45  ? 660  LEU   A C     1 
ATOM   2891  O  O     . LEU   A 1 660  ? 122.273 135.330 163.324 1.00 59.27  ? 660  LEU   A O     1 
ATOM   2892  C  CB    . LEU   A 1 660  ? 121.341 134.207 160.343 1.00 47.15  ? 660  LEU   A CB    1 
ATOM   2893  C  CG    . LEU   A 1 660  ? 120.267 133.236 159.853 1.00 55.23  ? 660  LEU   A CG    1 
ATOM   2894  C  CD1   . LEU   A 1 660  ? 120.899 132.042 159.159 1.00 54.71  ? 660  LEU   A CD1   1 
ATOM   2895  C  CD2   . LEU   A 1 660  ? 119.390 132.785 161.007 1.00 55.44  ? 660  LEU   A CD2   1 
ATOM   2896  N  N     . ILE   A 1 661  ? 122.859 136.660 161.604 1.00 49.30  ? 661  ILE   A N     1 
ATOM   2897  C  CA    . ILE   A 1 661  ? 124.017 137.188 162.324 1.00 48.57  ? 661  ILE   A CA    1 
ATOM   2898  C  C     . ILE   A 1 661  ? 123.569 137.924 163.582 1.00 53.95  ? 661  ILE   A C     1 
ATOM   2899  O  O     . ILE   A 1 661  ? 124.132 137.739 164.672 1.00 56.66  ? 661  ILE   A O     1 
ATOM   2900  C  CB    . ILE   A 1 661  ? 124.856 138.096 161.406 1.00 52.56  ? 661  ILE   A CB    1 
ATOM   2901  C  CG1   . ILE   A 1 661  ? 125.839 137.268 160.573 1.00 52.67  ? 661  ILE   A CG1   1 
ATOM   2902  C  CG2   . ILE   A 1 661  ? 125.594 139.144 162.220 1.00 51.99  ? 661  ILE   A CG2   1 
ATOM   2903  C  CD1   . ILE   A 1 661  ? 125.255 135.999 160.002 1.00 54.60  ? 661  ILE   A CD1   1 
ATOM   2904  N  N     . ALA   A 1 662  ? 122.547 138.773 163.448 1.00 57.49  ? 662  ALA   A N     1 
ATOM   2905  C  CA    . ALA   A 1 662  ? 122.046 139.515 164.598 1.00 50.39  ? 662  ALA   A CA    1 
ATOM   2906  C  C     . ALA   A 1 662  ? 121.480 138.576 165.654 1.00 54.79  ? 662  ALA   A C     1 
ATOM   2907  O  O     . ALA   A 1 662  ? 121.684 138.786 166.853 1.00 62.10  ? 662  ALA   A O     1 
ATOM   2908  C  CB    . ALA   A 1 662  ? 120.990 140.524 164.151 1.00 49.94  ? 662  ALA   A CB    1 
ATOM   2909  N  N     . LEU   A 1 663  ? 120.764 137.534 165.227 1.00 54.91  ? 663  LEU   A N     1 
ATOM   2910  C  CA    . LEU   A 1 663  ? 120.204 136.581 166.178 1.00 55.54  ? 663  LEU   A CA    1 
ATOM   2911  C  C     . LEU   A 1 663  ? 121.303 135.852 166.936 1.00 53.91  ? 663  LEU   A C     1 
ATOM   2912  O  O     . LEU   A 1 663  ? 121.189 135.636 168.146 1.00 57.23  ? 663  LEU   A O     1 
ATOM   2913  C  CB    . LEU   A 1 663  ? 119.300 135.586 165.451 1.00 57.04  ? 663  LEU   A CB    1 
ATOM   2914  C  CG    . LEU   A 1 663  ? 118.785 134.409 166.279 1.00 54.33  ? 663  LEU   A CG    1 
ATOM   2915  C  CD1   . LEU   A 1 663  ? 117.312 134.165 166.006 1.00 56.62  ? 663  LEU   A CD1   1 
ATOM   2916  C  CD2   . LEU   A 1 663  ? 119.596 133.159 165.986 1.00 55.42  ? 663  LEU   A CD2   1 
ATOM   2917  N  N     . GLY   A 1 664  ? 122.374 135.461 166.246 1.00 46.80  ? 664  GLY   A N     1 
ATOM   2918  C  CA    . GLY   A 1 664  ? 123.482 134.821 166.939 1.00 47.82  ? 664  GLY   A CA    1 
ATOM   2919  C  C     . GLY   A 1 664  ? 124.142 135.742 167.947 1.00 51.95  ? 664  GLY   A C     1 
ATOM   2920  O  O     . GLY   A 1 664  ? 124.386 135.361 169.099 1.00 57.85  ? 664  GLY   A O     1 
ATOM   2921  N  N     . PHE   A 1 665  ? 124.425 136.980 167.534 1.00 52.90  ? 665  PHE   A N     1 
ATOM   2922  C  CA    . PHE   A 1 665  ? 125.068 137.912 168.454 1.00 50.05  ? 665  PHE   A CA    1 
ATOM   2923  C  C     . PHE   A 1 665  ? 124.161 138.258 169.628 1.00 52.98  ? 665  PHE   A C     1 
ATOM   2924  O  O     . PHE   A 1 665  ? 124.654 138.555 170.723 1.00 54.66  ? 665  PHE   A O     1 
ATOM   2925  C  CB    . PHE   A 1 665  ? 125.502 139.174 167.711 1.00 48.89  ? 665  PHE   A CB    1 
ATOM   2926  C  CG    . PHE   A 1 665  ? 126.936 139.146 167.267 1.00 51.34  ? 665  PHE   A CG    1 
ATOM   2927  C  CD1   . PHE   A 1 665  ? 127.953 139.467 168.151 1.00 52.95  ? 665  PHE   A CD1   1 
ATOM   2928  C  CD2   . PHE   A 1 665  ? 127.270 138.787 165.974 1.00 51.41  ? 665  PHE   A CD2   1 
ATOM   2929  C  CE1   . PHE   A 1 665  ? 129.274 139.439 167.749 1.00 50.60  ? 665  PHE   A CE1   1 
ATOM   2930  C  CE2   . PHE   A 1 665  ? 128.591 138.757 165.567 1.00 53.58  ? 665  PHE   A CE2   1 
ATOM   2931  C  CZ    . PHE   A 1 665  ? 129.593 139.083 166.456 1.00 52.18  ? 665  PHE   A CZ    1 
ATOM   2932  N  N     . ILE   A 1 666  ? 122.843 138.234 169.425 1.00 50.98  ? 666  ILE   A N     1 
ATOM   2933  C  CA    . ILE   A 1 666  ? 121.916 138.421 170.535 1.00 49.49  ? 666  ILE   A CA    1 
ATOM   2934  C  C     . ILE   A 1 666  ? 121.936 137.206 171.452 1.00 52.63  ? 666  ILE   A C     1 
ATOM   2935  O  O     . ILE   A 1 666  ? 121.918 137.336 172.682 1.00 56.17  ? 666  ILE   A O     1 
ATOM   2936  C  CB    . ILE   A 1 666  ? 120.502 138.709 170.002 1.00 47.90  ? 666  ILE   A CB    1 
ATOM   2937  C  CG1   . ILE   A 1 666  ? 120.343 140.198 169.694 1.00 48.99  ? 666  ILE   A CG1   1 
ATOM   2938  C  CG2   . ILE   A 1 666  ? 119.454 138.251 171.000 1.00 46.17  ? 666  ILE   A CG2   1 
ATOM   2939  C  CD1   . ILE   A 1 666  ? 119.483 140.483 168.485 1.00 48.24  ? 666  ILE   A CD1   1 
ATOM   2940  N  N     . LEU   A 1 667  ? 121.975 136.005 170.869 1.00 54.27  ? 667  LEU   A N     1 
ATOM   2941  C  CA    . LEU   A 1 667  ? 122.082 134.793 171.670 1.00 48.51  ? 667  LEU   A CA    1 
ATOM   2942  C  C     . LEU   A 1 667  ? 123.313 134.834 172.560 1.00 53.92  ? 667  LEU   A C     1 
ATOM   2943  O  O     . LEU   A 1 667  ? 123.284 134.321 173.684 1.00 57.85  ? 667  LEU   A O     1 
ATOM   2944  C  CB    . LEU   A 1 667  ? 122.116 133.565 170.761 1.00 48.92  ? 667  LEU   A CB    1 
ATOM   2945  C  CG    . LEU   A 1 667  ? 120.779 133.146 170.145 1.00 53.79  ? 667  LEU   A CG    1 
ATOM   2946  C  CD1   . LEU   A 1 667  ? 120.789 131.673 169.770 1.00 53.81  ? 667  LEU   A CD1   1 
ATOM   2947  C  CD2   . LEU   A 1 667  ? 119.636 133.452 171.097 1.00 48.58  ? 667  LEU   A CD2   1 
ATOM   2948  N  N     . ILE   A 1 668  ? 124.402 135.438 172.082 1.00 55.90  ? 668  ILE   A N     1 
ATOM   2949  C  CA    . ILE   A 1 668  ? 125.538 135.687 172.968 1.00 51.36  ? 668  ILE   A CA    1 
ATOM   2950  C  C     . ILE   A 1 668  ? 125.108 136.582 174.125 1.00 52.94  ? 668  ILE   A C     1 
ATOM   2951  O  O     . ILE   A 1 668  ? 125.409 136.310 175.293 1.00 61.31  ? 668  ILE   A O     1 
ATOM   2952  C  CB    . ILE   A 1 668  ? 126.715 136.294 172.187 1.00 53.06  ? 668  ILE   A CB    1 
ATOM   2953  C  CG1   . ILE   A 1 668  ? 127.600 135.184 171.618 1.00 56.37  ? 668  ILE   A CG1   1 
ATOM   2954  C  CG2   . ILE   A 1 668  ? 127.528 137.214 173.084 1.00 50.61  ? 668  ILE   A CG2   1 
ATOM   2955  C  CD1   . ILE   A 1 668  ? 128.790 135.690 170.835 1.00 58.21  ? 668  ILE   A CD1   1 
ATOM   2956  N  N     . ALA   A 1 669  ? 124.400 137.669 173.813 1.00 53.98  ? 669  ALA   A N     1 
ATOM   2957  C  CA    . ALA   A 1 669  ? 123.698 138.473 174.808 1.00 50.30  ? 669  ALA   A CA    1 
ATOM   2958  C  C     . ALA   A 1 669  ? 124.633 139.318 175.665 1.00 54.92  ? 669  ALA   A C     1 
ATOM   2959  O  O     . ALA   A 1 669  ? 124.170 140.117 176.486 1.00 60.17  ? 669  ALA   A O     1 
ATOM   2960  C  CB    . ALA   A 1 669  ? 122.845 137.574 175.705 1.00 53.11  ? 669  ALA   A CB    1 
ATOM   2961  N  N     . GLU   A 1 670  ? 125.941 139.157 175.489 1.00 59.50  ? 670  GLU   A N     1 
ATOM   2962  C  CA    . GLU   A 1 670  ? 126.943 139.928 176.224 1.00 59.57  ? 670  GLU   A CA    1 
ATOM   2963  C  C     . GLU   A 1 670  ? 127.795 140.665 175.194 1.00 65.68  ? 670  GLU   A C     1 
ATOM   2964  O  O     . GLU   A 1 670  ? 128.832 140.162 174.757 1.00 68.91  ? 670  GLU   A O     1 
ATOM   2965  C  CB    . GLU   A 1 670  ? 127.788 139.026 177.118 1.00 59.84  ? 670  GLU   A CB    1 
ATOM   2966  N  N     . LEU   A 1 671  ? 127.354 141.864 174.816 1.00 65.14  ? 671  LEU   A N     1 
ATOM   2967  C  CA    . LEU   A 1 671  ? 127.949 142.603 173.712 1.00 66.32  ? 671  LEU   A CA    1 
ATOM   2968  C  C     . LEU   A 1 671  ? 128.778 143.802 174.153 1.00 67.83  ? 671  LEU   A C     1 
ATOM   2969  O  O     . LEU   A 1 671  ? 129.316 144.509 173.295 1.00 73.03  ? 671  LEU   A O     1 
ATOM   2970  C  CB    . LEU   A 1 671  ? 126.851 143.066 172.748 1.00 63.57  ? 671  LEU   A CB    1 
ATOM   2971  C  CG    . LEU   A 1 671  ? 126.039 141.953 172.085 1.00 61.78  ? 671  LEU   A CG    1 
ATOM   2972  C  CD1   . LEU   A 1 671  ? 125.331 142.468 170.844 1.00 63.72  ? 671  LEU   A CD1   1 
ATOM   2973  C  CD2   . LEU   A 1 671  ? 126.928 140.769 171.745 1.00 59.15  ? 671  LEU   A CD2   1 
ATOM   2974  N  N     . ASN   A 1 672  ? 128.900 144.053 175.458 1.00 66.58  ? 672  ASN   A N     1 
ATOM   2975  C  CA    . ASN   A 1 672  ? 129.619 145.241 175.909 1.00 68.66  ? 672  ASN   A CA    1 
ATOM   2976  C  C     . ASN   A 1 672  ? 131.070 145.236 175.448 1.00 69.20  ? 672  ASN   A C     1 
ATOM   2977  O  O     . ASN   A 1 672  ? 131.671 146.304 175.281 1.00 72.44  ? 672  ASN   A O     1 
ATOM   2978  C  CB    . ASN   A 1 672  ? 129.546 145.357 177.430 1.00 68.30  ? 672  ASN   A CB    1 
ATOM   2979  C  CG    . ASN   A 1 672  ? 128.700 146.529 177.881 1.00 72.60  ? 672  ASN   A CG    1 
ATOM   2980  O  OD1   . ASN   A 1 672  ? 127.684 146.848 177.264 1.00 68.81  ? 672  ASN   A OD1   1 
ATOM   2981  N  ND2   . ASN   A 1 672  ? 129.118 147.182 178.959 1.00 73.62  ? 672  ASN   A ND2   1 
ATOM   2982  N  N     . VAL   A 1 673  ? 131.651 144.055 175.237 1.00 59.95  ? 673  VAL   A N     1 
ATOM   2983  C  CA    . VAL   A 1 673  ? 133.046 143.974 174.818 1.00 61.24  ? 673  VAL   A CA    1 
ATOM   2984  C  C     . VAL   A 1 673  ? 133.223 144.113 173.310 1.00 63.15  ? 673  VAL   A C     1 
ATOM   2985  O  O     . VAL   A 1 673  ? 134.346 144.368 172.850 1.00 63.90  ? 673  VAL   A O     1 
ATOM   2986  C  CB    . VAL   A 1 673  ? 133.679 142.654 175.293 1.00 62.36  ? 673  VAL   A CB    1 
ATOM   2987  C  CG1   . VAL   A 1 673  ? 133.040 141.471 174.581 1.00 59.78  ? 673  VAL   A CG1   1 
ATOM   2988  C  CG2   . VAL   A 1 673  ? 135.184 142.674 175.070 1.00 59.73  ? 673  VAL   A CG2   1 
ATOM   2989  N  N     . ILE   A 1 674  ? 132.155 143.956 172.528 1.00 55.41  ? 674  ILE   A N     1 
ATOM   2990  C  CA    . ILE   A 1 674  ? 132.258 144.024 171.075 1.00 51.99  ? 674  ILE   A CA    1 
ATOM   2991  C  C     . ILE   A 1 674  ? 131.952 145.414 170.521 1.00 52.27  ? 674  ILE   A C     1 
ATOM   2992  O  O     . ILE   A 1 674  ? 132.368 145.721 169.394 1.00 55.48  ? 674  ILE   A O     1 
ATOM   2993  C  CB    . ILE   A 1 674  ? 131.334 142.980 170.414 1.00 53.23  ? 674  ILE   A CB    1 
ATOM   2994  C  CG1   . ILE   A 1 674  ? 131.665 141.577 170.926 1.00 53.86  ? 674  ILE   A CG1   1 
ATOM   2995  C  CG2   . ILE   A 1 674  ? 131.470 143.028 168.903 1.00 53.24  ? 674  ILE   A CG2   1 
ATOM   2996  C  CD1   . ILE   A 1 674  ? 132.828 140.924 170.217 1.00 53.55  ? 674  ILE   A CD1   1 
ATOM   2997  N  N     . ALA   A 1 675  ? 131.249 146.257 171.272 1.00 51.17  ? 675  ALA   A N     1 
ATOM   2998  C  CA    . ALA   A 1 675  ? 130.901 147.587 170.779 1.00 57.68  ? 675  ALA   A CA    1 
ATOM   2999  C  C     . ALA   A 1 675  ? 132.104 148.385 170.294 1.00 56.00  ? 675  ALA   A C     1 
ATOM   3000  O  O     . ALA   A 1 675  ? 132.007 149.007 169.221 1.00 54.18  ? 675  ALA   A O     1 
ATOM   3001  C  CB    . ALA   A 1 675  ? 130.156 148.360 171.876 1.00 47.76  ? 675  ALA   A CB    1 
ATOM   3002  N  N     . PRO   A 1 676  ? 133.230 148.425 171.007 1.00 49.12  ? 676  PRO   A N     1 
ATOM   3003  C  CA    . PRO   A 1 676  ? 134.384 149.184 170.504 1.00 51.66  ? 676  PRO   A CA    1 
ATOM   3004  C  C     . PRO   A 1 676  ? 134.878 148.716 169.148 1.00 53.79  ? 676  PRO   A C     1 
ATOM   3005  O  O     . PRO   A 1 676  ? 135.321 149.545 168.347 1.00 54.23  ? 676  PRO   A O     1 
ATOM   3006  C  CB    . PRO   A 1 676  ? 135.428 148.964 171.606 1.00 47.58  ? 676  PRO   A CB    1 
ATOM   3007  C  CG    . PRO   A 1 676  ? 135.029 147.635 172.194 1.00 50.45  ? 676  PRO   A CG    1 
ATOM   3008  C  CD    . PRO   A 1 676  ? 133.545 147.767 172.284 1.00 44.98  ? 676  PRO   A CD    1 
ATOM   3009  N  N     . ILE   A 1 677  ? 134.815 147.415 168.858 1.00 48.75  ? 677  ILE   A N     1 
ATOM   3010  C  CA    . ILE   A 1 677  ? 135.231 146.933 167.543 1.00 43.34  ? 677  ILE   A CA    1 
ATOM   3011  C  C     . ILE   A 1 677  ? 134.322 147.494 166.456 1.00 44.92  ? 677  ILE   A C     1 
ATOM   3012  O  O     . ILE   A 1 677  ? 134.786 147.899 165.383 1.00 51.18  ? 677  ILE   A O     1 
ATOM   3013  C  CB    . ILE   A 1 677  ? 135.259 145.394 167.523 1.00 47.21  ? 677  ILE   A CB    1 
ATOM   3014  C  CG1   . ILE   A 1 677  ? 136.105 144.864 168.682 1.00 48.43  ? 677  ILE   A CG1   1 
ATOM   3015  C  CG2   . ILE   A 1 677  ? 135.803 144.891 166.198 1.00 49.01  ? 677  ILE   A CG2   1 
ATOM   3016  C  CD1   . ILE   A 1 677  ? 135.948 143.379 168.924 1.00 52.63  ? 677  ILE   A CD1   1 
ATOM   3017  N  N     . ILE   A 1 678  ? 133.012 147.516 166.708 1.00 40.09  ? 678  ILE   A N     1 
ATOM   3018  C  CA    . ILE   A 1 678  ? 132.075 148.077 165.738 1.00 44.14  ? 678  ILE   A CA    1 
ATOM   3019  C  C     . ILE   A 1 678  ? 132.337 149.565 165.542 1.00 44.21  ? 678  ILE   A C     1 
ATOM   3020  O  O     . ILE   A 1 678  ? 132.317 150.076 164.413 1.00 53.51  ? 678  ILE   A O     1 
ATOM   3021  C  CB    . ILE   A 1 678  ? 130.626 147.808 166.183 1.00 43.02  ? 678  ILE   A CB    1 
ATOM   3022  C  CG1   . ILE   A 1 678  ? 130.404 146.311 166.407 1.00 44.94  ? 678  ILE   A CG1   1 
ATOM   3023  C  CG2   . ILE   A 1 678  ? 129.644 148.349 165.160 1.00 46.30  ? 678  ILE   A CG2   1 
ATOM   3024  C  CD1   . ILE   A 1 678  ? 131.186 145.424 165.464 1.00 45.54  ? 678  ILE   A CD1   1 
ATOM   3025  N  N     . SER   A 1 679  ? 132.574 150.287 166.640 1.00 35.24  ? 679  SER   A N     1 
ATOM   3026  C  CA    . SER   A 1 679  ? 132.900 151.704 166.526 1.00 37.16  ? 679  SER   A CA    1 
ATOM   3027  C  C     . SER   A 1 679  ? 134.164 151.907 165.702 1.00 43.41  ? 679  SER   A C     1 
ATOM   3028  O  O     . SER   A 1 679  ? 134.246 152.836 164.890 1.00 48.13  ? 679  SER   A O     1 
ATOM   3029  C  CB    . SER   A 1 679  ? 133.060 152.322 167.915 1.00 41.71  ? 679  SER   A CB    1 
ATOM   3030  O  OG    . SER   A 1 679  ? 131.955 152.011 168.744 1.00 46.56  ? 679  SER   A OG    1 
ATOM   3031  N  N     . ASN   A 1 680  ? 135.163 151.047 165.902 1.00 43.99  ? 680  ASN   A N     1 
ATOM   3032  C  CA    . ASN   A 1 680  ? 136.398 151.141 165.134 1.00 39.82  ? 680  ASN   A CA    1 
ATOM   3033  C  C     . ASN   A 1 680  ? 136.146 150.876 163.655 1.00 41.65  ? 680  ASN   A C     1 
ATOM   3034  O  O     . ASN   A 1 680  ? 136.745 151.523 162.791 1.00 49.39  ? 680  ASN   A O     1 
ATOM   3035  C  CB    . ASN   A 1 680  ? 137.429 150.163 165.693 1.00 47.17  ? 680  ASN   A CB    1 
ATOM   3036  C  CG    . ASN   A 1 680  ? 138.401 150.824 166.649 1.00 50.09  ? 680  ASN   A CG    1 
ATOM   3037  O  OD1   . ASN   A 1 680  ? 139.570 151.019 166.327 1.00 50.35  ? 680  ASN   A OD1   1 
ATOM   3038  N  ND2   . ASN   A 1 680  ? 137.917 151.177 167.833 1.00 44.82  ? 680  ASN   A ND2   1 
ATOM   3039  N  N     . PHE   A 1 681  ? 135.266 149.923 163.345 1.00 34.07  ? 681  PHE   A N     1 
ATOM   3040  C  CA    . PHE   A 1 681  ? 134.914 149.663 161.950 1.00 40.86  ? 681  PHE   A CA    1 
ATOM   3041  C  C     . PHE   A 1 681  ? 134.279 150.894 161.311 1.00 43.58  ? 681  PHE   A C     1 
ATOM   3042  O  O     . PHE   A 1 681  ? 134.633 151.289 160.190 1.00 42.45  ? 681  PHE   A O     1 
ATOM   3043  C  CB    . PHE   A 1 681  ? 133.965 148.468 161.868 1.00 38.11  ? 681  PHE   A CB    1 
ATOM   3044  C  CG    . PHE   A 1 681  ? 134.639 147.139 162.058 1.00 43.09  ? 681  PHE   A CG    1 
ATOM   3045  C  CD1   . PHE   A 1 681  ? 135.989 147.065 162.355 1.00 42.66  ? 681  PHE   A CD1   1 
ATOM   3046  C  CD2   . PHE   A 1 681  ? 133.919 145.963 161.947 1.00 42.68  ? 681  PHE   A CD2   1 
ATOM   3047  C  CE1   . PHE   A 1 681  ? 136.608 145.843 162.533 1.00 39.64  ? 681  PHE   A CE1   1 
ATOM   3048  C  CE2   . PHE   A 1 681  ? 134.533 144.740 162.123 1.00 42.78  ? 681  PHE   A CE2   1 
ATOM   3049  C  CZ    . PHE   A 1 681  ? 135.879 144.680 162.416 1.00 42.37  ? 681  PHE   A CZ    1 
ATOM   3050  N  N     . PHE   A 1 682  ? 133.329 151.513 162.015 1.00 38.41  ? 682  PHE   A N     1 
ATOM   3051  C  CA    . PHE   A 1 682  ? 132.690 152.716 161.488 1.00 37.23  ? 682  PHE   A CA    1 
ATOM   3052  C  C     . PHE   A 1 682  ? 133.703 153.840 161.296 1.00 39.89  ? 682  PHE   A C     1 
ATOM   3053  O  O     . PHE   A 1 682  ? 133.673 154.556 160.285 1.00 47.19  ? 682  PHE   A O     1 
ATOM   3054  C  CB    . PHE   A 1 682  ? 131.560 153.159 162.418 1.00 39.54  ? 682  PHE   A CB    1 
ATOM   3055  C  CG    . PHE   A 1 682  ? 130.296 152.361 162.262 1.00 39.03  ? 682  PHE   A CG    1 
ATOM   3056  C  CD1   . PHE   A 1 682  ? 130.173 151.108 162.834 1.00 38.49  ? 682  PHE   A CD1   1 
ATOM   3057  C  CD2   . PHE   A 1 682  ? 129.223 152.871 161.554 1.00 47.24  ? 682  PHE   A CD2   1 
ATOM   3058  C  CE1   . PHE   A 1 682  ? 129.010 150.376 162.693 1.00 39.55  ? 682  PHE   A CE1   1 
ATOM   3059  C  CE2   . PHE   A 1 682  ? 128.057 152.142 161.413 1.00 46.04  ? 682  PHE   A CE2   1 
ATOM   3060  C  CZ    . PHE   A 1 682  ? 127.952 150.894 161.983 1.00 37.18  ? 682  PHE   A CZ    1 
ATOM   3061  N  N     . LEU   A 1 683  ? 134.608 154.013 162.261 1.00 34.44  ? 683  LEU   A N     1 
ATOM   3062  C  CA    . LEU   A 1 683  ? 135.632 155.043 162.137 1.00 35.91  ? 683  LEU   A CA    1 
ATOM   3063  C  C     . LEU   A 1 683  ? 136.545 154.765 160.951 1.00 35.41  ? 683  LEU   A C     1 
ATOM   3064  O  O     . LEU   A 1 683  ? 136.962 155.691 160.247 1.00 39.03  ? 683  LEU   A O     1 
ATOM   3065  C  CB    . LEU   A 1 683  ? 136.442 155.133 163.430 1.00 43.68  ? 683  LEU   A CB    1 
ATOM   3066  C  CG    . LEU   A 1 683  ? 136.070 156.274 164.376 1.00 35.81  ? 683  LEU   A CG    1 
ATOM   3067  C  CD1   . LEU   A 1 683  ? 136.150 157.615 163.667 1.00 32.70  ? 683  LEU   A CD1   1 
ATOM   3068  C  CD2   . LEU   A 1 683  ? 134.682 156.046 164.947 1.00 43.83  ? 683  LEU   A CD2   1 
ATOM   3069  N  N     . ALA   A 1 684  ? 136.879 153.493 160.724 1.00 34.96  ? 684  ALA   A N     1 
ATOM   3070  C  CA    . ALA   A 1 684  ? 137.692 153.134 159.570 1.00 34.41  ? 684  ALA   A CA    1 
ATOM   3071  C  C     . ALA   A 1 684  ? 136.980 153.483 158.272 1.00 41.26  ? 684  ALA   A C     1 
ATOM   3072  O  O     . ALA   A 1 684  ? 137.605 153.969 157.324 1.00 44.18  ? 684  ALA   A O     1 
ATOM   3073  C  CB    . ALA   A 1 684  ? 138.036 151.646 159.611 1.00 36.97  ? 684  ALA   A CB    1 
ATOM   3074  N  N     . SER   A 1 685  ? 135.673 153.225 158.203 1.00 39.09  ? 685  SER   A N     1 
ATOM   3075  C  CA    . SER   A 1 685  ? 134.918 153.605 157.012 1.00 34.21  ? 685  SER   A CA    1 
ATOM   3076  C  C     . SER   A 1 685  ? 134.945 155.117 156.802 1.00 40.30  ? 685  SER   A C     1 
ATOM   3077  O  O     . SER   A 1 685  ? 135.119 155.598 155.672 1.00 42.99  ? 685  SER   A O     1 
ATOM   3078  C  CB    . SER   A 1 685  ? 133.481 153.100 157.120 1.00 37.50  ? 685  SER   A CB    1 
ATOM   3079  O  OG    . SER   A 1 685  ? 133.453 151.745 157.531 1.00 38.69  ? 685  SER   A OG    1 
ATOM   3080  N  N     . TYR   A 1 686  ? 134.772 155.881 157.881 1.00 33.18  ? 686  TYR   A N     1 
ATOM   3081  C  CA    . TYR   A 1 686  ? 134.828 157.338 157.776 1.00 30.42  ? 686  TYR   A CA    1 
ATOM   3082  C  C     . TYR   A 1 686  ? 136.187 157.789 157.251 1.00 32.19  ? 686  TYR   A C     1 
ATOM   3083  O  O     . TYR   A 1 686  ? 136.282 158.654 156.367 1.00 37.57  ? 686  TYR   A O     1 
ATOM   3084  C  CB    . TYR   A 1 686  ? 134.552 157.966 159.143 1.00 32.68  ? 686  TYR   A CB    1 
ATOM   3085  C  CG    . TYR   A 1 686  ? 133.116 157.884 159.614 1.00 34.17  ? 686  TYR   A CG    1 
ATOM   3086  C  CD1   . TYR   A 1 686  ? 132.271 156.876 159.171 1.00 32.09  ? 686  TYR   A CD1   1 
ATOM   3087  C  CD2   . TYR   A 1 686  ? 132.618 158.796 160.534 1.00 39.88  ? 686  TYR   A CD2   1 
ATOM   3088  C  CE1   . TYR   A 1 686  ? 130.964 156.794 159.611 1.00 40.65  ? 686  TYR   A CE1   1 
ATOM   3089  C  CE2   . TYR   A 1 686  ? 131.313 158.721 160.982 1.00 41.83  ? 686  TYR   A CE2   1 
ATOM   3090  C  CZ    . TYR   A 1 686  ? 130.491 157.718 160.517 1.00 43.33  ? 686  TYR   A CZ    1 
ATOM   3091  O  OH    . TYR   A 1 686  ? 129.192 157.642 160.961 1.00 39.14  ? 686  TYR   A OH    1 
ATOM   3092  N  N     . ALA   A 1 687  ? 137.256 157.203 157.794 1.00 37.68  ? 687  ALA   A N     1 
ATOM   3093  C  CA    . ALA   A 1 687  ? 138.602 157.555 157.363 1.00 34.32  ? 687  ALA   A CA    1 
ATOM   3094  C  C     . ALA   A 1 687  ? 138.825 157.182 155.905 1.00 37.87  ? 687  ALA   A C     1 
ATOM   3095  O  O     . ALA   A 1 687  ? 139.507 157.903 155.172 1.00 45.11  ? 687  ALA   A O     1 
ATOM   3096  C  CB    . ALA   A 1 687  ? 139.635 156.873 158.259 1.00 33.72  ? 687  ALA   A CB    1 
ATOM   3097  N  N     . LEU   A 1 688  ? 138.265 156.054 155.468 1.00 40.35  ? 688  LEU   A N     1 
ATOM   3098  C  CA    . LEU   A 1 688  ? 138.392 155.673 154.066 1.00 35.47  ? 688  LEU   A CA    1 
ATOM   3099  C  C     . LEU   A 1 688  ? 137.676 156.663 153.158 1.00 29.41  ? 688  LEU   A C     1 
ATOM   3100  O  O     . LEU   A 1 688  ? 138.163 156.966 152.067 1.00 42.35  ? 688  LEU   A O     1 
ATOM   3101  C  CB    . LEU   A 1 688  ? 137.861 154.259 153.842 1.00 35.64  ? 688  LEU   A CB    1 
ATOM   3102  C  CG    . LEU   A 1 688  ? 138.930 153.165 153.857 1.00 36.33  ? 688  LEU   A CG    1 
ATOM   3103  C  CD1   . LEU   A 1 688  ? 138.481 151.961 153.053 1.00 37.59  ? 688  LEU   A CD1   1 
ATOM   3104  C  CD2   . LEU   A 1 688  ? 140.247 153.700 153.327 1.00 37.86  ? 688  LEU   A CD2   1 
ATOM   3105  N  N     . ILE   A 1 689  ? 136.519 157.174 153.580 1.00 27.70  ? 689  ILE   A N     1 
ATOM   3106  C  CA    . ILE   A 1 689  ? 135.826 158.179 152.772 1.00 25.83  ? 689  ILE   A CA    1 
ATOM   3107  C  C     . ILE   A 1 689  ? 136.663 159.453 152.672 1.00 27.25  ? 689  ILE   A C     1 
ATOM   3108  O  O     . ILE   A 1 689  ? 136.837 160.034 151.587 1.00 31.45  ? 689  ILE   A O     1 
ATOM   3109  C  CB    . ILE   A 1 689  ? 134.429 158.464 153.352 1.00 29.97  ? 689  ILE   A CB    1 
ATOM   3110  C  CG1   . ILE   A 1 689  ? 133.477 157.312 153.031 1.00 27.70  ? 689  ILE   A CG1   1 
ATOM   3111  C  CG2   . ILE   A 1 689  ? 133.880 159.772 152.809 1.00 27.71  ? 689  ILE   A CG2   1 
ATOM   3112  C  CD1   . ILE   A 1 689  ? 132.184 157.349 153.810 1.00 26.70  ? 689  ILE   A CD1   1 
ATOM   3113  N  N     . ASN   A 1 690  ? 137.191 159.910 153.810 1.00 30.15  ? 690  ASN   A N     1 
ATOM   3114  C  CA    . ASN   A 1 690  ? 138.020 161.112 153.796 1.00 32.40  ? 690  ASN   A CA    1 
ATOM   3115  C  C     . ASN   A 1 690  ? 139.259 160.914 152.929 1.00 31.21  ? 690  ASN   A C     1 
ATOM   3116  O  O     . ASN   A 1 690  ? 139.649 161.810 152.167 1.00 34.33  ? 690  ASN   A O     1 
ATOM   3117  C  CB    . ASN   A 1 690  ? 138.408 161.500 155.222 1.00 35.05  ? 690  ASN   A CB    1 
ATOM   3118  C  CG    . ASN   A 1 690  ? 137.256 162.120 155.992 1.00 33.55  ? 690  ASN   A CG    1 
ATOM   3119  O  OD1   . ASN   A 1 690  ? 136.967 163.307 155.848 1.00 38.62  ? 690  ASN   A OD1   1 
ATOM   3120  N  ND2   . ASN   A 1 690  ? 136.591 161.316 156.812 1.00 37.30  ? 690  ASN   A ND2   1 
ATOM   3121  N  N     . PHE   A 1 691  ? 139.888 159.741 153.026 1.00 27.22  ? 691  PHE   A N     1 
ATOM   3122  C  CA    . PHE   A 1 691  ? 141.045 159.443 152.194 1.00 31.46  ? 691  PHE   A CA    1 
ATOM   3123  C  C     . PHE   A 1 691  ? 140.663 159.324 150.727 1.00 33.89  ? 691  PHE   A C     1 
ATOM   3124  O  O     . PHE   A 1 691  ? 141.474 159.639 149.856 1.00 44.29  ? 691  PHE   A O     1 
ATOM   3125  C  CB    . PHE   A 1 691  ? 141.725 158.160 152.669 1.00 28.83  ? 691  PHE   A CB    1 
ATOM   3126  C  CG    . PHE   A 1 691  ? 142.981 157.831 151.916 1.00 37.63  ? 691  PHE   A CG    1 
ATOM   3127  C  CD1   . PHE   A 1 691  ? 144.046 158.713 151.905 1.00 32.42  ? 691  PHE   A CD1   1 
ATOM   3128  C  CD2   . PHE   A 1 691  ? 143.093 156.644 151.213 1.00 42.77  ? 691  PHE   A CD2   1 
ATOM   3129  C  CE1   . PHE   A 1 691  ? 145.202 158.416 151.211 1.00 39.70  ? 691  PHE   A CE1   1 
ATOM   3130  C  CE2   . PHE   A 1 691  ? 144.247 156.342 150.517 1.00 38.12  ? 691  PHE   A CE2   1 
ATOM   3131  C  CZ    . PHE   A 1 691  ? 145.302 157.229 150.517 1.00 42.23  ? 691  PHE   A CZ    1 
ATOM   3132  N  N     . SER   A 1 692  ? 139.447 158.866 150.431 1.00 20.03  ? 692  SER   A N     1 
ATOM   3133  C  CA    . SER   A 1 692  ? 138.971 158.873 149.054 1.00 19.19  ? 692  SER   A CA    1 
ATOM   3134  C  C     . SER   A 1 692  ? 138.965 160.288 148.503 1.00 22.17  ? 692  SER   A C     1 
ATOM   3135  O  O     . SER   A 1 692  ? 139.470 160.548 147.404 1.00 28.92  ? 692  SER   A O     1 
ATOM   3136  C  CB    . SER   A 1 692  ? 137.567 158.271 148.980 1.00 25.42  ? 692  SER   A CB    1 
ATOM   3137  O  OG    . SER   A 1 692  ? 137.605 156.873 148.764 1.00 37.39  ? 692  SER   A OG    1 
ATOM   3138  N  N     . VAL   A 1 693  ? 138.399 161.223 149.265 1.00 26.14  ? 693  VAL   A N     1 
ATOM   3139  C  CA    . VAL   A 1 693  ? 138.345 162.606 148.795 1.00 18.40  ? 693  VAL   A CA    1 
ATOM   3140  C  C     . VAL   A 1 693  ? 139.755 163.165 148.632 1.00 24.51  ? 693  VAL   A C     1 
ATOM   3141  O  O     . VAL   A 1 693  ? 140.072 163.821 147.628 1.00 33.41  ? 693  VAL   A O     1 
ATOM   3142  C  CB    . VAL   A 1 693  ? 137.496 163.465 149.749 1.00 27.11  ? 693  VAL   A CB    1 
ATOM   3143  C  CG1   . VAL   A 1 693  ? 137.387 164.889 149.228 1.00 21.11  ? 693  VAL   A CG1   1 
ATOM   3144  C  CG2   . VAL   A 1 693  ? 136.119 162.851 149.919 1.00 30.78  ? 693  VAL   A CG2   1 
ATOM   3145  N  N     . PHE   A 1 694  ? 140.628 162.901 149.608 1.00 28.66  ? 694  PHE   A N     1 
ATOM   3146  C  CA    . PHE   A 1 694  ? 141.994 163.411 149.534 1.00 21.67  ? 694  PHE   A CA    1 
ATOM   3147  C  C     . PHE   A 1 694  ? 142.739 162.837 148.333 1.00 32.19  ? 694  PHE   A C     1 
ATOM   3148  O  O     . PHE   A 1 694  ? 143.441 163.565 147.623 1.00 32.11  ? 694  PHE   A O     1 
ATOM   3149  C  CB    . PHE   A 1 694  ? 142.742 163.095 150.828 1.00 28.29  ? 694  PHE   A CB    1 
ATOM   3150  C  CG    . PHE   A 1 694  ? 144.226 163.306 150.737 1.00 35.40  ? 694  PHE   A CG    1 
ATOM   3151  C  CD1   . PHE   A 1 694  ? 144.758 164.582 150.787 1.00 35.95  ? 694  PHE   A CD1   1 
ATOM   3152  C  CD2   . PHE   A 1 694  ? 145.089 162.233 150.596 1.00 31.84  ? 694  PHE   A CD2   1 
ATOM   3153  C  CE1   . PHE   A 1 694  ? 146.120 164.784 150.703 1.00 37.62  ? 694  PHE   A CE1   1 
ATOM   3154  C  CE2   . PHE   A 1 694  ? 146.452 162.430 150.510 1.00 28.10  ? 694  PHE   A CE2   1 
ATOM   3155  C  CZ    . PHE   A 1 694  ? 146.968 163.707 150.564 1.00 31.98  ? 694  PHE   A CZ    1 
ATOM   3156  N  N     . HIS   A 1 695  ? 142.610 161.529 148.099 1.00 32.32  ? 695  HIS   A N     1 
ATOM   3157  C  CA    . HIS   A 1 695  ? 143.264 160.891 146.962 1.00 23.73  ? 695  HIS   A CA    1 
ATOM   3158  C  C     . HIS   A 1 695  ? 142.746 161.449 145.645 1.00 31.31  ? 695  HIS   A C     1 
ATOM   3159  O  O     . HIS   A 1 695  ? 143.525 161.697 144.718 1.00 35.02  ? 695  HIS   A O     1 
ATOM   3160  C  CB    . HIS   A 1 695  ? 143.051 159.379 147.024 1.00 23.58  ? 695  HIS   A CB    1 
ATOM   3161  C  CG    . HIS   A 1 695  ? 144.188 158.582 146.467 1.00 33.78  ? 695  HIS   A CG    1 
ATOM   3162  N  ND1   . HIS   A 1 695  ? 144.031 157.682 145.435 1.00 35.04  ? 695  HIS   A ND1   1 
ATOM   3163  C  CD2   . HIS   A 1 695  ? 145.499 158.545 146.801 1.00 38.37  ? 695  HIS   A CD2   1 
ATOM   3164  C  CE1   . HIS   A 1 695  ? 145.197 157.127 145.156 1.00 37.70  ? 695  HIS   A CE1   1 
ATOM   3165  N  NE2   . HIS   A 1 695  ? 146.104 157.634 145.971 1.00 43.19  ? 695  HIS   A NE2   1 
ATOM   3166  N  N     . ALA   A 1 696  ? 141.431 161.644 145.539 1.00 32.14  ? 696  ALA   A N     1 
ATOM   3167  C  CA    . ALA   A 1 696  ? 140.876 162.220 144.322 1.00 19.69  ? 696  ALA   A CA    1 
ATOM   3168  C  C     . ALA   A 1 696  ? 141.440 163.610 144.072 1.00 31.16  ? 696  ALA   A C     1 
ATOM   3169  O  O     . ALA   A 1 696  ? 141.778 163.956 142.934 1.00 29.73  ? 696  ALA   A O     1 
ATOM   3170  C  CB    . ALA   A 1 696  ? 139.351 162.263 144.407 1.00 26.31  ? 696  ALA   A CB    1 
ATOM   3171  N  N     . SER   A 1 697  ? 141.551 164.424 145.124 1.00 33.37  ? 697  SER   A N     1 
ATOM   3172  C  CA    . SER   A 1 697  ? 142.146 165.745 144.947 1.00 31.28  ? 697  SER   A CA    1 
ATOM   3173  C  C     . SER   A 1 697  ? 143.636 165.658 144.630 1.00 35.56  ? 697  SER   A C     1 
ATOM   3174  O  O     . SER   A 1 697  ? 144.181 166.554 143.976 1.00 40.77  ? 697  SER   A O     1 
ATOM   3175  C  CB    . SER   A 1 697  ? 141.915 166.600 146.191 1.00 32.38  ? 697  SER   A CB    1 
ATOM   3176  O  OG    . SER   A 1 697  ? 140.701 167.322 146.092 1.00 41.22  ? 697  SER   A OG    1 
ATOM   3177  N  N     . LEU   A 1 698  ? 144.309 164.597 145.082 1.00 33.08  ? 698  LEU   A N     1 
ATOM   3178  C  CA    . LEU   A 1 698  ? 145.737 164.452 144.815 1.00 29.83  ? 698  LEU   A CA    1 
ATOM   3179  C  C     . LEU   A 1 698  ? 145.991 164.074 143.361 1.00 33.25  ? 698  LEU   A C     1 
ATOM   3180  O  O     . LEU   A 1 698  ? 146.866 164.647 142.703 1.00 39.76  ? 698  LEU   A O     1 
ATOM   3181  C  CB    . LEU   A 1 698  ? 146.343 163.412 145.758 1.00 38.85  ? 698  LEU   A CB    1 
ATOM   3182  C  CG    . LEU   A 1 698  ? 147.869 163.297 145.771 1.00 27.88  ? 698  LEU   A CG    1 
ATOM   3183  C  CD1   . LEU   A 1 698  ? 148.510 164.633 146.105 1.00 32.66  ? 698  LEU   A CD1   1 
ATOM   3184  C  CD2   . LEU   A 1 698  ? 148.314 162.225 146.750 1.00 24.66  ? 698  LEU   A CD2   1 
ATOM   3185  N  N     . ALA   A 1 699  ? 145.238 163.106 142.843 1.00 33.17  ? 699  ALA   A N     1 
ATOM   3186  C  CA    . ALA   A 1 699  ? 145.312 162.742 141.432 1.00 24.76  ? 699  ALA   A CA    1 
ATOM   3187  C  C     . ALA   A 1 699  ? 144.407 163.682 140.649 1.00 36.87  ? 699  ALA   A C     1 
ATOM   3188  O  O     . ALA   A 1 699  ? 143.179 163.554 140.692 1.00 53.19  ? 699  ALA   A O     1 
ATOM   3189  C  CB    . ALA   A 1 699  ? 144.910 161.285 141.228 1.00 22.63  ? 699  ALA   A CB    1 
ATOM   3190  N  N     . LYS   A 1 700  ? 145.008 164.626 139.926 1.00 27.53  ? 700  LYS   A N     1 
ATOM   3191  C  CA    . LYS   A 1 700  ? 144.256 165.700 139.279 1.00 31.20  ? 700  LYS   A CA    1 
ATOM   3192  C  C     . LYS   A 1 700  ? 143.590 165.205 137.993 1.00 33.92  ? 700  LYS   A C     1 
ATOM   3193  O  O     . LYS   A 1 700  ? 143.795 165.730 136.899 1.00 32.99  ? 700  LYS   A O     1 
ATOM   3194  C  CB    . LYS   A 1 700  ? 145.171 166.888 139.012 1.00 33.01  ? 700  LYS   A CB    1 
ATOM   3195  C  CG    . LYS   A 1 700  ? 145.790 167.477 140.268 1.00 33.88  ? 700  LYS   A CG    1 
ATOM   3196  C  CD    . LYS   A 1 700  ? 146.458 168.811 139.985 1.00 34.88  ? 700  LYS   A CD    1 
ATOM   3197  C  CE    . LYS   A 1 700  ? 147.588 169.078 140.963 1.00 41.23  ? 700  LYS   A CE    1 
ATOM   3198  N  NZ    . LYS   A 1 700  ? 148.486 167.899 141.103 1.00 37.99  ? 700  LYS   A NZ    1 
ATOM   3199  N  N     . SER   A 1 701  ? 142.774 164.173 138.149 1.00 32.79  ? 701  SER   A N     1 
ATOM   3200  C  CA    . SER   A 1 701  ? 142.008 163.649 137.026 1.00 30.20  ? 701  SER   A CA    1 
ATOM   3201  C  C     . SER   A 1 701  ? 141.000 164.692 136.553 1.00 30.47  ? 701  SER   A C     1 
ATOM   3202  O  O     . SER   A 1 701  ? 140.276 165.263 137.376 1.00 27.92  ? 701  SER   A O     1 
ATOM   3203  C  CB    . SER   A 1 701  ? 141.288 162.365 137.426 1.00 27.71  ? 701  SER   A CB    1 
ATOM   3204  O  OG    . SER   A 1 701  ? 140.548 161.835 136.342 1.00 28.30  ? 701  SER   A OG    1 
ATOM   3205  N  N     . PRO   A 1 702  ? 140.920 164.967 135.249 1.00 31.23  ? 702  PRO   A N     1 
ATOM   3206  C  CA    . PRO   A 1 702  ? 139.906 165.917 134.770 1.00 23.24  ? 702  PRO   A CA    1 
ATOM   3207  C  C     . PRO   A 1 702  ? 138.488 165.502 135.106 1.00 23.41  ? 702  PRO   A C     1 
ATOM   3208  O  O     . PRO   A 1 702  ? 137.610 166.364 135.229 1.00 26.71  ? 702  PRO   A O     1 
ATOM   3209  C  CB    . PRO   A 1 702  ? 140.162 165.921 133.257 1.00 23.02  ? 702  PRO   A CB    1 
ATOM   3210  C  CG    . PRO   A 1 702  ? 141.649 165.736 133.211 1.00 25.94  ? 702  PRO   A CG    1 
ATOM   3211  C  CD    . PRO   A 1 702  ? 141.783 164.549 134.133 1.00 27.77  ? 702  PRO   A CD    1 
ATOM   3212  N  N     . GLY   A 1 703  ? 138.236 164.207 135.259 1.00 24.30  ? 703  GLY   A N     1 
ATOM   3213  C  CA    . GLY   A 1 703  ? 136.921 163.707 135.582 1.00 24.46  ? 703  GLY   A CA    1 
ATOM   3214  C  C     . GLY   A 1 703  ? 136.584 163.680 137.055 1.00 34.43  ? 703  GLY   A C     1 
ATOM   3215  O  O     . GLY   A 1 703  ? 135.598 163.042 137.435 1.00 43.99  ? 703  GLY   A O     1 
ATOM   3216  N  N     . TRP   A 1 704  ? 137.367 164.351 137.903 1.00 31.02  ? 704  TRP   A N     1 
ATOM   3217  C  CA    . TRP   A 1 704  ? 137.015 164.422 139.317 1.00 18.60  ? 704  TRP   A CA    1 
ATOM   3218  C  C     . TRP   A 1 704  ? 135.784 165.296 139.520 1.00 33.10  ? 704  TRP   A C     1 
ATOM   3219  O  O     . TRP   A 1 704  ? 134.855 164.914 140.235 1.00 45.59  ? 704  TRP   A O     1 
ATOM   3220  C  CB    . TRP   A 1 704  ? 138.199 164.941 140.134 1.00 30.64  ? 704  TRP   A CB    1 
ATOM   3221  C  CG    . TRP   A 1 704  ? 137.891 165.179 141.591 1.00 34.60  ? 704  TRP   A CG    1 
ATOM   3222  C  CD1   . TRP   A 1 704  ? 138.390 166.175 142.379 1.00 35.47  ? 704  TRP   A CD1   1 
ATOM   3223  C  CD2   . TRP   A 1 704  ? 137.029 164.398 142.433 1.00 36.30  ? 704  TRP   A CD2   1 
ATOM   3224  N  NE1   . TRP   A 1 704  ? 137.887 166.070 143.653 1.00 33.31  ? 704  TRP   A NE1   1 
ATOM   3225  C  CE2   . TRP   A 1 704  ? 137.050 164.987 143.712 1.00 39.30  ? 704  TRP   A CE2   1 
ATOM   3226  C  CE3   . TRP   A 1 704  ? 136.239 163.262 142.227 1.00 33.21  ? 704  TRP   A CE3   1 
ATOM   3227  C  CZ2   . TRP   A 1 704  ? 136.312 164.480 144.780 1.00 32.33  ? 704  TRP   A CZ2   1 
ATOM   3228  C  CZ3   . TRP   A 1 704  ? 135.507 162.761 143.289 1.00 30.20  ? 704  TRP   A CZ3   1 
ATOM   3229  C  CH2   . TRP   A 1 704  ? 135.549 163.370 144.549 1.00 28.87  ? 704  TRP   A CH2   1 
ATOM   3230  N  N     . ARG   A 1 705  ? 135.785 166.496 138.935 1.00 28.96  ? 705  ARG   A N     1 
ATOM   3231  C  CA    . ARG   A 1 705  ? 134.588 167.286 138.650 1.00 27.97  ? 705  ARG   A CA    1 
ATOM   3232  C  C     . ARG   A 1 705  ? 133.457 167.057 139.648 1.00 25.55  ? 705  ARG   A C     1 
ATOM   3233  O  O     . ARG   A 1 705  ? 132.386 166.576 139.259 1.00 32.44  ? 705  ARG   A O     1 
ATOM   3234  C  CB    . ARG   A 1 705  ? 134.088 166.992 137.233 1.00 28.21  ? 705  ARG   A CB    1 
ATOM   3235  C  CG    . ARG   A 1 705  ? 134.621 167.951 136.183 1.00 27.75  ? 705  ARG   A CG    1 
ATOM   3236  C  CD    . ARG   A 1 705  ? 134.024 167.687 134.808 1.00 22.72  ? 705  ARG   A CD    1 
ATOM   3237  N  NE    . ARG   A 1 705  ? 134.313 166.342 134.327 1.00 16.57  ? 705  ARG   A NE    1 
ATOM   3238  C  CZ    . ARG   A 1 705  ? 133.400 165.497 133.867 1.00 23.90  ? 705  ARG   A CZ    1 
ATOM   3239  N  NH1   . ARG   A 1 705  ? 132.121 165.829 133.805 1.00 25.93  ? 705  ARG   A NH1   1 
ATOM   3240  N  NH2   . ARG   A 1 705  ? 133.780 164.292 133.455 1.00 25.95  ? 705  ARG   A NH2   1 
ATOM   3241  N  N     . PRO   A 1 706  ? 133.638 167.379 140.928 1.00 39.89  ? 706  PRO   A N     1 
ATOM   3242  C  CA    . PRO   A 1 706  ? 132.538 167.205 141.884 1.00 31.61  ? 706  PRO   A CA    1 
ATOM   3243  C  C     . PRO   A 1 706  ? 131.625 168.420 141.935 1.00 34.73  ? 706  PRO   A C     1 
ATOM   3244  O  O     . PRO   A 1 706  ? 132.064 169.570 141.866 1.00 39.60  ? 706  PRO   A O     1 
ATOM   3245  C  CB    . PRO   A 1 706  ? 133.269 167.000 143.219 1.00 24.98  ? 706  PRO   A CB    1 
ATOM   3246  C  CG    . PRO   A 1 706  ? 134.671 167.534 143.010 1.00 31.78  ? 706  PRO   A CG    1 
ATOM   3247  C  CD    . PRO   A 1 706  ? 134.841 167.930 141.569 1.00 40.68  ? 706  PRO   A CD    1 
ATOM   3248  N  N     . ALA   A 1 707  ? 130.326 168.149 142.070 1.00 29.40  ? 707  ALA   A N     1 
ATOM   3249  C  CA    . ALA   A 1 707  ? 129.316 169.198 142.042 1.00 24.99  ? 707  ALA   A CA    1 
ATOM   3250  C  C     . ALA   A 1 707  ? 129.151 169.912 143.376 1.00 32.89  ? 707  ALA   A C     1 
ATOM   3251  O  O     . ALA   A 1 707  ? 128.510 170.967 143.417 1.00 36.93  ? 707  ALA   A O     1 
ATOM   3252  C  CB    . ALA   A 1 707  ? 127.967 168.617 141.610 1.00 22.95  ? 707  ALA   A CB    1 
ATOM   3253  N  N     . PHE   A 1 708  ? 129.711 169.377 144.456 1.00 37.88  ? 708  PHE   A N     1 
ATOM   3254  C  CA    . PHE   A 1 708  ? 129.577 169.957 145.786 1.00 33.85  ? 708  PHE   A CA    1 
ATOM   3255  C  C     . PHE   A 1 708  ? 130.900 170.600 146.178 1.00 41.38  ? 708  PHE   A C     1 
ATOM   3256  O  O     . PHE   A 1 708  ? 131.935 169.927 146.209 1.00 43.55  ? 708  PHE   A O     1 
ATOM   3257  C  CB    . PHE   A 1 708  ? 129.165 168.892 146.804 1.00 34.96  ? 708  PHE   A CB    1 
ATOM   3258  C  CG    . PHE   A 1 708  ? 129.298 169.331 148.236 1.00 33.96  ? 708  PHE   A CG    1 
ATOM   3259  C  CD1   . PHE   A 1 708  ? 128.343 170.150 148.812 1.00 35.40  ? 708  PHE   A CD1   1 
ATOM   3260  C  CD2   . PHE   A 1 708  ? 130.367 168.913 149.010 1.00 37.28  ? 708  PHE   A CD2   1 
ATOM   3261  C  CE1   . PHE   A 1 708  ? 128.456 170.552 150.127 1.00 30.11  ? 708  PHE   A CE1   1 
ATOM   3262  C  CE2   . PHE   A 1 708  ? 130.484 169.313 150.327 1.00 42.48  ? 708  PHE   A CE2   1 
ATOM   3263  C  CZ    . PHE   A 1 708  ? 129.527 170.134 150.885 1.00 38.81  ? 708  PHE   A CZ    1 
ATOM   3264  N  N     . LYS   A 1 709  ? 130.864 171.898 146.468 1.00 47.27  ? 709  LYS   A N     1 
ATOM   3265  C  CA    . LYS   A 1 709  ? 132.045 172.627 146.913 1.00 49.88  ? 709  LYS   A CA    1 
ATOM   3266  C  C     . LYS   A 1 709  ? 132.240 172.409 148.414 1.00 53.02  ? 709  LYS   A C     1 
ATOM   3267  O  O     . LYS   A 1 709  ? 131.616 171.539 149.026 1.00 56.63  ? 709  LYS   A O     1 
ATOM   3268  C  CB    . LYS   A 1 709  ? 131.918 174.105 146.558 1.00 47.31  ? 709  LYS   A CB    1 
ATOM   3269  N  N     . TYR   A 1 710  ? 133.108 173.206 149.030 1.00 50.46  ? 710  TYR   A N     1 
ATOM   3270  C  CA    . TYR   A 1 710  ? 133.411 173.097 150.457 1.00 53.85  ? 710  TYR   A CA    1 
ATOM   3271  C  C     . TYR   A 1 710  ? 133.876 171.682 150.804 1.00 51.44  ? 710  TYR   A C     1 
ATOM   3272  O  O     . TYR   A 1 710  ? 133.324 171.008 151.674 1.00 54.18  ? 710  TYR   A O     1 
ATOM   3273  C  CB    . TYR   A 1 710  ? 132.207 173.493 151.319 1.00 49.07  ? 710  TYR   A CB    1 
ATOM   3274  C  CG    . TYR   A 1 710  ? 131.168 174.346 150.625 1.00 46.45  ? 710  TYR   A CG    1 
ATOM   3275  C  CD1   . TYR   A 1 710  ? 131.358 175.709 150.450 1.00 49.42  ? 710  TYR   A CD1   1 
ATOM   3276  C  CD2   . TYR   A 1 710  ? 129.991 173.783 150.153 1.00 48.23  ? 710  TYR   A CD2   1 
ATOM   3277  C  CE1   . TYR   A 1 710  ? 130.405 176.486 149.818 1.00 53.33  ? 710  TYR   A CE1   1 
ATOM   3278  C  CE2   . TYR   A 1 710  ? 129.037 174.549 149.520 1.00 51.21  ? 710  TYR   A CE2   1 
ATOM   3279  C  CZ    . TYR   A 1 710  ? 129.247 175.899 149.355 1.00 55.68  ? 710  TYR   A CZ    1 
ATOM   3280  O  OH    . TYR   A 1 710  ? 128.296 176.667 148.725 1.00 58.80  ? 710  TYR   A OH    1 
ATOM   3281  N  N     . TYR   A 1 711  ? 134.917 171.235 150.097 1.00 41.52  ? 711  TYR   A N     1 
ATOM   3282  C  CA    . TYR   A 1 711  ? 135.440 169.888 150.293 1.00 38.20  ? 711  TYR   A CA    1 
ATOM   3283  C  C     . TYR   A 1 711  ? 136.964 169.876 150.295 1.00 48.42  ? 711  TYR   A C     1 
ATOM   3284  O  O     . TYR   A 1 711  ? 137.577 168.893 149.867 1.00 58.71  ? 711  TYR   A O     1 
ATOM   3285  C  CB    . TYR   A 1 711  ? 134.911 168.930 149.222 1.00 43.98  ? 711  TYR   A CB    1 
ATOM   3286  C  CG    . TYR   A 1 711  ? 135.464 169.187 147.838 1.00 47.21  ? 711  TYR   A CG    1 
ATOM   3287  C  CD1   . TYR   A 1 711  ? 134.923 170.170 147.024 1.00 50.28  ? 711  TYR   A CD1   1 
ATOM   3288  C  CD2   . TYR   A 1 711  ? 136.522 168.436 147.342 1.00 41.62  ? 711  TYR   A CD2   1 
ATOM   3289  C  CE1   . TYR   A 1 711  ? 135.428 170.405 145.760 1.00 54.19  ? 711  TYR   A CE1   1 
ATOM   3290  C  CE2   . TYR   A 1 711  ? 137.032 168.663 146.084 1.00 45.52  ? 711  TYR   A CE2   1 
ATOM   3291  C  CZ    . TYR   A 1 711  ? 136.481 169.648 145.296 1.00 51.27  ? 711  TYR   A CZ    1 
ATOM   3292  O  OH    . TYR   A 1 711  ? 136.988 169.874 144.038 1.00 53.37  ? 711  TYR   A OH    1 
ATOM   3293  N  N     . ASN   A 1 712  ? 137.585 170.952 150.781 1.00 44.38  ? 712  ASN   A N     1 
ATOM   3294  C  CA    . ASN   A 1 712  ? 139.033 171.115 150.704 1.00 40.03  ? 712  ASN   A CA    1 
ATOM   3295  C  C     . ASN   A 1 712  ? 139.756 169.807 150.998 1.00 39.56  ? 712  ASN   A C     1 
ATOM   3296  O  O     . ASN   A 1 712  ? 139.422 169.091 151.944 1.00 39.65  ? 712  ASN   A O     1 
ATOM   3297  C  CB    . ASN   A 1 712  ? 139.491 172.198 151.683 1.00 41.81  ? 712  ASN   A CB    1 
ATOM   3298  C  CG    . ASN   A 1 712  ? 140.979 172.464 151.603 1.00 43.97  ? 712  ASN   A CG    1 
ATOM   3299  O  OD1   . ASN   A 1 712  ? 141.786 171.706 152.139 1.00 45.50  ? 712  ASN   A OD1   1 
ATOM   3300  N  ND2   . ASN   A 1 712  ? 141.351 173.546 150.929 1.00 46.94  ? 712  ASN   A ND2   1 
ATOM   3301  N  N     . MET   A 1 713  ? 140.754 169.504 150.166 1.00 41.55  ? 713  MET   A N     1 
ATOM   3302  C  CA    . MET   A 1 713  ? 141.459 168.230 150.277 1.00 42.18  ? 713  MET   A CA    1 
ATOM   3303  C  C     . MET   A 1 713  ? 142.192 168.113 151.605 1.00 47.80  ? 713  MET   A C     1 
ATOM   3304  O  O     . MET   A 1 713  ? 142.243 167.032 152.203 1.00 54.09  ? 713  MET   A O     1 
ATOM   3305  C  CB    . MET   A 1 713  ? 142.438 168.078 149.114 1.00 44.84  ? 713  MET   A CB    1 
ATOM   3306  C  CG    . MET   A 1 713  ? 143.523 169.143 149.086 1.00 46.41  ? 713  MET   A CG    1 
ATOM   3307  S  SD    . MET   A 1 713  ? 144.622 168.995 147.667 1.00 67.05  ? 713  MET   A SD    1 
ATOM   3308  C  CE    . MET   A 1 713  ? 145.249 167.335 147.900 1.00 46.91  ? 713  MET   A CE    1 
ATOM   3309  N  N     . TRP   A 1 714  ? 142.783 169.212 152.073 1.00 44.60  ? 714  TRP   A N     1 
ATOM   3310  C  CA    . TRP   A 1 714  ? 143.523 169.169 153.328 1.00 41.81  ? 714  TRP   A CA    1 
ATOM   3311  C  C     . TRP   A 1 714  ? 142.591 168.913 154.502 1.00 44.48  ? 714  TRP   A C     1 
ATOM   3312  O  O     . TRP   A 1 714  ? 142.950 168.195 155.441 1.00 43.67  ? 714  TRP   A O     1 
ATOM   3313  C  CB    . TRP   A 1 714  ? 144.299 170.468 153.517 1.00 44.12  ? 714  TRP   A CB    1 
ATOM   3314  C  CG    . TRP   A 1 714  ? 145.256 170.715 152.402 1.00 42.46  ? 714  TRP   A CG    1 
ATOM   3315  C  CD1   . TRP   A 1 714  ? 145.314 171.815 151.601 1.00 45.13  ? 714  TRP   A CD1   1 
ATOM   3316  C  CD2   . TRP   A 1 714  ? 146.273 169.823 151.936 1.00 39.46  ? 714  TRP   A CD2   1 
ATOM   3317  N  NE1   . TRP   A 1 714  ? 146.318 171.672 150.675 1.00 47.21  ? 714  TRP   A NE1   1 
ATOM   3318  C  CE2   . TRP   A 1 714  ? 146.920 170.456 150.859 1.00 44.69  ? 714  TRP   A CE2   1 
ATOM   3319  C  CE3   . TRP   A 1 714  ? 146.704 168.553 152.331 1.00 36.57  ? 714  TRP   A CE3   1 
ATOM   3320  C  CZ2   . TRP   A 1 714  ? 147.976 169.864 150.172 1.00 45.93  ? 714  TRP   A CZ2   1 
ATOM   3321  C  CZ3   . TRP   A 1 714  ? 147.750 167.967 151.649 1.00 42.78  ? 714  TRP   A CZ3   1 
ATOM   3322  C  CH2   . TRP   A 1 714  ? 148.375 168.622 150.581 1.00 46.35  ? 714  TRP   A CH2   1 
ATOM   3323  N  N     . ILE   A 1 715  ? 141.388 169.487 154.466 1.00 38.21  ? 715  ILE   A N     1 
ATOM   3324  C  CA    . ILE   A 1 715  ? 140.410 169.200 155.510 1.00 36.47  ? 715  ILE   A CA    1 
ATOM   3325  C  C     . ILE   A 1 715  ? 140.036 167.724 155.492 1.00 37.42  ? 715  ILE   A C     1 
ATOM   3326  O  O     . ILE   A 1 715  ? 139.850 167.105 156.543 1.00 44.41  ? 715  ILE   A O     1 
ATOM   3327  C  CB    . ILE   A 1 715  ? 139.172 170.101 155.356 1.00 38.42  ? 715  ILE   A CB    1 
ATOM   3328  C  CG1   . ILE   A 1 715  ? 139.433 171.480 155.965 1.00 39.45  ? 715  ILE   A CG1   1 
ATOM   3329  C  CG2   . ILE   A 1 715  ? 137.961 169.453 156.005 1.00 39.71  ? 715  ILE   A CG2   1 
ATOM   3330  C  CD1   . ILE   A 1 715  ? 140.297 172.369 155.106 1.00 45.31  ? 715  ILE   A CD1   1 
ATOM   3331  N  N     . SER   A 1 716  ? 139.924 167.134 154.300 1.00 31.12  ? 716  SER   A N     1 
ATOM   3332  C  CA    . SER   A 1 716  ? 139.595 165.714 154.210 1.00 24.99  ? 716  SER   A CA    1 
ATOM   3333  C  C     . SER   A 1 716  ? 140.722 164.844 154.755 1.00 29.25  ? 716  SER   A C     1 
ATOM   3334  O  O     . SER   A 1 716  ? 140.470 163.852 155.452 1.00 40.18  ? 716  SER   A O     1 
ATOM   3335  C  CB    . SER   A 1 716  ? 139.282 165.340 152.763 1.00 32.82  ? 716  SER   A CB    1 
ATOM   3336  O  OG    . SER   A 1 716  ? 137.923 165.594 152.456 1.00 41.95  ? 716  SER   A OG    1 
ATOM   3337  N  N     . LEU   A 1 717  ? 141.971 165.186 154.434 1.00 38.50  ? 717  LEU   A N     1 
ATOM   3338  C  CA    . LEU   A 1 717  ? 143.100 164.442 154.982 1.00 36.31  ? 717  LEU   A CA    1 
ATOM   3339  C  C     . LEU   A 1 717  ? 143.149 164.567 156.499 1.00 45.07  ? 717  LEU   A C     1 
ATOM   3340  O  O     . LEU   A 1 717  ? 143.389 163.581 157.209 1.00 44.68  ? 717  LEU   A O     1 
ATOM   3341  C  CB    . LEU   A 1 717  ? 144.404 164.936 154.356 1.00 33.58  ? 717  LEU   A CB    1 
ATOM   3342  C  CG    . LEU   A 1 717  ? 145.702 164.337 154.896 1.00 39.31  ? 717  LEU   A CG    1 
ATOM   3343  C  CD1   . LEU   A 1 717  ? 145.814 162.872 154.507 1.00 36.47  ? 717  LEU   A CD1   1 
ATOM   3344  C  CD2   . LEU   A 1 717  ? 146.898 165.124 154.393 1.00 37.28  ? 717  LEU   A CD2   1 
ATOM   3345  N  N     . LEU   A 1 718  ? 142.919 165.777 157.014 1.00 41.09  ? 718  LEU   A N     1 
ATOM   3346  C  CA    . LEU   A 1 718  ? 142.865 165.974 158.456 1.00 40.77  ? 718  LEU   A CA    1 
ATOM   3347  C  C     . LEU   A 1 718  ? 141.732 165.170 159.075 1.00 40.70  ? 718  LEU   A C     1 
ATOM   3348  O  O     . LEU   A 1 718  ? 141.869 164.646 160.182 1.00 43.50  ? 718  LEU   A O     1 
ATOM   3349  C  CB    . LEU   A 1 718  ? 142.709 167.459 158.778 1.00 42.67  ? 718  LEU   A CB    1 
ATOM   3350  C  CG    . LEU   A 1 718  ? 142.286 167.794 160.209 1.00 42.56  ? 718  LEU   A CG    1 
ATOM   3351  C  CD1   . LEU   A 1 718  ? 143.492 167.788 161.134 1.00 40.25  ? 718  LEU   A CD1   1 
ATOM   3352  C  CD2   . LEU   A 1 718  ? 141.570 169.134 160.259 1.00 39.14  ? 718  LEU   A CD2   1 
ATOM   3353  N  N     . GLY   A 1 719  ? 140.600 165.070 158.378 1.00 33.32  ? 719  GLY   A N     1 
ATOM   3354  C  CA    . GLY   A 1 719  ? 139.495 164.278 158.888 1.00 43.49  ? 719  GLY   A CA    1 
ATOM   3355  C  C     . GLY   A 1 719  ? 139.817 162.799 158.945 1.00 37.68  ? 719  GLY   A C     1 
ATOM   3356  O  O     . GLY   A 1 719  ? 139.449 162.114 159.899 1.00 37.05  ? 719  GLY   A O     1 
ATOM   3357  N  N     . ALA   A 1 720  ? 140.503 162.284 157.925 1.00 36.72  ? 720  ALA   A N     1 
ATOM   3358  C  CA    . ALA   A 1 720  ? 140.927 160.887 157.965 1.00 37.97  ? 720  ALA   A CA    1 
ATOM   3359  C  C     . ALA   A 1 720  ? 141.915 160.647 159.102 1.00 44.77  ? 720  ALA   A C     1 
ATOM   3360  O  O     . ALA   A 1 720  ? 141.827 159.637 159.818 1.00 43.13  ? 720  ALA   A O     1 
ATOM   3361  C  CB    . ALA   A 1 720  ? 141.540 160.485 156.624 1.00 33.71  ? 720  ALA   A CB    1 
ATOM   3362  N  N     . ILE   A 1 721  ? 142.858 161.573 159.292 1.00 46.51  ? 721  ILE   A N     1 
ATOM   3363  C  CA    . ILE   A 1 721  ? 143.814 161.439 160.387 1.00 41.39  ? 721  ILE   A CA    1 
ATOM   3364  C  C     . ILE   A 1 721  ? 143.092 161.475 161.728 1.00 41.62  ? 721  ILE   A C     1 
ATOM   3365  O  O     . ILE   A 1 721  ? 143.402 160.699 162.639 1.00 42.41  ? 721  ILE   A O     1 
ATOM   3366  C  CB    . ILE   A 1 721  ? 144.894 162.532 160.297 1.00 42.45  ? 721  ILE   A CB    1 
ATOM   3367  C  CG1   . ILE   A 1 721  ? 145.993 162.117 159.317 1.00 40.19  ? 721  ILE   A CG1   1 
ATOM   3368  C  CG2   . ILE   A 1 721  ? 145.491 162.801 161.667 1.00 45.72  ? 721  ILE   A CG2   1 
ATOM   3369  C  CD1   . ILE   A 1 721  ? 146.568 163.269 158.526 1.00 38.37  ? 721  ILE   A CD1   1 
ATOM   3370  N  N     . LEU   A 1 722  ? 142.130 162.387 161.874 1.00 38.75  ? 722  LEU   A N     1 
ATOM   3371  C  CA    . LEU   A 1 722  ? 141.361 162.474 163.109 1.00 33.42  ? 722  LEU   A CA    1 
ATOM   3372  C  C     . LEU   A 1 722  ? 140.544 161.212 163.334 1.00 33.59  ? 722  LEU   A C     1 
ATOM   3373  O  O     . LEU   A 1 722  ? 140.380 160.767 164.473 1.00 42.09  ? 722  LEU   A O     1 
ATOM   3374  C  CB    . LEU   A 1 722  ? 140.451 163.700 163.072 1.00 41.01  ? 722  LEU   A CB    1 
ATOM   3375  C  CG    . LEU   A 1 722  ? 141.136 165.053 163.257 1.00 38.90  ? 722  LEU   A CG    1 
ATOM   3376  C  CD1   . LEU   A 1 722  ? 140.110 166.149 163.472 1.00 39.22  ? 722  LEU   A CD1   1 
ATOM   3377  C  CD2   . LEU   A 1 722  ? 142.104 164.995 164.421 1.00 40.24  ? 722  LEU   A CD2   1 
ATOM   3378  N  N     . CYS   A 1 723  ? 140.004 160.632 162.263 1.00 45.04  ? 723  CYS   A N     1 
ATOM   3379  C  CA    . CYS   A 1 723  ? 139.272 159.380 162.394 1.00 42.45  ? 723  CYS   A CA    1 
ATOM   3380  C  C     . CYS   A 1 723  ? 140.179 158.278 162.918 1.00 42.47  ? 723  CYS   A C     1 
ATOM   3381  O  O     . CYS   A 1 723  ? 139.803 157.536 163.830 1.00 41.52  ? 723  CYS   A O     1 
ATOM   3382  C  CB    . CYS   A 1 723  ? 138.662 158.984 161.050 1.00 36.33  ? 723  CYS   A CB    1 
ATOM   3383  S  SG    . CYS   A 1 723  ? 137.211 159.948 160.577 1.00 50.54  ? 723  CYS   A SG    1 
ATOM   3384  N  N     . CYS   A 1 724  ? 141.391 158.174 162.370 1.00 42.93  ? 724  CYS   A N     1 
ATOM   3385  C  CA    . CYS   A 1 724  ? 142.337 157.178 162.869 1.00 41.87  ? 724  CYS   A CA    1 
ATOM   3386  C  C     . CYS   A 1 724  ? 142.703 157.441 164.328 1.00 48.03  ? 724  CYS   A C     1 
ATOM   3387  O  O     . CYS   A 1 724  ? 142.772 156.510 165.143 1.00 47.60  ? 724  CYS   A O     1 
ATOM   3388  C  CB    . CYS   A 1 724  ? 143.590 157.162 161.995 1.00 42.34  ? 724  CYS   A CB    1 
ATOM   3389  S  SG    . CYS   A 1 724  ? 143.333 156.509 160.330 1.00 59.79  ? 724  CYS   A SG    1 
ATOM   3390  N  N     . ILE   A 1 725  ? 142.938 158.707 164.678 1.00 46.03  ? 725  ILE   A N     1 
ATOM   3391  C  CA    . ILE   A 1 725  ? 143.343 159.042 166.039 1.00 38.54  ? 725  ILE   A CA    1 
ATOM   3392  C  C     . ILE   A 1 725  ? 142.227 158.727 167.028 1.00 44.87  ? 725  ILE   A C     1 
ATOM   3393  O  O     . ILE   A 1 725  ? 142.474 158.173 168.103 1.00 49.03  ? 725  ILE   A O     1 
ATOM   3394  C  CB    . ILE   A 1 725  ? 143.778 160.515 166.121 1.00 43.23  ? 725  ILE   A CB    1 
ATOM   3395  C  CG1   . ILE   A 1 725  ? 145.198 160.680 165.577 1.00 46.20  ? 725  ILE   A CG1   1 
ATOM   3396  C  CG2   . ILE   A 1 725  ? 143.698 161.011 167.554 1.00 46.40  ? 725  ILE   A CG2   1 
ATOM   3397  C  CD1   . ILE   A 1 725  ? 145.499 162.067 165.055 1.00 46.10  ? 725  ILE   A CD1   1 
ATOM   3398  N  N     . VAL   A 1 726  ? 140.987 159.090 166.693 1.00 44.65  ? 726  VAL   A N     1 
ATOM   3399  C  CA    . VAL   A 1 726  ? 139.850 158.770 167.553 1.00 36.46  ? 726  VAL   A CA    1 
ATOM   3400  C  C     . VAL   A 1 726  ? 139.657 157.264 167.641 1.00 38.82  ? 726  VAL   A C     1 
ATOM   3401  O  O     . VAL   A 1 726  ? 139.283 156.730 168.692 1.00 39.79  ? 726  VAL   A O     1 
ATOM   3402  C  CB    . VAL   A 1 726  ? 138.579 159.474 167.044 1.00 33.24  ? 726  VAL   A CB    1 
ATOM   3403  C  CG1   . VAL   A 1 726  ? 137.350 158.872 167.696 1.00 38.78  ? 726  VAL   A CG1   1 
ATOM   3404  C  CG2   . VAL   A 1 726  ? 138.653 160.963 167.323 1.00 37.57  ? 726  VAL   A CG2   1 
ATOM   3405  N  N     . MET   A 1 727  ? 139.898 156.556 166.538 1.00 44.60  ? 727  MET   A N     1 
ATOM   3406  C  CA    . MET   A 1 727  ? 139.831 155.102 166.562 1.00 42.67  ? 727  MET   A CA    1 
ATOM   3407  C  C     . MET   A 1 727  ? 140.808 154.541 167.584 1.00 48.45  ? 727  MET   A C     1 
ATOM   3408  O  O     . MET   A 1 727  ? 140.475 153.621 168.340 1.00 52.05  ? 727  MET   A O     1 
ATOM   3409  C  CB    . MET   A 1 727  ? 140.134 154.559 165.166 1.00 46.21  ? 727  MET   A CB    1 
ATOM   3410  C  CG    . MET   A 1 727  ? 139.406 153.288 164.792 1.00 48.08  ? 727  MET   A CG    1 
ATOM   3411  S  SD    . MET   A 1 727  ? 140.233 152.422 163.445 1.00 61.13  ? 727  MET   A SD    1 
ATOM   3412  C  CE    . MET   A 1 727  ? 140.209 153.681 162.171 1.00 44.63  ? 727  MET   A CE    1 
ATOM   3413  N  N     . PHE   A 1 728  ? 142.022 155.091 167.621 1.00 50.69  ? 728  PHE   A N     1 
ATOM   3414  C  CA    . PHE   A 1 728  ? 143.000 154.665 168.618 1.00 47.18  ? 728  PHE   A CA    1 
ATOM   3415  C  C     . PHE   A 1 728  ? 142.582 155.071 170.027 1.00 49.30  ? 728  PHE   A C     1 
ATOM   3416  O  O     . PHE   A 1 728  ? 142.789 154.315 170.983 1.00 46.23  ? 728  PHE   A O     1 
ATOM   3417  C  CB    . PHE   A 1 728  ? 144.373 155.242 168.284 1.00 44.43  ? 728  PHE   A CB    1 
ATOM   3418  C  CG    . PHE   A 1 728  ? 145.288 154.265 167.614 1.00 49.34  ? 728  PHE   A CG    1 
ATOM   3419  C  CD1   . PHE   A 1 728  ? 146.054 154.643 166.527 1.00 53.19  ? 728  PHE   A CD1   1 
ATOM   3420  C  CD2   . PHE   A 1 728  ? 145.383 152.965 168.075 1.00 48.37  ? 728  PHE   A CD2   1 
ATOM   3421  C  CE1   . PHE   A 1 728  ? 146.895 153.741 165.911 1.00 53.87  ? 728  PHE   A CE1   1 
ATOM   3422  C  CE2   . PHE   A 1 728  ? 146.222 152.061 167.465 1.00 51.90  ? 728  PHE   A CE2   1 
ATOM   3423  C  CZ    . PHE   A 1 728  ? 146.980 152.448 166.381 1.00 54.97  ? 728  PHE   A CZ    1 
ATOM   3424  N  N     . VAL   A 1 729  ? 141.988 156.258 170.175 1.00 50.83  ? 729  VAL   A N     1 
ATOM   3425  C  CA    . VAL   A 1 729  ? 141.693 156.794 171.501 1.00 41.56  ? 729  VAL   A CA    1 
ATOM   3426  C  C     . VAL   A 1 729  ? 140.773 155.864 172.276 1.00 44.91  ? 729  VAL   A C     1 
ATOM   3427  O  O     . VAL   A 1 729  ? 140.783 155.858 173.513 1.00 55.82  ? 729  VAL   A O     1 
ATOM   3428  C  CB    . VAL   A 1 729  ? 141.095 158.210 171.382 1.00 44.47  ? 729  VAL   A CB    1 
ATOM   3429  C  CG1   . VAL   A 1 729  ? 140.273 158.549 172.616 1.00 42.47  ? 729  VAL   A CG1   1 
ATOM   3430  C  CG2   . VAL   A 1 729  ? 142.199 159.233 171.176 1.00 43.86  ? 729  VAL   A CG2   1 
ATOM   3431  N  N     . ILE   A 1 730  ? 139.966 155.070 171.580 1.00 43.36  ? 730  ILE   A N     1 
ATOM   3432  C  CA    . ILE   A 1 730  ? 139.070 154.111 172.212 1.00 42.46  ? 730  ILE   A CA    1 
ATOM   3433  C  C     . ILE   A 1 730  ? 139.491 152.715 171.772 1.00 49.34  ? 730  ILE   A C     1 
ATOM   3434  O  O     . ILE   A 1 730  ? 139.519 152.412 170.572 1.00 57.95  ? 730  ILE   A O     1 
ATOM   3435  C  CB    . ILE   A 1 730  ? 137.599 154.399 171.870 1.00 45.04  ? 730  ILE   A CB    1 
ATOM   3436  C  CG1   . ILE   A 1 730  ? 137.147 153.630 170.629 1.00 45.84  ? 730  ILE   A CG1   1 
ATOM   3437  C  CG2   . ILE   A 1 730  ? 137.397 155.885 171.639 1.00 50.64  ? 730  ILE   A CG2   1 
ATOM   3438  C  CD1   . ILE   A 1 730  ? 135.774 154.026 170.141 1.00 42.03  ? 730  ILE   A CD1   1 
ATOM   3439  N  N     . ASN   A 1 731  ? 139.852 151.874 172.742 1.00 45.64  ? 731  ASN   A N     1 
ATOM   3440  C  CA    . ASN   A 1 731  ? 140.196 150.475 172.495 1.00 45.74  ? 731  ASN   A CA    1 
ATOM   3441  C  C     . ASN   A 1 731  ? 141.309 150.354 171.447 1.00 41.34  ? 731  ASN   A C     1 
ATOM   3442  O  O     . ASN   A 1 731  ? 141.110 149.883 170.326 1.00 51.22  ? 731  ASN   A O     1 
ATOM   3443  C  CB    . ASN   A 1 731  ? 138.961 149.665 172.089 1.00 44.72  ? 731  ASN   A CB    1 
ATOM   3444  C  CG    . ASN   A 1 731  ? 139.011 148.252 172.618 1.00 49.96  ? 731  ASN   A CG    1 
ATOM   3445  O  OD1   . ASN   A 1 731  ? 140.066 147.775 173.022 1.00 50.28  ? 731  ASN   A OD1   1 
ATOM   3446  N  ND2   . ASN   A 1 731  ? 137.876 147.573 172.619 1.00 57.41  ? 731  ASN   A ND2   1 
ATOM   3447  N  N     . TRP   A 1 732  ? 142.494 150.816 171.851 1.00 39.98  ? 732  TRP   A N     1 
ATOM   3448  C  CA    . TRP   A 1 732  ? 143.656 150.792 170.965 1.00 46.23  ? 732  TRP   A CA    1 
ATOM   3449  C  C     . TRP   A 1 732  ? 143.870 149.418 170.334 1.00 42.89  ? 732  TRP   A C     1 
ATOM   3450  O  O     . TRP   A 1 732  ? 144.206 149.318 169.147 1.00 56.13  ? 732  TRP   A O     1 
ATOM   3451  C  CB    . TRP   A 1 732  ? 144.901 151.224 171.742 1.00 51.24  ? 732  TRP   A CB    1 
ATOM   3452  C  CG    . TRP   A 1 732  ? 145.232 150.301 172.878 1.00 52.91  ? 732  TRP   A CG    1 
ATOM   3453  C  CD1   . TRP   A 1 732  ? 144.748 150.367 174.152 1.00 50.14  ? 732  TRP   A CD1   1 
ATOM   3454  C  CD2   . TRP   A 1 732  ? 146.099 149.162 172.838 1.00 50.94  ? 732  TRP   A CD2   1 
ATOM   3455  N  NE1   . TRP   A 1 732  ? 145.266 149.347 174.909 1.00 48.24  ? 732  TRP   A NE1   1 
ATOM   3456  C  CE2   . TRP   A 1 732  ? 146.098 148.591 174.126 1.00 47.64  ? 732  TRP   A CE2   1 
ATOM   3457  C  CE3   . TRP   A 1 732  ? 146.879 148.570 171.840 1.00 49.16  ? 732  TRP   A CE3   1 
ATOM   3458  C  CZ2   . TRP   A 1 732  ? 146.845 147.460 174.442 1.00 50.76  ? 732  TRP   A CZ2   1 
ATOM   3459  C  CZ3   . TRP   A 1 732  ? 147.620 147.447 172.156 1.00 48.60  ? 732  TRP   A CZ3   1 
ATOM   3460  C  CH2   . TRP   A 1 732  ? 147.598 146.904 173.446 1.00 51.96  ? 732  TRP   A CH2   1 
ATOM   3461  N  N     . TRP   A 1 733  ? 143.687 148.345 171.106 1.00 36.99  ? 733  TRP   A N     1 
ATOM   3462  C  CA    . TRP   A 1 733  ? 143.857 147.012 170.534 1.00 41.82  ? 733  TRP   A CA    1 
ATOM   3463  C  C     . TRP   A 1 733  ? 142.763 146.707 169.520 1.00 45.92  ? 733  TRP   A C     1 
ATOM   3464  O  O     . TRP   A 1 733  ? 143.009 146.026 168.517 1.00 52.89  ? 733  TRP   A O     1 
ATOM   3465  C  CB    . TRP   A 1 733  ? 143.906 145.955 171.640 1.00 49.06  ? 733  TRP   A CB    1 
ATOM   3466  C  CG    . TRP   A 1 733  ? 142.604 145.682 172.329 1.00 45.31  ? 733  TRP   A CG    1 
ATOM   3467  C  CD1   . TRP   A 1 733  ? 142.232 146.118 173.564 1.00 49.96  ? 733  TRP   A CD1   1 
ATOM   3468  C  CD2   . TRP   A 1 733  ? 141.515 144.886 171.840 1.00 46.02  ? 733  TRP   A CD2   1 
ATOM   3469  N  NE1   . TRP   A 1 733  ? 140.974 145.661 173.871 1.00 54.01  ? 733  TRP   A NE1   1 
ATOM   3470  C  CE2   . TRP   A 1 733  ? 140.512 144.900 172.829 1.00 48.14  ? 733  TRP   A CE2   1 
ATOM   3471  C  CE3   . TRP   A 1 733  ? 141.287 144.171 170.661 1.00 50.08  ? 733  TRP   A CE3   1 
ATOM   3472  C  CZ2   . TRP   A 1 733  ? 139.303 144.229 172.676 1.00 42.78  ? 733  TRP   A CZ2   1 
ATOM   3473  C  CZ3   . TRP   A 1 733  ? 140.085 143.506 170.510 1.00 49.29  ? 733  TRP   A CZ3   1 
ATOM   3474  C  CH2   . TRP   A 1 733  ? 139.109 143.538 171.512 1.00 44.56  ? 733  TRP   A CH2   1 
ATOM   3475  N  N     . ALA   A 1 734  ? 141.550 147.207 169.756 1.00 50.49  ? 734  ALA   A N     1 
ATOM   3476  C  CA    . ALA   A 1 734  ? 140.508 147.097 168.742 1.00 45.66  ? 734  ALA   A CA    1 
ATOM   3477  C  C     . ALA   A 1 734  ? 140.915 147.824 167.467 1.00 45.27  ? 734  ALA   A C     1 
ATOM   3478  O  O     . ALA   A 1 734  ? 140.671 147.336 166.358 1.00 58.27  ? 734  ALA   A O     1 
ATOM   3479  C  CB    . ALA   A 1 734  ? 139.188 147.646 169.280 1.00 47.89  ? 734  ALA   A CB    1 
ATOM   3480  N  N     . ALA   A 1 735  ? 141.537 148.998 167.607 1.00 39.07  ? 735  ALA   A N     1 
ATOM   3481  C  CA    . ALA   A 1 735  ? 142.018 149.722 166.436 1.00 39.88  ? 735  ALA   A CA    1 
ATOM   3482  C  C     . ALA   A 1 735  ? 143.066 148.915 165.682 1.00 47.89  ? 735  ALA   A C     1 
ATOM   3483  O  O     . ALA   A 1 735  ? 143.040 148.851 164.447 1.00 53.38  ? 735  ALA   A O     1 
ATOM   3484  C  CB    . ALA   A 1 735  ? 142.580 151.080 166.852 1.00 41.85  ? 735  ALA   A CB    1 
ATOM   3485  N  N     . LEU   A 1 736  ? 144.000 148.296 166.407 1.00 48.74  ? 736  LEU   A N     1 
ATOM   3486  C  CA    . LEU   A 1 736  ? 144.984 147.441 165.751 1.00 50.33  ? 736  LEU   A CA    1 
ATOM   3487  C  C     . LEU   A 1 736  ? 144.309 146.288 165.021 1.00 49.96  ? 736  LEU   A C     1 
ATOM   3488  O  O     . LEU   A 1 736  ? 144.699 145.937 163.901 1.00 50.16  ? 736  LEU   A O     1 
ATOM   3489  C  CB    . LEU   A 1 736  ? 145.989 146.909 166.773 1.00 51.66  ? 736  LEU   A CB    1 
ATOM   3490  C  CG    . LEU   A 1 736  ? 147.331 147.636 166.869 1.00 50.96  ? 736  LEU   A CG    1 
ATOM   3491  C  CD1   . LEU   A 1 736  ? 147.132 149.134 166.829 1.00 50.45  ? 736  LEU   A CD1   1 
ATOM   3492  C  CD2   . LEU   A 1 736  ? 148.064 147.228 168.135 1.00 53.09  ? 736  LEU   A CD2   1 
ATOM   3493  N  N     . LEU   A 1 737  ? 143.300 145.681 165.644 1.00 42.74  ? 737  LEU   A N     1 
ATOM   3494  C  CA    . LEU   A 1 737  ? 142.610 144.560 165.015 1.00 45.94  ? 737  LEU   A CA    1 
ATOM   3495  C  C     . LEU   A 1 737  ? 141.927 144.993 163.722 1.00 48.42  ? 737  LEU   A C     1 
ATOM   3496  O  O     . LEU   A 1 737  ? 142.019 144.307 162.696 1.00 52.28  ? 737  LEU   A O     1 
ATOM   3497  C  CB    . LEU   A 1 737  ? 141.596 143.959 165.988 1.00 46.38  ? 737  LEU   A CB    1 
ATOM   3498  C  CG    . LEU   A 1 737  ? 140.627 142.934 165.404 1.00 44.26  ? 737  LEU   A CG    1 
ATOM   3499  C  CD1   . LEU   A 1 737  ? 141.382 141.705 164.927 1.00 47.02  ? 737  LEU   A CD1   1 
ATOM   3500  C  CD2   . LEU   A 1 737  ? 139.569 142.555 166.425 1.00 46.74  ? 737  LEU   A CD2   1 
ATOM   3501  N  N     . THR   A 1 738  ? 141.233 146.135 163.752 1.00 49.80  ? 738  THR   A N     1 
ATOM   3502  C  CA    . THR   A 1 738  ? 140.579 146.621 162.539 1.00 54.82  ? 738  THR   A CA    1 
ATOM   3503  C  C     . THR   A 1 738  ? 141.598 146.964 161.461 1.00 52.41  ? 738  THR   A C     1 
ATOM   3504  O  O     . THR   A 1 738  ? 141.383 146.670 160.279 1.00 50.04  ? 738  THR   A O     1 
ATOM   3505  C  CB    . THR   A 1 738  ? 139.697 147.835 162.840 1.00 51.34  ? 738  THR   A CB    1 
ATOM   3506  O  OG1   . THR   A 1 738  ? 140.476 149.034 162.746 1.00 48.02  ? 738  THR   A OG1   1 
ATOM   3507  C  CG2   . THR   A 1 738  ? 139.071 147.729 164.216 1.00 48.94  ? 738  THR   A CG2   1 
ATOM   3508  N  N     . TYR   A 1 739  ? 142.709 147.597 161.844 1.00 51.54  ? 739  TYR   A N     1 
ATOM   3509  C  CA    . TYR   A 1 739  ? 143.746 147.906 160.866 1.00 49.95  ? 739  TYR   A CA    1 
ATOM   3510  C  C     . TYR   A 1 739  ? 144.276 146.637 160.215 1.00 49.21  ? 739  TYR   A C     1 
ATOM   3511  O  O     . TYR   A 1 739  ? 144.448 146.580 158.991 1.00 50.15  ? 739  TYR   A O     1 
ATOM   3512  C  CB    . TYR   A 1 739  ? 144.885 148.678 161.531 1.00 46.78  ? 739  TYR   A CB    1 
ATOM   3513  C  CG    . TYR   A 1 739  ? 144.561 150.120 161.841 1.00 51.32  ? 739  TYR   A CG    1 
ATOM   3514  C  CD1   . TYR   A 1 739  ? 143.577 150.799 161.139 1.00 54.80  ? 739  TYR   A CD1   1 
ATOM   3515  C  CD2   . TYR   A 1 739  ? 145.245 150.804 162.837 1.00 54.79  ? 739  TYR   A CD2   1 
ATOM   3516  C  CE1   . TYR   A 1 739  ? 143.281 152.118 161.420 1.00 53.06  ? 739  TYR   A CE1   1 
ATOM   3517  C  CE2   . TYR   A 1 739  ? 144.956 152.123 163.126 1.00 57.70  ? 739  TYR   A CE2   1 
ATOM   3518  C  CZ    . TYR   A 1 739  ? 143.974 152.775 162.414 1.00 57.00  ? 739  TYR   A CZ    1 
ATOM   3519  O  OH    . TYR   A 1 739  ? 143.683 154.089 162.698 1.00 55.17  ? 739  TYR   A OH    1 
ATOM   3520  N  N     . VAL   A 1 740  ? 144.539 145.607 161.020 1.00 52.15  ? 740  VAL   A N     1 
ATOM   3521  C  CA    . VAL   A 1 740  ? 145.059 144.353 160.485 1.00 48.57  ? 740  VAL   A CA    1 
ATOM   3522  C  C     . VAL   A 1 740  ? 144.046 143.710 159.549 1.00 52.41  ? 740  VAL   A C     1 
ATOM   3523  O  O     . VAL   A 1 740  ? 144.403 143.204 158.479 1.00 58.80  ? 740  VAL   A O     1 
ATOM   3524  C  CB    . VAL   A 1 740  ? 145.451 143.405 161.633 1.00 51.63  ? 740  VAL   A CB    1 
ATOM   3525  C  CG1   . VAL   A 1 740  ? 145.323 141.957 161.191 1.00 50.44  ? 740  VAL   A CG1   1 
ATOM   3526  C  CG2   . VAL   A 1 740  ? 146.866 143.702 162.106 1.00 53.80  ? 740  VAL   A CG2   1 
ATOM   3527  N  N     . ILE   A 1 741  ? 142.769 143.710 159.937 1.00 51.38  ? 741  ILE   A N     1 
ATOM   3528  C  CA    . ILE   A 1 741  ? 141.739 143.102 159.098 1.00 49.67  ? 741  ILE   A CA    1 
ATOM   3529  C  C     . ILE   A 1 741  ? 141.643 143.833 157.764 1.00 47.24  ? 741  ILE   A C     1 
ATOM   3530  O  O     . ILE   A 1 741  ? 141.566 143.212 156.695 1.00 53.75  ? 741  ILE   A O     1 
ATOM   3531  C  CB    . ILE   A 1 741  ? 140.387 143.092 159.832 1.00 49.13  ? 741  ILE   A CB    1 
ATOM   3532  C  CG1   . ILE   A 1 741  ? 140.478 142.249 161.104 1.00 49.10  ? 741  ILE   A CG1   1 
ATOM   3533  C  CG2   . ILE   A 1 741  ? 139.289 142.563 158.924 1.00 46.72  ? 741  ILE   A CG2   1 
ATOM   3534  C  CD1   . ILE   A 1 741  ? 139.151 141.689 161.557 1.00 47.73  ? 741  ILE   A CD1   1 
ATOM   3535  N  N     . VAL   A 1 742  ? 141.643 145.167 157.808 1.00 47.13  ? 742  VAL   A N     1 
ATOM   3536  C  CA    . VAL   A 1 742  ? 141.542 145.950 156.581 1.00 45.51  ? 742  VAL   A CA    1 
ATOM   3537  C  C     . VAL   A 1 742  ? 142.745 145.694 155.686 1.00 46.25  ? 742  VAL   A C     1 
ATOM   3538  O  O     . VAL   A 1 742  ? 142.605 145.515 154.470 1.00 48.06  ? 742  VAL   A O     1 
ATOM   3539  C  CB    . VAL   A 1 742  ? 141.388 147.447 156.909 1.00 42.75  ? 742  VAL   A CB    1 
ATOM   3540  C  CG1   . VAL   A 1 742  ? 141.333 148.264 155.631 1.00 44.69  ? 742  VAL   A CG1   1 
ATOM   3541  C  CG2   . VAL   A 1 742  ? 140.141 147.681 157.744 1.00 48.44  ? 742  VAL   A CG2   1 
ATOM   3542  N  N     . LEU   A 1 743  ? 143.947 145.675 156.267 1.00 49.25  ? 743  LEU   A N     1 
ATOM   3543  C  CA    . LEU   A 1 743  ? 145.145 145.431 155.472 1.00 48.85  ? 743  LEU   A CA    1 
ATOM   3544  C  C     . LEU   A 1 743  ? 145.118 144.043 154.846 1.00 48.99  ? 743  LEU   A C     1 
ATOM   3545  O  O     . LEU   A 1 743  ? 145.481 143.874 153.676 1.00 57.91  ? 743  LEU   A O     1 
ATOM   3546  C  CB    . LEU   A 1 743  ? 146.392 145.608 156.336 1.00 50.38  ? 743  LEU   A CB    1 
ATOM   3547  C  CG    . LEU   A 1 743  ? 147.725 145.255 155.678 1.00 50.04  ? 743  LEU   A CG    1 
ATOM   3548  C  CD1   . LEU   A 1 743  ? 148.440 146.510 155.205 1.00 49.17  ? 743  LEU   A CD1   1 
ATOM   3549  C  CD2   . LEU   A 1 743  ? 148.601 144.461 156.636 1.00 53.08  ? 743  LEU   A CD2   1 
ATOM   3550  N  N     . GLY   A 1 744  ? 144.690 143.035 155.607 1.00 44.26  ? 744  GLY   A N     1 
ATOM   3551  C  CA    . GLY   A 1 744  ? 144.614 141.692 155.057 1.00 47.77  ? 744  GLY   A CA    1 
ATOM   3552  C  C     . GLY   A 1 744  ? 143.629 141.595 153.910 1.00 49.73  ? 744  GLY   A C     1 
ATOM   3553  O  O     . GLY   A 1 744  ? 143.921 140.998 152.870 1.00 58.36  ? 744  GLY   A O     1 
ATOM   3554  N  N     . LEU   A 1 745  ? 142.441 142.179 154.084 1.00 48.88  ? 745  LEU   A N     1 
ATOM   3555  C  CA    . LEU   A 1 745  ? 141.455 142.157 153.009 1.00 44.98  ? 745  LEU   A CA    1 
ATOM   3556  C  C     . LEU   A 1 745  ? 141.971 142.891 151.779 1.00 52.19  ? 745  LEU   A C     1 
ATOM   3557  O  O     . LEU   A 1 745  ? 141.784 142.430 150.646 1.00 57.16  ? 745  LEU   A O     1 
ATOM   3558  C  CB    . LEU   A 1 745  ? 140.139 142.767 153.486 1.00 47.05  ? 745  LEU   A CB    1 
ATOM   3559  C  CG    . LEU   A 1 745  ? 139.274 141.885 154.386 1.00 52.02  ? 745  LEU   A CG    1 
ATOM   3560  C  CD1   . LEU   A 1 745  ? 138.218 142.715 155.094 1.00 52.66  ? 745  LEU   A CD1   1 
ATOM   3561  C  CD2   . LEU   A 1 745  ? 138.632 140.772 153.579 1.00 53.46  ? 745  LEU   A CD2   1 
ATOM   3562  N  N     . TYR   A 1 746  ? 142.622 144.038 151.982 1.00 46.62  ? 746  TYR   A N     1 
ATOM   3563  C  CA    . TYR   A 1 746  ? 143.156 144.799 150.859 1.00 47.78  ? 746  TYR   A CA    1 
ATOM   3564  C  C     . TYR   A 1 746  ? 144.216 144.000 150.113 1.00 50.85  ? 746  TYR   A C     1 
ATOM   3565  O  O     . TYR   A 1 746  ? 144.231 143.976 148.877 1.00 55.54  ? 746  TYR   A O     1 
ATOM   3566  C  CB    . TYR   A 1 746  ? 143.714 146.130 151.367 1.00 46.73  ? 746  TYR   A CB    1 
ATOM   3567  C  CG    . TYR   A 1 746  ? 144.428 146.983 150.340 1.00 46.39  ? 746  TYR   A CG    1 
ATOM   3568  C  CD1   . TYR   A 1 746  ? 145.710 146.669 149.908 1.00 47.04  ? 746  TYR   A CD1   1 
ATOM   3569  C  CD2   . TYR   A 1 746  ? 143.820 148.114 149.814 1.00 49.61  ? 746  TYR   A CD2   1 
ATOM   3570  C  CE1   . TYR   A 1 746  ? 146.360 147.454 148.975 1.00 52.84  ? 746  TYR   A CE1   1 
ATOM   3571  C  CE2   . TYR   A 1 746  ? 144.462 148.903 148.882 1.00 48.92  ? 746  TYR   A CE2   1 
ATOM   3572  C  CZ    . TYR   A 1 746  ? 145.731 148.569 148.467 1.00 54.38  ? 746  TYR   A CZ    1 
ATOM   3573  O  OH    . TYR   A 1 746  ? 146.372 149.356 147.538 1.00 55.44  ? 746  TYR   A OH    1 
ATOM   3574  N  N     . ILE   A 1 747  ? 145.108 143.331 150.847 1.00 48.62  ? 747  ILE   A N     1 
ATOM   3575  C  CA    . ILE   A 1 747  ? 146.143 142.521 150.208 1.00 47.85  ? 747  ILE   A CA    1 
ATOM   3576  C  C     . ILE   A 1 747  ? 145.518 141.365 149.438 1.00 48.27  ? 747  ILE   A C     1 
ATOM   3577  O  O     . ILE   A 1 747  ? 145.929 141.055 148.312 1.00 51.58  ? 747  ILE   A O     1 
ATOM   3578  C  CB    . ILE   A 1 747  ? 147.156 142.021 151.254 1.00 52.05  ? 747  ILE   A CB    1 
ATOM   3579  C  CG1   . ILE   A 1 747  ? 147.771 143.200 152.009 1.00 55.15  ? 747  ILE   A CG1   1 
ATOM   3580  C  CG2   . ILE   A 1 747  ? 148.240 141.184 150.590 1.00 51.81  ? 747  ILE   A CG2   1 
ATOM   3581  C  CD1   . ILE   A 1 747  ? 148.310 144.286 151.109 1.00 53.22  ? 747  ILE   A CD1   1 
ATOM   3582  N  N     . TYR   A 1 748  ? 144.526 140.700 150.034 1.00 47.37  ? 748  TYR   A N     1 
ATOM   3583  C  CA    . TYR   A 1 748  ? 143.883 139.583 149.350 1.00 50.01  ? 748  TYR   A CA    1 
ATOM   3584  C  C     . TYR   A 1 748  ? 143.204 140.047 148.068 1.00 58.03  ? 748  TYR   A C     1 
ATOM   3585  O  O     . TYR   A 1 748  ? 143.293 139.377 147.033 1.00 61.07  ? 748  TYR   A O     1 
ATOM   3586  C  CB    . TYR   A 1 748  ? 142.887 138.895 150.289 1.00 50.51  ? 748  TYR   A CB    1 
ATOM   3587  C  CG    . TYR   A 1 748  ? 141.919 137.935 149.620 1.00 52.15  ? 748  TYR   A CG    1 
ATOM   3588  C  CD1   . TYR   A 1 748  ? 140.849 138.397 148.860 1.00 54.72  ? 748  TYR   A CD1   1 
ATOM   3589  C  CD2   . TYR   A 1 748  ? 142.086 136.562 149.740 1.00 56.84  ? 748  TYR   A CD2   1 
ATOM   3590  C  CE1   . TYR   A 1 748  ? 139.973 137.520 148.251 1.00 60.64  ? 748  TYR   A CE1   1 
ATOM   3591  C  CE2   . TYR   A 1 748  ? 141.215 135.679 149.134 1.00 61.67  ? 748  TYR   A CE2   1 
ATOM   3592  C  CZ    . TYR   A 1 748  ? 140.161 136.163 148.391 1.00 64.38  ? 748  TYR   A CZ    1 
ATOM   3593  O  OH    . TYR   A 1 748  ? 139.292 135.284 147.786 1.00 64.11  ? 748  TYR   A OH    1 
ATOM   3594  N  N     . VAL   A 1 749  ? 142.519 141.190 148.117 1.00 61.41  ? 749  VAL   A N     1 
ATOM   3595  C  CA    . VAL   A 1 749  ? 141.850 141.697 146.923 1.00 55.68  ? 749  VAL   A CA    1 
ATOM   3596  C  C     . VAL   A 1 749  ? 142.872 142.091 145.864 1.00 56.42  ? 749  VAL   A C     1 
ATOM   3597  O  O     . VAL   A 1 749  ? 142.670 141.850 144.668 1.00 59.87  ? 749  VAL   A O     1 
ATOM   3598  C  CB    . VAL   A 1 749  ? 140.924 142.873 147.282 1.00 56.27  ? 749  VAL   A CB    1 
ATOM   3599  C  CG1   . VAL   A 1 749  ? 140.721 143.768 146.074 1.00 55.28  ? 749  VAL   A CG1   1 
ATOM   3600  C  CG2   . VAL   A 1 749  ? 139.589 142.359 147.798 1.00 54.86  ? 749  VAL   A CG2   1 
ATOM   3601  N  N     . THR   A 1 750  ? 143.981 142.709 146.280 1.00 56.59  ? 750  THR   A N     1 
ATOM   3602  C  CA    . THR   A 1 750  ? 145.019 143.078 145.324 1.00 56.46  ? 750  THR   A CA    1 
ATOM   3603  C  C     . THR   A 1 750  ? 145.596 141.848 144.639 1.00 57.48  ? 750  THR   A C     1 
ATOM   3604  O  O     . THR   A 1 750  ? 145.817 141.851 143.422 1.00 61.87  ? 750  THR   A O     1 
ATOM   3605  C  CB    . THR   A 1 750  ? 146.125 143.866 146.026 1.00 54.94  ? 750  THR   A CB    1 
ATOM   3606  O  OG1   . THR   A 1 750  ? 145.555 144.993 146.703 1.00 58.54  ? 750  THR   A OG1   1 
ATOM   3607  C  CG2   . THR   A 1 750  ? 147.150 144.356 145.018 1.00 53.77  ? 750  THR   A CG2   1 
ATOM   3608  N  N     . TYR   A 1 751  ? 145.847 140.783 145.403 1.00 61.40  ? 751  TYR   A N     1 
ATOM   3609  C  CA    . TYR   A 1 751  ? 146.380 139.565 144.801 1.00 59.97  ? 751  TYR   A CA    1 
ATOM   3610  C  C     . TYR   A 1 751  ? 145.348 138.873 143.921 1.00 61.10  ? 751  TYR   A C     1 
ATOM   3611  O  O     . TYR   A 1 751  ? 145.713 138.241 142.924 1.00 70.10  ? 751  TYR   A O     1 
ATOM   3612  C  CB    . TYR   A 1 751  ? 146.882 138.613 145.884 1.00 63.07  ? 751  TYR   A CB    1 
ATOM   3613  C  CG    . TYR   A 1 751  ? 148.351 138.779 146.201 1.00 69.79  ? 751  TYR   A CG    1 
ATOM   3614  C  CD1   . TYR   A 1 751  ? 149.223 139.328 145.270 1.00 65.57  ? 751  TYR   A CD1   1 
ATOM   3615  C  CD2   . TYR   A 1 751  ? 148.868 138.381 147.426 1.00 67.37  ? 751  TYR   A CD2   1 
ATOM   3616  C  CE1   . TYR   A 1 751  ? 150.566 139.481 145.551 1.00 64.60  ? 751  TYR   A CE1   1 
ATOM   3617  C  CE2   . TYR   A 1 751  ? 150.211 138.530 147.717 1.00 67.35  ? 751  TYR   A CE2   1 
ATOM   3618  C  CZ    . TYR   A 1 751  ? 151.055 139.080 146.776 1.00 69.86  ? 751  TYR   A CZ    1 
ATOM   3619  O  OH    . TYR   A 1 751  ? 152.393 139.229 147.063 1.00 71.80  ? 751  TYR   A OH    1 
ATOM   3620  N  N     . LYS   A 1 752  ? 144.063 138.975 144.268 1.00 55.49  ? 752  LYS   A N     1 
ATOM   3621  C  CA    . LYS   A 1 752  ? 143.029 138.367 143.439 1.00 61.17  ? 752  LYS   A CA    1 
ATOM   3622  C  C     . LYS   A 1 752  ? 142.929 139.045 142.079 1.00 66.44  ? 752  LYS   A C     1 
ATOM   3623  O  O     . LYS   A 1 752  ? 142.653 138.377 141.076 1.00 70.92  ? 752  LYS   A O     1 
ATOM   3624  C  CB    . LYS   A 1 752  ? 141.682 138.413 144.159 1.00 66.37  ? 752  LYS   A CB    1 
ATOM   3625  C  CG    . LYS   A 1 752  ? 140.691 137.353 143.702 1.00 66.38  ? 752  LYS   A CG    1 
ATOM   3626  C  CD    . LYS   A 1 752  ? 141.200 135.945 143.975 1.00 67.81  ? 752  LYS   A CD    1 
ATOM   3627  C  CE    . LYS   A 1 752  ? 142.137 135.907 145.170 1.00 66.83  ? 752  LYS   A CE    1 
ATOM   3628  N  NZ    . LYS   A 1 752  ? 142.880 134.619 145.249 1.00 65.14  ? 752  LYS   A NZ    1 
ATOM   3629  N  N     . LYS   A 1 753  ? 143.154 140.356 142.023 1.00 69.99  ? 753  LYS   A N     1 
ATOM   3630  C  CA    . LYS   A 1 753  ? 143.088 141.102 140.773 1.00 66.31  ? 753  LYS   A CA    1 
ATOM   3631  C  C     . LYS   A 1 753  ? 141.755 140.850 140.081 1.00 69.00  ? 753  LYS   A C     1 
ATOM   3632  O  O     . LYS   A 1 753  ? 141.706 140.158 139.056 1.00 69.14  ? 753  LYS   A O     1 
ATOM   3633  C  CB    . LYS   A 1 753  ? 144.250 140.717 139.856 1.00 65.54  ? 753  LYS   A CB    1 
ATOM   3634  C  CG    . LYS   A 1 753  ? 145.625 140.937 140.473 1.00 67.82  ? 753  LYS   A CG    1 
ATOM   3635  C  CD    . LYS   A 1 753  ? 146.738 140.783 139.444 1.00 70.66  ? 753  LYS   A CD    1 
ATOM   3636  C  CE    . LYS   A 1 753  ? 146.543 141.698 138.241 1.00 71.17  ? 753  LYS   A CE    1 
ATOM   3637  N  NZ    . LYS   A 1 753  ? 145.686 142.881 138.536 1.00 71.47  ? 753  LYS   A NZ    1 
ATOM   3638  N  N     . PRO   A 1 754  ? 140.657 141.391 140.602 1.00 61.78  ? 754  PRO   A N     1 
ATOM   3639  C  CA    . PRO   A 1 754  ? 139.351 141.116 140.002 1.00 60.03  ? 754  PRO   A CA    1 
ATOM   3640  C  C     . PRO   A 1 754  ? 139.193 141.810 138.660 1.00 59.63  ? 754  PRO   A C     1 
ATOM   3641  O  O     . PRO   A 1 754  ? 139.801 142.849 138.390 1.00 60.13  ? 754  PRO   A O     1 
ATOM   3642  C  CB    . PRO   A 1 754  ? 138.358 141.661 141.039 1.00 58.63  ? 754  PRO   A CB    1 
ATOM   3643  C  CG    . PRO   A 1 754  ? 139.194 142.438 142.055 1.00 55.23  ? 754  PRO   A CG    1 
ATOM   3644  C  CD    . PRO   A 1 754  ? 140.593 142.525 141.534 1.00 55.94  ? 754  PRO   A CD    1 
ATOM   3645  N  N     . ASP   A 1 755  ? 138.358 141.215 137.811 1.00 57.73  ? 755  ASP   A N     1 
ATOM   3646  C  CA    . ASP   A 1 755  ? 138.126 141.719 136.458 1.00 57.86  ? 755  ASP   A CA    1 
ATOM   3647  C  C     . ASP   A 1 755  ? 137.091 142.833 136.528 1.00 60.52  ? 755  ASP   A C     1 
ATOM   3648  O  O     . ASP   A 1 755  ? 135.889 142.612 136.369 1.00 66.37  ? 755  ASP   A O     1 
ATOM   3649  C  CB    . ASP   A 1 755  ? 137.675 140.593 135.535 1.00 54.61  ? 755  ASP   A CB    1 
ATOM   3650  N  N     . VAL   A 1 756  ? 137.567 144.054 136.771 1.00 50.54  ? 756  VAL   A N     1 
ATOM   3651  C  CA    . VAL   A 1 756  ? 136.696 145.220 136.841 1.00 49.74  ? 756  VAL   A CA    1 
ATOM   3652  C  C     . VAL   A 1 756  ? 137.546 146.456 136.600 1.00 45.49  ? 756  VAL   A C     1 
ATOM   3653  O  O     . VAL   A 1 756  ? 138.752 146.457 136.855 1.00 52.14  ? 756  VAL   A O     1 
ATOM   3654  C  CB    . VAL   A 1 756  ? 135.953 145.286 138.199 1.00 42.49  ? 756  VAL   A CB    1 
ATOM   3655  C  CG1   . VAL   A 1 756  ? 136.822 145.958 139.250 1.00 42.74  ? 756  VAL   A CG1   1 
ATOM   3656  C  CG2   . VAL   A 1 756  ? 134.629 146.013 138.042 1.00 47.51  ? 756  VAL   A CG2   1 
ATOM   3657  N  N     . ASN   A 1 757  ? 136.909 147.515 136.104 1.00 30.55  ? 757  ASN   A N     1 
ATOM   3658  C  CA    . ASN   A 1 757  ? 137.601 148.769 135.813 1.00 34.94  ? 757  ASN   A CA    1 
ATOM   3659  C  C     . ASN   A 1 757  ? 136.579 149.891 135.916 1.00 34.35  ? 757  ASN   A C     1 
ATOM   3660  O  O     . ASN   A 1 757  ? 135.664 149.974 135.093 1.00 36.96  ? 757  ASN   A O     1 
ATOM   3661  C  CB    . ASN   A 1 757  ? 138.249 148.731 134.431 1.00 31.23  ? 757  ASN   A CB    1 
ATOM   3662  C  CG    . ASN   A 1 757  ? 138.582 150.112 133.904 1.00 37.75  ? 757  ASN   A CG    1 
ATOM   3663  O  OD1   . ASN   A 1 757  ? 138.948 151.009 134.662 1.00 46.50  ? 757  ASN   A OD1   1 
ATOM   3664  N  ND2   . ASN   A 1 757  ? 138.466 150.286 132.593 1.00 34.09  ? 757  ASN   A ND2   1 
ATOM   3665  N  N     . TRP   A 1 758  ? 136.734 150.751 136.924 1.00 29.13  ? 758  TRP   A N     1 
ATOM   3666  C  CA    . TRP   A 1 758  ? 135.751 151.782 137.218 1.00 32.30  ? 758  TRP   A CA    1 
ATOM   3667  C  C     . TRP   A 1 758  ? 136.260 153.202 137.028 1.00 40.35  ? 758  TRP   A C     1 
ATOM   3668  O  O     . TRP   A 1 758  ? 135.443 154.128 136.989 1.00 50.88  ? 758  TRP   A O     1 
ATOM   3669  C  CB    . TRP   A 1 758  ? 135.241 151.635 138.660 1.00 33.52  ? 758  TRP   A CB    1 
ATOM   3670  C  CG    . TRP   A 1 758  ? 134.453 150.388 138.897 1.00 37.55  ? 758  TRP   A CG    1 
ATOM   3671  C  CD1   . TRP   A 1 758  ? 133.546 149.820 138.053 1.00 37.24  ? 758  TRP   A CD1   1 
ATOM   3672  C  CD2   . TRP   A 1 758  ? 134.507 149.546 140.053 1.00 35.94  ? 758  TRP   A CD2   1 
ATOM   3673  N  NE1   . TRP   A 1 758  ? 133.028 148.679 138.613 1.00 39.51  ? 758  TRP   A NE1   1 
ATOM   3674  C  CE2   . TRP   A 1 758  ? 133.602 148.489 139.842 1.00 34.72  ? 758  TRP   A CE2   1 
ATOM   3675  C  CE3   . TRP   A 1 758  ? 135.232 149.584 141.248 1.00 34.12  ? 758  TRP   A CE3   1 
ATOM   3676  C  CZ2   . TRP   A 1 758  ? 133.402 147.479 140.779 1.00 31.70  ? 758  TRP   A CZ2   1 
ATOM   3677  C  CZ3   . TRP   A 1 758  ? 135.031 148.582 142.177 1.00 30.02  ? 758  TRP   A CZ3   1 
ATOM   3678  C  CH2   . TRP   A 1 758  ? 134.125 147.543 141.937 1.00 32.93  ? 758  TRP   A CH2   1 
ATOM   3679  N  N     . GLY   A 1 759  ? 137.568 153.405 136.915 1.00 31.25  ? 759  GLY   A N     1 
ATOM   3680  C  CA    . GLY   A 1 759  ? 138.099 154.745 136.776 1.00 25.42  ? 759  GLY   A CA    1 
ATOM   3681  C  C     . GLY   A 1 759  ? 138.489 155.342 138.110 1.00 36.77  ? 759  GLY   A C     1 
ATOM   3682  O  O     . GLY   A 1 759  ? 138.278 156.533 138.354 1.00 41.32  ? 759  GLY   A O     1 
ATOM   3683  N  N     . SER   A 1 760  ? 139.060 154.517 138.982 1.00 38.57  ? 760  SER   A N     1 
ATOM   3684  C  CA    . SER   A 1 760  ? 139.430 154.959 140.315 1.00 23.49  ? 760  SER   A CA    1 
ATOM   3685  C  C     . SER   A 1 760  ? 140.543 156.000 140.252 1.00 28.24  ? 760  SER   A C     1 
ATOM   3686  O  O     . SER   A 1 760  ? 141.256 156.131 139.254 1.00 40.51  ? 760  SER   A O     1 
ATOM   3687  C  CB    . SER   A 1 760  ? 139.878 153.772 141.166 1.00 37.35  ? 760  SER   A CB    1 
ATOM   3688  O  OG    . SER   A 1 760  ? 141.280 153.586 141.081 1.00 43.92  ? 760  SER   A OG    1 
ATOM   3689  N  N     . SER   A 1 761  ? 140.683 156.754 141.345 1.00 31.26  ? 761  SER   A N     1 
ATOM   3690  C  CA    . SER   A 1 761  ? 141.767 157.723 141.438 1.00 33.81  ? 761  SER   A CA    1 
ATOM   3691  C  C     . SER   A 1 761  ? 143.133 157.053 141.488 1.00 36.75  ? 761  SER   A C     1 
ATOM   3692  O  O     . SER   A 1 761  ? 144.146 157.724 141.272 1.00 43.92  ? 761  SER   A O     1 
ATOM   3693  C  CB    . SER   A 1 761  ? 141.579 158.613 142.667 1.00 29.91  ? 761  SER   A CB    1 
ATOM   3694  O  OG    . SER   A 1 761  ? 141.519 157.838 143.852 1.00 32.90  ? 761  SER   A OG    1 
ATOM   3695  N  N     . THR   A 1 762  ? 143.183 155.748 141.769 1.00 34.55  ? 762  THR   A N     1 
ATOM   3696  C  CA    . THR   A 1 762  ? 144.457 155.037 141.766 1.00 33.99  ? 762  THR   A CA    1 
ATOM   3697  C  C     . THR   A 1 762  ? 145.091 155.042 140.380 1.00 38.41  ? 762  THR   A C     1 
ATOM   3698  O  O     . THR   A 1 762  ? 146.295 155.278 140.241 1.00 40.86  ? 762  THR   A O     1 
ATOM   3699  C  CB    . THR   A 1 762  ? 144.257 153.600 142.250 1.00 35.52  ? 762  THR   A CB    1 
ATOM   3700  O  OG1   . THR   A 1 762  ? 143.546 153.606 143.494 1.00 35.69  ? 762  THR   A OG1   1 
ATOM   3701  C  CG2   . THR   A 1 762  ? 145.598 152.910 142.443 1.00 38.40  ? 762  THR   A CG2   1 
ATOM   3702  N  N     . GLN   A 1 763  ? 144.295 154.778 139.342 1.00 25.52  ? 763  GLN   A N     1 
ATOM   3703  C  CA    . GLN   A 1 763  ? 144.825 154.773 137.983 1.00 25.81  ? 763  GLN   A CA    1 
ATOM   3704  C  C     . GLN   A 1 763  ? 145.272 156.168 137.557 1.00 28.96  ? 763  GLN   A C     1 
ATOM   3705  O  O     . GLN   A 1 763  ? 146.341 156.333 136.948 1.00 40.73  ? 763  GLN   A O     1 
ATOM   3706  C  CB    . GLN   A 1 763  ? 143.769 154.224 137.026 1.00 31.02  ? 763  GLN   A CB    1 
ATOM   3707  C  CG    . GLN   A 1 763  ? 143.310 152.813 137.362 1.00 28.33  ? 763  GLN   A CG    1 
ATOM   3708  C  CD    . GLN   A 1 763  ? 141.892 152.539 136.904 1.00 35.41  ? 763  GLN   A CD    1 
ATOM   3709  O  OE1   . GLN   A 1 763  ? 141.527 152.835 135.767 1.00 39.02  ? 763  GLN   A OE1   1 
ATOM   3710  N  NE2   . GLN   A 1 763  ? 141.083 151.972 137.790 1.00 35.90  ? 763  GLN   A NE2   1 
ATOM   3711  N  N     . ALA   A 1 764  ? 144.466 157.184 137.870 1.00 12.60  ? 764  ALA   A N     1 
ATOM   3712  C  CA    . ALA   A 1 764  ? 144.853 158.556 137.565 1.00 22.22  ? 764  ALA   A CA    1 
ATOM   3713  C  C     . ALA   A 1 764  ? 146.149 158.926 138.270 1.00 30.43  ? 764  ALA   A C     1 
ATOM   3714  O  O     . ALA   A 1 764  ? 147.014 159.593 137.691 1.00 45.84  ? 764  ALA   A O     1 
ATOM   3715  C  CB    . ALA   A 1 764  ? 143.731 159.515 137.959 1.00 17.98  ? 764  ALA   A CB    1 
ATOM   3716  N  N     . LEU   A 1 765  ? 146.304 158.496 139.523 1.00 24.79  ? 765  LEU   A N     1 
ATOM   3717  C  CA    . LEU   A 1 765  ? 147.523 158.795 140.263 1.00 25.82  ? 765  LEU   A CA    1 
ATOM   3718  C  C     . LEU   A 1 765  ? 148.714 158.043 139.688 1.00 28.37  ? 765  LEU   A C     1 
ATOM   3719  O  O     . LEU   A 1 765  ? 149.833 158.560 139.683 1.00 30.94  ? 765  LEU   A O     1 
ATOM   3720  C  CB    . LEU   A 1 765  ? 147.337 158.457 141.742 1.00 28.34  ? 765  LEU   A CB    1 
ATOM   3721  C  CG    . LEU   A 1 765  ? 148.563 158.639 142.636 1.00 29.06  ? 765  LEU   A CG    1 
ATOM   3722  C  CD1   . LEU   A 1 765  ? 148.534 159.994 143.325 1.00 30.21  ? 765  LEU   A CD1   1 
ATOM   3723  C  CD2   . LEU   A 1 765  ? 148.649 157.515 143.651 1.00 32.95  ? 765  LEU   A CD2   1 
ATOM   3724  N  N     . THR   A 1 766  ? 148.498 156.818 139.209 1.00 24.30  ? 766  THR   A N     1 
ATOM   3725  C  CA    . THR   A 1 766  ? 149.566 156.093 138.527 1.00 24.48  ? 766  THR   A CA    1 
ATOM   3726  C  C     . THR   A 1 766  ? 150.047 156.871 137.309 1.00 21.52  ? 766  THR   A C     1 
ATOM   3727  O  O     . THR   A 1 766  ? 151.256 157.059 137.105 1.00 31.61  ? 766  THR   A O     1 
ATOM   3728  C  CB    . THR   A 1 766  ? 149.074 154.703 138.120 1.00 11.43  ? 766  THR   A CB    1 
ATOM   3729  O  OG1   . THR   A 1 766  ? 148.643 153.986 139.283 1.00 32.17  ? 766  THR   A OG1   1 
ATOM   3730  C  CG2   . THR   A 1 766  ? 150.180 153.919 137.433 1.00 21.78  ? 766  THR   A CG2   1 
ATOM   3731  N  N     . TYR   A 1 767  ? 149.104 157.350 136.495 1.00 20.78  ? 767  TYR   A N     1 
ATOM   3732  C  CA    . TYR   A 1 767  ? 149.479 158.138 135.325 1.00 14.99  ? 767  TYR   A CA    1 
ATOM   3733  C  C     . TYR   A 1 767  ? 150.223 159.401 135.738 1.00 19.06  ? 767  TYR   A C     1 
ATOM   3734  O  O     . TYR   A 1 767  ? 151.240 159.763 135.134 1.00 30.11  ? 767  TYR   A O     1 
ATOM   3735  C  CB    . TYR   A 1 767  ? 148.243 158.491 134.494 1.00 15.07  ? 767  TYR   A CB    1 
ATOM   3736  C  CG    . TYR   A 1 767  ? 148.541 159.434 133.343 1.00 19.05  ? 767  TYR   A CG    1 
ATOM   3737  C  CD1   . TYR   A 1 767  ? 148.666 160.803 133.548 1.00 18.64  ? 767  TYR   A CD1   1 
ATOM   3738  C  CD2   . TYR   A 1 767  ? 148.718 158.949 132.054 1.00 21.65  ? 767  TYR   A CD2   1 
ATOM   3739  C  CE1   . TYR   A 1 767  ? 148.951 161.659 132.505 1.00 11.43  ? 767  TYR   A CE1   1 
ATOM   3740  C  CE2   . TYR   A 1 767  ? 149.001 159.800 131.004 1.00 16.56  ? 767  TYR   A CE2   1 
ATOM   3741  C  CZ    . TYR   A 1 767  ? 149.115 161.153 131.235 1.00 17.96  ? 767  TYR   A CZ    1 
ATOM   3742  O  OH    . TYR   A 1 767  ? 149.396 162.006 130.196 1.00 31.93  ? 767  TYR   A OH    1 
ATOM   3743  N  N     . LEU   A 1 768  ? 149.714 160.103 136.752 1.00 10.37  ? 768  LEU   A N     1 
ATOM   3744  C  CA    . LEU   A 1 768  ? 150.338 161.355 137.164 1.00 20.63  ? 768  LEU   A CA    1 
ATOM   3745  C  C     . LEU   A 1 768  ? 151.738 161.119 137.716 1.00 28.57  ? 768  LEU   A C     1 
ATOM   3746  O  O     . LEU   A 1 768  ? 152.648 161.921 137.482 1.00 29.72  ? 768  LEU   A O     1 
ATOM   3747  C  CB    . LEU   A 1 768  ? 149.464 162.065 138.196 1.00 20.34  ? 768  LEU   A CB    1 
ATOM   3748  C  CG    . LEU   A 1 768  ? 149.822 163.531 138.445 1.00 27.37  ? 768  LEU   A CG    1 
ATOM   3749  C  CD1   . LEU   A 1 768  ? 149.418 164.385 137.254 1.00 26.04  ? 768  LEU   A CD1   1 
ATOM   3750  C  CD2   . LEU   A 1 768  ? 149.168 164.037 139.715 1.00 28.47  ? 768  LEU   A CD2   1 
ATOM   3751  N  N     . ASN   A 1 769  ? 151.928 160.030 138.461 1.00 25.69  ? 769  ASN   A N     1 
ATOM   3752  C  CA    . ASN   A 1 769  ? 153.252 159.692 138.968 1.00 21.34  ? 769  ASN   A CA    1 
ATOM   3753  C  C     . ASN   A 1 769  ? 154.216 159.421 137.824 1.00 31.76  ? 769  ASN   A C     1 
ATOM   3754  O  O     . ASN   A 1 769  ? 155.355 159.904 137.826 1.00 30.12  ? 769  ASN   A O     1 
ATOM   3755  C  CB    . ASN   A 1 769  ? 153.166 158.479 139.894 1.00 24.94  ? 769  ASN   A CB    1 
ATOM   3756  C  CG    . ASN   A 1 769  ? 152.747 158.847 141.300 1.00 36.49  ? 769  ASN   A CG    1 
ATOM   3757  O  OD1   . ASN   A 1 769  ? 153.165 159.872 141.836 1.00 42.66  ? 769  ASN   A OD1   1 
ATOM   3758  N  ND2   . ASN   A 1 769  ? 151.921 158.006 141.911 1.00 35.45  ? 769  ASN   A ND2   1 
ATOM   3759  N  N     . ALA   A 1 770  ? 153.777 158.638 136.835 1.00 26.68  ? 770  ALA   A N     1 
ATOM   3760  C  CA    . ALA   A 1 770  ? 154.638 158.380 135.686 1.00 18.37  ? 770  ALA   A CA    1 
ATOM   3761  C  C     . ALA   A 1 770  ? 154.994 159.677 134.971 1.00 19.87  ? 770  ALA   A C     1 
ATOM   3762  O  O     . ALA   A 1 770  ? 156.151 159.890 134.590 1.00 16.14  ? 770  ALA   A O     1 
ATOM   3763  C  CB    . ALA   A 1 770  ? 153.962 157.401 134.728 1.00 17.17  ? 770  ALA   A CB    1 
ATOM   3764  N  N     . LEU   A 1 771  ? 154.012 160.562 134.793 1.00 21.04  ? 771  LEU   A N     1 
ATOM   3765  C  CA    . LEU   A 1 771  ? 154.264 161.834 134.122 1.00 16.59  ? 771  LEU   A CA    1 
ATOM   3766  C  C     . LEU   A 1 771  ? 155.270 162.675 134.898 1.00 20.25  ? 771  LEU   A C     1 
ATOM   3767  O  O     . LEU   A 1 771  ? 156.202 163.244 134.318 1.00 26.80  ? 771  LEU   A O     1 
ATOM   3768  C  CB    . LEU   A 1 771  ? 152.951 162.595 133.940 1.00 21.81  ? 771  LEU   A CB    1 
ATOM   3769  C  CG    . LEU   A 1 771  ? 153.030 163.960 133.255 1.00 23.44  ? 771  LEU   A CG    1 
ATOM   3770  C  CD1   . LEU   A 1 771  ? 153.716 163.849 131.905 1.00 17.75  ? 771  LEU   A CD1   1 
ATOM   3771  C  CD2   . LEU   A 1 771  ? 151.644 164.561 133.104 1.00 30.86  ? 771  LEU   A CD2   1 
ATOM   3772  N  N     . GLN   A 1 772  ? 155.091 162.771 136.217 1.00 19.46  ? 772  GLN   A N     1 
ATOM   3773  C  CA    . GLN   A 1 772  ? 155.994 163.576 137.031 1.00 22.52  ? 772  GLN   A CA    1 
ATOM   3774  C  C     . GLN   A 1 772  ? 157.410 163.022 136.993 1.00 27.39  ? 772  GLN   A C     1 
ATOM   3775  O  O     . GLN   A 1 772  ? 158.380 163.778 136.870 1.00 30.15  ? 772  GLN   A O     1 
ATOM   3776  C  CB    . GLN   A 1 772  ? 155.483 163.643 138.471 1.00 33.31  ? 772  GLN   A CB    1 
ATOM   3777  C  CG    . GLN   A 1 772  ? 154.242 164.505 138.670 1.00 35.37  ? 772  GLN   A CG    1 
ATOM   3778  C  CD    . GLN   A 1 772  ? 154.254 165.769 137.831 1.00 47.10  ? 772  GLN   A CD    1 
ATOM   3779  O  OE1   . GLN   A 1 772  ? 155.312 166.264 137.442 1.00 41.39  ? 772  GLN   A OE1   1 
ATOM   3780  N  NE2   . GLN   A 1 772  ? 153.070 166.298 137.545 1.00 45.68  ? 772  GLN   A NE2   1 
ATOM   3781  N  N     . HIS   A 1 773  ? 157.551 161.700 137.096 1.00 29.63  ? 773  HIS   A N     1 
ATOM   3782  C  CA    . HIS   A 1 773  ? 158.882 161.104 137.074 1.00 17.10  ? 773  HIS   A CA    1 
ATOM   3783  C  C     . HIS   A 1 773  ? 159.545 161.276 135.713 1.00 28.46  ? 773  HIS   A C     1 
ATOM   3784  O  O     . HIS   A 1 773  ? 160.755 161.518 135.635 1.00 31.77  ? 773  HIS   A O     1 
ATOM   3785  C  CB    . HIS   A 1 773  ? 158.801 159.632 137.472 1.00 17.29  ? 773  HIS   A CB    1 
ATOM   3786  C  CG    . HIS   A 1 773  ? 158.663 159.422 138.948 1.00 28.91  ? 773  HIS   A CG    1 
ATOM   3787  N  ND1   . HIS   A 1 773  ? 157.486 159.658 139.626 1.00 39.79  ? 773  HIS   A ND1   1 
ATOM   3788  C  CD2   . HIS   A 1 773  ? 159.557 159.013 139.878 1.00 26.43  ? 773  HIS   A CD2   1 
ATOM   3789  C  CE1   . HIS   A 1 773  ? 157.660 159.398 140.909 1.00 29.64  ? 773  HIS   A CE1   1 
ATOM   3790  N  NE2   . HIS   A 1 773  ? 158.908 159.004 141.089 1.00 24.07  ? 773  HIS   A NE2   1 
ATOM   3791  N  N     . SER   A 1 774  ? 158.776 161.159 134.628 1.00 28.50  ? 774  SER   A N     1 
ATOM   3792  C  CA    . SER   A 1 774  ? 159.344 161.397 133.305 1.00 12.32  ? 774  SER   A CA    1 
ATOM   3793  C  C     . SER   A 1 774  ? 159.791 162.845 133.152 1.00 12.18  ? 774  SER   A C     1 
ATOM   3794  O  O     . SER   A 1 774  ? 160.861 163.119 132.594 1.00 30.79  ? 774  SER   A O     1 
ATOM   3795  C  CB    . SER   A 1 774  ? 158.329 161.030 132.223 1.00 20.95  ? 774  SER   A CB    1 
ATOM   3796  O  OG    . SER   A 1 774  ? 157.816 159.725 132.422 1.00 34.17  ? 774  SER   A OG    1 
ATOM   3797  N  N     . ILE   A 1 775  ? 158.986 163.789 133.643 1.00 20.18  ? 775  ILE   A N     1 
ATOM   3798  C  CA    . ILE   A 1 775  ? 159.359 165.196 133.544 1.00 17.13  ? 775  ILE   A CA    1 
ATOM   3799  C  C     . ILE   A 1 775  ? 160.610 165.473 134.365 1.00 27.52  ? 775  ILE   A C     1 
ATOM   3800  O  O     . ILE   A 1 775  ? 161.459 166.283 133.975 1.00 34.90  ? 775  ILE   A O     1 
ATOM   3801  C  CB    . ILE   A 1 775  ? 158.186 166.093 133.976 1.00 26.47  ? 775  ILE   A CB    1 
ATOM   3802  C  CG1   . ILE   A 1 775  ? 157.294 166.410 132.775 1.00 24.72  ? 775  ILE   A CG1   1 
ATOM   3803  C  CG2   . ILE   A 1 775  ? 158.705 167.374 134.604 1.00 22.67  ? 775  ILE   A CG2   1 
ATOM   3804  C  CD1   . ILE   A 1 775  ? 155.901 166.858 133.151 1.00 21.61  ? 775  ILE   A CD1   1 
ATOM   3805  N  N     . ARG   A 1 776  ? 160.742 164.814 135.517 1.00 37.64  ? 776  ARG   A N     1 
ATOM   3806  C  CA    . ARG   A 1 776  ? 161.967 164.932 136.302 1.00 27.43  ? 776  ARG   A CA    1 
ATOM   3807  C  C     . ARG   A 1 776  ? 163.161 164.390 135.526 1.00 30.57  ? 776  ARG   A C     1 
ATOM   3808  O  O     . ARG   A 1 776  ? 164.206 165.044 135.429 1.00 35.95  ? 776  ARG   A O     1 
ATOM   3809  C  CB    . ARG   A 1 776  ? 161.812 164.189 137.629 1.00 26.71  ? 776  ARG   A CB    1 
ATOM   3810  C  CG    . ARG   A 1 776  ? 161.941 165.062 138.865 1.00 35.24  ? 776  ARG   A CG    1 
ATOM   3811  C  CD    . ARG   A 1 776  ? 161.688 164.255 140.129 1.00 39.45  ? 776  ARG   A CD    1 
ATOM   3812  N  NE    . ARG   A 1 776  ? 160.311 164.372 140.592 1.00 50.87  ? 776  ARG   A NE    1 
ATOM   3813  C  CZ    . ARG   A 1 776  ? 159.474 163.350 140.708 1.00 47.77  ? 776  ARG   A CZ    1 
ATOM   3814  N  NH1   . ARG   A 1 776  ? 159.844 162.116 140.406 1.00 46.39  ? 776  ARG   A NH1   1 
ATOM   3815  N  NH2   . ARG   A 1 776  ? 158.235 163.571 141.137 1.00 38.86  ? 776  ARG   A NH2   1 
ATOM   3816  N  N     . LEU   A 1 777  ? 163.017 163.190 134.959 1.00 24.57  ? 777  LEU   A N     1 
ATOM   3817  C  CA    . LEU   A 1 777  ? 164.112 162.576 134.216 1.00 17.74  ? 777  LEU   A CA    1 
ATOM   3818  C  C     . LEU   A 1 777  ? 164.523 163.417 133.017 1.00 23.55  ? 777  LEU   A C     1 
ATOM   3819  O  O     . LEU   A 1 777  ? 165.691 163.392 132.613 1.00 29.76  ? 777  LEU   A O     1 
ATOM   3820  C  CB    . LEU   A 1 777  ? 163.713 161.172 133.763 1.00 20.44  ? 777  LEU   A CB    1 
ATOM   3821  C  CG    . LEU   A 1 777  ? 164.654 160.490 132.769 1.00 22.64  ? 777  LEU   A CG    1 
ATOM   3822  C  CD1   . LEU   A 1 777  ? 166.026 160.275 133.388 1.00 17.01  ? 777  LEU   A CD1   1 
ATOM   3823  C  CD2   . LEU   A 1 777  ? 164.067 159.175 132.289 1.00 21.34  ? 777  LEU   A CD2   1 
ATOM   3824  N  N     . SER   A 1 778  ? 163.586 164.165 132.435 1.00 34.42  ? 778  SER   A N     1 
ATOM   3825  C  CA    . SER   A 1 778  ? 163.905 164.963 131.257 1.00 28.99  ? 778  SER   A CA    1 
ATOM   3826  C  C     . SER   A 1 778  ? 164.907 166.073 131.547 1.00 30.54  ? 778  SER   A C     1 
ATOM   3827  O  O     . SER   A 1 778  ? 165.457 166.647 130.602 1.00 32.40  ? 778  SER   A O     1 
ATOM   3828  C  CB    . SER   A 1 778  ? 162.631 165.570 130.669 1.00 26.82  ? 778  SER   A CB    1 
ATOM   3829  O  OG    . SER   A 1 778  ? 162.371 166.845 131.229 1.00 37.96  ? 778  SER   A OG    1 
ATOM   3830  N  N     . GLY   A 1 779  ? 165.157 166.387 132.815 1.00 28.40  ? 779  GLY   A N     1 
ATOM   3831  C  CA    . GLY   A 1 779  ? 166.089 167.441 133.161 1.00 34.89  ? 779  GLY   A CA    1 
ATOM   3832  C  C     . GLY   A 1 779  ? 167.442 166.941 133.625 1.00 41.19  ? 779  GLY   A C     1 
ATOM   3833  O  O     . GLY   A 1 779  ? 168.222 167.701 134.206 1.00 41.20  ? 779  GLY   A O     1 
ATOM   3834  N  N     . VAL   A 1 780  ? 167.738 165.669 133.372 1.00 38.17  ? 780  VAL   A N     1 
ATOM   3835  C  CA    . VAL   A 1 780  ? 168.974 165.037 133.820 1.00 29.30  ? 780  VAL   A CA    1 
ATOM   3836  C  C     . VAL   A 1 780  ? 169.917 164.919 132.632 1.00 37.37  ? 780  VAL   A C     1 
ATOM   3837  O  O     . VAL   A 1 780  ? 169.560 164.336 131.602 1.00 45.95  ? 780  VAL   A O     1 
ATOM   3838  C  CB    . VAL   A 1 780  ? 168.712 163.661 134.448 1.00 30.44  ? 780  VAL   A CB    1 
ATOM   3839  C  CG1   . VAL   A 1 780  ? 169.970 163.141 135.114 1.00 34.34  ? 780  VAL   A CG1   1 
ATOM   3840  C  CG2   . VAL   A 1 780  ? 167.581 163.748 135.452 1.00 37.65  ? 780  VAL   A CG2   1 
ATOM   3841  N  N     . GLU   A 1 781  ? 171.121 165.466 132.779 1.00 42.90  ? 781  GLU   A N     1 
ATOM   3842  C  CA    . GLU   A 1 781  ? 172.134 165.336 131.742 1.00 41.39  ? 781  GLU   A CA    1 
ATOM   3843  C  C     . GLU   A 1 781  ? 172.680 163.914 131.710 1.00 38.16  ? 781  GLU   A C     1 
ATOM   3844  O  O     . GLU   A 1 781  ? 172.820 163.261 132.747 1.00 45.31  ? 781  GLU   A O     1 
ATOM   3845  C  CB    . GLU   A 1 781  ? 173.268 166.331 131.980 1.00 35.92  ? 781  GLU   A CB    1 
ATOM   3846  N  N     . ASP   A 1 782  ? 172.996 163.437 130.509 1.00 39.02  ? 782  ASP   A N     1 
ATOM   3847  C  CA    . ASP   A 1 782  ? 173.486 162.079 130.327 1.00 40.29  ? 782  ASP   A CA    1 
ATOM   3848  C  C     . ASP   A 1 782  ? 174.991 162.017 130.551 1.00 45.99  ? 782  ASP   A C     1 
ATOM   3849  O  O     . ASP   A 1 782  ? 175.736 162.896 130.109 1.00 47.08  ? 782  ASP   A O     1 
ATOM   3850  C  CB    . ASP   A 1 782  ? 173.143 161.564 128.928 1.00 45.98  ? 782  ASP   A CB    1 
ATOM   3851  C  CG    . ASP   A 1 782  ? 173.467 162.569 127.841 1.00 58.51  ? 782  ASP   A CG    1 
ATOM   3852  O  OD1   . ASP   A 1 782  ? 173.697 162.144 126.689 1.00 64.18  ? 782  ASP   A OD1   1 
ATOM   3853  O  OD2   . ASP   A 1 782  ? 173.492 163.782 128.138 1.00 60.13  ? 782  ASP   A OD2   1 
ATOM   3854  N  N     . HIS   A 1 783  ? 175.431 160.969 131.244 1.00 35.47  ? 783  HIS   A N     1 
ATOM   3855  C  CA    . HIS   A 1 783  ? 176.837 160.757 131.549 1.00 26.25  ? 783  HIS   A CA    1 
ATOM   3856  C  C     . HIS   A 1 783  ? 177.232 159.350 131.127 1.00 30.29  ? 783  HIS   A C     1 
ATOM   3857  O  O     . HIS   A 1 783  ? 176.402 158.439 131.095 1.00 33.85  ? 783  HIS   A O     1 
ATOM   3858  C  CB    . HIS   A 1 783  ? 177.128 160.967 133.043 1.00 31.37  ? 783  HIS   A CB    1 
ATOM   3859  C  CG    . HIS   A 1 783  ? 178.575 161.201 133.351 1.00 36.39  ? 783  HIS   A CG    1 
ATOM   3860  N  ND1   . HIS   A 1 783  ? 179.465 160.173 133.571 1.00 29.02  ? 783  HIS   A ND1   1 
ATOM   3861  C  CD2   . HIS   A 1 783  ? 179.285 162.346 133.477 1.00 33.50  ? 783  HIS   A CD2   1 
ATOM   3862  C  CE1   . HIS   A 1 783  ? 180.662 160.674 133.818 1.00 30.72  ? 783  HIS   A CE1   1 
ATOM   3863  N  NE2   . HIS   A 1 783  ? 180.580 161.991 133.767 1.00 31.51  ? 783  HIS   A NE2   1 
ATOM   3864  N  N     . VAL   A 1 784  ? 178.515 159.182 130.801 1.00 27.46  ? 784  VAL   A N     1 
ATOM   3865  C  CA    . VAL   A 1 784  ? 178.983 157.912 130.250 1.00 26.64  ? 784  VAL   A CA    1 
ATOM   3866  C  C     . VAL   A 1 784  ? 178.739 156.779 131.239 1.00 29.50  ? 784  VAL   A C     1 
ATOM   3867  O  O     . VAL   A 1 784  ? 178.255 155.702 130.870 1.00 35.78  ? 784  VAL   A O     1 
ATOM   3868  C  CB    . VAL   A 1 784  ? 180.469 158.008 129.860 1.00 31.55  ? 784  VAL   A CB    1 
ATOM   3869  C  CG1   . VAL   A 1 784  ? 181.268 158.661 130.975 1.00 34.38  ? 784  VAL   A CG1   1 
ATOM   3870  C  CG2   . VAL   A 1 784  ? 181.021 156.628 129.539 1.00 27.27  ? 784  VAL   A CG2   1 
ATOM   3871  N  N     . LYS   A 1 785  ? 179.078 156.998 132.510 1.00 30.73  ? 785  LYS   A N     1 
ATOM   3872  C  CA    . LYS   A 1 785  ? 178.886 155.952 133.507 1.00 34.07  ? 785  LYS   A CA    1 
ATOM   3873  C  C     . LYS   A 1 785  ? 177.419 155.707 133.822 1.00 30.67  ? 785  LYS   A C     1 
ATOM   3874  O  O     . LYS   A 1 785  ? 177.102 154.702 134.468 1.00 38.54  ? 785  LYS   A O     1 
ATOM   3875  C  CB    . LYS   A 1 785  ? 179.651 156.295 134.787 1.00 28.25  ? 785  LYS   A CB    1 
ATOM   3876  C  CG    . LYS   A 1 785  ? 179.380 157.681 135.338 1.00 28.89  ? 785  LYS   A CG    1 
ATOM   3877  C  CD    . LYS   A 1 785  ? 180.600 158.215 136.073 1.00 34.18  ? 785  LYS   A CD    1 
ATOM   3878  C  CE    . LYS   A 1 785  ? 180.909 157.400 137.319 1.00 32.22  ? 785  LYS   A CE    1 
ATOM   3879  N  NZ    . LYS   A 1 785  ? 180.068 157.800 138.480 1.00 35.56  ? 785  LYS   A NZ    1 
ATOM   3880  N  N     . ASN   A 1 786  ? 176.524 156.584 133.375 1.00 26.70  ? 786  ASN   A N     1 
ATOM   3881  C  CA    . ASN   A 1 786  ? 175.091 156.406 133.550 1.00 22.71  ? 786  ASN   A CA    1 
ATOM   3882  C  C     . ASN   A 1 786  ? 174.413 155.866 132.297 1.00 25.19  ? 786  ASN   A C     1 
ATOM   3883  O  O     . ASN   A 1 786  ? 173.181 155.851 132.229 1.00 40.38  ? 786  ASN   A O     1 
ATOM   3884  C  CB    . ASN   A 1 786  ? 174.446 157.729 133.966 1.00 19.21  ? 786  ASN   A CB    1 
ATOM   3885  C  CG    . ASN   A 1 786  ? 174.326 157.871 135.469 1.00 27.05  ? 786  ASN   A CG    1 
ATOM   3886  O  OD1   . ASN   A 1 786  ? 174.310 156.879 136.198 1.00 31.58  ? 786  ASN   A OD1   1 
ATOM   3887  N  ND2   . ASN   A 1 786  ? 174.245 159.108 135.942 1.00 29.34  ? 786  ASN   A ND2   1 
ATOM   3888  N  N     . PHE   A 1 787  ? 175.186 155.426 131.307 1.00 25.45  ? 787  PHE   A N     1 
ATOM   3889  C  CA    . PHE   A 1 787  ? 174.606 154.895 130.082 1.00 18.90  ? 787  PHE   A CA    1 
ATOM   3890  C  C     . PHE   A 1 787  ? 173.867 153.592 130.354 1.00 20.99  ? 787  PHE   A C     1 
ATOM   3891  O  O     . PHE   A 1 787  ? 174.333 152.740 131.115 1.00 29.85  ? 787  PHE   A O     1 
ATOM   3892  C  CB    . PHE   A 1 787  ? 175.695 154.667 129.032 1.00 16.01  ? 787  PHE   A CB    1 
ATOM   3893  C  CG    . PHE   A 1 787  ? 175.241 153.850 127.853 1.00 22.17  ? 787  PHE   A CG    1 
ATOM   3894  C  CD1   . PHE   A 1 787  ? 175.363 152.471 127.856 1.00 16.85  ? 787  PHE   A CD1   1 
ATOM   3895  C  CD2   . PHE   A 1 787  ? 174.692 154.464 126.741 1.00 19.44  ? 787  PHE   A CD2   1 
ATOM   3896  C  CE1   . PHE   A 1 787  ? 174.942 151.723 126.774 1.00 19.61  ? 787  PHE   A CE1   1 
ATOM   3897  C  CE2   . PHE   A 1 787  ? 174.273 153.719 125.657 1.00 10.02  ? 787  PHE   A CE2   1 
ATOM   3898  C  CZ    . PHE   A 1 787  ? 174.398 152.348 125.674 1.00 15.13  ? 787  PHE   A CZ    1 
ATOM   3899  N  N     . ARG   A 1 788  ? 172.707 153.435 129.718 1.00 15.81  ? 788  ARG   A N     1 
ATOM   3900  C  CA    . ARG   A 1 788  ? 171.939 152.208 129.816 1.00 17.68  ? 788  ARG   A CA    1 
ATOM   3901  C  C     . ARG   A 1 788  ? 171.555 151.728 128.424 1.00 23.23  ? 788  ARG   A C     1 
ATOM   3902  O  O     . ARG   A 1 788  ? 171.269 152.544 127.540 1.00 26.01  ? 788  ARG   A O     1 
ATOM   3903  C  CB    . ARG   A 1 788  ? 170.670 152.411 130.655 1.00 18.02  ? 788  ARG   A CB    1 
ATOM   3904  C  CG    . ARG   A 1 788  ? 170.925 152.897 132.066 1.00 21.17  ? 788  ARG   A CG    1 
ATOM   3905  C  CD    . ARG   A 1 788  ? 169.626 153.258 132.756 1.00 20.31  ? 788  ARG   A CD    1 
ATOM   3906  N  NE    . ARG   A 1 788  ? 169.843 153.801 134.091 1.00 21.10  ? 788  ARG   A NE    1 
ATOM   3907  C  CZ    . ARG   A 1 788  ? 169.833 153.078 135.202 1.00 25.14  ? 788  ARG   A CZ    1 
ATOM   3908  N  NH1   . ARG   A 1 788  ? 169.628 151.772 135.175 1.00 22.93  ? 788  ARG   A NH1   1 
ATOM   3909  N  NH2   . ARG   A 1 788  ? 170.035 153.682 136.369 1.00 22.43  ? 788  ARG   A NH2   1 
ATOM   3910  N  N     . PRO   A 1 789  ? 171.545 150.417 128.195 1.00 27.44  ? 789  PRO   A N     1 
ATOM   3911  C  CA    . PRO   A 1 789  ? 171.067 149.901 126.906 1.00 22.50  ? 789  PRO   A CA    1 
ATOM   3912  C  C     . PRO   A 1 789  ? 169.562 150.048 126.759 1.00 29.71  ? 789  PRO   A C     1 
ATOM   3913  O  O     . PRO   A 1 789  ? 168.793 149.330 127.406 1.00 21.81  ? 789  PRO   A O     1 
ATOM   3914  C  CB    . PRO   A 1 789  ? 171.485 148.425 126.942 1.00 17.25  ? 789  PRO   A CB    1 
ATOM   3915  C  CG    . PRO   A 1 789  ? 171.641 148.118 128.395 1.00 29.16  ? 789  PRO   A CG    1 
ATOM   3916  C  CD    . PRO   A 1 789  ? 172.189 149.368 128.998 1.00 26.46  ? 789  PRO   A CD    1 
ATOM   3917  N  N     . GLN   A 1 790  ? 169.134 150.968 125.904 1.00 30.60  ? 790  GLN   A N     1 
ATOM   3918  C  CA    . GLN   A 1 790  ? 167.720 151.237 125.655 1.00 16.64  ? 790  GLN   A CA    1 
ATOM   3919  C  C     . GLN   A 1 790  ? 167.392 150.648 124.287 1.00 22.34  ? 790  GLN   A C     1 
ATOM   3920  O  O     . GLN   A 1 790  ? 167.706 151.242 123.253 1.00 19.58  ? 790  GLN   A O     1 
ATOM   3921  C  CB    . GLN   A 1 790  ? 167.440 152.735 125.725 1.00 20.95  ? 790  GLN   A CB    1 
ATOM   3922  C  CG    . GLN   A 1 790  ? 167.994 153.386 126.984 1.00 16.41  ? 790  GLN   A CG    1 
ATOM   3923  C  CD    . GLN   A 1 790  ? 167.501 154.802 127.188 1.00 30.04  ? 790  GLN   A CD    1 
ATOM   3924  O  OE1   . GLN   A 1 790  ? 166.366 155.022 127.609 1.00 46.17  ? 790  GLN   A OE1   1 
ATOM   3925  N  NE2   . GLN   A 1 790  ? 168.357 155.773 126.900 1.00 34.67  ? 790  GLN   A NE2   1 
ATOM   3926  N  N     . CYS   A 1 791  ? 166.752 149.484 124.289 1.00 33.57  ? 791  CYS   A N     1 
ATOM   3927  C  CA    . CYS   A 1 791  ? 166.665 148.631 123.114 1.00 25.13  ? 791  CYS   A CA    1 
ATOM   3928  C  C     . CYS   A 1 791  ? 165.277 148.681 122.489 1.00 32.11  ? 791  CYS   A C     1 
ATOM   3929  O  O     . CYS   A 1 791  ? 164.260 148.638 123.191 1.00 29.40  ? 791  CYS   A O     1 
ATOM   3930  C  CB    . CYS   A 1 791  ? 167.018 147.186 123.473 1.00 22.09  ? 791  CYS   A CB    1 
ATOM   3931  S  SG    . CYS   A 1 791  ? 168.591 147.000 124.344 1.00 54.58  ? 791  CYS   A SG    1 
ATOM   3932  N  N     . LEU   A 1 792  ? 165.253 148.781 121.163 1.00 29.44  ? 792  LEU   A N     1 
ATOM   3933  C  CA    . LEU   A 1 792  ? 164.050 148.645 120.354 1.00 18.29  ? 792  LEU   A CA    1 
ATOM   3934  C  C     . LEU   A 1 792  ? 164.190 147.347 119.571 1.00 20.64  ? 792  LEU   A C     1 
ATOM   3935  O  O     . LEU   A 1 792  ? 165.023 147.251 118.664 1.00 34.47  ? 792  LEU   A O     1 
ATOM   3936  C  CB    . LEU   A 1 792  ? 163.878 149.844 119.425 1.00 19.00  ? 792  LEU   A CB    1 
ATOM   3937  C  CG    . LEU   A 1 792  ? 162.986 149.655 118.199 1.00 28.95  ? 792  LEU   A CG    1 
ATOM   3938  C  CD1   . LEU   A 1 792  ? 161.542 149.450 118.614 1.00 22.50  ? 792  LEU   A CD1   1 
ATOM   3939  C  CD2   . LEU   A 1 792  ? 163.115 150.845 117.259 1.00 27.80  ? 792  LEU   A CD2   1 
ATOM   3940  N  N     . VAL   A 1 793  ? 163.394 146.350 119.935 1.00 19.41  ? 793  VAL   A N     1 
ATOM   3941  C  CA    . VAL   A 1 793  ? 163.481 145.017 119.352 1.00 27.30  ? 793  VAL   A CA    1 
ATOM   3942  C  C     . VAL   A 1 793  ? 162.401 144.890 118.289 1.00 34.63  ? 793  VAL   A C     1 
ATOM   3943  O  O     . VAL   A 1 793  ? 161.212 145.081 118.574 1.00 38.94  ? 793  VAL   A O     1 
ATOM   3944  C  CB    . VAL   A 1 793  ? 163.332 143.927 120.425 1.00 19.98  ? 793  VAL   A CB    1 
ATOM   3945  C  CG1   . VAL   A 1 793  ? 163.759 142.580 119.873 1.00 20.83  ? 793  VAL   A CG1   1 
ATOM   3946  C  CG2   . VAL   A 1 793  ? 164.144 144.285 121.656 1.00 21.98  ? 793  VAL   A CG2   1 
ATOM   3947  N  N     . MET   A 1 794  ? 162.812 144.568 117.064 1.00 28.71  ? 794  MET   A N     1 
ATOM   3948  C  CA    . MET   A 1 794  ? 161.878 144.379 115.955 1.00 23.86  ? 794  MET   A CA    1 
ATOM   3949  C  C     . MET   A 1 794  ? 161.444 142.920 115.952 1.00 30.34  ? 794  MET   A C     1 
ATOM   3950  O  O     . MET   A 1 794  ? 162.159 142.049 115.452 1.00 38.98  ? 794  MET   A O     1 
ATOM   3951  C  CB    . MET   A 1 794  ? 162.520 144.775 114.631 1.00 31.41  ? 794  MET   A CB    1 
ATOM   3952  C  CG    . MET   A 1 794  ? 163.017 146.206 114.593 1.00 37.93  ? 794  MET   A CG    1 
ATOM   3953  S  SD    . MET   A 1 794  ? 161.864 147.356 115.362 1.00 56.38  ? 794  MET   A SD    1 
ATOM   3954  C  CE    . MET   A 1 794  ? 160.345 146.922 114.520 1.00 31.43  ? 794  MET   A CE    1 
ATOM   3955  N  N     . THR   A 1 795  ? 160.264 142.650 116.512 1.00 40.69  ? 795  THR   A N     1 
ATOM   3956  C  CA    . THR   A 1 795  ? 159.778 141.286 116.658 1.00 44.42  ? 795  THR   A CA    1 
ATOM   3957  C  C     . THR   A 1 795  ? 158.379 141.058 116.107 1.00 48.73  ? 795  THR   A C     1 
ATOM   3958  O  O     . THR   A 1 795  ? 157.960 139.899 116.015 1.00 49.60  ? 795  THR   A O     1 
ATOM   3959  C  CB    . THR   A 1 795  ? 159.790 140.866 118.137 1.00 46.12  ? 795  THR   A CB    1 
ATOM   3960  O  OG1   . THR   A 1 795  ? 159.433 141.983 118.959 1.00 37.11  ? 795  THR   A OG1   1 
ATOM   3961  C  CG2   . THR   A 1 795  ? 161.171 140.377 118.536 1.00 50.59  ? 795  THR   A CG2   1 
ATOM   3962  N  N     . GLY   A 1 796  ? 157.649 142.105 115.736 1.00 41.99  ? 796  GLY   A N     1 
ATOM   3963  C  CA    . GLY   A 1 796  ? 156.268 141.932 115.335 1.00 34.25  ? 796  GLY   A CA    1 
ATOM   3964  C  C     . GLY   A 1 796  ? 155.410 141.535 116.516 1.00 45.37  ? 796  GLY   A C     1 
ATOM   3965  O  O     . GLY   A 1 796  ? 155.241 142.318 117.456 1.00 46.68  ? 796  GLY   A O     1 
ATOM   3966  N  N     . ALA   A 1 797  ? 154.863 140.328 116.485 1.00 46.59  ? 797  ALA   A N     1 
ATOM   3967  C  CA    . ALA   A 1 797  ? 154.156 139.803 117.644 1.00 36.55  ? 797  ALA   A CA    1 
ATOM   3968  C  C     . ALA   A 1 797  ? 155.171 139.383 118.698 1.00 40.68  ? 797  ALA   A C     1 
ATOM   3969  O  O     . ALA   A 1 797  ? 156.032 138.544 118.412 1.00 44.43  ? 797  ALA   A O     1 
ATOM   3970  C  CB    . ALA   A 1 797  ? 153.280 138.622 117.253 1.00 40.57  ? 797  ALA   A CB    1 
ATOM   3971  N  N     . PRO   A 1 798  ? 155.114 139.931 119.913 1.00 43.58  ? 798  PRO   A N     1 
ATOM   3972  C  CA    . PRO   A 1 798  ? 156.146 139.604 120.909 1.00 38.01  ? 798  PRO   A CA    1 
ATOM   3973  C  C     . PRO   A 1 798  ? 156.186 138.136 121.287 1.00 41.42  ? 798  PRO   A C     1 
ATOM   3974  O  O     . PRO   A 1 798  ? 157.197 137.684 121.840 1.00 50.27  ? 798  PRO   A O     1 
ATOM   3975  C  CB    . PRO   A 1 798  ? 155.760 140.485 122.106 1.00 37.45  ? 798  PRO   A CB    1 
ATOM   3976  C  CG    . PRO   A 1 798  ? 154.290 140.720 121.916 1.00 37.84  ? 798  PRO   A CG    1 
ATOM   3977  C  CD    . PRO   A 1 798  ? 154.160 140.919 120.438 1.00 41.87  ? 798  PRO   A CD    1 
ATOM   3978  N  N     . ASN   A 1 799  ? 155.130 137.377 121.012 1.00 43.99  ? 799  ASN   A N     1 
ATOM   3979  C  CA    . ASN   A 1 799  ? 155.094 135.956 121.329 1.00 48.51  ? 799  ASN   A CA    1 
ATOM   3980  C  C     . ASN   A 1 799  ? 155.565 135.077 120.179 1.00 50.67  ? 799  ASN   A C     1 
ATOM   3981  O  O     . ASN   A 1 799  ? 155.599 133.851 120.330 1.00 51.20  ? 799  ASN   A O     1 
ATOM   3982  C  CB    . ASN   A 1 799  ? 153.676 135.546 121.742 1.00 48.84  ? 799  ASN   A CB    1 
ATOM   3983  C  CG    . ASN   A 1 799  ? 152.696 135.592 120.586 1.00 53.85  ? 799  ASN   A CG    1 
ATOM   3984  O  OD1   . ASN   A 1 799  ? 152.978 136.176 119.540 1.00 56.77  ? 799  ASN   A OD1   1 
ATOM   3985  N  ND2   . ASN   A 1 799  ? 151.536 134.973 120.769 1.00 54.69  ? 799  ASN   A ND2   1 
ATOM   3986  N  N     . SER   A 1 800  ? 155.924 135.666 119.036 1.00 49.15  ? 800  SER   A N     1 
ATOM   3987  C  CA    . SER   A 1 800  ? 156.368 134.864 117.901 1.00 49.19  ? 800  SER   A CA    1 
ATOM   3988  C  C     . SER   A 1 800  ? 157.677 134.148 118.205 1.00 59.05  ? 800  SER   A C     1 
ATOM   3989  O  O     . SER   A 1 800  ? 157.821 132.955 117.914 1.00 63.33  ? 800  SER   A O     1 
ATOM   3990  C  CB    . SER   A 1 800  ? 156.514 135.747 116.662 1.00 52.70  ? 800  SER   A CB    1 
ATOM   3991  O  OG    . SER   A 1 800  ? 156.926 137.056 117.015 1.00 58.47  ? 800  SER   A OG    1 
ATOM   3992  N  N     . ARG   A 1 801  ? 158.642 134.856 118.786 1.00 54.18  ? 801  ARG   A N     1 
ATOM   3993  C  CA    . ARG   A 1 801  ? 159.933 134.278 119.157 1.00 51.84  ? 801  ARG   A CA    1 
ATOM   3994  C  C     . ARG   A 1 801  ? 160.188 134.566 120.630 1.00 51.80  ? 801  ARG   A C     1 
ATOM   3995  O  O     . ARG   A 1 801  ? 160.620 135.678 120.984 1.00 52.85  ? 801  ARG   A O     1 
ATOM   3996  C  CB    . ARG   A 1 801  ? 161.056 134.828 118.288 1.00 52.07  ? 801  ARG   A CB    1 
ATOM   3997  C  CG    . ARG   A 1 801  ? 160.797 134.702 116.795 1.00 50.71  ? 801  ARG   A CG    1 
ATOM   3998  C  CD    . ARG   A 1 801  ? 161.901 135.354 115.981 1.00 54.28  ? 801  ARG   A CD    1 
ATOM   3999  N  NE    . ARG   A 1 801  ? 161.679 136.782 115.793 1.00 60.86  ? 801  ARG   A NE    1 
ATOM   4000  C  CZ    . ARG   A 1 801  ? 162.285 137.518 114.871 1.00 58.90  ? 801  ARG   A CZ    1 
ATOM   4001  N  NH1   . ARG   A 1 801  ? 163.159 136.990 114.031 1.00 52.49  ? 801  ARG   A NH1   1 
ATOM   4002  N  NH2   . ARG   A 1 801  ? 162.007 138.816 114.791 1.00 57.90  ? 801  ARG   A NH2   1 
ATOM   4003  N  N     . PRO   A 1 802  ? 159.939 133.602 121.515 1.00 45.85  ? 802  PRO   A N     1 
ATOM   4004  C  CA    . PRO   A 1 802  ? 160.051 133.873 122.953 1.00 43.77  ? 802  PRO   A CA    1 
ATOM   4005  C  C     . PRO   A 1 802  ? 161.481 133.824 123.468 1.00 47.69  ? 802  PRO   A C     1 
ATOM   4006  O  O     . PRO   A 1 802  ? 161.826 134.540 124.412 1.00 47.99  ? 802  PRO   A O     1 
ATOM   4007  C  CB    . PRO   A 1 802  ? 159.189 132.770 123.586 1.00 44.75  ? 802  PRO   A CB    1 
ATOM   4008  C  CG    . PRO   A 1 802  ? 158.847 131.796 122.457 1.00 48.60  ? 802  PRO   A CG    1 
ATOM   4009  C  CD    . PRO   A 1 802  ? 159.637 132.189 121.251 1.00 45.07  ? 802  PRO   A CD    1 
ATOM   4010  N  N     . ALA   A 1 803  ? 162.321 132.982 122.862 1.00 40.18  ? 803  ALA   A N     1 
ATOM   4011  C  CA    . ALA   A 1 803  ? 163.706 132.885 123.311 1.00 31.99  ? 803  ALA   A CA    1 
ATOM   4012  C  C     . ALA   A 1 803  ? 164.447 134.199 123.102 1.00 34.12  ? 803  ALA   A C     1 
ATOM   4013  O  O     . ALA   A 1 803  ? 165.171 134.663 123.992 1.00 42.93  ? 803  ALA   A O     1 
ATOM   4014  C  CB    . ALA   A 1 803  ? 164.414 131.745 122.581 1.00 35.76  ? 803  ALA   A CB    1 
ATOM   4015  N  N     . LEU   A 1 804  ? 164.276 134.814 121.931 1.00 33.91  ? 804  LEU   A N     1 
ATOM   4016  C  CA    . LEU   A 1 804  ? 164.920 136.095 121.667 1.00 34.26  ? 804  LEU   A CA    1 
ATOM   4017  C  C     . LEU   A 1 804  ? 164.413 137.169 122.619 1.00 30.90  ? 804  LEU   A C     1 
ATOM   4018  O  O     . LEU   A 1 804  ? 165.191 137.994 123.112 1.00 42.93  ? 804  LEU   A O     1 
ATOM   4019  C  CB    . LEU   A 1 804  ? 164.686 136.506 120.214 1.00 27.73  ? 804  LEU   A CB    1 
ATOM   4020  C  CG    . LEU   A 1 804  ? 165.335 137.809 119.747 1.00 31.88  ? 804  LEU   A CG    1 
ATOM   4021  C  CD1   . LEU   A 1 804  ? 166.103 137.590 118.455 1.00 36.94  ? 804  LEU   A CD1   1 
ATOM   4022  C  CD2   . LEU   A 1 804  ? 164.289 138.893 119.574 1.00 29.57  ? 804  LEU   A CD2   1 
ATOM   4023  N  N     . LEU   A 1 805  ? 163.104 137.182 122.879 1.00 27.76  ? 805  LEU   A N     1 
ATOM   4024  C  CA    . LEU   A 1 805  ? 162.547 138.165 123.801 1.00 29.50  ? 805  LEU   A CA    1 
ATOM   4025  C  C     . LEU   A 1 805  ? 163.113 137.984 125.203 1.00 38.61  ? 805  LEU   A C     1 
ATOM   4026  O  O     . LEU   A 1 805  ? 163.468 138.964 125.867 1.00 41.95  ? 805  LEU   A O     1 
ATOM   4027  C  CB    . LEU   A 1 805  ? 161.022 138.062 123.812 1.00 35.60  ? 805  LEU   A CB    1 
ATOM   4028  C  CG    . LEU   A 1 805  ? 160.261 139.063 124.682 1.00 40.54  ? 805  LEU   A CG    1 
ATOM   4029  C  CD1   . LEU   A 1 805  ? 159.781 140.244 123.855 1.00 32.08  ? 805  LEU   A CD1   1 
ATOM   4030  C  CD2   . LEU   A 1 805  ? 159.092 138.382 125.365 1.00 39.57  ? 805  LEU   A CD2   1 
ATOM   4031  N  N     . HIS   A 1 806  ? 163.213 136.737 125.669 1.00 39.19  ? 806  HIS   A N     1 
ATOM   4032  C  CA    . HIS   A 1 806  ? 163.805 136.479 126.977 1.00 36.87  ? 806  HIS   A CA    1 
ATOM   4033  C  C     . HIS   A 1 806  ? 165.252 136.950 127.024 1.00 36.20  ? 806  HIS   A C     1 
ATOM   4034  O  O     . HIS   A 1 806  ? 165.675 137.609 127.982 1.00 45.89  ? 806  HIS   A O     1 
ATOM   4035  C  CB    . HIS   A 1 806  ? 163.720 134.988 127.306 1.00 38.89  ? 806  HIS   A CB    1 
ATOM   4036  C  CG    . HIS   A 1 806  ? 162.407 134.570 127.890 1.00 42.14  ? 806  HIS   A CG    1 
ATOM   4037  N  ND1   . HIS   A 1 806  ? 161.407 133.996 127.136 1.00 41.99  ? 806  HIS   A ND1   1 
ATOM   4038  C  CD2   . HIS   A 1 806  ? 161.933 134.636 129.157 1.00 42.65  ? 806  HIS   A CD2   1 
ATOM   4039  C  CE1   . HIS   A 1 806  ? 160.371 133.731 127.912 1.00 41.50  ? 806  HIS   A CE1   1 
ATOM   4040  N  NE2   . HIS   A 1 806  ? 160.664 134.111 129.142 1.00 44.65  ? 806  HIS   A NE2   1 
ATOM   4041  N  N     . LEU   A 1 807  ? 166.029 136.615 125.992 1.00 27.01  ? 807  LEU   A N     1 
ATOM   4042  C  CA    . LEU   A 1 807  ? 167.430 137.021 125.965 1.00 22.79  ? 807  LEU   A CA    1 
ATOM   4043  C  C     . LEU   A 1 807  ? 167.564 138.536 126.018 1.00 23.91  ? 807  LEU   A C     1 
ATOM   4044  O  O     . LEU   A 1 807  ? 168.390 139.067 126.769 1.00 34.06  ? 807  LEU   A O     1 
ATOM   4045  C  CB    . LEU   A 1 807  ? 168.115 136.462 124.718 1.00 25.30  ? 807  LEU   A CB    1 
ATOM   4046  C  CG    . LEU   A 1 807  ? 169.631 136.644 124.657 1.00 32.58  ? 807  LEU   A CG    1 
ATOM   4047  C  CD1   . LEU   A 1 807  ? 170.269 136.254 125.977 1.00 34.43  ? 807  LEU   A CD1   1 
ATOM   4048  C  CD2   . LEU   A 1 807  ? 170.220 135.831 123.522 1.00 37.06  ? 807  LEU   A CD2   1 
ATOM   4049  N  N     . VAL   A 1 808  ? 166.759 139.252 125.233 1.00 16.80  ? 808  VAL   A N     1 
ATOM   4050  C  CA    . VAL   A 1 808  ? 166.797 140.711 125.276 1.00 23.58  ? 808  VAL   A CA    1 
ATOM   4051  C  C     . VAL   A 1 808  ? 166.391 141.211 126.655 1.00 26.78  ? 808  VAL   A C     1 
ATOM   4052  O  O     . VAL   A 1 808  ? 166.947 142.190 127.167 1.00 28.52  ? 808  VAL   A O     1 
ATOM   4053  C  CB    . VAL   A 1 808  ? 165.905 141.307 124.171 1.00 29.62  ? 808  VAL   A CB    1 
ATOM   4054  C  CG1   . VAL   A 1 808  ? 165.991 142.825 124.181 1.00 23.04  ? 808  VAL   A CG1   1 
ATOM   4055  C  CG2   . VAL   A 1 808  ? 166.311 140.759 122.818 1.00 30.53  ? 808  VAL   A CG2   1 
ATOM   4056  N  N     . HIS   A 1 809  ? 165.413 140.550 127.278 1.00 39.22  ? 809  HIS   A N     1 
ATOM   4057  C  CA    . HIS   A 1 809  ? 164.996 140.927 128.624 1.00 26.61  ? 809  HIS   A CA    1 
ATOM   4058  C  C     . HIS   A 1 809  ? 166.147 140.807 129.613 1.00 35.95  ? 809  HIS   A C     1 
ATOM   4059  O  O     . HIS   A 1 809  ? 166.301 141.650 130.505 1.00 28.70  ? 809  HIS   A O     1 
ATOM   4060  C  CB    . HIS   A 1 809  ? 163.824 140.053 129.068 1.00 26.40  ? 809  HIS   A CB    1 
ATOM   4061  C  CG    . HIS   A 1 809  ? 162.970 140.675 130.127 1.00 37.81  ? 809  HIS   A CG    1 
ATOM   4062  N  ND1   . HIS   A 1 809  ? 162.283 139.929 131.060 1.00 33.68  ? 809  HIS   A ND1   1 
ATOM   4063  C  CD2   . HIS   A 1 809  ? 162.678 141.970 130.392 1.00 40.18  ? 809  HIS   A CD2   1 
ATOM   4064  C  CE1   . HIS   A 1 809  ? 161.616 140.739 131.862 1.00 36.77  ? 809  HIS   A CE1   1 
ATOM   4065  N  NE2   . HIS   A 1 809  ? 161.836 141.982 131.477 1.00 42.68  ? 809  HIS   A NE2   1 
ATOM   4066  N  N     . ASP   A 1 810  ? 166.965 139.764 129.468 1.00 43.65  ? 810  ASP   A N     1 
ATOM   4067  C  CA    . ASP   A 1 810  ? 167.990 139.474 130.465 1.00 33.69  ? 810  ASP   A CA    1 
ATOM   4068  C  C     . ASP   A 1 810  ? 168.902 140.674 130.697 1.00 31.32  ? 810  ASP   A C     1 
ATOM   4069  O  O     . ASP   A 1 810  ? 169.163 141.054 131.844 1.00 45.44  ? 810  ASP   A O     1 
ATOM   4070  C  CB    . ASP   A 1 810  ? 168.801 138.252 130.036 1.00 40.17  ? 810  ASP   A CB    1 
ATOM   4071  C  CG    . ASP   A 1 810  ? 168.047 136.953 130.241 1.00 47.95  ? 810  ASP   A CG    1 
ATOM   4072  O  OD1   . ASP   A 1 810  ? 167.096 136.937 131.050 1.00 43.89  ? 810  ASP   A OD1   1 
ATOM   4073  O  OD2   . ASP   A 1 810  ? 168.402 135.949 129.589 1.00 51.55  ? 810  ASP   A OD2   1 
ATOM   4074  N  N     . PHE   A 1 811  ? 169.393 141.293 129.623 1.00 31.52  ? 811  PHE   A N     1 
ATOM   4075  C  CA    . PHE   A 1 811  ? 170.299 142.428 129.744 1.00 31.49  ? 811  PHE   A CA    1 
ATOM   4076  C  C     . PHE   A 1 811  ? 169.577 143.769 129.690 1.00 31.01  ? 811  PHE   A C     1 
ATOM   4077  O  O     . PHE   A 1 811  ? 170.232 144.813 129.623 1.00 42.33  ? 811  PHE   A O     1 
ATOM   4078  C  CB    . PHE   A 1 811  ? 171.399 142.359 128.674 1.00 31.52  ? 811  PHE   A CB    1 
ATOM   4079  C  CG    . PHE   A 1 811  ? 170.922 142.623 127.271 1.00 29.75  ? 811  PHE   A CG    1 
ATOM   4080  C  CD1   . PHE   A 1 811  ? 170.790 143.917 126.798 1.00 28.65  ? 811  PHE   A CD1   1 
ATOM   4081  C  CD2   . PHE   A 1 811  ? 170.640 141.573 126.414 1.00 34.35  ? 811  PHE   A CD2   1 
ATOM   4082  C  CE1   . PHE   A 1 811  ? 170.362 144.157 125.508 1.00 24.78  ? 811  PHE   A CE1   1 
ATOM   4083  C  CE2   . PHE   A 1 811  ? 170.214 141.809 125.123 1.00 27.71  ? 811  PHE   A CE2   1 
ATOM   4084  C  CZ    . PHE   A 1 811  ? 170.075 143.102 124.670 1.00 18.24  ? 811  PHE   A CZ    1 
ATOM   4085  N  N     . THR   A 1 812  ? 168.248 143.764 129.720 1.00 26.78  ? 812  THR   A N     1 
ATOM   4086  C  CA    . THR   A 1 812  ? 167.462 144.983 129.857 1.00 30.58  ? 812  THR   A CA    1 
ATOM   4087  C  C     . THR   A 1 812  ? 166.593 145.008 131.103 1.00 32.78  ? 812  THR   A C     1 
ATOM   4088  O  O     . THR   A 1 812  ? 166.303 146.092 131.612 1.00 32.61  ? 812  THR   A O     1 
ATOM   4089  C  CB    . THR   A 1 812  ? 166.563 145.193 128.626 1.00 34.56  ? 812  THR   A CB    1 
ATOM   4090  O  OG1   . THR   A 1 812  ? 166.527 143.995 127.842 1.00 44.68  ? 812  THR   A OG1   1 
ATOM   4091  C  CG2   . THR   A 1 812  ? 167.083 146.337 127.775 1.00 35.66  ? 812  THR   A CG2   1 
ATOM   4092  N  N     . LYS   A 1 813  ? 166.171 143.850 131.602 1.00 35.01  ? 813  LYS   A N     1 
ATOM   4093  C  CA    . LYS   A 1 813  ? 165.305 143.793 132.772 1.00 31.25  ? 813  LYS   A CA    1 
ATOM   4094  C  C     . LYS   A 1 813  ? 165.960 144.488 133.958 1.00 39.44  ? 813  LYS   A C     1 
ATOM   4095  O  O     . LYS   A 1 813  ? 167.046 144.097 134.398 1.00 43.90  ? 813  LYS   A O     1 
ATOM   4096  C  CB    . LYS   A 1 813  ? 164.991 142.336 133.108 1.00 38.50  ? 813  LYS   A CB    1 
ATOM   4097  C  CG    . LYS   A 1 813  ? 164.472 142.107 134.515 1.00 40.31  ? 813  LYS   A CG    1 
ATOM   4098  C  CD    . LYS   A 1 813  ? 163.309 143.023 134.837 1.00 41.97  ? 813  LYS   A CD    1 
ATOM   4099  C  CE    . LYS   A 1 813  ? 162.813 142.788 136.250 1.00 43.42  ? 813  LYS   A CE    1 
ATOM   4100  N  NZ    . LYS   A 1 813  ? 163.052 141.385 136.685 1.00 45.48  ? 813  LYS   A NZ    1 
ATOM   4101  N  N     . ASN   A 1 814  ? 165.295 145.517 134.476 1.00 36.63  ? 814  ASN   A N     1 
ATOM   4102  C  CA    . ASN   A 1 814  ? 165.705 146.338 135.607 1.00 36.93  ? 814  ASN   A CA    1 
ATOM   4103  C  C     . ASN   A 1 814  ? 166.830 147.298 135.237 1.00 33.40  ? 814  ASN   A C     1 
ATOM   4104  O  O     . ASN   A 1 814  ? 167.194 148.136 136.061 1.00 42.01  ? 814  ASN   A O     1 
ATOM   4105  C  CB    . ASN   A 1 814  ? 166.143 145.508 136.830 1.00 35.82  ? 814  ASN   A CB    1 
ATOM   4106  C  CG    . ASN   A 1 814  ? 164.982 145.148 137.736 1.00 41.03  ? 814  ASN   A CG    1 
ATOM   4107  O  OD1   . ASN   A 1 814  ? 164.051 145.931 137.914 1.00 44.34  ? 814  ASN   A OD1   1 
ATOM   4108  N  ND2   . ASN   A 1 814  ? 165.033 143.953 138.313 1.00 46.34  ? 814  ASN   A ND2   1 
ATOM   4109  N  N     . VAL   A 1 815  ? 167.397 147.209 134.036 1.00 33.33  ? 815  VAL   A N     1 
ATOM   4110  C  CA    . VAL   A 1 815  ? 168.450 148.113 133.588 1.00 32.26  ? 815  VAL   A CA    1 
ATOM   4111  C  C     . VAL   A 1 815  ? 168.204 148.403 132.114 1.00 40.10  ? 815  VAL   A C     1 
ATOM   4112  O  O     . VAL   A 1 815  ? 168.401 147.526 131.266 1.00 50.83  ? 815  VAL   A O     1 
ATOM   4113  C  CB    . VAL   A 1 815  ? 169.858 147.535 133.799 1.00 34.42  ? 815  VAL   A CB    1 
ATOM   4114  C  CG1   . VAL   A 1 815  ? 169.949 146.125 133.236 1.00 27.50  ? 815  VAL   A CG1   1 
ATOM   4115  C  CG2   . VAL   A 1 815  ? 170.899 148.435 133.157 1.00 40.67  ? 815  VAL   A CG2   1 
ATOM   4116  N  N     . GLY   A 1 816  ? 167.775 149.623 131.806 1.00 33.23  ? 816  GLY   A N     1 
ATOM   4117  C  CA    . GLY   A 1 816  ? 167.518 150.020 130.439 1.00 28.53  ? 816  GLY   A CA    1 
ATOM   4118  C  C     . GLY   A 1 816  ? 166.077 149.801 130.011 1.00 17.32  ? 816  GLY   A C     1 
ATOM   4119  O  O     . GLY   A 1 816  ? 165.273 149.155 130.687 1.00 30.20  ? 816  GLY   A O     1 
ATOM   4120  N  N     . LEU   A 1 817  ? 165.755 150.361 128.850 1.00 29.55  ? 817  LEU   A N     1 
ATOM   4121  C  CA    . LEU   A 1 817  ? 164.411 150.334 128.295 1.00 20.94  ? 817  LEU   A CA    1 
ATOM   4122  C  C     . LEU   A 1 817  ? 164.287 149.251 127.228 1.00 22.45  ? 817  LEU   A C     1 
ATOM   4123  O  O     . LEU   A 1 817  ? 165.264 148.865 126.582 1.00 27.01  ? 817  LEU   A O     1 
ATOM   4124  C  CB    . LEU   A 1 817  ? 164.050 151.701 127.706 1.00 25.63  ? 817  LEU   A CB    1 
ATOM   4125  C  CG    . LEU   A 1 817  ? 162.779 151.782 126.861 1.00 28.15  ? 817  LEU   A CG    1 
ATOM   4126  C  CD1   . LEU   A 1 817  ? 161.544 151.725 127.747 1.00 29.66  ? 817  LEU   A CD1   1 
ATOM   4127  C  CD2   . LEU   A 1 817  ? 162.783 153.045 126.016 1.00 33.16  ? 817  LEU   A CD2   1 
ATOM   4128  N  N     . MET   A 1 818  ? 163.061 148.763 127.051 1.00 29.60  ? 818  MET   A N     1 
ATOM   4129  C  CA    . MET   A 1 818  ? 162.774 147.692 126.100 1.00 20.53  ? 818  MET   A CA    1 
ATOM   4130  C  C     . MET   A 1 818  ? 161.452 147.997 125.413 1.00 24.91  ? 818  MET   A C     1 
ATOM   4131  O  O     . MET   A 1 818  ? 160.400 147.997 126.060 1.00 25.10  ? 818  MET   A O     1 
ATOM   4132  C  CB    . MET   A 1 818  ? 162.721 146.334 126.799 1.00 21.98  ? 818  MET   A CB    1 
ATOM   4133  C  CG    . MET   A 1 818  ? 162.684 145.152 125.852 1.00 16.15  ? 818  MET   A CG    1 
ATOM   4134  S  SD    . MET   A 1 818  ? 162.761 143.572 126.710 1.00 49.58  ? 818  MET   A SD    1 
ATOM   4135  C  CE    . MET   A 1 818  ? 162.694 142.439 125.328 1.00 24.15  ? 818  MET   A CE    1 
ATOM   4136  N  N     . ILE   A 1 819  ? 161.500 148.257 124.109 1.00 28.06  ? 819  ILE   A N     1 
ATOM   4137  C  CA    . ILE   A 1 819  ? 160.305 148.519 123.315 1.00 18.03  ? 819  ILE   A CA    1 
ATOM   4138  C  C     . ILE   A 1 819  ? 160.220 147.461 122.227 1.00 18.17  ? 819  ILE   A C     1 
ATOM   4139  O  O     . ILE   A 1 819  ? 161.111 147.369 121.374 1.00 25.87  ? 819  ILE   A O     1 
ATOM   4140  C  CB    . ILE   A 1 819  ? 160.317 149.929 122.706 1.00 17.83  ? 819  ILE   A CB    1 
ATOM   4141  C  CG1   . ILE   A 1 819  ? 160.376 150.986 123.808 1.00 17.06  ? 819  ILE   A CG1   1 
ATOM   4142  C  CG2   . ILE   A 1 819  ? 159.082 150.145 121.856 1.00 21.65  ? 819  ILE   A CG2   1 
ATOM   4143  C  CD1   . ILE   A 1 819  ? 160.949 152.307 123.355 1.00 16.38  ? 819  ILE   A CD1   1 
ATOM   4144  N  N     . CYS   A 1 820  ? 159.149 146.673 122.247 1.00 20.31  ? 820  CYS   A N     1 
ATOM   4145  C  CA    . CYS   A 1 820  ? 158.911 145.659 121.222 1.00 23.33  ? 820  CYS   A CA    1 
ATOM   4146  C  C     . CYS   A 1 820  ? 158.110 146.308 120.101 1.00 24.83  ? 820  CYS   A C     1 
ATOM   4147  O  O     . CYS   A 1 820  ? 156.901 146.518 120.227 1.00 36.13  ? 820  CYS   A O     1 
ATOM   4148  C  CB    . CYS   A 1 820  ? 158.185 144.454 121.811 1.00 25.66  ? 820  CYS   A CB    1 
ATOM   4149  S  SG    . CYS   A 1 820  ? 158.606 144.095 123.530 1.00 47.69  ? 820  CYS   A SG    1 
ATOM   4150  N  N     . GLY   A 1 821  ? 158.785 146.630 119.000 1.00 25.53  ? 821  GLY   A N     1 
ATOM   4151  C  CA    . GLY   A 1 821  ? 158.141 147.301 117.885 1.00 17.08  ? 821  GLY   A CA    1 
ATOM   4152  C  C     . GLY   A 1 821  ? 157.488 146.315 116.931 1.00 27.55  ? 821  GLY   A C     1 
ATOM   4153  O  O     . GLY   A 1 821  ? 158.065 145.287 116.583 1.00 31.01  ? 821  GLY   A O     1 
ATOM   4154  N  N     . HIS   A 1 822  ? 156.269 146.647 116.513 1.00 35.94  ? 822  HIS   A N     1 
ATOM   4155  C  CA    . HIS   A 1 822  ? 155.507 145.839 115.572 1.00 29.20  ? 822  HIS   A CA    1 
ATOM   4156  C  C     . HIS   A 1 822  ? 154.992 146.738 114.460 1.00 31.41  ? 822  HIS   A C     1 
ATOM   4157  O  O     . HIS   A 1 822  ? 154.458 147.818 114.730 1.00 38.37  ? 822  HIS   A O     1 
ATOM   4158  C  CB    . HIS   A 1 822  ? 154.340 145.129 116.265 1.00 25.20  ? 822  HIS   A CB    1 
ATOM   4159  C  CG    . HIS   A 1 822  ? 153.683 144.081 115.422 1.00 33.78  ? 822  HIS   A CG    1 
ATOM   4160  N  ND1   . HIS   A 1 822  ? 154.124 143.759 114.158 1.00 40.84  ? 822  HIS   A ND1   1 
ATOM   4161  C  CD2   . HIS   A 1 822  ? 152.616 143.284 115.663 1.00 29.21  ? 822  HIS   A CD2   1 
ATOM   4162  C  CE1   . HIS   A 1 822  ? 153.358 142.807 113.656 1.00 36.58  ? 822  HIS   A CE1   1 
ATOM   4163  N  NE2   . HIS   A 1 822  ? 152.434 142.502 114.549 1.00 38.05  ? 822  HIS   A NE2   1 
ATOM   4164  N  N     . VAL   A 1 823  ? 155.152 146.293 113.217 1.00 27.14  ? 823  VAL   A N     1 
ATOM   4165  C  CA    . VAL   A 1 823  ? 154.712 147.038 112.043 1.00 28.95  ? 823  VAL   A CA    1 
ATOM   4166  C  C     . VAL   A 1 823  ? 153.519 146.315 111.436 1.00 36.64  ? 823  VAL   A C     1 
ATOM   4167  O  O     . VAL   A 1 823  ? 153.583 145.108 111.172 1.00 38.14  ? 823  VAL   A O     1 
ATOM   4168  C  CB    . VAL   A 1 823  ? 155.843 147.194 111.013 1.00 30.15  ? 823  VAL   A CB    1 
ATOM   4169  C  CG1   . VAL   A 1 823  ? 155.436 148.176 109.928 1.00 28.55  ? 823  VAL   A CG1   1 
ATOM   4170  C  CG2   . VAL   A 1 823  ? 157.121 147.653 111.696 1.00 27.54  ? 823  VAL   A CG2   1 
ATOM   4171  N  N     . HIS   A 1 824  ? 152.435 147.051 111.218 1.00 35.95  ? 824  HIS   A N     1 
ATOM   4172  C  CA    . HIS   A 1 824  ? 151.216 146.515 110.634 1.00 26.92  ? 824  HIS   A CA    1 
ATOM   4173  C  C     . HIS   A 1 824  ? 151.049 147.052 109.221 1.00 34.41  ? 824  HIS   A C     1 
ATOM   4174  O  O     . HIS   A 1 824  ? 151.249 148.244 108.972 1.00 37.06  ? 824  HIS   A O     1 
ATOM   4175  C  CB    . HIS   A 1 824  ? 149.994 146.875 111.480 1.00 27.02  ? 824  HIS   A CB    1 
ATOM   4176  C  CG    . HIS   A 1 824  ? 149.899 146.105 112.760 1.00 31.84  ? 824  HIS   A CG    1 
ATOM   4177  N  ND1   . HIS   A 1 824  ? 150.528 146.506 113.918 1.00 38.38  ? 824  HIS   A ND1   1 
ATOM   4178  C  CD2   . HIS   A 1 824  ? 149.251 144.956 113.061 1.00 36.88  ? 824  HIS   A CD2   1 
ATOM   4179  C  CE1   . HIS   A 1 824  ? 150.270 145.637 114.879 1.00 38.66  ? 824  HIS   A CE1   1 
ATOM   4180  N  NE2   . HIS   A 1 824  ? 149.497 144.687 114.386 1.00 42.84  ? 824  HIS   A NE2   1 
ATOM   4181  N  N     . MET   A 1 825  ? 150.678 146.168 108.299 1.00 43.86  ? 825  MET   A N     1 
ATOM   4182  C  CA    . MET   A 1 825  ? 150.568 146.511 106.891 1.00 40.44  ? 825  MET   A CA    1 
ATOM   4183  C  C     . MET   A 1 825  ? 149.171 146.177 106.388 1.00 41.51  ? 825  MET   A C     1 
ATOM   4184  O  O     . MET   A 1 825  ? 148.503 145.275 106.897 1.00 49.35  ? 825  MET   A O     1 
ATOM   4185  C  CB    . MET   A 1 825  ? 151.622 145.773 106.056 1.00 40.03  ? 825  MET   A CB    1 
ATOM   4186  C  CG    . MET   A 1 825  ? 152.927 146.531 105.904 1.00 40.35  ? 825  MET   A CG    1 
ATOM   4187  S  SD    . MET   A 1 825  ? 154.171 146.012 107.099 1.00 59.35  ? 825  MET   A SD    1 
ATOM   4188  C  CE    . MET   A 1 825  ? 154.130 144.236 106.885 1.00 49.12  ? 825  MET   A CE    1 
ATOM   4189  N  N     . GLY   A 1 826  ? 148.737 146.926 105.379 1.00 46.77  ? 826  GLY   A N     1 
ATOM   4190  C  CA    . GLY   A 1 826  ? 147.434 146.731 104.790 1.00 47.82  ? 826  GLY   A CA    1 
ATOM   4191  C  C     . GLY   A 1 826  ? 146.635 148.015 104.731 1.00 51.45  ? 826  GLY   A C     1 
ATOM   4192  O  O     . GLY   A 1 826  ? 147.167 149.115 104.907 1.00 54.16  ? 826  GLY   A O     1 
ATOM   4193  N  N     . PRO   A 1 827  ? 145.333 147.899 104.476 1.00 55.05  ? 827  PRO   A N     1 
ATOM   4194  C  CA    . PRO   A 1 827  ? 144.483 149.094 104.440 1.00 50.84  ? 827  PRO   A CA    1 
ATOM   4195  C  C     . PRO   A 1 827  ? 144.424 149.771 105.800 1.00 50.62  ? 827  PRO   A C     1 
ATOM   4196  O  O     . PRO   A 1 827  ? 144.438 149.119 106.846 1.00 55.38  ? 827  PRO   A O     1 
ATOM   4197  C  CB    . PRO   A 1 827  ? 143.111 148.545 104.023 1.00 51.58  ? 827  PRO   A CB    1 
ATOM   4198  C  CG    . PRO   A 1 827  ? 143.376 147.141 103.535 1.00 50.88  ? 827  PRO   A CG    1 
ATOM   4199  C  CD    . PRO   A 1 827  ? 144.549 146.666 104.316 1.00 53.52  ? 827  PRO   A CD    1 
ATOM   4200  N  N     . ARG   A 1 828  ? 144.347 151.103 105.774 1.00 48.75  ? 828  ARG   A N     1 
ATOM   4201  C  CA    . ARG   A 1 828  ? 144.371 151.870 107.016 1.00 49.84  ? 828  ARG   A CA    1 
ATOM   4202  C  C     . ARG   A 1 828  ? 143.175 151.541 107.902 1.00 54.17  ? 828  ARG   A C     1 
ATOM   4203  O  O     . ARG   A 1 828  ? 143.317 151.402 109.123 1.00 59.56  ? 828  ARG   A O     1 
ATOM   4204  C  CB    . ARG   A 1 828  ? 144.413 153.366 106.706 1.00 49.87  ? 828  ARG   A CB    1 
ATOM   4205  C  CG    . ARG   A 1 828  ? 144.573 154.248 107.933 1.00 51.19  ? 828  ARG   A CG    1 
ATOM   4206  C  CD    . ARG   A 1 828  ? 143.955 155.616 107.707 1.00 56.17  ? 828  ARG   A CD    1 
ATOM   4207  N  NE    . ARG   A 1 828  ? 142.940 155.585 106.662 1.00 58.69  ? 828  ARG   A NE    1 
ATOM   4208  C  CZ    . ARG   A 1 828  ? 141.633 155.594 106.883 1.00 59.86  ? 828  ARG   A CZ    1 
ATOM   4209  N  NH1   . ARG   A 1 828  ? 141.139 155.641 108.110 1.00 57.39  ? 828  ARG   A NH1   1 
ATOM   4210  N  NH2   . ARG   A 1 828  ? 140.799 155.554 105.848 1.00 56.31  ? 828  ARG   A NH2   1 
ATOM   4211  N  N     . ARG   A 1 829  ? 141.988 151.414 107.306 1.00 52.47  ? 829  ARG   A N     1 
ATOM   4212  C  CA    . ARG   A 1 829  ? 140.778 151.220 108.100 1.00 53.80  ? 829  ARG   A CA    1 
ATOM   4213  C  C     . ARG   A 1 829  ? 140.886 149.981 108.980 1.00 51.70  ? 829  ARG   A C     1 
ATOM   4214  O  O     . ARG   A 1 829  ? 140.881 150.078 110.212 1.00 52.88  ? 829  ARG   A O     1 
ATOM   4215  C  CB    . ARG   A 1 829  ? 139.561 151.126 107.179 1.00 52.92  ? 829  ARG   A CB    1 
ATOM   4216  N  N     . GLN   A 1 830  ? 140.986 148.802 108.363 1.00 48.84  ? 830  GLN   A N     1 
ATOM   4217  C  CA    . GLN   A 1 830  ? 141.105 147.574 109.143 1.00 51.30  ? 830  GLN   A CA    1 
ATOM   4218  C  C     . GLN   A 1 830  ? 142.390 147.550 109.960 1.00 56.99  ? 830  GLN   A C     1 
ATOM   4219  O  O     . GLN   A 1 830  ? 142.437 146.918 111.023 1.00 60.47  ? 830  GLN   A O     1 
ATOM   4220  C  CB    . GLN   A 1 830  ? 141.041 146.357 108.222 1.00 49.07  ? 830  GLN   A CB    1 
ATOM   4221  N  N     . ALA   A 1 831  ? 143.437 148.225 109.480 1.00 51.64  ? 831  ALA   A N     1 
ATOM   4222  C  CA    . ALA   A 1 831  ? 144.705 148.233 110.200 1.00 45.06  ? 831  ALA   A CA    1 
ATOM   4223  C  C     . ALA   A 1 831  ? 144.562 148.902 111.558 1.00 47.00  ? 831  ALA   A C     1 
ATOM   4224  O  O     . ALA   A 1 831  ? 145.160 148.457 112.542 1.00 51.57  ? 831  ALA   A O     1 
ATOM   4225  C  CB    . ALA   A 1 831  ? 145.780 148.932 109.370 1.00 48.13  ? 831  ALA   A CB    1 
ATOM   4226  N  N     . MET   A 1 832  ? 143.786 149.985 111.630 1.00 46.17  ? 832  MET   A N     1 
ATOM   4227  C  CA    . MET   A 1 832  ? 143.597 150.664 112.908 1.00 45.28  ? 832  MET   A CA    1 
ATOM   4228  C  C     . MET   A 1 832  ? 142.929 149.746 113.925 1.00 48.39  ? 832  MET   A C     1 
ATOM   4229  O  O     . MET   A 1 832  ? 143.350 149.676 115.085 1.00 50.09  ? 832  MET   A O     1 
ATOM   4230  C  CB    . MET   A 1 832  ? 142.783 151.941 112.712 1.00 43.10  ? 832  MET   A CB    1 
ATOM   4231  C  CG    . MET   A 1 832  ? 143.547 153.048 112.013 1.00 50.01  ? 832  MET   A CG    1 
ATOM   4232  S  SD    . MET   A 1 832  ? 145.322 152.737 112.017 1.00 65.89  ? 832  MET   A SD    1 
ATOM   4233  C  CE    . MET   A 1 832  ? 145.807 153.535 113.544 1.00 54.36  ? 832  MET   A CE    1 
ATOM   4234  N  N     . LYS   A 1 833  ? 141.885 149.029 113.506 1.00 48.14  ? 833  LYS   A N     1 
ATOM   4235  C  CA    . LYS   A 1 833  ? 141.211 148.112 114.419 1.00 48.18  ? 833  LYS   A CA    1 
ATOM   4236  C  C     . LYS   A 1 833  ? 142.132 146.972 114.836 1.00 50.54  ? 833  LYS   A C     1 
ATOM   4237  O  O     . LYS   A 1 833  ? 142.163 146.587 116.014 1.00 50.78  ? 833  LYS   A O     1 
ATOM   4238  C  CB    . LYS   A 1 833  ? 139.940 147.566 113.770 1.00 43.89  ? 833  LYS   A CB    1 
ATOM   4239  N  N     . GLU   A 1 834  ? 142.886 146.416 113.885 1.00 48.60  ? 834  GLU   A N     1 
ATOM   4240  C  CA    . GLU   A 1 834  ? 143.810 145.340 114.225 1.00 45.90  ? 834  GLU   A CA    1 
ATOM   4241  C  C     . GLU   A 1 834  ? 144.858 145.813 115.223 1.00 50.21  ? 834  GLU   A C     1 
ATOM   4242  O  O     . GLU   A 1 834  ? 145.176 145.104 116.183 1.00 55.90  ? 834  GLU   A O     1 
ATOM   4243  C  CB    . GLU   A 1 834  ? 144.475 144.795 112.962 1.00 43.42  ? 834  GLU   A CB    1 
ATOM   4244  C  CG    . GLU   A 1 834  ? 143.501 144.456 111.848 1.00 55.04  ? 834  GLU   A CG    1 
ATOM   4245  C  CD    . GLU   A 1 834  ? 143.782 143.108 111.213 1.00 60.06  ? 834  GLU   A CD    1 
ATOM   4246  O  OE1   . GLU   A 1 834  ? 143.445 142.075 111.828 1.00 61.77  ? 834  GLU   A OE1   1 
ATOM   4247  O  OE2   . GLU   A 1 834  ? 144.335 143.082 110.093 1.00 55.31  ? 834  GLU   A OE2   1 
ATOM   4248  N  N     . MET   A 1 835  ? 145.404 147.012 115.013 1.00 44.09  ? 835  MET   A N     1 
ATOM   4249  C  CA    . MET   A 1 835  ? 146.391 147.552 115.941 1.00 40.92  ? 835  MET   A CA    1 
ATOM   4250  C  C     . MET   A 1 835  ? 145.780 147.809 117.310 1.00 42.40  ? 835  MET   A C     1 
ATOM   4251  O  O     . MET   A 1 835  ? 146.416 147.550 118.336 1.00 45.21  ? 835  MET   A O     1 
ATOM   4252  C  CB    . MET   A 1 835  ? 147.000 148.833 115.374 1.00 40.35  ? 835  MET   A CB    1 
ATOM   4253  C  CG    . MET   A 1 835  ? 148.247 148.607 114.538 1.00 40.37  ? 835  MET   A CG    1 
ATOM   4254  S  SD    . MET   A 1 835  ? 148.789 150.098 113.687 1.00 59.56  ? 835  MET   A SD    1 
ATOM   4255  C  CE    . MET   A 1 835  ? 148.553 151.320 114.973 1.00 41.69  ? 835  MET   A CE    1 
ATOM   4256  N  N     . SER   A 1 836  ? 144.549 148.324 117.350 1.00 45.17  ? 836  SER   A N     1 
ATOM   4257  C  CA    . SER   A 1 836  ? 143.906 148.584 118.633 1.00 46.90  ? 836  SER   A CA    1 
ATOM   4258  C  C     . SER   A 1 836  ? 143.686 147.293 119.409 1.00 43.28  ? 836  SER   A C     1 
ATOM   4259  O  O     . SER   A 1 836  ? 143.860 147.258 120.632 1.00 42.40  ? 836  SER   A O     1 
ATOM   4260  C  CB    . SER   A 1 836  ? 142.582 149.315 118.418 1.00 49.30  ? 836  SER   A CB    1 
ATOM   4261  O  OG    . SER   A 1 836  ? 142.160 149.964 119.605 1.00 49.40  ? 836  SER   A OG    1 
ATOM   4262  N  N     . ILE   A 1 837  ? 143.302 146.219 118.717 1.00 39.77  ? 837  ILE   A N     1 
ATOM   4263  C  CA    . ILE   A 1 837  ? 143.124 144.935 119.391 1.00 35.61  ? 837  ILE   A CA    1 
ATOM   4264  C  C     . ILE   A 1 837  ? 144.469 144.389 119.860 1.00 41.02  ? 837  ILE   A C     1 
ATOM   4265  O  O     . ILE   A 1 837  ? 144.617 143.946 121.009 1.00 46.10  ? 837  ILE   A O     1 
ATOM   4266  C  CB    . ILE   A 1 837  ? 142.405 143.940 118.464 1.00 39.59  ? 837  ILE   A CB    1 
ATOM   4267  C  CG1   . ILE   A 1 837  ? 140.893 144.163 118.504 1.00 42.96  ? 837  ILE   A CG1   1 
ATOM   4268  C  CG2   . ILE   A 1 837  ? 142.744 142.510 118.853 1.00 39.88  ? 837  ILE   A CG2   1 
ATOM   4269  C  CD1   . ILE   A 1 837  ? 140.126 143.321 117.506 1.00 40.80  ? 837  ILE   A CD1   1 
ATOM   4270  N  N     . ASP   A 1 838  ? 145.469 144.419 118.975 1.00 40.27  ? 838  ASP   A N     1 
ATOM   4271  C  CA    . ASP   A 1 838  ? 146.760 143.816 119.280 1.00 33.93  ? 838  ASP   A CA    1 
ATOM   4272  C  C     . ASP   A 1 838  ? 147.461 144.546 120.415 1.00 37.69  ? 838  ASP   A C     1 
ATOM   4273  O  O     . ASP   A 1 838  ? 148.160 143.923 121.218 1.00 42.66  ? 838  ASP   A O     1 
ATOM   4274  C  CB    . ASP   A 1 838  ? 147.640 143.800 118.030 1.00 37.45  ? 838  ASP   A CB    1 
ATOM   4275  C  CG    . ASP   A 1 838  ? 147.293 142.666 117.088 1.00 43.82  ? 838  ASP   A CG    1 
ATOM   4276  O  OD1   . ASP   A 1 838  ? 146.814 141.620 117.571 1.00 45.09  ? 838  ASP   A OD1   1 
ATOM   4277  O  OD2   . ASP   A 1 838  ? 147.503 142.818 115.867 1.00 45.79  ? 838  ASP   A OD2   1 
ATOM   4278  N  N     . GLN   A 1 839  ? 147.301 145.867 120.494 1.00 31.07  ? 839  GLN   A N     1 
ATOM   4279  C  CA    . GLN   A 1 839  ? 147.934 146.611 121.576 1.00 33.57  ? 839  GLN   A CA    1 
ATOM   4280  C  C     . GLN   A 1 839  ? 147.510 146.059 122.928 1.00 43.84  ? 839  GLN   A C     1 
ATOM   4281  O  O     . GLN   A 1 839  ? 148.352 145.685 123.753 1.00 47.75  ? 839  GLN   A O     1 
ATOM   4282  C  CB    . GLN   A 1 839  ? 147.580 148.094 121.464 1.00 25.83  ? 839  GLN   A CB    1 
ATOM   4283  C  CG    . GLN   A 1 839  ? 147.754 148.869 122.756 1.00 31.31  ? 839  GLN   A CG    1 
ATOM   4284  C  CD    . GLN   A 1 839  ? 149.132 149.477 122.889 1.00 47.29  ? 839  GLN   A CD    1 
ATOM   4285  O  OE1   . GLN   A 1 839  ? 149.589 150.202 122.007 1.00 52.99  ? 839  GLN   A OE1   1 
ATOM   4286  N  NE2   . GLN   A 1 839  ? 149.805 149.182 123.995 1.00 44.25  ? 839  GLN   A NE2   1 
ATOM   4287  N  N     . ALA   A 1 840  ? 146.200 145.966 123.156 1.00 41.89  ? 840  ALA   A N     1 
ATOM   4288  C  CA    . ALA   A 1 840  ? 145.704 145.438 124.419 1.00 33.18  ? 840  ALA   A CA    1 
ATOM   4289  C  C     . ALA   A 1 840  ? 146.122 143.986 124.604 1.00 33.14  ? 840  ALA   A C     1 
ATOM   4290  O  O     . ALA   A 1 840  ? 146.624 143.603 125.669 1.00 39.59  ? 840  ALA   A O     1 
ATOM   4291  C  CB    . ALA   A 1 840  ? 144.183 145.577 124.482 1.00 35.69  ? 840  ALA   A CB    1 
ATOM   4292  N  N     . LYS   A 1 841  ? 145.938 143.163 123.567 1.00 30.18  ? 841  LYS   A N     1 
ATOM   4293  C  CA    . LYS   A 1 841  ? 146.256 141.744 123.696 1.00 26.57  ? 841  LYS   A CA    1 
ATOM   4294  C  C     . LYS   A 1 841  ? 147.701 141.544 124.132 1.00 33.72  ? 841  LYS   A C     1 
ATOM   4295  O  O     . LYS   A 1 841  ? 147.979 140.849 125.117 1.00 43.47  ? 841  LYS   A O     1 
ATOM   4296  C  CB    . LYS   A 1 841  ? 145.993 141.026 122.372 1.00 31.06  ? 841  LYS   A CB    1 
ATOM   4297  C  CG    . LYS   A 1 841  ? 146.084 139.514 122.462 1.00 33.54  ? 841  LYS   A CG    1 
ATOM   4298  C  CD    . LYS   A 1 841  ? 146.714 138.925 121.211 1.00 37.91  ? 841  LYS   A CD    1 
ATOM   4299  C  CE    . LYS   A 1 841  ? 145.736 138.893 120.052 1.00 39.27  ? 841  LYS   A CE    1 
ATOM   4300  N  NZ    . LYS   A 1 841  ? 146.168 137.936 118.997 1.00 39.80  ? 841  LYS   A NZ    1 
ATOM   4301  N  N     . TYR   A 1 842  ? 148.638 142.173 123.424 1.00 39.63  ? 842  TYR   A N     1 
ATOM   4302  C  CA    . TYR   A 1 842  ? 150.052 141.934 123.664 1.00 31.94  ? 842  TYR   A CA    1 
ATOM   4303  C  C     . TYR   A 1 842  ? 150.557 142.640 124.914 1.00 35.10  ? 842  TYR   A C     1 
ATOM   4304  O  O     . TYR   A 1 842  ? 151.450 142.117 125.584 1.00 37.69  ? 842  TYR   A O     1 
ATOM   4305  C  CB    . TYR   A 1 842  ? 150.861 142.352 122.438 1.00 30.51  ? 842  TYR   A CB    1 
ATOM   4306  C  CG    . TYR   A 1 842  ? 150.567 141.492 121.232 1.00 36.11  ? 842  TYR   A CG    1 
ATOM   4307  C  CD1   . TYR   A 1 842  ? 150.549 140.108 121.334 1.00 37.47  ? 842  TYR   A CD1   1 
ATOM   4308  C  CD2   . TYR   A 1 842  ? 150.289 142.060 119.998 1.00 34.39  ? 842  TYR   A CD2   1 
ATOM   4309  C  CE1   . TYR   A 1 842  ? 150.274 139.315 120.242 1.00 35.68  ? 842  TYR   A CE1   1 
ATOM   4310  C  CE2   . TYR   A 1 842  ? 150.012 141.274 118.898 1.00 38.14  ? 842  TYR   A CE2   1 
ATOM   4311  C  CZ    . TYR   A 1 842  ? 150.006 139.903 119.026 1.00 38.11  ? 842  TYR   A CZ    1 
ATOM   4312  O  OH    . TYR   A 1 842  ? 149.731 139.114 117.934 1.00 41.58  ? 842  TYR   A OH    1 
ATOM   4313  N  N     . GLN   A 1 843  ? 150.012 143.809 125.263 1.00 32.46  ? 843  GLN   A N     1 
ATOM   4314  C  CA    . GLN   A 1 843  ? 150.388 144.415 126.534 1.00 26.51  ? 843  GLN   A CA    1 
ATOM   4315  C  C     . GLN   A 1 843  ? 149.951 143.541 127.702 1.00 38.37  ? 843  GLN   A C     1 
ATOM   4316  O  O     . GLN   A 1 843  ? 150.710 143.346 128.660 1.00 40.68  ? 843  GLN   A O     1 
ATOM   4317  C  CB    . GLN   A 1 843  ? 149.794 145.817 126.650 1.00 29.43  ? 843  GLN   A CB    1 
ATOM   4318  C  CG    . GLN   A 1 843  ? 150.471 146.692 127.696 1.00 36.84  ? 843  GLN   A CG    1 
ATOM   4319  C  CD    . GLN   A 1 843  ? 151.986 146.681 127.585 1.00 41.77  ? 843  GLN   A CD    1 
ATOM   4320  O  OE1   . GLN   A 1 843  ? 152.630 145.656 127.805 1.00 44.07  ? 843  GLN   A OE1   1 
ATOM   4321  N  NE2   . GLN   A 1 843  ? 152.562 147.827 127.242 1.00 39.39  ? 843  GLN   A NE2   1 
ATOM   4322  N  N     . ARG   A 1 844  ? 148.733 142.995 127.639 1.00 40.66  ? 844  ARG   A N     1 
ATOM   4323  C  CA    . ARG   A 1 844  ? 148.294 142.076 128.682 1.00 43.04  ? 844  ARG   A CA    1 
ATOM   4324  C  C     . ARG   A 1 844  ? 149.166 140.828 128.710 1.00 43.84  ? 844  ARG   A C     1 
ATOM   4325  O  O     . ARG   A 1 844  ? 149.528 140.337 129.786 1.00 40.91  ? 844  ARG   A O     1 
ATOM   4326  C  CB    . ARG   A 1 844  ? 146.826 141.706 128.472 1.00 35.61  ? 844  ARG   A CB    1 
ATOM   4327  N  N     . TRP   A 1 845  ? 149.518 140.304 127.534 1.00 34.25  ? 845  TRP   A N     1 
ATOM   4328  C  CA    . TRP   A 1 845  ? 150.375 139.124 127.477 1.00 31.96  ? 845  TRP   A CA    1 
ATOM   4329  C  C     . TRP   A 1 845  ? 151.733 139.400 128.112 1.00 39.59  ? 845  TRP   A C     1 
ATOM   4330  O  O     . TRP   A 1 845  ? 152.257 138.569 128.862 1.00 45.58  ? 845  TRP   A O     1 
ATOM   4331  C  CB    . TRP   A 1 845  ? 150.537 138.670 126.027 1.00 35.74  ? 845  TRP   A CB    1 
ATOM   4332  C  CG    . TRP   A 1 845  ? 151.428 137.481 125.857 1.00 40.05  ? 845  TRP   A CG    1 
ATOM   4333  C  CD1   . TRP   A 1 845  ? 151.046 136.173 125.838 1.00 42.73  ? 845  TRP   A CD1   1 
ATOM   4334  C  CD2   . TRP   A 1 845  ? 152.848 137.487 125.665 1.00 44.05  ? 845  TRP   A CD2   1 
ATOM   4335  N  NE1   . TRP   A 1 845  ? 152.138 135.362 125.656 1.00 47.80  ? 845  TRP   A NE1   1 
ATOM   4336  C  CE2   . TRP   A 1 845  ? 153.257 136.145 125.545 1.00 44.66  ? 845  TRP   A CE2   1 
ATOM   4337  C  CE3   . TRP   A 1 845  ? 153.813 138.495 125.586 1.00 42.93  ? 845  TRP   A CE3   1 
ATOM   4338  C  CZ2   . TRP   A 1 845  ? 154.588 135.784 125.352 1.00 39.54  ? 845  TRP   A CZ2   1 
ATOM   4339  C  CZ3   . TRP   A 1 845  ? 155.134 138.135 125.395 1.00 40.56  ? 845  TRP   A CZ3   1 
ATOM   4340  C  CH2   . TRP   A 1 845  ? 155.509 136.792 125.280 1.00 37.23  ? 845  TRP   A CH2   1 
ATOM   4341  N  N     . LEU   A 1 846  ? 152.315 140.564 127.824 1.00 40.16  ? 846  LEU   A N     1 
ATOM   4342  C  CA    . LEU   A 1 846  ? 153.595 140.929 128.422 1.00 34.00  ? 846  LEU   A CA    1 
ATOM   4343  C  C     . LEU   A 1 846  ? 153.477 141.048 129.936 1.00 38.46  ? 846  LEU   A C     1 
ATOM   4344  O  O     . LEU   A 1 846  ? 154.278 140.473 130.681 1.00 45.04  ? 846  LEU   A O     1 
ATOM   4345  C  CB    . LEU   A 1 846  ? 154.099 142.239 127.816 1.00 37.72  ? 846  LEU   A CB    1 
ATOM   4346  C  CG    . LEU   A 1 846  ? 154.779 142.165 126.447 1.00 38.95  ? 846  LEU   A CG    1 
ATOM   4347  C  CD1   . LEU   A 1 846  ? 155.079 143.561 125.922 1.00 34.13  ? 846  LEU   A CD1   1 
ATOM   4348  C  CD2   . LEU   A 1 846  ? 156.046 141.330 126.513 1.00 41.84  ? 846  LEU   A CD2   1 
ATOM   4349  N  N     . ILE   A 1 847  ? 152.474 141.792 130.411 1.00 36.69  ? 847  ILE   A N     1 
ATOM   4350  C  CA    . ILE   A 1 847  ? 152.312 141.982 131.850 1.00 30.28  ? 847  ILE   A CA    1 
ATOM   4351  C  C     . ILE   A 1 847  ? 152.069 140.653 132.549 1.00 32.83  ? 847  ILE   A C     1 
ATOM   4352  O  O     . ILE   A 1 847  ? 152.426 140.484 133.721 1.00 43.87  ? 847  ILE   A O     1 
ATOM   4353  C  CB    . ILE   A 1 847  ? 151.178 142.986 132.136 1.00 36.99  ? 847  ILE   A CB    1 
ATOM   4354  C  CG1   . ILE   A 1 847  ? 151.466 144.323 131.452 1.00 39.30  ? 847  ILE   A CG1   1 
ATOM   4355  C  CG2   . ILE   A 1 847  ? 151.002 143.180 133.632 1.00 34.62  ? 847  ILE   A CG2   1 
ATOM   4356  C  CD1   . ILE   A 1 847  ? 152.256 145.290 132.307 1.00 39.47  ? 847  ILE   A CD1   1 
ATOM   4357  N  N     . LYS   A 1 848  ? 151.464 139.691 131.853 1.00 42.02  ? 848  LYS   A N     1 
ATOM   4358  C  CA    . LYS   A 1 848  ? 151.194 138.387 132.442 1.00 44.52  ? 848  LYS   A CA    1 
ATOM   4359  C  C     . LYS   A 1 848  ? 152.402 137.462 132.425 1.00 46.61  ? 848  LYS   A C     1 
ATOM   4360  O  O     . LYS   A 1 848  ? 152.331 136.369 132.997 1.00 52.45  ? 848  LYS   A O     1 
ATOM   4361  C  CB    . LYS   A 1 848  ? 150.026 137.716 131.716 1.00 37.05  ? 848  LYS   A CB    1 
ATOM   4362  N  N     . ASN   A 1 849  ? 153.503 137.865 131.791 1.00 40.75  ? 849  ASN   A N     1 
ATOM   4363  C  CA    . ASN   A 1 849  ? 154.706 137.044 131.723 1.00 37.78  ? 849  ASN   A CA    1 
ATOM   4364  C  C     . ASN   A 1 849  ? 155.910 137.711 132.374 1.00 46.59  ? 849  ASN   A C     1 
ATOM   4365  O  O     . ASN   A 1 849  ? 157.033 137.215 132.231 1.00 49.79  ? 849  ASN   A O     1 
ATOM   4366  C  CB    . ASN   A 1 849  ? 155.026 136.686 130.270 1.00 41.58  ? 849  ASN   A CB    1 
ATOM   4367  C  CG    . ASN   A 1 849  ? 154.167 135.553 129.748 1.00 50.17  ? 849  ASN   A CG    1 
ATOM   4368  O  OD1   . ASN   A 1 849  ? 153.656 134.742 130.519 1.00 51.78  ? 849  ASN   A OD1   1 
ATOM   4369  N  ND2   . ASN   A 1 849  ? 154.008 135.489 128.433 1.00 48.84  ? 849  ASN   A ND2   1 
ATOM   4370  N  N     . LYS   A 1 850  ? 155.709 138.822 133.082 1.00 43.41  ? 850  LYS   A N     1 
ATOM   4371  C  CA    . LYS   A 1 850  ? 156.770 139.477 133.841 1.00 43.11  ? 850  LYS   A CA    1 
ATOM   4372  C  C     . LYS   A 1 850  ? 157.841 140.083 132.939 1.00 47.71  ? 850  LYS   A C     1 
ATOM   4373  O  O     . LYS   A 1 850  ? 159.005 140.185 133.332 1.00 48.31  ? 850  LYS   A O     1 
ATOM   4374  C  CB    . LYS   A 1 850  ? 157.406 138.509 134.843 1.00 43.49  ? 850  LYS   A CB    1 
ATOM   4375  C  CG    . LYS   A 1 850  ? 156.400 137.767 135.707 1.00 41.79  ? 850  LYS   A CG    1 
ATOM   4376  C  CD    . LYS   A 1 850  ? 156.083 138.540 136.975 1.00 43.75  ? 850  LYS   A CD    1 
ATOM   4377  C  CE    . LYS   A 1 850  ? 154.811 138.029 137.628 1.00 42.93  ? 850  LYS   A CE    1 
ATOM   4378  N  NZ    . LYS   A 1 850  ? 153.589 138.509 136.925 1.00 48.98  ? 850  LYS   A NZ    1 
ATOM   4379  N  N     . MET   A 1 851  ? 157.463 140.490 131.731 1.00 42.12  ? 851  MET   A N     1 
ATOM   4380  C  CA    . MET   A 1 851  ? 158.364 141.177 130.816 1.00 33.01  ? 851  MET   A CA    1 
ATOM   4381  C  C     . MET   A 1 851  ? 158.146 142.678 130.947 1.00 37.72  ? 851  MET   A C     1 
ATOM   4382  O  O     . MET   A 1 851  ? 157.051 143.177 130.667 1.00 47.58  ? 851  MET   A O     1 
ATOM   4383  C  CB    . MET   A 1 851  ? 158.134 140.726 129.375 1.00 30.31  ? 851  MET   A CB    1 
ATOM   4384  C  CG    . MET   A 1 851  ? 158.453 139.266 129.122 1.00 38.96  ? 851  MET   A CG    1 
ATOM   4385  S  SD    . MET   A 1 851  ? 160.141 139.036 128.536 1.00 62.08  ? 851  MET   A SD    1 
ATOM   4386  C  CE    . MET   A 1 851  ? 160.254 137.252 128.530 1.00 42.70  ? 851  MET   A CE    1 
ATOM   4387  N  N     . LYS   A 1 852  ? 159.184 143.391 131.371 1.00 25.59  ? 852  LYS   A N     1 
ATOM   4388  C  CA    . LYS   A 1 852  ? 159.119 144.842 131.538 1.00 27.83  ? 852  LYS   A CA    1 
ATOM   4389  C  C     . LYS   A 1 852  ? 159.358 145.567 130.217 1.00 39.23  ? 852  LYS   A C     1 
ATOM   4390  O  O     . LYS   A 1 852  ? 160.199 146.457 130.110 1.00 46.20  ? 852  LYS   A O     1 
ATOM   4391  C  CB    . LYS   A 1 852  ? 160.120 145.287 132.597 1.00 32.32  ? 852  LYS   A CB    1 
ATOM   4392  C  CG    . LYS   A 1 852  ? 160.122 144.425 133.848 1.00 34.97  ? 852  LYS   A CG    1 
ATOM   4393  C  CD    . LYS   A 1 852  ? 159.287 145.054 134.951 1.00 39.22  ? 852  LYS   A CD    1 
ATOM   4394  C  CE    . LYS   A 1 852  ? 159.159 144.122 136.142 1.00 37.60  ? 852  LYS   A CE    1 
ATOM   4395  N  NZ    . LYS   A 1 852  ? 157.777 144.119 136.692 1.00 40.41  ? 852  LYS   A NZ    1 
ATOM   4396  N  N     . ALA   A 1 853  ? 158.605 145.181 129.194 1.00 25.71  ? 853  ALA   A N     1 
ATOM   4397  C  CA    . ALA   A 1 853  ? 158.721 145.758 127.866 1.00 14.81  ? 853  ALA   A CA    1 
ATOM   4398  C  C     . ALA   A 1 853  ? 157.474 146.562 127.524 1.00 24.34  ? 853  ALA   A C     1 
ATOM   4399  O  O     . ALA   A 1 853  ? 156.416 146.405 128.139 1.00 29.59  ? 853  ALA   A O     1 
ATOM   4400  C  CB    . ALA   A 1 853  ? 158.949 144.669 126.814 1.00 22.46  ? 853  ALA   A CB    1 
ATOM   4401  N  N     . PHE   A 1 854  ? 157.617 147.435 126.533 1.00 22.87  ? 854  PHE   A N     1 
ATOM   4402  C  CA    . PHE   A 1 854  ? 156.520 148.240 126.016 1.00 11.43  ? 854  PHE   A CA    1 
ATOM   4403  C  C     . PHE   A 1 854  ? 156.194 147.794 124.598 1.00 19.02  ? 854  PHE   A C     1 
ATOM   4404  O  O     . PHE   A 1 854  ? 157.081 147.753 123.739 1.00 29.30  ? 854  PHE   A O     1 
ATOM   4405  C  CB    . PHE   A 1 854  ? 156.875 149.728 126.027 1.00 8.92   ? 854  PHE   A CB    1 
ATOM   4406  C  CG    . PHE   A 1 854  ? 157.060 150.297 127.400 1.00 15.97  ? 854  PHE   A CG    1 
ATOM   4407  C  CD1   . PHE   A 1 854  ? 158.253 150.126 128.078 1.00 21.71  ? 854  PHE   A CD1   1 
ATOM   4408  C  CD2   . PHE   A 1 854  ? 156.046 151.011 128.010 1.00 17.72  ? 854  PHE   A CD2   1 
ATOM   4409  C  CE1   . PHE   A 1 854  ? 158.428 150.649 129.342 1.00 18.69  ? 854  PHE   A CE1   1 
ATOM   4410  C  CE2   . PHE   A 1 854  ? 156.215 151.537 129.273 1.00 24.73  ? 854  PHE   A CE2   1 
ATOM   4411  C  CZ    . PHE   A 1 854  ? 157.408 151.356 129.939 1.00 22.31  ? 854  PHE   A CZ    1 
ATOM   4412  N  N     . TYR   A 1 855  ? 154.930 147.457 124.360 1.00 24.71  ? 855  TYR   A N     1 
ATOM   4413  C  CA    . TYR   A 1 855  ? 154.467 147.148 123.015 1.00 18.17  ? 855  TYR   A CA    1 
ATOM   4414  C  C     . TYR   A 1 855  ? 154.302 148.441 122.227 1.00 25.91  ? 855  TYR   A C     1 
ATOM   4415  O  O     . TYR   A 1 855  ? 153.707 149.405 122.719 1.00 32.25  ? 855  TYR   A O     1 
ATOM   4416  C  CB    . TYR   A 1 855  ? 153.148 146.379 123.072 1.00 26.06  ? 855  TYR   A CB    1 
ATOM   4417  C  CG    . TYR   A 1 855  ? 152.676 145.871 121.732 1.00 30.00  ? 855  TYR   A CG    1 
ATOM   4418  C  CD1   . TYR   A 1 855  ? 153.461 145.009 120.980 1.00 28.72  ? 855  TYR   A CD1   1 
ATOM   4419  C  CD2   . TYR   A 1 855  ? 151.446 146.255 121.217 1.00 18.62  ? 855  TYR   A CD2   1 
ATOM   4420  C  CE1   . TYR   A 1 855  ? 153.035 144.544 119.756 1.00 30.91  ? 855  TYR   A CE1   1 
ATOM   4421  C  CE2   . TYR   A 1 855  ? 151.013 145.796 119.993 1.00 17.22  ? 855  TYR   A CE2   1 
ATOM   4422  C  CZ    . TYR   A 1 855  ? 151.810 144.941 119.267 1.00 27.69  ? 855  TYR   A CZ    1 
ATOM   4423  O  OH    . TYR   A 1 855  ? 151.376 144.482 118.047 1.00 41.81  ? 855  TYR   A OH    1 
ATOM   4424  N  N     . ALA   A 1 856  ? 154.831 148.465 121.005 1.00 22.27  ? 856  ALA   A N     1 
ATOM   4425  C  CA    . ALA   A 1 856  ? 154.839 149.664 120.166 1.00 20.61  ? 856  ALA   A CA    1 
ATOM   4426  C  C     . ALA   A 1 856  ? 154.373 149.306 118.762 1.00 27.38  ? 856  ALA   A C     1 
ATOM   4427  O  O     . ALA   A 1 856  ? 155.187 149.184 117.836 1.00 34.03  ? 856  ALA   A O     1 
ATOM   4428  C  CB    . ALA   A 1 856  ? 156.225 150.308 120.140 1.00 24.44  ? 856  ALA   A CB    1 
ATOM   4429  N  N     . PRO   A 1 857  ? 153.069 149.126 118.566 1.00 29.37  ? 857  PRO   A N     1 
ATOM   4430  C  CA    . PRO   A 1 857  ? 152.556 148.883 117.215 1.00 19.17  ? 857  PRO   A CA    1 
ATOM   4431  C  C     . PRO   A 1 857  ? 152.661 150.127 116.348 1.00 23.66  ? 857  PRO   A C     1 
ATOM   4432  O  O     . PRO   A 1 857  ? 152.630 151.259 116.835 1.00 25.93  ? 857  PRO   A O     1 
ATOM   4433  C  CB    . PRO   A 1 857  ? 151.093 148.498 117.459 1.00 16.11  ? 857  PRO   A CB    1 
ATOM   4434  C  CG    . PRO   A 1 857  ? 150.748 149.191 118.734 1.00 21.06  ? 857  PRO   A CG    1 
ATOM   4435  C  CD    . PRO   A 1 857  ? 151.994 149.130 119.573 1.00 24.44  ? 857  PRO   A CD    1 
ATOM   4436  N  N     . VAL   A 1 858  ? 152.782 149.902 115.041 1.00 29.07  ? 858  VAL   A N     1 
ATOM   4437  C  CA    . VAL   A 1 858  ? 152.854 150.988 114.072 1.00 24.66  ? 858  VAL   A CA    1 
ATOM   4438  C  C     . VAL   A 1 858  ? 152.344 150.468 112.736 1.00 22.44  ? 858  VAL   A C     1 
ATOM   4439  O  O     . VAL   A 1 858  ? 152.479 149.283 112.420 1.00 28.89  ? 858  VAL   A O     1 
ATOM   4440  C  CB    . VAL   A 1 858  ? 154.289 151.551 113.945 1.00 25.07  ? 858  VAL   A CB    1 
ATOM   4441  C  CG1   . VAL   A 1 858  ? 155.039 150.855 112.819 1.00 21.99  ? 858  VAL   A CG1   1 
ATOM   4442  C  CG2   . VAL   A 1 858  ? 154.255 153.054 113.733 1.00 22.01  ? 858  VAL   A CG2   1 
ATOM   4443  N  N     . HIS   A 1 859  ? 151.752 151.364 111.950 1.00 25.08  ? 859  HIS   A N     1 
ATOM   4444  C  CA    . HIS   A 1 859  ? 151.166 151.018 110.660 1.00 24.97  ? 859  HIS   A CA    1 
ATOM   4445  C  C     . HIS   A 1 859  ? 151.925 151.735 109.554 1.00 26.26  ? 859  HIS   A C     1 
ATOM   4446  O  O     . HIS   A 1 859  ? 152.046 152.964 109.576 1.00 29.71  ? 859  HIS   A O     1 
ATOM   4447  C  CB    . HIS   A 1 859  ? 149.681 151.384 110.614 1.00 26.96  ? 859  HIS   A CB    1 
ATOM   4448  C  CG    . HIS   A 1 859  ? 149.086 151.318 109.242 1.00 33.32  ? 859  HIS   A CG    1 
ATOM   4449  N  ND1   . HIS   A 1 859  ? 148.663 152.437 108.559 1.00 36.23  ? 859  HIS   A ND1   1 
ATOM   4450  C  CD2   . HIS   A 1 859  ? 148.851 150.266 108.423 1.00 35.45  ? 859  HIS   A CD2   1 
ATOM   4451  C  CE1   . HIS   A 1 859  ? 148.189 152.077 107.380 1.00 34.72  ? 859  HIS   A CE1   1 
ATOM   4452  N  NE2   . HIS   A 1 859  ? 148.293 150.765 107.272 1.00 28.60  ? 859  HIS   A NE2   1 
ATOM   4453  N  N     . ALA   A 1 860  ? 152.425 150.968 108.589 1.00 27.77  ? 860  ALA   A N     1 
ATOM   4454  C  CA    . ALA   A 1 860  ? 153.136 151.520 107.445 1.00 35.63  ? 860  ALA   A CA    1 
ATOM   4455  C  C     . ALA   A 1 860  ? 153.048 150.523 106.300 1.00 35.59  ? 860  ALA   A C     1 
ATOM   4456  O  O     . ALA   A 1 860  ? 152.576 149.396 106.466 1.00 36.20  ? 860  ALA   A O     1 
ATOM   4457  C  CB    . ALA   A 1 860  ? 154.594 151.841 107.788 1.00 36.92  ? 860  ALA   A CB    1 
ATOM   4458  N  N     . ASP   A 1 861  ? 153.516 150.953 105.126 1.00 35.14  ? 861  ASP   A N     1 
ATOM   4459  C  CA    . ASP   A 1 861  ? 153.427 150.102 103.944 1.00 42.32  ? 861  ASP   A CA    1 
ATOM   4460  C  C     . ASP   A 1 861  ? 154.424 148.952 104.005 1.00 39.16  ? 861  ASP   A C     1 
ATOM   4461  O  O     . ASP   A 1 861  ? 154.106 147.827 103.603 1.00 45.49  ? 861  ASP   A O     1 
ATOM   4462  C  CB    . ASP   A 1 861  ? 153.644 150.931 102.680 1.00 49.27  ? 861  ASP   A CB    1 
ATOM   4463  C  CG    . ASP   A 1 861  ? 153.895 152.392 102.980 1.00 55.58  ? 861  ASP   A CG    1 
ATOM   4464  O  OD1   . ASP   A 1 861  ? 154.679 152.679 103.907 1.00 52.73  ? 861  ASP   A OD1   1 
ATOM   4465  O  OD2   . ASP   A 1 861  ? 153.312 153.252 102.287 1.00 54.50  ? 861  ASP   A OD2   1 
ATOM   4466  N  N     . ASP   A 1 862  ? 155.634 149.210 104.494 1.00 42.28  ? 862  ASP   A N     1 
ATOM   4467  C  CA    . ASP   A 1 862  ? 156.669 148.192 104.573 1.00 41.00  ? 862  ASP   A CA    1 
ATOM   4468  C  C     . ASP   A 1 862  ? 157.379 148.277 105.917 1.00 42.69  ? 862  ASP   A C     1 
ATOM   4469  O  O     . ASP   A 1 862  ? 157.282 149.274 106.636 1.00 45.95  ? 862  ASP   A O     1 
ATOM   4470  C  CB    . ASP   A 1 862  ? 157.688 148.328 103.433 1.00 43.92  ? 862  ASP   A CB    1 
ATOM   4471  C  CG    . ASP   A 1 862  ? 158.334 149.696 103.388 1.00 51.33  ? 862  ASP   A CG    1 
ATOM   4472  O  OD1   . ASP   A 1 862  ? 157.690 150.674 103.820 1.00 56.90  ? 862  ASP   A OD1   1 
ATOM   4473  O  OD2   . ASP   A 1 862  ? 159.489 149.794 102.924 1.00 52.42  ? 862  ASP   A OD2   1 
ATOM   4474  N  N     . LEU   A 1 863  ? 158.106 147.206 106.242 1.00 36.49  ? 863  LEU   A N     1 
ATOM   4475  C  CA    . LEU   A 1 863  ? 158.811 147.146 107.517 1.00 32.10  ? 863  LEU   A CA    1 
ATOM   4476  C  C     . LEU   A 1 863  ? 159.856 148.246 107.637 1.00 31.31  ? 863  LEU   A C     1 
ATOM   4477  O  O     . LEU   A 1 863  ? 160.097 148.756 108.738 1.00 36.94  ? 863  LEU   A O     1 
ATOM   4478  C  CB    . LEU   A 1 863  ? 159.461 145.773 107.689 1.00 29.51  ? 863  LEU   A CB    1 
ATOM   4479  C  CG    . LEU   A 1 863  ? 160.662 145.703 108.631 1.00 30.39  ? 863  LEU   A CG    1 
ATOM   4480  C  CD1   . LEU   A 1 863  ? 160.241 146.012 110.056 1.00 34.77  ? 863  LEU   A CD1   1 
ATOM   4481  C  CD2   . LEU   A 1 863  ? 161.327 144.339 108.550 1.00 34.02  ? 863  LEU   A CD2   1 
ATOM   4482  N  N     . ARG   A 1 864  ? 160.487 148.624 106.524 1.00 30.53  ? 864  ARG   A N     1 
ATOM   4483  C  CA    . ARG   A 1 864  ? 161.484 149.688 106.566 1.00 31.51  ? 864  ARG   A CA    1 
ATOM   4484  C  C     . ARG   A 1 864  ? 160.884 150.980 107.103 1.00 39.87  ? 864  ARG   A C     1 
ATOM   4485  O  O     . ARG   A 1 864  ? 161.462 151.632 107.980 1.00 40.19  ? 864  ARG   A O     1 
ATOM   4486  C  CB    . ARG   A 1 864  ? 162.068 149.913 105.173 1.00 34.29  ? 864  ARG   A CB    1 
ATOM   4487  C  CG    . ARG   A 1 864  ? 163.376 149.199 104.911 1.00 42.31  ? 864  ARG   A CG    1 
ATOM   4488  C  CD    . ARG   A 1 864  ? 164.556 149.997 105.429 1.00 41.18  ? 864  ARG   A CD    1 
ATOM   4489  N  NE    . ARG   A 1 864  ? 164.740 151.250 104.706 1.00 42.93  ? 864  ARG   A NE    1 
ATOM   4490  C  CZ    . ARG   A 1 864  ? 165.008 151.341 103.411 1.00 45.84  ? 864  ARG   A CZ    1 
ATOM   4491  N  NH1   . ARG   A 1 864  ? 165.071 150.269 102.639 1.00 47.32  ? 864  ARG   A NH1   1 
ATOM   4492  N  NH2   . ARG   A 1 864  ? 165.211 152.541 102.874 1.00 45.88  ? 864  ARG   A NH2   1 
ATOM   4493  N  N     . GLU   A 1 865  ? 159.713 151.363 106.592 1.00 41.26  ? 865  GLU   A N     1 
ATOM   4494  C  CA    . GLU   A 1 865  ? 159.121 152.637 106.983 1.00 42.00  ? 865  GLU   A CA    1 
ATOM   4495  C  C     . GLU   A 1 865  ? 158.630 152.602 108.426 1.00 34.54  ? 865  GLU   A C     1 
ATOM   4496  O  O     . GLU   A 1 865  ? 158.729 153.603 109.144 1.00 35.08  ? 865  GLU   A O     1 
ATOM   4497  C  CB    . GLU   A 1 865  ? 157.988 152.999 106.024 1.00 38.12  ? 865  GLU   A CB    1 
ATOM   4498  C  CG    . GLU   A 1 865  ? 157.199 154.227 106.425 1.00 39.60  ? 865  GLU   A CG    1 
ATOM   4499  C  CD    . GLU   A 1 865  ? 156.327 154.748 105.301 1.00 50.88  ? 865  GLU   A CD    1 
ATOM   4500  O  OE1   . GLU   A 1 865  ? 156.883 155.205 104.281 1.00 52.99  ? 865  GLU   A OE1   1 
ATOM   4501  O  OE2   . GLU   A 1 865  ? 155.086 154.707 105.438 1.00 48.00  ? 865  GLU   A OE2   1 
ATOM   4502  N  N     . GLY   A 1 866  ? 158.100 151.463 108.872 1.00 23.40  ? 866  GLY   A N     1 
ATOM   4503  C  CA    . GLY   A 1 866  ? 157.702 151.349 110.266 1.00 25.83  ? 866  GLY   A CA    1 
ATOM   4504  C  C     . GLY   A 1 866  ? 158.883 151.427 111.215 1.00 29.29  ? 866  GLY   A C     1 
ATOM   4505  O  O     . GLY   A 1 866  ? 158.820 152.099 112.251 1.00 34.80  ? 866  GLY   A O     1 
ATOM   4506  N  N     . ALA   A 1 867  ? 159.977 150.739 110.878 1.00 30.93  ? 867  ALA   A N     1 
ATOM   4507  C  CA    . ALA   A 1 867  ? 161.191 150.861 111.674 1.00 19.18  ? 867  ALA   A CA    1 
ATOM   4508  C  C     . ALA   A 1 867  ? 161.716 152.288 111.667 1.00 18.26  ? 867  ALA   A C     1 
ATOM   4509  O  O     . ALA   A 1 867  ? 162.249 152.758 112.676 1.00 21.90  ? 867  ALA   A O     1 
ATOM   4510  C  CB    . ALA   A 1 867  ? 162.257 149.894 111.161 1.00 22.95  ? 867  ALA   A CB    1 
ATOM   4511  N  N     . GLN   A 1 868  ? 161.586 152.988 110.538 1.00 21.56  ? 868  GLN   A N     1 
ATOM   4512  C  CA    . GLN   A 1 868  ? 161.956 154.399 110.492 1.00 16.24  ? 868  GLN   A CA    1 
ATOM   4513  C  C     . GLN   A 1 868  ? 161.110 155.210 111.465 1.00 23.44  ? 868  GLN   A C     1 
ATOM   4514  O  O     . GLN   A 1 868  ? 161.632 156.025 112.235 1.00 20.53  ? 868  GLN   A O     1 
ATOM   4515  C  CB    . GLN   A 1 868  ? 161.798 154.929 109.067 1.00 15.47  ? 868  GLN   A CB    1 
ATOM   4516  C  CG    . GLN   A 1 868  ? 162.482 156.260 108.799 1.00 25.28  ? 868  GLN   A CG    1 
ATOM   4517  C  CD    . GLN   A 1 868  ? 163.920 156.288 109.268 1.00 39.42  ? 868  GLN   A CD    1 
ATOM   4518  O  OE1   . GLN   A 1 868  ? 164.587 155.255 109.324 1.00 37.05  ? 868  GLN   A OE1   1 
ATOM   4519  N  NE2   . GLN   A 1 868  ? 164.410 157.475 109.603 1.00 32.75  ? 868  GLN   A NE2   1 
ATOM   4520  N  N     . TYR   A 1 869  ? 159.793 154.991 111.442 1.00 30.14  ? 869  TYR   A N     1 
ATOM   4521  C  CA    . TYR   A 1 869  ? 158.905 155.644 112.398 1.00 13.22  ? 869  TYR   A CA    1 
ATOM   4522  C  C     . TYR   A 1 869  ? 159.402 155.431 113.819 1.00 17.86  ? 869  TYR   A C     1 
ATOM   4523  O  O     . TYR   A 1 869  ? 159.551 156.382 114.596 1.00 27.70  ? 869  TYR   A O     1 
ATOM   4524  C  CB    . TYR   A 1 869  ? 157.482 155.089 112.271 1.00 21.56  ? 869  TYR   A CB    1 
ATOM   4525  C  CG    . TYR   A 1 869  ? 156.763 155.364 110.970 1.00 25.94  ? 869  TYR   A CG    1 
ATOM   4526  C  CD1   . TYR   A 1 869  ? 157.333 156.151 109.984 1.00 25.54  ? 869  TYR   A CD1   1 
ATOM   4527  C  CD2   . TYR   A 1 869  ? 155.502 154.831 110.735 1.00 24.14  ? 869  TYR   A CD2   1 
ATOM   4528  C  CE1   . TYR   A 1 869  ? 156.667 156.400 108.800 1.00 31.73  ? 869  TYR   A CE1   1 
ATOM   4529  C  CE2   . TYR   A 1 869  ? 154.831 155.074 109.556 1.00 26.09  ? 869  TYR   A CE2   1 
ATOM   4530  C  CZ    . TYR   A 1 869  ? 155.416 155.859 108.592 1.00 31.52  ? 869  TYR   A CZ    1 
ATOM   4531  O  OH    . TYR   A 1 869  ? 154.749 156.102 107.415 1.00 29.53  ? 869  TYR   A OH    1 
ATOM   4532  N  N     . LEU   A 1 870  ? 159.667 154.172 114.169 1.00 15.11  ? 870  LEU   A N     1 
ATOM   4533  C  CA    . LEU   A 1 870  ? 160.035 153.839 115.541 1.00 15.53  ? 870  LEU   A CA    1 
ATOM   4534  C  C     . LEU   A 1 870  ? 161.365 154.474 115.930 1.00 22.98  ? 870  LEU   A C     1 
ATOM   4535  O  O     . LEU   A 1 870  ? 161.477 155.104 116.988 1.00 22.24  ? 870  LEU   A O     1 
ATOM   4536  C  CB    . LEU   A 1 870  ? 160.080 152.322 115.714 1.00 19.53  ? 870  LEU   A CB    1 
ATOM   4537  C  CG    . LEU   A 1 870  ? 158.715 151.638 115.641 1.00 21.53  ? 870  LEU   A CG    1 
ATOM   4538  C  CD1   . LEU   A 1 870  ? 158.863 150.129 115.576 1.00 24.79  ? 870  LEU   A CD1   1 
ATOM   4539  C  CD2   . LEU   A 1 870  ? 157.857 152.043 116.829 1.00 19.31  ? 870  LEU   A CD2   1 
ATOM   4540  N  N     . MET   A 1 871  ? 162.389 154.325 115.086 1.00 22.74  ? 871  MET   A N     1 
ATOM   4541  C  CA    . MET   A 1 871  ? 163.695 154.886 115.406 1.00 12.38  ? 871  MET   A CA    1 
ATOM   4542  C  C     . MET   A 1 871  ? 163.694 156.407 115.392 1.00 22.26  ? 871  MET   A C     1 
ATOM   4543  O  O     . MET   A 1 871  ? 164.611 157.017 115.950 1.00 34.96  ? 871  MET   A O     1 
ATOM   4544  C  CB    . MET   A 1 871  ? 164.760 154.363 114.438 1.00 17.86  ? 871  MET   A CB    1 
ATOM   4545  C  CG    . MET   A 1 871  ? 165.029 152.870 114.545 1.00 28.12  ? 871  MET   A CG    1 
ATOM   4546  S  SD    . MET   A 1 871  ? 165.910 152.199 113.118 1.00 37.16  ? 871  MET   A SD    1 
ATOM   4547  C  CE    . MET   A 1 871  ? 165.054 153.002 111.767 1.00 27.66  ? 871  MET   A CE    1 
ATOM   4548  N  N     . GLN   A 1 872  ? 162.698 157.035 114.771 1.00 26.20  ? 872  GLN   A N     1 
ATOM   4549  C  CA    . GLN   A 1 872  ? 162.643 158.490 114.780 1.00 20.20  ? 872  GLN   A CA    1 
ATOM   4550  C  C     . GLN   A 1 872  ? 161.849 159.047 115.954 1.00 31.14  ? 872  GLN   A C     1 
ATOM   4551  O  O     . GLN   A 1 872  ? 162.221 160.086 116.510 1.00 34.38  ? 872  GLN   A O     1 
ATOM   4552  C  CB    . GLN   A 1 872  ? 162.044 159.002 113.468 1.00 18.22  ? 872  GLN   A CB    1 
ATOM   4553  C  CG    . GLN   A 1 872  ? 162.883 158.704 112.245 1.00 24.19  ? 872  GLN   A CG    1 
ATOM   4554  C  CD    . GLN   A 1 872  ? 164.075 159.630 112.121 1.00 25.19  ? 872  GLN   A CD    1 
ATOM   4555  O  OE1   . GLN   A 1 872  ? 163.926 160.850 112.076 1.00 26.68  ? 872  GLN   A OE1   1 
ATOM   4556  N  NE2   . GLN   A 1 872  ? 165.267 159.053 112.067 1.00 27.55  ? 872  GLN   A NE2   1 
ATOM   4557  N  N     . ALA   A 1 873  ? 160.766 158.382 116.353 1.00 20.89  ? 873  ALA   A N     1 
ATOM   4558  C  CA    . ALA   A 1 873  ? 159.822 158.981 117.286 1.00 13.03  ? 873  ALA   A CA    1 
ATOM   4559  C  C     . ALA   A 1 873  ? 159.611 158.201 118.574 1.00 22.21  ? 873  ALA   A C     1 
ATOM   4560  O  O     . ALA   A 1 873  ? 159.292 158.815 119.594 1.00 27.60  ? 873  ALA   A O     1 
ATOM   4561  C  CB    . ALA   A 1 873  ? 158.459 159.179 116.607 1.00 22.08  ? 873  ALA   A CB    1 
ATOM   4562  N  N     . ALA   A 1 874  ? 159.774 156.880 118.564 1.00 20.20  ? 874  ALA   A N     1 
ATOM   4563  C  CA    . ALA   A 1 874  ? 159.455 156.083 119.742 1.00 10.48  ? 874  ALA   A CA    1 
ATOM   4564  C  C     . ALA   A 1 874  ? 160.222 156.581 120.959 1.00 19.69  ? 874  ALA   A C     1 
ATOM   4565  O  O     . ALA   A 1 874  ? 161.431 156.820 120.892 1.00 40.94  ? 874  ALA   A O     1 
ATOM   4566  C  CB    . ALA   A 1 874  ? 159.773 154.611 119.485 1.00 5.41   ? 874  ALA   A CB    1 
ATOM   4567  N  N     . GLY   A 1 875  ? 159.517 156.738 122.070 1.00 17.44  ? 875  GLY   A N     1 
ATOM   4568  C  CA    . GLY   A 1 875  ? 160.116 157.150 123.323 1.00 22.24  ? 875  GLY   A CA    1 
ATOM   4569  C  C     . GLY   A 1 875  ? 159.558 158.473 123.818 1.00 24.85  ? 875  GLY   A C     1 
ATOM   4570  O  O     . GLY   A 1 875  ? 158.898 159.220 123.099 1.00 23.99  ? 875  GLY   A O     1 
ATOM   4571  N  N     . LEU   A 1 876  ? 159.845 158.743 125.090 1.00 24.33  ? 876  LEU   A N     1 
ATOM   4572  C  CA    . LEU   A 1 876  ? 159.433 159.977 125.748 1.00 24.27  ? 876  LEU   A CA    1 
ATOM   4573  C  C     . LEU   A 1 876  ? 160.652 160.634 126.373 1.00 28.35  ? 876  LEU   A C     1 
ATOM   4574  O  O     . LEU   A 1 876  ? 161.341 160.016 127.191 1.00 36.81  ? 876  LEU   A O     1 
ATOM   4575  C  CB    . LEU   A 1 876  ? 158.366 159.709 126.813 1.00 27.85  ? 876  LEU   A CB    1 
ATOM   4576  C  CG    . LEU   A 1 876  ? 157.563 160.928 127.269 1.00 27.62  ? 876  LEU   A CG    1 
ATOM   4577  C  CD1   . LEU   A 1 876  ? 157.063 161.721 126.073 1.00 27.49  ? 876  LEU   A CD1   1 
ATOM   4578  C  CD2   . LEU   A 1 876  ? 156.408 160.510 128.158 1.00 30.03  ? 876  LEU   A CD2   1 
ATOM   4579  N  N     . GLY   A 1 877  ? 160.911 161.878 125.995 1.00 30.62  ? 877  GLY   A N     1 
ATOM   4580  C  CA    . GLY   A 1 877  ? 162.005 162.623 126.595 1.00 34.07  ? 877  GLY   A CA    1 
ATOM   4581  C  C     . GLY   A 1 877  ? 163.319 161.873 126.492 1.00 33.07  ? 877  GLY   A C     1 
ATOM   4582  O  O     . GLY   A 1 877  ? 163.819 161.589 125.397 1.00 38.39  ? 877  GLY   A O     1 
ATOM   4583  N  N     . ARG   A 1 878  ? 163.893 161.548 127.647 1.00 37.34  ? 878  ARG   A N     1 
ATOM   4584  C  CA    . ARG   A 1 878  ? 165.176 160.866 127.722 1.00 36.62  ? 878  ARG   A CA    1 
ATOM   4585  C  C     . ARG   A 1 878  ? 165.041 159.351 127.772 1.00 33.47  ? 878  ARG   A C     1 
ATOM   4586  O  O     . ARG   A 1 878  ? 166.060 158.653 127.776 1.00 32.78  ? 878  ARG   A O     1 
ATOM   4587  C  CB    . ARG   A 1 878  ? 165.958 161.354 128.944 1.00 25.52  ? 878  ARG   A CB    1 
ATOM   4588  C  CG    . ARG   A 1 878  ? 167.263 162.043 128.595 1.00 33.33  ? 878  ARG   A CG    1 
ATOM   4589  C  CD    . ARG   A 1 878  ? 167.944 162.611 129.824 1.00 40.48  ? 878  ARG   A CD    1 
ATOM   4590  N  NE    . ARG   A 1 878  ? 168.097 164.058 129.735 1.00 46.21  ? 878  ARG   A NE    1 
ATOM   4591  C  CZ    . ARG   A 1 878  ? 168.851 164.679 128.838 1.00 47.26  ? 878  ARG   A CZ    1 
ATOM   4592  N  NH1   . ARG   A 1 878  ? 169.525 164.008 127.919 1.00 48.49  ? 878  ARG   A NH1   1 
ATOM   4593  N  NH2   . ARG   A 1 878  ? 168.928 166.006 128.862 1.00 44.67  ? 878  ARG   A NH2   1 
ATOM   4594  N  N     . MET   A 1 879  ? 163.818 158.827 127.814 1.00 25.60  ? 879  MET   A N     1 
ATOM   4595  C  CA    . MET   A 1 879  ? 163.594 157.384 127.756 1.00 26.30  ? 879  MET   A CA    1 
ATOM   4596  C  C     . MET   A 1 879  ? 163.315 156.957 126.313 1.00 35.31  ? 879  MET   A C     1 
ATOM   4597  O  O     . MET   A 1 879  ? 162.221 156.526 125.953 1.00 39.49  ? 879  MET   A O     1 
ATOM   4598  C  CB    . MET   A 1 879  ? 162.457 156.987 128.689 1.00 27.21  ? 879  MET   A CB    1 
ATOM   4599  C  CG    . MET   A 1 879  ? 162.675 155.664 129.405 1.00 30.73  ? 879  MET   A CG    1 
ATOM   4600  S  SD    . MET   A 1 879  ? 161.529 155.390 130.771 1.00 57.77  ? 879  MET   A SD    1 
ATOM   4601  C  CE    . MET   A 1 879  ? 161.006 157.065 131.126 1.00 36.17  ? 879  MET   A CE    1 
ATOM   4602  N  N     . LYS   A 1 880  ? 164.346 157.089 125.481 1.00 33.42  ? 880  LYS   A N     1 
ATOM   4603  C  CA    . LYS   A 1 880  ? 164.234 156.817 124.059 1.00 21.77  ? 880  LYS   A CA    1 
ATOM   4604  C  C     . LYS   A 1 880  ? 165.267 155.784 123.628 1.00 21.75  ? 880  LYS   A C     1 
ATOM   4605  O  O     . LYS   A 1 880  ? 166.389 155.766 124.142 1.00 23.01  ? 880  LYS   A O     1 
ATOM   4606  C  CB    . LYS   A 1 880  ? 164.421 158.097 123.234 1.00 23.65  ? 880  LYS   A CB    1 
ATOM   4607  C  CG    . LYS   A 1 880  ? 165.814 158.696 123.324 1.00 20.85  ? 880  LYS   A CG    1 
ATOM   4608  C  CD    . LYS   A 1 880  ? 165.941 159.943 122.467 1.00 32.76  ? 880  LYS   A CD    1 
ATOM   4609  C  CE    . LYS   A 1 880  ? 165.592 159.654 121.019 1.00 35.18  ? 880  LYS   A CE    1 
ATOM   4610  N  NZ    . LYS   A 1 880  ? 166.165 158.360 120.558 1.00 36.39  ? 880  LYS   A NZ    1 
ATOM   4611  N  N     . PRO   A 1 881  ? 164.916 154.914 122.682 1.00 31.16  ? 881  PRO   A N     1 
ATOM   4612  C  CA    . PRO   A 1 881  ? 165.841 153.849 122.283 1.00 27.36  ? 881  PRO   A CA    1 
ATOM   4613  C  C     . PRO   A 1 881  ? 167.136 154.409 121.718 1.00 18.91  ? 881  PRO   A C     1 
ATOM   4614  O  O     . PRO   A 1 881  ? 167.162 155.461 121.077 1.00 23.47  ? 881  PRO   A O     1 
ATOM   4615  C  CB    . PRO   A 1 881  ? 165.060 153.079 121.212 1.00 13.43  ? 881  PRO   A CB    1 
ATOM   4616  C  CG    . PRO   A 1 881  ? 163.635 153.384 121.465 1.00 16.39  ? 881  PRO   A CG    1 
ATOM   4617  C  CD    . PRO   A 1 881  ? 163.565 154.731 122.124 1.00 19.00  ? 881  PRO   A CD    1 
ATOM   4618  N  N     . ASN   A 1 882  ? 168.224 153.684 121.972 1.00 27.45  ? 882  ASN   A N     1 
ATOM   4619  C  CA    . ASN   A 1 882  ? 169.505 153.951 121.338 1.00 10.88  ? 882  ASN   A CA    1 
ATOM   4620  C  C     . ASN   A 1 882  ? 170.097 152.727 120.662 1.00 9.10   ? 882  ASN   A C     1 
ATOM   4621  O  O     . ASN   A 1 882  ? 171.150 152.844 120.028 1.00 22.80  ? 882  ASN   A O     1 
ATOM   4622  C  CB    . ASN   A 1 882  ? 170.517 154.501 122.357 1.00 19.25  ? 882  ASN   A CB    1 
ATOM   4623  C  CG    . ASN   A 1 882  ? 170.740 153.563 123.529 1.00 18.14  ? 882  ASN   A CG    1 
ATOM   4624  O  OD1   . ASN   A 1 882  ? 170.774 152.343 123.371 1.00 24.09  ? 882  ASN   A OD1   1 
ATOM   4625  N  ND2   . ASN   A 1 882  ? 170.895 154.133 124.716 1.00 15.57  ? 882  ASN   A ND2   1 
ATOM   4626  N  N     . THR   A 1 883  ? 169.460 151.566 120.775 1.00 18.27  ? 883  THR   A N     1 
ATOM   4627  C  CA    . THR   A 1 883  ? 169.933 150.332 120.173 1.00 14.21  ? 883  THR   A CA    1 
ATOM   4628  C  C     . THR   A 1 883  ? 168.790 149.686 119.406 1.00 17.08  ? 883  THR   A C     1 
ATOM   4629  O  O     . THR   A 1 883  ? 167.643 149.702 119.859 1.00 28.07  ? 883  THR   A O     1 
ATOM   4630  C  CB    . THR   A 1 883  ? 170.463 149.360 121.237 1.00 22.02  ? 883  THR   A CB    1 
ATOM   4631  O  OG1   . THR   A 1 883  ? 171.496 149.998 121.996 1.00 22.92  ? 883  THR   A OG1   1 
ATOM   4632  C  CG2   . THR   A 1 883  ? 171.023 148.106 120.588 1.00 15.88  ? 883  THR   A CG2   1 
ATOM   4633  N  N     . LEU   A 1 884  ? 169.107 149.134 118.241 1.00 12.11  ? 884  LEU   A N     1 
ATOM   4634  C  CA    . LEU   A 1 884  ? 168.160 148.403 117.412 1.00 10.77  ? 884  LEU   A CA    1 
ATOM   4635  C  C     . LEU   A 1 884  ? 168.516 146.924 117.471 1.00 15.38  ? 884  LEU   A C     1 
ATOM   4636  O  O     . LEU   A 1 884  ? 169.651 146.542 117.158 1.00 24.16  ? 884  LEU   A O     1 
ATOM   4637  C  CB    . LEU   A 1 884  ? 168.188 148.915 115.971 1.00 20.43  ? 884  LEU   A CB    1 
ATOM   4638  C  CG    . LEU   A 1 884  ? 167.041 148.505 115.046 1.00 25.68  ? 884  LEU   A CG    1 
ATOM   4639  C  CD1   . LEU   A 1 884  ? 167.223 147.083 114.558 1.00 23.54  ? 884  LEU   A CD1   1 
ATOM   4640  C  CD2   . LEU   A 1 884  ? 165.705 148.665 115.751 1.00 23.20  ? 884  LEU   A CD2   1 
ATOM   4641  N  N     . VAL   A 1 885  ? 167.554 146.098 117.872 1.00 17.50  ? 885  VAL   A N     1 
ATOM   4642  C  CA    . VAL   A 1 885  ? 167.753 144.665 118.040 1.00 23.80  ? 885  VAL   A CA    1 
ATOM   4643  C  C     . VAL   A 1 885  ? 166.927 143.937 116.991 1.00 26.48  ? 885  VAL   A C     1 
ATOM   4644  O  O     . VAL   A 1 885  ? 165.724 144.193 116.845 1.00 27.57  ? 885  VAL   A O     1 
ATOM   4645  C  CB    . VAL   A 1 885  ? 167.373 144.204 119.457 1.00 19.81  ? 885  VAL   A CB    1 
ATOM   4646  C  CG1   . VAL   A 1 885  ? 167.671 142.724 119.633 1.00 15.82  ? 885  VAL   A CG1   1 
ATOM   4647  C  CG2   . VAL   A 1 885  ? 168.113 145.025 120.493 1.00 15.53  ? 885  VAL   A CG2   1 
ATOM   4648  N  N     . LEU   A 1 886  ? 167.580 143.046 116.250 1.00 22.95  ? 886  LEU   A N     1 
ATOM   4649  C  CA    . LEU   A 1 886  ? 166.921 142.204 115.265 1.00 18.96  ? 886  LEU   A CA    1 
ATOM   4650  C  C     . LEU   A 1 886  ? 167.270 140.746 115.517 1.00 21.51  ? 886  LEU   A C     1 
ATOM   4651  O  O     . LEU   A 1 886  ? 168.291 140.422 116.129 1.00 33.71  ? 886  LEU   A O     1 
ATOM   4652  C  CB    . LEU   A 1 886  ? 167.311 142.585 113.830 1.00 14.16  ? 886  LEU   A CB    1 
ATOM   4653  C  CG    . LEU   A 1 886  ? 167.351 144.072 113.480 1.00 23.30  ? 886  LEU   A CG    1 
ATOM   4654  C  CD1   . LEU   A 1 886  ? 168.290 144.336 112.316 1.00 26.87  ? 886  LEU   A CD1   1 
ATOM   4655  C  CD2   . LEU   A 1 886  ? 165.953 144.554 113.151 1.00 29.15  ? 886  LEU   A CD2   1 
ATOM   4656  N  N     . GLY   A 1 887  ? 166.392 139.869 115.048 1.00 24.99  ? 887  GLY   A N     1 
ATOM   4657  C  CA    . GLY   A 1 887  ? 166.660 138.448 115.009 1.00 28.55  ? 887  GLY   A CA    1 
ATOM   4658  C  C     . GLY   A 1 887  ? 167.134 138.050 113.625 1.00 33.82  ? 887  GLY   A C     1 
ATOM   4659  O  O     . GLY   A 1 887  ? 166.711 138.620 112.622 1.00 44.17  ? 887  GLY   A O     1 
ATOM   4660  N  N     . PHE   A 1 888  ? 168.025 137.064 113.579 1.00 36.84  ? 888  PHE   A N     1 
ATOM   4661  C  CA    . PHE   A 1 888  ? 168.583 136.633 112.306 1.00 30.59  ? 888  PHE   A CA    1 
ATOM   4662  C  C     . PHE   A 1 888  ? 167.480 136.145 111.378 1.00 38.49  ? 888  PHE   A C     1 
ATOM   4663  O  O     . PHE   A 1 888  ? 166.593 135.390 111.785 1.00 43.62  ? 888  PHE   A O     1 
ATOM   4664  C  CB    . PHE   A 1 888  ? 169.615 135.527 112.524 1.00 34.58  ? 888  PHE   A CB    1 
ATOM   4665  C  CG    . PHE   A 1 888  ? 170.411 135.194 111.295 1.00 38.90  ? 888  PHE   A CG    1 
ATOM   4666  C  CD1   . PHE   A 1 888  ? 171.403 136.047 110.844 1.00 36.93  ? 888  PHE   A CD1   1 
ATOM   4667  C  CD2   . PHE   A 1 888  ? 170.160 134.034 110.584 1.00 38.57  ? 888  PHE   A CD2   1 
ATOM   4668  C  CE1   . PHE   A 1 888  ? 172.135 135.744 109.713 1.00 41.08  ? 888  PHE   A CE1   1 
ATOM   4669  C  CE2   . PHE   A 1 888  ? 170.889 133.728 109.451 1.00 38.57  ? 888  PHE   A CE2   1 
ATOM   4670  C  CZ    . PHE   A 1 888  ? 171.876 134.584 109.015 1.00 37.08  ? 888  PHE   A CZ    1 
ATOM   4671  N  N     . LYS   A 1 889  ? 167.540 136.582 110.120 1.00 34.87  ? 889  LYS   A N     1 
ATOM   4672  C  CA    . LYS   A 1 889  ? 166.585 136.147 109.104 1.00 29.27  ? 889  LYS   A CA    1 
ATOM   4673  C  C     . LYS   A 1 889  ? 166.957 134.722 108.707 1.00 37.55  ? 889  LYS   A C     1 
ATOM   4674  O  O     . LYS   A 1 889  ? 167.657 134.470 107.723 1.00 46.22  ? 889  LYS   A O     1 
ATOM   4675  C  CB    . LYS   A 1 889  ? 166.596 137.097 107.914 1.00 34.31  ? 889  LYS   A CB    1 
ATOM   4676  C  CG    . LYS   A 1 889  ? 165.349 137.033 107.052 1.00 42.88  ? 889  LYS   A CG    1 
ATOM   4677  C  CD    . LYS   A 1 889  ? 165.086 138.366 106.369 1.00 41.84  ? 889  LYS   A CD    1 
ATOM   4678  C  CE    . LYS   A 1 889  ? 163.912 138.271 105.412 1.00 35.68  ? 889  LYS   A CE    1 
ATOM   4679  N  NZ    . LYS   A 1 889  ? 163.031 137.119 105.741 1.00 37.81  ? 889  LYS   A NZ    1 
ATOM   4680  N  N     . LYS   A 1 890  ? 166.475 133.769 109.507 1.00 36.77  ? 890  LYS   A N     1 
ATOM   4681  C  CA    . LYS   A 1 890  ? 166.850 132.373 109.320 1.00 43.37  ? 890  LYS   A CA    1 
ATOM   4682  C  C     . LYS   A 1 890  ? 166.353 131.807 107.997 1.00 53.22  ? 890  LYS   A C     1 
ATOM   4683  O  O     . LYS   A 1 890  ? 166.901 130.807 107.521 1.00 55.63  ? 890  LYS   A O     1 
ATOM   4684  C  CB    . LYS   A 1 890  ? 166.317 131.530 110.479 1.00 41.33  ? 890  LYS   A CB    1 
ATOM   4685  C  CG    . LYS   A 1 890  ? 166.768 132.008 111.849 1.00 52.36  ? 890  LYS   A CG    1 
ATOM   4686  C  CD    . LYS   A 1 890  ? 167.079 130.845 112.776 1.00 51.16  ? 890  LYS   A CD    1 
ATOM   4687  C  CE    . LYS   A 1 890  ? 168.488 130.323 112.543 1.00 54.46  ? 890  LYS   A CE    1 
ATOM   4688  N  NZ    . LYS   A 1 890  ? 169.286 130.296 113.800 1.00 49.91  ? 890  LYS   A NZ    1 
ATOM   4689  N  N     . ASP   A 1 891  ? 165.333 132.416 107.397 1.00 51.71  ? 891  ASP   A N     1 
ATOM   4690  C  CA    . ASP   A 1 891  ? 164.760 131.946 106.144 1.00 49.97  ? 891  ASP   A CA    1 
ATOM   4691  C  C     . ASP   A 1 891  ? 165.225 132.759 104.942 1.00 50.09  ? 891  ASP   A C     1 
ATOM   4692  O  O     . ASP   A 1 891  ? 164.630 132.648 103.866 1.00 53.60  ? 891  ASP   A O     1 
ATOM   4693  C  CB    . ASP   A 1 891  ? 163.233 131.963 106.229 1.00 53.86  ? 891  ASP   A CB    1 
ATOM   4694  C  CG    . ASP   A 1 891  ? 162.685 133.341 106.539 1.00 54.97  ? 891  ASP   A CG    1 
ATOM   4695  O  OD1   . ASP   A 1 891  ? 163.493 134.275 106.719 1.00 52.77  ? 891  ASP   A OD1   1 
ATOM   4696  O  OD2   . ASP   A 1 891  ? 161.447 133.490 106.604 1.00 60.58  ? 891  ASP   A OD2   1 
ATOM   4697  N  N     . TRP   A 1 892  ? 166.270 133.574 105.100 1.00 41.45  ? 892  TRP   A N     1 
ATOM   4698  C  CA    . TRP   A 1 892  ? 166.705 134.433 104.004 1.00 40.61  ? 892  TRP   A CA    1 
ATOM   4699  C  C     . TRP   A 1 892  ? 167.078 133.626 102.767 1.00 40.41  ? 892  TRP   A C     1 
ATOM   4700  O  O     . TRP   A 1 892  ? 166.939 134.119 101.642 1.00 42.95  ? 892  TRP   A O     1 
ATOM   4701  C  CB    . TRP   A 1 892  ? 167.884 135.297 104.450 1.00 39.42  ? 892  TRP   A CB    1 
ATOM   4702  C  CG    . TRP   A 1 892  ? 169.205 134.598 104.375 1.00 42.76  ? 892  TRP   A CG    1 
ATOM   4703  C  CD1   . TRP   A 1 892  ? 169.748 133.769 105.312 1.00 45.32  ? 892  TRP   A CD1   1 
ATOM   4704  C  CD2   . TRP   A 1 892  ? 170.152 134.668 103.303 1.00 41.91  ? 892  TRP   A CD2   1 
ATOM   4705  N  NE1   . TRP   A 1 892  ? 170.974 133.318 104.890 1.00 48.91  ? 892  TRP   A NE1   1 
ATOM   4706  C  CE2   . TRP   A 1 892  ? 171.246 133.855 103.660 1.00 39.60  ? 892  TRP   A CE2   1 
ATOM   4707  C  CE3   . TRP   A 1 892  ? 170.182 135.339 102.077 1.00 42.83  ? 892  TRP   A CE3   1 
ATOM   4708  C  CZ2   . TRP   A 1 892  ? 172.356 133.695 102.835 1.00 40.87  ? 892  TRP   A CZ2   1 
ATOM   4709  C  CZ3   . TRP   A 1 892  ? 171.285 135.179 101.261 1.00 46.16  ? 892  TRP   A CZ3   1 
ATOM   4710  C  CH2   . TRP   A 1 892  ? 172.357 134.364 101.643 1.00 45.54  ? 892  TRP   A CH2   1 
ATOM   4711  N  N     . LEU   A 1 893  ? 167.551 132.392 102.948 1.00 49.47  ? 893  LEU   A N     1 
ATOM   4712  C  CA    . LEU   A 1 893  ? 167.902 131.568 101.796 1.00 48.26  ? 893  LEU   A CA    1 
ATOM   4713  C  C     . LEU   A 1 893  ? 166.684 131.297 100.923 1.00 46.76  ? 893  LEU   A C     1 
ATOM   4714  O  O     . LEU   A 1 893  ? 166.765 131.370 99.691  1.00 50.48  ? 893  LEU   A O     1 
ATOM   4715  C  CB    . LEU   A 1 893  ? 168.535 130.258 102.260 1.00 50.64  ? 893  LEU   A CB    1 
ATOM   4716  C  CG    . LEU   A 1 893  ? 170.063 130.227 102.291 1.00 51.61  ? 893  LEU   A CG    1 
ATOM   4717  C  CD1   . LEU   A 1 893  ? 170.569 128.804 102.138 1.00 53.94  ? 893  LEU   A CD1   1 
ATOM   4718  C  CD2   . LEU   A 1 893  ? 170.636 131.123 101.207 1.00 46.35  ? 893  LEU   A CD2   1 
ATOM   4719  N  N     . GLN   A 1 894  ? 165.549 130.983 101.541 1.00 46.58  ? 894  GLN   A N     1 
ATOM   4720  C  CA    . GLN   A 1 894  ? 164.285 130.781 100.837 1.00 47.20  ? 894  GLN   A CA    1 
ATOM   4721  C  C     . GLN   A 1 894  ? 163.363 131.941 101.203 1.00 46.12  ? 894  GLN   A C     1 
ATOM   4722  O  O     . GLN   A 1 894  ? 162.559 131.858 102.131 1.00 49.08  ? 894  GLN   A O     1 
ATOM   4723  C  CB    . GLN   A 1 894  ? 163.668 129.426 101.197 1.00 45.06  ? 894  GLN   A CB    1 
ATOM   4724  N  N     . ALA   A 1 895  ? 163.489 133.034 100.457 1.00 42.36  ? 895  ALA   A N     1 
ATOM   4725  C  CA    . ALA   A 1 895  ? 162.696 134.231 100.698 1.00 41.54  ? 895  ALA   A CA    1 
ATOM   4726  C  C     . ALA   A 1 895  ? 162.977 135.233 99.592  1.00 49.35  ? 895  ALA   A C     1 
ATOM   4727  O  O     . ALA   A 1 895  ? 164.077 135.264 99.034  1.00 53.78  ? 895  ALA   A O     1 
ATOM   4728  C  CB    . ALA   A 1 895  ? 163.004 134.846 102.068 1.00 43.01  ? 895  ALA   A CB    1 
ATOM   4729  N  N     . ASP   A 1 896  ? 161.974 136.051 99.285  1.00 53.77  ? 896  ASP   A N     1 
ATOM   4730  C  CA    . ASP   A 1 896  ? 162.136 137.063 98.252  1.00 54.14  ? 896  ASP   A CA    1 
ATOM   4731  C  C     . ASP   A 1 896  ? 163.276 138.006 98.611  1.00 53.17  ? 896  ASP   A C     1 
ATOM   4732  O  O     . ASP   A 1 896  ? 163.395 138.460 99.752  1.00 54.10  ? 896  ASP   A O     1 
ATOM   4733  C  CB    . ASP   A 1 896  ? 160.838 137.849 98.070  1.00 51.71  ? 896  ASP   A CB    1 
ATOM   4734  N  N     . MET   A 1 897  ? 164.120 138.305 97.622  1.00 51.08  ? 897  MET   A N     1 
ATOM   4735  C  CA    . MET   A 1 897  ? 165.266 139.170 97.868  1.00 51.60  ? 897  MET   A CA    1 
ATOM   4736  C  C     . MET   A 1 897  ? 164.857 140.582 98.260  1.00 52.36  ? 897  MET   A C     1 
ATOM   4737  O  O     . MET   A 1 897  ? 165.686 141.327 98.793  1.00 57.21  ? 897  MET   A O     1 
ATOM   4738  C  CB    . MET   A 1 897  ? 166.172 139.204 96.639  1.00 53.38  ? 897  MET   A CB    1 
ATOM   4739  C  CG    . MET   A 1 897  ? 167.258 138.146 96.660  1.00 56.99  ? 897  MET   A CG    1 
ATOM   4740  S  SD    . MET   A 1 897  ? 168.477 138.499 97.942  1.00 62.81  ? 897  MET   A SD    1 
ATOM   4741  C  CE    . MET   A 1 897  ? 168.606 136.909 98.751  1.00 52.25  ? 897  MET   A CE    1 
ATOM   4742  N  N     . ARG   A 1 898  ? 163.605 140.969 98.015  1.00 49.21  ? 898  ARG   A N     1 
ATOM   4743  C  CA    . ARG   A 1 898  ? 163.132 142.255 98.512  1.00 49.58  ? 898  ARG   A CA    1 
ATOM   4744  C  C     . ARG   A 1 898  ? 163.128 142.281 100.036 1.00 54.17  ? 898  ARG   A C     1 
ATOM   4745  O  O     . ARG   A 1 898  ? 163.504 143.286 100.649 1.00 57.31  ? 898  ARG   A O     1 
ATOM   4746  C  CB    . ARG   A 1 898  ? 161.738 142.551 97.961  1.00 57.02  ? 898  ARG   A CB    1 
ATOM   4747  C  CG    . ARG   A 1 898  ? 161.449 141.890 96.625  1.00 60.28  ? 898  ARG   A CG    1 
ATOM   4748  C  CD    . ARG   A 1 898  ? 160.325 142.599 95.887  1.00 62.05  ? 898  ARG   A CD    1 
ATOM   4749  N  NE    . ARG   A 1 898  ? 160.367 144.044 96.075  1.00 65.49  ? 898  ARG   A NE    1 
ATOM   4750  C  CZ    . ARG   A 1 898  ? 161.179 144.859 95.416  1.00 65.14  ? 898  ARG   A CZ    1 
ATOM   4751  N  NH1   . ARG   A 1 898  ? 162.035 144.403 94.516  1.00 61.42  ? 898  ARG   A NH1   1 
ATOM   4752  N  NH2   . ARG   A 1 898  ? 161.128 146.165 95.662  1.00 63.41  ? 898  ARG   A NH2   1 
ATOM   4753  N  N     . ASP   A 1 899  ? 162.711 141.180 100.665 1.00 44.12  ? 899  ASP   A N     1 
ATOM   4754  C  CA    . ASP   A 1 899  ? 162.729 141.106 102.123 1.00 47.45  ? 899  ASP   A CA    1 
ATOM   4755  C  C     . ASP   A 1 899  ? 164.151 141.194 102.668 1.00 49.98  ? 899  ASP   A C     1 
ATOM   4756  O  O     . ASP   A 1 899  ? 164.400 141.878 103.668 1.00 47.37  ? 899  ASP   A O     1 
ATOM   4757  C  CB    . ASP   A 1 899  ? 162.054 139.817 102.589 1.00 45.68  ? 899  ASP   A CB    1 
ATOM   4758  N  N     . VAL   A 1 900  ? 165.096 140.498 102.034 1.00 40.13  ? 900  VAL   A N     1 
ATOM   4759  C  CA    . VAL   A 1 900  ? 166.485 140.553 102.484 1.00 30.73  ? 900  VAL   A CA    1 
ATOM   4760  C  C     . VAL   A 1 900  ? 167.050 141.955 102.298 1.00 34.36  ? 900  VAL   A C     1 
ATOM   4761  O  O     . VAL   A 1 900  ? 167.804 142.458 103.143 1.00 47.44  ? 900  VAL   A O     1 
ATOM   4762  C  CB    . VAL   A 1 900  ? 167.326 139.495 101.747 1.00 35.82  ? 900  VAL   A CB    1 
ATOM   4763  C  CG1   . VAL   A 1 900  ? 168.752 139.486 102.273 1.00 42.90  ? 900  VAL   A CG1   1 
ATOM   4764  C  CG2   . VAL   A 1 900  ? 166.692 138.122 101.894 1.00 33.58  ? 900  VAL   A CG2   1 
ATOM   4765  N  N     . ASP   A 1 901  ? 166.713 142.601 101.180 1.00 31.38  ? 901  ASP   A N     1 
ATOM   4766  C  CA    . ASP   A 1 901  ? 167.143 143.978 100.970 1.00 38.19  ? 901  ASP   A CA    1 
ATOM   4767  C  C     . ASP   A 1 901  ? 166.570 144.898 102.037 1.00 42.37  ? 901  ASP   A C     1 
ATOM   4768  O  O     . ASP   A 1 901  ? 167.260 145.797 102.525 1.00 41.12  ? 901  ASP   A O     1 
ATOM   4769  C  CB    . ASP   A 1 901  ? 166.737 144.451 99.575  1.00 38.18  ? 901  ASP   A CB    1 
ATOM   4770  C  CG    . ASP   A 1 901  ? 167.677 145.503 99.020  1.00 48.05  ? 901  ASP   A CG    1 
ATOM   4771  O  OD1   . ASP   A 1 901  ? 167.660 146.643 99.528  1.00 52.94  ? 901  ASP   A OD1   1 
ATOM   4772  O  OD2   . ASP   A 1 901  ? 168.436 145.191 98.079  1.00 55.87  ? 901  ASP   A OD2   1 
ATOM   4773  N  N     . MET   A 1 902  ? 165.307 144.690 102.409 1.00 38.57  ? 902  MET   A N     1 
ATOM   4774  C  CA    . MET   A 1 902  ? 164.702 145.485 103.472 1.00 34.10  ? 902  MET   A CA    1 
ATOM   4775  C  C     . MET   A 1 902  ? 165.405 145.249 104.803 1.00 45.79  ? 902  MET   A C     1 
ATOM   4776  O  O     . MET   A 1 902  ? 165.599 146.182 105.585 1.00 51.87  ? 902  MET   A O     1 
ATOM   4777  C  CB    . MET   A 1 902  ? 163.213 145.160 103.579 1.00 40.26  ? 902  MET   A CB    1 
ATOM   4778  C  CG    . MET   A 1 902  ? 162.396 146.189 104.340 1.00 47.55  ? 902  MET   A CG    1 
ATOM   4779  S  SD    . MET   A 1 902  ? 160.989 146.779 103.383 1.00 52.35  ? 902  MET   A SD    1 
ATOM   4780  C  CE    . MET   A 1 902  ? 160.306 145.228 102.805 1.00 48.33  ? 902  MET   A CE    1 
ATOM   4781  N  N     . TYR   A 1 903  ? 165.782 144.001 105.080 1.00 37.34  ? 903  TYR   A N     1 
ATOM   4782  C  CA    . TYR   A 1 903  ? 166.527 143.682 106.297 1.00 29.13  ? 903  TYR   A CA    1 
ATOM   4783  C  C     . TYR   A 1 903  ? 167.862 144.426 106.338 1.00 27.51  ? 903  TYR   A C     1 
ATOM   4784  O  O     . TYR   A 1 903  ? 168.196 145.103 107.325 1.00 34.37  ? 903  TYR   A O     1 
ATOM   4785  C  CB    . TYR   A 1 903  ? 166.733 142.166 106.358 1.00 33.06  ? 903  TYR   A CB    1 
ATOM   4786  C  CG    . TYR   A 1 903  ? 167.077 141.597 107.713 1.00 35.58  ? 903  TYR   A CG    1 
ATOM   4787  C  CD1   . TYR   A 1 903  ? 166.111 141.481 108.703 1.00 31.98  ? 903  TYR   A CD1   1 
ATOM   4788  C  CD2   . TYR   A 1 903  ? 168.356 141.137 107.989 1.00 29.21  ? 903  TYR   A CD2   1 
ATOM   4789  C  CE1   . TYR   A 1 903  ? 166.418 140.949 109.939 1.00 34.05  ? 903  TYR   A CE1   1 
ATOM   4790  C  CE2   . TYR   A 1 903  ? 168.672 140.603 109.221 1.00 30.33  ? 903  TYR   A CE2   1 
ATOM   4791  C  CZ    . TYR   A 1 903  ? 167.699 140.511 110.192 1.00 36.20  ? 903  TYR   A CZ    1 
ATOM   4792  O  OH    . TYR   A 1 903  ? 168.007 139.979 111.423 1.00 49.80  ? 903  TYR   A OH    1 
ATOM   4793  N  N     . ILE   A 1 904  ? 168.642 144.317 105.262 1.00 26.60  ? 904  ILE   A N     1 
ATOM   4794  C  CA    . ILE   A 1 904  ? 169.938 144.987 105.226 1.00 29.19  ? 904  ILE   A CA    1 
ATOM   4795  C  C     . ILE   A 1 904  ? 169.767 146.500 105.269 1.00 29.00  ? 904  ILE   A C     1 
ATOM   4796  O  O     . ILE   A 1 904  ? 170.584 147.210 105.867 1.00 32.68  ? 904  ILE   A O     1 
ATOM   4797  C  CB    . ILE   A 1 904  ? 170.739 144.537 103.992 1.00 38.83  ? 904  ILE   A CB    1 
ATOM   4798  C  CG1   . ILE   A 1 904  ? 170.998 143.033 104.060 1.00 34.84  ? 904  ILE   A CG1   1 
ATOM   4799  C  CG2   . ILE   A 1 904  ? 172.049 145.300 103.899 1.00 42.17  ? 904  ILE   A CG2   1 
ATOM   4800  C  CD1   . ILE   A 1 904  ? 171.247 142.525 105.462 1.00 24.90  ? 904  ILE   A CD1   1 
ATOM   4801  N  N     . ASN   A 1 905  ? 168.713 147.023 104.644 1.00 33.42  ? 905  ASN   A N     1 
ATOM   4802  C  CA    . ASN   A 1 905  ? 168.454 148.453 104.719 1.00 36.44  ? 905  ASN   A CA    1 
ATOM   4803  C  C     . ASN   A 1 905  ? 168.050 148.870 106.124 1.00 35.62  ? 905  ASN   A C     1 
ATOM   4804  O  O     . ASN   A 1 905  ? 168.345 149.990 106.540 1.00 38.73  ? 905  ASN   A O     1 
ATOM   4805  C  CB    . ASN   A 1 905  ? 167.378 148.846 103.710 1.00 37.03  ? 905  ASN   A CB    1 
ATOM   4806  C  CG    . ASN   A 1 905  ? 167.878 148.806 102.280 1.00 45.14  ? 905  ASN   A CG    1 
ATOM   4807  O  OD1   . ASN   A 1 905  ? 167.107 148.973 101.336 1.00 44.95  ? 905  ASN   A OD1   1 
ATOM   4808  N  ND2   . ASN   A 1 905  ? 169.176 148.582 102.114 1.00 43.00  ? 905  ASN   A ND2   1 
ATOM   4809  N  N     . LEU   A 1 906  ? 167.362 147.999 106.861 1.00 29.27  ? 906  LEU   A N     1 
ATOM   4810  C  CA    . LEU   A 1 906  ? 167.139 148.258 108.277 1.00 23.25  ? 906  LEU   A CA    1 
ATOM   4811  C  C     . LEU   A 1 906  ? 168.469 148.428 108.991 1.00 32.99  ? 906  LEU   A C     1 
ATOM   4812  O  O     . LEU   A 1 906  ? 168.661 149.372 109.765 1.00 30.40  ? 906  LEU   A O     1 
ATOM   4813  C  CB    . LEU   A 1 906  ? 166.334 147.119 108.904 1.00 28.52  ? 906  LEU   A CB    1 
ATOM   4814  C  CG    . LEU   A 1 906  ? 164.816 147.159 108.731 1.00 36.32  ? 906  LEU   A CG    1 
ATOM   4815  C  CD1   . LEU   A 1 906  ? 164.143 146.234 109.732 1.00 31.39  ? 906  LEU   A CD1   1 
ATOM   4816  C  CD2   . LEU   A 1 906  ? 164.306 148.578 108.880 1.00 35.56  ? 906  LEU   A CD2   1 
ATOM   4817  N  N     . PHE   A 1 907  ? 169.406 147.518 108.724 1.00 44.90  ? 907  PHE   A N     1 
ATOM   4818  C  CA    . PHE   A 1 907  ? 170.762 147.676 109.248 1.00 24.05  ? 907  PHE   A CA    1 
ATOM   4819  C  C     . PHE   A 1 907  ? 171.327 149.055 108.912 1.00 22.64  ? 907  PHE   A C     1 
ATOM   4820  O  O     . PHE   A 1 907  ? 171.852 149.767 109.781 1.00 20.21  ? 907  PHE   A O     1 
ATOM   4821  C  CB    . PHE   A 1 907  ? 171.671 146.588 108.675 1.00 24.10  ? 907  PHE   A CB    1 
ATOM   4822  C  CG    . PHE   A 1 907  ? 171.632 145.296 109.431 1.00 24.51  ? 907  PHE   A CG    1 
ATOM   4823  C  CD1   . PHE   A 1 907  ? 170.516 144.481 109.379 1.00 33.53  ? 907  PHE   A CD1   1 
ATOM   4824  C  CD2   . PHE   A 1 907  ? 172.723 144.881 110.172 1.00 20.97  ? 907  PHE   A CD2   1 
ATOM   4825  C  CE1   . PHE   A 1 907  ? 170.482 143.286 110.066 1.00 31.99  ? 907  PHE   A CE1   1 
ATOM   4826  C  CE2   . PHE   A 1 907  ? 172.694 143.686 110.859 1.00 27.05  ? 907  PHE   A CE2   1 
ATOM   4827  C  CZ    . PHE   A 1 907  ? 171.572 142.888 110.805 1.00 28.17  ? 907  PHE   A CZ    1 
ATOM   4828  N  N     . HIS   A 1 908  ? 171.233 149.437 107.638 1.00 32.09  ? 908  HIS   A N     1 
ATOM   4829  C  CA    . HIS   A 1 908  ? 171.876 150.664 107.174 1.00 28.54  ? 908  HIS   A CA    1 
ATOM   4830  C  C     . HIS   A 1 908  ? 171.239 151.907 107.784 1.00 33.96  ? 908  HIS   A C     1 
ATOM   4831  O  O     . HIS   A 1 908  ? 171.948 152.842 108.166 1.00 27.49  ? 908  HIS   A O     1 
ATOM   4832  C  CB    . HIS   A 1 908  ? 171.847 150.730 105.648 1.00 31.38  ? 908  HIS   A CB    1 
ATOM   4833  C  CG    . HIS   A 1 908  ? 172.904 149.898 104.992 1.00 32.78  ? 908  HIS   A CG    1 
ATOM   4834  N  ND1   . HIS   A 1 908  ? 174.247 150.183 105.103 1.00 29.69  ? 908  HIS   A ND1   1 
ATOM   4835  C  CD2   . HIS   A 1 908  ? 172.817 148.787 104.224 1.00 34.46  ? 908  HIS   A CD2   1 
ATOM   4836  C  CE1   . HIS   A 1 908  ? 174.943 149.285 104.429 1.00 34.93  ? 908  HIS   A CE1   1 
ATOM   4837  N  NE2   . HIS   A 1 908  ? 174.099 148.427 103.886 1.00 42.63  ? 908  HIS   A NE2   1 
ATOM   4838  N  N     . ASP   A 1 909  ? 169.909 151.950 107.873 1.00 38.73  ? 909  ASP   A N     1 
ATOM   4839  C  CA    . ASP   A 1 909  ? 169.260 153.095 108.506 1.00 25.94  ? 909  ASP   A CA    1 
ATOM   4840  C  C     . ASP   A 1 909  ? 169.536 153.132 110.002 1.00 31.61  ? 909  ASP   A C     1 
ATOM   4841  O  O     . ASP   A 1 909  ? 169.647 154.215 110.589 1.00 38.58  ? 909  ASP   A O     1 
ATOM   4842  C  CB    . ASP   A 1 909  ? 167.753 153.097 108.240 1.00 33.34  ? 909  ASP   A CB    1 
ATOM   4843  C  CG    . ASP   A 1 909  ? 167.416 153.082 106.762 1.00 49.76  ? 909  ASP   A CG    1 
ATOM   4844  O  OD1   . ASP   A 1 909  ? 167.342 154.175 106.165 1.00 51.36  ? 909  ASP   A OD1   1 
ATOM   4845  O  OD2   . ASP   A 1 909  ? 167.182 151.995 106.203 1.00 52.81  ? 909  ASP   A OD2   1 
ATOM   4846  N  N     . ALA   A 1 910  ? 169.654 151.967 110.641 1.00 29.86  ? 910  ALA   A N     1 
ATOM   4847  C  CA    . ALA   A 1 910  ? 170.055 151.946 112.042 1.00 20.11  ? 910  ALA   A CA    1 
ATOM   4848  C  C     . ALA   A 1 910  ? 171.416 152.604 112.220 1.00 21.43  ? 910  ALA   A C     1 
ATOM   4849  O  O     . ALA   A 1 910  ? 171.605 153.438 113.113 1.00 26.97  ? 910  ALA   A O     1 
ATOM   4850  C  CB    . ALA   A 1 910  ? 170.072 150.509 112.562 1.00 31.00  ? 910  ALA   A CB    1 
ATOM   4851  N  N     . PHE   A 1 911  ? 172.381 152.244 111.370 1.00 30.13  ? 911  PHE   A N     1 
ATOM   4852  C  CA    . PHE   A 1 911  ? 173.695 152.882 111.450 1.00 19.95  ? 911  PHE   A CA    1 
ATOM   4853  C  C     . PHE   A 1 911  ? 173.623 154.368 111.108 1.00 22.94  ? 911  PHE   A C     1 
ATOM   4854  O  O     . PHE   A 1 911  ? 174.305 155.189 111.731 1.00 24.73  ? 911  PHE   A O     1 
ATOM   4855  C  CB    . PHE   A 1 911  ? 174.693 152.164 110.543 1.00 21.35  ? 911  PHE   A CB    1 
ATOM   4856  C  CG    . PHE   A 1 911  ? 175.060 150.791 111.020 1.00 19.32  ? 911  PHE   A CG    1 
ATOM   4857  C  CD1   . PHE   A 1 911  ? 175.134 150.518 112.374 1.00 21.05  ? 911  PHE   A CD1   1 
ATOM   4858  C  CD2   . PHE   A 1 911  ? 175.326 149.773 110.123 1.00 25.26  ? 911  PHE   A CD2   1 
ATOM   4859  C  CE1   . PHE   A 1 911  ? 175.473 149.260 112.824 1.00 18.08  ? 911  PHE   A CE1   1 
ATOM   4860  C  CE2   . PHE   A 1 911  ? 175.662 148.508 110.569 1.00 23.43  ? 911  PHE   A CE2   1 
ATOM   4861  C  CZ    . PHE   A 1 911  ? 175.734 148.253 111.921 1.00 23.14  ? 911  PHE   A CZ    1 
ATOM   4862  N  N     . ASP   A 1 912  ? 172.807 154.732 110.118 1.00 36.51  ? 912  ASP   A N     1 
ATOM   4863  C  CA    . ASP   A 1 912  ? 172.713 156.127 109.704 1.00 32.19  ? 912  ASP   A CA    1 
ATOM   4864  C  C     . ASP   A 1 912  ? 172.118 157.001 110.797 1.00 38.83  ? 912  ASP   A C     1 
ATOM   4865  O  O     . ASP   A 1 912  ? 172.471 158.180 110.912 1.00 44.83  ? 912  ASP   A O     1 
ATOM   4866  C  CB    . ASP   A 1 912  ? 171.876 156.238 108.430 1.00 27.90  ? 912  ASP   A CB    1 
ATOM   4867  C  CG    . ASP   A 1 912  ? 172.726 156.348 107.181 1.00 50.01  ? 912  ASP   A CG    1 
ATOM   4868  O  OD1   . ASP   A 1 912  ? 173.958 156.507 107.309 1.00 52.30  ? 912  ASP   A OD1   1 
ATOM   4869  O  OD2   . ASP   A 1 912  ? 172.162 156.274 106.069 1.00 52.23  ? 912  ASP   A OD2   1 
ATOM   4870  N  N     . ILE   A 1 913  ? 171.219 156.448 111.602 1.00 40.31  ? 913  ILE   A N     1 
ATOM   4871  C  CA    . ILE   A 1 913  ? 170.561 157.200 112.658 1.00 26.83  ? 913  ILE   A CA    1 
ATOM   4872  C  C     . ILE   A 1 913  ? 171.374 157.168 113.955 1.00 27.64  ? 913  ILE   A C     1 
ATOM   4873  O  O     . ILE   A 1 913  ? 170.891 157.603 114.999 1.00 32.19  ? 913  ILE   A O     1 
ATOM   4874  C  CB    . ILE   A 1 913  ? 169.125 156.705 112.880 1.00 24.39  ? 913  ILE   A CB    1 
ATOM   4875  C  CG1   . ILE   A 1 913  ? 168.229 157.852 113.349 1.00 36.55  ? 913  ILE   A CG1   1 
ATOM   4876  C  CG2   . ILE   A 1 913  ? 169.102 155.546 113.854 1.00 33.30  ? 913  ILE   A CG2   1 
ATOM   4877  C  CD1   . ILE   A 1 913  ? 168.293 159.067 112.455 1.00 39.74  ? 913  ILE   A CD1   1 
ATOM   4878  N  N     . GLN   A 1 914  ? 172.607 156.662 113.899 1.00 34.09  ? 914  GLN   A N     1 
ATOM   4879  C  CA    . GLN   A 1 914  ? 173.497 156.596 115.059 1.00 28.66  ? 914  GLN   A CA    1 
ATOM   4880  C  C     . GLN   A 1 914  ? 172.936 155.674 116.140 1.00 29.12  ? 914  GLN   A C     1 
ATOM   4881  O  O     . GLN   A 1 914  ? 172.955 155.985 117.332 1.00 34.69  ? 914  GLN   A O     1 
ATOM   4882  C  CB    . GLN   A 1 914  ? 173.785 157.991 115.617 1.00 35.64  ? 914  GLN   A CB    1 
ATOM   4883  C  CG    . GLN   A 1 914  ? 174.258 158.981 114.568 1.00 40.97  ? 914  GLN   A CG    1 
ATOM   4884  C  CD    . GLN   A 1 914  ? 174.237 160.410 115.064 1.00 49.73  ? 914  GLN   A CD    1 
ATOM   4885  O  OE1   . GLN   A 1 914  ? 173.550 160.735 116.032 1.00 49.96  ? 914  GLN   A OE1   1 
ATOM   4886  N  NE2   . GLN   A 1 914  ? 174.992 161.277 114.399 1.00 45.92  ? 914  GLN   A NE2   1 
ATOM   4887  N  N     . TYR   A 1 915  ? 172.435 154.525 115.707 1.00 23.12  ? 915  TYR   A N     1 
ATOM   4888  C  CA    . TYR   A 1 915  ? 171.995 153.460 116.592 1.00 20.39  ? 915  TYR   A CA    1 
ATOM   4889  C  C     . TYR   A 1 915  ? 173.056 152.369 116.651 1.00 24.13  ? 915  TYR   A C     1 
ATOM   4890  O  O     . TYR   A 1 915  ? 173.861 152.212 115.731 1.00 40.35  ? 915  TYR   A O     1 
ATOM   4891  C  CB    . TYR   A 1 915  ? 170.670 152.867 116.106 1.00 24.41  ? 915  TYR   A CB    1 
ATOM   4892  C  CG    . TYR   A 1 915  ? 169.433 153.417 116.777 1.00 24.58  ? 915  TYR   A CG    1 
ATOM   4893  C  CD1   . TYR   A 1 915  ? 169.205 154.782 116.854 1.00 29.06  ? 915  TYR   A CD1   1 
ATOM   4894  C  CD2   . TYR   A 1 915  ? 168.466 152.562 117.288 1.00 22.64  ? 915  TYR   A CD2   1 
ATOM   4895  C  CE1   . TYR   A 1 915  ? 168.069 155.281 117.452 1.00 31.48  ? 915  TYR   A CE1   1 
ATOM   4896  C  CE2   . TYR   A 1 915  ? 167.326 153.051 117.883 1.00 25.90  ? 915  TYR   A CE2   1 
ATOM   4897  C  CZ    . TYR   A 1 915  ? 167.132 154.410 117.963 1.00 30.11  ? 915  TYR   A CZ    1 
ATOM   4898  O  OH    . TYR   A 1 915  ? 165.995 154.902 118.558 1.00 34.98  ? 915  TYR   A OH    1 
ATOM   4899  N  N     . GLY   A 1 916  ? 173.053 151.618 117.748 1.00 9.47   ? 916  GLY   A N     1 
ATOM   4900  C  CA    . GLY   A 1 916  ? 173.879 150.431 117.852 1.00 14.06  ? 916  GLY   A CA    1 
ATOM   4901  C  C     . GLY   A 1 916  ? 173.042 149.201 117.546 1.00 11.12  ? 916  GLY   A C     1 
ATOM   4902  O  O     . GLY   A 1 916  ? 171.937 149.048 118.052 1.00 32.76  ? 916  GLY   A O     1 
ATOM   4903  N  N     . VAL   A 1 917  ? 173.588 148.318 116.719 1.00 14.47  ? 917  VAL   A N     1 
ATOM   4904  C  CA    . VAL   A 1 917  ? 172.835 147.202 116.158 1.00 21.29  ? 917  VAL   A CA    1 
ATOM   4905  C  C     . VAL   A 1 917  ? 173.234 145.918 116.868 1.00 20.34  ? 917  VAL   A C     1 
ATOM   4906  O  O     . VAL   A 1 917  ? 174.426 145.612 117.001 1.00 21.28  ? 917  VAL   A O     1 
ATOM   4907  C  CB    . VAL   A 1 917  ? 173.052 147.083 114.641 1.00 21.40  ? 917  VAL   A CB    1 
ATOM   4908  C  CG1   . VAL   A 1 917  ? 172.275 145.901 114.086 1.00 16.38  ? 917  VAL   A CG1   1 
ATOM   4909  C  CG2   . VAL   A 1 917  ? 172.623 148.365 113.955 1.00 14.84  ? 917  VAL   A CG2   1 
ATOM   4910  N  N     . VAL   A 1 918  ? 172.234 145.165 117.317 1.00 19.69  ? 918  VAL   A N     1 
ATOM   4911  C  CA    . VAL   A 1 918  ? 172.439 143.854 117.921 1.00 18.85  ? 918  VAL   A CA    1 
ATOM   4912  C  C     . VAL   A 1 918  ? 171.601 142.847 117.149 1.00 20.12  ? 918  VAL   A C     1 
ATOM   4913  O  O     . VAL   A 1 918  ? 170.371 142.971 117.089 1.00 32.66  ? 918  VAL   A O     1 
ATOM   4914  C  CB    . VAL   A 1 918  ? 172.070 143.844 119.412 1.00 18.53  ? 918  VAL   A CB    1 
ATOM   4915  C  CG1   . VAL   A 1 918  ? 172.390 142.492 120.026 1.00 11.75  ? 918  VAL   A CG1   1 
ATOM   4916  C  CG2   . VAL   A 1 918  ? 172.797 144.954 120.145 1.00 20.58  ? 918  VAL   A CG2   1 
ATOM   4917  N  N     . VAL   A 1 919  ? 172.261 141.846 116.576 1.00 15.48  ? 919  VAL   A N     1 
ATOM   4918  C  CA    . VAL   A 1 919  ? 171.601 140.775 115.839 1.00 16.46  ? 919  VAL   A CA    1 
ATOM   4919  C  C     . VAL   A 1 919  ? 171.738 139.499 116.654 1.00 22.81  ? 919  VAL   A C     1 
ATOM   4920  O  O     . VAL   A 1 919  ? 172.855 139.064 116.955 1.00 35.33  ? 919  VAL   A O     1 
ATOM   4921  C  CB    . VAL   A 1 919  ? 172.200 140.599 114.436 1.00 17.98  ? 919  VAL   A CB    1 
ATOM   4922  C  CG1   . VAL   A 1 919  ? 171.343 139.657 113.610 1.00 24.25  ? 919  VAL   A CG1   1 
ATOM   4923  C  CG2   . VAL   A 1 919  ? 172.341 141.944 113.753 1.00 25.85  ? 919  VAL   A CG2   1 
ATOM   4924  N  N     . ILE   A 1 920  ? 170.609 138.893 117.003 1.00 11.89  ? 920  ILE   A N     1 
ATOM   4925  C  CA    . ILE   A 1 920  ? 170.580 137.707 117.849 1.00 14.28  ? 920  ILE   A CA    1 
ATOM   4926  C  C     . ILE   A 1 920  ? 170.205 136.511 116.991 1.00 20.77  ? 920  ILE   A C     1 
ATOM   4927  O  O     . ILE   A 1 920  ? 169.172 136.526 116.311 1.00 35.56  ? 920  ILE   A O     1 
ATOM   4928  C  CB    . ILE   A 1 920  ? 169.594 137.875 119.017 1.00 29.11  ? 920  ILE   A CB    1 
ATOM   4929  C  CG1   . ILE   A 1 920  ? 170.039 139.024 119.922 1.00 33.30  ? 920  ILE   A CG1   1 
ATOM   4930  C  CG2   . ILE   A 1 920  ? 169.482 136.581 119.803 1.00 30.87  ? 920  ILE   A CG2   1 
ATOM   4931  C  CD1   . ILE   A 1 920  ? 168.926 139.608 120.755 1.00 30.54  ? 920  ILE   A CD1   1 
ATOM   4932  N  N     . ARG   A 1 921  ? 171.039 135.475 117.021 1.00 28.39  ? 921  ARG   A N     1 
ATOM   4933  C  CA    . ARG   A 1 921  ? 170.769 134.233 116.309 1.00 28.33  ? 921  ARG   A CA    1 
ATOM   4934  C  C     . ARG   A 1 921  ? 170.799 133.087 117.308 1.00 34.63  ? 921  ARG   A C     1 
ATOM   4935  O  O     . ARG   A 1 921  ? 171.842 132.812 117.913 1.00 44.61  ? 921  ARG   A O     1 
ATOM   4936  C  CB    . ARG   A 1 921  ? 171.779 134.008 115.183 1.00 28.54  ? 921  ARG   A CB    1 
ATOM   4937  C  CG    . ARG   A 1 921  ? 171.721 132.621 114.576 1.00 24.44  ? 921  ARG   A CG    1 
ATOM   4938  C  CD    . ARG   A 1 921  ? 172.610 132.519 113.355 1.00 25.81  ? 921  ARG   A CD    1 
ATOM   4939  N  NE    . ARG   A 1 921  ? 172.213 131.412 112.495 1.00 29.16  ? 921  ARG   A NE    1 
ATOM   4940  C  CZ    . ARG   A 1 921  ? 172.643 131.238 111.254 1.00 36.65  ? 921  ARG   A CZ    1 
ATOM   4941  N  NH1   . ARG   A 1 921  ? 173.477 132.093 110.686 1.00 27.51  ? 921  ARG   A NH1   1 
ATOM   4942  N  NH2   . ARG   A 1 921  ? 172.225 130.180 110.566 1.00 39.33  ? 921  ARG   A NH2   1 
ATOM   4943  N  N     . LEU   A 1 922  ? 169.655 132.431 117.485 1.00 37.98  ? 922  LEU   A N     1 
ATOM   4944  C  CA    . LEU   A 1 922  ? 169.526 131.337 118.433 1.00 38.71  ? 922  LEU   A CA    1 
ATOM   4945  C  C     . LEU   A 1 922  ? 168.448 130.382 117.943 1.00 37.63  ? 922  LEU   A C     1 
ATOM   4946  O  O     . LEU   A 1 922  ? 167.598 130.741 117.125 1.00 43.11  ? 922  LEU   A O     1 
ATOM   4947  C  CB    . LEU   A 1 922  ? 169.194 131.847 119.840 1.00 37.74  ? 922  LEU   A CB    1 
ATOM   4948  C  CG    . LEU   A 1 922  ? 168.062 132.872 119.943 1.00 36.85  ? 922  LEU   A CG    1 
ATOM   4949  C  CD1   . LEU   A 1 922  ? 166.705 132.193 119.865 1.00 41.76  ? 922  LEU   A CD1   1 
ATOM   4950  C  CD2   . LEU   A 1 922  ? 168.184 133.672 121.228 1.00 31.22  ? 922  LEU   A CD2   1 
ATOM   4951  N  N     . LYS   A 1 923  ? 168.494 129.156 118.458 1.00 49.58  ? 923  LYS   A N     1 
ATOM   4952  C  CA    . LYS   A 1 923  ? 167.515 128.133 118.105 1.00 48.58  ? 923  LYS   A CA    1 
ATOM   4953  C  C     . LYS   A 1 923  ? 166.212 128.424 118.839 1.00 51.72  ? 923  LYS   A C     1 
ATOM   4954  O  O     . LYS   A 1 923  ? 166.130 128.267 120.061 1.00 52.34  ? 923  LYS   A O     1 
ATOM   4955  C  CB    . LYS   A 1 923  ? 168.046 126.746 118.453 1.00 47.27  ? 923  LYS   A CB    1 
ATOM   4956  N  N     . GLU   A 1 924  ? 165.190 128.849 118.094 1.00 64.07  ? 924  GLU   A N     1 
ATOM   4957  C  CA    . GLU   A 1 924  ? 163.909 129.201 118.693 1.00 60.72  ? 924  GLU   A CA    1 
ATOM   4958  C  C     . GLU   A 1 924  ? 163.080 127.986 119.085 1.00 63.67  ? 924  GLU   A C     1 
ATOM   4959  O  O     . GLU   A 1 924  ? 162.243 128.092 119.989 1.00 61.61  ? 924  GLU   A O     1 
ATOM   4960  C  CB    . GLU   A 1 924  ? 163.106 130.081 117.732 1.00 60.87  ? 924  GLU   A CB    1 
ATOM   4961  C  CG    . GLU   A 1 924  ? 163.042 131.542 118.140 1.00 60.21  ? 924  GLU   A CG    1 
ATOM   4962  C  CD    . GLU   A 1 924  ? 162.419 131.737 119.505 1.00 63.98  ? 924  GLU   A CD    1 
ATOM   4963  O  OE1   . GLU   A 1 924  ? 161.878 130.757 120.058 1.00 66.03  ? 924  GLU   A OE1   1 
ATOM   4964  O  OE2   . GLU   A 1 924  ? 162.474 132.869 120.028 1.00 64.63  ? 924  GLU   A OE2   1 
ATOM   4965  N  N     . GLY   A 1 925  ? 163.288 126.842 118.432 1.00 78.48  ? 925  GLY   A N     1 
ATOM   4966  C  CA    . GLY   A 1 925  ? 162.452 125.684 118.705 1.00 78.78  ? 925  GLY   A CA    1 
ATOM   4967  C  C     . GLY   A 1 925  ? 162.508 125.244 120.155 1.00 82.92  ? 925  GLY   A C     1 
ATOM   4968  O  O     . GLY   A 1 925  ? 161.486 124.876 120.741 1.00 81.82  ? 925  GLY   A O     1 
ATOM   4969  N  N     . LEU   A 1 926  ? 163.695 125.273 120.752 1.00 93.13  ? 926  LEU   A N     1 
ATOM   4970  C  CA    . LEU   A 1 926  ? 163.865 124.859 122.140 1.00 91.45  ? 926  LEU   A CA    1 
ATOM   4971  C  C     . LEU   A 1 926  ? 163.506 123.387 122.323 1.00 92.60  ? 926  LEU   A C     1 
ATOM   4972  O  O     . LEU   A 1 926  ? 164.082 122.513 121.676 1.00 93.82  ? 926  LEU   A O     1 
ATOM   4973  C  CB    . LEU   A 1 926  ? 163.011 125.727 123.068 1.00 88.35  ? 926  LEU   A CB    1 
ATOM   4974  N  N     . ASN   A 1 1022 ? 178.041 127.623 132.389 1.00 46.20  ? 1022 ASN   A N     1 
ATOM   4975  C  CA    . ASN   A 1 1022 ? 179.429 127.412 131.998 1.00 47.16  ? 1022 ASN   A CA    1 
ATOM   4976  C  C     . ASN   A 1 1022 ? 180.152 128.737 131.786 1.00 41.91  ? 1022 ASN   A C     1 
ATOM   4977  O  O     . ASN   A 1 1022 ? 180.505 129.419 132.747 1.00 47.36  ? 1022 ASN   A O     1 
ATOM   4978  C  CB    . ASN   A 1 1022 ? 179.506 126.563 130.728 1.00 47.11  ? 1022 ASN   A CB    1 
ATOM   4979  N  N     . THR   A 1 1023 ? 180.368 129.102 130.525 1.00 36.02  ? 1023 THR   A N     1 
ATOM   4980  C  CA    . THR   A 1 1023 ? 181.145 130.283 130.183 1.00 40.91  ? 1023 THR   A CA    1 
ATOM   4981  C  C     . THR   A 1 1023 ? 180.363 131.176 129.230 1.00 41.70  ? 1023 THR   A C     1 
ATOM   4982  O  O     . THR   A 1 1023 ? 179.382 130.764 128.606 1.00 43.67  ? 1023 THR   A O     1 
ATOM   4983  C  CB    . THR   A 1 1023 ? 182.492 129.905 129.549 1.00 41.65  ? 1023 THR   A CB    1 
ATOM   4984  O  OG1   . THR   A 1 1023 ? 183.122 131.083 129.031 1.00 41.52  ? 1023 THR   A OG1   1 
ATOM   4985  C  CG2   . THR   A 1 1023 ? 182.288 128.911 128.420 1.00 44.81  ? 1023 THR   A CG2   1 
ATOM   4986  N  N     . ILE   A 1 1024 ? 180.819 132.421 129.134 1.00 39.91  ? 1024 ILE   A N     1 
ATOM   4987  C  CA    . ILE   A 1 1024 ? 180.325 133.395 128.169 1.00 35.40  ? 1024 ILE   A CA    1 
ATOM   4988  C  C     . ILE   A 1 1024 ? 181.546 133.912 127.423 1.00 35.61  ? 1024 ILE   A C     1 
ATOM   4989  O  O     . ILE   A 1 1024 ? 182.417 134.556 128.021 1.00 35.63  ? 1024 ILE   A O     1 
ATOM   4990  C  CB    . ILE   A 1 1024 ? 179.560 134.545 128.836 1.00 29.78  ? 1024 ILE   A CB    1 
ATOM   4991  C  CG1   . ILE   A 1 1024 ? 178.255 134.031 129.446 1.00 36.23  ? 1024 ILE   A CG1   1 
ATOM   4992  C  CG2   . ILE   A 1 1024 ? 179.282 135.651 127.834 1.00 31.79  ? 1024 ILE   A CG2   1 
ATOM   4993  C  CD1   . ILE   A 1 1024 ? 177.170 135.078 129.535 1.00 43.08  ? 1024 ILE   A CD1   1 
ATOM   4994  N  N     . ASP   A 1 1025 ? 181.617 133.629 126.128 1.00 36.70  ? 1025 ASP   A N     1 
ATOM   4995  C  CA    . ASP   A 1 1025 ? 182.784 133.953 125.321 1.00 32.01  ? 1025 ASP   A CA    1 
ATOM   4996  C  C     . ASP   A 1 1025 ? 182.512 135.233 124.544 1.00 29.71  ? 1025 ASP   A C     1 
ATOM   4997  O  O     . ASP   A 1 1025 ? 181.541 135.309 123.784 1.00 32.90  ? 1025 ASP   A O     1 
ATOM   4998  C  CB    . ASP   A 1 1025 ? 183.125 132.802 124.377 1.00 33.13  ? 1025 ASP   A CB    1 
ATOM   4999  C  CG    . ASP   A 1 1025 ? 183.451 131.523 125.120 1.00 42.86  ? 1025 ASP   A CG    1 
ATOM   5000  O  OD1   . ASP   A 1 1025 ? 183.317 131.506 126.361 1.00 35.91  ? 1025 ASP   A OD1   1 
ATOM   5001  O  OD2   . ASP   A 1 1025 ? 183.847 130.536 124.465 1.00 47.83  ? 1025 ASP   A OD2   1 
ATOM   5002  N  N     . VAL   A 1 1026 ? 183.363 136.234 124.740 1.00 23.76  ? 1026 VAL   A N     1 
ATOM   5003  C  CA    . VAL   A 1 1026 ? 183.199 137.543 124.119 1.00 19.98  ? 1026 VAL   A CA    1 
ATOM   5004  C  C     . VAL   A 1 1026 ? 184.320 137.728 123.108 1.00 27.20  ? 1026 VAL   A C     1 
ATOM   5005  O  O     . VAL   A 1 1026 ? 185.480 137.935 123.484 1.00 32.14  ? 1026 VAL   A O     1 
ATOM   5006  C  CB    . VAL   A 1 1026 ? 183.195 138.671 125.158 1.00 23.84  ? 1026 VAL   A CB    1 
ATOM   5007  C  CG1   . VAL   A 1 1026 ? 182.628 139.944 124.553 1.00 24.29  ? 1026 VAL   A CG1   1 
ATOM   5008  C  CG2   . VAL   A 1 1026 ? 182.389 138.258 126.374 1.00 25.64  ? 1026 VAL   A CG2   1 
ATOM   5009  N  N     . TRP   A 1 1027 ? 183.976 137.645 121.825 1.00 23.16  ? 1027 TRP   A N     1 
ATOM   5010  C  CA    . TRP   A 1 1027 ? 184.923 137.889 120.738 1.00 20.66  ? 1027 TRP   A CA    1 
ATOM   5011  C  C     . TRP   A 1 1027 ? 184.709 139.293 120.181 1.00 25.82  ? 1027 TRP   A C     1 
ATOM   5012  O  O     . TRP   A 1 1027 ? 184.150 139.489 119.103 1.00 32.37  ? 1027 TRP   A O     1 
ATOM   5013  C  CB    . TRP   A 1 1027 ? 184.757 136.847 119.637 1.00 14.67  ? 1027 TRP   A CB    1 
ATOM   5014  C  CG    . TRP   A 1 1027 ? 184.895 135.429 120.061 1.00 16.16  ? 1027 TRP   A CG    1 
ATOM   5015  C  CD1   . TRP   A 1 1027 ? 184.164 134.780 121.008 1.00 23.07  ? 1027 TRP   A CD1   1 
ATOM   5016  C  CD2   . TRP   A 1 1027 ? 185.789 134.459 119.507 1.00 18.40  ? 1027 TRP   A CD2   1 
ATOM   5017  N  NE1   . TRP   A 1 1027 ? 184.565 133.471 121.100 1.00 30.76  ? 1027 TRP   A NE1   1 
ATOM   5018  C  CE2   . TRP   A 1 1027 ? 185.561 133.248 120.186 1.00 27.79  ? 1027 TRP   A CE2   1 
ATOM   5019  C  CE3   . TRP   A 1 1027 ? 186.767 134.501 118.511 1.00 9.28   ? 1027 TRP   A CE3   1 
ATOM   5020  C  CZ2   . TRP   A 1 1027 ? 186.275 132.090 119.903 1.00 26.32  ? 1027 TRP   A CZ2   1 
ATOM   5021  C  CZ3   . TRP   A 1 1027 ? 187.475 133.351 118.231 1.00 23.24  ? 1027 TRP   A CZ3   1 
ATOM   5022  C  CH2   . TRP   A 1 1027 ? 187.226 132.161 118.924 1.00 28.01  ? 1027 TRP   A CH2   1 
ATOM   5023  N  N     . TRP   A 1 1028 ? 185.172 140.284 120.929 1.00 21.24  ? 1028 TRP   A N     1 
ATOM   5024  C  CA    . TRP   A 1 1028 ? 185.074 141.665 120.482 1.00 34.31  ? 1028 TRP   A CA    1 
ATOM   5025  C  C     . TRP   A 1 1028 ? 186.432 142.084 119.928 1.00 37.06  ? 1028 TRP   A C     1 
ATOM   5026  O  O     . TRP   A 1 1028 ? 187.415 142.184 120.669 1.00 36.17  ? 1028 TRP   A O     1 
ATOM   5027  C  CB    . TRP   A 1 1028 ? 184.562 142.573 121.605 1.00 34.22  ? 1028 TRP   A CB    1 
ATOM   5028  C  CG    . TRP   A 1 1028 ? 185.556 143.247 122.495 1.00 29.07  ? 1028 TRP   A CG    1 
ATOM   5029  C  CD1   . TRP   A 1 1028 ? 186.535 142.658 123.239 1.00 40.03  ? 1028 TRP   A CD1   1 
ATOM   5030  C  CD2   . TRP   A 1 1028 ? 185.618 144.646 122.784 1.00 31.00  ? 1028 TRP   A CD2   1 
ATOM   5031  N  NE1   . TRP   A 1 1028 ? 187.225 143.611 123.949 1.00 44.44  ? 1028 TRP   A NE1   1 
ATOM   5032  C  CE2   . TRP   A 1 1028 ? 186.679 144.840 123.688 1.00 41.50  ? 1028 TRP   A CE2   1 
ATOM   5033  C  CE3   . TRP   A 1 1028 ? 184.887 145.757 122.354 1.00 32.74  ? 1028 TRP   A CE3   1 
ATOM   5034  C  CZ2   . TRP   A 1 1028 ? 187.025 146.098 124.173 1.00 42.06  ? 1028 TRP   A CZ2   1 
ATOM   5035  C  CZ3   . TRP   A 1 1028 ? 185.233 147.004 122.832 1.00 37.62  ? 1028 TRP   A CZ3   1 
ATOM   5036  C  CH2   . TRP   A 1 1028 ? 186.294 147.165 123.731 1.00 40.64  ? 1028 TRP   A CH2   1 
ATOM   5037  N  N     . LEU   A 1 1029 ? 186.485 142.274 118.610 1.00 35.30  ? 1029 LEU   A N     1 
ATOM   5038  C  CA    . LEU   A 1 1029 ? 187.727 142.509 117.892 1.00 27.09  ? 1029 LEU   A CA    1 
ATOM   5039  C  C     . LEU   A 1 1029 ? 187.851 143.923 117.354 1.00 35.10  ? 1029 LEU   A C     1 
ATOM   5040  O  O     . LEU   A 1 1029 ? 188.913 144.277 116.831 1.00 54.98  ? 1029 LEU   A O     1 
ATOM   5041  C  CB    . LEU   A 1 1029 ? 187.857 141.515 116.729 1.00 32.75  ? 1029 LEU   A CB    1 
ATOM   5042  C  CG    . LEU   A 1 1029 ? 187.296 140.117 116.992 1.00 31.88  ? 1029 LEU   A CG    1 
ATOM   5043  C  CD1   . LEU   A 1 1029 ? 186.998 139.404 115.686 1.00 27.77  ? 1029 LEU   A CD1   1 
ATOM   5044  C  CD2   . LEU   A 1 1029 ? 188.263 139.301 117.834 1.00 33.02  ? 1029 LEU   A CD2   1 
ATOM   5045  N  N     . PHE   A 1 1030 ? 186.806 144.735 117.465 1.00 22.24  ? 1030 PHE   A N     1 
ATOM   5046  C  CA    . PHE   A 1 1030 ? 186.846 146.116 117.015 1.00 23.13  ? 1030 PHE   A CA    1 
ATOM   5047  C  C     . PHE   A 1 1030 ? 186.173 146.980 118.066 1.00 31.96  ? 1030 PHE   A C     1 
ATOM   5048  O  O     . PHE   A 1 1030 ? 185.151 146.592 118.639 1.00 44.08  ? 1030 PHE   A O     1 
ATOM   5049  C  CB    . PHE   A 1 1030 ? 186.160 146.280 115.654 1.00 31.54  ? 1030 PHE   A CB    1 
ATOM   5050  C  CG    . PHE   A 1 1030 ? 186.472 145.174 114.686 1.00 40.40  ? 1030 PHE   A CG    1 
ATOM   5051  C  CD1   . PHE   A 1 1030 ? 187.639 145.192 113.941 1.00 43.05  ? 1030 PHE   A CD1   1 
ATOM   5052  C  CD2   . PHE   A 1 1030 ? 185.597 144.117 114.521 1.00 40.15  ? 1030 PHE   A CD2   1 
ATOM   5053  C  CE1   . PHE   A 1 1030 ? 187.927 144.173 113.053 1.00 38.11  ? 1030 PHE   A CE1   1 
ATOM   5054  C  CE2   . PHE   A 1 1030 ? 185.880 143.096 113.633 1.00 42.88  ? 1030 PHE   A CE2   1 
ATOM   5055  C  CZ    . PHE   A 1 1030 ? 187.046 143.125 112.898 1.00 38.51  ? 1030 PHE   A CZ    1 
ATOM   5056  N  N     . ASP   A 1 1031 ? 186.752 148.149 118.322 1.00 25.48  ? 1031 ASP   A N     1 
ATOM   5057  C  CA    . ASP   A 1 1031 ? 186.289 149.004 119.407 1.00 29.43  ? 1031 ASP   A CA    1 
ATOM   5058  C  C     . ASP   A 1 1031 ? 185.051 149.766 118.949 1.00 34.07  ? 1031 ASP   A C     1 
ATOM   5059  O  O     . ASP   A 1 1031 ? 185.151 150.732 118.186 1.00 39.22  ? 1031 ASP   A O     1 
ATOM   5060  C  CB    . ASP   A 1 1031 ? 187.398 149.955 119.846 1.00 27.12  ? 1031 ASP   A CB    1 
ATOM   5061  C  CG    . ASP   A 1 1031 ? 186.933 150.941 120.895 1.00 39.29  ? 1031 ASP   A CG    1 
ATOM   5062  O  OD1   . ASP   A 1 1031 ? 186.135 150.541 121.767 1.00 45.02  ? 1031 ASP   A OD1   1 
ATOM   5063  O  OD2   . ASP   A 1 1031 ? 187.365 152.111 120.853 1.00 44.81  ? 1031 ASP   A OD2   1 
ATOM   5064  N  N     . ASP   A 1 1032 ? 183.884 149.328 119.414 1.00 31.74  ? 1032 ASP   A N     1 
ATOM   5065  C  CA    . ASP   A 1 1032 ? 182.615 149.976 119.119 1.00 27.60  ? 1032 ASP   A CA    1 
ATOM   5066  C  C     . ASP   A 1 1032 ? 182.207 150.967 120.199 1.00 35.44  ? 1032 ASP   A C     1 
ATOM   5067  O  O     . ASP   A 1 1032 ? 181.094 151.500 120.151 1.00 38.92  ? 1032 ASP   A O     1 
ATOM   5068  C  CB    . ASP   A 1 1032 ? 181.519 148.926 118.935 1.00 28.69  ? 1032 ASP   A CB    1 
ATOM   5069  C  CG    . ASP   A 1 1032 ? 181.426 147.968 120.108 1.00 37.44  ? 1032 ASP   A CG    1 
ATOM   5070  O  OD1   . ASP   A 1 1032 ? 181.893 148.324 121.209 1.00 38.73  ? 1032 ASP   A OD1   1 
ATOM   5071  O  OD2   . ASP   A 1 1032 ? 180.885 146.857 119.931 1.00 45.71  ? 1032 ASP   A OD2   1 
ATOM   5072  N  N     . GLY   A 1 1033 ? 183.079 151.224 121.170 1.00 30.43  ? 1033 GLY   A N     1 
ATOM   5073  C  CA    . GLY   A 1 1033 ? 182.751 152.036 122.319 1.00 23.91  ? 1033 GLY   A CA    1 
ATOM   5074  C  C     . GLY   A 1 1033 ? 182.503 151.257 123.593 1.00 27.14  ? 1033 GLY   A C     1 
ATOM   5075  O  O     . GLY   A 1 1033 ? 182.372 151.874 124.657 1.00 33.13  ? 1033 GLY   A O     1 
ATOM   5076  N  N     . GLY   A 1 1034 ? 182.431 149.931 123.521 1.00 24.48  ? 1034 GLY   A N     1 
ATOM   5077  C  CA    . GLY   A 1 1034 ? 182.312 149.091 124.700 1.00 28.44  ? 1034 GLY   A CA    1 
ATOM   5078  C  C     . GLY   A 1 1034 ? 181.018 148.313 124.819 1.00 26.08  ? 1034 GLY   A C     1 
ATOM   5079  O  O     . GLY   A 1 1034 ? 180.898 147.491 125.739 1.00 29.76  ? 1034 GLY   A O     1 
ATOM   5080  N  N     . LEU   A 1 1035 ? 180.039 148.526 123.937 1.00 19.58  ? 1035 LEU   A N     1 
ATOM   5081  C  CA    . LEU   A 1 1035 ? 178.770 147.814 124.058 1.00 21.74  ? 1035 LEU   A CA    1 
ATOM   5082  C  C     . LEU   A 1 1035 ? 178.975 146.304 124.045 1.00 29.11  ? 1035 LEU   A C     1 
ATOM   5083  O  O     . LEU   A 1 1035 ? 178.287 145.568 124.766 1.00 30.20  ? 1035 LEU   A O     1 
ATOM   5084  C  CB    . LEU   A 1 1035 ? 177.824 148.236 122.935 1.00 24.60  ? 1035 LEU   A CB    1 
ATOM   5085  C  CG    . LEU   A 1 1035 ? 176.379 147.749 123.058 1.00 22.98  ? 1035 LEU   A CG    1 
ATOM   5086  C  CD1   . LEU   A 1 1035 ? 175.652 148.510 124.153 1.00 20.60  ? 1035 LEU   A CD1   1 
ATOM   5087  C  CD2   . LEU   A 1 1035 ? 175.649 147.884 121.735 1.00 20.10  ? 1035 LEU   A CD2   1 
ATOM   5088  N  N     . THR   A 1 1036 ? 179.925 145.825 123.236 1.00 24.15  ? 1036 THR   A N     1 
ATOM   5089  C  CA    . THR   A 1 1036 ? 180.164 144.389 123.138 1.00 26.26  ? 1036 THR   A CA    1 
ATOM   5090  C  C     . THR   A 1 1036 ? 180.561 143.796 124.482 1.00 32.32  ? 1036 THR   A C     1 
ATOM   5091  O  O     . THR   A 1 1036 ? 180.256 142.631 124.760 1.00 36.99  ? 1036 THR   A O     1 
ATOM   5092  C  CB    . THR   A 1 1036 ? 181.244 144.105 122.094 1.00 27.61  ? 1036 THR   A CB    1 
ATOM   5093  O  OG1   . THR   A 1 1036 ? 181.045 144.954 120.958 1.00 36.85  ? 1036 THR   A OG1   1 
ATOM   5094  C  CG2   . THR   A 1 1036 ? 181.185 142.652 121.647 1.00 29.32  ? 1036 THR   A CG2   1 
ATOM   5095  N  N     . LEU   A 1 1037 ? 181.245 144.572 125.320 1.00 25.24  ? 1037 LEU   A N     1 
ATOM   5096  C  CA    . LEU   A 1 1037 ? 181.564 144.137 126.673 1.00 29.64  ? 1037 LEU   A CA    1 
ATOM   5097  C  C     . LEU   A 1 1037 ? 180.462 144.464 127.668 1.00 27.79  ? 1037 LEU   A C     1 
ATOM   5098  O  O     . LEU   A 1 1037 ? 180.231 143.689 128.602 1.00 35.66  ? 1037 LEU   A O     1 
ATOM   5099  C  CB    . LEU   A 1 1037 ? 182.876 144.773 127.137 1.00 30.61  ? 1037 LEU   A CB    1 
ATOM   5100  C  CG    . LEU   A 1 1037 ? 184.100 143.865 127.056 1.00 33.85  ? 1037 LEU   A CG    1 
ATOM   5101  C  CD1   . LEU   A 1 1037 ? 183.870 142.600 127.862 1.00 31.10  ? 1037 LEU   A CD1   1 
ATOM   5102  C  CD2   . LEU   A 1 1037 ? 184.398 143.522 125.611 1.00 34.15  ? 1037 LEU   A CD2   1 
ATOM   5103  N  N     . LEU   A 1 1038 ? 179.776 145.594 127.487 1.00 15.55  ? 1038 LEU   A N     1 
ATOM   5104  C  CA    . LEU   A 1 1038 ? 178.744 145.991 128.438 1.00 27.72  ? 1038 LEU   A CA    1 
ATOM   5105  C  C     . LEU   A 1 1038 ? 177.587 144.998 128.453 1.00 22.91  ? 1038 LEU   A C     1 
ATOM   5106  O  O     . LEU   A 1 1038 ? 177.033 144.704 129.518 1.00 25.80  ? 1038 LEU   A O     1 
ATOM   5107  C  CB    . LEU   A 1 1038 ? 178.244 147.398 128.113 1.00 22.96  ? 1038 LEU   A CB    1 
ATOM   5108  C  CG    . LEU   A 1 1038 ? 177.195 147.993 129.055 1.00 25.80  ? 1038 LEU   A CG    1 
ATOM   5109  C  CD1   . LEU   A 1 1038 ? 177.706 148.020 130.486 1.00 26.53  ? 1038 LEU   A CD1   1 
ATOM   5110  C  CD2   . LEU   A 1 1038 ? 176.801 149.388 128.605 1.00 26.77  ? 1038 LEU   A CD2   1 
ATOM   5111  N  N     . ILE   A 1 1039 ? 177.201 144.474 127.286 1.00 13.18  ? 1039 ILE   A N     1 
ATOM   5112  C  CA    . ILE   A 1 1039 ? 176.061 143.554 127.237 1.00 26.99  ? 1039 ILE   A CA    1 
ATOM   5113  C  C     . ILE   A 1 1039 ? 176.331 142.266 128.004 1.00 34.99  ? 1039 ILE   A C     1 
ATOM   5114  O  O     . ILE   A 1 1039 ? 175.508 141.899 128.863 1.00 36.87  ? 1039 ILE   A O     1 
ATOM   5115  C  CB    . ILE   A 1 1039 ? 175.658 143.293 125.772 1.00 28.42  ? 1039 ILE   A CB    1 
ATOM   5116  C  CG1   . ILE   A 1 1039 ? 174.728 144.400 125.275 1.00 26.22  ? 1039 ILE   A CG1   1 
ATOM   5117  C  CG2   . ILE   A 1 1039 ? 174.982 141.934 125.639 1.00 23.26  ? 1039 ILE   A CG2   1 
ATOM   5118  C  CD1   . ILE   A 1 1039 ? 174.314 144.246 123.830 1.00 19.55  ? 1039 ILE   A CD1   1 
ATOM   5119  N  N     . PRO   A 1 1040 ? 177.425 141.539 127.766 1.00 24.45  ? 1040 PRO   A N     1 
ATOM   5120  C  CA    . PRO   A 1 1040 ? 177.648 140.295 128.523 1.00 24.03  ? 1040 PRO   A CA    1 
ATOM   5121  C  C     . PRO   A 1 1040 ? 177.858 140.527 130.007 1.00 26.86  ? 1040 PRO   A C     1 
ATOM   5122  O  O     . PRO   A 1 1040 ? 177.500 139.665 130.818 1.00 32.73  ? 1040 PRO   A O     1 
ATOM   5123  C  CB    . PRO   A 1 1040 ? 178.890 139.679 127.862 1.00 22.54  ? 1040 PRO   A CB    1 
ATOM   5124  C  CG    . PRO   A 1 1040 ? 179.414 140.680 126.905 1.00 20.92  ? 1040 PRO   A CG    1 
ATOM   5125  C  CD    . PRO   A 1 1040 ? 178.559 141.897 126.899 1.00 18.98  ? 1040 PRO   A CD    1 
ATOM   5126  N  N     . TYR   A 1 1041 ? 178.437 141.664 130.395 1.00 15.82  ? 1041 TYR   A N     1 
ATOM   5127  C  CA    . TYR   A 1 1041 ? 178.550 141.972 131.815 1.00 19.55  ? 1041 TYR   A CA    1 
ATOM   5128  C  C     . TYR   A 1 1041 ? 177.171 142.107 132.449 1.00 27.30  ? 1041 TYR   A C     1 
ATOM   5129  O  O     . TYR   A 1 1041 ? 176.923 141.582 133.543 1.00 42.28  ? 1041 TYR   A O     1 
ATOM   5130  C  CB    . TYR   A 1 1041 ? 179.366 143.248 132.016 1.00 29.74  ? 1041 TYR   A CB    1 
ATOM   5131  C  CG    . TYR   A 1 1041 ? 179.162 143.883 133.369 1.00 33.60  ? 1041 TYR   A CG    1 
ATOM   5132  C  CD1   . TYR   A 1 1041 ? 179.663 143.286 134.517 1.00 33.00  ? 1041 TYR   A CD1   1 
ATOM   5133  C  CD2   . TYR   A 1 1041 ? 178.460 145.072 133.502 1.00 31.09  ? 1041 TYR   A CD2   1 
ATOM   5134  C  CE1   . TYR   A 1 1041 ? 179.477 143.858 135.757 1.00 34.22  ? 1041 TYR   A CE1   1 
ATOM   5135  C  CE2   . TYR   A 1 1041 ? 178.268 145.651 134.738 1.00 31.04  ? 1041 TYR   A CE2   1 
ATOM   5136  C  CZ    . TYR   A 1 1041 ? 178.778 145.039 135.862 1.00 37.41  ? 1041 TYR   A CZ    1 
ATOM   5137  O  OH    . TYR   A 1 1041 ? 178.591 145.610 137.098 1.00 43.83  ? 1041 TYR   A OH    1 
ATOM   5138  N  N     . LEU   A 1 1042 ? 176.255 142.801 131.772 1.00 29.08  ? 1042 LEU   A N     1 
ATOM   5139  C  CA    . LEU   A 1 1042 ? 174.886 142.886 132.265 1.00 21.19  ? 1042 LEU   A CA    1 
ATOM   5140  C  C     . LEU   A 1 1042 ? 174.240 141.508 132.316 1.00 25.71  ? 1042 LEU   A C     1 
ATOM   5141  O  O     . LEU   A 1 1042 ? 173.453 141.216 133.223 1.00 30.30  ? 1042 LEU   A O     1 
ATOM   5142  C  CB    . LEU   A 1 1042 ? 174.071 143.836 131.390 1.00 16.91  ? 1042 LEU   A CB    1 
ATOM   5143  C  CG    . LEU   A 1 1042 ? 174.422 145.320 131.517 1.00 21.43  ? 1042 LEU   A CG    1 
ATOM   5144  C  CD1   . LEU   A 1 1042 ? 173.762 146.127 130.411 1.00 26.08  ? 1042 LEU   A CD1   1 
ATOM   5145  C  CD2   . LEU   A 1 1042 ? 174.027 145.856 132.884 1.00 23.82  ? 1042 LEU   A CD2   1 
ATOM   5146  N  N     . LEU   A 1 1043 ? 174.555 140.648 131.346 1.00 31.00  ? 1043 LEU   A N     1 
ATOM   5147  C  CA    . LEU   A 1 1043 ? 174.104 139.262 131.423 1.00 32.95  ? 1043 LEU   A CA    1 
ATOM   5148  C  C     . LEU   A 1 1043 ? 174.575 138.613 132.717 1.00 34.38  ? 1043 LEU   A C     1 
ATOM   5149  O  O     . LEU   A 1 1043 ? 173.799 137.961 133.424 1.00 35.45  ? 1043 LEU   A O     1 
ATOM   5150  C  CB    . LEU   A 1 1043 ? 174.614 138.474 130.216 1.00 29.78  ? 1043 LEU   A CB    1 
ATOM   5151  C  CG    . LEU   A 1 1043 ? 173.743 138.441 128.962 1.00 38.08  ? 1043 LEU   A CG    1 
ATOM   5152  C  CD1   . LEU   A 1 1043 ? 174.194 137.319 128.042 1.00 32.91  ? 1043 LEU   A CD1   1 
ATOM   5153  C  CD2   . LEU   A 1 1043 ? 172.285 138.271 129.337 1.00 36.51  ? 1043 LEU   A CD2   1 
ATOM   5154  N  N     . THR   A 1 1044 ? 175.858 138.780 133.036 1.00 34.23  ? 1044 THR   A N     1 
ATOM   5155  C  CA    . THR   A 1 1044 ? 176.409 138.228 134.267 1.00 29.18  ? 1044 THR   A CA    1 
ATOM   5156  C  C     . THR   A 1 1044 ? 175.776 138.846 135.506 1.00 30.31  ? 1044 THR   A C     1 
ATOM   5157  O  O     . THR   A 1 1044 ? 175.778 138.219 136.570 1.00 35.34  ? 1044 THR   A O     1 
ATOM   5158  C  CB    . THR   A 1 1044 ? 177.924 138.432 134.304 1.00 32.50  ? 1044 THR   A CB    1 
ATOM   5159  O  OG1   . THR   A 1 1044 ? 178.217 139.834 134.317 1.00 35.65  ? 1044 THR   A OG1   1 
ATOM   5160  C  CG2   . THR   A 1 1044 ? 178.574 137.801 133.084 1.00 26.96  ? 1044 THR   A CG2   1 
ATOM   5161  N  N     . THR   A 1 1045 ? 175.236 140.061 135.391 1.00 39.56  ? 1045 THR   A N     1 
ATOM   5162  C  CA    . THR   A 1 1045 ? 174.599 140.726 136.521 1.00 34.15  ? 1045 THR   A CA    1 
ATOM   5163  C  C     . THR   A 1 1045 ? 173.276 140.084 136.926 1.00 36.49  ? 1045 THR   A C     1 
ATOM   5164  O  O     . THR   A 1 1045 ? 172.745 140.422 137.989 1.00 42.30  ? 1045 THR   A O     1 
ATOM   5165  C  CB    . THR   A 1 1045 ? 174.376 142.207 136.194 1.00 36.16  ? 1045 THR   A CB    1 
ATOM   5166  O  OG1   . THR   A 1 1045 ? 175.623 142.809 135.830 1.00 36.93  ? 1045 THR   A OG1   1 
ATOM   5167  C  CG2   . THR   A 1 1045 ? 173.802 142.947 137.388 1.00 36.12  ? 1045 THR   A CG2   1 
ATOM   5168  N  N     . LYS   A 1 1046 ? 172.740 139.171 136.124 1.00 44.60  ? 1046 LYS   A N     1 
ATOM   5169  C  CA    . LYS   A 1 1046 ? 171.450 138.555 136.394 1.00 37.01  ? 1046 LYS   A CA    1 
ATOM   5170  C  C     . LYS   A 1 1046 ? 171.630 137.172 137.010 1.00 41.98  ? 1046 LYS   A C     1 
ATOM   5171  O  O     . LYS   A 1 1046 ? 172.695 136.558 136.923 1.00 49.87  ? 1046 LYS   A O     1 
ATOM   5172  C  CB    . LYS   A 1 1046 ? 170.617 138.456 135.114 1.00 41.16  ? 1046 LYS   A CB    1 
ATOM   5173  C  CG    . LYS   A 1 1046 ? 170.159 139.798 134.572 1.00 41.99  ? 1046 LYS   A CG    1 
ATOM   5174  C  CD    . LYS   A 1 1046 ? 170.158 140.857 135.660 1.00 40.59  ? 1046 LYS   A CD    1 
ATOM   5175  C  CE    . LYS   A 1 1046 ? 169.327 142.058 135.255 1.00 40.59  ? 1046 LYS   A CE    1 
ATOM   5176  N  NZ    . LYS   A 1 1046 ? 170.058 142.936 134.305 1.00 41.86  ? 1046 LYS   A NZ    1 
ATOM   5177  N  N     . LYS   A 1 1047 ? 170.559 136.687 137.642 1.00 43.31  ? 1047 LYS   A N     1 
ATOM   5178  C  CA    . LYS   A 1 1047 ? 170.619 135.410 138.342 1.00 41.36  ? 1047 LYS   A CA    1 
ATOM   5179  C  C     . LYS   A 1 1047 ? 170.621 134.221 137.392 1.00 47.16  ? 1047 LYS   A C     1 
ATOM   5180  O  O     . LYS   A 1 1047 ? 170.978 133.114 137.808 1.00 52.08  ? 1047 LYS   A O     1 
ATOM   5181  C  CB    . LYS   A 1 1047 ? 169.448 135.291 139.318 1.00 39.39  ? 1047 LYS   A CB    1 
ATOM   5182  N  N     . LYS   A 1 1048 ? 170.231 134.416 136.131 1.00 44.40  ? 1048 LYS   A N     1 
ATOM   5183  C  CA    . LYS   A 1 1048 ? 170.239 133.312 135.180 1.00 44.11  ? 1048 LYS   A CA    1 
ATOM   5184  C  C     . LYS   A 1 1048 ? 171.637 133.024 134.648 1.00 45.01  ? 1048 LYS   A C     1 
ATOM   5185  O  O     . LYS   A 1 1048 ? 171.913 131.896 134.225 1.00 47.38  ? 1048 LYS   A O     1 
ATOM   5186  C  CB    . LYS   A 1 1048 ? 169.289 133.607 134.019 1.00 48.74  ? 1048 LYS   A CB    1 
ATOM   5187  C  CG    . LYS   A 1 1048 ? 168.641 132.370 133.423 1.00 46.65  ? 1048 LYS   A CG    1 
ATOM   5188  C  CD    . LYS   A 1 1048 ? 168.403 132.535 131.934 1.00 50.54  ? 1048 LYS   A CD    1 
ATOM   5189  C  CE    . LYS   A 1 1048 ? 167.755 131.295 131.345 1.00 53.19  ? 1048 LYS   A CE    1 
ATOM   5190  N  NZ    . LYS   A 1 1048 ? 168.743 130.432 130.644 1.00 55.95  ? 1048 LYS   A NZ    1 
ATOM   5191  N  N     . TRP   A 1 1049 ? 172.523 134.021 134.658 1.00 43.14  ? 1049 TRP   A N     1 
ATOM   5192  C  CA    . TRP   A 1 1049 ? 173.892 133.863 134.177 1.00 46.23  ? 1049 TRP   A CA    1 
ATOM   5193  C  C     . TRP   A 1 1049 ? 174.917 134.181 135.259 1.00 42.99  ? 1049 TRP   A C     1 
ATOM   5194  O  O     . TRP   A 1 1049 ? 176.065 134.511 134.943 1.00 49.51  ? 1049 TRP   A O     1 
ATOM   5195  C  CB    . TRP   A 1 1049 ? 174.130 134.741 132.947 1.00 49.14  ? 1049 TRP   A CB    1 
ATOM   5196  C  CG    . TRP   A 1 1049 ? 172.978 134.756 131.994 1.00 45.03  ? 1049 TRP   A CG    1 
ATOM   5197  C  CD1   . TRP   A 1 1049 ? 171.967 135.669 131.947 1.00 41.09  ? 1049 TRP   A CD1   1 
ATOM   5198  C  CD2   . TRP   A 1 1049 ? 172.715 133.811 130.951 1.00 41.12  ? 1049 TRP   A CD2   1 
ATOM   5199  N  NE1   . TRP   A 1 1049 ? 171.089 135.351 130.940 1.00 38.31  ? 1049 TRP   A NE1   1 
ATOM   5200  C  CE2   . TRP   A 1 1049 ? 171.526 134.215 130.313 1.00 45.16  ? 1049 TRP   A CE2   1 
ATOM   5201  C  CE3   . TRP   A 1 1049 ? 173.369 132.663 130.494 1.00 41.67  ? 1049 TRP   A CE3   1 
ATOM   5202  C  CZ2   . TRP   A 1 1049 ? 170.978 133.513 129.243 1.00 47.55  ? 1049 TRP   A CZ2   1 
ATOM   5203  C  CZ3   . TRP   A 1 1049 ? 172.823 131.967 129.432 1.00 46.63  ? 1049 TRP   A CZ3   1 
ATOM   5204  C  CH2   . TRP   A 1 1049 ? 171.639 132.395 128.818 1.00 48.34  ? 1049 TRP   A CH2   1 
ATOM   5205  N  N     . LYS   A 1 1050 ? 174.527 134.089 136.531 1.00 47.17  ? 1050 LYS   A N     1 
ATOM   5206  C  CA    . LYS   A 1 1050 ? 175.455 134.407 137.612 1.00 46.61  ? 1050 LYS   A CA    1 
ATOM   5207  C  C     . LYS   A 1 1050 ? 176.641 133.451 137.624 1.00 48.54  ? 1050 LYS   A C     1 
ATOM   5208  O  O     . LYS   A 1 1050 ? 177.780 133.869 137.861 1.00 50.60  ? 1050 LYS   A O     1 
ATOM   5209  C  CB    . LYS   A 1 1050 ? 174.728 134.377 138.955 1.00 49.08  ? 1050 LYS   A CB    1 
ATOM   5210  C  CG    . LYS   A 1 1050 ? 175.146 135.484 139.906 1.00 51.17  ? 1050 LYS   A CG    1 
ATOM   5211  C  CD    . LYS   A 1 1050 ? 174.871 136.855 139.313 1.00 52.05  ? 1050 LYS   A CD    1 
ATOM   5212  C  CE    . LYS   A 1 1050 ? 174.657 137.890 140.404 1.00 52.55  ? 1050 LYS   A CE    1 
ATOM   5213  N  NZ    . LYS   A 1 1050 ? 173.435 137.608 141.207 1.00 47.49  ? 1050 LYS   A NZ    1 
ATOM   5214  N  N     . ASP   A 1 1051 ? 176.397 132.167 137.368 1.00 50.61  ? 1051 ASP   A N     1 
ATOM   5215  C  CA    . ASP   A 1 1051 ? 177.455 131.167 137.403 1.00 49.12  ? 1051 ASP   A CA    1 
ATOM   5216  C  C     . ASP   A 1 1051 ? 178.325 131.169 136.152 1.00 45.96  ? 1051 ASP   A C     1 
ATOM   5217  O  O     . ASP   A 1 1051 ? 179.327 130.447 136.117 1.00 50.67  ? 1051 ASP   A O     1 
ATOM   5218  C  CB    . ASP   A 1 1051 ? 176.854 129.774 137.604 1.00 50.09  ? 1051 ASP   A CB    1 
ATOM   5219  N  N     . CYS   A 1 1052 ? 177.974 131.950 135.135 1.00 49.86  ? 1052 CYS   A N     1 
ATOM   5220  C  CA    . CYS   A 1 1052 ? 178.732 131.992 133.892 1.00 52.71  ? 1052 CYS   A CA    1 
ATOM   5221  C  C     . CYS   A 1 1052 ? 179.895 132.965 134.026 1.00 53.06  ? 1052 CYS   A C     1 
ATOM   5222  O  O     . CYS   A 1 1052 ? 179.714 134.102 134.474 1.00 52.22  ? 1052 CYS   A O     1 
ATOM   5223  C  CB    . CYS   A 1 1052 ? 177.833 132.400 132.725 1.00 48.83  ? 1052 CYS   A CB    1 
ATOM   5224  S  SG    . CYS   A 1 1052 ? 176.800 131.067 132.078 1.00 62.96  ? 1052 CYS   A SG    1 
ATOM   5225  N  N     . LYS   A 1 1053 ? 181.084 132.517 133.635 1.00 44.11  ? 1053 LYS   A N     1 
ATOM   5226  C  CA    . LYS   A 1 1053 ? 182.293 133.324 133.711 1.00 45.01  ? 1053 LYS   A CA    1 
ATOM   5227  C  C     . LYS   A 1 1053 ? 182.637 133.863 132.330 1.00 44.80  ? 1053 LYS   A C     1 
ATOM   5228  O  O     . LYS   A 1 1053 ? 182.530 133.149 131.330 1.00 45.02  ? 1053 LYS   A O     1 
ATOM   5229  C  CB    . LYS   A 1 1053 ? 183.463 132.506 134.259 1.00 43.69  ? 1053 LYS   A CB    1 
ATOM   5230  C  CG    . LYS   A 1 1053 ? 183.211 131.902 135.634 1.00 48.48  ? 1053 LYS   A CG    1 
ATOM   5231  C  CD    . LYS   A 1 1053 ? 184.245 130.838 135.993 1.00 52.08  ? 1053 LYS   A CD    1 
ATOM   5232  C  CE    . LYS   A 1 1053 ? 184.542 129.879 134.840 1.00 51.48  ? 1053 LYS   A CE    1 
ATOM   5233  N  NZ    . LYS   A 1 1053 ? 183.418 129.705 133.872 1.00 46.38  ? 1053 LYS   A NZ    1 
ATOM   5234  N  N     . ILE   A 1 1054 ? 183.041 135.126 132.279 1.00 36.50  ? 1054 ILE   A N     1 
ATOM   5235  C  CA    . ILE   A 1 1054 ? 183.333 135.798 131.019 1.00 33.10  ? 1054 ILE   A CA    1 
ATOM   5236  C  C     . ILE   A 1 1054 ? 184.769 135.489 130.618 1.00 35.37  ? 1054 ILE   A C     1 
ATOM   5237  O  O     . ILE   A 1 1054 ? 185.707 135.771 131.372 1.00 43.65  ? 1054 ILE   A O     1 
ATOM   5238  C  CB    . ILE   A 1 1054 ? 183.113 137.312 131.133 1.00 29.70  ? 1054 ILE   A CB    1 
ATOM   5239  C  CG1   . ILE   A 1 1054 ? 181.649 137.663 130.869 1.00 38.08  ? 1054 ILE   A CG1   1 
ATOM   5240  C  CG2   . ILE   A 1 1054 ? 184.016 138.048 130.162 1.00 29.08  ? 1054 ILE   A CG2   1 
ATOM   5241  C  CD1   . ILE   A 1 1054 ? 181.240 139.011 131.415 1.00 39.85  ? 1054 ILE   A CD1   1 
ATOM   5242  N  N     . ARG   A 1 1055 ? 184.945 134.913 129.432 1.00 33.71  ? 1055 ARG   A N     1 
ATOM   5243  C  CA    . ARG   A 1 1055 ? 186.264 134.735 128.843 1.00 29.72  ? 1055 ARG   A CA    1 
ATOM   5244  C  C     . ARG   A 1 1055 ? 186.320 135.510 127.535 1.00 26.97  ? 1055 ARG   A C     1 
ATOM   5245  O  O     . ARG   A 1 1055 ? 185.382 135.453 126.731 1.00 41.73  ? 1055 ARG   A O     1 
ATOM   5246  C  CB    . ARG   A 1 1055 ? 186.594 133.257 128.625 1.00 29.35  ? 1055 ARG   A CB    1 
ATOM   5247  C  CG    . ARG   A 1 1055 ? 185.751 132.551 127.591 1.00 36.81  ? 1055 ARG   A CG    1 
ATOM   5248  C  CD    . ARG   A 1 1055 ? 185.811 131.050 127.813 1.00 38.96  ? 1055 ARG   A CD    1 
ATOM   5249  N  NE    . ARG   A 1 1055 ? 186.801 130.405 126.958 1.00 43.73  ? 1055 ARG   A NE    1 
ATOM   5250  C  CZ    . ARG   A 1 1055 ? 186.648 129.210 126.405 1.00 40.26  ? 1055 ARG   A CZ    1 
ATOM   5251  N  NH1   . ARG   A 1 1055 ? 185.554 128.493 126.599 1.00 42.99  ? 1055 ARG   A NH1   1 
ATOM   5252  N  NH2   . ARG   A 1 1055 ? 187.619 128.721 125.640 1.00 38.61  ? 1055 ARG   A NH2   1 
ATOM   5253  N  N     . VAL   A 1 1056 ? 187.413 136.235 127.334 1.00 25.71  ? 1056 VAL   A N     1 
ATOM   5254  C  CA    . VAL   A 1 1056 ? 187.529 137.189 126.240 1.00 26.75  ? 1056 VAL   A CA    1 
ATOM   5255  C  C     . VAL   A 1 1056 ? 188.458 136.630 125.174 1.00 30.63  ? 1056 VAL   A C     1 
ATOM   5256  O  O     . VAL   A 1 1056 ? 189.408 135.896 125.466 1.00 24.01  ? 1056 VAL   A O     1 
ATOM   5257  C  CB    . VAL   A 1 1056 ? 188.030 138.558 126.744 1.00 21.54  ? 1056 VAL   A CB    1 
ATOM   5258  C  CG1   . VAL   A 1 1056 ? 188.378 139.462 125.576 1.00 21.87  ? 1056 VAL   A CG1   1 
ATOM   5259  C  CG2   . VAL   A 1 1056 ? 186.982 139.206 127.628 1.00 24.47  ? 1056 VAL   A CG2   1 
ATOM   5260  N  N     . PHE   A 1 1057 ? 188.168 136.983 123.924 1.00 33.80  ? 1057 PHE   A N     1 
ATOM   5261  C  CA    . PHE   A 1 1057 ? 188.994 136.632 122.779 1.00 24.55  ? 1057 PHE   A CA    1 
ATOM   5262  C  C     . PHE   A 1 1057 ? 189.346 137.907 122.033 1.00 28.01  ? 1057 PHE   A C     1 
ATOM   5263  O  O     . PHE   A 1 1057 ? 188.465 138.724 121.746 1.00 32.02  ? 1057 PHE   A O     1 
ATOM   5264  C  CB    . PHE   A 1 1057 ? 188.270 135.662 121.842 1.00 7.94   ? 1057 PHE   A CB    1 
ATOM   5265  C  CG    . PHE   A 1 1057 ? 187.950 134.340 122.467 1.00 15.24  ? 1057 PHE   A CG    1 
ATOM   5266  C  CD1   . PHE   A 1 1057 ? 186.872 134.205 123.323 1.00 19.39  ? 1057 PHE   A CD1   1 
ATOM   5267  C  CD2   . PHE   A 1 1057 ? 188.722 133.227 122.193 1.00 20.28  ? 1057 PHE   A CD2   1 
ATOM   5268  C  CE1   . PHE   A 1 1057 ? 186.575 132.988 123.898 1.00 23.50  ? 1057 PHE   A CE1   1 
ATOM   5269  C  CE2   . PHE   A 1 1057 ? 188.428 132.007 122.766 1.00 27.60  ? 1057 PHE   A CE2   1 
ATOM   5270  C  CZ    . PHE   A 1 1057 ? 187.354 131.888 123.619 1.00 31.07  ? 1057 PHE   A CZ    1 
ATOM   5271  N  N     . ILE   A 1 1058 ? 190.629 138.079 121.723 1.00 33.53  ? 1058 ILE   A N     1 
ATOM   5272  C  CA    . ILE   A 1 1058 ? 191.104 139.222 120.956 1.00 30.96  ? 1058 ILE   A CA    1 
ATOM   5273  C  C     . ILE   A 1 1058 ? 192.078 138.721 119.898 1.00 34.01  ? 1058 ILE   A C     1 
ATOM   5274  O  O     . ILE   A 1 1058 ? 192.533 137.578 119.929 1.00 36.07  ? 1058 ILE   A O     1 
ATOM   5275  C  CB    . ILE   A 1 1058 ? 191.765 140.295 121.846 1.00 35.71  ? 1058 ILE   A CB    1 
ATOM   5276  C  CG1   . ILE   A 1 1058 ? 192.789 139.660 122.788 1.00 37.08  ? 1058 ILE   A CG1   1 
ATOM   5277  C  CG2   . ILE   A 1 1058 ? 190.710 141.056 122.633 1.00 35.55  ? 1058 ILE   A CG2   1 
ATOM   5278  C  CD1   . ILE   A 1 1058 ? 194.086 140.429 122.884 1.00 32.43  ? 1058 ILE   A CD1   1 
ATOM   5279  N  N     . GLY   A 1 1059 ? 192.379 139.594 118.942 1.00 40.51  ? 1059 GLY   A N     1 
ATOM   5280  C  CA    . GLY   A 1 1059 ? 193.297 139.287 117.862 1.00 42.72  ? 1059 GLY   A CA    1 
ATOM   5281  C  C     . GLY   A 1 1059 ? 194.606 140.037 118.047 1.00 45.73  ? 1059 GLY   A C     1 
ATOM   5282  O  O     . GLY   A 1 1059 ? 194.610 141.235 118.333 1.00 55.76  ? 1059 GLY   A O     1 
ATOM   5283  N  N     . GLY   A 1 1060 ? 195.711 139.310 117.882 1.00 55.48  ? 1060 GLY   A N     1 
ATOM   5284  C  CA    . GLY   A 1 1060 ? 197.034 139.879 118.019 1.00 57.99  ? 1060 GLY   A CA    1 
ATOM   5285  C  C     . GLY   A 1 1060 ? 197.970 139.371 116.937 1.00 64.55  ? 1060 GLY   A C     1 
ATOM   5286  O  O     . GLY   A 1 1060 ? 197.565 138.657 116.018 1.00 65.53  ? 1060 GLY   A O     1 
ATOM   5287  N  N     . LYS   A 1 1061 ? 199.234 139.759 117.075 1.00 72.06  ? 1061 LYS   A N     1 
ATOM   5288  C  CA    . LYS   A 1 1061 ? 200.286 139.375 116.146 1.00 68.45  ? 1061 LYS   A CA    1 
ATOM   5289  C  C     . LYS   A 1 1061 ? 201.241 138.404 116.824 1.00 71.99  ? 1061 LYS   A C     1 
ATOM   5290  O  O     . LYS   A 1 1061 ? 201.628 138.605 117.979 1.00 76.25  ? 1061 LYS   A O     1 
ATOM   5291  C  CB    . LYS   A 1 1061 ? 201.050 140.605 115.648 1.00 66.34  ? 1061 LYS   A CB    1 
ATOM   5292  C  CG    . LYS   A 1 1061 ? 201.851 140.369 114.380 1.00 72.84  ? 1061 LYS   A CG    1 
ATOM   5293  C  CD    . LYS   A 1 1061 ? 200.936 140.141 113.188 1.00 76.41  ? 1061 LYS   A CD    1 
ATOM   5294  C  CE    . LYS   A 1 1061 ? 199.951 141.287 113.016 1.00 75.75  ? 1061 LYS   A CE    1 
ATOM   5295  N  NZ    . LYS   A 1 1061 ? 200.639 142.600 112.879 1.00 74.71  ? 1061 LYS   A NZ    1 
ATOM   5296  N  N     . ILE   A 1 1062 ? 201.615 137.345 116.101 1.00 75.45  ? 1062 ILE   A N     1 
ATOM   5297  C  CA    . ILE   A 1 1062 ? 202.550 136.372 116.649 1.00 78.57  ? 1062 ILE   A CA    1 
ATOM   5298  C  C     . ILE   A 1 1062 ? 203.841 137.077 117.037 1.00 77.20  ? 1062 ILE   A C     1 
ATOM   5299  O  O     . ILE   A 1 1062 ? 204.259 138.052 116.398 1.00 76.43  ? 1062 ILE   A O     1 
ATOM   5300  C  CB    . ILE   A 1 1062 ? 202.808 135.243 115.636 1.00 80.32  ? 1062 ILE   A CB    1 
ATOM   5301  C  CG1   . ILE   A 1 1062 ? 201.510 134.492 115.335 1.00 78.36  ? 1062 ILE   A CG1   1 
ATOM   5302  C  CG2   . ILE   A 1 1062 ? 203.864 134.283 116.162 1.00 77.24  ? 1062 ILE   A CG2   1 
ATOM   5303  C  CD1   . ILE   A 1 1062 ? 201.011 133.644 116.484 1.00 78.23  ? 1062 ILE   A CD1   1 
ATOM   5304  N  N     . ASN   A 1 1063 ? 204.479 136.586 118.096 1.00 80.58  ? 1063 ASN   A N     1 
ATOM   5305  C  CA    . ASN   A 1 1063 ? 205.656 137.172 118.732 1.00 83.52  ? 1063 ASN   A CA    1 
ATOM   5306  C  C     . ASN   A 1 1063 ? 205.266 138.361 119.603 1.00 83.35  ? 1063 ASN   A C     1 
ATOM   5307  O  O     . ASN   A 1 1063 ? 206.144 138.957 120.240 1.00 84.39  ? 1063 ASN   A O     1 
ATOM   5308  C  CB    . ASN   A 1 1063 ? 206.727 137.614 117.722 1.00 79.65  ? 1063 ASN   A CB    1 
ATOM   5309  N  N     . ARG   A 1 1064 ? 203.982 138.726 119.656 1.00 75.85  ? 1064 ARG   A N     1 
ATOM   5310  C  CA    . ARG   A 1 1064 ? 203.502 139.822 120.489 1.00 73.50  ? 1064 ARG   A CA    1 
ATOM   5311  C  C     . ARG   A 1 1064 ? 202.273 139.415 121.295 1.00 72.77  ? 1064 ARG   A C     1 
ATOM   5312  O  O     . ARG   A 1 1064 ? 201.505 140.281 121.725 1.00 71.72  ? 1064 ARG   A O     1 
ATOM   5313  C  CB    . ARG   A 1 1064 ? 203.189 141.051 119.630 1.00 71.37  ? 1064 ARG   A CB    1 
ATOM   5314  C  CG    . ARG   A 1 1064 ? 203.229 142.371 120.377 1.00 71.81  ? 1064 ARG   A CG    1 
ATOM   5315  C  CD    . ARG   A 1 1064 ? 203.354 143.541 119.411 1.00 71.89  ? 1064 ARG   A CD    1 
ATOM   5316  N  NE    . ARG   A 1 1064 ? 203.697 144.791 120.079 1.00 79.39  ? 1064 ARG   A NE    1 
ATOM   5317  C  CZ    . ARG   A 1 1064 ? 204.732 144.955 120.893 1.00 79.87  ? 1064 ARG   A CZ    1 
ATOM   5318  N  NH1   . ARG   A 1 1064 ? 205.565 143.963 121.161 1.00 76.45  ? 1064 ARG   A NH1   1 
ATOM   5319  N  NH2   . ARG   A 1 1064 ? 204.938 146.145 121.449 1.00 76.91  ? 1064 ARG   A NH2   1 
ATOM   5320  N  N     . ILE   A 1 1065 ? 202.074 138.113 121.506 1.00 65.61  ? 1065 ILE   A N     1 
ATOM   5321  C  CA    . ILE   A 1 1065 ? 200.859 137.636 122.160 1.00 65.27  ? 1065 ILE   A CA    1 
ATOM   5322  C  C     . ILE   A 1 1065 ? 200.797 138.118 123.604 1.00 66.49  ? 1065 ILE   A C     1 
ATOM   5323  O  O     . ILE   A 1 1065 ? 199.760 138.604 124.069 1.00 70.47  ? 1065 ILE   A O     1 
ATOM   5324  C  CB    . ILE   A 1 1065 ? 200.776 136.102 122.077 1.00 64.42  ? 1065 ILE   A CB    1 
ATOM   5325  C  CG1   . ILE   A 1 1065 ? 200.051 135.672 120.799 1.00 66.87  ? 1065 ILE   A CG1   1 
ATOM   5326  C  CG2   . ILE   A 1 1065 ? 200.081 135.540 123.306 1.00 62.78  ? 1065 ILE   A CG2   1 
ATOM   5327  C  CD1   . ILE   A 1 1065 ? 200.782 136.048 119.530 1.00 67.90  ? 1065 ILE   A CD1   1 
ATOM   5328  N  N     . ASP   A 1 1066 ? 201.904 137.985 124.338 1.00 63.39  ? 1066 ASP   A N     1 
ATOM   5329  C  CA    . ASP   A 1 1066 ? 201.886 138.310 125.761 1.00 64.03  ? 1066 ASP   A CA    1 
ATOM   5330  C  C     . ASP   A 1 1066 ? 201.669 139.800 125.995 1.00 59.83  ? 1066 ASP   A C     1 
ATOM   5331  O  O     . ASP   A 1 1066 ? 200.958 140.188 126.929 1.00 63.36  ? 1066 ASP   A O     1 
ATOM   5332  C  CB    . ASP   A 1 1066 ? 203.179 137.840 126.424 1.00 66.38  ? 1066 ASP   A CB    1 
ATOM   5333  C  CG    . ASP   A 1 1066 ? 203.379 136.342 126.310 1.00 70.06  ? 1066 ASP   A CG    1 
ATOM   5334  O  OD1   . ASP   A 1 1066 ? 202.524 135.589 126.821 1.00 68.38  ? 1066 ASP   A OD1   1 
ATOM   5335  O  OD2   . ASP   A 1 1066 ? 204.391 135.917 125.714 1.00 70.84  ? 1066 ASP   A OD2   1 
ATOM   5336  N  N     . HIS   A 1 1067 ? 202.279 140.652 125.171 1.00 53.18  ? 1067 HIS   A N     1 
ATOM   5337  C  CA    . HIS   A 1 1067 ? 202.084 142.090 125.324 1.00 53.77  ? 1067 HIS   A CA    1 
ATOM   5338  C  C     . HIS   A 1 1067 ? 200.615 142.463 125.158 1.00 61.91  ? 1067 HIS   A C     1 
ATOM   5339  O  O     . HIS   A 1 1067 ? 200.055 143.216 125.965 1.00 67.14  ? 1067 HIS   A O     1 
ATOM   5340  C  CB    . HIS   A 1 1067 ? 202.951 142.843 124.316 1.00 59.83  ? 1067 HIS   A CB    1 
ATOM   5341  C  CG    . HIS   A 1 1067 ? 202.815 144.331 124.393 1.00 62.14  ? 1067 HIS   A CG    1 
ATOM   5342  N  ND1   . HIS   A 1 1067 ? 202.348 145.089 123.342 1.00 60.46  ? 1067 HIS   A ND1   1 
ATOM   5343  C  CD2   . HIS   A 1 1067 ? 203.087 145.201 125.394 1.00 63.99  ? 1067 HIS   A CD2   1 
ATOM   5344  C  CE1   . HIS   A 1 1067 ? 202.337 146.363 123.692 1.00 61.58  ? 1067 HIS   A CE1   1 
ATOM   5345  N  NE2   . HIS   A 1 1067 ? 202.781 146.458 124.932 1.00 66.07  ? 1067 HIS   A NE2   1 
ATOM   5346  N  N     . ASP   A 1 1068 ? 199.971 141.934 124.117 1.00 58.67  ? 1068 ASP   A N     1 
ATOM   5347  C  CA    . ASP   A 1 1068 ? 198.565 142.242 123.885 1.00 52.14  ? 1068 ASP   A CA    1 
ATOM   5348  C  C     . ASP   A 1 1068 ? 197.681 141.651 124.976 1.00 50.66  ? 1068 ASP   A C     1 
ATOM   5349  O  O     . ASP   A 1 1068 ? 196.691 142.269 125.381 1.00 56.24  ? 1068 ASP   A O     1 
ATOM   5350  C  CB    . ASP   A 1 1068 ? 198.139 141.737 122.507 1.00 57.52  ? 1068 ASP   A CB    1 
ATOM   5351  C  CG    . ASP   A 1 1068 ? 198.550 142.677 121.390 1.00 63.15  ? 1068 ASP   A CG    1 
ATOM   5352  O  OD1   . ASP   A 1 1068 ? 199.133 143.740 121.690 1.00 60.22  ? 1068 ASP   A OD1   1 
ATOM   5353  O  OD2   . ASP   A 1 1068 ? 198.286 142.356 120.213 1.00 65.32  ? 1068 ASP   A OD2   1 
ATOM   5354  N  N     . ARG   A 1 1069 ? 198.016 140.453 125.459 1.00 45.63  ? 1069 ARG   A N     1 
ATOM   5355  C  CA    . ARG   A 1 1069 ? 197.255 139.868 126.557 1.00 41.71  ? 1069 ARG   A CA    1 
ATOM   5356  C  C     . ARG   A 1 1069 ? 197.339 140.736 127.805 1.00 45.74  ? 1069 ARG   A C     1 
ATOM   5357  O  O     . ARG   A 1 1069 ? 196.330 140.965 128.483 1.00 49.86  ? 1069 ARG   A O     1 
ATOM   5358  C  CB    . ARG   A 1 1069 ? 197.761 138.457 126.851 1.00 41.78  ? 1069 ARG   A CB    1 
ATOM   5359  C  CG    . ARG   A 1 1069 ? 197.320 137.910 128.195 1.00 47.89  ? 1069 ARG   A CG    1 
ATOM   5360  C  CD    . ARG   A 1 1069 ? 196.515 136.633 128.041 1.00 50.19  ? 1069 ARG   A CD    1 
ATOM   5361  N  NE    . ARG   A 1 1069 ? 197.266 135.599 127.340 1.00 57.16  ? 1069 ARG   A NE    1 
ATOM   5362  C  CZ    . ARG   A 1 1069 ? 198.349 135.004 127.821 1.00 60.71  ? 1069 ARG   A CZ    1 
ATOM   5363  N  NH1   . ARG   A 1 1069 ? 198.844 135.323 129.006 1.00 57.30  ? 1069 ARG   A NH1   1 
ATOM   5364  N  NH2   . ARG   A 1 1069 ? 198.951 134.066 127.095 1.00 55.46  ? 1069 ARG   A NH2   1 
ATOM   5365  N  N     . ARG   A 1 1070 ? 198.536 141.229 128.125 1.00 49.46  ? 1070 ARG   A N     1 
ATOM   5366  C  CA    . ARG   A 1 1070 ? 198.689 142.107 129.280 1.00 49.35  ? 1070 ARG   A CA    1 
ATOM   5367  C  C     . ARG   A 1 1070 ? 197.922 143.408 129.086 1.00 49.62  ? 1070 ARG   A C     1 
ATOM   5368  O  O     . ARG   A 1 1070 ? 197.297 143.915 130.024 1.00 53.86  ? 1070 ARG   A O     1 
ATOM   5369  C  CB    . ARG   A 1 1070 ? 200.169 142.386 129.538 1.00 51.11  ? 1070 ARG   A CB    1 
ATOM   5370  C  CG    . ARG   A 1 1070 ? 200.956 141.168 129.990 1.00 53.04  ? 1070 ARG   A CG    1 
ATOM   5371  C  CD    . ARG   A 1 1070 ? 202.276 141.565 130.632 1.00 49.97  ? 1070 ARG   A CD    1 
ATOM   5372  N  NE    . ARG   A 1 1070 ? 203.402 141.397 129.720 1.00 54.60  ? 1070 ARG   A NE    1 
ATOM   5373  C  CZ    . ARG   A 1 1070 ? 203.878 142.351 128.931 1.00 58.22  ? 1070 ARG   A CZ    1 
ATOM   5374  N  NH1   . ARG   A 1 1070 ? 203.351 143.564 128.918 1.00 58.21  ? 1070 ARG   A NH1   1 
ATOM   5375  N  NH2   . ARG   A 1 1070 ? 204.910 142.081 128.137 1.00 51.34  ? 1070 ARG   A NH2   1 
ATOM   5376  N  N     . ALA   A 1 1071 ? 197.965 143.970 127.876 1.00 34.16  ? 1071 ALA   A N     1 
ATOM   5377  C  CA    . ALA   A 1 1071 ? 197.217 145.196 127.619 1.00 38.31  ? 1071 ALA   A CA    1 
ATOM   5378  C  C     . ALA   A 1 1071 ? 195.719 144.975 127.798 1.00 42.39  ? 1071 ALA   A C     1 
ATOM   5379  O  O     . ALA   A 1 1071 ? 195.028 145.803 128.403 1.00 41.27  ? 1071 ALA   A O     1 
ATOM   5380  C  CB    . ALA   A 1 1071 ? 197.522 145.713 126.214 1.00 42.97  ? 1071 ALA   A CB    1 
ATOM   5381  N  N     . MET   A 1 1072 ? 195.201 143.859 127.280 1.00 42.02  ? 1072 MET   A N     1 
ATOM   5382  C  CA    . MET   A 1 1072 ? 193.782 143.558 127.435 1.00 35.47  ? 1072 MET   A CA    1 
ATOM   5383  C  C     . MET   A 1 1072 ? 193.419 143.343 128.897 1.00 42.41  ? 1072 MET   A C     1 
ATOM   5384  O  O     . MET   A 1 1072 ? 192.363 143.792 129.354 1.00 42.26  ? 1072 MET   A O     1 
ATOM   5385  C  CB    . MET   A 1 1072 ? 193.411 142.331 126.601 1.00 38.49  ? 1072 MET   A CB    1 
ATOM   5386  C  CG    . MET   A 1 1072 ? 191.923 142.190 126.282 1.00 42.61  ? 1072 MET   A CG    1 
ATOM   5387  S  SD    . MET   A 1 1072 ? 190.972 143.721 126.130 1.00 54.47  ? 1072 MET   A SD    1 
ATOM   5388  C  CE    . MET   A 1 1072 ? 192.119 144.803 125.282 1.00 44.99  ? 1072 MET   A CE    1 
ATOM   5389  N  N     . ALA   A 1 1073 ? 194.278 142.648 129.645 1.00 42.75  ? 1073 ALA   A N     1 
ATOM   5390  C  CA    . ALA   A 1 1073 ? 194.012 142.441 131.064 1.00 32.47  ? 1073 ALA   A CA    1 
ATOM   5391  C  C     . ALA   A 1 1073 ? 193.980 143.766 131.814 1.00 35.05  ? 1073 ALA   A C     1 
ATOM   5392  O  O     . ALA   A 1 1073 ? 193.100 143.990 132.653 1.00 41.67  ? 1073 ALA   A O     1 
ATOM   5393  C  CB    . ALA   A 1 1073 ? 195.061 141.507 131.664 1.00 30.72  ? 1073 ALA   A CB    1 
ATOM   5394  N  N     . THR   A 1 1074 ? 194.928 144.658 131.523 1.00 29.01  ? 1074 THR   A N     1 
ATOM   5395  C  CA    . THR   A 1 1074 ? 194.932 145.967 132.167 1.00 25.57  ? 1074 THR   A CA    1 
ATOM   5396  C  C     . THR   A 1 1074 ? 193.678 146.756 131.818 1.00 27.91  ? 1074 THR   A C     1 
ATOM   5397  O  O     . THR   A 1 1074 ? 193.064 147.383 132.690 1.00 37.82  ? 1074 THR   A O     1 
ATOM   5398  C  CB    . THR   A 1 1074 ? 196.183 146.749 131.767 1.00 33.82  ? 1074 THR   A CB    1 
ATOM   5399  O  OG1   . THR   A 1 1074 ? 197.348 145.968 132.058 1.00 40.98  ? 1074 THR   A OG1   1 
ATOM   5400  C  CG2   . THR   A 1 1074 ? 196.258 148.071 132.520 1.00 32.84  ? 1074 THR   A CG2   1 
ATOM   5401  N  N     . LEU   A 1 1075 ? 193.281 146.740 130.544 1.00 28.82  ? 1075 LEU   A N     1 
ATOM   5402  C  CA    . LEU   A 1 1075 ? 192.092 147.481 130.139 1.00 29.02  ? 1075 LEU   A CA    1 
ATOM   5403  C  C     . LEU   A 1 1075 ? 190.846 146.934 130.821 1.00 30.53  ? 1075 LEU   A C     1 
ATOM   5404  O  O     . LEU   A 1 1075 ? 189.996 147.701 131.288 1.00 27.12  ? 1075 LEU   A O     1 
ATOM   5405  C  CB    . LEU   A 1 1075 ? 191.939 147.437 128.619 1.00 24.45  ? 1075 LEU   A CB    1 
ATOM   5406  C  CG    . LEU   A 1 1075 ? 190.701 148.128 128.046 1.00 27.40  ? 1075 LEU   A CG    1 
ATOM   5407  C  CD1   . LEU   A 1 1075 ? 190.913 149.631 127.971 1.00 26.87  ? 1075 LEU   A CD1   1 
ATOM   5408  C  CD2   . LEU   A 1 1075 ? 190.354 147.565 126.681 1.00 33.20  ? 1075 LEU   A CD2   1 
ATOM   5409  N  N     . LEU   A 1 1076 ? 190.721 145.608 130.893 1.00 32.03  ? 1076 LEU   A N     1 
ATOM   5410  C  CA    . LEU   A 1 1076 ? 189.569 145.009 131.555 1.00 23.34  ? 1076 LEU   A CA    1 
ATOM   5411  C  C     . LEU   A 1 1076 ? 189.565 145.318 133.046 1.00 29.26  ? 1076 LEU   A C     1 
ATOM   5412  O  O     . LEU   A 1 1076 ? 188.505 145.566 133.631 1.00 38.92  ? 1076 LEU   A O     1 
ATOM   5413  C  CB    . LEU   A 1 1076 ? 189.556 143.501 131.312 1.00 30.21  ? 1076 LEU   A CB    1 
ATOM   5414  C  CG    . LEU   A 1 1076 ? 189.352 143.088 129.853 1.00 37.02  ? 1076 LEU   A CG    1 
ATOM   5415  C  CD1   . LEU   A 1 1076 ? 189.177 141.585 129.722 1.00 30.78  ? 1076 LEU   A CD1   1 
ATOM   5416  C  CD2   . LEU   A 1 1076 ? 188.161 143.818 129.266 1.00 25.85  ? 1076 LEU   A CD2   1 
ATOM   5417  N  N     . SER   A 1 1077 ? 190.739 145.305 133.681 1.00 28.94  ? 1077 SER   A N     1 
ATOM   5418  C  CA    . SER   A 1 1077 ? 190.815 145.648 135.096 1.00 21.92  ? 1077 SER   A CA    1 
ATOM   5419  C  C     . SER   A 1 1077 ? 190.404 147.095 135.333 1.00 25.34  ? 1077 SER   A C     1 
ATOM   5420  O  O     . SER   A 1 1077 ? 189.698 147.397 136.302 1.00 33.65  ? 1077 SER   A O     1 
ATOM   5421  C  CB    . SER   A 1 1077 ? 192.226 145.395 135.622 1.00 32.82  ? 1077 SER   A CB    1 
ATOM   5422  O  OG    . SER   A 1 1077 ? 192.400 144.033 135.966 1.00 48.64  ? 1077 SER   A OG    1 
ATOM   5423  N  N     . LYS   A 1 1078 ? 190.841 148.007 134.462 1.00 17.70  ? 1078 LYS   A N     1 
ATOM   5424  C  CA    . LYS   A 1 1078 ? 190.430 149.401 134.595 1.00 15.96  ? 1078 LYS   A CA    1 
ATOM   5425  C  C     . LYS   A 1 1078 ? 188.921 149.551 134.467 1.00 26.32  ? 1078 LYS   A C     1 
ATOM   5426  O  O     . LYS   A 1 1078 ? 188.326 150.417 135.119 1.00 34.52  ? 1078 LYS   A O     1 
ATOM   5427  C  CB    . LYS   A 1 1078 ? 191.142 150.261 133.552 1.00 26.44  ? 1078 LYS   A CB    1 
ATOM   5428  C  CG    . LYS   A 1 1078 ? 192.611 150.499 133.843 1.00 21.35  ? 1078 LYS   A CG    1 
ATOM   5429  C  CD    . LYS   A 1 1078 ? 193.117 151.751 133.149 1.00 24.18  ? 1078 LYS   A CD    1 
ATOM   5430  C  CE    . LYS   A 1 1078 ? 194.566 152.024 133.509 1.00 29.60  ? 1078 LYS   A CE    1 
ATOM   5431  N  NZ    . LYS   A 1 1078 ? 194.826 151.761 134.951 1.00 36.03  ? 1078 LYS   A NZ    1 
ATOM   5432  N  N     . PHE   A 1 1079 ? 188.287 148.727 133.634 1.00 29.50  ? 1079 PHE   A N     1 
ATOM   5433  C  CA    . PHE   A 1 1079 ? 186.837 148.744 133.492 1.00 20.59  ? 1079 PHE   A CA    1 
ATOM   5434  C  C     . PHE   A 1 1079 ? 186.125 147.977 134.597 1.00 19.73  ? 1079 PHE   A C     1 
ATOM   5435  O  O     . PHE   A 1 1079 ? 184.910 148.134 134.753 1.00 18.55  ? 1079 PHE   A O     1 
ATOM   5436  C  CB    . PHE   A 1 1079 ? 186.436 148.168 132.132 1.00 16.87  ? 1079 PHE   A CB    1 
ATOM   5437  C  CG    . PHE   A 1 1079 ? 186.673 149.102 130.981 1.00 23.52  ? 1079 PHE   A CG    1 
ATOM   5438  C  CD1   . PHE   A 1 1079 ? 186.534 150.469 131.140 1.00 19.80  ? 1079 PHE   A CD1   1 
ATOM   5439  C  CD2   . PHE   A 1 1079 ? 187.033 148.610 129.738 1.00 18.81  ? 1079 PHE   A CD2   1 
ATOM   5440  C  CE1   . PHE   A 1 1079 ? 186.750 151.329 130.082 1.00 19.47  ? 1079 PHE   A CE1   1 
ATOM   5441  C  CE2   . PHE   A 1 1079 ? 187.252 149.466 128.677 1.00 17.08  ? 1079 PHE   A CE2   1 
ATOM   5442  C  CZ    . PHE   A 1 1079 ? 187.109 150.826 128.849 1.00 22.17  ? 1079 PHE   A CZ    1 
ATOM   5443  N  N     . ARG   A 1 1080 ? 186.847 147.160 135.361 1.00 23.39  ? 1080 ARG   A N     1 
ATOM   5444  C  CA    . ARG   A 1 1080 ? 186.266 146.387 136.457 1.00 20.84  ? 1080 ARG   A CA    1 
ATOM   5445  C  C     . ARG   A 1 1080 ? 185.273 145.349 135.940 1.00 20.48  ? 1080 ARG   A C     1 
ATOM   5446  O  O     . ARG   A 1 1080 ? 184.204 145.146 136.516 1.00 32.30  ? 1080 ARG   A O     1 
ATOM   5447  C  CB    . ARG   A 1 1080 ? 185.596 147.299 137.486 1.00 23.10  ? 1080 ARG   A CB    1 
ATOM   5448  C  CG    . ARG   A 1 1080 ? 186.551 148.197 138.237 1.00 15.71  ? 1080 ARG   A CG    1 
ATOM   5449  C  CD    . ARG   A 1 1080 ? 186.397 149.625 137.766 1.00 13.61  ? 1080 ARG   A CD    1 
ATOM   5450  N  NE    . ARG   A 1 1080 ? 184.994 150.017 137.715 1.00 16.52  ? 1080 ARG   A NE    1 
ATOM   5451  C  CZ    . ARG   A 1 1080 ? 184.486 150.878 136.843 1.00 26.73  ? 1080 ARG   A CZ    1 
ATOM   5452  N  NH1   . ARG   A 1 1080 ? 185.241 151.463 135.930 1.00 16.09  ? 1080 ARG   A NH1   1 
ATOM   5453  N  NH2   . ARG   A 1 1080 ? 183.188 151.163 136.896 1.00 26.16  ? 1080 ARG   A NH2   1 
ATOM   5454  N  N     . ILE   A 1 1081 ? 185.626 144.687 134.844 1.00 16.01  ? 1081 ILE   A N     1 
ATOM   5455  C  CA    . ILE   A 1 1081 ? 184.831 143.594 134.298 1.00 24.50  ? 1081 ILE   A CA    1 
ATOM   5456  C  C     . ILE   A 1 1081 ? 185.617 142.313 134.526 1.00 28.65  ? 1081 ILE   A C     1 
ATOM   5457  O  O     . ILE   A 1 1081 ? 186.695 142.122 133.950 1.00 35.37  ? 1081 ILE   A O     1 
ATOM   5458  C  CB    . ILE   A 1 1081 ? 184.507 143.799 132.813 1.00 27.00  ? 1081 ILE   A CB    1 
ATOM   5459  C  CG1   . ILE   A 1 1081 ? 183.471 144.911 132.643 1.00 33.70  ? 1081 ILE   A CG1   1 
ATOM   5460  C  CG2   . ILE   A 1 1081 ? 183.997 142.507 132.196 1.00 27.06  ? 1081 ILE   A CG2   1 
ATOM   5461  C  CD1   . ILE   A 1 1081 ? 184.006 146.150 131.971 1.00 34.87  ? 1081 ILE   A CD1   1 
ATOM   5462  N  N     . ASP   A 1 1082 ? 185.081 141.435 135.369 1.00 33.88  ? 1082 ASP   A N     1 
ATOM   5463  C  CA    . ASP   A 1 1082 ? 185.776 140.203 135.709 1.00 33.76  ? 1082 ASP   A CA    1 
ATOM   5464  C  C     . ASP   A 1 1082 ? 185.814 139.269 134.507 1.00 39.32  ? 1082 ASP   A C     1 
ATOM   5465  O  O     . ASP   A 1 1082 ? 184.812 139.098 133.807 1.00 39.52  ? 1082 ASP   A O     1 
ATOM   5466  C  CB    . ASP   A 1 1082 ? 185.092 139.518 136.890 1.00 21.66  ? 1082 ASP   A CB    1 
ATOM   5467  N  N     . PHE   A 1 1083 ? 186.973 138.663 134.271 1.00 29.93  ? 1083 PHE   A N     1 
ATOM   5468  C  CA    . PHE   A 1 1083 ? 187.154 137.719 133.180 1.00 26.15  ? 1083 PHE   A CA    1 
ATOM   5469  C  C     . PHE   A 1 1083 ? 187.878 136.485 133.696 1.00 29.00  ? 1083 PHE   A C     1 
ATOM   5470  O  O     . PHE   A 1 1083 ? 188.828 136.593 134.476 1.00 39.27  ? 1083 PHE   A O     1 
ATOM   5471  C  CB    . PHE   A 1 1083 ? 187.937 138.352 132.024 1.00 25.49  ? 1083 PHE   A CB    1 
ATOM   5472  C  CG    . PHE   A 1 1083 ? 189.238 138.975 132.441 1.00 31.99  ? 1083 PHE   A CG    1 
ATOM   5473  C  CD1   . PHE   A 1 1083 ? 190.377 138.202 132.584 1.00 30.14  ? 1083 PHE   A CD1   1 
ATOM   5474  C  CD2   . PHE   A 1 1083 ? 189.321 140.332 132.703 1.00 33.66  ? 1083 PHE   A CD2   1 
ATOM   5475  C  CE1   . PHE   A 1 1083 ? 191.573 138.771 132.967 1.00 34.77  ? 1083 PHE   A CE1   1 
ATOM   5476  C  CE2   . PHE   A 1 1083 ? 190.516 140.906 133.089 1.00 31.52  ? 1083 PHE   A CE2   1 
ATOM   5477  C  CZ    . PHE   A 1 1083 ? 191.642 140.124 133.222 1.00 31.54  ? 1083 PHE   A CZ    1 
ATOM   5478  N  N     . SER   A 1 1084 ? 187.417 135.311 133.265 1.00 37.09  ? 1084 SER   A N     1 
ATOM   5479  C  CA    . SER   A 1 1084 ? 188.082 134.074 133.659 1.00 34.10  ? 1084 SER   A CA    1 
ATOM   5480  C  C     . SER   A 1 1084 ? 189.399 133.901 132.912 1.00 40.45  ? 1084 SER   A C     1 
ATOM   5481  O  O     . SER   A 1 1084 ? 190.414 133.517 133.504 1.00 44.82  ? 1084 SER   A O     1 
ATOM   5482  C  CB    . SER   A 1 1084 ? 187.159 132.880 133.416 1.00 40.85  ? 1084 SER   A CB    1 
ATOM   5483  O  OG    . SER   A 1 1084 ? 186.541 132.961 132.145 1.00 48.37  ? 1084 SER   A OG    1 
ATOM   5484  N  N     . ASP   A 1 1085 ? 189.402 134.183 131.611 1.00 35.85  ? 1085 ASP   A N     1 
ATOM   5485  C  CA    . ASP   A 1 1085 ? 190.606 134.038 130.808 1.00 32.66  ? 1085 ASP   A CA    1 
ATOM   5486  C  C     . ASP   A 1 1085 ? 190.564 135.019 129.646 1.00 32.10  ? 1085 ASP   A C     1 
ATOM   5487  O  O     . ASP   A 1 1085 ? 189.501 135.502 129.246 1.00 35.36  ? 1085 ASP   A O     1 
ATOM   5488  C  CB    . ASP   A 1 1085 ? 190.766 132.603 130.292 1.00 32.60  ? 1085 ASP   A CB    1 
ATOM   5489  N  N     . ILE   A 1 1086 ? 191.748 135.309 129.112 1.00 34.54  ? 1086 ILE   A N     1 
ATOM   5490  C  CA    . ILE   A 1 1086 ? 191.911 136.116 127.909 1.00 33.40  ? 1086 ILE   A CA    1 
ATOM   5491  C  C     . ILE   A 1 1086 ? 192.718 135.302 126.910 1.00 35.31  ? 1086 ILE   A C     1 
ATOM   5492  O  O     . ILE   A 1 1086 ? 193.789 134.784 127.248 1.00 40.64  ? 1086 ILE   A O     1 
ATOM   5493  C  CB    . ILE   A 1 1086 ? 192.607 137.456 128.208 1.00 27.98  ? 1086 ILE   A CB    1 
ATOM   5494  C  CG1   . ILE   A 1 1086 ? 191.588 138.499 128.664 1.00 38.19  ? 1086 ILE   A CG1   1 
ATOM   5495  C  CG2   . ILE   A 1 1086 ? 193.354 137.948 126.982 1.00 25.77  ? 1086 ILE   A CG2   1 
ATOM   5496  C  CD1   . ILE   A 1 1086 ? 192.201 139.669 129.397 1.00 36.53  ? 1086 ILE   A CD1   1 
ATOM   5497  N  N     . MET   A 1 1087 ? 192.208 135.185 125.688 1.00 42.22  ? 1087 MET   A N     1 
ATOM   5498  C  CA    . MET   A 1 1087 ? 192.865 134.423 124.636 1.00 41.82  ? 1087 MET   A CA    1 
ATOM   5499  C  C     . MET   A 1 1087 ? 193.161 135.337 123.457 1.00 46.94  ? 1087 MET   A C     1 
ATOM   5500  O  O     . MET   A 1 1087 ? 192.254 135.984 122.923 1.00 46.04  ? 1087 MET   A O     1 
ATOM   5501  C  CB    . MET   A 1 1087 ? 191.998 133.245 124.187 1.00 41.86  ? 1087 MET   A CB    1 
ATOM   5502  C  CG    . MET   A 1 1087 ? 192.645 132.371 123.127 1.00 49.15  ? 1087 MET   A CG    1 
ATOM   5503  S  SD    . MET   A 1 1087 ? 191.686 130.889 122.759 1.00 70.62  ? 1087 MET   A SD    1 
ATOM   5504  C  CE    . MET   A 1 1087 ? 192.611 129.649 123.660 1.00 51.28  ? 1087 MET   A CE    1 
ATOM   5505  N  N     . VAL   A 1 1088 ? 194.425 135.371 123.044 1.00 43.76  ? 1088 VAL   A N     1 
ATOM   5506  C  CA    . VAL   A 1 1088 ? 194.867 136.162 121.904 1.00 44.33  ? 1088 VAL   A CA    1 
ATOM   5507  C  C     . VAL   A 1 1088 ? 195.134 135.214 120.746 1.00 48.56  ? 1088 VAL   A C     1 
ATOM   5508  O  O     . VAL   A 1 1088 ? 195.894 134.248 120.887 1.00 52.28  ? 1088 VAL   A O     1 
ATOM   5509  C  CB    . VAL   A 1 1088 ? 196.120 136.983 122.247 1.00 42.38  ? 1088 VAL   A CB    1 
ATOM   5510  C  CG1   . VAL   A 1 1088 ? 196.470 137.917 121.103 1.00 45.25  ? 1088 VAL   A CG1   1 
ATOM   5511  C  CG2   . VAL   A 1 1088 ? 195.900 137.765 123.527 1.00 42.30  ? 1088 VAL   A CG2   1 
ATOM   5512  N  N     . LEU   A 1 1089 ? 194.510 135.484 119.604 1.00 47.89  ? 1089 LEU   A N     1 
ATOM   5513  C  CA    . LEU   A 1 1089 ? 194.585 134.610 118.443 1.00 45.25  ? 1089 LEU   A CA    1 
ATOM   5514  C  C     . LEU   A 1 1089 ? 195.273 135.331 117.296 1.00 51.82  ? 1089 LEU   A C     1 
ATOM   5515  O  O     . LEU   A 1 1089 ? 194.870 136.436 116.918 1.00 53.66  ? 1089 LEU   A O     1 
ATOM   5516  C  CB    . LEU   A 1 1089 ? 193.190 134.148 118.012 1.00 43.74  ? 1089 LEU   A CB    1 
ATOM   5517  C  CG    . LEU   A 1 1089 ? 192.229 133.760 119.134 1.00 51.86  ? 1089 LEU   A CG    1 
ATOM   5518  C  CD1   . LEU   A 1 1089 ? 190.790 133.834 118.657 1.00 42.64  ? 1089 LEU   A CD1   1 
ATOM   5519  C  CD2   . LEU   A 1 1089 ? 192.551 132.367 119.646 1.00 53.71  ? 1089 LEU   A CD2   1 
ATOM   5520  N  N     . GLY   A 1 1090 ? 196.311 134.704 116.751 1.00 54.61  ? 1090 GLY   A N     1 
ATOM   5521  C  CA    . GLY   A 1 1090 ? 196.951 135.147 115.535 1.00 51.12  ? 1090 GLY   A CA    1 
ATOM   5522  C  C     . GLY   A 1 1090 ? 196.466 134.446 114.289 1.00 54.66  ? 1090 GLY   A C     1 
ATOM   5523  O  O     . GLY   A 1 1090 ? 196.919 134.777 113.190 1.00 56.21  ? 1090 GLY   A O     1 
ATOM   5524  N  N     . ASP   A 1 1091 ? 195.552 133.486 114.425 1.00 51.52  ? 1091 ASP   A N     1 
ATOM   5525  C  CA    . ASP   A 1 1091 ? 195.042 132.744 113.281 1.00 51.64  ? 1091 ASP   A CA    1 
ATOM   5526  C  C     . ASP   A 1 1091 ? 194.069 133.554 112.436 1.00 55.49  ? 1091 ASP   A C     1 
ATOM   5527  O  O     . ASP   A 1 1091 ? 193.753 133.138 111.317 1.00 57.58  ? 1091 ASP   A O     1 
ATOM   5528  C  CB    . ASP   A 1 1091 ? 194.364 131.456 113.753 1.00 52.68  ? 1091 ASP   A CB    1 
ATOM   5529  N  N     . ILE   A 1 1092 ? 193.585 134.692 112.939 1.00 50.36  ? 1092 ILE   A N     1 
ATOM   5530  C  CA    . ILE   A 1 1092 ? 192.786 135.577 112.104 1.00 53.98  ? 1092 ILE   A CA    1 
ATOM   5531  C  C     . ILE   A 1 1092 ? 193.648 136.137 110.978 1.00 57.36  ? 1092 ILE   A C     1 
ATOM   5532  O  O     . ILE   A 1 1092 ? 194.882 136.177 111.054 1.00 55.98  ? 1092 ILE   A O     1 
ATOM   5533  C  CB    . ILE   A 1 1092 ? 192.157 136.705 112.938 1.00 55.34  ? 1092 ILE   A CB    1 
ATOM   5534  C  CG1   . ILE   A 1 1092 ? 191.464 136.136 114.177 1.00 55.14  ? 1092 ILE   A CG1   1 
ATOM   5535  C  CG2   . ILE   A 1 1092 ? 191.178 137.513 112.100 1.00 51.68  ? 1092 ILE   A CG2   1 
ATOM   5536  C  CD1   . ILE   A 1 1092 ? 191.238 137.156 115.272 1.00 52.37  ? 1092 ILE   A CD1   1 
ATOM   5537  N  N     . ASN   A 1 1093 ? 192.981 136.575 109.912 1.00 51.68  ? 1093 ASN   A N     1 
ATOM   5538  C  CA    . ASN   A 1 1093 ? 193.612 137.138 108.723 1.00 47.59  ? 1093 ASN   A CA    1 
ATOM   5539  C  C     . ASN   A 1 1093 ? 194.287 136.082 107.859 1.00 47.00  ? 1093 ASN   A C     1 
ATOM   5540  O  O     . ASN   A 1 1093 ? 194.966 136.431 106.886 1.00 52.89  ? 1093 ASN   A O     1 
ATOM   5541  C  CB    . ASN   A 1 1093 ? 194.632 138.224 109.084 1.00 44.69  ? 1093 ASN   A CB    1 
ATOM   5542  C  CG    . ASN   A 1 1093 ? 193.976 139.510 109.538 1.00 52.04  ? 1093 ASN   A CG    1 
ATOM   5543  O  OD1   . ASN   A 1 1093 ? 192.766 139.687 109.397 1.00 57.80  ? 1093 ASN   A OD1   1 
ATOM   5544  N  ND2   . ASN   A 1 1093 ? 194.772 140.418 110.088 1.00 56.01  ? 1093 ASN   A ND2   1 
ATOM   5545  N  N     . THR   A 1 1094 ? 194.125 134.805 108.184 1.00 42.69  ? 1094 THR   A N     1 
ATOM   5546  C  CA    . THR   A 1 1094 ? 194.680 133.718 107.395 1.00 45.57  ? 1094 THR   A CA    1 
ATOM   5547  C  C     . THR   A 1 1094 ? 193.611 133.133 106.480 1.00 50.10  ? 1094 THR   A C     1 
ATOM   5548  O  O     . THR   A 1 1094 ? 192.411 133.227 106.746 1.00 52.95  ? 1094 THR   A O     1 
ATOM   5549  C  CB    . THR   A 1 1094 ? 195.253 132.622 108.299 1.00 43.15  ? 1094 THR   A CB    1 
ATOM   5550  O  OG1   . THR   A 1 1094 ? 194.196 132.025 109.059 1.00 48.00  ? 1094 THR   A OG1   1 
ATOM   5551  C  CG2   . THR   A 1 1094 ? 196.282 133.206 109.252 1.00 46.31  ? 1094 THR   A CG2   1 
ATOM   5552  N  N     . LYS   A 1 1095 ? 194.063 132.525 105.392 1.00 46.80  ? 1095 LYS   A N     1 
ATOM   5553  C  CA    . LYS   A 1 1095 ? 193.134 131.963 104.420 1.00 45.13  ? 1095 LYS   A CA    1 
ATOM   5554  C  C     . LYS   A 1 1095 ? 192.363 130.803 105.039 1.00 46.64  ? 1095 LYS   A C     1 
ATOM   5555  O  O     . LYS   A 1 1095 ? 192.977 129.876 105.580 1.00 48.48  ? 1095 LYS   A O     1 
ATOM   5556  C  CB    . LYS   A 1 1095 ? 193.879 131.490 103.176 1.00 47.11  ? 1095 LYS   A CB    1 
ATOM   5557  C  CG    . LYS   A 1 1095 ? 193.236 130.288 102.501 1.00 47.93  ? 1095 LYS   A CG    1 
ATOM   5558  C  CD    . LYS   A 1 1095 ? 193.653 130.174 101.046 1.00 46.78  ? 1095 LYS   A CD    1 
ATOM   5559  C  CE    . LYS   A 1 1095 ? 193.407 131.473 100.298 1.00 53.02  ? 1095 LYS   A CE    1 
ATOM   5560  N  NZ    . LYS   A 1 1095 ? 193.517 131.291 98.825  1.00 55.08  ? 1095 LYS   A NZ    1 
ATOM   5561  N  N     . PRO   A 1 1096 ? 191.032 130.812 104.981 1.00 47.36  ? 1096 PRO   A N     1 
ATOM   5562  C  CA    . PRO   A 1 1096 ? 190.267 129.663 105.486 1.00 44.98  ? 1096 PRO   A CA    1 
ATOM   5563  C  C     . PRO   A 1 1096 ? 190.516 128.414 104.657 1.00 48.01  ? 1096 PRO   A C     1 
ATOM   5564  O  O     . PRO   A 1 1096 ? 191.247 128.455 103.663 1.00 49.51  ? 1096 PRO   A O     1 
ATOM   5565  C  CB    . PRO   A 1 1096 ? 188.807 130.124 105.373 1.00 41.43  ? 1096 PRO   A CB    1 
ATOM   5566  C  CG    . PRO   A 1 1096 ? 188.832 131.340 104.503 1.00 40.72  ? 1096 PRO   A CG    1 
ATOM   5567  C  CD    . PRO   A 1 1096 ? 190.171 131.964 104.674 1.00 43.91  ? 1096 PRO   A CD    1 
ATOM   5568  N  N     . LYS   A 1 1097 ? 189.910 127.300 105.053 1.00 46.30  ? 1097 LYS   A N     1 
ATOM   5569  C  CA    . LYS   A 1 1097 ? 190.064 126.067 104.300 1.00 50.20  ? 1097 LYS   A CA    1 
ATOM   5570  C  C     . LYS   A 1 1097 ? 189.374 126.176 102.943 1.00 54.38  ? 1097 LYS   A C     1 
ATOM   5571  O  O     . LYS   A 1 1097 ? 188.495 127.015 102.724 1.00 57.92  ? 1097 LYS   A O     1 
ATOM   5572  C  CB    . LYS   A 1 1097 ? 189.498 124.884 105.083 1.00 49.88  ? 1097 LYS   A CB    1 
ATOM   5573  C  CG    . LYS   A 1 1097 ? 189.926 124.846 106.537 1.00 50.39  ? 1097 LYS   A CG    1 
ATOM   5574  C  CD    . LYS   A 1 1097 ? 190.714 123.586 106.844 1.00 51.75  ? 1097 LYS   A CD    1 
ATOM   5575  C  CE    . LYS   A 1 1097 ? 191.093 123.521 108.312 1.00 54.07  ? 1097 LYS   A CE    1 
ATOM   5576  N  NZ    . LYS   A 1 1097 ? 189.932 123.818 109.195 1.00 57.11  ? 1097 LYS   A NZ    1 
ATOM   5577  N  N     . LYS   A 1 1098 ? 189.790 125.307 102.020 1.00 59.10  ? 1098 LYS   A N     1 
ATOM   5578  C  CA    . LYS   A 1 1098 ? 189.188 125.296 100.691 1.00 56.39  ? 1098 LYS   A CA    1 
ATOM   5579  C  C     . LYS   A 1 1098 ? 187.718 124.904 100.756 1.00 60.03  ? 1098 LYS   A C     1 
ATOM   5580  O  O     . LYS   A 1 1098 ? 186.885 125.464 100.033 1.00 58.94  ? 1098 LYS   A O     1 
ATOM   5581  C  CB    . LYS   A 1 1098 ? 189.957 124.346 99.774  1.00 50.52  ? 1098 LYS   A CB    1 
ATOM   5582  N  N     . GLU   A 1 1099 ? 187.380 123.937 101.612 1.00 59.05  ? 1099 GLU   A N     1 
ATOM   5583  C  CA    . GLU   A 1 1099 ? 186.003 123.459 101.684 1.00 54.34  ? 1099 GLU   A CA    1 
ATOM   5584  C  C     . GLU   A 1 1099 ? 185.046 124.575 102.083 1.00 52.68  ? 1099 GLU   A C     1 
ATOM   5585  O  O     . GLU   A 1 1099 ? 183.963 124.710 101.502 1.00 57.43  ? 1099 GLU   A O     1 
ATOM   5586  C  CB    . GLU   A 1 1099 ? 185.905 122.293 102.666 1.00 50.92  ? 1099 GLU   A CB    1 
ATOM   5587  N  N     . ASN   A 1 1100 ? 185.423 125.384 103.074 1.00 52.96  ? 1100 ASN   A N     1 
ATOM   5588  C  CA    . ASN   A 1 1100 ? 184.535 126.450 103.528 1.00 54.92  ? 1100 ASN   A CA    1 
ATOM   5589  C  C     . ASN   A 1 1100 ? 184.382 127.537 102.471 1.00 56.30  ? 1100 ASN   A C     1 
ATOM   5590  O  O     . ASN   A 1 1100 ? 183.284 128.074 102.280 1.00 62.15  ? 1100 ASN   A O     1 
ATOM   5591  C  CB    . ASN   A 1 1100 ? 185.050 127.033 104.842 1.00 51.48  ? 1100 ASN   A CB    1 
ATOM   5592  C  CG    . ASN   A 1 1100 ? 185.321 125.965 105.882 1.00 54.17  ? 1100 ASN   A CG    1 
ATOM   5593  O  OD1   . ASN   A 1 1100 ? 184.417 125.235 106.289 1.00 54.72  ? 1100 ASN   A OD1   1 
ATOM   5594  N  ND2   . ASN   A 1 1100 ? 186.573 125.856 106.304 1.00 56.88  ? 1100 ASN   A ND2   1 
ATOM   5595  N  N     . ILE   A 1 1101 ? 185.466 127.873 101.770 1.00 47.10  ? 1101 ILE   A N     1 
ATOM   5596  C  CA    . ILE   A 1 1101 ? 185.370 128.854 100.693 1.00 51.82  ? 1101 ILE   A CA    1 
ATOM   5597  C  C     . ILE   A 1 1101 ? 184.455 128.337 99.590  1.00 54.69  ? 1101 ILE   A C     1 
ATOM   5598  O  O     . ILE   A 1 1101 ? 183.634 129.082 99.038  1.00 57.58  ? 1101 ILE   A O     1 
ATOM   5599  C  CB    . ILE   A 1 1101 ? 186.771 129.196 100.155 1.00 48.71  ? 1101 ILE   A CB    1 
ATOM   5600  C  CG1   . ILE   A 1 1101 ? 187.521 130.082 101.150 1.00 49.67  ? 1101 ILE   A CG1   1 
ATOM   5601  C  CG2   . ILE   A 1 1101 ? 186.665 129.888 98.809  1.00 49.98  ? 1101 ILE   A CG2   1 
ATOM   5602  C  CD1   . ILE   A 1 1101 ? 188.958 130.350 100.765 1.00 50.57  ? 1101 ILE   A CD1   1 
ATOM   5603  N  N     . ILE   A 1 1102 ? 184.582 127.052 99.253  1.00 55.47  ? 1102 ILE   A N     1 
ATOM   5604  C  CA    . ILE   A 1 1102 ? 183.729 126.464 98.225  1.00 54.78  ? 1102 ILE   A CA    1 
ATOM   5605  C  C     . ILE   A 1 1102 ? 182.272 126.481 98.667  1.00 57.32  ? 1102 ILE   A C     1 
ATOM   5606  O  O     . ILE   A 1 1102 ? 181.369 126.752 97.867  1.00 57.56  ? 1102 ILE   A O     1 
ATOM   5607  C  CB    . ILE   A 1 1102 ? 184.203 125.039 97.888  1.00 58.79  ? 1102 ILE   A CB    1 
ATOM   5608  C  CG1   . ILE   A 1 1102 ? 185.524 125.087 97.120  1.00 56.30  ? 1102 ILE   A CG1   1 
ATOM   5609  C  CG2   . ILE   A 1 1102 ? 183.143 124.303 97.087  1.00 57.70  ? 1102 ILE   A CG2   1 
ATOM   5610  C  CD1   . ILE   A 1 1102 ? 185.700 126.336 96.288  1.00 55.60  ? 1102 ILE   A CD1   1 
ATOM   5611  N  N     . ALA   A 1 1103 ? 182.015 126.172 99.939  1.00 49.52  ? 1103 ALA   A N     1 
ATOM   5612  C  CA    . ALA   A 1 1103 ? 180.645 126.206 100.441 1.00 49.82  ? 1103 ALA   A CA    1 
ATOM   5613  C  C     . ALA   A 1 1103 ? 180.071 127.616 100.384 1.00 52.49  ? 1103 ALA   A C     1 
ATOM   5614  O  O     . ALA   A 1 1103 ? 178.908 127.806 100.009 1.00 61.36  ? 1103 ALA   A O     1 
ATOM   5615  C  CB    . ALA   A 1 1103 ? 180.592 125.661 101.868 1.00 48.29  ? 1103 ALA   A CB    1 
ATOM   5616  N  N     . PHE   A 1 1104 ? 180.870 128.619 100.753 1.00 42.91  ? 1104 PHE   A N     1 
ATOM   5617  C  CA    . PHE   A 1 1104 ? 180.395 129.996 100.667 1.00 41.78  ? 1104 PHE   A CA    1 
ATOM   5618  C  C     . PHE   A 1 1104 ? 180.078 130.372 99.227  1.00 48.09  ? 1104 PHE   A C     1 
ATOM   5619  O  O     . PHE   A 1 1104 ? 179.052 131.007 98.953  1.00 51.93  ? 1104 PHE   A O     1 
ATOM   5620  C  CB    . PHE   A 1 1104 ? 181.430 130.953 101.257 1.00 41.76  ? 1104 PHE   A CB    1 
ATOM   5621  C  CG    . PHE   A 1 1104 ? 181.046 132.404 101.154 1.00 37.03  ? 1104 PHE   A CG    1 
ATOM   5622  C  CD1   . PHE   A 1 1104 ? 181.356 133.141 100.025 1.00 39.21  ? 1104 PHE   A CD1   1 
ATOM   5623  C  CD2   . PHE   A 1 1104 ? 180.377 133.030 102.189 1.00 39.43  ? 1104 PHE   A CD2   1 
ATOM   5624  C  CE1   . PHE   A 1 1104 ? 181.004 134.474 99.932  1.00 41.09  ? 1104 PHE   A CE1   1 
ATOM   5625  C  CE2   . PHE   A 1 1104 ? 180.025 134.363 102.101 1.00 35.44  ? 1104 PHE   A CE2   1 
ATOM   5626  C  CZ    . PHE   A 1 1104 ? 180.338 135.084 100.973 1.00 27.67  ? 1104 PHE   A CZ    1 
ATOM   5627  N  N     . GLU   A 1 1105 ? 180.950 129.992 98.291  1.00 48.23  ? 1105 GLU   A N     1 
ATOM   5628  C  CA    . GLU   A 1 1105 ? 180.697 130.297 96.886  1.00 49.80  ? 1105 GLU   A CA    1 
ATOM   5629  C  C     . GLU   A 1 1105 ? 179.432 129.606 96.393  1.00 54.67  ? 1105 GLU   A C     1 
ATOM   5630  O  O     . GLU   A 1 1105 ? 178.633 130.203 95.662  1.00 55.74  ? 1105 GLU   A O     1 
ATOM   5631  C  CB    . GLU   A 1 1105 ? 181.900 129.891 96.036  1.00 45.95  ? 1105 GLU   A CB    1 
ATOM   5632  N  N     . GLU   A 1 1106 ? 179.234 128.344 96.778  1.00 52.27  ? 1106 GLU   A N     1 
ATOM   5633  C  CA    . GLU   A 1 1106 ? 178.029 127.629 96.374  1.00 50.89  ? 1106 GLU   A CA    1 
ATOM   5634  C  C     . GLU   A 1 1106 ? 176.782 128.302 96.927  1.00 51.98  ? 1106 GLU   A C     1 
ATOM   5635  O  O     . GLU   A 1 1106 ? 175.772 128.432 96.225  1.00 54.00  ? 1106 GLU   A O     1 
ATOM   5636  C  CB    . GLU   A 1 1106 ? 178.104 126.173 96.834  1.00 50.05  ? 1106 GLU   A CB    1 
ATOM   5637  N  N     . ILE   A 1 1107 ? 176.831 128.733 98.188  1.00 47.55  ? 1107 ILE   A N     1 
ATOM   5638  C  CA    . ILE   A 1 1107 ? 175.686 129.415 98.784  1.00 49.51  ? 1107 ILE   A CA    1 
ATOM   5639  C  C     . ILE   A 1 1107 ? 175.405 130.723 98.055  1.00 48.71  ? 1107 ILE   A C     1 
ATOM   5640  O  O     . ILE   A 1 1107 ? 174.247 131.072 97.797  1.00 53.61  ? 1107 ILE   A O     1 
ATOM   5641  C  CB    . ILE   A 1 1107 ? 175.924 129.646 100.289 1.00 49.22  ? 1107 ILE   A CB    1 
ATOM   5642  C  CG1   . ILE   A 1 1107 ? 175.445 128.443 101.105 1.00 50.34  ? 1107 ILE   A CG1   1 
ATOM   5643  C  CG2   . ILE   A 1 1107 ? 175.228 130.916 100.751 1.00 49.16  ? 1107 ILE   A CG2   1 
ATOM   5644  C  CD1   . ILE   A 1 1107 ? 175.865 127.109 100.536 1.00 50.58  ? 1107 ILE   A CD1   1 
ATOM   5645  N  N     . ILE   A 1 1108 ? 176.461 131.466 97.710  1.00 42.57  ? 1108 ILE   A N     1 
ATOM   5646  C  CA    . ILE   A 1 1108 ? 176.298 132.795 97.121  1.00 44.51  ? 1108 ILE   A CA    1 
ATOM   5647  C  C     . ILE   A 1 1108 ? 176.017 132.768 95.628  1.00 56.65  ? 1108 ILE   A C     1 
ATOM   5648  O  O     . ILE   A 1 1108 ? 175.635 133.801 95.064  1.00 57.35  ? 1108 ILE   A O     1 
ATOM   5649  C  CB    . ILE   A 1 1108 ? 177.557 133.643 97.378  1.00 48.73  ? 1108 ILE   A CB    1 
ATOM   5650  C  CG1   . ILE   A 1 1108 ? 177.282 135.117 97.091  1.00 48.68  ? 1108 ILE   A CG1   1 
ATOM   5651  C  CG2   . ILE   A 1 1108 ? 178.715 133.150 96.523  1.00 47.63  ? 1108 ILE   A CG2   1 
ATOM   5652  C  CD1   . ILE   A 1 1108 ? 178.532 135.964 97.047  1.00 49.97  ? 1108 ILE   A CD1   1 
ATOM   5653  N  N     . GLU   A 1 1109 ? 176.198 131.623 94.971  1.00 59.28  ? 1109 GLU   A N     1 
ATOM   5654  C  CA    . GLU   A 1 1109 ? 176.036 131.548 93.519  1.00 51.98  ? 1109 GLU   A CA    1 
ATOM   5655  C  C     . GLU   A 1 1109 ? 174.702 132.081 93.013  1.00 54.62  ? 1109 GLU   A C     1 
ATOM   5656  O  O     . GLU   A 1 1109 ? 174.702 132.854 92.043  1.00 55.38  ? 1109 GLU   A O     1 
ATOM   5657  C  CB    . GLU   A 1 1109 ? 176.237 130.095 93.069  1.00 48.10  ? 1109 GLU   A CB    1 
ATOM   5658  N  N     . PRO   A 1 1110 ? 173.553 131.723 93.594  1.00 52.75  ? 1110 PRO   A N     1 
ATOM   5659  C  CA    . PRO   A 1 1110 ? 172.276 132.127 92.981  1.00 48.15  ? 1110 PRO   A CA    1 
ATOM   5660  C  C     . PRO   A 1 1110 ? 172.111 133.627 92.822  1.00 51.53  ? 1110 PRO   A C     1 
ATOM   5661  O  O     . PRO   A 1 1110 ? 171.428 134.066 91.888  1.00 55.63  ? 1110 PRO   A O     1 
ATOM   5662  C  CB    . PRO   A 1 1110 ? 171.234 131.545 93.946  1.00 47.76  ? 1110 PRO   A CB    1 
ATOM   5663  C  CG    . PRO   A 1 1110 ? 171.928 130.390 94.581  1.00 50.11  ? 1110 PRO   A CG    1 
ATOM   5664  C  CD    . PRO   A 1 1110 ? 173.350 130.838 94.752  1.00 52.15  ? 1110 PRO   A CD    1 
ATOM   5665  N  N     . TYR   A 1 1111 ? 172.712 134.430 93.696  1.00 50.35  ? 1111 TYR   A N     1 
ATOM   5666  C  CA    . TYR   A 1 1111 ? 172.545 135.876 93.674  1.00 50.05  ? 1111 TYR   A CA    1 
ATOM   5667  C  C     . TYR   A 1 1111 ? 173.690 136.593 92.970  1.00 54.98  ? 1111 TYR   A C     1 
ATOM   5668  O  O     . TYR   A 1 1111 ? 173.739 137.827 92.984  1.00 51.64  ? 1111 TYR   A O     1 
ATOM   5669  C  CB    . TYR   A 1 1111 ? 172.382 136.398 95.102  1.00 51.69  ? 1111 TYR   A CB    1 
ATOM   5670  C  CG    . TYR   A 1 1111 ? 171.611 135.447 95.987  1.00 58.36  ? 1111 TYR   A CG    1 
ATOM   5671  C  CD1   . TYR   A 1 1111 ? 172.269 134.529 96.796  1.00 58.20  ? 1111 TYR   A CD1   1 
ATOM   5672  C  CD2   . TYR   A 1 1111 ? 170.223 135.446 95.993  1.00 55.00  ? 1111 TYR   A CD2   1 
ATOM   5673  C  CE1   . TYR   A 1 1111 ? 171.566 133.652 97.597  1.00 55.70  ? 1111 TYR   A CE1   1 
ATOM   5674  C  CE2   . TYR   A 1 1111 ? 169.513 134.571 96.788  1.00 52.43  ? 1111 TYR   A CE2   1 
ATOM   5675  C  CZ    . TYR   A 1 1111 ? 170.188 133.678 97.589  1.00 55.28  ? 1111 TYR   A CZ    1 
ATOM   5676  O  OH    . TYR   A 1 1111 ? 169.482 132.806 98.384  1.00 60.36  ? 1111 TYR   A OH    1 
ATOM   5677  N  N     . ARG   A 1 1112 ? 174.608 135.850 92.358  1.00 64.46  ? 1112 ARG   A N     1 
ATOM   5678  C  CA    . ARG   A 1 1112 ? 175.718 136.461 91.640  1.00 61.88  ? 1112 ARG   A CA    1 
ATOM   5679  C  C     . ARG   A 1 1112 ? 175.237 137.117 90.351  1.00 65.32  ? 1112 ARG   A C     1 
ATOM   5680  O  O     . ARG   A 1 1112 ? 174.448 136.541 89.598  1.00 70.39  ? 1112 ARG   A O     1 
ATOM   5681  C  CB    . ARG   A 1 1112 ? 176.781 135.410 91.324  1.00 65.84  ? 1112 ARG   A CB    1 
ATOM   5682  C  CG    . ARG   A 1 1112 ? 177.628 135.000 92.515  1.00 64.87  ? 1112 ARG   A CG    1 
ATOM   5683  C  CD    . ARG   A 1 1112 ? 179.006 134.540 92.069  1.00 65.88  ? 1112 ARG   A CD    1 
ATOM   5684  N  NE    . ARG   A 1 1112 ? 179.689 135.551 91.272  1.00 63.96  ? 1112 ARG   A NE    1 
ATOM   5685  C  CZ    . ARG   A 1 1112 ? 180.996 135.770 91.300  1.00 65.90  ? 1112 ARG   A CZ    1 
ATOM   5686  N  NH1   . ARG   A 1 1112 ? 181.800 135.059 92.074  1.00 67.68  ? 1112 ARG   A NH1   1 
ATOM   5687  N  NH2   . ARG   A 1 1112 ? 181.511 136.723 90.529  1.00 66.21  ? 1112 ARG   A NH2   1 
ATOM   5688  N  N     . LEU   A 1 1113 ? 175.723 138.334 90.099  1.00 70.20  ? 1113 LEU   A N     1 
ATOM   5689  C  CA    . LEU   A 1 1113 ? 175.380 139.031 88.864  1.00 69.40  ? 1113 LEU   A CA    1 
ATOM   5690  C  C     . LEU   A 1 1113 ? 176.172 138.493 87.678  1.00 71.76  ? 1113 LEU   A C     1 
ATOM   5691  O  O     . LEU   A 1 1113 ? 175.630 138.370 86.573  1.00 75.15  ? 1113 LEU   A O     1 
ATOM   5692  C  CB    . LEU   A 1 1113 ? 175.608 140.536 89.033  1.00 68.71  ? 1113 LEU   A CB    1 
ATOM   5693  C  CG    . LEU   A 1 1113 ? 175.280 141.489 87.877  1.00 65.41  ? 1113 LEU   A CG    1 
ATOM   5694  C  CD1   . LEU   A 1 1113 ? 175.279 142.925 88.370  1.00 64.73  ? 1113 LEU   A CD1   1 
ATOM   5695  C  CD2   . LEU   A 1 1113 ? 176.264 141.343 86.730  1.00 72.86  ? 1113 LEU   A CD2   1 
ATOM   5696  N  N     . HIS   A 1 1114 ? 177.447 138.165 87.883  1.00 79.96  ? 1114 HIS   A N     1 
ATOM   5697  C  CA    . HIS   A 1 1114 ? 178.319 137.690 86.810  1.00 77.25  ? 1114 HIS   A CA    1 
ATOM   5698  C  C     . HIS   A 1 1114 ? 178.440 138.743 85.706  1.00 78.76  ? 1114 HIS   A C     1 
ATOM   5699  O  O     . HIS   A 1 1114 ? 178.109 138.511 84.542  1.00 82.42  ? 1114 HIS   A O     1 
ATOM   5700  C  CB    . HIS   A 1 1114 ? 177.818 136.353 86.253  1.00 78.55  ? 1114 HIS   A CB    1 
ATOM   5701  C  CG    . HIS   A 1 1114 ? 178.117 135.181 87.133  1.00 78.09  ? 1114 HIS   A CG    1 
ATOM   5702  N  ND1   . HIS   A 1 1114 ? 177.151 134.280 87.528  1.00 78.61  ? 1114 HIS   A ND1   1 
ATOM   5703  C  CD2   . HIS   A 1 1114 ? 179.275 134.758 87.693  1.00 78.86  ? 1114 HIS   A CD2   1 
ATOM   5704  C  CE1   . HIS   A 1 1114 ? 177.701 133.355 88.294  1.00 78.70  ? 1114 HIS   A CE1   1 
ATOM   5705  N  NE2   . HIS   A 1 1114 ? 178.989 133.622 88.410  1.00 79.76  ? 1114 HIS   A NE2   1 
ATOM   5706  N  N     . GLU   A 1 1115 ? 178.925 139.921 86.103  1.00 85.51  ? 1115 GLU   A N     1 
ATOM   5707  C  CA    . GLU   A 1 1115 ? 179.050 141.028 85.160  1.00 87.20  ? 1115 GLU   A CA    1 
ATOM   5708  C  C     . GLU   A 1 1115 ? 180.027 140.695 84.039  1.00 89.20  ? 1115 GLU   A C     1 
ATOM   5709  O  O     . GLU   A 1 1115 ? 179.832 141.116 82.892  1.00 90.97  ? 1115 GLU   A O     1 
ATOM   5710  C  CB    . GLU   A 1 1115 ? 179.484 142.295 85.900  1.00 87.71  ? 1115 GLU   A CB    1 
ATOM   5711  C  CG    . GLU   A 1 1115 ? 179.628 143.525 85.016  1.00 88.68  ? 1115 GLU   A CG    1 
ATOM   5712  C  CD    . GLU   A 1 1115 ? 181.037 143.705 84.484  1.00 93.00  ? 1115 GLU   A CD    1 
ATOM   5713  O  OE1   . GLU   A 1 1115 ? 181.860 142.779 84.643  1.00 91.42  ? 1115 GLU   A OE1   1 
ATOM   5714  O  OE2   . GLU   A 1 1115 ? 181.322 144.775 83.905  1.00 93.89  ? 1115 GLU   A OE2   1 
ATOM   5715  N  N     . ASP   A 1 1116 ? 181.085 139.945 84.349  1.00 91.35  ? 1116 ASP   A N     1 
ATOM   5716  C  CA    . ASP   A 1 1116 ? 182.090 139.633 83.337  1.00 91.36  ? 1116 ASP   A CA    1 
ATOM   5717  C  C     . ASP   A 1 1116 ? 181.489 138.832 82.187  1.00 93.44  ? 1116 ASP   A C     1 
ATOM   5718  O  O     . ASP   A 1 1116 ? 181.804 139.080 81.017  1.00 90.01  ? 1116 ASP   A O     1 
ATOM   5719  C  CB    . ASP   A 1 1116 ? 183.254 138.872 83.971  1.00 87.65  ? 1116 ASP   A CB    1 
ATOM   5720  N  N     . ASP   A 1 1117 ? 180.623 137.868 82.499  1.00 97.30  ? 1117 ASP   A N     1 
ATOM   5721  C  CA    . ASP   A 1 1117 ? 180.029 137.023 81.470  1.00 96.76  ? 1117 ASP   A CA    1 
ATOM   5722  C  C     . ASP   A 1 1117 ? 178.958 137.738 80.657  1.00 98.64  ? 1117 ASP   A C     1 
ATOM   5723  O  O     . ASP   A 1 1117 ? 178.457 137.161 79.687  1.00 97.47  ? 1117 ASP   A O     1 
ATOM   5724  C  CB    . ASP   A 1 1117 ? 179.436 135.764 82.105  1.00 94.72  ? 1117 ASP   A CB    1 
ATOM   5725  N  N     . LYS   A 1 1118 ? 178.596 138.965 81.021  1.00 100.62 ? 1118 LYS   A N     1 
ATOM   5726  C  CA    . LYS   A 1 1118 ? 177.556 139.713 80.334  1.00 98.57  ? 1118 LYS   A CA    1 
ATOM   5727  C  C     . LYS   A 1 1118 ? 178.107 141.038 79.825  1.00 97.92  ? 1118 LYS   A C     1 
ATOM   5728  O  O     . LYS   A 1 1118 ? 179.126 141.542 80.306  1.00 97.44  ? 1118 LYS   A O     1 
ATOM   5729  C  CB    . LYS   A 1 1118 ? 176.354 139.969 81.253  1.00 96.10  ? 1118 LYS   A CB    1 
ATOM   5730  C  CG    . LYS   A 1 1118 ? 176.029 138.816 82.185  1.00 94.50  ? 1118 LYS   A CG    1 
ATOM   5731  C  CD    . LYS   A 1 1118 ? 174.805 139.123 83.031  1.00 95.33  ? 1118 LYS   A CD    1 
ATOM   5732  C  CE    . LYS   A 1 1118 ? 174.230 137.860 83.648  1.00 95.61  ? 1118 LYS   A CE    1 
ATOM   5733  N  NZ    . LYS   A 1 1118 ? 174.729 136.635 82.965  1.00 96.23  ? 1118 LYS   A NZ    1 
ATOM   5734  N  N     . GLU   A 1 1119 ? 177.413 141.599 78.840  1.00 95.94  ? 1119 GLU   A N     1 
ATOM   5735  C  CA    . GLU   A 1 1119 ? 177.778 142.878 78.253  1.00 95.78  ? 1119 GLU   A CA    1 
ATOM   5736  C  C     . GLU   A 1 1119 ? 177.237 144.010 79.124  1.00 97.01  ? 1119 GLU   A C     1 
ATOM   5737  O  O     . GLU   A 1 1119 ? 176.800 143.799 80.258  1.00 98.30  ? 1119 GLU   A O     1 
ATOM   5738  C  CB    . GLU   A 1 1119 ? 177.265 142.965 76.817  1.00 94.16  ? 1119 GLU   A CB    1 
ATOM   5739  N  N     . GLN   A 1 1120 ? 177.261 145.236 78.597  1.00 96.94  ? 1120 GLN   A N     1 
ATOM   5740  C  CA    . GLN   A 1 1120 ? 176.762 146.383 79.343  1.00 96.88  ? 1120 GLN   A CA    1 
ATOM   5741  C  C     . GLN   A 1 1120 ? 175.273 146.288 79.645  1.00 99.08  ? 1120 GLN   A C     1 
ATOM   5742  O  O     . GLN   A 1 1120 ? 174.784 147.036 80.499  1.00 100.19 ? 1120 GLN   A O     1 
ATOM   5743  C  CB    . GLN   A 1 1120 ? 177.051 147.675 78.576  1.00 95.81  ? 1120 GLN   A CB    1 
ATOM   5744  N  N     . ASP   A 1 1121 ? 174.544 145.395 78.970  1.00 100.18 ? 1121 ASP   A N     1 
ATOM   5745  C  CA    . ASP   A 1 1121 ? 173.128 145.216 79.273  1.00 99.55  ? 1121 ASP   A CA    1 
ATOM   5746  C  C     . ASP   A 1 1121 ? 172.910 144.824 80.728  1.00 99.73  ? 1121 ASP   A C     1 
ATOM   5747  O  O     . ASP   A 1 1121 ? 171.849 145.107 81.296  1.00 97.30  ? 1121 ASP   A O     1 
ATOM   5748  C  CB    . ASP   A 1 1121 ? 172.522 144.168 78.337  1.00 100.08 ? 1121 ASP   A CB    1 
ATOM   5749  C  CG    . ASP   A 1 1121 ? 173.208 142.816 78.446  1.00 102.85 ? 1121 ASP   A CG    1 
ATOM   5750  O  OD1   . ASP   A 1 1121 ? 173.510 142.382 79.577  1.00 102.55 ? 1121 ASP   A OD1   1 
ATOM   5751  O  OD2   . ASP   A 1 1121 ? 173.445 142.184 77.395  1.00 100.97 ? 1121 ASP   A OD2   1 
ATOM   5752  N  N     . ILE   A 1 1122 ? 173.901 144.179 81.350  1.00 98.54  ? 1122 ILE   A N     1 
ATOM   5753  C  CA    . ILE   A 1 1122 ? 173.794 143.814 82.756  1.00 96.03  ? 1122 ILE   A CA    1 
ATOM   5754  C  C     . ILE   A 1 1122 ? 173.546 145.035 83.628  1.00 96.37  ? 1122 ILE   A C     1 
ATOM   5755  O  O     . ILE   A 1 1122 ? 173.030 144.905 84.743  1.00 96.65  ? 1122 ILE   A O     1 
ATOM   5756  C  CB    . ILE   A 1 1122 ? 175.060 143.061 83.212  1.00 94.89  ? 1122 ILE   A CB    1 
ATOM   5757  N  N     . ALA   A 1 1123 ? 173.889 146.230 83.140  1.00 98.89  ? 1123 ALA   A N     1 
ATOM   5758  C  CA    . ALA   A 1 1123 ? 173.630 147.449 83.893  1.00 97.86  ? 1123 ALA   A CA    1 
ATOM   5759  C  C     . ALA   A 1 1123 ? 172.147 147.661 84.163  1.00 99.47  ? 1123 ALA   A C     1 
ATOM   5760  O  O     . ALA   A 1 1123 ? 171.801 148.519 84.983  1.00 100.63 ? 1123 ALA   A O     1 
ATOM   5761  C  CB    . ALA   A 1 1123 ? 174.199 148.658 83.148  1.00 96.96  ? 1123 ALA   A CB    1 
ATOM   5762  N  N     . ASP   A 1 1124 ? 171.270 146.909 83.500  1.00 96.72  ? 1124 ASP   A N     1 
ATOM   5763  C  CA    . ASP   A 1 1124 ? 169.846 146.961 83.799  1.00 95.03  ? 1124 ASP   A CA    1 
ATOM   5764  C  C     . ASP   A 1 1124 ? 169.460 146.023 84.931  1.00 95.94  ? 1124 ASP   A C     1 
ATOM   5765  O  O     . ASP   A 1 1124 ? 168.545 146.338 85.702  1.00 94.99  ? 1124 ASP   A O     1 
ATOM   5766  C  CB    . ASP   A 1 1124 ? 169.030 146.620 82.550  1.00 91.47  ? 1124 ASP   A CB    1 
ATOM   5767  N  N     . LYS   A 1 1125 ? 170.137 144.878 85.053  1.00 93.08  ? 1125 LYS   A N     1 
ATOM   5768  C  CA    . LYS   A 1 1125 ? 169.882 143.995 86.186  1.00 89.19  ? 1125 LYS   A CA    1 
ATOM   5769  C  C     . LYS   A 1 1125 ? 170.297 144.653 87.495  1.00 88.14  ? 1125 LYS   A C     1 
ATOM   5770  O  O     . LYS   A 1 1125 ? 169.608 144.515 88.511  1.00 90.28  ? 1125 LYS   A O     1 
ATOM   5771  C  CB    . LYS   A 1 1125 ? 170.612 142.666 85.997  1.00 87.48  ? 1125 LYS   A CB    1 
ATOM   5772  C  CG    . LYS   A 1 1125 ? 170.208 141.909 84.746  1.00 88.74  ? 1125 LYS   A CG    1 
ATOM   5773  C  CD    . LYS   A 1 1125 ? 171.028 140.641 84.586  1.00 89.47  ? 1125 LYS   A CD    1 
ATOM   5774  C  CE    . LYS   A 1 1125 ? 170.342 139.459 85.250  1.00 89.71  ? 1125 LYS   A CE    1 
ATOM   5775  N  NZ    . LYS   A 1 1125 ? 170.424 139.540 86.734  1.00 86.71  ? 1125 LYS   A NZ    1 
ATOM   5776  N  N     . MET   A 1 1126 ? 171.417 145.378 87.486  1.00 91.49  ? 1126 MET   A N     1 
ATOM   5777  C  CA    . MET   A 1 1126 ? 171.880 146.069 88.682  1.00 92.06  ? 1126 MET   A CA    1 
ATOM   5778  C  C     . MET   A 1 1126 ? 170.950 147.200 89.100  1.00 92.88  ? 1126 MET   A C     1 
ATOM   5779  O  O     . MET   A 1 1126 ? 171.098 147.720 90.211  1.00 95.89  ? 1126 MET   A O     1 
ATOM   5780  C  CB    . MET   A 1 1126 ? 173.290 146.618 88.460  1.00 92.73  ? 1126 MET   A CB    1 
ATOM   5781  C  CG    . MET   A 1 1126 ? 174.094 146.814 89.736  1.00 91.02  ? 1126 MET   A CG    1 
ATOM   5782  S  SD    . MET   A 1 1126 ? 173.642 145.644 91.031  1.00 100.67 ? 1126 MET   A SD    1 
ATOM   5783  C  CE    . MET   A 1 1126 ? 174.410 146.403 92.459  1.00 93.27  ? 1126 MET   A CE    1 
ATOM   5784  N  N     . LYS   A 1 1127 ? 170.005 147.593 88.243  1.00 91.78  ? 1127 LYS   A N     1 
ATOM   5785  C  CA    . LYS   A 1 1127 ? 169.042 148.630 88.578  1.00 93.90  ? 1127 LYS   A CA    1 
ATOM   5786  C  C     . LYS   A 1 1127 ? 167.618 148.118 88.737  1.00 93.47  ? 1127 LYS   A C     1 
ATOM   5787  O  O     . LYS   A 1 1127 ? 166.804 148.801 89.364  1.00 94.51  ? 1127 LYS   A O     1 
ATOM   5788  C  CB    . LYS   A 1 1127 ? 169.055 149.735 87.511  1.00 91.58  ? 1127 LYS   A CB    1 
ATOM   5789  N  N     . GLU   A 1 1128 ? 167.299 146.942 88.196  1.00 90.91  ? 1128 GLU   A N     1 
ATOM   5790  C  CA    . GLU   A 1 1128 ? 165.969 146.358 88.326  1.00 90.75  ? 1128 GLU   A CA    1 
ATOM   5791  C  C     . GLU   A 1 1128 ? 165.987 145.093 89.174  1.00 92.77  ? 1128 GLU   A C     1 
ATOM   5792  O  O     . GLU   A 1 1128 ? 165.276 145.010 90.180  1.00 92.82  ? 1128 GLU   A O     1 
ATOM   5793  C  CB    . GLU   A 1 1128 ? 165.386 146.063 86.937  1.00 90.36  ? 1128 GLU   A CB    1 
ATOM   5794  N  N     . ASP   A 1 1129 ? 166.788 144.101 88.796  1.00 90.66  ? 1129 ASP   A N     1 
ATOM   5795  C  CA    . ASP   A 1 1129 ? 166.992 142.911 89.621  1.00 86.24  ? 1129 ASP   A CA    1 
ATOM   5796  C  C     . ASP   A 1 1129 ? 168.160 143.113 90.579  1.00 85.96  ? 1129 ASP   A C     1 
ATOM   5797  O  O     . ASP   A 1 1129 ? 169.085 142.306 90.655  1.00 89.58  ? 1129 ASP   A O     1 
ATOM   5798  C  CB    . ASP   A 1 1129 ? 167.213 141.692 88.734  1.00 87.15  ? 1129 ASP   A CB    1 
ATOM   5799  C  CG    . ASP   A 1 1129 ? 166.968 140.388 89.465  1.00 88.59  ? 1129 ASP   A CG    1 
ATOM   5800  O  OD1   . ASP   A 1 1129 ? 166.886 140.411 90.710  1.00 86.95  ? 1129 ASP   A OD1   1 
ATOM   5801  O  OD2   . ASP   A 1 1129 ? 166.856 139.340 88.796  1.00 88.76  ? 1129 ASP   A OD2   1 
ATOM   5802  N  N     . GLU   A 1 1130 ? 168.109 144.210 91.324  1.00 78.72  ? 1130 GLU   A N     1 
ATOM   5803  C  CA    . GLU   A 1 1130 ? 169.204 144.615 92.191  1.00 79.88  ? 1130 GLU   A CA    1 
ATOM   5804  C  C     . GLU   A 1 1130 ? 168.718 145.705 93.138  1.00 78.95  ? 1130 GLU   A C     1 
ATOM   5805  O  O     . GLU   A 1 1130 ? 167.557 146.124 93.054  1.00 79.59  ? 1130 GLU   A O     1 
ATOM   5806  C  CB    . GLU   A 1 1130 ? 170.394 145.095 91.361  1.00 83.74  ? 1130 GLU   A CB    1 
ATOM   5807  N  N     . PRO   A 1 1131 ? 169.568 146.195 94.048  1.00 77.67  ? 1131 PRO   A N     1 
ATOM   5808  C  CA    . PRO   A 1 1131 ? 170.993 145.879 94.218  1.00 77.00  ? 1131 PRO   A CA    1 
ATOM   5809  C  C     . PRO   A 1 1131 ? 171.231 144.574 94.967  1.00 77.22  ? 1131 PRO   A C     1 
ATOM   5810  O  O     . PRO   A 1 1131 ? 172.198 144.453 95.712  1.00 80.46  ? 1131 PRO   A O     1 
ATOM   5811  C  CB    . PRO   A 1 1131 ? 171.503 147.096 95.001  1.00 79.47  ? 1131 PRO   A CB    1 
ATOM   5812  C  CG    . PRO   A 1 1131 ? 170.335 147.432 95.877  1.00 78.52  ? 1131 PRO   A CG    1 
ATOM   5813  C  CD    . PRO   A 1 1131 ? 169.160 147.295 94.941  1.00 78.31  ? 1131 PRO   A CD    1 
ATOM   5814  N  N     . TRP   A 1 1132 ? 170.362 143.577 94.791  1.00 70.27  ? 1132 TRP   A N     1 
ATOM   5815  C  CA    . TRP   A 1 1132 ? 170.604 142.280 95.415  1.00 68.58  ? 1132 TRP   A CA    1 
ATOM   5816  C  C     . TRP   A 1 1132 ? 171.812 141.597 94.790  1.00 73.00  ? 1132 TRP   A C     1 
ATOM   5817  O  O     . TRP   A 1 1132 ? 172.645 141.017 95.496  1.00 72.78  ? 1132 TRP   A O     1 
ATOM   5818  C  CB    . TRP   A 1 1132 ? 169.375 141.378 95.284  1.00 62.60  ? 1132 TRP   A CB    1 
ATOM   5819  C  CG    . TRP   A 1 1132 ? 168.052 142.085 95.277  1.00 63.23  ? 1132 TRP   A CG    1 
ATOM   5820  C  CD1   . TRP   A 1 1132 ? 167.718 143.225 95.950  1.00 71.14  ? 1132 TRP   A CD1   1 
ATOM   5821  C  CD2   . TRP   A 1 1132 ? 166.873 141.675 94.575  1.00 68.38  ? 1132 TRP   A CD2   1 
ATOM   5822  N  NE1   . TRP   A 1 1132 ? 166.409 143.558 95.696  1.00 75.36  ? 1132 TRP   A NE1   1 
ATOM   5823  C  CE2   . TRP   A 1 1132 ? 165.868 142.620 94.857  1.00 75.82  ? 1132 TRP   A CE2   1 
ATOM   5824  C  CE3   . TRP   A 1 1132 ? 166.572 140.602 93.730  1.00 70.93  ? 1132 TRP   A CE3   1 
ATOM   5825  C  CZ2   . TRP   A 1 1132 ? 164.584 142.525 94.325  1.00 76.44  ? 1132 TRP   A CZ2   1 
ATOM   5826  C  CZ3   . TRP   A 1 1132 ? 165.297 140.509 93.204  1.00 75.47  ? 1132 TRP   A CZ3   1 
ATOM   5827  C  CH2   . TRP   A 1 1132 ? 164.319 141.465 93.502  1.00 76.23  ? 1132 TRP   A CH2   1 
ATOM   5828  N  N     . ARG   A 1 1133 ? 171.925 141.662 93.465  1.00 66.61  ? 1133 ARG   A N     1 
ATOM   5829  C  CA    . ARG   A 1 1133 ? 172.976 140.945 92.759  1.00 66.30  ? 1133 ARG   A CA    1 
ATOM   5830  C  C     . ARG   A 1 1133 ? 174.352 141.385 93.240  1.00 65.20  ? 1133 ARG   A C     1 
ATOM   5831  O  O     . ARG   A 1 1133 ? 174.604 142.574 93.455  1.00 66.25  ? 1133 ARG   A O     1 
ATOM   5832  C  CB    . ARG   A 1 1133 ? 172.842 141.172 91.252  1.00 68.17  ? 1133 ARG   A CB    1 
ATOM   5833  C  CG    . ARG   A 1 1133 ? 172.677 139.896 90.446  1.00 66.88  ? 1133 ARG   A CG    1 
ATOM   5834  C  CD    . ARG   A 1 1133 ? 171.231 139.431 90.424  1.00 60.90  ? 1133 ARG   A CD    1 
ATOM   5835  N  NE    . ARG   A 1 1133 ? 171.107 138.098 89.850  1.00 61.26  ? 1133 ARG   A NE    1 
ATOM   5836  C  CZ    . ARG   A 1 1133 ? 169.960 137.453 89.689  1.00 67.54  ? 1133 ARG   A CZ    1 
ATOM   5837  N  NH1   . ARG   A 1 1133 ? 168.807 137.993 90.047  1.00 70.79  ? 1133 ARG   A NH1   1 
ATOM   5838  N  NH2   . ARG   A 1 1133 ? 169.971 136.232 89.162  1.00 65.06  ? 1133 ARG   A NH2   1 
ATOM   5839  N  N     . ILE   A 1 1134 ? 175.242 140.415 93.412  1.00 55.14  ? 1134 ILE   A N     1 
ATOM   5840  C  CA    . ILE   A 1 1134 ? 176.605 140.676 93.859  1.00 53.65  ? 1134 ILE   A CA    1 
ATOM   5841  C  C     . ILE   A 1 1134 ? 177.477 140.904 92.633  1.00 55.27  ? 1134 ILE   A C     1 
ATOM   5842  O  O     . ILE   A 1 1134 ? 177.649 140.003 91.805  1.00 56.86  ? 1134 ILE   A O     1 
ATOM   5843  C  CB    . ILE   A 1 1134 ? 177.143 139.517 94.710  1.00 56.15  ? 1134 ILE   A CB    1 
ATOM   5844  C  CG1   . ILE   A 1 1134 ? 176.211 139.246 95.891  1.00 53.68  ? 1134 ILE   A CG1   1 
ATOM   5845  C  CG2   . ILE   A 1 1134 ? 178.546 139.826 95.201  1.00 57.65  ? 1134 ILE   A CG2   1 
ATOM   5846  C  CD1   . ILE   A 1 1134 ? 175.928 137.783 96.118  1.00 52.72  ? 1134 ILE   A CD1   1 
ATOM   5847  N  N     . THR   A 1 1135 ? 178.027 142.108 92.514  1.00 57.26  ? 1135 THR   A N     1 
ATOM   5848  C  CA    . THR   A 1 1135 ? 178.907 142.417 91.397  1.00 58.21  ? 1135 THR   A CA    1 
ATOM   5849  C  C     . THR   A 1 1135 ? 180.260 141.747 91.589  1.00 61.08  ? 1135 THR   A C     1 
ATOM   5850  O  O     . THR   A 1 1135 ? 180.831 141.764 92.682  1.00 66.90  ? 1135 THR   A O     1 
ATOM   5851  C  CB    . THR   A 1 1135 ? 179.084 143.929 91.260  1.00 58.63  ? 1135 THR   A CB    1 
ATOM   5852  O  OG1   . THR   A 1 1135 ? 180.111 144.376 92.153  1.00 59.61  ? 1135 THR   A OG1   1 
ATOM   5853  C  CG2   . THR   A 1 1135 ? 177.785 144.646 91.594  1.00 60.52  ? 1135 THR   A CG2   1 
ATOM   5854  N  N     . ASP   A 1 1136 ? 180.775 141.147 90.512  1.00 56.86  ? 1136 ASP   A N     1 
ATOM   5855  C  CA    . ASP   A 1 1136 ? 182.077 140.493 90.589  1.00 57.37  ? 1136 ASP   A CA    1 
ATOM   5856  C  C     . ASP   A 1 1136 ? 183.161 141.460 91.046  1.00 55.65  ? 1136 ASP   A C     1 
ATOM   5857  O  O     . ASP   A 1 1136 ? 184.109 141.054 91.728  1.00 56.47  ? 1136 ASP   A O     1 
ATOM   5858  C  CB    . ASP   A 1 1136 ? 182.443 139.885 89.235  1.00 52.06  ? 1136 ASP   A CB    1 
ATOM   5859  N  N     . ASN   A 1 1137 ? 183.036 142.739 90.688  1.00 53.28  ? 1137 ASN   A N     1 
ATOM   5860  C  CA    . ASN   A 1 1137 ? 184.020 143.727 91.116  1.00 50.87  ? 1137 ASN   A CA    1 
ATOM   5861  C  C     . ASN   A 1 1137 ? 184.096 143.797 92.635  1.00 55.43  ? 1137 ASN   A C     1 
ATOM   5862  O  O     . ASN   A 1 1137 ? 185.188 143.812 93.214  1.00 61.16  ? 1137 ASN   A O     1 
ATOM   5863  C  CB    . ASN   A 1 1137 ? 183.677 145.095 90.527  1.00 54.32  ? 1137 ASN   A CB    1 
ATOM   5864  N  N     . GLU   A 1 1138 ? 182.940 143.834 93.302  1.00 59.86  ? 1138 GLU   A N     1 
ATOM   5865  C  CA    . GLU   A 1 1138 ? 182.935 143.865 94.761  1.00 58.84  ? 1138 GLU   A CA    1 
ATOM   5866  C  C     . GLU   A 1 1138 ? 183.374 142.527 95.343  1.00 54.72  ? 1138 GLU   A C     1 
ATOM   5867  O  O     . GLU   A 1 1138 ? 184.095 142.487 96.347  1.00 49.67  ? 1138 GLU   A O     1 
ATOM   5868  C  CB    . GLU   A 1 1138 ? 181.547 144.251 95.275  1.00 54.70  ? 1138 GLU   A CB    1 
ATOM   5869  C  CG    . GLU   A 1 1138 ? 180.558 143.098 95.341  1.00 57.30  ? 1138 GLU   A CG    1 
ATOM   5870  C  CD    . GLU   A 1 1138 ? 179.260 143.480 96.024  1.00 62.22  ? 1138 GLU   A CD    1 
ATOM   5871  O  OE1   . GLU   A 1 1138 ? 179.167 144.614 96.538  1.00 61.44  ? 1138 GLU   A OE1   1 
ATOM   5872  O  OE2   . GLU   A 1 1138 ? 178.331 142.646 96.047  1.00 64.05  ? 1138 GLU   A OE2   1 
ATOM   5873  N  N     . LEU   A 1 1139 ? 182.951 141.420 94.728  1.00 51.14  ? 1139 LEU   A N     1 
ATOM   5874  C  CA    . LEU   A 1 1139 ? 183.348 140.106 95.222  1.00 47.77  ? 1139 LEU   A CA    1 
ATOM   5875  C  C     . LEU   A 1 1139 ? 184.862 139.941 95.187  1.00 53.73  ? 1139 LEU   A C     1 
ATOM   5876  O  O     . LEU   A 1 1139 ? 185.436 139.228 96.018  1.00 57.51  ? 1139 LEU   A O     1 
ATOM   5877  C  CB    . LEU   A 1 1139 ? 182.668 139.010 94.404  1.00 39.68  ? 1139 LEU   A CB    1 
ATOM   5878  N  N     . GLU   A 1 1140 ? 185.526 140.591 94.231  1.00 51.45  ? 1140 GLU   A N     1 
ATOM   5879  C  CA    . GLU   A 1 1140 ? 186.981 140.541 94.167  1.00 47.90  ? 1140 GLU   A CA    1 
ATOM   5880  C  C     . GLU   A 1 1140 ? 187.642 141.632 94.998  1.00 52.69  ? 1140 GLU   A C     1 
ATOM   5881  O  O     . GLU   A 1 1140 ? 188.787 141.456 95.428  1.00 63.38  ? 1140 GLU   A O     1 
ATOM   5882  C  CB    . GLU   A 1 1140 ? 187.449 140.646 92.714  1.00 49.87  ? 1140 GLU   A CB    1 
ATOM   5883  N  N     . LEU   A 1 1141 ? 186.954 142.749 95.231  1.00 47.63  ? 1141 LEU   A N     1 
ATOM   5884  C  CA    . LEU   A 1 1141 ? 187.512 143.852 96.000  1.00 44.62  ? 1141 LEU   A CA    1 
ATOM   5885  C  C     . LEU   A 1 1141 ? 187.373 143.665 97.504  1.00 51.36  ? 1141 LEU   A C     1 
ATOM   5886  O  O     . LEU   A 1 1141 ? 188.024 144.389 98.265  1.00 47.27  ? 1141 LEU   A O     1 
ATOM   5887  C  CB    . LEU   A 1 1141 ? 186.840 145.168 95.588  1.00 39.71  ? 1141 LEU   A CB    1 
ATOM   5888  C  CG    . LEU   A 1 1141 ? 187.434 146.472 96.122  1.00 45.19  ? 1141 LEU   A CG    1 
ATOM   5889  C  CD1   . LEU   A 1 1141 ? 187.242 147.597 95.118  1.00 49.77  ? 1141 LEU   A CD1   1 
ATOM   5890  C  CD2   . LEU   A 1 1141 ? 186.811 146.844 97.454  1.00 46.83  ? 1141 LEU   A CD2   1 
ATOM   5891  N  N     . TYR   A 1 1142 ? 186.552 142.714 97.949  1.00 53.35  ? 1142 TYR   A N     1 
ATOM   5892  C  CA    . TYR   A 1 1142 ? 186.319 142.472 99.368  1.00 45.88  ? 1142 TYR   A CA    1 
ATOM   5893  C  C     . TYR   A 1 1142 ? 186.567 141.013 99.737  1.00 50.44  ? 1142 TYR   A C     1 
ATOM   5894  O  O     . TYR   A 1 1142 ? 185.919 140.476 100.637 1.00 53.60  ? 1142 TYR   A O     1 
ATOM   5895  C  CB    . TYR   A 1 1142 ? 184.901 142.886 99.763  1.00 44.07  ? 1142 TYR   A CB    1 
ATOM   5896  C  CG    . TYR   A 1 1142 ? 184.681 144.381 99.817  1.00 45.24  ? 1142 TYR   A CG    1 
ATOM   5897  C  CD1   . TYR   A 1 1142 ? 185.274 145.156 100.804 1.00 49.87  ? 1142 TYR   A CD1   1 
ATOM   5898  C  CD2   . TYR   A 1 1142 ? 183.880 145.018 98.879  1.00 45.84  ? 1142 TYR   A CD2   1 
ATOM   5899  C  CE1   . TYR   A 1 1142 ? 185.074 146.522 100.856 1.00 53.17  ? 1142 TYR   A CE1   1 
ATOM   5900  C  CE2   . TYR   A 1 1142 ? 183.676 146.383 98.922  1.00 47.56  ? 1142 TYR   A CE2   1 
ATOM   5901  C  CZ    . TYR   A 1 1142 ? 184.275 147.130 99.912  1.00 56.21  ? 1142 TYR   A CZ    1 
ATOM   5902  O  OH    . TYR   A 1 1142 ? 184.074 148.490 99.960  1.00 54.25  ? 1142 TYR   A OH    1 
ATOM   5903  N  N     . LYS   A 1 1143 ? 187.499 140.354 99.045  1.00 44.37  ? 1143 LYS   A N     1 
ATOM   5904  C  CA    . LYS   A 1 1143 ? 187.819 138.972 99.386  1.00 47.20  ? 1143 LYS   A CA    1 
ATOM   5905  C  C     . LYS   A 1 1143 ? 188.357 138.860 100.805 1.00 49.15  ? 1143 LYS   A C     1 
ATOM   5906  O  O     . LYS   A 1 1143 ? 188.153 137.837 101.471 1.00 46.64  ? 1143 LYS   A O     1 
ATOM   5907  C  CB    . LYS   A 1 1143 ? 188.827 138.404 98.387  1.00 36.67  ? 1143 LYS   A CB    1 
ATOM   5908  N  N     . THR   A 1 1144 ? 189.036 139.903 101.288 1.00 42.47  ? 1144 THR   A N     1 
ATOM   5909  C  CA    . THR   A 1 1144 ? 189.573 139.864 102.642 1.00 42.19  ? 1144 THR   A CA    1 
ATOM   5910  C  C     . THR   A 1 1144 ? 188.462 139.714 103.671 1.00 44.30  ? 1144 THR   A C     1 
ATOM   5911  O  O     . THR   A 1 1144 ? 188.572 138.904 104.593 1.00 38.66  ? 1144 THR   A O     1 
ATOM   5912  C  CB    . THR   A 1 1144 ? 190.393 141.123 102.927 1.00 42.40  ? 1144 THR   A CB    1 
ATOM   5913  O  OG1   . THR   A 1 1144 ? 189.516 142.251 103.034 1.00 54.05  ? 1144 THR   A OG1   1 
ATOM   5914  C  CG2   . THR   A 1 1144 ? 191.395 141.368 101.812 1.00 36.87  ? 1144 THR   A CG2   1 
ATOM   5915  N  N     . LYS   A 1 1145 ? 187.374 140.474 103.521 1.00 42.68  ? 1145 LYS   A N     1 
ATOM   5916  C  CA    . LYS   A 1 1145 ? 186.300 140.420 104.510 1.00 40.79  ? 1145 LYS   A CA    1 
ATOM   5917  C  C     . LYS   A 1 1145 ? 185.557 139.088 104.462 1.00 37.97  ? 1145 LYS   A C     1 
ATOM   5918  O  O     . LYS   A 1 1145 ? 185.168 138.553 105.506 1.00 51.08  ? 1145 LYS   A O     1 
ATOM   5919  C  CB    . LYS   A 1 1145 ? 185.335 141.586 104.302 1.00 37.22  ? 1145 LYS   A CB    1 
ATOM   5920  C  CG    . LYS   A 1 1145 ? 185.889 142.924 104.762 1.00 39.88  ? 1145 LYS   A CG    1 
ATOM   5921  C  CD    . LYS   A 1 1145 ? 184.907 144.054 104.510 1.00 43.79  ? 1145 LYS   A CD    1 
ATOM   5922  C  CE    . LYS   A 1 1145 ? 183.806 144.075 105.557 1.00 34.80  ? 1145 LYS   A CE    1 
ATOM   5923  N  NZ    . LYS   A 1 1145 ? 184.352 144.101 106.940 1.00 38.71  ? 1145 LYS   A NZ    1 
ATOM   5924  N  N     . THR   A 1 1146 ? 185.341 138.539 103.266 1.00 32.58  ? 1146 THR   A N     1 
ATOM   5925  C  CA    . THR   A 1 1146 ? 184.700 137.231 103.164 1.00 39.95  ? 1146 THR   A CA    1 
ATOM   5926  C  C     . THR   A 1 1146 ? 185.562 136.148 103.802 1.00 49.88  ? 1146 THR   A C     1 
ATOM   5927  O  O     . THR   A 1 1146 ? 185.071 135.310 104.575 1.00 47.75  ? 1146 THR   A O     1 
ATOM   5928  C  CB    . THR   A 1 1146 ? 184.418 136.900 101.698 1.00 36.85  ? 1146 THR   A CB    1 
ATOM   5929  O  OG1   . THR   A 1 1146 ? 183.793 138.025 101.066 1.00 40.09  ? 1146 THR   A OG1   1 
ATOM   5930  C  CG2   . THR   A 1 1146 ? 183.509 135.691 101.588 1.00 42.20  ? 1146 THR   A CG2   1 
ATOM   5931  N  N     . TYR   A 1 1147 ? 186.856 136.147 103.481 1.00 47.24  ? 1147 TYR   A N     1 
ATOM   5932  C  CA    . TYR   A 1 1147 ? 187.760 135.190 104.101 1.00 37.31  ? 1147 TYR   A CA    1 
ATOM   5933  C  C     . TYR   A 1 1147 ? 187.792 135.381 105.610 1.00 39.30  ? 1147 TYR   A C     1 
ATOM   5934  O  O     . TYR   A 1 1147 ? 187.880 134.408 106.364 1.00 49.02  ? 1147 TYR   A O     1 
ATOM   5935  C  CB    . TYR   A 1 1147 ? 189.160 135.333 103.505 1.00 42.15  ? 1147 TYR   A CB    1 
ATOM   5936  C  CG    . TYR   A 1 1147 ? 189.307 134.689 102.147 1.00 53.77  ? 1147 TYR   A CG    1 
ATOM   5937  C  CD1   . TYR   A 1 1147 ? 188.395 134.944 101.134 1.00 42.79  ? 1147 TYR   A CD1   1 
ATOM   5938  C  CD2   . TYR   A 1 1147 ? 190.360 133.826 101.877 1.00 53.64  ? 1147 TYR   A CD2   1 
ATOM   5939  C  CE1   . TYR   A 1 1147 ? 188.524 134.359 99.894  1.00 44.83  ? 1147 TYR   A CE1   1 
ATOM   5940  C  CE2   . TYR   A 1 1147 ? 190.499 133.237 100.639 1.00 47.84  ? 1147 TYR   A CE2   1 
ATOM   5941  C  CZ    . TYR   A 1 1147 ? 189.578 133.507 99.652  1.00 50.01  ? 1147 TYR   A CZ    1 
ATOM   5942  O  OH    . TYR   A 1 1147 ? 189.712 132.921 98.417  1.00 52.26  ? 1147 TYR   A OH    1 
ATOM   5943  N  N     . ARG   A 1 1148 ? 187.717 136.633 106.067 1.00 33.67  ? 1148 ARG   A N     1 
ATOM   5944  C  CA    . ARG   A 1 1148 ? 187.704 136.914 107.495 1.00 35.44  ? 1148 ARG   A CA    1 
ATOM   5945  C  C     . ARG   A 1 1148 ? 186.462 136.328 108.151 1.00 34.18  ? 1148 ARG   A C     1 
ATOM   5946  O  O     . ARG   A 1 1148 ? 186.539 135.748 109.235 1.00 38.77  ? 1148 ARG   A O     1 
ATOM   5947  C  CB    . ARG   A 1 1148 ? 187.808 138.426 107.720 1.00 37.62  ? 1148 ARG   A CB    1 
ATOM   5948  C  CG    . ARG   A 1 1148 ? 188.584 138.817 108.966 1.00 38.68  ? 1148 ARG   A CG    1 
ATOM   5949  C  CD    . ARG   A 1 1148 ? 189.396 140.092 108.763 1.00 40.79  ? 1148 ARG   A CD    1 
ATOM   5950  N  NE    . ARG   A 1 1148 ? 188.609 141.235 108.320 1.00 41.31  ? 1148 ARG   A NE    1 
ATOM   5951  C  CZ    . ARG   A 1 1148 ? 187.605 141.769 108.998 1.00 41.64  ? 1148 ARG   A CZ    1 
ATOM   5952  N  NH1   . ARG   A 1 1148 ? 187.195 141.259 110.150 1.00 40.90  ? 1148 ARG   A NH1   1 
ATOM   5953  N  NH2   . ARG   A 1 1148 ? 186.993 142.841 108.507 1.00 40.08  ? 1148 ARG   A NH2   1 
ATOM   5954  N  N     . GLN   A 1 1149 ? 185.304 136.459 107.498 1.00 34.80  ? 1149 GLN   A N     1 
ATOM   5955  C  CA    . GLN   A 1 1149 ? 184.080 135.880 108.051 1.00 21.06  ? 1149 GLN   A CA    1 
ATOM   5956  C  C     . GLN   A 1 1149 ? 184.184 134.364 108.142 1.00 27.72  ? 1149 GLN   A C     1 
ATOM   5957  O  O     . GLN   A 1 1149 ? 183.827 133.765 109.167 1.00 34.53  ? 1149 GLN   A O     1 
ATOM   5958  C  CB    . GLN   A 1 1149 ? 182.869 136.281 107.205 1.00 29.35  ? 1149 GLN   A CB    1 
ATOM   5959  C  CG    . GLN   A 1 1149 ? 182.772 137.754 106.884 1.00 32.13  ? 1149 GLN   A CG    1 
ATOM   5960  C  CD    . GLN   A 1 1149 ? 183.027 138.627 108.085 1.00 33.61  ? 1149 GLN   A CD    1 
ATOM   5961  O  OE1   . GLN   A 1 1149 ? 182.874 138.196 109.228 1.00 37.30  ? 1149 GLN   A OE1   1 
ATOM   5962  N  NE2   . GLN   A 1 1149 ? 183.426 139.865 107.835 1.00 30.65  ? 1149 GLN   A NE2   1 
ATOM   5963  N  N     . ILE   A 1 1150 ? 184.682 133.723 107.084 1.00 30.06  ? 1150 ILE   A N     1 
ATOM   5964  C  CA    . ILE   A 1 1150 ? 184.767 132.265 107.096 1.00 30.23  ? 1150 ILE   A CA    1 
ATOM   5965  C  C     . ILE   A 1 1150 ? 185.765 131.793 108.150 1.00 40.66  ? 1150 ILE   A C     1 
ATOM   5966  O  O     . ILE   A 1 1150 ? 185.497 130.847 108.906 1.00 46.94  ? 1150 ILE   A O     1 
ATOM   5967  C  CB    . ILE   A 1 1150 ? 185.121 131.733 105.696 1.00 29.91  ? 1150 ILE   A CB    1 
ATOM   5968  C  CG1   . ILE   A 1 1150 ? 184.094 132.212 104.670 1.00 30.75  ? 1150 ILE   A CG1   1 
ATOM   5969  C  CG2   . ILE   A 1 1150 ? 185.181 130.214 105.703 1.00 28.83  ? 1150 ILE   A CG2   1 
ATOM   5970  C  CD1   . ILE   A 1 1150 ? 184.530 132.026 103.233 1.00 37.11  ? 1150 ILE   A CD1   1 
ATOM   5971  N  N     . ARG   A 1 1151 ? 186.927 132.445 108.222 1.00 30.64  ? 1151 ARG   A N     1 
ATOM   5972  C  CA    . ARG   A 1 1151 ? 187.933 132.087 109.212 1.00 24.80  ? 1151 ARG   A CA    1 
ATOM   5973  C  C     . ARG   A 1 1151 ? 187.417 132.317 110.626 1.00 35.43  ? 1151 ARG   A C     1 
ATOM   5974  O  O     . ARG   A 1 1151 ? 187.705 131.532 111.536 1.00 43.76  ? 1151 ARG   A O     1 
ATOM   5975  C  CB    . ARG   A 1 1151 ? 189.207 132.896 108.962 1.00 34.32  ? 1151 ARG   A CB    1 
ATOM   5976  C  CG    . ARG   A 1 1151 ? 190.428 132.442 109.745 1.00 36.88  ? 1151 ARG   A CG    1 
ATOM   5977  C  CD    . ARG   A 1 1151 ? 190.663 130.948 109.601 1.00 38.45  ? 1151 ARG   A CD    1 
ATOM   5978  N  NE    . ARG   A 1 1151 ? 191.837 130.504 110.344 1.00 41.77  ? 1151 ARG   A NE    1 
ATOM   5979  C  CZ    . ARG   A 1 1151 ? 191.817 129.601 111.315 1.00 46.08  ? 1151 ARG   A CZ    1 
ATOM   5980  N  NH1   . ARG   A 1 1151 ? 190.692 129.013 111.689 1.00 43.38  ? 1151 ARG   A NH1   1 
ATOM   5981  N  NH2   . ARG   A 1 1151 ? 192.953 129.279 111.925 1.00 42.25  ? 1151 ARG   A NH2   1 
ATOM   5982  N  N     . LEU   A 1 1152 ? 186.669 133.402 110.835 1.00 31.98  ? 1152 LEU   A N     1 
ATOM   5983  C  CA    . LEU   A 1 1152 ? 186.104 133.675 112.149 1.00 33.14  ? 1152 LEU   A CA    1 
ATOM   5984  C  C     . LEU   A 1 1152 ? 185.093 132.611 112.545 1.00 31.98  ? 1152 LEU   A C     1 
ATOM   5985  O  O     . LEU   A 1 1152 ? 185.029 132.212 113.710 1.00 43.46  ? 1152 LEU   A O     1 
ATOM   5986  C  CB    . LEU   A 1 1152 ? 185.461 135.060 112.163 1.00 31.52  ? 1152 LEU   A CB    1 
ATOM   5987  C  CG    . LEU   A 1 1152 ? 186.424 136.233 112.341 1.00 30.31  ? 1152 LEU   A CG    1 
ATOM   5988  C  CD1   . LEU   A 1 1152 ? 185.683 137.549 112.225 1.00 34.67  ? 1152 LEU   A CD1   1 
ATOM   5989  C  CD2   . LEU   A 1 1152 ? 187.148 136.141 113.672 1.00 34.62  ? 1152 LEU   A CD2   1 
ATOM   5990  N  N     . ASN   A 1 1153 ? 184.279 132.149 111.594 1.00 32.93  ? 1153 ASN   A N     1 
ATOM   5991  C  CA    . ASN   A 1 1153 ? 183.364 131.054 111.902 1.00 35.10  ? 1153 ASN   A CA    1 
ATOM   5992  C  C     . ASN   A 1 1153 ? 184.131 129.789 112.264 1.00 39.97  ? 1153 ASN   A C     1 
ATOM   5993  O  O     . ASN   A 1 1153 ? 183.754 129.067 113.196 1.00 39.78  ? 1153 ASN   A O     1 
ATOM   5994  C  CB    . ASN   A 1 1153 ? 182.426 130.795 110.724 1.00 33.68  ? 1153 ASN   A CB    1 
ATOM   5995  C  CG    . ASN   A 1 1153 ? 181.269 129.883 111.090 1.00 37.45  ? 1153 ASN   A CG    1 
ATOM   5996  O  OD1   . ASN   A 1 1153 ? 181.176 128.757 110.605 1.00 42.78  ? 1153 ASN   A OD1   1 
ATOM   5997  N  ND2   . ASN   A 1 1153 ? 180.378 130.370 111.947 1.00 32.36  ? 1153 ASN   A ND2   1 
ATOM   5998  N  N     . GLU   A 1 1154 ? 185.212 129.504 111.536 1.00 44.59  ? 1154 GLU   A N     1 
ATOM   5999  C  CA    . GLU   A 1 1154 ? 186.055 128.361 111.883 1.00 43.69  ? 1154 GLU   A CA    1 
ATOM   6000  C  C     . GLU   A 1 1154 ? 186.583 128.488 113.307 1.00 39.35  ? 1154 GLU   A C     1 
ATOM   6001  O  O     . GLU   A 1 1154 ? 186.532 127.535 114.095 1.00 38.04  ? 1154 GLU   A O     1 
ATOM   6002  C  CB    . GLU   A 1 1154 ? 187.217 128.250 110.897 1.00 41.29  ? 1154 GLU   A CB    1 
ATOM   6003  C  CG    . GLU   A 1 1154 ? 187.138 127.075 109.945 1.00 45.19  ? 1154 GLU   A CG    1 
ATOM   6004  C  CD    . GLU   A 1 1154 ? 188.087 127.227 108.773 1.00 50.53  ? 1154 GLU   A CD    1 
ATOM   6005  O  OE1   . GLU   A 1 1154 ? 189.083 127.967 108.907 1.00 51.90  ? 1154 GLU   A OE1   1 
ATOM   6006  O  OE2   . GLU   A 1 1154 ? 187.843 126.607 107.719 1.00 54.36  ? 1154 GLU   A OE2   1 
ATOM   6007  N  N     . LEU   A 1 1155 ? 187.100 129.669 113.650 1.00 35.28  ? 1155 LEU   A N     1 
ATOM   6008  C  CA    . LEU   A 1 1155 ? 187.658 129.889 114.980 1.00 33.99  ? 1155 LEU   A CA    1 
ATOM   6009  C  C     . LEU   A 1 1155 ? 186.590 129.752 116.057 1.00 32.97  ? 1155 LEU   A C     1 
ATOM   6010  O  O     . LEU   A 1 1155 ? 186.834 129.160 117.114 1.00 40.98  ? 1155 LEU   A O     1 
ATOM   6011  C  CB    . LEU   A 1 1155 ? 188.314 131.268 115.045 1.00 35.66  ? 1155 LEU   A CB    1 
ATOM   6012  C  CG    . LEU   A 1 1155 ? 189.660 131.419 114.334 1.00 38.45  ? 1155 LEU   A CG    1 
ATOM   6013  C  CD1   . LEU   A 1 1155 ? 190.143 132.858 114.392 1.00 36.59  ? 1155 LEU   A CD1   1 
ATOM   6014  C  CD2   . LEU   A 1 1155 ? 190.695 130.484 114.935 1.00 37.20  ? 1155 LEU   A CD2   1 
ATOM   6015  N  N     . LEU   A 1 1156 ? 185.400 130.304 115.810 1.00 38.06  ? 1156 LEU   A N     1 
ATOM   6016  C  CA    . LEU   A 1 1156 ? 184.311 130.188 116.773 1.00 26.45  ? 1156 LEU   A CA    1 
ATOM   6017  C  C     . LEU   A 1 1156 ? 183.925 128.733 116.989 1.00 32.07  ? 1156 LEU   A C     1 
ATOM   6018  O  O     . LEU   A 1 1156 ? 183.702 128.303 118.126 1.00 32.87  ? 1156 LEU   A O     1 
ATOM   6019  C  CB    . LEU   A 1 1156 ? 183.104 130.994 116.297 1.00 29.57  ? 1156 LEU   A CB    1 
ATOM   6020  C  CG    . LEU   A 1 1156 ? 183.235 132.517 116.301 1.00 24.09  ? 1156 LEU   A CG    1 
ATOM   6021  C  CD1   . LEU   A 1 1156 ? 182.051 133.153 115.597 1.00 40.43  ? 1156 LEU   A CD1   1 
ATOM   6022  C  CD2   . LEU   A 1 1156 ? 183.344 133.030 117.720 1.00 21.08  ? 1156 LEU   A CD2   1 
ATOM   6023  N  N     . LYS   A 1 1157 ? 183.838 127.956 115.907 1.00 41.86  ? 1157 LYS   A N     1 
ATOM   6024  C  CA    . LYS   A 1 1157 ? 183.505 126.544 116.052 1.00 43.22  ? 1157 LYS   A CA    1 
ATOM   6025  C  C     . LYS   A 1 1157 ? 184.592 125.799 116.815 1.00 45.96  ? 1157 LYS   A C     1 
ATOM   6026  O  O     . LYS   A 1 1157 ? 184.296 124.913 117.624 1.00 44.71  ? 1157 LYS   A O     1 
ATOM   6027  C  CB    . LYS   A 1 1157 ? 183.273 125.912 114.680 1.00 39.39  ? 1157 LYS   A CB    1 
ATOM   6028  C  CG    . LYS   A 1 1157 ? 182.216 126.621 113.851 1.00 48.01  ? 1157 LYS   A CG    1 
ATOM   6029  C  CD    . LYS   A 1 1157 ? 181.167 125.647 113.343 1.00 46.61  ? 1157 LYS   A CD    1 
ATOM   6030  C  CE    . LYS   A 1 1157 ? 181.768 124.623 112.398 1.00 49.56  ? 1157 LYS   A CE    1 
ATOM   6031  N  NZ    . LYS   A 1 1157 ? 180.786 124.185 111.370 1.00 47.80  ? 1157 LYS   A NZ    1 
ATOM   6032  N  N     . GLU   A 1 1158 ? 185.857 126.145 116.572 1.00 47.39  ? 1158 GLU   A N     1 
ATOM   6033  C  CA    . GLU   A 1 1158 ? 186.957 125.432 117.213 1.00 44.87  ? 1158 GLU   A CA    1 
ATOM   6034  C  C     . GLU   A 1 1158 ? 187.125 125.804 118.682 1.00 46.61  ? 1158 GLU   A C     1 
ATOM   6035  O  O     . GLU   A 1 1158 ? 187.587 124.974 119.472 1.00 51.03  ? 1158 GLU   A O     1 
ATOM   6036  C  CB    . GLU   A 1 1158 ? 188.261 125.691 116.457 1.00 44.31  ? 1158 GLU   A CB    1 
ATOM   6037  C  CG    . GLU   A 1 1158 ? 189.513 125.500 117.297 1.00 44.47  ? 1158 GLU   A CG    1 
ATOM   6038  C  CD    . GLU   A 1 1158 ? 190.694 126.295 116.775 1.00 55.12  ? 1158 GLU   A CD    1 
ATOM   6039  O  OE1   . GLU   A 1 1158 ? 191.102 126.068 115.617 1.00 54.33  ? 1158 GLU   A OE1   1 
ATOM   6040  O  OE2   . GLU   A 1 1158 ? 191.215 127.149 117.522 1.00 57.30  ? 1158 GLU   A OE2   1 
ATOM   6041  N  N     . HIS   A 1 1159 ? 186.766 127.026 119.071 1.00 43.77  ? 1159 HIS   A N     1 
ATOM   6042  C  CA    . HIS   A 1 1159 ? 187.013 127.514 120.423 1.00 34.75  ? 1159 HIS   A CA    1 
ATOM   6043  C  C     . HIS   A 1 1159 ? 185.749 127.696 121.250 1.00 42.63  ? 1159 HIS   A C     1 
ATOM   6044  O  O     . HIS   A 1 1159 ? 185.699 127.259 122.404 1.00 43.68  ? 1159 HIS   A O     1 
ATOM   6045  C  CB    . HIS   A 1 1159 ? 187.779 128.844 120.366 1.00 29.50  ? 1159 HIS   A CB    1 
ATOM   6046  C  CG    . HIS   A 1 1159 ? 189.249 128.689 120.131 1.00 44.54  ? 1159 HIS   A CG    1 
ATOM   6047  N  ND1   . HIS   A 1 1159 ? 190.006 127.723 120.759 1.00 46.49  ? 1159 HIS   A ND1   1 
ATOM   6048  C  CD2   . HIS   A 1 1159 ? 190.103 129.382 119.342 1.00 41.12  ? 1159 HIS   A CD2   1 
ATOM   6049  C  CE1   . HIS   A 1 1159 ? 191.263 127.828 120.365 1.00 41.80  ? 1159 HIS   A CE1   1 
ATOM   6050  N  NE2   . HIS   A 1 1159 ? 191.348 128.826 119.505 1.00 43.42  ? 1159 HIS   A NE2   1 
ATOM   6051  N  N     . SER   A 1 1160 ? 184.718 128.331 120.692 1.00 50.81  ? 1160 SER   A N     1 
ATOM   6052  C  CA    . SER   A 1 1160 ? 183.554 128.763 121.454 1.00 38.68  ? 1160 SER   A CA    1 
ATOM   6053  C  C     . SER   A 1 1160 ? 182.370 127.810 121.322 1.00 40.10  ? 1160 SER   A C     1 
ATOM   6054  O  O     . SER   A 1 1160 ? 181.256 128.157 121.730 1.00 43.74  ? 1160 SER   A O     1 
ATOM   6055  C  CB    . SER   A 1 1160 ? 183.146 130.173 121.026 1.00 38.96  ? 1160 SER   A CB    1 
ATOM   6056  O  OG    . SER   A 1 1160 ? 182.461 130.847 122.065 1.00 37.72  ? 1160 SER   A OG    1 
ATOM   6057  N  N     . SER   A 1 1161 ? 182.584 126.620 120.759 1.00 42.02  ? 1161 SER   A N     1 
ATOM   6058  C  CA    . SER   A 1 1161 ? 181.486 125.680 120.568 1.00 44.88  ? 1161 SER   A CA    1 
ATOM   6059  C  C     . SER   A 1 1161 ? 180.808 125.294 121.877 1.00 44.75  ? 1161 SER   A C     1 
ATOM   6060  O  O     . SER   A 1 1161 ? 179.629 124.924 121.864 1.00 48.41  ? 1161 SER   A O     1 
ATOM   6061  C  CB    . SER   A 1 1161 ? 181.990 124.423 119.858 1.00 45.06  ? 1161 SER   A CB    1 
ATOM   6062  O  OG    . SER   A 1 1161 ? 182.973 123.759 120.633 1.00 49.41  ? 1161 SER   A OG    1 
ATOM   6063  N  N     . THR   A 1 1162 ? 181.521 125.363 123.000 1.00 45.29  ? 1162 THR   A N     1 
ATOM   6064  C  CA    . THR   A 1 1162 ? 180.984 124.961 124.293 1.00 46.64  ? 1162 THR   A CA    1 
ATOM   6065  C  C     . THR   A 1 1162 ? 180.422 126.125 125.100 1.00 49.45  ? 1162 THR   A C     1 
ATOM   6066  O  O     . THR   A 1 1162 ? 179.981 125.916 126.233 1.00 50.94  ? 1162 THR   A O     1 
ATOM   6067  C  CB    . THR   A 1 1162 ? 182.066 124.251 125.114 1.00 49.96  ? 1162 THR   A CB    1 
ATOM   6068  O  OG1   . THR   A 1 1162 ? 183.323 124.913 124.923 1.00 53.20  ? 1162 THR   A OG1   1 
ATOM   6069  C  CG2   . THR   A 1 1162 ? 182.194 122.801 124.682 1.00 50.42  ? 1162 THR   A CG2   1 
ATOM   6070  N  N     . ALA   A 1 1163 ? 180.426 127.335 124.550 1.00 46.26  ? 1163 ALA   A N     1 
ATOM   6071  C  CA    . ALA   A 1 1163 ? 179.952 128.494 125.292 1.00 44.41  ? 1163 ALA   A CA    1 
ATOM   6072  C  C     . ALA   A 1 1163 ? 178.437 128.454 125.464 1.00 47.29  ? 1163 ALA   A C     1 
ATOM   6073  O  O     . ALA   A 1 1163 ? 177.707 127.908 124.633 1.00 53.63  ? 1163 ALA   A O     1 
ATOM   6074  C  CB    . ALA   A 1 1163 ? 180.360 129.784 124.584 1.00 37.04  ? 1163 ALA   A CB    1 
ATOM   6075  N  N     . ASN   A 1 1164 ? 177.967 129.042 126.566 1.00 36.70  ? 1164 ASN   A N     1 
ATOM   6076  C  CA    . ASN   A 1 1164 ? 176.531 129.230 126.742 1.00 33.91  ? 1164 ASN   A CA    1 
ATOM   6077  C  C     . ASN   A 1 1164 ? 176.006 130.313 125.811 1.00 38.87  ? 1164 ASN   A C     1 
ATOM   6078  O  O     . ASN   A 1 1164 ? 174.885 130.214 125.300 1.00 45.34  ? 1164 ASN   A O     1 
ATOM   6079  C  CB    . ASN   A 1 1164 ? 176.215 129.576 128.197 1.00 35.81  ? 1164 ASN   A CB    1 
ATOM   6080  C  CG    . ASN   A 1 1164 ? 176.141 128.352 129.085 1.00 43.16  ? 1164 ASN   A CG    1 
ATOM   6081  O  OD1   . ASN   A 1 1164 ? 177.159 127.855 129.565 1.00 46.53  ? 1164 ASN   A OD1   1 
ATOM   6082  N  ND2   . ASN   A 1 1164 ? 174.929 127.860 129.312 1.00 50.71  ? 1164 ASN   A ND2   1 
ATOM   6083  N  N     . ILE   A 1 1165 ? 176.803 131.355 125.580 1.00 41.22  ? 1165 ILE   A N     1 
ATOM   6084  C  CA    . ILE   A 1 1165 ? 176.452 132.417 124.648 1.00 37.90  ? 1165 ILE   A CA    1 
ATOM   6085  C  C     . ILE   A 1 1165 ? 177.742 133.003 124.096 1.00 35.90  ? 1165 ILE   A C     1 
ATOM   6086  O  O     . ILE   A 1 1165 ? 178.760 133.071 124.789 1.00 32.18  ? 1165 ILE   A O     1 
ATOM   6087  C  CB    . ILE   A 1 1165 ? 175.587 133.510 125.314 1.00 32.41  ? 1165 ILE   A CB    1 
ATOM   6088  C  CG1   . ILE   A 1 1165 ? 175.202 134.580 124.292 1.00 40.74  ? 1165 ILE   A CG1   1 
ATOM   6089  C  CG2   . ILE   A 1 1165 ? 176.329 134.139 126.480 1.00 30.40  ? 1165 ILE   A CG2   1 
ATOM   6090  C  CD1   . ILE   A 1 1165 ? 174.423 135.733 124.879 1.00 41.64  ? 1165 ILE   A CD1   1 
ATOM   6091  N  N     . ILE   A 1 1166 ? 177.697 133.420 122.835 1.00 27.19  ? 1166 ILE   A N     1 
ATOM   6092  C  CA    . ILE   A 1 1166 ? 178.817 134.084 122.183 1.00 21.22  ? 1166 ILE   A CA    1 
ATOM   6093  C  C     . ILE   A 1 1166 ? 178.411 135.518 121.884 1.00 19.66  ? 1166 ILE   A C     1 
ATOM   6094  O  O     . ILE   A 1 1166 ? 177.276 135.777 121.472 1.00 30.86  ? 1166 ILE   A O     1 
ATOM   6095  C  CB    . ILE   A 1 1166 ? 179.243 133.362 120.890 1.00 22.09  ? 1166 ILE   A CB    1 
ATOM   6096  C  CG1   . ILE   A 1 1166 ? 179.610 131.908 121.182 1.00 25.74  ? 1166 ILE   A CG1   1 
ATOM   6097  C  CG2   . ILE   A 1 1166 ? 180.408 134.087 120.241 1.00 20.47  ? 1166 ILE   A CG2   1 
ATOM   6098  C  CD1   . ILE   A 1 1166 ? 178.602 130.914 120.654 1.00 33.40  ? 1166 ILE   A CD1   1 
ATOM   6099  N  N     . VAL   A 1 1167 ? 179.329 136.450 122.114 1.00 21.50  ? 1167 VAL   A N     1 
ATOM   6100  C  CA    . VAL   A 1 1167 ? 179.155 137.841 121.720 1.00 20.85  ? 1167 VAL   A CA    1 
ATOM   6101  C  C     . VAL   A 1 1167 ? 180.316 138.192 120.805 1.00 23.22  ? 1167 VAL   A C     1 
ATOM   6102  O  O     . VAL   A 1 1167 ? 181.482 138.061 121.197 1.00 39.13  ? 1167 VAL   A O     1 
ATOM   6103  C  CB    . VAL   A 1 1167 ? 179.101 138.783 122.932 1.00 12.73  ? 1167 VAL   A CB    1 
ATOM   6104  C  CG1   . VAL   A 1 1167 ? 179.175 140.231 122.484 1.00 17.84  ? 1167 VAL   A CG1   1 
ATOM   6105  C  CG2   . VAL   A 1 1167 ? 177.840 138.534 123.738 1.00 18.84  ? 1167 VAL   A CG2   1 
ATOM   6106  N  N     . MET   A 1 1168 ? 180.005 138.634 119.590 1.00 23.93  ? 1168 MET   A N     1 
ATOM   6107  C  CA    . MET   A 1 1168 ? 181.025 138.901 118.589 1.00 14.53  ? 1168 MET   A CA    1 
ATOM   6108  C  C     . MET   A 1 1168 ? 180.749 140.234 117.912 1.00 18.95  ? 1168 MET   A C     1 
ATOM   6109  O  O     . MET   A 1 1168 ? 179.599 140.657 117.785 1.00 34.75  ? 1168 MET   A O     1 
ATOM   6110  C  CB    . MET   A 1 1168 ? 181.081 137.779 117.541 1.00 14.90  ? 1168 MET   A CB    1 
ATOM   6111  C  CG    . MET   A 1 1168 ? 181.707 138.183 116.218 1.00 28.45  ? 1168 MET   A CG    1 
ATOM   6112  S  SD    . MET   A 1 1168 ? 183.471 137.823 116.153 1.00 49.98  ? 1168 MET   A SD    1 
ATOM   6113  C  CE    . MET   A 1 1168 ? 183.450 136.035 116.218 1.00 32.24  ? 1168 MET   A CE    1 
ATOM   6114  N  N     . SER   A 1 1169 ? 181.820 140.888 117.468 1.00 23.98  ? 1169 SER   A N     1 
ATOM   6115  C  CA    . SER   A 1 1169 ? 181.676 142.153 116.764 1.00 30.08  ? 1169 SER   A CA    1 
ATOM   6116  C  C     . SER   A 1 1169 ? 180.879 141.957 115.480 1.00 33.72  ? 1169 SER   A C     1 
ATOM   6117  O  O     . SER   A 1 1169 ? 181.055 140.970 114.762 1.00 37.39  ? 1169 SER   A O     1 
ATOM   6118  C  CB    . SER   A 1 1169 ? 183.050 142.740 116.446 1.00 30.00  ? 1169 SER   A CB    1 
ATOM   6119  O  OG    . SER   A 1 1169 ? 183.812 142.910 117.627 1.00 31.40  ? 1169 SER   A OG    1 
ATOM   6120  N  N     . LEU   A 1 1170 ? 180.001 142.913 115.190 1.00 30.19  ? 1170 LEU   A N     1 
ATOM   6121  C  CA    . LEU   A 1 1170 ? 179.141 142.822 114.020 1.00 24.45  ? 1170 LEU   A CA    1 
ATOM   6122  C  C     . LEU   A 1 1170 ? 179.838 143.445 112.820 1.00 28.94  ? 1170 LEU   A C     1 
ATOM   6123  O  O     . LEU   A 1 1170 ? 180.160 144.640 112.858 1.00 33.92  ? 1170 LEU   A O     1 
ATOM   6124  C  CB    . LEU   A 1 1170 ? 177.818 143.522 114.271 1.00 26.32  ? 1170 LEU   A CB    1 
ATOM   6125  C  CG    . LEU   A 1 1170 ? 176.847 143.571 113.090 1.00 28.65  ? 1170 LEU   A CG    1 
ATOM   6126  C  CD1   . LEU   A 1 1170 ? 176.223 142.210 112.847 1.00 31.18  ? 1170 LEU   A CD1   1 
ATOM   6127  C  CD2   . LEU   A 1 1170 ? 175.775 144.614 113.329 1.00 27.40  ? 1170 LEU   A CD2   1 
ATOM   6128  N  N     . PRO   A 1 1171 ? 180.092 142.692 111.751 1.00 21.38  ? 1171 PRO   A N     1 
ATOM   6129  C  CA    . PRO   A 1 1171 ? 180.703 143.295 110.563 1.00 22.62  ? 1171 PRO   A CA    1 
ATOM   6130  C  C     . PRO   A 1 1171 ? 179.867 144.463 110.064 1.00 30.30  ? 1171 PRO   A C     1 
ATOM   6131  O  O     . PRO   A 1 1171 ? 178.635 144.415 110.069 1.00 42.32  ? 1171 PRO   A O     1 
ATOM   6132  C  CB    . PRO   A 1 1171 ? 180.722 142.149 109.547 1.00 24.33  ? 1171 PRO   A CB    1 
ATOM   6133  C  CG    . PRO   A 1 1171 ? 180.600 140.900 110.339 1.00 25.50  ? 1171 PRO   A CG    1 
ATOM   6134  C  CD    . PRO   A 1 1171 ? 180.091 141.221 111.710 1.00 20.57  ? 1171 PRO   A CD    1 
ATOM   6135  N  N     . VAL   A 1 1172 ? 180.547 145.521 109.635 1.00 29.91  ? 1172 VAL   A N     1 
ATOM   6136  C  CA    . VAL   A 1 1172 ? 179.897 146.716 109.112 1.00 31.38  ? 1172 VAL   A CA    1 
ATOM   6137  C  C     . VAL   A 1 1172 ? 180.300 146.880 107.656 1.00 34.46  ? 1172 VAL   A C     1 
ATOM   6138  O  O     . VAL   A 1 1172 ? 181.494 146.920 107.336 1.00 43.20  ? 1172 VAL   A O     1 
ATOM   6139  C  CB    . VAL   A 1 1172 ? 180.263 147.969 109.927 1.00 32.50  ? 1172 VAL   A CB    1 
ATOM   6140  C  CG1   . VAL   A 1 1172 ? 179.998 149.222 109.114 1.00 31.91  ? 1172 VAL   A CG1   1 
ATOM   6141  C  CG2   . VAL   A 1 1172 ? 179.478 147.999 111.223 1.00 29.80  ? 1172 VAL   A CG2   1 
ATOM   6142  N  N     . ALA   A 1 1173 ? 179.308 146.973 106.778 1.00 33.46  ? 1173 ALA   A N     1 
ATOM   6143  C  CA    . ALA   A 1 1173 ? 179.528 147.153 105.351 1.00 42.98  ? 1173 ALA   A CA    1 
ATOM   6144  C  C     . ALA   A 1 1173 ? 179.148 148.573 104.961 1.00 47.42  ? 1173 ALA   A C     1 
ATOM   6145  O  O     . ALA   A 1 1173 ? 178.053 149.039 105.292 1.00 47.84  ? 1173 ALA   A O     1 
ATOM   6146  C  CB    . ALA   A 1 1173 ? 178.715 146.143 104.539 1.00 43.63  ? 1173 ALA   A CB    1 
ATOM   6147  N  N     . ARG   A 1 1174 ? 180.051 149.256 104.262 1.00 46.46  ? 1174 ARG   A N     1 
ATOM   6148  C  CA    . ARG   A 1 1174 ? 179.759 150.605 103.803 1.00 46.68  ? 1174 ARG   A CA    1 
ATOM   6149  C  C     . ARG   A 1 1174 ? 178.583 150.584 102.836 1.00 50.62  ? 1174 ARG   A C     1 
ATOM   6150  O  O     . ARG   A 1 1174 ? 178.507 149.736 101.942 1.00 46.34  ? 1174 ARG   A O     1 
ATOM   6151  C  CB    . ARG   A 1 1174 ? 180.989 151.214 103.129 1.00 45.41  ? 1174 ARG   A CB    1 
ATOM   6152  C  CG    . ARG   A 1 1174 ? 180.895 152.714 102.911 1.00 49.75  ? 1174 ARG   A CG    1 
ATOM   6153  C  CD    . ARG   A 1 1174 ? 182.228 153.291 102.465 1.00 52.76  ? 1174 ARG   A CD    1 
ATOM   6154  N  NE    . ARG   A 1 1174 ? 183.351 152.466 102.892 1.00 46.62  ? 1174 ARG   A NE    1 
ATOM   6155  C  CZ    . ARG   A 1 1174 ? 184.151 152.758 103.907 1.00 53.41  ? 1174 ARG   A CZ    1 
ATOM   6156  N  NH1   . ARG   A 1 1174 ? 183.990 153.862 104.619 1.00 49.28  ? 1174 ARG   A NH1   1 
ATOM   6157  N  NH2   . ARG   A 1 1174 ? 185.138 151.922 104.217 1.00 56.19  ? 1174 ARG   A NH2   1 
ATOM   6158  N  N     . LYS   A 1 1175 ? 177.658 151.522 103.018 1.00 51.13  ? 1175 LYS   A N     1 
ATOM   6159  C  CA    . LYS   A 1 1175 ? 176.474 151.563 102.172 1.00 50.30  ? 1175 LYS   A CA    1 
ATOM   6160  C  C     . LYS   A 1 1175 ? 176.856 152.010 100.767 1.00 52.10  ? 1175 LYS   A C     1 
ATOM   6161  O  O     . LYS   A 1 1175 ? 177.559 153.008 100.589 1.00 51.06  ? 1175 LYS   A O     1 
ATOM   6162  C  CB    . LYS   A 1 1175 ? 175.424 152.499 102.768 1.00 47.59  ? 1175 LYS   A CB    1 
ATOM   6163  C  CG    . LYS   A 1 1175 ? 175.902 153.922 102.996 1.00 51.44  ? 1175 LYS   A CG    1 
ATOM   6164  C  CD    . LYS   A 1 1175 ? 174.763 154.811 103.468 1.00 48.71  ? 1175 LYS   A CD    1 
ATOM   6165  C  CE    . LYS   A 1 1175 ? 175.283 156.031 104.206 1.00 47.66  ? 1175 LYS   A CE    1 
ATOM   6166  N  NZ    . LYS   A 1 1175 ? 176.186 156.845 103.349 1.00 56.48  ? 1175 LYS   A NZ    1 
ATOM   6167  N  N     . GLY   A 1 1176 ? 176.389 151.265 99.767  1.00 52.32  ? 1176 GLY   A N     1 
ATOM   6168  C  CA    . GLY   A 1 1176 ? 176.736 151.515 98.389  1.00 51.99  ? 1176 GLY   A CA    1 
ATOM   6169  C  C     . GLY   A 1 1176 ? 177.926 150.729 97.882  1.00 52.38  ? 1176 GLY   A C     1 
ATOM   6170  O  O     . GLY   A 1 1176 ? 178.120 150.644 96.664  1.00 54.50  ? 1176 GLY   A O     1 
ATOM   6171  N  N     . ALA   A 1 1177 ? 178.724 150.149 98.777  1.00 53.71  ? 1177 ALA   A N     1 
ATOM   6172  C  CA    . ALA   A 1 1177 ? 179.886 149.367 98.375  1.00 50.97  ? 1177 ALA   A CA    1 
ATOM   6173  C  C     . ALA   A 1 1177 ? 179.600 147.875 98.302  1.00 50.31  ? 1177 ALA   A C     1 
ATOM   6174  O  O     . ALA   A 1 1177 ? 180.171 147.185 97.449  1.00 57.89  ? 1177 ALA   A O     1 
ATOM   6175  C  CB    . ALA   A 1 1177 ? 181.047 149.615 99.341  1.00 51.08  ? 1177 ALA   A CB    1 
ATOM   6176  N  N     . VAL   A 1 1178 ? 178.735 147.361 99.172  1.00 41.48  ? 1178 VAL   A N     1 
ATOM   6177  C  CA    . VAL   A 1 1178 ? 178.419 145.941 99.235  1.00 42.15  ? 1178 VAL   A CA    1 
ATOM   6178  C  C     . VAL   A 1 1178 ? 176.925 145.761 99.014  1.00 45.76  ? 1178 VAL   A C     1 
ATOM   6179  O  O     . VAL   A 1 1178 ? 176.114 146.536 99.532  1.00 45.86  ? 1178 VAL   A O     1 
ATOM   6180  C  CB    . VAL   A 1 1178 ? 178.845 145.321 100.581 1.00 42.17  ? 1178 VAL   A CB    1 
ATOM   6181  C  CG1   . VAL   A 1 1178 ? 179.141 143.845 100.413 1.00 39.72  ? 1178 VAL   A CG1   1 
ATOM   6182  C  CG2   . VAL   A 1 1178 ? 180.055 146.048 101.138 1.00 47.40  ? 1178 VAL   A CG2   1 
ATOM   6183  N  N     . SER   A 1 1179 ? 176.566 144.740 98.242  1.00 45.39  ? 1179 SER   A N     1 
ATOM   6184  C  CA    . SER   A 1 1179 ? 175.165 144.428 98.021  1.00 39.45  ? 1179 SER   A CA    1 
ATOM   6185  C  C     . SER   A 1 1179 ? 174.546 143.827 99.280  1.00 44.40  ? 1179 SER   A C     1 
ATOM   6186  O  O     . SER   A 1 1179 ? 175.236 143.296 100.155 1.00 52.22  ? 1179 SER   A O     1 
ATOM   6187  C  CB    . SER   A 1 1179 ? 175.008 143.462 96.846  1.00 48.43  ? 1179 SER   A CB    1 
ATOM   6188  O  OG    . SER   A 1 1179 ? 176.087 142.546 96.791  1.00 50.97  ? 1179 SER   A OG    1 
ATOM   6189  N  N     . SER   A 1 1180 ? 173.217 143.917 99.363  1.00 37.05  ? 1180 SER   A N     1 
ATOM   6190  C  CA    . SER   A 1 1180 ? 172.512 143.358 100.511 1.00 34.78  ? 1180 SER   A CA    1 
ATOM   6191  C  C     . SER   A 1 1180 ? 172.707 141.850 100.598 1.00 38.07  ? 1180 SER   A C     1 
ATOM   6192  O  O     . SER   A 1 1180 ? 172.877 141.298 101.693 1.00 45.20  ? 1180 SER   A O     1 
ATOM   6193  C  CB    . SER   A 1 1180 ? 171.024 143.702 100.434 1.00 37.63  ? 1180 SER   A CB    1 
ATOM   6194  O  OG    . SER   A 1 1180 ? 170.830 145.082 100.183 1.00 43.37  ? 1180 SER   A OG    1 
ATOM   6195  N  N     . ALA   A 1 1181 ? 172.684 141.164 99.454  1.00 32.16  ? 1181 ALA   A N     1 
ATOM   6196  C  CA    . ALA   A 1 1181 ? 172.860 139.716 99.461  1.00 37.75  ? 1181 ALA   A CA    1 
ATOM   6197  C  C     . ALA   A 1 1181 ? 174.226 139.330 100.012 1.00 44.82  ? 1181 ALA   A C     1 
ATOM   6198  O  O     . ALA   A 1 1181 ? 174.342 138.381 100.795 1.00 52.22  ? 1181 ALA   A O     1 
ATOM   6199  C  CB    . ALA   A 1 1181 ? 172.669 139.157 98.052  1.00 36.06  ? 1181 ALA   A CB    1 
ATOM   6200  N  N     . LEU   A 1 1182 ? 175.275 140.055 99.617  1.00 38.47  ? 1182 LEU   A N     1 
ATOM   6201  C  CA    . LEU   A 1 1182 ? 176.611 139.739 100.109 1.00 33.40  ? 1182 LEU   A CA    1 
ATOM   6202  C  C     . LEU   A 1 1182 ? 176.726 139.999 101.606 1.00 38.76  ? 1182 LEU   A C     1 
ATOM   6203  O  O     . LEU   A 1 1182 ? 177.376 139.234 102.325 1.00 47.22  ? 1182 LEU   A O     1 
ATOM   6204  C  CB    . LEU   A 1 1182 ? 177.662 140.538 99.340  1.00 43.69  ? 1182 LEU   A CB    1 
ATOM   6205  C  CG    . LEU   A 1 1182 ? 179.111 140.300 99.768  1.00 42.48  ? 1182 LEU   A CG    1 
ATOM   6206  C  CD1   . LEU   A 1 1182 ? 179.483 138.838 99.592  1.00 37.13  ? 1182 LEU   A CD1   1 
ATOM   6207  C  CD2   . LEU   A 1 1182 ? 180.055 141.186 98.977  1.00 39.59  ? 1182 LEU   A CD2   1 
ATOM   6208  N  N     . TYR   A 1 1183 ? 176.119 141.083 102.093 1.00 37.58  ? 1183 TYR   A N     1 
ATOM   6209  C  CA    . TYR   A 1 1183 ? 176.129 141.360 103.527 1.00 28.97  ? 1183 TYR   A CA    1 
ATOM   6210  C  C     . TYR   A 1 1183 ? 175.417 140.254 104.301 1.00 24.83  ? 1183 TYR   A C     1 
ATOM   6211  O  O     . TYR   A 1 1183 ? 175.914 139.779 105.334 1.00 40.13  ? 1183 TYR   A O     1 
ATOM   6212  C  CB    . TYR   A 1 1183 ? 175.476 142.719 103.783 1.00 27.33  ? 1183 TYR   A CB    1 
ATOM   6213  C  CG    . TYR   A 1 1183 ? 175.796 143.354 105.118 1.00 27.18  ? 1183 TYR   A CG    1 
ATOM   6214  C  CD1   . TYR   A 1 1183 ? 176.556 142.688 106.068 1.00 32.89  ? 1183 TYR   A CD1   1 
ATOM   6215  C  CD2   . TYR   A 1 1183 ? 175.350 144.634 105.416 1.00 25.95  ? 1183 TYR   A CD2   1 
ATOM   6216  C  CE1   . TYR   A 1 1183 ? 176.851 143.275 107.284 1.00 31.72  ? 1183 TYR   A CE1   1 
ATOM   6217  C  CE2   . TYR   A 1 1183 ? 175.640 145.229 106.626 1.00 28.54  ? 1183 TYR   A CE2   1 
ATOM   6218  C  CZ    . TYR   A 1 1183 ? 176.390 144.546 107.557 1.00 35.89  ? 1183 TYR   A CZ    1 
ATOM   6219  O  OH    . TYR   A 1 1183 ? 176.680 145.138 108.763 1.00 44.60  ? 1183 TYR   A OH    1 
ATOM   6220  N  N     . MET   A 1 1184 ? 174.251 139.828 103.809 1.00 27.92  ? 1184 MET   A N     1 
ATOM   6221  C  CA    . MET   A 1 1184 ? 173.528 138.738 104.454 1.00 33.51  ? 1184 MET   A CA    1 
ATOM   6222  C  C     . MET   A 1 1184 ? 174.344 137.453 104.441 1.00 37.13  ? 1184 MET   A C     1 
ATOM   6223  O  O     . MET   A 1 1184 ? 174.344 136.700 105.421 1.00 34.51  ? 1184 MET   A O     1 
ATOM   6224  C  CB    . MET   A 1 1184 ? 172.178 138.528 103.768 1.00 33.90  ? 1184 MET   A CB    1 
ATOM   6225  C  CG    . MET   A 1 1184 ? 171.317 137.445 104.396 1.00 40.14  ? 1184 MET   A CG    1 
ATOM   6226  S  SD    . MET   A 1 1184 ? 171.029 137.663 106.162 1.00 59.05  ? 1184 MET   A SD    1 
ATOM   6227  C  CE    . MET   A 1 1184 ? 170.827 139.437 106.255 1.00 42.38  ? 1184 MET   A CE    1 
ATOM   6228  N  N     . ALA   A 1 1185 ? 175.037 137.178 103.334 1.00 38.20  ? 1185 ALA   A N     1 
ATOM   6229  C  CA    . ALA   A 1 1185 ? 175.877 135.986 103.268 1.00 33.69  ? 1185 ALA   A CA    1 
ATOM   6230  C  C     . ALA   A 1 1185 ? 177.041 136.078 104.245 1.00 34.30  ? 1185 ALA   A C     1 
ATOM   6231  O  O     . ALA   A 1 1185 ? 177.420 135.078 104.862 1.00 38.23  ? 1185 ALA   A O     1 
ATOM   6232  C  CB    . ALA   A 1 1185 ? 176.386 135.777 101.843 1.00 33.75  ? 1185 ALA   A CB    1 
ATOM   6233  N  N     . TRP   A 1 1186 ? 177.627 137.267 104.391 1.00 27.95  ? 1186 TRP   A N     1 
ATOM   6234  C  CA    . TRP   A 1 1186 ? 178.660 137.466 105.402 1.00 24.30  ? 1186 TRP   A CA    1 
ATOM   6235  C  C     . TRP   A 1 1186 ? 178.135 137.103 106.782 1.00 30.21  ? 1186 TRP   A C     1 
ATOM   6236  O  O     . TRP   A 1 1186 ? 178.768 136.343 107.526 1.00 33.18  ? 1186 TRP   A O     1 
ATOM   6237  C  CB    . TRP   A 1 1186 ? 179.135 138.919 105.390 1.00 24.65  ? 1186 TRP   A CB    1 
ATOM   6238  C  CG    . TRP   A 1 1186 ? 180.115 139.255 104.316 1.00 30.25  ? 1186 TRP   A CG    1 
ATOM   6239  C  CD1   . TRP   A 1 1186 ? 180.752 138.388 103.479 1.00 29.06  ? 1186 TRP   A CD1   1 
ATOM   6240  C  CD2   . TRP   A 1 1186 ? 180.576 140.563 103.966 1.00 27.86  ? 1186 TRP   A CD2   1 
ATOM   6241  N  NE1   . TRP   A 1 1186 ? 181.579 139.077 102.626 1.00 28.00  ? 1186 TRP   A NE1   1 
ATOM   6242  C  CE2   . TRP   A 1 1186 ? 181.490 140.415 102.906 1.00 25.69  ? 1186 TRP   A CE2   1 
ATOM   6243  C  CE3   . TRP   A 1 1186 ? 180.304 141.847 104.447 1.00 28.58  ? 1186 TRP   A CE3   1 
ATOM   6244  C  CZ2   . TRP   A 1 1186 ? 182.132 141.500 102.318 1.00 31.17  ? 1186 TRP   A CZ2   1 
ATOM   6245  C  CZ3   . TRP   A 1 1186 ? 180.942 142.923 103.863 1.00 31.49  ? 1186 TRP   A CZ3   1 
ATOM   6246  C  CH2   . TRP   A 1 1186 ? 181.846 142.744 102.810 1.00 37.76  ? 1186 TRP   A CH2   1 
ATOM   6247  N  N     . LEU   A 1 1187 ? 176.969 137.646 107.140 1.00 30.21  ? 1187 LEU   A N     1 
ATOM   6248  C  CA    . LEU   A 1 1187 ? 176.401 137.363 108.456 1.00 23.75  ? 1187 LEU   A CA    1 
ATOM   6249  C  C     . LEU   A 1 1187 ? 176.118 135.876 108.628 1.00 28.29  ? 1187 LEU   A C     1 
ATOM   6250  O  O     . LEU   A 1 1187 ? 176.415 135.293 109.680 1.00 33.85  ? 1187 LEU   A O     1 
ATOM   6251  C  CB    . LEU   A 1 1187 ? 175.127 138.180 108.662 1.00 24.54  ? 1187 LEU   A CB    1 
ATOM   6252  C  CG    . LEU   A 1 1187 ? 175.311 139.695 108.755 1.00 24.89  ? 1187 LEU   A CG    1 
ATOM   6253  C  CD1   . LEU   A 1 1187 ? 174.150 140.332 109.495 1.00 29.95  ? 1187 LEU   A CD1   1 
ATOM   6254  C  CD2   . LEU   A 1 1187 ? 176.627 140.031 109.433 1.00 30.74  ? 1187 LEU   A CD2   1 
ATOM   6255  N  N     . GLU   A 1 1188 ? 175.548 135.242 107.601 1.00 26.93  ? 1188 GLU   A N     1 
ATOM   6256  C  CA    . GLU   A 1 1188 ? 175.208 133.827 107.699 1.00 36.29  ? 1188 GLU   A CA    1 
ATOM   6257  C  C     . GLU   A 1 1188 ? 176.455 132.971 107.863 1.00 35.24  ? 1188 GLU   A C     1 
ATOM   6258  O  O     . GLU   A 1 1188 ? 176.481 132.050 108.687 1.00 37.63  ? 1188 GLU   A O     1 
ATOM   6259  C  CB    . GLU   A 1 1188 ? 174.420 133.391 106.466 1.00 28.40  ? 1188 GLU   A CB    1 
ATOM   6260  C  CG    . GLU   A 1 1188 ? 173.308 132.404 106.767 1.00 36.26  ? 1188 GLU   A CG    1 
ATOM   6261  C  CD    . GLU   A 1 1188 ? 173.822 130.995 106.979 1.00 45.78  ? 1188 GLU   A CD    1 
ATOM   6262  O  OE1   . GLU   A 1 1188 ? 174.689 130.552 106.197 1.00 50.10  ? 1188 GLU   A OE1   1 
ATOM   6263  O  OE2   . GLU   A 1 1188 ? 173.360 130.328 107.927 1.00 40.51  ? 1188 GLU   A OE2   1 
ATOM   6264  N  N     . ALA   A 1 1189 ? 177.501 133.258 107.087 1.00 30.37  ? 1189 ALA   A N     1 
ATOM   6265  C  CA    . ALA   A 1 1189 ? 178.748 132.518 107.227 1.00 28.98  ? 1189 ALA   A CA    1 
ATOM   6266  C  C     . ALA   A 1 1189 ? 179.347 132.720 108.610 1.00 34.06  ? 1189 ALA   A C     1 
ATOM   6267  O  O     . ALA   A 1 1189 ? 179.865 131.774 109.214 1.00 41.37  ? 1189 ALA   A O     1 
ATOM   6268  C  CB    . ALA   A 1 1189 ? 179.739 132.946 106.145 1.00 26.62  ? 1189 ALA   A CB    1 
ATOM   6269  N  N     . LEU   A 1 1190 ? 179.292 133.949 109.126 1.00 26.63  ? 1190 LEU   A N     1 
ATOM   6270  C  CA    . LEU   A 1 1190 ? 179.858 134.222 110.442 1.00 20.96  ? 1190 LEU   A CA    1 
ATOM   6271  C  C     . LEU   A 1 1190 ? 179.137 133.439 111.532 1.00 36.38  ? 1190 LEU   A C     1 
ATOM   6272  O  O     . LEU   A 1 1190 ? 179.774 132.819 112.392 1.00 35.85  ? 1190 LEU   A O     1 
ATOM   6273  C  CB    . LEU   A 1 1190 ? 179.802 135.722 110.732 1.00 25.49  ? 1190 LEU   A CB    1 
ATOM   6274  C  CG    . LEU   A 1 1190 ? 180.509 136.191 112.005 1.00 36.06  ? 1190 LEU   A CG    1 
ATOM   6275  C  CD1   . LEU   A 1 1190 ? 181.972 135.784 111.987 1.00 30.50  ? 1190 LEU   A CD1   1 
ATOM   6276  C  CD2   . LEU   A 1 1190 ? 180.374 137.695 112.167 1.00 32.07  ? 1190 LEU   A CD2   1 
ATOM   6277  N  N     . SER   A 1 1191 ? 177.805 133.450 111.512 1.00 33.12  ? 1191 SER   A N     1 
ATOM   6278  C  CA    . SER   A 1 1191 ? 177.015 132.958 112.633 1.00 27.14  ? 1191 SER   A CA    1 
ATOM   6279  C  C     . SER   A 1 1191 ? 176.506 131.530 112.461 1.00 32.04  ? 1191 SER   A C     1 
ATOM   6280  O  O     . SER   A 1 1191 ? 175.807 131.033 113.348 1.00 27.22  ? 1191 SER   A O     1 
ATOM   6281  C  CB    . SER   A 1 1191 ? 175.828 133.892 112.878 1.00 37.97  ? 1191 SER   A CB    1 
ATOM   6282  O  OG    . SER   A 1 1191 ? 176.247 135.244 112.915 1.00 41.35  ? 1191 SER   A OG    1 
ATOM   6283  N  N     . LYS   A 1 1192 ? 176.833 130.858 111.363 1.00 33.81  ? 1192 LYS   A N     1 
ATOM   6284  C  CA    . LYS   A 1 1192 ? 176.228 129.561 111.085 1.00 37.63  ? 1192 LYS   A CA    1 
ATOM   6285  C  C     . LYS   A 1 1192 ? 176.696 128.494 112.071 1.00 40.53  ? 1192 LYS   A C     1 
ATOM   6286  O  O     . LYS   A 1 1192 ? 177.885 128.390 112.385 1.00 49.33  ? 1192 LYS   A O     1 
ATOM   6287  C  CB    . LYS   A 1 1192 ? 176.552 129.117 109.660 1.00 32.00  ? 1192 LYS   A CB    1 
ATOM   6288  C  CG    . LYS   A 1 1192 ? 177.919 129.549 109.165 1.00 37.66  ? 1192 LYS   A CG    1 
ATOM   6289  C  CD    . LYS   A 1 1192 ? 178.475 128.545 108.169 1.00 43.89  ? 1192 LYS   A CD    1 
ATOM   6290  C  CE    . LYS   A 1 1192 ? 178.669 127.181 108.817 1.00 46.22  ? 1192 LYS   A CE    1 
ATOM   6291  N  NZ    . LYS   A 1 1192 ? 179.540 126.287 108.004 1.00 45.72  ? 1192 LYS   A NZ    1 
ATOM   6292  N  N     . ASP   A 1 1193 ? 175.744 127.692 112.554 1.00 52.65  ? 1193 ASP   A N     1 
ATOM   6293  C  CA    . ASP   A 1 1193 ? 176.021 126.474 113.319 1.00 49.26  ? 1193 ASP   A CA    1 
ATOM   6294  C  C     . ASP   A 1 1193 ? 176.877 126.830 114.538 1.00 45.00  ? 1193 ASP   A C     1 
ATOM   6295  O  O     . ASP   A 1 1193 ? 178.075 126.554 114.601 1.00 58.61  ? 1193 ASP   A O     1 
ATOM   6296  C  CB    . ASP   A 1 1193 ? 176.675 125.409 112.414 1.00 51.00  ? 1193 ASP   A CB    1 
ATOM   6297  C  CG    . ASP   A 1 1193 ? 177.352 124.247 113.176 1.00 60.35  ? 1193 ASP   A CG    1 
ATOM   6298  O  OD1   . ASP   A 1 1193 ? 177.585 123.213 112.512 1.00 62.30  ? 1193 ASP   A OD1   1 
ATOM   6299  O  OD2   . ASP   A 1 1193 ? 177.586 124.293 114.403 1.00 60.43  ? 1193 ASP   A OD2   1 
ATOM   6300  N  N     . LEU   A 1 1194 ? 176.265 127.556 115.462 1.00 36.79  ? 1194 LEU   A N     1 
ATOM   6301  C  CA    . LEU   A 1 1194 ? 176.935 127.996 116.675 1.00 36.92  ? 1194 LEU   A CA    1 
ATOM   6302  C  C     . LEU   A 1 1194 ? 175.923 128.082 117.805 1.00 42.83  ? 1194 LEU   A C     1 
ATOM   6303  O  O     . LEU   A 1 1194 ? 174.714 128.155 117.560 1.00 47.89  ? 1194 LEU   A O     1 
ATOM   6304  C  CB    . LEU   A 1 1194 ? 177.610 129.361 116.479 1.00 37.91  ? 1194 LEU   A CB    1 
ATOM   6305  C  CG    . LEU   A 1 1194 ? 179.023 129.377 115.901 1.00 40.69  ? 1194 LEU   A CG    1 
ATOM   6306  C  CD1   . LEU   A 1 1194 ? 179.429 130.801 115.578 1.00 36.22  ? 1194 LEU   A CD1   1 
ATOM   6307  C  CD2   . LEU   A 1 1194 ? 179.996 128.749 116.877 1.00 39.10  ? 1194 LEU   A CD2   1 
ATOM   6308  N  N     . PRO   A 1 1195 ? 176.383 128.058 119.052 1.00 43.43  ? 1195 PRO   A N     1 
ATOM   6309  C  CA    . PRO   A 1 1195 ? 175.490 128.339 120.180 1.00 35.74  ? 1195 PRO   A CA    1 
ATOM   6310  C  C     . PRO   A 1 1195 ? 174.836 129.698 120.016 1.00 39.71  ? 1195 PRO   A C     1 
ATOM   6311  O  O     . PRO   A 1 1195 ? 175.183 130.452 119.094 1.00 43.68  ? 1195 PRO   A O     1 
ATOM   6312  C  CB    . PRO   A 1 1195 ? 176.432 128.324 121.392 1.00 34.42  ? 1195 PRO   A CB    1 
ATOM   6313  C  CG    . PRO   A 1 1195 ? 177.593 127.493 120.982 1.00 38.38  ? 1195 PRO   A CG    1 
ATOM   6314  C  CD    . PRO   A 1 1195 ? 177.643 127.425 119.479 1.00 37.26  ? 1195 PRO   A CD    1 
ATOM   6315  N  N     . PRO   A 1 1196 ? 173.870 130.043 120.878 1.00 45.36  ? 1196 PRO   A N     1 
ATOM   6316  C  CA    . PRO   A 1 1196 ? 173.270 131.382 120.812 1.00 39.54  ? 1196 PRO   A CA    1 
ATOM   6317  C  C     . PRO   A 1 1196 ? 174.327 132.454 120.622 1.00 27.84  ? 1196 PRO   A C     1 
ATOM   6318  O  O     . PRO   A 1 1196 ? 175.312 132.492 121.364 1.00 28.32  ? 1196 PRO   A O     1 
ATOM   6319  C  CB    . PRO   A 1 1196 ? 172.571 131.523 122.169 1.00 27.81  ? 1196 PRO   A CB    1 
ATOM   6320  C  CG    . PRO   A 1 1196 ? 172.350 130.129 122.653 1.00 29.94  ? 1196 PRO   A CG    1 
ATOM   6321  C  CD    . PRO   A 1 1196 ? 173.175 129.170 121.835 1.00 40.35  ? 1196 PRO   A CD    1 
ATOM   6322  N  N     . ILE   A 1 1197 ? 174.145 133.326 119.635 1.00 30.58  ? 1197 ILE   A N     1 
ATOM   6323  C  CA    . ILE   A 1 1197 ? 175.166 134.297 119.268 1.00 26.36  ? 1197 ILE   A CA    1 
ATOM   6324  C  C     . ILE   A 1 1197 ? 174.541 135.679 119.158 1.00 29.02  ? 1197 ILE   A C     1 
ATOM   6325  O  O     . ILE   A 1 1197 ? 173.405 135.830 118.694 1.00 32.83  ? 1197 ILE   A O     1 
ATOM   6326  C  CB    . ILE   A 1 1197 ? 175.873 133.913 117.951 1.00 23.04  ? 1197 ILE   A CB    1 
ATOM   6327  C  CG1   . ILE   A 1 1197 ? 176.947 134.946 117.603 1.00 27.44  ? 1197 ILE   A CG1   1 
ATOM   6328  C  CG2   . ILE   A 1 1197 ? 174.868 133.777 116.827 1.00 28.25  ? 1197 ILE   A CG2   1 
ATOM   6329  C  CD1   . ILE   A 1 1197 ? 178.226 134.348 117.060 1.00 27.41  ? 1197 ILE   A CD1   1 
ATOM   6330  N  N     . LEU   A 1 1198 ? 175.290 136.686 119.598 1.00 26.84  ? 1198 LEU   A N     1 
ATOM   6331  C  CA    . LEU   A 1 1198 ? 174.901 138.087 119.497 1.00 22.58  ? 1198 LEU   A CA    1 
ATOM   6332  C  C     . LEU   A 1 1198 ? 175.994 138.828 118.739 1.00 27.20  ? 1198 LEU   A C     1 
ATOM   6333  O  O     . LEU   A 1 1198 ? 177.116 138.971 119.239 1.00 23.96  ? 1198 LEU   A O     1 
ATOM   6334  C  CB    . LEU   A 1 1198 ? 174.686 138.698 120.882 1.00 19.59  ? 1198 LEU   A CB    1 
ATOM   6335  C  CG    . LEU   A 1 1198 ? 173.310 138.532 121.528 1.00 27.72  ? 1198 LEU   A CG    1 
ATOM   6336  C  CD1   . LEU   A 1 1198 ? 173.043 137.077 121.867 1.00 33.47  ? 1198 LEU   A CD1   1 
ATOM   6337  C  CD2   . LEU   A 1 1198 ? 173.202 139.394 122.773 1.00 24.22  ? 1198 LEU   A CD2   1 
ATOM   6338  N  N     . LEU   A 1 1199 ? 175.670 139.293 117.537 1.00 28.54  ? 1199 LEU   A N     1 
ATOM   6339  C  CA    . LEU   A 1 1199 ? 176.561 140.155 116.770 1.00 20.65  ? 1199 LEU   A CA    1 
ATOM   6340  C  C     . LEU   A 1 1199 ? 176.238 141.595 117.143 1.00 21.13  ? 1199 LEU   A C     1 
ATOM   6341  O  O     . LEU   A 1 1199 ? 175.142 142.088 116.860 1.00 34.68  ? 1199 LEU   A O     1 
ATOM   6342  C  CB    . LEU   A 1 1199 ? 176.401 139.912 115.272 1.00 6.98   ? 1199 LEU   A CB    1 
ATOM   6343  C  CG    . LEU   A 1 1199 ? 176.242 138.447 114.861 1.00 16.78  ? 1199 LEU   A CG    1 
ATOM   6344  C  CD1   . LEU   A 1 1199 ? 176.003 138.320 113.367 1.00 23.48  ? 1199 LEU   A CD1   1 
ATOM   6345  C  CD2   . LEU   A 1 1199 ? 177.462 137.646 115.278 1.00 22.89  ? 1199 LEU   A CD2   1 
ATOM   6346  N  N     . VAL   A 1 1200 ? 177.188 142.261 117.791 1.00 22.12  ? 1200 VAL   A N     1 
ATOM   6347  C  CA    . VAL   A 1 1200 ? 176.982 143.587 118.358 1.00 20.43  ? 1200 VAL   A CA    1 
ATOM   6348  C  C     . VAL   A 1 1200 ? 177.907 144.570 117.661 1.00 21.78  ? 1200 VAL   A C     1 
ATOM   6349  O  O     . VAL   A 1 1200 ? 179.114 144.327 117.551 1.00 28.91  ? 1200 VAL   A O     1 
ATOM   6350  C  CB    . VAL   A 1 1200 ? 177.226 143.597 119.878 1.00 18.94  ? 1200 VAL   A CB    1 
ATOM   6351  C  CG1   . VAL   A 1 1200 ? 176.779 144.919 120.474 1.00 20.08  ? 1200 VAL   A CG1   1 
ATOM   6352  C  CG2   . VAL   A 1 1200 ? 176.500 142.438 120.538 1.00 20.81  ? 1200 VAL   A CG2   1 
ATOM   6353  N  N     . ARG   A 1 1201 ? 177.338 145.677 117.189 1.00 17.69  ? 1201 ARG   A N     1 
ATOM   6354  C  CA    . ARG   A 1 1201 ? 178.098 146.815 116.687 1.00 15.54  ? 1201 ARG   A CA    1 
ATOM   6355  C  C     . ARG   A 1 1201 ? 177.560 148.054 117.384 1.00 18.26  ? 1201 ARG   A C     1 
ATOM   6356  O  O     . ARG   A 1 1201 ? 176.445 148.495 117.092 1.00 36.24  ? 1201 ARG   A O     1 
ATOM   6357  C  CB    . ARG   A 1 1201 ? 177.982 146.945 115.169 1.00 29.05  ? 1201 ARG   A CB    1 
ATOM   6358  C  CG    . ARG   A 1 1201 ? 178.354 148.319 114.637 1.00 31.88  ? 1201 ARG   A CG    1 
ATOM   6359  C  CD    . ARG   A 1 1201 ? 179.853 148.539 114.673 1.00 22.67  ? 1201 ARG   A CD    1 
ATOM   6360  N  NE    . ARG   A 1 1201 ? 180.587 147.312 114.395 1.00 35.18  ? 1201 ARG   A NE    1 
ATOM   6361  C  CZ    . ARG   A 1 1201 ? 181.739 147.258 113.740 1.00 39.70  ? 1201 ARG   A CZ    1 
ATOM   6362  N  NH1   . ARG   A 1 1201 ? 182.319 148.350 113.271 1.00 35.03  ? 1201 ARG   A NH1   1 
ATOM   6363  N  NH2   . ARG   A 1 1201 ? 182.323 146.079 113.553 1.00 37.92  ? 1201 ARG   A NH2   1 
ATOM   6364  N  N     . GLY   A 1 1202 ? 178.343 148.610 118.303 1.00 21.82  ? 1202 GLY   A N     1 
ATOM   6365  C  CA    . GLY   A 1 1202 ? 177.898 149.733 119.093 1.00 4.48   ? 1202 GLY   A CA    1 
ATOM   6366  C  C     . GLY   A 1 1202 ? 177.955 151.046 118.340 1.00 21.77  ? 1202 GLY   A C     1 
ATOM   6367  O  O     . GLY   A 1 1202 ? 178.386 151.134 117.191 1.00 33.77  ? 1202 GLY   A O     1 
ATOM   6368  N  N     . ASN   A 1 1203 ? 177.506 152.096 119.027 1.00 26.55  ? 1203 ASN   A N     1 
ATOM   6369  C  CA    . ASN   A 1 1203 ? 177.458 153.429 118.439 1.00 21.23  ? 1203 ASN   A CA    1 
ATOM   6370  C  C     . ASN   A 1 1203 ? 178.836 153.953 118.058 1.00 29.61  ? 1203 ASN   A C     1 
ATOM   6371  O  O     . ASN   A 1 1203 ? 178.931 154.865 117.231 1.00 32.15  ? 1203 ASN   A O     1 
ATOM   6372  C  CB    . ASN   A 1 1203 ? 176.789 154.395 119.417 1.00 29.12  ? 1203 ASN   A CB    1 
ATOM   6373  C  CG    . ASN   A 1 1203 ? 176.002 155.478 118.718 1.00 38.39  ? 1203 ASN   A CG    1 
ATOM   6374  O  OD1   . ASN   A 1 1203 ? 175.417 155.250 117.661 1.00 47.15  ? 1203 ASN   A OD1   1 
ATOM   6375  N  ND2   . ASN   A 1 1203 ? 175.975 156.666 119.311 1.00 38.89  ? 1203 ASN   A ND2   1 
ATOM   6376  N  N     . HIS   A 1 1204 ? 179.898 153.403 118.640 1.00 39.29  ? 1204 HIS   A N     1 
ATOM   6377  C  CA    . HIS   A 1 1204 ? 181.270 153.898 118.576 1.00 31.57  ? 1204 HIS   A CA    1 
ATOM   6378  C  C     . HIS   A 1 1204 ? 181.446 155.084 119.514 1.00 35.24  ? 1204 HIS   A C     1 
ATOM   6379  O  O     . HIS   A 1 1204 ? 182.533 155.674 119.549 1.00 41.77  ? 1204 HIS   A O     1 
ATOM   6380  C  CB    . HIS   A 1 1204 ? 181.718 154.295 117.161 1.00 29.14  ? 1204 HIS   A CB    1 
ATOM   6381  C  CG    . HIS   A 1 1204 ? 182.206 153.144 116.340 1.00 34.38  ? 1204 HIS   A CG    1 
ATOM   6382  N  ND1   . HIS   A 1 1204 ? 183.296 153.235 115.502 1.00 38.38  ? 1204 HIS   A ND1   1 
ATOM   6383  C  CD2   . HIS   A 1 1204 ? 181.752 151.873 116.229 1.00 36.88  ? 1204 HIS   A CD2   1 
ATOM   6384  C  CE1   . HIS   A 1 1204 ? 183.493 152.070 114.911 1.00 38.32  ? 1204 HIS   A CE1   1 
ATOM   6385  N  NE2   . HIS   A 1 1204 ? 182.570 151.227 115.335 1.00 38.46  ? 1204 HIS   A NE2   1 
ATOM   6386  N  N     . GLN   A 1 1205 ? 180.416 155.458 120.266 1.00 37.33  ? 1205 GLN   A N     1 
ATOM   6387  C  CA    . GLN   A 1 1205 ? 180.553 156.404 121.361 1.00 36.93  ? 1205 GLN   A CA    1 
ATOM   6388  C  C     . GLN   A 1 1205 ? 180.923 155.640 122.623 1.00 36.84  ? 1205 GLN   A C     1 
ATOM   6389  O  O     . GLN   A 1 1205 ? 180.425 154.536 122.860 1.00 40.33  ? 1205 GLN   A O     1 
ATOM   6390  C  CB    . GLN   A 1 1205 ? 179.254 157.181 121.575 1.00 36.43  ? 1205 GLN   A CB    1 
ATOM   6391  C  CG    . GLN   A 1 1205 ? 179.332 158.641 121.173 1.00 39.65  ? 1205 GLN   A CG    1 
ATOM   6392  C  CD    . GLN   A 1 1205 ? 179.982 158.836 119.819 1.00 45.89  ? 1205 GLN   A CD    1 
ATOM   6393  O  OE1   . GLN   A 1 1205 ? 179.371 158.579 118.782 1.00 47.60  ? 1205 GLN   A OE1   1 
ATOM   6394  N  NE2   . GLN   A 1 1205 ? 181.227 159.296 119.821 1.00 43.78  ? 1205 GLN   A NE2   1 
ATOM   6395  N  N     . SER   A 1 1206 ? 181.806 156.226 123.425 1.00 36.37  ? 1206 SER   A N     1 
ATOM   6396  C  CA    . SER   A 1 1206 ? 182.308 155.530 124.602 1.00 29.23  ? 1206 SER   A CA    1 
ATOM   6397  C  C     . SER   A 1 1206 ? 181.155 155.130 125.513 1.00 31.98  ? 1206 SER   A C     1 
ATOM   6398  O  O     . SER   A 1 1206 ? 180.352 155.973 125.923 1.00 38.63  ? 1206 SER   A O     1 
ATOM   6399  C  CB    . SER   A 1 1206 ? 183.304 156.413 125.350 1.00 36.87  ? 1206 SER   A CB    1 
ATOM   6400  O  OG    . SER   A 1 1206 ? 184.632 155.977 125.119 1.00 43.83  ? 1206 SER   A OG    1 
ATOM   6401  N  N     . VAL   A 1 1207 ? 181.077 153.839 125.821 1.00 28.39  ? 1207 VAL   A N     1 
ATOM   6402  C  CA    . VAL   A 1 1207 ? 180.035 153.315 126.691 1.00 24.69  ? 1207 VAL   A CA    1 
ATOM   6403  C  C     . VAL   A 1 1207 ? 180.581 152.845 128.032 1.00 31.22  ? 1207 VAL   A C     1 
ATOM   6404  O  O     . VAL   A 1 1207 ? 179.800 152.709 128.986 1.00 32.90  ? 1207 VAL   A O     1 
ATOM   6405  C  CB    . VAL   A 1 1207 ? 179.257 152.176 125.998 1.00 10.56  ? 1207 VAL   A CB    1 
ATOM   6406  C  CG1   . VAL   A 1 1207 ? 179.207 150.940 126.879 1.00 25.91  ? 1207 VAL   A CG1   1 
ATOM   6407  C  CG2   . VAL   A 1 1207 ? 177.860 152.638 125.631 1.00 13.08  ? 1207 VAL   A CG2   1 
ATOM   6408  N  N     . LEU   A 1 1208 ? 181.883 152.610 128.142 1.00 24.91  ? 1208 LEU   A N     1 
ATOM   6409  C  CA    . LEU   A 1 1208 ? 182.540 152.283 129.395 1.00 10.22  ? 1208 LEU   A CA    1 
ATOM   6410  C  C     . LEU   A 1 1208 ? 183.520 153.389 129.760 1.00 19.75  ? 1208 LEU   A C     1 
ATOM   6411  O  O     . LEU   A 1 1208 ? 183.902 154.217 128.929 1.00 36.50  ? 1208 LEU   A O     1 
ATOM   6412  C  CB    . LEU   A 1 1208 ? 183.267 150.937 129.297 1.00 13.75  ? 1208 LEU   A CB    1 
ATOM   6413  C  CG    . LEU   A 1 1208 ? 182.469 149.767 128.720 1.00 20.07  ? 1208 LEU   A CG    1 
ATOM   6414  C  CD1   . LEU   A 1 1208 ? 183.401 148.716 128.141 1.00 10.57  ? 1208 LEU   A CD1   1 
ATOM   6415  C  CD2   . LEU   A 1 1208 ? 181.572 149.161 129.785 1.00 19.26  ? 1208 LEU   A CD2   1 
ATOM   6416  N  N     . THR   A 1 1209 ? 183.920 153.400 131.027 1.00 28.04  ? 1209 THR   A N     1 
ATOM   6417  C  CA    . THR   A 1 1209 ? 184.908 154.358 131.499 1.00 29.70  ? 1209 THR   A CA    1 
ATOM   6418  C  C     . THR   A 1 1209 ? 185.589 153.787 132.732 1.00 27.09  ? 1209 THR   A C     1 
ATOM   6419  O  O     . THR   A 1 1209 ? 185.012 152.970 133.453 1.00 37.03  ? 1209 THR   A O     1 
ATOM   6420  C  CB    . THR   A 1 1209 ? 184.275 155.717 131.818 1.00 25.38  ? 1209 THR   A CB    1 
ATOM   6421  O  OG1   . THR   A 1 1209 ? 185.303 156.700 131.991 1.00 32.87  ? 1209 THR   A OG1   1 
ATOM   6422  C  CG2   . THR   A 1 1209 ? 183.450 155.636 133.086 1.00 24.93  ? 1209 THR   A CG2   1 
ATOM   6423  N  N     . PHE   A 1 1210 ? 186.828 154.218 132.958 1.00 27.55  ? 1210 PHE   A N     1 
ATOM   6424  C  CA    . PHE   A 1 1210 ? 187.554 153.882 134.175 1.00 31.12  ? 1210 PHE   A CA    1 
ATOM   6425  C  C     . PHE   A 1 1210 ? 187.885 155.119 135.000 1.00 28.66  ? 1210 PHE   A C     1 
ATOM   6426  O  O     . PHE   A 1 1210 ? 188.895 155.140 135.709 1.00 40.37  ? 1210 PHE   A O     1 
ATOM   6427  C  CB    . PHE   A 1 1210 ? 188.822 153.090 133.850 1.00 32.99  ? 1210 PHE   A CB    1 
ATOM   6428  C  CG    . PHE   A 1 1210 ? 189.548 153.567 132.627 1.00 29.84  ? 1210 PHE   A CG    1 
ATOM   6429  C  CD1   . PHE   A 1 1210 ? 190.124 154.823 132.588 1.00 27.21  ? 1210 PHE   A CD1   1 
ATOM   6430  C  CD2   . PHE   A 1 1210 ? 189.668 152.746 131.519 1.00 33.46  ? 1210 PHE   A CD2   1 
ATOM   6431  C  CE1   . PHE   A 1 1210 ? 190.798 155.253 131.463 1.00 33.10  ? 1210 PHE   A CE1   1 
ATOM   6432  C  CE2   . PHE   A 1 1210 ? 190.339 153.173 130.393 1.00 34.48  ? 1210 PHE   A CE2   1 
ATOM   6433  C  CZ    . PHE   A 1 1210 ? 190.904 154.428 130.365 1.00 33.24  ? 1210 PHE   A CZ    1 
ATOM   6434  N  N     . TYR   A 1 1211 ? 187.050 156.150 134.918 1.00 29.76  ? 1211 TYR   A N     1 
ATOM   6435  C  CA    . TYR   A 1 1211 ? 187.167 157.336 135.749 1.00 27.07  ? 1211 TYR   A CA    1 
ATOM   6436  C  C     . TYR   A 1 1211 ? 185.938 157.439 136.640 1.00 36.71  ? 1211 TYR   A C     1 
ATOM   6437  O  O     . TYR   A 1 1211 ? 184.805 157.304 136.167 1.00 41.69  ? 1211 TYR   A O     1 
ATOM   6438  C  CB    . TYR   A 1 1211 ? 187.309 158.596 134.894 1.00 28.00  ? 1211 TYR   A CB    1 
ATOM   6439  C  CG    . TYR   A 1 1211 ? 188.508 158.560 133.977 1.00 36.48  ? 1211 TYR   A CG    1 
ATOM   6440  C  CD1   . TYR   A 1 1211 ? 189.778 158.867 134.447 1.00 38.42  ? 1211 TYR   A CD1   1 
ATOM   6441  C  CD2   . TYR   A 1 1211 ? 188.372 158.201 132.644 1.00 39.25  ? 1211 TYR   A CD2   1 
ATOM   6442  C  CE1   . TYR   A 1 1211 ? 190.875 158.827 133.610 1.00 33.98  ? 1211 TYR   A CE1   1 
ATOM   6443  C  CE2   . TYR   A 1 1211 ? 189.461 158.160 131.802 1.00 39.50  ? 1211 TYR   A CE2   1 
ATOM   6444  C  CZ    . TYR   A 1 1211 ? 190.711 158.473 132.289 1.00 40.92  ? 1211 TYR   A CZ    1 
ATOM   6445  O  OH    . TYR   A 1 1211 ? 191.801 158.431 131.452 1.00 50.29  ? 1211 TYR   A OH    1 
ATOM   6446  N  N     . SER   A 1 1212 ? 186.164 157.668 137.927 1.00 49.27  ? 1212 SER   A N     1 
ATOM   6447  C  CA    . SER   A 1 1212 ? 185.068 157.761 138.882 1.00 44.11  ? 1212 SER   A CA    1 
ATOM   6448  C  C     . SER   A 1 1212 ? 184.407 159.133 138.814 1.00 47.20  ? 1212 SER   A C     1 
ATOM   6449  O  O     . SER   A 1 1212 ? 183.184 159.239 138.735 1.00 56.34  ? 1212 SER   A O     1 
ATOM   6450  C  CB    . SER   A 1 1212 ? 185.564 157.482 140.300 1.00 45.30  ? 1212 SER   A CB    1 
ATOM   6451  O  OG    . SER   A 1 1212 ? 186.318 158.573 140.797 1.00 54.49  ? 1212 SER   A OG    1 
HETATM 6452  N  N     . TPO   B 1 217  ? 192.130 146.616 107.440 1.00 117.56 ? 217  TPO   B N     1 
HETATM 6453  C  CA    . TPO   B 1 217  ? 190.799 147.074 107.833 1.00 118.75 ? 217  TPO   B CA    1 
HETATM 6454  C  CB    . TPO   B 1 217  ? 190.071 145.976 108.630 1.00 119.23 ? 217  TPO   B CB    1 
HETATM 6455  C  CG2   . TPO   B 1 217  ? 190.586 145.927 110.071 1.00 117.78 ? 217  TPO   B CG2   1 
HETATM 6456  O  OG1   . TPO   B 1 217  ? 188.661 146.229 108.642 1.00 120.13 ? 217  TPO   B OG1   1 
HETATM 6457  P  P     . TPO   B 1 217  ? 187.954 145.221 107.603 1.00 123.95 ? 217  TPO   B P     1 
HETATM 6458  O  O1P   . TPO   B 1 217  ? 187.604 143.965 108.301 1.00 120.33 ? 217  TPO   B O1P   1 
HETATM 6459  O  O2P   . TPO   B 1 217  ? 186.646 145.912 106.957 1.00 118.69 ? 217  TPO   B O2P   1 
HETATM 6460  O  O3P   . TPO   B 1 217  ? 188.987 144.862 106.425 1.00 120.55 ? 217  TPO   B O3P   1 
HETATM 6461  C  C     . TPO   B 1 217  ? 190.879 148.372 108.644 1.00 118.67 ? 217  TPO   B C     1 
HETATM 6462  O  O     . TPO   B 1 217  ? 191.747 148.523 109.503 1.00 119.03 ? 217  TPO   B O     1 
ATOM   6463  N  N     . MET   B 1 218  ? 189.976 149.309 108.364 1.00 107.22 ? 218  MET   B N     1 
ATOM   6464  C  CA    . MET   B 1 218  ? 189.965 150.594 109.064 1.00 105.97 ? 218  MET   B CA    1 
ATOM   6465  C  C     . MET   B 1 218  ? 189.303 150.467 110.432 1.00 105.98 ? 218  MET   B C     1 
ATOM   6466  O  O     . MET   B 1 218  ? 189.214 151.437 111.186 1.00 105.48 ? 218  MET   B O     1 
ATOM   6467  C  CB    . MET   B 1 218  ? 189.250 151.662 108.229 1.00 105.47 ? 218  MET   B CB    1 
ATOM   6468  C  CG    . MET   B 1 218  ? 189.485 153.092 108.709 1.00 106.17 ? 218  MET   B CG    1 
ATOM   6469  S  SD    . MET   B 1 218  ? 188.406 154.286 107.896 1.00 110.38 ? 218  MET   B SD    1 
ATOM   6470  C  CE    . MET   B 1 218  ? 187.614 153.233 106.685 1.00 105.58 ? 218  MET   B CE    1 
ATOM   6471  N  N     . ASP   B 1 219  ? 188.839 149.261 110.748 1.00 104.01 ? 219  ASP   B N     1 
ATOM   6472  C  CA    . ASP   B 1 219  ? 188.252 148.995 112.052 1.00 103.23 ? 219  ASP   B CA    1 
ATOM   6473  C  C     . ASP   B 1 219  ? 189.362 148.785 113.073 1.00 103.40 ? 219  ASP   B C     1 
ATOM   6474  O  O     . ASP   B 1 219  ? 190.282 147.992 112.850 1.00 105.24 ? 219  ASP   B O     1 
ATOM   6475  C  CB    . ASP   B 1 219  ? 187.340 147.771 111.989 1.00 103.61 ? 219  ASP   B CB    1 
ATOM   6476  C  CG    . ASP   B 1 219  ? 186.051 147.968 112.758 1.00 105.04 ? 219  ASP   B CG    1 
ATOM   6477  O  OD1   . ASP   B 1 219  ? 186.100 148.556 113.857 1.00 103.46 ? 219  ASP   B OD1   1 
ATOM   6478  O  OD2   . ASP   B 1 219  ? 184.990 147.534 112.264 1.00 106.22 ? 219  ASP   B OD2   1 
ATOM   6479  N  N     . ALA   B 1 220  ? 189.273 149.496 114.193 1.00 94.00  ? 220  ALA   B N     1 
ATOM   6480  C  CA    . ALA   B 1 220  ? 190.328 149.498 115.195 1.00 94.56  ? 220  ALA   B CA    1 
ATOM   6481  C  C     . ALA   B 1 220  ? 190.031 148.464 116.272 1.00 95.20  ? 220  ALA   B C     1 
ATOM   6482  O  O     . ALA   B 1 220  ? 188.912 148.402 116.791 1.00 97.01  ? 220  ALA   B O     1 
ATOM   6483  C  CB    . ALA   B 1 220  ? 190.472 150.886 115.820 1.00 94.32  ? 220  ALA   B CB    1 
ATOM   6484  N  N     . VAL   B 1 221  ? 191.034 147.658 116.601 1.00 87.39  ? 221  VAL   B N     1 
ATOM   6485  C  CA    . VAL   B 1 221  ? 190.915 146.654 117.654 1.00 86.08  ? 221  VAL   B CA    1 
ATOM   6486  C  C     . VAL   B 1 221  ? 190.780 147.374 118.990 1.00 86.98  ? 221  VAL   B C     1 
ATOM   6487  O  O     . VAL   B 1 221  ? 191.201 148.533 119.113 1.00 85.17  ? 221  VAL   B O     1 
ATOM   6488  C  CB    . VAL   B 1 221  ? 192.119 145.699 117.659 1.00 85.79  ? 221  VAL   B CB    1 
ATOM   6489  C  CG1   . VAL   B 1 221  ? 192.283 145.045 116.297 1.00 86.74  ? 221  VAL   B CG1   1 
ATOM   6490  C  CG2   . VAL   B 1 221  ? 193.385 146.445 118.057 1.00 85.13  ? 221  VAL   B CG2   1 
ATOM   6491  N  N     . PRO   B 1 222  ? 190.195 146.743 120.005 1.00 88.67  ? 222  PRO   B N     1 
ATOM   6492  C  CA    . PRO   B 1 222  ? 190.084 147.402 121.312 1.00 85.26  ? 222  PRO   B CA    1 
ATOM   6493  C  C     . PRO   B 1 222  ? 191.459 147.768 121.852 1.00 86.65  ? 222  PRO   B C     1 
ATOM   6494  O  O     . PRO   B 1 222  ? 192.407 146.984 121.770 1.00 87.33  ? 222  PRO   B O     1 
ATOM   6495  C  CB    . PRO   B 1 222  ? 189.392 146.348 122.184 1.00 84.15  ? 222  PRO   B CB    1 
ATOM   6496  C  CG    . PRO   B 1 222  ? 188.774 145.380 121.219 1.00 84.52  ? 222  PRO   B CG    1 
ATOM   6497  C  CD    . PRO   B 1 222  ? 189.661 145.372 120.022 1.00 87.49  ? 222  PRO   B CD    1 
ATOM   6498  N  N     . ARG   B 1 223  ? 191.560 148.972 122.411 1.00 85.44  ? 223  ARG   B N     1 
ATOM   6499  C  CA    . ARG   B 1 223  ? 192.839 149.481 122.882 1.00 84.58  ? 223  ARG   B CA    1 
ATOM   6500  C  C     . ARG   B 1 223  ? 192.598 150.540 123.949 1.00 84.99  ? 223  ARG   B C     1 
ATOM   6501  O  O     . ARG   B 1 223  ? 191.692 151.367 123.819 1.00 86.80  ? 223  ARG   B O     1 
ATOM   6502  C  CB    . ARG   B 1 223  ? 193.660 150.054 121.722 1.00 85.95  ? 223  ARG   B CB    1 
ATOM   6503  C  CG    . ARG   B 1 223  ? 194.629 151.154 122.105 1.00 87.12  ? 223  ARG   B CG    1 
ATOM   6504  C  CD    . ARG   B 1 223  ? 195.128 151.876 120.865 1.00 87.08  ? 223  ARG   B CD    1 
ATOM   6505  N  NE    . ARG   B 1 223  ? 195.424 150.944 119.784 1.00 88.17  ? 223  ARG   B NE    1 
ATOM   6506  C  CZ    . ARG   B 1 223  ? 196.599 150.359 119.594 1.00 89.13  ? 223  ARG   B CZ    1 
ATOM   6507  N  NH1   . ARG   B 1 223  ? 197.623 150.587 120.400 1.00 88.62  ? 223  ARG   B NH1   1 
ATOM   6508  N  NH2   . ARG   B 1 223  ? 196.750 149.525 118.569 1.00 87.36  ? 223  ARG   B NH2   1 
ATOM   6509  N  N     . ILE   B 1 224  ? 193.424 150.510 124.998 1.00 81.08  ? 224  ILE   B N     1 
ATOM   6510  C  CA    . ILE   B 1 224  ? 193.236 151.395 126.141 1.00 81.19  ? 224  ILE   B CA    1 
ATOM   6511  C  C     . ILE   B 1 224  ? 193.321 152.864 125.752 1.00 82.01  ? 224  ILE   B C     1 
ATOM   6512  O  O     . ILE   B 1 224  ? 192.844 153.727 126.496 1.00 83.77  ? 224  ILE   B O     1 
ATOM   6513  C  CB    . ILE   B 1 224  ? 194.268 151.064 127.239 1.00 82.73  ? 224  ILE   B CB    1 
ATOM   6514  C  CG1   . ILE   B 1 224  ? 194.054 151.952 128.466 1.00 82.58  ? 224  ILE   B CG1   1 
ATOM   6515  C  CG2   . ILE   B 1 224  ? 195.682 151.231 126.709 1.00 82.55  ? 224  ILE   B CG2   1 
ATOM   6516  C  CD1   . ILE   B 1 224  ? 194.162 151.213 129.781 1.00 81.13  ? 224  ILE   B CD1   1 
ATOM   6517  N  N     . ASP   B 1 225  ? 193.913 153.173 124.598 1.00 87.22  ? 225  ASP   B N     1 
ATOM   6518  C  CA    . ASP   B 1 225  ? 194.100 154.567 124.212 1.00 86.16  ? 225  ASP   B CA    1 
ATOM   6519  C  C     . ASP   B 1 225  ? 192.800 155.229 123.774 1.00 86.70  ? 225  ASP   B C     1 
ATOM   6520  O  O     . ASP   B 1 225  ? 192.646 156.444 123.940 1.00 88.70  ? 225  ASP   B O     1 
ATOM   6521  C  CB    . ASP   B 1 225  ? 195.142 154.667 123.097 1.00 88.69  ? 225  ASP   B CB    1 
ATOM   6522  C  CG    . ASP   B 1 225  ? 196.394 153.868 123.398 1.00 89.53  ? 225  ASP   B CG    1 
ATOM   6523  O  OD1   . ASP   B 1 225  ? 196.497 153.323 124.517 1.00 89.55  ? 225  ASP   B OD1   1 
ATOM   6524  O  OD2   . ASP   B 1 225  ? 197.277 153.788 122.518 1.00 88.93  ? 225  ASP   B OD2   1 
ATOM   6525  N  N     . HIS   B 1 226  ? 191.859 154.465 123.215 1.00 83.59  ? 226  HIS   B N     1 
ATOM   6526  C  CA    . HIS   B 1 226  ? 190.589 155.057 122.806 1.00 83.35  ? 226  HIS   B CA    1 
ATOM   6527  C  C     . HIS   B 1 226  ? 189.819 155.596 124.005 1.00 84.95  ? 226  HIS   B C     1 
ATOM   6528  O  O     . HIS   B 1 226  ? 189.218 156.674 123.933 1.00 85.42  ? 226  HIS   B O     1 
ATOM   6529  C  CB    . HIS   B 1 226  ? 189.741 154.037 122.047 1.00 82.49  ? 226  HIS   B CB    1 
ATOM   6530  C  CG    . HIS   B 1 226  ? 190.505 153.240 121.037 1.00 81.94  ? 226  HIS   B CG    1 
ATOM   6531  N  ND1   . HIS   B 1 226  ? 191.153 153.818 119.968 1.00 83.11  ? 226  HIS   B ND1   1 
ATOM   6532  C  CD2   . HIS   B 1 226  ? 190.702 151.906 120.919 1.00 82.96  ? 226  HIS   B CD2   1 
ATOM   6533  C  CE1   . HIS   B 1 226  ? 191.730 152.876 119.244 1.00 84.40  ? 226  HIS   B CE1   1 
ATOM   6534  N  NE2   . HIS   B 1 226  ? 191.470 151.707 119.798 1.00 83.32  ? 226  HIS   B NE2   1 
ATOM   6535  N  N     . TYR   B 1 227  ? 189.820 154.856 125.112 1.00 83.23  ? 227  TYR   B N     1 
ATOM   6536  C  CA    . TYR   B 1 227  ? 189.051 155.234 126.290 1.00 80.46  ? 227  TYR   B CA    1 
ATOM   6537  C  C     . TYR   B 1 227  ? 189.805 156.162 127.231 1.00 81.36  ? 227  TYR   B C     1 
ATOM   6538  O  O     . TYR   B 1 227  ? 189.175 156.803 128.081 1.00 82.83  ? 227  TYR   B O     1 
ATOM   6539  C  CB    . TYR   B 1 227  ? 188.619 153.981 127.055 1.00 79.66  ? 227  TYR   B CB    1 
ATOM   6540  C  CG    . TYR   B 1 227  ? 187.894 152.967 126.203 1.00 81.37  ? 227  TYR   B CG    1 
ATOM   6541  C  CD1   . TYR   B 1 227  ? 188.595 152.020 125.469 1.00 80.06  ? 227  TYR   B CD1   1 
ATOM   6542  C  CD2   . TYR   B 1 227  ? 186.507 152.958 126.130 1.00 80.31  ? 227  TYR   B CD2   1 
ATOM   6543  C  CE1   . TYR   B 1 227  ? 187.936 151.092 124.689 1.00 80.79  ? 227  TYR   B CE1   1 
ATOM   6544  C  CE2   . TYR   B 1 227  ? 185.839 152.033 125.353 1.00 79.93  ? 227  TYR   B CE2   1 
ATOM   6545  C  CZ    . TYR   B 1 227  ? 186.558 151.103 124.635 1.00 81.33  ? 227  TYR   B CZ    1 
ATOM   6546  O  OH    . TYR   B 1 227  ? 185.898 150.180 123.860 1.00 81.31  ? 227  TYR   B OH    1 
ATOM   6547  N  N     . ARG   B 1 228  ? 191.126 156.250 127.107 1.00 92.79  ? 228  ARG   B N     1 
ATOM   6548  C  CA    . ARG   B 1 228  ? 191.937 157.102 127.976 1.00 92.20  ? 228  ARG   B CA    1 
ATOM   6549  C  C     . ARG   B 1 228  ? 191.944 158.508 127.389 1.00 92.90  ? 228  ARG   B C     1 
ATOM   6550  O  O     . ARG   B 1 228  ? 192.777 158.853 126.550 1.00 97.45  ? 228  ARG   B O     1 
ATOM   6551  C  CB    . ARG   B 1 228  ? 193.347 156.538 128.110 1.00 92.37  ? 228  ARG   B CB    1 
ATOM   6552  C  CG    . ARG   B 1 228  ? 194.410 157.570 128.439 1.00 93.38  ? 228  ARG   B CG    1 
ATOM   6553  C  CD    . ARG   B 1 228  ? 195.745 156.906 128.733 1.00 93.45  ? 228  ARG   B CD    1 
ATOM   6554  N  NE    . ARG   B 1 228  ? 195.625 155.822 129.701 1.00 95.03  ? 228  ARG   B NE    1 
ATOM   6555  C  CZ    . ARG   B 1 228  ? 195.238 155.976 130.960 1.00 95.85  ? 228  ARG   B CZ    1 
ATOM   6556  N  NH1   . ARG   B 1 228  ? 194.919 157.165 131.445 1.00 94.85  ? 228  ARG   B NH1   1 
ATOM   6557  N  NH2   . ARG   B 1 228  ? 195.170 154.911 131.753 1.00 94.76  ? 228  ARG   B NH2   1 
ATOM   6558  N  N     . HIS   B 1 229  ? 190.992 159.333 127.828 1.00 90.66  ? 229  HIS   B N     1 
ATOM   6559  C  CA    . HIS   B 1 229  ? 190.884 160.691 127.304 1.00 94.07  ? 229  HIS   B CA    1 
ATOM   6560  C  C     . HIS   B 1 229  ? 190.656 161.777 128.345 1.00 94.73  ? 229  HIS   B C     1 
ATOM   6561  O  O     . HIS   B 1 229  ? 190.841 162.953 128.015 1.00 94.67  ? 229  HIS   B O     1 
ATOM   6562  N  N     . THR   B 1 230  ? 190.271 161.453 129.578 1.00 103.31 ? 230  THR   B N     1 
ATOM   6563  C  CA    . THR   B 1 230  ? 189.967 162.472 130.576 1.00 104.30 ? 230  THR   B CA    1 
ATOM   6564  C  C     . THR   B 1 230  ? 191.114 162.725 131.544 1.00 105.64 ? 230  THR   B C     1 
ATOM   6565  O  O     . THR   B 1 230  ? 191.377 163.880 131.894 1.00 105.68 ? 230  THR   B O     1 
ATOM   6566  C  CB    . THR   B 1 230  ? 188.715 162.085 131.370 1.00 104.08 ? 230  THR   B CB    1 
ATOM   6567  O  OG1   . THR   B 1 230  ? 189.023 160.995 132.246 1.00 102.73 ? 230  THR   B OG1   1 
ATOM   6568  C  CG2   . THR   B 1 230  ? 187.598 161.666 130.428 1.00 101.80 ? 230  THR   B CG2   1 
ATOM   6569  N  N     . ALA   B 1 231  ? 191.802 161.675 131.990 1.00 105.58 ? 231  ALA   B N     1 
ATOM   6570  C  CA    . ALA   B 1 231  ? 192.914 161.808 132.921 1.00 102.51 ? 231  ALA   B CA    1 
ATOM   6571  C  C     . ALA   B 1 231  ? 194.270 161.602 132.259 1.00 103.95 ? 231  ALA   B C     1 
ATOM   6572  O  O     . ALA   B 1 231  ? 195.289 161.558 132.957 1.00 103.36 ? 231  ALA   B O     1 
ATOM   6573  N  N     . ALA   B 1 232  ? 194.310 161.475 130.935 1.00 113.92 ? 232  ALA   B N     1 
ATOM   6574  C  CA    . ALA   B 1 232  ? 195.566 161.279 130.228 1.00 114.28 ? 232  ALA   B CA    1 
ATOM   6575  C  C     . ALA   B 1 232  ? 195.389 161.702 128.779 1.00 114.70 ? 232  ALA   B C     1 
ATOM   6576  O  O     . ALA   B 1 232  ? 194.268 161.802 128.273 1.00 112.26 ? 232  ALA   B O     1 
ATOM   6577  C  CB    . ALA   B 1 232  ? 196.041 159.825 130.314 1.00 113.59 ? 232  ALA   B CB    1 
ATOM   6578  N  N     . GLN   B 1 233  ? 196.516 161.948 128.117 1.00 126.15 ? 233  GLN   B N     1 
ATOM   6579  C  CA    . GLN   B 1 233  ? 196.492 162.331 126.713 1.00 126.74 ? 233  GLN   B CA    1 
ATOM   6580  C  C     . GLN   B 1 233  ? 196.034 161.163 125.849 1.00 127.57 ? 233  GLN   B C     1 
ATOM   6581  O  O     . GLN   B 1 233  ? 196.344 160.001 126.129 1.00 127.51 ? 233  GLN   B O     1 
ATOM   6582  C  CB    . GLN   B 1 233  ? 197.876 162.804 126.268 1.00 124.94 ? 233  GLN   B CB    1 
ATOM   6583  N  N     . LEU   B 1 234  ? 195.285 161.479 124.791 1.00 126.33 ? 234  LEU   B N     1 
ATOM   6584  C  CA    . LEU   B 1 234  ? 194.802 160.438 123.889 1.00 125.34 ? 234  LEU   B CA    1 
ATOM   6585  C  C     . LEU   B 1 234  ? 195.910 159.961 122.957 1.00 126.10 ? 234  LEU   B C     1 
ATOM   6586  O  O     . LEU   B 1 234  ? 196.191 158.759 122.873 1.00 126.14 ? 234  LEU   B O     1 
ATOM   6587  N  N     . GLY   B 1 235  ? 196.546 160.884 122.250 1.00 126.55 ? 235  GLY   B N     1 
ATOM   6588  C  CA    . GLY   B 1 235  ? 197.621 160.563 121.333 1.00 126.24 ? 235  GLY   B CA    1 
ATOM   6589  C  C     . GLY   B 1 235  ? 197.172 160.662 119.884 1.00 126.13 ? 235  GLY   B C     1 
ATOM   6590  O  O     . GLY   B 1 235  ? 196.025 160.984 119.572 1.00 125.52 ? 235  GLY   B O     1 
ATOM   6591  N  N     . GLU   B 1 236  ? 198.120 160.370 118.994 1.00 125.73 ? 236  GLU   B N     1 
ATOM   6592  C  CA    . GLU   B 1 236  ? 197.867 160.413 117.557 1.00 125.74 ? 236  GLU   B CA    1 
ATOM   6593  C  C     . GLU   B 1 236  ? 197.147 159.155 117.078 1.00 126.43 ? 236  GLU   B C     1 
ATOM   6594  O  O     . GLU   B 1 236  ? 196.056 159.235 116.504 1.00 125.30 ? 236  GLU   B O     1 
ATOM   6595  N  N     . LYS   B 1 237  ? 197.748 157.987 117.308 1.00 121.41 ? 237  LYS   B N     1 
ATOM   6596  C  CA    . LYS   B 1 237  ? 197.141 156.725 116.906 1.00 120.44 ? 237  LYS   B CA    1 
ATOM   6597  C  C     . LYS   B 1 237  ? 196.048 156.258 117.856 1.00 120.24 ? 237  LYS   B C     1 
ATOM   6598  O  O     . LYS   B 1 237  ? 195.320 155.317 117.521 1.00 118.10 ? 237  LYS   B O     1 
ATOM   6599  N  N     . LEU   B 1 238  ? 195.916 156.883 119.026 1.00 113.30 ? 238  LEU   B N     1 
ATOM   6600  C  CA    . LEU   B 1 238  ? 194.882 156.511 119.993 1.00 111.74 ? 238  LEU   B CA    1 
ATOM   6601  C  C     . LEU   B 1 238  ? 193.581 157.241 119.657 1.00 112.19 ? 238  LEU   B C     1 
ATOM   6602  O  O     . LEU   B 1 238  ? 193.131 158.153 120.353 1.00 110.98 ? 238  LEU   B O     1 
ATOM   6603  N  N     . LEU   B 1 239  ? 192.975 156.813 118.552 1.00 104.56 ? 239  LEU   B N     1 
ATOM   6604  C  CA    . LEU   B 1 239  ? 191.717 157.395 118.092 1.00 103.22 ? 239  LEU   B CA    1 
ATOM   6605  C  C     . LEU   B 1 239  ? 190.977 156.337 117.287 1.00 101.14 ? 239  LEU   B C     1 
ATOM   6606  O  O     . LEU   B 1 239  ? 191.348 156.058 116.144 1.00 101.93 ? 239  LEU   B O     1 
ATOM   6607  C  CB    . LEU   B 1 239  ? 191.962 158.649 117.258 1.00 102.55 ? 239  LEU   B CB    1 
ATOM   6608  C  CG    . LEU   B 1 239  ? 192.079 159.965 118.028 1.00 103.92 ? 239  LEU   B CG    1 
ATOM   6609  C  CD1   . LEU   B 1 239  ? 192.523 161.087 117.103 1.00 102.29 ? 239  LEU   B CD1   1 
ATOM   6610  C  CD2   . LEU   B 1 239  ? 190.761 160.311 118.706 1.00 101.31 ? 239  LEU   B CD2   1 
ATOM   6611  N  N     . ARG   B 1 240  ? 189.936 155.774 117.904 1.00 87.90  ? 240  ARG   B N     1 
ATOM   6612  C  CA    . ARG   B 1 240  ? 189.116 154.755 117.213 1.00 87.30  ? 240  ARG   B CA    1 
ATOM   6613  C  C     . ARG   B 1 240  ? 188.394 155.442 116.064 1.00 87.58  ? 240  ARG   B C     1 
ATOM   6614  O  O     . ARG   B 1 240  ? 188.110 156.650 116.174 1.00 86.52  ? 240  ARG   B O     1 
ATOM   6615  C  CB    . ARG   B 1 240  ? 188.082 154.136 118.160 1.00 85.84  ? 240  ARG   B CB    1 
ATOM   6616  C  CG    . ARG   B 1 240  ? 186.910 155.049 118.490 1.00 84.34  ? 240  ARG   B CG    1 
ATOM   6617  C  CD    . ARG   B 1 240  ? 185.717 154.354 119.121 1.00 82.90  ? 240  ARG   B CD    1 
ATOM   6618  N  NE    . ARG   B 1 240  ? 185.946 154.020 120.518 1.00 86.43  ? 240  ARG   B NE    1 
ATOM   6619  C  CZ    . ARG   B 1 240  ? 185.595 154.777 121.550 1.00 85.61  ? 240  ARG   B CZ    1 
ATOM   6620  N  NH1   . ARG   B 1 240  ? 184.980 155.930 121.350 1.00 86.03  ? 240  ARG   B NH1   1 
ATOM   6621  N  NH2   . ARG   B 1 240  ? 185.859 154.377 122.781 1.00 83.73  ? 240  ARG   B NH2   1 
ATOM   6622  N  N     . PRO   B 1 241  ? 188.105 154.739 114.956 1.00 87.09  ? 241  PRO   B N     1 
ATOM   6623  C  CA    . PRO   B 1 241  ? 187.303 155.324 113.879 1.00 85.58  ? 241  PRO   B CA    1 
ATOM   6624  C  C     . PRO   B 1 241  ? 185.863 155.536 114.312 1.00 86.24  ? 241  PRO   B C     1 
ATOM   6625  O  O     . PRO   B 1 241  ? 185.287 154.740 115.057 1.00 86.90  ? 241  PRO   B O     1 
ATOM   6626  C  CB    . PRO   B 1 241  ? 187.401 154.283 112.759 1.00 86.39  ? 241  PRO   B CB    1 
ATOM   6627  C  CG    . PRO   B 1 241  ? 187.649 152.999 113.469 1.00 86.29  ? 241  PRO   B CG    1 
ATOM   6628  C  CD    . PRO   B 1 241  ? 188.478 153.341 114.677 1.00 86.54  ? 241  PRO   B CD    1 
ATOM   6629  N  N     . SER   B 1 242  ? 185.282 156.633 113.835 1.00 82.30  ? 242  SER   B N     1 
ATOM   6630  C  CA    . SER   B 1 242  ? 183.875 156.902 114.079 1.00 79.19  ? 242  SER   B CA    1 
ATOM   6631  C  C     . SER   B 1 242  ? 183.011 156.003 113.205 1.00 80.51  ? 242  SER   B C     1 
ATOM   6632  O  O     . SER   B 1 242  ? 183.430 155.553 112.135 1.00 84.24  ? 242  SER   B O     1 
ATOM   6633  C  CB    . SER   B 1 242  ? 183.548 158.370 113.808 1.00 79.88  ? 242  SER   B CB    1 
ATOM   6634  O  OG    . SER   B 1 242  ? 183.269 158.586 112.436 1.00 83.81  ? 242  SER   B OG    1 
ATOM   6635  N  N     . LEU   B 1 243  ? 181.791 155.740 113.675 1.00 77.35  ? 243  LEU   B N     1 
ATOM   6636  C  CA    . LEU   B 1 243  ? 180.891 154.879 112.917 1.00 75.92  ? 243  LEU   B CA    1 
ATOM   6637  C  C     . LEU   B 1 243  ? 180.600 155.454 111.538 1.00 78.31  ? 243  LEU   B C     1 
ATOM   6638  O  O     . LEU   B 1 243  ? 180.422 154.699 110.574 1.00 81.15  ? 243  LEU   B O     1 
ATOM   6639  C  CB    . LEU   B 1 243  ? 179.593 154.664 113.696 1.00 76.74  ? 243  LEU   B CB    1 
ATOM   6640  C  CG    . LEU   B 1 243  ? 178.448 153.978 112.950 1.00 77.77  ? 243  LEU   B CG    1 
ATOM   6641  C  CD1   . LEU   B 1 243  ? 178.694 152.480 112.851 1.00 74.14  ? 243  LEU   B CD1   1 
ATOM   6642  C  CD2   . LEU   B 1 243  ? 177.117 154.264 113.630 1.00 79.71  ? 243  LEU   B CD2   1 
ATOM   6643  N  N     . ALA   B 1 244  ? 180.548 156.783 111.421 1.00 80.37  ? 244  ALA   B N     1 
ATOM   6644  C  CA    . ALA   B 1 244  ? 180.330 157.404 110.120 1.00 79.16  ? 244  ALA   B CA    1 
ATOM   6645  C  C     . ALA   B 1 244  ? 181.501 157.147 109.178 1.00 81.46  ? 244  ALA   B C     1 
ATOM   6646  O  O     . ALA   B 1 244  ? 181.299 156.877 107.989 1.00 84.55  ? 244  ALA   B O     1 
ATOM   6647  C  CB    . ALA   B 1 244  ? 180.093 158.904 110.288 1.00 78.60  ? 244  ALA   B CB    1 
ATOM   6648  N  N     . GLU   B 1 245  ? 182.732 157.223 109.691 1.00 84.15  ? 245  GLU   B N     1 
ATOM   6649  C  CA    . GLU   B 1 245  ? 183.904 157.001 108.851 1.00 83.52  ? 245  GLU   B CA    1 
ATOM   6650  C  C     . GLU   B 1 245  ? 183.982 155.573 108.329 1.00 84.82  ? 245  GLU   B C     1 
ATOM   6651  O  O     . GLU   B 1 245  ? 184.725 155.317 107.375 1.00 88.95  ? 245  GLU   B O     1 
ATOM   6652  C  CB    . GLU   B 1 245  ? 185.182 157.337 109.622 1.00 83.23  ? 245  GLU   B CB    1 
ATOM   6653  C  CG    . GLU   B 1 245  ? 185.163 158.694 110.306 1.00 86.80  ? 245  GLU   B CG    1 
ATOM   6654  C  CD    . GLU   B 1 245  ? 186.376 158.917 111.190 1.00 89.00  ? 245  GLU   B CD    1 
ATOM   6655  O  OE1   . GLU   B 1 245  ? 187.341 158.132 111.084 1.00 88.61  ? 245  GLU   B OE1   1 
ATOM   6656  O  OE2   . GLU   B 1 245  ? 186.362 159.873 111.993 1.00 87.65  ? 245  GLU   B OE2   1 
ATOM   6657  N  N     . LEU   B 1 246  ? 183.239 154.642 108.928 1.00 80.35  ? 246  LEU   B N     1 
ATOM   6658  C  CA    . LEU   B 1 246  ? 183.234 153.256 108.488 1.00 82.20  ? 246  LEU   B CA    1 
ATOM   6659  C  C     . LEU   B 1 246  ? 181.969 152.856 107.747 1.00 83.36  ? 246  LEU   B C     1 
ATOM   6660  O  O     . LEU   B 1 246  ? 181.996 151.870 107.004 1.00 84.08  ? 246  LEU   B O     1 
ATOM   6661  C  CB    . LEU   B 1 246  ? 183.420 152.314 109.687 1.00 83.21  ? 246  LEU   B CB    1 
ATOM   6662  C  CG    . LEU   B 1 246  ? 184.776 152.365 110.393 1.00 83.23  ? 246  LEU   B CG    1 
ATOM   6663  C  CD1   . LEU   B 1 246  ? 184.702 151.667 111.740 1.00 83.64  ? 246  LEU   B CD1   1 
ATOM   6664  C  CD2   . LEU   B 1 246  ? 185.860 151.746 109.527 1.00 85.44  ? 246  LEU   B CD2   1 
ATOM   6665  N  N     . HIS   B 1 247  ? 180.871 153.584 107.929 1.00 83.86  ? 247  HIS   B N     1 
ATOM   6666  C  CA    . HIS   B 1 247  ? 179.602 153.263 107.287 1.00 83.44  ? 247  HIS   B CA    1 
ATOM   6667  C  C     . HIS   B 1 247  ? 179.211 154.250 106.200 1.00 84.10  ? 247  HIS   B C     1 
ATOM   6668  O  O     . HIS   B 1 247  ? 178.601 153.853 105.205 1.00 84.15  ? 247  HIS   B O     1 
ATOM   6669  C  CB    . HIS   B 1 247  ? 178.486 153.196 108.336 1.00 82.09  ? 247  HIS   B CB    1 
ATOM   6670  C  CG    . HIS   B 1 247  ? 177.109 153.142 107.754 1.00 81.20  ? 247  HIS   B CG    1 
ATOM   6671  N  ND1   . HIS   B 1 247  ? 176.111 154.020 108.117 1.00 82.45  ? 247  HIS   B ND1   1 
ATOM   6672  C  CD2   . HIS   B 1 247  ? 176.559 152.304 106.843 1.00 81.11  ? 247  HIS   B CD2   1 
ATOM   6673  C  CE1   . HIS   B 1 247  ? 175.008 153.731 107.450 1.00 83.23  ? 247  HIS   B CE1   1 
ATOM   6674  N  NE2   . HIS   B 1 247  ? 175.253 152.694 106.670 1.00 81.10  ? 247  HIS   B NE2   1 
ATOM   6675  N  N     . ASP   B 1 248  ? 179.552 155.527 106.360 1.00 90.69  ? 248  ASP   B N     1 
ATOM   6676  C  CA    . ASP   B 1 248  ? 179.189 156.526 105.365 1.00 90.99  ? 248  ASP   B CA    1 
ATOM   6677  C  C     . ASP   B 1 248  ? 179.869 156.231 104.035 1.00 91.91  ? 248  ASP   B C     1 
ATOM   6678  O  O     . ASP   B 1 248  ? 180.980 155.696 103.988 1.00 92.38  ? 248  ASP   B O     1 
ATOM   6679  C  CB    . ASP   B 1 248  ? 179.569 157.924 105.853 1.00 91.52  ? 248  ASP   B CB    1 
ATOM   6680  C  CG    . ASP   B 1 248  ? 178.365 158.741 106.274 1.00 92.09  ? 248  ASP   B CG    1 
ATOM   6681  O  OD1   . ASP   B 1 248  ? 177.250 158.450 105.792 1.00 93.06  ? 248  ASP   B OD1   1 
ATOM   6682  O  OD2   . ASP   B 1 248  ? 178.532 159.676 107.084 1.00 93.17  ? 248  ASP   B OD2   1 
ATOM   6683  N  N     . GLU   B 1 249  ? 179.191 156.587 102.947 1.00 103.54 ? 249  GLU   B N     1 
ATOM   6684  C  CA    . GLU   B 1 249  ? 179.697 156.313 101.611 1.00 104.02 ? 249  GLU   B CA    1 
ATOM   6685  C  C     . GLU   B 1 249  ? 180.607 157.440 101.139 1.00 105.15 ? 249  GLU   B C     1 
ATOM   6686  O  O     . GLU   B 1 249  ? 180.304 158.622 101.323 1.00 104.34 ? 249  GLU   B O     1 
ATOM   6687  C  CB    . GLU   B 1 249  ? 178.537 156.132 100.632 1.00 103.31 ? 249  GLU   B CB    1 
ATOM   6688  C  CG    . GLU   B 1 249  ? 178.952 155.655 99.251  1.00 105.64 ? 249  GLU   B CG    1 
ATOM   6689  C  CD    . GLU   B 1 249  ? 180.131 154.703 99.294  1.00 107.12 ? 249  GLU   B CD    1 
ATOM   6690  O  OE1   . GLU   B 1 249  ? 181.284 155.183 99.313  1.00 107.01 ? 249  GLU   B OE1   1 
ATOM   6691  O  OE2   . GLU   B 1 249  ? 179.905 153.475 99.311  1.00 107.04 ? 249  GLU   B OE2   1 
ATOM   6692  N  N     . LEU   B 1 250  ? 181.724 157.063 100.525 1.00 106.28 ? 250  LEU   B N     1 
ATOM   6693  C  CA    . LEU   B 1 250  ? 182.690 158.028 100.014 1.00 104.50 ? 250  LEU   B CA    1 
ATOM   6694  C  C     . LEU   B 1 250  ? 183.896 157.315 99.411  1.00 103.51 ? 250  LEU   B C     1 
ATOM   6695  O  O     . LEU   B 1 250  ? 184.288 156.243 99.872  1.00 102.71 ? 250  LEU   B O     1 
ATOM   6696  C  CB    . LEU   B 1 250  ? 183.142 158.981 101.122 1.00 103.51 ? 250  LEU   B CB    1 
ATOM   6697  N  N     . VAL   B 1 282  ? 203.987 163.960 141.349 1.00 58.92  ? 282  VAL   B N     1 
ATOM   6698  C  CA    . VAL   B 1 282  ? 205.433 163.870 141.505 1.00 63.35  ? 282  VAL   B CA    1 
ATOM   6699  C  C     . VAL   B 1 282  ? 205.782 162.924 142.645 1.00 65.40  ? 282  VAL   B C     1 
ATOM   6700  O  O     . VAL   B 1 282  ? 206.593 162.013 142.482 1.00 64.06  ? 282  VAL   B O     1 
ATOM   6701  C  CB    . VAL   B 1 282  ? 206.054 165.256 141.742 1.00 65.16  ? 282  VAL   B CB    1 
ATOM   6702  C  CG1   . VAL   B 1 282  ? 207.561 165.138 141.908 1.00 62.03  ? 282  VAL   B CG1   1 
ATOM   6703  C  CG2   . VAL   B 1 282  ? 205.712 166.191 140.594 1.00 63.84  ? 282  VAL   B CG2   1 
ATOM   6704  N  N     . VAL   B 1 283  ? 205.161 163.141 143.801 1.00 57.37  ? 283  VAL   B N     1 
ATOM   6705  C  CA    . VAL   B 1 283  ? 205.388 162.328 144.990 1.00 56.14  ? 283  VAL   B CA    1 
ATOM   6706  C  C     . VAL   B 1 283  ? 204.188 161.411 145.169 1.00 54.38  ? 283  VAL   B C     1 
ATOM   6707  O  O     . VAL   B 1 283  ? 203.060 161.882 145.359 1.00 52.51  ? 283  VAL   B O     1 
ATOM   6708  C  CB    . VAL   B 1 283  ? 205.612 163.196 146.237 1.00 57.80  ? 283  VAL   B CB    1 
ATOM   6709  C  CG1   . VAL   B 1 283  ? 205.566 162.342 147.493 1.00 55.50  ? 283  VAL   B CG1   1 
ATOM   6710  C  CG2   . VAL   B 1 283  ? 206.937 163.932 146.135 1.00 58.71  ? 283  VAL   B CG2   1 
ATOM   6711  N  N     . LYS   B 1 284  ? 204.431 160.104 145.111 1.00 48.14  ? 284  LYS   B N     1 
ATOM   6712  C  CA    . LYS   B 1 284  ? 203.392 159.096 145.254 1.00 47.28  ? 284  LYS   B CA    1 
ATOM   6713  C  C     . LYS   B 1 284  ? 203.800 158.104 146.331 1.00 48.43  ? 284  LYS   B C     1 
ATOM   6714  O  O     . LYS   B 1 284  ? 204.933 157.612 146.336 1.00 53.45  ? 284  LYS   B O     1 
ATOM   6715  C  CB    . LYS   B 1 284  ? 203.141 158.360 143.931 1.00 46.04  ? 284  LYS   B CB    1 
ATOM   6716  C  CG    . LYS   B 1 284  ? 201.921 158.842 143.163 1.00 44.10  ? 284  LYS   B CG    1 
ATOM   6717  C  CD    . LYS   B 1 284  ? 201.719 160.337 143.316 1.00 46.41  ? 284  LYS   B CD    1 
ATOM   6718  C  CE    . LYS   B 1 284  ? 200.681 160.858 142.338 1.00 45.55  ? 284  LYS   B CE    1 
ATOM   6719  N  NZ    . LYS   B 1 284  ? 200.407 162.305 142.543 1.00 47.13  ? 284  LYS   B NZ    1 
ATOM   6720  N  N     . PHE   B 1 285  ? 202.875 157.807 147.236 1.00 35.88  ? 285  PHE   B N     1 
ATOM   6721  C  CA    . PHE   B 1 285  ? 203.137 156.925 148.361 1.00 33.15  ? 285  PHE   B CA    1 
ATOM   6722  C  C     . PHE   B 1 285  ? 202.491 155.566 148.135 1.00 35.07  ? 285  PHE   B C     1 
ATOM   6723  O  O     . PHE   B 1 285  ? 201.490 155.444 147.424 1.00 43.89  ? 285  PHE   B O     1 
ATOM   6724  C  CB    . PHE   B 1 285  ? 202.615 157.531 149.666 1.00 38.71  ? 285  PHE   B CB    1 
ATOM   6725  C  CG    . PHE   B 1 285  ? 203.315 158.793 150.071 1.00 42.38  ? 285  PHE   B CG    1 
ATOM   6726  C  CD1   . PHE   B 1 285  ? 204.554 158.747 150.684 1.00 44.02  ? 285  PHE   B CD1   1 
ATOM   6727  C  CD2   . PHE   B 1 285  ? 202.735 160.027 149.840 1.00 42.58  ? 285  PHE   B CD2   1 
ATOM   6728  C  CE1   . PHE   B 1 285  ? 205.200 159.907 151.058 1.00 41.68  ? 285  PHE   B CE1   1 
ATOM   6729  C  CE2   . PHE   B 1 285  ? 203.377 161.189 150.213 1.00 43.41  ? 285  PHE   B CE2   1 
ATOM   6730  C  CZ    . PHE   B 1 285  ? 204.611 161.129 150.822 1.00 41.00  ? 285  PHE   B CZ    1 
ATOM   6731  N  N     . GLY   B 1 286  ? 203.079 154.541 148.747 1.00 32.48  ? 286  GLY   B N     1 
ATOM   6732  C  CA    . GLY   B 1 286  ? 202.515 153.211 148.710 1.00 29.97  ? 286  GLY   B CA    1 
ATOM   6733  C  C     . GLY   B 1 286  ? 201.378 153.044 149.700 1.00 31.49  ? 286  GLY   B C     1 
ATOM   6734  O  O     . GLY   B 1 286  ? 200.972 153.970 150.401 1.00 39.88  ? 286  GLY   B O     1 
ATOM   6735  N  N     . TRP   B 1 287  ? 200.854 151.818 149.753 1.00 25.30  ? 287  TRP   B N     1 
ATOM   6736  C  CA    . TRP   B 1 287  ? 199.710 151.550 150.618 1.00 22.77  ? 287  TRP   B CA    1 
ATOM   6737  C  C     . TRP   B 1 287  ? 200.107 151.497 152.087 1.00 33.00  ? 287  TRP   B C     1 
ATOM   6738  O  O     . TRP   B 1 287  ? 199.272 151.759 152.960 1.00 35.02  ? 287  TRP   B O     1 
ATOM   6739  C  CB    . TRP   B 1 287  ? 199.033 150.244 150.206 1.00 34.63  ? 287  TRP   B CB    1 
ATOM   6740  C  CG    . TRP   B 1 287  ? 199.838 149.026 150.518 1.00 29.49  ? 287  TRP   B CG    1 
ATOM   6741  C  CD1   . TRP   B 1 287  ? 200.866 148.516 149.784 1.00 28.32  ? 287  TRP   B CD1   1 
ATOM   6742  C  CD2   . TRP   B 1 287  ? 199.676 148.154 151.641 1.00 26.62  ? 287  TRP   B CD2   1 
ATOM   6743  N  NE1   . TRP   B 1 287  ? 201.358 147.383 150.382 1.00 34.48  ? 287  TRP   B NE1   1 
ATOM   6744  C  CE2   . TRP   B 1 287  ? 200.644 147.139 151.525 1.00 30.75  ? 287  TRP   B CE2   1 
ATOM   6745  C  CE3   . TRP   B 1 287  ? 198.807 148.134 152.736 1.00 30.58  ? 287  TRP   B CE3   1 
ATOM   6746  C  CZ2   . TRP   B 1 287  ? 200.768 146.116 152.460 1.00 37.84  ? 287  TRP   B CZ2   1 
ATOM   6747  C  CZ3   . TRP   B 1 287  ? 198.932 147.118 153.663 1.00 29.49  ? 287  TRP   B CZ3   1 
ATOM   6748  C  CH2   . TRP   B 1 287  ? 199.904 146.123 153.519 1.00 35.79  ? 287  TRP   B CH2   1 
ATOM   6749  N  N     . ILE   B 1 288  ? 201.362 151.162 152.382 1.00 38.89  ? 288  ILE   B N     1 
ATOM   6750  C  CA    . ILE   B 1 288  ? 201.811 151.085 153.771 1.00 34.97  ? 288  ILE   B CA    1 
ATOM   6751  C  C     . ILE   B 1 288  ? 202.107 152.475 154.319 1.00 34.70  ? 288  ILE   B C     1 
ATOM   6752  O  O     . ILE   B 1 288  ? 201.490 152.925 155.291 1.00 36.85  ? 288  ILE   B O     1 
ATOM   6753  C  CB    . ILE   B 1 288  ? 203.037 150.163 153.893 1.00 27.26  ? 288  ILE   B CB    1 
ATOM   6754  C  CG1   . ILE   B 1 288  ? 202.614 148.700 153.768 1.00 32.90  ? 288  ILE   B CG1   1 
ATOM   6755  C  CG2   . ILE   B 1 288  ? 203.741 150.391 155.217 1.00 33.71  ? 288  ILE   B CG2   1 
ATOM   6756  C  CD1   . ILE   B 1 288  ? 203.730 147.771 153.360 1.00 38.38  ? 288  ILE   B CD1   1 
ATOM   6757  N  N     . LYS   B 1 289  ? 203.060 153.175 153.705 1.00 39.41  ? 289  LYS   B N     1 
ATOM   6758  C  CA    . LYS   B 1 289  ? 203.440 154.506 154.159 1.00 39.13  ? 289  LYS   B CA    1 
ATOM   6759  C  C     . LYS   B 1 289  ? 202.402 155.568 153.828 1.00 35.91  ? 289  LYS   B C     1 
ATOM   6760  O  O     . LYS   B 1 289  ? 202.524 156.700 154.309 1.00 41.41  ? 289  LYS   B O     1 
ATOM   6761  C  CB    . LYS   B 1 289  ? 204.788 154.901 153.550 1.00 41.61  ? 289  LYS   B CB    1 
ATOM   6762  C  CG    . LYS   B 1 289  ? 205.398 156.156 154.153 1.00 36.24  ? 289  LYS   B CG    1 
ATOM   6763  C  CD    . LYS   B 1 289  ? 206.887 156.241 153.864 1.00 33.78  ? 289  LYS   B CD    1 
ATOM   6764  C  CE    . LYS   B 1 289  ? 207.262 155.394 152.661 1.00 36.41  ? 289  LYS   B CE    1 
ATOM   6765  N  NZ    . LYS   B 1 289  ? 208.578 155.782 152.081 1.00 43.34  ? 289  LYS   B NZ    1 
ATOM   6766  N  N     . GLY   B 1 290  ? 201.392 155.239 153.028 1.00 29.23  ? 290  GLY   B N     1 
ATOM   6767  C  CA    . GLY   B 1 290  ? 200.412 156.222 152.615 1.00 31.88  ? 290  GLY   B CA    1 
ATOM   6768  C  C     . GLY   B 1 290  ? 199.052 156.074 153.264 1.00 30.81  ? 290  GLY   B C     1 
ATOM   6769  O  O     . GLY   B 1 290  ? 198.375 157.072 153.527 1.00 34.26  ? 290  GLY   B O     1 
ATOM   6770  N  N     . VAL   B 1 291  ? 198.633 154.836 153.526 1.00 34.20  ? 291  VAL   B N     1 
ATOM   6771  C  CA    . VAL   B 1 291  ? 197.310 154.543 154.062 1.00 35.89  ? 291  VAL   B CA    1 
ATOM   6772  C  C     . VAL   B 1 291  ? 197.395 153.854 155.419 1.00 34.04  ? 291  VAL   B C     1 
ATOM   6773  O  O     . VAL   B 1 291  ? 196.750 154.276 156.383 1.00 43.52  ? 291  VAL   B O     1 
ATOM   6774  C  CB    . VAL   B 1 291  ? 196.476 153.698 153.073 1.00 33.49  ? 291  VAL   B CB    1 
ATOM   6775  C  CG1   . VAL   B 1 291  ? 195.037 153.593 153.545 1.00 26.50  ? 291  VAL   B CG1   1 
ATOM   6776  C  CG2   . VAL   B 1 291  ? 196.543 154.294 151.676 1.00 30.86  ? 291  VAL   B CG2   1 
ATOM   6777  N  N     . LEU   B 1 292  ? 198.189 152.786 155.512 1.00 24.64  ? 292  LEU   B N     1 
ATOM   6778  C  CA    . LEU   B 1 292  ? 198.249 152.018 156.752 1.00 29.59  ? 292  LEU   B CA    1 
ATOM   6779  C  C     . LEU   B 1 292  ? 198.743 152.875 157.910 1.00 26.74  ? 292  LEU   B C     1 
ATOM   6780  O  O     . LEU   B 1 292  ? 198.091 152.963 158.958 1.00 36.65  ? 292  LEU   B O     1 
ATOM   6781  C  CB    . LEU   B 1 292  ? 199.152 150.799 156.564 1.00 33.51  ? 292  LEU   B CB    1 
ATOM   6782  C  CG    . LEU   B 1 292  ? 199.292 149.851 157.756 1.00 30.36  ? 292  LEU   B CG    1 
ATOM   6783  C  CD1   . LEU   B 1 292  ? 197.944 149.260 158.131 1.00 26.63  ? 292  LEU   B CD1   1 
ATOM   6784  C  CD2   . LEU   B 1 292  ? 200.297 148.752 157.456 1.00 32.17  ? 292  LEU   B CD2   1 
ATOM   6785  N  N     . VAL   B 1 293  ? 199.892 153.529 157.733 1.00 31.74  ? 293  VAL   B N     1 
ATOM   6786  C  CA    . VAL   B 1 293  ? 200.495 154.286 158.826 1.00 37.98  ? 293  VAL   B CA    1 
ATOM   6787  C  C     . VAL   B 1 293  ? 199.599 155.452 159.223 1.00 35.83  ? 293  VAL   B C     1 
ATOM   6788  O  O     . VAL   B 1 293  ? 199.359 155.696 160.410 1.00 35.23  ? 293  VAL   B O     1 
ATOM   6789  C  CB    . VAL   B 1 293  ? 201.905 154.766 158.435 1.00 35.88  ? 293  VAL   B CB    1 
ATOM   6790  C  CG1   . VAL   B 1 293  ? 202.359 155.893 159.352 1.00 33.06  ? 293  VAL   B CG1   1 
ATOM   6791  C  CG2   . VAL   B 1 293  ? 202.888 153.609 158.475 1.00 30.54  ? 293  VAL   B CG2   1 
ATOM   6792  N  N     . ARG   B 1 294  ? 199.097 156.194 158.234 1.00 30.32  ? 294  ARG   B N     1 
ATOM   6793  C  CA    . ARG   B 1 294  ? 198.271 157.357 158.542 1.00 29.21  ? 294  ARG   B CA    1 
ATOM   6794  C  C     . ARG   B 1 294  ? 196.978 156.948 159.236 1.00 34.07  ? 294  ARG   B C     1 
ATOM   6795  O  O     . ARG   B 1 294  ? 196.566 157.580 160.215 1.00 42.00  ? 294  ARG   B O     1 
ATOM   6796  C  CB    . ARG   B 1 294  ? 197.976 158.144 157.266 1.00 30.46  ? 294  ARG   B CB    1 
ATOM   6797  C  CG    . ARG   B 1 294  ? 199.190 158.851 156.689 1.00 36.93  ? 294  ARG   B CG    1 
ATOM   6798  C  CD    . ARG   B 1 294  ? 198.809 159.789 155.560 1.00 35.94  ? 294  ARG   B CD    1 
ATOM   6799  N  NE    . ARG   B 1 294  ? 197.683 160.643 155.916 1.00 38.62  ? 294  ARG   B NE    1 
ATOM   6800  C  CZ    . ARG   B 1 294  ? 197.795 161.914 156.278 1.00 40.80  ? 294  ARG   B CZ    1 
ATOM   6801  N  NH1   . ARG   B 1 294  ? 198.974 162.509 156.356 1.00 33.54  ? 294  ARG   B NH1   1 
ATOM   6802  N  NH2   . ARG   B 1 294  ? 196.697 162.605 156.569 1.00 41.74  ? 294  ARG   B NH2   1 
ATOM   6803  N  N     . CYS   B 1 295  ? 196.326 155.890 158.749 1.00 37.59  ? 295  CYS   B N     1 
ATOM   6804  C  CA    . CYS   B 1 295  ? 195.100 155.424 159.388 1.00 36.48  ? 295  CYS   B CA    1 
ATOM   6805  C  C     . CYS   B 1 295  ? 195.361 154.972 160.819 1.00 33.86  ? 295  CYS   B C     1 
ATOM   6806  O  O     . CYS   B 1 295  ? 194.607 155.321 161.736 1.00 38.51  ? 295  CYS   B O     1 
ATOM   6807  C  CB    . CYS   B 1 295  ? 194.482 154.289 158.571 1.00 37.24  ? 295  CYS   B CB    1 
ATOM   6808  S  SG    . CYS   B 1 295  ? 193.569 154.828 157.108 1.00 49.18  ? 295  CYS   B SG    1 
ATOM   6809  N  N     . MET   B 1 296  ? 196.432 154.203 161.031 1.00 37.44  ? 296  MET   B N     1 
ATOM   6810  C  CA    . MET   B 1 296  ? 196.740 153.727 162.375 1.00 34.05  ? 296  MET   B CA    1 
ATOM   6811  C  C     . MET   B 1 296  ? 197.055 154.884 163.314 1.00 35.41  ? 296  MET   B C     1 
ATOM   6812  O  O     . MET   B 1 296  ? 196.640 154.878 164.479 1.00 41.59  ? 296  MET   B O     1 
ATOM   6813  C  CB    . MET   B 1 296  ? 197.905 152.739 162.328 1.00 35.26  ? 296  MET   B CB    1 
ATOM   6814  C  CG    . MET   B 1 296  ? 197.519 151.356 161.833 1.00 40.10  ? 296  MET   B CG    1 
ATOM   6815  S  SD    . MET   B 1 296  ? 198.895 150.194 161.848 1.00 59.15  ? 296  MET   B SD    1 
ATOM   6816  C  CE    . MET   B 1 296  ? 200.283 151.322 161.871 1.00 40.60  ? 296  MET   B CE    1 
ATOM   6817  N  N     . LEU   B 1 297  ? 197.790 155.885 162.829 1.00 34.76  ? 297  LEU   B N     1 
ATOM   6818  C  CA    . LEU   B 1 297  ? 198.165 157.002 163.688 1.00 30.19  ? 297  LEU   B CA    1 
ATOM   6819  C  C     . LEU   B 1 297  ? 196.982 157.914 163.978 1.00 30.14  ? 297  LEU   B C     1 
ATOM   6820  O  O     . LEU   B 1 297  ? 196.907 158.501 165.063 1.00 39.45  ? 297  LEU   B O     1 
ATOM   6821  C  CB    . LEU   B 1 297  ? 199.305 157.792 163.050 1.00 34.11  ? 297  LEU   B CB    1 
ATOM   6822  C  CG    . LEU   B 1 297  ? 200.678 157.127 163.158 1.00 37.00  ? 297  LEU   B CG    1 
ATOM   6823  C  CD1   . LEU   B 1 297  ? 201.776 158.063 162.689 1.00 35.83  ? 297  LEU   B CD1   1 
ATOM   6824  C  CD2   . LEU   B 1 297  ? 200.931 156.678 164.585 1.00 34.87  ? 297  LEU   B CD2   1 
ATOM   6825  N  N     . ASN   B 1 298  ? 196.054 158.051 163.031 1.00 29.83  ? 298  ASN   B N     1 
ATOM   6826  C  CA    . ASN   B 1 298  ? 194.880 158.879 163.271 1.00 31.91  ? 298  ASN   B CA    1 
ATOM   6827  C  C     . ASN   B 1 298  ? 193.876 158.186 164.183 1.00 28.78  ? 298  ASN   B C     1 
ATOM   6828  O  O     . ASN   B 1 298  ? 193.225 158.851 164.995 1.00 34.24  ? 298  ASN   B O     1 
ATOM   6829  C  CB    . ASN   B 1 298  ? 194.221 159.253 161.943 1.00 36.37  ? 298  ASN   B CB    1 
ATOM   6830  C  CG    . ASN   B 1 298  ? 193.386 160.515 162.041 1.00 37.51  ? 298  ASN   B CG    1 
ATOM   6831  O  OD1   . ASN   B 1 298  ? 193.768 161.476 162.706 1.00 32.76  ? 298  ASN   B OD1   1 
ATOM   6832  N  ND2   . ASN   B 1 298  ? 192.240 160.517 161.371 1.00 39.74  ? 298  ASN   B ND2   1 
ATOM   6833  N  N     . ILE   B 1 299  ? 193.741 156.863 164.070 1.00 22.84  ? 299  ILE   B N     1 
ATOM   6834  C  CA    . ILE   B 1 299  ? 192.800 156.144 164.922 1.00 24.66  ? 299  ILE   B CA    1 
ATOM   6835  C  C     . ILE   B 1 299  ? 193.256 156.177 166.376 1.00 33.19  ? 299  ILE   B C     1 
ATOM   6836  O  O     . ILE   B 1 299  ? 192.440 156.324 167.293 1.00 46.16  ? 299  ILE   B O     1 
ATOM   6837  C  CB    . ILE   B 1 299  ? 192.615 154.703 164.417 1.00 34.83  ? 299  ILE   B CB    1 
ATOM   6838  C  CG1   . ILE   B 1 299  ? 192.029 154.704 163.004 1.00 32.11  ? 299  ILE   B CG1   1 
ATOM   6839  C  CG2   . ILE   B 1 299  ? 191.714 153.927 165.357 1.00 35.11  ? 299  ILE   B CG2   1 
ATOM   6840  C  CD1   . ILE   B 1 299  ? 191.748 153.325 162.456 1.00 28.20  ? 299  ILE   B CD1   1 
ATOM   6841  N  N     . TRP   B 1 300  ? 194.557 156.038 166.612 1.00 38.00  ? 300  TRP   B N     1 
ATOM   6842  C  CA    . TRP   B 1 300  ? 195.085 156.047 167.968 1.00 31.59  ? 300  TRP   B CA    1 
ATOM   6843  C  C     . TRP   B 1 300  ? 195.238 157.476 168.470 1.00 36.51  ? 300  TRP   B C     1 
ATOM   6844  O  O     . TRP   B 1 300  ? 195.863 158.313 167.811 1.00 37.65  ? 300  TRP   B O     1 
ATOM   6845  C  CB    . TRP   B 1 300  ? 196.428 155.321 168.025 1.00 24.78  ? 300  TRP   B CB    1 
ATOM   6846  C  CG    . TRP   B 1 300  ? 196.298 153.837 168.096 1.00 32.38  ? 300  TRP   B CG    1 
ATOM   6847  C  CD1   . TRP   B 1 300  ? 195.232 153.130 168.567 1.00 36.25  ? 300  TRP   B CD1   1 
ATOM   6848  C  CD2   . TRP   B 1 300  ? 197.266 152.871 167.675 1.00 33.26  ? 300  TRP   B CD2   1 
ATOM   6849  N  NE1   . TRP   B 1 300  ? 195.478 151.783 168.471 1.00 40.09  ? 300  TRP   B NE1   1 
ATOM   6850  C  CE2   . TRP   B 1 300  ? 196.720 151.597 167.925 1.00 35.87  ? 300  TRP   B CE2   1 
ATOM   6851  C  CE3   . TRP   B 1 300  ? 198.542 152.959 167.112 1.00 30.04  ? 300  TRP   B CE3   1 
ATOM   6852  C  CZ2   . TRP   B 1 300  ? 197.405 150.423 167.632 1.00 32.53  ? 300  TRP   B CZ2   1 
ATOM   6853  C  CZ3   . TRP   B 1 300  ? 199.219 151.793 166.823 1.00 34.51  ? 300  TRP   B CZ3   1 
ATOM   6854  C  CH2   . TRP   B 1 300  ? 198.650 150.541 167.083 1.00 36.36  ? 300  TRP   B CH2   1 
ATOM   6855  N  N     . GLY   B 1 301  ? 194.663 157.751 169.635 1.00 41.53  ? 301  GLY   B N     1 
ATOM   6856  C  CA    . GLY   B 1 301  ? 194.753 159.047 170.279 1.00 38.18  ? 301  GLY   B CA    1 
ATOM   6857  C  C     . GLY   B 1 301  ? 195.294 158.893 171.687 1.00 43.07  ? 301  GLY   B C     1 
ATOM   6858  O  O     . GLY   B 1 301  ? 196.178 158.079 171.952 1.00 42.74  ? 301  GLY   B O     1 
ATOM   6859  N  N     . VAL   B 1 302  ? 194.750 159.687 172.606 1.00 51.73  ? 302  VAL   B N     1 
ATOM   6860  C  CA    . VAL   B 1 302  ? 195.173 159.632 174.001 1.00 42.20  ? 302  VAL   B CA    1 
ATOM   6861  C  C     . VAL   B 1 302  ? 194.284 158.697 174.824 1.00 43.25  ? 302  VAL   B C     1 
ATOM   6862  O  O     . VAL   B 1 302  ? 194.336 158.720 176.052 1.00 48.04  ? 302  VAL   B O     1 
ATOM   6863  C  CB    . VAL   B 1 302  ? 195.237 161.029 174.635 1.00 41.32  ? 302  VAL   B CB    1 
ATOM   6864  C  CG1   . VAL   B 1 302  ? 195.891 162.026 173.688 1.00 44.51  ? 302  VAL   B CG1   1 
ATOM   6865  C  CG2   . VAL   B 1 302  ? 193.850 161.479 175.056 1.00 43.05  ? 302  VAL   B CG2   1 
ATOM   6866  N  N     . MET   B 1 303  ? 193.471 157.872 174.169 1.00 46.09  ? 303  MET   B N     1 
ATOM   6867  C  CA    . MET   B 1 303  ? 192.611 156.934 174.877 1.00 43.00  ? 303  MET   B CA    1 
ATOM   6868  C  C     . MET   B 1 303  ? 193.329 155.650 175.274 1.00 44.49  ? 303  MET   B C     1 
ATOM   6869  O  O     . MET   B 1 303  ? 192.805 154.893 176.098 1.00 48.11  ? 303  MET   B O     1 
ATOM   6870  C  CB    . MET   B 1 303  ? 191.383 156.598 174.021 1.00 38.75  ? 303  MET   B CB    1 
ATOM   6871  C  CG    . MET   B 1 303  ? 190.772 155.233 174.292 1.00 40.00  ? 303  MET   B CG    1 
ATOM   6872  S  SD    . MET   B 1 303  ? 189.530 155.271 175.598 1.00 53.86  ? 303  MET   B SD    1 
ATOM   6873  C  CE    . MET   B 1 303  ? 188.483 156.609 175.036 1.00 43.11  ? 303  MET   B CE    1 
ATOM   6874  N  N     . LEU   B 1 304  ? 194.522 155.401 174.737 1.00 45.30  ? 304  LEU   B N     1 
ATOM   6875  C  CA    . LEU   B 1 304  ? 195.282 154.208 175.081 1.00 41.60  ? 304  LEU   B CA    1 
ATOM   6876  C  C     . LEU   B 1 304  ? 196.112 154.373 176.347 1.00 44.09  ? 304  LEU   B C     1 
ATOM   6877  O  O     . LEU   B 1 304  ? 196.659 153.382 176.841 1.00 48.23  ? 304  LEU   B O     1 
ATOM   6878  C  CB    . LEU   B 1 304  ? 196.203 153.815 173.921 1.00 45.46  ? 304  LEU   B CB    1 
ATOM   6879  C  CG    . LEU   B 1 304  ? 195.729 152.667 173.026 1.00 48.64  ? 304  LEU   B CG    1 
ATOM   6880  C  CD1   . LEU   B 1 304  ? 196.635 152.520 171.815 1.00 45.64  ? 304  LEU   B CD1   1 
ATOM   6881  C  CD2   . LEU   B 1 304  ? 195.659 151.365 173.808 1.00 45.50  ? 304  LEU   B CD2   1 
ATOM   6882  N  N     . PHE   B 1 305  ? 196.219 155.592 176.882 1.00 48.98  ? 305  PHE   B N     1 
ATOM   6883  C  CA    . PHE   B 1 305  ? 197.013 155.846 178.075 1.00 46.03  ? 305  PHE   B CA    1 
ATOM   6884  C  C     . PHE   B 1 305  ? 196.300 156.704 179.111 1.00 46.78  ? 305  PHE   B C     1 
ATOM   6885  O  O     . PHE   B 1 305  ? 196.852 156.914 180.197 1.00 52.69  ? 305  PHE   B O     1 
ATOM   6886  C  CB    . PHE   B 1 305  ? 198.339 156.527 177.701 1.00 48.66  ? 305  PHE   B CB    1 
ATOM   6887  C  CG    . PHE   B 1 305  ? 199.062 155.872 176.560 1.00 54.49  ? 305  PHE   B CG    1 
ATOM   6888  C  CD1   . PHE   B 1 305  ? 199.486 154.558 176.651 1.00 52.53  ? 305  PHE   B CD1   1 
ATOM   6889  C  CD2   . PHE   B 1 305  ? 199.320 156.574 175.394 1.00 51.46  ? 305  PHE   B CD2   1 
ATOM   6890  C  CE1   . PHE   B 1 305  ? 200.152 153.956 175.601 1.00 49.52  ? 305  PHE   B CE1   1 
ATOM   6891  C  CE2   . PHE   B 1 305  ? 199.986 155.978 174.342 1.00 50.30  ? 305  PHE   B CE2   1 
ATOM   6892  C  CZ    . PHE   B 1 305  ? 200.402 154.667 174.445 1.00 49.73  ? 305  PHE   B CZ    1 
ATOM   6893  N  N     . ILE   B 1 306  ? 195.102 157.206 178.815 1.00 45.48  ? 306  ILE   B N     1 
ATOM   6894  C  CA    . ILE   B 1 306  ? 194.413 158.170 179.663 1.00 45.11  ? 306  ILE   B CA    1 
ATOM   6895  C  C     . ILE   B 1 306  ? 193.042 157.661 180.092 1.00 51.36  ? 306  ILE   B C     1 
ATOM   6896  O  O     . ILE   B 1 306  ? 192.675 157.749 181.268 1.00 55.23  ? 306  ILE   B O     1 
ATOM   6897  C  CB    . ILE   B 1 306  ? 194.287 159.542 178.963 1.00 47.41  ? 306  ILE   B CB    1 
ATOM   6898  C  CG1   . ILE   B 1 306  ? 195.517 160.403 179.253 1.00 46.47  ? 306  ILE   B CG1   1 
ATOM   6899  C  CG2   . ILE   B 1 306  ? 193.017 160.252 179.406 1.00 50.94  ? 306  ILE   B CG2   1 
ATOM   6900  C  CD1   . ILE   B 1 306  ? 195.521 161.725 178.520 1.00 44.65  ? 306  ILE   B CD1   1 
ATOM   6901  N  N     . ARG   B 1 307  ? 192.267 157.124 179.149 1.00 48.51  ? 307  ARG   B N     1 
ATOM   6902  C  CA    . ARG   B 1 307  ? 190.868 156.813 179.396 1.00 48.28  ? 307  ARG   B CA    1 
ATOM   6903  C  C     . ARG   B 1 307  ? 190.519 155.336 179.307 1.00 48.47  ? 307  ARG   B C     1 
ATOM   6904  O  O     . ARG   B 1 307  ? 189.491 154.936 179.863 1.00 56.53  ? 307  ARG   B O     1 
ATOM   6905  C  CB    . ARG   B 1 307  ? 189.970 157.583 178.414 1.00 51.44  ? 307  ARG   B CB    1 
ATOM   6906  C  CG    . ARG   B 1 307  ? 189.401 158.873 178.977 1.00 51.48  ? 307  ARG   B CG    1 
ATOM   6907  C  CD    . ARG   B 1 307  ? 188.491 158.605 180.165 1.00 58.81  ? 307  ARG   B CD    1 
ATOM   6908  N  NE    . ARG   B 1 307  ? 187.339 159.499 180.190 1.00 64.20  ? 307  ARG   B NE    1 
ATOM   6909  C  CZ    . ARG   B 1 307  ? 187.418 160.822 180.249 1.00 63.20  ? 307  ARG   B CZ    1 
ATOM   6910  N  NH1   . ARG   B 1 307  ? 188.585 161.443 180.287 1.00 58.51  ? 307  ARG   B NH1   1 
ATOM   6911  N  NH2   . ARG   B 1 307  ? 186.298 161.538 180.275 1.00 60.54  ? 307  ARG   B NH2   1 
ATOM   6912  N  N     . LEU   B 1 308  ? 191.328 154.518 178.633 1.00 40.55  ? 308  LEU   B N     1 
ATOM   6913  C  CA    . LEU   B 1 308  ? 190.977 153.109 178.489 1.00 48.30  ? 308  LEU   B CA    1 
ATOM   6914  C  C     . LEU   B 1 308  ? 190.940 152.411 179.842 1.00 48.84  ? 308  LEU   B C     1 
ATOM   6915  O  O     . LEU   B 1 308  ? 190.054 151.589 180.102 1.00 48.67  ? 308  LEU   B O     1 
ATOM   6916  C  CB    . LEU   B 1 308  ? 191.960 152.412 177.550 1.00 47.54  ? 308  LEU   B CB    1 
ATOM   6917  C  CG    . LEU   B 1 308  ? 191.572 150.981 177.175 1.00 44.78  ? 308  LEU   B CG    1 
ATOM   6918  C  CD1   . LEU   B 1 308  ? 190.114 150.924 176.755 1.00 45.47  ? 308  LEU   B CD1   1 
ATOM   6919  C  CD2   . LEU   B 1 308  ? 192.468 150.444 176.073 1.00 45.79  ? 308  LEU   B CD2   1 
ATOM   6920  N  N     . SER   B 1 309  ? 191.898 152.724 180.717 1.00 51.77  ? 309  SER   B N     1 
ATOM   6921  C  CA    . SER   B 1 309  ? 191.897 152.136 182.051 1.00 48.10  ? 309  SER   B CA    1 
ATOM   6922  C  C     . SER   B 1 309  ? 190.642 152.524 182.821 1.00 45.15  ? 309  SER   B C     1 
ATOM   6923  O  O     . SER   B 1 309  ? 190.009 151.676 183.461 1.00 45.98  ? 309  SER   B O     1 
ATOM   6924  C  CB    . SER   B 1 309  ? 193.148 152.567 182.815 1.00 47.26  ? 309  SER   B CB    1 
ATOM   6925  O  OG    . SER   B 1 309  ? 193.239 153.979 182.890 1.00 48.37  ? 309  SER   B OG    1 
ATOM   6926  N  N     . TRP   B 1 310  ? 190.264 153.803 182.769 1.00 48.59  ? 310  TRP   B N     1 
ATOM   6927  C  CA    . TRP   B 1 310  ? 189.062 154.239 183.471 1.00 49.48  ? 310  TRP   B CA    1 
ATOM   6928  C  C     . TRP   B 1 310  ? 187.821 153.564 182.905 1.00 49.12  ? 310  TRP   B C     1 
ATOM   6929  O  O     . TRP   B 1 310  ? 186.914 153.187 183.655 1.00 53.32  ? 310  TRP   B O     1 
ATOM   6930  C  CB    . TRP   B 1 310  ? 188.922 155.757 183.395 1.00 48.53  ? 310  TRP   B CB    1 
ATOM   6931  C  CG    . TRP   B 1 310  ? 187.643 156.249 183.990 1.00 50.86  ? 310  TRP   B CG    1 
ATOM   6932  C  CD1   . TRP   B 1 310  ? 187.398 156.504 185.307 1.00 52.63  ? 310  TRP   B CD1   1 
ATOM   6933  C  CD2   . TRP   B 1 310  ? 186.422 156.523 183.294 1.00 50.07  ? 310  TRP   B CD2   1 
ATOM   6934  N  NE1   . TRP   B 1 310  ? 186.104 156.932 185.474 1.00 54.79  ? 310  TRP   B NE1   1 
ATOM   6935  C  CE2   . TRP   B 1 310  ? 185.483 156.951 184.253 1.00 51.97  ? 310  TRP   B CE2   1 
ATOM   6936  C  CE3   . TRP   B 1 310  ? 186.032 156.454 181.954 1.00 49.03  ? 310  TRP   B CE3   1 
ATOM   6937  C  CZ2   . TRP   B 1 310  ? 184.181 157.308 183.914 1.00 48.79  ? 310  TRP   B CZ2   1 
ATOM   6938  C  CZ3   . TRP   B 1 310  ? 184.739 156.808 181.620 1.00 47.95  ? 310  TRP   B CZ3   1 
ATOM   6939  C  CH2   . TRP   B 1 310  ? 183.829 157.230 182.596 1.00 50.24  ? 310  TRP   B CH2   1 
ATOM   6940  N  N     . ILE   B 1 311  ? 187.756 153.414 181.582 1.00 45.66  ? 311  ILE   B N     1 
ATOM   6941  C  CA    . ILE   B 1 311  ? 186.611 152.748 180.969 1.00 44.10  ? 311  ILE   B CA    1 
ATOM   6942  C  C     . ILE   B 1 311  ? 186.534 151.297 181.423 1.00 48.05  ? 311  ILE   B C     1 
ATOM   6943  O  O     . ILE   B 1 311  ? 185.457 150.793 181.764 1.00 52.36  ? 311  ILE   B O     1 
ATOM   6944  C  CB    . ILE   B 1 311  ? 186.685 152.862 179.436 1.00 51.81  ? 311  ILE   B CB    1 
ATOM   6945  C  CG1   . ILE   B 1 311  ? 186.393 154.298 179.001 1.00 48.88  ? 311  ILE   B CG1   1 
ATOM   6946  C  CG2   . ILE   B 1 311  ? 185.717 151.887 178.779 1.00 47.12  ? 311  ILE   B CG2   1 
ATOM   6947  C  CD1   . ILE   B 1 311  ? 186.294 154.476 177.508 1.00 47.57  ? 311  ILE   B CD1   1 
ATOM   6948  N  N     . VAL   B 1 312  ? 187.673 150.602 181.439 1.00 48.88  ? 312  VAL   B N     1 
ATOM   6949  C  CA    . VAL   B 1 312  ? 187.676 149.204 181.860 1.00 50.02  ? 312  VAL   B CA    1 
ATOM   6950  C  C     . VAL   B 1 312  ? 187.285 149.090 183.328 1.00 54.81  ? 312  VAL   B C     1 
ATOM   6951  O  O     . VAL   B 1 312  ? 186.635 148.122 183.738 1.00 53.39  ? 312  VAL   B O     1 
ATOM   6952  C  CB    . VAL   B 1 312  ? 189.048 148.563 181.588 1.00 51.76  ? 312  VAL   B CB    1 
ATOM   6953  C  CG1   . VAL   B 1 312  ? 189.312 147.440 182.576 1.00 51.03  ? 312  VAL   B CG1   1 
ATOM   6954  C  CG2   . VAL   B 1 312  ? 189.115 148.047 180.163 1.00 53.30  ? 312  VAL   B CG2   1 
ATOM   6955  N  N     . GLY   B 1 313  ? 187.693 150.058 184.147 1.00 55.31  ? 313  GLY   B N     1 
ATOM   6956  C  CA    . GLY   B 1 313  ? 187.259 150.058 185.534 1.00 50.64  ? 313  GLY   B CA    1 
ATOM   6957  C  C     . GLY   B 1 313  ? 185.761 150.263 185.671 1.00 51.91  ? 313  GLY   B C     1 
ATOM   6958  O  O     . GLY   B 1 313  ? 185.087 149.540 186.410 1.00 58.34  ? 313  GLY   B O     1 
ATOM   6959  N  N     . GLN   B 1 314  ? 185.220 151.247 184.950 1.00 50.64  ? 314  GLN   B N     1 
ATOM   6960  C  CA    . GLN   B 1 314  ? 183.802 151.573 185.075 1.00 46.65  ? 314  GLN   B CA    1 
ATOM   6961  C  C     . GLN   B 1 314  ? 182.923 150.413 184.627 1.00 47.96  ? 314  GLN   B C     1 
ATOM   6962  O  O     . GLN   B 1 314  ? 181.922 150.095 185.280 1.00 62.88  ? 314  GLN   B O     1 
ATOM   6963  C  CB    . GLN   B 1 314  ? 183.484 152.829 184.266 1.00 51.14  ? 314  GLN   B CB    1 
ATOM   6964  C  CG    . GLN   B 1 314  ? 183.831 154.128 184.971 1.00 54.69  ? 314  GLN   B CG    1 
ATOM   6965  C  CD    . GLN   B 1 314  ? 182.795 154.525 186.002 1.00 56.46  ? 314  GLN   B CD    1 
ATOM   6966  O  OE1   . GLN   B 1 314  ? 181.637 154.117 185.924 1.00 58.19  ? 314  GLN   B OE1   1 
ATOM   6967  N  NE2   . GLN   B 1 314  ? 183.207 155.329 186.975 1.00 55.84  ? 314  GLN   B NE2   1 
ATOM   6968  N  N     . ALA   B 1 315  ? 183.274 149.774 183.517 1.00 43.17  ? 315  ALA   B N     1 
ATOM   6969  C  CA    . ALA   B 1 315  ? 182.547 148.622 183.005 1.00 47.36  ? 315  ALA   B CA    1 
ATOM   6970  C  C     . ALA   B 1 315  ? 183.495 147.438 182.909 1.00 51.37  ? 315  ALA   B C     1 
ATOM   6971  O  O     . ALA   B 1 315  ? 184.645 147.587 182.486 1.00 56.25  ? 315  ALA   B O     1 
ATOM   6972  C  CB    . ALA   B 1 315  ? 181.928 148.917 181.636 1.00 48.68  ? 315  ALA   B CB    1 
ATOM   6973  N  N     . GLY   B 1 316  ? 183.002 146.259 183.276 1.00 53.20  ? 316  GLY   B N     1 
ATOM   6974  C  CA    . GLY   B 1 316  ? 183.855 145.093 183.388 1.00 53.68  ? 316  GLY   B CA    1 
ATOM   6975  C  C     . GLY   B 1 316  ? 184.620 144.774 182.121 1.00 54.05  ? 316  GLY   B C     1 
ATOM   6976  O  O     . GLY   B 1 316  ? 184.415 145.414 181.086 1.00 59.92  ? 316  GLY   B O     1 
ATOM   6977  N  N     . ILE   B 1 317  ? 185.508 143.781 182.192 1.00 48.79  ? 317  ILE   B N     1 
ATOM   6978  C  CA    . ILE   B 1 317  ? 186.312 143.418 181.028 1.00 45.20  ? 317  ILE   B CA    1 
ATOM   6979  C  C     . ILE   B 1 317  ? 185.409 143.067 179.854 1.00 48.67  ? 317  ILE   B C     1 
ATOM   6980  O  O     . ILE   B 1 317  ? 185.605 143.543 178.728 1.00 56.09  ? 317  ILE   B O     1 
ATOM   6981  C  CB    . ILE   B 1 317  ? 187.262 142.259 181.375 1.00 46.62  ? 317  ILE   B CB    1 
ATOM   6982  C  CG1   . ILE   B 1 317  ? 188.440 142.762 182.211 1.00 53.68  ? 317  ILE   B CG1   1 
ATOM   6983  C  CG2   . ILE   B 1 317  ? 187.750 141.571 180.110 1.00 47.35  ? 317  ILE   B CG2   1 
ATOM   6984  C  CD1   . ILE   B 1 317  ? 189.378 141.665 182.668 1.00 49.87  ? 317  ILE   B CD1   1 
ATOM   6985  N  N     . GLY   B 1 318  ? 184.397 142.235 180.103 1.00 48.00  ? 318  GLY   B N     1 
ATOM   6986  C  CA    . GLY   B 1 318  ? 183.511 141.824 179.028 1.00 53.48  ? 318  GLY   B CA    1 
ATOM   6987  C  C     . GLY   B 1 318  ? 182.759 142.985 178.408 1.00 51.52  ? 318  GLY   B C     1 
ATOM   6988  O  O     . GLY   B 1 318  ? 182.647 143.081 177.185 1.00 53.68  ? 318  GLY   B O     1 
ATOM   6989  N  N     . LEU   B 1 319  ? 182.236 143.887 179.241 1.00 48.58  ? 319  LEU   B N     1 
ATOM   6990  C  CA    . LEU   B 1 319  ? 181.457 145.003 178.715 1.00 48.34  ? 319  LEU   B CA    1 
ATOM   6991  C  C     . LEU   B 1 319  ? 182.337 145.980 177.945 1.00 50.50  ? 319  LEU   B C     1 
ATOM   6992  O  O     . LEU   B 1 319  ? 181.925 146.508 176.904 1.00 57.87  ? 319  LEU   B O     1 
ATOM   6993  C  CB    . LEU   B 1 319  ? 180.726 145.714 179.853 1.00 49.81  ? 319  LEU   B CB    1 
ATOM   6994  C  CG    . LEU   B 1 319  ? 179.327 145.181 180.173 1.00 46.08  ? 319  LEU   B CG    1 
ATOM   6995  C  CD1   . LEU   B 1 319  ? 178.460 146.266 180.791 1.00 47.41  ? 319  LEU   B CD1   1 
ATOM   6996  C  CD2   . LEU   B 1 319  ? 178.670 144.605 178.928 1.00 42.77  ? 319  LEU   B CD2   1 
ATOM   6997  N  N     . SER   B 1 320  ? 183.552 146.236 178.435 1.00 48.91  ? 320  SER   B N     1 
ATOM   6998  C  CA    . SER   B 1 320  ? 184.469 147.098 177.698 1.00 53.79  ? 320  SER   B CA    1 
ATOM   6999  C  C     . SER   B 1 320  ? 184.845 146.477 176.359 1.00 50.40  ? 320  SER   B C     1 
ATOM   7000  O  O     . SER   B 1 320  ? 184.906 147.170 175.335 1.00 51.69  ? 320  SER   B O     1 
ATOM   7001  C  CB    . SER   B 1 320  ? 185.719 147.374 178.534 1.00 51.99  ? 320  SER   B CB    1 
ATOM   7002  O  OG    . SER   B 1 320  ? 186.446 146.182 178.770 1.00 54.93  ? 320  SER   B OG    1 
ATOM   7003  N  N     . VAL   B 1 321  ? 185.095 145.165 176.347 1.00 45.21  ? 321  VAL   B N     1 
ATOM   7004  C  CA    . VAL   B 1 321  ? 185.398 144.482 175.094 1.00 44.29  ? 321  VAL   B CA    1 
ATOM   7005  C  C     . VAL   B 1 321  ? 184.215 144.576 174.139 1.00 48.29  ? 321  VAL   B C     1 
ATOM   7006  O  O     . VAL   B 1 321  ? 184.387 144.769 172.931 1.00 54.69  ? 321  VAL   B O     1 
ATOM   7007  C  CB    . VAL   B 1 321  ? 185.795 143.019 175.365 1.00 44.38  ? 321  VAL   B CB    1 
ATOM   7008  C  CG1   . VAL   B 1 321  ? 185.672 142.192 174.097 1.00 45.92  ? 321  VAL   B CG1   1 
ATOM   7009  C  CG2   . VAL   B 1 321  ? 187.209 142.946 175.918 1.00 46.97  ? 321  VAL   B CG2   1 
ATOM   7010  N  N     . LEU   B 1 322  ? 183.002 144.518 174.681 1.00 46.67  ? 322  LEU   B N     1 
ATOM   7011  C  CA    . LEU   B 1 322  ? 181.792 144.660 173.829 1.00 47.40  ? 322  LEU   B CA    1 
ATOM   7012  C  C     . LEU   B 1 322  ? 181.756 146.072 173.236 1.00 48.84  ? 322  LEU   B C     1 
ATOM   7013  O  O     . LEU   B 1 322  ? 181.426 146.199 172.048 1.00 56.79  ? 322  LEU   B O     1 
ATOM   7014  C  CB    . LEU   B 1 322  ? 180.544 144.389 174.671 1.00 46.64  ? 322  LEU   B CB    1 
ATOM   7015  C  CG    . LEU   B 1 322  ? 179.212 144.658 173.976 1.00 50.55  ? 322  LEU   B CG    1 
ATOM   7016  C  CD1   . LEU   B 1 322  ? 178.999 143.689 172.824 1.00 54.32  ? 322  LEU   B CD1   1 
ATOM   7017  C  CD2   . LEU   B 1 322  ? 178.059 144.573 174.963 1.00 53.23  ? 322  LEU   B CD2   1 
ATOM   7018  N  N     . VAL   B 1 323  ? 182.070 147.091 174.033 1.00 41.10  ? 323  VAL   B N     1 
ATOM   7019  C  CA    . VAL   B 1 323  ? 181.993 148.495 173.541 1.00 42.94  ? 323  VAL   B CA    1 
ATOM   7020  C  C     . VAL   B 1 323  ? 182.967 148.636 172.371 1.00 48.29  ? 323  VAL   B C     1 
ATOM   7021  O  O     . VAL   B 1 323  ? 182.558 149.156 171.291 1.00 53.60  ? 323  VAL   B O     1 
ATOM   7022  C  CB    . VAL   B 1 323  ? 182.321 149.492 174.666 1.00 45.10  ? 323  VAL   B CB    1 
ATOM   7023  C  CG1   . VAL   B 1 323  ? 182.621 150.882 174.128 1.00 45.92  ? 323  VAL   B CG1   1 
ATOM   7024  C  CG2   . VAL   B 1 323  ? 181.219 149.546 175.710 1.00 45.83  ? 323  VAL   B CG2   1 
ATOM   7025  N  N     . ILE   B 1 324  ? 184.196 148.159 172.566 1.00 40.23  ? 324  ILE   B N     1 
ATOM   7026  C  CA    . ILE   B 1 324  ? 185.225 148.251 171.497 1.00 38.39  ? 324  ILE   B CA    1 
ATOM   7027  C  C     . ILE   B 1 324  ? 184.672 147.556 170.257 1.00 43.25  ? 324  ILE   B C     1 
ATOM   7028  O  O     . ILE   B 1 324  ? 184.701 148.166 169.190 1.00 43.02  ? 324  ILE   B O     1 
ATOM   7029  C  CB    . ILE   B 1 324  ? 186.544 147.608 171.968 1.00 37.04  ? 324  ILE   B CB    1 
ATOM   7030  C  CG1   . ILE   B 1 324  ? 187.031 148.213 173.287 1.00 41.57  ? 324  ILE   B CG1   1 
ATOM   7031  C  CG2   . ILE   B 1 324  ? 187.608 147.693 170.886 1.00 34.80  ? 324  ILE   B CG2   1 
ATOM   7032  C  CD1   . ILE   B 1 324  ? 188.310 147.602 173.805 1.00 44.27  ? 324  ILE   B CD1   1 
ATOM   7033  N  N     . MET   B 1 325  ? 184.146 146.346 170.412 1.00 44.44  ? 325  MET   B N     1 
ATOM   7034  C  CA    . MET   B 1 325  ? 183.662 145.554 169.255 1.00 39.43  ? 325  MET   B CA    1 
ATOM   7035  C  C     . MET   B 1 325  ? 182.540 146.293 168.514 1.00 42.46  ? 325  MET   B C     1 
ATOM   7036  O  O     . MET   B 1 325  ? 182.537 146.233 167.288 1.00 53.12  ? 325  MET   B O     1 
ATOM   7037  C  CB    . MET   B 1 325  ? 183.163 144.186 169.726 1.00 40.46  ? 325  MET   B CB    1 
ATOM   7038  N  N     . MET   B 1 326  ? 181.616 146.936 169.228 1.00 34.27  ? 326  MET   B N     1 
ATOM   7039  C  CA    . MET   B 1 326  ? 180.482 147.663 168.590 1.00 40.79  ? 326  MET   B CA    1 
ATOM   7040  C  C     . MET   B 1 326  ? 181.001 148.895 167.837 1.00 47.94  ? 326  MET   B C     1 
ATOM   7041  O  O     . MET   B 1 326  ? 180.517 149.188 166.696 1.00 45.11  ? 326  MET   B O     1 
ATOM   7042  C  CB    . MET   B 1 326  ? 179.476 148.107 169.654 1.00 30.00  ? 326  MET   B CB    1 
ATOM   7043  C  CG    . MET   B 1 326  ? 178.759 146.957 170.330 1.00 30.00  ? 326  MET   B CG    1 
ATOM   7044  S  SD    . MET   B 1 326  ? 177.802 147.498 171.769 1.00 30.00  ? 326  MET   B SD    1 
ATOM   7045  C  CE    . MET   B 1 326  ? 176.732 148.722 171.016 1.00 30.00  ? 326  MET   B CE    1 
ATOM   7046  N  N     . ALA   B 1 327  ? 181.955 149.598 168.443 1.00 40.07  ? 327  ALA   B N     1 
ATOM   7047  C  CA    . ALA   B 1 327  ? 182.553 150.745 167.732 1.00 38.94  ? 327  ALA   B CA    1 
ATOM   7048  C  C     . ALA   B 1 327  ? 183.236 150.228 166.463 1.00 41.27  ? 327  ALA   B C     1 
ATOM   7049  O  O     . ALA   B 1 327  ? 183.179 150.919 165.418 1.00 40.95  ? 327  ALA   B O     1 
ATOM   7050  C  CB    . ALA   B 1 327  ? 183.519 151.440 168.649 1.00 41.16  ? 327  ALA   B CB    1 
ATOM   7051  N  N     . THR   B 1 328  ? 183.846 149.048 166.550 1.00 36.74  ? 328  THR   B N     1 
ATOM   7052  C  CA    . THR   B 1 328  ? 184.571 148.467 165.397 1.00 37.53  ? 328  THR   B CA    1 
ATOM   7053  C  C     . THR   B 1 328  ? 183.555 148.092 164.320 1.00 37.44  ? 328  THR   B C     1 
ATOM   7054  O  O     . THR   B 1 328  ? 183.876 148.242 163.140 1.00 42.49  ? 328  THR   B O     1 
ATOM   7055  C  CB    . THR   B 1 328  ? 185.432 147.293 165.868 1.00 36.92  ? 328  THR   B CB    1 
ATOM   7056  O  OG1   . THR   B 1 328  ? 186.324 147.802 166.858 1.00 37.54  ? 328  THR   B OG1   1 
ATOM   7057  C  CG2   . THR   B 1 328  ? 186.213 146.639 164.750 1.00 38.97  ? 328  THR   B CG2   1 
ATOM   7058  N  N     . VAL   B 1 329  ? 182.395 147.587 164.716 1.00 30.53  ? 329  VAL   B N     1 
ATOM   7059  C  CA    . VAL   B 1 329  ? 181.316 147.292 163.741 1.00 36.09  ? 329  VAL   B CA    1 
ATOM   7060  C  C     . VAL   B 1 329  ? 181.008 148.599 163.026 1.00 35.10  ? 329  VAL   B C     1 
ATOM   7061  O  O     . VAL   B 1 329  ? 181.025 148.609 161.793 1.00 41.93  ? 329  VAL   B O     1 
ATOM   7062  C  CB    . VAL   B 1 329  ? 180.063 146.741 164.442 1.00 38.45  ? 329  VAL   B CB    1 
ATOM   7063  C  CG1   . VAL   B 1 329  ? 178.829 146.827 163.558 1.00 34.64  ? 329  VAL   B CG1   1 
ATOM   7064  C  CG2   . VAL   B 1 329  ? 180.274 145.321 164.939 1.00 41.34  ? 329  VAL   B CG2   1 
ATOM   7065  N  N     . VAL   B 1 330  ? 180.768 149.669 163.778 1.00 34.88  ? 330  VAL   B N     1 
ATOM   7066  C  CA    . VAL   B 1 330  ? 180.393 150.909 163.045 1.00 31.51  ? 330  VAL   B CA    1 
ATOM   7067  C  C     . VAL   B 1 330  ? 181.528 151.272 162.086 1.00 31.92  ? 330  VAL   B C     1 
ATOM   7068  O  O     . VAL   B 1 330  ? 181.222 151.625 160.950 1.00 35.99  ? 330  VAL   B O     1 
ATOM   7069  C  CB    . VAL   B 1 330  ? 180.056 152.068 163.997 1.00 36.98  ? 330  VAL   B CB    1 
ATOM   7070  C  CG1   . VAL   B 1 330  ? 179.761 153.354 163.242 1.00 33.84  ? 330  VAL   B CG1   1 
ATOM   7071  C  CG2   . VAL   B 1 330  ? 178.893 151.712 164.909 1.00 35.07  ? 330  VAL   B CG2   1 
ATOM   7072  N  N     . THR   B 1 331  ? 182.785 151.159 162.515 1.00 37.26  ? 331  THR   B N     1 
ATOM   7073  C  CA    . THR   B 1 331  ? 183.925 151.595 161.661 1.00 29.39  ? 331  THR   B CA    1 
ATOM   7074  C  C     . THR   B 1 331  ? 184.184 150.604 160.515 1.00 23.89  ? 331  THR   B C     1 
ATOM   7075  O  O     . THR   B 1 331  ? 184.472 151.073 159.396 1.00 28.30  ? 331  THR   B O     1 
ATOM   7076  C  CB    . THR   B 1 331  ? 185.158 151.870 162.527 1.00 32.46  ? 331  THR   B CB    1 
ATOM   7077  O  OG1   . THR   B 1 331  ? 185.475 150.680 163.247 1.00 40.52  ? 331  THR   B OG1   1 
ATOM   7078  C  CG2   . THR   B 1 331  ? 184.936 153.020 163.483 1.00 32.40  ? 331  THR   B CG2   1 
ATOM   7079  N  N     . THR   B 1 332  ? 184.094 149.299 160.784 1.00 26.12  ? 332  THR   B N     1 
ATOM   7080  C  CA    . THR   B 1 332  ? 184.339 148.315 159.737 1.00 25.39  ? 332  THR   B CA    1 
ATOM   7081  C  C     . THR   B 1 332  ? 183.305 148.423 158.627 1.00 26.22  ? 332  THR   B C     1 
ATOM   7082  O  O     . THR   B 1 332  ? 183.642 148.297 157.445 1.00 32.42  ? 332  THR   B O     1 
ATOM   7083  C  CB    . THR   B 1 332  ? 184.339 146.906 160.330 1.00 27.66  ? 332  THR   B CB    1 
ATOM   7084  O  OG1   . THR   B 1 332  ? 185.141 146.886 161.518 1.00 41.65  ? 332  THR   B OG1   1 
ATOM   7085  C  CG2   . THR   B 1 332  ? 184.899 145.906 159.333 1.00 28.46  ? 332  THR   B CG2   1 
ATOM   7086  N  N     . ILE   B 1 333  ? 182.040 148.647 158.983 1.00 27.76  ? 333  ILE   B N     1 
ATOM   7087  C  CA    . ILE   B 1 333  ? 181.026 148.874 157.956 1.00 28.16  ? 333  ILE   B CA    1 
ATOM   7088  C  C     . ILE   B 1 333  ? 181.375 150.117 157.147 1.00 30.32  ? 333  ILE   B C     1 
ATOM   7089  O  O     . ILE   B 1 333  ? 181.303 150.123 155.909 1.00 30.55  ? 333  ILE   B O     1 
ATOM   7090  C  CB    . ILE   B 1 333  ? 179.629 148.984 158.592 1.00 26.89  ? 333  ILE   B CB    1 
ATOM   7091  C  CG1   . ILE   B 1 333  ? 179.227 147.651 159.225 1.00 29.81  ? 333  ILE   B CG1   1 
ATOM   7092  C  CG2   . ILE   B 1 333  ? 178.605 149.413 157.553 1.00 26.58  ? 333  ILE   B CG2   1 
ATOM   7093  C  CD1   . ILE   B 1 333  ? 177.796 147.611 159.708 1.00 32.93  ? 333  ILE   B CD1   1 
ATOM   7094  N  N     . THR   B 1 334  ? 181.771 151.190 157.839 1.00 34.71  ? 334  THR   B N     1 
ATOM   7095  C  CA    . THR   B 1 334  ? 182.159 152.406 157.130 1.00 24.05  ? 334  THR   B CA    1 
ATOM   7096  C  C     . THR   B 1 334  ? 183.344 152.154 156.204 1.00 29.36  ? 334  THR   B C     1 
ATOM   7097  O  O     . THR   B 1 334  ? 183.372 152.646 155.071 1.00 38.65  ? 334  THR   B O     1 
ATOM   7098  C  CB    . THR   B 1 334  ? 182.483 153.519 158.127 1.00 31.84  ? 334  THR   B CB    1 
ATOM   7099  O  OG1   . THR   B 1 334  ? 181.420 153.628 159.082 1.00 39.03  ? 334  THR   B OG1   1 
ATOM   7100  C  CG2   . THR   B 1 334  ? 182.646 154.848 157.406 1.00 26.39  ? 334  THR   B CG2   1 
ATOM   7101  N  N     . GLY   B 1 335  ? 184.334 151.391 156.670 1.00 31.69  ? 335  GLY   B N     1 
ATOM   7102  C  CA    . GLY   B 1 335  ? 185.496 151.110 155.843 1.00 26.05  ? 335  GLY   B CA    1 
ATOM   7103  C  C     . GLY   B 1 335  ? 185.170 150.251 154.636 1.00 28.76  ? 335  GLY   B C     1 
ATOM   7104  O  O     . GLY   B 1 335  ? 185.720 150.456 153.551 1.00 34.30  ? 335  GLY   B O     1 
ATOM   7105  N  N     . LEU   B 1 336  ? 184.288 149.266 154.810 1.00 25.82  ? 336  LEU   B N     1 
ATOM   7106  C  CA    . LEU   B 1 336  ? 183.861 148.460 153.673 1.00 20.72  ? 336  LEU   B CA    1 
ATOM   7107  C  C     . LEU   B 1 336  ? 183.162 149.324 152.634 1.00 23.06  ? 336  LEU   B C     1 
ATOM   7108  O  O     . LEU   B 1 336  ? 183.426 149.204 151.430 1.00 34.14  ? 336  LEU   B O     1 
ATOM   7109  C  CB    . LEU   B 1 336  ? 182.939 147.333 154.139 1.00 27.08  ? 336  LEU   B CB    1 
ATOM   7110  C  CG    . LEU   B 1 336  ? 183.576 146.162 154.887 1.00 26.13  ? 336  LEU   B CG    1 
ATOM   7111  C  CD1   . LEU   B 1 336  ? 182.530 145.112 155.220 1.00 25.80  ? 336  LEU   B CD1   1 
ATOM   7112  C  CD2   . LEU   B 1 336  ? 184.707 145.555 154.080 1.00 22.55  ? 336  LEU   B CD2   1 
ATOM   7113  N  N     . SER   B 1 337  ? 182.273 150.215 153.082 1.00 28.31  ? 337  SER   B N     1 
ATOM   7114  C  CA    . SER   B 1 337  ? 181.615 151.116 152.142 1.00 22.55  ? 337  SER   B CA    1 
ATOM   7115  C  C     . SER   B 1 337  ? 182.627 152.024 151.452 1.00 23.07  ? 337  SER   B C     1 
ATOM   7116  O  O     . SER   B 1 337  ? 182.513 152.294 150.251 1.00 33.35  ? 337  SER   B O     1 
ATOM   7117  C  CB    . SER   B 1 337  ? 180.549 151.942 152.861 1.00 27.02  ? 337  SER   B CB    1 
ATOM   7118  O  OG    . SER   B 1 337  ? 179.536 151.111 153.398 1.00 29.34  ? 337  SER   B OG    1 
ATOM   7119  N  N     . THR   B 1 338  ? 183.627 152.504 152.195 1.00 25.16  ? 338  THR   B N     1 
ATOM   7120  C  CA    . THR   B 1 338  ? 184.643 153.368 151.601 1.00 26.74  ? 338  THR   B CA    1 
ATOM   7121  C  C     . THR   B 1 338  ? 185.440 152.633 150.531 1.00 22.28  ? 338  THR   B C     1 
ATOM   7122  O  O     . THR   B 1 338  ? 185.705 153.182 149.457 1.00 33.26  ? 338  THR   B O     1 
ATOM   7123  C  CB    . THR   B 1 338  ? 185.578 153.904 152.685 1.00 23.27  ? 338  THR   B CB    1 
ATOM   7124  O  OG1   . THR   B 1 338  ? 184.843 154.751 153.575 1.00 27.52  ? 338  THR   B OG1   1 
ATOM   7125  C  CG2   . THR   B 1 338  ? 186.717 154.697 152.064 1.00 21.81  ? 338  THR   B CG2   1 
ATOM   7126  N  N     . SER   B 1 339  ? 185.838 151.391 150.810 1.00 23.38  ? 339  SER   B N     1 
ATOM   7127  C  CA    . SER   B 1 339  ? 186.576 150.617 149.818 1.00 30.82  ? 339  SER   B CA    1 
ATOM   7128  C  C     . SER   B 1 339  ? 185.721 150.350 148.586 1.00 19.86  ? 339  SER   B C     1 
ATOM   7129  O  O     . SER   B 1 339  ? 186.206 150.437 147.450 1.00 26.48  ? 339  SER   B O     1 
ATOM   7130  C  CB    . SER   B 1 339  ? 187.065 149.305 150.431 1.00 28.11  ? 339  SER   B CB    1 
ATOM   7131  O  OG    . SER   B 1 339  ? 186.028 148.658 151.143 1.00 30.96  ? 339  SER   B OG    1 
ATOM   7132  N  N     . ALA   B 1 340  ? 184.440 150.033 148.790 1.00 24.02  ? 340  ALA   B N     1 
ATOM   7133  C  CA    . ALA   B 1 340  ? 183.548 149.828 147.655 1.00 25.78  ? 340  ALA   B CA    1 
ATOM   7134  C  C     . ALA   B 1 340  ? 183.436 151.089 146.810 1.00 28.15  ? 340  ALA   B C     1 
ATOM   7135  O  O     . ALA   B 1 340  ? 183.466 151.025 145.576 1.00 32.10  ? 340  ALA   B O     1 
ATOM   7136  C  CB    . ALA   B 1 340  ? 182.170 149.383 148.142 1.00 23.03  ? 340  ALA   B CB    1 
ATOM   7137  N  N     . ILE   B 1 341  ? 183.309 152.248 147.457 1.00 29.65  ? 341  ILE   B N     1 
ATOM   7138  C  CA    . ILE   B 1 341  ? 183.173 153.498 146.720 1.00 19.61  ? 341  ILE   B CA    1 
ATOM   7139  C  C     . ILE   B 1 341  ? 184.489 153.945 146.098 1.00 22.35  ? 341  ILE   B C     1 
ATOM   7140  O  O     . ILE   B 1 341  ? 184.481 154.760 145.168 1.00 36.69  ? 341  ILE   B O     1 
ATOM   7141  C  CB    . ILE   B 1 341  ? 182.625 154.601 147.640 1.00 24.47  ? 341  ILE   B CB    1 
ATOM   7142  C  CG1   . ILE   B 1 341  ? 181.516 155.382 146.939 1.00 33.15  ? 341  ILE   B CG1   1 
ATOM   7143  C  CG2   . ILE   B 1 341  ? 183.738 155.536 148.078 1.00 36.97  ? 341  ILE   B CG2   1 
ATOM   7144  C  CD1   . ILE   B 1 341  ? 180.208 154.628 146.852 1.00 37.50  ? 341  ILE   B CD1   1 
ATOM   7145  N  N     . ALA   B 1 342  ? 185.620 153.437 146.584 1.00 21.33  ? 342  ALA   B N     1 
ATOM   7146  C  CA    . ALA   B 1 342  ? 186.919 153.827 146.057 1.00 22.04  ? 342  ALA   B CA    1 
ATOM   7147  C  C     . ALA   B 1 342  ? 187.452 152.877 144.996 1.00 27.39  ? 342  ALA   B C     1 
ATOM   7148  O  O     . ALA   B 1 342  ? 188.400 153.235 144.290 1.00 36.99  ? 342  ALA   B O     1 
ATOM   7149  C  CB    . ALA   B 1 342  ? 187.944 153.930 147.193 1.00 25.99  ? 342  ALA   B CB    1 
ATOM   7150  N  N     . THR   B 1 343  ? 186.872 151.684 144.863 1.00 30.87  ? 343  THR   B N     1 
ATOM   7151  C  CA    . THR   B 1 343  ? 187.300 150.725 143.853 1.00 25.20  ? 343  THR   B CA    1 
ATOM   7152  C  C     . THR   B 1 343  ? 186.416 150.751 142.610 1.00 29.12  ? 343  THR   B C     1 
ATOM   7153  O  O     . THR   B 1 343  ? 186.201 149.710 141.981 1.00 31.25  ? 343  THR   B O     1 
ATOM   7154  C  CB    . THR   B 1 343  ? 187.343 149.313 144.438 1.00 28.39  ? 343  THR   B CB    1 
ATOM   7155  O  OG1   . THR   B 1 343  ? 186.155 149.071 145.203 1.00 33.11  ? 343  THR   B OG1   1 
ATOM   7156  C  CG2   . THR   B 1 343  ? 188.564 149.140 145.323 1.00 26.56  ? 343  THR   B CG2   1 
ATOM   7157  N  N     . ASN   B 1 344  ? 185.902 151.924 142.239 1.00 30.08  ? 344  ASN   B N     1 
ATOM   7158  C  CA    . ASN   B 1 344  ? 185.058 152.060 141.056 1.00 24.98  ? 344  ASN   B CA    1 
ATOM   7159  C  C     . ASN   B 1 344  ? 185.797 152.714 139.894 1.00 32.08  ? 344  ASN   B C     1 
ATOM   7160  O  O     . ASN   B 1 344  ? 185.911 152.127 138.817 1.00 44.76  ? 344  ASN   B O     1 
ATOM   7161  C  CB    . ASN   B 1 344  ? 183.792 152.855 141.399 1.00 29.23  ? 344  ASN   B CB    1 
ATOM   7162  C  CG    . ASN   B 1 344  ? 182.758 152.803 140.293 1.00 31.48  ? 344  ASN   B CG    1 
ATOM   7163  O  OD1   . ASN   B 1 344  ? 182.815 151.940 139.420 1.00 40.80  ? 344  ASN   B OD1   1 
ATOM   7164  N  ND2   . ASN   B 1 344  ? 181.802 153.724 140.328 1.00 26.05  ? 344  ASN   B ND2   1 
ATOM   7165  N  N     . GLY   B 1 345  ? 186.314 153.924 140.095 1.00 40.99  ? 345  GLY   B N     1 
ATOM   7166  C  CA    . GLY   B 1 345  ? 187.079 154.610 139.076 1.00 38.28  ? 345  GLY   B CA    1 
ATOM   7167  C  C     . GLY   B 1 345  ? 188.372 155.162 139.648 1.00 39.36  ? 345  GLY   B C     1 
ATOM   7168  O  O     . GLY   B 1 345  ? 188.700 154.948 140.816 1.00 47.55  ? 345  GLY   B O     1 
ATOM   7169  N  N     . PHE   B 1 346  ? 189.091 155.885 138.797 1.00 39.63  ? 346  PHE   B N     1 
ATOM   7170  C  CA    . PHE   B 1 346  ? 190.318 156.530 139.238 1.00 41.63  ? 346  PHE   B CA    1 
ATOM   7171  C  C     . PHE   B 1 346  ? 189.978 157.722 140.121 1.00 49.44  ? 346  PHE   B C     1 
ATOM   7172  O  O     . PHE   B 1 346  ? 189.207 158.601 139.726 1.00 52.61  ? 346  PHE   B O     1 
ATOM   7173  C  CB    . PHE   B 1 346  ? 191.148 156.975 138.035 1.00 39.11  ? 346  PHE   B CB    1 
ATOM   7174  C  CG    . PHE   B 1 346  ? 192.278 157.896 138.390 1.00 48.19  ? 346  PHE   B CG    1 
ATOM   7175  C  CD1   . PHE   B 1 346  ? 193.403 157.416 139.038 1.00 49.71  ? 346  PHE   B CD1   1 
ATOM   7176  C  CD2   . PHE   B 1 346  ? 192.210 159.245 138.089 1.00 48.84  ? 346  PHE   B CD2   1 
ATOM   7177  C  CE1   . PHE   B 1 346  ? 194.442 158.262 139.370 1.00 47.43  ? 346  PHE   B CE1   1 
ATOM   7178  C  CE2   . PHE   B 1 346  ? 193.245 160.096 138.420 1.00 50.91  ? 346  PHE   B CE2   1 
ATOM   7179  C  CZ    . PHE   B 1 346  ? 194.363 159.603 139.060 1.00 49.86  ? 346  PHE   B CZ    1 
ATOM   7180  N  N     . VAL   B 1 347  ? 190.558 157.757 141.318 1.00 45.27  ? 347  VAL   B N     1 
ATOM   7181  C  CA    . VAL   B 1 347  ? 190.283 158.813 142.286 1.00 43.54  ? 347  VAL   B CA    1 
ATOM   7182  C  C     . VAL   B 1 347  ? 191.287 159.929 142.019 1.00 44.63  ? 347  VAL   B C     1 
ATOM   7183  O  O     . VAL   B 1 347  ? 192.462 159.823 142.369 1.00 51.83  ? 347  VAL   B O     1 
ATOM   7184  C  CB    . VAL   B 1 347  ? 190.363 158.303 143.725 1.00 44.71  ? 347  VAL   B CB    1 
ATOM   7185  C  CG1   . VAL   B 1 347  ? 189.577 159.215 144.651 1.00 49.13  ? 347  VAL   B CG1   1 
ATOM   7186  C  CG2   . VAL   B 1 347  ? 189.841 156.880 143.808 1.00 43.07  ? 347  VAL   B CG2   1 
ATOM   7187  N  N     . ARG   B 1 348  ? 190.812 161.008 141.395 1.00 52.82  ? 348  ARG   B N     1 
ATOM   7188  C  CA    . ARG   B 1 348  ? 191.711 162.075 140.970 1.00 58.23  ? 348  ARG   B CA    1 
ATOM   7189  C  C     . ARG   B 1 348  ? 192.447 162.679 142.159 1.00 63.43  ? 348  ARG   B C     1 
ATOM   7190  O  O     . ARG   B 1 348  ? 193.679 162.787 142.153 1.00 64.28  ? 348  ARG   B O     1 
ATOM   7191  C  CB    . ARG   B 1 348  ? 190.923 163.149 140.222 1.00 52.82  ? 348  ARG   B CB    1 
ATOM   7192  C  CG    . ARG   B 1 348  ? 191.709 163.849 139.132 1.00 54.92  ? 348  ARG   B CG    1 
ATOM   7193  C  CD    . ARG   B 1 348  ? 190.786 164.331 138.026 1.00 60.38  ? 348  ARG   B CD    1 
ATOM   7194  N  NE    . ARG   B 1 348  ? 190.561 163.318 137.000 1.00 64.53  ? 348  ARG   B NE    1 
ATOM   7195  C  CZ    . ARG   B 1 348  ? 191.519 162.694 136.328 1.00 63.89  ? 348  ARG   B CZ    1 
ATOM   7196  N  NH1   . ARG   B 1 348  ? 192.798 162.964 136.531 1.00 60.33  ? 348  ARG   B NH1   1 
ATOM   7197  N  NH2   . ARG   B 1 348  ? 191.184 161.777 135.425 1.00 63.29  ? 348  ARG   B NH2   1 
ATOM   7198  N  N     . GLY   B 1 349  ? 191.707 163.076 143.190 1.00 44.43  ? 349  GLY   B N     1 
ATOM   7199  C  CA    . GLY   B 1 349  ? 192.310 163.683 144.358 1.00 36.42  ? 349  GLY   B CA    1 
ATOM   7200  C  C     . GLY   B 1 349  ? 191.364 163.766 145.536 1.00 43.12  ? 349  GLY   B C     1 
ATOM   7201  O  O     . GLY   B 1 349  ? 190.578 162.845 145.773 1.00 54.35  ? 349  GLY   B O     1 
ATOM   7202  N  N     . GLY   B 1 350  ? 191.428 164.868 146.279 1.00 46.56  ? 350  GLY   B N     1 
ATOM   7203  C  CA    . GLY   B 1 350  ? 190.580 165.041 147.441 1.00 41.89  ? 350  GLY   B CA    1 
ATOM   7204  C  C     . GLY   B 1 350  ? 190.634 163.858 148.384 1.00 44.70  ? 350  GLY   B C     1 
ATOM   7205  O  O     . GLY   B 1 350  ? 191.622 163.118 148.404 1.00 52.75  ? 350  GLY   B O     1 
ATOM   7206  N  N     . GLY   B 1 351  ? 189.576 163.661 149.162 1.00 28.46  ? 351  GLY   B N     1 
ATOM   7207  C  CA    . GLY   B 1 351  ? 189.521 162.543 150.082 1.00 34.13  ? 351  GLY   B CA    1 
ATOM   7208  C  C     . GLY   B 1 351  ? 188.178 161.848 150.044 1.00 37.96  ? 351  GLY   B C     1 
ATOM   7209  O  O     . GLY   B 1 351  ? 187.702 161.469 148.971 1.00 41.38  ? 351  GLY   B O     1 
ATOM   7210  N  N     . ALA   B 1 352  ? 187.557 161.667 151.211 1.00 43.67  ? 352  ALA   B N     1 
ATOM   7211  C  CA    . ALA   B 1 352  ? 186.196 161.146 151.234 1.00 39.08  ? 352  ALA   B CA    1 
ATOM   7212  C  C     . ALA   B 1 352  ? 185.244 162.063 150.481 1.00 34.98  ? 352  ALA   B C     1 
ATOM   7213  O  O     . ALA   B 1 352  ? 184.210 161.610 149.979 1.00 37.92  ? 352  ALA   B O     1 
ATOM   7214  C  CB    . ALA   B 1 352  ? 185.726 160.956 152.675 1.00 35.07  ? 352  ALA   B CB    1 
ATOM   7215  N  N     . TYR   B 1 353  ? 185.579 163.353 150.388 1.00 34.99  ? 353  TYR   B N     1 
ATOM   7216  C  CA    . TYR   B 1 353  ? 184.738 164.282 149.642 1.00 33.01  ? 353  TYR   B CA    1 
ATOM   7217  C  C     . TYR   B 1 353  ? 184.656 163.896 148.173 1.00 34.45  ? 353  TYR   B C     1 
ATOM   7218  O  O     . TYR   B 1 353  ? 183.572 163.910 147.582 1.00 37.71  ? 353  TYR   B O     1 
ATOM   7219  C  CB    . TYR   B 1 353  ? 185.272 165.707 149.772 1.00 34.06  ? 353  TYR   B CB    1 
ATOM   7220  C  CG    . TYR   B 1 353  ? 184.929 166.564 148.575 1.00 30.31  ? 353  TYR   B CG    1 
ATOM   7221  C  CD1   . TYR   B 1 353  ? 185.913 166.976 147.688 1.00 34.81  ? 353  TYR   B CD1   1 
ATOM   7222  C  CD2   . TYR   B 1 353  ? 183.619 166.947 148.323 1.00 33.07  ? 353  TYR   B CD2   1 
ATOM   7223  C  CE1   . TYR   B 1 353  ? 185.603 167.751 146.589 1.00 36.70  ? 353  TYR   B CE1   1 
ATOM   7224  C  CE2   . TYR   B 1 353  ? 183.300 167.722 147.228 1.00 27.27  ? 353  TYR   B CE2   1 
ATOM   7225  C  CZ    . TYR   B 1 353  ? 184.295 168.122 146.365 1.00 31.44  ? 353  TYR   B CZ    1 
ATOM   7226  O  OH    . TYR   B 1 353  ? 183.982 168.896 145.272 1.00 35.97  ? 353  TYR   B OH    1 
ATOM   7227  N  N     . TYR   B 1 354  ? 185.795 163.572 147.560 1.00 28.60  ? 354  TYR   B N     1 
ATOM   7228  C  CA    . TYR   B 1 354  ? 185.790 163.207 146.149 1.00 26.49  ? 354  TYR   B CA    1 
ATOM   7229  C  C     . TYR   B 1 354  ? 184.943 161.964 145.916 1.00 37.39  ? 354  TYR   B C     1 
ATOM   7230  O  O     . TYR   B 1 354  ? 184.123 161.917 144.990 1.00 39.89  ? 354  TYR   B O     1 
ATOM   7231  C  CB    . TYR   B 1 354  ? 187.222 162.989 145.658 1.00 24.47  ? 354  TYR   B CB    1 
ATOM   7232  C  CG    . TYR   B 1 354  ? 187.347 162.919 144.153 1.00 36.16  ? 354  TYR   B CG    1 
ATOM   7233  C  CD1   . TYR   B 1 354  ? 187.550 164.067 143.399 1.00 39.08  ? 354  TYR   B CD1   1 
ATOM   7234  C  CD2   . TYR   B 1 354  ? 187.261 161.705 143.487 1.00 33.78  ? 354  TYR   B CD2   1 
ATOM   7235  C  CE1   . TYR   B 1 354  ? 187.663 164.006 142.026 1.00 31.23  ? 354  TYR   B CE1   1 
ATOM   7236  C  CE2   . TYR   B 1 354  ? 187.374 161.635 142.115 1.00 33.57  ? 354  TYR   B CE2   1 
ATOM   7237  C  CZ    . TYR   B 1 354  ? 187.574 162.787 141.389 1.00 33.95  ? 354  TYR   B CZ    1 
ATOM   7238  O  OH    . TYR   B 1 354  ? 187.686 162.721 140.020 1.00 45.80  ? 354  TYR   B OH    1 
ATOM   7239  N  N     . LEU   B 1 355  ? 185.117 160.948 146.762 1.00 33.80  ? 355  LEU   B N     1 
ATOM   7240  C  CA    . LEU   B 1 355  ? 184.332 159.728 146.623 1.00 32.97  ? 355  LEU   B CA    1 
ATOM   7241  C  C     . LEU   B 1 355  ? 182.844 160.017 146.768 1.00 31.15  ? 355  LEU   B C     1 
ATOM   7242  O  O     . LEU   B 1 355  ? 182.033 159.589 145.940 1.00 44.65  ? 355  LEU   B O     1 
ATOM   7243  C  CB    . LEU   B 1 355  ? 184.787 158.699 147.658 1.00 31.64  ? 355  LEU   B CB    1 
ATOM   7244  C  CG    . LEU   B 1 355  ? 186.265 158.309 147.620 1.00 26.45  ? 355  LEU   B CG    1 
ATOM   7245  C  CD1   . LEU   B 1 355  ? 186.612 157.410 148.792 1.00 31.63  ? 355  LEU   B CD1   1 
ATOM   7246  C  CD2   . LEU   B 1 355  ? 186.602 157.623 146.308 1.00 30.26  ? 355  LEU   B CD2   1 
ATOM   7247  N  N     . ILE   B 1 356  ? 182.470 160.771 147.804 1.00 25.48  ? 356  ILE   B N     1 
ATOM   7248  C  CA    . ILE   B 1 356  ? 181.055 161.026 148.062 1.00 32.63  ? 356  ILE   B CA    1 
ATOM   7249  C  C     . ILE   B 1 356  ? 180.437 161.826 146.923 1.00 34.64  ? 356  ILE   B C     1 
ATOM   7250  O  O     . ILE   B 1 356  ? 179.320 161.535 146.474 1.00 38.18  ? 356  ILE   B O     1 
ATOM   7251  C  CB    . ILE   B 1 356  ? 180.878 161.737 149.416 1.00 31.93  ? 356  ILE   B CB    1 
ATOM   7252  C  CG1   . ILE   B 1 356  ? 180.845 160.715 150.554 1.00 33.24  ? 356  ILE   B CG1   1 
ATOM   7253  C  CG2   . ILE   B 1 356  ? 179.611 162.579 149.415 1.00 28.90  ? 356  ILE   B CG2   1 
ATOM   7254  C  CD1   . ILE   B 1 356  ? 180.908 161.334 151.931 1.00 37.19  ? 356  ILE   B CD1   1 
ATOM   7255  N  N     . SER   B 1 357  ? 181.140 162.858 146.450 1.00 29.52  ? 357  SER   B N     1 
ATOM   7256  C  CA    . SER   B 1 357  ? 180.606 163.670 145.364 1.00 28.48  ? 357  SER   B CA    1 
ATOM   7257  C  C     . SER   B 1 357  ? 180.449 162.844 144.096 1.00 28.61  ? 357  SER   B C     1 
ATOM   7258  O  O     . SER   B 1 357  ? 179.351 162.759 143.536 1.00 36.27  ? 357  SER   B O     1 
ATOM   7259  C  CB    . SER   B 1 357  ? 181.508 164.880 145.120 1.00 33.35  ? 357  SER   B CB    1 
ATOM   7260  O  OG    . SER   B 1 357  ? 182.835 164.482 144.825 1.00 33.77  ? 357  SER   B OG    1 
ATOM   7261  N  N     . ARG   B 1 358  ? 181.522 162.174 143.662 1.00 32.55  ? 358  ARG   B N     1 
ATOM   7262  C  CA    . ARG   B 1 358  ? 181.448 161.386 142.439 1.00 25.26  ? 358  ARG   B CA    1 
ATOM   7263  C  C     . ARG   B 1 358  ? 180.447 160.247 142.557 1.00 29.42  ? 358  ARG   B C     1 
ATOM   7264  O  O     . ARG   B 1 358  ? 179.985 159.734 141.533 1.00 43.84  ? 358  ARG   B O     1 
ATOM   7265  C  CB    . ARG   B 1 358  ? 182.829 160.834 142.079 1.00 27.37  ? 358  ARG   B CB    1 
ATOM   7266  C  CG    . ARG   B 1 358  ? 183.710 161.794 141.287 1.00 31.92  ? 358  ARG   B CG    1 
ATOM   7267  C  CD    . ARG   B 1 358  ? 183.603 163.214 141.818 1.00 32.53  ? 358  ARG   B CD    1 
ATOM   7268  N  NE    . ARG   B 1 358  ? 184.243 164.189 140.943 1.00 30.39  ? 358  ARG   B NE    1 
ATOM   7269  C  CZ    . ARG   B 1 358  ? 184.539 165.430 141.303 1.00 34.98  ? 358  ARG   B CZ    1 
ATOM   7270  N  NH1   . ARG   B 1 358  ? 184.256 165.885 142.512 1.00 34.40  ? 358  ARG   B NH1   1 
ATOM   7271  N  NH2   . ARG   B 1 358  ? 185.137 166.234 140.429 1.00 36.54  ? 358  ARG   B NH2   1 
ATOM   7272  N  N     . SER   B 1 359  ? 180.105 159.836 143.779 1.00 26.59  ? 359  SER   B N     1 
ATOM   7273  C  CA    . SER   B 1 359  ? 179.103 158.794 143.958 1.00 26.82  ? 359  SER   B CA    1 
ATOM   7274  C  C     . SER   B 1 359  ? 177.689 159.352 143.838 1.00 35.19  ? 359  SER   B C     1 
ATOM   7275  O  O     . SER   B 1 359  ? 176.913 158.920 142.979 1.00 40.97  ? 359  SER   B O     1 
ATOM   7276  C  CB    . SER   B 1 359  ? 179.296 158.110 145.313 1.00 33.00  ? 359  SER   B CB    1 
ATOM   7277  O  OG    . SER   B 1 359  ? 180.637 157.695 145.486 1.00 43.63  ? 359  SER   B OG    1 
ATOM   7278  N  N     . LEU   B 1 360  ? 177.334 160.314 144.688 1.00 31.82  ? 360  LEU   B N     1 
ATOM   7279  C  CA    . LEU   B 1 360  ? 175.942 160.740 144.793 1.00 36.97  ? 360  LEU   B CA    1 
ATOM   7280  C  C     . LEU   B 1 360  ? 175.786 162.256 144.727 1.00 35.02  ? 360  LEU   B C     1 
ATOM   7281  O  O     . LEU   B 1 360  ? 175.036 162.852 145.505 1.00 49.51  ? 360  LEU   B O     1 
ATOM   7282  C  CB    . LEU   B 1 360  ? 175.295 160.181 146.060 1.00 42.85  ? 360  LEU   B CB    1 
ATOM   7283  C  CG    . LEU   B 1 360  ? 175.951 160.358 147.432 1.00 34.45  ? 360  LEU   B CG    1 
ATOM   7284  C  CD1   . LEU   B 1 360  ? 176.209 161.813 147.772 1.00 40.58  ? 360  LEU   B CD1   1 
ATOM   7285  C  CD2   . LEU   B 1 360  ? 175.082 159.707 148.498 1.00 33.62  ? 360  LEU   B CD2   1 
ATOM   7286  N  N     . GLY   B 1 361  ? 176.463 162.909 143.787 1.00 28.48  ? 361  GLY   B N     1 
ATOM   7287  C  CA    . GLY   B 1 361  ? 176.059 164.231 143.375 1.00 32.00  ? 361  GLY   B CA    1 
ATOM   7288  C  C     . GLY   B 1 361  ? 176.670 165.389 144.139 1.00 36.94  ? 361  GLY   B C     1 
ATOM   7289  O  O     . GLY   B 1 361  ? 177.079 165.278 145.303 1.00 42.08  ? 361  GLY   B O     1 
ATOM   7290  N  N     . PRO   B 1 362  ? 176.703 166.550 143.481 1.00 36.72  ? 362  PRO   B N     1 
ATOM   7291  C  CA    . PRO   B 1 362  ? 177.356 167.720 144.083 1.00 40.61  ? 362  PRO   B CA    1 
ATOM   7292  C  C     . PRO   B 1 362  ? 176.689 168.226 145.348 1.00 42.05  ? 362  PRO   B C     1 
ATOM   7293  O  O     . PRO   B 1 362  ? 177.371 168.829 146.177 1.00 50.42  ? 362  PRO   B O     1 
ATOM   7294  C  CB    . PRO   B 1 362  ? 177.300 168.764 142.960 1.00 42.08  ? 362  PRO   B CB    1 
ATOM   7295  C  CG    . PRO   B 1 362  ? 176.150 168.351 142.118 1.00 45.25  ? 362  PRO   B CG    1 
ATOM   7296  C  CD    . PRO   B 1 362  ? 176.122 166.853 142.162 1.00 41.46  ? 362  PRO   B CD    1 
ATOM   7297  N  N     . GLU   B 1 363  ? 175.391 168.001 145.539 1.00 47.01  ? 363  GLU   B N     1 
ATOM   7298  C  CA    . GLU   B 1 363  ? 174.722 168.527 146.725 1.00 48.59  ? 363  GLU   B CA    1 
ATOM   7299  C  C     . GLU   B 1 363  ? 175.329 167.939 147.995 1.00 51.79  ? 363  GLU   B C     1 
ATOM   7300  O  O     . GLU   B 1 363  ? 175.951 168.651 148.802 1.00 56.37  ? 363  GLU   B O     1 
ATOM   7301  C  CB    . GLU   B 1 363  ? 173.223 168.222 146.664 1.00 47.81  ? 363  GLU   B CB    1 
ATOM   7302  C  CG    . GLU   B 1 363  ? 172.596 168.459 145.297 1.00 49.96  ? 363  GLU   B CG    1 
ATOM   7303  C  CD    . GLU   B 1 363  ? 172.709 167.245 144.389 1.00 59.43  ? 363  GLU   B CD    1 
ATOM   7304  O  OE1   . GLU   B 1 363  ? 173.370 166.264 144.789 1.00 62.58  ? 363  GLU   B OE1   1 
ATOM   7305  O  OE2   . GLU   B 1 363  ? 172.145 167.273 143.275 1.00 58.55  ? 363  GLU   B OE2   1 
ATOM   7306  N  N     . PHE   B 1 364  ? 175.160 166.624 148.161 1.00 47.36  ? 364  PHE   B N     1 
ATOM   7307  C  CA    . PHE   B 1 364  ? 175.777 165.934 149.285 1.00 43.64  ? 364  PHE   B CA    1 
ATOM   7308  C  C     . PHE   B 1 364  ? 177.289 166.079 149.247 1.00 43.31  ? 364  PHE   B C     1 
ATOM   7309  O  O     . PHE   B 1 364  ? 177.932 166.205 150.296 1.00 44.76  ? 364  PHE   B O     1 
ATOM   7310  C  CB    . PHE   B 1 364  ? 175.383 164.457 149.283 1.00 38.49  ? 364  PHE   B CB    1 
ATOM   7311  C  CG    . PHE   B 1 364  ? 173.989 164.193 149.776 1.00 41.38  ? 364  PHE   B CG    1 
ATOM   7312  C  CD1   . PHE   B 1 364  ? 173.574 164.664 151.010 1.00 45.69  ? 364  PHE   B CD1   1 
ATOM   7313  C  CD2   . PHE   B 1 364  ? 173.097 163.464 149.010 1.00 45.84  ? 364  PHE   B CD2   1 
ATOM   7314  C  CE1   . PHE   B 1 364  ? 172.293 164.416 151.467 1.00 43.85  ? 364  PHE   B CE1   1 
ATOM   7315  C  CE2   . PHE   B 1 364  ? 171.816 163.213 149.462 1.00 47.45  ? 364  PHE   B CE2   1 
ATOM   7316  C  CZ    . PHE   B 1 364  ? 171.414 163.689 150.692 1.00 43.34  ? 364  PHE   B CZ    1 
ATOM   7317  N  N     . GLY   B 1 365  ? 177.881 166.061 148.049 1.00 39.44  ? 365  GLY   B N     1 
ATOM   7318  C  CA    . GLY   B 1 365  ? 179.324 166.201 147.964 1.00 41.57  ? 365  GLY   B CA    1 
ATOM   7319  C  C     . GLY   B 1 365  ? 179.821 167.469 148.629 1.00 40.63  ? 365  GLY   B C     1 
ATOM   7320  O  O     . GLY   B 1 365  ? 180.704 167.429 149.486 1.00 46.40  ? 365  GLY   B O     1 
ATOM   7321  N  N     . GLY   B 1 366  ? 179.240 168.612 148.261 1.00 39.60  ? 366  GLY   B N     1 
ATOM   7322  C  CA    . GLY   B 1 366  ? 179.663 169.873 148.841 1.00 43.96  ? 366  GLY   B CA    1 
ATOM   7323  C  C     . GLY   B 1 366  ? 179.335 169.979 150.316 1.00 46.64  ? 366  GLY   B C     1 
ATOM   7324  O  O     . GLY   B 1 366  ? 180.155 170.458 151.108 1.00 53.18  ? 366  GLY   B O     1 
ATOM   7325  N  N     . ALA   B 1 367  ? 178.137 169.539 150.712 1.00 34.42  ? 367  ALA   B N     1 
ATOM   7326  C  CA    . ALA   B 1 367  ? 177.793 169.600 152.130 1.00 38.40  ? 367  ALA   B CA    1 
ATOM   7327  C  C     . ALA   B 1 367  ? 178.808 168.828 152.967 1.00 43.01  ? 367  ALA   B C     1 
ATOM   7328  O  O     . ALA   B 1 367  ? 179.407 169.371 153.910 1.00 45.56  ? 367  ALA   B O     1 
ATOM   7329  C  CB    . ALA   B 1 367  ? 176.381 169.056 152.350 1.00 40.44  ? 367  ALA   B CB    1 
ATOM   7330  N  N     . ILE   B 1 368  ? 179.038 167.562 152.611 1.00 40.64  ? 368  ILE   B N     1 
ATOM   7331  C  CA    . ILE   B 1 368  ? 179.947 166.724 153.379 1.00 38.53  ? 368  ILE   B CA    1 
ATOM   7332  C  C     . ILE   B 1 368  ? 181.374 167.241 153.280 1.00 38.30  ? 368  ILE   B C     1 
ATOM   7333  O  O     . ILE   B 1 368  ? 182.137 167.157 154.244 1.00 47.02  ? 368  ILE   B O     1 
ATOM   7334  C  CB    . ILE   B 1 368  ? 179.837 165.256 152.928 1.00 41.44  ? 368  ILE   B CB    1 
ATOM   7335  C  CG1   . ILE   B 1 368  ? 180.152 164.320 154.097 1.00 44.63  ? 368  ILE   B CG1   1 
ATOM   7336  C  CG2   . ILE   B 1 368  ? 180.760 164.984 151.751 1.00 40.07  ? 368  ILE   B CG2   1 
ATOM   7337  C  CD1   . ILE   B 1 368  ? 179.084 164.286 155.168 1.00 39.57  ? 368  ILE   B CD1   1 
ATOM   7338  N  N     . GLY   B 1 369  ? 181.767 167.780 152.124 1.00 30.85  ? 369  GLY   B N     1 
ATOM   7339  C  CA    . GLY   B 1 369  ? 183.120 168.291 151.995 1.00 32.38  ? 369  GLY   B CA    1 
ATOM   7340  C  C     . GLY   B 1 369  ? 183.381 169.465 152.916 1.00 44.00  ? 369  GLY   B C     1 
ATOM   7341  O  O     . GLY   B 1 369  ? 184.394 169.508 153.619 1.00 48.13  ? 369  GLY   B O     1 
ATOM   7342  N  N     . LEU   B 1 370  ? 182.458 170.429 152.938 1.00 38.02  ? 370  LEU   B N     1 
ATOM   7343  C  CA    . LEU   B 1 370  ? 182.616 171.566 153.838 1.00 36.78  ? 370  LEU   B CA    1 
ATOM   7344  C  C     . LEU   B 1 370  ? 182.650 171.105 155.290 1.00 40.77  ? 370  LEU   B C     1 
ATOM   7345  O  O     . LEU   B 1 370  ? 183.533 171.506 156.065 1.00 46.46  ? 370  LEU   B O     1 
ATOM   7346  C  CB    . LEU   B 1 370  ? 181.487 172.573 153.615 1.00 40.76  ? 370  LEU   B CB    1 
ATOM   7347  C  CG    . LEU   B 1 370  ? 181.838 174.046 153.828 1.00 39.40  ? 370  LEU   B CG    1 
ATOM   7348  C  CD1   . LEU   B 1 370  ? 183.263 174.328 153.385 1.00 39.15  ? 370  LEU   B CD1   1 
ATOM   7349  C  CD2   . LEU   B 1 370  ? 180.859 174.948 153.094 1.00 42.06  ? 370  LEU   B CD2   1 
ATOM   7350  N  N     . ILE   B 1 371  ? 181.708 170.238 155.673 1.00 39.71  ? 371  ILE   B N     1 
ATOM   7351  C  CA    . ILE   B 1 371  ? 181.643 169.809 157.068 1.00 40.34  ? 371  ILE   B CA    1 
ATOM   7352  C  C     . ILE   B 1 371  ? 182.905 169.049 157.457 1.00 36.75  ? 371  ILE   B C     1 
ATOM   7353  O  O     . ILE   B 1 371  ? 183.462 169.259 158.540 1.00 40.15  ? 371  ILE   B O     1 
ATOM   7354  C  CB    . ILE   B 1 371  ? 180.373 168.976 157.317 1.00 39.46  ? 371  ILE   B CB    1 
ATOM   7355  C  CG1   . ILE   B 1 371  ? 179.217 169.894 157.716 1.00 38.04  ? 371  ILE   B CG1   1 
ATOM   7356  C  CG2   . ILE   B 1 371  ? 180.622 167.936 158.393 1.00 35.30  ? 371  ILE   B CG2   1 
ATOM   7357  C  CD1   . ILE   B 1 371  ? 177.871 169.222 157.712 1.00 42.57  ? 371  ILE   B CD1   1 
ATOM   7358  N  N     . PHE   B 1 372  ? 183.379 168.158 156.584 1.00 34.45  ? 372  PHE   B N     1 
ATOM   7359  C  CA    . PHE   B 1 372  ? 184.550 167.345 156.889 1.00 38.50  ? 372  PHE   B CA    1 
ATOM   7360  C  C     . PHE   B 1 372  ? 185.814 168.192 156.965 1.00 38.22  ? 372  PHE   B C     1 
ATOM   7361  O  O     . PHE   B 1 372  ? 186.664 167.973 157.839 1.00 42.48  ? 372  PHE   B O     1 
ATOM   7362  C  CB    . PHE   B 1 372  ? 184.691 166.245 155.836 1.00 33.26  ? 372  PHE   B CB    1 
ATOM   7363  C  CG    . PHE   B 1 372  ? 185.423 165.028 156.318 1.00 36.96  ? 372  PHE   B CG    1 
ATOM   7364  C  CD1   . PHE   B 1 372  ? 185.029 164.380 157.474 1.00 42.17  ? 372  PHE   B CD1   1 
ATOM   7365  C  CD2   . PHE   B 1 372  ? 186.491 164.517 155.604 1.00 35.97  ? 372  PHE   B CD2   1 
ATOM   7366  C  CE1   . PHE   B 1 372  ? 185.696 163.257 157.918 1.00 39.02  ? 372  PHE   B CE1   1 
ATOM   7367  C  CE2   . PHE   B 1 372  ? 187.160 163.394 156.043 1.00 39.67  ? 372  PHE   B CE2   1 
ATOM   7368  C  CZ    . PHE   B 1 372  ? 186.762 162.763 157.200 1.00 37.40  ? 372  PHE   B CZ    1 
ATOM   7369  N  N     . ALA   B 1 373  ? 185.964 169.160 156.056 1.00 28.92  ? 373  ALA   B N     1 
ATOM   7370  C  CA    . ALA   B 1 373  ? 187.122 170.043 156.120 1.00 34.99  ? 373  ALA   B CA    1 
ATOM   7371  C  C     . ALA   B 1 373  ? 187.127 170.842 157.415 1.00 36.35  ? 373  ALA   B C     1 
ATOM   7372  O  O     . ALA   B 1 373  ? 188.168 170.968 158.075 1.00 40.19  ? 373  ALA   B O     1 
ATOM   7373  C  CB    . ALA   B 1 373  ? 187.141 170.976 154.909 1.00 37.36  ? 373  ALA   B CB    1 
ATOM   7374  N  N     . PHE   B 1 374  ? 185.967 171.380 157.806 1.00 32.99  ? 374  PHE   B N     1 
ATOM   7375  C  CA    . PHE   B 1 374  ? 185.901 172.104 159.071 1.00 31.30  ? 374  PHE   B CA    1 
ATOM   7376  C  C     . PHE   B 1 374  ? 186.213 171.185 160.246 1.00 33.87  ? 374  PHE   B C     1 
ATOM   7377  O  O     . PHE   B 1 374  ? 186.904 171.584 161.192 1.00 40.91  ? 374  PHE   B O     1 
ATOM   7378  C  CB    . PHE   B 1 374  ? 184.525 172.747 159.242 1.00 38.34  ? 374  PHE   B CB    1 
ATOM   7379  C  CG    . PHE   B 1 374  ? 184.498 173.858 160.252 1.00 41.95  ? 374  PHE   B CG    1 
ATOM   7380  C  CD1   . PHE   B 1 374  ? 185.066 175.087 159.965 1.00 37.78  ? 374  PHE   B CD1   1 
ATOM   7381  C  CD2   . PHE   B 1 374  ? 183.907 173.673 161.490 1.00 40.07  ? 374  PHE   B CD2   1 
ATOM   7382  C  CE1   . PHE   B 1 374  ? 185.043 176.110 160.893 1.00 43.74  ? 374  PHE   B CE1   1 
ATOM   7383  C  CE2   . PHE   B 1 374  ? 183.882 174.693 162.421 1.00 39.44  ? 374  PHE   B CE2   1 
ATOM   7384  C  CZ    . PHE   B 1 374  ? 184.450 175.912 162.122 1.00 41.82  ? 374  PHE   B CZ    1 
ATOM   7385  N  N     . ALA   B 1 375  ? 185.705 169.952 160.206 1.00 35.91  ? 375  ALA   B N     1 
ATOM   7386  C  CA    . ALA   B 1 375  ? 185.965 169.011 161.288 1.00 36.89  ? 375  ALA   B CA    1 
ATOM   7387  C  C     . ALA   B 1 375  ? 187.454 168.731 161.429 1.00 37.38  ? 375  ALA   B C     1 
ATOM   7388  O  O     . ALA   B 1 375  ? 187.983 168.714 162.544 1.00 40.60  ? 375  ALA   B O     1 
ATOM   7389  C  CB    . ALA   B 1 375  ? 185.192 167.714 161.051 1.00 38.43  ? 375  ALA   B CB    1 
ATOM   7390  N  N     . ASN   B 1 376  ? 188.149 168.512 160.311 1.00 38.16  ? 376  ASN   B N     1 
ATOM   7391  C  CA    . ASN   B 1 376  ? 189.587 168.258 160.384 1.00 37.83  ? 376  ASN   B CA    1 
ATOM   7392  C  C     . ASN   B 1 376  ? 190.344 169.485 160.882 1.00 33.47  ? 376  ASN   B C     1 
ATOM   7393  O  O     . ASN   B 1 376  ? 191.266 169.369 161.706 1.00 38.93  ? 376  ASN   B O     1 
ATOM   7394  C  CB    . ASN   B 1 376  ? 190.110 167.814 159.020 1.00 36.29  ? 376  ASN   B CB    1 
ATOM   7395  C  CG    . ASN   B 1 376  ? 190.107 166.307 158.860 1.00 37.67  ? 376  ASN   B CG    1 
ATOM   7396  O  OD1   . ASN   B 1 376  ? 190.974 165.614 159.391 1.00 44.38  ? 376  ASN   B OD1   1 
ATOM   7397  N  ND2   . ASN   B 1 376  ? 189.124 165.791 158.133 1.00 31.72  ? 376  ASN   B ND2   1 
ATOM   7398  N  N     . ALA   B 1 377  ? 189.964 170.672 160.403 1.00 39.24  ? 377  ALA   B N     1 
ATOM   7399  C  CA    . ALA   B 1 377  ? 190.629 171.886 160.861 1.00 39.81  ? 377  ALA   B CA    1 
ATOM   7400  C  C     . ALA   B 1 377  ? 190.485 172.056 162.368 1.00 44.34  ? 377  ALA   B C     1 
ATOM   7401  O  O     . ALA   B 1 377  ? 191.459 172.374 163.060 1.00 43.90  ? 377  ALA   B O     1 
ATOM   7402  C  CB    . ALA   B 1 377  ? 190.069 173.102 160.124 1.00 41.51  ? 377  ALA   B CB    1 
ATOM   7403  N  N     . VAL   B 1 378  ? 189.278 171.842 162.897 1.00 38.00  ? 378  VAL   B N     1 
ATOM   7404  C  CA    . VAL   B 1 378  ? 189.065 171.980 164.336 1.00 31.33  ? 378  VAL   B CA    1 
ATOM   7405  C  C     . VAL   B 1 378  ? 189.784 170.872 165.099 1.00 33.78  ? 378  VAL   B C     1 
ATOM   7406  O  O     . VAL   B 1 378  ? 190.299 171.092 166.203 1.00 45.31  ? 378  VAL   B O     1 
ATOM   7407  C  CB    . VAL   B 1 378  ? 187.559 172.005 164.654 1.00 37.71  ? 378  VAL   B CB    1 
ATOM   7408  C  CG1   . VAL   B 1 378  ? 187.334 172.313 166.124 1.00 37.37  ? 378  VAL   B CG1   1 
ATOM   7409  C  CG2   . VAL   B 1 378  ? 186.852 173.029 163.783 1.00 38.58  ? 378  VAL   B CG2   1 
ATOM   7410  N  N     . ALA   B 1 379  ? 189.809 169.660 164.539 1.00 35.43  ? 379  ALA   B N     1 
ATOM   7411  C  CA    . ALA   B 1 379  ? 190.520 168.564 165.184 1.00 37.65  ? 379  ALA   B CA    1 
ATOM   7412  C  C     . ALA   B 1 379  ? 191.997 168.879 165.344 1.00 39.42  ? 379  ALA   B C     1 
ATOM   7413  O  O     . ALA   B 1 379  ? 192.620 168.453 166.321 1.00 47.19  ? 379  ALA   B O     1 
ATOM   7414  C  CB    . ALA   B 1 379  ? 190.334 167.273 164.386 1.00 37.77  ? 379  ALA   B CB    1 
ATOM   7415  N  N     . VAL   B 1 380  ? 192.580 169.613 164.394 1.00 40.20  ? 380  VAL   B N     1 
ATOM   7416  C  CA    . VAL   B 1 380  ? 193.976 170.022 164.551 1.00 39.39  ? 380  VAL   B CA    1 
ATOM   7417  C  C     . VAL   B 1 380  ? 194.157 170.776 165.865 1.00 36.56  ? 380  VAL   B C     1 
ATOM   7418  O  O     . VAL   B 1 380  ? 195.042 170.461 166.675 1.00 38.68  ? 380  VAL   B O     1 
ATOM   7419  C  CB    . VAL   B 1 380  ? 194.426 170.871 163.348 1.00 39.02  ? 380  VAL   B CB    1 
ATOM   7420  C  CG1   . VAL   B 1 380  ? 195.801 171.472 163.605 1.00 36.83  ? 380  VAL   B CG1   1 
ATOM   7421  C  CG2   . VAL   B 1 380  ? 194.434 170.037 162.079 1.00 41.57  ? 380  VAL   B CG2   1 
ATOM   7422  N  N     . ALA   B 1 381  ? 193.298 171.769 166.106 1.00 43.68  ? 381  ALA   B N     1 
ATOM   7423  C  CA    . ALA   B 1 381  ? 193.391 172.552 167.333 1.00 38.56  ? 381  ALA   B CA    1 
ATOM   7424  C  C     . ALA   B 1 381  ? 193.115 171.693 168.559 1.00 38.88  ? 381  ALA   B C     1 
ATOM   7425  O  O     . ALA   B 1 381  ? 193.755 171.865 169.601 1.00 50.26  ? 381  ALA   B O     1 
ATOM   7426  C  CB    . ALA   B 1 381  ? 192.426 173.735 167.278 1.00 39.91  ? 381  ALA   B CB    1 
ATOM   7427  N  N     . MET   B 1 382  ? 192.155 170.772 168.461 1.00 43.40  ? 382  MET   B N     1 
ATOM   7428  C  CA    . MET   B 1 382  ? 191.843 169.923 169.609 1.00 41.79  ? 382  MET   B CA    1 
ATOM   7429  C  C     . MET   B 1 382  ? 193.032 169.047 169.996 1.00 41.21  ? 382  MET   B C     1 
ATOM   7430  O  O     . MET   B 1 382  ? 193.361 168.916 171.183 1.00 48.65  ? 382  MET   B O     1 
ATOM   7431  C  CB    . MET   B 1 382  ? 190.615 169.064 169.313 1.00 40.04  ? 382  MET   B CB    1 
ATOM   7432  C  CG    . MET   B 1 382  ? 189.308 169.836 169.310 1.00 44.94  ? 382  MET   B CG    1 
ATOM   7433  S  SD    . MET   B 1 382  ? 187.864 168.760 169.340 1.00 70.07  ? 382  MET   B SD    1 
ATOM   7434  C  CE    . MET   B 1 382  ? 186.546 169.971 169.341 1.00 52.72  ? 382  MET   B CE    1 
ATOM   7435  N  N     . TYR   B 1 383  ? 193.695 168.442 169.009 1.00 39.48  ? 383  TYR   B N     1 
ATOM   7436  C  CA    . TYR   B 1 383  ? 194.868 167.625 169.304 1.00 35.79  ? 383  TYR   B CA    1 
ATOM   7437  C  C     . TYR   B 1 383  ? 196.010 168.473 169.853 1.00 37.99  ? 383  TYR   B C     1 
ATOM   7438  O  O     . TYR   B 1 383  ? 196.728 168.044 170.767 1.00 40.74  ? 383  TYR   B O     1 
ATOM   7439  C  CB    . TYR   B 1 383  ? 195.311 166.857 168.058 1.00 41.96  ? 383  TYR   B CB    1 
ATOM   7440  C  CG    . TYR   B 1 383  ? 194.362 165.753 167.648 1.00 42.01  ? 383  TYR   B CG    1 
ATOM   7441  C  CD1   . TYR   B 1 383  ? 194.243 164.598 168.408 1.00 42.28  ? 383  TYR   B CD1   1 
ATOM   7442  C  CD2   . TYR   B 1 383  ? 193.592 165.860 166.499 1.00 39.99  ? 383  TYR   B CD2   1 
ATOM   7443  C  CE1   . TYR   B 1 383  ? 193.379 163.586 168.037 1.00 42.13  ? 383  TYR   B CE1   1 
ATOM   7444  C  CE2   . TYR   B 1 383  ? 192.725 164.855 166.122 1.00 44.61  ? 383  TYR   B CE2   1 
ATOM   7445  C  CZ    . TYR   B 1 383  ? 192.622 163.720 166.894 1.00 44.20  ? 383  TYR   B CZ    1 
ATOM   7446  O  OH    . TYR   B 1 383  ? 191.761 162.714 166.523 1.00 50.37  ? 383  TYR   B OH    1 
ATOM   7447  N  N     . VAL   B 1 384  ? 196.198 169.679 169.313 1.00 46.56  ? 384  VAL   B N     1 
ATOM   7448  C  CA    . VAL   B 1 384  ? 197.242 170.549 169.848 1.00 44.83  ? 384  VAL   B CA    1 
ATOM   7449  C  C     . VAL   B 1 384  ? 196.935 170.916 171.295 1.00 43.19  ? 384  VAL   B C     1 
ATOM   7450  O  O     . VAL   B 1 384  ? 197.839 171.015 172.134 1.00 46.13  ? 384  VAL   B O     1 
ATOM   7451  C  CB    . VAL   B 1 384  ? 197.409 171.800 168.968 1.00 45.20  ? 384  VAL   B CB    1 
ATOM   7452  C  CG1   . VAL   B 1 384  ? 198.082 172.907 169.759 1.00 46.24  ? 384  VAL   B CG1   1 
ATOM   7453  C  CG2   . VAL   B 1 384  ? 198.207 171.468 167.718 1.00 43.20  ? 384  VAL   B CG2   1 
ATOM   7454  N  N     . VAL   B 1 385  ? 195.655 171.120 171.611 1.00 45.86  ? 385  VAL   B N     1 
ATOM   7455  C  CA    . VAL   B 1 385  ? 195.265 171.435 172.981 1.00 40.98  ? 385  VAL   B CA    1 
ATOM   7456  C  C     . VAL   B 1 385  ? 195.523 170.248 173.897 1.00 42.21  ? 385  VAL   B C     1 
ATOM   7457  O  O     . VAL   B 1 385  ? 195.930 170.416 175.050 1.00 53.78  ? 385  VAL   B O     1 
ATOM   7458  C  CB    . VAL   B 1 385  ? 193.791 171.878 173.030 1.00 44.99  ? 385  VAL   B CB    1 
ATOM   7459  C  CG1   . VAL   B 1 385  ? 193.203 171.604 174.402 1.00 43.42  ? 385  VAL   B CG1   1 
ATOM   7460  C  CG2   . VAL   B 1 385  ? 193.671 173.352 172.683 1.00 46.13  ? 385  VAL   B CG2   1 
ATOM   7461  N  N     . GLY   B 1 386  ? 195.276 169.032 173.410 1.00 41.80  ? 386  GLY   B N     1 
ATOM   7462  C  CA    . GLY   B 1 386  ? 195.618 167.857 174.199 1.00 42.19  ? 386  GLY   B CA    1 
ATOM   7463  C  C     . GLY   B 1 386  ? 197.106 167.768 174.487 1.00 45.33  ? 386  GLY   B C     1 
ATOM   7464  O  O     . GLY   B 1 386  ? 197.521 167.461 175.611 1.00 52.73  ? 386  GLY   B O     1 
ATOM   7465  N  N     . PHE   B 1 387  ? 197.929 168.040 173.472 1.00 44.72  ? 387  PHE   B N     1 
ATOM   7466  C  CA    . PHE   B 1 387  ? 199.377 168.076 173.673 1.00 36.20  ? 387  PHE   B CA    1 
ATOM   7467  C  C     . PHE   B 1 387  ? 199.758 169.117 174.719 1.00 45.14  ? 387  PHE   B C     1 
ATOM   7468  O  O     . PHE   B 1 387  ? 200.576 168.855 175.614 1.00 50.13  ? 387  PHE   B O     1 
ATOM   7469  C  CB    . PHE   B 1 387  ? 200.071 168.367 172.341 1.00 41.74  ? 387  PHE   B CB    1 
ATOM   7470  C  CG    . PHE   B 1 387  ? 201.571 168.388 172.423 1.00 45.72  ? 387  PHE   B CG    1 
ATOM   7471  C  CD1   . PHE   B 1 387  ? 202.305 167.224 172.292 1.00 47.27  ? 387  PHE   B CD1   1 
ATOM   7472  C  CD2   . PHE   B 1 387  ? 202.247 169.581 172.616 1.00 42.19  ? 387  PHE   B CD2   1 
ATOM   7473  C  CE1   . PHE   B 1 387  ? 203.684 167.248 172.361 1.00 43.89  ? 387  PHE   B CE1   1 
ATOM   7474  C  CE2   . PHE   B 1 387  ? 203.624 169.609 172.686 1.00 40.98  ? 387  PHE   B CE2   1 
ATOM   7475  C  CZ    . PHE   B 1 387  ? 204.343 168.442 172.559 1.00 40.94  ? 387  PHE   B CZ    1 
ATOM   7476  N  N     . ALA   B 1 388  ? 199.172 170.311 174.618 1.00 53.13  ? 388  ALA   B N     1 
ATOM   7477  C  CA    . ALA   B 1 388  ? 199.464 171.366 175.580 1.00 48.41  ? 388  ALA   B CA    1 
ATOM   7478  C  C     . ALA   B 1 388  ? 199.053 170.956 176.987 1.00 45.13  ? 388  ALA   B C     1 
ATOM   7479  O  O     . ALA   B 1 388  ? 199.768 171.235 177.953 1.00 50.90  ? 388  ALA   B O     1 
ATOM   7480  C  CB    . ALA   B 1 388  ? 198.764 172.661 175.169 1.00 47.68  ? 388  ALA   B CB    1 
ATOM   7481  N  N     . GLU   B 1 389  ? 197.898 170.302 177.124 1.00 47.86  ? 389  GLU   B N     1 
ATOM   7482  C  CA    . GLU   B 1 389  ? 197.454 169.848 178.437 1.00 49.25  ? 389  GLU   B CA    1 
ATOM   7483  C  C     . GLU   B 1 389  ? 198.424 168.834 179.027 1.00 52.65  ? 389  GLU   B C     1 
ATOM   7484  O  O     . GLU   B 1 389  ? 198.761 168.904 180.216 1.00 56.93  ? 389  GLU   B O     1 
ATOM   7485  C  CB    . GLU   B 1 389  ? 196.052 169.246 178.341 1.00 46.55  ? 389  GLU   B CB    1 
ATOM   7486  C  CG    . GLU   B 1 389  ? 194.990 170.198 177.827 1.00 53.76  ? 389  GLU   B CG    1 
ATOM   7487  C  CD    . GLU   B 1 389  ? 193.647 169.519 177.641 1.00 59.68  ? 389  GLU   B CD    1 
ATOM   7488  O  OE1   . GLU   B 1 389  ? 193.618 168.277 177.514 1.00 59.04  ? 389  GLU   B OE1   1 
ATOM   7489  O  OE2   . GLU   B 1 389  ? 192.619 170.228 177.623 1.00 59.31  ? 389  GLU   B OE2   1 
ATOM   7490  N  N     . THR   B 1 390  ? 198.876 167.876 178.215 1.00 50.23  ? 390  THR   B N     1 
ATOM   7491  C  CA    . THR   B 1 390  ? 199.829 166.892 178.720 1.00 49.43  ? 390  THR   B CA    1 
ATOM   7492  C  C     . THR   B 1 390  ? 201.124 167.562 179.168 1.00 49.11  ? 390  THR   B C     1 
ATOM   7493  O  O     . THR   B 1 390  ? 201.658 167.250 180.242 1.00 54.16  ? 390  THR   B O     1 
ATOM   7494  C  CB    . THR   B 1 390  ? 200.117 165.831 177.658 1.00 53.94  ? 390  THR   B CB    1 
ATOM   7495  O  OG1   . THR   B 1 390  ? 198.988 164.957 177.535 1.00 58.77  ? 390  THR   B OG1   1 
ATOM   7496  C  CG2   . THR   B 1 390  ? 201.336 165.013 178.049 1.00 51.37  ? 390  THR   B CG2   1 
ATOM   7497  N  N     . VAL   B 1 391  ? 201.637 168.498 178.366 1.00 50.43  ? 391  VAL   B N     1 
ATOM   7498  C  CA    . VAL   B 1 391  ? 202.882 169.172 178.731 1.00 52.59  ? 391  VAL   B CA    1 
ATOM   7499  C  C     . VAL   B 1 391  ? 202.687 170.006 179.992 1.00 51.12  ? 391  VAL   B C     1 
ATOM   7500  O  O     . VAL   B 1 391  ? 203.573 170.075 180.855 1.00 56.05  ? 391  VAL   B O     1 
ATOM   7501  C  CB    . VAL   B 1 391  ? 203.395 170.028 177.559 1.00 55.60  ? 391  VAL   B CB    1 
ATOM   7502  C  CG1   . VAL   B 1 391  ? 204.202 171.206 178.080 1.00 55.67  ? 391  VAL   B CG1   1 
ATOM   7503  C  CG2   . VAL   B 1 391  ? 204.232 169.181 176.613 1.00 53.10  ? 391  VAL   B CG2   1 
ATOM   7504  N  N     . VAL   B 1 392  ? 201.528 170.654 180.119 1.00 54.19  ? 392  VAL   B N     1 
ATOM   7505  C  CA    . VAL   B 1 392  ? 201.252 171.472 181.294 1.00 54.03  ? 392  VAL   B CA    1 
ATOM   7506  C  C     . VAL   B 1 392  ? 201.206 170.607 182.543 1.00 54.87  ? 392  VAL   B C     1 
ATOM   7507  O  O     . VAL   B 1 392  ? 201.747 170.978 183.588 1.00 58.52  ? 392  VAL   B O     1 
ATOM   7508  C  CB    . VAL   B 1 392  ? 199.943 172.260 181.103 1.00 55.05  ? 392  VAL   B CB    1 
ATOM   7509  C  CG1   . VAL   B 1 392  ? 199.364 172.659 182.451 1.00 51.89  ? 392  VAL   B CG1   1 
ATOM   7510  C  CG2   . VAL   B 1 392  ? 200.183 173.486 180.236 1.00 57.38  ? 392  VAL   B CG2   1 
ATOM   7511  N  N     . GLU   B 1 393  ? 200.553 169.447 182.461 1.00 55.43  ? 393  GLU   B N     1 
ATOM   7512  C  CA    . GLU   B 1 393  ? 200.525 168.546 183.609 1.00 54.98  ? 393  GLU   B CA    1 
ATOM   7513  C  C     . GLU   B 1 393  ? 201.932 168.082 183.968 1.00 56.52  ? 393  GLU   B C     1 
ATOM   7514  O  O     . GLU   B 1 393  ? 202.315 168.062 185.146 1.00 56.10  ? 393  GLU   B O     1 
ATOM   7515  C  CB    . GLU   B 1 393  ? 199.618 167.351 183.318 1.00 54.30  ? 393  GLU   B CB    1 
ATOM   7516  N  N     . LEU   B 1 394  ? 202.726 167.722 182.956 1.00 60.94  ? 394  LEU   B N     1 
ATOM   7517  C  CA    . LEU   B 1 394  ? 204.081 167.250 183.224 1.00 59.86  ? 394  LEU   B CA    1 
ATOM   7518  C  C     . LEU   B 1 394  ? 204.913 168.320 183.919 1.00 60.43  ? 394  LEU   B C     1 
ATOM   7519  O  O     . LEU   B 1 394  ? 205.641 168.026 184.874 1.00 64.29  ? 394  LEU   B O     1 
ATOM   7520  C  CB    . LEU   B 1 394  ? 204.755 166.808 181.926 1.00 61.26  ? 394  LEU   B CB    1 
ATOM   7521  C  CG    . LEU   B 1 394  ? 205.983 165.911 182.097 1.00 59.55  ? 394  LEU   B CG    1 
ATOM   7522  C  CD1   . LEU   B 1 394  ? 205.845 165.040 183.336 1.00 60.28  ? 394  LEU   B CD1   1 
ATOM   7523  C  CD2   . LEU   B 1 394  ? 206.209 165.057 180.861 1.00 63.13  ? 394  LEU   B CD2   1 
ATOM   7524  N  N     . LEU   B 1 395  ? 204.820 169.570 183.459 1.00 64.14  ? 395  LEU   B N     1 
ATOM   7525  C  CA    . LEU   B 1 395  ? 205.613 170.634 184.065 1.00 63.16  ? 395  LEU   B CA    1 
ATOM   7526  C  C     . LEU   B 1 395  ? 205.037 171.122 185.389 1.00 66.75  ? 395  LEU   B C     1 
ATOM   7527  O  O     . LEU   B 1 395  ? 205.780 171.687 186.199 1.00 70.54  ? 395  LEU   B O     1 
ATOM   7528  C  CB    . LEU   B 1 395  ? 205.753 171.811 183.096 1.00 59.36  ? 395  LEU   B CB    1 
ATOM   7529  C  CG    . LEU   B 1 395  ? 204.488 172.560 182.681 1.00 62.25  ? 395  LEU   B CG    1 
ATOM   7530  C  CD1   . LEU   B 1 395  ? 204.104 173.601 183.720 1.00 64.15  ? 395  LEU   B CD1   1 
ATOM   7531  C  CD2   . LEU   B 1 395  ? 204.692 173.210 181.325 1.00 63.82  ? 395  LEU   B CD2   1 
ATOM   7532  N  N     . LYS   B 1 396  ? 203.740 170.924 185.626 1.00 64.31  ? 396  LYS   B N     1 
ATOM   7533  C  CA    . LYS   B 1 396  ? 203.158 171.263 186.918 1.00 63.61  ? 396  LYS   B CA    1 
ATOM   7534  C  C     . LYS   B 1 396  ? 203.508 170.229 187.975 1.00 66.26  ? 396  LYS   B C     1 
ATOM   7535  O  O     . LYS   B 1 396  ? 203.567 170.560 189.165 1.00 68.27  ? 396  LYS   B O     1 
ATOM   7536  C  CB    . LYS   B 1 396  ? 201.640 171.400 186.795 1.00 63.55  ? 396  LYS   B CB    1 
ATOM   7537  N  N     . GLU   B 1 397  ? 203.740 168.980 187.567 1.00 70.79  ? 397  GLU   B N     1 
ATOM   7538  C  CA    . GLU   B 1 397  ? 204.221 167.985 188.518 1.00 70.09  ? 397  GLU   B CA    1 
ATOM   7539  C  C     . GLU   B 1 397  ? 205.550 168.390 189.140 1.00 69.13  ? 397  GLU   B C     1 
ATOM   7540  O  O     . GLU   B 1 397  ? 205.894 167.895 190.219 1.00 72.31  ? 397  GLU   B O     1 
ATOM   7541  C  CB    . GLU   B 1 397  ? 204.356 166.623 187.836 1.00 69.68  ? 397  GLU   B CB    1 
ATOM   7542  N  N     . HIS   B 1 398  ? 206.304 169.278 188.486 1.00 69.29  ? 398  HIS   B N     1 
ATOM   7543  C  CA    . HIS   B 1 398  ? 207.582 169.760 188.998 1.00 71.01  ? 398  HIS   B CA    1 
ATOM   7544  C  C     . HIS   B 1 398  ? 207.577 171.267 189.238 1.00 73.21  ? 398  HIS   B C     1 
ATOM   7545  O  O     . HIS   B 1 398  ? 208.629 171.850 189.516 1.00 72.51  ? 398  HIS   B O     1 
ATOM   7546  C  CB    . HIS   B 1 398  ? 208.716 169.375 188.046 1.00 69.72  ? 398  HIS   B CB    1 
ATOM   7547  C  CG    . HIS   B 1 398  ? 208.784 167.909 187.751 1.00 72.41  ? 398  HIS   B CG    1 
ATOM   7548  N  ND1   . HIS   B 1 398  ? 209.449 167.016 188.563 1.00 74.90  ? 398  HIS   B ND1   1 
ATOM   7549  C  CD2   . HIS   B 1 398  ? 208.269 167.179 186.733 1.00 72.83  ? 398  HIS   B CD2   1 
ATOM   7550  C  CE1   . HIS   B 1 398  ? 209.342 165.800 188.059 1.00 72.74  ? 398  HIS   B CE1   1 
ATOM   7551  N  NE2   . HIS   B 1 398  ? 208.631 165.871 186.948 1.00 73.33  ? 398  HIS   B NE2   1 
ATOM   7552  N  N     . SER   B 1 399  ? 206.415 171.908 189.133 1.00 75.25  ? 399  SER   B N     1 
ATOM   7553  C  CA    . SER   B 1 399  ? 206.246 173.324 189.462 1.00 73.52  ? 399  SER   B CA    1 
ATOM   7554  C  C     . SER   B 1 399  ? 207.203 174.205 188.654 1.00 73.26  ? 399  SER   B C     1 
ATOM   7555  O  O     . SER   B 1 399  ? 208.096 174.865 189.185 1.00 74.55  ? 399  SER   B O     1 
ATOM   7556  C  CB    . SER   B 1 399  ? 206.430 173.551 190.965 1.00 76.08  ? 399  SER   B CB    1 
ATOM   7557  O  OG    . SER   B 1 399  ? 206.333 174.928 191.285 1.00 78.02  ? 399  SER   B OG    1 
ATOM   7558  N  N     . ILE   B 1 400  ? 206.986 174.198 187.340 1.00 69.72  ? 400  ILE   B N     1 
ATOM   7559  C  CA    . ILE   B 1 400  ? 207.747 175.050 186.433 1.00 66.19  ? 400  ILE   B CA    1 
ATOM   7560  C  C     . ILE   B 1 400  ? 206.784 175.855 185.571 1.00 70.12  ? 400  ILE   B C     1 
ATOM   7561  O  O     . ILE   B 1 400  ? 207.161 176.370 184.513 1.00 70.70  ? 400  ILE   B O     1 
ATOM   7562  C  CB    . ILE   B 1 400  ? 208.709 174.222 185.562 1.00 64.09  ? 400  ILE   B CB    1 
ATOM   7563  N  N     . LEU   B 1 401  ? 205.537 175.972 186.021 1.00 75.89  ? 401  LEU   B N     1 
ATOM   7564  C  CA    . LEU   B 1 401  ? 204.524 176.684 185.257 1.00 76.42  ? 401  LEU   B CA    1 
ATOM   7565  C  C     . LEU   B 1 401  ? 204.807 178.182 185.234 1.00 78.29  ? 401  LEU   B C     1 
ATOM   7566  O  O     . LEU   B 1 401  ? 205.432 178.736 186.142 1.00 76.89  ? 401  LEU   B O     1 
ATOM   7567  C  CB    . LEU   B 1 401  ? 203.136 176.427 185.842 1.00 70.92  ? 401  LEU   B CB    1 
ATOM   7568  N  N     . MET   B 1 402  ? 204.337 178.839 184.175 1.00 73.13  ? 402  MET   B N     1 
ATOM   7569  C  CA    . MET   B 1 402  ? 204.497 180.276 184.013 1.00 70.20  ? 402  MET   B CA    1 
ATOM   7570  C  C     . MET   B 1 402  ? 203.190 180.883 183.525 1.00 71.28  ? 402  MET   B C     1 
ATOM   7571  O  O     . MET   B 1 402  ? 202.569 180.369 182.591 1.00 72.34  ? 402  MET   B O     1 
ATOM   7572  C  CB    . MET   B 1 402  ? 205.626 180.608 183.029 1.00 62.91  ? 402  MET   B CB    1 
ATOM   7573  N  N     . ILE   B 1 403  ? 202.784 181.980 184.160 1.00 69.83  ? 403  ILE   B N     1 
ATOM   7574  C  CA    . ILE   B 1 403  ? 201.586 182.716 183.769 1.00 68.74  ? 403  ILE   B CA    1 
ATOM   7575  C  C     . ILE   B 1 403  ? 200.368 181.803 183.817 1.00 69.31  ? 403  ILE   B C     1 
ATOM   7576  O  O     . ILE   B 1 403  ? 199.702 181.586 182.798 1.00 73.13  ? 403  ILE   B O     1 
ATOM   7577  C  CB    . ILE   B 1 403  ? 201.750 183.337 182.370 1.00 63.41  ? 403  ILE   B CB    1 
ATOM   7578  N  N     . ASP   B 1 404  ? 200.071 181.260 184.997 1.00 65.41  ? 404  ASP   B N     1 
ATOM   7579  C  CA    . ASP   B 1 404  ? 198.870 180.454 185.190 1.00 66.34  ? 404  ASP   B CA    1 
ATOM   7580  C  C     . ASP   B 1 404  ? 198.977 179.123 184.457 1.00 69.29  ? 404  ASP   B C     1 
ATOM   7581  O  O     . ASP   B 1 404  ? 200.075 178.699 184.084 1.00 72.70  ? 404  ASP   B O     1 
ATOM   7582  C  CB    . ASP   B 1 404  ? 197.629 181.219 184.725 1.00 64.79  ? 404  ASP   B CB    1 
ATOM   7583  N  N     . GLU   B 1 405  ? 197.841 178.459 184.247 1.00 67.85  ? 405  GLU   B N     1 
ATOM   7584  C  CA    . GLU   B 1 405  ? 197.789 177.169 183.570 1.00 66.55  ? 405  GLU   B CA    1 
ATOM   7585  C  C     . GLU   B 1 405  ? 197.142 177.249 182.195 1.00 68.01  ? 405  GLU   B C     1 
ATOM   7586  O  O     . GLU   B 1 405  ? 197.720 176.776 181.213 1.00 70.19  ? 405  GLU   B O     1 
ATOM   7587  C  CB    . GLU   B 1 405  ? 197.037 176.149 184.439 1.00 61.36  ? 405  GLU   B CB    1 
ATOM   7588  N  N     . ILE   B 1 406  ? 195.947 177.835 182.098 1.00 65.63  ? 406  ILE   B N     1 
ATOM   7589  C  CA    . ILE   B 1 406  ? 195.293 177.981 180.800 1.00 66.08  ? 406  ILE   B CA    1 
ATOM   7590  C  C     . ILE   B 1 406  ? 196.112 178.892 179.893 1.00 70.15  ? 406  ILE   B C     1 
ATOM   7591  O  O     . ILE   B 1 406  ? 196.266 178.633 178.691 1.00 75.39  ? 406  ILE   B O     1 
ATOM   7592  C  CB    . ILE   B 1 406  ? 193.856 178.504 180.978 1.00 63.20  ? 406  ILE   B CB    1 
ATOM   7593  N  N     . ASN   B 1 407  ? 196.632 179.987 180.450 1.00 64.86  ? 407  ASN   B N     1 
ATOM   7594  C  CA    . ASN   B 1 407  ? 197.453 180.904 179.671 1.00 64.41  ? 407  ASN   B CA    1 
ATOM   7595  C  C     . ASN   B 1 407  ? 198.774 180.285 179.237 1.00 63.75  ? 407  ASN   B C     1 
ATOM   7596  O  O     . ASN   B 1 407  ? 199.381 180.775 178.279 1.00 66.71  ? 407  ASN   B O     1 
ATOM   7597  C  CB    . ASN   B 1 407  ? 197.712 182.182 180.470 1.00 65.52  ? 407  ASN   B CB    1 
ATOM   7598  C  CG    . ASN   B 1 407  ? 196.432 182.833 180.955 1.00 68.37  ? 407  ASN   B CG    1 
ATOM   7599  O  OD1   . ASN   B 1 407  ? 195.410 182.805 180.269 1.00 66.99  ? 407  ASN   B OD1   1 
ATOM   7600  N  ND2   . ASN   B 1 407  ? 196.481 183.424 182.143 1.00 67.72  ? 407  ASN   B ND2   1 
ATOM   7601  N  N     . ASP   B 1 408  ? 199.234 179.233 179.912 1.00 56.15  ? 408  ASP   B N     1 
ATOM   7602  C  CA    . ASP   B 1 408  ? 200.392 178.468 179.470 1.00 56.22  ? 408  ASP   B CA    1 
ATOM   7603  C  C     . ASP   B 1 408  ? 200.019 177.437 178.413 1.00 57.55  ? 408  ASP   B C     1 
ATOM   7604  O  O     . ASP   B 1 408  ? 200.795 177.184 177.484 1.00 62.80  ? 408  ASP   B O     1 
ATOM   7605  C  CB    . ASP   B 1 408  ? 201.058 177.777 180.666 1.00 57.50  ? 408  ASP   B CB    1 
ATOM   7606  N  N     . ILE   B 1 409  ? 198.836 176.837 178.544 1.00 53.87  ? 409  ILE   B N     1 
ATOM   7607  C  CA    . ILE   B 1 409  ? 198.311 175.912 177.548 1.00 54.06  ? 409  ILE   B CA    1 
ATOM   7608  C  C     . ILE   B 1 409  ? 198.225 176.646 176.221 1.00 56.09  ? 409  ILE   B C     1 
ATOM   7609  O  O     . ILE   B 1 409  ? 198.598 176.107 175.175 1.00 59.60  ? 409  ILE   B O     1 
ATOM   7610  C  CB    . ILE   B 1 409  ? 196.934 175.356 177.956 1.00 51.95  ? 409  ILE   B CB    1 
ATOM   7611  C  CG1   . ILE   B 1 409  ? 197.069 174.387 179.131 1.00 58.30  ? 409  ILE   B CG1   1 
ATOM   7612  C  CG2   . ILE   B 1 409  ? 196.263 174.673 176.773 1.00 50.53  ? 409  ILE   B CG2   1 
ATOM   7613  C  CD1   . ILE   B 1 409  ? 195.772 173.705 179.505 1.00 56.99  ? 409  ILE   B CD1   1 
ATOM   7614  N  N     . ARG   B 1 410  ? 197.724 177.881 176.258 1.00 53.84  ? 410  ARG   B N     1 
ATOM   7615  C  CA    . ARG   B 1 410  ? 197.595 178.661 175.031 1.00 50.99  ? 410  ARG   B CA    1 
ATOM   7616  C  C     . ARG   B 1 410  ? 198.949 178.852 174.355 1.00 52.35  ? 410  ARG   B C     1 
ATOM   7617  O  O     . ARG   B 1 410  ? 199.088 178.633 173.145 1.00 60.80  ? 410  ARG   B O     1 
ATOM   7618  C  CB    . ARG   B 1 410  ? 196.949 180.012 175.334 1.00 48.71  ? 410  ARG   B CB    1 
ATOM   7619  C  CG    . ARG   B 1 410  ? 195.549 179.918 175.912 1.00 51.22  ? 410  ARG   B CG    1 
ATOM   7620  C  CD    . ARG   B 1 410  ? 195.242 181.118 176.790 1.00 56.67  ? 410  ARG   B CD    1 
ATOM   7621  N  NE    . ARG   B 1 410  ? 193.854 181.135 177.234 1.00 54.77  ? 410  ARG   B NE    1 
ATOM   7622  C  CZ    . ARG   B 1 410  ? 192.887 181.820 176.640 1.00 55.97  ? 410  ARG   B CZ    1 
ATOM   7623  N  NH1   . ARG   B 1 410  ? 193.123 182.567 175.574 1.00 56.66  ? 410  ARG   B NH1   1 
ATOM   7624  N  NH2   . ARG   B 1 410  ? 191.653 181.757 177.130 1.00 54.38  ? 410  ARG   B NH2   1 
ATOM   7625  N  N     . ILE   B 1 411  ? 199.964 179.249 175.125 1.00 50.67  ? 411  ILE   B N     1 
ATOM   7626  C  CA    . ILE   B 1 411  ? 201.281 179.520 174.553 1.00 52.18  ? 411  ILE   B CA    1 
ATOM   7627  C  C     . ILE   B 1 411  ? 201.880 178.248 173.965 1.00 55.04  ? 411  ILE   B C     1 
ATOM   7628  O  O     . ILE   B 1 411  ? 202.380 178.236 172.829 1.00 58.73  ? 411  ILE   B O     1 
ATOM   7629  C  CB    . ILE   B 1 411  ? 202.208 180.134 175.618 1.00 53.41  ? 411  ILE   B CB    1 
ATOM   7630  C  CG1   . ILE   B 1 411  ? 201.731 181.537 175.999 1.00 56.37  ? 411  ILE   B CG1   1 
ATOM   7631  C  CG2   . ILE   B 1 411  ? 203.644 180.166 175.122 1.00 53.10  ? 411  ILE   B CG2   1 
ATOM   7632  C  CD1   . ILE   B 1 411  ? 202.552 182.183 177.094 1.00 54.64  ? 411  ILE   B CD1   1 
ATOM   7633  N  N     . ILE   B 1 412  ? 201.849 177.159 174.736 1.00 53.78  ? 412  ILE   B N     1 
ATOM   7634  C  CA    . ILE   B 1 412  ? 202.444 175.913 174.265 1.00 53.11  ? 412  ILE   B CA    1 
ATOM   7635  C  C     . ILE   B 1 412  ? 201.727 175.424 173.015 1.00 56.72  ? 412  ILE   B C     1 
ATOM   7636  O  O     . ILE   B 1 412  ? 202.364 175.000 172.042 1.00 57.97  ? 412  ILE   B O     1 
ATOM   7637  C  CB    . ILE   B 1 412  ? 202.432 174.853 175.383 1.00 55.54  ? 412  ILE   B CB    1 
ATOM   7638  C  CG1   . ILE   B 1 412  ? 202.870 173.493 174.836 1.00 54.34  ? 412  ILE   B CG1   1 
ATOM   7639  C  CG2   . ILE   B 1 412  ? 201.055 174.758 176.016 1.00 56.94  ? 412  ILE   B CG2   1 
ATOM   7640  C  CD1   . ILE   B 1 412  ? 204.312 173.452 174.384 1.00 53.29  ? 412  ILE   B CD1   1 
ATOM   7641  N  N     . GLY   B 1 413  ? 200.393 175.476 173.017 1.00 51.90  ? 413  GLY   B N     1 
ATOM   7642  C  CA    . GLY   B 1 413  ? 199.646 175.049 171.849 1.00 50.56  ? 413  GLY   B CA    1 
ATOM   7643  C  C     . GLY   B 1 413  ? 199.947 175.889 170.625 1.00 53.69  ? 413  GLY   B C     1 
ATOM   7644  O  O     . GLY   B 1 413  ? 200.048 175.366 169.515 1.00 60.67  ? 413  GLY   B O     1 
ATOM   7645  N  N     . ALA   B 1 414  ? 200.093 177.203 170.807 1.00 51.28  ? 414  ALA   B N     1 
ATOM   7646  C  CA    . ALA   B 1 414  ? 200.443 178.057 169.677 1.00 52.56  ? 414  ALA   B CA    1 
ATOM   7647  C  C     . ALA   B 1 414  ? 201.807 177.685 169.111 1.00 52.67  ? 414  ALA   B C     1 
ATOM   7648  O  O     . ALA   B 1 414  ? 201.985 177.618 167.887 1.00 57.35  ? 414  ALA   B O     1 
ATOM   7649  C  CB    . ALA   B 1 414  ? 200.415 179.526 170.099 1.00 50.99  ? 414  ALA   B CB    1 
ATOM   7650  N  N     . ILE   B 1 415  ? 202.783 177.431 169.986 1.00 48.30  ? 415  ILE   B N     1 
ATOM   7651  C  CA    . ILE   B 1 415  ? 204.114 177.060 169.506 1.00 49.44  ? 415  ILE   B CA    1 
ATOM   7652  C  C     . ILE   B 1 415  ? 204.051 175.745 168.733 1.00 52.88  ? 415  ILE   B C     1 
ATOM   7653  O  O     . ILE   B 1 415  ? 204.635 175.609 167.648 1.00 56.33  ? 415  ILE   B O     1 
ATOM   7654  C  CB    . ILE   B 1 415  ? 205.108 176.978 170.678 1.00 51.77  ? 415  ILE   B CB    1 
ATOM   7655  C  CG1   . ILE   B 1 415  ? 205.370 178.371 171.255 1.00 51.23  ? 415  ILE   B CG1   1 
ATOM   7656  C  CG2   . ILE   B 1 415  ? 206.412 176.343 170.223 1.00 49.32  ? 415  ILE   B CG2   1 
ATOM   7657  C  CD1   . ILE   B 1 415  ? 205.652 179.424 170.209 1.00 50.85  ? 415  ILE   B CD1   1 
ATOM   7658  N  N     . THR   B 1 416  ? 203.338 174.756 169.280 1.00 53.52  ? 416  THR   B N     1 
ATOM   7659  C  CA    . THR   B 1 416  ? 203.229 173.472 168.592 1.00 49.90  ? 416  THR   B CA    1 
ATOM   7660  C  C     . THR   B 1 416  ? 202.508 173.615 167.258 1.00 46.00  ? 416  THR   B C     1 
ATOM   7661  O  O     . THR   B 1 416  ? 202.873 172.958 166.278 1.00 50.41  ? 416  THR   B O     1 
ATOM   7662  C  CB    . THR   B 1 416  ? 202.523 172.435 169.470 1.00 54.23  ? 416  THR   B CB    1 
ATOM   7663  O  OG1   . THR   B 1 416  ? 201.106 172.511 169.269 1.00 53.11  ? 416  THR   B OG1   1 
ATOM   7664  C  CG2   . THR   B 1 416  ? 202.859 172.629 170.936 1.00 51.80  ? 416  THR   B CG2   1 
ATOM   7665  N  N     . VAL   B 1 417  ? 201.475 174.457 167.199 1.00 47.91  ? 417  VAL   B N     1 
ATOM   7666  C  CA    . VAL   B 1 417  ? 200.755 174.650 165.944 1.00 50.49  ? 417  VAL   B CA    1 
ATOM   7667  C  C     . VAL   B 1 417  ? 201.659 175.298 164.904 1.00 53.21  ? 417  VAL   B C     1 
ATOM   7668  O  O     . VAL   B 1 417  ? 201.631 174.931 163.724 1.00 55.05  ? 417  VAL   B O     1 
ATOM   7669  C  CB    . VAL   B 1 417  ? 199.469 175.466 166.178 1.00 48.29  ? 417  VAL   B CB    1 
ATOM   7670  C  CG1   . VAL   B 1 417  ? 199.757 176.955 166.127 1.00 51.18  ? 417  VAL   B CG1   1 
ATOM   7671  C  CG2   . VAL   B 1 417  ? 198.412 175.096 165.150 1.00 46.89  ? 417  VAL   B CG2   1 
ATOM   7672  N  N     . VAL   B 1 418  ? 202.478 176.267 165.319 1.00 50.60  ? 418  VAL   B N     1 
ATOM   7673  C  CA    . VAL   B 1 418  ? 203.419 176.881 164.384 1.00 47.60  ? 418  VAL   B CA    1 
ATOM   7674  C  C     . VAL   B 1 418  ? 204.401 175.840 163.859 1.00 48.55  ? 418  VAL   B C     1 
ATOM   7675  O  O     . VAL   B 1 418  ? 204.689 175.782 162.654 1.00 50.13  ? 418  VAL   B O     1 
ATOM   7676  C  CB    . VAL   B 1 418  ? 204.148 178.061 165.053 1.00 48.96  ? 418  VAL   B CB    1 
ATOM   7677  C  CG1   . VAL   B 1 418  ? 205.425 178.389 164.297 1.00 45.14  ? 418  VAL   B CG1   1 
ATOM   7678  C  CG2   . VAL   B 1 418  ? 203.237 179.276 165.124 1.00 49.18  ? 418  VAL   B CG2   1 
ATOM   7679  N  N     . ILE   B 1 419  ? 204.929 175.002 164.753 1.00 49.78  ? 419  ILE   B N     1 
ATOM   7680  C  CA    . ILE   B 1 419  ? 205.882 173.979 164.326 1.00 48.40  ? 419  ILE   B CA    1 
ATOM   7681  C  C     . ILE   B 1 419  ? 205.222 173.005 163.357 1.00 49.03  ? 419  ILE   B C     1 
ATOM   7682  O  O     . ILE   B 1 419  ? 205.819 172.604 162.349 1.00 51.63  ? 419  ILE   B O     1 
ATOM   7683  C  CB    . ILE   B 1 419  ? 206.471 173.250 165.547 1.00 51.42  ? 419  ILE   B CB    1 
ATOM   7684  C  CG1   . ILE   B 1 419  ? 207.425 174.173 166.307 1.00 50.63  ? 419  ILE   B CG1   1 
ATOM   7685  C  CG2   . ILE   B 1 419  ? 207.190 171.982 165.113 1.00 50.16  ? 419  ILE   B CG2   1 
ATOM   7686  C  CD1   . ILE   B 1 419  ? 208.163 175.151 165.422 1.00 50.30  ? 419  ILE   B CD1   1 
ATOM   7687  N  N     . LEU   B 1 420  ? 203.987 172.596 163.654 1.00 49.72  ? 420  LEU   B N     1 
ATOM   7688  C  CA    . LEU   B 1 420  ? 203.283 171.663 162.782 1.00 49.70  ? 420  LEU   B CA    1 
ATOM   7689  C  C     . LEU   B 1 420  ? 203.017 172.278 161.416 1.00 52.80  ? 420  LEU   B C     1 
ATOM   7690  O  O     . LEU   B 1 420  ? 203.136 171.601 160.389 1.00 57.37  ? 420  LEU   B O     1 
ATOM   7691  C  CB    . LEU   B 1 420  ? 201.974 171.218 163.434 1.00 47.50  ? 420  LEU   B CB    1 
ATOM   7692  C  CG    . LEU   B 1 420  ? 202.103 170.522 164.789 1.00 49.48  ? 420  LEU   B CG    1 
ATOM   7693  C  CD1   . LEU   B 1 420  ? 200.757 169.991 165.249 1.00 48.11  ? 420  LEU   B CD1   1 
ATOM   7694  C  CD2   . LEU   B 1 420  ? 203.126 169.402 164.714 1.00 48.35  ? 420  LEU   B CD2   1 
ATOM   7695  N  N     . LEU   B 1 421  ? 202.639 173.557 161.382 1.00 50.07  ? 421  LEU   B N     1 
ATOM   7696  C  CA    . LEU   B 1 421  ? 202.440 174.226 160.102 1.00 49.52  ? 421  LEU   B CA    1 
ATOM   7697  C  C     . LEU   B 1 421  ? 203.732 174.264 159.300 1.00 48.52  ? 421  LEU   B C     1 
ATOM   7698  O  O     . LEU   B 1 421  ? 203.727 174.025 158.086 1.00 53.07  ? 421  LEU   B O     1 
ATOM   7699  C  CB    . LEU   B 1 421  ? 201.905 175.640 160.320 1.00 50.65  ? 421  LEU   B CB    1 
ATOM   7700  C  CG    . LEU   B 1 421  ? 201.976 176.543 159.088 1.00 47.79  ? 421  LEU   B CG    1 
ATOM   7701  C  CD1   . LEU   B 1 421  ? 200.907 176.157 158.077 1.00 48.37  ? 421  LEU   B CD1   1 
ATOM   7702  C  CD2   . LEU   B 1 421  ? 201.851 178.006 159.478 1.00 48.85  ? 421  LEU   B CD2   1 
ATOM   7703  N  N     . GLY   B 1 422  ? 204.850 174.569 159.960 1.00 47.92  ? 422  GLY   B N     1 
ATOM   7704  C  CA    . GLY   B 1 422  ? 206.126 174.537 159.264 1.00 49.17  ? 422  GLY   B CA    1 
ATOM   7705  C  C     . GLY   B 1 422  ? 206.430 173.167 158.688 1.00 48.45  ? 422  GLY   B C     1 
ATOM   7706  O  O     . GLY   B 1 422  ? 206.823 173.036 157.526 1.00 49.66  ? 422  GLY   B O     1 
ATOM   7707  N  N     . ILE   B 1 423  ? 206.235 172.123 159.494 1.00 47.98  ? 423  ILE   B N     1 
ATOM   7708  C  CA    . ILE   B 1 423  ? 206.514 170.767 159.029 1.00 46.02  ? 423  ILE   B CA    1 
ATOM   7709  C  C     . ILE   B 1 423  ? 205.636 170.424 157.833 1.00 47.11  ? 423  ILE   B C     1 
ATOM   7710  O  O     . ILE   B 1 423  ? 206.105 169.854 156.840 1.00 46.16  ? 423  ILE   B O     1 
ATOM   7711  C  CB    . ILE   B 1 423  ? 206.325 169.755 160.173 1.00 45.33  ? 423  ILE   B CB    1 
ATOM   7712  C  CG1   . ILE   B 1 423  ? 207.419 169.929 161.227 1.00 50.71  ? 423  ILE   B CG1   1 
ATOM   7713  C  CG2   . ILE   B 1 423  ? 206.332 168.336 159.630 1.00 41.80  ? 423  ILE   B CG2   1 
ATOM   7714  C  CD1   . ILE   B 1 423  ? 207.013 169.459 162.605 1.00 45.83  ? 423  ILE   B CD1   1 
ATOM   7715  N  N     . SER   B 1 424  ? 204.346 170.757 157.910 1.00 44.98  ? 424  SER   B N     1 
ATOM   7716  C  CA    . SER   B 1 424  ? 203.435 170.442 156.815 1.00 42.66  ? 424  SER   B CA    1 
ATOM   7717  C  C     . SER   B 1 424  ? 203.830 171.177 155.542 1.00 49.59  ? 424  SER   B C     1 
ATOM   7718  O  O     . SER   B 1 424  ? 203.827 170.591 154.453 1.00 51.09  ? 424  SER   B O     1 
ATOM   7719  C  CB    . SER   B 1 424  ? 202.000 170.787 157.211 1.00 50.61  ? 424  SER   B CB    1 
ATOM   7720  O  OG    . SER   B 1 424  ? 201.706 172.143 156.924 1.00 59.55  ? 424  SER   B OG    1 
ATOM   7721  N  N     . VAL   B 1 425  ? 204.171 172.463 155.656 1.00 48.83  ? 425  VAL   B N     1 
ATOM   7722  C  CA    . VAL   B 1 425  ? 204.601 173.219 154.483 1.00 43.59  ? 425  VAL   B CA    1 
ATOM   7723  C  C     . VAL   B 1 425  ? 205.903 172.659 153.928 1.00 46.94  ? 425  VAL   B C     1 
ATOM   7724  O  O     . VAL   B 1 425  ? 206.180 172.783 152.729 1.00 45.79  ? 425  VAL   B O     1 
ATOM   7725  C  CB    . VAL   B 1 425  ? 204.728 174.716 154.826 1.00 44.56  ? 425  VAL   B CB    1 
ATOM   7726  C  CG1   . VAL   B 1 425  ? 205.641 175.412 153.832 1.00 46.20  ? 425  VAL   B CG1   1 
ATOM   7727  C  CG2   . VAL   B 1 425  ? 203.359 175.373 154.843 1.00 45.98  ? 425  VAL   B CG2   1 
ATOM   7728  N  N     . ALA   B 1 426  ? 206.717 172.031 154.779 1.00 52.25  ? 426  ALA   B N     1 
ATOM   7729  C  CA    . ALA   B 1 426  ? 208.006 171.516 154.331 1.00 46.53  ? 426  ALA   B CA    1 
ATOM   7730  C  C     . ALA   B 1 426  ? 207.871 170.478 153.224 1.00 49.33  ? 426  ALA   B C     1 
ATOM   7731  O  O     . ALA   B 1 426  ? 208.870 170.152 152.573 1.00 55.44  ? 426  ALA   B O     1 
ATOM   7732  C  CB    . ALA   B 1 426  ? 208.770 170.914 155.510 1.00 52.08  ? 426  ALA   B CB    1 
ATOM   7733  N  N     . GLY   B 1 427  ? 206.675 169.950 152.997 1.00 48.62  ? 427  GLY   B N     1 
ATOM   7734  C  CA    . GLY   B 1 427  ? 206.434 168.978 151.954 1.00 49.80  ? 427  GLY   B CA    1 
ATOM   7735  C  C     . GLY   B 1 427  ? 205.728 167.751 152.482 1.00 50.97  ? 427  GLY   B C     1 
ATOM   7736  O  O     . GLY   B 1 427  ? 205.381 167.651 153.658 1.00 55.41  ? 427  GLY   B O     1 
ATOM   7737  N  N     . MET   B 1 428  ? 205.514 166.797 151.577 1.00 50.15  ? 428  MET   B N     1 
ATOM   7738  C  CA    . MET   B 1 428  ? 204.789 165.577 151.906 1.00 48.64  ? 428  MET   B CA    1 
ATOM   7739  C  C     . MET   B 1 428  ? 205.701 164.450 152.371 1.00 50.57  ? 428  MET   B C     1 
ATOM   7740  O  O     . MET   B 1 428  ? 205.259 163.585 153.137 1.00 54.30  ? 428  MET   B O     1 
ATOM   7741  C  CB    . MET   B 1 428  ? 203.977 165.108 150.694 1.00 51.18  ? 428  MET   B CB    1 
ATOM   7742  C  CG    . MET   B 1 428  ? 202.791 164.225 151.042 1.00 50.51  ? 428  MET   B CG    1 
ATOM   7743  S  SD    . MET   B 1 428  ? 201.240 165.136 151.152 1.00 56.28  ? 428  MET   B SD    1 
ATOM   7744  C  CE    . MET   B 1 428  ? 201.185 165.507 152.903 1.00 50.00  ? 428  MET   B CE    1 
ATOM   7745  N  N     . GLU   B 1 429  ? 206.960 164.435 151.929 1.00 48.88  ? 429  GLU   B N     1 
ATOM   7746  C  CA    . GLU   B 1 429  ? 207.884 163.392 152.364 1.00 50.15  ? 429  GLU   B CA    1 
ATOM   7747  C  C     . GLU   B 1 429  ? 208.340 163.618 153.801 1.00 54.57  ? 429  GLU   B C     1 
ATOM   7748  O  O     . GLU   B 1 429  ? 208.437 162.667 154.587 1.00 60.26  ? 429  GLU   B O     1 
ATOM   7749  C  CB    . GLU   B 1 429  ? 209.084 163.330 151.420 1.00 48.23  ? 429  GLU   B CB    1 
ATOM   7750  N  N     . TRP   B 1 430  ? 208.630 164.871 154.160 1.00 52.49  ? 430  TRP   B N     1 
ATOM   7751  C  CA    . TRP   B 1 430  ? 209.021 165.176 155.532 1.00 50.18  ? 430  TRP   B CA    1 
ATOM   7752  C  C     . TRP   B 1 430  ? 207.907 164.816 156.505 1.00 53.94  ? 430  TRP   B C     1 
ATOM   7753  O  O     . TRP   B 1 430  ? 208.164 164.288 157.595 1.00 54.25  ? 430  TRP   B O     1 
ATOM   7754  C  CB    . TRP   B 1 430  ? 209.383 166.655 155.656 1.00 52.65  ? 430  TRP   B CB    1 
ATOM   7755  C  CG    . TRP   B 1 430  ? 210.591 167.049 154.865 1.00 54.19  ? 430  TRP   B CG    1 
ATOM   7756  C  CD1   . TRP   B 1 430  ? 210.686 168.075 153.971 1.00 53.10  ? 430  TRP   B CD1   1 
ATOM   7757  C  CD2   . TRP   B 1 430  ? 211.879 166.423 154.895 1.00 54.02  ? 430  TRP   B CD2   1 
ATOM   7758  N  NE1   . TRP   B 1 430  ? 211.952 168.127 153.442 1.00 54.88  ? 430  TRP   B NE1   1 
ATOM   7759  C  CE2   . TRP   B 1 430  ? 212.704 167.124 153.993 1.00 54.45  ? 430  TRP   B CE2   1 
ATOM   7760  C  CE3   . TRP   B 1 430  ? 212.415 165.339 155.596 1.00 55.33  ? 430  TRP   B CE3   1 
ATOM   7761  C  CZ2   . TRP   B 1 430  ? 214.034 166.776 153.775 1.00 56.23  ? 430  TRP   B CZ2   1 
ATOM   7762  C  CZ3   . TRP   B 1 430  ? 213.736 164.996 155.378 1.00 53.75  ? 430  TRP   B CZ3   1 
ATOM   7763  C  CH2   . TRP   B 1 430  ? 214.530 165.712 154.475 1.00 55.72  ? 430  TRP   B CH2   1 
ATOM   7764  N  N     . GLU   B 1 431  ? 206.661 165.108 156.131 1.00 50.67  ? 431  GLU   B N     1 
ATOM   7765  C  CA    . GLU   B 1 431  ? 205.530 164.731 156.968 1.00 46.98  ? 431  GLU   B CA    1 
ATOM   7766  C  C     . GLU   B 1 431  ? 205.469 163.221 157.155 1.00 50.44  ? 431  GLU   B C     1 
ATOM   7767  O  O     . GLU   B 1 431  ? 205.180 162.737 158.253 1.00 55.35  ? 431  GLU   B O     1 
ATOM   7768  C  CB    . GLU   B 1 431  ? 204.230 165.252 156.355 1.00 48.86  ? 431  GLU   B CB    1 
ATOM   7769  C  CG    . GLU   B 1 431  ? 203.032 165.198 157.288 1.00 54.73  ? 431  GLU   B CG    1 
ATOM   7770  C  CD    . GLU   B 1 431  ? 202.057 164.097 156.921 1.00 58.04  ? 431  GLU   B CD    1 
ATOM   7771  O  OE1   . GLU   B 1 431  ? 202.141 163.584 155.786 1.00 59.32  ? 431  GLU   B OE1   1 
ATOM   7772  O  OE2   . GLU   B 1 431  ? 201.205 163.747 157.765 1.00 57.42  ? 431  GLU   B OE2   1 
ATOM   7773  N  N     . ALA   B 1 432  ? 205.739 162.461 156.092 1.00 38.73  ? 432  ALA   B N     1 
ATOM   7774  C  CA    . ALA   B 1 432  ? 205.730 161.006 156.206 1.00 42.54  ? 432  ALA   B CA    1 
ATOM   7775  C  C     . ALA   B 1 432  ? 206.833 160.516 157.136 1.00 50.58  ? 432  ALA   B C     1 
ATOM   7776  O  O     . ALA   B 1 432  ? 206.619 159.599 157.939 1.00 53.13  ? 432  ALA   B O     1 
ATOM   7777  C  CB    . ALA   B 1 432  ? 205.869 160.372 154.823 1.00 42.57  ? 432  ALA   B CB    1 
ATOM   7778  N  N     . LYS   B 1 433  ? 208.025 161.109 157.037 1.00 48.62  ? 433  LYS   B N     1 
ATOM   7779  C  CA    . LYS   B 1 433  ? 209.110 160.726 157.936 1.00 49.49  ? 433  LYS   B CA    1 
ATOM   7780  C  C     . LYS   B 1 433  ? 208.751 161.020 159.388 1.00 50.08  ? 433  LYS   B C     1 
ATOM   7781  O  O     . LYS   B 1 433  ? 208.987 160.192 160.280 1.00 49.77  ? 433  LYS   B O     1 
ATOM   7782  C  CB    . LYS   B 1 433  ? 210.394 161.452 157.539 1.00 49.41  ? 433  LYS   B CB    1 
ATOM   7783  C  CG    . LYS   B 1 433  ? 211.026 160.932 156.261 1.00 49.55  ? 433  LYS   B CG    1 
ATOM   7784  C  CD    . LYS   B 1 433  ? 211.806 162.021 155.544 1.00 50.90  ? 433  LYS   B CD    1 
ATOM   7785  C  CE    . LYS   B 1 433  ? 212.374 161.513 154.230 1.00 52.12  ? 433  LYS   B CE    1 
ATOM   7786  N  NZ    . LYS   B 1 433  ? 213.007 162.603 153.438 1.00 51.67  ? 433  LYS   B NZ    1 
ATOM   7787  N  N     . ALA   B 1 434  ? 208.179 162.198 159.643 1.00 45.94  ? 434  ALA   B N     1 
ATOM   7788  C  CA    . ALA   B 1 434  ? 207.755 162.534 160.998 1.00 45.29  ? 434  ALA   B CA    1 
ATOM   7789  C  C     . ALA   B 1 434  ? 206.681 161.572 161.489 1.00 50.01  ? 434  ALA   B C     1 
ATOM   7790  O  O     . ALA   B 1 434  ? 206.680 161.171 162.659 1.00 55.33  ? 434  ALA   B O     1 
ATOM   7791  C  CB    . ALA   B 1 434  ? 207.252 163.976 161.048 1.00 45.61  ? 434  ALA   B CB    1 
ATOM   7792  N  N     . GLN   B 1 435  ? 205.753 161.194 160.607 1.00 47.61  ? 435  GLN   B N     1 
ATOM   7793  C  CA    . GLN   B 1 435  ? 204.719 160.236 160.978 1.00 49.06  ? 435  GLN   B CA    1 
ATOM   7794  C  C     . GLN   B 1 435  ? 205.329 158.895 161.358 1.00 49.27  ? 435  GLN   B C     1 
ATOM   7795  O  O     . GLN   B 1 435  ? 204.902 158.262 162.329 1.00 48.39  ? 435  GLN   B O     1 
ATOM   7796  C  CB    . GLN   B 1 435  ? 203.730 160.066 159.825 1.00 50.88  ? 435  GLN   B CB    1 
ATOM   7797  C  CG    . GLN   B 1 435  ? 202.749 161.217 159.653 1.00 50.12  ? 435  GLN   B CG    1 
ATOM   7798  C  CD    . GLN   B 1 435  ? 202.079 161.620 160.950 1.00 54.02  ? 435  GLN   B CD    1 
ATOM   7799  O  OE1   . GLN   B 1 435  ? 201.945 160.816 161.870 1.00 57.40  ? 435  GLN   B OE1   1 
ATOM   7800  N  NE2   . GLN   B 1 435  ? 201.649 162.873 161.026 1.00 54.07  ? 435  GLN   B NE2   1 
ATOM   7801  N  N     . ILE   B 1 436  ? 206.330 158.443 160.599 1.00 41.94  ? 436  ILE   B N     1 
ATOM   7802  C  CA    . ILE   B 1 436  ? 206.985 157.176 160.916 1.00 42.51  ? 436  ILE   B CA    1 
ATOM   7803  C  C     . ILE   B 1 436  ? 207.683 157.261 162.268 1.00 50.20  ? 436  ILE   B C     1 
ATOM   7804  O  O     . ILE   B 1 436  ? 207.621 156.326 163.077 1.00 53.64  ? 436  ILE   B O     1 
ATOM   7805  C  CB    . ILE   B 1 436  ? 207.966 156.783 159.797 1.00 39.56  ? 436  ILE   B CB    1 
ATOM   7806  C  CG1   . ILE   B 1 436  ? 207.203 156.319 158.555 1.00 46.16  ? 436  ILE   B CG1   1 
ATOM   7807  C  CG2   . ILE   B 1 436  ? 208.908 155.692 160.278 1.00 40.97  ? 436  ILE   B CG2   1 
ATOM   7808  C  CD1   . ILE   B 1 436  ? 206.902 154.837 158.538 1.00 44.83  ? 436  ILE   B CD1   1 
ATOM   7809  N  N     . VAL   B 1 437  ? 208.366 158.377 162.531 1.00 40.70  ? 437  VAL   B N     1 
ATOM   7810  C  CA    . VAL   B 1 437  ? 209.048 158.540 163.814 1.00 37.02  ? 437  VAL   B CA    1 
ATOM   7811  C  C     . VAL   B 1 437  ? 208.042 158.497 164.960 1.00 42.30  ? 437  VAL   B C     1 
ATOM   7812  O  O     . VAL   B 1 437  ? 208.254 157.826 165.981 1.00 43.86  ? 437  VAL   B O     1 
ATOM   7813  C  CB    . VAL   B 1 437  ? 209.862 159.846 163.827 1.00 36.41  ? 437  VAL   B CB    1 
ATOM   7814  C  CG1   . VAL   B 1 437  ? 209.983 160.380 165.243 1.00 37.83  ? 437  VAL   B CG1   1 
ATOM   7815  C  CG2   . VAL   B 1 437  ? 211.237 159.622 163.220 1.00 39.07  ? 437  VAL   B CG2   1 
ATOM   7816  N  N     . LEU   B 1 438  ? 206.930 159.221 164.808 1.00 40.43  ? 438  LEU   B N     1 
ATOM   7817  C  CA    . LEU   B 1 438  ? 205.907 159.235 165.848 1.00 35.59  ? 438  LEU   B CA    1 
ATOM   7818  C  C     . LEU   B 1 438  ? 205.316 157.848 166.059 1.00 38.52  ? 438  LEU   B C     1 
ATOM   7819  O  O     . LEU   B 1 438  ? 205.060 157.440 167.199 1.00 44.09  ? 438  LEU   B O     1 
ATOM   7820  C  CB    . LEU   B 1 438  ? 204.811 160.238 165.489 1.00 37.67  ? 438  LEU   B CB    1 
ATOM   7821  C  CG    . LEU   B 1 438  ? 205.014 161.672 165.982 1.00 41.31  ? 438  LEU   B CG    1 
ATOM   7822  C  CD1   . LEU   B 1 438  ? 206.489 162.027 166.019 1.00 40.39  ? 438  LEU   B CD1   1 
ATOM   7823  C  CD2   . LEU   B 1 438  ? 204.252 162.653 165.108 1.00 41.93  ? 438  LEU   B CD2   1 
ATOM   7824  N  N     . LEU   B 1 439  ? 205.080 157.112 164.971 1.00 39.61  ? 439  LEU   B N     1 
ATOM   7825  C  CA    . LEU   B 1 439  ? 204.562 155.755 165.097 1.00 43.87  ? 439  LEU   B CA    1 
ATOM   7826  C  C     . LEU   B 1 439  ? 205.536 154.866 165.855 1.00 43.00  ? 439  LEU   B C     1 
ATOM   7827  O  O     . LEU   B 1 439  ? 205.126 154.074 166.711 1.00 46.36  ? 439  LEU   B O     1 
ATOM   7828  C  CB    . LEU   B 1 439  ? 204.271 155.172 163.715 1.00 44.53  ? 439  LEU   B CB    1 
ATOM   7829  C  CG    . LEU   B 1 439  ? 203.678 153.761 163.708 1.00 42.89  ? 439  LEU   B CG    1 
ATOM   7830  C  CD1   . LEU   B 1 439  ? 202.164 153.811 163.613 1.00 42.24  ? 439  LEU   B CD1   1 
ATOM   7831  C  CD2   . LEU   B 1 439  ? 204.261 152.933 162.575 1.00 41.15  ? 439  LEU   B CD2   1 
ATOM   7832  N  N     . VAL   B 1 440  ? 206.830 154.977 165.551 1.00 40.22  ? 440  VAL   B N     1 
ATOM   7833  C  CA    . VAL   B 1 440  ? 207.822 154.174 166.259 1.00 42.27  ? 440  VAL   B CA    1 
ATOM   7834  C  C     . VAL   B 1 440  ? 207.802 154.502 167.746 1.00 42.10  ? 440  VAL   B C     1 
ATOM   7835  O  O     . VAL   B 1 440  ? 207.841 153.605 168.598 1.00 43.66  ? 440  VAL   B O     1 
ATOM   7836  C  CB    . VAL   B 1 440  ? 209.222 154.386 165.651 1.00 44.40  ? 440  VAL   B CB    1 
ATOM   7837  C  CG1   . VAL   B 1 440  ? 210.295 154.212 166.714 1.00 43.46  ? 440  VAL   B CG1   1 
ATOM   7838  C  CG2   . VAL   B 1 440  ? 209.451 153.425 164.496 1.00 45.50  ? 440  VAL   B CG2   1 
ATOM   7839  N  N     . ILE   B 1 441  ? 207.730 155.792 168.081 1.00 43.88  ? 441  ILE   B N     1 
ATOM   7840  C  CA    . ILE   B 1 441  ? 207.693 156.187 169.488 1.00 39.31  ? 441  ILE   B CA    1 
ATOM   7841  C  C     . ILE   B 1 441  ? 206.456 155.617 170.176 1.00 39.83  ? 441  ILE   B C     1 
ATOM   7842  O  O     . ILE   B 1 441  ? 206.526 155.121 171.309 1.00 41.92  ? 441  ILE   B O     1 
ATOM   7843  C  CB    . ILE   B 1 441  ? 207.755 157.720 169.614 1.00 40.16  ? 441  ILE   B CB    1 
ATOM   7844  C  CG1   . ILE   B 1 441  ? 209.118 158.236 169.150 1.00 37.74  ? 441  ILE   B CG1   1 
ATOM   7845  C  CG2   . ILE   B 1 441  ? 207.484 158.149 171.045 1.00 43.72  ? 441  ILE   B CG2   1 
ATOM   7846  C  CD1   . ILE   B 1 441  ? 209.320 159.717 169.376 1.00 39.58  ? 441  ILE   B CD1   1 
ATOM   7847  N  N     . LEU   B 1 442  ? 205.303 155.686 169.509 1.00 43.37  ? 442  LEU   B N     1 
ATOM   7848  C  CA    . LEU   B 1 442  ? 204.069 155.198 170.119 1.00 43.37  ? 442  LEU   B CA    1 
ATOM   7849  C  C     . LEU   B 1 442  ? 204.102 153.685 170.315 1.00 45.23  ? 442  LEU   B C     1 
ATOM   7850  O  O     . LEU   B 1 442  ? 203.637 153.174 171.344 1.00 48.15  ? 442  LEU   B O     1 
ATOM   7851  C  CB    . LEU   B 1 442  ? 202.868 155.613 169.268 1.00 44.84  ? 442  LEU   B CB    1 
ATOM   7852  C  CG    . LEU   B 1 442  ? 201.538 154.914 169.549 1.00 44.56  ? 442  LEU   B CG    1 
ATOM   7853  C  CD1   . LEU   B 1 442  ? 200.383 155.883 169.377 1.00 44.40  ? 442  LEU   B CD1   1 
ATOM   7854  C  CD2   . LEU   B 1 442  ? 201.363 153.716 168.636 1.00 46.50  ? 442  LEU   B CD2   1 
ATOM   7855  N  N     . LEU   B 1 443  ? 204.638 152.947 169.339 1.00 44.22  ? 443  LEU   B N     1 
ATOM   7856  C  CA    . LEU   B 1 443  ? 204.782 151.505 169.521 1.00 44.38  ? 443  LEU   B CA    1 
ATOM   7857  C  C     . LEU   B 1 443  ? 205.743 151.194 170.658 1.00 48.73  ? 443  LEU   B C     1 
ATOM   7858  O  O     . LEU   B 1 443  ? 205.532 150.240 171.416 1.00 51.68  ? 443  LEU   B O     1 
ATOM   7859  C  CB    . LEU   B 1 443  ? 205.246 150.831 168.228 1.00 44.93  ? 443  LEU   B CB    1 
ATOM   7860  C  CG    . LEU   B 1 443  ? 204.311 150.837 167.017 1.00 49.76  ? 443  LEU   B CG    1 
ATOM   7861  C  CD1   . LEU   B 1 443  ? 204.954 151.517 165.824 1.00 53.03  ? 443  LEU   B CD1   1 
ATOM   7862  C  CD2   . LEU   B 1 443  ? 203.893 149.418 166.663 1.00 48.73  ? 443  LEU   B CD2   1 
ATOM   7863  N  N     . LEU   B 1 444  ? 206.810 151.984 170.792 1.00 48.34  ? 444  LEU   B N     1 
ATOM   7864  C  CA    . LEU   B 1 444  ? 207.705 151.808 171.929 1.00 46.88  ? 444  LEU   B CA    1 
ATOM   7865  C  C     . LEU   B 1 444  ? 206.962 152.008 173.242 1.00 46.72  ? 444  LEU   B C     1 
ATOM   7866  O  O     . LEU   B 1 444  ? 207.165 151.255 174.197 1.00 54.47  ? 444  LEU   B O     1 
ATOM   7867  C  CB    . LEU   B 1 444  ? 208.885 152.773 171.829 1.00 46.54  ? 444  LEU   B CB    1 
ATOM   7868  C  CG    . LEU   B 1 444  ? 209.900 152.491 170.722 1.00 51.02  ? 444  LEU   B CG    1 
ATOM   7869  C  CD1   . LEU   B 1 444  ? 211.060 153.468 170.802 1.00 51.29  ? 444  LEU   B CD1   1 
ATOM   7870  C  CD2   . LEU   B 1 444  ? 210.396 151.060 170.816 1.00 50.03  ? 444  LEU   B CD2   1 
ATOM   7871  N  N     . ALA   B 1 445  ? 206.100 153.023 173.309 1.00 45.30  ? 445  ALA   B N     1 
ATOM   7872  C  CA    . ALA   B 1 445  ? 205.332 153.254 174.531 1.00 48.12  ? 445  ALA   B CA    1 
ATOM   7873  C  C     . ALA   B 1 445  ? 204.406 152.080 174.838 1.00 49.58  ? 445  ALA   B C     1 
ATOM   7874  O  O     . ALA   B 1 445  ? 204.299 151.643 175.993 1.00 53.23  ? 445  ALA   B O     1 
ATOM   7875  C  CB    . ALA   B 1 445  ? 204.533 154.551 174.410 1.00 49.39  ? 445  ALA   B CB    1 
ATOM   7876  N  N     . ILE   B 1 446  ? 203.722 151.560 173.817 1.00 53.16  ? 446  ILE   B N     1 
ATOM   7877  C  CA    . ILE   B 1 446  ? 202.814 150.434 174.034 1.00 51.78  ? 446  ILE   B CA    1 
ATOM   7878  C  C     . ILE   B 1 446  ? 203.589 149.217 174.527 1.00 53.76  ? 446  ILE   B C     1 
ATOM   7879  O  O     . ILE   B 1 446  ? 203.185 148.538 175.482 1.00 53.56  ? 446  ILE   B O     1 
ATOM   7880  C  CB    . ILE   B 1 446  ? 202.028 150.119 172.749 1.00 49.26  ? 446  ILE   B CB    1 
ATOM   7881  C  CG1   . ILE   B 1 446  ? 200.996 151.213 172.473 1.00 51.79  ? 446  ILE   B CG1   1 
ATOM   7882  C  CG2   . ILE   B 1 446  ? 201.348 148.763 172.860 1.00 50.57  ? 446  ILE   B CG2   1 
ATOM   7883  C  CD1   . ILE   B 1 446  ? 200.326 151.094 171.120 1.00 52.75  ? 446  ILE   B CD1   1 
ATOM   7884  N  N     . GLY   B 1 447  ? 204.717 148.923 173.878 1.00 53.81  ? 447  GLY   B N     1 
ATOM   7885  C  CA    . GLY   B 1 447  ? 205.542 147.814 174.318 1.00 53.11  ? 447  GLY   B CA    1 
ATOM   7886  C  C     . GLY   B 1 447  ? 206.093 148.012 175.714 1.00 55.25  ? 447  GLY   B C     1 
ATOM   7887  O  O     . GLY   B 1 447  ? 206.239 147.049 176.468 1.00 57.56  ? 447  GLY   B O     1 
ATOM   7888  N  N     . ASP   B 1 448  ? 206.408 149.256 176.077 1.00 57.32  ? 448  ASP   B N     1 
ATOM   7889  C  CA    . ASP   B 1 448  ? 206.882 149.543 177.424 1.00 51.95  ? 448  ASP   B CA    1 
ATOM   7890  C  C     . ASP   B 1 448  ? 205.798 149.225 178.442 1.00 54.70  ? 448  ASP   B C     1 
ATOM   7891  O  O     . ASP   B 1 448  ? 206.064 148.605 179.478 1.00 61.84  ? 448  ASP   B O     1 
ATOM   7892  C  CB    . ASP   B 1 448  ? 207.321 151.011 177.504 1.00 51.23  ? 448  ASP   B CB    1 
ATOM   7893  C  CG    . ASP   B 1 448  ? 207.357 151.572 178.928 1.00 60.13  ? 448  ASP   B CG    1 
ATOM   7894  O  OD1   . ASP   B 1 448  ? 207.120 150.843 179.912 1.00 67.98  ? 448  ASP   B OD1   1 
ATOM   7895  O  OD2   . ASP   B 1 448  ? 207.632 152.783 179.060 1.00 61.01  ? 448  ASP   B OD2   1 
ATOM   7896  N  N     . PHE   B 1 449  ? 204.561 149.643 178.165 1.00 51.68  ? 449  PHE   B N     1 
ATOM   7897  C  CA    . PHE   B 1 449  ? 203.475 149.320 179.085 1.00 53.14  ? 449  PHE   B CA    1 
ATOM   7898  C  C     . PHE   B 1 449  ? 203.299 147.812 179.209 1.00 49.05  ? 449  PHE   B C     1 
ATOM   7899  O  O     . PHE   B 1 449  ? 203.138 147.283 180.317 1.00 51.69  ? 449  PHE   B O     1 
ATOM   7900  C  CB    . PHE   B 1 449  ? 202.168 149.969 178.629 1.00 56.13  ? 449  PHE   B CB    1 
ATOM   7901  C  CG    . PHE   B 1 449  ? 200.941 149.353 179.247 1.00 52.07  ? 449  PHE   B CG    1 
ATOM   7902  C  CD1   . PHE   B 1 449  ? 200.537 149.717 180.520 1.00 48.20  ? 449  PHE   B CD1   1 
ATOM   7903  C  CD2   . PHE   B 1 449  ? 200.200 148.405 178.562 1.00 53.31  ? 449  PHE   B CD2   1 
ATOM   7904  C  CE1   . PHE   B 1 449  ? 199.415 149.153 181.095 1.00 51.77  ? 449  PHE   B CE1   1 
ATOM   7905  C  CE2   . PHE   B 1 449  ? 199.076 147.838 179.135 1.00 51.34  ? 449  PHE   B CE2   1 
ATOM   7906  C  CZ    . PHE   B 1 449  ? 198.685 148.213 180.401 1.00 49.01  ? 449  PHE   B CZ    1 
ATOM   7907  N  N     . VAL   B 1 450  ? 203.338 147.100 178.080 1.00 52.55  ? 450  VAL   B N     1 
ATOM   7908  C  CA    . VAL   B 1 450  ? 203.117 145.657 178.119 1.00 54.17  ? 450  VAL   B CA    1 
ATOM   7909  C  C     . VAL   B 1 450  ? 204.246 144.958 178.870 1.00 56.20  ? 450  VAL   B C     1 
ATOM   7910  O  O     . VAL   B 1 450  ? 204.014 143.986 179.598 1.00 59.33  ? 450  VAL   B O     1 
ATOM   7911  C  CB    . VAL   B 1 450  ? 202.949 145.098 176.695 1.00 56.23  ? 450  VAL   B CB    1 
ATOM   7912  C  CG1   . VAL   B 1 450  ? 203.306 143.621 176.662 1.00 55.21  ? 450  VAL   B CG1   1 
ATOM   7913  C  CG2   . VAL   B 1 450  ? 201.525 145.312 176.208 1.00 56.10  ? 450  VAL   B CG2   1 
ATOM   7914  N  N     . ILE   B 1 451  ? 205.482 145.427 178.701 1.00 53.22  ? 451  ILE   B N     1 
ATOM   7915  C  CA    . ILE   B 1 451  ? 206.606 144.843 179.427 1.00 46.29  ? 451  ILE   B CA    1 
ATOM   7916  C  C     . ILE   B 1 451  ? 206.468 145.111 180.919 1.00 49.64  ? 451  ILE   B C     1 
ATOM   7917  O  O     . ILE   B 1 451  ? 206.652 144.214 181.749 1.00 53.07  ? 451  ILE   B O     1 
ATOM   7918  C  CB    . ILE   B 1 451  ? 207.939 145.381 178.878 1.00 43.92  ? 451  ILE   B CB    1 
ATOM   7919  N  N     . GLY   B 1 452  ? 206.141 146.352 181.283 1.00 51.83  ? 452  GLY   B N     1 
ATOM   7920  C  CA    . GLY   B 1 452  ? 205.990 146.688 182.687 1.00 45.66  ? 452  GLY   B CA    1 
ATOM   7921  C  C     . GLY   B 1 452  ? 204.864 145.931 183.360 1.00 47.33  ? 452  GLY   B C     1 
ATOM   7922  O  O     . GLY   B 1 452  ? 204.907 145.697 184.570 1.00 54.21  ? 452  GLY   B O     1 
ATOM   7923  N  N     . THR   B 1 453  ? 203.844 145.540 182.594 1.00 48.36  ? 453  THR   B N     1 
ATOM   7924  C  CA    . THR   B 1 453  ? 202.759 144.766 183.187 1.00 47.62  ? 453  THR   B CA    1 
ATOM   7925  C  C     . THR   B 1 453  ? 203.191 143.362 183.594 1.00 49.54  ? 453  THR   B C     1 
ATOM   7926  O  O     . THR   B 1 453  ? 202.446 142.692 184.318 1.00 49.91  ? 453  THR   B O     1 
ATOM   7927  C  CB    . THR   B 1 453  ? 201.575 144.679 182.222 1.00 48.42  ? 453  THR   B CB    1 
ATOM   7928  O  OG1   . THR   B 1 453  ? 200.370 144.463 182.965 1.00 53.90  ? 453  THR   B OG1   1 
ATOM   7929  C  CG2   . THR   B 1 453  ? 201.762 143.530 181.250 1.00 48.21  ? 453  THR   B CG2   1 
ATOM   7930  N  N     . PHE   B 1 454  ? 204.365 142.905 183.156 1.00 55.20  ? 454  PHE   B N     1 
ATOM   7931  C  CA    . PHE   B 1 454  ? 204.890 141.595 183.521 1.00 55.63  ? 454  PHE   B CA    1 
ATOM   7932  C  C     . PHE   B 1 454  ? 205.983 141.667 184.580 1.00 54.43  ? 454  PHE   B C     1 
ATOM   7933  O  O     . PHE   B 1 454  ? 206.551 140.631 184.939 1.00 54.31  ? 454  PHE   B O     1 
ATOM   7934  C  CB    . PHE   B 1 454  ? 205.424 140.869 182.284 1.00 52.55  ? 454  PHE   B CB    1 
ATOM   7935  C  CG    . PHE   B 1 454  ? 204.381 140.089 181.538 1.00 55.43  ? 454  PHE   B CG    1 
ATOM   7936  C  CD1   . PHE   B 1 454  ? 203.053 140.471 181.571 1.00 58.92  ? 454  PHE   B CD1   1 
ATOM   7937  C  CD2   . PHE   B 1 454  ? 204.731 138.967 180.808 1.00 56.00  ? 454  PHE   B CD2   1 
ATOM   7938  C  CE1   . PHE   B 1 454  ? 202.094 139.751 180.887 1.00 58.32  ? 454  PHE   B CE1   1 
ATOM   7939  C  CE2   . PHE   B 1 454  ? 203.776 138.244 180.123 1.00 55.70  ? 454  PHE   B CE2   1 
ATOM   7940  C  CZ    . PHE   B 1 454  ? 202.457 138.637 180.162 1.00 56.28  ? 454  PHE   B CZ    1 
ATOM   7941  N  N     . ILE   B 1 455  ? 206.293 142.856 185.086 1.00 50.96  ? 455  ILE   B N     1 
ATOM   7942  C  CA    . ILE   B 1 455  ? 207.354 143.008 186.077 1.00 47.09  ? 455  ILE   B CA    1 
ATOM   7943  C  C     . ILE   B 1 455  ? 206.751 143.510 187.383 1.00 54.80  ? 455  ILE   B C     1 
ATOM   7944  O  O     . ILE   B 1 455  ? 206.896 144.696 187.714 1.00 56.16  ? 455  ILE   B O     1 
ATOM   7945  C  CB    . ILE   B 1 455  ? 208.453 143.957 185.574 1.00 41.67  ? 455  ILE   B CB    1 
ATOM   7946  N  N     . PRO   B 1 456  ? 206.065 142.660 188.146 1.00 60.71  ? 456  PRO   B N     1 
ATOM   7947  C  CA    . PRO   B 1 456  ? 205.534 143.099 189.446 1.00 56.70  ? 456  PRO   B CA    1 
ATOM   7948  C  C     . PRO   B 1 456  ? 206.646 143.649 190.325 1.00 60.65  ? 456  PRO   B C     1 
ATOM   7949  O  O     . PRO   B 1 456  ? 207.721 143.058 190.442 1.00 61.66  ? 456  PRO   B O     1 
ATOM   7950  C  CB    . PRO   B 1 456  ? 204.925 141.822 190.039 1.00 56.10  ? 456  PRO   B CB    1 
ATOM   7951  C  CG    . PRO   B 1 456  ? 204.885 140.814 188.945 1.00 58.89  ? 456  PRO   B CG    1 
ATOM   7952  C  CD    . PRO   B 1 456  ? 205.527 141.360 187.715 1.00 59.89  ? 456  PRO   B CD    1 
ATOM   7953  N  N     . LEU   B 1 457  ? 206.375 144.792 190.952 1.00 64.74  ? 457  LEU   B N     1 
ATOM   7954  C  CA    . LEU   B 1 457  ? 207.327 145.455 191.831 1.00 62.32  ? 457  LEU   B CA    1 
ATOM   7955  C  C     . LEU   B 1 457  ? 206.602 145.909 193.088 1.00 63.94  ? 457  LEU   B C     1 
ATOM   7956  O  O     . LEU   B 1 457  ? 205.556 146.560 193.003 1.00 67.30  ? 457  LEU   B O     1 
ATOM   7957  C  CB    . LEU   B 1 457  ? 207.989 146.650 191.136 1.00 56.41  ? 457  LEU   B CB    1 
ATOM   7958  N  N     . GLU   B 1 458  ? 207.158 145.563 194.251 1.00 66.56  ? 458  GLU   B N     1 
ATOM   7959  C  CA    . GLU   B 1 458  ? 206.517 145.908 195.514 1.00 67.05  ? 458  GLU   B CA    1 
ATOM   7960  C  C     . GLU   B 1 458  ? 206.348 147.412 195.685 1.00 67.16  ? 458  GLU   B C     1 
ATOM   7961  O  O     . GLU   B 1 458  ? 205.482 147.843 196.454 1.00 67.46  ? 458  GLU   B O     1 
ATOM   7962  C  CB    . GLU   B 1 458  ? 207.319 145.336 196.683 1.00 65.15  ? 458  GLU   B CB    1 
ATOM   7963  N  N     . SER   B 1 459  ? 207.148 148.219 194.988 1.00 70.56  ? 459  SER   B N     1 
ATOM   7964  C  CA    . SER   B 1 459  ? 207.011 149.667 195.106 1.00 71.55  ? 459  SER   B CA    1 
ATOM   7965  C  C     . SER   B 1 459  ? 205.625 150.125 194.673 1.00 72.78  ? 459  SER   B C     1 
ATOM   7966  O  O     . SER   B 1 459  ? 205.041 151.026 195.286 1.00 71.87  ? 459  SER   B O     1 
ATOM   7967  C  CB    . SER   B 1 459  ? 208.092 150.363 194.280 1.00 74.67  ? 459  SER   B CB    1 
ATOM   7968  O  OG    . SER   B 1 459  ? 207.882 151.764 194.239 1.00 76.51  ? 459  SER   B OG    1 
ATOM   7969  N  N     . LYS   B 1 460  ? 205.082 149.516 193.620 1.00 70.49  ? 460  LYS   B N     1 
ATOM   7970  C  CA    . LYS   B 1 460  ? 203.755 149.865 193.129 1.00 66.17  ? 460  LYS   B CA    1 
ATOM   7971  C  C     . LYS   B 1 460  ? 202.640 149.175 193.900 1.00 68.07  ? 460  LYS   B C     1 
ATOM   7972  O  O     . LYS   B 1 460  ? 201.465 149.440 193.624 1.00 70.09  ? 460  LYS   B O     1 
ATOM   7973  C  CB    . LYS   B 1 460  ? 203.631 149.526 191.640 1.00 66.30  ? 460  LYS   B CB    1 
ATOM   7974  C  CG    . LYS   B 1 460  ? 204.550 150.328 190.733 1.00 66.86  ? 460  LYS   B CG    1 
ATOM   7975  C  CD    . LYS   B 1 460  ? 205.067 149.477 189.583 1.00 65.03  ? 460  LYS   B CD    1 
ATOM   7976  C  CE    . LYS   B 1 460  ? 206.050 150.254 188.724 1.00 65.46  ? 460  LYS   B CE    1 
ATOM   7977  N  NZ    . LYS   B 1 460  ? 206.779 149.361 187.784 1.00 64.92  ? 460  LYS   B NZ    1 
ATOM   7978  N  N     . LYS   B 1 461  ? 202.972 148.302 194.849 1.00 66.76  ? 461  LYS   B N     1 
ATOM   7979  C  CA    . LYS   B 1 461  ? 201.949 147.620 195.639 1.00 60.06  ? 461  LYS   B CA    1 
ATOM   7980  C  C     . LYS   B 1 461  ? 200.952 148.583 196.267 1.00 61.14  ? 461  LYS   B C     1 
ATOM   7981  O  O     . LYS   B 1 461  ? 199.742 148.309 196.207 1.00 56.58  ? 461  LYS   B O     1 
ATOM   7982  C  CB    . LYS   B 1 461  ? 202.636 146.752 196.702 1.00 59.68  ? 461  LYS   B CB    1 
ATOM   7983  N  N     . PRO   B 1 462  ? 201.366 149.701 196.867 1.00 70.94  ? 462  PRO   B N     1 
ATOM   7984  C  CA    . PRO   B 1 462  ? 200.370 150.690 197.352 1.00 68.61  ? 462  PRO   B CA    1 
ATOM   7985  C  C     . PRO   B 1 462  ? 199.444 151.201 196.267 1.00 71.38  ? 462  PRO   B C     1 
ATOM   7986  O  O     . PRO   B 1 462  ? 198.269 151.481 196.539 1.00 70.79  ? 462  PRO   B O     1 
ATOM   7987  C  CB    . PRO   B 1 462  ? 201.350 151.749 197.873 1.00 70.83  ? 462  PRO   B CB    1 
ATOM   7988  C  CG    . PRO   B 1 462  ? 202.255 150.658 198.303 1.00 72.37  ? 462  PRO   B CG    1 
ATOM   7989  C  CD    . PRO   B 1 462  ? 202.655 150.400 197.059 1.00 71.19  ? 462  PRO   B CD    1 
ATOM   7990  N  N     . LYS   B 1 463  ? 199.943 151.334 195.041 1.00 75.72  ? 463  LYS   B N     1 
ATOM   7991  C  CA    . LYS   B 1 463  ? 199.083 151.581 193.898 1.00 70.81  ? 463  LYS   B CA    1 
ATOM   7992  C  C     . LYS   B 1 463  ? 198.315 150.313 193.532 1.00 67.03  ? 463  LYS   B C     1 
ATOM   7993  O  O     . LYS   B 1 463  ? 198.640 149.208 193.972 1.00 70.92  ? 463  LYS   B O     1 
ATOM   7994  C  CB    . LYS   B 1 463  ? 199.905 152.063 192.701 1.00 70.66  ? 463  LYS   B CB    1 
ATOM   7995  C  CG    . LYS   B 1 463  ? 201.018 153.042 193.040 1.00 70.37  ? 463  LYS   B CG    1 
ATOM   7996  C  CD    . LYS   B 1 463  ? 200.451 154.335 193.591 1.00 69.05  ? 463  LYS   B CD    1 
ATOM   7997  C  CE    . LYS   B 1 463  ? 201.554 155.273 194.047 1.00 70.81  ? 463  LYS   B CE    1 
ATOM   7998  N  NZ    . LYS   B 1 463  ? 202.825 154.550 194.320 1.00 71.08  ? 463  LYS   B NZ    1 
ATOM   7999  N  N     . GLY   B 1 464  ? 197.280 150.486 192.708 1.00 57.47  ? 464  GLY   B N     1 
ATOM   8000  C  CA    . GLY   B 1 464  ? 196.421 149.363 192.368 1.00 61.93  ? 464  GLY   B CA    1 
ATOM   8001  C  C     . GLY   B 1 464  ? 197.143 148.219 191.684 1.00 63.32  ? 464  GLY   B C     1 
ATOM   8002  O  O     . GLY   B 1 464  ? 196.700 147.069 191.758 1.00 64.57  ? 464  GLY   B O     1 
ATOM   8003  N  N     . PHE   B 1 465  ? 198.254 148.507 191.011 1.00 58.30  ? 465  PHE   B N     1 
ATOM   8004  C  CA    . PHE   B 1 465  ? 198.946 147.481 190.241 1.00 58.90  ? 465  PHE   B CA    1 
ATOM   8005  C  C     . PHE   B 1 465  ? 199.409 146.351 191.152 1.00 56.18  ? 465  PHE   B C     1 
ATOM   8006  O  O     . PHE   B 1 465  ? 199.991 146.590 192.213 1.00 56.57  ? 465  PHE   B O     1 
ATOM   8007  C  CB    . PHE   B 1 465  ? 200.132 148.099 189.501 1.00 57.11  ? 465  PHE   B CB    1 
ATOM   8008  C  CG    . PHE   B 1 465  ? 200.943 147.109 188.714 1.00 53.90  ? 465  PHE   B CG    1 
ATOM   8009  C  CD1   . PHE   B 1 465  ? 200.325 146.121 187.966 1.00 52.54  ? 465  PHE   B CD1   1 
ATOM   8010  C  CD2   . PHE   B 1 465  ? 202.325 147.174 188.712 1.00 54.45  ? 465  PHE   B CD2   1 
ATOM   8011  C  CE1   . PHE   B 1 465  ? 201.073 145.211 187.239 1.00 52.81  ? 465  PHE   B CE1   1 
ATOM   8012  C  CE2   . PHE   B 1 465  ? 203.076 146.267 187.986 1.00 55.17  ? 465  PHE   B CE2   1 
ATOM   8013  C  CZ    . PHE   B 1 465  ? 202.449 145.285 187.250 1.00 53.16  ? 465  PHE   B CZ    1 
ATOM   8014  N  N     . PHE   B 1 466  ? 199.147 145.112 190.732 1.00 63.61  ? 466  PHE   B N     1 
ATOM   8015  C  CA    . PHE   B 1 466  ? 199.456 143.956 191.566 1.00 62.43  ? 466  PHE   B CA    1 
ATOM   8016  C  C     . PHE   B 1 466  ? 200.278 142.898 190.838 1.00 62.53  ? 466  PHE   B C     1 
ATOM   8017  O  O     . PHE   B 1 466  ? 201.039 142.167 191.479 1.00 67.12  ? 466  PHE   B O     1 
ATOM   8018  C  CB    . PHE   B 1 466  ? 198.171 143.337 192.117 1.00 63.32  ? 466  PHE   B CB    1 
ATOM   8019  C  CG    . PHE   B 1 466  ? 197.847 143.772 193.519 1.00 64.42  ? 466  PHE   B CG    1 
ATOM   8020  C  CD1   . PHE   B 1 466  ? 198.779 143.626 194.533 1.00 63.54  ? 466  PHE   B CD1   1 
ATOM   8021  C  CD2   . PHE   B 1 466  ? 196.618 144.333 193.823 1.00 64.07  ? 466  PHE   B CD2   1 
ATOM   8022  C  CE1   . PHE   B 1 466  ? 198.490 144.028 195.823 1.00 65.33  ? 466  PHE   B CE1   1 
ATOM   8023  C  CE2   . PHE   B 1 466  ? 196.325 144.736 195.114 1.00 64.07  ? 466  PHE   B CE2   1 
ATOM   8024  C  CZ    . PHE   B 1 466  ? 197.261 144.583 196.113 1.00 65.75  ? 466  PHE   B CZ    1 
ATOM   8025  N  N     . GLY   B 1 467  ? 200.150 142.797 189.515 1.00 66.18  ? 467  GLY   B N     1 
ATOM   8026  C  CA    . GLY   B 1 467  ? 200.992 141.851 188.807 1.00 66.32  ? 467  GLY   B CA    1 
ATOM   8027  C  C     . GLY   B 1 467  ? 200.319 140.723 188.050 1.00 66.39  ? 467  GLY   B C     1 
ATOM   8028  O  O     . GLY   B 1 467  ? 200.838 139.602 188.030 1.00 71.96  ? 467  GLY   B O     1 
ATOM   8029  N  N     . TYR   B 1 468  ? 199.167 140.984 187.430 1.00 61.99  ? 468  TYR   B N     1 
ATOM   8030  C  CA    . TYR   B 1 468  ? 198.518 139.993 186.570 1.00 63.34  ? 468  TYR   B CA    1 
ATOM   8031  C  C     . TYR   B 1 468  ? 198.013 138.795 187.379 1.00 64.76  ? 468  TYR   B C     1 
ATOM   8032  O  O     . TYR   B 1 468  ? 198.314 137.641 187.072 1.00 66.84  ? 468  TYR   B O     1 
ATOM   8033  C  CB    . TYR   B 1 468  ? 199.476 139.538 185.464 1.00 67.34  ? 468  TYR   B CB    1 
ATOM   8034  C  CG    . TYR   B 1 468  ? 198.813 139.091 184.180 1.00 70.37  ? 468  TYR   B CG    1 
ATOM   8035  C  CD1   . TYR   B 1 468  ? 198.955 139.828 183.012 1.00 65.46  ? 468  TYR   B CD1   1 
ATOM   8036  C  CD2   . TYR   B 1 468  ? 198.060 137.925 184.131 1.00 72.71  ? 468  TYR   B CD2   1 
ATOM   8037  C  CE1   . TYR   B 1 468  ? 198.357 139.423 181.833 1.00 69.23  ? 468  TYR   B CE1   1 
ATOM   8038  C  CE2   . TYR   B 1 468  ? 197.458 137.512 182.957 1.00 72.81  ? 468  TYR   B CE2   1 
ATOM   8039  C  CZ    . TYR   B 1 468  ? 197.609 138.264 181.812 1.00 72.01  ? 468  TYR   B CZ    1 
ATOM   8040  O  OH    . TYR   B 1 468  ? 197.010 137.852 180.643 1.00 64.54  ? 468  TYR   B OH    1 
ATOM   8041  N  N     . LYS   B 1 469  ? 197.235 139.082 188.419 1.00 64.95  ? 469  LYS   B N     1 
ATOM   8042  C  CA    . LYS   B 1 469  ? 196.685 138.059 189.297 1.00 62.24  ? 469  LYS   B CA    1 
ATOM   8043  C  C     . LYS   B 1 469  ? 195.248 137.735 188.906 1.00 62.51  ? 469  LYS   B C     1 
ATOM   8044  O  O     . LYS   B 1 469  ? 194.450 138.634 188.626 1.00 64.70  ? 469  LYS   B O     1 
ATOM   8045  C  CB    . LYS   B 1 469  ? 196.739 138.508 190.758 1.00 62.88  ? 469  LYS   B CB    1 
ATOM   8046  C  CG    . LYS   B 1 469  ? 198.134 138.482 191.352 1.00 64.84  ? 469  LYS   B CG    1 
ATOM   8047  C  CD    . LYS   B 1 469  ? 198.880 137.229 190.930 1.00 63.68  ? 469  LYS   B CD    1 
ATOM   8048  C  CE    . LYS   B 1 469  ? 200.371 137.489 190.827 1.00 63.74  ? 469  LYS   B CE    1 
ATOM   8049  N  NZ    . LYS   B 1 469  ? 200.857 138.346 191.942 1.00 63.55  ? 469  LYS   B NZ    1 
ATOM   8050  N  N     . SER   B 1 470  ? 194.930 136.438 188.889 1.00 63.32  ? 470  SER   B N     1 
ATOM   8051  C  CA    . SER   B 1 470  ? 193.612 135.995 188.442 1.00 65.42  ? 470  SER   B CA    1 
ATOM   8052  C  C     . SER   B 1 470  ? 192.495 136.645 189.249 1.00 64.13  ? 470  SER   B C     1 
ATOM   8053  O  O     . SER   B 1 470  ? 191.502 137.115 188.680 1.00 68.63  ? 470  SER   B O     1 
ATOM   8054  C  CB    . SER   B 1 470  ? 193.516 134.472 188.527 1.00 65.21  ? 470  SER   B CB    1 
ATOM   8055  O  OG    . SER   B 1 470  ? 194.237 133.854 187.475 1.00 66.74  ? 470  SER   B OG    1 
ATOM   8056  N  N     . GLU   B 1 471  ? 192.639 136.683 190.577 1.00 67.02  ? 471  GLU   B N     1 
ATOM   8057  C  CA    . GLU   B 1 471  ? 191.577 137.217 191.426 1.00 71.93  ? 471  GLU   B CA    1 
ATOM   8058  C  C     . GLU   B 1 471  ? 191.135 138.597 190.959 1.00 75.38  ? 471  GLU   B C     1 
ATOM   8059  O  O     . GLU   B 1 471  ? 189.936 138.902 190.941 1.00 75.20  ? 471  GLU   B O     1 
ATOM   8060  C  CB    . GLU   B 1 471  ? 192.044 137.271 192.881 1.00 72.44  ? 471  GLU   B CB    1 
ATOM   8061  C  CG    . GLU   B 1 471  ? 192.435 135.922 193.465 1.00 74.90  ? 471  GLU   B CG    1 
ATOM   8062  C  CD    . GLU   B 1 471  ? 193.894 135.588 193.229 1.00 77.21  ? 471  GLU   B CD    1 
ATOM   8063  O  OE1   . GLU   B 1 471  ? 194.739 136.498 193.361 1.00 75.18  ? 471  GLU   B OE1   1 
ATOM   8064  O  OE2   . GLU   B 1 471  ? 194.197 134.418 192.915 1.00 78.15  ? 471  GLU   B OE2   1 
ATOM   8065  N  N     . ILE   B 1 472  ? 192.089 139.446 190.574 1.00 64.63  ? 472  ILE   B N     1 
ATOM   8066  C  CA    . ILE   B 1 472  ? 191.742 140.756 190.032 1.00 57.50  ? 472  ILE   B CA    1 
ATOM   8067  C  C     . ILE   B 1 472  ? 190.914 140.599 188.765 1.00 60.36  ? 472  ILE   B C     1 
ATOM   8068  O  O     . ILE   B 1 472  ? 189.952 141.341 188.537 1.00 59.28  ? 472  ILE   B O     1 
ATOM   8069  C  CB    . ILE   B 1 472  ? 193.015 141.584 189.777 1.00 53.57  ? 472  ILE   B CB    1 
ATOM   8070  C  CG1   . ILE   B 1 472  ? 193.674 141.967 191.102 1.00 57.18  ? 472  ILE   B CG1   1 
ATOM   8071  C  CG2   . ILE   B 1 472  ? 192.684 142.827 188.969 1.00 59.87  ? 472  ILE   B CG2   1 
ATOM   8072  C  CD1   . ILE   B 1 472  ? 195.179 142.070 191.024 1.00 58.21  ? 472  ILE   B CD1   1 
ATOM   8073  N  N     . PHE   B 1 473  ? 191.279 139.635 187.916 1.00 60.95  ? 473  PHE   B N     1 
ATOM   8074  C  CA    . PHE   B 1 473  ? 190.530 139.407 186.685 1.00 58.31  ? 473  PHE   B CA    1 
ATOM   8075  C  C     . PHE   B 1 473  ? 189.081 139.046 186.984 1.00 62.12  ? 473  PHE   B C     1 
ATOM   8076  O  O     . PHE   B 1 473  ? 188.153 139.612 186.395 1.00 63.77  ? 473  PHE   B O     1 
ATOM   8077  C  CB    . PHE   B 1 473  ? 191.202 138.310 185.858 1.00 58.10  ? 473  PHE   B CB    1 
ATOM   8078  C  CG    . PHE   B 1 473  ? 190.385 137.847 184.683 1.00 61.34  ? 473  PHE   B CG    1 
ATOM   8079  C  CD1   . PHE   B 1 473  ? 189.454 136.831 184.822 1.00 61.85  ? 473  PHE   B CD1   1 
ATOM   8080  C  CD2   . PHE   B 1 473  ? 190.545 138.434 183.439 1.00 63.91  ? 473  PHE   B CD2   1 
ATOM   8081  C  CE1   . PHE   B 1 473  ? 188.701 136.409 183.743 1.00 62.09  ? 473  PHE   B CE1   1 
ATOM   8082  C  CE2   . PHE   B 1 473  ? 189.795 138.014 182.358 1.00 63.73  ? 473  PHE   B CE2   1 
ATOM   8083  C  CZ    . PHE   B 1 473  ? 188.872 137.001 182.511 1.00 62.47  ? 473  PHE   B CZ    1 
ATOM   8084  N  N     . ASN   B 1 474  ? 188.867 138.099 187.900 1.00 65.31  ? 474  ASN   B N     1 
ATOM   8085  C  CA    . ASN   B 1 474  ? 187.499 137.718 188.240 1.00 60.94  ? 474  ASN   B CA    1 
ATOM   8086  C  C     . ASN   B 1 474  ? 186.744 138.872 188.882 1.00 61.79  ? 474  ASN   B C     1 
ATOM   8087  O  O     . ASN   B 1 474  ? 185.547 139.047 188.629 1.00 64.73  ? 474  ASN   B O     1 
ATOM   8088  C  CB    . ASN   B 1 474  ? 187.488 136.497 189.160 1.00 63.36  ? 474  ASN   B CB    1 
ATOM   8089  C  CG    . ASN   B 1 474  ? 188.625 135.537 188.876 1.00 67.77  ? 474  ASN   B CG    1 
ATOM   8090  O  OD1   . ASN   B 1 474  ? 189.698 135.633 189.469 1.00 67.08  ? 474  ASN   B OD1   1 
ATOM   8091  N  ND2   . ASN   B 1 474  ? 188.395 134.606 187.959 1.00 65.22  ? 474  ASN   B ND2   1 
ATOM   8092  N  N     . GLU   B 1 475  ? 187.419 139.669 189.711 1.00 60.33  ? 475  GLU   B N     1 
ATOM   8093  C  CA    . GLU   B 1 475  ? 186.762 140.819 190.320 1.00 60.93  ? 475  GLU   B CA    1 
ATOM   8094  C  C     . GLU   B 1 475  ? 186.318 141.826 189.266 1.00 66.30  ? 475  GLU   B C     1 
ATOM   8095  O  O     . GLU   B 1 475  ? 185.209 142.367 189.340 1.00 65.32  ? 475  GLU   B O     1 
ATOM   8096  C  CB    . GLU   B 1 475  ? 187.696 141.480 191.333 1.00 59.58  ? 475  GLU   B CB    1 
ATOM   8097  N  N     . ASN   B 1 476  ? 187.168 142.087 188.274 1.00 64.15  ? 476  ASN   B N     1 
ATOM   8098  C  CA    . ASN   B 1 476  ? 186.926 143.136 187.293 1.00 55.12  ? 476  ASN   B CA    1 
ATOM   8099  C  C     . ASN   B 1 476  ? 186.125 142.668 186.084 1.00 56.72  ? 476  ASN   B C     1 
ATOM   8100  O  O     . ASN   B 1 476  ? 185.720 143.505 185.271 1.00 65.22  ? 476  ASN   B O     1 
ATOM   8101  C  CB    . ASN   B 1 476  ? 188.258 143.728 186.824 1.00 52.97  ? 476  ASN   B CB    1 
ATOM   8102  C  CG    . ASN   B 1 476  ? 188.853 144.688 187.832 1.00 55.44  ? 476  ASN   B CG    1 
ATOM   8103  O  OD1   . ASN   B 1 476  ? 188.169 145.154 188.742 1.00 54.08  ? 476  ASN   B OD1   1 
ATOM   8104  N  ND2   . ASN   B 1 476  ? 190.138 144.985 187.679 1.00 56.13  ? 476  ASN   B ND2   1 
ATOM   8105  N  N     . PHE   B 1 477  ? 185.878 141.365 185.943 1.00 51.45  ? 477  PHE   B N     1 
ATOM   8106  C  CA    . PHE   B 1 477  ? 185.128 140.882 184.790 1.00 48.03  ? 477  PHE   B CA    1 
ATOM   8107  C  C     . PHE   B 1 477  ? 183.694 141.393 184.767 1.00 45.22  ? 477  PHE   B C     1 
ATOM   8108  O  O     . PHE   B 1 477  ? 183.052 141.336 183.714 1.00 51.74  ? 477  PHE   B O     1 
ATOM   8109  C  CB    . PHE   B 1 477  ? 185.139 139.351 184.755 1.00 50.58  ? 477  PHE   B CB    1 
ATOM   8110  C  CG    . PHE   B 1 477  ? 184.587 138.766 183.482 1.00 48.66  ? 477  PHE   B CG    1 
ATOM   8111  C  CD1   . PHE   B 1 477  ? 183.233 138.511 183.344 1.00 49.44  ? 477  PHE   B CD1   1 
ATOM   8112  C  CD2   . PHE   B 1 477  ? 185.426 138.482 182.418 1.00 54.88  ? 477  PHE   B CD2   1 
ATOM   8113  C  CE1   . PHE   B 1 477  ? 182.729 137.979 182.173 1.00 50.93  ? 477  PHE   B CE1   1 
ATOM   8114  C  CE2   . PHE   B 1 477  ? 184.927 137.950 181.245 1.00 54.53  ? 477  PHE   B CE2   1 
ATOM   8115  C  CZ    . PHE   B 1 477  ? 183.577 137.699 181.123 1.00 51.70  ? 477  PHE   B CZ    1 
ATOM   8116  N  N     . GLY   B 1 478  ? 183.184 141.905 185.884 1.00 45.27  ? 478  GLY   B N     1 
ATOM   8117  C  CA    . GLY   B 1 478  ? 181.825 142.384 185.946 1.00 47.53  ? 478  GLY   B CA    1 
ATOM   8118  C  C     . GLY   B 1 478  ? 181.726 143.895 185.971 1.00 47.03  ? 478  GLY   B C     1 
ATOM   8119  O  O     . GLY   B 1 478  ? 182.657 144.603 186.367 1.00 50.48  ? 478  GLY   B O     1 
ATOM   8120  N  N     . PRO   B 1 479  ? 180.580 144.417 185.545 1.00 41.50  ? 479  PRO   B N     1 
ATOM   8121  C  CA    . PRO   B 1 479  ? 180.396 145.871 185.514 1.00 42.79  ? 479  PRO   B CA    1 
ATOM   8122  C  C     . PRO   B 1 479  ? 180.384 146.477 186.907 1.00 49.56  ? 479  PRO   B C     1 
ATOM   8123  O  O     . PRO   B 1 479  ? 179.981 145.844 187.886 1.00 58.26  ? 479  PRO   B O     1 
ATOM   8124  C  CB    . PRO   B 1 479  ? 179.034 146.041 184.830 1.00 45.43  ? 479  PRO   B CB    1 
ATOM   8125  C  CG    . PRO   B 1 479  ? 178.779 144.737 184.138 1.00 49.60  ? 479  PRO   B CG    1 
ATOM   8126  C  CD    . PRO   B 1 479  ? 179.416 143.702 185.001 1.00 45.54  ? 479  PRO   B CD    1 
ATOM   8127  N  N     . ASP   B 1 480  ? 180.843 147.726 186.986 1.00 53.51  ? 480  ASP   B N     1 
ATOM   8128  C  CA    . ASP   B 1 480  ? 180.713 148.533 188.192 1.00 52.06  ? 480  ASP   B CA    1 
ATOM   8129  C  C     . ASP   B 1 480  ? 179.827 149.750 187.960 1.00 53.18  ? 480  ASP   B C     1 
ATOM   8130  O  O     . ASP   B 1 480  ? 178.840 149.947 188.674 1.00 65.15  ? 480  ASP   B O     1 
ATOM   8131  C  CB    . ASP   B 1 480  ? 182.097 148.971 188.691 1.00 52.52  ? 480  ASP   B CB    1 
ATOM   8132  C  CG    . ASP   B 1 480  ? 182.021 150.109 189.692 1.00 60.42  ? 480  ASP   B CG    1 
ATOM   8133  O  OD1   . ASP   B 1 480  ? 181.961 151.280 189.262 1.00 61.56  ? 480  ASP   B OD1   1 
ATOM   8134  O  OD2   . ASP   B 1 480  ? 182.023 149.833 190.910 1.00 56.94  ? 480  ASP   B OD2   1 
ATOM   8135  N  N     . PHE   B 1 481  ? 180.154 150.571 186.962 1.00 57.22  ? 481  PHE   B N     1 
ATOM   8136  C  CA    . PHE   B 1 481  ? 179.390 151.773 186.633 1.00 59.52  ? 481  PHE   B CA    1 
ATOM   8137  C  C     . PHE   B 1 481  ? 179.176 152.646 187.870 1.00 58.89  ? 481  PHE   B C     1 
ATOM   8138  O  O     . PHE   B 1 481  ? 178.053 152.879 188.322 1.00 63.15  ? 481  PHE   B O     1 
ATOM   8139  C  CB    . PHE   B 1 481  ? 178.060 151.413 185.964 1.00 57.28  ? 481  PHE   B CB    1 
ATOM   8140  C  CG    . PHE   B 1 481  ? 178.222 150.735 184.637 1.00 57.40  ? 481  PHE   B CG    1 
ATOM   8141  C  CD1   . PHE   B 1 481  ? 178.397 151.479 183.485 1.00 58.24  ? 481  PHE   B CD1   1 
ATOM   8142  C  CD2   . PHE   B 1 481  ? 178.198 149.356 184.538 1.00 57.64  ? 481  PHE   B CD2   1 
ATOM   8143  C  CE1   . PHE   B 1 481  ? 178.551 150.861 182.263 1.00 62.54  ? 481  PHE   B CE1   1 
ATOM   8144  C  CE2   . PHE   B 1 481  ? 178.347 148.734 183.316 1.00 58.83  ? 481  PHE   B CE2   1 
ATOM   8145  C  CZ    . PHE   B 1 481  ? 178.524 149.487 182.178 1.00 60.34  ? 481  PHE   B CZ    1 
ATOM   8146  N  N     . ARG   B 1 482  ? 180.289 153.132 188.412 1.00 58.47  ? 482  ARG   B N     1 
ATOM   8147  C  CA    . ARG   B 1 482  ? 180.250 154.018 189.562 1.00 59.88  ? 482  ARG   B CA    1 
ATOM   8148  C  C     . ARG   B 1 482  ? 179.698 155.383 189.155 1.00 59.91  ? 482  ARG   B C     1 
ATOM   8149  O  O     . ARG   B 1 482  ? 179.383 155.638 187.989 1.00 63.52  ? 482  ARG   B O     1 
ATOM   8150  C  CB    . ARG   B 1 482  ? 181.645 154.156 190.165 1.00 60.11  ? 482  ARG   B CB    1 
ATOM   8151  C  CG    . ARG   B 1 482  ? 181.678 154.204 191.680 1.00 61.03  ? 482  ARG   B CG    1 
ATOM   8152  C  CD    . ARG   B 1 482  ? 183.062 153.857 192.198 1.00 61.06  ? 482  ARG   B CD    1 
ATOM   8153  N  NE    . ARG   B 1 482  ? 183.282 152.417 192.224 1.00 60.82  ? 482  ARG   B NE    1 
ATOM   8154  C  CZ    . ARG   B 1 482  ? 184.351 151.830 192.744 1.00 63.22  ? 482  ARG   B CZ    1 
ATOM   8155  N  NH1   . ARG   B 1 482  ? 185.326 152.534 193.296 1.00 60.94  ? 482  ARG   B NH1   1 
ATOM   8156  N  NH2   . ARG   B 1 482  ? 184.446 150.504 192.709 1.00 64.01  ? 482  ARG   B NH2   1 
ATOM   8157  N  N     . GLU   B 1 483  ? 179.584 156.270 190.134 1.00 63.08  ? 483  GLU   B N     1 
ATOM   8158  C  CA    . GLU   B 1 483  ? 179.156 157.653 189.912 1.00 64.77  ? 483  GLU   B CA    1 
ATOM   8159  C  C     . GLU   B 1 483  ? 177.885 157.648 189.060 1.00 65.03  ? 483  GLU   B C     1 
ATOM   8160  O  O     . GLU   B 1 483  ? 177.131 156.669 189.050 1.00 62.86  ? 483  GLU   B O     1 
ATOM   8161  C  CB    . GLU   B 1 483  ? 180.310 158.445 189.325 1.00 59.42  ? 483  GLU   B CB    1 
ATOM   8162  N  N     . GLU   B 1 484  ? 177.635 158.737 188.339 1.00 67.26  ? 484  GLU   B N     1 
ATOM   8163  C  CA    . GLU   B 1 484  ? 176.486 158.826 187.441 1.00 67.77  ? 484  GLU   B CA    1 
ATOM   8164  C  C     . GLU   B 1 484  ? 176.917 158.427 186.030 1.00 69.14  ? 484  GLU   B C     1 
ATOM   8165  O  O     . GLU   B 1 484  ? 176.902 159.215 185.084 1.00 70.09  ? 484  GLU   B O     1 
ATOM   8166  C  CB    . GLU   B 1 484  ? 175.893 160.232 187.476 1.00 66.99  ? 484  GLU   B CB    1 
ATOM   8167  N  N     . GLU   B 1 485  ? 177.311 157.161 185.911 1.00 68.07  ? 485  GLU   B N     1 
ATOM   8168  C  CA    . GLU   B 1 485  ? 177.800 156.602 184.658 1.00 62.43  ? 485  GLU   B CA    1 
ATOM   8169  C  C     . GLU   B 1 485  ? 176.938 155.414 184.265 1.00 64.47  ? 485  GLU   B C     1 
ATOM   8170  O  O     . GLU   B 1 485  ? 176.510 154.641 185.127 1.00 69.32  ? 485  GLU   B O     1 
ATOM   8171  C  CB    . GLU   B 1 485  ? 179.266 156.176 184.778 1.00 64.83  ? 485  GLU   B CB    1 
ATOM   8172  C  CG    . GLU   B 1 485  ? 180.205 157.303 185.164 1.00 70.27  ? 485  GLU   B CG    1 
ATOM   8173  C  CD    . GLU   B 1 485  ? 180.393 158.307 184.046 1.00 72.30  ? 485  GLU   B CD    1 
ATOM   8174  O  OE1   . GLU   B 1 485  ? 180.048 159.491 184.242 1.00 73.86  ? 485  GLU   B OE1   1 
ATOM   8175  O  OE2   . GLU   B 1 485  ? 180.885 157.912 182.968 1.00 71.03  ? 485  GLU   B OE2   1 
ATOM   8176  N  N     . THR   B 1 486  ? 176.685 155.277 182.967 1.00 59.24  ? 486  THR   B N     1 
ATOM   8177  C  CA    . THR   B 1 486  ? 175.915 154.171 182.423 1.00 58.46  ? 486  THR   B CA    1 
ATOM   8178  C  C     . THR   B 1 486  ? 176.648 153.573 181.228 1.00 60.91  ? 486  THR   B C     1 
ATOM   8179  O  O     . THR   B 1 486  ? 177.577 154.171 180.679 1.00 66.50  ? 486  THR   B O     1 
ATOM   8180  C  CB    . THR   B 1 486  ? 174.507 154.616 182.004 1.00 64.21  ? 486  THR   B CB    1 
ATOM   8181  O  OG1   . THR   B 1 486  ? 173.901 153.594 181.203 1.00 65.66  ? 486  THR   B OG1   1 
ATOM   8182  C  CG2   . THR   B 1 486  ? 174.568 155.910 181.208 1.00 65.14  ? 486  THR   B CG2   1 
ATOM   8183  N  N     . PHE   B 1 487  ? 176.218 152.372 180.834 1.00 53.95  ? 487  PHE   B N     1 
ATOM   8184  C  CA    . PHE   B 1 487  ? 176.858 151.680 179.719 1.00 52.50  ? 487  PHE   B CA    1 
ATOM   8185  C  C     . PHE   B 1 487  ? 176.919 152.560 178.478 1.00 52.11  ? 487  PHE   B C     1 
ATOM   8186  O  O     . PHE   B 1 487  ? 177.954 152.633 177.804 1.00 54.74  ? 487  PHE   B O     1 
ATOM   8187  C  CB    . PHE   B 1 487  ? 176.113 150.380 179.415 1.00 51.46  ? 487  PHE   B CB    1 
ATOM   8188  C  CG    . PHE   B 1 487  ? 176.667 149.620 178.243 1.00 49.18  ? 487  PHE   B CG    1 
ATOM   8189  C  CD1   . PHE   B 1 487  ? 176.227 149.883 176.956 1.00 52.86  ? 487  PHE   B CD1   1 
ATOM   8190  C  CD2   . PHE   B 1 487  ? 177.624 148.637 178.428 1.00 50.82  ? 487  PHE   B CD2   1 
ATOM   8191  C  CE1   . PHE   B 1 487  ? 176.734 149.184 175.879 1.00 54.41  ? 487  PHE   B CE1   1 
ATOM   8192  C  CE2   . PHE   B 1 487  ? 178.133 147.934 177.353 1.00 52.61  ? 487  PHE   B CE2   1 
ATOM   8193  C  CZ    . PHE   B 1 487  ? 177.688 148.208 176.077 1.00 52.79  ? 487  PHE   B CZ    1 
ATOM   8194  N  N     . PHE   B 1 488  ? 175.816 153.232 178.152 1.00 54.65  ? 488  PHE   B N     1 
ATOM   8195  C  CA    . PHE   B 1 488  ? 175.808 154.074 176.964 1.00 55.41  ? 488  PHE   B CA    1 
ATOM   8196  C  C     . PHE   B 1 488  ? 176.716 155.284 177.131 1.00 56.28  ? 488  PHE   B C     1 
ATOM   8197  O  O     . PHE   B 1 488  ? 177.310 155.747 176.153 1.00 64.90  ? 488  PHE   B O     1 
ATOM   8198  C  CB    . PHE   B 1 488  ? 174.379 154.500 176.634 1.00 57.83  ? 488  PHE   B CB    1 
ATOM   8199  C  CG    . PHE   B 1 488  ? 173.563 153.414 175.995 1.00 60.66  ? 488  PHE   B CG    1 
ATOM   8200  C  CD1   . PHE   B 1 488  ? 174.104 152.627 174.993 1.00 58.49  ? 488  PHE   B CD1   1 
ATOM   8201  C  CD2   . PHE   B 1 488  ? 172.262 153.172 176.401 1.00 62.80  ? 488  PHE   B CD2   1 
ATOM   8202  C  CE1   . PHE   B 1 488  ? 173.362 151.622 174.404 1.00 57.33  ? 488  PHE   B CE1   1 
ATOM   8203  C  CE2   . PHE   B 1 488  ? 171.515 152.168 175.814 1.00 63.02  ? 488  PHE   B CE2   1 
ATOM   8204  C  CZ    . PHE   B 1 488  ? 172.066 151.393 174.814 1.00 60.17  ? 488  PHE   B CZ    1 
ATOM   8205  N  N     . SER   B 1 489  ? 176.853 155.801 178.354 1.00 47.11  ? 489  SER   B N     1 
ATOM   8206  C  CA    . SER   B 1 489  ? 177.772 156.912 178.577 1.00 53.35  ? 489  SER   B CA    1 
ATOM   8207  C  C     . SER   B 1 489  ? 179.215 156.498 178.311 1.00 53.96  ? 489  SER   B C     1 
ATOM   8208  O  O     . SER   B 1 489  ? 179.972 157.231 177.662 1.00 54.07  ? 489  SER   B O     1 
ATOM   8209  C  CB    . SER   B 1 489  ? 177.617 157.444 180.002 1.00 54.14  ? 489  SER   B CB    1 
ATOM   8210  O  OG    . SER   B 1 489  ? 177.579 156.384 180.942 1.00 61.58  ? 489  SER   B OG    1 
ATOM   8211  N  N     . VAL   B 1 490  ? 179.613 155.316 178.787 1.00 51.16  ? 490  VAL   B N     1 
ATOM   8212  C  CA    . VAL   B 1 490  ? 180.975 154.850 178.544 1.00 53.37  ? 490  VAL   B CA    1 
ATOM   8213  C  C     . VAL   B 1 490  ? 181.173 154.533 177.068 1.00 52.57  ? 490  VAL   B C     1 
ATOM   8214  O  O     . VAL   B 1 490  ? 182.249 154.777 176.506 1.00 52.39  ? 490  VAL   B O     1 
ATOM   8215  C  CB    . VAL   B 1 490  ? 181.307 153.640 179.439 1.00 52.24  ? 490  VAL   B CB    1 
ATOM   8216  C  CG1   . VAL   B 1 490  ? 180.225 152.585 179.344 1.00 53.35  ? 490  VAL   B CG1   1 
ATOM   8217  C  CG2   . VAL   B 1 490  ? 182.657 153.053 179.054 1.00 50.21  ? 490  VAL   B CG2   1 
ATOM   8218  N  N     . PHE   B 1 491  ? 180.148 153.984 176.413 1.00 50.14  ? 491  PHE   B N     1 
ATOM   8219  C  CA    . PHE   B 1 491  ? 180.248 153.751 174.976 1.00 50.49  ? 491  PHE   B CA    1 
ATOM   8220  C  C     . PHE   B 1 491  ? 180.444 155.061 174.224 1.00 51.91  ? 491  PHE   B C     1 
ATOM   8221  O  O     . PHE   B 1 491  ? 181.250 155.135 173.289 1.00 54.17  ? 491  PHE   B O     1 
ATOM   8222  C  CB    . PHE   B 1 491  ? 179.007 153.008 174.474 1.00 49.56  ? 491  PHE   B CB    1 
ATOM   8223  C  CG    . PHE   B 1 491  ? 178.948 152.847 172.975 1.00 52.10  ? 491  PHE   B CG    1 
ATOM   8224  C  CD1   . PHE   B 1 491  ? 178.583 153.905 172.157 1.00 51.55  ? 491  PHE   B CD1   1 
ATOM   8225  C  CD2   . PHE   B 1 491  ? 179.272 151.637 172.385 1.00 52.96  ? 491  PHE   B CD2   1 
ATOM   8226  C  CE1   . PHE   B 1 491  ? 178.532 153.756 170.786 1.00 52.00  ? 491  PHE   B CE1   1 
ATOM   8227  C  CE2   . PHE   B 1 491  ? 179.224 151.484 171.012 1.00 47.27  ? 491  PHE   B CE2   1 
ATOM   8228  C  CZ    . PHE   B 1 491  ? 178.854 152.544 170.212 1.00 49.89  ? 491  PHE   B CZ    1 
ATOM   8229  N  N     . ALA   B 1 492  ? 179.706 156.104 174.609 1.00 45.78  ? 492  ALA   B N     1 
ATOM   8230  C  CA    . ALA   B 1 492  ? 179.864 157.403 173.968 1.00 41.69  ? 492  ALA   B CA    1 
ATOM   8231  C  C     . ALA   B 1 492  ? 181.252 157.972 174.222 1.00 43.04  ? 492  ALA   B C     1 
ATOM   8232  O  O     . ALA   B 1 492  ? 181.844 158.606 173.341 1.00 49.84  ? 492  ALA   B O     1 
ATOM   8233  C  CB    . ALA   B 1 492  ? 178.789 158.368 174.465 1.00 40.77  ? 492  ALA   B CB    1 
ATOM   8234  N  N     . ILE   B 1 493  ? 181.785 157.760 175.426 1.00 44.79  ? 493  ILE   B N     1 
ATOM   8235  C  CA    . ILE   B 1 493  ? 183.128 158.241 175.729 1.00 44.31  ? 493  ILE   B CA    1 
ATOM   8236  C  C     . ILE   B 1 493  ? 184.158 157.530 174.860 1.00 48.21  ? 493  ILE   B C     1 
ATOM   8237  O  O     . ILE   B 1 493  ? 185.091 158.155 174.342 1.00 46.62  ? 493  ILE   B O     1 
ATOM   8238  C  CB    . ILE   B 1 493  ? 183.435 158.064 177.227 1.00 51.30  ? 493  ILE   B CB    1 
ATOM   8239  C  CG1   . ILE   B 1 493  ? 182.523 158.956 178.071 1.00 50.89  ? 493  ILE   B CG1   1 
ATOM   8240  C  CG2   . ILE   B 1 493  ? 184.897 158.376 177.515 1.00 45.23  ? 493  ILE   B CG2   1 
ATOM   8241  C  CD1   . ILE   B 1 493  ? 182.275 160.317 177.469 1.00 50.82  ? 493  ILE   B CD1   1 
ATOM   8242  N  N     . PHE   B 1 494  ? 184.007 156.216 174.685 1.00 43.71  ? 494  PHE   B N     1 
ATOM   8243  C  CA    . PHE   B 1 494  ? 185.014 155.443 173.966 1.00 36.54  ? 494  PHE   B CA    1 
ATOM   8244  C  C     . PHE   B 1 494  ? 184.930 155.627 172.453 1.00 40.73  ? 494  PHE   B C     1 
ATOM   8245  O  O     . PHE   B 1 494  ? 185.966 155.666 171.780 1.00 47.00  ? 494  PHE   B O     1 
ATOM   8246  C  CB    . PHE   B 1 494  ? 184.892 153.959 174.312 1.00 33.61  ? 494  PHE   B CB    1 
ATOM   8247  C  CG    . PHE   B 1 494  ? 185.795 153.080 173.497 1.00 40.78  ? 494  PHE   B CG    1 
ATOM   8248  C  CD1   . PHE   B 1 494  ? 187.118 152.897 173.857 1.00 42.82  ? 494  PHE   B CD1   1 
ATOM   8249  C  CD2   . PHE   B 1 494  ? 185.325 152.450 172.357 1.00 41.51  ? 494  PHE   B CD2   1 
ATOM   8250  C  CE1   . PHE   B 1 494  ? 187.951 152.095 173.102 1.00 40.28  ? 494  PHE   B CE1   1 
ATOM   8251  C  CE2   . PHE   B 1 494  ? 186.154 151.649 171.600 1.00 40.21  ? 494  PHE   B CE2   1 
ATOM   8252  C  CZ    . PHE   B 1 494  ? 187.468 151.473 171.972 1.00 40.63  ? 494  PHE   B CZ    1 
ATOM   8253  N  N     . PHE   B 1 495  ? 183.723 155.739 171.899 1.00 42.26  ? 495  PHE   B N     1 
ATOM   8254  C  CA    . PHE   B 1 495  ? 183.548 155.606 170.452 1.00 35.67  ? 495  PHE   B CA    1 
ATOM   8255  C  C     . PHE   B 1 495  ? 184.474 156.498 169.635 1.00 39.45  ? 495  PHE   B C     1 
ATOM   8256  O  O     . PHE   B 1 495  ? 185.036 156.013 168.640 1.00 44.08  ? 495  PHE   B O     1 
ATOM   8257  C  CB    . PHE   B 1 495  ? 182.082 155.873 170.084 1.00 37.56  ? 495  PHE   B CB    1 
ATOM   8258  C  CG    . PHE   B 1 495  ? 181.773 155.633 168.634 1.00 43.00  ? 495  PHE   B CG    1 
ATOM   8259  C  CD1   . PHE   B 1 495  ? 181.437 154.367 168.187 1.00 43.36  ? 495  PHE   B CD1   1 
ATOM   8260  C  CD2   . PHE   B 1 495  ? 181.825 156.669 167.717 1.00 40.80  ? 495  PHE   B CD2   1 
ATOM   8261  C  CE1   . PHE   B 1 495  ? 181.155 154.138 166.855 1.00 41.53  ? 495  PHE   B CE1   1 
ATOM   8262  C  CE2   . PHE   B 1 495  ? 181.545 156.446 166.384 1.00 40.94  ? 495  PHE   B CE2   1 
ATOM   8263  C  CZ    . PHE   B 1 495  ? 181.209 155.179 165.953 1.00 43.24  ? 495  PHE   B CZ    1 
ATOM   8264  N  N     . PRO   B 1 496  ? 184.674 157.775 169.969 1.00 41.41  ? 496  PRO   B N     1 
ATOM   8265  C  CA    . PRO   B 1 496  ? 185.582 158.609 169.168 1.00 38.01  ? 496  PRO   B CA    1 
ATOM   8266  C  C     . PRO   B 1 496  ? 186.949 157.973 168.966 1.00 34.80  ? 496  PRO   B C     1 
ATOM   8267  O  O     . PRO   B 1 496  ? 187.649 158.288 167.999 1.00 35.46  ? 496  PRO   B O     1 
ATOM   8268  C  CB    . PRO   B 1 496  ? 185.679 159.901 169.986 1.00 37.00  ? 496  PRO   B CB    1 
ATOM   8269  C  CG    . PRO   B 1 496  ? 184.397 159.960 170.730 1.00 38.24  ? 496  PRO   B CG    1 
ATOM   8270  C  CD    . PRO   B 1 496  ? 184.035 158.540 171.053 1.00 39.51  ? 496  PRO   B CD    1 
ATOM   8271  N  N     . ALA   B 1 497  ? 187.341 157.075 169.874 1.00 42.71  ? 497  ALA   B N     1 
ATOM   8272  C  CA    . ALA   B 1 497  ? 188.607 156.369 169.714 1.00 41.01  ? 497  ALA   B CA    1 
ATOM   8273  C  C     . ALA   B 1 497  ? 188.614 155.505 168.460 1.00 44.16  ? 497  ALA   B C     1 
ATOM   8274  O  O     . ALA   B 1 497  ? 189.668 155.316 167.843 1.00 48.42  ? 497  ALA   B O     1 
ATOM   8275  C  CB    . ALA   B 1 497  ? 188.893 155.514 170.950 1.00 39.01  ? 497  ALA   B CB    1 
ATOM   8276  N  N     . ALA   B 1 498  ? 187.458 154.966 168.072 1.00 36.72  ? 498  ALA   B N     1 
ATOM   8277  C  CA    . ALA   B 1 498  ? 187.371 154.127 166.883 1.00 32.52  ? 498  ALA   B CA    1 
ATOM   8278  C  C     . ALA   B 1 498  ? 187.402 154.926 165.587 1.00 34.12  ? 498  ALA   B C     1 
ATOM   8279  O  O     . ALA   B 1 498  ? 187.582 154.330 164.520 1.00 39.97  ? 498  ALA   B O     1 
ATOM   8280  C  CB    . ALA   B 1 498  ? 186.101 153.277 166.933 1.00 32.44  ? 498  ALA   B CB    1 
ATOM   8281  N  N     . THR   B 1 499  ? 187.233 156.244 165.649 1.00 34.43  ? 499  THR   B N     1 
ATOM   8282  C  CA    . THR   B 1 499  ? 187.192 157.062 164.448 1.00 30.40  ? 499  THR   B CA    1 
ATOM   8283  C  C     . THR   B 1 499  ? 188.597 157.227 163.870 1.00 40.04  ? 499  THR   B C     1 
ATOM   8284  O  O     . THR   B 1 499  ? 189.568 156.620 164.330 1.00 42.78  ? 499  THR   B O     1 
ATOM   8285  C  CB    . THR   B 1 499  ? 186.563 158.419 164.752 1.00 35.02  ? 499  THR   B CB    1 
ATOM   8286  O  OG1   . THR   B 1 499  ? 187.245 159.029 165.855 1.00 48.01  ? 499  THR   B OG1   1 
ATOM   8287  C  CG2   . THR   B 1 499  ? 185.094 158.256 165.101 1.00 39.35  ? 499  THR   B CG2   1 
ATOM   8288  N  N     . GLY   B 1 500  ? 188.701 158.063 162.840 1.00 44.44  ? 500  GLY   B N     1 
ATOM   8289  C  CA    . GLY   B 1 500  ? 189.967 158.299 162.176 1.00 39.76  ? 500  GLY   B CA    1 
ATOM   8290  C  C     . GLY   B 1 500  ? 190.323 157.309 161.092 1.00 38.00  ? 500  GLY   B C     1 
ATOM   8291  O  O     . GLY   B 1 500  ? 191.496 157.227 160.712 1.00 34.36  ? 500  GLY   B O     1 
ATOM   8292  N  N     . ILE   B 1 501  ? 189.348 156.554 160.577 1.00 31.95  ? 501  ILE   B N     1 
ATOM   8293  C  CA    . ILE   B 1 501  ? 189.629 155.522 159.581 1.00 28.82  ? 501  ILE   B CA    1 
ATOM   8294  C  C     . ILE   B 1 501  ? 189.851 156.072 158.183 1.00 31.96  ? 501  ILE   B C     1 
ATOM   8295  O  O     . ILE   B 1 501  ? 190.279 155.321 157.298 1.00 41.47  ? 501  ILE   B O     1 
ATOM   8296  C  CB    . ILE   B 1 501  ? 188.484 154.495 159.516 1.00 30.06  ? 501  ILE   B CB    1 
ATOM   8297  C  CG1   . ILE   B 1 501  ? 187.224 155.145 158.942 1.00 33.93  ? 501  ILE   B CG1   1 
ATOM   8298  C  CG2   . ILE   B 1 501  ? 188.209 153.922 160.894 1.00 33.44  ? 501  ILE   B CG2   1 
ATOM   8299  C  CD1   . ILE   B 1 501  ? 185.996 154.273 159.014 1.00 32.65  ? 501  ILE   B CD1   1 
ATOM   8300  N  N     . LEU   B 1 502  ? 189.573 157.353 157.952 1.00 28.81  ? 502  LEU   B N     1 
ATOM   8301  C  CA    . LEU   B 1 502  ? 189.642 157.940 156.620 1.00 32.49  ? 502  LEU   B CA    1 
ATOM   8302  C  C     . LEU   B 1 502  ? 190.908 158.753 156.389 1.00 32.44  ? 502  LEU   B C     1 
ATOM   8303  O  O     . LEU   B 1 502  ? 190.985 159.490 155.402 1.00 38.23  ? 502  LEU   B O     1 
ATOM   8304  C  CB    . LEU   B 1 502  ? 188.411 158.813 156.367 1.00 33.97  ? 502  LEU   B CB    1 
ATOM   8305  C  CG    . LEU   B 1 502  ? 187.072 158.081 156.261 1.00 29.36  ? 502  LEU   B CG    1 
ATOM   8306  C  CD1   . LEU   B 1 502  ? 185.960 159.044 155.893 1.00 30.73  ? 502  LEU   B CD1   1 
ATOM   8307  C  CD2   . LEU   B 1 502  ? 187.156 156.955 155.247 1.00 26.70  ? 502  LEU   B CD2   1 
ATOM   8308  N  N     . ALA   B 1 503  ? 191.904 158.638 157.270 1.00 38.41  ? 503  ALA   B N     1 
ATOM   8309  C  CA    . ALA   B 1 503  ? 193.133 159.403 157.088 1.00 33.63  ? 503  ALA   B CA    1 
ATOM   8310  C  C     . ALA   B 1 503  ? 193.837 159.024 155.790 1.00 37.26  ? 503  ALA   B C     1 
ATOM   8311  O  O     . ALA   B 1 503  ? 194.291 159.899 155.044 1.00 37.01  ? 503  ALA   B O     1 
ATOM   8312  C  CB    . ALA   B 1 503  ? 194.062 159.196 158.283 1.00 34.26  ? 503  ALA   B CB    1 
ATOM   8313  N  N     . GLY   B 1 504  ? 193.940 157.725 155.503 1.00 39.73  ? 504  GLY   B N     1 
ATOM   8314  C  CA    . GLY   B 1 504  ? 194.595 157.304 154.275 1.00 37.96  ? 504  GLY   B CA    1 
ATOM   8315  C  C     . GLY   B 1 504  ? 193.838 157.725 153.030 1.00 39.73  ? 504  GLY   B C     1 
ATOM   8316  O  O     . GLY   B 1 504  ? 194.437 158.187 152.055 1.00 42.88  ? 504  GLY   B O     1 
ATOM   8317  N  N     . ALA   B 1 505  ? 192.512 157.576 153.044 1.00 41.58  ? 505  ALA   B N     1 
ATOM   8318  C  CA    . ALA   B 1 505  ? 191.706 157.980 151.899 1.00 41.73  ? 505  ALA   B CA    1 
ATOM   8319  C  C     . ALA   B 1 505  ? 191.728 159.486 151.684 1.00 38.09  ? 505  ALA   B C     1 
ATOM   8320  O  O     . ALA   B 1 505  ? 191.410 159.947 150.583 1.00 44.01  ? 505  ALA   B O     1 
ATOM   8321  C  CB    . ALA   B 1 505  ? 190.266 157.498 152.071 1.00 38.08  ? 505  ALA   B CB    1 
ATOM   8322  N  N     . ASN   B 1 506  ? 192.092 160.260 152.706 1.00 33.72  ? 506  ASN   B N     1 
ATOM   8323  C  CA    . ASN   B 1 506  ? 192.211 161.702 152.541 1.00 34.83  ? 506  ASN   B CA    1 
ATOM   8324  C  C     . ASN   B 1 506  ? 193.431 162.080 151.713 1.00 39.13  ? 506  ASN   B C     1 
ATOM   8325  O  O     . ASN   B 1 506  ? 193.523 163.221 151.249 1.00 45.65  ? 506  ASN   B O     1 
ATOM   8326  C  CB    . ASN   B 1 506  ? 192.274 162.377 153.912 1.00 40.09  ? 506  ASN   B CB    1 
ATOM   8327  C  CG    . ASN   B 1 506  ? 190.899 162.664 154.484 1.00 46.80  ? 506  ASN   B CG    1 
ATOM   8328  O  OD1   . ASN   B 1 506  ? 190.007 161.818 154.437 1.00 44.61  ? 506  ASN   B OD1   1 
ATOM   8329  N  ND2   . ASN   B 1 506  ? 190.727 163.855 155.041 1.00 49.82  ? 506  ASN   B ND2   1 
ATOM   8330  N  N     . ILE   B 1 507  ? 194.358 161.148 151.518 1.00 40.97  ? 507  ILE   B N     1 
ATOM   8331  C  CA    . ILE   B 1 507  ? 195.581 161.392 150.766 1.00 36.88  ? 507  ILE   B CA    1 
ATOM   8332  C  C     . ILE   B 1 507  ? 195.491 160.786 149.359 1.00 40.04  ? 507  ILE   B C     1 
ATOM   8333  O  O     . ILE   B 1 507  ? 196.507 160.564 148.705 1.00 46.76  ? 507  ILE   B O     1 
ATOM   8334  C  CB    . ILE   B 1 507  ? 196.808 160.882 151.546 1.00 40.72  ? 507  ILE   B CB    1 
ATOM   8335  C  CG1   . ILE   B 1 507  ? 197.133 161.844 152.688 1.00 45.63  ? 507  ILE   B CG1   1 
ATOM   8336  C  CG2   . ILE   B 1 507  ? 198.054 160.776 150.685 1.00 46.91  ? 507  ILE   B CG2   1 
ATOM   8337  C  CD1   . ILE   B 1 507  ? 196.841 163.296 152.368 1.00 43.91  ? 507  ILE   B CD1   1 
ATOM   8338  N  N     . SER   B 1 508  ? 194.271 160.548 148.870 1.00 42.21  ? 508  SER   B N     1 
ATOM   8339  C  CA    . SER   B 1 508  ? 194.099 159.877 147.585 1.00 40.52  ? 508  SER   B CA    1 
ATOM   8340  C  C     . SER   B 1 508  ? 194.822 160.606 146.459 1.00 43.75  ? 508  SER   B C     1 
ATOM   8341  O  O     . SER   B 1 508  ? 195.314 159.965 145.523 1.00 48.35  ? 508  SER   B O     1 
ATOM   8342  C  CB    . SER   B 1 508  ? 192.612 159.747 147.260 1.00 42.30  ? 508  SER   B CB    1 
ATOM   8343  O  OG    . SER   B 1 508  ? 191.991 161.020 147.208 1.00 41.17  ? 508  SER   B OG    1 
ATOM   8344  N  N     . GLY   B 1 509  ? 194.901 161.934 146.527 1.00 47.46  ? 509  GLY   B N     1 
ATOM   8345  C  CA    . GLY   B 1 509  ? 195.547 162.695 145.473 1.00 40.77  ? 509  GLY   B CA    1 
ATOM   8346  C  C     . GLY   B 1 509  ? 197.050 162.530 145.403 1.00 40.05  ? 509  GLY   B C     1 
ATOM   8347  O  O     . GLY   B 1 509  ? 197.664 163.031 144.455 1.00 45.26  ? 509  GLY   B O     1 
ATOM   8348  N  N     . ASP   B 1 510  ? 197.655 161.843 146.375 1.00 47.47  ? 510  ASP   B N     1 
ATOM   8349  C  CA    . ASP   B 1 510  ? 199.097 161.638 146.395 1.00 42.21  ? 510  ASP   B CA    1 
ATOM   8350  C  C     . ASP   B 1 510  ? 199.481 160.175 146.583 1.00 40.60  ? 510  ASP   B C     1 
ATOM   8351  O  O     . ASP   B 1 510  ? 200.640 159.889 146.901 1.00 45.69  ? 510  ASP   B O     1 
ATOM   8352  C  CB    . ASP   B 1 510  ? 199.747 162.488 147.493 1.00 44.08  ? 510  ASP   B CB    1 
ATOM   8353  C  CG    . ASP   B 1 510  ? 199.169 163.887 147.565 1.00 49.62  ? 510  ASP   B CG    1 
ATOM   8354  O  OD1   . ASP   B 1 510  ? 197.957 164.018 147.832 1.00 55.44  ? 510  ASP   B OD1   1 
ATOM   8355  O  OD2   . ASP   B 1 510  ? 199.926 164.858 147.353 1.00 53.59  ? 510  ASP   B OD2   1 
ATOM   8356  N  N     . LEU   B 1 511  ? 198.549 159.245 146.399 1.00 38.13  ? 511  LEU   B N     1 
ATOM   8357  C  CA    . LEU   B 1 511  ? 198.860 157.828 146.485 1.00 41.02  ? 511  LEU   B CA    1 
ATOM   8358  C  C     . LEU   B 1 511  ? 199.339 157.307 145.137 1.00 40.15  ? 511  LEU   B C     1 
ATOM   8359  O  O     . LEU   B 1 511  ? 198.919 157.781 144.079 1.00 43.65  ? 511  LEU   B O     1 
ATOM   8360  C  CB    . LEU   B 1 511  ? 197.643 157.025 146.945 1.00 40.35  ? 511  LEU   B CB    1 
ATOM   8361  C  CG    . LEU   B 1 511  ? 197.069 157.378 148.317 1.00 41.99  ? 511  LEU   B CG    1 
ATOM   8362  C  CD1   . LEU   B 1 511  ? 195.785 156.607 148.574 1.00 38.78  ? 511  LEU   B CD1   1 
ATOM   8363  C  CD2   . LEU   B 1 511  ? 198.091 157.106 149.409 1.00 41.69  ? 511  LEU   B CD2   1 
ATOM   8364  N  N     . ALA   B 1 512  ? 200.231 156.316 145.187 1.00 44.46  ? 512  ALA   B N     1 
ATOM   8365  C  CA    . ALA   B 1 512  ? 200.731 155.716 143.956 1.00 44.60  ? 512  ALA   B CA    1 
ATOM   8366  C  C     . ALA   B 1 512  ? 199.618 155.006 143.199 1.00 49.12  ? 512  ALA   B C     1 
ATOM   8367  O  O     . ALA   B 1 512  ? 199.570 155.055 141.964 1.00 50.93  ? 512  ALA   B O     1 
ATOM   8368  C  CB    . ALA   B 1 512  ? 201.872 154.749 144.265 1.00 43.64  ? 512  ALA   B CB    1 
ATOM   8369  N  N     . ASP   B 1 513  ? 198.716 154.344 143.917 1.00 53.81  ? 513  ASP   B N     1 
ATOM   8370  C  CA    . ASP   B 1 513  ? 197.652 153.591 143.270 1.00 51.70  ? 513  ASP   B CA    1 
ATOM   8371  C  C     . ASP   B 1 513  ? 196.453 153.422 144.195 1.00 49.86  ? 513  ASP   B C     1 
ATOM   8372  O  O     . ASP   B 1 513  ? 196.309 152.374 144.837 1.00 51.38  ? 513  ASP   B O     1 
ATOM   8373  C  CB    . ASP   B 1 513  ? 198.163 152.220 142.823 1.00 55.58  ? 513  ASP   B CB    1 
ATOM   8374  C  CG    . ASP   B 1 513  ? 197.069 151.358 142.217 1.00 58.86  ? 513  ASP   B CG    1 
ATOM   8375  O  OD1   . ASP   B 1 513  ? 196.006 151.904 141.857 1.00 53.59  ? 513  ASP   B OD1   1 
ATOM   8376  O  OD2   . ASP   B 1 513  ? 197.272 150.131 142.104 1.00 63.10  ? 513  ASP   B OD2   1 
ATOM   8377  N  N     . PRO   B 1 514  ? 195.574 154.417 144.293 1.00 43.75  ? 514  PRO   B N     1 
ATOM   8378  C  CA    . PRO   B 1 514  ? 194.291 154.193 144.966 1.00 39.85  ? 514  PRO   B CA    1 
ATOM   8379  C  C     . PRO   B 1 514  ? 193.526 153.077 144.273 1.00 44.18  ? 514  PRO   B C     1 
ATOM   8380  O  O     . PRO   B 1 514  ? 193.876 152.627 143.180 1.00 50.72  ? 514  PRO   B O     1 
ATOM   8381  C  CB    . PRO   B 1 514  ? 193.570 155.540 144.849 1.00 39.12  ? 514  PRO   B CB    1 
ATOM   8382  C  CG    . PRO   B 1 514  ? 194.622 156.523 144.443 1.00 39.69  ? 514  PRO   B CG    1 
ATOM   8383  C  CD    . PRO   B 1 514  ? 195.659 155.756 143.692 1.00 38.79  ? 514  PRO   B CD    1 
ATOM   8384  N  N     . GLN   B 1 515  ? 192.458 152.627 144.923 1.00 43.03  ? 515  GLN   B N     1 
ATOM   8385  C  CA    . GLN   B 1 515  ? 191.671 151.458 144.557 1.00 47.90  ? 515  GLN   B CA    1 
ATOM   8386  C  C     . GLN   B 1 515  ? 192.390 150.170 144.938 1.00 45.67  ? 515  GLN   B C     1 
ATOM   8387  O  O     . GLN   B 1 515  ? 191.809 149.094 144.795 1.00 50.19  ? 515  GLN   B O     1 
ATOM   8388  C  CB    . GLN   B 1 515  ? 191.322 151.404 143.057 1.00 41.86  ? 515  GLN   B CB    1 
ATOM   8389  C  CG    . GLN   B 1 515  ? 190.735 152.687 142.500 1.00 42.60  ? 515  GLN   B CG    1 
ATOM   8390  C  CD    . GLN   B 1 515  ? 190.289 152.540 141.060 1.00 51.62  ? 515  GLN   B CD    1 
ATOM   8391  O  OE1   . GLN   B 1 515  ? 190.675 153.328 140.197 1.00 54.44  ? 515  GLN   B OE1   1 
ATOM   8392  N  NE2   . GLN   B 1 515  ? 189.475 151.525 140.791 1.00 47.51  ? 515  GLN   B NE2   1 
ATOM   8393  N  N     . SER   B 1 516  ? 193.631 150.236 145.416 1.00 41.67  ? 516  SER   B N     1 
ATOM   8394  C  CA    . SER   B 1 516  ? 194.336 149.064 145.914 1.00 38.08  ? 516  SER   B CA    1 
ATOM   8395  C  C     . SER   B 1 516  ? 194.956 149.374 147.270 1.00 40.36  ? 516  SER   B C     1 
ATOM   8396  O  O     . SER   B 1 516  ? 195.082 148.489 148.122 1.00 49.95  ? 516  SER   B O     1 
ATOM   8397  C  CB    . SER   B 1 516  ? 195.407 148.611 144.919 1.00 39.89  ? 516  SER   B CB    1 
ATOM   8398  O  OG    . SER   B 1 516  ? 196.217 149.697 144.507 1.00 40.66  ? 516  SER   B OG    1 
ATOM   8399  N  N     . ALA   B 1 517  ? 195.343 150.631 147.476 1.00 34.51  ? 517  ALA   B N     1 
ATOM   8400  C  CA    . ALA   B 1 517  ? 195.952 151.055 148.729 1.00 31.93  ? 517  ALA   B CA    1 
ATOM   8401  C  C     . ALA   B 1 517  ? 194.919 151.425 149.786 1.00 31.05  ? 517  ALA   B C     1 
ATOM   8402  O  O     . ALA   B 1 517  ? 195.061 151.038 150.950 1.00 37.83  ? 517  ALA   B O     1 
ATOM   8403  C  CB    . ALA   B 1 517  ? 196.892 152.238 148.482 1.00 32.38  ? 517  ALA   B CB    1 
ATOM   8404  N  N     . ILE   B 1 518  ? 193.879 152.171 149.406 1.00 25.68  ? 518  ILE   B N     1 
ATOM   8405  C  CA    . ILE   B 1 518  ? 192.889 152.617 150.387 1.00 30.38  ? 518  ILE   B CA    1 
ATOM   8406  C  C     . ILE   B 1 518  ? 192.185 151.444 151.060 1.00 32.78  ? 518  ILE   B C     1 
ATOM   8407  O  O     . ILE   B 1 518  ? 192.172 151.388 152.300 1.00 39.82  ? 518  ILE   B O     1 
ATOM   8408  C  CB    . ILE   B 1 518  ? 191.901 153.595 149.734 1.00 23.62  ? 518  ILE   B CB    1 
ATOM   8409  C  CG1   . ILE   B 1 518  ? 192.534 154.979 149.579 1.00 23.87  ? 518  ILE   B CG1   1 
ATOM   8410  C  CG2   . ILE   B 1 518  ? 190.617 153.681 150.545 1.00 24.47  ? 518  ILE   B CG2   1 
ATOM   8411  C  CD1   . ILE   B 1 518  ? 191.741 155.918 148.695 1.00 26.64  ? 518  ILE   B CD1   1 
ATOM   8412  N  N     . PRO   B 1 519  ? 191.604 150.491 150.335 1.00 33.36  ? 519  PRO   B N     1 
ATOM   8413  C  CA    . PRO   B 1 519  ? 190.819 149.440 150.998 1.00 36.48  ? 519  PRO   B CA    1 
ATOM   8414  C  C     . PRO   B 1 519  ? 191.635 148.586 151.955 1.00 32.24  ? 519  PRO   B C     1 
ATOM   8415  O  O     . PRO   B 1 519  ? 191.305 148.483 153.143 1.00 41.66  ? 519  PRO   B O     1 
ATOM   8416  C  CB    . PRO   B 1 519  ? 190.286 148.603 149.824 1.00 30.25  ? 519  PRO   B CB    1 
ATOM   8417  C  CG    . PRO   B 1 519  ? 191.101 149.007 148.639 1.00 35.62  ? 519  PRO   B CG    1 
ATOM   8418  C  CD    . PRO   B 1 519  ? 191.492 150.424 148.870 1.00 33.32  ? 519  PRO   B CD    1 
ATOM   8419  N  N     . LYS   B 1 520  ? 192.699 147.962 151.444 1.00 31.67  ? 520  LYS   B N     1 
ATOM   8420  C  CA    . LYS   B 1 520  ? 193.491 147.060 152.272 1.00 34.32  ? 520  LYS   B CA    1 
ATOM   8421  C  C     . LYS   B 1 520  ? 194.163 147.807 153.417 1.00 34.34  ? 520  LYS   B C     1 
ATOM   8422  O  O     . LYS   B 1 520  ? 194.189 147.321 154.554 1.00 43.87  ? 520  LYS   B O     1 
ATOM   8423  C  CB    . LYS   B 1 520  ? 194.523 146.330 151.411 1.00 30.59  ? 520  LYS   B CB    1 
ATOM   8424  C  CG    . LYS   B 1 520  ? 195.849 147.051 151.262 1.00 31.01  ? 520  LYS   B CG    1 
ATOM   8425  C  CD    . LYS   B 1 520  ? 196.949 146.089 150.859 1.00 35.45  ? 520  LYS   B CD    1 
ATOM   8426  C  CE    . LYS   B 1 520  ? 196.812 145.692 149.402 1.00 37.92  ? 520  LYS   B CE    1 
ATOM   8427  N  NZ    . LYS   B 1 520  ? 197.569 146.608 148.508 1.00 38.35  ? 520  LYS   B NZ    1 
ATOM   8428  N  N     . GLY   B 1 521  ? 194.701 148.996 153.142 1.00 28.35  ? 521  GLY   B N     1 
ATOM   8429  C  CA    . GLY   B 1 521  ? 195.334 149.766 154.199 1.00 25.27  ? 521  GLY   B CA    1 
ATOM   8430  C  C     . GLY   B 1 521  ? 194.364 150.140 155.303 1.00 32.41  ? 521  GLY   B C     1 
ATOM   8431  O  O     . GLY   B 1 521  ? 194.660 149.978 156.489 1.00 44.15  ? 521  GLY   B O     1 
ATOM   8432  N  N     . THR   B 1 522  ? 193.184 150.639 154.925 1.00 26.98  ? 522  THR   B N     1 
ATOM   8433  C  CA    . THR   B 1 522  ? 192.195 151.031 155.925 1.00 27.03  ? 522  THR   B CA    1 
ATOM   8434  C  C     . THR   B 1 522  ? 191.726 149.831 156.737 1.00 30.44  ? 522  THR   B C     1 
ATOM   8435  O  O     . THR   B 1 522  ? 191.597 149.913 157.966 1.00 36.89  ? 522  THR   B O     1 
ATOM   8436  C  CB    . THR   B 1 522  ? 191.008 151.717 155.249 1.00 26.52  ? 522  THR   B CB    1 
ATOM   8437  O  OG1   . THR   B 1 522  ? 191.474 152.838 154.490 1.00 31.24  ? 522  THR   B OG1   1 
ATOM   8438  C  CG2   . THR   B 1 522  ? 190.007 152.201 156.288 1.00 29.12  ? 522  THR   B CG2   1 
ATOM   8439  N  N     . LEU   B 1 523  ? 191.466 148.704 156.071 1.00 26.96  ? 523  LEU   B N     1 
ATOM   8440  C  CA    . LEU   B 1 523  ? 190.999 147.528 156.795 1.00 30.99  ? 523  LEU   B CA    1 
ATOM   8441  C  C     . LEU   B 1 523  ? 192.066 147.008 157.751 1.00 35.65  ? 523  LEU   B C     1 
ATOM   8442  O  O     . LEU   B 1 523  ? 191.758 146.637 158.892 1.00 39.10  ? 523  LEU   B O     1 
ATOM   8443  C  CB    . LEU   B 1 523  ? 190.573 146.442 155.809 1.00 32.63  ? 523  LEU   B CB    1 
ATOM   8444  C  CG    . LEU   B 1 523  ? 189.446 146.850 154.858 1.00 37.61  ? 523  LEU   B CG    1 
ATOM   8445  C  CD1   . LEU   B 1 523  ? 188.810 145.634 154.209 1.00 37.37  ? 523  LEU   B CD1   1 
ATOM   8446  C  CD2   . LEU   B 1 523  ? 188.402 147.672 155.590 1.00 33.10  ? 523  LEU   B CD2   1 
ATOM   8447  N  N     . LEU   B 1 524  ? 193.327 146.982 157.311 1.00 29.90  ? 524  LEU   B N     1 
ATOM   8448  C  CA    . LEU   B 1 524  ? 194.405 146.550 158.194 1.00 28.39  ? 524  LEU   B CA    1 
ATOM   8449  C  C     . LEU   B 1 524  ? 194.550 147.487 159.383 1.00 32.98  ? 524  LEU   B C     1 
ATOM   8450  O  O     . LEU   B 1 524  ? 194.767 147.038 160.515 1.00 40.66  ? 524  LEU   B O     1 
ATOM   8451  C  CB    . LEU   B 1 524  ? 195.718 146.464 157.417 1.00 28.19  ? 524  LEU   B CB    1 
ATOM   8452  C  CG    . LEU   B 1 524  ? 196.553 145.203 157.640 1.00 37.69  ? 524  LEU   B CG    1 
ATOM   8453  C  CD1   . LEU   B 1 524  ? 195.661 143.978 157.690 1.00 37.84  ? 524  LEU   B CD1   1 
ATOM   8454  C  CD2   . LEU   B 1 524  ? 197.603 145.060 156.553 1.00 40.07  ? 524  LEU   B CD2   1 
ATOM   8455  N  N     . ALA   B 1 525  ? 194.445 148.796 159.146 1.00 29.97  ? 525  ALA   B N     1 
ATOM   8456  C  CA    . ALA   B 1 525  ? 194.525 149.747 160.247 1.00 31.91  ? 525  ALA   B CA    1 
ATOM   8457  C  C     . ALA   B 1 525  ? 193.420 149.495 161.262 1.00 29.23  ? 525  ALA   B C     1 
ATOM   8458  O  O     . ALA   B 1 525  ? 193.668 149.462 162.473 1.00 35.80  ? 525  ALA   B O     1 
ATOM   8459  C  CB    . ALA   B 1 525  ? 194.452 151.176 159.711 1.00 28.02  ? 525  ALA   B CB    1 
ATOM   8460  N  N     . ILE   B 1 526  ? 192.189 149.302 160.783 1.00 25.38  ? 526  ILE   B N     1 
ATOM   8461  C  CA    . ILE   B 1 526  ? 191.073 149.062 161.695 1.00 26.28  ? 526  ILE   B CA    1 
ATOM   8462  C  C     . ILE   B 1 526  ? 191.321 147.797 162.506 1.00 32.85  ? 526  ILE   B C     1 
ATOM   8463  O  O     . ILE   B 1 526  ? 191.166 147.781 163.735 1.00 40.14  ? 526  ILE   B O     1 
ATOM   8464  C  CB    . ILE   B 1 526  ? 189.749 148.976 160.915 1.00 34.41  ? 526  ILE   B CB    1 
ATOM   8465  C  CG1   . ILE   B 1 526  ? 189.361 150.346 160.356 1.00 33.62  ? 526  ILE   B CG1   1 
ATOM   8466  C  CG2   . ILE   B 1 526  ? 188.639 148.428 161.802 1.00 27.94  ? 526  ILE   B CG2   1 
ATOM   8467  C  CD1   . ILE   B 1 526  ? 188.128 150.316 159.477 1.00 31.18  ? 526  ILE   B CD1   1 
ATOM   8468  N  N     . LEU   B 1 527  ? 191.723 146.720 161.829 1.00 29.71  ? 527  LEU   B N     1 
ATOM   8469  C  CA    . LEU   B 1 527  ? 191.942 145.451 162.515 1.00 30.42  ? 527  LEU   B CA    1 
ATOM   8470  C  C     . LEU   B 1 527  ? 193.015 145.584 163.588 1.00 33.56  ? 527  LEU   B C     1 
ATOM   8471  O  O     . LEU   B 1 527  ? 192.816 145.175 164.738 1.00 39.38  ? 527  LEU   B O     1 
ATOM   8472  C  CB    . LEU   B 1 527  ? 192.323 144.372 161.501 1.00 31.16  ? 527  LEU   B CB    1 
ATOM   8473  C  CG    . LEU   B 1 527  ? 192.646 142.984 162.057 1.00 33.68  ? 527  LEU   B CG    1 
ATOM   8474  C  CD1   . LEU   B 1 527  ? 191.389 142.295 162.562 1.00 34.96  ? 527  LEU   B CD1   1 
ATOM   8475  C  CD2   . LEU   B 1 527  ? 193.345 142.132 161.011 1.00 32.60  ? 527  LEU   B CD2   1 
ATOM   8476  N  N     . ILE   B 1 528  ? 194.164 146.158 163.226 1.00 29.82  ? 528  ILE   B N     1 
ATOM   8477  C  CA    . ILE   B 1 528  ? 195.275 146.259 164.167 1.00 28.90  ? 528  ILE   B CA    1 
ATOM   8478  C  C     . ILE   B 1 528  ? 194.901 147.146 165.347 1.00 33.10  ? 528  ILE   B C     1 
ATOM   8479  O  O     . ILE   B 1 528  ? 195.187 146.816 166.506 1.00 43.07  ? 528  ILE   B O     1 
ATOM   8480  C  CB    . ILE   B 1 528  ? 196.535 146.773 163.447 1.00 33.65  ? 528  ILE   B CB    1 
ATOM   8481  C  CG1   . ILE   B 1 528  ? 197.151 145.659 162.598 1.00 29.54  ? 528  ILE   B CG1   1 
ATOM   8482  C  CG2   . ILE   B 1 528  ? 197.544 147.307 164.451 1.00 34.24  ? 528  ILE   B CG2   1 
ATOM   8483  C  CD1   . ILE   B 1 528  ? 198.238 146.135 161.662 1.00 32.24  ? 528  ILE   B CD1   1 
ATOM   8484  N  N     . THR   B 1 529  ? 194.269 148.290 165.076 1.00 31.99  ? 529  THR   B N     1 
ATOM   8485  C  CA    . THR   B 1 529  ? 193.900 149.195 166.158 1.00 39.00  ? 529  THR   B CA    1 
ATOM   8486  C  C     . THR   B 1 529  ? 192.918 148.537 167.118 1.00 38.47  ? 529  THR   B C     1 
ATOM   8487  O  O     . THR   B 1 529  ? 193.067 148.648 168.342 1.00 32.33  ? 529  THR   B O     1 
ATOM   8488  C  CB    . THR   B 1 529  ? 193.313 150.484 165.586 1.00 38.72  ? 529  THR   B CB    1 
ATOM   8489  O  OG1   . THR   B 1 529  ? 194.375 151.361 165.188 1.00 28.77  ? 529  THR   B OG1   1 
ATOM   8490  C  CG2   . THR   B 1 529  ? 192.457 151.178 166.626 1.00 43.12  ? 529  THR   B CG2   1 
ATOM   8491  N  N     . THR   B 1 530  ? 191.906 147.845 166.587 1.00 35.92  ? 530  THR   B N     1 
ATOM   8492  C  CA    . THR   B 1 530  ? 190.937 147.190 167.461 1.00 34.16  ? 530  THR   B CA    1 
ATOM   8493  C  C     . THR   B 1 530  ? 191.590 146.079 168.273 1.00 37.11  ? 530  THR   B C     1 
ATOM   8494  O  O     . THR   B 1 530  ? 191.298 145.919 169.466 1.00 42.52  ? 530  THR   B O     1 
ATOM   8495  C  CB    . THR   B 1 530  ? 189.772 146.643 166.638 1.00 35.80  ? 530  THR   B CB    1 
ATOM   8496  O  OG1   . THR   B 1 530  ? 189.000 147.734 166.123 1.00 38.56  ? 530  THR   B OG1   1 
ATOM   8497  C  CG2   . THR   B 1 530  ? 188.878 145.762 167.497 1.00 35.52  ? 530  THR   B CG2   1 
ATOM   8498  N  N     . LEU   B 1 531  ? 192.477 145.301 167.647 1.00 38.55  ? 531  LEU   B N     1 
ATOM   8499  C  CA    . LEU   B 1 531  ? 193.165 144.246 168.380 1.00 36.03  ? 531  LEU   B CA    1 
ATOM   8500  C  C     . LEU   B 1 531  ? 193.994 144.824 169.518 1.00 33.91  ? 531  LEU   B C     1 
ATOM   8501  O  O     . LEU   B 1 531  ? 193.977 144.300 170.638 1.00 38.68  ? 531  LEU   B O     1 
ATOM   8502  C  CB    . LEU   B 1 531  ? 194.047 143.438 167.430 1.00 37.16  ? 531  LEU   B CB    1 
ATOM   8503  C  CG    . LEU   B 1 531  ? 193.332 142.376 166.594 1.00 42.40  ? 531  LEU   B CG    1 
ATOM   8504  C  CD1   . LEU   B 1 531  ? 194.335 141.435 165.946 1.00 40.41  ? 531  LEU   B CD1   1 
ATOM   8505  C  CD2   . LEU   B 1 531  ? 192.340 141.606 167.448 1.00 35.85  ? 531  LEU   B CD2   1 
ATOM   8506  N  N     . VAL   B 1 532  ? 194.723 145.909 169.250 1.00 32.86  ? 532  VAL   B N     1 
ATOM   8507  C  CA    . VAL   B 1 532  ? 195.547 146.521 170.288 1.00 35.11  ? 532  VAL   B CA    1 
ATOM   8508  C  C     . VAL   B 1 532  ? 194.672 147.064 171.409 1.00 35.82  ? 532  VAL   B C     1 
ATOM   8509  O  O     . VAL   B 1 532  ? 195.003 146.934 172.594 1.00 42.56  ? 532  VAL   B O     1 
ATOM   8510  C  CB    . VAL   B 1 532  ? 196.444 147.618 169.686 1.00 35.01  ? 532  VAL   B CB    1 
ATOM   8511  C  CG1   . VAL   B 1 532  ? 196.827 148.634 170.750 1.00 36.71  ? 532  VAL   B CG1   1 
ATOM   8512  C  CG2   . VAL   B 1 532  ? 197.684 147.003 169.058 1.00 29.93  ? 532  VAL   B CG2   1 
ATOM   8513  N  N     . TYR   B 1 533  ? 193.545 147.689 171.056 1.00 36.55  ? 533  TYR   B N     1 
ATOM   8514  C  CA    . TYR   B 1 533  ? 192.643 148.211 172.076 1.00 33.26  ? 533  TYR   B CA    1 
ATOM   8515  C  C     . TYR   B 1 533  ? 192.142 147.095 172.983 1.00 39.60  ? 533  TYR   B C     1 
ATOM   8516  O  O     . TYR   B 1 533  ? 192.156 147.222 174.214 1.00 44.01  ? 533  TYR   B O     1 
ATOM   8517  C  CB    . TYR   B 1 533  ? 191.466 148.932 171.417 1.00 36.77  ? 533  TYR   B CB    1 
ATOM   8518  C  CG    . TYR   B 1 533  ? 191.718 150.392 171.118 1.00 41.74  ? 533  TYR   B CG    1 
ATOM   8519  C  CD1   . TYR   B 1 533  ? 192.361 151.209 172.036 1.00 36.10  ? 533  TYR   B CD1   1 
ATOM   8520  C  CD2   . TYR   B 1 533  ? 191.302 150.955 169.918 1.00 42.20  ? 533  TYR   B CD2   1 
ATOM   8521  C  CE1   . TYR   B 1 533  ? 192.591 152.542 171.766 1.00 38.12  ? 533  TYR   B CE1   1 
ATOM   8522  C  CE2   . TYR   B 1 533  ? 191.527 152.288 169.639 1.00 39.80  ? 533  TYR   B CE2   1 
ATOM   8523  C  CZ    . TYR   B 1 533  ? 192.171 153.077 170.566 1.00 43.48  ? 533  TYR   B CZ    1 
ATOM   8524  O  OH    . TYR   B 1 533  ? 192.397 154.405 170.293 1.00 41.17  ? 533  TYR   B OH    1 
ATOM   8525  N  N     . VAL   B 1 534  ? 191.695 145.986 172.388 1.00 45.15  ? 534  VAL   B N     1 
ATOM   8526  C  CA    . VAL   B 1 534  ? 191.182 144.873 173.184 1.00 45.39  ? 534  VAL   B CA    1 
ATOM   8527  C  C     . VAL   B 1 534  ? 192.278 144.303 174.075 1.00 44.74  ? 534  VAL   B C     1 
ATOM   8528  O  O     . VAL   B 1 534  ? 192.057 144.023 175.263 1.00 47.50  ? 534  VAL   B O     1 
ATOM   8529  C  CB    . VAL   B 1 534  ? 190.579 143.792 172.267 1.00 42.94  ? 534  VAL   B CB    1 
ATOM   8530  C  CG1   . VAL   B 1 534  ? 190.107 142.605 173.088 1.00 43.70  ? 534  VAL   B CG1   1 
ATOM   8531  C  CG2   . VAL   B 1 534  ? 189.434 144.365 171.449 1.00 44.86  ? 534  VAL   B CG2   1 
ATOM   8532  N  N     . GLY   B 1 535  ? 193.474 144.113 173.515 1.00 42.75  ? 535  GLY   B N     1 
ATOM   8533  C  CA    . GLY   B 1 535  ? 194.568 143.578 174.307 1.00 38.54  ? 535  GLY   B CA    1 
ATOM   8534  C  C     . GLY   B 1 535  ? 194.906 144.456 175.494 1.00 40.21  ? 535  GLY   B C     1 
ATOM   8535  O  O     . GLY   B 1 535  ? 195.073 143.970 176.615 1.00 51.25  ? 535  GLY   B O     1 
ATOM   8536  N  N     . ILE   B 1 536  ? 195.008 145.767 175.265 1.00 40.77  ? 536  ILE   B N     1 
ATOM   8537  C  CA    . ILE   B 1 536  ? 195.355 146.678 176.351 1.00 40.97  ? 536  ILE   B CA    1 
ATOM   8538  C  C     . ILE   B 1 536  ? 194.254 146.705 177.402 1.00 44.92  ? 536  ILE   B C     1 
ATOM   8539  O  O     . ILE   B 1 536  ? 194.531 146.727 178.607 1.00 47.96  ? 536  ILE   B O     1 
ATOM   8540  C  CB    . ILE   B 1 536  ? 195.646 148.085 175.799 1.00 46.19  ? 536  ILE   B CB    1 
ATOM   8541  C  CG1   . ILE   B 1 536  ? 196.877 148.055 174.894 1.00 45.36  ? 536  ILE   B CG1   1 
ATOM   8542  C  CG2   . ILE   B 1 536  ? 195.842 149.072 176.938 1.00 44.76  ? 536  ILE   B CG2   1 
ATOM   8543  C  CD1   . ILE   B 1 536  ? 197.851 146.948 175.224 1.00 44.86  ? 536  ILE   B CD1   1 
ATOM   8544  N  N     . ALA   B 1 537  ? 192.991 146.710 176.969 1.00 48.20  ? 537  ALA   B N     1 
ATOM   8545  C  CA    . ALA   B 1 537  ? 191.892 146.704 177.927 1.00 42.77  ? 537  ALA   B CA    1 
ATOM   8546  C  C     . ALA   B 1 537  ? 191.955 145.472 178.819 1.00 47.73  ? 537  ALA   B C     1 
ATOM   8547  O  O     . ALA   B 1 537  ? 191.890 145.577 180.051 1.00 53.51  ? 537  ALA   B O     1 
ATOM   8548  C  CB    . ALA   B 1 537  ? 190.554 146.771 177.189 1.00 43.58  ? 537  ALA   B CB    1 
ATOM   8549  N  N     . VAL   B 1 538  ? 192.100 144.290 178.214 1.00 45.22  ? 538  VAL   B N     1 
ATOM   8550  C  CA    . VAL   B 1 538  ? 192.150 143.062 179.005 1.00 44.47  ? 538  VAL   B CA    1 
ATOM   8551  C  C     . VAL   B 1 538  ? 193.355 143.076 179.939 1.00 47.13  ? 538  VAL   B C     1 
ATOM   8552  O  O     . VAL   B 1 538  ? 193.246 142.728 181.123 1.00 48.24  ? 538  VAL   B O     1 
ATOM   8553  C  CB    . VAL   B 1 538  ? 192.161 141.828 178.084 1.00 41.09  ? 538  VAL   B CB    1 
ATOM   8554  C  CG1   . VAL   B 1 538  ? 192.833 140.657 178.778 1.00 43.18  ? 538  VAL   B CG1   1 
ATOM   8555  C  CG2   . VAL   B 1 538  ? 190.745 141.462 177.668 1.00 43.21  ? 538  VAL   B CG2   1 
ATOM   8556  N  N     . SER   B 1 539  ? 194.520 143.481 179.428 1.00 44.44  ? 539  SER   B N     1 
ATOM   8557  C  CA    . SER   B 1 539  ? 195.725 143.469 180.250 1.00 42.47  ? 539  SER   B CA    1 
ATOM   8558  C  C     . SER   B 1 539  ? 195.584 144.392 181.453 1.00 49.70  ? 539  SER   B C     1 
ATOM   8559  O  O     . SER   B 1 539  ? 195.930 144.013 182.578 1.00 57.58  ? 539  SER   B O     1 
ATOM   8560  C  CB    . SER   B 1 539  ? 196.937 143.863 179.407 1.00 47.13  ? 539  SER   B CB    1 
ATOM   8561  O  OG    . SER   B 1 539  ? 197.253 145.233 179.579 1.00 53.78  ? 539  SER   B OG    1 
ATOM   8562  N  N     . VAL   B 1 540  ? 195.073 145.606 181.241 1.00 48.58  ? 540  VAL   B N     1 
ATOM   8563  C  CA    . VAL   B 1 540  ? 194.893 146.521 182.362 1.00 49.99  ? 540  VAL   B CA    1 
ATOM   8564  C  C     . VAL   B 1 540  ? 193.848 145.987 183.330 1.00 52.81  ? 540  VAL   B C     1 
ATOM   8565  O  O     . VAL   B 1 540  ? 193.967 146.176 184.547 1.00 52.29  ? 540  VAL   B O     1 
ATOM   8566  C  CB    . VAL   B 1 540  ? 194.532 147.932 181.862 1.00 49.17  ? 540  VAL   B CB    1 
ATOM   8567  C  CG1   . VAL   B 1 540  ? 193.030 148.067 181.679 1.00 49.79  ? 540  VAL   B CG1   1 
ATOM   8568  C  CG2   . VAL   B 1 540  ? 195.043 148.975 182.837 1.00 44.20  ? 540  VAL   B CG2   1 
ATOM   8569  N  N     . GLY   B 1 541  ? 192.813 145.313 182.823 1.00 52.80  ? 541  GLY   B N     1 
ATOM   8570  C  CA    . GLY   B 1 541  ? 191.806 144.765 183.711 1.00 51.01  ? 541  GLY   B CA    1 
ATOM   8571  C  C     . GLY   B 1 541  ? 192.261 143.543 184.479 1.00 51.60  ? 541  GLY   B C     1 
ATOM   8572  O  O     . GLY   B 1 541  ? 191.616 143.167 185.462 1.00 53.30  ? 541  GLY   B O     1 
ATOM   8573  N  N     . SER   B 1 542  ? 193.355 142.915 184.053 1.00 53.53  ? 542  SER   B N     1 
ATOM   8574  C  CA    . SER   B 1 542  ? 193.870 141.724 184.715 1.00 51.34  ? 542  SER   B CA    1 
ATOM   8575  C  C     . SER   B 1 542  ? 195.054 142.012 185.632 1.00 53.60  ? 542  SER   B C     1 
ATOM   8576  O  O     . SER   B 1 542  ? 195.677 141.069 186.129 1.00 58.02  ? 542  SER   B O     1 
ATOM   8577  C  CB    . SER   B 1 542  ? 194.265 140.674 183.676 1.00 51.56  ? 542  SER   B CB    1 
ATOM   8578  O  OG    . SER   B 1 542  ? 193.121 140.077 183.091 1.00 54.80  ? 542  SER   B OG    1 
ATOM   8579  N  N     . CYS   B 1 543  ? 195.386 143.283 185.865 1.00 52.96  ? 543  CYS   B N     1 
ATOM   8580  C  CA    . CYS   B 1 543  ? 196.544 143.605 186.691 1.00 51.89  ? 543  CYS   B CA    1 
ATOM   8581  C  C     . CYS   B 1 543  ? 196.335 144.746 187.674 1.00 57.34  ? 543  CYS   B C     1 
ATOM   8582  O  O     . CYS   B 1 543  ? 197.265 145.044 188.429 1.00 57.28  ? 543  CYS   B O     1 
ATOM   8583  C  CB    . CYS   B 1 543  ? 197.751 143.943 185.803 1.00 54.78  ? 543  CYS   B CB    1 
ATOM   8584  S  SG    . CYS   B 1 543  ? 198.113 142.712 184.533 1.00 66.70  ? 543  CYS   B SG    1 
ATOM   8585  N  N     . VAL   B 1 544  ? 195.174 145.394 187.704 1.00 52.39  ? 544  VAL   B N     1 
ATOM   8586  C  CA    . VAL   B 1 544  ? 194.942 146.534 188.583 1.00 51.43  ? 544  VAL   B CA    1 
ATOM   8587  C  C     . VAL   B 1 544  ? 193.545 146.423 189.175 1.00 53.71  ? 544  VAL   B C     1 
ATOM   8588  O  O     . VAL   B 1 544  ? 192.601 146.003 188.496 1.00 55.32  ? 544  VAL   B O     1 
ATOM   8589  C  CB    . VAL   B 1 544  ? 195.119 147.872 187.838 1.00 52.03  ? 544  VAL   B CB    1 
ATOM   8590  C  CG1   . VAL   B 1 544  ? 194.599 149.023 188.681 1.00 52.17  ? 544  VAL   B CG1   1 
ATOM   8591  C  CG2   . VAL   B 1 544  ? 196.578 148.085 187.483 1.00 51.06  ? 544  VAL   B CG2   1 
ATOM   8592  N  N     . VAL   B 1 545  ? 193.416 146.798 190.439 1.00 52.75  ? 545  VAL   B N     1 
ATOM   8593  C  CA    . VAL   B 1 545  ? 192.140 146.773 191.143 1.00 53.62  ? 545  VAL   B CA    1 
ATOM   8594  C  C     . VAL   B 1 545  ? 191.456 148.121 190.969 1.00 53.58  ? 545  VAL   B C     1 
ATOM   8595  O  O     . VAL   B 1 545  ? 192.106 149.154 190.783 1.00 50.49  ? 545  VAL   B O     1 
ATOM   8596  C  CB    . VAL   B 1 545  ? 192.341 146.422 192.632 1.00 55.71  ? 545  VAL   B CB    1 
ATOM   8597  C  CG1   . VAL   B 1 545  ? 192.929 145.029 192.767 1.00 51.20  ? 545  VAL   B CG1   1 
ATOM   8598  C  CG2   . VAL   B 1 545  ? 193.240 147.448 193.303 1.00 51.42  ? 545  VAL   B CG2   1 
ATOM   8599  N  N     . ARG   B 1 546  ? 190.119 148.123 191.002 1.00 53.53  ? 546  ARG   B N     1 
ATOM   8600  C  CA    . ARG   B 1 546  ? 189.371 149.381 190.715 1.00 57.10  ? 546  ARG   B CA    1 
ATOM   8601  C  C     . ARG   B 1 546  ? 189.702 150.481 191.728 1.00 60.13  ? 546  ARG   B C     1 
ATOM   8602  O  O     . ARG   B 1 546  ? 189.907 151.624 191.296 1.00 60.10  ? 546  ARG   B O     1 
ATOM   8603  C  CB    . ARG   B 1 546  ? 187.860 149.137 190.673 1.00 51.71  ? 546  ARG   B CB    1 
ATOM   8604  C  CG    . ARG   B 1 546  ? 187.400 148.226 189.545 1.00 53.27  ? 546  ARG   B CG    1 
ATOM   8605  C  CD    . ARG   B 1 546  ? 185.887 148.173 189.489 1.00 53.14  ? 546  ARG   B CD    1 
ATOM   8606  N  NE    . ARG   B 1 546  ? 185.375 146.829 189.274 1.00 57.83  ? 546  ARG   B NE    1 
ATOM   8607  C  CZ    . ARG   B 1 546  ? 184.976 146.350 188.103 1.00 57.07  ? 546  ARG   B CZ    1 
ATOM   8608  N  NH1   . ARG   B 1 546  ? 185.022 147.110 187.024 1.00 55.65  ? 546  ARG   B NH1   1 
ATOM   8609  N  NH2   . ARG   B 1 546  ? 184.523 145.113 188.016 1.00 52.50  ? 546  ARG   B NH2   1 
ATOM   8610  N  N     . ASP   B 1 547  ? 189.712 150.159 193.019 1.00 61.44  ? 547  ASP   B N     1 
ATOM   8611  C  CA    . ASP   B 1 547  ? 189.961 151.162 194.043 1.00 58.66  ? 547  ASP   B CA    1 
ATOM   8612  C  C     . ASP   B 1 547  ? 191.266 150.856 194.763 1.00 59.53  ? 547  ASP   B C     1 
ATOM   8613  O  O     . ASP   B 1 547  ? 191.662 149.695 194.900 1.00 59.80  ? 547  ASP   B O     1 
ATOM   8614  C  CB    . ASP   B 1 547  ? 188.809 151.224 195.054 1.00 55.19  ? 547  ASP   B CB    1 
ATOM   8615  N  N     . ALA   B 1 548  ? 191.934 151.912 195.222 1.00 65.45  ? 548  ALA   B N     1 
ATOM   8616  C  CA    . ALA   B 1 548  ? 193.203 151.750 195.914 1.00 65.68  ? 548  ALA   B CA    1 
ATOM   8617  C  C     . ALA   B 1 548  ? 193.568 153.052 196.606 1.00 70.16  ? 548  ALA   B C     1 
ATOM   8618  O  O     . ALA   B 1 548  ? 193.129 154.126 196.188 1.00 71.28  ? 548  ALA   B O     1 
ATOM   8619  C  CB    . ALA   B 1 548  ? 194.315 151.336 194.944 1.00 65.96  ? 548  ALA   B CB    1 
ATOM   8620  N  N     . THR   B 1 549  ? 194.369 152.943 197.663 1.00 79.86  ? 549  THR   B N     1 
ATOM   8621  C  CA    . THR   B 1 549  ? 194.920 154.089 198.381 1.00 76.31  ? 549  THR   B CA    1 
ATOM   8622  C  C     . THR   B 1 549  ? 196.418 153.857 198.522 1.00 74.96  ? 549  THR   B C     1 
ATOM   8623  O  O     . THR   B 1 549  ? 196.846 152.980 199.280 1.00 76.45  ? 549  THR   B O     1 
ATOM   8624  C  CB    . THR   B 1 549  ? 194.256 154.264 199.746 1.00 70.63  ? 549  THR   B CB    1 
ATOM   8625  N  N     . GLY   B 1 550  ? 197.210 154.643 197.799 1.00 78.96  ? 550  GLY   B N     1 
ATOM   8626  C  CA    . GLY   B 1 550  ? 198.636 154.401 197.720 1.00 80.06  ? 550  GLY   B CA    1 
ATOM   8627  C  C     . GLY   B 1 550  ? 199.427 154.983 198.872 1.00 84.20  ? 550  GLY   B C     1 
ATOM   8628  O  O     . GLY   B 1 550  ? 199.701 156.186 198.910 1.00 84.69  ? 550  GLY   B O     1 
ATOM   8629  N  N     . ASN   B 1 551  ? 199.799 154.127 199.821 1.00 91.64  ? 551  ASN   B N     1 
ATOM   8630  C  CA    . ASN   B 1 551  ? 200.625 154.537 200.946 1.00 90.34  ? 551  ASN   B CA    1 
ATOM   8631  C  C     . ASN   B 1 551  ? 201.235 153.292 201.573 1.00 91.47  ? 551  ASN   B C     1 
ATOM   8632  O  O     . ASN   B 1 551  ? 200.526 152.324 201.858 1.00 89.57  ? 551  ASN   B O     1 
ATOM   8633  N  N     . VAL   B 1 552  ? 202.552 153.328 201.786 1.00 95.36  ? 552  VAL   B N     1 
ATOM   8634  C  CA    . VAL   B 1 552  ? 203.217 152.210 202.446 1.00 91.87  ? 552  VAL   B CA    1 
ATOM   8635  C  C     . VAL   B 1 552  ? 202.743 152.085 203.886 1.00 96.34  ? 552  VAL   B C     1 
ATOM   8636  O  O     . VAL   B 1 552  ? 202.640 150.974 204.421 1.00 95.91  ? 552  VAL   B O     1 
ATOM   8637  N  N     . ASN   B 1 553  ? 202.447 153.213 204.534 1.00 102.77 ? 553  ASN   B N     1 
ATOM   8638  C  CA    . ASN   B 1 553  ? 201.904 153.172 205.887 1.00 102.22 ? 553  ASN   B CA    1 
ATOM   8639  C  C     . ASN   B 1 553  ? 200.596 152.396 205.938 1.00 102.93 ? 553  ASN   B C     1 
ATOM   8640  O  O     . ASN   B 1 553  ? 200.215 151.890 206.999 1.00 101.41 ? 553  ASN   B O     1 
ATOM   8641  C  CB    . ASN   B 1 553  ? 201.705 154.595 206.409 1.00 101.88 ? 553  ASN   B CB    1 
ATOM   8642  C  CG    . ASN   B 1 553  ? 201.797 154.682 207.918 1.00 102.50 ? 553  ASN   B CG    1 
ATOM   8643  O  OD1   . ASN   B 1 553  ? 202.334 153.789 208.572 1.00 103.72 ? 553  ASN   B OD1   1 
ATOM   8644  N  ND2   . ASN   B 1 553  ? 201.277 155.767 208.479 1.00 101.80 ? 553  ASN   B ND2   1 
ATOM   8645  N  N     . ASP   B 1 554  ? 199.896 152.292 204.811 1.00 94.69  ? 554  ASP   B N     1 
ATOM   8646  C  CA    . ASP   B 1 554  ? 198.663 151.526 204.771 1.00 92.40  ? 554  ASP   B CA    1 
ATOM   8647  C  C     . ASP   B 1 554  ? 198.950 150.055 205.067 1.00 92.21  ? 554  ASP   B C     1 
ATOM   8648  O  O     . ASP   B 1 554  ? 200.099 149.609 205.114 1.00 91.18  ? 554  ASP   B O     1 
ATOM   8649  N  N     . THR   B 1 555  ? 197.876 149.294 205.261 1.00 91.93  ? 555  THR   B N     1 
ATOM   8650  C  CA    . THR   B 1 555  ? 197.999 147.897 205.649 1.00 92.48  ? 555  THR   B CA    1 
ATOM   8651  C  C     . THR   B 1 555  ? 198.354 147.048 204.436 1.00 91.19  ? 555  THR   B C     1 
ATOM   8652  O  O     . THR   B 1 555  ? 197.597 146.991 203.461 1.00 91.28  ? 555  THR   B O     1 
ATOM   8653  N  N     . ILE   B 1 556  ? 199.514 146.391 204.498 1.00 103.39 ? 556  ILE   B N     1 
ATOM   8654  C  CA    . ILE   B 1 556  ? 199.954 145.479 203.451 1.00 105.41 ? 556  ILE   B CA    1 
ATOM   8655  C  C     . ILE   B 1 556  ? 200.349 144.111 203.982 1.00 106.94 ? 556  ILE   B C     1 
ATOM   8656  O  O     . ILE   B 1 556  ? 200.697 143.232 203.193 1.00 106.49 ? 556  ILE   B O     1 
ATOM   8657  N  N     . VAL   B 1 557  ? 200.305 143.900 205.299 1.00 119.31 ? 557  VAL   B N     1 
ATOM   8658  C  CA    . VAL   B 1 557  ? 200.706 142.612 205.860 1.00 119.31 ? 557  VAL   B CA    1 
ATOM   8659  C  C     . VAL   B 1 557  ? 199.715 141.522 205.471 1.00 120.20 ? 557  VAL   B C     1 
ATOM   8660  O  O     . VAL   B 1 557  ? 200.103 140.383 205.187 1.00 120.63 ? 557  VAL   B O     1 
ATOM   8661  N  N     . THR   B 1 558  ? 198.423 141.850 205.455 1.00 123.68 ? 558  THR   B N     1 
ATOM   8662  C  CA    . THR   B 1 558  ? 197.373 140.877 205.172 1.00 123.26 ? 558  THR   B CA    1 
ATOM   8663  C  C     . THR   B 1 558  ? 197.087 139.970 206.364 1.00 125.50 ? 558  THR   B C     1 
ATOM   8664  O  O     . THR   B 1 558  ? 196.648 138.830 206.196 1.00 125.64 ? 558  THR   B O     1 
ATOM   8665  N  N     . GLU   B 1 559  ? 197.331 140.470 207.575 1.00 127.72 ? 559  GLU   B N     1 
ATOM   8666  C  CA    . GLU   B 1 559  ? 197.108 139.700 208.793 1.00 125.21 ? 559  GLU   B CA    1 
ATOM   8667  C  C     . GLU   B 1 559  ? 195.628 139.382 208.962 1.00 126.94 ? 559  GLU   B C     1 
ATOM   8668  O  O     . GLU   B 1 559  ? 194.805 139.779 208.132 1.00 127.72 ? 559  GLU   B O     1 
ATOM   8669  N  N     . LEU   B 1 560  ? 195.287 138.656 210.025 1.00 128.62 ? 560  LEU   B N     1 
ATOM   8670  C  CA    . LEU   B 1 560  ? 193.907 138.247 210.260 1.00 129.12 ? 560  LEU   B CA    1 
ATOM   8671  C  C     . LEU   B 1 560  ? 192.960 139.430 210.114 1.00 129.75 ? 560  LEU   B C     1 
ATOM   8672  O  O     . LEU   B 1 560  ? 193.033 140.399 210.875 1.00 129.00 ? 560  LEU   B O     1 
ATOM   8673  N  N     . THR   B 1 561  ? 192.070 139.341 209.127 1.00 131.48 ? 561  THR   B N     1 
ATOM   8674  C  CA    . THR   B 1 561  ? 191.085 140.382 208.861 1.00 131.17 ? 561  THR   B CA    1 
ATOM   8675  C  C     . THR   B 1 561  ? 190.007 139.834 207.936 1.00 131.13 ? 561  THR   B C     1 
ATOM   8676  O  O     . THR   B 1 561  ? 190.319 139.274 206.880 1.00 130.51 ? 561  THR   B O     1 
ATOM   8677  N  N     . ASN   B 1 562  ? 188.739 139.982 208.320 1.00 133.65 ? 562  ASN   B N     1 
ATOM   8678  C  CA    . ASN   B 1 562  ? 187.653 139.376 207.560 1.00 133.53 ? 562  ASN   B CA    1 
ATOM   8679  C  C     . ASN   B 1 562  ? 187.631 139.892 206.126 1.00 134.66 ? 562  ASN   B C     1 
ATOM   8680  O  O     . ASN   B 1 562  ? 187.900 139.132 205.190 1.00 135.39 ? 562  ASN   B O     1 
ATOM   8681  C  CB    . ASN   B 1 562  ? 186.312 139.648 208.243 1.00 133.04 ? 562  ASN   B CB    1 
ATOM   8682  C  CG    . ASN   B 1 562  ? 185.867 138.501 209.127 1.00 133.82 ? 562  ASN   B CG    1 
ATOM   8683  O  OD1   . ASN   B 1 562  ? 185.406 137.469 208.640 1.00 133.14 ? 562  ASN   B OD1   1 
ATOM   8684  N  ND2   . ASN   B 1 562  ? 186.007 138.676 210.436 1.00 133.69 ? 562  ASN   B ND2   1 
ATOM   8685  N  N     . CYS   B 1 563  ? 187.329 141.176 205.951 1.00 137.98 ? 563  CYS   B N     1 
ATOM   8686  C  CA    . CYS   B 1 563  ? 187.388 141.850 204.653 1.00 138.80 ? 563  CYS   B CA    1 
ATOM   8687  C  C     . CYS   B 1 563  ? 186.871 140.945 203.531 1.00 138.54 ? 563  CYS   B C     1 
ATOM   8688  O  O     . CYS   B 1 563  ? 187.578 140.594 202.587 1.00 137.34 ? 563  CYS   B O     1 
ATOM   8689  C  CB    . CYS   B 1 563  ? 188.802 142.364 204.374 1.00 139.19 ? 563  CYS   B CB    1 
ATOM   8690  S  SG    . CYS   B 1 563  ? 190.002 141.138 203.818 1.00 144.57 ? 563  CYS   B SG    1 
ATOM   8691  N  N     . THR   B 1 564  ? 185.593 140.574 203.658 1.00 131.08 ? 564  THR   B N     1 
ATOM   8692  C  CA    . THR   B 1 564  ? 184.984 139.621 202.733 1.00 129.93 ? 564  THR   B CA    1 
ATOM   8693  C  C     . THR   B 1 564  ? 185.274 139.949 201.274 1.00 129.69 ? 564  THR   B C     1 
ATOM   8694  O  O     . THR   B 1 564  ? 185.258 139.052 200.422 1.00 128.69 ? 564  THR   B O     1 
ATOM   8695  N  N     . SER   B 1 565  ? 185.538 141.217 200.961 1.00 121.32 ? 565  SER   B N     1 
ATOM   8696  C  CA    . SER   B 1 565  ? 185.857 141.612 199.594 1.00 119.24 ? 565  SER   B CA    1 
ATOM   8697  C  C     . SER   B 1 565  ? 187.028 140.798 199.055 1.00 118.56 ? 565  SER   B C     1 
ATOM   8698  O  O     . SER   B 1 565  ? 187.788 140.204 199.828 1.00 120.31 ? 565  SER   B O     1 
ATOM   8699  N  N     . ALA   B 1 566  ? 187.181 140.766 197.731 1.00 106.08 ? 566  ALA   B N     1 
ATOM   8700  C  CA    . ALA   B 1 566  ? 188.220 139.961 197.102 1.00 106.96 ? 566  ALA   B CA    1 
ATOM   8701  C  C     . ALA   B 1 566  ? 189.560 140.677 197.004 1.00 107.49 ? 566  ALA   B C     1 
ATOM   8702  O  O     . ALA   B 1 566  ? 190.557 140.040 196.649 1.00 107.25 ? 566  ALA   B O     1 
ATOM   8703  N  N     . ALA   B 1 567  ? 189.612 141.975 197.313 1.00 104.01 ? 567  ALA   B N     1 
ATOM   8704  C  CA    . ALA   B 1 567  ? 190.872 142.703 197.237 1.00 101.49 ? 567  ALA   B CA    1 
ATOM   8705  C  C     . ALA   B 1 567  ? 191.937 142.108 198.146 1.00 104.07 ? 567  ALA   B C     1 
ATOM   8706  O  O     . ALA   B 1 567  ? 193.131 142.249 197.858 1.00 102.88 ? 567  ALA   B O     1 
ATOM   8707  C  CB    . ALA   B 1 567  ? 190.651 144.176 197.584 1.00 101.17 ? 567  ALA   B CB    1 
ATOM   8708  N  N     . CYS   B 1 568  ? 191.538 141.448 199.234 1.00 102.82 ? 568  CYS   B N     1 
ATOM   8709  C  CA    . CYS   B 1 568  ? 192.491 140.828 200.146 1.00 99.41  ? 568  CYS   B CA    1 
ATOM   8710  C  C     . CYS   B 1 568  ? 193.016 139.490 199.648 1.00 98.58  ? 568  CYS   B C     1 
ATOM   8711  O  O     . CYS   B 1 568  ? 193.943 138.948 200.260 1.00 98.14  ? 568  CYS   B O     1 
ATOM   8712  C  CB    . CYS   B 1 568  ? 191.864 140.625 201.527 1.00 102.01 ? 568  CYS   B CB    1 
ATOM   8713  S  SG    . CYS   B 1 568  ? 190.635 141.842 202.022 1.00 110.71 ? 568  CYS   B SG    1 
ATOM   8714  N  N     . LYS   B 1 569  ? 192.446 138.942 198.570 1.00 94.35  ? 569  LYS   B N     1 
ATOM   8715  C  CA    . LYS   B 1 569  ? 192.835 137.612 198.110 1.00 92.91  ? 569  LYS   B CA    1 
ATOM   8716  C  C     . LYS   B 1 569  ? 194.348 137.438 198.055 1.00 93.44  ? 569  LYS   B C     1 
ATOM   8717  O  O     . LYS   B 1 569  ? 194.854 136.331 198.270 1.00 93.43  ? 569  LYS   B O     1 
ATOM   8718  N  N     . LEU   B 1 570  ? 195.083 138.510 197.773 1.00 92.85  ? 570  LEU   B N     1 
ATOM   8719  C  CA    . LEU   B 1 570  ? 196.541 138.484 197.755 1.00 91.77  ? 570  LEU   B CA    1 
ATOM   8720  C  C     . LEU   B 1 570  ? 197.172 139.361 198.823 1.00 92.20  ? 570  LEU   B C     1 
ATOM   8721  O  O     . LEU   B 1 570  ? 198.206 138.992 199.385 1.00 92.17  ? 570  LEU   B O     1 
ATOM   8722  N  N     . ASN   B 1 571  ? 196.575 140.511 199.119 1.00 94.64  ? 571  ASN   B N     1 
ATOM   8723  C  CA    . ASN   B 1 571  ? 197.087 141.418 200.137 1.00 93.05  ? 571  ASN   B CA    1 
ATOM   8724  C  C     . ASN   B 1 571  ? 195.988 142.418 200.476 1.00 93.82  ? 571  ASN   B C     1 
ATOM   8725  O  O     . ASN   B 1 571  ? 194.924 142.437 199.852 1.00 93.87  ? 571  ASN   B O     1 
ATOM   8726  N  N     . PHE   B 1 572  ? 196.256 143.256 201.475 1.00 93.00  ? 572  PHE   B N     1 
ATOM   8727  C  CA    . PHE   B 1 572  ? 195.311 144.272 201.912 1.00 92.27  ? 572  PHE   B CA    1 
ATOM   8728  C  C     . PHE   B 1 572  ? 195.740 145.686 201.552 1.00 92.59  ? 572  PHE   B C     1 
ATOM   8729  O  O     . PHE   B 1 572  ? 195.088 146.644 201.980 1.00 90.89  ? 572  PHE   B O     1 
ATOM   8730  N  N     . ASP   B 1 573  ? 196.815 145.844 200.784 1.00 92.82  ? 573  ASP   B N     1 
ATOM   8731  C  CA    . ASP   B 1 573  ? 197.261 147.171 200.384 1.00 93.58  ? 573  ASP   B CA    1 
ATOM   8732  C  C     . ASP   B 1 573  ? 196.208 147.837 199.507 1.00 99.03  ? 573  ASP   B C     1 
ATOM   8733  O  O     . ASP   B 1 573  ? 195.673 147.221 198.580 1.00 99.18  ? 573  ASP   B O     1 
ATOM   8734  N  N     . PHE   B 1 574  ? 195.911 149.102 199.801 1.00 89.17  ? 574  PHE   B N     1 
ATOM   8735  C  CA    . PHE   B 1 574  ? 194.938 149.876 199.035 1.00 83.64  ? 574  PHE   B CA    1 
ATOM   8736  C  C     . PHE   B 1 574  ? 193.558 149.214 199.083 1.00 82.70  ? 574  PHE   B C     1 
ATOM   8737  O  O     . PHE   B 1 574  ? 192.991 148.811 198.066 1.00 78.00  ? 574  PHE   B O     1 
ATOM   8738  C  CB    . PHE   B 1 574  ? 195.414 150.065 197.592 1.00 81.38  ? 574  PHE   B CB    1 
ATOM   8739  N  N     . SER   B 1 575  ? 193.030 149.101 200.299 1.00 93.51  ? 575  SER   B N     1 
ATOM   8740  C  CA    . SER   B 1 575  ? 191.738 148.472 200.524 1.00 92.51  ? 575  SER   B CA    1 
ATOM   8741  C  C     . SER   B 1 575  ? 190.980 149.232 201.602 1.00 92.10  ? 575  SER   B C     1 
ATOM   8742  O  O     . SER   B 1 575  ? 191.562 149.967 202.403 1.00 91.04  ? 575  SER   B O     1 
ATOM   8743  C  CB    . SER   B 1 575  ? 191.890 146.999 200.928 1.00 92.30  ? 575  SER   B CB    1 
ATOM   8744  O  OG    . SER   B 1 575  ? 193.048 146.808 201.723 1.00 90.02  ? 575  SER   B OG    1 
ATOM   8745  N  N     . SER   B 1 576  ? 189.660 149.040 201.609 1.00 89.91  ? 576  SER   B N     1 
ATOM   8746  C  CA    . SER   B 1 576  ? 188.793 149.559 202.666 1.00 89.04  ? 576  SER   B CA    1 
ATOM   8747  C  C     . SER   B 1 576  ? 188.611 151.075 202.576 1.00 90.74  ? 576  SER   B C     1 
ATOM   8748  O  O     . SER   B 1 576  ? 188.556 151.763 203.596 1.00 88.45  ? 576  SER   B O     1 
ATOM   8749  C  CB    . SER   B 1 576  ? 189.315 149.161 204.049 1.00 88.63  ? 576  SER   B CB    1 
ATOM   8750  N  N     . CYS   B 1 577  ? 188.518 151.604 201.355 1.00 103.59 ? 577  CYS   B N     1 
ATOM   8751  C  CA    . CYS   B 1 577  ? 188.088 152.982 201.147 1.00 103.15 ? 577  CYS   B CA    1 
ATOM   8752  C  C     . CYS   B 1 577  ? 186.736 153.039 200.441 1.00 102.17 ? 577  CYS   B C     1 
ATOM   8753  O  O     . CYS   B 1 577  ? 186.465 153.964 199.672 1.00 101.79 ? 577  CYS   B O     1 
ATOM   8754  C  CB    . CYS   B 1 577  ? 189.130 153.788 200.368 1.00 103.59 ? 577  CYS   B CB    1 
ATOM   8755  S  SG    . CYS   B 1 577  ? 189.750 153.059 198.834 1.00 107.87 ? 577  CYS   B SG    1 
ATOM   8756  N  N     . GLU   B 1 578  ? 185.875 152.050 200.698 1.00 93.00  ? 578  GLU   B N     1 
ATOM   8757  C  CA    . GLU   B 1 578  ? 184.547 152.040 200.096 1.00 90.83  ? 578  GLU   B CA    1 
ATOM   8758  C  C     . GLU   B 1 578  ? 183.696 153.211 200.565 1.00 92.05  ? 578  GLU   B C     1 
ATOM   8759  O  O     . GLU   B 1 578  ? 182.683 153.522 199.928 1.00 90.82  ? 578  GLU   B O     1 
ATOM   8760  C  CB    . GLU   B 1 578  ? 183.839 150.721 200.408 1.00 88.41  ? 578  GLU   B CB    1 
ATOM   8761  N  N     . SER   B 1 579  ? 184.079 153.864 201.660 1.00 99.97  ? 579  SER   B N     1 
ATOM   8762  C  CA    . SER   B 1 579  ? 183.390 155.044 202.163 1.00 100.12 ? 579  SER   B CA    1 
ATOM   8763  C  C     . SER   B 1 579  ? 184.223 156.308 202.020 1.00 99.37  ? 579  SER   B C     1 
ATOM   8764  O  O     . SER   B 1 579  ? 183.700 157.356 201.631 1.00 99.49  ? 579  SER   B O     1 
ATOM   8765  N  N     . SER   B 1 580  ? 185.513 156.233 202.328 1.00 99.52  ? 580  SER   B N     1 
ATOM   8766  C  CA    . SER   B 1 580  ? 186.425 157.354 202.136 1.00 99.98  ? 580  SER   B CA    1 
ATOM   8767  C  C     . SER   B 1 580  ? 186.960 157.332 200.710 1.00 102.03 ? 580  SER   B C     1 
ATOM   8768  O  O     . SER   B 1 580  ? 187.462 156.295 200.262 1.00 104.45 ? 580  SER   B O     1 
ATOM   8769  N  N     . PRO   B 1 581  ? 186.869 158.436 199.971 1.00 98.66  ? 581  PRO   B N     1 
ATOM   8770  C  CA    . PRO   B 1 581  ? 187.317 158.419 198.574 1.00 97.90  ? 581  PRO   B CA    1 
ATOM   8771  C  C     . PRO   B 1 581  ? 188.780 158.015 198.468 1.00 98.08  ? 581  PRO   B C     1 
ATOM   8772  O  O     . PRO   B 1 581  ? 189.619 158.428 199.270 1.00 97.90  ? 581  PRO   B O     1 
ATOM   8773  C  CB    . PRO   B 1 581  ? 187.093 159.864 198.112 1.00 97.47  ? 581  PRO   B CB    1 
ATOM   8774  C  CG    . PRO   B 1 581  ? 187.079 160.669 199.375 1.00 96.80  ? 581  PRO   B CG    1 
ATOM   8775  C  CD    . PRO   B 1 581  ? 186.451 159.779 200.403 1.00 97.18  ? 581  PRO   B CD    1 
ATOM   8776  N  N     . CYS   B 1 582  ? 189.079 157.198 197.461 1.00 95.60  ? 582  CYS   B N     1 
ATOM   8777  C  CA    . CYS   B 1 582  ? 190.427 156.698 197.252 1.00 94.50  ? 582  CYS   B CA    1 
ATOM   8778  C  C     . CYS   B 1 582  ? 191.159 157.601 196.259 1.00 93.52  ? 582  CYS   B C     1 
ATOM   8779  O  O     . CYS   B 1 582  ? 190.550 158.359 195.502 1.00 94.28  ? 582  CYS   B O     1 
ATOM   8780  C  CB    . CYS   B 1 582  ? 190.387 155.247 196.769 1.00 95.15  ? 582  CYS   B CB    1 
ATOM   8781  S  SG    . CYS   B 1 582  ? 188.984 154.273 197.392 1.00 106.61 ? 582  CYS   B SG    1 
ATOM   8782  N  N     . SER   B 1 583  ? 192.491 157.524 196.262 1.00 75.84  ? 583  SER   B N     1 
ATOM   8783  C  CA    . SER   B 1 583  ? 193.307 158.373 195.408 1.00 71.19  ? 583  SER   B CA    1 
ATOM   8784  C  C     . SER   B 1 583  ? 193.986 157.637 194.262 1.00 72.30  ? 583  SER   B C     1 
ATOM   8785  O  O     . SER   B 1 583  ? 194.737 158.264 193.508 1.00 73.67  ? 583  SER   B O     1 
ATOM   8786  N  N     . TYR   B 1 584  ? 193.749 156.338 194.108 1.00 67.84  ? 584  TYR   B N     1 
ATOM   8787  C  CA    . TYR   B 1 584  ? 194.355 155.553 193.041 1.00 64.69  ? 584  TYR   B CA    1 
ATOM   8788  C  C     . TYR   B 1 584  ? 193.336 154.517 192.577 1.00 67.82  ? 584  TYR   B C     1 
ATOM   8789  O  O     . TYR   B 1 584  ? 192.154 154.579 192.928 1.00 70.27  ? 584  TYR   B O     1 
ATOM   8790  C  CB    . TYR   B 1 584  ? 195.669 154.918 193.517 1.00 68.07  ? 584  TYR   B CB    1 
ATOM   8791  C  CG    . TYR   B 1 584  ? 196.815 155.899 193.632 1.00 70.28  ? 584  TYR   B CG    1 
ATOM   8792  C  CD1   . TYR   B 1 584  ? 197.003 156.649 194.785 1.00 70.52  ? 584  TYR   B CD1   1 
ATOM   8793  C  CD2   . TYR   B 1 584  ? 197.707 156.078 192.584 1.00 69.46  ? 584  TYR   B CD2   1 
ATOM   8794  C  CE1   . TYR   B 1 584  ? 198.048 157.547 194.891 1.00 70.41  ? 584  TYR   B CE1   1 
ATOM   8795  C  CE2   . TYR   B 1 584  ? 198.753 156.972 192.680 1.00 67.96  ? 584  TYR   B CE2   1 
ATOM   8796  C  CZ    . TYR   B 1 584  ? 198.920 157.704 193.835 1.00 73.16  ? 584  TYR   B CZ    1 
ATOM   8797  O  OH    . TYR   B 1 584  ? 199.963 158.596 193.933 1.00 74.42  ? 584  TYR   B OH    1 
ATOM   8798  N  N     . GLY   B 1 585  ? 193.794 153.561 191.777 1.00 58.03  ? 585  GLY   B N     1 
ATOM   8799  C  CA    . GLY   B 1 585  ? 192.947 152.496 191.284 1.00 58.00  ? 585  GLY   B CA    1 
ATOM   8800  C  C     . GLY   B 1 585  ? 192.424 152.765 189.883 1.00 60.20  ? 585  GLY   B C     1 
ATOM   8801  O  O     . GLY   B 1 585  ? 192.626 153.829 189.292 1.00 62.08  ? 585  GLY   B O     1 
ATOM   8802  N  N     . LEU   B 1 586  ? 191.728 151.763 189.351 1.00 57.29  ? 586  LEU   B N     1 
ATOM   8803  C  CA    . LEU   B 1 586  ? 191.189 151.806 187.998 1.00 46.85  ? 586  LEU   B CA    1 
ATOM   8804  C  C     . LEU   B 1 586  ? 189.944 152.677 187.878 1.00 53.07  ? 586  LEU   B C     1 
ATOM   8805  O  O     . LEU   B 1 586  ? 189.304 152.667 186.821 1.00 59.13  ? 586  LEU   B O     1 
ATOM   8806  C  CB    . LEU   B 1 586  ? 190.872 150.388 187.519 1.00 44.08  ? 586  LEU   B CB    1 
ATOM   8807  C  CG    . LEU   B 1 586  ? 191.996 149.654 186.785 1.00 48.51  ? 586  LEU   B CG    1 
ATOM   8808  C  CD1   . LEU   B 1 586  ? 191.440 148.537 185.921 1.00 48.86  ? 586  LEU   B CD1   1 
ATOM   8809  C  CD2   . LEU   B 1 586  ? 192.800 150.628 185.947 1.00 56.92  ? 586  LEU   B CD2   1 
ATOM   8810  N  N     . MET   B 1 587  ? 189.585 153.426 188.923 1.00 56.89  ? 587  MET   B N     1 
ATOM   8811  C  CA    . MET   B 1 587  ? 188.415 154.293 188.882 1.00 55.97  ? 587  MET   B CA    1 
ATOM   8812  C  C     . MET   B 1 587  ? 188.675 155.710 189.370 1.00 57.43  ? 587  MET   B C     1 
ATOM   8813  O  O     . MET   B 1 587  ? 187.777 156.550 189.256 1.00 61.84  ? 587  MET   B O     1 
ATOM   8814  C  CB    . MET   B 1 587  ? 187.270 153.694 189.713 1.00 54.23  ? 587  MET   B CB    1 
ATOM   8815  C  CG    . MET   B 1 587  ? 185.894 154.211 189.331 1.00 59.44  ? 587  MET   B CG    1 
ATOM   8816  S  SD    . MET   B 1 587  ? 184.626 152.934 189.398 1.00 72.32  ? 587  MET   B SD    1 
ATOM   8817  C  CE    . MET   B 1 587  ? 185.405 151.636 188.449 1.00 56.97  ? 587  MET   B CE    1 
ATOM   8818  N  N     . ASN   B 1 588  ? 189.861 156.006 189.901 1.00 56.25  ? 588  ASN   B N     1 
ATOM   8819  C  CA    . ASN   B 1 588  ? 190.165 157.336 190.406 1.00 60.99  ? 588  ASN   B CA    1 
ATOM   8820  C  C     . ASN   B 1 588  ? 191.463 157.917 189.869 1.00 60.32  ? 588  ASN   B C     1 
ATOM   8821  O  O     . ASN   B 1 588  ? 191.686 159.122 190.029 1.00 63.24  ? 588  ASN   B O     1 
ATOM   8822  C  CB    . ASN   B 1 588  ? 190.226 157.329 191.942 1.00 59.28  ? 588  ASN   B CB    1 
ATOM   8823  N  N     . ASN   B 1 589  ? 192.320 157.114 189.247 1.00 56.79  ? 589  ASN   B N     1 
ATOM   8824  C  CA    . ASN   B 1 589  ? 193.568 157.589 188.671 1.00 57.68  ? 589  ASN   B CA    1 
ATOM   8825  C  C     . ASN   B 1 589  ? 193.612 157.231 187.193 1.00 63.76  ? 589  ASN   B C     1 
ATOM   8826  O  O     . ASN   B 1 589  ? 193.273 156.108 186.806 1.00 67.16  ? 589  ASN   B O     1 
ATOM   8827  C  CB    . ASN   B 1 589  ? 194.776 156.989 189.394 1.00 58.53  ? 589  ASN   B CB    1 
ATOM   8828  C  CG    . ASN   B 1 589  ? 196.087 157.590 188.934 1.00 62.53  ? 589  ASN   B CG    1 
ATOM   8829  O  OD1   . ASN   B 1 589  ? 196.152 158.768 188.582 1.00 64.25  ? 589  ASN   B OD1   1 
ATOM   8830  N  ND2   . ASN   B 1 589  ? 197.142 156.785 188.939 1.00 60.56  ? 589  ASN   B ND2   1 
ATOM   8831  N  N     . PHE   B 1 590  ? 194.028 158.190 186.369 1.00 57.82  ? 590  PHE   B N     1 
ATOM   8832  C  CA    . PHE   B 1 590  ? 194.122 157.975 184.933 1.00 54.76  ? 590  PHE   B CA    1 
ATOM   8833  C  C     . PHE   B 1 590  ? 195.531 157.652 184.463 1.00 58.10  ? 590  PHE   B C     1 
ATOM   8834  O  O     . PHE   B 1 590  ? 195.691 157.121 183.359 1.00 65.70  ? 590  PHE   B O     1 
ATOM   8835  C  CB    . PHE   B 1 590  ? 193.603 159.207 184.182 1.00 53.03  ? 590  PHE   B CB    1 
ATOM   8836  C  CG    . PHE   B 1 590  ? 192.181 159.554 184.511 1.00 54.33  ? 590  PHE   B CG    1 
ATOM   8837  C  CD1   . PHE   B 1 590  ? 191.886 160.406 185.559 1.00 56.43  ? 590  PHE   B CD1   1 
ATOM   8838  C  CD2   . PHE   B 1 590  ? 191.138 159.019 183.776 1.00 54.86  ? 590  PHE   B CD2   1 
ATOM   8839  C  CE1   . PHE   B 1 590  ? 190.577 160.720 185.866 1.00 57.34  ? 590  PHE   B CE1   1 
ATOM   8840  C  CE2   . PHE   B 1 590  ? 189.828 159.331 184.078 1.00 55.18  ? 590  PHE   B CE2   1 
ATOM   8841  C  CZ    . PHE   B 1 590  ? 189.548 160.182 185.124 1.00 54.84  ? 590  PHE   B CZ    1 
ATOM   8842  N  N     . GLN   B 1 591  ? 196.548 157.945 185.271 1.00 49.72  ? 591  GLN   B N     1 
ATOM   8843  C  CA    . GLN   B 1 591  ? 197.934 157.679 184.916 1.00 51.79  ? 591  GLN   B CA    1 
ATOM   8844  C  C     . GLN   B 1 591  ? 198.337 156.232 185.156 1.00 56.04  ? 591  GLN   B C     1 
ATOM   8845  O  O     . GLN   B 1 591  ? 199.538 155.936 185.175 1.00 62.64  ? 591  GLN   B O     1 
ATOM   8846  C  CB    . GLN   B 1 591  ? 198.872 158.604 185.697 1.00 55.34  ? 591  GLN   B CB    1 
ATOM   8847  C  CG    . GLN   B 1 591  ? 198.455 160.066 185.737 1.00 56.14  ? 591  GLN   B CG    1 
ATOM   8848  C  CD    . GLN   B 1 591  ? 197.802 160.532 184.454 1.00 60.12  ? 591  GLN   B CD    1 
ATOM   8849  O  OE1   . GLN   B 1 591  ? 196.659 160.184 184.163 1.00 62.37  ? 591  GLN   B OE1   1 
ATOM   8850  N  NE2   . GLN   B 1 591  ? 198.528 161.324 183.676 1.00 61.91  ? 591  GLN   B NE2   1 
ATOM   8851  N  N     . VAL   B 1 592  ? 197.371 155.326 185.323 1.00 48.52  ? 592  VAL   B N     1 
ATOM   8852  C  CA    . VAL   B 1 592  ? 197.702 153.965 185.736 1.00 52.65  ? 592  VAL   B CA    1 
ATOM   8853  C  C     . VAL   B 1 592  ? 198.677 153.332 184.753 1.00 54.92  ? 592  VAL   B C     1 
ATOM   8854  O  O     . VAL   B 1 592  ? 199.637 152.663 185.155 1.00 60.22  ? 592  VAL   B O     1 
ATOM   8855  C  CB    . VAL   B 1 592  ? 196.422 153.122 185.902 1.00 51.65  ? 592  VAL   B CB    1 
ATOM   8856  C  CG1   . VAL   B 1 592  ? 195.265 153.995 186.362 1.00 50.61  ? 592  VAL   B CG1   1 
ATOM   8857  C  CG2   . VAL   B 1 592  ? 196.075 152.390 184.615 1.00 53.02  ? 592  VAL   B CG2   1 
ATOM   8858  N  N     . MET   B 1 593  ? 198.466 153.549 183.452 1.00 53.91  ? 593  MET   B N     1 
ATOM   8859  C  CA    . MET   B 1 593  ? 199.400 153.024 182.462 1.00 52.56  ? 593  MET   B CA    1 
ATOM   8860  C  C     . MET   B 1 593  ? 200.819 153.485 182.765 1.00 60.01  ? 593  MET   B C     1 
ATOM   8861  O  O     . MET   B 1 593  ? 201.741 152.670 182.881 1.00 66.43  ? 593  MET   B O     1 
ATOM   8862  C  CB    . MET   B 1 593  ? 198.982 153.464 181.058 1.00 57.05  ? 593  MET   B CB    1 
ATOM   8863  C  CG    . MET   B 1 593  ? 197.499 153.330 180.768 1.00 60.08  ? 593  MET   B CG    1 
ATOM   8864  S  SD    . MET   B 1 593  ? 197.080 151.736 180.044 1.00 64.93  ? 593  MET   B SD    1 
ATOM   8865  C  CE    . MET   B 1 593  ? 195.570 151.364 180.924 1.00 59.28  ? 593  MET   B CE    1 
ATOM   8866  N  N     . SER   B 1 594  ? 201.002 154.797 182.932 1.00 54.76  ? 594  SER   B N     1 
ATOM   8867  C  CA    . SER   B 1 594  ? 202.321 155.321 183.268 1.00 50.01  ? 594  SER   B CA    1 
ATOM   8868  C  C     . SER   B 1 594  ? 202.874 154.653 184.519 1.00 56.10  ? 594  SER   B C     1 
ATOM   8869  O  O     . SER   B 1 594  ? 204.084 154.418 184.624 1.00 59.85  ? 594  SER   B O     1 
ATOM   8870  C  CB    . SER   B 1 594  ? 202.251 156.836 183.452 1.00 47.98  ? 594  SER   B CB    1 
ATOM   8871  N  N     . MET   B 1 595  ? 202.004 154.339 185.481 1.00 55.14  ? 595  MET   B N     1 
ATOM   8872  C  CA    . MET   B 1 595  ? 202.462 153.669 186.693 1.00 53.66  ? 595  MET   B CA    1 
ATOM   8873  C  C     . MET   B 1 595  ? 202.759 152.198 186.434 1.00 52.19  ? 595  MET   B C     1 
ATOM   8874  O  O     . MET   B 1 595  ? 203.710 151.643 186.996 1.00 57.72  ? 595  MET   B O     1 
ATOM   8875  C  CB    . MET   B 1 595  ? 201.423 153.823 187.802 1.00 56.85  ? 595  MET   B CB    1 
ATOM   8876  C  CG    . MET   B 1 595  ? 201.763 153.070 189.075 1.00 57.41  ? 595  MET   B CG    1 
ATOM   8877  S  SD    . MET   B 1 595  ? 200.827 151.539 189.237 1.00 64.65  ? 595  MET   B SD    1 
ATOM   8878  C  CE    . MET   B 1 595  ? 199.154 152.176 189.257 1.00 53.09  ? 595  MET   B CE    1 
ATOM   8879  N  N     . VAL   B 1 596  ? 201.958 151.546 185.585 1.00 47.72  ? 596  VAL   B N     1 
ATOM   8880  C  CA    . VAL   B 1 596  ? 202.135 150.116 185.339 1.00 46.09  ? 596  VAL   B CA    1 
ATOM   8881  C  C     . VAL   B 1 596  ? 203.239 149.822 184.339 1.00 52.20  ? 596  VAL   B C     1 
ATOM   8882  O  O     . VAL   B 1 596  ? 203.570 148.650 184.121 1.00 55.31  ? 596  VAL   B O     1 
ATOM   8883  C  CB    . VAL   B 1 596  ? 200.819 149.482 184.850 1.00 47.57  ? 596  VAL   B CB    1 
ATOM   8884  C  CG1   . VAL   B 1 596  ? 200.942 147.969 184.792 1.00 52.46  ? 596  VAL   B CG1   1 
ATOM   8885  C  CG2   . VAL   B 1 596  ? 199.670 149.886 185.756 1.00 51.79  ? 596  VAL   B CG2   1 
ATOM   8886  N  N     . SER   B 1 597  ? 203.826 150.848 183.735 1.00 54.86  ? 597  SER   B N     1 
ATOM   8887  C  CA    . SER   B 1 597  ? 204.846 150.655 182.715 1.00 52.61  ? 597  SER   B CA    1 
ATOM   8888  C  C     . SER   B 1 597  ? 206.204 150.431 183.377 1.00 55.14  ? 597  SER   B C     1 
ATOM   8889  O  O     . SER   B 1 597  ? 206.312 150.223 184.589 1.00 64.39  ? 597  SER   B O     1 
ATOM   8890  C  CB    . SER   B 1 597  ? 204.869 151.849 181.765 1.00 57.75  ? 597  SER   B CB    1 
ATOM   8891  O  OG    . SER   B 1 597  ? 205.512 152.960 182.364 1.00 61.68  ? 597  SER   B OG    1 
ATOM   8892  N  N     . GLY   B 1 598  ? 207.260 150.468 182.572 1.00 47.75  ? 598  GLY   B N     1 
ATOM   8893  C  CA    . GLY   B 1 598  ? 208.616 150.412 183.075 1.00 49.98  ? 598  GLY   B CA    1 
ATOM   8894  C  C     . GLY   B 1 598  ? 209.177 151.813 183.172 1.00 55.36  ? 598  GLY   B C     1 
ATOM   8895  O  O     . GLY   B 1 598  ? 208.889 152.535 184.132 1.00 59.85  ? 598  GLY   B O     1 
ATOM   8896  N  N     . PHE   B 1 599  ? 209.981 152.211 182.190 1.00 54.79  ? 599  PHE   B N     1 
ATOM   8897  C  CA    . PHE   B 1 599  ? 210.414 153.598 182.101 1.00 53.18  ? 599  PHE   B CA    1 
ATOM   8898  C  C     . PHE   B 1 599  ? 209.194 154.512 182.103 1.00 54.25  ? 599  PHE   B C     1 
ATOM   8899  O  O     . PHE   B 1 599  ? 208.250 154.308 181.335 1.00 56.10  ? 599  PHE   B O     1 
ATOM   8900  C  CB    . PHE   B 1 599  ? 211.235 153.806 180.827 1.00 54.16  ? 599  PHE   B CB    1 
ATOM   8901  C  CG    . PHE   B 1 599  ? 212.296 154.861 180.951 1.00 55.53  ? 599  PHE   B CG    1 
ATOM   8902  C  CD1   . PHE   B 1 599  ? 212.218 155.834 181.929 1.00 55.32  ? 599  PHE   B CD1   1 
ATOM   8903  C  CD2   . PHE   B 1 599  ? 213.371 154.881 180.079 1.00 57.71  ? 599  PHE   B CD2   1 
ATOM   8904  C  CE1   . PHE   B 1 599  ? 213.197 156.802 182.042 1.00 56.84  ? 599  PHE   B CE1   1 
ATOM   8905  C  CE2   . PHE   B 1 599  ? 214.351 155.848 180.186 1.00 57.10  ? 599  PHE   B CE2   1 
ATOM   8906  C  CZ    . PHE   B 1 599  ? 214.263 156.810 181.168 1.00 59.12  ? 599  PHE   B CZ    1 
ATOM   8907  N  N     . THR   B 1 600  ? 209.214 155.516 182.976 1.00 56.68  ? 600  THR   B N     1 
ATOM   8908  C  CA    . THR   B 1 600  ? 208.050 156.373 183.177 1.00 52.96  ? 600  THR   B CA    1 
ATOM   8909  C  C     . THR   B 1 600  ? 207.891 157.386 182.048 1.00 59.50  ? 600  THR   B C     1 
ATOM   8910  O  O     . THR   B 1 600  ? 206.826 157.452 181.421 1.00 66.42  ? 600  THR   B O     1 
ATOM   8911  C  CB    . THR   B 1 600  ? 208.146 157.098 184.521 1.00 50.72  ? 600  THR   B CB    1 
ATOM   8912  N  N     . PRO   B 1 601  ? 208.915 158.192 181.759 1.00 51.60  ? 601  PRO   B N     1 
ATOM   8913  C  CA    . PRO   B 1 601  ? 208.761 159.225 180.720 1.00 55.49  ? 601  PRO   B CA    1 
ATOM   8914  C  C     . PRO   B 1 601  ? 208.496 158.670 179.332 1.00 58.62  ? 601  PRO   B C     1 
ATOM   8915  O  O     . PRO   B 1 601  ? 208.040 159.421 178.462 1.00 58.46  ? 601  PRO   B O     1 
ATOM   8916  C  CB    . PRO   B 1 601  ? 210.095 159.985 180.772 1.00 56.79  ? 601  PRO   B CB    1 
ATOM   8917  C  CG    . PRO   B 1 601  ? 211.038 159.085 181.484 1.00 56.11  ? 601  PRO   B CG    1 
ATOM   8918  C  CD    . PRO   B 1 601  ? 210.220 158.272 182.432 1.00 54.81  ? 601  PRO   B CD    1 
ATOM   8919  N  N     . LEU   B 1 602  ? 208.780 157.391 179.083 1.00 55.88  ? 602  LEU   B N     1 
ATOM   8920  C  CA    . LEU   B 1 602  ? 208.505 156.836 177.764 1.00 48.70  ? 602  LEU   B CA    1 
ATOM   8921  C  C     . LEU   B 1 602  ? 207.008 156.787 177.478 1.00 47.75  ? 602  LEU   B C     1 
ATOM   8922  O  O     . LEU   B 1 602  ? 206.592 156.978 176.331 1.00 56.10  ? 602  LEU   B O     1 
ATOM   8923  C  CB    . LEU   B 1 602  ? 209.132 155.448 177.635 1.00 52.96  ? 602  LEU   B CB    1 
ATOM   8924  C  CG    . LEU   B 1 602  ? 208.952 154.757 176.284 1.00 52.48  ? 602  LEU   B CG    1 
ATOM   8925  C  CD1   . LEU   B 1 602  ? 209.955 155.297 175.279 1.00 52.85  ? 602  LEU   B CD1   1 
ATOM   8926  C  CD2   . LEU   B 1 602  ? 209.114 153.258 176.433 1.00 54.58  ? 602  LEU   B CD2   1 
ATOM   8927  N  N     . ILE   B 1 603  ? 206.184 156.544 178.500 1.00 47.18  ? 603  ILE   B N     1 
ATOM   8928  C  CA    . ILE   B 1 603  ? 204.736 156.599 178.309 1.00 49.34  ? 603  ILE   B CA    1 
ATOM   8929  C  C     . ILE   B 1 603  ? 204.302 158.014 177.946 1.00 52.53  ? 603  ILE   B C     1 
ATOM   8930  O  O     . ILE   B 1 603  ? 203.441 158.215 177.080 1.00 56.72  ? 603  ILE   B O     1 
ATOM   8931  C  CB    . ILE   B 1 603  ? 204.007 156.089 179.565 1.00 51.89  ? 603  ILE   B CB    1 
ATOM   8932  C  CG1   . ILE   B 1 603  ? 204.156 154.573 179.692 1.00 53.46  ? 603  ILE   B CG1   1 
ATOM   8933  C  CG2   . ILE   B 1 603  ? 202.537 156.479 179.520 1.00 50.04  ? 603  ILE   B CG2   1 
ATOM   8934  C  CD1   . ILE   B 1 603  ? 203.727 153.810 178.460 1.00 48.84  ? 603  ILE   B CD1   1 
ATOM   8935  N  N     . SER   B 1 604  ? 204.881 159.016 178.610 1.00 55.33  ? 604  SER   B N     1 
ATOM   8936  C  CA    . SER   B 1 604  ? 204.564 160.400 178.275 1.00 51.42  ? 604  SER   B CA    1 
ATOM   8937  C  C     . SER   B 1 604  ? 204.988 160.728 176.849 1.00 52.50  ? 604  SER   B C     1 
ATOM   8938  O  O     . SER   B 1 604  ? 204.285 161.450 176.133 1.00 57.57  ? 604  SER   B O     1 
ATOM   8939  C  CB    . SER   B 1 604  ? 205.234 161.346 179.270 1.00 53.97  ? 604  SER   B CB    1 
ATOM   8940  O  OG    . SER   B 1 604  ? 204.844 161.046 180.599 1.00 61.34  ? 604  SER   B OG    1 
ATOM   8941  N  N     . ALA   B 1 605  ? 206.140 160.209 176.422 1.00 49.72  ? 605  ALA   B N     1 
ATOM   8942  C  CA    . ALA   B 1 605  ? 206.575 160.408 175.042 1.00 47.83  ? 605  ALA   B CA    1 
ATOM   8943  C  C     . ALA   B 1 605  ? 205.611 159.751 174.062 1.00 49.81  ? 605  ALA   B C     1 
ATOM   8944  O  O     . ALA   B 1 605  ? 205.310 160.311 173.002 1.00 51.66  ? 605  ALA   B O     1 
ATOM   8945  C  CB    . ALA   B 1 605  ? 207.989 159.863 174.851 1.00 50.68  ? 605  ALA   B CB    1 
ATOM   8946  N  N     . GLY   B 1 606  ? 205.134 158.550 174.391 1.00 50.93  ? 606  GLY   B N     1 
ATOM   8947  C  CA    . GLY   B 1 606  ? 204.135 157.909 173.552 1.00 47.55  ? 606  GLY   B CA    1 
ATOM   8948  C  C     . GLY   B 1 606  ? 202.854 158.714 173.467 1.00 49.63  ? 606  GLY   B C     1 
ATOM   8949  O  O     . GLY   B 1 606  ? 202.225 158.791 172.410 1.00 54.51  ? 606  GLY   B O     1 
ATOM   8950  N  N     . ILE   B 1 607  ? 202.455 159.333 174.580 1.00 48.13  ? 607  ILE   B N     1 
ATOM   8951  C  CA    . ILE   B 1 607  ? 201.276 160.196 174.566 1.00 47.30  ? 607  ILE   B CA    1 
ATOM   8952  C  C     . ILE   B 1 607  ? 201.516 161.412 173.680 1.00 50.27  ? 607  ILE   B C     1 
ATOM   8953  O  O     . ILE   B 1 607  ? 200.636 161.824 172.913 1.00 54.59  ? 607  ILE   B O     1 
ATOM   8954  C  CB    . ILE   B 1 607  ? 200.896 160.607 176.000 1.00 51.17  ? 607  ILE   B CB    1 
ATOM   8955  C  CG1   . ILE   B 1 607  ? 200.187 159.456 176.715 1.00 53.89  ? 607  ILE   B CG1   1 
ATOM   8956  C  CG2   . ILE   B 1 607  ? 200.020 161.848 175.982 1.00 48.97  ? 607  ILE   B CG2   1 
ATOM   8957  C  CD1   . ILE   B 1 607  ? 199.437 159.880 177.958 1.00 51.80  ? 607  ILE   B CD1   1 
ATOM   8958  N  N     . PHE   B 1 608  ? 202.703 162.012 173.779 1.00 49.13  ? 608  PHE   B N     1 
ATOM   8959  C  CA    . PHE   B 1 608  ? 203.042 163.133 172.909 1.00 44.06  ? 608  PHE   B CA    1 
ATOM   8960  C  C     . PHE   B 1 608  ? 202.945 162.726 171.445 1.00 46.18  ? 608  PHE   B C     1 
ATOM   8961  O  O     . PHE   B 1 608  ? 202.376 163.451 170.621 1.00 52.93  ? 608  PHE   B O     1 
ATOM   8962  C  CB    . PHE   B 1 608  ? 204.449 163.644 173.221 1.00 47.17  ? 608  PHE   B CB    1 
ATOM   8963  C  CG    . PHE   B 1 608  ? 204.583 164.282 174.572 1.00 51.33  ? 608  PHE   B CG    1 
ATOM   8964  C  CD1   . PHE   B 1 608  ? 203.723 165.290 174.968 1.00 51.41  ? 608  PHE   B CD1   1 
ATOM   8965  C  CD2   . PHE   B 1 608  ? 205.588 163.889 175.438 1.00 49.92  ? 608  PHE   B CD2   1 
ATOM   8966  C  CE1   . PHE   B 1 608  ? 203.854 165.882 176.207 1.00 51.65  ? 608  PHE   B CE1   1 
ATOM   8967  C  CE2   . PHE   B 1 608  ? 205.722 164.477 176.678 1.00 51.53  ? 608  PHE   B CE2   1 
ATOM   8968  C  CZ    . PHE   B 1 608  ? 204.854 165.475 177.063 1.00 49.14  ? 608  PHE   B CZ    1 
ATOM   8969  N  N     . SER   B 1 609  ? 203.508 161.566 171.104 1.00 46.71  ? 609  SER   B N     1 
ATOM   8970  C  CA    . SER   B 1 609  ? 203.473 161.100 169.722 1.00 46.26  ? 609  SER   B CA    1 
ATOM   8971  C  C     . SER   B 1 609  ? 202.044 160.857 169.259 1.00 44.23  ? 609  SER   B C     1 
ATOM   8972  O  O     . SER   B 1 609  ? 201.675 161.222 168.136 1.00 45.14  ? 609  SER   B O     1 
ATOM   8973  C  CB    . SER   B 1 609  ? 204.305 159.827 169.578 1.00 42.25  ? 609  SER   B CB    1 
ATOM   8974  O  OG    . SER   B 1 609  ? 203.554 158.686 169.952 1.00 47.39  ? 609  SER   B OG    1 
ATOM   8975  N  N     . ALA   B 1 610  ? 201.225 160.234 170.109 1.00 40.05  ? 610  ALA   B N     1 
ATOM   8976  C  CA    . ALA   B 1 610  ? 199.840 159.966 169.743 1.00 40.26  ? 610  ALA   B CA    1 
ATOM   8977  C  C     . ALA   B 1 610  ? 199.074 161.260 169.505 1.00 43.63  ? 610  ALA   B C     1 
ATOM   8978  O  O     . ALA   B 1 610  ? 198.279 161.356 168.563 1.00 47.70  ? 610  ALA   B O     1 
ATOM   8979  C  CB    . ALA   B 1 610  ? 199.163 159.132 170.829 1.00 36.57  ? 610  ALA   B CB    1 
ATOM   8980  N  N     . THR   B 1 611  ? 199.298 162.267 170.349 1.00 42.07  ? 611  THR   B N     1 
ATOM   8981  C  CA    . THR   B 1 611  ? 198.580 163.526 170.197 1.00 46.04  ? 611  THR   B CA    1 
ATOM   8982  C  C     . THR   B 1 611  ? 199.102 164.351 169.027 1.00 39.72  ? 611  THR   B C     1 
ATOM   8983  O  O     . THR   B 1 611  ? 198.349 165.144 168.451 1.00 40.36  ? 611  THR   B O     1 
ATOM   8984  C  CB    . THR   B 1 611  ? 198.664 164.341 171.489 1.00 46.22  ? 611  THR   B CB    1 
ATOM   8985  O  OG1   . THR   B 1 611  ? 197.683 165.384 171.464 1.00 50.48  ? 611  THR   B OG1   1 
ATOM   8986  C  CG2   . THR   B 1 611  ? 200.042 164.959 171.636 1.00 45.75  ? 611  THR   B CG2   1 
ATOM   8987  N  N     . LEU   B 1 612  ? 200.373 164.185 168.661 1.00 39.71  ? 612  LEU   B N     1 
ATOM   8988  C  CA    . LEU   B 1 612  ? 200.950 164.972 167.579 1.00 35.96  ? 612  LEU   B CA    1 
ATOM   8989  C  C     . LEU   B 1 612  ? 200.699 164.367 166.205 1.00 40.97  ? 612  LEU   B C     1 
ATOM   8990  O  O     . LEU   B 1 612  ? 200.517 165.112 165.234 1.00 49.12  ? 612  LEU   B O     1 
ATOM   8991  C  CB    . LEU   B 1 612  ? 202.458 165.134 167.795 1.00 35.54  ? 612  LEU   B CB    1 
ATOM   8992  C  CG    . LEU   B 1 612  ? 202.905 166.257 168.735 1.00 38.65  ? 612  LEU   B CG    1 
ATOM   8993  C  CD1   . LEU   B 1 612  ? 204.420 166.279 168.857 1.00 40.55  ? 612  LEU   B CD1   1 
ATOM   8994  C  CD2   . LEU   B 1 612  ? 202.383 167.608 168.274 1.00 39.72  ? 612  LEU   B CD2   1 
ATOM   8995  N  N     . SER   B 1 613  ? 200.682 163.036 166.097 1.00 41.61  ? 613  SER   B N     1 
ATOM   8996  C  CA    . SER   B 1 613  ? 200.440 162.406 164.804 1.00 39.43  ? 613  SER   B CA    1 
ATOM   8997  C  C     . SER   B 1 613  ? 199.044 162.726 164.288 1.00 41.42  ? 613  SER   B C     1 
ATOM   8998  O  O     . SER   B 1 613  ? 198.862 163.003 163.097 1.00 44.56  ? 613  SER   B O     1 
ATOM   8999  C  CB    . SER   B 1 613  ? 200.639 160.895 164.910 1.00 38.55  ? 613  SER   B CB    1 
ATOM   9000  O  OG    . SER   B 1 613  ? 200.046 160.387 166.091 1.00 47.69  ? 613  SER   B OG    1 
ATOM   9001  N  N     . SER   B 1 614  ? 198.042 162.687 165.169 1.00 36.60  ? 614  SER   B N     1 
ATOM   9002  C  CA    . SER   B 1 614  ? 196.681 163.007 164.752 1.00 37.63  ? 614  SER   B CA    1 
ATOM   9003  C  C     . SER   B 1 614  ? 196.567 164.460 164.307 1.00 42.24  ? 614  SER   B C     1 
ATOM   9004  O  O     . SER   B 1 614  ? 195.902 164.762 163.309 1.00 49.82  ? 614  SER   B O     1 
ATOM   9005  C  CB    . SER   B 1 614  ? 195.703 162.714 165.888 1.00 41.29  ? 614  SER   B CB    1 
ATOM   9006  O  OG    . SER   B 1 614  ? 196.038 161.504 166.543 1.00 41.03  ? 614  SER   B OG    1 
ATOM   9007  N  N     . ALA   B 1 615  ? 197.205 165.375 165.039 1.00 42.09  ? 615  ALA   B N     1 
ATOM   9008  C  CA    . ALA   B 1 615  ? 197.179 166.778 164.643 1.00 40.96  ? 615  ALA   B CA    1 
ATOM   9009  C  C     . ALA   B 1 615  ? 197.844 166.978 163.288 1.00 39.45  ? 615  ALA   B C     1 
ATOM   9010  O  O     . ALA   B 1 615  ? 197.328 167.713 162.437 1.00 45.49  ? 615  ALA   B O     1 
ATOM   9011  C  CB    . ALA   B 1 615  ? 197.860 167.639 165.706 1.00 39.43  ? 615  ALA   B CB    1 
ATOM   9012  N  N     . LEU   B 1 616  ? 198.991 166.332 163.068 1.00 36.94  ? 616  LEU   B N     1 
ATOM   9013  C  CA    . LEU   B 1 616  ? 199.662 166.442 161.777 1.00 35.56  ? 616  LEU   B CA    1 
ATOM   9014  C  C     . LEU   B 1 616  ? 198.787 165.893 160.658 1.00 43.66  ? 616  LEU   B C     1 
ATOM   9015  O  O     . LEU   B 1 616  ? 198.658 166.514 159.594 1.00 48.20  ? 616  LEU   B O     1 
ATOM   9016  C  CB    . LEU   B 1 616  ? 201.001 165.705 161.821 1.00 37.18  ? 616  LEU   B CB    1 
ATOM   9017  C  CG    . LEU   B 1 616  ? 202.138 166.243 160.952 1.00 46.94  ? 616  LEU   B CG    1 
ATOM   9018  C  CD1   . LEU   B 1 616  ? 202.095 167.760 160.882 1.00 45.02  ? 616  LEU   B CD1   1 
ATOM   9019  C  CD2   . LEU   B 1 616  ? 203.485 165.764 161.471 1.00 42.30  ? 616  LEU   B CD2   1 
ATOM   9020  N  N     . ALA   B 1 617  ? 198.167 164.734 160.886 1.00 43.86  ? 617  ALA   B N     1 
ATOM   9021  C  CA    . ALA   B 1 617  ? 197.316 164.136 159.865 1.00 41.27  ? 617  ALA   B CA    1 
ATOM   9022  C  C     . ALA   B 1 617  ? 196.138 165.038 159.530 1.00 41.13  ? 617  ALA   B C     1 
ATOM   9023  O  O     . ALA   B 1 617  ? 195.802 165.218 158.355 1.00 45.67  ? 617  ALA   B O     1 
ATOM   9024  C  CB    . ALA   B 1 617  ? 196.828 162.764 160.329 1.00 42.11  ? 617  ALA   B CB    1 
ATOM   9025  N  N     . SER   B 1 618  ? 195.489 165.608 160.548 1.00 34.02  ? 618  SER   B N     1 
ATOM   9026  C  CA    . SER   B 1 618  ? 194.355 166.491 160.293 1.00 35.09  ? 618  SER   B CA    1 
ATOM   9027  C  C     . SER   B 1 618  ? 194.791 167.752 159.556 1.00 40.71  ? 618  SER   B C     1 
ATOM   9028  O  O     . SER   B 1 618  ? 194.121 168.195 158.613 1.00 43.73  ? 618  SER   B O     1 
ATOM   9029  C  CB    . SER   B 1 618  ? 193.663 166.849 161.608 1.00 42.45  ? 618  SER   B CB    1 
ATOM   9030  O  OG    . SER   B 1 618  ? 193.093 165.704 162.217 1.00 51.43  ? 618  SER   B OG    1 
ATOM   9031  N  N     . LEU   B 1 619  ? 195.910 168.349 159.975 1.00 40.85  ? 619  LEU   B N     1 
ATOM   9032  C  CA    . LEU   B 1 619  ? 196.386 169.560 159.319 1.00 35.03  ? 619  LEU   B CA    1 
ATOM   9033  C  C     . LEU   B 1 619  ? 196.761 169.292 157.870 1.00 41.95  ? 619  LEU   B C     1 
ATOM   9034  O  O     . LEU   B 1 619  ? 196.646 170.185 157.024 1.00 55.11  ? 619  LEU   B O     1 
ATOM   9035  C  CB    . LEU   B 1 619  ? 197.578 170.134 160.086 1.00 38.43  ? 619  LEU   B CB    1 
ATOM   9036  C  CG    . LEU   B 1 619  ? 198.264 171.373 159.510 1.00 41.26  ? 619  LEU   B CG    1 
ATOM   9037  C  CD1   . LEU   B 1 619  ? 197.275 172.514 159.352 1.00 41.47  ? 619  LEU   B CD1   1 
ATOM   9038  C  CD2   . LEU   B 1 619  ? 199.427 171.788 160.393 1.00 38.25  ? 619  LEU   B CD2   1 
ATOM   9039  N  N     . VAL   B 1 620  ? 197.215 168.076 157.566 1.00 39.65  ? 620  VAL   B N     1 
ATOM   9040  C  CA    . VAL   B 1 620  ? 197.507 167.722 156.181 1.00 41.70  ? 620  VAL   B CA    1 
ATOM   9041  C  C     . VAL   B 1 620  ? 196.216 167.496 155.400 1.00 43.18  ? 620  VAL   B C     1 
ATOM   9042  O  O     . VAL   B 1 620  ? 196.064 167.970 154.268 1.00 47.66  ? 620  VAL   B O     1 
ATOM   9043  C  CB    . VAL   B 1 620  ? 198.424 166.487 156.124 1.00 38.08  ? 620  VAL   B CB    1 
ATOM   9044  C  CG1   . VAL   B 1 620  ? 198.112 165.651 154.894 1.00 36.07  ? 620  VAL   B CG1   1 
ATOM   9045  C  CG2   . VAL   B 1 620  ? 199.883 166.909 156.130 1.00 40.78  ? 620  VAL   B CG2   1 
ATOM   9046  N  N     . SER   B 1 621  ? 195.266 166.769 155.994 1.00 38.75  ? 621  SER   B N     1 
ATOM   9047  C  CA    . SER   B 1 621  ? 194.102 166.308 155.244 1.00 37.90  ? 621  SER   B CA    1 
ATOM   9048  C  C     . SER   B 1 621  ? 193.113 167.434 154.966 1.00 37.54  ? 621  SER   B C     1 
ATOM   9049  O  O     . SER   B 1 621  ? 192.559 167.516 153.864 1.00 47.25  ? 621  SER   B O     1 
ATOM   9050  C  CB    . SER   B 1 621  ? 193.413 165.170 155.996 1.00 35.45  ? 621  SER   B CB    1 
ATOM   9051  O  OG    . SER   B 1 621  ? 193.417 165.404 157.392 1.00 43.29  ? 621  SER   B OG    1 
ATOM   9052  N  N     . ALA   B 1 622  ? 192.867 168.306 155.946 1.00 38.63  ? 622  ALA   B N     1 
ATOM   9053  C  CA    . ALA   B 1 622  ? 191.836 169.327 155.763 1.00 38.21  ? 622  ALA   B CA    1 
ATOM   9054  C  C     . ALA   B 1 622  ? 192.081 170.191 154.535 1.00 41.41  ? 622  ALA   B C     1 
ATOM   9055  O  O     . ALA   B 1 622  ? 191.149 170.363 153.725 1.00 40.78  ? 622  ALA   B O     1 
ATOM   9056  C  CB    . ALA   B 1 622  ? 191.731 170.183 157.029 1.00 33.96  ? 622  ALA   B CB    1 
ATOM   9057  N  N     . PRO   B 1 623  ? 193.271 170.756 154.328 1.00 34.29  ? 623  PRO   B N     1 
ATOM   9058  C  CA    . PRO   B 1 623  ? 193.503 171.530 153.100 1.00 33.90  ? 623  PRO   B CA    1 
ATOM   9059  C  C     . PRO   B 1 623  ? 193.316 170.716 151.835 1.00 39.34  ? 623  PRO   B C     1 
ATOM   9060  O  O     . PRO   B 1 623  ? 192.884 171.271 150.821 1.00 43.89  ? 623  PRO   B O     1 
ATOM   9061  C  CB    . PRO   B 1 623  ? 194.952 172.014 153.254 1.00 35.99  ? 623  PRO   B CB    1 
ATOM   9062  C  CG    . PRO   B 1 623  ? 195.549 171.153 154.318 1.00 34.97  ? 623  PRO   B CG    1 
ATOM   9063  C  CD    . PRO   B 1 623  ? 194.431 170.786 155.231 1.00 36.51  ? 623  PRO   B CD    1 
ATOM   9064  N  N     . LYS   B 1 624  ? 193.628 169.419 151.855 1.00 40.35  ? 624  LYS   B N     1 
ATOM   9065  C  CA    . LYS   B 1 624  ? 193.416 168.590 150.673 1.00 33.70  ? 624  LYS   B CA    1 
ATOM   9066  C  C     . LYS   B 1 624  ? 191.947 168.592 150.265 1.00 33.75  ? 624  LYS   B C     1 
ATOM   9067  O  O     . LYS   B 1 624  ? 191.604 168.870 149.107 1.00 40.79  ? 624  LYS   B O     1 
ATOM   9068  C  CB    . LYS   B 1 624  ? 193.886 167.161 150.950 1.00 36.85  ? 624  LYS   B CB    1 
ATOM   9069  C  CG    . LYS   B 1 624  ? 195.388 167.005 151.111 1.00 34.92  ? 624  LYS   B CG    1 
ATOM   9070  C  CD    . LYS   B 1 624  ? 196.153 167.871 150.134 1.00 40.33  ? 624  LYS   B CD    1 
ATOM   9071  C  CE    . LYS   B 1 624  ? 197.648 167.769 150.379 1.00 41.80  ? 624  LYS   B CE    1 
ATOM   9072  N  NZ    . LYS   B 1 624  ? 198.162 166.401 150.111 1.00 37.22  ? 624  LYS   B NZ    1 
ATOM   9073  N  N     . ILE   B 1 625  ? 191.063 168.283 151.216 1.00 25.87  ? 625  ILE   B N     1 
ATOM   9074  C  CA    . ILE   B 1 625  ? 189.633 168.245 150.932 1.00 31.36  ? 625  ILE   B CA    1 
ATOM   9075  C  C     . ILE   B 1 625  ? 189.137 169.620 150.517 1.00 31.77  ? 625  ILE   B C     1 
ATOM   9076  O  O     . ILE   B 1 625  ? 188.332 169.752 149.586 1.00 40.08  ? 625  ILE   B O     1 
ATOM   9077  C  CB    . ILE   B 1 625  ? 188.859 167.717 152.152 1.00 30.46  ? 625  ILE   B CB    1 
ATOM   9078  C  CG1   . ILE   B 1 625  ? 189.386 166.344 152.567 1.00 33.44  ? 625  ILE   B CG1   1 
ATOM   9079  C  CG2   . ILE   B 1 625  ? 187.370 167.658 151.854 1.00 31.25  ? 625  ILE   B CG2   1 
ATOM   9080  C  CD1   . ILE   B 1 625  ? 188.845 165.871 153.891 1.00 35.53  ? 625  ILE   B CD1   1 
ATOM   9081  N  N     . PHE   B 1 626  ? 189.582 170.666 151.218 1.00 39.64  ? 626  PHE   B N     1 
ATOM   9082  C  CA    . PHE   B 1 626  ? 189.107 172.003 150.883 1.00 33.73  ? 626  PHE   B CA    1 
ATOM   9083  C  C     . PHE   B 1 626  ? 189.531 172.398 149.474 1.00 41.23  ? 626  PHE   B C     1 
ATOM   9084  O  O     . PHE   B 1 626  ? 188.736 172.963 148.716 1.00 49.08  ? 626  PHE   B O     1 
ATOM   9085  C  CB    . PHE   B 1 626  ? 189.609 173.018 151.907 1.00 41.32  ? 626  PHE   B CB    1 
ATOM   9086  C  CG    . PHE   B 1 626  ? 188.874 174.326 151.863 1.00 43.14  ? 626  PHE   B CG    1 
ATOM   9087  C  CD1   . PHE   B 1 626  ? 187.492 174.356 151.934 1.00 44.61  ? 626  PHE   B CD1   1 
ATOM   9088  C  CD2   . PHE   B 1 626  ? 189.559 175.522 151.752 1.00 41.13  ? 626  PHE   B CD2   1 
ATOM   9089  C  CE1   . PHE   B 1 626  ? 186.807 175.552 151.893 1.00 43.41  ? 626  PHE   B CE1   1 
ATOM   9090  C  CE2   . PHE   B 1 626  ? 188.877 176.722 151.712 1.00 46.25  ? 626  PHE   B CE2   1 
ATOM   9091  C  CZ    . PHE   B 1 626  ? 187.500 176.736 151.782 1.00 45.91  ? 626  PHE   B CZ    1 
ATOM   9092  N  N     . GLN   B 1 627  ? 190.774 172.093 149.095 1.00 37.93  ? 627  GLN   B N     1 
ATOM   9093  C  CA    . GLN   B 1 627  ? 191.244 172.422 147.755 1.00 30.89  ? 627  GLN   B CA    1 
ATOM   9094  C  C     . GLN   B 1 627  ? 190.495 171.627 146.695 1.00 35.96  ? 627  GLN   B C     1 
ATOM   9095  O  O     . GLN   B 1 627  ? 190.180 172.159 145.626 1.00 46.70  ? 627  GLN   B O     1 
ATOM   9096  C  CB    . GLN   B 1 627  ? 192.747 172.173 147.649 1.00 34.33  ? 627  GLN   B CB    1 
ATOM   9097  C  CG    . GLN   B 1 627  ? 193.243 171.968 146.231 1.00 36.83  ? 627  GLN   B CG    1 
ATOM   9098  C  CD    . GLN   B 1 627  ? 194.464 171.078 146.174 1.00 42.17  ? 627  GLN   B CD    1 
ATOM   9099  O  OE1   . GLN   B 1 627  ? 194.377 169.872 146.398 1.00 48.54  ? 627  GLN   B OE1   1 
ATOM   9100  N  NE2   . GLN   B 1 627  ? 195.615 171.670 145.879 1.00 40.14  ? 627  GLN   B NE2   1 
ATOM   9101  N  N     . ALA   B 1 628  ? 190.213 170.350 146.959 1.00 38.61  ? 628  ALA   B N     1 
ATOM   9102  C  CA    . ALA   B 1 628  ? 189.437 169.570 145.999 1.00 31.85  ? 628  ALA   B CA    1 
ATOM   9103  C  C     . ALA   B 1 628  ? 188.046 170.166 145.811 1.00 29.59  ? 628  ALA   B C     1 
ATOM   9104  O  O     . ALA   B 1 628  ? 187.608 170.423 144.680 1.00 34.15  ? 628  ALA   B O     1 
ATOM   9105  C  CB    . ALA   B 1 628  ? 189.347 168.115 146.456 1.00 35.18  ? 628  ALA   B CB    1 
ATOM   9106  N  N     . LEU   B 1 629  ? 187.344 170.416 146.918 1.00 38.09  ? 629  LEU   B N     1 
ATOM   9107  C  CA    . LEU   B 1 629  ? 186.004 170.983 146.840 1.00 34.52  ? 629  LEU   B CA    1 
ATOM   9108  C  C     . LEU   B 1 629  ? 186.011 172.392 146.268 1.00 39.20  ? 629  LEU   B C     1 
ATOM   9109  O  O     . LEU   B 1 629  ? 184.978 172.852 145.770 1.00 40.23  ? 629  LEU   B O     1 
ATOM   9110  C  CB    . LEU   B 1 629  ? 185.356 170.984 148.226 1.00 30.06  ? 629  LEU   B CB    1 
ATOM   9111  C  CG    . LEU   B 1 629  ? 184.176 171.933 148.439 1.00 37.13  ? 629  LEU   B CG    1 
ATOM   9112  C  CD1   . LEU   B 1 629  ? 182.865 171.164 148.407 1.00 40.89  ? 629  LEU   B CD1   1 
ATOM   9113  C  CD2   . LEU   B 1 629  ? 184.322 172.698 149.742 1.00 37.07  ? 629  LEU   B CD2   1 
ATOM   9114  N  N     . CYS   B 1 630  ? 187.149 173.083 146.323 1.00 45.97  ? 630  CYS   B N     1 
ATOM   9115  C  CA    . CYS   B 1 630  ? 187.231 174.431 145.779 1.00 44.21  ? 630  CYS   B CA    1 
ATOM   9116  C  C     . CYS   B 1 630  ? 187.512 174.401 144.282 1.00 44.39  ? 630  CYS   B C     1 
ATOM   9117  O  O     . CYS   B 1 630  ? 186.973 175.218 143.528 1.00 50.25  ? 630  CYS   B O     1 
ATOM   9118  C  CB    . CYS   B 1 630  ? 188.317 175.212 146.516 1.00 43.91  ? 630  CYS   B CB    1 
ATOM   9119  S  SG    . CYS   B 1 630  ? 187.744 176.021 148.024 1.00 55.64  ? 630  CYS   B SG    1 
ATOM   9120  N  N     . LYS   B 1 631  ? 188.357 173.468 143.840 1.00 39.50  ? 631  LYS   B N     1 
ATOM   9121  C  CA    . LYS   B 1 631  ? 188.549 173.258 142.411 1.00 39.80  ? 631  LYS   B CA    1 
ATOM   9122  C  C     . LYS   B 1 631  ? 187.267 172.775 141.753 1.00 41.61  ? 631  LYS   B C     1 
ATOM   9123  O  O     . LYS   B 1 631  ? 187.039 173.040 140.568 1.00 46.59  ? 631  LYS   B O     1 
ATOM   9124  C  CB    . LYS   B 1 631  ? 189.681 172.261 142.169 1.00 36.73  ? 631  LYS   B CB    1 
ATOM   9125  N  N     . ASP   B 1 632  ? 186.421 172.062 142.501 1.00 44.69  ? 632  ASP   B N     1 
ATOM   9126  C  CA    . ASP   B 1 632  ? 185.113 171.704 141.967 1.00 43.70  ? 632  ASP   B CA    1 
ATOM   9127  C  C     . ASP   B 1 632  ? 184.213 172.916 141.760 1.00 45.14  ? 632  ASP   B C     1 
ATOM   9128  O  O     . ASP   B 1 632  ? 183.204 172.802 141.057 1.00 47.97  ? 632  ASP   B O     1 
ATOM   9129  C  CB    . ASP   B 1 632  ? 184.424 170.698 142.890 1.00 48.85  ? 632  ASP   B CB    1 
ATOM   9130  C  CG    . ASP   B 1 632  ? 184.637 169.265 142.449 1.00 50.68  ? 632  ASP   B CG    1 
ATOM   9131  O  OD1   . ASP   B 1 632  ? 185.171 169.059 141.339 1.00 48.64  ? 632  ASP   B OD1   1 
ATOM   9132  O  OD2   . ASP   B 1 632  ? 184.274 168.345 143.211 1.00 56.75  ? 632  ASP   B OD2   1 
ATOM   9133  N  N     . ASN   B 1 633  ? 184.556 174.062 142.345 1.00 51.01  ? 633  ASN   B N     1 
ATOM   9134  C  CA    . ASN   B 1 633  ? 183.800 175.301 142.168 1.00 49.33  ? 633  ASN   B CA    1 
ATOM   9135  C  C     . ASN   B 1 633  ? 182.317 175.093 142.466 1.00 50.14  ? 633  ASN   B C     1 
ATOM   9136  O  O     . ASN   B 1 633  ? 181.446 175.346 141.632 1.00 52.87  ? 633  ASN   B O     1 
ATOM   9137  C  CB    . ASN   B 1 633  ? 184.003 175.865 140.761 1.00 47.74  ? 633  ASN   B CB    1 
ATOM   9138  N  N     . ILE   B 1 634  ? 182.032 174.629 143.681 1.00 51.95  ? 634  ILE   B N     1 
ATOM   9139  C  CA    . ILE   B 1 634  ? 180.656 174.406 144.111 1.00 48.20  ? 634  ILE   B CA    1 
ATOM   9140  C  C     . ILE   B 1 634  ? 180.199 175.610 144.922 1.00 51.70  ? 634  ILE   B C     1 
ATOM   9141  O  O     . ILE   B 1 634  ? 179.010 175.947 144.942 1.00 56.49  ? 634  ILE   B O     1 
ATOM   9142  C  CB    . ILE   B 1 634  ? 180.525 173.102 144.918 1.00 48.63  ? 634  ILE   B CB    1 
ATOM   9143  C  CG1   . ILE   B 1 634  ? 180.499 171.900 143.974 1.00 49.33  ? 634  ILE   B CG1   1 
ATOM   9144  C  CG2   . ILE   B 1 634  ? 179.269 173.129 145.768 1.00 50.16  ? 634  ILE   B CG2   1 
ATOM   9145  C  CD1   . ILE   B 1 634  ? 180.172 170.596 144.656 1.00 52.09  ? 634  ILE   B CD1   1 
ATOM   9146  N  N     . TYR   B 1 635  ? 181.141 176.263 145.595 1.00 56.42  ? 635  TYR   B N     1 
ATOM   9147  C  CA    . TYR   B 1 635  ? 180.907 177.554 146.242 1.00 54.02  ? 635  TYR   B CA    1 
ATOM   9148  C  C     . TYR   B 1 635  ? 181.805 178.582 145.570 1.00 56.06  ? 635  TYR   B C     1 
ATOM   9149  O  O     . TYR   B 1 635  ? 183.021 178.611 145.827 1.00 57.00  ? 635  TYR   B O     1 
ATOM   9150  C  CB    . TYR   B 1 635  ? 181.181 177.492 147.744 1.00 51.33  ? 635  TYR   B CB    1 
ATOM   9151  C  CG    . TYR   B 1 635  ? 180.561 176.303 148.444 1.00 50.12  ? 635  TYR   B CG    1 
ATOM   9152  C  CD1   . TYR   B 1 635  ? 181.237 175.094 148.536 1.00 52.01  ? 635  TYR   B CD1   1 
ATOM   9153  C  CD2   . TYR   B 1 635  ? 179.298 176.391 149.013 1.00 50.51  ? 635  TYR   B CD2   1 
ATOM   9154  C  CE1   . TYR   B 1 635  ? 180.672 174.008 149.177 1.00 54.97  ? 635  TYR   B CE1   1 
ATOM   9155  C  CE2   . TYR   B 1 635  ? 178.725 175.311 149.654 1.00 53.46  ? 635  TYR   B CE2   1 
ATOM   9156  C  CZ    . TYR   B 1 635  ? 179.416 174.122 149.734 1.00 54.70  ? 635  TYR   B CZ    1 
ATOM   9157  O  OH    . TYR   B 1 635  ? 178.851 173.042 150.371 1.00 50.23  ? 635  TYR   B OH    1 
ATOM   9158  N  N     . PRO   B 1 636  ? 181.261 179.439 144.703 1.00 55.01  ? 636  PRO   B N     1 
ATOM   9159  C  CA    . PRO   B 1 636  ? 182.128 180.329 143.913 1.00 51.07  ? 636  PRO   B CA    1 
ATOM   9160  C  C     . PRO   B 1 636  ? 183.024 181.217 144.756 1.00 56.64  ? 636  PRO   B C     1 
ATOM   9161  O  O     . PRO   B 1 636  ? 184.142 181.532 144.331 1.00 59.80  ? 636  PRO   B O     1 
ATOM   9162  C  CB    . PRO   B 1 636  ? 181.128 181.157 143.094 1.00 54.72  ? 636  PRO   B CB    1 
ATOM   9163  C  CG    . PRO   B 1 636  ? 179.866 180.360 143.089 1.00 55.94  ? 636  PRO   B CG    1 
ATOM   9164  C  CD    . PRO   B 1 636  ? 179.835 179.599 144.375 1.00 54.63  ? 636  PRO   B CD    1 
ATOM   9165  N  N     . ALA   B 1 637  ? 182.570 181.636 145.938 1.00 56.61  ? 637  ALA   B N     1 
ATOM   9166  C  CA    . ALA   B 1 637  ? 183.382 182.509 146.776 1.00 54.74  ? 637  ALA   B CA    1 
ATOM   9167  C  C     . ALA   B 1 637  ? 184.677 181.845 147.225 1.00 56.79  ? 637  ALA   B C     1 
ATOM   9168  O  O     . ALA   B 1 637  ? 185.612 182.547 147.626 1.00 61.46  ? 637  ALA   B O     1 
ATOM   9169  C  CB    . ALA   B 1 637  ? 182.579 182.962 147.995 1.00 55.89  ? 637  ALA   B CB    1 
ATOM   9170  N  N     . PHE   B 1 638  ? 184.758 180.518 147.167 1.00 61.09  ? 638  PHE   B N     1 
ATOM   9171  C  CA    . PHE   B 1 638  ? 185.905 179.782 147.680 1.00 59.89  ? 638  PHE   B CA    1 
ATOM   9172  C  C     . PHE   B 1 638  ? 186.889 179.371 146.593 1.00 57.58  ? 638  PHE   B C     1 
ATOM   9173  O  O     . PHE   B 1 638  ? 187.789 178.571 146.860 1.00 63.64  ? 638  PHE   B O     1 
ATOM   9174  C  CB    . PHE   B 1 638  ? 185.434 178.544 148.445 1.00 60.02  ? 638  PHE   B CB    1 
ATOM   9175  C  CG    . PHE   B 1 638  ? 184.766 178.857 149.750 1.00 58.75  ? 638  PHE   B CG    1 
ATOM   9176  C  CD1   . PHE   B 1 638  ? 184.006 177.902 150.401 1.00 58.14  ? 638  PHE   B CD1   1 
ATOM   9177  C  CD2   . PHE   B 1 638  ? 184.895 180.109 150.324 1.00 61.05  ? 638  PHE   B CD2   1 
ATOM   9178  C  CE1   . PHE   B 1 638  ? 183.390 178.190 151.602 1.00 59.05  ? 638  PHE   B CE1   1 
ATOM   9179  C  CE2   . PHE   B 1 638  ? 184.280 180.402 151.525 1.00 62.45  ? 638  PHE   B CE2   1 
ATOM   9180  C  CZ    . PHE   B 1 638  ? 183.527 179.441 152.164 1.00 61.54  ? 638  PHE   B CZ    1 
ATOM   9181  N  N     . GLN   B 1 639  ? 186.759 179.910 145.384 1.00 49.59  ? 639  GLN   B N     1 
ATOM   9182  C  CA    . GLN   B 1 639  ? 187.616 179.484 144.284 1.00 52.95  ? 639  GLN   B CA    1 
ATOM   9183  C  C     . GLN   B 1 639  ? 189.078 179.817 144.563 1.00 53.57  ? 639  GLN   B C     1 
ATOM   9184  O  O     . GLN   B 1 639  ? 189.976 179.296 143.894 1.00 51.41  ? 639  GLN   B O     1 
ATOM   9185  C  CB    . GLN   B 1 639  ? 187.165 180.133 142.974 1.00 50.72  ? 639  GLN   B CB    1 
ATOM   9186  N  N     . MET   B 1 640  ? 189.326 180.680 145.548 1.00 54.44  ? 640  MET   B N     1 
ATOM   9187  C  CA    . MET   B 1 640  ? 190.691 181.093 145.856 1.00 52.35  ? 640  MET   B CA    1 
ATOM   9188  C  C     . MET   B 1 640  ? 191.519 179.940 146.413 1.00 54.67  ? 640  MET   B C     1 
ATOM   9189  O  O     . MET   B 1 640  ? 192.653 179.716 145.978 1.00 57.04  ? 640  MET   B O     1 
ATOM   9190  C  CB    . MET   B 1 640  ? 190.672 182.263 146.840 1.00 53.39  ? 640  MET   B CB    1 
ATOM   9191  C  CG    . MET   B 1 640  ? 191.935 182.395 147.670 1.00 55.36  ? 640  MET   B CG    1 
ATOM   9192  S  SD    . MET   B 1 640  ? 191.946 183.910 148.644 1.00 67.53  ? 640  MET   B SD    1 
ATOM   9193  C  CE    . MET   B 1 640  ? 190.197 184.290 148.677 1.00 55.03  ? 640  MET   B CE    1 
ATOM   9194  N  N     . PHE   B 1 641  ? 190.971 179.197 147.375 1.00 53.92  ? 641  PHE   B N     1 
ATOM   9195  C  CA    . PHE   B 1 641  ? 191.703 178.111 148.029 1.00 51.58  ? 641  PHE   B CA    1 
ATOM   9196  C  C     . PHE   B 1 641  ? 191.699 176.850 147.162 1.00 54.39  ? 641  PHE   B C     1 
ATOM   9197  O  O     . PHE   B 1 641  ? 191.257 175.774 147.564 1.00 61.56  ? 641  PHE   B O     1 
ATOM   9198  C  CB    . PHE   B 1 641  ? 191.119 177.836 149.409 1.00 49.36  ? 641  PHE   B CB    1 
ATOM   9199  C  CG    . PHE   B 1 641  ? 191.007 179.057 150.275 1.00 50.68  ? 641  PHE   B CG    1 
ATOM   9200  C  CD1   . PHE   B 1 641  ? 192.116 179.556 150.937 1.00 52.13  ? 641  PHE   B CD1   1 
ATOM   9201  C  CD2   . PHE   B 1 641  ? 189.797 179.709 150.424 1.00 51.49  ? 641  PHE   B CD2   1 
ATOM   9202  C  CE1   . PHE   B 1 641  ? 192.017 180.678 151.735 1.00 52.15  ? 641  PHE   B CE1   1 
ATOM   9203  C  CE2   . PHE   B 1 641  ? 189.693 180.832 151.219 1.00 52.93  ? 641  PHE   B CE2   1 
ATOM   9204  C  CZ    . PHE   B 1 641  ? 190.804 181.317 151.875 1.00 51.80  ? 641  PHE   B CZ    1 
ATOM   9205  N  N     . ALA   B 1 642  ? 192.205 177.006 145.941 1.00 49.07  ? 642  ALA   B N     1 
ATOM   9206  C  CA    . ALA   B 1 642  ? 192.394 175.886 145.030 1.00 43.08  ? 642  ALA   B CA    1 
ATOM   9207  C  C     . ALA   B 1 642  ? 193.765 175.852 144.375 1.00 52.39  ? 642  ALA   B C     1 
ATOM   9208  O  O     . ALA   B 1 642  ? 194.138 174.805 143.832 1.00 55.04  ? 642  ALA   B O     1 
ATOM   9209  C  CB    . ALA   B 1 642  ? 191.322 175.895 143.931 1.00 46.31  ? 642  ALA   B CB    1 
ATOM   9210  N  N     . LYS   B 1 643  ? 194.522 176.945 144.405 1.00 59.57  ? 643  LYS   B N     1 
ATOM   9211  C  CA    . LYS   B 1 643  ? 195.829 176.974 143.767 1.00 57.83  ? 643  LYS   B CA    1 
ATOM   9212  C  C     . LYS   B 1 643  ? 196.783 175.999 144.445 1.00 60.09  ? 643  LYS   B C     1 
ATOM   9213  O  O     . LYS   B 1 643  ? 196.769 175.837 145.668 1.00 62.73  ? 643  LYS   B O     1 
ATOM   9214  C  CB    . LYS   B 1 643  ? 196.402 178.390 143.812 1.00 56.89  ? 643  LYS   B CB    1 
ATOM   9215  C  CG    . LYS   B 1 643  ? 197.371 178.706 142.689 1.00 62.58  ? 643  LYS   B CG    1 
ATOM   9216  C  CD    . LYS   B 1 643  ? 197.237 180.153 142.246 1.00 63.77  ? 643  LYS   B CD    1 
ATOM   9217  C  CE    . LYS   B 1 643  ? 198.050 180.423 140.992 1.00 62.70  ? 643  LYS   B CE    1 
ATOM   9218  N  NZ    . LYS   B 1 643  ? 198.976 181.575 141.169 1.00 62.39  ? 643  LYS   B NZ    1 
ATOM   9219  N  N     . GLY   B 1 644  ? 197.614 175.344 143.639 1.00 61.87  ? 644  GLY   B N     1 
ATOM   9220  C  CA    . GLY   B 1 644  ? 198.643 174.449 144.134 1.00 61.65  ? 644  GLY   B CA    1 
ATOM   9221  C  C     . GLY   B 1 644  ? 200.019 174.976 143.773 1.00 62.96  ? 644  GLY   B C     1 
ATOM   9222  O  O     . GLY   B 1 644  ? 200.195 175.631 142.744 1.00 68.83  ? 644  GLY   B O     1 
ATOM   9223  N  N     . TYR   B 1 645  ? 200.997 174.690 144.628 1.00 61.67  ? 645  TYR   B N     1 
ATOM   9224  C  CA    . TYR   B 1 645  ? 202.362 175.158 144.443 1.00 62.01  ? 645  TYR   B CA    1 
ATOM   9225  C  C     . TYR   B 1 645  ? 203.316 173.975 144.368 1.00 61.92  ? 645  TYR   B C     1 
ATOM   9226  O  O     . TYR   B 1 645  ? 203.039 172.896 144.901 1.00 63.56  ? 645  TYR   B O     1 
ATOM   9227  C  CB    . TYR   B 1 645  ? 202.809 176.096 145.580 1.00 64.16  ? 645  TYR   B CB    1 
ATOM   9228  C  CG    . TYR   B 1 645  ? 202.118 177.445 145.623 1.00 66.48  ? 645  TYR   B CG    1 
ATOM   9229  C  CD1   . TYR   B 1 645  ? 202.799 178.575 146.056 1.00 67.12  ? 645  TYR   B CD1   1 
ATOM   9230  C  CD2   . TYR   B 1 645  ? 200.790 177.588 145.249 1.00 64.49  ? 645  TYR   B CD2   1 
ATOM   9231  C  CE1   . TYR   B 1 645  ? 202.179 179.809 146.103 1.00 68.25  ? 645  TYR   B CE1   1 
ATOM   9232  C  CE2   . TYR   B 1 645  ? 200.162 178.817 145.294 1.00 67.94  ? 645  TYR   B CE2   1 
ATOM   9233  C  CZ    . TYR   B 1 645  ? 200.861 179.925 145.722 1.00 70.18  ? 645  TYR   B CZ    1 
ATOM   9234  O  OH    . TYR   B 1 645  ? 200.240 181.152 145.769 1.00 67.03  ? 645  TYR   B OH    1 
ATOM   9235  N  N     . GLY   B 1 646  ? 204.445 174.189 143.697 1.00 56.43  ? 646  GLY   B N     1 
ATOM   9236  C  CA    . GLY   B 1 646  ? 205.485 173.185 143.629 1.00 57.55  ? 646  GLY   B CA    1 
ATOM   9237  C  C     . GLY   B 1 646  ? 205.201 172.100 142.609 1.00 59.13  ? 646  GLY   B C     1 
ATOM   9238  O  O     . GLY   B 1 646  ? 204.202 172.109 141.888 1.00 55.88  ? 646  GLY   B O     1 
ATOM   9239  N  N     . LYS   B 1 647  ? 206.123 171.136 142.556 1.00 64.47  ? 647  LYS   B N     1 
ATOM   9240  C  CA    . LYS   B 1 647  ? 205.973 170.021 141.628 1.00 64.68  ? 647  LYS   B CA    1 
ATOM   9241  C  C     . LYS   B 1 647  ? 204.696 169.241 141.910 1.00 62.95  ? 647  LYS   B C     1 
ATOM   9242  O  O     . LYS   B 1 647  ? 203.961 168.882 140.983 1.00 61.83  ? 647  LYS   B O     1 
ATOM   9243  C  CB    . LYS   B 1 647  ? 207.193 169.104 141.709 1.00 62.19  ? 647  LYS   B CB    1 
ATOM   9244  N  N     . ASN   B 1 648  ? 204.416 168.970 143.180 1.00 61.76  ? 648  ASN   B N     1 
ATOM   9245  C  CA    . ASN   B 1 648  ? 203.168 168.344 143.595 1.00 62.24  ? 648  ASN   B CA    1 
ATOM   9246  C  C     . ASN   B 1 648  ? 202.246 169.429 144.135 1.00 61.66  ? 648  ASN   B C     1 
ATOM   9247  O  O     . ASN   B 1 648  ? 202.591 170.111 145.106 1.00 66.18  ? 648  ASN   B O     1 
ATOM   9248  C  CB    . ASN   B 1 648  ? 203.414 167.269 144.652 1.00 58.14  ? 648  ASN   B CB    1 
ATOM   9249  N  N     . ASN   B 1 649  ? 201.085 169.589 143.505 1.00 52.49  ? 649  ASN   B N     1 
ATOM   9250  C  CA    . ASN   B 1 649  ? 200.147 170.631 143.904 1.00 53.65  ? 649  ASN   B CA    1 
ATOM   9251  C  C     . ASN   B 1 649  ? 199.886 170.570 145.400 1.00 59.25  ? 649  ASN   B C     1 
ATOM   9252  O  O     . ASN   B 1 649  ? 199.339 169.587 145.907 1.00 62.18  ? 649  ASN   B O     1 
ATOM   9253  C  CB    . ASN   B 1 649  ? 198.839 170.479 143.127 1.00 52.73  ? 649  ASN   B CB    1 
ATOM   9254  N  N     . GLU   B 1 650  ? 200.278 171.628 146.105 1.00 57.93  ? 650  GLU   B N     1 
ATOM   9255  C  CA    . GLU   B 1 650  ? 200.150 171.702 147.554 1.00 51.92  ? 650  GLU   B CA    1 
ATOM   9256  C  C     . GLU   B 1 650  ? 199.288 172.902 147.916 1.00 50.70  ? 650  GLU   B C     1 
ATOM   9257  O  O     . GLU   B 1 650  ? 199.659 174.044 147.594 1.00 56.93  ? 650  GLU   B O     1 
ATOM   9258  C  CB    . GLU   B 1 650  ? 201.524 171.811 148.216 1.00 51.46  ? 650  GLU   B CB    1 
ATOM   9259  C  CG    . GLU   B 1 650  ? 202.261 170.488 148.352 1.00 55.36  ? 650  GLU   B CG    1 
ATOM   9260  C  CD    . GLU   B 1 650  ? 201.402 169.394 148.951 1.00 59.82  ? 650  GLU   B CD    1 
ATOM   9261  O  OE1   . GLU   B 1 650  ? 200.444 169.721 149.680 1.00 60.41  ? 650  GLU   B OE1   1 
ATOM   9262  O  OE2   . GLU   B 1 650  ? 201.688 168.205 148.693 1.00 59.58  ? 650  GLU   B OE2   1 
ATOM   9263  N  N     . PRO   B 1 651  ? 198.151 172.711 148.581 1.00 41.98  ? 651  PRO   B N     1 
ATOM   9264  C  CA    . PRO   B 1 651  ? 197.277 173.851 148.886 1.00 45.19  ? 651  PRO   B CA    1 
ATOM   9265  C  C     . PRO   B 1 651  ? 197.848 174.745 149.973 1.00 49.63  ? 651  PRO   B C     1 
ATOM   9266  O  O     . PRO   B 1 651  ? 197.457 174.645 151.140 1.00 55.51  ? 651  PRO   B O     1 
ATOM   9267  C  CB    . PRO   B 1 651  ? 195.976 173.178 149.335 1.00 46.79  ? 651  PRO   B CB    1 
ATOM   9268  C  CG    . PRO   B 1 651  ? 196.415 171.871 149.895 1.00 48.57  ? 651  PRO   B CG    1 
ATOM   9269  C  CD    . PRO   B 1 651  ? 197.607 171.439 149.085 1.00 44.32  ? 651  PRO   B CD    1 
ATOM   9270  N  N     . LEU   B 1 652  ? 198.778 175.625 149.598 1.00 44.50  ? 652  LEU   B N     1 
ATOM   9271  C  CA    . LEU   B 1 652  ? 199.405 176.499 150.584 1.00 41.16  ? 652  LEU   B CA    1 
ATOM   9272  C  C     . LEU   B 1 652  ? 198.378 177.400 151.259 1.00 50.04  ? 652  LEU   B C     1 
ATOM   9273  O  O     . LEU   B 1 652  ? 198.404 177.575 152.484 1.00 57.07  ? 652  LEU   B O     1 
ATOM   9274  C  CB    . LEU   B 1 652  ? 200.502 177.330 149.922 1.00 48.39  ? 652  LEU   B CB    1 
ATOM   9275  C  CG    . LEU   B 1 652  ? 201.907 176.728 149.949 1.00 51.70  ? 652  LEU   B CG    1 
ATOM   9276  C  CD1   . LEU   B 1 652  ? 202.535 176.927 151.313 1.00 48.80  ? 652  LEU   B CD1   1 
ATOM   9277  C  CD2   . LEU   B 1 652  ? 201.870 175.253 149.587 1.00 49.09  ? 652  LEU   B CD2   1 
ATOM   9278  N  N     . ARG   B 1 653  ? 197.466 177.985 150.479 1.00 46.40  ? 653  ARG   B N     1 
ATOM   9279  C  CA    . ARG   B 1 653  ? 196.421 178.811 151.075 1.00 48.80  ? 653  ARG   B CA    1 
ATOM   9280  C  C     . ARG   B 1 653  ? 195.549 177.993 152.017 1.00 51.58  ? 653  ARG   B C     1 
ATOM   9281  O  O     . ARG   B 1 653  ? 195.160 178.472 153.090 1.00 55.11  ? 653  ARG   B O     1 
ATOM   9282  C  CB    . ARG   B 1 653  ? 195.567 179.462 149.986 1.00 48.49  ? 653  ARG   B CB    1 
ATOM   9283  C  CG    . ARG   B 1 653  ? 196.350 180.049 148.825 1.00 47.76  ? 653  ARG   B CG    1 
ATOM   9284  C  CD    . ARG   B 1 653  ? 195.722 181.358 148.367 1.00 49.88  ? 653  ARG   B CD    1 
ATOM   9285  N  NE    . ARG   B 1 653  ? 195.732 181.507 146.916 1.00 50.64  ? 653  ARG   B NE    1 
ATOM   9286  C  CZ    . ARG   B 1 653  ? 196.823 181.699 146.189 1.00 54.31  ? 653  ARG   B CZ    1 
ATOM   9287  N  NH1   . ARG   B 1 653  ? 198.021 181.774 146.745 1.00 51.82  ? 653  ARG   B NH1   1 
ATOM   9288  N  NH2   . ARG   B 1 653  ? 196.710 181.819 144.869 1.00 54.00  ? 653  ARG   B NH2   1 
ATOM   9289  N  N     . GLY   B 1 654  ? 195.223 176.760 151.631 1.00 50.82  ? 654  GLY   B N     1 
ATOM   9290  C  CA    . GLY   B 1 654  ? 194.471 175.896 152.524 1.00 48.72  ? 654  GLY   B CA    1 
ATOM   9291  C  C     . GLY   B 1 654  ? 195.222 175.598 153.806 1.00 50.88  ? 654  GLY   B C     1 
ATOM   9292  O  O     . GLY   B 1 654  ? 194.634 175.573 154.890 1.00 55.29  ? 654  GLY   B O     1 
ATOM   9293  N  N     . TYR   B 1 655  ? 196.532 175.369 153.701 1.00 46.55  ? 655  TYR   B N     1 
ATOM   9294  C  CA    . TYR   B 1 655  ? 197.342 175.146 154.893 1.00 42.54  ? 655  TYR   B CA    1 
ATOM   9295  C  C     . TYR   B 1 655  ? 197.296 176.360 155.812 1.00 49.72  ? 655  TYR   B C     1 
ATOM   9296  O  O     . TYR   B 1 655  ? 197.134 176.228 157.030 1.00 56.24  ? 655  TYR   B O     1 
ATOM   9297  C  CB    . TYR   B 1 655  ? 198.784 174.830 154.495 1.00 44.13  ? 655  TYR   B CB    1 
ATOM   9298  C  CG    . TYR   B 1 655  ? 199.024 173.386 154.120 1.00 46.42  ? 655  TYR   B CG    1 
ATOM   9299  C  CD1   . TYR   B 1 655  ? 198.895 172.372 155.059 1.00 47.62  ? 655  TYR   B CD1   1 
ATOM   9300  C  CD2   . TYR   B 1 655  ? 199.385 173.037 152.827 1.00 44.56  ? 655  TYR   B CD2   1 
ATOM   9301  C  CE1   . TYR   B 1 655  ? 199.115 171.053 154.719 1.00 44.64  ? 655  TYR   B CE1   1 
ATOM   9302  C  CE2   . TYR   B 1 655  ? 199.607 171.721 152.478 1.00 48.15  ? 655  TYR   B CE2   1 
ATOM   9303  C  CZ    . TYR   B 1 655  ? 199.471 170.733 153.428 1.00 51.45  ? 655  TYR   B CZ    1 
ATOM   9304  O  OH    . TYR   B 1 655  ? 199.691 169.420 153.084 1.00 53.87  ? 655  TYR   B OH    1 
ATOM   9305  N  N     . ILE   B 1 656  ? 197.430 177.557 155.239 1.00 46.15  ? 656  ILE   B N     1 
ATOM   9306  C  CA    . ILE   B 1 656  ? 197.408 178.773 156.047 1.00 44.71  ? 656  ILE   B CA    1 
ATOM   9307  C  C     . ILE   B 1 656  ? 196.053 178.944 156.723 1.00 47.62  ? 656  ILE   B C     1 
ATOM   9308  O  O     . ILE   B 1 656  ? 195.971 179.303 157.904 1.00 55.08  ? 656  ILE   B O     1 
ATOM   9309  C  CB    . ILE   B 1 656  ? 197.767 179.996 155.183 1.00 44.86  ? 656  ILE   B CB    1 
ATOM   9310  C  CG1   . ILE   B 1 656  ? 199.262 180.299 155.284 1.00 46.82  ? 656  ILE   B CG1   1 
ATOM   9311  C  CG2   . ILE   B 1 656  ? 196.946 181.202 155.602 1.00 46.07  ? 656  ILE   B CG2   1 
ATOM   9312  C  CD1   . ILE   B 1 656  ? 200.143 179.092 155.079 1.00 44.97  ? 656  ILE   B CD1   1 
ATOM   9313  N  N     . LEU   B 1 657  ? 194.968 178.708 155.982 1.00 41.48  ? 657  LEU   B N     1 
ATOM   9314  C  CA    . LEU   B 1 657  ? 193.634 178.860 156.555 1.00 41.23  ? 657  LEU   B CA    1 
ATOM   9315  C  C     . LEU   B 1 657  ? 193.394 177.854 157.676 1.00 48.78  ? 657  LEU   B C     1 
ATOM   9316  O  O     . LEU   B 1 657  ? 192.829 178.202 158.722 1.00 53.47  ? 657  LEU   B O     1 
ATOM   9317  C  CB    . LEU   B 1 657  ? 192.578 178.714 155.461 1.00 43.18  ? 657  LEU   B CB    1 
ATOM   9318  C  CG    . LEU   B 1 657  ? 191.115 178.785 155.894 1.00 41.50  ? 657  LEU   B CG    1 
ATOM   9319  C  CD1   . LEU   B 1 657  ? 190.646 180.229 155.950 1.00 46.65  ? 657  LEU   B CD1   1 
ATOM   9320  C  CD2   . LEU   B 1 657  ? 190.242 177.972 154.953 1.00 42.63  ? 657  LEU   B CD2   1 
ATOM   9321  N  N     . THR   B 1 658  ? 193.814 176.602 157.477 1.00 52.25  ? 658  THR   B N     1 
ATOM   9322  C  CA    . THR   B 1 658  ? 193.672 175.603 158.530 1.00 53.70  ? 658  THR   B CA    1 
ATOM   9323  C  C     . THR   B 1 658  ? 194.493 175.982 159.755 1.00 50.93  ? 658  THR   B C     1 
ATOM   9324  O  O     . THR   B 1 658  ? 194.038 175.819 160.893 1.00 51.96  ? 658  THR   B O     1 
ATOM   9325  C  CB    . THR   B 1 658  ? 194.085 174.226 158.010 1.00 50.04  ? 658  THR   B CB    1 
ATOM   9326  O  OG1   . THR   B 1 658  ? 193.442 173.979 156.754 1.00 50.44  ? 658  THR   B OG1   1 
ATOM   9327  C  CG2   . THR   B 1 658  ? 193.683 173.141 158.995 1.00 48.47  ? 658  THR   B CG2   1 
ATOM   9328  N  N     . PHE   B 1 659  ? 195.707 176.494 159.540 1.00 49.54  ? 659  PHE   B N     1 
ATOM   9329  C  CA    . PHE   B 1 659  ? 196.524 176.943 160.660 1.00 50.12  ? 659  PHE   B CA    1 
ATOM   9330  C  C     . PHE   B 1 659  ? 195.840 178.070 161.420 1.00 53.58  ? 659  PHE   B C     1 
ATOM   9331  O  O     . PHE   B 1 659  ? 195.844 178.085 162.654 1.00 57.36  ? 659  PHE   B O     1 
ATOM   9332  C  CB    . PHE   B 1 659  ? 197.898 177.391 160.162 1.00 51.86  ? 659  PHE   B CB    1 
ATOM   9333  C  CG    . PHE   B 1 659  ? 198.554 178.424 161.036 1.00 53.46  ? 659  PHE   B CG    1 
ATOM   9334  C  CD1   . PHE   B 1 659  ? 199.249 178.050 162.173 1.00 56.42  ? 659  PHE   B CD1   1 
ATOM   9335  C  CD2   . PHE   B 1 659  ? 198.475 179.769 160.720 1.00 54.16  ? 659  PHE   B CD2   1 
ATOM   9336  C  CE1   . PHE   B 1 659  ? 199.853 178.998 162.976 1.00 56.23  ? 659  PHE   B CE1   1 
ATOM   9337  C  CE2   . PHE   B 1 659  ? 199.077 180.721 161.521 1.00 57.07  ? 659  PHE   B CE2   1 
ATOM   9338  C  CZ    . PHE   B 1 659  ? 199.766 180.334 162.649 1.00 57.55  ? 659  PHE   B CZ    1 
ATOM   9339  N  N     . LEU   B 1 660  ? 195.252 179.027 160.700 1.00 52.10  ? 660  LEU   B N     1 
ATOM   9340  C  CA    . LEU   B 1 660  ? 194.572 180.134 161.366 1.00 50.01  ? 660  LEU   B CA    1 
ATOM   9341  C  C     . LEU   B 1 660  ? 193.380 179.642 162.178 1.00 51.32  ? 660  LEU   B C     1 
ATOM   9342  O  O     . LEU   B 1 660  ? 193.175 180.073 163.320 1.00 57.96  ? 660  LEU   B O     1 
ATOM   9343  C  CB    . LEU   B 1 660  ? 194.129 181.172 160.336 1.00 45.69  ? 660  LEU   B CB    1 
ATOM   9344  C  CG    . LEU   B 1 660  ? 195.223 182.110 159.826 1.00 52.54  ? 660  LEU   B CG    1 
ATOM   9345  C  CD1   . LEU   B 1 660  ? 194.635 183.184 158.928 1.00 53.47  ? 660  LEU   B CD1   1 
ATOM   9346  C  CD2   . LEU   B 1 660  ? 195.975 182.735 160.988 1.00 52.66  ? 660  LEU   B CD2   1 
ATOM   9347  N  N     . ILE   B 1 661  ? 192.581 178.739 161.606 1.00 47.78  ? 661  ILE   B N     1 
ATOM   9348  C  CA    . ILE   B 1 661  ? 191.421 178.222 162.328 1.00 48.64  ? 661  ILE   B CA    1 
ATOM   9349  C  C     . ILE   B 1 661  ? 191.861 177.473 163.579 1.00 51.87  ? 661  ILE   B C     1 
ATOM   9350  O  O     . ILE   B 1 661  ? 191.286 177.645 164.665 1.00 53.75  ? 661  ILE   B O     1 
ATOM   9351  C  CB    . ILE   B 1 661  ? 190.569 177.333 161.404 1.00 52.95  ? 661  ILE   B CB    1 
ATOM   9352  C  CG1   . ILE   B 1 661  ? 189.437 178.145 160.774 1.00 52.21  ? 661  ILE   B CG1   1 
ATOM   9353  C  CG2   . ILE   B 1 661  ? 190.014 176.145 162.170 1.00 49.45  ? 661  ILE   B CG2   1 
ATOM   9354  C  CD1   . ILE   B 1 661  ? 189.914 179.272 159.890 1.00 52.62  ? 661  ILE   B CD1   1 
ATOM   9355  N  N     . ALA   B 1 662  ? 192.885 176.626 163.448 1.00 54.94  ? 662  ALA   B N     1 
ATOM   9356  C  CA    . ALA   B 1 662  ? 193.382 175.884 164.600 1.00 49.33  ? 662  ALA   B CA    1 
ATOM   9357  C  C     . ALA   B 1 662  ? 193.935 176.825 165.662 1.00 52.98  ? 662  ALA   B C     1 
ATOM   9358  O  O     . ALA   B 1 662  ? 193.718 176.615 166.859 1.00 56.73  ? 662  ALA   B O     1 
ATOM   9359  C  CB    . ALA   B 1 662  ? 194.448 174.882 164.159 1.00 47.46  ? 662  ALA   B CB    1 
ATOM   9360  N  N     . LEU   B 1 663  ? 194.651 177.869 165.243 1.00 54.13  ? 663  LEU   B N     1 
ATOM   9361  C  CA    . LEU   B 1 663  ? 195.194 178.825 166.200 1.00 52.99  ? 663  LEU   B CA    1 
ATOM   9362  C  C     . LEU   B 1 663  ? 194.082 179.552 166.943 1.00 52.32  ? 663  LEU   B C     1 
ATOM   9363  O  O     . LEU   B 1 663  ? 194.187 179.787 168.150 1.00 56.06  ? 663  LEU   B O     1 
ATOM   9364  C  CB    . LEU   B 1 663  ? 196.109 179.820 165.487 1.00 55.43  ? 663  LEU   B CB    1 
ATOM   9365  C  CG    . LEU   B 1 663  ? 196.449 181.106 166.241 1.00 53.03  ? 663  LEU   B CG    1 
ATOM   9366  C  CD1   . LEU   B 1 663  ? 197.873 181.537 165.945 1.00 54.85  ? 663  LEU   B CD1   1 
ATOM   9367  C  CD2   . LEU   B 1 663  ? 195.474 182.211 165.875 1.00 53.01  ? 663  LEU   B CD2   1 
ATOM   9368  N  N     . GLY   B 1 664  ? 193.012 179.925 166.240 1.00 44.95  ? 664  GLY   B N     1 
ATOM   9369  C  CA    . GLY   B 1 664  ? 191.890 180.555 166.922 1.00 46.41  ? 664  GLY   B CA    1 
ATOM   9370  C  C     . GLY   B 1 664  ? 191.235 179.633 167.933 1.00 49.81  ? 664  GLY   B C     1 
ATOM   9371  O  O     . GLY   B 1 664  ? 190.993 180.015 169.086 1.00 52.88  ? 664  GLY   B O     1 
ATOM   9372  N  N     . PHE   B 1 665  ? 190.954 178.395 167.522 1.00 49.55  ? 665  PHE   B N     1 
ATOM   9373  C  CA    . PHE   B 1 665  ? 190.330 177.451 168.442 1.00 47.67  ? 665  PHE   B CA    1 
ATOM   9374  C  C     . PHE   B 1 665  ? 191.252 177.071 169.593 1.00 50.65  ? 665  PHE   B C     1 
ATOM   9375  O  O     . PHE   B 1 665  ? 190.767 176.628 170.639 1.00 49.76  ? 665  PHE   B O     1 
ATOM   9376  C  CB    . PHE   B 1 665  ? 189.873 176.201 167.691 1.00 46.29  ? 665  PHE   B CB    1 
ATOM   9377  C  CG    . PHE   B 1 665  ? 188.445 176.263 167.232 1.00 45.36  ? 665  PHE   B CG    1 
ATOM   9378  C  CD1   . PHE   B 1 665  ? 187.408 176.077 168.129 1.00 48.36  ? 665  PHE   B CD1   1 
ATOM   9379  C  CD2   . PHE   B 1 665  ? 188.138 176.519 165.907 1.00 46.27  ? 665  PHE   B CD2   1 
ATOM   9380  C  CE1   . PHE   B 1 665  ? 186.093 176.135 167.714 1.00 47.57  ? 665  PHE   B CE1   1 
ATOM   9381  C  CE2   . PHE   B 1 665  ? 186.823 176.580 165.486 1.00 49.93  ? 665  PHE   B CE2   1 
ATOM   9382  C  CZ    . PHE   B 1 665  ? 185.800 176.388 166.391 1.00 49.96  ? 665  PHE   B CZ    1 
ATOM   9383  N  N     . ILE   B 1 666  ? 192.564 177.230 169.422 1.00 50.32  ? 666  ILE   B N     1 
ATOM   9384  C  CA    . ILE   B 1 666  ? 193.492 177.008 170.524 1.00 46.66  ? 666  ILE   B CA    1 
ATOM   9385  C  C     . ILE   B 1 666  ? 193.521 178.220 171.444 1.00 49.98  ? 666  ILE   B C     1 
ATOM   9386  O  O     . ILE   B 1 666  ? 193.645 178.085 172.667 1.00 54.99  ? 666  ILE   B O     1 
ATOM   9387  C  CB    . ILE   B 1 666  ? 194.888 176.678 169.971 1.00 46.53  ? 666  ILE   B CB    1 
ATOM   9388  C  CG1   . ILE   B 1 666  ? 194.998 175.185 169.662 1.00 47.64  ? 666  ILE   B CG1   1 
ATOM   9389  C  CG2   . ILE   B 1 666  ? 195.963 177.099 170.957 1.00 44.25  ? 666  ILE   B CG2   1 
ATOM   9390  C  CD1   . ILE   B 1 666  ? 195.984 174.866 168.563 1.00 45.34  ? 666  ILE   B CD1   1 
ATOM   9391  N  N     . LEU   B 1 667  ? 193.403 179.419 170.872 1.00 52.37  ? 667  LEU   B N     1 
ATOM   9392  C  CA    . LEU   B 1 667  ? 193.306 180.623 171.686 1.00 46.92  ? 667  LEU   B CA    1 
ATOM   9393  C  C     . LEU   B 1 667  ? 192.072 180.572 172.573 1.00 49.82  ? 667  LEU   B C     1 
ATOM   9394  O  O     . LEU   B 1 667  ? 192.093 181.065 173.707 1.00 52.97  ? 667  LEU   B O     1 
ATOM   9395  C  CB    . LEU   B 1 667  ? 193.282 181.863 170.792 1.00 47.01  ? 667  LEU   B CB    1 
ATOM   9396  C  CG    . LEU   B 1 667  ? 194.604 182.239 170.120 1.00 50.23  ? 667  LEU   B CG    1 
ATOM   9397  C  CD1   . LEU   B 1 667  ? 194.563 183.667 169.599 1.00 49.13  ? 667  LEU   B CD1   1 
ATOM   9398  C  CD2   . LEU   B 1 667  ? 195.764 182.052 171.083 1.00 45.61  ? 667  LEU   B CD2   1 
ATOM   9399  N  N     . ILE   B 1 668  ? 190.985 179.978 172.077 1.00 51.73  ? 668  ILE   B N     1 
ATOM   9400  C  CA    . ILE   B 1 668  ? 189.849 179.704 172.956 1.00 47.67  ? 668  ILE   B CA    1 
ATOM   9401  C  C     . ILE   B 1 668  ? 190.291 178.811 174.111 1.00 51.17  ? 668  ILE   B C     1 
ATOM   9402  O  O     . ILE   B 1 668  ? 189.983 179.075 175.279 1.00 59.44  ? 668  ILE   B O     1 
ATOM   9403  C  CB    . ILE   B 1 668  ? 188.688 179.076 172.165 1.00 51.27  ? 668  ILE   B CB    1 
ATOM   9404  C  CG1   . ILE   B 1 668  ? 187.936 180.155 171.384 1.00 53.04  ? 668  ILE   B CG1   1 
ATOM   9405  C  CG2   . ILE   B 1 668  ? 187.747 178.331 173.100 1.00 48.95  ? 668  ILE   B CG2   1 
ATOM   9406  C  CD1   . ILE   B 1 668  ? 186.581 179.713 170.877 1.00 54.15  ? 668  ILE   B CD1   1 
ATOM   9407  N  N     . ALA   B 1 669  ? 191.016 177.738 173.797 1.00 54.52  ? 669  ALA   B N     1 
ATOM   9408  C  CA    . ALA   B 1 669  ? 191.751 176.952 174.783 1.00 50.68  ? 669  ALA   B CA    1 
ATOM   9409  C  C     . ALA   B 1 669  ? 190.850 176.090 175.660 1.00 54.01  ? 669  ALA   B C     1 
ATOM   9410  O  O     . ALA   B 1 669  ? 191.344 175.299 176.469 1.00 59.78  ? 669  ALA   B O     1 
ATOM   9411  C  CB    . ALA   B 1 669  ? 192.599 177.873 175.663 1.00 51.00  ? 669  ALA   B CB    1 
ATOM   9412  N  N     . GLU   B 1 670  ? 189.535 176.224 175.510 1.00 58.39  ? 670  GLU   B N     1 
ATOM   9413  C  CA    . GLU   B 1 670  ? 188.567 175.420 176.254 1.00 59.60  ? 670  GLU   B CA    1 
ATOM   9414  C  C     . GLU   B 1 670  ? 187.675 174.719 175.234 1.00 64.85  ? 670  GLU   B C     1 
ATOM   9415  O  O     . GLU   B 1 670  ? 186.605 175.220 174.881 1.00 66.33  ? 670  GLU   B O     1 
ATOM   9416  C  CB    . GLU   B 1 670  ? 187.757 176.282 177.218 1.00 59.82  ? 670  GLU   B CB    1 
ATOM   9417  N  N     . LEU   B 1 671  ? 188.117 173.553 174.769 1.00 67.33  ? 671  LEU   B N     1 
ATOM   9418  C  CA    . LEU   B 1 671  ? 187.453 172.831 173.693 1.00 65.82  ? 671  LEU   B CA    1 
ATOM   9419  C  C     . LEU   B 1 671  ? 186.653 171.630 174.180 1.00 67.33  ? 671  LEU   B C     1 
ATOM   9420  O  O     . LEU   B 1 671  ? 186.164 170.852 173.356 1.00 72.27  ? 671  LEU   B O     1 
ATOM   9421  C  CB    . LEU   B 1 671  ? 188.484 172.383 172.656 1.00 62.95  ? 671  LEU   B CB    1 
ATOM   9422  C  CG    . LEU   B 1 671  ? 189.368 173.491 172.081 1.00 60.72  ? 671  LEU   B CG    1 
ATOM   9423  C  CD1   . LEU   B 1 671  ? 190.097 173.009 170.840 1.00 64.16  ? 671  LEU   B CD1   1 
ATOM   9424  C  CD2   . LEU   B 1 671  ? 188.541 174.726 171.772 1.00 59.25  ? 671  LEU   B CD2   1 
ATOM   9425  N  N     . ASN   B 1 672  ? 186.505 171.458 175.495 1.00 66.86  ? 672  ASN   B N     1 
ATOM   9426  C  CA    . ASN   B 1 672  ? 185.813 170.277 176.002 1.00 66.77  ? 672  ASN   B CA    1 
ATOM   9427  C  C     . ASN   B 1 672  ? 184.363 170.228 175.538 1.00 67.59  ? 672  ASN   B C     1 
ATOM   9428  O  O     . ASN   B 1 672  ? 183.786 169.140 175.422 1.00 70.89  ? 672  ASN   B O     1 
ATOM   9429  C  CB    . ASN   B 1 672  ? 185.883 170.238 177.528 1.00 68.52  ? 672  ASN   B CB    1 
ATOM   9430  C  CG    . ASN   B 1 672  ? 186.484 168.948 178.046 1.00 72.52  ? 672  ASN   B CG    1 
ATOM   9431  O  OD1   . ASN   B 1 672  ? 187.498 168.475 177.533 1.00 71.00  ? 672  ASN   B OD1   1 
ATOM   9432  N  ND2   . ASN   B 1 672  ? 185.858 168.368 179.063 1.00 72.19  ? 672  ASN   B ND2   1 
ATOM   9433  N  N     . VAL   B 1 673  ? 183.758 171.384 175.267 1.00 56.67  ? 673  VAL   B N     1 
ATOM   9434  C  CA    . VAL   B 1 673  ? 182.361 171.418 174.849 1.00 59.17  ? 673  VAL   B CA    1 
ATOM   9435  C  C     . VAL   B 1 673  ? 182.184 171.262 173.342 1.00 60.74  ? 673  VAL   B C     1 
ATOM   9436  O  O     . VAL   B 1 673  ? 181.066 170.985 172.886 1.00 60.09  ? 673  VAL   B O     1 
ATOM   9437  C  CB    . VAL   B 1 673  ? 181.686 172.722 175.310 1.00 59.52  ? 673  VAL   B CB    1 
ATOM   9438  C  CG1   . VAL   B 1 673  ? 182.231 173.906 174.526 1.00 58.68  ? 673  VAL   B CG1   1 
ATOM   9439  C  CG2   . VAL   B 1 673  ? 180.175 172.621 175.158 1.00 59.21  ? 673  VAL   B CG2   1 
ATOM   9440  N  N     . ILE   B 1 674  ? 183.249 171.431 172.557 1.00 56.25  ? 674  ILE   B N     1 
ATOM   9441  C  CA    . ILE   B 1 674  ? 183.129 171.362 171.105 1.00 52.69  ? 674  ILE   B CA    1 
ATOM   9442  C  C     . ILE   B 1 674  ? 183.408 169.967 170.553 1.00 54.15  ? 674  ILE   B C     1 
ATOM   9443  O  O     . ILE   B 1 674  ? 183.005 169.669 169.420 1.00 54.49  ? 674  ILE   B O     1 
ATOM   9444  C  CB    . ILE   B 1 674  ? 184.067 172.386 170.442 1.00 52.68  ? 674  ILE   B CB    1 
ATOM   9445  C  CG1   . ILE   B 1 674  ? 183.653 173.807 170.825 1.00 53.05  ? 674  ILE   B CG1   1 
ATOM   9446  C  CG2   . ILE   B 1 674  ? 184.049 172.231 168.932 1.00 55.26  ? 674  ILE   B CG2   1 
ATOM   9447  C  CD1   . ILE   B 1 674  ? 182.756 174.478 169.813 1.00 53.81  ? 674  ILE   B CD1   1 
ATOM   9448  N  N     . ALA   B 1 675  ? 184.071 169.104 171.321 1.00 53.62  ? 675  ALA   B N     1 
ATOM   9449  C  CA    . ALA   B 1 675  ? 184.400 167.761 170.845 1.00 55.39  ? 675  ALA   B CA    1 
ATOM   9450  C  C     . ALA   B 1 675  ? 183.195 167.002 170.308 1.00 54.19  ? 675  ALA   B C     1 
ATOM   9451  O  O     . ALA   B 1 675  ? 183.308 166.388 169.234 1.00 57.32  ? 675  ALA   B O     1 
ATOM   9452  C  CB    . ALA   B 1 675  ? 185.075 166.976 171.977 1.00 48.42  ? 675  ALA   B CB    1 
ATOM   9453  N  N     . PRO   B 1 676  ? 182.042 166.988 170.980 1.00 47.69  ? 676  PRO   B N     1 
ATOM   9454  C  CA    . PRO   B 1 676  ? 180.886 166.270 170.421 1.00 50.59  ? 676  PRO   B CA    1 
ATOM   9455  C  C     . PRO   B 1 676  ? 180.473 166.768 169.049 1.00 51.38  ? 676  PRO   B C     1 
ATOM   9456  O  O     . PRO   B 1 676  ? 180.029 165.965 168.221 1.00 51.00  ? 676  PRO   B O     1 
ATOM   9457  C  CB    . PRO   B 1 676  ? 179.787 166.509 171.466 1.00 47.15  ? 676  PRO   B CB    1 
ATOM   9458  C  CG    . PRO   B 1 676  ? 180.234 167.711 172.234 1.00 50.14  ? 676  PRO   B CG    1 
ATOM   9459  C  CD    . PRO   B 1 676  ? 181.724 167.648 172.256 1.00 44.88  ? 676  PRO   B CD    1 
ATOM   9460  N  N     . ILE   B 1 677  ? 180.605 168.067 168.777 1.00 46.33  ? 677  ILE   B N     1 
ATOM   9461  C  CA    . ILE   B 1 677  ? 180.256 168.588 167.458 1.00 45.12  ? 677  ILE   B CA    1 
ATOM   9462  C  C     . ILE   B 1 677  ? 181.139 167.954 166.390 1.00 47.04  ? 677  ILE   B C     1 
ATOM   9463  O  O     . ILE   B 1 677  ? 180.663 167.527 165.330 1.00 48.56  ? 677  ILE   B O     1 
ATOM   9464  C  CB    . ILE   B 1 677  ? 180.365 170.123 167.441 1.00 47.84  ? 677  ILE   B CB    1 
ATOM   9465  C  CG1   . ILE   B 1 677  ? 179.472 170.737 168.520 1.00 46.30  ? 677  ILE   B CG1   1 
ATOM   9466  C  CG2   . ILE   B 1 677  ? 179.995 170.667 166.071 1.00 48.69  ? 677  ILE   B CG2   1 
ATOM   9467  C  CD1   . ILE   B 1 677  ? 178.112 170.095 168.628 1.00 48.96  ? 677  ILE   B CD1   1 
ATOM   9468  N  N     . ILE   B 1 678  ? 182.445 167.887 166.653 1.00 41.64  ? 678  ILE   B N     1 
ATOM   9469  C  CA    . ILE   B 1 678  ? 183.373 167.290 165.698 1.00 43.90  ? 678  ILE   B CA    1 
ATOM   9470  C  C     . ILE   B 1 678  ? 183.085 165.803 165.531 1.00 45.95  ? 678  ILE   B C     1 
ATOM   9471  O  O     . ILE   B 1 678  ? 183.112 165.270 164.412 1.00 54.46  ? 678  ILE   B O     1 
ATOM   9472  C  CB    . ILE   B 1 678  ? 184.824 167.542 166.142 1.00 42.96  ? 678  ILE   B CB    1 
ATOM   9473  C  CG1   . ILE   B 1 678  ? 185.066 169.039 166.345 1.00 44.87  ? 678  ILE   B CG1   1 
ATOM   9474  C  CG2   . ILE   B 1 678  ? 185.801 166.972 165.128 1.00 45.87  ? 678  ILE   B CG2   1 
ATOM   9475  C  CD1   . ILE   B 1 678  ? 184.308 169.921 165.377 1.00 45.68  ? 678  ILE   B CD1   1 
ATOM   9476  N  N     . SER   B 1 679  ? 182.820 165.106 166.638 1.00 33.21  ? 679  SER   B N     1 
ATOM   9477  C  CA    . SER   B 1 679  ? 182.498 163.686 166.546 1.00 35.73  ? 679  SER   B CA    1 
ATOM   9478  C  C     . SER   B 1 679  ? 181.253 163.462 165.699 1.00 42.49  ? 679  SER   B C     1 
ATOM   9479  O  O     . SER   B 1 679  ? 181.201 162.532 164.886 1.00 47.68  ? 679  SER   B O     1 
ATOM   9480  C  CB    . SER   B 1 679  ? 182.313 163.096 167.943 1.00 38.90  ? 679  SER   B CB    1 
ATOM   9481  O  OG    . SER   B 1 679  ? 183.359 163.497 168.809 1.00 46.31  ? 679  SER   B OG    1 
ATOM   9482  N  N     . ASN   B 1 680  ? 180.238 164.311 165.872 1.00 43.46  ? 680  ASN   B N     1 
ATOM   9483  C  CA    . ASN   B 1 680  ? 179.017 164.169 165.090 1.00 42.25  ? 680  ASN   B CA    1 
ATOM   9484  C  C     . ASN   B 1 680  ? 179.248 164.509 163.624 1.00 43.16  ? 680  ASN   B C     1 
ATOM   9485  O  O     . ASN   B 1 680  ? 178.633 163.895 162.749 1.00 48.99  ? 680  ASN   B O     1 
ATOM   9486  C  CB    . ASN   B 1 680  ? 177.912 165.042 165.681 1.00 48.03  ? 680  ASN   B CB    1 
ATOM   9487  C  CG    . ASN   B 1 680  ? 177.068 164.298 166.696 1.00 49.64  ? 680  ASN   B CG    1 
ATOM   9488  O  OD1   . ASN   B 1 680  ? 175.995 164.754 167.084 1.00 52.18  ? 680  ASN   B OD1   1 
ATOM   9489  N  ND2   . ASN   B 1 680  ? 177.552 163.141 167.132 1.00 48.64  ? 680  ASN   B ND2   1 
ATOM   9490  N  N     . PHE   B 1 681  ? 180.128 165.468 163.332 1.00 36.76  ? 681  PHE   B N     1 
ATOM   9491  C  CA    . PHE   B 1 681  ? 180.489 165.734 161.941 1.00 39.50  ? 681  PHE   B CA    1 
ATOM   9492  C  C     . PHE   B 1 681  ? 181.131 164.507 161.302 1.00 40.17  ? 681  PHE   B C     1 
ATOM   9493  O  O     . PHE   B 1 681  ? 180.785 164.115 160.177 1.00 40.53  ? 681  PHE   B O     1 
ATOM   9494  C  CB    . PHE   B 1 681  ? 181.436 166.932 161.866 1.00 39.06  ? 681  PHE   B CB    1 
ATOM   9495  C  CG    . PHE   B 1 681  ? 180.761 168.258 162.070 1.00 43.83  ? 681  PHE   B CG    1 
ATOM   9496  C  CD1   . PHE   B 1 681  ? 179.415 168.328 162.380 1.00 39.52  ? 681  PHE   B CD1   1 
ATOM   9497  C  CD2   . PHE   B 1 681  ? 181.477 169.436 161.955 1.00 42.72  ? 681  PHE   B CD2   1 
ATOM   9498  C  CE1   . PHE   B 1 681  ? 178.795 169.548 162.569 1.00 35.91  ? 681  PHE   B CE1   1 
ATOM   9499  C  CE2   . PHE   B 1 681  ? 180.863 170.657 162.142 1.00 41.63  ? 681  PHE   B CE2   1 
ATOM   9500  C  CZ    . PHE   B 1 681  ? 179.521 170.713 162.449 1.00 38.48  ? 681  PHE   B CZ    1 
ATOM   9501  N  N     . PHE   B 1 682  ? 182.075 163.885 162.012 1.00 36.13  ? 682  PHE   B N     1 
ATOM   9502  C  CA    . PHE   B 1 682  ? 182.723 162.686 161.488 1.00 36.02  ? 682  PHE   B CA    1 
ATOM   9503  C  C     . PHE   B 1 682  ? 181.714 161.563 161.281 1.00 37.94  ? 682  PHE   B C     1 
ATOM   9504  O  O     . PHE   B 1 682  ? 181.750 160.857 160.263 1.00 41.88  ? 682  PHE   B O     1 
ATOM   9505  C  CB    . PHE   B 1 682  ? 183.837 162.239 162.435 1.00 39.70  ? 682  PHE   B CB    1 
ATOM   9506  C  CG    . PHE   B 1 682  ? 185.120 163.002 162.268 1.00 37.69  ? 682  PHE   B CG    1 
ATOM   9507  C  CD1   . PHE   B 1 682  ? 185.217 164.318 162.681 1.00 36.72  ? 682  PHE   B CD1   1 
ATOM   9508  C  CD2   . PHE   B 1 682  ? 186.232 162.400 161.709 1.00 44.50  ? 682  PHE   B CD2   1 
ATOM   9509  C  CE1   . PHE   B 1 682  ? 186.395 165.021 162.533 1.00 37.38  ? 682  PHE   B CE1   1 
ATOM   9510  C  CE2   . PHE   B 1 682  ? 187.414 163.102 161.559 1.00 45.55  ? 682  PHE   B CE2   1 
ATOM   9511  C  CZ    . PHE   B 1 682  ? 187.493 164.413 161.972 1.00 37.40  ? 682  PHE   B CZ    1 
ATOM   9512  N  N     . LEU   B 1 683  ? 180.807 161.378 162.241 1.00 33.85  ? 683  LEU   B N     1 
ATOM   9513  C  CA    . LEU   B 1 683  ? 179.793 160.339 162.105 1.00 32.95  ? 683  LEU   B CA    1 
ATOM   9514  C  C     . LEU   B 1 683  ? 178.861 160.629 160.936 1.00 33.61  ? 683  LEU   B C     1 
ATOM   9515  O  O     . LEU   B 1 683  ? 178.423 159.708 160.239 1.00 38.90  ? 683  LEU   B O     1 
ATOM   9516  C  CB    . LEU   B 1 683  ? 179.001 160.201 163.404 1.00 40.19  ? 683  LEU   B CB    1 
ATOM   9517  C  CG    . LEU   B 1 683  ? 179.651 159.331 164.480 1.00 38.46  ? 683  LEU   B CG    1 
ATOM   9518  C  CD1   . LEU   B 1 683  ? 179.314 159.852 165.866 1.00 41.17  ? 683  LEU   B CD1   1 
ATOM   9519  C  CD2   . LEU   B 1 683  ? 179.227 157.879 164.329 1.00 34.74  ? 683  LEU   B CD2   1 
ATOM   9520  N  N     . ALA   B 1 684  ? 178.534 161.903 160.715 1.00 33.31  ? 684  ALA   B N     1 
ATOM   9521  C  CA    . ALA   B 1 684  ? 177.718 162.270 159.565 1.00 33.24  ? 684  ALA   B CA    1 
ATOM   9522  C  C     . ALA   B 1 684  ? 178.424 161.924 158.264 1.00 39.59  ? 684  ALA   B C     1 
ATOM   9523  O  O     . ALA   B 1 684  ? 177.797 161.436 157.318 1.00 41.56  ? 684  ALA   B O     1 
ATOM   9524  C  CB    . ALA   B 1 684  ? 177.382 163.759 159.613 1.00 35.33  ? 684  ALA   B CB    1 
ATOM   9525  N  N     . SER   B 1 685  ? 179.731 162.183 158.190 1.00 37.45  ? 685  SER   B N     1 
ATOM   9526  C  CA    . SER   B 1 685  ? 180.482 161.800 156.997 1.00 31.19  ? 685  SER   B CA    1 
ATOM   9527  C  C     . SER   B 1 685  ? 180.455 160.288 156.792 1.00 36.32  ? 685  SER   B C     1 
ATOM   9528  O  O     . SER   B 1 685  ? 180.275 159.804 155.665 1.00 35.88  ? 685  SER   B O     1 
ATOM   9529  C  CB    . SER   B 1 685  ? 181.919 162.307 157.097 1.00 33.66  ? 685  SER   B CB    1 
ATOM   9530  O  OG    . SER   B 1 685  ? 181.967 163.560 157.755 1.00 34.08  ? 685  SER   B OG    1 
ATOM   9531  N  N     . TYR   B 1 686  ? 180.633 159.525 157.873 1.00 31.54  ? 686  TYR   B N     1 
ATOM   9532  C  CA    . TYR   B 1 686  ? 180.574 158.069 157.765 1.00 29.49  ? 686  TYR   B CA    1 
ATOM   9533  C  C     . TYR   B 1 686  ? 179.210 157.615 157.256 1.00 30.34  ? 686  TYR   B C     1 
ATOM   9534  O  O     . TYR   B 1 686  ? 179.113 156.747 156.374 1.00 34.96  ? 686  TYR   B O     1 
ATOM   9535  C  CB    . TYR   B 1 686  ? 180.865 157.433 159.125 1.00 31.40  ? 686  TYR   B CB    1 
ATOM   9536  C  CG    . TYR   B 1 686  ? 182.296 157.557 159.600 1.00 30.39  ? 686  TYR   B CG    1 
ATOM   9537  C  CD1   . TYR   B 1 686  ? 183.166 158.475 159.030 1.00 28.95  ? 686  TYR   B CD1   1 
ATOM   9538  C  CD2   . TYR   B 1 686  ? 182.768 156.767 160.640 1.00 32.59  ? 686  TYR   B CD2   1 
ATOM   9539  C  CE1   . TYR   B 1 686  ? 184.469 158.592 159.471 1.00 35.76  ? 686  TYR   B CE1   1 
ATOM   9540  C  CE2   . TYR   B 1 686  ? 184.069 156.878 161.088 1.00 37.58  ? 686  TYR   B CE2   1 
ATOM   9541  C  CZ    . TYR   B 1 686  ? 184.915 157.792 160.501 1.00 39.13  ? 686  TYR   B CZ    1 
ATOM   9542  O  OH    . TYR   B 1 686  ? 186.212 157.904 160.946 1.00 33.47  ? 686  TYR   B OH    1 
ATOM   9543  N  N     . ALA   B 1 687  ? 178.144 158.191 157.812 1.00 32.84  ? 687  ALA   B N     1 
ATOM   9544  C  CA    . ALA   B 1 687  ? 176.794 157.838 157.394 1.00 33.86  ? 687  ALA   B CA    1 
ATOM   9545  C  C     . ALA   B 1 687  ? 176.562 158.198 155.936 1.00 35.81  ? 687  ALA   B C     1 
ATOM   9546  O  O     . ALA   B 1 687  ? 175.884 157.466 155.210 1.00 43.42  ? 687  ALA   B O     1 
ATOM   9547  C  CB    . ALA   B 1 687  ? 175.770 158.533 158.291 1.00 35.32  ? 687  ALA   B CB    1 
ATOM   9548  N  N     . LEU   B 1 688  ? 177.106 159.330 155.488 1.00 38.75  ? 688  LEU   B N     1 
ATOM   9549  C  CA    . LEU   B 1 688  ? 176.955 159.704 154.088 1.00 33.40  ? 688  LEU   B CA    1 
ATOM   9550  C  C     . LEU   B 1 688  ? 177.692 158.734 153.175 1.00 28.62  ? 688  LEU   B C     1 
ATOM   9551  O  O     . LEU   B 1 688  ? 177.217 158.434 152.080 1.00 42.33  ? 688  LEU   B O     1 
ATOM   9552  C  CB    . LEU   B 1 688  ? 177.440 161.134 153.858 1.00 33.52  ? 688  LEU   B CB    1 
ATOM   9553  C  CG    . LEU   B 1 688  ? 176.318 162.172 153.782 1.00 34.81  ? 688  LEU   B CG    1 
ATOM   9554  C  CD1   . LEU   B 1 688  ? 176.826 163.485 153.216 1.00 34.58  ? 688  LEU   B CD1   1 
ATOM   9555  C  CD2   . LEU   B 1 688  ? 175.153 161.648 152.959 1.00 36.10  ? 688  LEU   B CD2   1 
ATOM   9556  N  N     . ILE   B 1 689  ? 178.850 158.229 153.603 1.00 24.86  ? 689  ILE   B N     1 
ATOM   9557  C  CA    . ILE   B 1 689  ? 179.555 157.232 152.795 1.00 20.56  ? 689  ILE   B CA    1 
ATOM   9558  C  C     . ILE   B 1 689  ? 178.731 155.950 152.691 1.00 24.35  ? 689  ILE   B C     1 
ATOM   9559  O  O     . ILE   B 1 689  ? 178.561 155.372 151.603 1.00 26.34  ? 689  ILE   B O     1 
ATOM   9560  C  CB    . ILE   B 1 689  ? 180.953 156.960 153.379 1.00 24.37  ? 689  ILE   B CB    1 
ATOM   9561  C  CG1   . ILE   B 1 689  ? 181.848 158.188 153.207 1.00 26.38  ? 689  ILE   B CG1   1 
ATOM   9562  C  CG2   . ILE   B 1 689  ? 181.583 155.744 152.722 1.00 23.75  ? 689  ILE   B CG2   1 
ATOM   9563  C  CD1   . ILE   B 1 689  ? 183.275 157.973 153.655 1.00 26.58  ? 689  ILE   B CD1   1 
ATOM   9564  N  N     . ASN   B 1 690  ? 178.204 155.486 153.827 1.00 31.71  ? 690  ASN   B N     1 
ATOM   9565  C  CA    . ASN   B 1 690  ? 177.389 154.274 153.810 1.00 32.80  ? 690  ASN   B CA    1 
ATOM   9566  C  C     . ASN   B 1 690  ? 176.141 154.462 152.955 1.00 30.35  ? 690  ASN   B C     1 
ATOM   9567  O  O     . ASN   B 1 690  ? 175.758 153.568 152.188 1.00 32.43  ? 690  ASN   B O     1 
ATOM   9568  C  CB    . ASN   B 1 690  ? 177.017 153.868 155.236 1.00 30.28  ? 690  ASN   B CB    1 
ATOM   9569  C  CG    . ASN   B 1 690  ? 178.220 153.432 156.050 1.00 31.70  ? 690  ASN   B CG    1 
ATOM   9570  O  OD1   . ASN   B 1 690  ? 178.513 152.242 156.153 1.00 36.17  ? 690  ASN   B OD1   1 
ATOM   9571  N  ND2   . ASN   B 1 690  ? 178.923 154.396 156.632 1.00 37.44  ? 690  ASN   B ND2   1 
ATOM   9572  N  N     . PHE   B 1 691  ? 175.496 155.625 153.069 1.00 23.65  ? 691  PHE   B N     1 
ATOM   9573  C  CA    . PHE   B 1 691  ? 174.330 155.915 152.246 1.00 29.00  ? 691  PHE   B CA    1 
ATOM   9574  C  C     . PHE   B 1 691  ? 174.703 156.058 150.779 1.00 31.78  ? 691  PHE   B C     1 
ATOM   9575  O  O     . PHE   B 1 691  ? 173.891 155.745 149.910 1.00 40.13  ? 691  PHE   B O     1 
ATOM   9576  C  CB    . PHE   B 1 691  ? 173.633 157.181 152.739 1.00 28.65  ? 691  PHE   B CB    1 
ATOM   9577  C  CG    . PHE   B 1 691  ? 172.426 157.557 151.930 1.00 35.35  ? 691  PHE   B CG    1 
ATOM   9578  C  CD1   . PHE   B 1 691  ? 171.263 156.811 152.007 1.00 30.33  ? 691  PHE   B CD1   1 
ATOM   9579  C  CD2   . PHE   B 1 691  ? 172.457 158.653 151.085 1.00 40.43  ? 691  PHE   B CD2   1 
ATOM   9580  C  CE1   . PHE   B 1 691  ? 170.154 157.154 151.260 1.00 35.74  ? 691  PHE   B CE1   1 
ATOM   9581  C  CE2   . PHE   B 1 691  ? 171.351 159.000 150.336 1.00 35.96  ? 691  PHE   B CE2   1 
ATOM   9582  C  CZ    . PHE   B 1 691  ? 170.198 158.250 150.424 1.00 37.59  ? 691  PHE   B CZ    1 
ATOM   9583  N  N     . SER   B 1 692  ? 175.914 156.527 150.482 1.00 23.88  ? 692  SER   B N     1 
ATOM   9584  C  CA    . SER   B 1 692  ? 176.384 156.540 149.103 1.00 20.61  ? 692  SER   B CA    1 
ATOM   9585  C  C     . SER   B 1 692  ? 176.409 155.131 148.538 1.00 22.35  ? 692  SER   B C     1 
ATOM   9586  O  O     . SER   B 1 692  ? 175.907 154.877 147.437 1.00 30.19  ? 692  SER   B O     1 
ATOM   9587  C  CB    . SER   B 1 692  ? 177.776 157.167 149.028 1.00 25.32  ? 692  SER   B CB    1 
ATOM   9588  O  OG    . SER   B 1 692  ? 177.720 158.517 148.609 1.00 34.47  ? 692  SER   B OG    1 
ATOM   9589  N  N     . VAL   B 1 693  ? 176.989 154.196 149.289 1.00 25.36  ? 693  VAL   B N     1 
ATOM   9590  C  CA    . VAL   B 1 693  ? 177.051 152.819 148.804 1.00 20.14  ? 693  VAL   B CA    1 
ATOM   9591  C  C     . VAL   B 1 693  ? 175.646 152.248 148.642 1.00 23.00  ? 693  VAL   B C     1 
ATOM   9592  O  O     . VAL   B 1 693  ? 175.325 151.614 147.626 1.00 32.87  ? 693  VAL   B O     1 
ATOM   9593  C  CB    . VAL   B 1 693  ? 177.915 151.956 149.741 1.00 27.26  ? 693  VAL   B CB    1 
ATOM   9594  C  CG1   . VAL   B 1 693  ? 177.776 150.484 149.388 1.00 23.60  ? 693  VAL   B CG1   1 
ATOM   9595  C  CG2   . VAL   B 1 693  ? 179.368 152.388 149.657 1.00 28.38  ? 693  VAL   B CG2   1 
ATOM   9596  N  N     . PHE   B 1 694  ? 174.778 152.484 149.630 1.00 28.28  ? 694  PHE   B N     1 
ATOM   9597  C  CA    . PHE   B 1 694  ? 173.419 151.953 149.558 1.00 23.73  ? 694  PHE   B CA    1 
ATOM   9598  C  C     . PHE   B 1 694  ? 172.652 152.543 148.378 1.00 31.91  ? 694  PHE   B C     1 
ATOM   9599  O  O     . PHE   B 1 694  ? 171.931 151.826 147.677 1.00 30.65  ? 694  PHE   B O     1 
ATOM   9600  C  CB    . PHE   B 1 694  ? 172.679 152.223 150.868 1.00 26.29  ? 694  PHE   B CB    1 
ATOM   9601  C  CG    . PHE   B 1 694  ? 171.192 152.021 150.777 1.00 33.34  ? 694  PHE   B CG    1 
ATOM   9602  C  CD1   . PHE   B 1 694  ? 170.647 150.756 150.909 1.00 35.98  ? 694  PHE   B CD1   1 
ATOM   9603  C  CD2   . PHE   B 1 694  ? 170.341 153.091 150.563 1.00 29.84  ? 694  PHE   B CD2   1 
ATOM   9604  C  CE1   . PHE   B 1 694  ? 169.284 150.562 150.826 1.00 36.85  ? 694  PHE   B CE1   1 
ATOM   9605  C  CE2   . PHE   B 1 694  ? 168.976 152.902 150.478 1.00 25.33  ? 694  PHE   B CE2   1 
ATOM   9606  C  CZ    . PHE   B 1 694  ? 168.447 151.635 150.611 1.00 30.68  ? 694  PHE   B CZ    1 
ATOM   9607  N  N     . HIS   B 1 695  ? 172.782 153.853 148.156 1.00 32.48  ? 695  HIS   B N     1 
ATOM   9608  C  CA    . HIS   B 1 695  ? 172.082 154.517 147.063 1.00 21.51  ? 695  HIS   B CA    1 
ATOM   9609  C  C     . HIS   B 1 695  ? 172.601 154.050 145.712 1.00 27.95  ? 695  HIS   B C     1 
ATOM   9610  O  O     . HIS   B 1 695  ? 171.824 153.888 144.764 1.00 33.13  ? 695  HIS   B O     1 
ATOM   9611  C  CB    . HIS   B 1 695  ? 172.232 156.032 147.210 1.00 22.02  ? 695  HIS   B CB    1 
ATOM   9612  C  CG    . HIS   B 1 695  ? 171.267 156.824 146.386 1.00 32.16  ? 695  HIS   B CG    1 
ATOM   9613  N  ND1   . HIS   B 1 695  ? 171.663 157.612 145.327 1.00 38.42  ? 695  HIS   B ND1   1 
ATOM   9614  C  CD2   . HIS   B 1 695  ? 169.923 156.961 146.473 1.00 33.54  ? 695  HIS   B CD2   1 
ATOM   9615  C  CE1   . HIS   B 1 695  ? 170.605 158.195 144.794 1.00 36.73  ? 695  HIS   B CE1   1 
ATOM   9616  N  NE2   . HIS   B 1 695  ? 169.536 157.816 145.470 1.00 39.56  ? 695  HIS   B NE2   1 
ATOM   9617  N  N     . ALA   B 1 696  ? 173.913 153.833 145.600 1.00 29.81  ? 696  ALA   B N     1 
ATOM   9618  C  CA    . ALA   B 1 696  ? 174.461 153.287 144.366 1.00 19.17  ? 696  ALA   B CA    1 
ATOM   9619  C  C     . ALA   B 1 696  ? 173.954 151.876 144.116 1.00 27.23  ? 696  ALA   B C     1 
ATOM   9620  O  O     . ALA   B 1 696  ? 173.765 151.480 142.962 1.00 28.36  ? 696  ALA   B O     1 
ATOM   9621  C  CB    . ALA   B 1 696  ? 175.988 153.305 144.411 1.00 22.43  ? 696  ALA   B CB    1 
ATOM   9622  N  N     . SER   B 1 697  ? 173.739 151.099 145.179 1.00 32.37  ? 697  SER   B N     1 
ATOM   9623  C  CA    . SER   B 1 697  ? 173.158 149.773 144.994 1.00 28.74  ? 697  SER   B CA    1 
ATOM   9624  C  C     . SER   B 1 697  ? 171.671 149.848 144.662 1.00 31.08  ? 697  SER   B C     1 
ATOM   9625  O  O     . SER   B 1 697  ? 171.146 148.964 143.976 1.00 37.59  ? 697  SER   B O     1 
ATOM   9626  C  CB    . SER   B 1 697  ? 173.385 148.919 146.240 1.00 33.22  ? 697  SER   B CB    1 
ATOM   9627  O  OG    . SER   B 1 697  ? 174.622 148.233 146.166 1.00 35.38  ? 697  SER   B OG    1 
ATOM   9628  N  N     . LEU   B 1 698  ? 170.979 150.887 145.135 1.00 31.40  ? 698  LEU   B N     1 
ATOM   9629  C  CA    . LEU   B 1 698  ? 169.563 151.050 144.819 1.00 30.96  ? 698  LEU   B CA    1 
ATOM   9630  C  C     . LEU   B 1 698  ? 169.366 151.324 143.334 1.00 33.26  ? 698  LEU   B C     1 
ATOM   9631  O  O     . LEU   B 1 698  ? 168.695 150.560 142.631 1.00 39.18  ? 698  LEU   B O     1 
ATOM   9632  C  CB    . LEU   B 1 698  ? 168.962 152.176 145.663 1.00 38.00  ? 698  LEU   B CB    1 
ATOM   9633  C  CG    . LEU   B 1 698  ? 167.487 152.028 146.044 1.00 28.20  ? 698  LEU   B CG    1 
ATOM   9634  C  CD1   . LEU   B 1 698  ? 167.110 150.564 146.204 1.00 33.29  ? 698  LEU   B CD1   1 
ATOM   9635  C  CD2   . LEU   B 1 698  ? 167.180 152.807 147.311 1.00 30.15  ? 698  LEU   B CD2   1 
ATOM   9636  N  N     . ALA   B 1 699  ? 169.940 152.416 142.839 1.00 31.20  ? 699  ALA   B N     1 
ATOM   9637  C  CA    . ALA   B 1 699  ? 169.979 152.642 141.402 1.00 25.68  ? 699  ALA   B CA    1 
ATOM   9638  C  C     . ALA   B 1 699  ? 170.889 151.605 140.761 1.00 35.16  ? 699  ALA   B C     1 
ATOM   9639  O  O     . ALA   B 1 699  ? 172.031 151.417 141.191 1.00 52.11  ? 699  ALA   B O     1 
ATOM   9640  C  CB    . ALA   B 1 699  ? 170.468 154.055 141.093 1.00 21.20  ? 699  ALA   B CB    1 
ATOM   9641  N  N     . LYS   B 1 700  ? 170.390 150.933 139.729 1.00 24.79  ? 700  LYS   B N     1 
ATOM   9642  C  CA    . LYS   B 1 700  ? 171.073 149.783 139.141 1.00 28.05  ? 700  LYS   B CA    1 
ATOM   9643  C  C     . LYS   B 1 700  ? 171.861 150.164 137.897 1.00 32.02  ? 700  LYS   B C     1 
ATOM   9644  O  O     . LYS   B 1 700  ? 171.926 149.403 136.928 1.00 36.02  ? 700  LYS   B O     1 
ATOM   9645  C  CB    . LYS   B 1 700  ? 170.072 148.675 138.834 1.00 33.59  ? 700  LYS   B CB    1 
ATOM   9646  C  CG    . LYS   B 1 700  ? 169.713 147.835 140.049 1.00 31.55  ? 700  LYS   B CG    1 
ATOM   9647  C  CD    . LYS   B 1 700  ? 168.713 146.746 139.709 1.00 33.78  ? 700  LYS   B CD    1 
ATOM   9648  C  CE    . LYS   B 1 700  ? 167.710 146.560 140.833 1.00 37.01  ? 700  LYS   B CE    1 
ATOM   9649  N  NZ    . LYS   B 1 700  ? 167.167 147.864 141.304 1.00 36.55  ? 700  LYS   B NZ    1 
ATOM   9650  N  N     . SER   B 1 701  ? 172.458 151.350 137.903 1.00 31.07  ? 701  SER   B N     1 
ATOM   9651  C  CA    . SER   B 1 701  ? 173.248 151.802 136.768 1.00 33.64  ? 701  SER   B CA    1 
ATOM   9652  C  C     . SER   B 1 701  ? 174.358 150.799 136.463 1.00 29.71  ? 701  SER   B C     1 
ATOM   9653  O  O     . SER   B 1 701  ? 175.060 150.358 137.383 1.00 23.32  ? 701  SER   B O     1 
ATOM   9654  C  CB    . SER   B 1 701  ? 173.850 153.176 137.055 1.00 25.25  ? 701  SER   B CB    1 
ATOM   9655  O  OG    . SER   B 1 701  ? 174.986 153.416 136.245 1.00 25.42  ? 701  SER   B OG    1 
ATOM   9656  N  N     . PRO   B 1 702  ? 174.550 150.417 135.198 1.00 29.25  ? 702  PRO   B N     1 
ATOM   9657  C  CA    . PRO   B 1 702  ? 175.636 149.480 134.872 1.00 23.55  ? 702  PRO   B CA    1 
ATOM   9658  C  C     . PRO   B 1 702  ? 177.016 150.010 135.209 1.00 20.79  ? 702  PRO   B C     1 
ATOM   9659  O  O     . PRO   B 1 702  ? 177.961 149.218 135.300 1.00 25.59  ? 702  PRO   B O     1 
ATOM   9660  C  CB    . PRO   B 1 702  ? 175.471 149.267 133.361 1.00 23.54  ? 702  PRO   B CB    1 
ATOM   9661  C  CG    . PRO   B 1 702  ? 174.036 149.593 133.093 1.00 23.51  ? 702  PRO   B CG    1 
ATOM   9662  C  CD    . PRO   B 1 702  ? 173.722 150.728 134.022 1.00 21.57  ? 702  PRO   B CD    1 
ATOM   9663  N  N     . GLY   B 1 703  ? 177.166 151.318 135.389 1.00 22.23  ? 703  GLY   B N     1 
ATOM   9664  C  CA    . GLY   B 1 703  ? 178.445 151.911 135.710 1.00 25.29  ? 703  GLY   B CA    1 
ATOM   9665  C  C     . GLY   B 1 703  ? 178.863 151.817 137.156 1.00 30.75  ? 703  GLY   B C     1 
ATOM   9666  O  O     . GLY   B 1 703  ? 179.923 152.338 137.515 1.00 38.28  ? 703  GLY   B O     1 
ATOM   9667  N  N     . TRP   B 1 704  ? 178.064 151.168 138.006 1.00 24.02  ? 704  TRP   B N     1 
ATOM   9668  C  CA    . TRP   B 1 704  ? 178.463 150.976 139.396 1.00 15.53  ? 704  TRP   B CA    1 
ATOM   9669  C  C     . TRP   B 1 704  ? 179.767 150.192 139.473 1.00 32.45  ? 704  TRP   B C     1 
ATOM   9670  O  O     . TRP   B 1 704  ? 180.786 150.704 139.946 1.00 39.69  ? 704  TRP   B O     1 
ATOM   9671  C  CB    . TRP   B 1 704  ? 177.347 150.264 140.165 1.00 25.34  ? 704  TRP   B CB    1 
ATOM   9672  C  CG    . TRP   B 1 704  ? 177.563 150.157 141.657 1.00 29.62  ? 704  TRP   B CG    1 
ATOM   9673  C  CD1   . TRP   B 1 704  ? 176.939 149.291 142.507 1.00 29.10  ? 704  TRP   B CD1   1 
ATOM   9674  C  CD2   . TRP   B 1 704  ? 178.442 150.950 142.472 1.00 33.37  ? 704  TRP   B CD2   1 
ATOM   9675  N  NE1   . TRP   B 1 704  ? 177.382 149.483 143.792 1.00 31.64  ? 704  TRP   B NE1   1 
ATOM   9676  C  CE2   . TRP   B 1 704  ? 178.303 150.496 143.799 1.00 34.73  ? 704  TRP   B CE2   1 
ATOM   9677  C  CE3   . TRP   B 1 704  ? 179.336 151.994 142.209 1.00 33.94  ? 704  TRP   B CE3   1 
ATOM   9678  C  CZ2   . TRP   B 1 704  ? 179.022 151.047 144.857 1.00 28.61  ? 704  TRP   B CZ2   1 
ATOM   9679  C  CZ3   . TRP   B 1 704  ? 180.049 152.539 143.263 1.00 27.12  ? 704  TRP   B CZ3   1 
ATOM   9680  C  CH2   . TRP   B 1 704  ? 179.888 152.065 144.569 1.00 23.83  ? 704  TRP   B CH2   1 
ATOM   9681  N  N     . ARG   B 1 705  ? 179.747 148.941 139.008 1.00 27.36  ? 705  ARG   B N     1 
ATOM   9682  C  CA    . ARG   B 1 705  ? 180.927 148.107 138.788 1.00 27.28  ? 705  ARG   B CA    1 
ATOM   9683  C  C     . ARG   B 1 705  ? 182.045 148.362 139.793 1.00 25.53  ? 705  ARG   B C     1 
ATOM   9684  O  O     . ARG   B 1 705  ? 183.152 148.743 139.392 1.00 28.05  ? 705  ARG   B O     1 
ATOM   9685  C  CB    . ARG   B 1 705  ? 181.467 148.325 137.373 1.00 25.40  ? 705  ARG   B CB    1 
ATOM   9686  C  CG    . ARG   B 1 705  ? 180.672 147.643 136.278 1.00 24.91  ? 705  ARG   B CG    1 
ATOM   9687  C  CD    . ARG   B 1 705  ? 181.414 147.698 134.952 1.00 20.32  ? 705  ARG   B CD    1 
ATOM   9688  N  NE    . ARG   B 1 705  ? 181.026 148.867 134.173 1.00 18.42  ? 705  ARG   B NE    1 
ATOM   9689  C  CZ    . ARG   B 1 705  ? 181.869 149.793 133.737 1.00 23.29  ? 705  ARG   B CZ    1 
ATOM   9690  N  NH1   . ARG   B 1 705  ? 183.169 149.706 133.963 1.00 23.29  ? 705  ARG   B NH1   1 
ATOM   9691  N  NH2   . ARG   B 1 705  ? 181.395 150.833 133.057 1.00 27.57  ? 705  ARG   B NH2   1 
ATOM   9692  N  N     . PRO   B 1 706  ? 181.814 148.173 141.089 1.00 34.27  ? 706  PRO   B N     1 
ATOM   9693  C  CA    . PRO   B 1 706  ? 182.914 148.312 142.050 1.00 28.46  ? 706  PRO   B CA    1 
ATOM   9694  C  C     . PRO   B 1 706  ? 183.830 147.098 142.021 1.00 31.42  ? 706  PRO   B C     1 
ATOM   9695  O  O     . PRO   B 1 706  ? 183.379 145.953 141.941 1.00 33.24  ? 706  PRO   B O     1 
ATOM   9696  C  CB    . PRO   B 1 706  ? 182.194 148.439 143.397 1.00 24.57  ? 706  PRO   B CB    1 
ATOM   9697  C  CG    . PRO   B 1 706  ? 180.907 147.729 143.194 1.00 29.26  ? 706  PRO   B CG    1 
ATOM   9698  C  CD    . PRO   B 1 706  ? 180.521 147.942 141.756 1.00 30.97  ? 706  PRO   B CD    1 
ATOM   9699  N  N     . ALA   B 1 707  ? 185.136 147.362 142.091 1.00 26.43  ? 707  ALA   B N     1 
ATOM   9700  C  CA    . ALA   B 1 707  ? 186.125 146.293 142.056 1.00 21.98  ? 707  ALA   B CA    1 
ATOM   9701  C  C     . ALA   B 1 707  ? 186.234 145.546 143.377 1.00 28.45  ? 707  ALA   B C     1 
ATOM   9702  O  O     . ALA   B 1 707  ? 186.749 144.423 143.397 1.00 33.57  ? 707  ALA   B O     1 
ATOM   9703  C  CB    . ALA   B 1 707  ? 187.496 146.855 141.676 1.00 21.84  ? 707  ALA   B CB    1 
ATOM   9704  N  N     . PHE   B 1 708  ? 185.765 146.137 144.471 1.00 36.20  ? 708  PHE   B N     1 
ATOM   9705  C  CA    . PHE   B 1 708  ? 185.854 145.537 145.795 1.00 33.51  ? 708  PHE   B CA    1 
ATOM   9706  C  C     . PHE   B 1 708  ? 184.527 144.871 146.135 1.00 38.21  ? 708  PHE   B C     1 
ATOM   9707  O  O     . PHE   B 1 708  ? 183.477 145.521 146.107 1.00 42.97  ? 708  PHE   B O     1 
ATOM   9708  C  CB    . PHE   B 1 708  ? 186.212 146.593 146.841 1.00 32.89  ? 708  PHE   B CB    1 
ATOM   9709  C  CG    . PHE   B 1 708  ? 186.134 146.099 148.258 1.00 31.22  ? 708  PHE   B CG    1 
ATOM   9710  C  CD1   . PHE   B 1 708  ? 187.097 145.242 148.759 1.00 33.96  ? 708  PHE   B CD1   1 
ATOM   9711  C  CD2   . PHE   B 1 708  ? 185.103 146.498 149.090 1.00 34.46  ? 708  PHE   B CD2   1 
ATOM   9712  C  CE1   . PHE   B 1 708  ? 187.030 144.788 150.061 1.00 31.77  ? 708  PHE   B CE1   1 
ATOM   9713  C  CE2   . PHE   B 1 708  ? 185.032 146.048 150.393 1.00 38.85  ? 708  PHE   B CE2   1 
ATOM   9714  C  CZ    . PHE   B 1 708  ? 185.996 145.191 150.878 1.00 37.81  ? 708  PHE   B CZ    1 
ATOM   9715  N  N     . LYS   B 1 709  ? 184.576 143.580 146.448 1.00 44.78  ? 709  LYS   B N     1 
ATOM   9716  C  CA    . LYS   B 1 709  ? 183.395 142.844 146.880 1.00 48.23  ? 709  LYS   B CA    1 
ATOM   9717  C  C     . LYS   B 1 709  ? 183.201 143.043 148.383 1.00 53.14  ? 709  LYS   B C     1 
ATOM   9718  O  O     . LYS   B 1 709  ? 183.834 143.898 149.007 1.00 54.94  ? 709  LYS   B O     1 
ATOM   9719  C  CB    . LYS   B 1 709  ? 183.524 141.371 146.503 1.00 45.93  ? 709  LYS   B CB    1 
ATOM   9720  N  N     . TYR   B 1 710  ? 182.325 142.245 148.990 1.00 49.14  ? 710  TYR   B N     1 
ATOM   9721  C  CA    . TYR   B 1 710  ? 182.035 142.334 150.422 1.00 50.57  ? 710  TYR   B CA    1 
ATOM   9722  C  C     . TYR   B 1 710  ? 181.539 143.734 150.788 1.00 50.17  ? 710  TYR   B C     1 
ATOM   9723  O  O     . TYR   B 1 710  ? 182.081 144.407 151.667 1.00 51.33  ? 710  TYR   B O     1 
ATOM   9724  C  CB    . TYR   B 1 710  ? 183.263 141.963 151.264 1.00 45.07  ? 710  TYR   B CB    1 
ATOM   9725  C  CG    . TYR   B 1 710  ? 184.249 141.033 150.594 1.00 43.49  ? 710  TYR   B CG    1 
ATOM   9726  C  CD1   . TYR   B 1 710  ? 184.010 139.669 150.513 1.00 48.12  ? 710  TYR   B CD1   1 
ATOM   9727  C  CD2   . TYR   B 1 710  ? 185.427 141.524 150.050 1.00 46.45  ? 710  TYR   B CD2   1 
ATOM   9728  C  CE1   . TYR   B 1 710  ? 184.916 138.821 149.903 1.00 51.08  ? 710  TYR   B CE1   1 
ATOM   9729  C  CE2   . TYR   B 1 710  ? 186.335 140.688 149.438 1.00 51.37  ? 710  TYR   B CE2   1 
ATOM   9730  C  CZ    . TYR   B 1 710  ? 186.076 139.338 149.367 1.00 53.76  ? 710  TYR   B CZ    1 
ATOM   9731  O  OH    . TYR   B 1 710  ? 186.980 138.500 148.758 1.00 56.06  ? 710  TYR   B OH    1 
ATOM   9732  N  N     . TYR   B 1 711  ? 180.486 144.169 150.093 1.00 43.54  ? 711  TYR   B N     1 
ATOM   9733  C  CA    . TYR   B 1 711  ? 179.958 145.511 150.304 1.00 39.36  ? 711  TYR   B CA    1 
ATOM   9734  C  C     . TYR   B 1 711  ? 178.435 145.520 150.319 1.00 48.34  ? 711  TYR   B C     1 
ATOM   9735  O  O     . TYR   B 1 711  ? 177.817 146.510 149.914 1.00 58.31  ? 711  TYR   B O     1 
ATOM   9736  C  CB    . TYR   B 1 711  ? 180.478 146.480 149.237 1.00 43.45  ? 711  TYR   B CB    1 
ATOM   9737  C  CG    . TYR   B 1 711  ? 179.922 146.234 147.852 1.00 45.78  ? 711  TYR   B CG    1 
ATOM   9738  C  CD1   . TYR   B 1 711  ? 180.514 145.317 146.996 1.00 47.74  ? 711  TYR   B CD1   1 
ATOM   9739  C  CD2   . TYR   B 1 711  ? 178.815 146.935 147.393 1.00 41.16  ? 711  TYR   B CD2   1 
ATOM   9740  C  CE1   . TYR   B 1 711  ? 180.006 145.094 145.731 1.00 51.95  ? 711  TYR   B CE1   1 
ATOM   9741  C  CE2   . TYR   B 1 711  ? 178.302 146.719 146.135 1.00 45.99  ? 711  TYR   B CE2   1 
ATOM   9742  C  CZ    . TYR   B 1 711  ? 178.901 145.799 145.306 1.00 51.43  ? 711  TYR   B CZ    1 
ATOM   9743  O  OH    . TYR   B 1 711  ? 178.391 145.586 144.047 1.00 52.05  ? 711  TYR   B OH    1 
ATOM   9744  N  N     . ASN   B 1 712  ? 177.817 144.441 150.798 1.00 40.46  ? 712  ASN   B N     1 
ATOM   9745  C  CA    . ASN   B 1 712  ? 176.369 144.274 150.722 1.00 37.52  ? 712  ASN   B CA    1 
ATOM   9746  C  C     . ASN   B 1 712  ? 175.642 145.580 151.015 1.00 36.08  ? 712  ASN   B C     1 
ATOM   9747  O  O     . ASN   B 1 712  ? 175.966 146.288 151.972 1.00 35.31  ? 712  ASN   B O     1 
ATOM   9748  C  CB    . ASN   B 1 712  ? 175.921 143.191 151.705 1.00 40.11  ? 712  ASN   B CB    1 
ATOM   9749  C  CG    . ASN   B 1 712  ? 174.435 142.912 151.625 1.00 40.88  ? 712  ASN   B CG    1 
ATOM   9750  O  OD1   . ASN   B 1 712  ? 173.619 143.686 152.124 1.00 42.63  ? 712  ASN   B OD1   1 
ATOM   9751  N  ND2   . ASN   B 1 712  ? 174.075 141.800 150.995 1.00 42.44  ? 712  ASN   B ND2   1 
ATOM   9752  N  N     . MET   B 1 713  ? 174.657 145.895 150.171 1.00 37.35  ? 713  MET   B N     1 
ATOM   9753  C  CA    . MET   B 1 713  ? 173.977 147.183 150.261 1.00 39.79  ? 713  MET   B CA    1 
ATOM   9754  C  C     . MET   B 1 713  ? 173.214 147.322 151.572 1.00 45.42  ? 713  MET   B C     1 
ATOM   9755  O  O     . MET   B 1 713  ? 173.181 148.405 152.170 1.00 49.52  ? 713  MET   B O     1 
ATOM   9756  C  CB    . MET   B 1 713  ? 173.037 147.354 149.068 1.00 39.59  ? 713  MET   B CB    1 
ATOM   9757  C  CG    . MET   B 1 713  ? 171.647 146.777 149.280 1.00 43.93  ? 713  MET   B CG    1 
ATOM   9758  S  SD    . MET   B 1 713  ? 170.683 146.691 147.760 1.00 61.52  ? 713  MET   B SD    1 
ATOM   9759  C  CE    . MET   B 1 713  ? 169.771 148.229 147.848 1.00 43.92  ? 713  MET   B CE    1 
ATOM   9760  N  N     . TRP   B 1 714  ? 172.582 146.241 152.028 1.00 44.79  ? 714  TRP   B N     1 
ATOM   9761  C  CA    . TRP   B 1 714  ? 171.837 146.305 153.279 1.00 40.73  ? 714  TRP   B CA    1 
ATOM   9762  C  C     . TRP   B 1 714  ? 172.771 146.535 154.457 1.00 42.96  ? 714  TRP   B C     1 
ATOM   9763  O  O     . TRP   B 1 714  ? 172.422 147.249 155.403 1.00 43.80  ? 714  TRP   B O     1 
ATOM   9764  C  CB    . TRP   B 1 714  ? 171.019 145.031 153.466 1.00 40.77  ? 714  TRP   B CB    1 
ATOM   9765  C  CG    . TRP   B 1 714  ? 170.087 144.785 152.330 1.00 41.63  ? 714  TRP   B CG    1 
ATOM   9766  C  CD1   . TRP   B 1 714  ? 170.080 143.710 151.494 1.00 43.83  ? 714  TRP   B CD1   1 
ATOM   9767  C  CD2   . TRP   B 1 714  ? 169.041 145.652 151.881 1.00 40.15  ? 714  TRP   B CD2   1 
ATOM   9768  N  NE1   . TRP   B 1 714  ? 169.083 143.845 150.560 1.00 46.75  ? 714  TRP   B NE1   1 
ATOM   9769  C  CE2   . TRP   B 1 714  ? 168.431 145.030 150.775 1.00 44.34  ? 714  TRP   B CE2   1 
ATOM   9770  C  CE3   . TRP   B 1 714  ? 168.556 146.890 152.311 1.00 36.84  ? 714  TRP   B CE3   1 
ATOM   9771  C  CZ2   . TRP   B 1 714  ? 167.361 145.603 150.093 1.00 44.54  ? 714  TRP   B CZ2   1 
ATOM   9772  C  CZ3   . TRP   B 1 714  ? 167.494 147.458 151.633 1.00 41.57  ? 714  TRP   B CZ3   1 
ATOM   9773  C  CH2   . TRP   B 1 714  ? 166.908 146.814 150.536 1.00 45.68  ? 714  TRP   B CH2   1 
ATOM   9774  N  N     . ILE   B 1 715  ? 173.968 145.948 154.412 1.00 34.75  ? 715  ILE   B N     1 
ATOM   9775  C  CA    . ILE   B 1 715  ? 174.954 146.203 155.456 1.00 36.45  ? 715  ILE   B CA    1 
ATOM   9776  C  C     . ILE   B 1 715  ? 175.347 147.674 155.466 1.00 34.37  ? 715  ILE   B C     1 
ATOM   9777  O  O     . ILE   B 1 715  ? 175.502 148.281 156.530 1.00 38.98  ? 715  ILE   B O     1 
ATOM   9778  C  CB    . ILE   B 1 715  ? 176.180 145.290 155.273 1.00 38.18  ? 715  ILE   B CB    1 
ATOM   9779  C  CG1   . ILE   B 1 715  ? 175.764 143.819 155.335 1.00 39.32  ? 715  ILE   B CG1   1 
ATOM   9780  C  CG2   . ILE   B 1 715  ? 177.234 145.597 156.327 1.00 33.94  ? 715  ILE   B CG2   1 
ATOM   9781  C  CD1   . ILE   B 1 715  ? 175.829 143.224 156.722 1.00 34.07  ? 715  ILE   B CD1   1 
ATOM   9782  N  N     . SER   B 1 716  ? 175.516 148.271 154.285 1.00 29.66  ? 716  SER   B N     1 
ATOM   9783  C  CA    . SER   B 1 716  ? 175.866 149.688 154.219 1.00 25.59  ? 716  SER   B CA    1 
ATOM   9784  C  C     . SER   B 1 716  ? 174.741 150.566 154.757 1.00 27.28  ? 716  SER   B C     1 
ATOM   9785  O  O     . SER   B 1 716  ? 174.994 151.548 155.466 1.00 35.97  ? 716  SER   B O     1 
ATOM   9786  C  CB    . SER   B 1 716  ? 176.208 150.076 152.782 1.00 29.37  ? 716  SER   B CB    1 
ATOM   9787  O  OG    . SER   B 1 716  ? 177.335 149.357 152.315 1.00 36.26  ? 716  SER   B OG    1 
ATOM   9788  N  N     . LEU   B 1 717  ? 173.492 150.239 154.418 1.00 34.90  ? 717  LEU   B N     1 
ATOM   9789  C  CA    . LEU   B 1 717  ? 172.367 151.002 154.949 1.00 35.56  ? 717  LEU   B CA    1 
ATOM   9790  C  C     . LEU   B 1 717  ? 172.289 150.875 156.465 1.00 40.23  ? 717  LEU   B C     1 
ATOM   9791  O  O     . LEU   B 1 717  ? 172.052 151.864 157.173 1.00 40.82  ? 717  LEU   B O     1 
ATOM   9792  C  CB    . LEU   B 1 717  ? 171.066 150.535 154.297 1.00 32.35  ? 717  LEU   B CB    1 
ATOM   9793  C  CG    . LEU   B 1 717  ? 169.761 151.049 154.904 1.00 38.35  ? 717  LEU   B CG    1 
ATOM   9794  C  CD1   . LEU   B 1 717  ? 169.482 152.471 154.445 1.00 35.09  ? 717  LEU   B CD1   1 
ATOM   9795  C  CD2   . LEU   B 1 717  ? 168.611 150.129 154.537 1.00 36.93  ? 717  LEU   B CD2   1 
ATOM   9796  N  N     . LEU   B 1 718  ? 172.491 149.661 156.982 1.00 35.69  ? 718  LEU   B N     1 
ATOM   9797  C  CA    . LEU   B 1 718  ? 172.514 149.463 158.425 1.00 37.39  ? 718  LEU   B CA    1 
ATOM   9798  C  C     . LEU   B 1 718  ? 173.649 150.249 159.065 1.00 36.86  ? 718  LEU   B C     1 
ATOM   9799  O  O     . LEU   B 1 718  ? 173.499 150.777 160.170 1.00 39.80  ? 718  LEU   B O     1 
ATOM   9800  C  CB    . LEU   B 1 718  ? 172.642 147.975 158.749 1.00 40.27  ? 718  LEU   B CB    1 
ATOM   9801  C  CG    . LEU   B 1 718  ? 173.144 147.632 160.152 1.00 41.12  ? 718  LEU   B CG    1 
ATOM   9802  C  CD1   . LEU   B 1 718  ? 172.008 147.725 161.157 1.00 37.00  ? 718  LEU   B CD1   1 
ATOM   9803  C  CD2   . LEU   B 1 718  ? 173.779 146.252 160.177 1.00 36.98  ? 718  LEU   B CD2   1 
ATOM   9804  N  N     . GLY   B 1 719  ? 174.795 150.330 158.389 1.00 30.33  ? 719  GLY   B N     1 
ATOM   9805  C  CA    . GLY   B 1 719  ? 175.901 151.110 158.918 1.00 38.26  ? 719  GLY   B CA    1 
ATOM   9806  C  C     . GLY   B 1 719  ? 175.592 152.592 158.977 1.00 35.36  ? 719  GLY   B C     1 
ATOM   9807  O  O     . GLY   B 1 719  ? 175.947 153.269 159.942 1.00 35.01  ? 719  GLY   B O     1 
ATOM   9808  N  N     . ALA   B 1 720  ? 174.937 153.120 157.943 1.00 36.50  ? 720  ALA   B N     1 
ATOM   9809  C  CA    . ALA   B 1 720  ? 174.529 154.522 157.980 1.00 35.84  ? 720  ALA   B CA    1 
ATOM   9810  C  C     . ALA   B 1 720  ? 173.529 154.772 159.104 1.00 40.71  ? 720  ALA   B C     1 
ATOM   9811  O  O     . ALA   B 1 720  ? 173.620 155.779 159.824 1.00 41.09  ? 720  ALA   B O     1 
ATOM   9812  C  CB    . ALA   B 1 720  ? 173.941 154.935 156.632 1.00 31.34  ? 720  ALA   B CB    1 
ATOM   9813  N  N     . ILE   B 1 721  ? 172.573 153.857 159.279 1.00 42.81  ? 721  ILE   B N     1 
ATOM   9814  C  CA    . ILE   B 1 721  ? 171.611 153.990 160.368 1.00 39.46  ? 721  ILE   B CA    1 
ATOM   9815  C  C     . ILE   B 1 721  ? 172.325 153.954 161.713 1.00 39.38  ? 721  ILE   B C     1 
ATOM   9816  O  O     . ILE   B 1 721  ? 172.010 154.731 162.622 1.00 40.11  ? 721  ILE   B O     1 
ATOM   9817  C  CB    . ILE   B 1 721  ? 170.532 152.895 160.272 1.00 38.64  ? 721  ILE   B CB    1 
ATOM   9818  C  CG1   . ILE   B 1 721  ? 169.882 152.904 158.888 1.00 36.74  ? 721  ILE   B CG1   1 
ATOM   9819  C  CG2   . ILE   B 1 721  ? 169.482 153.086 161.354 1.00 38.27  ? 721  ILE   B CG2   1 
ATOM   9820  C  CD1   . ILE   B 1 721  ? 168.581 152.139 158.823 1.00 34.48  ? 721  ILE   B CD1   1 
ATOM   9821  N  N     . LEU   B 1 722  ? 173.287 153.044 161.863 1.00 37.63  ? 722  LEU   B N     1 
ATOM   9822  C  CA    . LEU   B 1 722  ? 174.042 152.949 163.106 1.00 31.80  ? 722  LEU   B CA    1 
ATOM   9823  C  C     . LEU   B 1 722  ? 174.851 154.211 163.355 1.00 31.59  ? 722  LEU   B C     1 
ATOM   9824  O  O     . LEU   B 1 722  ? 174.986 154.651 164.499 1.00 42.49  ? 722  LEU   B O     1 
ATOM   9825  C  CB    . LEU   B 1 722  ? 174.956 151.725 163.074 1.00 38.40  ? 722  LEU   B CB    1 
ATOM   9826  C  CG    . LEU   B 1 722  ? 174.264 150.363 163.110 1.00 36.42  ? 722  LEU   B CG    1 
ATOM   9827  C  CD1   . LEU   B 1 722  ? 175.283 149.244 163.020 1.00 37.58  ? 722  LEU   B CD1   1 
ATOM   9828  C  CD2   . LEU   B 1 722  ? 173.435 150.227 164.371 1.00 35.69  ? 722  LEU   B CD2   1 
ATOM   9829  N  N     . CYS   B 1 723  ? 175.415 154.798 162.300 1.00 39.98  ? 723  CYS   B N     1 
ATOM   9830  C  CA    . CYS   B 1 723  ? 176.157 156.043 162.459 1.00 41.48  ? 723  CYS   B CA    1 
ATOM   9831  C  C     . CYS   B 1 723  ? 175.245 157.152 162.961 1.00 40.61  ? 723  CYS   B C     1 
ATOM   9832  O  O     . CYS   B 1 723  ? 175.599 157.897 163.884 1.00 41.24  ? 723  CYS   B O     1 
ATOM   9833  C  CB    . CYS   B 1 723  ? 176.809 156.438 161.134 1.00 35.62  ? 723  CYS   B CB    1 
ATOM   9834  S  SG    . CYS   B 1 723  ? 178.096 155.309 160.567 1.00 51.46  ? 723  CYS   B SG    1 
ATOM   9835  N  N     . CYS   B 1 724  ? 174.053 157.268 162.372 1.00 44.65  ? 724  CYS   B N     1 
ATOM   9836  C  CA    . CYS   B 1 724  ? 173.106 158.279 162.836 1.00 46.16  ? 724  CYS   B CA    1 
ATOM   9837  C  C     . CYS   B 1 724  ? 172.702 158.032 164.286 1.00 46.94  ? 724  CYS   B C     1 
ATOM   9838  O  O     . CYS   B 1 724  ? 172.659 158.965 165.100 1.00 45.97  ? 724  CYS   B O     1 
ATOM   9839  C  CB    . CYS   B 1 724  ? 171.877 158.299 161.928 1.00 43.95  ? 724  CYS   B CB    1 
ATOM   9840  S  SG    . CYS   B 1 724  ? 172.003 159.438 160.530 1.00 60.42  ? 724  CYS   B SG    1 
ATOM   9841  N  N     . ILE   B 1 725  ? 172.417 156.774 164.632 1.00 44.64  ? 725  ILE   B N     1 
ATOM   9842  C  CA    . ILE   B 1 725  ? 171.986 156.452 165.988 1.00 39.43  ? 725  ILE   B CA    1 
ATOM   9843  C  C     . ILE   B 1 725  ? 173.099 156.733 166.988 1.00 43.52  ? 725  ILE   B C     1 
ATOM   9844  O  O     . ILE   B 1 725  ? 172.849 157.244 168.084 1.00 47.20  ? 725  ILE   B O     1 
ATOM   9845  C  CB    . ILE   B 1 725  ? 171.509 154.990 166.064 1.00 41.31  ? 725  ILE   B CB    1 
ATOM   9846  C  CG1   . ILE   B 1 725  ? 170.159 154.834 165.361 1.00 45.68  ? 725  ILE   B CG1   1 
ATOM   9847  C  CG2   . ILE   B 1 725  ? 171.412 154.539 167.510 1.00 45.07  ? 725  ILE   B CG2   1 
ATOM   9848  C  CD1   . ILE   B 1 725  ? 169.759 153.396 165.114 1.00 44.29  ? 725  ILE   B CD1   1 
ATOM   9849  N  N     . VAL   B 1 726  ? 174.340 156.391 166.639 1.00 42.17  ? 726  VAL   B N     1 
ATOM   9850  C  CA    . VAL   B 1 726  ? 175.468 156.636 167.533 1.00 40.83  ? 726  VAL   B CA    1 
ATOM   9851  C  C     . VAL   B 1 726  ? 175.693 158.129 167.711 1.00 43.02  ? 726  VAL   B C     1 
ATOM   9852  O  O     . VAL   B 1 726  ? 175.975 158.600 168.820 1.00 42.82  ? 726  VAL   B O     1 
ATOM   9853  C  CB    . VAL   B 1 726  ? 176.732 155.933 167.006 1.00 34.76  ? 726  VAL   B CB    1 
ATOM   9854  C  CG1   . VAL   B 1 726  ? 177.970 156.536 167.638 1.00 37.66  ? 726  VAL   B CG1   1 
ATOM   9855  C  CG2   . VAL   B 1 726  ? 176.667 154.445 167.295 1.00 38.82  ? 726  VAL   B CG2   1 
ATOM   9856  N  N     . MET   B 1 727  ? 175.581 158.901 166.628 1.00 46.17  ? 727  MET   B N     1 
ATOM   9857  C  CA    . MET   B 1 727  ? 175.769 160.339 166.761 1.00 44.12  ? 727  MET   B CA    1 
ATOM   9858  C  C     . MET   B 1 727  ? 174.669 160.963 167.608 1.00 46.48  ? 727  MET   B C     1 
ATOM   9859  O  O     . MET   B 1 727  ? 174.919 161.941 168.321 1.00 50.95  ? 727  MET   B O     1 
ATOM   9860  C  CB    . MET   B 1 727  ? 175.843 160.994 165.381 1.00 44.23  ? 727  MET   B CB    1 
ATOM   9861  C  CG    . MET   B 1 727  ? 174.624 161.803 164.987 1.00 48.14  ? 727  MET   B CG    1 
ATOM   9862  S  SD    . MET   B 1 727  ? 174.944 162.799 163.519 1.00 59.98  ? 727  MET   B SD    1 
ATOM   9863  C  CE    . MET   B 1 727  ? 174.999 161.527 162.262 1.00 44.24  ? 727  MET   B CE    1 
ATOM   9864  N  N     . PHE   B 1 728  ? 173.453 160.415 167.553 1.00 49.29  ? 728  PHE   B N     1 
ATOM   9865  C  CA    . PHE   B 1 728  ? 172.420 160.853 168.488 1.00 46.80  ? 728  PHE   B CA    1 
ATOM   9866  C  C     . PHE   B 1 728  ? 172.747 160.433 169.917 1.00 47.84  ? 728  PHE   B C     1 
ATOM   9867  O  O     . PHE   B 1 728  ? 172.502 161.189 170.864 1.00 47.36  ? 728  PHE   B O     1 
ATOM   9868  C  CB    . PHE   B 1 728  ? 171.055 160.309 168.071 1.00 43.54  ? 728  PHE   B CB    1 
ATOM   9869  C  CG    . PHE   B 1 728  ? 170.182 161.327 167.402 1.00 49.42  ? 728  PHE   B CG    1 
ATOM   9870  C  CD1   . PHE   B 1 728  ? 170.035 162.591 167.946 1.00 48.14  ? 728  PHE   B CD1   1 
ATOM   9871  C  CD2   . PHE   B 1 728  ? 169.509 161.024 166.234 1.00 50.84  ? 728  PHE   B CD2   1 
ATOM   9872  C  CE1   . PHE   B 1 728  ? 169.233 163.533 167.336 1.00 49.33  ? 728  PHE   B CE1   1 
ATOM   9873  C  CE2   . PHE   B 1 728  ? 168.705 161.962 165.620 1.00 51.48  ? 728  PHE   B CE2   1 
ATOM   9874  C  CZ    . PHE   B 1 728  ? 168.567 163.219 166.172 1.00 52.11  ? 728  PHE   B CZ    1 
ATOM   9875  N  N     . VAL   B 1 729  ? 173.306 159.234 170.089 1.00 49.63  ? 729  VAL   B N     1 
ATOM   9876  C  CA    . VAL   B 1 729  ? 173.549 158.702 171.427 1.00 41.46  ? 729  VAL   B CA    1 
ATOM   9877  C  C     . VAL   B 1 729  ? 174.424 159.654 172.229 1.00 42.39  ? 729  VAL   B C     1 
ATOM   9878  O  O     . VAL   B 1 729  ? 174.184 159.888 173.419 1.00 56.61  ? 729  VAL   B O     1 
ATOM   9879  C  CB    . VAL   B 1 729  ? 174.174 157.297 171.337 1.00 42.44  ? 729  VAL   B CB    1 
ATOM   9880  C  CG1   . VAL   B 1 729  ? 175.012 157.006 172.572 1.00 41.37  ? 729  VAL   B CG1   1 
ATOM   9881  C  CG2   . VAL   B 1 729  ? 173.092 156.246 171.158 1.00 42.26  ? 729  VAL   B CG2   1 
ATOM   9882  N  N     . ILE   B 1 730  ? 175.448 160.215 171.597 1.00 38.58  ? 730  ILE   B N     1 
ATOM   9883  C  CA    . ILE   B 1 730  ? 176.330 161.180 172.238 1.00 39.59  ? 730  ILE   B CA    1 
ATOM   9884  C  C     . ILE   B 1 730  ? 175.907 162.572 171.788 1.00 46.71  ? 730  ILE   B C     1 
ATOM   9885  O  O     . ILE   B 1 730  ? 175.868 162.863 170.586 1.00 55.26  ? 730  ILE   B O     1 
ATOM   9886  C  CB    . ILE   B 1 730  ? 177.806 160.902 171.908 1.00 43.60  ? 730  ILE   B CB    1 
ATOM   9887  C  CG1   . ILE   B 1 730  ? 178.285 161.749 170.728 1.00 46.01  ? 730  ILE   B CG1   1 
ATOM   9888  C  CG2   . ILE   B 1 730  ? 178.003 159.435 171.579 1.00 47.73  ? 730  ILE   B CG2   1 
ATOM   9889  C  CD1   . ILE   B 1 730  ? 179.614 161.306 170.167 1.00 42.36  ? 730  ILE   B CD1   1 
ATOM   9890  N  N     . ASN   B 1 731  ? 175.553 163.425 172.748 1.00 43.92  ? 731  ASN   B N     1 
ATOM   9891  C  CA    . ASN   B 1 731  ? 175.267 164.832 172.481 1.00 42.16  ? 731  ASN   B CA    1 
ATOM   9892  C  C     . ASN   B 1 731  ? 174.143 164.982 171.449 1.00 40.72  ? 731  ASN   B C     1 
ATOM   9893  O  O     . ASN   B 1 731  ? 174.337 165.447 170.325 1.00 47.90  ? 731  ASN   B O     1 
ATOM   9894  C  CB    . ASN   B 1 731  ? 176.540 165.560 172.042 1.00 43.95  ? 731  ASN   B CB    1 
ATOM   9895  C  CG    . ASN   B 1 731  ? 176.749 166.851 172.793 1.00 48.97  ? 731  ASN   B CG    1 
ATOM   9896  O  OD1   . ASN   B 1 731  ? 175.997 167.805 172.622 1.00 48.03  ? 731  ASN   B OD1   1 
ATOM   9897  N  ND2   . ASN   B 1 731  ? 177.756 166.879 173.657 1.00 51.09  ? 731  ASN   B ND2   1 
ATOM   9898  N  N     . TRP   B 1 732  ? 172.951 164.554 171.874 1.00 41.21  ? 732  TRP   B N     1 
ATOM   9899  C  CA    . TRP   B 1 732  ? 171.779 164.583 171.001 1.00 47.89  ? 732  TRP   B CA    1 
ATOM   9900  C  C     . TRP   B 1 732  ? 171.580 165.947 170.346 1.00 46.05  ? 732  TRP   B C     1 
ATOM   9901  O  O     . TRP   B 1 732  ? 171.244 166.029 169.157 1.00 57.55  ? 732  TRP   B O     1 
ATOM   9902  C  CB    . TRP   B 1 732  ? 170.534 164.186 171.799 1.00 50.16  ? 732  TRP   B CB    1 
ATOM   9903  C  CG    . TRP   B 1 732  ? 170.206 165.150 172.903 1.00 52.48  ? 732  TRP   B CG    1 
ATOM   9904  C  CD1   . TRP   B 1 732  ? 170.733 165.163 174.161 1.00 50.77  ? 732  TRP   B CD1   1 
ATOM   9905  C  CD2   . TRP   B 1 732  ? 169.293 166.253 172.841 1.00 52.31  ? 732  TRP   B CD2   1 
ATOM   9906  N  NE1   . TRP   B 1 732  ? 170.200 166.198 174.888 1.00 48.12  ? 732  TRP   B NE1   1 
ATOM   9907  C  CE2   . TRP   B 1 732  ? 169.314 166.884 174.100 1.00 49.76  ? 732  TRP   B CE2   1 
ATOM   9908  C  CE3   . TRP   B 1 732  ? 168.459 166.767 171.844 1.00 49.05  ? 732  TRP   B CE3   1 
ATOM   9909  C  CZ2   . TRP   B 1 732  ? 168.533 167.999 174.389 1.00 50.50  ? 732  TRP   B CZ2   1 
ATOM   9910  C  CZ3   . TRP   B 1 732  ? 167.684 167.874 172.133 1.00 48.36  ? 732  TRP   B CZ3   1 
ATOM   9911  C  CH2   . TRP   B 1 732  ? 167.727 168.478 173.395 1.00 51.54  ? 732  TRP   B CH2   1 
ATOM   9912  N  N     . TRP   B 1 733  ? 171.773 167.032 171.099 1.00 36.34  ? 733  TRP   B N     1 
ATOM   9913  C  CA    . TRP   B 1 733  ? 171.595 168.351 170.501 1.00 41.10  ? 733  TRP   B CA    1 
ATOM   9914  C  C     . TRP   B 1 733  ? 172.679 168.637 169.472 1.00 45.74  ? 733  TRP   B C     1 
ATOM   9915  O  O     . TRP   B 1 733  ? 172.421 169.319 168.474 1.00 51.04  ? 733  TRP   B O     1 
ATOM   9916  C  CB    . TRP   B 1 733  ? 171.572 169.437 171.578 1.00 46.62  ? 733  TRP   B CB    1 
ATOM   9917  C  CG    . TRP   B 1 733  ? 172.862 169.632 172.309 1.00 45.03  ? 733  TRP   B CG    1 
ATOM   9918  C  CD1   . TRP   B 1 733  ? 173.224 169.069 173.497 1.00 47.04  ? 733  TRP   B CD1   1 
ATOM   9919  C  CD2   . TRP   B 1 733  ? 173.949 170.480 171.919 1.00 45.42  ? 733  TRP   B CD2   1 
ATOM   9920  N  NE1   . TRP   B 1 733  ? 174.477 169.499 173.861 1.00 51.11  ? 733  TRP   B NE1   1 
ATOM   9921  C  CE2   . TRP   B 1 733  ? 174.941 170.370 172.911 1.00 48.84  ? 733  TRP   B CE2   1 
ATOM   9922  C  CE3   . TRP   B 1 733  ? 174.181 171.315 170.823 1.00 44.38  ? 733  TRP   B CE3   1 
ATOM   9923  C  CZ2   . TRP   B 1 733  ? 176.149 171.058 172.838 1.00 45.08  ? 733  TRP   B CZ2   1 
ATOM   9924  C  CZ3   . TRP   B 1 733  ? 175.379 172.001 170.754 1.00 44.16  ? 733  TRP   B CZ3   1 
ATOM   9925  C  CH2   . TRP   B 1 733  ? 176.347 171.868 171.755 1.00 44.01  ? 733  TRP   B CH2   1 
ATOM   9926  N  N     . ALA   B 1 734  ? 173.889 168.118 169.689 1.00 51.00  ? 734  ALA   B N     1 
ATOM   9927  C  CA    . ALA   B 1 734  ? 174.924 168.211 168.667 1.00 43.53  ? 734  ALA   B CA    1 
ATOM   9928  C  C     . ALA   B 1 734  ? 174.507 167.480 167.398 1.00 44.15  ? 734  ALA   B C     1 
ATOM   9929  O  O     . ALA   B 1 734  ? 174.754 167.959 166.285 1.00 55.00  ? 734  ALA   B O     1 
ATOM   9930  C  CB    . ALA   B 1 734  ? 176.240 167.650 169.202 1.00 45.10  ? 734  ALA   B CB    1 
ATOM   9931  N  N     . ALA   B 1 735  ? 173.881 166.310 167.545 1.00 38.53  ? 735  ALA   B N     1 
ATOM   9932  C  CA    . ALA   B 1 735  ? 173.395 165.583 166.378 1.00 37.39  ? 735  ALA   B CA    1 
ATOM   9933  C  C     . ALA   B 1 735  ? 172.323 166.376 165.644 1.00 45.74  ? 735  ALA   B C     1 
ATOM   9934  O  O     . ALA   B 1 735  ? 172.320 166.437 164.408 1.00 50.68  ? 735  ALA   B O     1 
ATOM   9935  C  CB    . ALA   B 1 735  ? 172.861 164.214 166.796 1.00 41.24  ? 735  ALA   B CB    1 
ATOM   9936  N  N     . LEU   B 1 736  ? 171.400 166.990 166.385 1.00 48.22  ? 736  LEU   B N     1 
ATOM   9937  C  CA    . LEU   B 1 736  ? 170.380 167.809 165.738 1.00 49.68  ? 736  LEU   B CA    1 
ATOM   9938  C  C     . LEU   B 1 736  ? 171.007 168.992 165.010 1.00 49.58  ? 736  LEU   B C     1 
ATOM   9939  O  O     . LEU   B 1 736  ? 170.606 169.328 163.889 1.00 48.56  ? 736  LEU   B O     1 
ATOM   9940  C  CB    . LEU   B 1 736  ? 169.356 168.285 166.767 1.00 47.12  ? 736  LEU   B CB    1 
ATOM   9941  C  CG    . LEU   B 1 736  ? 168.354 167.227 167.229 1.00 48.12  ? 736  LEU   B CG    1 
ATOM   9942  C  CD1   . LEU   B 1 736  ? 167.385 167.807 168.247 1.00 51.12  ? 736  LEU   B CD1   1 
ATOM   9943  C  CD2   . LEU   B 1 736  ? 167.605 166.651 166.040 1.00 48.53  ? 736  LEU   B CD2   1 
ATOM   9944  N  N     . LEU   B 1 737  ? 172.001 169.632 165.630 1.00 43.64  ? 737  LEU   B N     1 
ATOM   9945  C  CA    . LEU   B 1 737  ? 172.664 170.764 164.992 1.00 45.09  ? 737  LEU   B CA    1 
ATOM   9946  C  C     . LEU   B 1 737  ? 173.376 170.342 163.713 1.00 48.30  ? 737  LEU   B C     1 
ATOM   9947  O  O     . LEU   B 1 737  ? 173.300 171.036 162.692 1.00 51.62  ? 737  LEU   B O     1 
ATOM   9948  C  CB    . LEU   B 1 737  ? 173.650 171.406 165.966 1.00 45.53  ? 737  LEU   B CB    1 
ATOM   9949  C  CG    . LEU   B 1 737  ? 174.555 172.495 165.393 1.00 45.38  ? 737  LEU   B CG    1 
ATOM   9950  C  CD1   . LEU   B 1 737  ? 173.802 173.808 165.270 1.00 47.89  ? 737  LEU   B CD1   1 
ATOM   9951  C  CD2   . LEU   B 1 737  ? 175.799 172.663 166.246 1.00 47.52  ? 737  LEU   B CD2   1 
ATOM   9952  N  N     . THR   B 1 738  ? 174.085 169.211 163.750 1.00 50.80  ? 738  THR   B N     1 
ATOM   9953  C  CA    . THR   B 1 738  ? 174.772 168.741 162.551 1.00 52.85  ? 738  THR   B CA    1 
ATOM   9954  C  C     . THR   B 1 738  ? 173.776 168.379 161.456 1.00 51.15  ? 738  THR   B C     1 
ATOM   9955  O  O     . THR   B 1 738  ? 174.010 168.669 160.277 1.00 50.58  ? 738  THR   B O     1 
ATOM   9956  C  CB    . THR   B 1 738  ? 175.675 167.550 162.878 1.00 50.38  ? 738  THR   B CB    1 
ATOM   9957  O  OG1   . THR   B 1 738  ? 176.447 167.203 161.721 1.00 54.88  ? 738  THR   B OG1   1 
ATOM   9958  C  CG2   . THR   B 1 738  ? 174.856 166.347 163.299 1.00 47.57  ? 738  THR   B CG2   1 
ATOM   9959  N  N     . TYR   B 1 739  ? 172.658 167.746 161.824 1.00 50.80  ? 739  TYR   B N     1 
ATOM   9960  C  CA    . TYR   B 1 739  ? 171.625 167.450 160.838 1.00 49.11  ? 739  TYR   B CA    1 
ATOM   9961  C  C     . TYR   B 1 739  ? 171.099 168.728 160.200 1.00 48.71  ? 739  TYR   B C     1 
ATOM   9962  O  O     . TYR   B 1 739  ? 170.921 168.796 158.977 1.00 50.92  ? 739  TYR   B O     1 
ATOM   9963  C  CB    . TYR   B 1 739  ? 170.482 166.676 161.492 1.00 46.80  ? 739  TYR   B CB    1 
ATOM   9964  C  CG    . TYR   B 1 739  ? 170.807 165.237 161.812 1.00 51.48  ? 739  TYR   B CG    1 
ATOM   9965  C  CD1   . TYR   B 1 739  ? 170.172 164.582 162.858 1.00 53.21  ? 739  TYR   B CD1   1 
ATOM   9966  C  CD2   . TYR   B 1 739  ? 171.742 164.532 161.069 1.00 54.72  ? 739  TYR   B CD2   1 
ATOM   9967  C  CE1   . TYR   B 1 739  ? 170.461 163.266 163.156 1.00 55.05  ? 739  TYR   B CE1   1 
ATOM   9968  C  CE2   . TYR   B 1 739  ? 172.037 163.214 161.360 1.00 52.75  ? 739  TYR   B CE2   1 
ATOM   9969  C  CZ    . TYR   B 1 739  ? 171.394 162.586 162.405 1.00 54.92  ? 739  TYR   B CZ    1 
ATOM   9970  O  OH    . TYR   B 1 739  ? 171.684 161.275 162.699 1.00 53.79  ? 739  TYR   B OH    1 
ATOM   9971  N  N     . VAL   B 1 740  ? 170.841 169.752 161.015 1.00 50.73  ? 740  VAL   B N     1 
ATOM   9972  C  CA    . VAL   B 1 740  ? 170.324 171.011 160.489 1.00 48.39  ? 740  VAL   B CA    1 
ATOM   9973  C  C     . VAL   B 1 740  ? 171.333 171.649 159.545 1.00 53.25  ? 740  VAL   B C     1 
ATOM   9974  O  O     . VAL   B 1 740  ? 170.970 172.158 158.478 1.00 59.38  ? 740  VAL   B O     1 
ATOM   9975  C  CB    . VAL   B 1 740  ? 169.951 171.960 161.643 1.00 50.03  ? 740  VAL   B CB    1 
ATOM   9976  C  CG1   . VAL   B 1 740  ? 170.091 173.408 161.204 1.00 49.38  ? 740  VAL   B CG1   1 
ATOM   9977  C  CG2   . VAL   B 1 740  ? 168.537 171.678 162.125 1.00 52.67  ? 740  VAL   B CG2   1 
ATOM   9978  N  N     . ILE   B 1 741  ? 172.612 171.641 159.923 1.00 50.74  ? 741  ILE   B N     1 
ATOM   9979  C  CA    . ILE   B 1 741  ? 173.640 172.239 159.074 1.00 49.34  ? 741  ILE   B CA    1 
ATOM   9980  C  C     . ILE   B 1 741  ? 173.737 171.492 157.749 1.00 46.04  ? 741  ILE   B C     1 
ATOM   9981  O  O     . ILE   B 1 741  ? 173.832 172.104 156.676 1.00 51.41  ? 741  ILE   B O     1 
ATOM   9982  C  CB    . ILE   B 1 741  ? 174.991 172.264 159.810 1.00 48.82  ? 741  ILE   B CB    1 
ATOM   9983  C  CG1   . ILE   B 1 741  ? 174.881 173.086 161.094 1.00 47.66  ? 741  ILE   B CG1   1 
ATOM   9984  C  CG2   . ILE   B 1 741  ? 176.078 172.829 158.912 1.00 47.57  ? 741  ILE   B CG2   1 
ATOM   9985  C  CD1   . ILE   B 1 741  ? 176.207 173.593 161.608 1.00 46.52  ? 741  ILE   B CD1   1 
ATOM   9986  N  N     . VAL   B 1 742  ? 173.721 170.158 157.802 1.00 45.58  ? 742  VAL   B N     1 
ATOM   9987  C  CA    . VAL   B 1 742  ? 173.803 169.365 156.580 1.00 45.28  ? 742  VAL   B CA    1 
ATOM   9988  C  C     . VAL   B 1 742  ? 172.615 169.660 155.678 1.00 46.51  ? 742  VAL   B C     1 
ATOM   9989  O  O     . VAL   B 1 742  ? 172.768 169.845 154.465 1.00 47.23  ? 742  VAL   B O     1 
ATOM   9990  C  CB    . VAL   B 1 742  ? 173.896 167.865 156.918 1.00 44.73  ? 742  VAL   B CB    1 
ATOM   9991  C  CG1   . VAL   B 1 742  ? 173.435 167.029 155.738 1.00 46.96  ? 742  VAL   B CG1   1 
ATOM   9992  C  CG2   . VAL   B 1 742  ? 175.312 167.494 157.313 1.00 45.29  ? 742  VAL   B CG2   1 
ATOM   9993  N  N     . LEU   B 1 743  ? 171.411 169.707 156.252 1.00 48.61  ? 743  LEU   B N     1 
ATOM   9994  C  CA    . LEU   B 1 743  ? 170.221 169.977 155.452 1.00 49.40  ? 743  LEU   B CA    1 
ATOM   9995  C  C     . LEU   B 1 743  ? 170.271 171.371 154.840 1.00 50.41  ? 743  LEU   B C     1 
ATOM   9996  O  O     . LEU   B 1 743  ? 169.895 171.561 153.678 1.00 59.57  ? 743  LEU   B O     1 
ATOM   9997  C  CB    . LEU   B 1 743  ? 168.967 169.806 156.307 1.00 51.28  ? 743  LEU   B CB    1 
ATOM   9998  C  CG    . LEU   B 1 743  ? 167.637 170.161 155.642 1.00 51.87  ? 743  LEU   B CG    1 
ATOM   9999  C  CD1   . LEU   B 1 743  ? 166.913 168.903 155.191 1.00 50.85  ? 743  LEU   B CD1   1 
ATOM   10000 C  CD2   . LEU   B 1 743  ? 166.768 170.975 156.587 1.00 54.26  ? 743  LEU   B CD2   1 
ATOM   10001 N  N     . GLY   B 1 744  ? 170.726 172.362 155.607 1.00 43.29  ? 744  GLY   B N     1 
ATOM   10002 C  CA    . GLY   B 1 744  ? 170.826 173.708 155.068 1.00 47.29  ? 744  GLY   B CA    1 
ATOM   10003 C  C     . GLY   B 1 744  ? 171.802 173.793 153.912 1.00 49.65  ? 744  GLY   B C     1 
ATOM   10004 O  O     . GLY   B 1 744  ? 171.513 174.406 152.880 1.00 57.53  ? 744  GLY   B O     1 
ATOM   10005 N  N     . LEU   B 1 745  ? 172.975 173.176 154.068 1.00 48.16  ? 745  LEU   B N     1 
ATOM   10006 C  CA    . LEU   B 1 745  ? 173.946 173.177 152.979 1.00 46.98  ? 745  LEU   B CA    1 
ATOM   10007 C  C     . LEU   B 1 745  ? 173.403 172.443 151.760 1.00 51.22  ? 745  LEU   B C     1 
ATOM   10008 O  O     . LEU   B 1 745  ? 173.603 172.880 150.620 1.00 55.14  ? 745  LEU   B O     1 
ATOM   10009 C  CB    . LEU   B 1 745  ? 175.262 172.555 153.442 1.00 47.47  ? 745  LEU   B CB    1 
ATOM   10010 C  CG    . LEU   B 1 745  ? 176.114 173.424 154.368 1.00 50.97  ? 745  LEU   B CG    1 
ATOM   10011 C  CD1   . LEU   B 1 745  ? 177.131 172.577 155.113 1.00 51.32  ? 745  LEU   B CD1   1 
ATOM   10012 C  CD2   . LEU   B 1 745  ? 176.800 174.523 153.579 1.00 52.34  ? 745  LEU   B CD2   1 
ATOM   10013 N  N     . TYR   B 1 746  ? 172.715 171.322 151.982 1.00 44.68  ? 746  TYR   B N     1 
ATOM   10014 C  CA    . TYR   B 1 746  ? 172.124 170.577 150.877 1.00 45.59  ? 746  TYR   B CA    1 
ATOM   10015 C  C     . TYR   B 1 746  ? 171.114 171.430 150.121 1.00 49.79  ? 746  TYR   B C     1 
ATOM   10016 O  O     . TYR   B 1 746  ? 171.114 171.465 148.885 1.00 52.64  ? 746  TYR   B O     1 
ATOM   10017 C  CB    . TYR   B 1 746  ? 171.470 169.303 151.414 1.00 45.95  ? 746  TYR   B CB    1 
ATOM   10018 C  CG    . TYR   B 1 746  ? 170.908 168.383 150.357 1.00 45.58  ? 746  TYR   B CG    1 
ATOM   10019 C  CD1   . TYR   B 1 746  ? 169.634 168.581 149.843 1.00 48.33  ? 746  TYR   B CD1   1 
ATOM   10020 C  CD2   . TYR   B 1 746  ? 171.646 167.310 149.881 1.00 48.53  ? 746  TYR   B CD2   1 
ATOM   10021 C  CE1   . TYR   B 1 746  ? 169.113 167.739 148.882 1.00 50.82  ? 746  TYR   B CE1   1 
ATOM   10022 C  CE2   . TYR   B 1 746  ? 171.135 166.463 148.919 1.00 47.78  ? 746  TYR   B CE2   1 
ATOM   10023 C  CZ    . TYR   B 1 746  ? 169.868 166.682 148.424 1.00 51.34  ? 746  TYR   B CZ    1 
ATOM   10024 O  OH    . TYR   B 1 746  ? 169.356 165.839 147.465 1.00 55.97  ? 746  TYR   B OH    1 
ATOM   10025 N  N     . ILE   B 1 747  ? 170.244 172.131 150.851 1.00 49.51  ? 747  ILE   B N     1 
ATOM   10026 C  CA    . ILE   B 1 747  ? 169.246 172.978 150.204 1.00 48.04  ? 747  ILE   B CA    1 
ATOM   10027 C  C     . ILE   B 1 747  ? 169.920 174.109 149.438 1.00 48.21  ? 747  ILE   B C     1 
ATOM   10028 O  O     . ILE   B 1 747  ? 169.530 174.434 148.309 1.00 52.94  ? 747  ILE   B O     1 
ATOM   10029 C  CB    . ILE   B 1 747  ? 168.243 173.517 151.242 1.00 53.38  ? 747  ILE   B CB    1 
ATOM   10030 C  CG1   . ILE   B 1 747  ? 167.127 172.500 151.497 1.00 54.77  ? 747  ILE   B CG1   1 
ATOM   10031 C  CG2   . ILE   B 1 747  ? 167.658 174.841 150.781 1.00 53.50  ? 747  ILE   B CG2   1 
ATOM   10032 C  CD1   . ILE   B 1 747  ? 167.619 171.132 151.894 1.00 53.91  ? 747  ILE   B CD1   1 
ATOM   10033 N  N     . TYR   B 1 748  ? 170.933 174.735 150.041 1.00 46.67  ? 748  TYR   B N     1 
ATOM   10034 C  CA    . TYR   B 1 748  ? 171.628 175.823 149.362 1.00 50.04  ? 748  TYR   B CA    1 
ATOM   10035 C  C     . TYR   B 1 748  ? 172.274 175.342 148.070 1.00 55.64  ? 748  TYR   B C     1 
ATOM   10036 O  O     . TYR   B 1 748  ? 172.188 176.015 147.036 1.00 59.33  ? 748  TYR   B O     1 
ATOM   10037 C  CB    . TYR   B 1 748  ? 172.674 176.441 150.290 1.00 49.75  ? 748  TYR   B CB    1 
ATOM   10038 C  CG    . TYR   B 1 748  ? 173.543 177.491 149.634 1.00 51.73  ? 748  TYR   B CG    1 
ATOM   10039 C  CD1   . TYR   B 1 748  ? 174.671 177.135 148.905 1.00 53.85  ? 748  TYR   B CD1   1 
ATOM   10040 C  CD2   . TYR   B 1 748  ? 173.230 178.839 149.735 1.00 54.75  ? 748  TYR   B CD2   1 
ATOM   10041 C  CE1   . TYR   B 1 748  ? 175.465 178.090 148.304 1.00 57.88  ? 748  TYR   B CE1   1 
ATOM   10042 C  CE2   . TYR   B 1 748  ? 174.018 179.801 149.136 1.00 59.49  ? 748  TYR   B CE2   1 
ATOM   10043 C  CZ    . TYR   B 1 748  ? 175.134 179.422 148.422 1.00 61.93  ? 748  TYR   B CZ    1 
ATOM   10044 O  OH    . TYR   B 1 748  ? 175.920 180.379 147.825 1.00 61.27  ? 748  TYR   B OH    1 
ATOM   10045 N  N     . VAL   B 1 749  ? 172.926 174.179 148.107 1.00 58.35  ? 749  VAL   B N     1 
ATOM   10046 C  CA    . VAL   B 1 749  ? 173.580 173.664 146.908 1.00 53.65  ? 749  VAL   B CA    1 
ATOM   10047 C  C     . VAL   B 1 749  ? 172.546 173.289 145.854 1.00 56.44  ? 749  VAL   B C     1 
ATOM   10048 O  O     . VAL   B 1 749  ? 172.747 173.529 144.658 1.00 58.79  ? 749  VAL   B O     1 
ATOM   10049 C  CB    . VAL   B 1 749  ? 174.488 172.474 147.260 1.00 54.25  ? 749  VAL   B CB    1 
ATOM   10050 C  CG1   . VAL   B 1 749  ? 174.732 171.617 146.031 1.00 53.77  ? 749  VAL   B CG1   1 
ATOM   10051 C  CG2   . VAL   B 1 749  ? 175.805 172.965 147.837 1.00 54.52  ? 749  VAL   B CG2   1 
ATOM   10052 N  N     . THR   B 1 750  ? 171.429 172.690 146.275 1.00 56.24  ? 750  THR   B N     1 
ATOM   10053 C  CA    . THR   B 1 750  ? 170.389 172.324 145.320 1.00 55.60  ? 750  THR   B CA    1 
ATOM   10054 C  C     . THR   B 1 750  ? 169.814 173.556 144.634 1.00 57.93  ? 750  THR   B C     1 
ATOM   10055 O  O     . THR   B 1 750  ? 169.580 173.547 143.420 1.00 61.24  ? 750  THR   B O     1 
ATOM   10056 C  CB    . THR   B 1 750  ? 169.282 171.539 146.023 1.00 53.89  ? 750  THR   B CB    1 
ATOM   10057 O  OG1   . THR   B 1 750  ? 169.662 170.161 146.124 1.00 57.85  ? 750  THR   B OG1   1 
ATOM   10058 C  CG2   . THR   B 1 750  ? 167.983 171.641 145.245 1.00 54.07  ? 750  THR   B CG2   1 
ATOM   10059 N  N     . TYR   B 1 751  ? 169.579 174.628 145.394 1.00 61.66  ? 751  TYR   B N     1 
ATOM   10060 C  CA    . TYR   B 1 751  ? 169.035 175.841 144.793 1.00 60.68  ? 751  TYR   B CA    1 
ATOM   10061 C  C     . TYR   B 1 751  ? 170.068 176.562 143.938 1.00 59.98  ? 751  TYR   B C     1 
ATOM   10062 O  O     . TYR   B 1 751  ? 169.706 177.204 142.946 1.00 67.62  ? 751  TYR   B O     1 
ATOM   10063 C  CB    . TYR   B 1 751  ? 168.495 176.774 145.875 1.00 62.41  ? 751  TYR   B CB    1 
ATOM   10064 C  CG    . TYR   B 1 751  ? 167.030 176.563 146.180 1.00 68.20  ? 751  TYR   B CG    1 
ATOM   10065 C  CD1   . TYR   B 1 751  ? 166.191 175.952 145.257 1.00 66.05  ? 751  TYR   B CD1   1 
ATOM   10066 C  CD2   . TYR   B 1 751  ? 166.482 176.981 147.385 1.00 65.57  ? 751  TYR   B CD2   1 
ATOM   10067 C  CE1   . TYR   B 1 751  ? 164.851 175.758 145.528 1.00 64.02  ? 751  TYR   B CE1   1 
ATOM   10068 C  CE2   . TYR   B 1 751  ? 165.142 176.792 147.665 1.00 65.90  ? 751  TYR   B CE2   1 
ATOM   10069 C  CZ    . TYR   B 1 751  ? 164.332 176.180 146.733 1.00 67.65  ? 751  TYR   B CZ    1 
ATOM   10070 O  OH    . TYR   B 1 751  ? 162.998 175.991 147.009 1.00 68.18  ? 751  TYR   B OH    1 
ATOM   10071 N  N     . LYS   B 1 752  ? 171.350 176.474 144.299 1.00 53.29  ? 752  LYS   B N     1 
ATOM   10072 C  CA    . LYS   B 1 752  ? 172.379 177.131 143.501 1.00 58.82  ? 752  LYS   B CA    1 
ATOM   10073 C  C     . LYS   B 1 752  ? 172.525 176.482 142.131 1.00 64.18  ? 752  LYS   B C     1 
ATOM   10074 O  O     . LYS   B 1 752  ? 172.924 177.151 141.171 1.00 67.20  ? 752  LYS   B O     1 
ATOM   10075 C  CB    . LYS   B 1 752  ? 173.712 177.115 144.247 1.00 62.02  ? 752  LYS   B CB    1 
ATOM   10076 C  CG    . LYS   B 1 752  ? 174.716 178.137 143.744 1.00 61.05  ? 752  LYS   B CG    1 
ATOM   10077 C  CD    . LYS   B 1 752  ? 174.149 179.545 143.813 1.00 64.09  ? 752  LYS   B CD    1 
ATOM   10078 C  CE    . LYS   B 1 752  ? 173.395 179.778 145.111 1.00 64.09  ? 752  LYS   B CE    1 
ATOM   10079 N  NZ    . LYS   B 1 752  ? 173.313 181.225 145.454 1.00 65.16  ? 752  LYS   B NZ    1 
ATOM   10080 N  N     . LYS   B 1 753  ? 172.205 175.194 142.020 1.00 68.66  ? 753  LYS   B N     1 
ATOM   10081 C  CA    . LYS   B 1 753  ? 172.266 174.479 140.751 1.00 63.87  ? 753  LYS   B CA    1 
ATOM   10082 C  C     . LYS   B 1 753  ? 173.640 174.640 140.113 1.00 66.45  ? 753  LYS   B C     1 
ATOM   10083 O  O     . LYS   B 1 753  ? 173.778 175.344 139.105 1.00 67.73  ? 753  LYS   B O     1 
ATOM   10084 C  CB    . LYS   B 1 753  ? 171.177 174.981 139.802 1.00 63.66  ? 753  LYS   B CB    1 
ATOM   10085 C  CG    . LYS   B 1 753  ? 169.767 174.867 140.359 1.00 65.65  ? 753  LYS   B CG    1 
ATOM   10086 C  CD    . LYS   B 1 753  ? 168.741 174.758 139.244 1.00 68.99  ? 753  LYS   B CD    1 
ATOM   10087 C  CE    . LYS   B 1 753  ? 168.481 173.308 138.872 1.00 69.15  ? 753  LYS   B CE    1 
ATOM   10088 N  NZ    . LYS   B 1 753  ? 169.727 172.601 138.467 1.00 70.02  ? 753  LYS   B NZ    1 
ATOM   10089 N  N     . PRO   B 1 754  ? 174.674 174.010 140.662 1.00 62.79  ? 754  PRO   B N     1 
ATOM   10090 C  CA    . PRO   B 1 754  ? 176.013 174.167 140.087 1.00 59.93  ? 754  PRO   B CA    1 
ATOM   10091 C  C     . PRO   B 1 754  ? 176.109 173.521 138.715 1.00 60.47  ? 754  PRO   B C     1 
ATOM   10092 O  O     . PRO   B 1 754  ? 175.417 172.549 138.405 1.00 62.00  ? 754  PRO   B O     1 
ATOM   10093 C  CB    . PRO   B 1 754  ? 176.932 173.469 141.100 1.00 57.57  ? 754  PRO   B CB    1 
ATOM   10094 C  CG    . PRO   B 1 754  ? 176.038 172.775 142.087 1.00 55.13  ? 754  PRO   B CG    1 
ATOM   10095 C  CD    . PRO   B 1 754  ? 174.613 172.951 141.682 1.00 58.86  ? 754  PRO   B CD    1 
ATOM   10096 N  N     . ASP   B 1 755  ? 176.988 174.083 137.884 1.00 59.00  ? 755  ASP   B N     1 
ATOM   10097 C  CA    . ASP   B 1 755  ? 177.182 173.606 136.515 1.00 57.17  ? 755  ASP   B CA    1 
ATOM   10098 C  C     . ASP   B 1 755  ? 178.263 172.530 136.526 1.00 59.74  ? 755  ASP   B C     1 
ATOM   10099 O  O     . ASP   B 1 755  ? 179.445 172.778 136.280 1.00 63.27  ? 755  ASP   B O     1 
ATOM   10100 C  CB    . ASP   B 1 755  ? 177.541 174.763 135.590 1.00 54.46  ? 755  ASP   B CB    1 
ATOM   10101 N  N     . VAL   B 1 756  ? 177.837 171.303 136.823 1.00 50.61  ? 756  VAL   B N     1 
ATOM   10102 C  CA    . VAL   B 1 756  ? 178.746 170.167 136.906 1.00 49.35  ? 756  VAL   B CA    1 
ATOM   10103 C  C     . VAL   B 1 756  ? 177.960 168.896 136.622 1.00 44.63  ? 756  VAL   B C     1 
ATOM   10104 O  O     . VAL   B 1 756  ? 176.754 168.822 136.868 1.00 49.37  ? 756  VAL   B O     1 
ATOM   10105 C  CB    . VAL   B 1 756  ? 179.444 170.096 138.283 1.00 43.08  ? 756  VAL   B CB    1 
ATOM   10106 C  CG1   . VAL   B 1 756  ? 178.579 169.343 139.282 1.00 43.44  ? 756  VAL   B CG1   1 
ATOM   10107 C  CG2   . VAL   B 1 756  ? 180.813 169.456 138.149 1.00 43.12  ? 756  VAL   B CG2   1 
ATOM   10108 N  N     . ASN   B 1 757  ? 178.657 167.890 136.098 1.00 32.14  ? 757  ASN   B N     1 
ATOM   10109 C  CA    . ASN   B 1 757  ? 178.028 166.620 135.741 1.00 31.78  ? 757  ASN   B CA    1 
ATOM   10110 C  C     . ASN   B 1 757  ? 179.049 165.510 135.944 1.00 34.07  ? 757  ASN   B C     1 
ATOM   10111 O  O     . ASN   B 1 757  ? 180.027 165.426 135.196 1.00 40.43  ? 757  ASN   B O     1 
ATOM   10112 C  CB    . ASN   B 1 757  ? 177.526 166.648 134.300 1.00 34.80  ? 757  ASN   B CB    1 
ATOM   10113 C  CG    . ASN   B 1 757  ? 176.757 165.400 133.924 1.00 37.59  ? 757  ASN   B CG    1 
ATOM   10114 O  OD1   . ASN   B 1 757  ? 176.183 164.726 134.779 1.00 43.93  ? 757  ASN   B OD1   1 
ATOM   10115 N  ND2   . ASN   B 1 757  ? 176.743 165.083 132.636 1.00 33.30  ? 757  ASN   B ND2   1 
ATOM   10116 N  N     . TRP   B 1 758  ? 178.822 164.659 136.946 1.00 28.56  ? 758  TRP   B N     1 
ATOM   10117 C  CA    . TRP   B 1 758  ? 179.721 163.549 137.239 1.00 29.96  ? 758  TRP   B CA    1 
ATOM   10118 C  C     . TRP   B 1 758  ? 179.045 162.188 137.128 1.00 33.85  ? 758  TRP   B C     1 
ATOM   10119 O  O     . TRP   B 1 758  ? 179.675 161.171 137.441 1.00 37.32  ? 758  TRP   B O     1 
ATOM   10120 C  CB    . TRP   B 1 758  ? 180.331 163.697 138.637 1.00 29.54  ? 758  TRP   B CB    1 
ATOM   10121 C  CG    . TRP   B 1 758  ? 181.023 164.999 138.880 1.00 32.07  ? 758  TRP   B CG    1 
ATOM   10122 C  CD1   . TRP   B 1 758  ? 181.899 165.628 138.047 1.00 32.72  ? 758  TRP   B CD1   1 
ATOM   10123 C  CD2   . TRP   B 1 758  ? 180.921 165.818 140.049 1.00 31.98  ? 758  TRP   B CD2   1 
ATOM   10124 N  NE1   . TRP   B 1 758  ? 182.338 166.797 138.618 1.00 35.41  ? 758  TRP   B NE1   1 
ATOM   10125 C  CE2   . TRP   B 1 758  ? 181.753 166.935 139.849 1.00 34.22  ? 758  TRP   B CE2   1 
ATOM   10126 C  CE3   . TRP   B 1 758  ? 180.201 165.719 141.242 1.00 31.75  ? 758  TRP   B CE3   1 
ATOM   10127 C  CZ2   . TRP   B 1 758  ? 181.885 167.946 140.796 1.00 29.49  ? 758  TRP   B CZ2   1 
ATOM   10128 C  CZ3   . TRP   B 1 758  ? 180.333 166.723 142.181 1.00 29.51  ? 758  TRP   B CZ3   1 
ATOM   10129 C  CH2   . TRP   B 1 758  ? 181.168 167.822 141.953 1.00 28.72  ? 758  TRP   B CH2   1 
ATOM   10130 N  N     . GLY   B 1 759  ? 177.791 162.135 136.690 1.00 30.94  ? 759  GLY   B N     1 
ATOM   10131 C  CA    . GLY   B 1 759  ? 177.096 160.867 136.597 1.00 26.80  ? 759  GLY   B CA    1 
ATOM   10132 C  C     . GLY   B 1 759  ? 176.844 160.231 137.947 1.00 32.46  ? 759  GLY   B C     1 
ATOM   10133 O  O     . GLY   B 1 759  ? 177.168 159.060 138.164 1.00 35.36  ? 759  GLY   B O     1 
ATOM   10134 N  N     . SER   B 1 760  ? 176.266 161.000 138.865 1.00 39.03  ? 760  SER   B N     1 
ATOM   10135 C  CA    . SER   B 1 760  ? 176.009 160.518 140.211 1.00 23.43  ? 760  SER   B CA    1 
ATOM   10136 C  C     . SER   B 1 760  ? 174.909 159.458 140.207 1.00 27.28  ? 760  SER   B C     1 
ATOM   10137 O  O     . SER   B 1 760  ? 174.200 159.255 139.218 1.00 41.09  ? 760  SER   B O     1 
ATOM   10138 C  CB    . SER   B 1 760  ? 175.618 161.678 141.123 1.00 33.67  ? 760  SER   B CB    1 
ATOM   10139 O  OG    . SER   B 1 760  ? 174.215 161.875 141.115 1.00 40.84  ? 760  SER   B OG    1 
ATOM   10140 N  N     . SER   B 1 761  ? 174.780 158.768 141.342 1.00 33.06  ? 761  SER   B N     1 
ATOM   10141 C  CA    . SER   B 1 761  ? 173.730 157.769 141.500 1.00 34.16  ? 761  SER   B CA    1 
ATOM   10142 C  C     . SER   B 1 761  ? 172.338 158.388 141.500 1.00 36.88  ? 761  SER   B C     1 
ATOM   10143 O  O     . SER   B 1 761  ? 171.359 157.685 141.229 1.00 42.46  ? 761  SER   B O     1 
ATOM   10144 C  CB    . SER   B 1 761  ? 173.953 156.981 142.792 1.00 29.87  ? 761  SER   B CB    1 
ATOM   10145 O  OG    . SER   B 1 761  ? 173.178 155.797 142.808 1.00 40.42  ? 761  SER   B OG    1 
ATOM   10146 N  N     . THR   B 1 762  ? 172.230 159.685 141.796 1.00 33.41  ? 762  THR   B N     1 
ATOM   10147 C  CA    . THR   B 1 762  ? 170.929 160.344 141.801 1.00 33.89  ? 762  THR   B CA    1 
ATOM   10148 C  C     . THR   B 1 762  ? 170.298 160.341 140.414 1.00 36.55  ? 762  THR   B C     1 
ATOM   10149 O  O     . THR   B 1 762  ? 169.095 160.103 140.272 1.00 37.86  ? 762  THR   B O     1 
ATOM   10150 C  CB    . THR   B 1 762  ? 171.072 161.776 142.318 1.00 34.24  ? 762  THR   B CB    1 
ATOM   10151 O  OG1   . THR   B 1 762  ? 171.305 161.752 143.731 1.00 33.29  ? 762  THR   B OG1   1 
ATOM   10152 C  CG2   . THR   B 1 762  ? 169.814 162.577 142.031 1.00 38.96  ? 762  THR   B CG2   1 
ATOM   10153 N  N     . GLN   B 1 763  ? 171.094 160.616 139.380 1.00 25.50  ? 763  GLN   B N     1 
ATOM   10154 C  CA    . GLN   B 1 763  ? 170.569 160.629 138.018 1.00 24.06  ? 763  GLN   B CA    1 
ATOM   10155 C  C     . GLN   B 1 763  ? 170.131 159.235 137.579 1.00 29.05  ? 763  GLN   B C     1 
ATOM   10156 O  O     . GLN   B 1 763  ? 169.065 159.069 136.967 1.00 39.01  ? 763  GLN   B O     1 
ATOM   10157 C  CB    . GLN   B 1 763  ? 171.630 161.190 137.076 1.00 27.69  ? 763  GLN   B CB    1 
ATOM   10158 C  CG    . GLN   B 1 763  ? 172.597 162.137 137.771 1.00 23.03  ? 763  GLN   B CG    1 
ATOM   10159 C  CD    . GLN   B 1 763  ? 173.515 162.861 136.809 1.00 34.84  ? 763  GLN   B CD    1 
ATOM   10160 O  OE1   . GLN   B 1 763  ? 173.492 162.615 135.604 1.00 41.63  ? 763  GLN   B OE1   1 
ATOM   10161 N  NE2   . GLN   B 1 763  ? 174.337 163.756 137.342 1.00 32.42  ? 763  GLN   B NE2   1 
ATOM   10162 N  N     . ALA   B 1 764  ? 170.945 158.222 137.880 1.00 16.33  ? 764  ALA   B N     1 
ATOM   10163 C  CA    . ALA   B 1 764  ? 170.559 156.851 137.576 1.00 22.18  ? 764  ALA   B CA    1 
ATOM   10164 C  C     . ALA   B 1 764  ? 169.267 156.478 138.289 1.00 25.63  ? 764  ALA   B C     1 
ATOM   10165 O  O     . ALA   B 1 764  ? 168.396 155.816 137.712 1.00 36.56  ? 764  ALA   B O     1 
ATOM   10166 C  CB    . ALA   B 1 764  ? 171.685 155.892 137.959 1.00 16.88  ? 764  ALA   B CB    1 
ATOM   10167 N  N     . LEU   B 1 765  ? 169.126 156.897 139.548 1.00 23.97  ? 765  LEU   B N     1 
ATOM   10168 C  CA    . LEU   B 1 765  ? 167.905 156.604 140.289 1.00 24.90  ? 765  LEU   B CA    1 
ATOM   10169 C  C     . LEU   B 1 765  ? 166.711 157.337 139.693 1.00 26.10  ? 765  LEU   B C     1 
ATOM   10170 O  O     . LEU   B 1 765  ? 165.600 156.802 139.671 1.00 27.29  ? 765  LEU   B O     1 
ATOM   10171 C  CB    . LEU   B 1 765  ? 168.083 156.973 141.761 1.00 28.10  ? 765  LEU   B CB    1 
ATOM   10172 C  CG    . LEU   B 1 765  ? 166.854 156.795 142.652 1.00 26.96  ? 765  LEU   B CG    1 
ATOM   10173 C  CD1   . LEU   B 1 765  ? 166.847 155.416 143.292 1.00 26.37  ? 765  LEU   B CD1   1 
ATOM   10174 C  CD2   . LEU   B 1 765  ? 166.802 157.884 143.708 1.00 29.56  ? 765  LEU   B CD2   1 
ATOM   10175 N  N     . THR   B 1 766  ? 166.915 158.565 139.218 1.00 21.62  ? 766  THR   B N     1 
ATOM   10176 C  CA    . THR   B 1 766  ? 165.846 159.284 138.533 1.00 22.16  ? 766  THR   B CA    1 
ATOM   10177 C  C     . THR   B 1 766  ? 165.368 158.503 137.316 1.00 20.92  ? 766  THR   B C     1 
ATOM   10178 O  O     . THR   B 1 766  ? 164.160 158.314 137.110 1.00 27.66  ? 766  THR   B O     1 
ATOM   10179 C  CB    . THR   B 1 766  ? 166.334 160.675 138.123 1.00 13.42  ? 766  THR   B CB    1 
ATOM   10180 O  OG1   . THR   B 1 766  ? 166.956 161.315 139.244 1.00 26.65  ? 766  THR   B OG1   1 
ATOM   10181 C  CG2   . THR   B 1 766  ? 165.178 161.533 137.637 1.00 19.56  ? 766  THR   B CG2   1 
ATOM   10182 N  N     . TYR   B 1 767  ? 166.313 158.027 136.503 1.00 22.39  ? 767  TYR   B N     1 
ATOM   10183 C  CA    . TYR   B 1 767  ? 165.940 157.239 135.333 1.00 15.01  ? 767  TYR   B CA    1 
ATOM   10184 C  C     . TYR   B 1 767  ? 165.187 155.980 135.742 1.00 18.58  ? 767  TYR   B C     1 
ATOM   10185 O  O     . TYR   B 1 767  ? 164.160 155.634 135.147 1.00 29.99  ? 767  TYR   B O     1 
ATOM   10186 C  CB    . TYR   B 1 767  ? 167.177 156.872 134.510 1.00 14.43  ? 767  TYR   B CB    1 
ATOM   10187 C  CG    . TYR   B 1 767  ? 166.862 155.955 133.346 1.00 17.62  ? 767  TYR   B CG    1 
ATOM   10188 C  CD1   . TYR   B 1 767  ? 166.771 154.580 133.520 1.00 18.06  ? 767  TYR   B CD1   1 
ATOM   10189 C  CD2   . TYR   B 1 767  ? 166.639 156.467 132.076 1.00 19.94  ? 767  TYR   B CD2   1 
ATOM   10190 C  CE1   . TYR   B 1 767  ? 166.472 153.744 132.465 1.00 14.04  ? 767  TYR   B CE1   1 
ATOM   10191 C  CE2   . TYR   B 1 767  ? 166.342 155.637 131.013 1.00 15.38  ? 767  TYR   B CE2   1 
ATOM   10192 C  CZ    . TYR   B 1 767  ? 166.260 154.277 131.215 1.00 16.46  ? 767  TYR   B CZ    1 
ATOM   10193 O  OH    . TYR   B 1 767  ? 165.966 153.443 130.163 1.00 28.29  ? 767  TYR   B OH    1 
ATOM   10194 N  N     . LEU   B 1 768  ? 165.701 155.267 136.746 1.00 13.30  ? 768  LEU   B N     1 
ATOM   10195 C  CA    . LEU   B 1 768  ? 165.073 154.013 137.147 1.00 19.50  ? 768  LEU   B CA    1 
ATOM   10196 C  C     . LEU   B 1 768  ? 163.672 154.250 137.696 1.00 27.27  ? 768  LEU   B C     1 
ATOM   10197 O  O     . LEU   B 1 768  ? 162.755 153.464 137.438 1.00 27.56  ? 768  LEU   B O     1 
ATOM   10198 C  CB    . LEU   B 1 768  ? 165.942 153.293 138.176 1.00 20.60  ? 768  LEU   B CB    1 
ATOM   10199 C  CG    . LEU   B 1 768  ? 165.584 151.825 138.404 1.00 26.70  ? 768  LEU   B CG    1 
ATOM   10200 C  CD1   . LEU   B 1 768  ? 166.006 150.988 137.207 1.00 23.99  ? 768  LEU   B CD1   1 
ATOM   10201 C  CD2   . LEU   B 1 768  ? 166.223 151.304 139.675 1.00 28.84  ? 768  LEU   B CD2   1 
ATOM   10202 N  N     . ASN   B 1 769  ? 163.490 155.327 138.462 1.00 22.21  ? 769  ASN   B N     1 
ATOM   10203 C  CA    . ASN   B 1 769  ? 162.170 155.659 138.983 1.00 19.13  ? 769  ASN   B CA    1 
ATOM   10204 C  C     . ASN   B 1 769  ? 161.200 155.947 137.849 1.00 30.09  ? 769  ASN   B C     1 
ATOM   10205 O  O     . ASN   B 1 769  ? 160.067 155.448 137.842 1.00 30.34  ? 769  ASN   B O     1 
ATOM   10206 C  CB    . ASN   B 1 769  ? 162.265 156.860 139.924 1.00 22.95  ? 769  ASN   B CB    1 
ATOM   10207 C  CG    . ASN   B 1 769  ? 162.697 156.472 141.321 1.00 35.82  ? 769  ASN   B CG    1 
ATOM   10208 O  OD1   . ASN   B 1 769  ? 162.561 155.319 141.727 1.00 35.78  ? 769  ASN   B OD1   1 
ATOM   10209 N  ND2   . ASN   B 1 769  ? 163.218 157.438 142.069 1.00 33.64  ? 769  ASN   B ND2   1 
ATOM   10210 N  N     . ALA   B 1 770  ? 161.627 156.758 136.878 1.00 25.29  ? 770  ALA   B N     1 
ATOM   10211 C  CA    . ALA   B 1 770  ? 160.754 157.050 135.747 1.00 16.44  ? 770  ALA   B CA    1 
ATOM   10212 C  C     . ALA   B 1 770  ? 160.386 155.775 135.000 1.00 19.42  ? 770  ALA   B C     1 
ATOM   10213 O  O     . ALA   B 1 770  ? 159.222 155.573 134.632 1.00 18.26  ? 770  ALA   B O     1 
ATOM   10214 C  CB    . ALA   B 1 770  ? 161.422 158.054 134.810 1.00 10.96  ? 770  ALA   B CB    1 
ATOM   10215 N  N     . LEU   B 1 771  ? 161.363 154.894 134.780 1.00 14.37  ? 771  LEU   B N     1 
ATOM   10216 C  CA    . LEU   B 1 771  ? 161.092 153.667 134.040 1.00 17.98  ? 771  LEU   B CA    1 
ATOM   10217 C  C     . LEU   B 1 771  ? 160.131 152.759 134.800 1.00 15.44  ? 771  LEU   B C     1 
ATOM   10218 O  O     . LEU   B 1 771  ? 159.211 152.186 134.206 1.00 22.37  ? 771  LEU   B O     1 
ATOM   10219 C  CB    . LEU   B 1 771  ? 162.399 152.936 133.736 1.00 24.50  ? 771  LEU   B CB    1 
ATOM   10220 C  CG    . LEU   B 1 771  ? 162.265 151.459 133.366 1.00 22.52  ? 771  LEU   B CG    1 
ATOM   10221 C  CD1   . LEU   B 1 771  ? 161.917 151.316 131.895 1.00 16.58  ? 771  LEU   B CD1   1 
ATOM   10222 C  CD2   . LEU   B 1 771  ? 163.540 150.703 133.690 1.00 22.36  ? 771  LEU   B CD2   1 
ATOM   10223 N  N     . GLN   B 1 772  ? 160.327 152.614 136.112 1.00 19.84  ? 772  GLN   B N     1 
ATOM   10224 C  CA    . GLN   B 1 772  ? 159.442 151.761 136.896 1.00 22.45  ? 772  GLN   B CA    1 
ATOM   10225 C  C     . GLN   B 1 772  ? 158.027 152.323 136.939 1.00 28.29  ? 772  GLN   B C     1 
ATOM   10226 O  O     . GLN   B 1 772  ? 157.050 151.570 136.844 1.00 30.43  ? 772  GLN   B O     1 
ATOM   10227 C  CB    . GLN   B 1 772  ? 160.001 151.582 138.308 1.00 27.72  ? 772  GLN   B CB    1 
ATOM   10228 C  CG    . GLN   B 1 772  ? 160.626 150.216 138.547 1.00 32.98  ? 772  GLN   B CG    1 
ATOM   10229 C  CD    . GLN   B 1 772  ? 161.849 150.274 139.441 1.00 44.55  ? 772  GLN   B CD    1 
ATOM   10230 O  OE1   . GLN   B 1 772  ? 162.075 151.259 140.144 1.00 40.85  ? 772  GLN   B OE1   1 
ATOM   10231 N  NE2   . GLN   B 1 772  ? 162.652 149.217 139.411 1.00 43.63  ? 772  GLN   B NE2   1 
ATOM   10232 N  N     . HIS   B 1 773  ? 157.892 153.642 137.075 1.00 29.02  ? 773  HIS   B N     1 
ATOM   10233 C  CA    . HIS   B 1 773  ? 156.563 154.242 137.082 1.00 19.53  ? 773  HIS   B CA    1 
ATOM   10234 C  C     . HIS   B 1 773  ? 155.879 154.085 135.729 1.00 26.15  ? 773  HIS   B C     1 
ATOM   10235 O  O     . HIS   B 1 773  ? 154.670 153.829 135.665 1.00 29.28  ? 773  HIS   B O     1 
ATOM   10236 C  CB    . HIS   B 1 773  ? 156.661 155.709 137.490 1.00 16.96  ? 773  HIS   B CB    1 
ATOM   10237 C  CG    . HIS   B 1 773  ? 156.726 155.910 138.972 1.00 25.85  ? 773  HIS   B CG    1 
ATOM   10238 N  ND1   . HIS   B 1 773  ? 157.917 156.044 139.652 1.00 31.16  ? 773  HIS   B ND1   1 
ATOM   10239 C  CD2   . HIS   B 1 773  ? 155.749 155.989 139.905 1.00 23.60  ? 773  HIS   B CD2   1 
ATOM   10240 C  CE1   . HIS   B 1 773  ? 157.670 156.196 140.941 1.00 25.31  ? 773  HIS   B CE1   1 
ATOM   10241 N  NE2   . HIS   B 1 773  ? 156.362 156.171 141.120 1.00 23.82  ? 773  HIS   B NE2   1 
ATOM   10242 N  N     . SER   B 1 774  ? 156.632 154.227 134.636 1.00 27.28  ? 774  SER   B N     1 
ATOM   10243 C  CA    . SER   B 1 774  ? 156.056 153.998 133.316 1.00 15.71  ? 774  SER   B CA    1 
ATOM   10244 C  C     . SER   B 1 774  ? 155.614 152.549 133.152 1.00 15.52  ? 774  SER   B C     1 
ATOM   10245 O  O     . SER   B 1 774  ? 154.551 152.275 132.583 1.00 27.50  ? 774  SER   B O     1 
ATOM   10246 C  CB    . SER   B 1 774  ? 157.062 154.377 132.230 1.00 23.03  ? 774  SER   B CB    1 
ATOM   10247 O  OG    . SER   B 1 774  ? 157.053 155.773 131.988 1.00 35.03  ? 774  SER   B OG    1 
ATOM   10248 N  N     . ILE   B 1 775  ? 156.419 151.606 133.644 1.00 21.05  ? 775  ILE   B N     1 
ATOM   10249 C  CA    . ILE   B 1 775  ? 156.054 150.196 133.537 1.00 18.08  ? 775  ILE   B CA    1 
ATOM   10250 C  C     . ILE   B 1 775  ? 154.800 149.911 134.350 1.00 25.99  ? 775  ILE   B C     1 
ATOM   10251 O  O     . ILE   B 1 775  ? 153.943 149.118 133.942 1.00 30.45  ? 775  ILE   B O     1 
ATOM   10252 C  CB    . ILE   B 1 775  ? 157.229 149.303 133.973 1.00 24.46  ? 775  ILE   B CB    1 
ATOM   10253 C  CG1   . ILE   B 1 775  ? 158.137 149.005 132.780 1.00 23.50  ? 775  ILE   B CG1   1 
ATOM   10254 C  CG2   . ILE   B 1 775  ? 156.716 148.009 134.580 1.00 22.10  ? 775  ILE   B CG2   1 
ATOM   10255 C  CD1   . ILE   B 1 775  ? 159.463 148.389 133.158 1.00 22.58  ? 775  ILE   B CD1   1 
ATOM   10256 N  N     . ARG   B 1 776  ? 154.674 150.545 135.517 1.00 32.61  ? 776  ARG   B N     1 
ATOM   10257 C  CA    . ARG   B 1 776  ? 153.443 150.423 136.292 1.00 27.94  ? 776  ARG   B CA    1 
ATOM   10258 C  C     . ARG   B 1 776  ? 152.253 150.959 135.506 1.00 29.73  ? 776  ARG   B C     1 
ATOM   10259 O  O     . ARG   B 1 776  ? 151.220 150.292 135.384 1.00 29.54  ? 776  ARG   B O     1 
ATOM   10260 C  CB    . ARG   B 1 776  ? 153.577 151.167 137.622 1.00 27.21  ? 776  ARG   B CB    1 
ATOM   10261 C  CG    . ARG   B 1 776  ? 154.337 150.421 138.705 1.00 31.12  ? 776  ARG   B CG    1 
ATOM   10262 C  CD    . ARG   B 1 776  ? 153.926 150.911 140.087 1.00 36.21  ? 776  ARG   B CD    1 
ATOM   10263 N  NE    . ARG   B 1 776  ? 154.683 152.085 140.503 1.00 41.90  ? 776  ARG   B NE    1 
ATOM   10264 C  CZ    . ARG   B 1 776  ? 155.962 152.070 140.851 1.00 42.36  ? 776  ARG   B CZ    1 
ATOM   10265 N  NH1   . ARG   B 1 776  ? 156.665 150.949 140.852 1.00 42.99  ? 776  ARG   B NH1   1 
ATOM   10266 N  NH2   . ARG   B 1 776  ? 156.551 153.207 141.209 1.00 38.33  ? 776  ARG   B NH2   1 
ATOM   10267 N  N     . LEU   B 1 777  ? 152.387 152.171 134.962 1.00 25.80  ? 777  LEU   B N     1 
ATOM   10268 C  CA    . LEU   B 1 777  ? 151.282 152.785 134.234 1.00 18.14  ? 777  LEU   B CA    1 
ATOM   10269 C  C     . LEU   B 1 777  ? 150.885 151.970 133.012 1.00 21.45  ? 777  LEU   B C     1 
ATOM   10270 O  O     . LEU   B 1 777  ? 149.719 151.992 132.604 1.00 26.80  ? 777  LEU   B O     1 
ATOM   10271 C  CB    . LEU   B 1 777  ? 151.654 154.208 133.820 1.00 20.40  ? 777  LEU   B CB    1 
ATOM   10272 C  CG    . LEU   B 1 777  ? 150.774 154.845 132.744 1.00 17.80  ? 777  LEU   B CG    1 
ATOM   10273 C  CD1   . LEU   B 1 777  ? 149.411 155.213 133.311 1.00 17.65  ? 777  LEU   B CD1   1 
ATOM   10274 C  CD2   . LEU   B 1 777  ? 151.455 156.061 132.142 1.00 19.44  ? 777  LEU   B CD2   1 
ATOM   10275 N  N     . SER   B 1 778  ? 151.833 151.247 132.415 1.00 31.72  ? 778  SER   B N     1 
ATOM   10276 C  CA    . SER   B 1 778  ? 151.526 150.463 131.224 1.00 28.27  ? 778  SER   B CA    1 
ATOM   10277 C  C     . SER   B 1 778  ? 150.527 149.347 131.492 1.00 27.92  ? 778  SER   B C     1 
ATOM   10278 O  O     . SER   B 1 778  ? 149.958 148.807 130.537 1.00 31.27  ? 778  SER   B O     1 
ATOM   10279 C  CB    . SER   B 1 778  ? 152.809 149.872 130.639 1.00 27.41  ? 778  SER   B CB    1 
ATOM   10280 O  OG    . SER   B 1 778  ? 153.104 148.616 131.223 1.00 32.78  ? 778  SER   B OG    1 
ATOM   10281 N  N     . GLY   B 1 779  ? 150.300 148.989 132.752 1.00 26.55  ? 779  GLY   B N     1 
ATOM   10282 C  CA    . GLY   B 1 779  ? 149.347 147.964 133.119 1.00 32.32  ? 779  GLY   B CA    1 
ATOM   10283 C  C     . GLY   B 1 779  ? 148.000 148.468 133.587 1.00 39.66  ? 779  GLY   B C     1 
ATOM   10284 O  O     . GLY   B 1 779  ? 147.218 147.678 134.129 1.00 40.15  ? 779  GLY   B O     1 
ATOM   10285 N  N     . VAL   B 1 780  ? 147.697 149.748 133.394 1.00 34.75  ? 780  VAL   B N     1 
ATOM   10286 C  CA    . VAL   B 1 780  ? 146.458 150.351 133.873 1.00 25.77  ? 780  VAL   B CA    1 
ATOM   10287 C  C     . VAL   B 1 780  ? 145.492 150.461 132.702 1.00 35.89  ? 780  VAL   B C     1 
ATOM   10288 O  O     . VAL   B 1 780  ? 145.825 151.043 131.664 1.00 38.72  ? 780  VAL   B O     1 
ATOM   10289 C  CB    . VAL   B 1 780  ? 146.715 151.726 134.506 1.00 24.90  ? 780  VAL   B CB    1 
ATOM   10290 C  CG1   . VAL   B 1 780  ? 145.443 152.560 134.501 1.00 27.49  ? 780  VAL   B CG1   1 
ATOM   10291 C  CG2   . VAL   B 1 780  ? 147.251 151.566 135.915 1.00 30.57  ? 780  VAL   B CG2   1 
ATOM   10292 N  N     . GLU   B 1 781  ? 144.294 149.907 132.869 1.00 41.05  ? 781  GLU   B N     1 
ATOM   10293 C  CA    . GLU   B 1 781  ? 143.282 149.978 131.827 1.00 37.14  ? 781  GLU   B CA    1 
ATOM   10294 C  C     . GLU   B 1 781  ? 142.744 151.400 131.699 1.00 33.58  ? 781  GLU   B C     1 
ATOM   10295 O  O     . GLU   B 1 781  ? 142.799 152.204 132.634 1.00 36.84  ? 781  GLU   B O     1 
ATOM   10296 C  CB    . GLU   B 1 781  ? 142.139 149.006 132.121 1.00 31.98  ? 781  GLU   B CB    1 
ATOM   10297 N  N     . ASP   B 1 782  ? 142.214 151.706 130.519 1.00 39.02  ? 782  ASP   B N     1 
ATOM   10298 C  CA    . ASP   B 1 782  ? 141.729 153.045 130.217 1.00 38.56  ? 782  ASP   B CA    1 
ATOM   10299 C  C     . ASP   B 1 782  ? 140.248 153.171 130.545 1.00 43.81  ? 782  ASP   B C     1 
ATOM   10300 O  O     . ASP   B 1 782  ? 139.452 152.276 130.248 1.00 45.39  ? 782  ASP   B O     1 
ATOM   10301 C  CB    . ASP   B 1 782  ? 141.964 153.386 128.745 1.00 45.01  ? 782  ASP   B CB    1 
ATOM   10302 C  CG    . ASP   B 1 782  ? 142.343 154.838 128.539 1.00 52.57  ? 782  ASP   B CG    1 
ATOM   10303 O  OD1   . ASP   B 1 782  ? 141.946 155.678 129.374 1.00 48.16  ? 782  ASP   B OD1   1 
ATOM   10304 O  OD2   . ASP   B 1 782  ? 143.036 155.140 127.545 1.00 51.78  ? 782  ASP   B OD2   1 
ATOM   10305 N  N     . HIS   B 1 783  ? 139.887 154.295 131.159 1.00 34.02  ? 783  HIS   B N     1 
ATOM   10306 C  CA    . HIS   B 1 783  ? 138.509 154.589 131.515 1.00 24.12  ? 783  HIS   B CA    1 
ATOM   10307 C  C     . HIS   B 1 783  ? 138.177 156.017 131.109 1.00 28.60  ? 783  HIS   B C     1 
ATOM   10308 O  O     . HIS   B 1 783  ? 139.044 156.894 131.102 1.00 34.84  ? 783  HIS   B O     1 
ATOM   10309 C  CB    . HIS   B 1 783  ? 138.261 154.398 133.019 1.00 27.38  ? 783  HIS   B CB    1 
ATOM   10310 C  CG    . HIS   B 1 783  ? 136.827 154.147 133.367 1.00 34.27  ? 783  HIS   B CG    1 
ATOM   10311 N  ND1   . HIS   B 1 783  ? 135.907 155.163 133.508 1.00 26.26  ? 783  HIS   B ND1   1 
ATOM   10312 C  CD2   . HIS   B 1 783  ? 136.155 152.996 133.600 1.00 34.73  ? 783  HIS   B CD2   1 
ATOM   10313 C  CE1   . HIS   B 1 783  ? 134.730 154.648 133.813 1.00 25.76  ? 783  HIS   B CE1   1 
ATOM   10314 N  NE2   . HIS   B 1 783  ? 134.853 153.335 133.875 1.00 29.05  ? 783  HIS   B NE2   1 
ATOM   10315 N  N     . VAL   B 1 784  ? 136.906 156.240 130.768 1.00 23.65  ? 784  VAL   B N     1 
ATOM   10316 C  CA    . VAL   B 1 784  ? 136.477 157.565 130.331 1.00 22.56  ? 784  VAL   B CA    1 
ATOM   10317 C  C     . VAL   B 1 784  ? 136.666 158.581 131.450 1.00 27.48  ? 784  VAL   B C     1 
ATOM   10318 O  O     . VAL   B 1 784  ? 136.997 159.746 131.202 1.00 29.54  ? 784  VAL   B O     1 
ATOM   10319 C  CB    . VAL   B 1 784  ? 135.017 157.523 129.846 1.00 28.27  ? 784  VAL   B CB    1 
ATOM   10320 C  CG1   . VAL   B 1 784  ? 134.136 156.836 130.877 1.00 30.90  ? 784  VAL   B CG1   1 
ATOM   10321 C  CG2   . VAL   B 1 784  ? 134.512 158.927 129.560 1.00 24.39  ? 784  VAL   B CG2   1 
ATOM   10322 N  N     . LYS   B 1 785  ? 136.452 158.159 132.698 1.00 29.21  ? 785  LYS   B N     1 
ATOM   10323 C  CA    . LYS   B 1 785  ? 136.641 159.066 133.824 1.00 27.17  ? 785  LYS   B CA    1 
ATOM   10324 C  C     . LYS   B 1 785  ? 138.085 159.534 133.926 1.00 27.13  ? 785  LYS   B C     1 
ATOM   10325 O  O     . LYS   B 1 785  ? 138.349 160.628 134.436 1.00 31.71  ? 785  LYS   B O     1 
ATOM   10326 C  CB    . LYS   B 1 785  ? 136.219 158.386 135.126 1.00 23.70  ? 785  LYS   B CB    1 
ATOM   10327 C  CG    . LYS   B 1 785  ? 134.719 158.335 135.347 1.00 34.55  ? 785  LYS   B CG    1 
ATOM   10328 C  CD    . LYS   B 1 785  ? 134.363 157.488 136.557 1.00 27.68  ? 785  LYS   B CD    1 
ATOM   10329 C  CE    . LYS   B 1 785  ? 134.737 158.190 137.850 1.00 28.25  ? 785  LYS   B CE    1 
ATOM   10330 N  NZ    . LYS   B 1 785  ? 135.180 157.231 138.899 1.00 34.84  ? 785  LYS   B NZ    1 
ATOM   10331 N  N     . ASN   B 1 786  ? 139.028 158.726 133.448 1.00 24.23  ? 786  ASN   B N     1 
ATOM   10332 C  CA    . ASN   B 1 786  ? 140.448 159.011 133.574 1.00 22.16  ? 786  ASN   B CA    1 
ATOM   10333 C  C     . ASN   B 1 786  ? 141.063 159.552 132.291 1.00 23.79  ? 786  ASN   B C     1 
ATOM   10334 O  O     . ASN   B 1 786  ? 142.291 159.636 132.195 1.00 35.87  ? 786  ASN   B O     1 
ATOM   10335 C  CB    . ASN   B 1 786  ? 141.193 157.752 134.020 1.00 20.02  ? 786  ASN   B CB    1 
ATOM   10336 C  CG    . ASN   B 1 786  ? 141.102 157.522 135.514 1.00 25.73  ? 786  ASN   B CG    1 
ATOM   10337 O  OD1   . ASN   B 1 786  ? 141.040 158.470 136.296 1.00 28.46  ? 786  ASN   B OD1   1 
ATOM   10338 N  ND2   . ASN   B 1 786  ? 141.093 156.258 135.918 1.00 28.12  ? 786  ASN   B ND2   1 
ATOM   10339 N  N     . PHE   B 1 787  ? 140.249 159.918 131.304 1.00 22.70  ? 787  PHE   B N     1 
ATOM   10340 C  CA    . PHE   B 1 787  ? 140.796 160.466 130.071 1.00 19.76  ? 787  PHE   B CA    1 
ATOM   10341 C  C     . PHE   B 1 787  ? 141.521 161.777 130.341 1.00 19.45  ? 787  PHE   B C     1 
ATOM   10342 O  O     . PHE   B 1 787  ? 141.032 162.640 131.074 1.00 25.50  ? 787  PHE   B O     1 
ATOM   10343 C  CB    . PHE   B 1 787  ? 139.690 160.692 129.038 1.00 14.97  ? 787  PHE   B CB    1 
ATOM   10344 C  CG    . PHE   B 1 787  ? 140.127 161.521 127.861 1.00 18.91  ? 787  PHE   B CG    1 
ATOM   10345 C  CD1   . PHE   B 1 787  ? 140.685 160.921 126.745 1.00 17.24  ? 787  PHE   B CD1   1 
ATOM   10346 C  CD2   . PHE   B 1 787  ? 139.986 162.898 127.871 1.00 12.05  ? 787  PHE   B CD2   1 
ATOM   10347 C  CE1   . PHE   B 1 787  ? 141.092 161.677 125.664 1.00 9.96   ? 787  PHE   B CE1   1 
ATOM   10348 C  CE2   . PHE   B 1 787  ? 140.394 163.658 126.793 1.00 19.52  ? 787  PHE   B CE2   1 
ATOM   10349 C  CZ    . PHE   B 1 787  ? 140.946 163.046 125.688 1.00 13.59  ? 787  PHE   B CZ    1 
ATOM   10350 N  N     . ARG   B 1 788  ? 142.691 161.927 129.732 1.00 14.98  ? 788  ARG   B N     1 
ATOM   10351 C  CA    . ARG   B 1 788  ? 143.462 163.153 129.812 1.00 15.33  ? 788  ARG   B CA    1 
ATOM   10352 C  C     . ARG   B 1 788  ? 143.810 163.630 128.412 1.00 21.29  ? 788  ARG   B C     1 
ATOM   10353 O  O     . ARG   B 1 788  ? 144.010 162.815 127.506 1.00 25.46  ? 788  ARG   B O     1 
ATOM   10354 C  CB    . ARG   B 1 788  ? 144.755 162.948 130.612 1.00 15.75  ? 788  ARG   B CB    1 
ATOM   10355 C  CG    . ARG   B 1 788  ? 144.542 162.737 132.093 1.00 22.63  ? 788  ARG   B CG    1 
ATOM   10356 C  CD    . ARG   B 1 788  ? 145.820 162.280 132.760 1.00 22.25  ? 788  ARG   B CD    1 
ATOM   10357 N  NE    . ARG   B 1 788  ? 145.565 161.620 134.034 1.00 20.74  ? 788  ARG   B NE    1 
ATOM   10358 C  CZ    . ARG   B 1 788  ? 145.583 162.236 135.207 1.00 21.94  ? 788  ARG   B CZ    1 
ATOM   10359 N  NH1   . ARG   B 1 788  ? 145.824 163.533 135.303 1.00 19.60  ? 788  ARG   B NH1   1 
ATOM   10360 N  NH2   . ARG   B 1 788  ? 145.352 161.533 136.312 1.00 20.80  ? 788  ARG   B NH2   1 
ATOM   10361 N  N     . PRO   B 1 789  ? 143.890 164.940 128.205 1.00 24.88  ? 789  PRO   B N     1 
ATOM   10362 C  CA    . PRO   B 1 789  ? 144.326 165.448 126.900 1.00 23.82  ? 789  PRO   B CA    1 
ATOM   10363 C  C     . PRO   B 1 789  ? 145.833 165.355 126.734 1.00 27.18  ? 789  PRO   B C     1 
ATOM   10364 O  O     . PRO   B 1 789  ? 146.582 166.153 127.306 1.00 21.85  ? 789  PRO   B O     1 
ATOM   10365 C  CB    . PRO   B 1 789  ? 143.844 166.901 126.915 1.00 16.73  ? 789  PRO   B CB    1 
ATOM   10366 C  CG    . PRO   B 1 789  ? 143.870 167.276 128.354 1.00 22.61  ? 789  PRO   B CG    1 
ATOM   10367 C  CD    . PRO   B 1 789  ? 143.550 166.027 129.139 1.00 22.65  ? 789  PRO   B CD    1 
ATOM   10368 N  N     . GLN   B 1 790  ? 146.284 164.387 125.944 1.00 23.91  ? 790  GLN   B N     1 
ATOM   10369 C  CA    . GLN   B 1 790  ? 147.704 164.160 125.690 1.00 17.61  ? 790  GLN   B CA    1 
ATOM   10370 C  C     . GLN   B 1 790  ? 148.014 164.756 124.323 1.00 19.55  ? 790  GLN   B C     1 
ATOM   10371 O  O     . GLN   B 1 790  ? 147.723 164.153 123.288 1.00 22.58  ? 790  GLN   B O     1 
ATOM   10372 C  CB    . GLN   B 1 790  ? 148.028 162.673 125.764 1.00 22.85  ? 790  GLN   B CB    1 
ATOM   10373 C  CG    . GLN   B 1 790  ? 147.346 161.974 126.932 1.00 14.41  ? 790  GLN   B CG    1 
ATOM   10374 C  CD    . GLN   B 1 790  ? 147.887 160.586 127.196 1.00 24.59  ? 790  GLN   B CD    1 
ATOM   10375 O  OE1   . GLN   B 1 790  ? 149.028 160.423 127.627 1.00 39.17  ? 790  GLN   B OE1   1 
ATOM   10376 N  NE2   . GLN   B 1 790  ? 147.063 159.574 126.953 1.00 29.19  ? 790  GLN   B NE2   1 
ATOM   10377 N  N     . CYS   B 1 791  ? 148.611 165.943 124.323 1.00 24.90  ? 791  CYS   B N     1 
ATOM   10378 C  CA    . CYS   B 1 791  ? 148.682 166.783 123.137 1.00 22.89  ? 791  CYS   B CA    1 
ATOM   10379 C  C     . CYS   B 1 791  ? 150.067 166.723 122.508 1.00 29.18  ? 791  CYS   B C     1 
ATOM   10380 O  O     . CYS   B 1 791  ? 151.082 166.825 123.206 1.00 24.33  ? 791  CYS   B O     1 
ATOM   10381 C  CB    . CYS   B 1 791  ? 148.325 168.229 123.483 1.00 20.71  ? 791  CYS   B CB    1 
ATOM   10382 S  SG    . CYS   B 1 791  ? 146.727 168.422 124.305 1.00 49.34  ? 791  CYS   B SG    1 
ATOM   10383 N  N     . LEU   B 1 792  ? 150.095 166.545 121.191 1.00 29.45  ? 792  LEU   B N     1 
ATOM   10384 C  CA    . LEU   B 1 792  ? 151.300 166.677 120.383 1.00 21.19  ? 792  LEU   B CA    1 
ATOM   10385 C  C     . LEU   B 1 792  ? 151.174 167.981 119.609 1.00 21.02  ? 792  LEU   B C     1 
ATOM   10386 O  O     . LEU   B 1 792  ? 150.366 168.081 118.680 1.00 32.68  ? 792  LEU   B O     1 
ATOM   10387 C  CB    . LEU   B 1 792  ? 151.465 165.483 119.446 1.00 20.33  ? 792  LEU   B CB    1 
ATOM   10388 C  CG    . LEU   B 1 792  ? 152.310 165.710 118.193 1.00 26.80  ? 792  LEU   B CG    1 
ATOM   10389 C  CD1   . LEU   B 1 792  ? 153.757 165.972 118.569 1.00 18.42  ? 792  LEU   B CD1   1 
ATOM   10390 C  CD2   . LEU   B 1 792  ? 152.201 164.518 117.253 1.00 29.53  ? 792  LEU   B CD2   1 
ATOM   10391 N  N     . VAL   B 1 793  ? 151.954 168.981 120.002 1.00 17.51  ? 793  VAL   B N     1 
ATOM   10392 C  CA    . VAL   B 1 793  ? 151.873 170.317 119.425 1.00 21.18  ? 793  VAL   B CA    1 
ATOM   10393 C  C     . VAL   B 1 793  ? 152.951 170.440 118.359 1.00 29.16  ? 793  VAL   B C     1 
ATOM   10394 O  O     . VAL   B 1 793  ? 154.146 170.312 118.655 1.00 36.93  ? 793  VAL   B O     1 
ATOM   10395 C  CB    . VAL   B 1 793  ? 152.031 171.402 120.501 1.00 21.17  ? 793  VAL   B CB    1 
ATOM   10396 C  CG1   . VAL   B 1 793  ? 151.812 172.780 119.904 1.00 20.66  ? 793  VAL   B CG1   1 
ATOM   10397 C  CG2   . VAL   B 1 793  ? 151.064 171.153 121.645 1.00 22.70  ? 793  VAL   B CG2   1 
ATOM   10398 N  N     . MET   B 1 794  ? 152.531 170.689 117.119 1.00 29.77  ? 794  MET   B N     1 
ATOM   10399 C  CA    . MET   B 1 794  ? 153.458 170.855 116.000 1.00 22.89  ? 794  MET   B CA    1 
ATOM   10400 C  C     . MET   B 1 794  ? 153.881 172.316 115.968 1.00 28.17  ? 794  MET   B C     1 
ATOM   10401 O  O     . MET   B 1 794  ? 153.220 173.165 115.370 1.00 35.47  ? 794  MET   B O     1 
ATOM   10402 C  CB    . MET   B 1 794  ? 152.811 170.422 114.691 1.00 27.82  ? 794  MET   B CB    1 
ATOM   10403 C  CG    . MET   B 1 794  ? 153.747 169.692 113.741 1.00 33.56  ? 794  MET   B CG    1 
ATOM   10404 S  SD    . MET   B 1 794  ? 154.638 168.306 114.480 1.00 51.70  ? 794  MET   B SD    1 
ATOM   10405 C  CE    . MET   B 1 794  ? 153.523 167.811 115.793 1.00 27.43  ? 794  MET   B CE    1 
ATOM   10406 N  N     . THR   B 1 795  ? 155.001 172.614 116.624 1.00 40.42  ? 795  THR   B N     1 
ATOM   10407 C  CA    . THR   B 1 795  ? 155.460 173.983 116.793 1.00 44.86  ? 795  THR   B CA    1 
ATOM   10408 C  C     . THR   B 1 795  ? 156.849 174.251 116.234 1.00 45.69  ? 795  THR   B C     1 
ATOM   10409 O  O     . THR   B 1 795  ? 157.263 175.416 116.198 1.00 46.19  ? 795  THR   B O     1 
ATOM   10410 C  CB    . THR   B 1 795  ? 155.448 174.369 118.281 1.00 45.72  ? 795  THR   B CB    1 
ATOM   10411 O  OG1   . THR   B 1 795  ? 155.758 175.761 118.419 1.00 53.34  ? 795  THR   B OG1   1 
ATOM   10412 C  CG2   . THR   B 1 795  ? 156.467 173.544 119.054 1.00 35.91  ? 795  THR   B CG2   1 
ATOM   10413 N  N     . GLY   B 1 796  ? 157.577 173.228 115.798 1.00 38.94  ? 796  GLY   B N     1 
ATOM   10414 C  CA    . GLY   B 1 796  ? 158.946 173.432 115.371 1.00 34.00  ? 796  GLY   B CA    1 
ATOM   10415 C  C     . GLY   B 1 796  ? 159.820 173.838 116.537 1.00 41.15  ? 796  GLY   B C     1 
ATOM   10416 O  O     . GLY   B 1 796  ? 159.901 173.116 117.535 1.00 43.10  ? 796  GLY   B O     1 
ATOM   10417 N  N     . ALA   B 1 797  ? 160.481 174.981 116.428 1.00 42.34  ? 797  ALA   B N     1 
ATOM   10418 C  CA    . ALA   B 1 797  ? 161.219 175.513 117.565 1.00 35.47  ? 797  ALA   B CA    1 
ATOM   10419 C  C     . ALA   B 1 797  ? 160.233 175.933 118.648 1.00 38.63  ? 797  ALA   B C     1 
ATOM   10420 O  O     . ALA   B 1 797  ? 159.309 176.707 118.372 1.00 38.96  ? 797  ALA   B O     1 
ATOM   10421 C  CB    . ALA   B 1 797  ? 162.085 176.696 117.143 1.00 38.95  ? 797  ALA   B CB    1 
ATOM   10422 N  N     . PRO   B 1 798  ? 160.389 175.453 119.886 1.00 44.55  ? 798  PRO   B N     1 
ATOM   10423 C  CA    . PRO   B 1 798  ? 159.390 175.743 120.924 1.00 39.48  ? 798  PRO   B CA    1 
ATOM   10424 C  C     . PRO   B 1 798  ? 159.410 177.177 121.425 1.00 40.99  ? 798  PRO   B C     1 
ATOM   10425 O  O     . PRO   B 1 798  ? 158.699 177.484 122.388 1.00 48.49  ? 798  PRO   B O     1 
ATOM   10426 C  CB    . PRO   B 1 798  ? 159.760 174.764 122.053 1.00 38.45  ? 798  PRO   B CB    1 
ATOM   10427 C  CG    . PRO   B 1 798  ? 160.733 173.791 121.445 1.00 39.25  ? 798  PRO   B CG    1 
ATOM   10428 C  CD    . PRO   B 1 798  ? 161.435 174.541 120.368 1.00 42.10  ? 798  PRO   B CD    1 
ATOM   10429 N  N     . ASN   B 1 799  ? 160.189 178.065 120.810 1.00 46.10  ? 799  ASN   B N     1 
ATOM   10430 C  CA    . ASN   B 1 799  ? 160.245 179.463 121.208 1.00 49.14  ? 799  ASN   B CA    1 
ATOM   10431 C  C     . ASN   B 1 799  ? 159.805 180.412 120.103 1.00 51.27  ? 799  ASN   B C     1 
ATOM   10432 O  O     . ASN   B 1 799  ? 159.808 181.630 120.313 1.00 50.90  ? 799  ASN   B O     1 
ATOM   10433 C  CB    . ASN   B 1 799  ? 161.662 179.825 121.667 1.00 48.08  ? 799  ASN   B CB    1 
ATOM   10434 C  CG    . ASN   B 1 799  ? 162.594 180.114 120.507 1.00 54.54  ? 799  ASN   B CG    1 
ATOM   10435 O  OD1   . ASN   B 1 799  ? 162.708 179.318 119.575 1.00 57.21  ? 799  ASN   B OD1   1 
ATOM   10436 N  ND2   . ASN   B 1 799  ? 163.266 181.258 120.558 1.00 55.46  ? 799  ASN   B ND2   1 
ATOM   10437 N  N     . SER   B 1 800  ? 159.431 179.891 118.933 1.00 49.17  ? 800  SER   B N     1 
ATOM   10438 C  CA    . SER   B 1 800  ? 158.992 180.758 117.844 1.00 50.81  ? 800  SER   B CA    1 
ATOM   10439 C  C     . SER   B 1 800  ? 157.668 181.435 118.174 1.00 58.14  ? 800  SER   B C     1 
ATOM   10440 O  O     . SER   B 1 800  ? 157.497 182.633 117.921 1.00 61.69  ? 800  SER   B O     1 
ATOM   10441 C  CB    . SER   B 1 800  ? 158.874 179.954 116.550 1.00 54.79  ? 800  SER   B CB    1 
ATOM   10442 O  OG    . SER   B 1 800  ? 158.520 178.608 116.817 1.00 57.26  ? 800  SER   B OG    1 
ATOM   10443 N  N     . ARG   B 1 801  ? 156.721 180.686 118.734 1.00 53.24  ? 801  ARG   B N     1 
ATOM   10444 C  CA    . ARG   B 1 801  ? 155.410 181.212 119.112 1.00 50.84  ? 801  ARG   B CA    1 
ATOM   10445 C  C     . ARG   B 1 801  ? 155.186 180.922 120.589 1.00 48.71  ? 801  ARG   B C     1 
ATOM   10446 O  O     . ARG   B 1 801  ? 154.692 179.848 120.958 1.00 49.62  ? 801  ARG   B O     1 
ATOM   10447 C  CB    . ARG   B 1 801  ? 154.303 180.616 118.246 1.00 50.96  ? 801  ARG   B CB    1 
ATOM   10448 C  CG    . ARG   B 1 801  ? 154.664 180.513 116.774 1.00 49.04  ? 801  ARG   B CG    1 
ATOM   10449 C  CD    . ARG   B 1 801  ? 153.526 179.920 115.964 1.00 52.03  ? 801  ARG   B CD    1 
ATOM   10450 N  NE    . ARG   B 1 801  ? 153.681 178.485 115.762 1.00 57.47  ? 801  ARG   B NE    1 
ATOM   10451 C  CZ    . ARG   B 1 801  ? 153.062 177.793 114.816 1.00 57.61  ? 801  ARG   B CZ    1 
ATOM   10452 N  NH1   . ARG   B 1 801  ? 152.234 178.375 113.964 1.00 52.57  ? 801  ARG   B NH1   1 
ATOM   10453 N  NH2   . ARG   B 1 801  ? 153.277 176.484 114.723 1.00 55.70  ? 801  ARG   B NH2   1 
ATOM   10454 N  N     . PRO   B 1 802  ? 155.538 181.861 121.465 1.00 41.75  ? 802  PRO   B N     1 
ATOM   10455 C  CA    . PRO   B 1 802  ? 155.420 181.613 122.908 1.00 42.15  ? 802  PRO   B CA    1 
ATOM   10456 C  C     . PRO   B 1 802  ? 153.984 181.630 123.406 1.00 46.12  ? 802  PRO   B C     1 
ATOM   10457 O  O     . PRO   B 1 802  ? 153.630 180.866 124.308 1.00 44.28  ? 802  PRO   B O     1 
ATOM   10458 C  CB    . PRO   B 1 802  ? 156.238 182.755 123.521 1.00 44.67  ? 802  PRO   B CB    1 
ATOM   10459 C  CG    . PRO   B 1 802  ? 156.136 183.856 122.522 1.00 46.60  ? 802  PRO   B CG    1 
ATOM   10460 C  CD    . PRO   B 1 802  ? 156.077 183.200 121.170 1.00 43.59  ? 802  PRO   B CD    1 
ATOM   10461 N  N     . ALA   B 1 803  ? 153.151 182.505 122.839 1.00 43.94  ? 803  ALA   B N     1 
ATOM   10462 C  CA    . ALA   B 1 803  ? 151.772 182.613 123.305 1.00 34.22  ? 803  ALA   B CA    1 
ATOM   10463 C  C     . ALA   B 1 803  ? 151.011 181.310 123.097 1.00 34.52  ? 803  ALA   B C     1 
ATOM   10464 O  O     . ALA   B 1 803  ? 150.284 180.856 123.990 1.00 39.18  ? 803  ALA   B O     1 
ATOM   10465 C  CB    . ALA   B 1 803  ? 151.068 183.767 122.593 1.00 38.14  ? 803  ALA   B CB    1 
ATOM   10466 N  N     . LEU   B 1 804  ? 151.162 180.692 121.924 1.00 37.13  ? 804  LEU   B N     1 
ATOM   10467 C  CA    . LEU   B 1 804  ? 150.469 179.436 121.660 1.00 37.43  ? 804  LEU   B CA    1 
ATOM   10468 C  C     . LEU   B 1 804  ? 150.967 178.331 122.582 1.00 33.65  ? 804  LEU   B C     1 
ATOM   10469 O  O     . LEU   B 1 804  ? 150.178 177.509 123.064 1.00 41.13  ? 804  LEU   B O     1 
ATOM   10470 C  CB    . LEU   B 1 804  ? 150.644 179.036 120.195 1.00 32.18  ? 804  LEU   B CB    1 
ATOM   10471 C  CG    . LEU   B 1 804  ? 150.208 177.620 119.816 1.00 32.20  ? 804  LEU   B CG    1 
ATOM   10472 C  CD1   . LEU   B 1 804  ? 149.538 177.614 118.453 1.00 36.67  ? 804  LEU   B CD1   1 
ATOM   10473 C  CD2   . LEU   B 1 804  ? 151.391 176.669 119.838 1.00 33.98  ? 804  LEU   B CD2   1 
ATOM   10474 N  N     . LEU   B 1 805  ? 152.277 178.290 122.832 1.00 28.25  ? 805  LEU   B N     1 
ATOM   10475 C  CA    . LEU   B 1 805  ? 152.817 177.290 123.745 1.00 30.64  ? 805  LEU   B CA    1 
ATOM   10476 C  C     . LEU   B 1 805  ? 152.268 177.483 125.152 1.00 37.94  ? 805  LEU   B C     1 
ATOM   10477 O  O     . LEU   B 1 805  ? 151.894 176.512 125.818 1.00 39.95  ? 805  LEU   B O     1 
ATOM   10478 C  CB    . LEU   B 1 805  ? 154.345 177.352 123.742 1.00 33.99  ? 805  LEU   B CB    1 
ATOM   10479 C  CG    . LEU   B 1 805  ? 155.079 176.348 124.632 1.00 38.77  ? 805  LEU   B CG    1 
ATOM   10480 C  CD1   . LEU   B 1 805  ? 155.628 175.196 123.808 1.00 32.38  ? 805  LEU   B CD1   1 
ATOM   10481 C  CD2   . LEU   B 1 805  ? 156.193 177.037 125.396 1.00 38.69  ? 805  LEU   B CD2   1 
ATOM   10482 N  N     . HIS   B 1 806  ? 152.201 178.732 125.618 1.00 37.77  ? 806  HIS   B N     1 
ATOM   10483 C  CA    . HIS   B 1 806  ? 151.596 179.014 126.916 1.00 34.98  ? 806  HIS   B CA    1 
ATOM   10484 C  C     . HIS   B 1 806  ? 150.152 178.535 126.959 1.00 34.52  ? 806  HIS   B C     1 
ATOM   10485 O  O     . HIS   B 1 806  ? 149.730 177.872 127.914 1.00 38.95  ? 806  HIS   B O     1 
ATOM   10486 C  CB    . HIS   B 1 806  ? 151.664 180.514 127.211 1.00 37.92  ? 806  HIS   B CB    1 
ATOM   10487 C  CG    . HIS   B 1 806  ? 153.006 180.985 127.676 1.00 41.62  ? 806  HIS   B CG    1 
ATOM   10488 N  ND1   . HIS   B 1 806  ? 153.632 180.471 128.791 1.00 42.30  ? 806  HIS   B ND1   1 
ATOM   10489 C  CD2   . HIS   B 1 806  ? 153.843 181.924 127.175 1.00 42.49  ? 806  HIS   B CD2   1 
ATOM   10490 C  CE1   . HIS   B 1 806  ? 154.795 181.075 128.958 1.00 40.81  ? 806  HIS   B CE1   1 
ATOM   10491 N  NE2   . HIS   B 1 806  ? 154.948 181.960 127.989 1.00 45.31  ? 806  HIS   B NE2   1 
ATOM   10492 N  N     . LEU   B 1 807  ? 149.376 178.869 125.927 1.00 30.09  ? 807  LEU   B N     1 
ATOM   10493 C  CA    . LEU   B 1 807  ? 147.966 178.494 125.905 1.00 23.95  ? 807  LEU   B CA    1 
ATOM   10494 C  C     . LEU   B 1 807  ? 147.800 176.981 125.961 1.00 19.91  ? 807  LEU   B C     1 
ATOM   10495 O  O     . LEU   B 1 807  ? 146.970 176.463 126.716 1.00 29.33  ? 807  LEU   B O     1 
ATOM   10496 C  CB    . LEU   B 1 807  ? 147.295 179.071 124.659 1.00 27.78  ? 807  LEU   B CB    1 
ATOM   10497 C  CG    . LEU   B 1 807  ? 145.769 179.156 124.663 1.00 30.82  ? 807  LEU   B CG    1 
ATOM   10498 C  CD1   . LEU   B 1 807  ? 145.178 177.951 123.960 1.00 29.97  ? 807  LEU   B CD1   1 
ATOM   10499 C  CD2   . LEU   B 1 807  ? 145.239 179.258 126.081 1.00 31.32  ? 807  LEU   B CD2   1 
ATOM   10500 N  N     . VAL   B 1 808  ? 148.585 176.253 125.166 1.00 16.92  ? 808  VAL   B N     1 
ATOM   10501 C  CA    . VAL   B 1 808  ? 148.486 174.797 125.177 1.00 21.68  ? 808  VAL   B CA    1 
ATOM   10502 C  C     . VAL   B 1 808  ? 148.948 174.232 126.512 1.00 22.93  ? 808  VAL   B C     1 
ATOM   10503 O  O     . VAL   B 1 808  ? 148.420 173.217 126.981 1.00 23.22  ? 808  VAL   B O     1 
ATOM   10504 C  CB    . VAL   B 1 808  ? 149.280 174.192 124.004 1.00 23.05  ? 808  VAL   B CB    1 
ATOM   10505 C  CG1   . VAL   B 1 808  ? 149.520 172.709 124.236 1.00 19.11  ? 808  VAL   B CG1   1 
ATOM   10506 C  CG2   . VAL   B 1 808  ? 148.536 174.407 122.702 1.00 27.17  ? 808  VAL   B CG2   1 
ATOM   10507 N  N     . HIS   B 1 809  ? 149.932 174.872 127.147 1.00 37.56  ? 809  HIS   B N     1 
ATOM   10508 C  CA    . HIS   B 1 809  ? 150.457 174.372 128.412 1.00 25.41  ? 809  HIS   B CA    1 
ATOM   10509 C  C     . HIS   B 1 809  ? 149.494 174.632 129.562 1.00 31.35  ? 809  HIS   B C     1 
ATOM   10510 O  O     . HIS   B 1 809  ? 149.515 173.908 130.563 1.00 33.71  ? 809  HIS   B O     1 
ATOM   10511 C  CB    . HIS   B 1 809  ? 151.823 175.012 128.672 1.00 21.61  ? 809  HIS   B CB    1 
ATOM   10512 C  CG    . HIS   B 1 809  ? 152.357 174.787 130.052 1.00 32.02  ? 809  HIS   B CG    1 
ATOM   10513 N  ND1   . HIS   B 1 809  ? 152.085 175.636 131.103 1.00 39.37  ? 809  HIS   B ND1   1 
ATOM   10514 C  CD2   . HIS   B 1 809  ? 153.166 173.821 130.548 1.00 32.10  ? 809  HIS   B CD2   1 
ATOM   10515 C  CE1   . HIS   B 1 809  ? 152.696 175.198 132.189 1.00 33.31  ? 809  HIS   B CE1   1 
ATOM   10516 N  NE2   . HIS   B 1 809  ? 153.358 174.098 131.880 1.00 32.75  ? 809  HIS   B NE2   1 
ATOM   10517 N  N     . ASP   B 1 810  ? 148.636 175.645 129.431 1.00 39.73  ? 810  ASP   B N     1 
ATOM   10518 C  CA    . ASP   B 1 810  ? 147.677 175.943 130.490 1.00 30.56  ? 810  ASP   B CA    1 
ATOM   10519 C  C     . ASP   B 1 810  ? 146.752 174.760 130.751 1.00 30.35  ? 810  ASP   B C     1 
ATOM   10520 O  O     . ASP   B 1 810  ? 146.561 174.350 131.902 1.00 44.77  ? 810  ASP   B O     1 
ATOM   10521 C  CB    . ASP   B 1 810  ? 146.869 177.189 130.129 1.00 34.17  ? 810  ASP   B CB    1 
ATOM   10522 C  CG    . ASP   B 1 810  ? 147.684 178.461 130.232 1.00 43.29  ? 810  ASP   B CG    1 
ATOM   10523 O  OD1   . ASP   B 1 810  ? 148.620 178.506 131.057 1.00 40.22  ? 810  ASP   B OD1   1 
ATOM   10524 O  OD2   . ASP   B 1 810  ? 147.387 179.420 129.488 1.00 45.44  ? 810  ASP   B OD2   1 
ATOM   10525 N  N     . PHE   B 1 811  ? 146.173 174.190 129.695 1.00 28.88  ? 811  PHE   B N     1 
ATOM   10526 C  CA    . PHE   B 1 811  ? 145.233 173.086 129.839 1.00 28.20  ? 811  PHE   B CA    1 
ATOM   10527 C  C     . PHE   B 1 811  ? 145.906 171.721 129.756 1.00 28.87  ? 811  PHE   B C     1 
ATOM   10528 O  O     . PHE   B 1 811  ? 145.213 170.708 129.621 1.00 35.75  ? 811  PHE   B O     1 
ATOM   10529 C  CB    . PHE   B 1 811  ? 144.108 173.200 128.799 1.00 31.05  ? 811  PHE   B CB    1 
ATOM   10530 C  CG    . PHE   B 1 811  ? 144.526 172.871 127.390 1.00 26.28  ? 811  PHE   B CG    1 
ATOM   10531 C  CD1   . PHE   B 1 811  ? 144.535 171.563 126.938 1.00 25.87  ? 811  PHE   B CD1   1 
ATOM   10532 C  CD2   . PHE   B 1 811  ? 144.876 173.878 126.508 1.00 30.75  ? 811  PHE   B CD2   1 
ATOM   10533 C  CE1   . PHE   B 1 811  ? 144.911 171.266 125.646 1.00 25.13  ? 811  PHE   B CE1   1 
ATOM   10534 C  CE2   . PHE   B 1 811  ? 145.250 173.585 125.212 1.00 24.45  ? 811  PHE   B CE2   1 
ATOM   10535 C  CZ    . PHE   B 1 811  ? 145.267 172.278 124.781 1.00 18.48  ? 811  PHE   B CZ    1 
ATOM   10536 N  N     . THR   B 1 812  ? 147.231 171.671 129.842 1.00 27.10  ? 812  THR   B N     1 
ATOM   10537 C  CA    . THR   B 1 812  ? 147.964 170.413 129.878 1.00 30.72  ? 812  THR   B CA    1 
ATOM   10538 C  C     . THR   B 1 812  ? 148.846 170.252 131.106 1.00 31.43  ? 812  THR   B C     1 
ATOM   10539 O  O     . THR   B 1 812  ? 149.159 169.119 131.473 1.00 35.52  ? 812  THR   B O     1 
ATOM   10540 C  CB    . THR   B 1 812  ? 148.839 170.260 128.622 1.00 31.40  ? 812  THR   B CB    1 
ATOM   10541 O  OG1   . THR   B 1 812  ? 149.078 171.546 128.038 1.00 40.07  ? 812  THR   B OG1   1 
ATOM   10542 C  CG2   . THR   B 1 812  ? 148.158 169.363 127.603 1.00 27.34  ? 812  THR   B CG2   1 
ATOM   10543 N  N     . LYS   B 1 813  ? 149.249 171.344 131.750 1.00 29.20  ? 813  LYS   B N     1 
ATOM   10544 C  CA    . LYS   B 1 813  ? 150.176 171.252 132.870 1.00 29.76  ? 813  LYS   B CA    1 
ATOM   10545 C  C     . LYS   B 1 813  ? 149.504 170.583 134.063 1.00 37.25  ? 813  LYS   B C     1 
ATOM   10546 O  O     . LYS   B 1 813  ? 148.414 170.986 134.483 1.00 41.11  ? 813  LYS   B O     1 
ATOM   10547 C  CB    . LYS   B 1 813  ? 150.679 172.641 133.253 1.00 31.17  ? 813  LYS   B CB    1 
ATOM   10548 C  CG    . LYS   B 1 813  ? 151.476 172.683 134.543 1.00 35.42  ? 813  LYS   B CG    1 
ATOM   10549 C  CD    . LYS   B 1 813  ? 151.662 174.112 135.021 1.00 36.50  ? 813  LYS   B CD    1 
ATOM   10550 C  CE    . LYS   B 1 813  ? 151.597 174.207 136.533 1.00 39.94  ? 813  LYS   B CE    1 
ATOM   10551 N  NZ    . LYS   B 1 813  ? 152.888 173.821 137.162 1.00 44.71  ? 813  LYS   B NZ    1 
ATOM   10552 N  N     . ASN   B 1 814  ? 150.158 169.555 134.604 1.00 36.11  ? 814  ASN   B N     1 
ATOM   10553 C  CA    . ASN   B 1 814  ? 149.644 168.797 135.740 1.00 35.34  ? 814  ASN   B CA    1 
ATOM   10554 C  C     . ASN   B 1 814  ? 148.485 167.900 135.327 1.00 33.11  ? 814  ASN   B C     1 
ATOM   10555 O  O     . ASN   B 1 814  ? 148.042 167.051 136.107 1.00 46.09  ? 814  ASN   B O     1 
ATOM   10556 C  CB    . ASN   B 1 814  ? 149.207 169.738 136.865 1.00 33.38  ? 814  ASN   B CB    1 
ATOM   10557 C  CG    . ASN   B 1 814  ? 150.376 170.271 137.667 1.00 38.86  ? 814  ASN   B CG    1 
ATOM   10558 O  OD1   . ASN   B 1 814  ? 151.314 169.539 137.980 1.00 40.36  ? 814  ASN   B OD1   1 
ATOM   10559 N  ND2   . ASN   B 1 814  ? 150.326 171.554 138.005 1.00 42.96  ? 814  ASN   B ND2   1 
ATOM   10560 N  N     . VAL   B 1 815  ? 147.983 168.083 134.108 1.00 29.92  ? 815  VAL   B N     1 
ATOM   10561 C  CA    . VAL   B 1 815  ? 146.913 167.249 133.577 1.00 32.31  ? 815  VAL   B CA    1 
ATOM   10562 C  C     . VAL   B 1 815  ? 147.193 166.952 132.110 1.00 35.78  ? 815  VAL   B C     1 
ATOM   10563 O  O     . VAL   B 1 815  ? 146.983 167.807 131.243 1.00 43.17  ? 815  VAL   B O     1 
ATOM   10564 C  CB    . VAL   B 1 815  ? 145.539 167.920 133.753 1.00 33.24  ? 815  VAL   B CB    1 
ATOM   10565 C  CG1   . VAL   B 1 815  ? 145.620 169.398 133.408 1.00 29.15  ? 815  VAL   B CG1   1 
ATOM   10566 C  CG2   . VAL   B 1 815  ? 144.498 167.223 132.894 1.00 35.46  ? 815  VAL   B CG2   1 
ATOM   10567 N  N     . GLY   B 1 816  ? 147.665 165.747 131.822 1.00 31.38  ? 816  GLY   B N     1 
ATOM   10568 C  CA    . GLY   B 1 816  ? 147.896 165.333 130.456 1.00 27.55  ? 816  GLY   B CA    1 
ATOM   10569 C  C     . GLY   B 1 816  ? 149.319 165.583 129.986 1.00 23.11  ? 816  GLY   B C     1 
ATOM   10570 O  O     . GLY   B 1 816  ? 150.091 166.325 130.590 1.00 30.58  ? 816  GLY   B O     1 
ATOM   10571 N  N     . LEU   B 1 817  ? 149.657 164.939 128.874 1.00 29.55  ? 817  LEU   B N     1 
ATOM   10572 C  CA    . LEU   B 1 817  ? 150.985 165.006 128.286 1.00 18.58  ? 817  LEU   B CA    1 
ATOM   10573 C  C     . LEU   B 1 817  ? 151.070 166.135 127.263 1.00 21.71  ? 817  LEU   B C     1 
ATOM   10574 O  O     . LEU   B 1 817  ? 150.068 166.571 126.692 1.00 31.01  ? 817  LEU   B O     1 
ATOM   10575 C  CB    . LEU   B 1 817  ? 151.342 163.671 127.631 1.00 24.49  ? 817  LEU   B CB    1 
ATOM   10576 C  CG    . LEU   B 1 817  ? 152.671 163.593 126.880 1.00 29.30  ? 817  LEU   B CG    1 
ATOM   10577 C  CD1   . LEU   B 1 817  ? 153.835 163.784 127.837 1.00 30.50  ? 817  LEU   B CD1   1 
ATOM   10578 C  CD2   . LEU   B 1 817  ? 152.787 162.268 126.142 1.00 32.14  ? 817  LEU   B CD2   1 
ATOM   10579 N  N     . MET   B 1 818  ? 152.294 166.609 127.036 1.00 25.99  ? 818  MET   B N     1 
ATOM   10580 C  CA    . MET   B 1 818  ? 152.549 167.695 126.093 1.00 20.62  ? 818  MET   B CA    1 
ATOM   10581 C  C     . MET   B 1 818  ? 153.886 167.435 125.414 1.00 26.63  ? 818  MET   B C     1 
ATOM   10582 O  O     . MET   B 1 818  ? 154.935 167.500 126.061 1.00 25.62  ? 818  MET   B O     1 
ATOM   10583 C  CB    . MET   B 1 818  ? 152.548 169.050 126.799 1.00 22.65  ? 818  MET   B CB    1 
ATOM   10584 C  CG    . MET   B 1 818  ? 152.707 170.235 125.867 1.00 16.17  ? 818  MET   B CG    1 
ATOM   10585 S  SD    . MET   B 1 818  ? 152.737 171.809 126.741 1.00 45.88  ? 818  MET   B SD    1 
ATOM   10586 C  CE    . MET   B 1 818  ? 152.728 172.957 125.369 1.00 22.45  ? 818  MET   B CE    1 
ATOM   10587 N  N     . ILE   B 1 819  ? 153.849 167.139 124.118 1.00 27.73  ? 819  ILE   B N     1 
ATOM   10588 C  CA    . ILE   B 1 819  ? 155.050 166.854 123.341 1.00 17.05  ? 819  ILE   B CA    1 
ATOM   10589 C  C     . ILE   B 1 819  ? 155.179 167.917 122.261 1.00 19.89  ? 819  ILE   B C     1 
ATOM   10590 O  O     . ILE   B 1 819  ? 154.296 168.049 121.406 1.00 24.99  ? 819  ILE   B O     1 
ATOM   10591 C  CB    . ILE   B 1 819  ? 155.010 165.450 122.720 1.00 16.42  ? 819  ILE   B CB    1 
ATOM   10592 C  CG1   . ILE   B 1 819  ? 154.955 164.385 123.814 1.00 12.92  ? 819  ILE   B CG1   1 
ATOM   10593 C  CG2   . ILE   B 1 819  ? 156.226 165.226 121.846 1.00 19.95  ? 819  ILE   B CG2   1 
ATOM   10594 C  CD1   . ILE   B 1 819  ? 154.915 162.972 123.284 1.00 13.33  ? 819  ILE   B CD1   1 
ATOM   10595 N  N     . CYS   B 1 820  ? 156.281 168.660 122.286 1.00 26.61  ? 820  CYS   B N     1 
ATOM   10596 C  CA    . CYS   B 1 820  ? 156.559 169.673 121.273 1.00 23.55  ? 820  CYS   B CA    1 
ATOM   10597 C  C     . CYS   B 1 820  ? 157.314 169.008 120.128 1.00 25.96  ? 820  CYS   B C     1 
ATOM   10598 O  O     . CYS   B 1 820  ? 158.483 168.640 120.278 1.00 37.78  ? 820  CYS   B O     1 
ATOM   10599 C  CB    . CYS   B 1 820  ? 157.359 170.828 121.868 1.00 28.95  ? 820  CYS   B CB    1 
ATOM   10600 S  SG    . CYS   B 1 820  ? 156.507 171.728 123.183 1.00 54.86  ? 820  CYS   B SG    1 
ATOM   10601 N  N     . GLY   B 1 821  ? 156.647 168.851 118.985 1.00 25.43  ? 821  GLY   B N     1 
ATOM   10602 C  CA    . GLY   B 1 821  ? 157.236 168.163 117.852 1.00 17.01  ? 821  GLY   B CA    1 
ATOM   10603 C  C     . GLY   B 1 821  ? 157.909 169.127 116.895 1.00 26.59  ? 821  GLY   B C     1 
ATOM   10604 O  O     . GLY   B 1 821  ? 157.323 170.139 116.502 1.00 30.97  ? 821  GLY   B O     1 
ATOM   10605 N  N     . HIS   B 1 822  ? 159.147 168.807 116.525 1.00 32.66  ? 822  HIS   B N     1 
ATOM   10606 C  CA    . HIS   B 1 822  ? 159.922 169.600 115.581 1.00 24.61  ? 822  HIS   B CA    1 
ATOM   10607 C  C     . HIS   B 1 822  ? 160.425 168.690 114.472 1.00 26.99  ? 822  HIS   B C     1 
ATOM   10608 O  O     . HIS   B 1 822  ? 160.939 167.601 114.745 1.00 35.49  ? 822  HIS   B O     1 
ATOM   10609 C  CB    . HIS   B 1 822  ? 161.099 170.295 116.272 1.00 24.87  ? 822  HIS   B CB    1 
ATOM   10610 C  CG    . HIS   B 1 822  ? 161.742 171.361 115.443 1.00 32.62  ? 822  HIS   B CG    1 
ATOM   10611 N  ND1   . HIS   B 1 822  ? 161.279 171.713 114.193 1.00 36.00  ? 822  HIS   B ND1   1 
ATOM   10612 C  CD2   . HIS   B 1 822  ? 162.814 172.152 115.682 1.00 29.26  ? 822  HIS   B CD2   1 
ATOM   10613 C  CE1   . HIS   B 1 822  ? 162.037 172.675 113.700 1.00 34.52  ? 822  HIS   B CE1   1 
ATOM   10614 N  NE2   . HIS   B 1 822  ? 162.976 172.960 114.583 1.00 33.73  ? 822  HIS   B NE2   1 
ATOM   10615 N  N     . VAL   B 1 823  ? 160.274 169.134 113.227 1.00 25.99  ? 823  VAL   B N     1 
ATOM   10616 C  CA    . VAL   B 1 823  ? 160.704 168.379 112.056 1.00 28.62  ? 823  VAL   B CA    1 
ATOM   10617 C  C     . VAL   B 1 823  ? 161.890 169.095 111.429 1.00 33.12  ? 823  VAL   B C     1 
ATOM   10618 O  O     . VAL   B 1 823  ? 161.825 170.300 111.156 1.00 37.40  ? 823  VAL   B O     1 
ATOM   10619 C  CB    . VAL   B 1 823  ? 159.562 168.213 111.039 1.00 27.50  ? 823  VAL   B CB    1 
ATOM   10620 C  CG1   . VAL   B 1 823  ? 159.963 167.229 109.952 1.00 27.33  ? 823  VAL   B CG1   1 
ATOM   10621 C  CG2   . VAL   B 1 823  ? 158.294 167.752 111.736 1.00 27.78  ? 823  VAL   B CG2   1 
ATOM   10622 N  N     . HIS   B 1 824  ? 162.972 168.357 111.206 1.00 31.47  ? 824  HIS   B N     1 
ATOM   10623 C  CA    . HIS   B 1 824  ? 164.177 168.885 110.588 1.00 28.90  ? 824  HIS   B CA    1 
ATOM   10624 C  C     . HIS   B 1 824  ? 164.344 168.305 109.191 1.00 34.66  ? 824  HIS   B C     1 
ATOM   10625 O  O     . HIS   B 1 824  ? 164.233 167.094 108.985 1.00 37.95  ? 824  HIS   B O     1 
ATOM   10626 C  CB    . HIS   B 1 824  ? 165.416 168.570 111.430 1.00 28.07  ? 824  HIS   B CB    1 
ATOM   10627 C  CG    . HIS   B 1 824  ? 165.452 169.287 112.743 1.00 31.87  ? 824  HIS   B CG    1 
ATOM   10628 N  ND1   . HIS   B 1 824  ? 164.790 168.829 113.861 1.00 36.44  ? 824  HIS   B ND1   1 
ATOM   10629 C  CD2   . HIS   B 1 824  ? 166.073 170.431 113.116 1.00 35.43  ? 824  HIS   B CD2   1 
ATOM   10630 C  CE1   . HIS   B 1 824  ? 165.000 169.659 114.866 1.00 35.42  ? 824  HIS   B CE1   1 
ATOM   10631 N  NE2   . HIS   B 1 824  ? 165.776 170.640 114.441 1.00 39.41  ? 824  HIS   B NE2   1 
ATOM   10632 N  N     . MET   B 1 825  ? 164.615 169.185 108.231 1.00 43.61  ? 825  MET   B N     1 
ATOM   10633 C  CA    . MET   B 1 825  ? 164.810 168.800 106.843 1.00 40.96  ? 825  MET   B CA    1 
ATOM   10634 C  C     . MET   B 1 825  ? 166.250 169.084 106.439 1.00 39.89  ? 825  MET   B C     1 
ATOM   10635 O  O     . MET   B 1 825  ? 166.991 169.778 107.139 1.00 44.84  ? 825  MET   B O     1 
ATOM   10636 C  CB    . MET   B 1 825  ? 163.836 169.540 105.917 1.00 39.15  ? 825  MET   B CB    1 
ATOM   10637 C  CG    . MET   B 1 825  ? 162.473 168.881 105.797 1.00 39.74  ? 825  MET   B CG    1 
ATOM   10638 S  SD    . MET   B 1 825  ? 161.326 169.413 107.080 1.00 59.44  ? 825  MET   B SD    1 
ATOM   10639 C  CE    . MET   B 1 825  ? 161.674 171.168 107.140 1.00 49.53  ? 825  MET   B CE    1 
ATOM   10640 N  N     . GLY   B 1 826  ? 166.645 168.534 105.295 1.00 44.92  ? 826  GLY   B N     1 
ATOM   10641 C  CA    . GLY   B 1 826  ? 167.979 168.728 104.781 1.00 48.21  ? 826  GLY   B CA    1 
ATOM   10642 C  C     . GLY   B 1 826  ? 168.794 167.452 104.778 1.00 50.28  ? 826  GLY   B C     1 
ATOM   10643 O  O     . GLY   B 1 826  ? 168.287 166.359 105.047 1.00 51.08  ? 826  GLY   B O     1 
ATOM   10644 N  N     . PRO   B 1 827  ? 170.084 167.570 104.466 1.00 52.68  ? 827  PRO   B N     1 
ATOM   10645 C  CA    . PRO   B 1 827  ? 170.950 166.385 104.455 1.00 47.64  ? 827  PRO   B CA    1 
ATOM   10646 C  C     . PRO   B 1 827  ? 170.987 165.711 105.818 1.00 48.39  ? 827  PRO   B C     1 
ATOM   10647 O  O     . PRO   B 1 827  ? 170.962 166.369 106.859 1.00 52.27  ? 827  PRO   B O     1 
ATOM   10648 C  CB    . PRO   B 1 827  ? 172.321 166.953 104.069 1.00 48.84  ? 827  PRO   B CB    1 
ATOM   10649 C  CG    . PRO   B 1 827  ? 172.019 168.243 103.383 1.00 47.16  ? 827  PRO   B CG    1 
ATOM   10650 C  CD    . PRO   B 1 827  ? 170.803 168.788 104.061 1.00 49.35  ? 827  PRO   B CD    1 
ATOM   10651 N  N     . ARG   B 1 828  ? 171.053 164.378 105.799 1.00 48.98  ? 828  ARG   B N     1 
ATOM   10652 C  CA    . ARG   B 1 828  ? 171.007 163.616 107.043 1.00 49.54  ? 828  ARG   B CA    1 
ATOM   10653 C  C     . ARG   B 1 828  ? 172.203 163.921 107.937 1.00 53.09  ? 828  ARG   B C     1 
ATOM   10654 O  O     . ARG   B 1 828  ? 172.053 164.077 109.155 1.00 59.87  ? 828  ARG   B O     1 
ATOM   10655 C  CB    . ARG   B 1 828  ? 170.940 162.120 106.737 1.00 50.37  ? 828  ARG   B CB    1 
ATOM   10656 C  CG    . ARG   B 1 828  ? 171.125 161.233 107.955 1.00 51.00  ? 828  ARG   B CG    1 
ATOM   10657 C  CD    . ARG   B 1 828  ? 171.347 159.787 107.551 1.00 55.50  ? 828  ARG   B CD    1 
ATOM   10658 N  NE    . ARG   B 1 828  ? 172.355 159.668 106.505 1.00 59.30  ? 828  ARG   B NE    1 
ATOM   10659 C  CZ    . ARG   B 1 828  ? 173.660 159.787 106.704 1.00 59.09  ? 828  ARG   B CZ    1 
ATOM   10660 N  NH1   . ARG   B 1 828  ? 174.158 160.019 107.907 1.00 56.18  ? 828  ARG   B NH1   1 
ATOM   10661 N  NH2   . ARG   B 1 828  ? 174.487 159.670 105.669 1.00 55.54  ? 828  ARG   B NH2   1 
ATOM   10662 N  N     . ARG   B 1 829  ? 173.401 164.002 107.354 1.00 46.97  ? 829  ARG   B N     1 
ATOM   10663 C  CA    . ARG   B 1 829  ? 174.608 164.132 108.165 1.00 49.75  ? 829  ARG   B CA    1 
ATOM   10664 C  C     . ARG   B 1 829  ? 174.573 165.399 109.010 1.00 48.73  ? 829  ARG   B C     1 
ATOM   10665 O  O     . ARG   B 1 829  ? 174.754 165.349 110.232 1.00 50.31  ? 829  ARG   B O     1 
ATOM   10666 C  CB    . ARG   B 1 829  ? 175.844 164.115 107.265 1.00 48.96  ? 829  ARG   B CB    1 
ATOM   10667 N  N     . GLN   B 1 830  ? 174.337 166.549 108.377 1.00 47.51  ? 830  GLN   B N     1 
ATOM   10668 C  CA    . GLN   B 1 830  ? 174.242 167.794 109.131 1.00 48.31  ? 830  GLN   B CA    1 
ATOM   10669 C  C     . GLN   B 1 830  ? 172.980 167.835 109.981 1.00 52.87  ? 830  GLN   B C     1 
ATOM   10670 O  O     . GLN   B 1 830  ? 172.970 168.463 111.048 1.00 56.73  ? 830  GLN   B O     1 
ATOM   10671 C  CB    . GLN   B 1 830  ? 174.283 168.990 108.182 1.00 46.12  ? 830  GLN   B CB    1 
ATOM   10672 N  N     . ALA   B 1 831  ? 171.911 167.179 109.523 1.00 50.07  ? 831  ALA   B N     1 
ATOM   10673 C  CA    . ALA   B 1 831  ? 170.659 167.184 110.269 1.00 44.38  ? 831  ALA   B CA    1 
ATOM   10674 C  C     . ALA   B 1 831  ? 170.825 166.517 111.626 1.00 46.39  ? 831  ALA   B C     1 
ATOM   10675 O  O     . ALA   B 1 831  ? 170.228 166.952 112.615 1.00 50.42  ? 831  ALA   B O     1 
ATOM   10676 C  CB    . ALA   B 1 831  ? 169.563 166.492 109.461 1.00 44.95  ? 831  ALA   B CB    1 
ATOM   10677 N  N     . MET   B 1 832  ? 171.616 165.445 111.691 1.00 45.21  ? 832  MET   B N     1 
ATOM   10678 C  CA    . MET   B 1 832  ? 171.822 164.767 112.966 1.00 44.93  ? 832  MET   B CA    1 
ATOM   10679 C  C     . MET   B 1 832  ? 172.491 165.687 113.980 1.00 48.33  ? 832  MET   B C     1 
ATOM   10680 O  O     . MET   B 1 832  ? 172.074 165.757 115.140 1.00 49.00  ? 832  MET   B O     1 
ATOM   10681 C  CB    . MET   B 1 832  ? 172.642 163.495 112.761 1.00 43.98  ? 832  MET   B CB    1 
ATOM   10682 C  CG    . MET   B 1 832  ? 171.906 162.417 111.993 1.00 49.23  ? 832  MET   B CG    1 
ATOM   10683 S  SD    . MET   B 1 832  ? 170.127 162.703 112.012 1.00 62.68  ? 832  MET   B SD    1 
ATOM   10684 C  CE    . MET   B 1 832  ? 169.636 161.697 113.409 1.00 51.51  ? 832  MET   B CE    1 
ATOM   10685 N  N     . LYS   B 1 833  ? 173.533 166.408 113.559 1.00 48.22  ? 833  LYS   B N     1 
ATOM   10686 C  CA    . LYS   B 1 833  ? 174.191 167.342 114.467 1.00 48.29  ? 833  LYS   B CA    1 
ATOM   10687 C  C     . LYS   B 1 833  ? 173.255 168.478 114.862 1.00 51.54  ? 833  LYS   B C     1 
ATOM   10688 O  O     . LYS   B 1 833  ? 173.221 168.890 116.032 1.00 52.18  ? 833  LYS   B O     1 
ATOM   10689 C  CB    . LYS   B 1 833  ? 175.462 167.893 113.822 1.00 45.94  ? 833  LYS   B CB    1 
ATOM   10690 N  N     . GLU   B 1 834  ? 172.491 169.000 113.900 1.00 47.80  ? 834  GLU   B N     1 
ATOM   10691 C  CA    . GLU   B 1 834  ? 171.548 170.068 114.211 1.00 46.05  ? 834  GLU   B CA    1 
ATOM   10692 C  C     . GLU   B 1 834  ? 170.540 169.611 115.255 1.00 48.92  ? 834  GLU   B C     1 
ATOM   10693 O  O     . GLU   B 1 834  ? 170.259 170.328 116.221 1.00 52.09  ? 834  GLU   B O     1 
ATOM   10694 C  CB    . GLU   B 1 834  ? 170.838 170.530 112.938 1.00 45.60  ? 834  GLU   B CB    1 
ATOM   10695 C  CG    . GLU   B 1 834  ? 171.777 170.913 111.807 1.00 54.25  ? 834  GLU   B CG    1 
ATOM   10696 C  CD    . GLU   B 1 834  ? 171.789 172.403 111.534 1.00 58.39  ? 834  GLU   B CD    1 
ATOM   10697 O  OE1   . GLU   B 1 834  ? 171.830 173.187 112.505 1.00 61.33  ? 834  GLU   B OE1   1 
ATOM   10698 O  OE2   . GLU   B 1 834  ? 171.762 172.790 110.347 1.00 53.50  ? 834  GLU   B OE2   1 
ATOM   10699 N  N     . MET   B 1 835  ? 169.994 168.406 115.082 1.00 42.66  ? 835  MET   B N     1 
ATOM   10700 C  CA    . MET   B 1 835  ? 169.028 167.880 116.039 1.00 40.17  ? 835  MET   B CA    1 
ATOM   10701 C  C     . MET   B 1 835  ? 169.674 167.614 117.391 1.00 42.33  ? 835  MET   B C     1 
ATOM   10702 O  O     . MET   B 1 835  ? 169.055 167.845 118.434 1.00 46.72  ? 835  MET   B O     1 
ATOM   10703 C  CB    . MET   B 1 835  ? 168.384 166.607 115.492 1.00 39.94  ? 835  MET   B CB    1 
ATOM   10704 C  CG    . MET   B 1 835  ? 167.221 166.858 114.549 1.00 39.60  ? 835  MET   B CG    1 
ATOM   10705 S  SD    . MET   B 1 835  ? 166.660 165.360 113.724 1.00 52.71  ? 835  MET   B SD    1 
ATOM   10706 C  CE    . MET   B 1 835  ? 166.894 164.154 115.024 1.00 40.48  ? 835  MET   B CE    1 
ATOM   10707 N  N     . SER   B 1 836  ? 170.917 167.128 117.396 1.00 44.98  ? 836  SER   B N     1 
ATOM   10708 C  CA    . SER   B 1 836  ? 171.594 166.863 118.660 1.00 44.93  ? 836  SER   B CA    1 
ATOM   10709 C  C     . SER   B 1 836  ? 171.786 168.145 119.459 1.00 42.15  ? 836  SER   B C     1 
ATOM   10710 O  O     . SER   B 1 836  ? 171.592 168.159 120.679 1.00 44.61  ? 836  SER   B O     1 
ATOM   10711 C  CB    . SER   B 1 836  ? 172.937 166.182 118.405 1.00 49.50  ? 836  SER   B CB    1 
ATOM   10712 O  OG    . SER   B 1 836  ? 173.279 165.316 119.473 1.00 49.16  ? 836  SER   B OG    1 
ATOM   10713 N  N     . ILE   B 1 837  ? 172.171 169.233 118.790 1.00 38.16  ? 837  ILE   B N     1 
ATOM   10714 C  CA    . ILE   B 1 837  ? 172.329 170.500 119.500 1.00 34.11  ? 837  ILE   B CA    1 
ATOM   10715 C  C     . ILE   B 1 837  ? 170.970 171.057 119.916 1.00 41.76  ? 837  ILE   B C     1 
ATOM   10716 O  O     . ILE   B 1 837  ? 170.802 171.555 121.040 1.00 47.81  ? 837  ILE   B O     1 
ATOM   10717 C  CB    . ILE   B 1 837  ? 173.121 171.505 118.643 1.00 37.70  ? 837  ILE   B CB    1 
ATOM   10718 C  CG1   . ILE   B 1 837  ? 172.273 172.011 117.475 1.00 44.45  ? 837  ILE   B CG1   1 
ATOM   10719 C  CG2   . ILE   B 1 837  ? 174.406 170.874 118.134 1.00 40.75  ? 837  ILE   B CG2   1 
ATOM   10720 C  CD1   . ILE   B 1 837  ? 172.811 173.270 116.831 1.00 44.88  ? 837  ILE   B CD1   1 
ATOM   10721 N  N     . ASP   B 1 838  ? 169.980 170.976 119.022 1.00 40.79  ? 838  ASP   B N     1 
ATOM   10722 C  CA    . ASP   B 1 838  ? 168.672 171.563 119.288 1.00 33.19  ? 838  ASP   B CA    1 
ATOM   10723 C  C     . ASP   B 1 838  ? 167.972 170.865 120.444 1.00 34.71  ? 838  ASP   B C     1 
ATOM   10724 O  O     . ASP   B 1 838  ? 167.277 171.511 121.231 1.00 41.55  ? 838  ASP   B O     1 
ATOM   10725 C  CB    . ASP   B 1 838  ? 167.808 171.509 118.029 1.00 37.13  ? 838  ASP   B CB    1 
ATOM   10726 C  CG    . ASP   B 1 838  ? 168.067 172.673 117.094 1.00 42.28  ? 838  ASP   B CG    1 
ATOM   10727 O  OD1   . ASP   B 1 838  ? 168.964 173.488 117.392 1.00 45.17  ? 838  ASP   B OD1   1 
ATOM   10728 O  OD2   . ASP   B 1 838  ? 167.373 172.774 116.060 1.00 40.98  ? 838  ASP   B OD2   1 
ATOM   10729 N  N     . GLN   B 1 839  ? 168.125 169.545 120.555 1.00 31.76  ? 839  GLN   B N     1 
ATOM   10730 C  CA    . GLN   B 1 839  ? 167.483 168.827 121.649 1.00 34.44  ? 839  GLN   B CA    1 
ATOM   10731 C  C     . GLN   B 1 839  ? 167.914 169.395 122.992 1.00 42.29  ? 839  GLN   B C     1 
ATOM   10732 O  O     . GLN   B 1 839  ? 167.077 169.769 123.822 1.00 44.58  ? 839  GLN   B O     1 
ATOM   10733 C  CB    . GLN   B 1 839  ? 167.816 167.339 121.564 1.00 25.69  ? 839  GLN   B CB    1 
ATOM   10734 C  CG    . GLN   B 1 839  ? 167.524 166.578 122.841 1.00 34.79  ? 839  GLN   B CG    1 
ATOM   10735 C  CD    . GLN   B 1 839  ? 166.300 165.697 122.722 1.00 47.69  ? 839  GLN   B CD    1 
ATOM   10736 O  OE1   . GLN   B 1 839  ? 166.084 165.053 121.696 1.00 52.17  ? 839  GLN   B OE1   1 
ATOM   10737 N  NE2   . GLN   B 1 839  ? 165.483 165.673 123.768 1.00 43.05  ? 839  GLN   B NE2   1 
ATOM   10738 N  N     . ALA   B 1 840  ? 169.226 169.485 123.213 1.00 39.69  ? 840  ALA   B N     1 
ATOM   10739 C  CA    . ALA   B 1 840  ? 169.729 170.035 124.465 1.00 33.51  ? 840  ALA   B CA    1 
ATOM   10740 C  C     . ALA   B 1 840  ? 169.288 171.481 124.639 1.00 33.44  ? 840  ALA   B C     1 
ATOM   10741 O  O     . ALA   B 1 840  ? 168.768 171.861 125.697 1.00 36.67  ? 840  ALA   B O     1 
ATOM   10742 C  CB    . ALA   B 1 840  ? 171.253 169.923 124.508 1.00 35.80  ? 840  ALA   B CB    1 
ATOM   10743 N  N     . LYS   B 1 841  ? 169.471 172.303 123.600 1.00 31.72  ? 841  LYS   B N     1 
ATOM   10744 C  CA    . LYS   B 1 841  ? 169.129 173.716 123.715 1.00 28.71  ? 841  LYS   B CA    1 
ATOM   10745 C  C     . LYS   B 1 841  ? 167.680 173.898 124.151 1.00 33.33  ? 841  LYS   B C     1 
ATOM   10746 O  O     . LYS   B 1 841  ? 167.389 174.610 125.118 1.00 39.20  ? 841  LYS   B O     1 
ATOM   10747 C  CB    . LYS   B 1 841  ? 169.374 174.422 122.381 1.00 28.53  ? 841  LYS   B CB    1 
ATOM   10748 C  CG    . LYS   B 1 841  ? 168.609 175.724 122.226 1.00 33.72  ? 841  LYS   B CG    1 
ATOM   10749 C  CD    . LYS   B 1 841  ? 169.406 176.750 121.443 1.00 37.67  ? 841  LYS   B CD    1 
ATOM   10750 C  CE    . LYS   B 1 841  ? 169.379 176.437 119.956 1.00 38.79  ? 841  LYS   B CE    1 
ATOM   10751 N  NZ    . LYS   B 1 841  ? 169.103 177.646 119.134 1.00 40.89  ? 841  LYS   B NZ    1 
ATOM   10752 N  N     . TYR   B 1 842  ? 166.758 173.229 123.460 1.00 37.73  ? 842  TYR   B N     1 
ATOM   10753 C  CA    . TYR   B 1 842  ? 165.339 173.459 123.684 1.00 32.28  ? 842  TYR   B CA    1 
ATOM   10754 C  C     . TYR   B 1 842  ? 164.829 172.776 124.944 1.00 33.42  ? 842  TYR   B C     1 
ATOM   10755 O  O     . TYR   B 1 842  ? 163.941 173.317 125.606 1.00 36.17  ? 842  TYR   B O     1 
ATOM   10756 C  CB    . TYR   B 1 842  ? 164.546 173.009 122.458 1.00 32.06  ? 842  TYR   B CB    1 
ATOM   10757 C  CG    . TYR   B 1 842  ? 164.830 173.868 121.250 1.00 32.15  ? 842  TYR   B CG    1 
ATOM   10758 C  CD1   . TYR   B 1 842  ? 164.830 175.252 121.348 1.00 34.31  ? 842  TYR   B CD1   1 
ATOM   10759 C  CD2   . TYR   B 1 842  ? 165.123 173.299 120.020 1.00 32.41  ? 842  TYR   B CD2   1 
ATOM   10760 C  CE1   . TYR   B 1 842  ? 165.098 176.045 120.255 1.00 32.84  ? 842  TYR   B CE1   1 
ATOM   10761 C  CE2   . TYR   B 1 842  ? 165.392 174.085 118.919 1.00 38.14  ? 842  TYR   B CE2   1 
ATOM   10762 C  CZ    . TYR   B 1 842  ? 165.379 175.457 119.042 1.00 38.90  ? 842  TYR   B CZ    1 
ATOM   10763 O  OH    . TYR   B 1 842  ? 165.647 176.246 117.949 1.00 41.83  ? 842  TYR   B OH    1 
ATOM   10764 N  N     . GLN   B 1 843  ? 165.361 171.606 125.308 1.00 30.30  ? 843  GLN   B N     1 
ATOM   10765 C  CA    . GLN   B 1 843  ? 164.991 171.027 126.594 1.00 24.91  ? 843  GLN   B CA    1 
ATOM   10766 C  C     . GLN   B 1 843  ? 165.428 171.927 127.741 1.00 37.87  ? 843  GLN   B C     1 
ATOM   10767 O  O     . GLN   B 1 843  ? 164.665 172.153 128.692 1.00 41.41  ? 843  GLN   B O     1 
ATOM   10768 C  CB    . GLN   B 1 843  ? 165.590 169.630 126.739 1.00 28.31  ? 843  GLN   B CB    1 
ATOM   10769 C  CG    . GLN   B 1 843  ? 164.877 168.759 127.762 1.00 34.08  ? 843  GLN   B CG    1 
ATOM   10770 C  CD    . GLN   B 1 843  ? 163.381 168.683 127.525 1.00 36.56  ? 843  GLN   B CD    1 
ATOM   10771 O  OE1   . GLN   B 1 843  ? 162.919 168.028 126.590 1.00 42.41  ? 843  GLN   B OE1   1 
ATOM   10772 N  NE2   . GLN   B 1 843  ? 162.614 169.355 128.375 1.00 32.75  ? 843  GLN   B NE2   1 
ATOM   10773 N  N     . ARG   B 1 844  ? 166.651 172.460 127.668 1.00 39.29  ? 844  ARG   B N     1 
ATOM   10774 C  CA    . ARG   B 1 844  ? 167.101 173.389 128.697 1.00 40.35  ? 844  ARG   B CA    1 
ATOM   10775 C  C     . ARG   B 1 844  ? 166.229 174.637 128.723 1.00 41.51  ? 844  ARG   B C     1 
ATOM   10776 O  O     . ARG   B 1 844  ? 165.875 175.133 129.798 1.00 42.51  ? 844  ARG   B O     1 
ATOM   10777 C  CB    . ARG   B 1 844  ? 168.567 173.758 128.468 1.00 35.30  ? 844  ARG   B CB    1 
ATOM   10778 N  N     . TRP   B 1 845  ? 165.868 175.156 127.547 1.00 31.94  ? 845  TRP   B N     1 
ATOM   10779 C  CA    . TRP   B 1 845  ? 165.014 176.338 127.495 1.00 32.31  ? 845  TRP   B CA    1 
ATOM   10780 C  C     . TRP   B 1 845  ? 163.651 176.060 128.117 1.00 38.44  ? 845  TRP   B C     1 
ATOM   10781 O  O     . TRP   B 1 845  ? 163.122 176.887 128.869 1.00 45.95  ? 845  TRP   B O     1 
ATOM   10782 C  CB    . TRP   B 1 845  ? 164.862 176.808 126.049 1.00 33.39  ? 845  TRP   B CB    1 
ATOM   10783 C  CG    . TRP   B 1 845  ? 163.919 177.959 125.883 1.00 39.69  ? 845  TRP   B CG    1 
ATOM   10784 C  CD1   . TRP   B 1 845  ? 164.238 179.283 125.906 1.00 41.12  ? 845  TRP   B CD1   1 
ATOM   10785 C  CD2   . TRP   B 1 845  ? 162.505 177.891 125.660 1.00 42.29  ? 845  TRP   B CD2   1 
ATOM   10786 N  NE1   . TRP   B 1 845  ? 163.113 180.046 125.717 1.00 45.62  ? 845  TRP   B NE1   1 
ATOM   10787 C  CE2   . TRP   B 1 845  ? 162.035 179.215 125.563 1.00 40.49  ? 845  TRP   B CE2   1 
ATOM   10788 C  CE3   . TRP   B 1 845  ? 161.591 176.841 125.536 1.00 39.95  ? 845  TRP   B CE3   1 
ATOM   10789 C  CZ2   . TRP   B 1 845  ? 160.693 179.517 125.347 1.00 36.55  ? 845  TRP   B CZ2   1 
ATOM   10790 C  CZ3   . TRP   B 1 845  ? 160.258 177.143 125.323 1.00 38.27  ? 845  TRP   B CZ3   1 
ATOM   10791 C  CH2   . TRP   B 1 845  ? 159.822 178.470 125.231 1.00 35.59  ? 845  TRP   B CH2   1 
ATOM   10792 N  N     . LEU   B 1 846  ? 163.066 174.900 127.815 1.00 37.28  ? 846  LEU   B N     1 
ATOM   10793 C  CA    . LEU   B 1 846  ? 161.769 174.547 128.380 1.00 33.65  ? 846  LEU   B CA    1 
ATOM   10794 C  C     . LEU   B 1 846  ? 161.844 174.443 129.897 1.00 36.02  ? 846  LEU   B C     1 
ATOM   10795 O  O     . LEU   B 1 846  ? 161.017 175.019 130.613 1.00 39.27  ? 846  LEU   B O     1 
ATOM   10796 C  CB    . LEU   B 1 846  ? 161.275 173.232 127.777 1.00 33.05  ? 846  LEU   B CB    1 
ATOM   10797 C  CG    . LEU   B 1 846  ? 160.656 173.281 126.379 1.00 34.43  ? 846  LEU   B CG    1 
ATOM   10798 C  CD1   . LEU   B 1 846  ? 160.509 171.878 125.811 1.00 33.24  ? 846  LEU   B CD1   1 
ATOM   10799 C  CD2   . LEU   B 1 846  ? 159.315 173.992 126.406 1.00 38.40  ? 846  LEU   B CD2   1 
ATOM   10800 N  N     . ILE   B 1 847  ? 162.836 173.709 130.408 1.00 32.06  ? 847  ILE   B N     1 
ATOM   10801 C  CA    . ILE   B 1 847  ? 162.938 173.523 131.853 1.00 28.26  ? 847  ILE   B CA    1 
ATOM   10802 C  C     . ILE   B 1 847  ? 163.188 174.856 132.545 1.00 33.29  ? 847  ILE   B C     1 
ATOM   10803 O  O     . ILE   B 1 847  ? 162.633 175.131 133.616 1.00 41.57  ? 847  ILE   B O     1 
ATOM   10804 C  CB    . ILE   B 1 847  ? 164.030 172.492 132.188 1.00 29.49  ? 847  ILE   B CB    1 
ATOM   10805 C  CG1   . ILE   B 1 847  ? 163.502 171.075 131.960 1.00 31.54  ? 847  ILE   B CG1   1 
ATOM   10806 C  CG2   . ILE   B 1 847  ? 164.491 172.656 133.626 1.00 31.88  ? 847  ILE   B CG2   1 
ATOM   10807 C  CD1   . ILE   B 1 847  ? 164.579 170.022 131.904 1.00 38.80  ? 847  ILE   B CD1   1 
ATOM   10808 N  N     . LYS   B 1 848  ? 164.028 175.703 131.948 1.00 39.34  ? 848  LYS   B N     1 
ATOM   10809 C  CA    . LYS   B 1 848  ? 164.280 177.020 132.523 1.00 42.38  ? 848  LYS   B CA    1 
ATOM   10810 C  C     . LYS   B 1 848  ? 163.025 177.882 132.527 1.00 43.08  ? 848  LYS   B C     1 
ATOM   10811 O  O     . LYS   B 1 848  ? 162.893 178.780 133.367 1.00 47.84  ? 848  LYS   B O     1 
ATOM   10812 C  CB    . LYS   B 1 848  ? 165.404 177.717 131.756 1.00 36.22  ? 848  LYS   B CB    1 
ATOM   10813 N  N     . ASN   B 1 849  ? 162.096 177.631 131.608 1.00 37.54  ? 849  ASN   B N     1 
ATOM   10814 C  CA    . ASN   B 1 849  ? 160.884 178.430 131.496 1.00 37.96  ? 849  ASN   B CA    1 
ATOM   10815 C  C     . ASN   B 1 849  ? 159.682 177.796 132.185 1.00 45.71  ? 849  ASN   B C     1 
ATOM   10816 O  O     . ASN   B 1 849  ? 158.573 178.329 132.076 1.00 47.90  ? 849  ASN   B O     1 
ATOM   10817 C  CB    . ASN   B 1 849  ? 160.558 178.690 130.023 1.00 43.69  ? 849  ASN   B CB    1 
ATOM   10818 C  CG    . ASN   B 1 849  ? 160.908 180.099 129.592 1.00 48.03  ? 849  ASN   B CG    1 
ATOM   10819 O  OD1   . ASN   B 1 849  ? 161.305 180.928 130.411 1.00 48.44  ? 849  ASN   B OD1   1 
ATOM   10820 N  ND2   . ASN   B 1 849  ? 160.754 180.382 128.305 1.00 47.57  ? 849  ASN   B ND2   1 
ATOM   10821 N  N     . LYS   B 1 850  ? 159.869 176.677 132.885 1.00 42.59  ? 850  LYS   B N     1 
ATOM   10822 C  CA    . LYS   B 1 850  ? 158.820 176.065 133.696 1.00 41.39  ? 850  LYS   B CA    1 
ATOM   10823 C  C     . LYS   B 1 850  ? 157.737 175.402 132.849 1.00 45.83  ? 850  LYS   B C     1 
ATOM   10824 O  O     . LYS   B 1 850  ? 156.579 175.325 133.265 1.00 48.17  ? 850  LYS   B O     1 
ATOM   10825 C  CB    . LYS   B 1 850  ? 158.192 177.089 134.648 1.00 41.15  ? 850  LYS   B CB    1 
ATOM   10826 C  CG    . LYS   B 1 850  ? 159.167 177.681 135.651 1.00 40.11  ? 850  LYS   B CG    1 
ATOM   10827 C  CD    . LYS   B 1 850  ? 159.152 176.906 136.957 1.00 42.56  ? 850  LYS   B CD    1 
ATOM   10828 C  CE    . LYS   B 1 850  ? 160.402 177.175 137.777 1.00 42.94  ? 850  LYS   B CE    1 
ATOM   10829 N  NZ    . LYS   B 1 850  ? 161.637 177.080 136.954 1.00 46.42  ? 850  LYS   B NZ    1 
ATOM   10830 N  N     . MET   B 1 851  ? 158.094 174.917 131.664 1.00 43.04  ? 851  MET   B N     1 
ATOM   10831 C  CA    . MET   B 1 851  ? 157.176 174.172 130.813 1.00 31.72  ? 851  MET   B CA    1 
ATOM   10832 C  C     . MET   B 1 851  ? 157.379 172.681 131.042 1.00 37.05  ? 851  MET   B C     1 
ATOM   10833 O  O     . MET   B 1 851  ? 158.484 172.164 130.847 1.00 46.44  ? 851  MET   B O     1 
ATOM   10834 C  CB    . MET   B 1 851  ? 157.385 174.513 129.339 1.00 31.61  ? 851  MET   B CB    1 
ATOM   10835 C  CG    . MET   B 1 851  ? 157.082 175.949 128.985 1.00 37.75  ? 851  MET   B CG    1 
ATOM   10836 S  SD    . MET   B 1 851  ? 155.353 176.141 128.520 1.00 58.54  ? 851  MET   B SD    1 
ATOM   10837 C  CE    . MET   B 1 851  ? 155.197 177.921 128.528 1.00 40.21  ? 851  MET   B CE    1 
ATOM   10838 N  N     . LYS   B 1 852  ? 156.316 171.997 131.452 1.00 23.17  ? 852  LYS   B N     1 
ATOM   10839 C  CA    . LYS   B 1 852  ? 156.353 170.548 131.639 1.00 27.82  ? 852  LYS   B CA    1 
ATOM   10840 C  C     . LYS   B 1 852  ? 156.084 169.817 130.328 1.00 36.35  ? 852  LYS   B C     1 
ATOM   10841 O  O     . LYS   B 1 852  ? 155.233 168.934 130.242 1.00 42.85  ? 852  LYS   B O     1 
ATOM   10842 C  CB    . LYS   B 1 852  ? 155.353 170.134 132.714 1.00 30.69  ? 852  LYS   B CB    1 
ATOM   10843 C  CG    . LYS   B 1 852  ? 155.011 171.223 133.723 1.00 34.41  ? 852  LYS   B CG    1 
ATOM   10844 C  CD    . LYS   B 1 852  ? 156.255 171.786 134.397 1.00 40.13  ? 852  LYS   B CD    1 
ATOM   10845 C  CE    . LYS   B 1 852  ? 156.755 170.871 135.503 1.00 35.24  ? 852  LYS   B CE    1 
ATOM   10846 N  NZ    . LYS   B 1 852  ? 155.860 170.886 136.690 1.00 39.27  ? 852  LYS   B NZ    1 
ATOM   10847 N  N     . ALA   B 1 853  ? 156.822 170.190 129.288 1.00 26.69  ? 853  ALA   B N     1 
ATOM   10848 C  CA    . ALA   B 1 853  ? 156.675 169.608 127.965 1.00 16.57  ? 853  ALA   B CA    1 
ATOM   10849 C  C     . ALA   B 1 853  ? 157.916 168.807 127.596 1.00 21.79  ? 853  ALA   B C     1 
ATOM   10850 O  O     . ALA   B 1 853  ? 158.976 168.937 128.214 1.00 29.78  ? 853  ALA   B O     1 
ATOM   10851 C  CB    . ALA   B 1 853  ? 156.420 170.693 126.915 1.00 24.60  ? 853  ALA   B CB    1 
ATOM   10852 N  N     . PHE   B 1 854  ? 157.766 167.968 126.576 1.00 23.36  ? 854  PHE   B N     1 
ATOM   10853 C  CA    . PHE   B 1 854  ? 158.855 167.163 126.040 1.00 13.40  ? 854  PHE   B CA    1 
ATOM   10854 C  C     . PHE   B 1 854  ? 159.164 167.617 124.622 1.00 19.08  ? 854  PHE   B C     1 
ATOM   10855 O  O     . PHE   B 1 854  ? 158.269 167.661 123.772 1.00 27.95  ? 854  PHE   B O     1 
ATOM   10856 C  CB    . PHE   B 1 854  ? 158.495 165.677 126.045 1.00 6.94   ? 854  PHE   B CB    1 
ATOM   10857 C  CG    . PHE   B 1 854  ? 158.327 165.098 127.416 1.00 15.91  ? 854  PHE   B CG    1 
ATOM   10858 C  CD1   . PHE   B 1 854  ? 157.140 165.262 128.109 1.00 20.54  ? 854  PHE   B CD1   1 
ATOM   10859 C  CD2   . PHE   B 1 854  ? 159.349 164.384 128.013 1.00 17.20  ? 854  PHE   B CD2   1 
ATOM   10860 C  CE1   . PHE   B 1 854  ? 156.980 164.730 129.370 1.00 18.17  ? 854  PHE   B CE1   1 
ATOM   10861 C  CE2   . PHE   B 1 854  ? 159.194 163.850 129.274 1.00 19.42  ? 854  PHE   B CE2   1 
ATOM   10862 C  CZ    . PHE   B 1 854  ? 158.008 164.023 129.953 1.00 17.74  ? 854  PHE   B CZ    1 
ATOM   10863 N  N     . TYR   B 1 855  ? 160.426 167.955 124.372 1.00 22.52  ? 855  TYR   B N     1 
ATOM   10864 C  CA    . TYR   B 1 855  ? 160.871 168.295 123.028 1.00 19.11  ? 855  TYR   B CA    1 
ATOM   10865 C  C     . TYR   B 1 855  ? 161.108 167.016 122.235 1.00 23.63  ? 855  TYR   B C     1 
ATOM   10866 O  O     . TYR   B 1 855  ? 161.780 166.096 122.711 1.00 30.16  ? 855  TYR   B O     1 
ATOM   10867 C  CB    . TYR   B 1 855  ? 162.145 169.136 123.090 1.00 25.62  ? 855  TYR   B CB    1 
ATOM   10868 C  CG    . TYR   B 1 855  ? 162.657 169.578 121.743 1.00 29.97  ? 855  TYR   B CG    1 
ATOM   10869 C  CD1   . TYR   B 1 855  ? 161.929 170.460 120.958 1.00 28.58  ? 855  TYR   B CD1   1 
ATOM   10870 C  CD2   . TYR   B 1 855  ? 163.870 169.114 121.254 1.00 18.29  ? 855  TYR   B CD2   1 
ATOM   10871 C  CE1   . TYR   B 1 855  ? 162.393 170.867 119.726 1.00 30.17  ? 855  TYR   B CE1   1 
ATOM   10872 C  CE2   . TYR   B 1 855  ? 164.342 169.514 120.024 1.00 16.85  ? 855  TYR   B CE2   1 
ATOM   10873 C  CZ    . TYR   B 1 855  ? 163.600 170.391 119.264 1.00 25.65  ? 855  TYR   B CZ    1 
ATOM   10874 O  OH    . TYR   B 1 855  ? 164.070 170.791 118.036 1.00 36.95  ? 855  TYR   B OH    1 
ATOM   10875 N  N     . ALA   B 1 856  ? 160.548 166.952 121.027 1.00 21.62  ? 856  ALA   B N     1 
ATOM   10876 C  CA    . ALA   B 1 856  ? 160.606 165.752 120.193 1.00 21.56  ? 856  ALA   B CA    1 
ATOM   10877 C  C     . ALA   B 1 856  ? 160.981 166.132 118.767 1.00 27.48  ? 856  ALA   B C     1 
ATOM   10878 O  O     . ALA   B 1 856  ? 160.108 166.431 117.940 1.00 34.14  ? 856  ALA   B O     1 
ATOM   10879 C  CB    . ALA   B 1 856  ? 159.280 164.996 120.227 1.00 22.31  ? 856  ALA   B CB    1 
ATOM   10880 N  N     . PRO   B 1 857  ? 162.273 166.132 118.440 1.00 29.63  ? 857  PRO   B N     1 
ATOM   10881 C  CA    . PRO   B 1 857  ? 162.693 166.406 117.062 1.00 21.43  ? 857  PRO   B CA    1 
ATOM   10882 C  C     . PRO   B 1 857  ? 162.814 165.141 116.226 1.00 23.93  ? 857  PRO   B C     1 
ATOM   10883 O  O     . PRO   B 1 857  ? 163.272 164.095 116.689 1.00 29.52  ? 857  PRO   B O     1 
ATOM   10884 C  CB    . PRO   B 1 857  ? 164.065 167.064 117.255 1.00 21.93  ? 857  PRO   B CB    1 
ATOM   10885 C  CG    . PRO   B 1 857  ? 164.599 166.431 118.501 1.00 19.01  ? 857  PRO   B CG    1 
ATOM   10886 C  CD    . PRO   B 1 857  ? 163.423 166.000 119.351 1.00 24.49  ? 857  PRO   B CD    1 
ATOM   10887 N  N     . VAL   B 1 858  ? 162.388 165.249 114.968 1.00 25.76  ? 858  VAL   B N     1 
ATOM   10888 C  CA    . VAL   B 1 858  ? 162.533 164.180 113.990 1.00 22.36  ? 858  VAL   B CA    1 
ATOM   10889 C  C     . VAL   B 1 858  ? 163.168 164.761 112.735 1.00 25.52  ? 858  VAL   B C     1 
ATOM   10890 O  O     . VAL   B 1 858  ? 163.133 165.969 112.493 1.00 25.15  ? 858  VAL   B O     1 
ATOM   10891 C  CB    . VAL   B 1 858  ? 161.188 163.503 113.643 1.00 21.26  ? 858  VAL   B CB    1 
ATOM   10892 C  CG1   . VAL   B 1 858  ? 160.717 162.627 114.791 1.00 26.50  ? 858  VAL   B CG1   1 
ATOM   10893 C  CG2   . VAL   B 1 858  ? 160.141 164.546 113.291 1.00 22.10  ? 858  VAL   B CG2   1 
ATOM   10894 N  N     . HIS   B 1 859  ? 163.756 163.879 111.933 1.00 30.24  ? 859  HIS   B N     1 
ATOM   10895 C  CA    . HIS   B 1 859  ? 164.339 164.247 110.649 1.00 22.50  ? 859  HIS   B CA    1 
ATOM   10896 C  C     . HIS   B 1 859  ? 163.538 163.588 109.536 1.00 25.94  ? 859  HIS   B C     1 
ATOM   10897 O  O     . HIS   B 1 859  ? 163.378 162.363 109.522 1.00 30.26  ? 859  HIS   B O     1 
ATOM   10898 C  CB    . HIS   B 1 859  ? 165.809 163.836 110.567 1.00 28.29  ? 859  HIS   B CB    1 
ATOM   10899 C  CG    . HIS   B 1 859  ? 166.413 164.027 109.211 1.00 32.97  ? 859  HIS   B CG    1 
ATOM   10900 N  ND1   . HIS   B 1 859  ? 166.799 162.972 108.412 1.00 32.72  ? 859  HIS   B ND1   1 
ATOM   10901 C  CD2   . HIS   B 1 859  ? 166.687 165.150 108.507 1.00 35.07  ? 859  HIS   B CD2   1 
ATOM   10902 C  CE1   . HIS   B 1 859  ? 167.291 163.438 107.278 1.00 34.75  ? 859  HIS   B CE1   1 
ATOM   10903 N  NE2   . HIS   B 1 859  ? 167.233 164.757 107.310 1.00 29.33  ? 859  HIS   B NE2   1 
ATOM   10904 N  N     . ALA   B 1 860  ? 163.049 164.400 108.605 1.00 31.10  ? 860  ALA   B N     1 
ATOM   10905 C  CA    . ALA   B 1 860  ? 162.298 163.908 107.460 1.00 32.68  ? 860  ALA   B CA    1 
ATOM   10906 C  C     . ALA   B 1 860  ? 162.416 164.929 106.340 1.00 31.90  ? 860  ALA   B C     1 
ATOM   10907 O  O     . ALA   B 1 860  ? 162.822 166.072 106.561 1.00 34.71  ? 860  ALA   B O     1 
ATOM   10908 C  CB    . ALA   B 1 860  ? 160.830 163.649 107.813 1.00 33.43  ? 860  ALA   B CB    1 
ATOM   10909 N  N     . ASP   B 1 861  ? 162.052 164.501 105.132 1.00 32.28  ? 861  ASP   B N     1 
ATOM   10910 C  CA    . ASP   B 1 861  ? 162.175 165.364 103.965 1.00 40.81  ? 861  ASP   B CA    1 
ATOM   10911 C  C     . ASP   B 1 861  ? 160.996 166.312 103.795 1.00 36.40  ? 861  ASP   B C     1 
ATOM   10912 O  O     . ASP   B 1 861  ? 161.042 167.175 102.913 1.00 46.24  ? 861  ASP   B O     1 
ATOM   10913 C  CB    . ASP   B 1 861  ? 162.346 164.518 102.701 1.00 48.52  ? 861  ASP   B CB    1 
ATOM   10914 C  CG    . ASP   B 1 861  ? 161.497 163.266 102.722 1.00 49.71  ? 861  ASP   B CG    1 
ATOM   10915 O  OD1   . ASP   B 1 861  ? 160.670 163.129 103.645 1.00 46.03  ? 861  ASP   B OD1   1 
ATOM   10916 O  OD2   . ASP   B 1 861  ? 161.658 162.419 101.818 1.00 50.08  ? 861  ASP   B OD2   1 
ATOM   10917 N  N     . ASP   B 1 862  ? 159.950 166.178 104.607 1.00 34.67  ? 862  ASP   B N     1 
ATOM   10918 C  CA    . ASP   B 1 862  ? 158.839 167.118 104.574 1.00 36.88  ? 862  ASP   B CA    1 
ATOM   10919 C  C     . ASP   B 1 862  ? 158.094 167.043 105.897 1.00 38.67  ? 862  ASP   B C     1 
ATOM   10920 O  O     . ASP   B 1 862  ? 158.185 166.054 106.629 1.00 40.70  ? 862  ASP   B O     1 
ATOM   10921 C  CB    . ASP   B 1 862  ? 157.897 166.842 103.396 1.00 38.12  ? 862  ASP   B CB    1 
ATOM   10922 C  CG    . ASP   B 1 862  ? 156.997 165.647 103.633 1.00 46.27  ? 862  ASP   B CG    1 
ATOM   10923 O  OD1   . ASP   B 1 862  ? 157.411 164.721 104.360 1.00 48.31  ? 862  ASP   B OD1   1 
ATOM   10924 O  OD2   . ASP   B 1 862  ? 155.872 165.635 103.092 1.00 48.17  ? 862  ASP   B OD2   1 
ATOM   10925 N  N     . LEU   B 1 863  ? 157.348 168.110 106.193 1.00 32.58  ? 863  LEU   B N     1 
ATOM   10926 C  CA    . LEU   B 1 863  ? 156.627 168.182 107.459 1.00 30.64  ? 863  LEU   B CA    1 
ATOM   10927 C  C     . LEU   B 1 863  ? 155.572 167.091 107.570 1.00 27.41  ? 863  LEU   B C     1 
ATOM   10928 O  O     . LEU   B 1 863  ? 155.307 166.592 108.671 1.00 30.03  ? 863  LEU   B O     1 
ATOM   10929 C  CB    . LEU   B 1 863  ? 155.986 169.561 107.615 1.00 28.60  ? 863  LEU   B CB    1 
ATOM   10930 C  CG    . LEU   B 1 863  ? 154.790 169.665 108.562 1.00 29.81  ? 863  LEU   B CG    1 
ATOM   10931 C  CD1   . LEU   B 1 863  ? 155.208 169.354 109.988 1.00 33.23  ? 863  LEU   B CD1   1 
ATOM   10932 C  CD2   . LEU   B 1 863  ? 154.162 171.045 108.473 1.00 29.39  ? 863  LEU   B CD2   1 
ATOM   10933 N  N     . ARG   B 1 864  ? 154.961 166.706 106.448 1.00 27.50  ? 864  ARG   B N     1 
ATOM   10934 C  CA    . ARG   B 1 864  ? 153.915 165.690 106.486 1.00 29.30  ? 864  ARG   B CA    1 
ATOM   10935 C  C     . ARG   B 1 864  ? 154.428 164.392 107.096 1.00 34.46  ? 864  ARG   B C     1 
ATOM   10936 O  O     . ARG   B 1 864  ? 153.835 163.857 108.040 1.00 36.98  ? 864  ARG   B O     1 
ATOM   10937 C  CB    . ARG   B 1 864  ? 153.384 165.438 105.076 1.00 33.00  ? 864  ARG   B CB    1 
ATOM   10938 C  CG    . ARG   B 1 864  ? 152.042 166.073 104.786 1.00 38.13  ? 864  ARG   B CG    1 
ATOM   10939 C  CD    . ARG   B 1 864  ? 150.912 165.283 105.417 1.00 35.72  ? 864  ARG   B CD    1 
ATOM   10940 N  NE    . ARG   B 1 864  ? 150.617 164.054 104.690 1.00 39.44  ? 864  ARG   B NE    1 
ATOM   10941 C  CZ    . ARG   B 1 864  ? 150.269 163.997 103.411 1.00 41.09  ? 864  ARG   B CZ    1 
ATOM   10942 N  NH1   . ARG   B 1 864  ? 150.207 165.085 102.662 1.00 43.78  ? 864  ARG   B NH1   1 
ATOM   10943 N  NH2   . ARG   B 1 864  ? 149.985 162.818 102.869 1.00 39.61  ? 864  ARG   B NH2   1 
ATOM   10944 N  N     . GLU   B 1 865  ? 155.543 163.874 106.581 1.00 36.30  ? 865  GLU   B N     1 
ATOM   10945 C  CA    . GLU   B 1 865  ? 156.012 162.576 107.048 1.00 39.08  ? 865  GLU   B CA    1 
ATOM   10946 C  C     . GLU   B 1 865  ? 156.679 162.666 108.415 1.00 33.00  ? 865  GLU   B C     1 
ATOM   10947 O  O     . GLU   B 1 865  ? 156.685 161.682 109.157 1.00 36.34  ? 865  GLU   B O     1 
ATOM   10948 C  CB    . GLU   B 1 865  ? 156.955 161.951 106.019 1.00 34.92  ? 865  GLU   B CB    1 
ATOM   10949 C  CG    . GLU   B 1 865  ? 158.423 162.245 106.224 1.00 34.32  ? 865  GLU   B CG    1 
ATOM   10950 C  CD    . GLU   B 1 865  ? 159.305 161.328 105.400 1.00 47.51  ? 865  GLU   B CD    1 
ATOM   10951 O  OE1   . GLU   B 1 865  ? 160.536 161.336 105.607 1.00 47.33  ? 865  GLU   B OE1   1 
ATOM   10952 O  OE2   . GLU   B 1 865  ? 158.765 160.599 104.542 1.00 48.78  ? 865  GLU   B OE2   1 
ATOM   10953 N  N     . GLY   B 1 866  ? 157.225 163.827 108.779 1.00 23.46  ? 866  GLY   B N     1 
ATOM   10954 C  CA    . GLY   B 1 866  ? 157.691 164.002 110.146 1.00 23.13  ? 866  GLY   B CA    1 
ATOM   10955 C  C     . GLY   B 1 866  ? 156.553 163.941 111.147 1.00 25.91  ? 866  GLY   B C     1 
ATOM   10956 O  O     . GLY   B 1 866  ? 156.641 163.264 112.178 1.00 29.75  ? 866  GLY   B O     1 
ATOM   10957 N  N     . ALA   B 1 867  ? 155.459 164.649 110.852 1.00 30.04  ? 867  ALA   B N     1 
ATOM   10958 C  CA    . ALA   B 1 867  ? 154.272 164.542 111.689 1.00 20.95  ? 867  ALA   B CA    1 
ATOM   10959 C  C     . ALA   B 1 867  ? 153.723 163.124 111.689 1.00 18.40  ? 867  ALA   B C     1 
ATOM   10960 O  O     . ALA   B 1 867  ? 153.177 162.670 112.699 1.00 22.11  ? 867  ALA   B O     1 
ATOM   10961 C  CB    . ALA   B 1 867  ? 153.206 165.531 111.219 1.00 18.47  ? 867  ALA   B CB    1 
ATOM   10962 N  N     . GLN   B 1 868  ? 153.849 162.414 110.567 1.00 21.17  ? 868  GLN   B N     1 
ATOM   10963 C  CA    . GLN   B 1 868  ? 153.454 161.009 110.534 1.00 17.73  ? 868  GLN   B CA    1 
ATOM   10964 C  C     . GLN   B 1 868  ? 154.294 160.186 111.503 1.00 20.63  ? 868  GLN   B C     1 
ATOM   10965 O  O     . GLN   B 1 868  ? 153.763 159.378 112.276 1.00 19.64  ? 868  GLN   B O     1 
ATOM   10966 C  CB    . GLN   B 1 868  ? 153.583 160.467 109.111 1.00 15.76  ? 868  GLN   B CB    1 
ATOM   10967 C  CG    . GLN   B 1 868  ? 152.978 159.088 108.902 1.00 24.00  ? 868  GLN   B CG    1 
ATOM   10968 C  CD    . GLN   B 1 868  ? 151.492 159.045 109.194 1.00 34.25  ? 868  GLN   B CD    1 
ATOM   10969 O  OE1   . GLN   B 1 868  ? 150.915 157.971 109.365 1.00 32.03  ? 868  GLN   B OE1   1 
ATOM   10970 N  NE2   . GLN   B 1 868  ? 150.862 160.212 109.246 1.00 28.31  ? 868  GLN   B NE2   1 
ATOM   10971 N  N     . TYR   B 1 869  ? 155.615 160.377 111.469 1.00 29.79  ? 869  TYR   B N     1 
ATOM   10972 C  CA    . TYR   B 1 869  ? 156.494 159.726 112.433 1.00 16.78  ? 869  TYR   B CA    1 
ATOM   10973 C  C     . TYR   B 1 869  ? 156.003 159.979 113.849 1.00 19.54  ? 869  TYR   B C     1 
ATOM   10974 O  O     . TYR   B 1 869  ? 155.854 159.050 114.651 1.00 25.38  ? 869  TYR   B O     1 
ATOM   10975 C  CB    . TYR   B 1 869  ? 157.927 160.253 112.296 1.00 18.74  ? 869  TYR   B CB    1 
ATOM   10976 C  CG    . TYR   B 1 869  ? 158.621 159.998 110.978 1.00 24.40  ? 869  TYR   B CG    1 
ATOM   10977 C  CD1   . TYR   B 1 869  ? 158.061 159.180 110.013 1.00 25.45  ? 869  TYR   B CD1   1 
ATOM   10978 C  CD2   . TYR   B 1 869  ? 159.855 160.578 110.708 1.00 24.44  ? 869  TYR   B CD2   1 
ATOM   10979 C  CE1   . TYR   B 1 869  ? 158.707 158.950 108.813 1.00 32.15  ? 869  TYR   B CE1   1 
ATOM   10980 C  CE2   . TYR   B 1 869  ? 160.505 160.355 109.515 1.00 19.93  ? 869  TYR   B CE2   1 
ATOM   10981 C  CZ    . TYR   B 1 869  ? 159.929 159.540 108.571 1.00 27.95  ? 869  TYR   B CZ    1 
ATOM   10982 O  OH    . TYR   B 1 869  ? 160.577 159.316 107.379 1.00 29.44  ? 869  TYR   B OH    1 
ATOM   10983 N  N     . LEU   B 1 870  ? 155.744 161.248 114.165 1.00 14.74  ? 870  LEU   B N     1 
ATOM   10984 C  CA    . LEU   B 1 870  ? 155.389 161.613 115.532 1.00 14.38  ? 870  LEU   B CA    1 
ATOM   10985 C  C     . LEU   B 1 870  ? 154.059 160.995 115.951 1.00 21.79  ? 870  LEU   B C     1 
ATOM   10986 O  O     . LEU   B 1 870  ? 153.953 160.422 117.041 1.00 23.61  ? 870  LEU   B O     1 
ATOM   10987 C  CB    . LEU   B 1 870  ? 155.353 163.133 115.671 1.00 17.27  ? 870  LEU   B CB    1 
ATOM   10988 C  CG    . LEU   B 1 870  ? 156.729 163.799 115.709 1.00 21.41  ? 870  LEU   B CG    1 
ATOM   10989 C  CD1   . LEU   B 1 870  ? 156.608 165.304 115.554 1.00 23.79  ? 870  LEU   B CD1   1 
ATOM   10990 C  CD2   . LEU   B 1 870  ? 157.461 163.446 116.994 1.00 19.19  ? 870  LEU   B CD2   1 
ATOM   10991 N  N     . MET   B 1 871  ? 153.035 161.092 115.101 1.00 21.66  ? 871  MET   B N     1 
ATOM   10992 C  CA    . MET   B 1 871  ? 151.730 160.542 115.443 1.00 15.91  ? 871  MET   B CA    1 
ATOM   10993 C  C     . MET   B 1 871  ? 151.702 159.021 115.415 1.00 24.12  ? 871  MET   B C     1 
ATOM   10994 O  O     . MET   B 1 871  ? 150.758 158.429 115.949 1.00 33.87  ? 871  MET   B O     1 
ATOM   10995 C  CB    . MET   B 1 871  ? 150.650 161.086 114.505 1.00 21.45  ? 871  MET   B CB    1 
ATOM   10996 C  CG    . MET   B 1 871  ? 150.479 162.596 114.544 1.00 27.70  ? 871  MET   B CG    1 
ATOM   10997 S  SD    . MET   B 1 871  ? 149.518 163.236 113.156 1.00 36.86  ? 871  MET   B SD    1 
ATOM   10998 C  CE    . MET   B 1 871  ? 150.364 162.490 111.768 1.00 26.24  ? 871  MET   B CE    1 
ATOM   10999 N  N     . GLN   B 1 872  ? 152.696 158.374 114.810 1.00 24.86  ? 872  GLN   B N     1 
ATOM   11000 C  CA    . GLN   B 1 872  ? 152.724 156.919 114.806 1.00 20.45  ? 872  GLN   B CA    1 
ATOM   11001 C  C     . GLN   B 1 872  ? 153.558 156.333 115.935 1.00 29.23  ? 872  GLN   B C     1 
ATOM   11002 O  O     . GLN   B 1 872  ? 153.217 155.263 116.451 1.00 30.84  ? 872  GLN   B O     1 
ATOM   11003 C  CB    . GLN   B 1 872  ? 153.255 156.408 113.465 1.00 19.36  ? 872  GLN   B CB    1 
ATOM   11004 C  CG    . GLN   B 1 872  ? 152.328 156.678 112.298 1.00 25.74  ? 872  GLN   B CG    1 
ATOM   11005 C  CD    . GLN   B 1 872  ? 151.299 155.582 112.111 1.00 25.39  ? 872  GLN   B CD    1 
ATOM   11006 O  OE1   . GLN   B 1 872  ? 151.228 154.639 112.898 1.00 26.39  ? 872  GLN   B OE1   1 
ATOM   11007 N  NE2   . GLN   B 1 872  ? 150.491 155.703 111.066 1.00 30.12  ? 872  GLN   B NE2   1 
ATOM   11008 N  N     . ALA   B 1 873  ? 154.635 157.004 116.340 1.00 21.73  ? 873  ALA   B N     1 
ATOM   11009 C  CA    . ALA   B 1 873  ? 155.590 156.413 117.268 1.00 10.12  ? 873  ALA   B CA    1 
ATOM   11010 C  C     . ALA   B 1 873  ? 155.806 157.205 118.547 1.00 21.45  ? 873  ALA   B C     1 
ATOM   11011 O  O     . ALA   B 1 873  ? 156.153 156.605 119.566 1.00 25.09  ? 873  ALA   B O     1 
ATOM   11012 C  CB    . ALA   B 1 873  ? 156.948 156.218 116.578 1.00 16.67  ? 873  ALA   B CB    1 
ATOM   11013 N  N     . ALA   B 1 874  ? 155.614 158.522 118.531 1.00 17.54  ? 874  ALA   B N     1 
ATOM   11014 C  CA    . ALA   B 1 874  ? 155.928 159.331 119.702 1.00 8.44   ? 874  ALA   B CA    1 
ATOM   11015 C  C     . ALA   B 1 874  ? 155.171 158.833 120.927 1.00 19.56  ? 874  ALA   B C     1 
ATOM   11016 O  O     . ALA   B 1 874  ? 153.975 158.538 120.864 1.00 38.00  ? 874  ALA   B O     1 
ATOM   11017 C  CB    . ALA   B 1 874  ? 155.590 160.798 119.440 1.00 7.13   ? 874  ALA   B CB    1 
ATOM   11018 N  N     . GLY   B 1 875  ? 155.877 158.741 122.046 1.00 16.74  ? 875  GLY   B N     1 
ATOM   11019 C  CA    . GLY   B 1 875  ? 155.298 158.321 123.306 1.00 22.22  ? 875  GLY   B CA    1 
ATOM   11020 C  C     . GLY   B 1 875  ? 155.881 157.002 123.786 1.00 21.09  ? 875  GLY   B C     1 
ATOM   11021 O  O     . GLY   B 1 875  ? 156.700 156.365 123.123 1.00 21.96  ? 875  GLY   B O     1 
ATOM   11022 N  N     . LEU   B 1 876  ? 155.431 156.604 124.974 1.00 20.97  ? 876  LEU   B N     1 
ATOM   11023 C  CA    . LEU   B 1 876  ? 155.892 155.368 125.598 1.00 20.59  ? 876  LEU   B CA    1 
ATOM   11024 C  C     . LEU   B 1 876  ? 154.740 154.748 126.371 1.00 24.83  ? 876  LEU   B C     1 
ATOM   11025 O  O     . LEU   B 1 876  ? 154.156 155.401 127.240 1.00 33.19  ? 876  LEU   B O     1 
ATOM   11026 C  CB    . LEU   B 1 876  ? 157.080 155.627 126.525 1.00 26.57  ? 876  LEU   B CB    1 
ATOM   11027 C  CG    . LEU   B 1 876  ? 157.714 154.380 127.142 1.00 24.86  ? 876  LEU   B CG    1 
ATOM   11028 C  CD1   . LEU   B 1 876  ? 158.531 153.630 126.105 1.00 24.62  ? 876  LEU   B CD1   1 
ATOM   11029 C  CD2   . LEU   B 1 876  ? 158.571 154.748 128.339 1.00 24.24  ? 876  LEU   B CD2   1 
ATOM   11030 N  N     . GLY   B 1 877  ? 154.422 153.500 126.060 1.00 26.67  ? 877  GLY   B N     1 
ATOM   11031 C  CA    . GLY   B 1 877  ? 153.349 152.822 126.765 1.00 28.82  ? 877  GLY   B CA    1 
ATOM   11032 C  C     . GLY   B 1 877  ? 152.041 153.571 126.613 1.00 27.00  ? 877  GLY   B C     1 
ATOM   11033 O  O     . GLY   B 1 877  ? 151.564 153.823 125.500 1.00 31.38  ? 877  GLY   B O     1 
ATOM   11034 N  N     . ARG   B 1 878  ? 151.444 153.938 127.743 1.00 34.97  ? 878  ARG   B N     1 
ATOM   11035 C  CA    . ARG   B 1 878  ? 150.172 154.645 127.757 1.00 34.81  ? 878  ARG   B CA    1 
ATOM   11036 C  C     . ARG   B 1 878  ? 150.331 156.158 127.781 1.00 31.64  ? 878  ARG   B C     1 
ATOM   11037 O  O     . ARG   B 1 878  ? 149.323 156.871 127.784 1.00 33.78  ? 878  ARG   B O     1 
ATOM   11038 C  CB    . ARG   B 1 878  ? 149.332 154.194 128.955 1.00 24.21  ? 878  ARG   B CB    1 
ATOM   11039 C  CG    . ARG   B 1 878  ? 148.374 153.067 128.627 1.00 29.33  ? 878  ARG   B CG    1 
ATOM   11040 C  CD    . ARG   B 1 878  ? 147.515 152.684 129.817 1.00 37.29  ? 878  ARG   B CD    1 
ATOM   11041 N  NE    . ARG   B 1 878  ? 147.237 151.253 129.837 1.00 44.24  ? 878  ARG   B NE    1 
ATOM   11042 C  CZ    . ARG   B 1 878  ? 146.516 150.619 128.922 1.00 43.93  ? 878  ARG   B CZ    1 
ATOM   11043 N  NH1   . ARG   B 1 878  ? 145.997 151.259 127.887 1.00 40.50  ? 878  ARG   B NH1   1 
ATOM   11044 N  NH2   . ARG   B 1 878  ? 146.312 149.311 129.048 1.00 42.56  ? 878  ARG   B NH2   1 
ATOM   11045 N  N     . MET   B 1 879  ? 151.562 156.666 127.804 1.00 24.84  ? 879  MET   B N     1 
ATOM   11046 C  CA    . MET   B 1 879  ? 151.822 158.100 127.699 1.00 25.69  ? 879  MET   B CA    1 
ATOM   11047 C  C     . MET   B 1 879  ? 152.020 158.528 126.252 1.00 35.70  ? 879  MET   B C     1 
ATOM   11048 O  O     . MET   B 1 879  ? 153.045 159.119 125.904 1.00 41.98  ? 879  MET   B O     1 
ATOM   11049 C  CB    . MET   B 1 879  ? 153.030 158.488 128.545 1.00 26.54  ? 879  MET   B CB    1 
ATOM   11050 C  CG    . MET   B 1 879  ? 152.682 159.255 129.811 1.00 31.40  ? 879  MET   B CG    1 
ATOM   11051 S  SD    . MET   B 1 879  ? 154.106 159.557 130.877 1.00 57.98  ? 879  MET   B SD    1 
ATOM   11052 C  CE    . MET   B 1 879  ? 154.703 157.889 131.137 1.00 36.96  ? 879  MET   B CE    1 
ATOM   11053 N  N     . LYS   B 1 880  ? 151.043 158.237 125.383 1.00 33.55  ? 880  LYS   B N     1 
ATOM   11054 C  CA    . LYS   B 1 880  ? 151.129 158.596 123.977 1.00 21.24  ? 880  LYS   B CA    1 
ATOM   11055 C  C     . LYS   B 1 880  ? 150.120 159.688 123.639 1.00 23.46  ? 880  LYS   B C     1 
ATOM   11056 O  O     . LYS   B 1 880  ? 149.036 159.748 124.227 1.00 25.62  ? 880  LYS   B O     1 
ATOM   11057 C  CB    . LYS   B 1 880  ? 150.871 157.376 123.098 1.00 25.46  ? 880  LYS   B CB    1 
ATOM   11058 C  CG    . LYS   B 1 880  ? 149.580 156.642 123.420 1.00 25.25  ? 880  LYS   B CG    1 
ATOM   11059 C  CD    . LYS   B 1 880  ? 149.445 155.368 122.604 1.00 30.56  ? 880  LYS   B CD    1 
ATOM   11060 C  CE    . LYS   B 1 880  ? 149.950 155.567 121.186 1.00 32.63  ? 880  LYS   B CE    1 
ATOM   11061 N  NZ    . LYS   B 1 880  ? 149.157 156.590 120.453 1.00 28.34  ? 880  LYS   B NZ    1 
ATOM   11062 N  N     . PRO   B 1 881  ? 150.452 160.557 122.689 1.00 28.59  ? 881  PRO   B N     1 
ATOM   11063 C  CA    . PRO   B 1 881  ? 149.537 161.647 122.336 1.00 25.57  ? 881  PRO   B CA    1 
ATOM   11064 C  C     . PRO   B 1 881  ? 148.265 161.121 121.691 1.00 23.06  ? 881  PRO   B C     1 
ATOM   11065 O  O     . PRO   B 1 881  ? 148.243 160.072 121.044 1.00 22.66  ? 881  PRO   B O     1 
ATOM   11066 C  CB    . PRO   B 1 881  ? 150.346 162.501 121.350 1.00 14.48  ? 881  PRO   B CB    1 
ATOM   11067 C  CG    . PRO   B 1 881  ? 151.745 161.959 121.379 1.00 17.48  ? 881  PRO   B CG    1 
ATOM   11068 C  CD    . PRO   B 1 881  ? 151.667 160.553 121.861 1.00 19.02  ? 881  PRO   B CD    1 
ATOM   11069 N  N     . ASN   B 1 882  ? 147.185 161.878 121.887 1.00 25.53  ? 882  ASN   B N     1 
ATOM   11070 C  CA    . ASN   B 1 882  ? 145.917 161.570 121.239 1.00 11.75  ? 882  ASN   B CA    1 
ATOM   11071 C  C     . ASN   B 1 882  ? 145.278 162.801 120.610 1.00 11.09  ? 882  ASN   B C     1 
ATOM   11072 O  O     . ASN   B 1 882  ? 144.141 162.711 120.133 1.00 22.04  ? 882  ASN   B O     1 
ATOM   11073 C  CB    . ASN   B 1 882  ? 144.936 160.928 122.231 1.00 17.65  ? 882  ASN   B CB    1 
ATOM   11074 C  CG    . ASN   B 1 882  ? 144.680 161.796 123.449 1.00 17.42  ? 882  ASN   B CG    1 
ATOM   11075 O  OD1   . ASN   B 1 882  ? 144.590 163.018 123.351 1.00 21.37  ? 882  ASN   B OD1   1 
ATOM   11076 N  ND2   . ASN   B 1 882  ? 144.562 161.162 124.608 1.00 11.47  ? 882  ASN   B ND2   1 
ATOM   11077 N  N     . THR   B 1 883  ? 145.966 163.940 120.590 1.00 18.79  ? 883  THR   B N     1 
ATOM   11078 C  CA    . THR   B 1 883  ? 145.396 165.175 120.064 1.00 20.10  ? 883  THR   B CA    1 
ATOM   11079 C  C     . THR   B 1 883  ? 146.493 165.972 119.380 1.00 23.43  ? 883  THR   B C     1 
ATOM   11080 O  O     . THR   B 1 883  ? 147.442 166.412 120.036 1.00 30.45  ? 883  THR   B O     1 
ATOM   11081 C  CB    . THR   B 1 883  ? 144.753 166.006 121.178 1.00 19.03  ? 883  THR   B CB    1 
ATOM   11082 O  OG1   . THR   B 1 883  ? 143.731 165.238 121.822 1.00 27.18  ? 883  THR   B OG1   1 
ATOM   11083 C  CG2   . THR   B 1 883  ? 144.143 167.278 120.609 1.00 19.72  ? 883  THR   B CG2   1 
ATOM   11084 N  N     . LEU   B 1 884  ? 146.354 166.170 118.073 1.00 10.96  ? 884  LEU   B N     1 
ATOM   11085 C  CA    . LEU   B 1 884  ? 147.275 167.012 117.327 1.00 16.65  ? 884  LEU   B CA    1 
ATOM   11086 C  C     . LEU   B 1 884  ? 146.890 168.476 117.499 1.00 16.28  ? 884  LEU   B C     1 
ATOM   11087 O  O     . LEU   B 1 884  ? 145.741 168.860 117.253 1.00 23.62  ? 884  LEU   B O     1 
ATOM   11088 C  CB    . LEU   B 1 884  ? 147.265 166.627 115.847 1.00 20.67  ? 884  LEU   B CB    1 
ATOM   11089 C  CG    . LEU   B 1 884  ? 148.043 167.525 114.883 1.00 22.58  ? 884  LEU   B CG    1 
ATOM   11090 C  CD1   . LEU   B 1 884  ? 149.529 167.502 115.202 1.00 18.45  ? 884  LEU   B CD1   1 
ATOM   11091 C  CD2   . LEU   B 1 884  ? 147.792 167.111 113.442 1.00 21.18  ? 884  LEU   B CD2   1 
ATOM   11092 N  N     . VAL   B 1 885  ? 147.852 169.290 117.924 1.00 17.49  ? 885  VAL   B N     1 
ATOM   11093 C  CA    . VAL   B 1 885  ? 147.653 170.719 118.124 1.00 22.08  ? 885  VAL   B CA    1 
ATOM   11094 C  C     . VAL   B 1 885  ? 148.450 171.459 117.061 1.00 28.31  ? 885  VAL   B C     1 
ATOM   11095 O  O     . VAL   B 1 885  ? 149.652 171.215 116.887 1.00 24.65  ? 885  VAL   B O     1 
ATOM   11096 C  CB    . VAL   B 1 885  ? 148.068 171.161 119.538 1.00 16.26  ? 885  VAL   B CB    1 
ATOM   11097 C  CG1   . VAL   B 1 885  ? 147.885 172.660 119.701 1.00 13.79  ? 885  VAL   B CG1   1 
ATOM   11098 C  CG2   . VAL   B 1 885  ? 147.263 170.411 120.581 1.00 16.66  ? 885  VAL   B CG2   1 
ATOM   11099 N  N     . LEU   B 1 886  ? 147.775 172.354 116.346 1.00 28.04  ? 886  LEU   B N     1 
ATOM   11100 C  CA    . LEU   B 1 886  ? 148.366 173.116 115.261 1.00 19.08  ? 886  LEU   B CA    1 
ATOM   11101 C  C     . LEU   B 1 886  ? 148.119 174.598 115.487 1.00 20.79  ? 886  LEU   B C     1 
ATOM   11102 O  O     . LEU   B 1 886  ? 147.134 174.993 116.116 1.00 30.02  ? 886  LEU   B O     1 
ATOM   11103 C  CB    . LEU   B 1 886  ? 147.783 172.698 113.903 1.00 13.70  ? 886  LEU   B CB    1 
ATOM   11104 C  CG    . LEU   B 1 886  ? 148.268 171.370 113.321 1.00 23.64  ? 886  LEU   B CG    1 
ATOM   11105 C  CD1   . LEU   B 1 886  ? 147.428 170.964 112.121 1.00 31.05  ? 886  LEU   B CD1   1 
ATOM   11106 C  CD2   . LEU   B 1 886  ? 149.731 171.470 112.937 1.00 34.41  ? 886  LEU   B CD2   1 
ATOM   11107 N  N     . GLY   B 1 887  ? 149.037 175.413 114.981 1.00 27.06  ? 887  GLY   B N     1 
ATOM   11108 C  CA    . GLY   B 1 887  ? 148.855 176.852 114.935 1.00 29.14  ? 887  GLY   B CA    1 
ATOM   11109 C  C     . GLY   B 1 887  ? 148.330 177.254 113.569 1.00 30.99  ? 887  GLY   B C     1 
ATOM   11110 O  O     . GLY   B 1 887  ? 148.730 176.693 112.550 1.00 42.72  ? 887  GLY   B O     1 
ATOM   11111 N  N     . PHE   B 1 888  ? 147.425 178.228 113.560 1.00 32.29  ? 888  PHE   B N     1 
ATOM   11112 C  CA    . PHE   B 1 888  ? 146.827 178.663 112.307 1.00 31.61  ? 888  PHE   B CA    1 
ATOM   11113 C  C     . PHE   B 1 888  ? 147.897 179.212 111.373 1.00 38.77  ? 888  PHE   B C     1 
ATOM   11114 O  O     . PHE   B 1 888  ? 148.737 180.021 111.777 1.00 43.32  ? 888  PHE   B O     1 
ATOM   11115 C  CB    . PHE   B 1 888  ? 145.758 179.722 112.566 1.00 32.82  ? 888  PHE   B CB    1 
ATOM   11116 C  CG    . PHE   B 1 888  ? 145.021 180.152 111.331 1.00 39.06  ? 888  PHE   B CG    1 
ATOM   11117 C  CD1   . PHE   B 1 888  ? 144.038 179.349 110.781 1.00 37.51  ? 888  PHE   B CD1   1 
ATOM   11118 C  CD2   . PHE   B 1 888  ? 145.315 181.356 110.715 1.00 35.94  ? 888  PHE   B CD2   1 
ATOM   11119 C  CE1   . PHE   B 1 888  ? 143.360 179.740 109.644 1.00 38.21  ? 888  PHE   B CE1   1 
ATOM   11120 C  CE2   . PHE   B 1 888  ? 144.640 181.752 109.578 1.00 34.78  ? 888  PHE   B CE2   1 
ATOM   11121 C  CZ    . PHE   B 1 888  ? 143.662 180.942 109.042 1.00 35.51  ? 888  PHE   B CZ    1 
ATOM   11122 N  N     . LYS   B 1 889  ? 147.862 178.769 110.119 1.00 32.29  ? 889  LYS   B N     1 
ATOM   11123 C  CA    . LYS   B 1 889  ? 148.800 179.266 109.123 1.00 28.92  ? 889  LYS   B CA    1 
ATOM   11124 C  C     . LYS   B 1 889  ? 148.406 180.681 108.725 1.00 35.01  ? 889  LYS   B C     1 
ATOM   11125 O  O     . LYS   B 1 889  ? 147.601 180.874 107.809 1.00 46.45  ? 889  LYS   B O     1 
ATOM   11126 C  CB    . LYS   B 1 889  ? 148.831 178.343 107.904 1.00 33.13  ? 889  LYS   B CB    1 
ATOM   11127 C  CG    . LYS   B 1 889  ? 150.222 178.090 107.352 1.00 38.99  ? 889  LYS   B CG    1 
ATOM   11128 C  CD    . LYS   B 1 889  ? 150.200 177.035 106.257 1.00 38.74  ? 889  LYS   B CD    1 
ATOM   11129 C  CE    . LYS   B 1 889  ? 151.270 177.303 105.214 1.00 32.75  ? 889  LYS   B CE    1 
ATOM   11130 N  NZ    . LYS   B 1 889  ? 152.518 177.820 105.836 1.00 34.87  ? 889  LYS   B NZ    1 
ATOM   11131 N  N     . LYS   B 1 890  ? 148.968 181.676 109.411 1.00 35.23  ? 890  LYS   B N     1 
ATOM   11132 C  CA    . LYS   B 1 890  ? 148.574 183.059 109.175 1.00 42.78  ? 890  LYS   B CA    1 
ATOM   11133 C  C     . LYS   B 1 890  ? 149.118 183.603 107.861 1.00 49.73  ? 890  LYS   B C     1 
ATOM   11134 O  O     . LYS   B 1 890  ? 148.592 184.598 107.352 1.00 51.06  ? 890  LYS   B O     1 
ATOM   11135 C  CB    . LYS   B 1 890  ? 149.037 183.937 110.337 1.00 41.86  ? 890  LYS   B CB    1 
ATOM   11136 C  CG    . LYS   B 1 890  ? 148.575 183.444 111.697 1.00 47.26  ? 890  LYS   B CG    1 
ATOM   11137 C  CD    . LYS   B 1 890  ? 148.349 184.593 112.662 1.00 46.70  ? 890  LYS   B CD    1 
ATOM   11138 C  CE    . LYS   B 1 890  ? 146.937 185.140 112.537 1.00 50.51  ? 890  LYS   B CE    1 
ATOM   11139 N  NZ    . LYS   B 1 890  ? 146.193 185.056 113.824 1.00 48.14  ? 890  LYS   B NZ    1 
ATOM   11140 N  N     . ASP   B 1 891  ? 150.152 182.978 107.307 1.00 50.68  ? 891  ASP   B N     1 
ATOM   11141 C  CA    . ASP   B 1 891  ? 150.748 183.405 106.049 1.00 49.22  ? 891  ASP   B CA    1 
ATOM   11142 C  C     . ASP   B 1 891  ? 150.207 182.645 104.846 1.00 50.53  ? 891  ASP   B C     1 
ATOM   11143 O  O     . ASP   B 1 891  ? 150.729 182.814 103.740 1.00 55.35  ? 891  ASP   B O     1 
ATOM   11144 C  CB    . ASP   B 1 891  ? 152.270 183.249 106.111 1.00 54.00  ? 891  ASP   B CB    1 
ATOM   11145 C  CG    . ASP   B 1 891  ? 152.693 181.942 106.747 1.00 56.09  ? 891  ASP   B CG    1 
ATOM   11146 O  OD1   . ASP   B 1 891  ? 151.897 180.981 106.711 1.00 52.66  ? 891  ASP   B OD1   1 
ATOM   11147 O  OD2   . ASP   B 1 891  ? 153.818 181.874 107.284 1.00 60.82  ? 891  ASP   B OD2   1 
ATOM   11148 N  N     . TRP   B 1 892  ? 149.181 181.810 105.034 1.00 37.16  ? 892  TRP   B N     1 
ATOM   11149 C  CA    . TRP   B 1 892  ? 148.707 180.965 103.942 1.00 37.43  ? 892  TRP   B CA    1 
ATOM   11150 C  C     . TRP   B 1 892  ? 148.304 181.786 102.725 1.00 40.35  ? 892  TRP   B C     1 
ATOM   11151 O  O     . TRP   B 1 892  ? 148.415 181.306 101.591 1.00 41.88  ? 892  TRP   B O     1 
ATOM   11152 C  CB    . TRP   B 1 892  ? 147.537 180.103 104.415 1.00 36.93  ? 892  TRP   B CB    1 
ATOM   11153 C  CG    . TRP   B 1 892  ? 146.215 180.801 104.374 1.00 41.14  ? 892  TRP   B CG    1 
ATOM   11154 C  CD1   . TRP   B 1 892  ? 145.676 181.596 105.343 1.00 42.42  ? 892  TRP   B CD1   1 
ATOM   11155 C  CD2   . TRP   B 1 892  ? 145.257 180.762 103.309 1.00 38.43  ? 892  TRP   B CD2   1 
ATOM   11156 N  NE1   . TRP   B 1 892  ? 144.445 182.056 104.946 1.00 43.61  ? 892  TRP   B NE1   1 
ATOM   11157 C  CE2   . TRP   B 1 892  ? 144.163 181.558 103.702 1.00 37.58  ? 892  TRP   B CE2   1 
ATOM   11158 C  CE3   . TRP   B 1 892  ? 145.218 180.130 102.063 1.00 37.83  ? 892  TRP   B CE3   1 
ATOM   11159 C  CZ2   . TRP   B 1 892  ? 143.045 181.740 102.893 1.00 40.06  ? 892  TRP   B CZ2   1 
ATOM   11160 C  CZ3   . TRP   B 1 892  ? 144.107 180.312 101.262 1.00 42.33  ? 892  TRP   B CZ3   1 
ATOM   11161 C  CH2   . TRP   B 1 892  ? 143.035 181.110 101.680 1.00 42.70  ? 892  TRP   B CH2   1 
ATOM   11162 N  N     . LEU   B 1 893  ? 147.835 183.018 102.930 1.00 47.77  ? 893  LEU   B N     1 
ATOM   11163 C  CA    . LEU   B 1 893  ? 147.472 183.858 101.793 1.00 46.02  ? 893  LEU   B CA    1 
ATOM   11164 C  C     . LEU   B 1 893  ? 148.684 184.145 100.917 1.00 45.13  ? 893  LEU   B C     1 
ATOM   11165 O  O     . LEU   B 1 893  ? 148.592 184.105 99.684  1.00 47.93  ? 893  LEU   B O     1 
ATOM   11166 C  CB    . LEU   B 1 893  ? 146.838 185.160 102.280 1.00 48.03  ? 893  LEU   B CB    1 
ATOM   11167 C  CG    . LEU   B 1 893  ? 145.311 185.178 102.349 1.00 47.95  ? 893  LEU   B CG    1 
ATOM   11168 C  CD1   . LEU   B 1 893  ? 144.790 186.598 102.209 1.00 50.20  ? 893  LEU   B CD1   1 
ATOM   11169 C  CD2   . LEU   B 1 893  ? 144.719 184.279 101.277 1.00 44.46  ? 893  LEU   B CD2   1 
ATOM   11170 N  N     . GLN   B 1 894  ? 149.828 184.431 101.531 1.00 44.96  ? 894  GLN   B N     1 
ATOM   11171 C  CA    . GLN   B 1 894  ? 151.085 184.649 100.820 1.00 45.91  ? 894  GLN   B CA    1 
ATOM   11172 C  C     . GLN   B 1 894  ? 152.023 183.500 101.182 1.00 48.44  ? 894  GLN   B C     1 
ATOM   11173 O  O     . GLN   B 1 894  ? 152.824 183.600 102.113 1.00 49.65  ? 894  GLN   B O     1 
ATOM   11174 C  CB    . GLN   B 1 894  ? 151.690 186.005 101.177 1.00 44.02  ? 894  GLN   B CB    1 
ATOM   11175 N  N     . ALA   B 1 895  ? 151.917 182.405 100.436 1.00 45.86  ? 895  ALA   B N     1 
ATOM   11176 C  CA    . ALA   B 1 895  ? 152.737 181.224 100.669 1.00 44.02  ? 895  ALA   B CA    1 
ATOM   11177 C  C     . ALA   B 1 895  ? 152.456 180.212 99.572  1.00 47.28  ? 895  ALA   B C     1 
ATOM   11178 O  O     . ALA   B 1 895  ? 151.344 180.153 99.039  1.00 52.36  ? 895  ALA   B O     1 
ATOM   11179 C  CB    . ALA   B 1 895  ? 152.461 180.609 102.046 1.00 44.75  ? 895  ALA   B CB    1 
ATOM   11180 N  N     . ASP   B 1 896  ? 153.470 179.416 99.245  1.00 54.57  ? 896  ASP   B N     1 
ATOM   11181 C  CA    . ASP   B 1 896  ? 153.305 178.388 98.228  1.00 55.73  ? 896  ASP   B CA    1 
ATOM   11182 C  C     . ASP   B 1 896  ? 152.178 177.444 98.621  1.00 52.53  ? 896  ASP   B C     1 
ATOM   11183 O  O     . ASP   B 1 896  ? 152.096 176.999 99.769  1.00 53.76  ? 896  ASP   B O     1 
ATOM   11184 C  CB    . ASP   B 1 896  ? 154.608 177.612 98.041  1.00 52.24  ? 896  ASP   B CB    1 
ATOM   11185 N  N     . MET   B 1 897  ? 151.307 177.132 97.661  1.00 52.91  ? 897  MET   B N     1 
ATOM   11186 C  CA    . MET   B 1 897  ? 150.152 176.298 97.965  1.00 55.13  ? 897  MET   B CA    1 
ATOM   11187 C  C     . MET   B 1 897  ? 150.530 174.861 98.292  1.00 55.80  ? 897  MET   B C     1 
ATOM   11188 O  O     . MET   B 1 897  ? 149.681 174.118 98.793  1.00 59.84  ? 897  MET   B O     1 
ATOM   11189 C  CB    . MET   B 1 897  ? 149.160 176.325 96.804  1.00 54.14  ? 897  MET   B CB    1 
ATOM   11190 C  CG    . MET   B 1 897  ? 148.354 177.608 96.728  1.00 57.64  ? 897  MET   B CG    1 
ATOM   11191 S  SD    . MET   B 1 897  ? 146.920 177.568 97.821  1.00 65.60  ? 897  MET   B SD    1 
ATOM   11192 C  CE    . MET   B 1 897  ? 146.603 175.809 97.899  1.00 59.13  ? 897  MET   B CE    1 
ATOM   11193 N  N     . ARG   B 1 898  ? 151.772 174.452 98.030  1.00 52.82  ? 898  ARG   B N     1 
ATOM   11194 C  CA    . ARG   B 1 898  ? 152.223 173.152 98.509  1.00 53.26  ? 898  ARG   B CA    1 
ATOM   11195 C  C     . ARG   B 1 898  ? 152.257 173.118 100.032 1.00 56.19  ? 898  ARG   B C     1 
ATOM   11196 O  O     . ARG   B 1 898  ? 151.892 172.111 100.647 1.00 58.12  ? 898  ARG   B O     1 
ATOM   11197 C  CB    . ARG   B 1 898  ? 153.596 172.819 97.927  1.00 57.44  ? 898  ARG   B CB    1 
ATOM   11198 C  CG    . ARG   B 1 898  ? 153.872 173.458 96.578  1.00 59.91  ? 898  ARG   B CG    1 
ATOM   11199 C  CD    . ARG   B 1 898  ? 155.090 172.834 95.914  1.00 62.34  ? 898  ARG   B CD    1 
ATOM   11200 N  NE    . ARG   B 1 898  ? 155.083 171.380 96.011  1.00 66.61  ? 898  ARG   B NE    1 
ATOM   11201 C  CZ    . ARG   B 1 898  ? 154.238 170.590 95.363  1.00 65.97  ? 898  ARG   B CZ    1 
ATOM   11202 N  NH1   . ARG   B 1 898  ? 153.307 171.084 94.562  1.00 61.82  ? 898  ARG   B NH1   1 
ATOM   11203 N  NH2   . ARG   B 1 898  ? 154.329 169.273 95.520  1.00 64.44  ? 898  ARG   B NH2   1 
ATOM   11204 N  N     . ASP   B 1 899  ? 152.694 174.213 100.659 1.00 44.54  ? 899  ASP   B N     1 
ATOM   11205 C  CA    . ASP   B 1 899  ? 152.682 174.285 102.117 1.00 46.62  ? 899  ASP   B CA    1 
ATOM   11206 C  C     . ASP   B 1 899  ? 151.262 174.199 102.667 1.00 48.08  ? 899  ASP   B C     1 
ATOM   11207 O  O     . ASP   B 1 899  ? 151.014 173.510 103.663 1.00 47.77  ? 899  ASP   B O     1 
ATOM   11208 C  CB    . ASP   B 1 899  ? 153.361 175.574 102.581 1.00 45.45  ? 899  ASP   B CB    1 
ATOM   11209 N  N     . VAL   B 1 900  ? 150.318 174.901 102.038 1.00 40.68  ? 900  VAL   B N     1 
ATOM   11210 C  CA    . VAL   B 1 900  ? 148.930 174.849 102.489 1.00 34.20  ? 900  VAL   B CA    1 
ATOM   11211 C  C     . VAL   B 1 900  ? 148.361 173.449 102.298 1.00 36.45  ? 900  VAL   B C     1 
ATOM   11212 O  O     . VAL   B 1 900  ? 147.610 172.943 103.144 1.00 45.60  ? 900  VAL   B O     1 
ATOM   11213 C  CB    . VAL   B 1 900  ? 148.091 175.911 101.756 1.00 39.61  ? 900  VAL   B CB    1 
ATOM   11214 C  CG1   . VAL   B 1 900  ? 146.632 175.817 102.169 1.00 44.99  ? 900  VAL   B CG1   1 
ATOM   11215 C  CG2   . VAL   B 1 900  ? 148.639 177.300 102.037 1.00 39.48  ? 900  VAL   B CG2   1 
ATOM   11216 N  N     . ASP   B 1 901  ? 148.694 172.806 101.178 1.00 33.02  ? 901  ASP   B N     1 
ATOM   11217 C  CA    . ASP   B 1 901  ? 148.255 171.433 100.960 1.00 37.30  ? 901  ASP   B CA    1 
ATOM   11218 C  C     . ASP   B 1 901  ? 148.822 170.504 102.022 1.00 42.22  ? 901  ASP   B C     1 
ATOM   11219 O  O     . ASP   B 1 901  ? 148.126 169.609 102.509 1.00 41.27  ? 901  ASP   B O     1 
ATOM   11220 C  CB    . ASP   B 1 901  ? 148.660 170.967 99.562  1.00 39.87  ? 901  ASP   B CB    1 
ATOM   11221 C  CG    . ASP   B 1 901  ? 147.726 169.911 99.008  1.00 46.23  ? 901  ASP   B CG    1 
ATOM   11222 O  OD1   . ASP   B 1 901  ? 147.808 168.749 99.456  1.00 48.46  ? 901  ASP   B OD1   1 
ATOM   11223 O  OD2   . ASP   B 1 901  ? 146.908 170.241 98.125  1.00 51.43  ? 901  ASP   B OD2   1 
ATOM   11224 N  N     . MET   B 1 902  ? 150.090 170.698 102.390 1.00 39.48  ? 902  MET   B N     1 
ATOM   11225 C  CA    . MET   B 1 902  ? 150.692 169.892 103.446 1.00 34.00  ? 902  MET   B CA    1 
ATOM   11226 C  C     . MET   B 1 902  ? 149.992 170.122 104.779 1.00 44.71  ? 902  MET   B C     1 
ATOM   11227 O  O     . MET   B 1 902  ? 149.770 169.179 105.542 1.00 50.85  ? 902  MET   B O     1 
ATOM   11228 C  CB    . MET   B 1 902  ? 152.183 170.213 103.554 1.00 38.66  ? 902  MET   B CB    1 
ATOM   11229 C  CG    . MET   B 1 902  ? 153.013 169.144 104.243 1.00 45.07  ? 902  MET   B CG    1 
ATOM   11230 S  SD    . MET   B 1 902  ? 154.409 168.615 103.235 1.00 53.07  ? 902  MET   B SD    1 
ATOM   11231 C  CE    . MET   B 1 902  ? 155.187 170.190 102.888 1.00 48.29  ? 902  MET   B CE    1 
ATOM   11232 N  N     . TYR   B 1 903  ? 149.643 171.373 105.076 1.00 35.97  ? 903  TYR   B N     1 
ATOM   11233 C  CA    . TYR   B 1 903  ? 148.895 171.687 106.293 1.00 27.97  ? 903  TYR   B CA    1 
ATOM   11234 C  C     . TYR   B 1 903  ? 147.554 170.952 106.326 1.00 26.25  ? 903  TYR   B C     1 
ATOM   11235 O  O     . TYR   B 1 903  ? 147.202 170.292 107.317 1.00 34.32  ? 903  TYR   B O     1 
ATOM   11236 C  CB    . TYR   B 1 903  ? 148.695 173.202 106.366 1.00 30.86  ? 903  TYR   B CB    1 
ATOM   11237 C  CG    . TYR   B 1 903  ? 148.356 173.759 107.728 1.00 33.70  ? 903  TYR   B CG    1 
ATOM   11238 C  CD1   . TYR   B 1 903  ? 149.259 173.683 108.778 1.00 32.69  ? 903  TYR   B CD1   1 
ATOM   11239 C  CD2   . TYR   B 1 903  ? 147.141 174.389 107.954 1.00 28.49  ? 903  TYR   B CD2   1 
ATOM   11240 C  CE1   . TYR   B 1 903  ? 148.953 174.203 110.020 1.00 34.50  ? 903  TYR   B CE1   1 
ATOM   11241 C  CE2   . TYR   B 1 903  ? 146.827 174.912 109.191 1.00 26.83  ? 903  TYR   B CE2   1 
ATOM   11242 C  CZ    . TYR   B 1 903  ? 147.736 174.816 110.221 1.00 34.05  ? 903  TYR   B CZ    1 
ATOM   11243 O  OH    . TYR   B 1 903  ? 147.426 175.335 111.456 1.00 46.89  ? 903  TYR   B OH    1 
ATOM   11244 N  N     . ILE   B 1 904  ? 146.790 171.054 105.240 1.00 28.09  ? 904  ILE   B N     1 
ATOM   11245 C  CA    . ILE   B 1 904  ? 145.470 170.432 105.209 1.00 29.70  ? 904  ILE   B CA    1 
ATOM   11246 C  C     . ILE   B 1 904  ? 145.591 168.913 105.253 1.00 29.93  ? 904  ILE   B C     1 
ATOM   11247 O  O     . ILE   B 1 904  ? 144.774 168.227 105.878 1.00 31.18  ? 904  ILE   B O     1 
ATOM   11248 C  CB    . ILE   B 1 904  ? 144.683 170.913 103.978 1.00 37.69  ? 904  ILE   B CB    1 
ATOM   11249 C  CG1   . ILE   B 1 904  ? 144.334 172.394 104.126 1.00 34.24  ? 904  ILE   B CG1   1 
ATOM   11250 C  CG2   . ILE   B 1 904  ? 143.425 170.084 103.794 1.00 38.88  ? 904  ILE   B CG2   1 
ATOM   11251 C  CD1   . ILE   B 1 904  ? 144.044 172.814 105.551 1.00 26.85  ? 904  ILE   B CD1   1 
ATOM   11252 N  N     . ASN   B 1 905  ? 146.604 168.359 104.587 1.00 30.12  ? 905  ASN   B N     1 
ATOM   11253 C  CA    . ASN   B 1 905  ? 146.821 166.921 104.655 1.00 32.30  ? 905  ASN   B CA    1 
ATOM   11254 C  C     . ASN   B 1 905  ? 147.296 166.497 106.035 1.00 32.78  ? 905  ASN   B C     1 
ATOM   11255 O  O     . ASN   B 1 905  ? 147.071 165.355 106.439 1.00 36.15  ? 905  ASN   B O     1 
ATOM   11256 C  CB    . ASN   B 1 905  ? 147.814 166.490 103.579 1.00 35.21  ? 905  ASN   B CB    1 
ATOM   11257 C  CG    . ASN   B 1 905  ? 147.334 166.822 102.180 1.00 43.13  ? 905  ASN   B CG    1 
ATOM   11258 O  OD1   . ASN   B 1 905  ? 146.152 167.087 101.966 1.00 43.19  ? 905  ASN   B OD1   1 
ATOM   11259 N  ND2   . ASN   B 1 905  ? 148.250 166.809 101.219 1.00 38.69  ? 905  ASN   B ND2   1 
ATOM   11260 N  N     . LEU   B 1 906  ? 147.950 167.394 106.771 1.00 27.51  ? 906  LEU   B N     1 
ATOM   11261 C  CA    . LEU   B 1 906  ? 148.221 167.138 108.179 1.00 20.67  ? 906  LEU   B CA    1 
ATOM   11262 C  C     . LEU   B 1 906  ? 146.917 166.974 108.943 1.00 31.90  ? 906  LEU   B C     1 
ATOM   11263 O  O     . LEU   B 1 906  ? 146.752 166.035 109.730 1.00 28.78  ? 906  LEU   B O     1 
ATOM   11264 C  CB    . LEU   B 1 906  ? 149.050 168.281 108.762 1.00 23.22  ? 906  LEU   B CB    1 
ATOM   11265 C  CG    . LEU   B 1 906  ? 150.206 167.915 109.688 1.00 27.20  ? 906  LEU   B CG    1 
ATOM   11266 C  CD1   . LEU   B 1 906  ? 151.228 167.077 108.946 1.00 27.20  ? 906  LEU   B CD1   1 
ATOM   11267 C  CD2   . LEU   B 1 906  ? 150.847 169.175 110.243 1.00 30.19  ? 906  LEU   B CD2   1 
ATOM   11268 N  N     . PHE   B 1 907  ? 145.974 167.886 108.708 1.00 42.20  ? 907  PHE   B N     1 
ATOM   11269 C  CA    . PHE   B 1 907  ? 144.628 167.720 109.257 1.00 22.85  ? 907  PHE   B CA    1 
ATOM   11270 C  C     . PHE   B 1 907  ? 144.060 166.344 108.913 1.00 19.26  ? 907  PHE   B C     1 
ATOM   11271 O  O     . PHE   B 1 907  ? 143.551 165.618 109.781 1.00 14.65  ? 907  PHE   B O     1 
ATOM   11272 C  CB    . PHE   B 1 907  ? 143.707 168.812 108.713 1.00 22.53  ? 907  PHE   B CB    1 
ATOM   11273 C  CG    . PHE   B 1 907  ? 143.801 170.114 109.445 1.00 21.97  ? 907  PHE   B CG    1 
ATOM   11274 C  CD1   . PHE   B 1 907  ? 144.900 170.938 109.283 1.00 31.80  ? 907  PHE   B CD1   1 
ATOM   11275 C  CD2   . PHE   B 1 907  ? 142.773 170.533 110.269 1.00 16.53  ? 907  PHE   B CD2   1 
ATOM   11276 C  CE1   . PHE   B 1 907  ? 144.984 172.142 109.948 1.00 29.34  ? 907  PHE   B CE1   1 
ATOM   11277 C  CE2   . PHE   B 1 907  ? 142.850 171.738 110.933 1.00 23.40  ? 907  PHE   B CE2   1 
ATOM   11278 C  CZ    . PHE   B 1 907  ? 143.958 172.544 110.771 1.00 27.39  ? 907  PHE   B CZ    1 
ATOM   11279 N  N     . HIS   B 1 908  ? 144.131 165.984 107.632 1.00 31.33  ? 908  HIS   B N     1 
ATOM   11280 C  CA    . HIS   B 1 908  ? 143.500 164.757 107.157 1.00 28.77  ? 908  HIS   B CA    1 
ATOM   11281 C  C     . HIS   B 1 908  ? 144.147 163.519 107.767 1.00 30.93  ? 908  HIS   B C     1 
ATOM   11282 O  O     . HIS   B 1 908  ? 143.449 162.576 108.151 1.00 25.64  ? 908  HIS   B O     1 
ATOM   11283 C  CB    . HIS   B 1 908  ? 143.551 164.706 105.631 1.00 29.38  ? 908  HIS   B CB    1 
ATOM   11284 C  CG    . HIS   B 1 908  ? 142.462 165.489 104.969 1.00 30.65  ? 908  HIS   B CG    1 
ATOM   11285 N  ND1   . HIS   B 1 908  ? 141.132 165.335 105.296 1.00 26.79  ? 908  HIS   B ND1   1 
ATOM   11286 C  CD2   . HIS   B 1 908  ? 142.505 166.447 104.012 1.00 30.58  ? 908  HIS   B CD2   1 
ATOM   11287 C  CE1   . HIS   B 1 908  ? 140.402 166.155 104.561 1.00 33.66  ? 908  HIS   B CE1   1 
ATOM   11288 N  NE2   . HIS   B 1 908  ? 141.211 166.842 103.775 1.00 38.06  ? 908  HIS   B NE2   1 
ATOM   11289 N  N     . ASP   B 1 909  ? 145.476 163.497 107.860 1.00 38.87  ? 909  ASP   B N     1 
ATOM   11290 C  CA    . ASP   B 1 909  ? 146.155 162.359 108.471 1.00 28.91  ? 909  ASP   B CA    1 
ATOM   11291 C  C     . ASP   B 1 909  ? 145.879 162.291 109.966 1.00 31.08  ? 909  ASP   B C     1 
ATOM   11292 O  O     . ASP   B 1 909  ? 145.764 161.198 110.533 1.00 37.01  ? 909  ASP   B O     1 
ATOM   11293 C  CB    . ASP   B 1 909  ? 147.657 162.429 108.203 1.00 30.82  ? 909  ASP   B CB    1 
ATOM   11294 C  CG    . ASP   B 1 909  ? 148.000 162.213 106.743 1.00 44.67  ? 909  ASP   B CG    1 
ATOM   11295 O  OD1   . ASP   B 1 909  ? 148.056 161.043 106.313 1.00 48.46  ? 909  ASP   B OD1   1 
ATOM   11296 O  OD2   . ASP   B 1 909  ? 148.225 163.208 106.025 1.00 49.43  ? 909  ASP   B OD2   1 
ATOM   11297 N  N     . ALA   B 1 910  ? 145.766 163.447 110.623 1.00 31.15  ? 910  ALA   B N     1 
ATOM   11298 C  CA    . ALA   B 1 910  ? 145.377 163.453 112.027 1.00 25.29  ? 910  ALA   B CA    1 
ATOM   11299 C  C     . ALA   B 1 910  ? 144.028 162.773 112.213 1.00 22.20  ? 910  ALA   B C     1 
ATOM   11300 O  O     . ALA   B 1 910  ? 143.861 161.930 113.101 1.00 26.19  ? 910  ALA   B O     1 
ATOM   11301 C  CB    . ALA   B 1 910  ? 145.342 164.886 112.557 1.00 32.70  ? 910  ALA   B CB    1 
ATOM   11302 N  N     . PHE   B 1 911  ? 143.049 163.123 111.375 1.00 30.51  ? 911  PHE   B N     1 
ATOM   11303 C  CA    . PHE   B 1 911  ? 141.748 162.463 111.482 1.00 24.57  ? 911  PHE   B CA    1 
ATOM   11304 C  C     . PHE   B 1 911  ? 141.834 160.984 111.109 1.00 26.56  ? 911  PHE   B C     1 
ATOM   11305 O  O     . PHE   B 1 911  ? 141.163 160.146 111.721 1.00 23.84  ? 911  PHE   B O     1 
ATOM   11306 C  CB    . PHE   B 1 911  ? 140.704 163.176 110.625 1.00 17.09  ? 911  PHE   B CB    1 
ATOM   11307 C  CG    . PHE   B 1 911  ? 140.398 164.572 111.079 1.00 19.92  ? 911  PHE   B CG    1 
ATOM   11308 C  CD1   . PHE   B 1 911  ? 140.152 164.839 112.413 1.00 20.51  ? 911  PHE   B CD1   1 
ATOM   11309 C  CD2   . PHE   B 1 911  ? 140.332 165.615 110.172 1.00 25.38  ? 911  PHE   B CD2   1 
ATOM   11310 C  CE1   . PHE   B 1 911  ? 139.866 166.119 112.837 1.00 14.64  ? 911  PHE   B CE1   1 
ATOM   11311 C  CE2   . PHE   B 1 911  ? 140.045 166.899 110.591 1.00 24.48  ? 911  PHE   B CE2   1 
ATOM   11312 C  CZ    . PHE   B 1 911  ? 139.811 167.151 111.925 1.00 21.45  ? 911  PHE   B CZ    1 
ATOM   11313 N  N     . ASP   B 1 912  ? 142.648 160.644 110.108 1.00 35.36  ? 912  ASP   B N     1 
ATOM   11314 C  CA    . ASP   B 1 912  ? 142.778 159.249 109.697 1.00 31.96  ? 912  ASP   B CA    1 
ATOM   11315 C  C     . ASP   B 1 912  ? 143.374 158.389 110.801 1.00 38.17  ? 912  ASP   B C     1 
ATOM   11316 O  O     . ASP   B 1 912  ? 143.060 157.197 110.897 1.00 42.51  ? 912  ASP   B O     1 
ATOM   11317 C  CB    . ASP   B 1 912  ? 143.635 159.150 108.435 1.00 29.27  ? 912  ASP   B CB    1 
ATOM   11318 C  CG    . ASP   B 1 912  ? 142.881 159.552 107.185 1.00 46.27  ? 912  ASP   B CG    1 
ATOM   11319 O  OD1   . ASP   B 1 912  ? 141.674 159.248 107.096 1.00 51.08  ? 912  ASP   B OD1   1 
ATOM   11320 O  OD2   . ASP   B 1 912  ? 143.496 160.171 106.292 1.00 45.95  ? 912  ASP   B OD2   1 
ATOM   11321 N  N     . ILE   B 1 913  ? 144.235 158.967 111.635 1.00 38.98  ? 913  ILE   B N     1 
ATOM   11322 C  CA    . ILE   B 1 913  ? 144.871 158.235 112.723 1.00 26.85  ? 913  ILE   B CA    1 
ATOM   11323 C  C     . ILE   B 1 913  ? 143.987 158.331 113.960 1.00 26.57  ? 913  ILE   B C     1 
ATOM   11324 O  O     . ILE   B 1 913  ? 144.425 158.042 115.078 1.00 36.02  ? 913  ILE   B O     1 
ATOM   11325 C  CB    . ILE   B 1 913  ? 146.288 158.773 112.996 1.00 27.62  ? 913  ILE   B CB    1 
ATOM   11326 C  CG1   . ILE   B 1 913  ? 147.159 157.696 113.645 1.00 38.46  ? 913  ILE   B CG1   1 
ATOM   11327 C  CG2   . ILE   B 1 913  ? 146.231 160.025 113.856 1.00 37.86  ? 913  ILE   B CG2   1 
ATOM   11328 C  CD1   . ILE   B 1 913  ? 147.062 156.350 112.968 1.00 40.39  ? 913  ILE   B CD1   1 
ATOM   11329 N  N     . GLN   B 1 914  ? 142.732 158.734 113.755 1.00 32.08  ? 914  GLN   B N     1 
ATOM   11330 C  CA    . GLN   B 1 914  ? 141.760 158.957 114.828 1.00 31.41  ? 914  GLN   B CA    1 
ATOM   11331 C  C     . GLN   B 1 914  ? 142.373 159.748 115.981 1.00 29.95  ? 914  GLN   B C     1 
ATOM   11332 O  O     . GLN   B 1 914  ? 142.329 159.346 117.146 1.00 28.67  ? 914  GLN   B O     1 
ATOM   11333 C  CB    . GLN   B 1 914  ? 141.144 157.643 115.318 1.00 31.98  ? 914  GLN   B CB    1 
ATOM   11334 C  CG    . GLN   B 1 914  ? 142.096 156.478 115.481 1.00 42.78  ? 914  GLN   B CG    1 
ATOM   11335 C  CD    . GLN   B 1 914  ? 141.444 155.155 115.134 1.00 47.72  ? 914  GLN   B CD    1 
ATOM   11336 O  OE1   . GLN   B 1 914  ? 140.643 155.071 114.202 1.00 41.73  ? 914  GLN   B OE1   1 
ATOM   11337 N  NE2   . GLN   B 1 914  ? 141.776 154.115 115.888 1.00 44.96  ? 914  GLN   B NE2   1 
ATOM   11338 N  N     . TYR   B 1 915  ? 142.950 160.893 115.639 1.00 26.83  ? 915  TYR   B N     1 
ATOM   11339 C  CA    . TYR   B 1 915  ? 143.379 161.894 116.600 1.00 18.31  ? 915  TYR   B CA    1 
ATOM   11340 C  C     . TYR   B 1 915  ? 142.328 162.990 116.692 1.00 22.61  ? 915  TYR   B C     1 
ATOM   11341 O  O     . TYR   B 1 915  ? 141.609 163.265 115.728 1.00 37.71  ? 915  TYR   B O     1 
ATOM   11342 C  CB    . TYR   B 1 915  ? 144.718 162.518 116.190 1.00 20.46  ? 915  TYR   B CB    1 
ATOM   11343 C  CG    . TYR   B 1 915  ? 145.955 161.903 116.806 1.00 23.45  ? 915  TYR   B CG    1 
ATOM   11344 C  CD1   . TYR   B 1 915  ? 146.054 160.536 117.014 1.00 27.01  ? 915  TYR   B CD1   1 
ATOM   11345 C  CD2   . TYR   B 1 915  ? 147.037 162.700 117.159 1.00 21.96  ? 915  TYR   B CD2   1 
ATOM   11346 C  CE1   . TYR   B 1 915  ? 147.191 159.982 117.568 1.00 29.50  ? 915  TYR   B CE1   1 
ATOM   11347 C  CE2   . TYR   B 1 915  ? 148.174 162.156 117.713 1.00 24.94  ? 915  TYR   B CE2   1 
ATOM   11348 C  CZ    . TYR   B 1 915  ? 148.247 160.798 117.914 1.00 28.03  ? 915  TYR   B CZ    1 
ATOM   11349 O  OH    . TYR   B 1 915  ? 149.382 160.253 118.466 1.00 33.14  ? 915  TYR   B OH    1 
ATOM   11350 N  N     . GLY   B 1 916  ? 142.237 163.612 117.862 1.00 13.53  ? 916  GLY   B N     1 
ATOM   11351 C  CA    . GLY   B 1 916  ? 141.575 164.892 117.946 1.00 13.78  ? 916  GLY   B CA    1 
ATOM   11352 C  C     . GLY   B 1 916  ? 142.444 165.979 117.351 1.00 11.55  ? 916  GLY   B C     1 
ATOM   11353 O  O     . GLY   B 1 916  ? 143.652 165.825 117.197 1.00 27.26  ? 916  GLY   B O     1 
ATOM   11354 N  N     . VAL   B 1 917  ? 141.826 167.097 116.990 1.00 13.30  ? 917  VAL   B N     1 
ATOM   11355 C  CA    . VAL   B 1 917  ? 142.542 168.184 116.336 1.00 17.73  ? 917  VAL   B CA    1 
ATOM   11356 C  C     . VAL   B 1 917  ? 142.158 169.496 116.997 1.00 17.56  ? 917  VAL   B C     1 
ATOM   11357 O  O     . VAL   B 1 917  ? 140.972 169.831 117.082 1.00 25.32  ? 917  VAL   B O     1 
ATOM   11358 C  CB    . VAL   B 1 917  ? 142.249 168.232 114.825 1.00 21.13  ? 917  VAL   B CB    1 
ATOM   11359 C  CG1   . VAL   B 1 917  ? 142.875 169.469 114.205 1.00 15.79  ? 917  VAL   B CG1   1 
ATOM   11360 C  CG2   . VAL   B 1 917  ? 142.762 166.974 114.152 1.00 15.15  ? 917  VAL   B CG2   1 
ATOM   11361 N  N     . VAL   B 1 918  ? 143.158 170.245 117.451 1.00 19.08  ? 918  VAL   B N     1 
ATOM   11362 C  CA    . VAL   B 1 918  ? 142.946 171.570 118.018 1.00 19.88  ? 918  VAL   B CA    1 
ATOM   11363 C  C     . VAL   B 1 918  ? 143.783 172.556 117.221 1.00 20.95  ? 918  VAL   B C     1 
ATOM   11364 O  O     . VAL   B 1 918  ? 145.008 172.412 117.142 1.00 27.95  ? 918  VAL   B O     1 
ATOM   11365 C  CB    . VAL   B 1 918  ? 143.309 171.622 119.509 1.00 16.52  ? 918  VAL   B CB    1 
ATOM   11366 C  CG1   . VAL   B 1 918  ? 143.054 173.013 120.064 1.00 17.03  ? 918  VAL   B CG1   1 
ATOM   11367 C  CG2   . VAL   B 1 918  ? 142.524 170.581 120.281 1.00 21.19  ? 918  VAL   B CG2   1 
ATOM   11368 N  N     . VAL   B 1 919  ? 143.129 173.564 116.652 1.00 19.91  ? 919  VAL   B N     1 
ATOM   11369 C  CA    . VAL   B 1 919  ? 143.791 174.610 115.883 1.00 17.00  ? 919  VAL   B CA    1 
ATOM   11370 C  C     . VAL   B 1 919  ? 143.669 175.904 116.671 1.00 21.81  ? 919  VAL   B C     1 
ATOM   11371 O  O     . VAL   B 1 919  ? 142.558 176.335 117.000 1.00 32.24  ? 919  VAL   B O     1 
ATOM   11372 C  CB    . VAL   B 1 919  ? 143.180 174.758 114.483 1.00 17.08  ? 919  VAL   B CB    1 
ATOM   11373 C  CG1   . VAL   B 1 919  ? 143.864 175.882 113.720 1.00 24.94  ? 919  VAL   B CG1   1 
ATOM   11374 C  CG2   . VAL   B 1 919  ? 143.279 173.451 113.729 1.00 22.18  ? 919  VAL   B CG2   1 
ATOM   11375 N  N     . ILE   B 1 920  ? 144.803 176.529 116.966 1.00 18.11  ? 920  ILE   B N     1 
ATOM   11376 C  CA    . ILE   B 1 920  ? 144.851 177.711 117.817 1.00 16.58  ? 920  ILE   B CA    1 
ATOM   11377 C  C     . ILE   B 1 920  ? 145.153 178.922 116.950 1.00 20.21  ? 920  ILE   B C     1 
ATOM   11378 O  O     . ILE   B 1 920  ? 146.150 178.938 116.218 1.00 33.14  ? 920  ILE   B O     1 
ATOM   11379 C  CB    . ILE   B 1 920  ? 145.897 177.558 118.933 1.00 27.35  ? 920  ILE   B CB    1 
ATOM   11380 C  CG1   . ILE   B 1 920  ? 145.556 176.355 119.812 1.00 30.24  ? 920  ILE   B CG1   1 
ATOM   11381 C  CG2   . ILE   B 1 920  ? 145.972 178.827 119.764 1.00 30.37  ? 920  ILE   B CG2   1 
ATOM   11382 C  CD1   . ILE   B 1 920  ? 146.458 176.205 121.009 1.00 30.17  ? 920  ILE   B CD1   1 
ATOM   11383 N  N     . ARG   B 1 921  ? 144.293 179.936 117.034 1.00 29.89  ? 921  ARG   B N     1 
ATOM   11384 C  CA    . ARG   B 1 921  ? 144.457 181.182 116.295 1.00 30.69  ? 921  ARG   B CA    1 
ATOM   11385 C  C     . ARG   B 1 921  ? 144.502 182.320 117.304 1.00 35.54  ? 921  ARG   B C     1 
ATOM   11386 O  O     . ARG   B 1 921  ? 143.494 182.623 117.953 1.00 43.63  ? 921  ARG   B O     1 
ATOM   11387 C  CB    . ARG   B 1 921  ? 143.323 181.371 115.289 1.00 31.46  ? 921  ARG   B CB    1 
ATOM   11388 C  CG    . ARG   B 1 921  ? 143.277 182.739 114.640 1.00 24.65  ? 921  ARG   B CG    1 
ATOM   11389 C  CD    . ARG   B 1 921  ? 143.373 182.614 113.134 1.00 26.61  ? 921  ARG   B CD    1 
ATOM   11390 N  NE    . ARG   B 1 921  ? 143.519 183.910 112.483 1.00 32.04  ? 921  ARG   B NE    1 
ATOM   11391 C  CZ    . ARG   B 1 921  ? 142.856 184.278 111.396 1.00 36.75  ? 921  ARG   B CZ    1 
ATOM   11392 N  NH1   . ARG   B 1 921  ? 142.001 183.464 110.799 1.00 28.06  ? 921  ARG   B NH1   1 
ATOM   11393 N  NH2   . ARG   B 1 921  ? 143.064 185.490 110.890 1.00 38.47  ? 921  ARG   B NH2   1 
ATOM   11394 N  N     . LEU   B 1 922  ? 145.670 182.940 117.444 1.00 36.56  ? 922  LEU   B N     1 
ATOM   11395 C  CA    . LEU   B 1 922  ? 145.858 184.014 118.407 1.00 37.16  ? 922  LEU   B CA    1 
ATOM   11396 C  C     . LEU   B 1 922  ? 147.003 184.900 117.943 1.00 35.76  ? 922  LEU   B C     1 
ATOM   11397 O  O     . LEU   B 1 922  ? 147.848 184.489 117.144 1.00 44.00  ? 922  LEU   B O     1 
ATOM   11398 C  CB    . LEU   B 1 922  ? 146.135 183.471 119.814 1.00 37.08  ? 922  LEU   B CB    1 
ATOM   11399 C  CG    . LEU   B 1 922  ? 147.499 182.828 120.074 1.00 34.34  ? 922  LEU   B CG    1 
ATOM   11400 C  CD1   . LEU   B 1 922  ? 147.578 182.322 121.503 1.00 32.24  ? 922  LEU   B CD1   1 
ATOM   11401 C  CD2   . LEU   B 1 922  ? 147.772 181.699 119.095 1.00 42.60  ? 922  LEU   B CD2   1 
ATOM   11402 N  N     . LYS   B 1 923  ? 147.018 186.127 118.455 1.00 46.33  ? 923  LYS   B N     1 
ATOM   11403 C  CA    . LYS   B 1 923  ? 148.067 187.080 118.122 1.00 46.77  ? 923  LYS   B CA    1 
ATOM   11404 C  C     . LYS   B 1 923  ? 149.298 186.825 118.982 1.00 52.54  ? 923  LYS   B C     1 
ATOM   11405 O  O     . LYS   B 1 923  ? 149.197 186.714 120.208 1.00 55.59  ? 923  LYS   B O     1 
ATOM   11406 C  CB    . LYS   B 1 923  ? 147.568 188.511 118.320 1.00 45.38  ? 923  LYS   B CB    1 
ATOM   11407 N  N     . GLU   B 1 924  ? 150.461 186.733 118.338 1.00 59.41  ? 924  GLU   B N     1 
ATOM   11408 C  CA    . GLU   B 1 924  ? 151.707 186.465 119.046 1.00 59.01  ? 924  GLU   B CA    1 
ATOM   11409 C  C     . GLU   B 1 924  ? 152.488 187.735 119.359 1.00 64.29  ? 924  GLU   B C     1 
ATOM   11410 O  O     . GLU   B 1 924  ? 153.081 187.845 120.438 1.00 60.88  ? 924  GLU   B O     1 
ATOM   11411 C  CB    . GLU   B 1 924  ? 152.579 185.508 118.231 1.00 61.43  ? 924  GLU   B CB    1 
ATOM   11412 C  CG    . GLU   B 1 924  ? 153.455 184.607 119.078 1.00 62.97  ? 924  GLU   B CG    1 
ATOM   11413 C  CD    . GLU   B 1 924  ? 152.752 183.327 119.477 1.00 62.06  ? 924  GLU   B CD    1 
ATOM   11414 O  OE1   . GLU   B 1 924  ? 151.901 182.848 118.700 1.00 62.22  ? 924  GLU   B OE1   1 
ATOM   11415 O  OE2   . GLU   B 1 924  ? 153.046 182.804 120.571 1.00 60.14  ? 924  GLU   B OE2   1 
ATOM   11416 N  N     . GLY   B 1 925  ? 152.506 188.696 118.434 1.00 78.04  ? 925  GLY   B N     1 
ATOM   11417 C  CA    . GLY   B 1 925  ? 153.261 189.916 118.668 1.00 79.47  ? 925  GLY   B CA    1 
ATOM   11418 C  C     . GLY   B 1 925  ? 152.776 190.683 119.882 1.00 84.23  ? 925  GLY   B C     1 
ATOM   11419 O  O     . GLY   B 1 925  ? 153.578 191.197 120.665 1.00 82.54  ? 925  GLY   B O     1 
ATOM   11420 N  N     . LEU   B 1 926  ? 151.461 190.769 120.058 1.00 91.07  ? 926  LEU   B N     1 
ATOM   11421 C  CA    . LEU   B 1 926  ? 150.887 191.481 121.193 1.00 88.60  ? 926  LEU   B CA    1 
ATOM   11422 C  C     . LEU   B 1 926  ? 149.428 191.092 121.403 1.00 87.36  ? 926  LEU   B C     1 
ATOM   11423 O  O     . LEU   B 1 926  ? 148.533 191.627 120.749 1.00 89.32  ? 926  LEU   B O     1 
ATOM   11424 C  CB    . LEU   B 1 926  ? 151.006 192.994 120.994 1.00 88.17  ? 926  LEU   B CB    1 
ATOM   11425 N  N     . ASN   B 1 1022 ? 135.311 189.077 131.928 1.00 44.32  ? 1022 ASN   B N     1 
ATOM   11426 C  CA    . ASN   B 1 1022 ? 136.160 187.894 131.849 1.00 46.92  ? 1022 ASN   B CA    1 
ATOM   11427 C  C     . ASN   B 1 1022 ? 135.318 186.639 131.662 1.00 40.34  ? 1022 ASN   B C     1 
ATOM   11428 O  O     . ASN   B 1 1022 ? 134.782 186.092 132.623 1.00 42.20  ? 1022 ASN   B O     1 
ATOM   11429 C  CB    . ASN   B 1 1022 ? 137.024 187.768 133.105 1.00 39.19  ? 1022 ASN   B CB    1 
ATOM   11430 N  N     . THR   B 1 1023 ? 135.205 186.185 130.416 1.00 35.09  ? 1023 THR   B N     1 
ATOM   11431 C  CA    . THR   B 1 1023 ? 134.364 185.045 130.088 1.00 36.70  ? 1023 THR   B CA    1 
ATOM   11432 C  C     . THR   B 1 1023 ? 135.072 184.141 129.091 1.00 38.50  ? 1023 THR   B C     1 
ATOM   11433 O  O     . THR   B 1 1023 ? 135.943 184.578 128.335 1.00 42.74  ? 1023 THR   B O     1 
ATOM   11434 C  CB    . THR   B 1 1023 ? 133.012 185.486 129.512 1.00 38.58  ? 1023 THR   B CB    1 
ATOM   11435 O  OG1   . THR   B 1 1023 ? 132.131 184.359 129.441 1.00 42.38  ? 1023 THR   B OG1   1 
ATOM   11436 C  CG2   . THR   B 1 1023 ? 133.191 186.071 128.123 1.00 38.25  ? 1023 THR   B CG2   1 
ATOM   11437 N  N     . ILE   B 1 1024 ? 134.687 182.869 129.108 1.00 37.53  ? 1024 ILE   B N     1 
ATOM   11438 C  CA    . ILE   B 1 1024 ? 135.122 181.879 128.133 1.00 36.25  ? 1024 ILE   B CA    1 
ATOM   11439 C  C     . ILE   B 1 1024 ? 133.874 181.419 127.395 1.00 34.75  ? 1024 ILE   B C     1 
ATOM   11440 O  O     . ILE   B 1 1024 ? 132.985 180.798 127.992 1.00 35.45  ? 1024 ILE   B O     1 
ATOM   11441 C  CB    . ILE   B 1 1024 ? 135.846 180.698 128.791 1.00 29.61  ? 1024 ILE   B CB    1 
ATOM   11442 C  CG1   . ILE   B 1 1024 ? 137.132 181.174 129.467 1.00 34.89  ? 1024 ILE   B CG1   1 
ATOM   11443 C  CG2   . ILE   B 1 1024 ? 136.144 179.618 127.767 1.00 33.33  ? 1024 ILE   B CG2   1 
ATOM   11444 C  CD1   . ILE   B 1 1024 ? 138.210 180.118 129.543 1.00 41.20  ? 1024 ILE   B CD1   1 
ATOM   11445 N  N     . ASP   B 1 1025 ? 133.799 181.728 126.106 1.00 34.06  ? 1025 ASP   B N     1 
ATOM   11446 C  CA    . ASP   B 1 1025 ? 132.627 181.424 125.299 1.00 31.57  ? 1025 ASP   B CA    1 
ATOM   11447 C  C     . ASP   B 1 1025 ? 132.882 180.142 124.519 1.00 27.96  ? 1025 ASP   B C     1 
ATOM   11448 O  O     . ASP   B 1 1025 ? 133.827 180.069 123.727 1.00 30.13  ? 1025 ASP   B O     1 
ATOM   11449 C  CB    . ASP   B 1 1025 ? 132.301 182.581 124.357 1.00 31.83  ? 1025 ASP   B CB    1 
ATOM   11450 C  CG    . ASP   B 1 1025 ? 131.977 183.859 125.101 1.00 41.63  ? 1025 ASP   B CG    1 
ATOM   11451 O  OD1   . ASP   B 1 1025 ? 132.262 183.926 126.316 1.00 33.82  ? 1025 ASP   B OD1   1 
ATOM   11452 O  OD2   . ASP   B 1 1025 ? 131.433 184.793 124.477 1.00 43.61  ? 1025 ASP   B OD2   1 
ATOM   11453 N  N     . VAL   B 1 1026 ? 132.043 179.137 124.748 1.00 23.33  ? 1026 VAL   B N     1 
ATOM   11454 C  CA    . VAL   B 1 1026 ? 132.198 177.824 124.133 1.00 22.16  ? 1026 VAL   B CA    1 
ATOM   11455 C  C     . VAL   B 1 1026 ? 131.088 177.657 123.105 1.00 27.30  ? 1026 VAL   B C     1 
ATOM   11456 O  O     . VAL   B 1 1026 ? 129.925 177.441 123.463 1.00 29.53  ? 1026 VAL   B O     1 
ATOM   11457 C  CB    . VAL   B 1 1026 ? 132.166 176.698 125.174 1.00 23.28  ? 1026 VAL   B CB    1 
ATOM   11458 C  CG1   . VAL   B 1 1026 ? 132.394 175.355 124.504 1.00 20.01  ? 1026 VAL   B CG1   1 
ATOM   11459 C  CG2   . VAL   B 1 1026 ? 133.215 176.944 126.243 1.00 21.97  ? 1026 VAL   B CG2   1 
ATOM   11460 N  N     . TRP   B 1 1027 ? 131.448 177.770 121.828 1.00 24.84  ? 1027 TRP   B N     1 
ATOM   11461 C  CA    . TRP   B 1 1027 ? 130.510 177.577 120.724 1.00 18.14  ? 1027 TRP   B CA    1 
ATOM   11462 C  C     . TRP   B 1 1027 ? 130.670 176.170 120.154 1.00 21.65  ? 1027 TRP   B C     1 
ATOM   11463 O  O     . TRP   B 1 1027 ? 131.139 175.971 119.034 1.00 32.04  ? 1027 TRP   B O     1 
ATOM   11464 C  CB    . TRP   B 1 1027 ? 130.743 178.623 119.640 1.00 14.82  ? 1027 TRP   B CB    1 
ATOM   11465 C  CG    . TRP   B 1 1027 ? 130.553 180.035 120.060 1.00 15.60  ? 1027 TRP   B CG    1 
ATOM   11466 C  CD1   . TRP   B 1 1027 ? 131.260 180.709 121.008 1.00 20.24  ? 1027 TRP   B CD1   1 
ATOM   11467 C  CD2   . TRP   B 1 1027 ? 129.632 180.976 119.501 1.00 20.68  ? 1027 TRP   B CD2   1 
ATOM   11468 N  NE1   . TRP   B 1 1027 ? 130.816 182.004 121.098 1.00 29.57  ? 1027 TRP   B NE1   1 
ATOM   11469 C  CE2   . TRP   B 1 1027 ? 129.818 182.194 120.180 1.00 27.49  ? 1027 TRP   B CE2   1 
ATOM   11470 C  CE3   . TRP   B 1 1027 ? 128.658 180.902 118.500 1.00 13.92  ? 1027 TRP   B CE3   1 
ATOM   11471 C  CZ2   . TRP   B 1 1027 ? 129.068 183.329 119.892 1.00 25.24  ? 1027 TRP   B CZ2   1 
ATOM   11472 C  CZ3   . TRP   B 1 1027 ? 127.916 182.029 118.217 1.00 24.01  ? 1027 TRP   B CZ3   1 
ATOM   11473 C  CH2   . TRP   B 1 1027 ? 128.124 183.227 118.910 1.00 27.87  ? 1027 TRP   B CH2   1 
ATOM   11474 N  N     . TRP   B 1 1028 ? 130.272 175.180 120.939 1.00 16.10  ? 1028 TRP   B N     1 
ATOM   11475 C  CA    . TRP   B 1 1028 ? 130.352 173.798 120.493 1.00 30.79  ? 1028 TRP   B CA    1 
ATOM   11476 C  C     . TRP   B 1 1028 ? 128.987 173.391 119.948 1.00 34.78  ? 1028 TRP   B C     1 
ATOM   11477 O  O     . TRP   B 1 1028 ? 127.992 173.379 120.679 1.00 31.35  ? 1028 TRP   B O     1 
ATOM   11478 C  CB    . TRP   B 1 1028 ? 130.860 172.883 121.612 1.00 33.84  ? 1028 TRP   B CB    1 
ATOM   11479 C  CG    . TRP   B 1 1028 ? 129.861 172.185 122.480 1.00 28.49  ? 1028 TRP   B CG    1 
ATOM   11480 C  CD1   . TRP   B 1 1028 ? 128.858 172.752 123.211 1.00 36.36  ? 1028 TRP   B CD1   1 
ATOM   11481 C  CD2   . TRP   B 1 1028 ? 129.809 170.781 122.748 1.00 30.88  ? 1028 TRP   B CD2   1 
ATOM   11482 N  NE1   . TRP   B 1 1028 ? 128.169 171.782 123.898 1.00 42.96  ? 1028 TRP   B NE1   1 
ATOM   11483 C  CE2   . TRP   B 1 1028 ? 128.735 170.563 123.632 1.00 41.56  ? 1028 TRP   B CE2   1 
ATOM   11484 C  CE3   . TRP   B 1 1028 ? 130.560 169.684 122.317 1.00 30.65  ? 1028 TRP   B CE3   1 
ATOM   11485 C  CZ2   . TRP   B 1 1028 ? 128.395 169.294 124.092 1.00 40.89  ? 1028 TRP   B CZ2   1 
ATOM   11486 C  CZ3   . TRP   B 1 1028 ? 130.221 168.427 122.773 1.00 34.25  ? 1028 TRP   B CZ3   1 
ATOM   11487 C  CH2   . TRP   B 1 1028 ? 129.147 168.241 123.651 1.00 38.28  ? 1028 TRP   B CH2   1 
ATOM   11488 N  N     . LEU   B 1 1029 ? 128.942 173.113 118.645 1.00 38.07  ? 1029 LEU   B N     1 
ATOM   11489 C  CA    . LEU   B 1 1029 ? 127.700 172.880 117.926 1.00 26.52  ? 1029 LEU   B CA    1 
ATOM   11490 C  C     . LEU   B 1 1029 ? 127.566 171.462 117.400 1.00 32.88  ? 1029 LEU   B C     1 
ATOM   11491 O  O     . LEU   B 1 1029 ? 126.490 171.100 116.913 1.00 48.53  ? 1029 LEU   B O     1 
ATOM   11492 C  CB    . LEU   B 1 1029 ? 127.581 173.862 116.752 1.00 30.71  ? 1029 LEU   B CB    1 
ATOM   11493 C  CG    . LEU   B 1 1029 ? 128.200 175.243 116.972 1.00 31.48  ? 1029 LEU   B CG    1 
ATOM   11494 C  CD1   . LEU   B 1 1029 ? 128.400 175.957 115.650 1.00 26.65  ? 1029 LEU   B CD1   1 
ATOM   11495 C  CD2   . LEU   B 1 1029 ? 127.325 176.075 117.891 1.00 28.73  ? 1029 LEU   B CD2   1 
ATOM   11496 N  N     . PHE   B 1 1030 ? 128.618 170.656 117.481 1.00 21.56  ? 1030 PHE   B N     1 
ATOM   11497 C  CA    . PHE   B 1 1030 ? 128.572 169.277 117.027 1.00 22.00  ? 1030 PHE   B CA    1 
ATOM   11498 C  C     . PHE   B 1 1030 ? 129.235 168.403 118.077 1.00 28.33  ? 1030 PHE   B C     1 
ATOM   11499 O  O     . PHE   B 1 1030 ? 130.271 168.771 118.637 1.00 39.81  ? 1030 PHE   B O     1 
ATOM   11500 C  CB    . PHE   B 1 1030 ? 129.262 169.115 115.668 1.00 28.43  ? 1030 PHE   B CB    1 
ATOM   11501 C  CG    . PHE   B 1 1030 ? 128.941 170.213 114.696 1.00 37.64  ? 1030 PHE   B CG    1 
ATOM   11502 C  CD1   . PHE   B 1 1030 ? 127.754 170.203 113.982 1.00 41.58  ? 1030 PHE   B CD1   1 
ATOM   11503 C  CD2   . PHE   B 1 1030 ? 129.824 171.257 114.495 1.00 37.26  ? 1030 PHE   B CD2   1 
ATOM   11504 C  CE1   . PHE   B 1 1030 ? 127.455 171.216 113.090 1.00 35.41  ? 1030 PHE   B CE1   1 
ATOM   11505 C  CE2   . PHE   B 1 1030 ? 129.531 172.271 113.603 1.00 39.08  ? 1030 PHE   B CE2   1 
ATOM   11506 C  CZ    . PHE   B 1 1030 ? 128.345 172.250 112.900 1.00 35.75  ? 1030 PHE   B CZ    1 
ATOM   11507 N  N     . ASP   B 1 1031 ? 128.631 167.251 118.344 1.00 25.79  ? 1031 ASP   B N     1 
ATOM   11508 C  CA    . ASP   B 1 1031 ? 129.095 166.384 119.419 1.00 27.95  ? 1031 ASP   B CA    1 
ATOM   11509 C  C     . ASP   B 1 1031 ? 130.335 165.632 118.950 1.00 32.80  ? 1031 ASP   B C     1 
ATOM   11510 O  O     . ASP   B 1 1031 ? 130.240 164.689 118.158 1.00 38.61  ? 1031 ASP   B O     1 
ATOM   11511 C  CB    . ASP   B 1 1031 ? 127.989 165.424 119.846 1.00 24.90  ? 1031 ASP   B CB    1 
ATOM   11512 C  CG    . ASP   B 1 1031 ? 128.481 164.363 120.804 1.00 37.41  ? 1031 ASP   B CG    1 
ATOM   11513 O  OD1   . ASP   B 1 1031 ? 129.158 164.727 121.788 1.00 41.37  ? 1031 ASP   B OD1   1 
ATOM   11514 O  OD2   . ASP   B 1 1031 ? 128.190 163.171 120.582 1.00 42.65  ? 1031 ASP   B OD2   1 
ATOM   11515 N  N     . ASP   B 1 1032 ? 131.499 166.053 119.439 1.00 31.20  ? 1032 ASP   B N     1 
ATOM   11516 C  CA    . ASP   B 1 1032 ? 132.769 165.414 119.131 1.00 28.66  ? 1032 ASP   B CA    1 
ATOM   11517 C  C     . ASP   B 1 1032 ? 133.183 164.407 120.193 1.00 35.07  ? 1032 ASP   B C     1 
ATOM   11518 O  O     . ASP   B 1 1032 ? 134.292 163.870 120.128 1.00 36.93  ? 1032 ASP   B O     1 
ATOM   11519 C  CB    . ASP   B 1 1032 ? 133.861 166.471 118.966 1.00 27.31  ? 1032 ASP   B CB    1 
ATOM   11520 C  CG    . ASP   B 1 1032 ? 133.941 167.413 120.151 1.00 35.44  ? 1032 ASP   B CG    1 
ATOM   11521 O  OD1   . ASP   B 1 1032 ? 133.136 167.253 121.092 1.00 37.46  ? 1032 ASP   B OD1   1 
ATOM   11522 O  OD2   . ASP   B 1 1032 ? 134.806 168.312 120.144 1.00 39.73  ? 1032 ASP   B OD2   1 
ATOM   11523 N  N     . GLY   B 1 1033 ? 132.316 164.142 121.167 1.00 31.85  ? 1033 GLY   B N     1 
ATOM   11524 C  CA    . GLY   B 1 1033 ? 132.640 163.322 122.313 1.00 26.26  ? 1033 GLY   B CA    1 
ATOM   11525 C  C     . GLY   B 1 1033 ? 132.849 164.103 123.591 1.00 28.25  ? 1033 GLY   B C     1 
ATOM   11526 O  O     . GLY   B 1 1033 ? 132.868 163.500 124.672 1.00 34.42  ? 1033 GLY   B O     1 
ATOM   11527 N  N     . GLY   B 1 1034 ? 133.013 165.420 123.504 1.00 27.27  ? 1034 GLY   B N     1 
ATOM   11528 C  CA    . GLY   B 1 1034 ? 133.114 166.271 124.676 1.00 28.26  ? 1034 GLY   B CA    1 
ATOM   11529 C  C     . GLY   B 1 1034 ? 134.390 167.078 124.787 1.00 26.90  ? 1034 GLY   B C     1 
ATOM   11530 O  O     . GLY   B 1 1034 ? 134.482 167.929 125.684 1.00 30.58  ? 1034 GLY   B O     1 
ATOM   11531 N  N     . LEU   B 1 1035 ? 135.382 166.860 123.921 1.00 21.79  ? 1035 LEU   B N     1 
ATOM   11532 C  CA    . LEU   B 1 1035 ? 136.654 167.562 124.065 1.00 21.57  ? 1035 LEU   B CA    1 
ATOM   11533 C  C     . LEU   B 1 1035 ? 136.466 169.073 123.995 1.00 27.61  ? 1035 LEU   B C     1 
ATOM   11534 O  O     . LEU   B 1 1035 ? 137.128 169.824 124.724 1.00 24.87  ? 1035 LEU   B O     1 
ATOM   11535 C  CB    . LEU   B 1 1035 ? 137.636 167.091 122.994 1.00 22.25  ? 1035 LEU   B CB    1 
ATOM   11536 C  CG    . LEU   B 1 1035 ? 139.046 167.680 123.069 1.00 28.41  ? 1035 LEU   B CG    1 
ATOM   11537 C  CD1   . LEU   B 1 1035 ? 139.924 166.844 123.983 1.00 20.09  ? 1035 LEU   B CD1   1 
ATOM   11538 C  CD2   . LEU   B 1 1035 ? 139.662 167.783 121.687 1.00 24.81  ? 1035 LEU   B CD2   1 
ATOM   11539 N  N     . THR   B 1 1036 ? 135.564 169.537 123.125 1.00 28.34  ? 1036 THR   B N     1 
ATOM   11540 C  CA    . THR   B 1 1036 ? 135.310 170.969 123.013 1.00 29.33  ? 1036 THR   B CA    1 
ATOM   11541 C  C     . THR   B 1 1036 ? 134.857 171.558 124.341 1.00 32.31  ? 1036 THR   B C     1 
ATOM   11542 O  O     . THR   B 1 1036 ? 135.115 172.734 124.620 1.00 36.94  ? 1036 THR   B O     1 
ATOM   11543 C  CB    . THR   B 1 1036 ? 134.261 171.237 121.933 1.00 28.00  ? 1036 THR   B CB    1 
ATOM   11544 O  OG1   . THR   B 1 1036 ? 134.358 170.237 120.913 1.00 40.10  ? 1036 THR   B OG1   1 
ATOM   11545 C  CG2   . THR   B 1 1036 ? 134.475 172.609 121.308 1.00 32.15  ? 1036 THR   B CG2   1 
ATOM   11546 N  N     . LEU   B 1 1037 ? 134.179 170.764 125.165 1.00 27.31  ? 1037 LEU   B N     1 
ATOM   11547 C  CA    . LEU   B 1 1037 ? 133.787 171.205 126.495 1.00 29.02  ? 1037 LEU   B CA    1 
ATOM   11548 C  C     . LEU   B 1 1037 ? 134.846 170.898 127.543 1.00 26.90  ? 1037 LEU   B C     1 
ATOM   11549 O  O     . LEU   B 1 1037 ? 135.029 171.685 128.479 1.00 32.46  ? 1037 LEU   B O     1 
ATOM   11550 C  CB    . LEU   B 1 1037 ? 132.462 170.551 126.893 1.00 30.33  ? 1037 LEU   B CB    1 
ATOM   11551 C  CG    . LEU   B 1 1037 ? 131.639 171.277 127.955 1.00 28.24  ? 1037 LEU   B CG    1 
ATOM   11552 C  CD1   . LEU   B 1 1037 ? 131.884 172.771 127.874 1.00 30.24  ? 1037 LEU   B CD1   1 
ATOM   11553 C  CD2   . LEU   B 1 1037 ? 130.164 170.967 127.780 1.00 38.88  ? 1037 LEU   B CD2   1 
ATOM   11554 N  N     . LEU   B 1 1038 ? 135.553 169.776 127.401 1.00 21.53  ? 1038 LEU   B N     1 
ATOM   11555 C  CA    . LEU   B 1 1038 ? 136.548 169.387 128.391 1.00 25.32  ? 1038 LEU   B CA    1 
ATOM   11556 C  C     . LEU   B 1 1038 ? 137.769 170.296 128.389 1.00 23.09  ? 1038 LEU   B C     1 
ATOM   11557 O  O     . LEU   B 1 1038 ? 138.438 170.409 129.421 1.00 23.89  ? 1038 LEU   B O     1 
ATOM   11558 C  CB    . LEU   B 1 1038 ? 136.982 167.939 128.159 1.00 21.57  ? 1038 LEU   B CB    1 
ATOM   11559 C  CG    . LEU   B 1 1038 ? 138.112 167.422 129.053 1.00 23.10  ? 1038 LEU   B CG    1 
ATOM   11560 C  CD1   . LEU   B 1 1038 ? 137.706 167.460 130.517 1.00 26.82  ? 1038 LEU   B CD1   1 
ATOM   11561 C  CD2   . LEU   B 1 1038 ? 138.520 166.016 128.651 1.00 24.05  ? 1038 LEU   B CD2   1 
ATOM   11562 N  N     . ILE   B 1 1039 ? 138.076 170.947 127.271 1.00 19.83  ? 1039 ILE   B N     1 
ATOM   11563 C  CA    . ILE   B 1 1039 ? 139.270 171.788 127.196 1.00 24.62  ? 1039 ILE   B CA    1 
ATOM   11564 C  C     . ILE   B 1 1039 ? 139.054 173.081 127.977 1.00 31.03  ? 1039 ILE   B C     1 
ATOM   11565 O  O     . ILE   B 1 1039 ? 139.865 173.413 128.857 1.00 36.46  ? 1039 ILE   B O     1 
ATOM   11566 C  CB    . ILE   B 1 1039 ? 139.653 172.086 125.738 1.00 27.12  ? 1039 ILE   B CB    1 
ATOM   11567 C  CG1   . ILE   B 1 1039 ? 140.545 170.973 125.187 1.00 23.98  ? 1039 ILE   B CG1   1 
ATOM   11568 C  CG2   . ILE   B 1 1039 ? 140.365 173.426 125.640 1.00 22.56  ? 1039 ILE   B CG2   1 
ATOM   11569 C  CD1   . ILE   B 1 1039 ? 141.084 171.255 123.806 1.00 19.04  ? 1039 ILE   B CD1   1 
ATOM   11570 N  N     . PRO   B 1 1040 ? 137.995 173.843 127.697 1.00 22.15  ? 1040 PRO   B N     1 
ATOM   11571 C  CA    . PRO   B 1 1040 ? 137.782 175.087 128.454 1.00 23.26  ? 1040 PRO   B CA    1 
ATOM   11572 C  C     . PRO   B 1 1040 ? 137.561 174.860 129.939 1.00 27.60  ? 1040 PRO   B C     1 
ATOM   11573 O  O     . PRO   B 1 1040 ? 137.880 175.741 130.746 1.00 31.92  ? 1040 PRO   B O     1 
ATOM   11574 C  CB    . PRO   B 1 1040 ? 136.549 175.701 127.777 1.00 24.27  ? 1040 PRO   B CB    1 
ATOM   11575 C  CG    . PRO   B 1 1040 ? 135.841 174.547 127.166 1.00 24.76  ? 1040 PRO   B CG    1 
ATOM   11576 C  CD    . PRO   B 1 1040 ? 136.907 173.583 126.739 1.00 20.22  ? 1040 PRO   B CD    1 
ATOM   11577 N  N     . TYR   B 1 1041 ? 137.034 173.700 130.334 1.00 19.16  ? 1041 TYR   B N     1 
ATOM   11578 C  CA    . TYR   B 1 1041 ? 136.887 173.419 131.757 1.00 19.00  ? 1041 TYR   B CA    1 
ATOM   11579 C  C     . TYR   B 1 1041 ? 138.251 173.314 132.430 1.00 28.69  ? 1041 TYR   B C     1 
ATOM   11580 O  O     . TYR   B 1 1041 ? 138.489 173.924 133.480 1.00 40.81  ? 1041 TYR   B O     1 
ATOM   11581 C  CB    . TYR   B 1 1041 ? 136.079 172.138 131.965 1.00 27.29  ? 1041 TYR   B CB    1 
ATOM   11582 C  CG    . TYR   B 1 1041 ? 136.269 171.525 133.332 1.00 31.09  ? 1041 TYR   B CG    1 
ATOM   11583 C  CD1   . TYR   B 1 1041 ? 135.625 172.052 134.443 1.00 31.86  ? 1041 TYR   B CD1   1 
ATOM   11584 C  CD2   . TYR   B 1 1041 ? 137.096 170.427 133.514 1.00 28.58  ? 1041 TYR   B CD2   1 
ATOM   11585 C  CE1   . TYR   B 1 1041 ? 135.797 171.502 135.694 1.00 34.81  ? 1041 TYR   B CE1   1 
ATOM   11586 C  CE2   . TYR   B 1 1041 ? 137.274 169.869 134.763 1.00 27.98  ? 1041 TYR   B CE2   1 
ATOM   11587 C  CZ    . TYR   B 1 1041 ? 136.623 170.412 135.850 1.00 36.66  ? 1041 TYR   B CZ    1 
ATOM   11588 O  OH    . TYR   B 1 1041 ? 136.794 169.862 137.098 1.00 41.46  ? 1041 TYR   B OH    1 
ATOM   11589 N  N     . LEU   B 1 1042 ? 139.165 172.545 131.835 1.00 29.07  ? 1042 LEU   B N     1 
ATOM   11590 C  CA    . LEU   B 1 1042 ? 140.529 172.500 132.349 1.00 23.86  ? 1042 LEU   B CA    1 
ATOM   11591 C  C     . LEU   B 1 1042 ? 141.168 173.881 132.321 1.00 26.86  ? 1042 LEU   B C     1 
ATOM   11592 O  O     . LEU   B 1 1042 ? 141.971 174.220 133.198 1.00 29.13  ? 1042 LEU   B O     1 
ATOM   11593 C  CB    . LEU   B 1 1042 ? 141.365 171.504 131.547 1.00 19.93  ? 1042 LEU   B CB    1 
ATOM   11594 C  CG    . LEU   B 1 1042 ? 140.843 170.069 131.495 1.00 24.41  ? 1042 LEU   B CG    1 
ATOM   11595 C  CD1   . LEU   B 1 1042 ? 141.540 169.287 130.398 1.00 25.60  ? 1042 LEU   B CD1   1 
ATOM   11596 C  CD2   . LEU   B 1 1042 ? 141.033 169.388 132.838 1.00 23.68  ? 1042 LEU   B CD2   1 
ATOM   11597 N  N     . LEU   B 1 1043 ? 140.829 174.691 131.317 1.00 30.55  ? 1043 LEU   B N     1 
ATOM   11598 C  CA    . LEU   B 1 1043 ? 141.300 176.072 131.299 1.00 32.44  ? 1043 LEU   B CA    1 
ATOM   11599 C  C     . LEU   B 1 1043 ? 140.859 176.807 132.558 1.00 35.67  ? 1043 LEU   B C     1 
ATOM   11600 O  O     . LEU   B 1 1043 ? 141.663 177.471 133.223 1.00 34.62  ? 1043 LEU   B O     1 
ATOM   11601 C  CB    . LEU   B 1 1043 ? 140.782 176.783 130.049 1.00 31.57  ? 1043 LEU   B CB    1 
ATOM   11602 C  CG    . LEU   B 1 1043 ? 141.648 177.901 129.471 1.00 37.33  ? 1043 LEU   B CG    1 
ATOM   11603 C  CD1   . LEU   B 1 1043 ? 143.099 177.463 129.387 1.00 35.21  ? 1043 LEU   B CD1   1 
ATOM   11604 C  CD2   . LEU   B 1 1043 ? 141.130 178.315 128.103 1.00 32.65  ? 1043 LEU   B CD2   1 
ATOM   11605 N  N     . THR   B 1 1044 ? 139.576 176.694 132.901 1.00 37.21  ? 1044 THR   B N     1 
ATOM   11606 C  CA    . THR   B 1 1044 ? 139.047 177.298 134.118 1.00 29.37  ? 1044 THR   B CA    1 
ATOM   11607 C  C     . THR   B 1 1044 ? 139.600 176.654 135.382 1.00 31.02  ? 1044 THR   B C     1 
ATOM   11608 O  O     . THR   B 1 1044 ? 139.473 177.240 136.462 1.00 34.57  ? 1044 THR   B O     1 
ATOM   11609 C  CB    . THR   B 1 1044 ? 137.518 177.215 134.131 1.00 29.59  ? 1044 THR   B CB    1 
ATOM   11610 O  OG1   . THR   B 1 1044 ? 137.114 175.865 134.386 1.00 31.40  ? 1044 THR   B OG1   1 
ATOM   11611 C  CG2   . THR   B 1 1044 ? 136.946 177.663 132.798 1.00 25.33  ? 1044 THR   B CG2   1 
ATOM   11612 N  N     . THR   B 1 1045 ? 140.204 175.472 135.275 1.00 38.24  ? 1045 THR   B N     1 
ATOM   11613 C  CA    . THR   B 1 1045 ? 140.764 174.784 136.432 1.00 34.03  ? 1045 THR   B CA    1 
ATOM   11614 C  C     . THR   B 1 1045 ? 142.086 175.383 136.901 1.00 37.42  ? 1045 THR   B C     1 
ATOM   11615 O  O     . THR   B 1 1045 ? 142.520 175.088 138.020 1.00 41.47  ? 1045 THR   B O     1 
ATOM   11616 C  CB    . THR   B 1 1045 ? 140.944 173.295 136.102 1.00 35.23  ? 1045 THR   B CB    1 
ATOM   11617 O  OG1   . THR   B 1 1045 ? 139.707 172.604 136.312 1.00 36.19  ? 1045 THR   B OG1   1 
ATOM   11618 C  CG2   . THR   B 1 1045 ? 142.018 172.657 136.968 1.00 33.98  ? 1045 THR   B CG2   1 
ATOM   11619 N  N     . LYS   B 1 1046 ? 142.715 176.239 136.103 1.00 41.95  ? 1046 LYS   B N     1 
ATOM   11620 C  CA    . LYS   B 1 1046 ? 144.009 176.815 136.436 1.00 35.61  ? 1046 LYS   B CA    1 
ATOM   11621 C  C     . LYS   B 1 1046 ? 143.847 178.212 137.022 1.00 40.87  ? 1046 LYS   B C     1 
ATOM   11622 O  O     . LYS   B 1 1046 ? 142.825 178.877 136.840 1.00 46.12  ? 1046 LYS   B O     1 
ATOM   11623 C  CB    . LYS   B 1 1046 ? 144.915 176.865 135.203 1.00 40.13  ? 1046 LYS   B CB    1 
ATOM   11624 C  CG    . LYS   B 1 1046 ? 145.126 175.519 134.531 1.00 40.11  ? 1046 LYS   B CG    1 
ATOM   11625 C  CD    . LYS   B 1 1046 ? 145.300 174.413 135.559 1.00 38.48  ? 1046 LYS   B CD    1 
ATOM   11626 C  CE    . LYS   B 1 1046 ? 145.244 173.041 134.910 1.00 37.63  ? 1046 LYS   B CE    1 
ATOM   11627 N  NZ    . LYS   B 1 1046 ? 146.601 172.535 134.565 1.00 36.00  ? 1046 LYS   B NZ    1 
ATOM   11628 N  N     . LYS   B 1 1047 ? 144.886 178.651 137.736 1.00 41.49  ? 1047 LYS   B N     1 
ATOM   11629 C  CA    . LYS   B 1 1047 ? 144.834 179.931 138.432 1.00 39.77  ? 1047 LYS   B CA    1 
ATOM   11630 C  C     . LYS   B 1 1047 ? 144.759 181.116 137.479 1.00 44.25  ? 1047 LYS   B C     1 
ATOM   11631 O  O     . LYS   B 1 1047 ? 144.311 182.192 137.887 1.00 47.81  ? 1047 LYS   B O     1 
ATOM   11632 C  CB    . LYS   B 1 1047 ? 146.050 180.081 139.348 1.00 37.80  ? 1047 LYS   B CB    1 
ATOM   11633 N  N     . LYS   B 1 1048 ? 145.183 180.951 136.225 1.00 42.61  ? 1048 LYS   B N     1 
ATOM   11634 C  CA    . LYS   B 1 1048 ? 145.145 182.056 135.276 1.00 42.50  ? 1048 LYS   B CA    1 
ATOM   11635 C  C     . LYS   B 1 1048 ? 143.760 182.273 134.680 1.00 44.14  ? 1048 LYS   B C     1 
ATOM   11636 O  O     . LYS   B 1 1048 ? 143.511 183.334 134.098 1.00 44.84  ? 1048 LYS   B O     1 
ATOM   11637 C  CB    . LYS   B 1 1048 ? 146.158 181.821 134.153 1.00 46.93  ? 1048 LYS   B CB    1 
ATOM   11638 C  CG    . LYS   B 1 1048 ? 146.183 182.916 133.099 1.00 48.06  ? 1048 LYS   B CG    1 
ATOM   11639 C  CD    . LYS   B 1 1048 ? 147.258 182.662 132.056 1.00 48.71  ? 1048 LYS   B CD    1 
ATOM   11640 C  CE    . LYS   B 1 1048 ? 147.612 183.939 131.312 1.00 50.33  ? 1048 LYS   B CE    1 
ATOM   11641 N  NZ    . LYS   B 1 1048 ? 146.624 185.021 131.576 1.00 52.62  ? 1048 LYS   B NZ    1 
ATOM   11642 N  N     . TRP   B 1 1049 ? 142.854 181.301 134.818 1.00 42.92  ? 1049 TRP   B N     1 
ATOM   11643 C  CA    . TRP   B 1 1049 ? 141.503 181.415 134.278 1.00 43.99  ? 1049 TRP   B CA    1 
ATOM   11644 C  C     . TRP   B 1 1049 ? 140.441 181.145 135.339 1.00 42.88  ? 1049 TRP   B C     1 
ATOM   11645 O  O     . TRP   B 1 1049 ? 139.309 180.789 134.997 1.00 47.84  ? 1049 TRP   B O     1 
ATOM   11646 C  CB    . TRP   B 1 1049 ? 141.314 180.469 133.089 1.00 47.63  ? 1049 TRP   B CB    1 
ATOM   11647 C  CG    . TRP   B 1 1049 ? 142.451 180.500 132.113 1.00 43.26  ? 1049 TRP   B CG    1 
ATOM   11648 C  CD1   . TRP   B 1 1049 ? 143.495 179.627 132.043 1.00 40.87  ? 1049 TRP   B CD1   1 
ATOM   11649 C  CD2   . TRP   B 1 1049 ? 142.657 181.456 131.067 1.00 38.46  ? 1049 TRP   B CD2   1 
ATOM   11650 N  NE1   . TRP   B 1 1049 ? 144.340 179.980 131.020 1.00 38.06  ? 1049 TRP   B NE1   1 
ATOM   11651 C  CE2   . TRP   B 1 1049 ? 143.847 181.100 130.405 1.00 41.72  ? 1049 TRP   B CE2   1 
ATOM   11652 C  CE3   . TRP   B 1 1049 ? 141.950 182.579 130.627 1.00 40.81  ? 1049 TRP   B CE3   1 
ATOM   11653 C  CZ2   . TRP   B 1 1049 ? 144.346 181.825 129.327 1.00 46.44  ? 1049 TRP   B CZ2   1 
ATOM   11654 C  CZ3   . TRP   B 1 1049 ? 142.447 183.297 129.557 1.00 45.18  ? 1049 TRP   B CZ3   1 
ATOM   11655 C  CH2   . TRP   B 1 1049 ? 143.634 182.918 128.919 1.00 47.03  ? 1049 TRP   B CH2   1 
ATOM   11656 N  N     . LYS   B 1 1050 ? 140.782 181.307 136.619 1.00 44.17  ? 1050 LYS   B N     1 
ATOM   11657 C  CA    . LYS   B 1 1050 ? 139.808 181.068 137.677 1.00 41.74  ? 1050 LYS   B CA    1 
ATOM   11658 C  C     . LYS   B 1 1050 ? 138.664 182.073 137.631 1.00 44.73  ? 1050 LYS   B C     1 
ATOM   11659 O  O     . LYS   B 1 1050 ? 137.518 181.718 137.926 1.00 47.24  ? 1050 LYS   B O     1 
ATOM   11660 C  CB    . LYS   B 1 1050 ? 140.495 181.111 139.042 1.00 45.48  ? 1050 LYS   B CB    1 
ATOM   11661 C  CG    . LYS   B 1 1050 ? 141.110 179.789 139.471 1.00 48.67  ? 1050 LYS   B CG    1 
ATOM   11662 C  CD    . LYS   B 1 1050 ? 140.197 178.622 139.140 1.00 47.65  ? 1050 LYS   B CD    1 
ATOM   11663 C  CE    . LYS   B 1 1050 ? 140.249 177.558 140.225 1.00 49.77  ? 1050 LYS   B CE    1 
ATOM   11664 N  NZ    . LYS   B 1 1050 ? 141.552 177.564 140.946 1.00 44.87  ? 1050 LYS   B NZ    1 
ATOM   11665 N  N     . ASP   B 1 1051 ? 138.950 183.323 137.265 1.00 49.78  ? 1051 ASP   B N     1 
ATOM   11666 C  CA    . ASP   B 1 1051 ? 137.918 184.352 137.264 1.00 48.81  ? 1051 ASP   B CA    1 
ATOM   11667 C  C     . ASP   B 1 1051 ? 136.964 184.219 136.084 1.00 46.09  ? 1051 ASP   B C     1 
ATOM   11668 O  O     . ASP   B 1 1051 ? 135.783 184.562 136.210 1.00 50.01  ? 1051 ASP   B O     1 
ATOM   11669 C  CB    . ASP   B 1 1051 ? 138.562 185.739 137.258 1.00 49.24  ? 1051 ASP   B CB    1 
ATOM   11670 N  N     . CYS   B 1 1052 ? 137.443 183.730 134.943 1.00 47.00  ? 1052 CYS   B N     1 
ATOM   11671 C  CA    . CYS   B 1 1052 ? 136.600 183.636 133.758 1.00 48.57  ? 1052 CYS   B CA    1 
ATOM   11672 C  C     . CYS   B 1 1052 ? 135.498 182.604 133.966 1.00 50.31  ? 1052 CYS   B C     1 
ATOM   11673 O  O     . CYS   B 1 1052 ? 135.746 181.505 134.470 1.00 51.49  ? 1052 CYS   B O     1 
ATOM   11674 C  CB    . CYS   B 1 1052 ? 137.442 183.274 132.536 1.00 46.01  ? 1052 CYS   B CB    1 
ATOM   11675 S  SG    . CYS   B 1 1052 ? 139.006 184.170 132.414 1.00 64.54  ? 1052 CYS   B SG    1 
ATOM   11676 N  N     . LYS   B 1 1053 ? 134.279 182.962 133.573 1.00 41.20  ? 1053 LYS   B N     1 
ATOM   11677 C  CA    . LYS   B 1 1053 ? 133.125 182.082 133.682 1.00 43.23  ? 1053 LYS   B CA    1 
ATOM   11678 C  C     . LYS   B 1 1053 ? 132.776 181.527 132.308 1.00 42.22  ? 1053 LYS   B C     1 
ATOM   11679 O  O     . LYS   B 1 1053 ? 132.937 182.210 131.294 1.00 43.98  ? 1053 LYS   B O     1 
ATOM   11680 C  CB    . LYS   B 1 1053 ? 131.924 182.825 134.269 1.00 43.37  ? 1053 LYS   B CB    1 
ATOM   11681 C  CG    . LYS   B 1 1053 ? 132.168 183.403 135.655 1.00 47.39  ? 1053 LYS   B CG    1 
ATOM   11682 C  CD    . LYS   B 1 1053 ? 131.086 184.401 136.039 1.00 51.42  ? 1053 LYS   B CD    1 
ATOM   11683 C  CE    . LYS   B 1 1053 ? 130.871 185.438 134.946 1.00 49.48  ? 1053 LYS   B CE    1 
ATOM   11684 N  NZ    . LYS   B 1 1053 ? 132.135 185.796 134.242 1.00 45.96  ? 1053 LYS   B NZ    1 
ATOM   11685 N  N     . ILE   B 1 1054 ? 132.301 180.288 132.280 1.00 35.14  ? 1054 ILE   B N     1 
ATOM   11686 C  CA    . ILE   B 1 1054 ? 132.018 179.594 131.029 1.00 32.71  ? 1054 ILE   B CA    1 
ATOM   11687 C  C     . ILE   B 1 1054 ? 130.594 179.915 130.596 1.00 34.43  ? 1054 ILE   B C     1 
ATOM   11688 O  O     . ILE   B 1 1054 ? 129.636 179.629 131.322 1.00 42.34  ? 1054 ILE   B O     1 
ATOM   11689 C  CB    . ILE   B 1 1054 ? 132.216 178.079 131.177 1.00 32.13  ? 1054 ILE   B CB    1 
ATOM   11690 C  CG1   . ILE   B 1 1054 ? 133.705 177.733 131.172 1.00 37.05  ? 1054 ILE   B CG1   1 
ATOM   11691 C  CG2   . ILE   B 1 1054 ? 131.494 177.342 130.064 1.00 29.98  ? 1054 ILE   B CG2   1 
ATOM   11692 C  CD1   . ILE   B 1 1054 ? 133.986 176.250 131.097 1.00 38.17  ? 1054 ILE   B CD1   1 
ATOM   11693 N  N     . ARG   B 1 1055 ? 130.453 180.507 129.414 1.00 34.12  ? 1055 ARG   B N     1 
ATOM   11694 C  CA    . ARG   B 1 1055 ? 129.151 180.726 128.798 1.00 29.28  ? 1055 ARG   B CA    1 
ATOM   11695 C  C     . ARG   B 1 1055 ? 129.084 179.924 127.508 1.00 30.16  ? 1055 ARG   B C     1 
ATOM   11696 O  O     . ARG   B 1 1055 ? 130.008 179.977 126.687 1.00 42.59  ? 1055 ARG   B O     1 
ATOM   11697 C  CB    . ARG   B 1 1055 ? 128.897 182.213 128.539 1.00 27.76  ? 1055 ARG   B CB    1 
ATOM   11698 C  CG    . ARG   B 1 1055 ? 129.868 182.863 127.582 1.00 39.25  ? 1055 ARG   B CG    1 
ATOM   11699 C  CD    . ARG   B 1 1055 ? 129.777 184.379 127.671 1.00 41.69  ? 1055 ARG   B CD    1 
ATOM   11700 N  NE    . ARG   B 1 1055 ? 128.615 184.913 126.971 1.00 41.79  ? 1055 ARG   B NE    1 
ATOM   11701 C  CZ    . ARG   B 1 1055 ? 128.562 186.120 126.425 1.00 39.19  ? 1055 ARG   B CZ    1 
ATOM   11702 N  NH1   . ARG   B 1 1055 ? 129.589 186.951 126.486 1.00 40.04  ? 1055 ARG   B NH1   1 
ATOM   11703 N  NH2   . ARG   B 1 1055 ? 127.451 186.503 125.804 1.00 41.08  ? 1055 ARG   B NH2   1 
ATOM   11704 N  N     . VAL   B 1 1056 ? 128.000 179.181 127.338 1.00 25.88  ? 1056 VAL   B N     1 
ATOM   11705 C  CA    . VAL   B 1 1056 ? 127.880 178.216 126.254 1.00 26.15  ? 1056 VAL   B CA    1 
ATOM   11706 C  C     . VAL   B 1 1056 ? 126.953 178.765 125.182 1.00 30.35  ? 1056 VAL   B C     1 
ATOM   11707 O  O     . VAL   B 1 1056 ? 126.000 179.500 125.464 1.00 23.65  ? 1056 VAL   B O     1 
ATOM   11708 C  CB    . VAL   B 1 1056 ? 127.379 176.855 126.781 1.00 24.00  ? 1056 VAL   B CB    1 
ATOM   11709 C  CG1   . VAL   B 1 1056 ? 127.002 175.942 125.630 1.00 24.51  ? 1056 VAL   B CG1   1 
ATOM   11710 C  CG2   . VAL   B 1 1056 ? 128.439 176.209 127.653 1.00 23.82  ? 1056 VAL   B CG2   1 
ATOM   11711 N  N     . PHE   B 1 1057 ? 127.244 178.405 123.934 1.00 34.19  ? 1057 PHE   B N     1 
ATOM   11712 C  CA    . PHE   B 1 1057 ? 126.412 178.744 122.789 1.00 23.64  ? 1057 PHE   B CA    1 
ATOM   11713 C  C     . PHE   B 1 1057 ? 126.070 177.461 122.051 1.00 25.08  ? 1057 PHE   B C     1 
ATOM   11714 O  O     . PHE   B 1 1057 ? 126.960 176.657 121.756 1.00 28.61  ? 1057 PHE   B O     1 
ATOM   11715 C  CB    . PHE   B 1 1057 ? 127.125 179.716 121.846 1.00 5.48   ? 1057 PHE   B CB    1 
ATOM   11716 C  CG    . PHE   B 1 1057 ? 127.449 181.039 122.468 1.00 17.06  ? 1057 PHE   B CG    1 
ATOM   11717 C  CD1   . PHE   B 1 1057 ? 128.535 181.174 123.313 1.00 23.13  ? 1057 PHE   B CD1   1 
ATOM   11718 C  CD2   . PHE   B 1 1057 ? 126.674 182.151 122.201 1.00 20.24  ? 1057 PHE   B CD2   1 
ATOM   11719 C  CE1   . PHE   B 1 1057 ? 128.837 182.392 123.885 1.00 25.90  ? 1057 PHE   B CE1   1 
ATOM   11720 C  CE2   . PHE   B 1 1057 ? 126.972 183.371 122.770 1.00 27.31  ? 1057 PHE   B CE2   1 
ATOM   11721 C  CZ    . PHE   B 1 1057 ? 128.055 183.491 123.613 1.00 31.19  ? 1057 PHE   B CZ    1 
ATOM   11722 N  N     . ILE   B 1 1058 ? 124.786 177.268 121.758 1.00 33.56  ? 1058 ILE   B N     1 
ATOM   11723 C  CA    . ILE   B 1 1058 ? 124.331 176.113 121.000 1.00 32.56  ? 1058 ILE   B CA    1 
ATOM   11724 C  C     . ILE   B 1 1058 ? 123.355 176.589 119.935 1.00 33.02  ? 1058 ILE   B C     1 
ATOM   11725 O  O     . ILE   B 1 1058 ? 122.852 177.713 119.977 1.00 34.43  ? 1058 ILE   B O     1 
ATOM   11726 C  CB    . ILE   B 1 1058 ? 123.680 175.036 121.895 1.00 37.91  ? 1058 ILE   B CB    1 
ATOM   11727 C  CG1   . ILE   B 1 1058 ? 122.614 175.657 122.798 1.00 33.77  ? 1058 ILE   B CG1   1 
ATOM   11728 C  CG2   . ILE   B 1 1058 ? 124.737 174.323 122.723 1.00 34.25  ? 1058 ILE   B CG2   1 
ATOM   11729 C  CD1   . ILE   B 1 1058 ? 121.340 174.848 122.877 1.00 31.95  ? 1058 ILE   B CD1   1 
ATOM   11730 N  N     . GLY   B 1 1059 ? 123.108 175.721 118.962 1.00 40.09  ? 1059 GLY   B N     1 
ATOM   11731 C  CA    . GLY   B 1 1059 ? 122.165 176.001 117.893 1.00 41.94  ? 1059 GLY   B CA    1 
ATOM   11732 C  C     . GLY   B 1 1059 ? 120.827 175.338 118.171 1.00 44.35  ? 1059 GLY   B C     1 
ATOM   11733 O  O     . GLY   B 1 1059 ? 120.770 174.214 118.669 1.00 54.18  ? 1059 GLY   B O     1 
ATOM   11734 N  N     . GLY   B 1 1060 ? 119.750 176.051 117.840 1.00 52.10  ? 1060 GLY   B N     1 
ATOM   11735 C  CA    . GLY   B 1 1060 ? 118.415 175.541 118.071 1.00 54.82  ? 1060 GLY   B CA    1 
ATOM   11736 C  C     . GLY   B 1 1060 ? 117.449 176.034 117.017 1.00 59.28  ? 1060 GLY   B C     1 
ATOM   11737 O  O     . GLY   B 1 1060 ? 117.785 176.860 116.166 1.00 60.28  ? 1060 GLY   B O     1 
ATOM   11738 N  N     . LYS   B 1 1061 ? 116.229 175.509 117.089 1.00 67.33  ? 1061 LYS   B N     1 
ATOM   11739 C  CA    . LYS   B 1 1061 ? 115.161 175.862 116.165 1.00 64.94  ? 1061 LYS   B CA    1 
ATOM   11740 C  C     . LYS   B 1 1061 ? 114.249 176.894 116.814 1.00 66.19  ? 1061 LYS   B C     1 
ATOM   11741 O  O     . LYS   B 1 1061 ? 113.879 176.752 117.984 1.00 70.97  ? 1061 LYS   B O     1 
ATOM   11742 C  CB    . LYS   B 1 1061 ? 114.356 174.625 115.766 1.00 64.05  ? 1061 LYS   B CB    1 
ATOM   11743 C  CG    . LYS   B 1 1061 ? 115.183 173.521 115.133 1.00 67.66  ? 1061 LYS   B CG    1 
ATOM   11744 C  CD    . LYS   B 1 1061 ? 114.366 172.726 114.131 1.00 67.29  ? 1061 LYS   B CD    1 
ATOM   11745 C  CE    . LYS   B 1 1061 ? 114.753 171.256 114.149 1.00 67.95  ? 1061 LYS   B CE    1 
ATOM   11746 N  NZ    . LYS   B 1 1061 ? 116.227 171.072 114.244 1.00 67.92  ? 1061 LYS   B NZ    1 
ATOM   11747 N  N     . ILE   B 1 1062 ? 113.894 177.931 116.054 1.00 70.63  ? 1062 ILE   B N     1 
ATOM   11748 C  CA    . ILE   B 1 1062 ? 112.980 178.939 116.570 1.00 73.52  ? 1062 ILE   B CA    1 
ATOM   11749 C  C     . ILE   B 1 1062 ? 111.663 178.277 116.969 1.00 72.26  ? 1062 ILE   B C     1 
ATOM   11750 O  O     . ILE   B 1 1062 ? 111.240 177.271 116.383 1.00 71.17  ? 1062 ILE   B O     1 
ATOM   11751 C  CB    . ILE   B 1 1062 ? 112.752 180.052 115.532 1.00 74.96  ? 1062 ILE   B CB    1 
ATOM   11752 C  CG1   . ILE   B 1 1062 ? 114.015 180.903 115.380 1.00 73.22  ? 1062 ILE   B CG1   1 
ATOM   11753 C  CG2   . ILE   B 1 1062 ? 111.569 180.924 115.924 1.00 72.67  ? 1062 ILE   B CG2   1 
ATOM   11754 C  CD1   . ILE   B 1 1062 ? 114.384 181.679 116.627 1.00 71.22  ? 1062 ILE   B CD1   1 
ATOM   11755 N  N     . ASN   B 1 1063 ? 111.009 178.849 117.977 1.00 76.69  ? 1063 ASN   B N     1 
ATOM   11756 C  CA    . ASN   B 1 1063 ? 109.767 178.377 118.583 1.00 79.65  ? 1063 ASN   B CA    1 
ATOM   11757 C  C     . ASN   B 1 1063 ? 110.016 177.257 119.588 1.00 79.91  ? 1063 ASN   B C     1 
ATOM   11758 O  O     . ASN   B 1 1063 ? 109.070 176.840 120.268 1.00 80.33  ? 1063 ASN   B O     1 
ATOM   11759 C  CB    . ASN   B 1 1063 ? 108.741 177.895 117.544 1.00 75.43  ? 1063 ASN   B CB    1 
ATOM   11760 N  N     . ARG   B 1 1064 ? 111.248 176.755 119.710 1.00 70.87  ? 1064 ARG   B N     1 
ATOM   11761 C  CA    . ARG   B 1 1064 ? 111.584 175.766 120.727 1.00 69.03  ? 1064 ARG   B CA    1 
ATOM   11762 C  C     . ARG   B 1 1064 ? 112.919 176.092 121.390 1.00 67.98  ? 1064 ARG   B C     1 
ATOM   11763 O  O     . ARG   B 1 1064 ? 113.681 175.185 121.742 1.00 66.54  ? 1064 ARG   B O     1 
ATOM   11764 C  CB    . ARG   B 1 1064 ? 111.612 174.355 120.137 1.00 65.94  ? 1064 ARG   B CB    1 
ATOM   11765 C  CG    . ARG   B 1 1064 ? 112.818 174.065 119.262 1.00 70.09  ? 1064 ARG   B CG    1 
ATOM   11766 C  CD    . ARG   B 1 1064 ? 112.710 172.701 118.597 1.00 68.69  ? 1064 ARG   B CD    1 
ATOM   11767 N  NE    . ARG   B 1 1064 ? 112.566 171.622 119.567 1.00 70.08  ? 1064 ARG   B NE    1 
ATOM   11768 C  CZ    . ARG   B 1 1064 ? 111.405 171.170 120.021 1.00 73.19  ? 1064 ARG   B CZ    1 
ATOM   11769 N  NH1   . ARG   B 1 1064 ? 110.256 171.681 119.610 1.00 71.39  ? 1064 ARG   B NH1   1 
ATOM   11770 N  NH2   . ARG   B 1 1064 ? 111.397 170.180 120.908 1.00 72.47  ? 1064 ARG   B NH2   1 
ATOM   11771 N  N     . ILE   B 1 1065 ? 113.212 177.380 121.570 1.00 63.04  ? 1065 ILE   B N     1 
ATOM   11772 C  CA    . ILE   B 1 1065 ? 114.488 177.784 122.155 1.00 61.13  ? 1065 ILE   B CA    1 
ATOM   11773 C  C     . ILE   B 1 1065 ? 114.584 177.317 123.602 1.00 63.72  ? 1065 ILE   B C     1 
ATOM   11774 O  O     . ILE   B 1 1065 ? 115.613 176.787 124.036 1.00 68.74  ? 1065 ILE   B O     1 
ATOM   11775 C  CB    . ILE   B 1 1065 ? 114.669 179.308 122.044 1.00 61.55  ? 1065 ILE   B CB    1 
ATOM   11776 C  CG1   . ILE   B 1 1065 ? 115.404 179.668 120.752 1.00 63.86  ? 1065 ILE   B CG1   1 
ATOM   11777 C  CG2   . ILE   B 1 1065 ? 115.413 179.845 123.256 1.00 60.59  ? 1065 ILE   B CG2   1 
ATOM   11778 C  CD1   . ILE   B 1 1065 ? 114.664 179.264 119.499 1.00 65.35  ? 1065 ILE   B CD1   1 
ATOM   11779 N  N     . ASP   B 1 1066 ? 113.512 177.514 124.372 1.00 60.51  ? 1066 ASP   B N     1 
ATOM   11780 C  CA    . ASP   B 1 1066 ? 113.566 177.225 125.802 1.00 62.02  ? 1066 ASP   B CA    1 
ATOM   11781 C  C     . ASP   B 1 1066 ? 113.746 175.736 126.071 1.00 58.52  ? 1066 ASP   B C     1 
ATOM   11782 O  O     . ASP   B 1 1066 ? 114.475 175.353 126.993 1.00 59.97  ? 1066 ASP   B O     1 
ATOM   11783 C  CB    . ASP   B 1 1066 ? 112.307 177.750 126.490 1.00 62.93  ? 1066 ASP   B CB    1 
ATOM   11784 C  CG    . ASP   B 1 1066 ? 112.055 179.214 126.198 1.00 66.32  ? 1066 ASP   B CG    1 
ATOM   11785 O  OD1   . ASP   B 1 1066 ? 112.865 180.055 126.642 1.00 67.37  ? 1066 ASP   B OD1   1 
ATOM   11786 O  OD2   . ASP   B 1 1066 ? 111.049 179.525 125.528 1.00 66.63  ? 1066 ASP   B OD2   1 
ATOM   11787 N  N     . HIS   B 1 1067 ? 113.085 174.880 125.291 1.00 51.55  ? 1067 HIS   B N     1 
ATOM   11788 C  CA    . HIS   B 1 1067 ? 113.237 173.443 125.497 1.00 52.90  ? 1067 HIS   B CA    1 
ATOM   11789 C  C     . HIS   B 1 1067 ? 114.680 173.005 125.275 1.00 60.80  ? 1067 HIS   B C     1 
ATOM   11790 O  O     . HIS   B 1 1067 ? 115.240 172.245 126.075 1.00 65.86  ? 1067 HIS   B O     1 
ATOM   11791 C  CB    . HIS   B 1 1067 ? 112.289 172.683 124.570 1.00 56.78  ? 1067 HIS   B CB    1 
ATOM   11792 C  CG    . HIS   B 1 1067 ? 112.642 171.239 124.394 1.00 59.80  ? 1067 HIS   B CG    1 
ATOM   11793 N  ND1   . HIS   B 1 1067 ? 113.585 170.808 123.486 1.00 60.43  ? 1067 HIS   B ND1   1 
ATOM   11794 C  CD2   . HIS   B 1 1067 ? 112.178 170.127 125.011 1.00 60.70  ? 1067 HIS   B CD2   1 
ATOM   11795 C  CE1   . HIS   B 1 1067 ? 113.685 169.493 123.551 1.00 60.81  ? 1067 HIS   B CE1   1 
ATOM   11796 N  NE2   . HIS   B 1 1067 ? 112.842 169.055 124.468 1.00 61.72  ? 1067 HIS   B NE2   1 
ATOM   11797 N  N     . ASP   B 1 1068 ? 115.304 173.489 124.200 1.00 55.73  ? 1068 ASP   B N     1 
ATOM   11798 C  CA    . ASP   B 1 1068 ? 116.692 173.129 123.931 1.00 48.71  ? 1068 ASP   B CA    1 
ATOM   11799 C  C     . ASP   B 1 1068 ? 117.628 173.718 124.978 1.00 47.75  ? 1068 ASP   B C     1 
ATOM   11800 O  O     . ASP   B 1 1068 ? 118.613 173.079 125.366 1.00 51.51  ? 1068 ASP   B O     1 
ATOM   11801 C  CB    . ASP   B 1 1068 ? 117.089 173.586 122.529 1.00 54.39  ? 1068 ASP   B CB    1 
ATOM   11802 C  CG    . ASP   B 1 1068 ? 116.773 172.550 121.469 1.00 60.35  ? 1068 ASP   B CG    1 
ATOM   11803 O  OD1   . ASP   B 1 1068 ? 116.446 171.402 121.837 1.00 58.14  ? 1068 ASP   B OD1   1 
ATOM   11804 O  OD2   . ASP   B 1 1068 ? 116.856 172.880 120.268 1.00 61.48  ? 1068 ASP   B OD2   1 
ATOM   11805 N  N     . ARG   B 1 1069 ? 117.345 174.937 125.444 1.00 45.60  ? 1069 ARG   B N     1 
ATOM   11806 C  CA    . ARG   B 1 1069 ? 118.166 175.520 126.499 1.00 43.97  ? 1069 ARG   B CA    1 
ATOM   11807 C  C     . ARG   B 1 1069 ? 118.081 174.696 127.776 1.00 44.86  ? 1069 ARG   B C     1 
ATOM   11808 O  O     . ARG   B 1 1069 ? 119.092 174.475 128.449 1.00 50.54  ? 1069 ARG   B O     1 
ATOM   11809 C  CB    . ARG   B 1 1069 ? 117.746 176.963 126.764 1.00 41.27  ? 1069 ARG   B CB    1 
ATOM   11810 C  CG    . ARG   B 1 1069 ? 118.663 177.690 127.731 1.00 44.63  ? 1069 ARG   B CG    1 
ATOM   11811 C  CD    . ARG   B 1 1069 ? 117.878 178.438 128.791 1.00 50.80  ? 1069 ARG   B CD    1 
ATOM   11812 N  NE    . ARG   B 1 1069 ? 116.978 179.423 128.204 1.00 57.22  ? 1069 ARG   B NE    1 
ATOM   11813 C  CZ    . ARG   B 1 1069 ? 117.378 180.496 127.537 1.00 58.98  ? 1069 ARG   B CZ    1 
ATOM   11814 N  NH1   . ARG   B 1 1069 ? 118.662 180.752 127.345 1.00 55.37  ? 1069 ARG   B NH1   1 
ATOM   11815 N  NH2   . ARG   B 1 1069 ? 116.467 181.333 127.048 1.00 55.92  ? 1069 ARG   B NH2   1 
ATOM   11816 N  N     . ARG   B 1 1070 ? 116.879 174.236 128.128 1.00 47.96  ? 1070 ARG   B N     1 
ATOM   11817 C  CA    . ARG   B 1 1070 ? 116.735 173.380 129.300 1.00 47.93  ? 1070 ARG   B CA    1 
ATOM   11818 C  C     . ARG   B 1 1070 ? 117.478 172.065 129.111 1.00 48.36  ? 1070 ARG   B C     1 
ATOM   11819 O  O     . ARG   B 1 1070 ? 118.114 171.563 130.044 1.00 51.54  ? 1070 ARG   B O     1 
ATOM   11820 C  CB    . ARG   B 1 1070 ? 115.258 173.122 129.595 1.00 50.05  ? 1070 ARG   B CB    1 
ATOM   11821 C  CG    . ARG   B 1 1070 ? 114.474 174.363 129.987 1.00 52.67  ? 1070 ARG   B CG    1 
ATOM   11822 C  CD    . ARG   B 1 1070 ? 113.150 174.003 130.646 1.00 48.03  ? 1070 ARG   B CD    1 
ATOM   11823 N  NE    . ARG   B 1 1070 ? 112.021 174.118 129.731 1.00 52.81  ? 1070 ARG   B NE    1 
ATOM   11824 C  CZ    . ARG   B 1 1070 ? 111.608 173.151 128.922 1.00 57.56  ? 1070 ARG   B CZ    1 
ATOM   11825 N  NH1   . ARG   B 1 1070 ? 112.207 171.972 128.893 1.00 58.52  ? 1070 ARG   B NH1   1 
ATOM   11826 N  NH2   . ARG   B 1 1070 ? 110.565 173.371 128.127 1.00 52.04  ? 1070 ARG   B NH2   1 
ATOM   11827 N  N     . ALA   B 1 1071 ? 117.401 171.485 127.913 1.00 36.35  ? 1071 ALA   B N     1 
ATOM   11828 C  CA    . ALA   B 1 1071 ? 118.130 170.247 127.657 1.00 38.40  ? 1071 ALA   B CA    1 
ATOM   11829 C  C     . ALA   B 1 1071 ? 119.631 170.449 127.823 1.00 42.58  ? 1071 ALA   B C     1 
ATOM   11830 O  O     . ALA   B 1 1071 ? 120.314 169.622 128.440 1.00 44.40  ? 1071 ALA   B O     1 
ATOM   11831 C  CB    . ALA   B 1 1071 ? 117.806 169.726 126.258 1.00 42.82  ? 1071 ALA   B CB    1 
ATOM   11832 N  N     . MET   B 1 1072 ? 120.162 171.546 127.281 1.00 41.80  ? 1072 MET   B N     1 
ATOM   11833 C  CA    . MET   B 1 1072 ? 121.591 171.821 127.407 1.00 34.09  ? 1072 MET   B CA    1 
ATOM   11834 C  C     . MET   B 1 1072 ? 121.983 172.084 128.855 1.00 39.50  ? 1072 MET   B C     1 
ATOM   11835 O  O     . MET   B 1 1072 ? 123.046 171.643 129.306 1.00 41.84  ? 1072 MET   B O     1 
ATOM   11836 C  CB    . MET   B 1 1072 ? 121.979 173.004 126.519 1.00 36.91  ? 1072 MET   B CB    1 
ATOM   11837 C  CG    . MET   B 1 1072 ? 123.481 173.213 126.361 1.00 39.75  ? 1072 MET   B CG    1 
ATOM   11838 S  SD    . MET   B 1 1072 ? 124.459 171.713 126.113 1.00 52.01  ? 1072 MET   B SD    1 
ATOM   11839 C  CE    . MET   B 1 1072 ? 123.324 170.675 125.195 1.00 43.29  ? 1072 MET   B CE    1 
ATOM   11840 N  N     . ALA   B 1 1073 ? 121.145 172.811 129.596 1.00 39.82  ? 1073 ALA   B N     1 
ATOM   11841 C  CA    . ALA   B 1 1073 ? 121.427 173.046 131.006 1.00 33.96  ? 1073 ALA   B CA    1 
ATOM   11842 C  C     . ALA   B 1 1073 ? 121.460 171.738 131.783 1.00 35.07  ? 1073 ALA   B C     1 
ATOM   11843 O  O     . ALA   B 1 1073 ? 122.347 171.523 132.616 1.00 40.02  ? 1073 ALA   B O     1 
ATOM   11844 C  CB    . ALA   B 1 1073 ? 120.389 173.999 131.597 1.00 33.45  ? 1073 ALA   B CB    1 
ATOM   11845 N  N     . THR   B 1 1074 ? 120.503 170.847 131.518 1.00 30.15  ? 1074 THR   B N     1 
ATOM   11846 C  CA    . THR   B 1 1074 ? 120.498 169.551 132.186 1.00 26.94  ? 1074 THR   B CA    1 
ATOM   11847 C  C     . THR   B 1 1074 ? 121.741 168.748 131.830 1.00 28.40  ? 1074 THR   B C     1 
ATOM   11848 O  O     . THR   B 1 1074 ? 122.362 168.128 132.702 1.00 37.35  ? 1074 THR   B O     1 
ATOM   11849 C  CB    . THR   B 1 1074 ? 119.233 168.775 131.818 1.00 32.71  ? 1074 THR   B CB    1 
ATOM   11850 O  OG1   . THR   B 1 1074 ? 118.132 169.262 132.593 1.00 39.01  ? 1074 THR   B OG1   1 
ATOM   11851 C  CG2   . THR   B 1 1074 ? 119.416 167.286 132.084 1.00 32.09  ? 1074 THR   B CG2   1 
ATOM   11852 N  N     . LEU   B 1 1075 ? 122.127 168.755 130.553 1.00 27.03  ? 1075 LEU   B N     1 
ATOM   11853 C  CA    . LEU   B 1 1075 ? 123.315 168.016 130.142 1.00 27.77  ? 1075 LEU   B CA    1 
ATOM   11854 C  C     . LEU   B 1 1075 ? 124.563 168.555 130.830 1.00 30.22  ? 1075 LEU   B C     1 
ATOM   11855 O  O     . LEU   B 1 1075 ? 125.404 167.782 131.301 1.00 28.46  ? 1075 LEU   B O     1 
ATOM   11856 C  CB    . LEU   B 1 1075 ? 123.471 168.077 128.623 1.00 24.44  ? 1075 LEU   B CB    1 
ATOM   11857 C  CG    . LEU   B 1 1075 ? 124.616 167.254 128.028 1.00 25.86  ? 1075 LEU   B CG    1 
ATOM   11858 C  CD1   . LEU   B 1 1075 ? 124.407 165.770 128.284 1.00 25.60  ? 1075 LEU   B CD1   1 
ATOM   11859 C  CD2   . LEU   B 1 1075 ? 124.761 167.530 126.543 1.00 29.46  ? 1075 LEU   B CD2   1 
ATOM   11860 N  N     . LEU   B 1 1076 ? 124.697 169.880 130.901 1.00 30.09  ? 1076 LEU   B N     1 
ATOM   11861 C  CA    . LEU   B 1 1076 ? 125.862 170.468 131.553 1.00 23.56  ? 1076 LEU   B CA    1 
ATOM   11862 C  C     . LEU   B 1 1076 ? 125.862 170.185 133.050 1.00 28.71  ? 1076 LEU   B C     1 
ATOM   11863 O  O     . LEU   B 1 1076 ? 126.924 169.964 133.644 1.00 39.15  ? 1076 LEU   B O     1 
ATOM   11864 C  CB    . LEU   B 1 1076 ? 125.908 171.972 131.287 1.00 31.45  ? 1076 LEU   B CB    1 
ATOM   11865 C  CG    . LEU   B 1 1076 ? 126.028 172.375 129.816 1.00 34.72  ? 1076 LEU   B CG    1 
ATOM   11866 C  CD1   . LEU   B 1 1076 ? 126.121 173.884 129.672 1.00 29.27  ? 1076 LEU   B CD1   1 
ATOM   11867 C  CD2   . LEU   B 1 1076 ? 127.233 171.700 129.187 1.00 26.59  ? 1076 LEU   B CD2   1 
ATOM   11868 N  N     . SER   B 1 1077 ? 124.685 170.185 133.678 1.00 27.50  ? 1077 SER   B N     1 
ATOM   11869 C  CA    . SER   B 1 1077 ? 124.613 169.884 135.103 1.00 21.30  ? 1077 SER   B CA    1 
ATOM   11870 C  C     . SER   B 1 1077 ? 124.978 168.431 135.378 1.00 22.75  ? 1077 SER   B C     1 
ATOM   11871 O  O     . SER   B 1 1077 ? 125.616 168.127 136.391 1.00 28.99  ? 1077 SER   B O     1 
ATOM   11872 C  CB    . SER   B 1 1077 ? 123.216 170.199 135.636 1.00 30.87  ? 1077 SER   B CB    1 
ATOM   11873 O  OG    . SER   B 1 1077 ? 122.366 169.070 135.536 1.00 39.13  ? 1077 SER   B OG    1 
ATOM   11874 N  N     . LYS   B 1 1078 ? 124.579 167.519 134.489 1.00 14.84  ? 1078 LYS   B N     1 
ATOM   11875 C  CA    . LYS   B 1 1078 ? 124.952 166.120 134.660 1.00 13.38  ? 1078 LYS   B CA    1 
ATOM   11876 C  C     . LYS   B 1 1078 ? 126.452 165.917 134.498 1.00 25.77  ? 1078 LYS   B C     1 
ATOM   11877 O  O     . LYS   B 1 1078 ? 127.030 165.035 135.142 1.00 31.96  ? 1078 LYS   B O     1 
ATOM   11878 C  CB    . LYS   B 1 1078 ? 124.181 165.246 133.673 1.00 21.76  ? 1078 LYS   B CB    1 
ATOM   11879 C  CG    . LYS   B 1 1078 ? 122.689 165.517 133.659 1.00 27.78  ? 1078 LYS   B CG    1 
ATOM   11880 C  CD    . LYS   B 1 1078 ? 121.896 164.272 134.001 1.00 26.31  ? 1078 LYS   B CD    1 
ATOM   11881 C  CE    . LYS   B 1 1078 ? 122.189 163.151 133.023 1.00 29.81  ? 1078 LYS   B CE    1 
ATOM   11882 N  NZ    . LYS   B 1 1078 ? 121.141 162.098 133.073 1.00 34.94  ? 1078 LYS   B NZ    1 
ATOM   11883 N  N     . PHE   B 1 1079 ? 127.098 166.716 133.648 1.00 28.12  ? 1079 PHE   B N     1 
ATOM   11884 C  CA    . PHE   B 1 1079 ? 128.546 166.666 133.506 1.00 18.52  ? 1079 PHE   B CA    1 
ATOM   11885 C  C     . PHE   B 1 1079 ? 129.272 167.421 134.610 1.00 19.69  ? 1079 PHE   B C     1 
ATOM   11886 O  O     . PHE   B 1 1079 ? 130.484 167.241 134.769 1.00 18.43  ? 1079 PHE   B O     1 
ATOM   11887 C  CB    . PHE   B 1 1079 ? 128.963 167.230 132.145 1.00 19.58  ? 1079 PHE   B CB    1 
ATOM   11888 C  CG    . PHE   B 1 1079 ? 128.707 166.300 130.995 1.00 23.42  ? 1079 PHE   B CG    1 
ATOM   11889 C  CD1   . PHE   B 1 1079 ? 128.863 164.933 131.143 1.00 19.43  ? 1079 PHE   B CD1   1 
ATOM   11890 C  CD2   . PHE   B 1 1079 ? 128.318 166.795 129.762 1.00 19.58  ? 1079 PHE   B CD2   1 
ATOM   11891 C  CE1   . PHE   B 1 1079 ? 128.631 164.077 130.085 1.00 17.20  ? 1079 PHE   B CE1   1 
ATOM   11892 C  CE2   . PHE   B 1 1079 ? 128.085 165.943 128.702 1.00 18.14  ? 1079 PHE   B CE2   1 
ATOM   11893 C  CZ    . PHE   B 1 1079 ? 128.242 164.583 128.863 1.00 20.13  ? 1079 PHE   B CZ    1 
ATOM   11894 N  N     . ARG   B 1 1080 ? 128.564 168.255 135.370 1.00 24.62  ? 1080 ARG   B N     1 
ATOM   11895 C  CA    . ARG   B 1 1080 ? 129.156 169.017 136.467 1.00 20.07  ? 1080 ARG   B CA    1 
ATOM   11896 C  C     . ARG   B 1 1080 ? 130.139 170.063 135.950 1.00 19.93  ? 1080 ARG   B C     1 
ATOM   11897 O  O     . ARG   B 1 1080 ? 131.201 170.285 136.533 1.00 29.38  ? 1080 ARG   B O     1 
ATOM   11898 C  CB    . ARG   B 1 1080 ? 129.839 168.094 137.478 1.00 21.22  ? 1080 ARG   B CB    1 
ATOM   11899 C  CG    . ARG   B 1 1080 ? 128.890 167.215 138.260 1.00 15.00  ? 1080 ARG   B CG    1 
ATOM   11900 C  CD    . ARG   B 1 1080 ? 128.973 165.791 137.760 1.00 13.92  ? 1080 ARG   B CD    1 
ATOM   11901 N  NE    . ARG   B 1 1080 ? 130.353 165.323 137.727 1.00 17.18  ? 1080 ARG   B NE    1 
ATOM   11902 C  CZ    . ARG   B 1 1080 ? 130.829 164.451 136.850 1.00 23.74  ? 1080 ARG   B CZ    1 
ATOM   11903 N  NH1   . ARG   B 1 1080 ? 130.060 163.922 135.913 1.00 17.42  ? 1080 ARG   B NH1   1 
ATOM   11904 N  NH2   . ARG   B 1 1080 ? 132.109 164.097 136.917 1.00 22.02  ? 1080 ARG   B NH2   1 
ATOM   11905 N  N     . ILE   B 1 1081 ? 129.786 170.711 134.846 1.00 15.89  ? 1081 ILE   B N     1 
ATOM   11906 C  CA    . ILE   B 1 1081 ? 130.578 171.800 134.288 1.00 23.56  ? 1081 ILE   B CA    1 
ATOM   11907 C  C     . ILE   B 1 1081 ? 129.796 173.085 134.511 1.00 27.00  ? 1081 ILE   B C     1 
ATOM   11908 O  O     . ILE   B 1 1081 ? 128.736 173.292 133.908 1.00 33.03  ? 1081 ILE   B O     1 
ATOM   11909 C  CB    . ILE   B 1 1081 ? 130.894 171.586 132.802 1.00 25.63  ? 1081 ILE   B CB    1 
ATOM   11910 C  CG1   . ILE   B 1 1081 ? 131.930 170.473 132.633 1.00 30.29  ? 1081 ILE   B CG1   1 
ATOM   11911 C  CG2   . ILE   B 1 1081 ? 131.397 172.875 132.173 1.00 25.34  ? 1081 ILE   B CG2   1 
ATOM   11912 C  CD1   . ILE   B 1 1081 ? 131.393 169.229 131.972 1.00 30.35  ? 1081 ILE   B CD1   1 
ATOM   11913 N  N     . ASP   B 1 1082 ? 130.314 173.946 135.381 1.00 33.85  ? 1082 ASP   B N     1 
ATOM   11914 C  CA    . ASP   B 1 1082 ? 129.623 175.183 135.713 1.00 33.48  ? 1082 ASP   B CA    1 
ATOM   11915 C  C     . ASP   B 1 1082 ? 129.590 176.110 134.506 1.00 37.27  ? 1082 ASP   B C     1 
ATOM   11916 O  O     . ASP   B 1 1082 ? 130.592 176.272 133.803 1.00 38.08  ? 1082 ASP   B O     1 
ATOM   11917 C  CB    . ASP   B 1 1082 ? 130.307 175.872 136.892 1.00 22.74  ? 1082 ASP   B CB    1 
ATOM   11918 N  N     . PHE   B 1 1083 ? 128.434 176.723 134.270 1.00 28.26  ? 1083 PHE   B N     1 
ATOM   11919 C  CA    . PHE   B 1 1083 ? 128.254 177.671 133.183 1.00 24.88  ? 1083 PHE   B CA    1 
ATOM   11920 C  C     . PHE   B 1 1083 ? 127.522 178.898 133.699 1.00 30.18  ? 1083 PHE   B C     1 
ATOM   11921 O  O     . PHE   B 1 1083 ? 126.563 178.782 134.468 1.00 36.90  ? 1083 PHE   B O     1 
ATOM   11922 C  CB    . PHE   B 1 1083 ? 127.478 177.043 132.021 1.00 26.52  ? 1083 PHE   B CB    1 
ATOM   11923 C  CG    . PHE   B 1 1083 ? 126.159 176.451 132.423 1.00 30.46  ? 1083 PHE   B CG    1 
ATOM   11924 C  CD1   . PHE   B 1 1083 ? 125.011 177.223 132.426 1.00 30.71  ? 1083 PHE   B CD1   1 
ATOM   11925 C  CD2   . PHE   B 1 1083 ? 126.066 175.121 132.797 1.00 32.93  ? 1083 PHE   B CD2   1 
ATOM   11926 C  CE1   . PHE   B 1 1083 ? 123.798 176.681 132.795 1.00 33.89  ? 1083 PHE   B CE1   1 
ATOM   11927 C  CE2   . PHE   B 1 1083 ? 124.854 174.574 133.166 1.00 29.86  ? 1083 PHE   B CE2   1 
ATOM   11928 C  CZ    . PHE   B 1 1083 ? 123.719 175.355 133.165 1.00 29.96  ? 1083 PHE   B CZ    1 
ATOM   11929 N  N     . SER   B 1 1084 ? 127.982 180.077 133.279 1.00 36.30  ? 1084 SER   B N     1 
ATOM   11930 C  CA    . SER   B 1 1084 ? 127.318 181.310 133.682 1.00 33.51  ? 1084 SER   B CA    1 
ATOM   11931 C  C     . SER   B 1 1084 ? 126.036 181.549 132.897 1.00 38.05  ? 1084 SER   B C     1 
ATOM   11932 O  O     . SER   B 1 1084 ? 125.078 182.107 133.442 1.00 41.86  ? 1084 SER   B O     1 
ATOM   11933 C  CB    . SER   B 1 1084 ? 128.264 182.499 133.515 1.00 39.55  ? 1084 SER   B CB    1 
ATOM   11934 O  OG    . SER   B 1 1084 ? 128.880 182.488 132.240 1.00 45.55  ? 1084 SER   B OG    1 
ATOM   11935 N  N     . ASP   B 1 1085 ? 125.996 181.142 131.631 1.00 34.46  ? 1085 ASP   B N     1 
ATOM   11936 C  CA    . ASP   B 1 1085 ? 124.809 181.339 130.814 1.00 31.58  ? 1085 ASP   B CA    1 
ATOM   11937 C  C     . ASP   B 1 1085 ? 124.842 180.375 129.638 1.00 29.23  ? 1085 ASP   B C     1 
ATOM   11938 O  O     . ASP   B 1 1085 ? 125.899 179.872 129.248 1.00 36.13  ? 1085 ASP   B O     1 
ATOM   11939 C  CB    . ASP   B 1 1085 ? 124.703 182.787 130.321 1.00 29.77  ? 1085 ASP   B CB    1 
ATOM   11940 N  N     . ILE   B 1 1086 ? 123.659 180.128 129.081 1.00 31.40  ? 1086 ILE   B N     1 
ATOM   11941 C  CA    . ILE   B 1 1086 ? 123.490 179.311 127.886 1.00 31.89  ? 1086 ILE   B CA    1 
ATOM   11942 C  C     . ILE   B 1 1086 ? 122.690 180.122 126.878 1.00 34.96  ? 1086 ILE   B C     1 
ATOM   11943 O  O     . ILE   B 1 1086 ? 121.632 180.665 127.214 1.00 37.62  ? 1086 ILE   B O     1 
ATOM   11944 C  CB    . ILE   B 1 1086 ? 122.779 177.980 128.194 1.00 26.73  ? 1086 ILE   B CB    1 
ATOM   11945 C  CG1   . ILE   B 1 1086 ? 123.744 177.000 128.860 1.00 36.10  ? 1086 ILE   B CG1   1 
ATOM   11946 C  CG2   . ILE   B 1 1086 ? 122.207 177.378 126.925 1.00 23.37  ? 1086 ILE   B CG2   1 
ATOM   11947 C  CD1   . ILE   B 1 1086 ? 123.195 175.599 128.991 1.00 35.95  ? 1086 ILE   B CD1   1 
ATOM   11948 N  N     . MET   B 1 1087 ? 123.193 180.210 125.650 1.00 41.31  ? 1087 MET   B N     1 
ATOM   11949 C  CA    . MET   B 1 1087 ? 122.540 180.967 124.591 1.00 41.04  ? 1087 MET   B CA    1 
ATOM   11950 C  C     . MET   B 1 1087 ? 122.226 180.034 123.432 1.00 46.42  ? 1087 MET   B C     1 
ATOM   11951 O  O     . MET   B 1 1087 ? 123.127 179.384 122.891 1.00 47.24  ? 1087 MET   B O     1 
ATOM   11952 C  CB    . MET   B 1 1087 ? 123.417 182.129 124.123 1.00 40.14  ? 1087 MET   B CB    1 
ATOM   11953 C  CG    . MET   B 1 1087 ? 122.652 183.224 123.400 1.00 45.75  ? 1087 MET   B CG    1 
ATOM   11954 S  SD    . MET   B 1 1087 ? 123.703 184.237 122.342 1.00 69.80  ? 1087 MET   B SD    1 
ATOM   11955 C  CE    . MET   B 1 1087 ? 123.746 185.769 123.267 1.00 48.14  ? 1087 MET   B CE    1 
ATOM   11956 N  N     . VAL   B 1 1088 ? 120.955 179.987 123.043 1.00 42.96  ? 1088 VAL   B N     1 
ATOM   11957 C  CA    . VAL   B 1 1088 ? 120.499 179.196 121.907 1.00 44.30  ? 1088 VAL   B CA    1 
ATOM   11958 C  C     . VAL   B 1 1088 ? 120.294 180.136 120.731 1.00 47.61  ? 1088 VAL   B C     1 
ATOM   11959 O  O     . VAL   B 1 1088 ? 119.597 181.152 120.852 1.00 52.21  ? 1088 VAL   B O     1 
ATOM   11960 C  CB    . VAL   B 1 1088 ? 119.206 178.433 122.241 1.00 44.32  ? 1088 VAL   B CB    1 
ATOM   11961 C  CG1   . VAL   B 1 1088 ? 118.669 177.734 121.006 1.00 45.33  ? 1088 VAL   B CG1   1 
ATOM   11962 C  CG2   . VAL   B 1 1088 ? 119.457 177.437 123.356 1.00 43.72  ? 1088 VAL   B CG2   1 
ATOM   11963 N  N     . LEU   B 1 1089 ? 120.899 179.803 119.595 1.00 48.02  ? 1089 LEU   B N     1 
ATOM   11964 C  CA    . LEU   B 1 1089 ? 120.920 180.671 118.428 1.00 46.56  ? 1089 LEU   B CA    1 
ATOM   11965 C  C     . LEU   B 1 1089 ? 120.153 180.017 117.290 1.00 52.83  ? 1089 LEU   B C     1 
ATOM   11966 O  O     . LEU   B 1 1089 ? 120.445 178.878 116.911 1.00 52.48  ? 1089 LEU   B O     1 
ATOM   11967 C  CB    . LEU   B 1 1089 ? 122.358 180.966 117.994 1.00 47.00  ? 1089 LEU   B CB    1 
ATOM   11968 C  CG    . LEU   B 1 1089 ? 123.159 181.900 118.901 1.00 51.67  ? 1089 LEU   B CG    1 
ATOM   11969 C  CD1   . LEU   B 1 1089 ? 124.394 182.417 118.185 1.00 46.92  ? 1089 LEU   B CD1   1 
ATOM   11970 C  CD2   . LEU   B 1 1089 ? 122.292 183.055 119.372 1.00 51.10  ? 1089 LEU   B CD2   1 
ATOM   11971 N  N     . GLY   B 1 1090 ? 119.172 180.738 116.754 1.00 56.11  ? 1090 GLY   B N     1 
ATOM   11972 C  CA    . GLY   B 1 1090 ? 118.442 180.328 115.577 1.00 51.97  ? 1090 GLY   B CA    1 
ATOM   11973 C  C     . GLY   B 1 1090 ? 118.891 180.990 114.296 1.00 56.73  ? 1090 GLY   B C     1 
ATOM   11974 O  O     . GLY   B 1 1090 ? 118.289 180.749 113.245 1.00 58.58  ? 1090 GLY   B O     1 
ATOM   11975 N  N     . ASP   B 1 1091 ? 119.934 181.813 114.346 1.00 52.41  ? 1091 ASP   B N     1 
ATOM   11976 C  CA    . ASP   B 1 1091 ? 120.402 182.555 113.184 1.00 52.68  ? 1091 ASP   B CA    1 
ATOM   11977 C  C     . ASP   B 1 1091 ? 121.407 181.778 112.345 1.00 56.11  ? 1091 ASP   B C     1 
ATOM   11978 O  O     . ASP   B 1 1091 ? 121.885 182.304 111.335 1.00 55.96  ? 1091 ASP   B O     1 
ATOM   11979 C  CB    . ASP   B 1 1091 ? 121.019 183.885 113.628 1.00 53.19  ? 1091 ASP   B CB    1 
ATOM   11980 N  N     . ILE   B 1 1092 ? 121.743 180.550 112.733 1.00 53.58  ? 1092 ILE   B N     1 
ATOM   11981 C  CA    . ILE   B 1 1092 ? 122.588 179.694 111.909 1.00 54.47  ? 1092 ILE   B CA    1 
ATOM   11982 C  C     . ILE   B 1 1092 ? 121.752 179.183 110.744 1.00 57.54  ? 1092 ILE   B C     1 
ATOM   11983 O  O     . ILE   B 1 1092 ? 120.520 179.274 110.765 1.00 55.17  ? 1092 ILE   B O     1 
ATOM   11984 C  CB    . ILE   B 1 1092 ? 123.187 178.532 112.722 1.00 53.58  ? 1092 ILE   B CB    1 
ATOM   11985 C  CG1   . ILE   B 1 1092 ? 123.722 179.036 114.063 1.00 54.63  ? 1092 ILE   B CG1   1 
ATOM   11986 C  CG2   . ILE   B 1 1092 ? 124.294 177.844 111.941 1.00 52.20  ? 1092 ILE   B CG2   1 
ATOM   11987 C  CD1   . ILE   B 1 1092 ? 124.010 177.931 115.059 1.00 53.01  ? 1092 ILE   B CD1   1 
ATOM   11988 N  N     . ASN   B 1 1093 ? 122.412 178.638 109.723 1.00 54.20  ? 1093 ASN   B N     1 
ATOM   11989 C  CA    . ASN   B 1 1093 ? 121.731 178.161 108.520 1.00 49.08  ? 1093 ASN   B CA    1 
ATOM   11990 C  C     . ASN   B 1 1093 ? 120.892 179.267 107.885 1.00 49.37  ? 1093 ASN   B C     1 
ATOM   11991 O  O     . ASN   B 1 1093 ? 119.784 179.034 107.401 1.00 59.37  ? 1093 ASN   B O     1 
ATOM   11992 C  CB    . ASN   B 1 1093 ? 120.870 176.932 108.816 1.00 46.96  ? 1093 ASN   B CB    1 
ATOM   11993 C  CG    . ASN   B 1 1093 ? 121.542 175.965 109.770 1.00 52.47  ? 1093 ASN   B CG    1 
ATOM   11994 O  OD1   . ASN   B 1 1093 ? 122.040 176.357 110.824 1.00 56.78  ? 1093 ASN   B OD1   1 
ATOM   11995 N  ND2   . ASN   B 1 1093 ? 121.557 174.689 109.403 1.00 51.22  ? 1093 ASN   B ND2   1 
ATOM   11996 N  N     . THR   B 1 1094 ? 121.428 180.484 107.886 1.00 45.96  ? 1094 THR   B N     1 
ATOM   11997 C  CA    . THR   B 1 1094 ? 120.807 181.623 107.229 1.00 47.38  ? 1094 THR   B CA    1 
ATOM   11998 C  C     . THR   B 1 1094 ? 121.858 182.334 106.393 1.00 50.79  ? 1094 THR   B C     1 
ATOM   11999 O  O     . THR   B 1 1094 ? 123.027 182.406 106.785 1.00 53.10  ? 1094 THR   B O     1 
ATOM   12000 C  CB    . THR   B 1 1094 ? 120.187 182.594 108.242 1.00 42.86  ? 1094 THR   B CB    1 
ATOM   12001 O  OG1   . THR   B 1 1094 ? 121.180 183.527 108.685 1.00 48.31  ? 1094 THR   B OG1   1 
ATOM   12002 C  CG2   . THR   B 1 1094 ? 119.643 181.836 109.437 1.00 46.70  ? 1094 THR   B CG2   1 
ATOM   12003 N  N     . LYS   B 1 1095 ? 121.445 182.848 105.242 1.00 44.30  ? 1095 LYS   B N     1 
ATOM   12004 C  CA    . LYS   B 1 1095 ? 122.395 183.470 104.333 1.00 43.74  ? 1095 LYS   B CA    1 
ATOM   12005 C  C     . LYS   B 1 1095 ? 123.087 184.639 105.026 1.00 44.35  ? 1095 LYS   B C     1 
ATOM   12006 O  O     . LYS   B 1 1095 ? 122.411 185.499 105.606 1.00 43.12  ? 1095 LYS   B O     1 
ATOM   12007 C  CB    . LYS   B 1 1095 ? 121.697 183.952 103.064 1.00 45.34  ? 1095 LYS   B CB    1 
ATOM   12008 C  CG    . LYS   B 1 1095 ? 122.619 184.687 102.103 1.00 46.76  ? 1095 LYS   B CG    1 
ATOM   12009 C  CD    . LYS   B 1 1095 ? 121.836 185.472 101.066 1.00 47.84  ? 1095 LYS   B CD    1 
ATOM   12010 C  CE    . LYS   B 1 1095 ? 121.099 184.541 100.121 1.00 49.60  ? 1095 LYS   B CE    1 
ATOM   12011 N  NZ    . LYS   B 1 1095 ? 121.838 183.266 99.916  1.00 52.90  ? 1095 LYS   B NZ    1 
ATOM   12012 N  N     . PRO   B 1 1096 ? 124.416 184.706 104.998 1.00 46.80  ? 1096 PRO   B N     1 
ATOM   12013 C  CA    . PRO   B 1 1096 ? 125.105 185.865 105.577 1.00 43.31  ? 1096 PRO   B CA    1 
ATOM   12014 C  C     . PRO   B 1 1096 ? 124.927 187.112 104.727 1.00 47.03  ? 1096 PRO   B C     1 
ATOM   12015 O  O     . PRO   B 1 1096 ? 124.211 187.091 103.722 1.00 48.47  ? 1096 PRO   B O     1 
ATOM   12016 C  CB    . PRO   B 1 1096 ? 126.570 185.416 105.622 1.00 39.47  ? 1096 PRO   B CB    1 
ATOM   12017 C  CG    . PRO   B 1 1096 ? 126.680 184.400 104.541 1.00 38.75  ? 1096 PRO   B CG    1 
ATOM   12018 C  CD    . PRO   B 1 1096 ? 125.357 183.693 104.492 1.00 41.32  ? 1096 PRO   B CD    1 
ATOM   12019 N  N     . LYS   B 1 1097 ? 125.576 188.202 105.123 1.00 43.87  ? 1097 LYS   B N     1 
ATOM   12020 C  CA    . LYS   B 1 1097 ? 125.470 189.443 104.372 1.00 45.74  ? 1097 LYS   B CA    1 
ATOM   12021 C  C     . LYS   B 1 1097 ? 126.093 189.288 102.990 1.00 51.17  ? 1097 LYS   B C     1 
ATOM   12022 O  O     . LYS   B 1 1097 ? 126.978 188.457 102.770 1.00 54.02  ? 1097 LYS   B O     1 
ATOM   12023 C  CB    . LYS   B 1 1097 ? 126.153 190.581 105.128 1.00 46.69  ? 1097 LYS   B CB    1 
ATOM   12024 C  CG    . LYS   B 1 1097 ? 125.582 190.833 106.509 1.00 48.19  ? 1097 LYS   B CG    1 
ATOM   12025 C  CD    . LYS   B 1 1097 ? 124.454 191.846 106.462 1.00 50.11  ? 1097 LYS   B CD    1 
ATOM   12026 C  CE    . LYS   B 1 1097 ? 123.882 192.089 107.846 1.00 49.94  ? 1097 LYS   B CE    1 
ATOM   12027 N  NZ    . LYS   B 1 1097 ? 124.854 191.718 108.911 1.00 50.99  ? 1097 LYS   B NZ    1 
ATOM   12028 N  N     . LYS   B 1 1098 ? 125.615 190.104 102.048 1.00 54.81  ? 1098 LYS   B N     1 
ATOM   12029 C  CA    . LYS   B 1 1098 ? 126.186 190.088 100.705 1.00 51.81  ? 1098 LYS   B CA    1 
ATOM   12030 C  C     . LYS   B 1 1098 ? 127.653 190.494 100.731 1.00 54.59  ? 1098 LYS   B C     1 
ATOM   12031 O  O     . LYS   B 1 1098 ? 128.480 189.912 100.019 1.00 55.86  ? 1098 LYS   B O     1 
ATOM   12032 C  CB    . LYS   B 1 1098 ? 125.388 191.011 99.784  1.00 46.96  ? 1098 LYS   B CB    1 
ATOM   12033 N  N     . GLU   B 1 1099 ? 127.993 191.495 101.545 1.00 54.58  ? 1099 GLU   B N     1 
ATOM   12034 C  CA    . GLU   B 1 1099 ? 129.373 191.961 101.610 1.00 52.17  ? 1099 GLU   B CA    1 
ATOM   12035 C  C     . GLU   B 1 1099 ? 130.316 190.848 102.048 1.00 50.01  ? 1099 GLU   B C     1 
ATOM   12036 O  O     . GLU   B 1 1099 ? 131.415 190.706 101.502 1.00 53.30  ? 1099 GLU   B O     1 
ATOM   12037 C  CB    . GLU   B 1 1099 ? 129.478 193.156 102.558 1.00 47.96  ? 1099 GLU   B CB    1 
ATOM   12038 N  N     . ASN   B 1 1100 ? 129.908 190.050 103.036 1.00 49.30  ? 1100 ASN   B N     1 
ATOM   12039 C  CA    . ASN   B 1 1100 ? 130.775 188.979 103.518 1.00 50.77  ? 1100 ASN   B CA    1 
ATOM   12040 C  C     . ASN   B 1 1100 ? 130.964 187.898 102.461 1.00 51.49  ? 1100 ASN   B C     1 
ATOM   12041 O  O     . ASN   B 1 1100 ? 132.073 187.377 102.288 1.00 56.53  ? 1100 ASN   B O     1 
ATOM   12042 C  CB    . ASN   B 1 1100 ? 130.205 188.389 104.806 1.00 47.80  ? 1100 ASN   B CB    1 
ATOM   12043 C  CG    . ASN   B 1 1100 ? 130.350 189.327 105.988 1.00 50.34  ? 1100 ASN   B CG    1 
ATOM   12044 O  OD1   . ASN   B 1 1100 ? 131.439 189.830 106.266 1.00 54.54  ? 1100 ASN   B OD1   1 
ATOM   12045 N  ND2   . ASN   B 1 1100 ? 129.249 189.579 106.683 1.00 52.12  ? 1100 ASN   B ND2   1 
ATOM   12046 N  N     . ILE   B 1 1101 ? 129.897 187.548 101.740 1.00 44.41  ? 1101 ILE   B N     1 
ATOM   12047 C  CA    . ILE   B 1 1101 ? 130.020 186.563 100.670 1.00 47.27  ? 1101 ILE   B CA    1 
ATOM   12048 C  C     . ILE   B 1 1101 ? 130.943 187.084 99.576  1.00 51.29  ? 1101 ILE   B C     1 
ATOM   12049 O  O     . ILE   B 1 1101 ? 131.770 186.343 99.029  1.00 54.79  ? 1101 ILE   B O     1 
ATOM   12050 C  CB    . ILE   B 1 1101 ? 128.631 186.200 100.116 1.00 45.37  ? 1101 ILE   B CB    1 
ATOM   12051 C  CG1   . ILE   B 1 1101 ? 127.731 185.673 101.236 1.00 45.73  ? 1101 ILE   B CG1   1 
ATOM   12052 C  CG2   . ILE   B 1 1101 ? 128.756 185.169 99.010  1.00 45.18  ? 1101 ILE   B CG2   1 
ATOM   12053 C  CD1   . ILE   B 1 1101 ? 126.330 185.329 100.784 1.00 49.07  ? 1101 ILE   B CD1   1 
ATOM   12054 N  N     . ILE   B 1 1102 ? 130.817 188.370 99.240  1.00 53.15  ? 1102 ILE   B N     1 
ATOM   12055 C  CA    . ILE   B 1 1102 ? 131.678 188.960 98.220  1.00 51.90  ? 1102 ILE   B CA    1 
ATOM   12056 C  C     . ILE   B 1 1102 ? 133.131 188.949 98.676  1.00 53.71  ? 1102 ILE   B C     1 
ATOM   12057 O  O     . ILE   B 1 1102 ? 134.042 188.681 97.885  1.00 53.51  ? 1102 ILE   B O     1 
ATOM   12058 C  CB    . ILE   B 1 1102 ? 131.203 190.384 97.876  1.00 54.28  ? 1102 ILE   B CB    1 
ATOM   12059 C  CG1   . ILE   B 1 1102 ? 129.765 190.356 97.357  1.00 54.28  ? 1102 ILE   B CG1   1 
ATOM   12060 C  CG2   . ILE   B 1 1102 ? 132.130 191.019 96.853  1.00 53.45  ? 1102 ILE   B CG2   1 
ATOM   12061 C  CD1   . ILE   B 1 1102 ? 129.408 189.091 96.610  1.00 51.78  ? 1102 ILE   B CD1   1 
ATOM   12062 N  N     . ALA   B 1 1103 ? 133.373 189.262 99.950  1.00 50.29  ? 1103 ALA   B N     1 
ATOM   12063 C  CA    . ALA   B 1 1103 ? 134.736 189.227 100.471 1.00 48.75  ? 1103 ALA   B CA    1 
ATOM   12064 C  C     . ALA   B 1 1103 ? 135.310 187.818 100.418 1.00 49.22  ? 1103 ALA   B C     1 
ATOM   12065 O  O     . ALA   B 1 1103 ? 136.479 187.628 100.059 1.00 56.71  ? 1103 ALA   B O     1 
ATOM   12066 C  CB    . ALA   B 1 1103 ? 134.770 189.769 101.899 1.00 46.27  ? 1103 ALA   B CB    1 
ATOM   12067 N  N     . PHE   B 1 1104 ? 134.508 186.815 100.781 1.00 40.28  ? 1104 PHE   B N     1 
ATOM   12068 C  CA    . PHE   B 1 1104 ? 134.987 185.439 100.699 1.00 38.78  ? 1104 PHE   B CA    1 
ATOM   12069 C  C     . PHE   B 1 1104 ? 135.325 185.066 99.262  1.00 45.84  ? 1104 PHE   B C     1 
ATOM   12070 O  O     . PHE   B 1 1104 ? 136.356 184.434 99.003  1.00 49.72  ? 1104 PHE   B O     1 
ATOM   12071 C  CB    . PHE   B 1 1104 ? 133.946 184.479 101.276 1.00 41.09  ? 1104 PHE   B CB    1 
ATOM   12072 C  CG    . PHE   B 1 1104 ? 134.327 183.027 101.164 1.00 39.26  ? 1104 PHE   B CG    1 
ATOM   12073 C  CD1   . PHE   B 1 1104 ? 134.075 182.312 100.006 1.00 39.60  ? 1104 PHE   B CD1   1 
ATOM   12074 C  CD2   . PHE   B 1 1104 ? 134.943 182.379 102.219 1.00 39.81  ? 1104 PHE   B CD2   1 
ATOM   12075 C  CE1   . PHE   B 1 1104 ? 134.426 180.979 99.908  1.00 40.13  ? 1104 PHE   B CE1   1 
ATOM   12076 C  CE2   . PHE   B 1 1104 ? 135.294 181.046 102.125 1.00 34.52  ? 1104 PHE   B CE2   1 
ATOM   12077 C  CZ    . PHE   B 1 1104 ? 135.037 180.347 100.969 1.00 27.61  ? 1104 PHE   B CZ    1 
ATOM   12078 N  N     . GLU   B 1 1105 ? 134.466 185.446 98.314  1.00 46.38  ? 1105 GLU   B N     1 
ATOM   12079 C  CA    . GLU   B 1 1105 ? 134.742 185.145 96.913  1.00 45.36  ? 1105 GLU   B CA    1 
ATOM   12080 C  C     . GLU   B 1 1105 ? 136.013 185.840 96.440  1.00 50.43  ? 1105 GLU   B C     1 
ATOM   12081 O  O     . GLU   B 1 1105 ? 136.829 185.245 95.727  1.00 50.95  ? 1105 GLU   B O     1 
ATOM   12082 C  CB    . GLU   B 1 1105 ? 133.552 185.549 96.045  1.00 43.42  ? 1105 GLU   B CB    1 
ATOM   12083 N  N     . GLU   B 1 1106 ? 136.199 187.103 96.826  1.00 51.58  ? 1106 GLU   B N     1 
ATOM   12084 C  CA    . GLU   B 1 1106 ? 137.405 187.824 96.436  1.00 50.04  ? 1106 GLU   B CA    1 
ATOM   12085 C  C     . GLU   B 1 1106 ? 138.649 187.156 97.003  1.00 51.31  ? 1106 GLU   B C     1 
ATOM   12086 O  O     . GLU   B 1 1106 ? 139.666 187.028 96.311  1.00 53.60  ? 1106 GLU   B O     1 
ATOM   12087 C  CB    . GLU   B 1 1106 ? 137.319 189.279 96.896  1.00 50.17  ? 1106 GLU   B CB    1 
ATOM   12088 N  N     . ILE   B 1 1107 ? 138.589 186.726 98.264  1.00 46.54  ? 1107 ILE   B N     1 
ATOM   12089 C  CA    . ILE   B 1 1107 ? 139.728 186.047 98.873  1.00 47.26  ? 1107 ILE   B CA    1 
ATOM   12090 C  C     . ILE   B 1 1107 ? 140.020 184.741 98.145  1.00 47.34  ? 1107 ILE   B C     1 
ATOM   12091 O  O     . ILE   B 1 1107 ? 141.180 184.401 97.886  1.00 50.32  ? 1107 ILE   B O     1 
ATOM   12092 C  CB    . ILE   B 1 1107 ? 139.474 185.814 100.374 1.00 46.70  ? 1107 ILE   B CB    1 
ATOM   12093 C  CG1   . ILE   B 1 1107 ? 139.957 187.011 101.196 1.00 47.98  ? 1107 ILE   B CG1   1 
ATOM   12094 C  CG2   . ILE   B 1 1107 ? 140.156 184.537 100.839 1.00 47.38  ? 1107 ILE   B CG2   1 
ATOM   12095 C  CD1   . ILE   B 1 1107 ? 139.513 188.348 100.650 1.00 48.55  ? 1107 ILE   B CD1   1 
ATOM   12096 N  N     . ILE   B 1 1108 ? 138.971 183.987 97.805  1.00 46.83  ? 1108 ILE   B N     1 
ATOM   12097 C  CA    . ILE   B 1 1108 ? 139.144 182.666 97.202  1.00 47.83  ? 1108 ILE   B CA    1 
ATOM   12098 C  C     . ILE   B 1 1108 ? 139.419 182.711 95.709  1.00 55.59  ? 1108 ILE   B C     1 
ATOM   12099 O  O     . ILE   B 1 1108 ? 139.732 181.670 95.117  1.00 59.00  ? 1108 ILE   B O     1 
ATOM   12100 C  CB    . ILE   B 1 1108 ? 137.892 181.803 97.452  1.00 50.15  ? 1108 ILE   B CB    1 
ATOM   12101 C  CG1   . ILE   B 1 1108 ? 138.179 180.334 97.152  1.00 48.64  ? 1108 ILE   B CG1   1 
ATOM   12102 C  CG2   . ILE   B 1 1108 ? 136.732 182.291 96.598  1.00 49.75  ? 1108 ILE   B CG2   1 
ATOM   12103 C  CD1   . ILE   B 1 1108 ? 136.938 179.474 97.110  1.00 49.12  ? 1108 ILE   B CD1   1 
ATOM   12104 N  N     . GLU   B 1 1109 ? 139.308 183.881 95.081  1.00 58.86  ? 1109 GLU   B N     1 
ATOM   12105 C  CA    . GLU   B 1 1109 ? 139.430 183.970 93.627  1.00 54.65  ? 1109 GLU   B CA    1 
ATOM   12106 C  C     . GLU   B 1 1109 ? 140.697 183.339 93.066  1.00 56.48  ? 1109 GLU   B C     1 
ATOM   12107 O  O     . GLU   B 1 1109 ? 140.588 182.505 92.153  1.00 55.17  ? 1109 GLU   B O     1 
ATOM   12108 C  CB    . GLU   B 1 1109 ? 139.336 185.444 93.210  1.00 52.20  ? 1109 GLU   B CB    1 
ATOM   12109 N  N     . PRO   B 1 1110 ? 141.902 183.668 93.539  1.00 53.37  ? 1110 PRO   B N     1 
ATOM   12110 C  CA    . PRO   B 1 1110 ? 143.103 183.146 92.872  1.00 49.89  ? 1110 PRO   B CA    1 
ATOM   12111 C  C     . PRO   B 1 1110 ? 143.432 181.715 93.265  1.00 51.06  ? 1110 PRO   B C     1 
ATOM   12112 O  O     . PRO   B 1 1110 ? 144.601 181.381 93.481  1.00 58.48  ? 1110 PRO   B O     1 
ATOM   12113 C  CB    . PRO   B 1 1110 ? 144.210 184.110 93.328  1.00 51.23  ? 1110 PRO   B CB    1 
ATOM   12114 C  CG    . PRO   B 1 1110 ? 143.520 185.206 94.109  1.00 50.74  ? 1110 PRO   B CG    1 
ATOM   12115 C  CD    . PRO   B 1 1110 ? 142.235 184.632 94.596  1.00 49.98  ? 1110 PRO   B CD    1 
ATOM   12116 N  N     . TYR   B 1 1111 ? 142.412 180.861 93.352  1.00 49.99  ? 1111 TYR   B N     1 
ATOM   12117 C  CA    . TYR   B 1 1111 ? 142.613 179.433 93.553  1.00 51.78  ? 1111 TYR   B CA    1 
ATOM   12118 C  C     . TYR   B 1 1111 ? 141.590 178.576 92.821  1.00 54.92  ? 1111 TYR   B C     1 
ATOM   12119 O  O     . TYR   B 1 1111 ? 141.605 177.353 92.989  1.00 53.10  ? 1111 TYR   B O     1 
ATOM   12120 C  CB    . TYR   B 1 1111 ? 142.597 179.089 95.053  1.00 51.64  ? 1111 TYR   B CB    1 
ATOM   12121 C  CG    . TYR   B 1 1111 ? 143.546 179.932 95.876  1.00 54.54  ? 1111 TYR   B CG    1 
ATOM   12122 C  CD1   . TYR   B 1 1111 ? 144.911 179.677 95.871  1.00 53.72  ? 1111 TYR   B CD1   1 
ATOM   12123 C  CD2   . TYR   B 1 1111 ? 143.080 180.985 96.650  1.00 56.51  ? 1111 TYR   B CD2   1 
ATOM   12124 C  CE1   . TYR   B 1 1111 ? 145.783 180.445 96.614  1.00 52.06  ? 1111 TYR   B CE1   1 
ATOM   12125 C  CE2   . TYR   B 1 1111 ? 143.946 181.758 97.397  1.00 53.36  ? 1111 TYR   B CE2   1 
ATOM   12126 C  CZ    . TYR   B 1 1111 ? 145.295 181.483 97.376  1.00 52.21  ? 1111 TYR   B CZ    1 
ATOM   12127 O  OH    . TYR   B 1 1111 ? 146.158 182.252 98.120  1.00 55.19  ? 1111 TYR   B OH    1 
ATOM   12128 N  N     . ARG   B 1 1112 ? 140.710 179.171 92.020  1.00 63.06  ? 1112 ARG   B N     1 
ATOM   12129 C  CA    . ARG   B 1 1112 ? 139.614 178.441 91.404  1.00 61.71  ? 1112 ARG   B CA    1 
ATOM   12130 C  C     . ARG   B 1 1112 ? 140.062 177.753 90.122  1.00 65.93  ? 1112 ARG   B C     1 
ATOM   12131 O  O     . ARG   B 1 1112 ? 140.839 178.305 89.338  1.00 67.45  ? 1112 ARG   B O     1 
ATOM   12132 C  CB    . ARG   B 1 1112 ? 138.450 179.386 91.110  1.00 64.54  ? 1112 ARG   B CB    1 
ATOM   12133 C  CG    . ARG   B 1 1112 ? 138.112 180.315 92.264  1.00 65.10  ? 1112 ARG   B CG    1 
ATOM   12134 C  CD    . ARG   B 1 1112 ? 136.641 180.689 92.266  1.00 66.81  ? 1112 ARG   B CD    1 
ATOM   12135 N  NE    . ARG   B 1 1112 ? 135.803 179.620 91.736  1.00 66.02  ? 1112 ARG   B NE    1 
ATOM   12136 C  CZ    . ARG   B 1 1112 ? 134.608 179.808 91.193  1.00 66.17  ? 1112 ARG   B CZ    1 
ATOM   12137 N  NH1   . ARG   B 1 1112 ? 134.082 181.016 91.083  1.00 64.86  ? 1112 ARG   B NH1   1 
ATOM   12138 N  NH2   . ARG   B 1 1112 ? 133.926 178.757 90.748  1.00 66.10  ? 1112 ARG   B NH2   1 
ATOM   12139 N  N     . LEU   B 1 1113 ? 139.562 176.536 89.915  1.00 72.69  ? 1113 LEU   B N     1 
ATOM   12140 C  CA    . LEU   B 1 1113 ? 139.862 175.790 88.702  1.00 69.24  ? 1113 LEU   B CA    1 
ATOM   12141 C  C     . LEU   B 1 1113 ? 139.058 176.273 87.503  1.00 71.27  ? 1113 LEU   B C     1 
ATOM   12142 O  O     . LEU   B 1 1113 ? 139.437 175.981 86.364  1.00 76.29  ? 1113 LEU   B O     1 
ATOM   12143 C  CB    . LEU   B 1 1113 ? 139.602 174.301 88.930  1.00 68.64  ? 1113 LEU   B CB    1 
ATOM   12144 C  CG    . LEU   B 1 1113 ? 139.751 173.382 87.719  1.00 67.85  ? 1113 LEU   B CG    1 
ATOM   12145 C  CD1   . LEU   B 1 1113 ? 141.164 173.457 87.172  1.00 67.65  ? 1113 LEU   B CD1   1 
ATOM   12146 C  CD2   . LEU   B 1 1113 ? 139.385 171.952 88.084  1.00 68.30  ? 1113 LEU   B CD2   1 
ATOM   12147 N  N     . HIS   B 1 1114 ? 137.976 177.010 87.733  1.00 75.16  ? 1114 HIS   B N     1 
ATOM   12148 C  CA    . HIS   B 1 1114 ? 137.134 177.554 86.670  1.00 74.11  ? 1114 HIS   B CA    1 
ATOM   12149 C  C     . HIS   B 1 1114 ? 136.899 176.516 85.574  1.00 76.37  ? 1114 HIS   B C     1 
ATOM   12150 O  O     . HIS   B 1 1114 ? 137.215 176.715 84.401  1.00 78.40  ? 1114 HIS   B O     1 
ATOM   12151 C  CB    . HIS   B 1 1114 ? 137.741 178.832 86.101  1.00 75.91  ? 1114 HIS   B CB    1 
ATOM   12152 C  CG    . HIS   B 1 1114 ? 137.578 180.020 86.996  1.00 74.49  ? 1114 HIS   B CG    1 
ATOM   12153 N  ND1   . HIS   B 1 1114 ? 136.354 180.603 87.241  1.00 74.52  ? 1114 HIS   B ND1   1 
ATOM   12154 C  CD2   . HIS   B 1 1114 ? 138.481 180.719 87.723  1.00 75.33  ? 1114 HIS   B CD2   1 
ATOM   12155 C  CE1   . HIS   B 1 1114 ? 136.511 181.619 88.070  1.00 76.13  ? 1114 HIS   B CE1   1 
ATOM   12156 N  NE2   . HIS   B 1 1114 ? 137.792 181.711 88.379  1.00 76.43  ? 1114 HIS   B NE2   1 
ATOM   12157 N  N     . GLU   B 1 1115 ? 136.334 175.380 85.988  1.00 84.39  ? 1115 GLU   B N     1 
ATOM   12158 C  CA    . GLU   B 1 1115 ? 136.081 174.297 85.044  1.00 85.35  ? 1115 GLU   B CA    1 
ATOM   12159 C  C     . GLU   B 1 1115 ? 135.127 174.733 83.939  1.00 87.26  ? 1115 GLU   B C     1 
ATOM   12160 O  O     . GLU   B 1 1115 ? 135.318 174.360 82.776  1.00 88.06  ? 1115 GLU   B O     1 
ATOM   12161 C  CB    . GLU   B 1 1115 ? 135.581 173.066 85.819  1.00 85.81  ? 1115 GLU   B CB    1 
ATOM   12162 C  CG    . GLU   B 1 1115 ? 135.336 171.745 85.051  1.00 87.23  ? 1115 GLU   B CG    1 
ATOM   12163 C  CD    . GLU   B 1 1115 ? 134.207 171.749 84.018  1.00 90.66  ? 1115 GLU   B CD    1 
ATOM   12164 O  OE1   . GLU   B 1 1115 ? 133.573 172.790 83.757  1.00 90.45  ? 1115 GLU   B OE1   1 
ATOM   12165 O  OE2   . GLU   B 1 1115 ? 133.951 170.667 83.452  1.00 91.20  ? 1115 GLU   B OE2   1 
ATOM   12166 N  N     . ASP   B 1 1116 ? 134.097 175.516 84.271  1.00 87.84  ? 1116 ASP   B N     1 
ATOM   12167 C  CA    . ASP   B 1 1116 ? 133.125 175.921 83.257  1.00 88.33  ? 1116 ASP   B CA    1 
ATOM   12168 C  C     . ASP   B 1 1116 ? 133.774 176.753 82.157  1.00 88.66  ? 1116 ASP   B C     1 
ATOM   12169 O  O     . ASP   B 1 1116 ? 133.489 176.551 80.971  1.00 85.50  ? 1116 ASP   B O     1 
ATOM   12170 C  CB    . ASP   B 1 1116 ? 131.981 176.699 83.907  1.00 85.06  ? 1116 ASP   B CB    1 
ATOM   12171 N  N     . ASP   B 1 1117 ? 134.638 177.700 82.525  1.00 91.64  ? 1117 ASP   B N     1 
ATOM   12172 C  CA    . ASP   B 1 1117 ? 135.266 178.545 81.514  1.00 90.84  ? 1117 ASP   B CA    1 
ATOM   12173 C  C     . ASP   B 1 1117 ? 136.209 177.752 80.619  1.00 91.90  ? 1117 ASP   B C     1 
ATOM   12174 O  O     . ASP   B 1 1117 ? 136.320 178.046 79.424  1.00 92.29  ? 1117 ASP   B O     1 
ATOM   12175 C  CB    . ASP   B 1 1117 ? 136.013 179.699 82.182  1.00 89.33  ? 1117 ASP   B CB    1 
ATOM   12176 N  N     . LYS   B 1 1118 ? 136.888 176.751 81.169  1.00 93.97  ? 1118 LYS   B N     1 
ATOM   12177 C  CA    . LYS   B 1 1118 ? 137.847 175.949 80.431  1.00 92.89  ? 1118 LYS   B CA    1 
ATOM   12178 C  C     . LYS   B 1 1118 ? 137.176 174.680 79.905  1.00 92.23  ? 1118 LYS   B C     1 
ATOM   12179 O  O     . LYS   B 1 1118 ? 135.955 174.516 79.978  1.00 90.34  ? 1118 LYS   B O     1 
ATOM   12180 C  CB    . LYS   B 1 1118 ? 139.054 175.639 81.317  1.00 90.72  ? 1118 LYS   B CB    1 
ATOM   12181 C  CG    . LYS   B 1 1118 ? 140.009 176.811 81.477  1.00 88.95  ? 1118 LYS   B CG    1 
ATOM   12182 C  CD    . LYS   B 1 1118 ? 140.557 176.897 82.890  1.00 87.87  ? 1118 LYS   B CD    1 
ATOM   12183 C  CE    . LYS   B 1 1118 ? 140.503 175.550 83.588  1.00 89.28  ? 1118 LYS   B CE    1 
ATOM   12184 N  NZ    . LYS   B 1 1118 ? 141.187 175.584 84.909  1.00 92.18  ? 1118 LYS   B NZ    1 
ATOM   12185 N  N     . GLU   B 1 1119 ? 137.981 173.772 79.367  1.00 91.71  ? 1119 GLU   B N     1 
ATOM   12186 C  CA    . GLU   B 1 1119 ? 137.505 172.540 78.756  1.00 90.30  ? 1119 GLU   B CA    1 
ATOM   12187 C  C     . GLU   B 1 1119 ? 138.158 171.344 79.446  1.00 90.32  ? 1119 GLU   B C     1 
ATOM   12188 O  O     . GLU   B 1 1119 ? 138.766 171.469 80.513  1.00 92.08  ? 1119 GLU   B O     1 
ATOM   12189 C  CB    . GLU   B 1 1119 ? 137.784 172.545 77.251  1.00 88.78  ? 1119 GLU   B CB    1 
ATOM   12190 N  N     . GLN   B 1 1120 ? 138.027 170.170 78.824  1.00 89.53  ? 1120 GLN   B N     1 
ATOM   12191 C  CA    . GLN   B 1 1120 ? 138.567 168.953 79.418  1.00 90.88  ? 1120 GLN   B CA    1 
ATOM   12192 C  C     . GLN   B 1 1120 ? 140.069 169.044 79.653  1.00 92.59  ? 1120 GLN   B C     1 
ATOM   12193 O  O     . GLN   B 1 1120 ? 140.596 168.319 80.504  1.00 93.41  ? 1120 GLN   B O     1 
ATOM   12194 C  CB    . GLN   B 1 1120 ? 138.251 167.750 78.530  1.00 89.89  ? 1120 GLN   B CB    1 
ATOM   12195 N  N     . ASP   B 1 1121 ? 140.768 169.920 78.927  1.00 93.46  ? 1121 ASP   B N     1 
ATOM   12196 C  CA    . ASP   B 1 1121 ? 142.190 170.119 79.186  1.00 93.74  ? 1121 ASP   B CA    1 
ATOM   12197 C  C     . ASP   B 1 1121 ? 142.436 170.547 80.626  1.00 94.63  ? 1121 ASP   B C     1 
ATOM   12198 O  O     . ASP   B 1 1121 ? 143.506 170.273 81.182  1.00 92.67  ? 1121 ASP   B O     1 
ATOM   12199 C  CB    . ASP   B 1 1121 ? 142.764 171.150 78.213  1.00 94.34  ? 1121 ASP   B CB    1 
ATOM   12200 C  CG    . ASP   B 1 1121 ? 142.135 172.524 78.373  1.00 97.19  ? 1121 ASP   B CG    1 
ATOM   12201 O  OD1   . ASP   B 1 1121 ? 142.181 173.081 79.490  1.00 95.64  ? 1121 ASP   B OD1   1 
ATOM   12202 O  OD2   . ASP   B 1 1121 ? 141.596 173.050 77.377  1.00 96.16  ? 1121 ASP   B OD2   1 
ATOM   12203 N  N     . ILE   B 1 1122 ? 141.459 171.213 81.247  1.00 92.77  ? 1122 ILE   B N     1 
ATOM   12204 C  CA    . ILE   B 1 1122 ? 141.593 171.629 82.636  1.00 90.39  ? 1122 ILE   B CA    1 
ATOM   12205 C  C     . ILE   B 1 1122 ? 141.834 170.440 83.551  1.00 90.75  ? 1122 ILE   B C     1 
ATOM   12206 O  O     . ILE   B 1 1122 ? 142.379 170.604 84.648  1.00 90.15  ? 1122 ILE   B O     1 
ATOM   12207 C  CB    . ILE   B 1 1122 ? 140.344 172.418 83.080  1.00 89.28  ? 1122 ILE   B CB    1 
ATOM   12208 N  N     . ALA   B 1 1123 ? 141.437 169.237 83.128  1.00 91.07  ? 1123 ALA   B N     1 
ATOM   12209 C  CA    . ALA   B 1 1123 ? 141.700 168.052 83.937  1.00 88.73  ? 1123 ALA   B CA    1 
ATOM   12210 C  C     . ALA   B 1 1123 ? 143.188 167.883 84.210  1.00 90.32  ? 1123 ALA   B C     1 
ATOM   12211 O  O     . ALA   B 1 1123 ? 143.569 167.316 85.240  1.00 90.75  ? 1123 ALA   B O     1 
ATOM   12212 C  CB    . ALA   B 1 1123 ? 141.140 166.809 83.246  1.00 88.15  ? 1123 ALA   B CB    1 
ATOM   12213 N  N     . ASP   B 1 1124 ? 144.042 168.363 83.303  1.00 91.13  ? 1124 ASP   B N     1 
ATOM   12214 C  CA    . ASP   B 1 1124 ? 145.479 168.320 83.551  1.00 89.85  ? 1124 ASP   B CA    1 
ATOM   12215 C  C     . ASP   B 1 1124 ? 145.852 169.169 84.760  1.00 90.71  ? 1124 ASP   B C     1 
ATOM   12216 O  O     . ASP   B 1 1124 ? 146.664 168.752 85.594  1.00 90.28  ? 1124 ASP   B O     1 
ATOM   12217 C  CB    . ASP   B 1 1124 ? 146.240 168.787 82.311  1.00 86.91  ? 1124 ASP   B CB    1 
ATOM   12218 N  N     . LYS   B 1 1125 ? 145.266 170.364 84.872  1.00 86.60  ? 1125 LYS   B N     1 
ATOM   12219 C  CA    . LYS   B 1 1125 ? 145.556 171.220 86.017  1.00 85.42  ? 1125 LYS   B CA    1 
ATOM   12220 C  C     . LYS   B 1 1125 ? 145.108 170.579 87.322  1.00 83.34  ? 1125 LYS   B C     1 
ATOM   12221 O  O     . LYS   B 1 1125 ? 145.717 170.816 88.371  1.00 83.22  ? 1125 LYS   B O     1 
ATOM   12222 C  CB    . LYS   B 1 1125 ? 144.887 172.583 85.839  1.00 83.28  ? 1125 LYS   B CB    1 
ATOM   12223 C  CG    . LYS   B 1 1125 ? 145.733 173.752 86.311  1.00 82.70  ? 1125 LYS   B CG    1 
ATOM   12224 C  CD    . LYS   B 1 1125 ? 145.397 175.021 85.548  1.00 82.61  ? 1125 LYS   B CD    1 
ATOM   12225 C  CE    . LYS   B 1 1125 ? 144.324 175.825 86.263  1.00 82.98  ? 1125 LYS   B CE    1 
ATOM   12226 N  NZ    . LYS   B 1 1125 ? 143.925 177.028 85.484  1.00 85.18  ? 1125 LYS   B NZ    1 
ATOM   12227 N  N     . MET   B 1 1126 ? 144.049 169.768 87.280  1.00 87.56  ? 1126 MET   B N     1 
ATOM   12228 C  CA    . MET   B 1 1126 ? 143.576 169.096 88.483  1.00 87.83  ? 1126 MET   B CA    1 
ATOM   12229 C  C     . MET   B 1 1126 ? 144.589 168.095 89.021  1.00 87.73  ? 1126 MET   B C     1 
ATOM   12230 O  O     . MET   B 1 1126 ? 144.459 167.658 90.169  1.00 88.87  ? 1126 MET   B O     1 
ATOM   12231 C  CB    . MET   B 1 1126 ? 142.246 168.393 88.205  1.00 89.07  ? 1126 MET   B CB    1 
ATOM   12232 C  CG    . MET   B 1 1126 ? 141.359 168.215 89.428  1.00 87.36  ? 1126 MET   B CG    1 
ATOM   12233 S  SD    . MET   B 1 1126 ? 141.566 169.523 90.651  1.00 90.00  ? 1126 MET   B SD    1 
ATOM   12234 C  CE    . MET   B 1 1126 ? 140.930 168.720 92.120  1.00 88.40  ? 1126 MET   B CE    1 
ATOM   12235 N  N     . LYS   B 1 1127 ? 145.583 167.714 88.220  1.00 87.93  ? 1127 LYS   B N     1 
ATOM   12236 C  CA    . LYS   B 1 1127 ? 146.616 166.783 88.648  1.00 89.54  ? 1127 LYS   B CA    1 
ATOM   12237 C  C     . LYS   B 1 1127 ? 148.010 167.397 88.662  1.00 89.42  ? 1127 LYS   B C     1 
ATOM   12238 O  O     . LYS   B 1 1127 ? 148.963 166.721 89.064  1.00 90.60  ? 1127 LYS   B O     1 
ATOM   12239 C  CB    . LYS   B 1 1127 ? 146.611 165.540 87.750  1.00 87.40  ? 1127 LYS   B CB    1 
ATOM   12240 N  N     . GLU   B 1 1128 ? 148.158 168.650 88.239  1.00 88.03  ? 1128 GLU   B N     1 
ATOM   12241 C  CA    . GLU   B 1 1128 ? 149.450 169.328 88.242  1.00 87.97  ? 1128 GLU   B CA    1 
ATOM   12242 C  C     . GLU   B 1 1128 ? 149.466 170.584 89.096  1.00 88.83  ? 1128 GLU   B C     1 
ATOM   12243 O  O     . GLU   B 1 1128 ? 150.420 170.800 89.849  1.00 89.27  ? 1128 GLU   B O     1 
ATOM   12244 C  CB    . GLU   B 1 1128 ? 149.862 169.685 86.806  1.00 85.75  ? 1128 GLU   B CB    1 
ATOM   12245 N  N     . ASP   B 1 1129 ? 148.435 171.421 89.001  1.00 84.35  ? 1129 ASP   B N     1 
ATOM   12246 C  CA    . ASP   B 1 1129 ? 148.272 172.576 89.873  1.00 80.46  ? 1129 ASP   B CA    1 
ATOM   12247 C  C     . ASP   B 1 1129 ? 147.325 172.288 91.029  1.00 79.18  ? 1129 ASP   B C     1 
ATOM   12248 O  O     . ASP   B 1 1129 ? 147.005 173.199 91.799  1.00 83.75  ? 1129 ASP   B O     1 
ATOM   12249 C  CB    . ASP   B 1 1129 ? 147.775 173.783 89.075  1.00 81.57  ? 1129 ASP   B CB    1 
ATOM   12250 C  CG    . ASP   B 1 1129 ? 148.548 175.049 89.390  1.00 83.73  ? 1129 ASP   B CG    1 
ATOM   12251 O  OD1   . ASP   B 1 1129 ? 148.922 175.241 90.566  1.00 82.79  ? 1129 ASP   B OD1   1 
ATOM   12252 O  OD2   . ASP   B 1 1129 ? 148.783 175.851 88.462  1.00 82.57  ? 1129 ASP   B OD2   1 
ATOM   12253 N  N     . GLU   B 1 1130 ? 146.875 171.046 91.167  1.00 74.98  ? 1130 GLU   B N     1 
ATOM   12254 C  CA    . GLU   B 1 1130 ? 145.904 170.679 92.187  1.00 76.50  ? 1130 GLU   B CA    1 
ATOM   12255 C  C     . GLU   B 1 1130 ? 146.505 169.640 93.126  1.00 74.41  ? 1130 GLU   B C     1 
ATOM   12256 O  O     . GLU   B 1 1130 ? 147.633 169.182 92.904  1.00 74.61  ? 1130 GLU   B O     1 
ATOM   12257 C  CB    . GLU   B 1 1130 ? 144.624 170.155 91.538  1.00 79.04  ? 1130 GLU   B CB    1 
ATOM   12258 N  N     . PRO   B 1 1131 ? 145.787 169.239 94.180  1.00 75.56  ? 1131 PRO   B N     1 
ATOM   12259 C  CA    . PRO   B 1 1131 ? 144.391 169.570 94.488  1.00 76.63  ? 1131 PRO   B CA    1 
ATOM   12260 C  C     . PRO   B 1 1131 ? 144.236 170.918 95.182  1.00 75.15  ? 1131 PRO   B C     1 
ATOM   12261 O  O     . PRO   B 1 1131 ? 143.434 171.061 96.099  1.00 77.66  ? 1131 PRO   B O     1 
ATOM   12262 C  CB    . PRO   B 1 1131 ? 143.968 168.405 95.388  1.00 77.83  ? 1131 PRO   B CB    1 
ATOM   12263 C  CG    . PRO   B 1 1131 ? 145.220 168.081 96.154  1.00 77.45  ? 1131 PRO   B CG    1 
ATOM   12264 C  CD    . PRO   B 1 1131 ? 146.363 168.329 95.188  1.00 76.32  ? 1131 PRO   B CD    1 
ATOM   12265 N  N     . TRP   B 1 1132 ? 144.998 171.930 94.760  1.00 68.52  ? 1132 TRP   B N     1 
ATOM   12266 C  CA    . TRP   B 1 1132 ? 144.800 173.273 95.294  1.00 67.44  ? 1132 TRP   B CA    1 
ATOM   12267 C  C     . TRP   B 1 1132 ? 143.559 173.914 94.688  1.00 70.68  ? 1132 TRP   B C     1 
ATOM   12268 O  O     . TRP   B 1 1132 ? 142.714 174.462 95.406  1.00 71.58  ? 1132 TRP   B O     1 
ATOM   12269 C  CB    . TRP   B 1 1132 ? 146.019 174.159 95.016  1.00 61.63  ? 1132 TRP   B CB    1 
ATOM   12270 C  CG    . TRP   B 1 1132 ? 147.363 173.490 95.021  1.00 62.96  ? 1132 TRP   B CG    1 
ATOM   12271 C  CD1   . TRP   B 1 1132 ? 147.693 172.282 95.568  1.00 68.79  ? 1132 TRP   B CD1   1 
ATOM   12272 C  CD2   . TRP   B 1 1132 ? 148.567 174.009 94.445  1.00 69.31  ? 1132 TRP   B CD2   1 
ATOM   12273 N  NE1   . TRP   B 1 1132 ? 149.024 172.017 95.364  1.00 73.40  ? 1132 TRP   B NE1   1 
ATOM   12274 C  CE2   . TRP   B 1 1132 ? 149.584 173.063 94.678  1.00 74.26  ? 1132 TRP   B CE2   1 
ATOM   12275 C  CE3   . TRP   B 1 1132 ? 148.883 175.183 93.754  1.00 71.28  ? 1132 TRP   B CE3   1 
ATOM   12276 C  CZ2   . TRP   B 1 1132 ? 150.894 173.255 94.245  1.00 74.44  ? 1132 TRP   B CZ2   1 
ATOM   12277 C  CZ3   . TRP   B 1 1132 ? 150.183 175.371 93.326  1.00 73.09  ? 1132 TRP   B CZ3   1 
ATOM   12278 C  CH2   . TRP   B 1 1132 ? 151.173 174.413 93.572  1.00 73.17  ? 1132 TRP   B CH2   1 
ATOM   12279 N  N     . ARG   B 1 1133 ? 143.435 173.848 93.365  1.00 63.98  ? 1133 ARG   B N     1 
ATOM   12280 C  CA    . ARG   B 1 1133 ? 142.375 174.561 92.667  1.00 64.36  ? 1133 ARG   B CA    1 
ATOM   12281 C  C     . ARG   B 1 1133 ? 141.006 174.138 93.181  1.00 63.54  ? 1133 ARG   B C     1 
ATOM   12282 O  O     . ARG   B 1 1133 ? 140.726 172.949 93.356  1.00 63.81  ? 1133 ARG   B O     1 
ATOM   12283 C  CB    . ARG   B 1 1133 ? 142.474 174.309 91.162  1.00 66.82  ? 1133 ARG   B CB    1 
ATOM   12284 C  CG    . ARG   B 1 1133 ? 143.872 174.484 90.593  1.00 63.96  ? 1133 ARG   B CG    1 
ATOM   12285 C  CD    . ARG   B 1 1133 ? 144.438 175.854 90.921  1.00 63.72  ? 1133 ARG   B CD    1 
ATOM   12286 N  NE    . ARG   B 1 1133 ? 144.268 176.797 89.822  1.00 63.34  ? 1133 ARG   B NE    1 
ATOM   12287 C  CZ    . ARG   B 1 1133 ? 144.999 177.890 89.655  1.00 65.32  ? 1133 ARG   B CZ    1 
ATOM   12288 N  NH1   . ARG   B 1 1133 ? 145.972 178.206 90.494  1.00 64.73  ? 1133 ARG   B NH1   1 
ATOM   12289 N  NH2   . ARG   B 1 1133 ? 144.750 178.686 88.619  1.00 62.78  ? 1133 ARG   B NH2   1 
ATOM   12290 N  N     . ILE   B 1 1134 ? 140.150 175.125 93.422  1.00 57.05  ? 1134 ILE   B N     1 
ATOM   12291 C  CA    . ILE   B 1 1134 ? 138.789 174.886 93.883  1.00 54.07  ? 1134 ILE   B CA    1 
ATOM   12292 C  C     . ILE   B 1 1134 ? 137.916 174.669 92.653  1.00 54.55  ? 1134 ILE   B C     1 
ATOM   12293 O  O     . ILE   B 1 1134 ? 137.728 175.582 91.846  1.00 56.10  ? 1134 ILE   B O     1 
ATOM   12294 C  CB    . ILE   B 1 1134 ? 138.272 176.050 94.735  1.00 56.70  ? 1134 ILE   B CB    1 
ATOM   12295 C  CG1   . ILE   B 1 1134 ? 139.093 176.174 96.019  1.00 53.23  ? 1134 ILE   B CG1   1 
ATOM   12296 C  CG2   . ILE   B 1 1134 ? 136.802 175.854 95.061  1.00 57.79  ? 1134 ILE   B CG2   1 
ATOM   12297 C  CD1   . ILE   B 1 1134 ? 139.521 177.586 96.329  1.00 52.07  ? 1134 ILE   B CD1   1 
ATOM   12298 N  N     . THR   B 1 1135 ? 137.388 173.458 92.505  1.00 57.68  ? 1135 THR   B N     1 
ATOM   12299 C  CA    . THR   B 1 1135 ? 136.522 173.165 91.377  1.00 59.04  ? 1135 THR   B CA    1 
ATOM   12300 C  C     . THR   B 1 1135 ? 135.228 173.972 91.483  1.00 60.08  ? 1135 THR   B C     1 
ATOM   12301 O  O     . THR   B 1 1135 ? 134.885 174.520 92.532  1.00 66.26  ? 1135 THR   B O     1 
ATOM   12302 C  CB    . THR   B 1 1135 ? 136.208 171.671 91.315  1.00 58.79  ? 1135 THR   B CB    1 
ATOM   12303 O  OG1   . THR   B 1 1135 ? 135.015 171.400 92.061  1.00 60.85  ? 1135 THR   B OG1   1 
ATOM   12304 C  CG2   . THR   B 1 1135 ? 137.354 170.864 91.898  1.00 58.05  ? 1135 THR   B CG2   1 
ATOM   12305 N  N     . ASP   B 1 1136 ? 134.507 174.047 90.363  1.00 57.02  ? 1136 ASP   B N     1 
ATOM   12306 C  CA    . ASP   B 1 1136 ? 133.208 174.708 90.373  1.00 55.87  ? 1136 ASP   B CA    1 
ATOM   12307 C  C     . ASP   B 1 1136 ? 132.127 173.792 90.934  1.00 54.76  ? 1136 ASP   B C     1 
ATOM   12308 O  O     . ASP   B 1 1136 ? 131.218 174.253 91.633  1.00 55.71  ? 1136 ASP   B O     1 
ATOM   12309 C  CB    . ASP   B 1 1136 ? 132.840 175.169 88.963  1.00 52.34  ? 1136 ASP   B CB    1 
ATOM   12310 N  N     . ASN   B 1 1137 ? 132.218 172.493 90.644  1.00 51.41  ? 1137 ASN   B N     1 
ATOM   12311 C  CA    . ASN   B 1 1137 ? 131.232 171.548 91.157  1.00 51.08  ? 1137 ASN   B CA    1 
ATOM   12312 C  C     . ASN   B 1 1137 ? 131.239 171.524 92.679  1.00 56.64  ? 1137 ASN   B C     1 
ATOM   12313 O  O     . ASN   B 1 1137 ? 130.182 171.563 93.317  1.00 61.31  ? 1137 ASN   B O     1 
ATOM   12314 C  CB    . ASN   B 1 1137 ? 131.503 170.153 90.593  1.00 52.40  ? 1137 ASN   B CB    1 
ATOM   12315 N  N     . GLU   B 1 1138 ? 132.429 171.463 93.281  1.00 60.57  ? 1138 GLU   B N     1 
ATOM   12316 C  CA    . GLU   B 1 1138 ? 132.516 171.454 94.738  1.00 59.77  ? 1138 GLU   B CA    1 
ATOM   12317 C  C     . GLU   B 1 1138 ? 132.063 172.784 95.327  1.00 56.41  ? 1138 GLU   B C     1 
ATOM   12318 O  O     . GLU   B 1 1138 ? 131.354 172.812 96.340  1.00 52.07  ? 1138 GLU   B O     1 
ATOM   12319 C  CB    . GLU   B 1 1138 ? 133.942 171.117 95.178  1.00 55.94  ? 1138 GLU   B CB    1 
ATOM   12320 C  CG    . GLU   B 1 1138 ? 134.878 172.311 95.265  1.00 58.12  ? 1138 GLU   B CG    1 
ATOM   12321 C  CD    . GLU   B 1 1138 ? 136.128 172.015 96.071  1.00 62.80  ? 1138 GLU   B CD    1 
ATOM   12322 O  OE1   . GLU   B 1 1138 ? 136.290 170.860 96.517  1.00 63.51  ? 1138 GLU   B OE1   1 
ATOM   12323 O  OE2   . GLU   B 1 1138 ? 136.951 172.936 96.254  1.00 63.17  ? 1138 GLU   B OE2   1 
ATOM   12324 N  N     . LEU   B 1 1139 ? 132.460 173.898 94.708  1.00 53.06  ? 1139 LEU   B N     1 
ATOM   12325 C  CA    . LEU   B 1 1139 ? 132.050 175.204 95.210  1.00 50.58  ? 1139 LEU   B CA    1 
ATOM   12326 C  C     . LEU   B 1 1139 ? 130.533 175.343 95.208  1.00 54.16  ? 1139 LEU   B C     1 
ATOM   12327 O  O     . LEU   B 1 1139 ? 129.949 175.876 96.159  1.00 56.40  ? 1139 LEU   B O     1 
ATOM   12328 C  CB    . LEU   B 1 1139 ? 132.693 176.313 94.378  1.00 44.09  ? 1139 LEU   B CB    1 
ATOM   12329 N  N     . GLU   B 1 1140 ? 129.876 174.869 94.148  1.00 52.43  ? 1140 GLU   B N     1 
ATOM   12330 C  CA    . GLU   B 1 1140 ? 128.423 174.961 94.078  1.00 50.78  ? 1140 GLU   B CA    1 
ATOM   12331 C  C     . GLU   B 1 1140 ? 127.735 173.936 94.970  1.00 52.97  ? 1140 GLU   B C     1 
ATOM   12332 O  O     . GLU   B 1 1140 ? 126.636 174.198 95.471  1.00 61.26  ? 1140 GLU   B O     1 
ATOM   12333 C  CB    . GLU   B 1 1140 ? 127.955 174.793 92.632  1.00 51.85  ? 1140 GLU   B CB    1 
ATOM   12334 N  N     . LEU   B 1 1141 ? 128.354 172.777 95.182  1.00 47.70  ? 1141 LEU   B N     1 
ATOM   12335 C  CA    . LEU   B 1 1141 ? 127.753 171.692 95.945  1.00 44.46  ? 1141 LEU   B CA    1 
ATOM   12336 C  C     . LEU   B 1 1141 ? 127.976 171.824 97.447  1.00 50.33  ? 1141 LEU   B C     1 
ATOM   12337 O  O     . LEU   B 1 1141 ? 127.392 171.052 98.214  1.00 48.83  ? 1141 LEU   B O     1 
ATOM   12338 C  CB    . LEU   B 1 1141 ? 128.301 170.346 95.447  1.00 42.16  ? 1141 LEU   B CB    1 
ATOM   12339 C  CG    . LEU   B 1 1141 ? 128.022 169.061 96.231  1.00 45.47  ? 1141 LEU   B CG    1 
ATOM   12340 C  CD1   . LEU   B 1 1141 ? 128.078 167.859 95.304  1.00 48.40  ? 1141 LEU   B CD1   1 
ATOM   12341 C  CD2   . LEU   B 1 1141 ? 129.014 168.887 97.362  1.00 49.61  ? 1141 LEU   B CD2   1 
ATOM   12342 N  N     . TYR   B 1 1142 ? 128.792 172.784 97.887  1.00 52.63  ? 1142 TYR   B N     1 
ATOM   12343 C  CA    . TYR   B 1 1142 ? 129.059 172.998 99.304  1.00 45.31  ? 1142 TYR   B CA    1 
ATOM   12344 C  C     . TYR   B 1 1142 ? 128.798 174.447 99.699  1.00 50.14  ? 1142 TYR   B C     1 
ATOM   12345 O  O     . TYR   B 1 1142 ? 129.423 174.965 100.628 1.00 51.45  ? 1142 TYR   B O     1 
ATOM   12346 C  CB    . TYR   B 1 1142 ? 130.492 172.602 99.663  1.00 45.08  ? 1142 TYR   B CB    1 
ATOM   12347 C  CG    . TYR   B 1 1142 ? 130.718 171.111 99.784  1.00 45.22  ? 1142 TYR   B CG    1 
ATOM   12348 C  CD1   . TYR   B 1 1142 ? 130.098 170.374 100.783 1.00 49.30  ? 1142 TYR   B CD1   1 
ATOM   12349 C  CD2   . TYR   B 1 1142 ? 131.561 170.443 98.906  1.00 47.41  ? 1142 TYR   B CD2   1 
ATOM   12350 C  CE1   . TYR   B 1 1142 ? 130.304 169.013 100.899 1.00 49.95  ? 1142 TYR   B CE1   1 
ATOM   12351 C  CE2   . TYR   B 1 1142 ? 131.773 169.083 99.014  1.00 49.47  ? 1142 TYR   B CE2   1 
ATOM   12352 C  CZ    . TYR   B 1 1142 ? 131.142 168.373 100.011 1.00 53.65  ? 1142 TYR   B CZ    1 
ATOM   12353 O  OH    . TYR   B 1 1142 ? 131.351 167.017 100.122 1.00 53.21  ? 1142 TYR   B OH    1 
ATOM   12354 N  N     . LYS   B 1 1143 ? 127.877 175.117 99.002  1.00 44.38  ? 1143 LYS   B N     1 
ATOM   12355 C  CA    . LYS   B 1 1143 ? 127.563 176.502 99.340  1.00 44.53  ? 1143 LYS   B CA    1 
ATOM   12356 C  C     . LYS   B 1 1143 ? 127.020 176.620 100.756 1.00 47.47  ? 1143 LYS   B C     1 
ATOM   12357 O  O     . LYS   B 1 1143 ? 127.251 177.632 101.430 1.00 45.48  ? 1143 LYS   B O     1 
ATOM   12358 C  CB    . LYS   B 1 1143 ? 126.561 177.074 98.337  1.00 36.30  ? 1143 LYS   B CB    1 
ATOM   12359 N  N     . THR   B 1 1144 ? 126.300 175.599 101.225 1.00 39.84  ? 1144 THR   B N     1 
ATOM   12360 C  CA    . THR   B 1 1144 ? 125.755 175.643 102.576 1.00 41.05  ? 1144 THR   B CA    1 
ATOM   12361 C  C     . THR   B 1 1144 ? 126.866 175.740 103.613 1.00 41.16  ? 1144 THR   B C     1 
ATOM   12362 O  O     . THR   B 1 1144 ? 126.774 176.534 104.553 1.00 35.77  ? 1144 THR   B O     1 
ATOM   12363 C  CB    . THR   B 1 1144 ? 124.886 174.412 102.837 1.00 41.20  ? 1144 THR   B CB    1 
ATOM   12364 O  OG1   . THR   B 1 1144 ? 125.720 173.256 102.979 1.00 50.60  ? 1144 THR   B OG1   1 
ATOM   12365 C  CG2   . THR   B 1 1144 ? 123.917 174.191 101.688 1.00 38.75  ? 1144 THR   B CG2   1 
ATOM   12366 N  N     . LYS   B 1 1145 ? 127.929 174.950 103.456 1.00 40.28  ? 1145 LYS   B N     1 
ATOM   12367 C  CA    . LYS   B 1 1145 ? 129.012 174.973 104.436 1.00 39.24  ? 1145 LYS   B CA    1 
ATOM   12368 C  C     . LYS   B 1 1145 ? 129.756 176.305 104.421 1.00 36.59  ? 1145 LYS   B C     1 
ATOM   12369 O  O     . LYS   B 1 1145 ? 130.122 176.832 105.479 1.00 45.45  ? 1145 LYS   B O     1 
ATOM   12370 C  CB    . LYS   B 1 1145 ? 129.971 173.813 104.179 1.00 35.21  ? 1145 LYS   B CB    1 
ATOM   12371 C  CG    . LYS   B 1 1145 ? 130.451 173.139 105.447 1.00 33.99  ? 1145 LYS   B CG    1 
ATOM   12372 C  CD    . LYS   B 1 1145 ? 130.547 171.636 105.273 1.00 36.54  ? 1145 LYS   B CD    1 
ATOM   12373 C  CE    . LYS   B 1 1145 ? 131.146 170.987 106.508 1.00 41.51  ? 1145 LYS   B CE    1 
ATOM   12374 N  NZ    . LYS   B 1 1145 ? 131.926 169.763 106.189 1.00 42.92  ? 1145 LYS   B NZ    1 
ATOM   12375 N  N     . THR   B 1 1146 ? 130.001 176.860 103.233 1.00 31.62  ? 1146 THR   B N     1 
ATOM   12376 C  CA    . THR   B 1 1146 ? 130.670 178.155 103.147 1.00 37.31  ? 1146 THR   B CA    1 
ATOM   12377 C  C     . THR   B 1 1146 ? 129.831 179.247 103.797 1.00 45.56  ? 1146 THR   B C     1 
ATOM   12378 O  O     . THR   B 1 1146 ? 130.341 180.071 104.571 1.00 44.49  ? 1146 THR   B O     1 
ATOM   12379 C  CB    . THR   B 1 1146 ? 130.958 178.496 101.685 1.00 36.75  ? 1146 THR   B CB    1 
ATOM   12380 O  OG1   . THR   B 1 1146 ? 131.585 177.378 101.048 1.00 36.15  ? 1146 THR   B OG1   1 
ATOM   12381 C  CG2   . THR   B 1 1146 ? 131.872 179.705 101.588 1.00 40.49  ? 1146 THR   B CG2   1 
ATOM   12382 N  N     . TYR   B 1 1147 ? 128.536 179.281 103.479 1.00 44.31  ? 1147 TYR   B N     1 
ATOM   12383 C  CA    . TYR   B 1 1147 ? 127.666 180.257 104.116 1.00 36.17  ? 1147 TYR   B CA    1 
ATOM   12384 C  C     . TYR   B 1 1147 ? 127.601 180.028 105.616 1.00 37.11  ? 1147 TYR   B C     1 
ATOM   12385 O  O     . TYR   B 1 1147 ? 127.503 180.990 106.384 1.00 46.09  ? 1147 TYR   B O     1 
ATOM   12386 C  CB    . TYR   B 1 1147 ? 126.273 180.213 103.493 1.00 38.96  ? 1147 TYR   B CB    1 
ATOM   12387 C  CG    . TYR   B 1 1147 ? 126.236 180.797 102.104 1.00 49.03  ? 1147 TYR   B CG    1 
ATOM   12388 C  CD1   . TYR   B 1 1147 ? 127.233 181.658 101.675 1.00 44.95  ? 1147 TYR   B CD1   1 
ATOM   12389 C  CD2   . TYR   B 1 1147 ? 125.206 180.496 101.222 1.00 45.83  ? 1147 TYR   B CD2   1 
ATOM   12390 C  CE1   . TYR   B 1 1147 ? 127.213 182.201 100.411 1.00 38.73  ? 1147 TYR   B CE1   1 
ATOM   12391 C  CE2   . TYR   B 1 1147 ? 125.175 181.037 99.949  1.00 43.47  ? 1147 TYR   B CE2   1 
ATOM   12392 C  CZ    . TYR   B 1 1147 ? 126.181 181.889 99.550  1.00 45.45  ? 1147 TYR   B CZ    1 
ATOM   12393 O  OH    . TYR   B 1 1147 ? 126.157 182.430 98.286  1.00 48.22  ? 1147 TYR   B OH    1 
ATOM   12394 N  N     . ARG   B 1 1148 ? 127.681 178.771 106.055 1.00 32.84  ? 1148 ARG   B N     1 
ATOM   12395 C  CA    . ARG   B 1 1148 ? 127.716 178.496 107.485 1.00 33.03  ? 1148 ARG   B CA    1 
ATOM   12396 C  C     . ARG   B 1 1148 ? 128.953 179.102 108.128 1.00 32.68  ? 1148 ARG   B C     1 
ATOM   12397 O  O     . ARG   B 1 1148 ? 128.870 179.702 109.200 1.00 38.54  ? 1148 ARG   B O     1 
ATOM   12398 C  CB    . ARG   B 1 1148 ? 127.700 176.991 107.745 1.00 32.13  ? 1148 ARG   B CB    1 
ATOM   12399 C  CG    . ARG   B 1 1148 ? 128.264 176.638 109.115 1.00 37.30  ? 1148 ARG   B CG    1 
ATOM   12400 C  CD    . ARG   B 1 1148 ? 127.331 175.734 109.899 1.00 36.34  ? 1148 ARG   B CD    1 
ATOM   12401 N  NE    . ARG   B 1 1148 ? 126.676 174.743 109.054 1.00 39.02  ? 1148 ARG   B NE    1 
ATOM   12402 C  CZ    . ARG   B 1 1148 ? 127.306 173.710 108.512 1.00 39.80  ? 1148 ARG   B CZ    1 
ATOM   12403 N  NH1   . ARG   B 1 1148 ? 128.605 173.528 108.684 1.00 35.91  ? 1148 ARG   B NH1   1 
ATOM   12404 N  NH2   . ARG   B 1 1148 ? 126.613 172.827 107.797 1.00 39.98  ? 1148 ARG   B NH2   1 
ATOM   12405 N  N     . GLN   B 1 1149 ? 130.118 178.942 107.492 1.00 29.69  ? 1149 GLN   B N     1 
ATOM   12406 C  CA    . GLN   B 1 1149 ? 131.346 179.517 108.045 1.00 20.30  ? 1149 GLN   B CA    1 
ATOM   12407 C  C     . GLN   B 1 1149 ? 131.252 181.037 108.123 1.00 27.37  ? 1149 GLN   B C     1 
ATOM   12408 O  O     . GLN   B 1 1149 ? 131.609 181.642 109.144 1.00 31.59  ? 1149 GLN   B O     1 
ATOM   12409 C  CB    . GLN   B 1 1149 ? 132.547 179.091 107.200 1.00 28.18  ? 1149 GLN   B CB    1 
ATOM   12410 C  CG    . GLN   B 1 1149 ? 132.585 177.606 106.877 1.00 32.70  ? 1149 GLN   B CG    1 
ATOM   12411 C  CD    . GLN   B 1 1149 ? 132.355 176.746 108.095 1.00 30.80  ? 1149 GLN   B CD    1 
ATOM   12412 O  OE1   . GLN   B 1 1149 ? 132.629 177.162 109.217 1.00 37.81  ? 1149 GLN   B OE1   1 
ATOM   12413 N  NE2   . GLN   B 1 1149 ? 131.824 175.546 107.885 1.00 28.21  ? 1149 GLN   B NE2   1 
ATOM   12414 N  N     . ILE   B 1 1150 ? 130.759 181.673 107.059 1.00 28.93  ? 1150 ILE   B N     1 
ATOM   12415 C  CA    . ILE   B 1 1150 ? 130.675 183.132 107.060 1.00 31.72  ? 1150 ILE   B CA    1 
ATOM   12416 C  C     . ILE   B 1 1150 ? 129.684 183.617 108.117 1.00 38.47  ? 1150 ILE   B C     1 
ATOM   12417 O  O     . ILE   B 1 1150 ? 129.973 184.546 108.887 1.00 43.44  ? 1150 ILE   B O     1 
ATOM   12418 C  CB    . ILE   B 1 1150 ? 130.311 183.645 105.655 1.00 29.95  ? 1150 ILE   B CB    1 
ATOM   12419 C  CG1   . ILE   B 1 1150 ? 131.329 183.146 104.626 1.00 28.67  ? 1150 ILE   B CG1   1 
ATOM   12420 C  CG2   . ILE   B 1 1150 ? 130.248 185.162 105.642 1.00 29.55  ? 1150 ILE   B CG2   1 
ATOM   12421 C  CD1   . ILE   B 1 1150 ? 130.983 183.501 103.197 1.00 31.98  ? 1150 ILE   B CD1   1 
ATOM   12422 N  N     . ARG   B 1 1151 ? 128.505 182.995 108.182 1.00 31.50  ? 1151 ARG   B N     1 
ATOM   12423 C  CA    . ARG   B 1 1151 ? 127.508 183.400 109.164 1.00 26.36  ? 1151 ARG   B CA    1 
ATOM   12424 C  C     . ARG   B 1 1151 ? 127.991 183.129 110.582 1.00 35.05  ? 1151 ARG   B C     1 
ATOM   12425 O  O     . ARG   B 1 1151 ? 127.683 183.891 111.504 1.00 42.29  ? 1151 ARG   B O     1 
ATOM   12426 C  CB    . ARG   B 1 1151 ? 126.190 182.676 108.896 1.00 33.57  ? 1151 ARG   B CB    1 
ATOM   12427 C  CG    . ARG   B 1 1151 ? 125.097 182.957 109.914 1.00 37.69  ? 1151 ARG   B CG    1 
ATOM   12428 C  CD    . ARG   B 1 1151 ? 124.276 184.176 109.517 1.00 36.41  ? 1151 ARG   B CD    1 
ATOM   12429 N  NE    . ARG   B 1 1151 ? 123.557 184.754 110.645 1.00 42.68  ? 1151 ARG   B NE    1 
ATOM   12430 C  CZ    . ARG   B 1 1151 ? 123.892 185.887 111.247 1.00 43.74  ? 1151 ARG   B CZ    1 
ATOM   12431 N  NH1   . ARG   B 1 1151 ? 124.941 186.593 110.858 1.00 44.69  ? 1151 ARG   B NH1   1 
ATOM   12432 N  NH2   . ARG   B 1 1151 ? 123.154 186.325 112.263 1.00 41.97  ? 1151 ARG   B NH2   1 
ATOM   12433 N  N     . LEU   B 1 1152 ? 128.736 182.040 110.782 1.00 31.10  ? 1152 LEU   B N     1 
ATOM   12434 C  CA    . LEU   B 1 1152 ? 129.281 181.738 112.099 1.00 32.28  ? 1152 LEU   B CA    1 
ATOM   12435 C  C     . LEU   B 1 1152 ? 130.298 182.786 112.523 1.00 31.64  ? 1152 LEU   B C     1 
ATOM   12436 O  O     . LEU   B 1 1152 ? 130.336 183.185 113.692 1.00 38.60  ? 1152 LEU   B O     1 
ATOM   12437 C  CB    . LEU   B 1 1152 ? 129.911 180.346 112.093 1.00 33.27  ? 1152 LEU   B CB    1 
ATOM   12438 C  CG    . LEU   B 1 1152 ? 128.976 179.178 112.409 1.00 30.07  ? 1152 LEU   B CG    1 
ATOM   12439 C  CD1   . LEU   B 1 1152 ? 129.770 177.900 112.600 1.00 31.42  ? 1152 LEU   B CD1   1 
ATOM   12440 C  CD2   . LEU   B 1 1152 ? 128.135 179.474 113.637 1.00 35.59  ? 1152 LEU   B CD2   1 
ATOM   12441 N  N     . ASN   B 1 1153 ? 131.143 183.236 111.593 1.00 32.41  ? 1153 ASN   B N     1 
ATOM   12442 C  CA    . ASN   B 1 1153 ? 132.065 184.318 111.924 1.00 33.90  ? 1153 ASN   B CA    1 
ATOM   12443 C  C     . ASN   B 1 1153 ? 131.301 185.590 112.268 1.00 36.34  ? 1153 ASN   B C     1 
ATOM   12444 O  O     . ASN   B 1 1153 ? 131.665 186.312 113.207 1.00 36.77  ? 1153 ASN   B O     1 
ATOM   12445 C  CB    . ASN   B 1 1153 ? 133.037 184.562 110.769 1.00 32.04  ? 1153 ASN   B CB    1 
ATOM   12446 C  CG    . ASN   B 1 1153 ? 134.002 185.700 111.048 1.00 35.61  ? 1153 ASN   B CG    1 
ATOM   12447 O  OD1   . ASN   B 1 1153 ? 135.046 185.508 111.673 1.00 27.07  ? 1153 ASN   B OD1   1 
ATOM   12448 N  ND2   . ASN   B 1 1153 ? 133.656 186.895 110.586 1.00 38.93  ? 1153 ASN   B ND2   1 
ATOM   12449 N  N     . GLU   B 1 1154 ? 130.229 185.876 111.525 1.00 40.27  ? 1154 GLU   B N     1 
ATOM   12450 C  CA    . GLU   B 1 1154 ? 129.380 187.017 111.859 1.00 42.00  ? 1154 GLU   B CA    1 
ATOM   12451 C  C     . GLU   B 1 1154 ? 128.839 186.896 113.279 1.00 37.79  ? 1154 GLU   B C     1 
ATOM   12452 O  O     . GLU   B 1 1154 ? 128.883 187.851 114.063 1.00 35.81  ? 1154 GLU   B O     1 
ATOM   12453 C  CB    . GLU   B 1 1154 ? 128.225 187.118 110.863 1.00 40.74  ? 1154 GLU   B CB    1 
ATOM   12454 C  CG    . GLU   B 1 1154 ? 128.312 188.276 109.888 1.00 43.70  ? 1154 GLU   B CG    1 
ATOM   12455 C  CD    . GLU   B 1 1154 ? 127.362 188.106 108.717 1.00 46.57  ? 1154 GLU   B CD    1 
ATOM   12456 O  OE1   . GLU   B 1 1154 ? 126.306 187.468 108.900 1.00 47.58  ? 1154 GLU   B OE1   1 
ATOM   12457 O  OE2   . GLU   B 1 1154 ? 127.670 188.603 107.615 1.00 49.90  ? 1154 GLU   B OE2   1 
ATOM   12458 N  N     . LEU   B 1 1155 ? 128.321 185.717 113.623 1.00 35.42  ? 1155 LEU   B N     1 
ATOM   12459 C  CA    . LEU   B 1 1155 ? 127.740 185.501 114.944 1.00 32.42  ? 1155 LEU   B CA    1 
ATOM   12460 C  C     . LEU   B 1 1155 ? 128.788 185.646 116.039 1.00 31.60  ? 1155 LEU   B C     1 
ATOM   12461 O  O     . LEU   B 1 1155 ? 128.520 186.237 117.092 1.00 41.33  ? 1155 LEU   B O     1 
ATOM   12462 C  CB    . LEU   B 1 1155 ? 127.090 184.119 115.003 1.00 34.81  ? 1155 LEU   B CB    1 
ATOM   12463 C  CG    . LEU   B 1 1155 ? 125.717 183.977 114.343 1.00 39.38  ? 1155 LEU   B CG    1 
ATOM   12464 C  CD1   . LEU   B 1 1155 ? 125.248 182.534 114.394 1.00 36.62  ? 1155 LEU   B CD1   1 
ATOM   12465 C  CD2   . LEU   B 1 1155 ? 124.704 184.892 115.008 1.00 37.58  ? 1155 LEU   B CD2   1 
ATOM   12466 N  N     . LEU   B 1 1156 ? 129.984 185.099 115.817 1.00 34.16  ? 1156 LEU   B N     1 
ATOM   12467 C  CA    . LEU   B 1 1156 ? 131.044 185.210 116.813 1.00 27.40  ? 1156 LEU   B CA    1 
ATOM   12468 C  C     . LEU   B 1 1156 ? 131.461 186.659 117.012 1.00 31.44  ? 1156 LEU   B C     1 
ATOM   12469 O  O     . LEU   B 1 1156 ? 131.702 187.094 118.144 1.00 32.23  ? 1156 LEU   B O     1 
ATOM   12470 C  CB    . LEU   B 1 1156 ? 132.246 184.359 116.406 1.00 28.68  ? 1156 LEU   B CB    1 
ATOM   12471 C  CG    . LEU   B 1 1156 ? 132.050 182.844 116.410 1.00 24.00  ? 1156 LEU   B CG    1 
ATOM   12472 C  CD1   . LEU   B 1 1156 ? 132.874 182.203 115.308 1.00 37.57  ? 1156 LEU   B CD1   1 
ATOM   12473 C  CD2   . LEU   B 1 1156 ? 132.417 182.261 117.762 1.00 22.07  ? 1156 LEU   B CD2   1 
ATOM   12474 N  N     . LYS   B 1 1157 ? 131.557 187.425 115.923 1.00 41.02  ? 1157 LYS   B N     1 
ATOM   12475 C  CA    . LYS   B 1 1157 ? 131.870 188.843 116.059 1.00 40.91  ? 1157 LYS   B CA    1 
ATOM   12476 C  C     . LYS   B 1 1157 ? 130.760 189.577 116.800 1.00 44.32  ? 1157 LYS   B C     1 
ATOM   12477 O  O     . LYS   B 1 1157 ? 131.024 190.515 117.562 1.00 43.72  ? 1157 LYS   B O     1 
ATOM   12478 C  CB    . LYS   B 1 1157 ? 132.102 189.464 114.683 1.00 37.01  ? 1157 LYS   B CB    1 
ATOM   12479 C  CG    . LYS   B 1 1157 ? 133.507 189.255 114.150 1.00 43.80  ? 1157 LYS   B CG    1 
ATOM   12480 C  CD    . LYS   B 1 1157 ? 134.042 190.511 113.490 1.00 44.36  ? 1157 LYS   B CD    1 
ATOM   12481 C  CE    . LYS   B 1 1157 ? 133.606 190.600 112.039 1.00 43.31  ? 1157 LYS   B CE    1 
ATOM   12482 N  NZ    . LYS   B 1 1157 ? 134.637 191.275 111.207 1.00 44.85  ? 1157 LYS   B NZ    1 
ATOM   12483 N  N     . GLU   B 1 1158 ? 129.511 189.164 116.585 1.00 45.06  ? 1158 GLU   B N     1 
ATOM   12484 C  CA    . GLU   B 1 1158 ? 128.379 189.817 117.230 1.00 42.00  ? 1158 GLU   B CA    1 
ATOM   12485 C  C     . GLU   B 1 1158 ? 128.280 189.498 118.717 1.00 43.38  ? 1158 GLU   B C     1 
ATOM   12486 O  O     . GLU   B 1 1158 ? 127.851 190.353 119.499 1.00 48.07  ? 1158 GLU   B O     1 
ATOM   12487 C  CB    . GLU   B 1 1158 ? 127.083 189.419 116.524 1.00 43.83  ? 1158 GLU   B CB    1 
ATOM   12488 C  CG    . GLU   B 1 1158 ? 125.906 190.323 116.828 1.00 48.50  ? 1158 GLU   B CG    1 
ATOM   12489 C  CD    . GLU   B 1 1158 ? 124.628 189.545 117.062 1.00 54.07  ? 1158 GLU   B CD    1 
ATOM   12490 O  OE1   . GLU   B 1 1158 ? 124.713 188.380 117.503 1.00 55.81  ? 1158 GLU   B OE1   1 
ATOM   12491 O  OE2   . GLU   B 1 1158 ? 123.538 190.099 116.811 1.00 53.22  ? 1158 GLU   B OE2   1 
ATOM   12492 N  N     . HIS   B 1 1159 ? 128.663 188.291 119.129 1.00 41.32  ? 1159 HIS   B N     1 
ATOM   12493 C  CA    . HIS   B 1 1159 ? 128.463 187.838 120.501 1.00 34.29  ? 1159 HIS   B CA    1 
ATOM   12494 C  C     . HIS   B 1 1159 ? 129.753 187.696 121.294 1.00 40.82  ? 1159 HIS   B C     1 
ATOM   12495 O  O     . HIS   B 1 1159 ? 129.851 188.216 122.409 1.00 41.56  ? 1159 HIS   B O     1 
ATOM   12496 C  CB    . HIS   B 1 1159 ? 127.712 186.498 120.502 1.00 29.65  ? 1159 HIS   B CB    1 
ATOM   12497 C  CG    . HIS   B 1 1159 ? 126.255 186.620 120.178 1.00 41.66  ? 1159 HIS   B CG    1 
ATOM   12498 N  ND1   . HIS   B 1 1159 ? 125.462 187.626 120.686 1.00 43.66  ? 1159 HIS   B ND1   1 
ATOM   12499 C  CD2   . HIS   B 1 1159 ? 125.448 185.861 119.401 1.00 40.25  ? 1159 HIS   B CD2   1 
ATOM   12500 C  CE1   . HIS   B 1 1159 ? 124.228 187.481 120.236 1.00 38.50  ? 1159 HIS   B CE1   1 
ATOM   12501 N  NE2   . HIS   B 1 1159 ? 124.194 186.418 119.453 1.00 36.56  ? 1159 HIS   B NE2   1 
ATOM   12502 N  N     . SER   B 1 1160 ? 130.754 187.006 120.748 1.00 44.81  ? 1160 SER   B N     1 
ATOM   12503 C  CA    . SER   B 1 1160 ? 131.953 186.643 121.492 1.00 37.50  ? 1160 SER   B CA    1 
ATOM   12504 C  C     . SER   B 1 1160 ? 133.097 187.631 121.301 1.00 38.97  ? 1160 SER   B C     1 
ATOM   12505 O  O     . SER   B 1 1160 ? 134.240 187.310 121.643 1.00 42.59  ? 1160 SER   B O     1 
ATOM   12506 C  CB    . SER   B 1 1160 ? 132.412 185.239 121.095 1.00 37.88  ? 1160 SER   B CB    1 
ATOM   12507 O  OG    . SER   B 1 1160 ? 131.520 184.254 121.585 1.00 38.82  ? 1160 SER   B OG    1 
ATOM   12508 N  N     . SER   B 1 1161 ? 132.822 188.821 120.766 1.00 39.69  ? 1161 SER   B N     1 
ATOM   12509 C  CA    . SER   B 1 1161 ? 133.886 189.792 120.537 1.00 43.53  ? 1161 SER   B CA    1 
ATOM   12510 C  C     . SER   B 1 1161 ? 134.561 190.236 121.829 1.00 44.01  ? 1161 SER   B C     1 
ATOM   12511 O  O     . SER   B 1 1161 ? 135.678 190.762 121.780 1.00 45.50  ? 1161 SER   B O     1 
ATOM   12512 C  CB    . SER   B 1 1161 ? 133.334 191.011 119.797 1.00 43.93  ? 1161 SER   B CB    1 
ATOM   12513 O  OG    . SER   B 1 1161 ? 132.649 191.878 120.684 1.00 46.81  ? 1161 SER   B OG    1 
ATOM   12514 N  N     . THR   B 1 1162 ? 133.914 190.044 122.977 1.00 43.57  ? 1162 THR   B N     1 
ATOM   12515 C  CA    . THR   B 1 1162 ? 134.455 190.467 124.262 1.00 45.28  ? 1162 THR   B CA    1 
ATOM   12516 C  C     . THR   B 1 1162 ? 134.971 189.304 125.099 1.00 47.82  ? 1162 THR   B C     1 
ATOM   12517 O  O     . THR   B 1 1162 ? 135.329 189.503 126.264 1.00 48.16  ? 1162 THR   B O     1 
ATOM   12518 C  CB    . THR   B 1 1162 ? 133.397 191.241 125.052 1.00 49.01  ? 1162 THR   B CB    1 
ATOM   12519 O  OG1   . THR   B 1 1162 ? 132.140 190.558 124.964 1.00 52.77  ? 1162 THR   B OG1   1 
ATOM   12520 C  CG2   . THR   B 1 1162 ? 133.242 192.647 124.498 1.00 48.91  ? 1162 THR   B CG2   1 
ATOM   12521 N  N     . ALA   B 1 1163 ? 135.017 188.098 124.540 1.00 44.57  ? 1163 ALA   B N     1 
ATOM   12522 C  CA    . ALA   B 1 1163 ? 135.466 186.941 125.298 1.00 40.35  ? 1163 ALA   B CA    1 
ATOM   12523 C  C     . ALA   B 1 1163 ? 136.979 186.959 125.480 1.00 42.15  ? 1163 ALA   B C     1 
ATOM   12524 O  O     . ALA   B 1 1163 ? 137.725 187.473 124.642 1.00 50.69  ? 1163 ALA   B O     1 
ATOM   12525 C  CB    . ALA   B 1 1163 ? 135.044 185.648 124.601 1.00 35.23  ? 1163 ALA   B CB    1 
ATOM   12526 N  N     . ASN   B 1 1164 ? 137.431 186.387 126.598 1.00 36.04  ? 1164 ASN   B N     1 
ATOM   12527 C  CA    . ASN   B 1 1164 ? 138.863 186.187 126.791 1.00 36.49  ? 1164 ASN   B CA    1 
ATOM   12528 C  C     . ASN   B 1 1164 ? 139.388 185.102 125.861 1.00 37.15  ? 1164 ASN   B C     1 
ATOM   12529 O  O     . ASN   B 1 1164 ? 140.499 185.212 125.330 1.00 44.33  ? 1164 ASN   B O     1 
ATOM   12530 C  CB    . ASN   B 1 1164 ? 139.154 185.833 128.249 1.00 34.62  ? 1164 ASN   B CB    1 
ATOM   12531 C  CG    . ASN   B 1 1164 ? 139.165 187.047 129.153 1.00 41.18  ? 1164 ASN   B CG    1 
ATOM   12532 O  OD1   . ASN   B 1 1164 ? 138.521 188.056 128.867 1.00 45.36  ? 1164 ASN   B OD1   1 
ATOM   12533 N  ND2   . ASN   B 1 1164 ? 139.896 186.955 130.257 1.00 45.01  ? 1164 ASN   B ND2   1 
ATOM   12534 N  N     . ILE   B 1 1165 ? 138.602 184.047 125.655 1.00 38.11  ? 1165 ILE   B N     1 
ATOM   12535 C  CA    . ILE   B 1 1165 ? 138.941 182.987 124.716 1.00 37.30  ? 1165 ILE   B CA    1 
ATOM   12536 C  C     . ILE   B 1 1165 ? 137.648 182.437 124.139 1.00 33.85  ? 1165 ILE   B C     1 
ATOM   12537 O  O     . ILE   B 1 1165 ? 136.600 182.450 124.791 1.00 33.11  ? 1165 ILE   B O     1 
ATOM   12538 C  CB    . ILE   B 1 1165 ? 139.771 181.865 125.383 1.00 34.65  ? 1165 ILE   B CB    1 
ATOM   12539 C  CG1   . ILE   B 1 1165 ? 140.485 181.029 124.320 1.00 38.24  ? 1165 ILE   B CG1   1 
ATOM   12540 C  CG2   . ILE   B 1 1165 ? 138.880 180.981 126.237 1.00 32.74  ? 1165 ILE   B CG2   1 
ATOM   12541 C  CD1   . ILE   B 1 1165 ? 141.080 179.746 124.851 1.00 40.39  ? 1165 ILE   B CD1   1 
ATOM   12542 N  N     . ILE   B 1 1166 ? 137.723 181.957 122.902 1.00 20.80  ? 1166 ILE   B N     1 
ATOM   12543 C  CA    . ILE   B 1 1166 ? 136.601 181.317 122.231 1.00 19.39  ? 1166 ILE   B CA    1 
ATOM   12544 C  C     . ILE   B 1 1166 ? 136.987 179.880 121.929 1.00 19.16  ? 1166 ILE   B C     1 
ATOM   12545 O  O     . ILE   B 1 1166 ? 138.121 179.607 121.524 1.00 27.82  ? 1166 ILE   B O     1 
ATOM   12546 C  CB    . ILE   B 1 1166 ? 136.204 182.049 120.933 1.00 23.31  ? 1166 ILE   B CB    1 
ATOM   12547 C  CG1   . ILE   B 1 1166 ? 135.759 183.478 121.233 1.00 27.28  ? 1166 ILE   B CG1   1 
ATOM   12548 C  CG2   . ILE   B 1 1166 ? 135.100 181.291 120.219 1.00 17.44  ? 1166 ILE   B CG2   1 
ATOM   12549 C  CD1   . ILE   B 1 1166 ? 136.476 184.517 120.406 1.00 28.36  ? 1166 ILE   B CD1   1 
ATOM   12550 N  N     . VAL   B 1 1167 ? 136.054 178.960 122.144 1.00 21.34  ? 1167 VAL   B N     1 
ATOM   12551 C  CA    . VAL   B 1 1167 ? 136.208 177.572 121.732 1.00 16.52  ? 1167 VAL   B CA    1 
ATOM   12552 C  C     . VAL   B 1 1167 ? 135.055 177.255 120.795 1.00 20.66  ? 1167 VAL   B C     1 
ATOM   12553 O  O     . VAL   B 1 1167 ? 133.886 177.426 121.163 1.00 34.64  ? 1167 VAL   B O     1 
ATOM   12554 C  CB    . VAL   B 1 1167 ? 136.229 176.611 122.930 1.00 13.79  ? 1167 VAL   B CB    1 
ATOM   12555 C  CG1   . VAL   B 1 1167 ? 136.338 175.174 122.453 1.00 14.71  ? 1167 VAL   B CG1   1 
ATOM   12556 C  CG2   . VAL   B 1 1167 ? 137.374 176.955 123.860 1.00 18.71  ? 1167 VAL   B CG2   1 
ATOM   12557 N  N     . MET   B 1 1168 ? 135.379 176.793 119.592 1.00 21.67  ? 1168 MET   B N     1 
ATOM   12558 C  CA    . MET   B 1 1168 ? 134.378 176.539 118.570 1.00 14.36  ? 1168 MET   B CA    1 
ATOM   12559 C  C     . MET   B 1 1168 ? 134.615 175.162 117.973 1.00 17.57  ? 1168 MET   B C     1 
ATOM   12560 O  O     . MET   B 1 1168 ? 135.710 174.604 118.069 1.00 30.72  ? 1168 MET   B O     1 
ATOM   12561 C  CB    . MET   B 1 1168 ? 134.409 177.622 117.478 1.00 17.27  ? 1168 MET   B CB    1 
ATOM   12562 C  CG    . MET   B 1 1168 ? 133.739 177.235 116.170 1.00 29.81  ? 1168 MET   B CG    1 
ATOM   12563 S  SD    . MET   B 1 1168 ? 131.959 177.512 116.192 1.00 46.45  ? 1168 MET   B SD    1 
ATOM   12564 C  CE    . MET   B 1 1168 ? 131.890 179.300 116.230 1.00 29.12  ? 1168 MET   B CE    1 
ATOM   12565 N  N     . SER   B 1 1169 ? 133.565 174.605 117.378 1.00 23.32  ? 1169 SER   B N     1 
ATOM   12566 C  CA    . SER   B 1 1169 ? 133.677 173.303 116.736 1.00 26.13  ? 1169 SER   B CA    1 
ATOM   12567 C  C     . SER   B 1 1169 ? 134.445 173.432 115.428 1.00 29.27  ? 1169 SER   B C     1 
ATOM   12568 O  O     . SER   B 1 1169 ? 134.141 174.292 114.597 1.00 38.66  ? 1169 SER   B O     1 
ATOM   12569 C  CB    . SER   B 1 1169 ? 132.290 172.717 116.483 1.00 30.11  ? 1169 SER   B CB    1 
ATOM   12570 O  OG    . SER   B 1 1169 ? 131.773 172.119 117.657 1.00 34.05  ? 1169 SER   B OG    1 
ATOM   12571 N  N     . LEU   B 1 1170 ? 135.440 172.574 115.246 1.00 26.04  ? 1170 LEU   B N     1 
ATOM   12572 C  CA    . LEU   B 1 1170 ? 136.264 172.626 114.047 1.00 23.92  ? 1170 LEU   B CA    1 
ATOM   12573 C  C     . LEU   B 1 1170 ? 135.538 171.950 112.891 1.00 25.70  ? 1170 LEU   B C     1 
ATOM   12574 O  O     . LEU   B 1 1170 ? 135.196 170.767 112.997 1.00 30.66  ? 1170 LEU   B O     1 
ATOM   12575 C  CB    . LEU   B 1 1170 ? 137.605 171.953 114.293 1.00 28.29  ? 1170 LEU   B CB    1 
ATOM   12576 C  CG    . LEU   B 1 1170 ? 138.517 171.795 113.076 1.00 26.29  ? 1170 LEU   B CG    1 
ATOM   12577 C  CD1   . LEU   B 1 1170 ? 139.291 173.072 112.812 1.00 26.35  ? 1170 LEU   B CD1   1 
ATOM   12578 C  CD2   . LEU   B 1 1170 ? 139.466 170.629 113.277 1.00 24.05  ? 1170 LEU   B CD2   1 
ATOM   12579 N  N     . PRO   B 1 1171 ? 135.288 172.646 111.784 1.00 21.32  ? 1171 PRO   B N     1 
ATOM   12580 C  CA    . PRO   B 1 1171 ? 134.609 172.005 110.651 1.00 21.01  ? 1171 PRO   B CA    1 
ATOM   12581 C  C     . PRO   B 1 1171 ? 135.472 170.895 110.070 1.00 26.93  ? 1171 PRO   B C     1 
ATOM   12582 O  O     . PRO   B 1 1171 ? 136.682 171.054 109.901 1.00 38.07  ? 1171 PRO   B O     1 
ATOM   12583 C  CB    . PRO   B 1 1171 ? 134.405 173.151 109.651 1.00 24.09  ? 1171 PRO   B CB    1 
ATOM   12584 C  CG    . PRO   B 1 1171 ? 134.885 174.400 110.334 1.00 23.78  ? 1171 PRO   B CG    1 
ATOM   12585 C  CD    . PRO   B 1 1171 ? 135.764 173.999 111.461 1.00 19.46  ? 1171 PRO   B CD    1 
ATOM   12586 N  N     . VAL   B 1 1172 ? 134.840 169.766 109.767 1.00 27.76  ? 1172 VAL   B N     1 
ATOM   12587 C  CA    . VAL   B 1 1172 ? 135.521 168.616 109.187 1.00 29.52  ? 1172 VAL   B CA    1 
ATOM   12588 C  C     . VAL   B 1 1172 ? 135.125 168.509 107.723 1.00 34.53  ? 1172 VAL   B C     1 
ATOM   12589 O  O     . VAL   B 1 1172 ? 133.933 168.459 107.396 1.00 39.14  ? 1172 VAL   B O     1 
ATOM   12590 C  CB    . VAL   B 1 1172 ? 135.182 167.323 109.947 1.00 28.76  ? 1172 VAL   B CB    1 
ATOM   12591 C  CG1   . VAL   B 1 1172 ? 135.303 166.121 109.027 1.00 29.50  ? 1172 VAL   B CG1   1 
ATOM   12592 C  CG2   . VAL   B 1 1172 ? 136.087 167.168 111.153 1.00 31.55  ? 1172 VAL   B CG2   1 
ATOM   12593 N  N     . ALA   B 1 1173 ? 136.119 168.479 106.843 1.00 32.53  ? 1173 ALA   B N     1 
ATOM   12594 C  CA    . ALA   B 1 1173 ? 135.895 168.356 105.411 1.00 40.44  ? 1173 ALA   B CA    1 
ATOM   12595 C  C     . ALA   B 1 1173 ? 136.197 166.930 104.976 1.00 46.30  ? 1173 ALA   B C     1 
ATOM   12596 O  O     . ALA   B 1 1173 ? 137.256 166.388 105.305 1.00 46.88  ? 1173 ALA   B O     1 
ATOM   12597 C  CB    . ALA   B 1 1173 ? 136.765 169.344 104.634 1.00 41.03  ? 1173 ALA   B CB    1 
ATOM   12598 N  N     . ARG   B 1 1174 ? 135.265 166.326 104.244 1.00 48.01  ? 1174 ARG   B N     1 
ATOM   12599 C  CA    . ARG   B 1 1174 ? 135.480 164.975 103.746 1.00 44.70  ? 1174 ARG   B CA    1 
ATOM   12600 C  C     . ARG   B 1 1174 ? 136.710 164.942 102.849 1.00 47.24  ? 1174 ARG   B C     1 
ATOM   12601 O  O     . ARG   B 1 1174 ? 136.883 165.799 101.979 1.00 45.99  ? 1174 ARG   B O     1 
ATOM   12602 C  CB    . ARG   B 1 1174 ? 134.249 164.490 102.982 1.00 45.49  ? 1174 ARG   B CB    1 
ATOM   12603 C  CG    . ARG   B 1 1174 ? 134.188 162.983 102.801 1.00 46.21  ? 1174 ARG   B CG    1 
ATOM   12604 C  CD    . ARG   B 1 1174 ? 132.770 162.519 102.521 1.00 47.10  ? 1174 ARG   B CD    1 
ATOM   12605 N  NE    . ARG   B 1 1174 ? 132.120 161.986 103.712 1.00 47.77  ? 1174 ARG   B NE    1 
ATOM   12606 C  CZ    . ARG   B 1 1174 ? 131.032 162.504 104.264 1.00 53.02  ? 1174 ARG   B CZ    1 
ATOM   12607 N  NH1   . ARG   B 1 1174 ? 130.450 163.581 103.763 1.00 53.80  ? 1174 ARG   B NH1   1 
ATOM   12608 N  NH2   . ARG   B 1 1174 ? 130.516 161.929 105.346 1.00 51.72  ? 1174 ARG   B NH2   1 
ATOM   12609 N  N     . LYS   B 1 1175 ? 137.567 163.949 103.065 1.00 49.27  ? 1175 LYS   B N     1 
ATOM   12610 C  CA    . LYS   B 1 1175 ? 138.794 163.835 102.291 1.00 50.03  ? 1175 LYS   B CA    1 
ATOM   12611 C  C     . LYS   B 1 1175 ? 138.481 163.323 100.891 1.00 53.31  ? 1175 LYS   B C     1 
ATOM   12612 O  O     . LYS   B 1 1175 ? 137.833 162.284 100.728 1.00 52.94  ? 1175 LYS   B O     1 
ATOM   12613 C  CB    . LYS   B 1 1175 ? 139.786 162.912 102.998 1.00 46.65  ? 1175 LYS   B CB    1 
ATOM   12614 C  CG    . LYS   B 1 1175 ? 139.365 161.455 103.048 1.00 49.61  ? 1175 LYS   B CG    1 
ATOM   12615 C  CD    . LYS   B 1 1175 ? 140.564 160.552 103.284 1.00 49.39  ? 1175 LYS   B CD    1 
ATOM   12616 C  CE    . LYS   B 1 1175 ? 140.156 159.091 103.328 1.00 50.15  ? 1175 LYS   B CE    1 
ATOM   12617 N  NZ    . LYS   B 1 1175 ? 139.841 158.653 104.715 1.00 49.69  ? 1175 LYS   B NZ    1 
ATOM   12618 N  N     . GLY   B 1 1176 ? 138.944 164.056 99.882  1.00 49.02  ? 1176 GLY   B N     1 
ATOM   12619 C  CA    . GLY   B 1 1176 ? 138.638 163.755 98.502  1.00 47.95  ? 1176 GLY   B CA    1 
ATOM   12620 C  C     . GLY   B 1 1176 ? 137.480 164.541 97.928  1.00 51.92  ? 1176 GLY   B C     1 
ATOM   12621 O  O     . GLY   B 1 1176 ? 137.316 164.563 96.702  1.00 54.18  ? 1176 GLY   B O     1 
ATOM   12622 N  N     . ALA   B 1 1177 ? 136.677 165.187 98.772  1.00 55.29  ? 1177 ALA   B N     1 
ATOM   12623 C  CA    . ALA   B 1 1177 ? 135.536 165.970 98.317  1.00 51.64  ? 1177 ALA   B CA    1 
ATOM   12624 C  C     . ALA   B 1 1177 ? 135.807 167.465 98.272  1.00 51.86  ? 1177 ALA   B C     1 
ATOM   12625 O  O     . ALA   B 1 1177 ? 135.241 168.160 97.422  1.00 55.80  ? 1177 ALA   B O     1 
ATOM   12626 C  CB    . ALA   B 1 1177 ? 134.323 165.710 99.217  1.00 51.13  ? 1177 ALA   B CB    1 
ATOM   12627 N  N     . VAL   B 1 1178 ? 136.652 167.977 99.163  1.00 45.00  ? 1178 VAL   B N     1 
ATOM   12628 C  CA    . VAL   B 1 1178 ? 136.950 169.400 99.252  1.00 43.14  ? 1178 VAL   B CA    1 
ATOM   12629 C  C     . VAL   B 1 1178 ? 138.438 169.606 99.018  1.00 44.75  ? 1178 VAL   B C     1 
ATOM   12630 O  O     . VAL   B 1 1178 ? 139.269 168.869 99.559  1.00 45.14  ? 1178 VAL   B O     1 
ATOM   12631 C  CB    . VAL   B 1 1178 ? 136.531 169.985 100.616 1.00 45.25  ? 1178 VAL   B CB    1 
ATOM   12632 C  CG1   . VAL   B 1 1178 ? 136.355 171.485 100.513 1.00 42.98  ? 1178 VAL   B CG1   1 
ATOM   12633 C  CG2   . VAL   B 1 1178 ? 135.251 169.330 101.105 1.00 47.28  ? 1178 VAL   B CG2   1 
ATOM   12634 N  N     . SER   B 1 1179 ? 138.771 170.609 98.211  1.00 44.41  ? 1179 SER   B N     1 
ATOM   12635 C  CA    . SER   B 1 1179 ? 140.166 170.935 97.965  1.00 41.23  ? 1179 SER   B CA    1 
ATOM   12636 C  C     . SER   B 1 1179 ? 140.797 171.558 99.208  1.00 48.08  ? 1179 SER   B C     1 
ATOM   12637 O  O     . SER   B 1 1179 ? 140.114 172.088 100.089 1.00 52.41  ? 1179 SER   B O     1 
ATOM   12638 C  CB    . SER   B 1 1179 ? 140.294 171.884 96.774  1.00 48.91  ? 1179 SER   B CB    1 
ATOM   12639 O  OG    . SER   B 1 1179 ? 140.223 173.238 97.185  1.00 48.45  ? 1179 SER   B OG    1 
ATOM   12640 N  N     . SER   B 1 1180 ? 142.128 171.489 99.269  1.00 38.34  ? 1180 SER   B N     1 
ATOM   12641 C  CA    . SER   B 1 1180 ? 142.845 172.028 100.420 1.00 34.42  ? 1180 SER   B CA    1 
ATOM   12642 C  C     . SER   B 1 1180 ? 142.650 173.535 100.538 1.00 36.84  ? 1180 SER   B C     1 
ATOM   12643 O  O     . SER   B 1 1180 ? 142.475 174.064 101.643 1.00 43.26  ? 1180 SER   B O     1 
ATOM   12644 C  CB    . SER   B 1 1180 ? 144.331 171.684 100.317 1.00 37.58  ? 1180 SER   B CB    1 
ATOM   12645 O  OG    . SER   B 1 1180 ? 144.598 170.403 100.860 1.00 46.14  ? 1180 SER   B OG    1 
ATOM   12646 N  N     . ALA   B 1 1181 ? 142.676 174.245 99.408  1.00 29.78  ? 1181 ALA   B N     1 
ATOM   12647 C  CA    . ALA   B 1 1181 ? 142.521 175.694 99.447  1.00 33.50  ? 1181 ALA   B CA    1 
ATOM   12648 C  C     . ALA   B 1 1181 ? 141.158 176.088 100.001 1.00 41.79  ? 1181 ALA   B C     1 
ATOM   12649 O  O     . ALA   B 1 1181 ? 141.046 177.051 100.768 1.00 49.54  ? 1181 ALA   B O     1 
ATOM   12650 C  CB    . ALA   B 1 1181 ? 142.726 176.284 98.052  1.00 36.43  ? 1181 ALA   B CB    1 
ATOM   12651 N  N     . LEU   B 1 1182 ? 140.108 175.353 99.630  1.00 35.57  ? 1182 LEU   B N     1 
ATOM   12652 C  CA    . LEU   B 1 1182 ? 138.779 175.679 100.135 1.00 31.58  ? 1182 LEU   B CA    1 
ATOM   12653 C  C     . LEU   B 1 1182 ? 138.666 175.383 101.626 1.00 36.33  ? 1182 LEU   B C     1 
ATOM   12654 O  O     . LEU   B 1 1182 ? 138.004 176.122 102.359 1.00 42.48  ? 1182 LEU   B O     1 
ATOM   12655 C  CB    . LEU   B 1 1182 ? 137.710 174.924 99.348  1.00 40.98  ? 1182 LEU   B CB    1 
ATOM   12656 C  CG    . LEU   B 1 1182 ? 136.275 175.141 99.830  1.00 41.40  ? 1182 LEU   B CG    1 
ATOM   12657 C  CD1   . LEU   B 1 1182 ? 135.815 176.549 99.495  1.00 36.46  ? 1182 LEU   B CD1   1 
ATOM   12658 C  CD2   . LEU   B 1 1182 ? 135.342 174.122 99.207  1.00 38.21  ? 1182 LEU   B CD2   1 
ATOM   12659 N  N     . TYR   B 1 1183 ? 139.296 174.303 102.092 1.00 36.57  ? 1183 TYR   B N     1 
ATOM   12660 C  CA    . TYR   B 1 1183 ? 139.355 174.037 103.528 1.00 26.00  ? 1183 TYR   B CA    1 
ATOM   12661 C  C     . TYR   B 1 1183 ? 140.028 175.189 104.267 1.00 25.04  ? 1183 TYR   B C     1 
ATOM   12662 O  O     . TYR   B 1 1183 ? 139.527 175.674 105.292 1.00 37.16  ? 1183 TYR   B O     1 
ATOM   12663 C  CB    . TYR   B 1 1183 ? 140.105 172.728 103.777 1.00 28.44  ? 1183 TYR   B CB    1 
ATOM   12664 C  CG    . TYR   B 1 1183 ? 139.713 171.994 105.039 1.00 28.32  ? 1183 TYR   B CG    1 
ATOM   12665 C  CD1   . TYR   B 1 1183 ? 139.104 172.655 106.096 1.00 31.17  ? 1183 TYR   B CD1   1 
ATOM   12666 C  CD2   . TYR   B 1 1183 ? 139.968 170.635 105.177 1.00 29.25  ? 1183 TYR   B CD2   1 
ATOM   12667 C  CE1   . TYR   B 1 1183 ? 138.750 171.982 107.250 1.00 31.30  ? 1183 TYR   B CE1   1 
ATOM   12668 C  CE2   . TYR   B 1 1183 ? 139.619 169.955 106.326 1.00 28.49  ? 1183 TYR   B CE2   1 
ATOM   12669 C  CZ    . TYR   B 1 1183 ? 139.011 170.632 107.359 1.00 35.44  ? 1183 TYR   B CZ    1 
ATOM   12670 O  OH    . TYR   B 1 1183 ? 138.664 169.955 108.504 1.00 42.03  ? 1183 TYR   B OH    1 
ATOM   12671 N  N     . MET   B 1 1184 ? 141.179 175.633 103.758 1.00 29.80  ? 1184 MET   B N     1 
ATOM   12672 C  CA    . MET   B 1 1184 ? 141.891 176.738 104.389 1.00 30.82  ? 1184 MET   B CA    1 
ATOM   12673 C  C     . MET   B 1 1184 ? 141.046 178.004 104.396 1.00 37.62  ? 1184 MET   B C     1 
ATOM   12674 O  O     . MET   B 1 1184 ? 141.033 178.748 105.384 1.00 33.45  ? 1184 MET   B O     1 
ATOM   12675 C  CB    . MET   B 1 1184 ? 143.220 176.976 103.672 1.00 31.20  ? 1184 MET   B CB    1 
ATOM   12676 C  CG    . MET   B 1 1184 ? 144.132 177.968 104.364 1.00 37.15  ? 1184 MET   B CG    1 
ATOM   12677 S  SD    . MET   B 1 1184 ? 144.243 177.687 106.139 1.00 55.62  ? 1184 MET   B SD    1 
ATOM   12678 C  CE    . MET   B 1 1184 ? 145.052 176.092 106.165 1.00 40.12  ? 1184 MET   B CE    1 
ATOM   12679 N  N     . ALA   B 1 1185 ? 140.336 178.269 103.297 1.00 36.64  ? 1185 ALA   B N     1 
ATOM   12680 C  CA    . ALA   B 1 1185 ? 139.473 179.443 103.237 1.00 29.48  ? 1185 ALA   B CA    1 
ATOM   12681 C  C     . ALA   B 1 1185 ? 138.308 179.323 104.211 1.00 33.01  ? 1185 ALA   B C     1 
ATOM   12682 O  O     . ALA   B 1 1185 ? 137.887 180.320 104.805 1.00 35.39  ? 1185 ALA   B O     1 
ATOM   12683 C  CB    . ALA   B 1 1185 ? 138.964 179.652 101.812 1.00 29.60  ? 1185 ALA   B CB    1 
ATOM   12684 N  N     . TRP   B 1 1186 ? 137.772 178.115 104.385 1.00 32.06  ? 1186 TRP   B N     1 
ATOM   12685 C  CA    . TRP   B 1 1186 ? 136.736 177.902 105.389 1.00 22.57  ? 1186 TRP   B CA    1 
ATOM   12686 C  C     . TRP   B 1 1186 ? 137.250 178.264 106.774 1.00 28.00  ? 1186 TRP   B C     1 
ATOM   12687 O  O     . TRP   B 1 1186 ? 136.580 178.970 107.537 1.00 29.45  ? 1186 TRP   B O     1 
ATOM   12688 C  CB    . TRP   B 1 1186 ? 136.269 176.447 105.369 1.00 23.54  ? 1186 TRP   B CB    1 
ATOM   12689 C  CG    . TRP   B 1 1186 ? 135.287 176.112 104.295 1.00 26.06  ? 1186 TRP   B CG    1 
ATOM   12690 C  CD1   . TRP   B 1 1186 ? 134.650 176.980 103.460 1.00 27.10  ? 1186 TRP   B CD1   1 
ATOM   12691 C  CD2   . TRP   B 1 1186 ? 134.820 174.804 103.949 1.00 25.45  ? 1186 TRP   B CD2   1 
ATOM   12692 N  NE1   . TRP   B 1 1186 ? 133.820 176.293 102.609 1.00 27.67  ? 1186 TRP   B NE1   1 
ATOM   12693 C  CE2   . TRP   B 1 1186 ? 133.905 174.955 102.890 1.00 27.08  ? 1186 TRP   B CE2   1 
ATOM   12694 C  CE3   . TRP   B 1 1186 ? 135.089 173.520 104.431 1.00 27.14  ? 1186 TRP   B CE3   1 
ATOM   12695 C  CZ2   . TRP   B 1 1186 ? 133.258 173.870 102.305 1.00 31.75  ? 1186 TRP   B CZ2   1 
ATOM   12696 C  CZ3   . TRP   B 1 1186 ? 134.446 172.445 103.849 1.00 30.31  ? 1186 TRP   B CZ3   1 
ATOM   12697 C  CH2   . TRP   B 1 1186 ? 133.541 172.627 102.798 1.00 36.13  ? 1186 TRP   B CH2   1 
ATOM   12698 N  N     . LEU   B 1 1187 ? 138.445 177.780 107.115 1.00 31.72  ? 1187 LEU   B N     1 
ATOM   12699 C  CA    . LEU   B 1 1187 ? 139.010 178.088 108.426 1.00 24.61  ? 1187 LEU   B CA    1 
ATOM   12700 C  C     . LEU   B 1 1187 ? 139.247 179.585 108.587 1.00 28.30  ? 1187 LEU   B C     1 
ATOM   12701 O  O     . LEU   B 1 1187 ? 138.942 180.163 109.639 1.00 32.70  ? 1187 LEU   B O     1 
ATOM   12702 C  CB    . LEU   B 1 1187 ? 140.308 177.309 108.638 1.00 24.95  ? 1187 LEU   B CB    1 
ATOM   12703 C  CG    . LEU   B 1 1187 ? 140.164 175.787 108.672 1.00 26.89  ? 1187 LEU   B CG    1 
ATOM   12704 C  CD1   . LEU   B 1 1187 ? 141.436 175.135 109.186 1.00 27.33  ? 1187 LEU   B CD1   1 
ATOM   12705 C  CD2   . LEU   B 1 1187 ? 138.972 175.382 109.522 1.00 28.05  ? 1187 LEU   B CD2   1 
ATOM   12706 N  N     . GLU   B 1 1188 ? 139.781 180.233 107.549 1.00 30.94  ? 1188 GLU   B N     1 
ATOM   12707 C  CA    . GLU   B 1 1188 ? 140.029 181.670 107.618 1.00 34.29  ? 1188 GLU   B CA    1 
ATOM   12708 C  C     . GLU   B 1 1188 ? 138.735 182.451 107.799 1.00 37.48  ? 1188 GLU   B C     1 
ATOM   12709 O  O     . GLU   B 1 1188 ? 138.669 183.380 108.613 1.00 35.65  ? 1188 GLU   B O     1 
ATOM   12710 C  CB    . GLU   B 1 1188 ? 140.762 182.137 106.362 1.00 25.88  ? 1188 GLU   B CB    1 
ATOM   12711 C  CG    . GLU   B 1 1188 ? 140.979 183.641 106.304 1.00 32.97  ? 1188 GLU   B CG    1 
ATOM   12712 C  CD    . GLU   B 1 1188 ? 142.195 184.087 107.085 1.00 43.37  ? 1188 GLU   B CD    1 
ATOM   12713 O  OE1   . GLU   B 1 1188 ? 143.246 183.422 106.976 1.00 41.87  ? 1188 GLU   B OE1   1 
ATOM   12714 O  OE2   . GLU   B 1 1188 ? 142.101 185.099 107.810 1.00 43.96  ? 1188 GLU   B OE2   1 
ATOM   12715 N  N     . ALA   B 1 1189 ? 137.696 182.098 107.041 1.00 29.85  ? 1189 ALA   B N     1 
ATOM   12716 C  CA    . ALA   B 1 1189 ? 136.412 182.770 107.191 1.00 28.24  ? 1189 ALA   B CA    1 
ATOM   12717 C  C     . ALA   B 1 1189 ? 135.845 182.557 108.586 1.00 32.97  ? 1189 ALA   B C     1 
ATOM   12718 O  O     . ALA   B 1 1189 ? 135.320 183.492 109.200 1.00 41.60  ? 1189 ALA   B O     1 
ATOM   12719 C  CB    . ALA   B 1 1189 ? 135.432 182.272 106.129 1.00 28.08  ? 1189 ALA   B CB    1 
ATOM   12720 N  N     . LEU   B 1 1190 ? 135.942 181.331 109.105 1.00 23.45  ? 1190 LEU   B N     1 
ATOM   12721 C  CA    . LEU   B 1 1190 ? 135.428 181.053 110.440 1.00 21.99  ? 1190 LEU   B CA    1 
ATOM   12722 C  C     . LEU   B 1 1190 ? 136.129 181.909 111.486 1.00 35.07  ? 1190 LEU   B C     1 
ATOM   12723 O  O     . LEU   B 1 1190 ? 135.477 182.546 112.322 1.00 32.42  ? 1190 LEU   B O     1 
ATOM   12724 C  CB    . LEU   B 1 1190 ? 135.588 179.568 110.763 1.00 24.27  ? 1190 LEU   B CB    1 
ATOM   12725 C  CG    . LEU   B 1 1190 ? 134.914 179.100 112.053 1.00 33.51  ? 1190 LEU   B CG    1 
ATOM   12726 C  CD1   . LEU   B 1 1190 ? 133.450 179.509 112.063 1.00 28.75  ? 1190 LEU   B CD1   1 
ATOM   12727 C  CD2   . LEU   B 1 1190 ? 135.056 177.597 112.221 1.00 29.64  ? 1190 LEU   B CD2   1 
ATOM   12728 N  N     . SER   B 1 1191 ? 137.459 181.942 111.454 1.00 34.02  ? 1191 SER   B N     1 
ATOM   12729 C  CA    . SER   B 1 1191 ? 138.248 182.679 112.434 1.00 24.05  ? 1191 SER   B CA    1 
ATOM   12730 C  C     . SER   B 1 1191 ? 138.926 183.866 111.763 1.00 37.69  ? 1191 SER   B C     1 
ATOM   12731 O  O     . SER   B 1 1191 ? 139.771 183.686 110.880 1.00 52.92  ? 1191 SER   B O     1 
ATOM   12732 C  CB    . SER   B 1 1191 ? 139.286 181.770 113.089 1.00 28.83  ? 1191 SER   B CB    1 
ATOM   12733 O  OG    . SER   B 1 1191 ? 139.729 180.774 112.186 1.00 44.49  ? 1191 SER   B OG    1 
ATOM   12734 N  N     . LYS   B 1 1192 ? 138.560 185.073 112.187 1.00 37.52  ? 1192 LYS   B N     1 
ATOM   12735 C  CA    . LYS   B 1 1192 ? 139.226 186.287 111.739 1.00 39.14  ? 1192 LYS   B CA    1 
ATOM   12736 C  C     . LYS   B 1 1192 ? 138.680 187.460 112.538 1.00 41.10  ? 1192 LYS   B C     1 
ATOM   12737 O  O     . LYS   B 1 1192 ? 137.504 187.472 112.912 1.00 48.15  ? 1192 LYS   B O     1 
ATOM   12738 C  CB    . LYS   B 1 1192 ? 139.026 186.519 110.236 1.00 30.70  ? 1192 LYS   B CB    1 
ATOM   12739 C  CG    . LYS   B 1 1192 ? 137.695 186.022 109.704 1.00 36.04  ? 1192 LYS   B CG    1 
ATOM   12740 C  CD    . LYS   B 1 1192 ? 137.417 186.573 108.319 1.00 44.52  ? 1192 LYS   B CD    1 
ATOM   12741 C  CE    . LYS   B 1 1192 ? 137.495 188.090 108.304 1.00 47.91  ? 1192 LYS   B CE    1 
ATOM   12742 N  NZ    . LYS   B 1 1192 ? 136.568 188.714 109.287 1.00 45.41  ? 1192 LYS   B NZ    1 
ATOM   12743 N  N     . ASP   B 1 1193 ? 139.542 188.446 112.784 1.00 50.43  ? 1193 ASP   B N     1 
ATOM   12744 C  CA    . ASP   B 1 1193 ? 139.179 189.625 113.568 1.00 45.27  ? 1193 ASP   B CA    1 
ATOM   12745 C  C     . ASP   B 1 1193 ? 138.463 189.218 114.854 1.00 45.22  ? 1193 ASP   B C     1 
ATOM   12746 O  O     . ASP   B 1 1193 ? 137.400 189.739 115.200 1.00 54.72  ? 1193 ASP   B O     1 
ATOM   12747 C  CB    . ASP   B 1 1193 ? 138.324 190.589 112.744 1.00 47.23  ? 1193 ASP   B CB    1 
ATOM   12748 C  CG    . ASP   B 1 1193 ? 138.738 190.636 111.287 1.00 54.13  ? 1193 ASP   B CG    1 
ATOM   12749 O  OD1   . ASP   B 1 1193 ? 139.944 190.809 111.016 1.00 54.79  ? 1193 ASP   B OD1   1 
ATOM   12750 O  OD2   . ASP   B 1 1193 ? 137.857 190.500 110.412 1.00 53.26  ? 1193 ASP   B OD2   1 
ATOM   12751 N  N     . LEU   B 1 1194 ? 139.057 188.270 115.563 1.00 34.13  ? 1194 LEU   B N     1 
ATOM   12752 C  CA    . LEU   B 1 1194 ? 138.471 187.669 116.748 1.00 37.97  ? 1194 LEU   B CA    1 
ATOM   12753 C  C     . LEU   B 1 1194 ? 139.505 187.592 117.858 1.00 41.98  ? 1194 LEU   B C     1 
ATOM   12754 O  O     . LEU   B 1 1194 ? 140.711 187.686 117.604 1.00 43.95  ? 1194 LEU   B O     1 
ATOM   12755 C  CB    . LEU   B 1 1194 ? 137.938 186.260 116.445 1.00 36.55  ? 1194 LEU   B CB    1 
ATOM   12756 C  CG    . LEU   B 1 1194 ? 136.501 186.155 115.932 1.00 38.82  ? 1194 LEU   B CG    1 
ATOM   12757 C  CD1   . LEU   B 1 1194 ? 136.140 184.706 115.657 1.00 34.46  ? 1194 LEU   B CD1   1 
ATOM   12758 C  CD2   . LEU   B 1 1194 ? 135.530 186.772 116.922 1.00 38.98  ? 1194 LEU   B CD2   1 
ATOM   12759 N  N     . PRO   B 1 1195 ? 139.065 187.433 119.101 1.00 40.77  ? 1195 PRO   B N     1 
ATOM   12760 C  CA    . PRO   B 1 1195 ? 140.003 187.162 120.192 1.00 36.61  ? 1195 PRO   B CA    1 
ATOM   12761 C  C     . PRO   B 1 1195 ? 140.634 185.794 120.016 1.00 39.33  ? 1195 PRO   B C     1 
ATOM   12762 O  O     . PRO   B 1 1195 ? 140.343 185.095 119.034 1.00 41.72  ? 1195 PRO   B O     1 
ATOM   12763 C  CB    . PRO   B 1 1195 ? 139.115 187.212 121.446 1.00 32.32  ? 1195 PRO   B CB    1 
ATOM   12764 C  CG    . PRO   B 1 1195 ? 137.857 187.905 121.011 1.00 38.18  ? 1195 PRO   B CG    1 
ATOM   12765 C  CD    . PRO   B 1 1195 ? 137.678 187.528 119.579 1.00 35.26  ? 1195 PRO   B CD    1 
ATOM   12766 N  N     . PRO   B 1 1196 ? 141.505 185.375 120.932 1.00 40.53  ? 1196 PRO   B N     1 
ATOM   12767 C  CA    . PRO   B 1 1196 ? 142.109 184.045 120.805 1.00 35.21  ? 1196 PRO   B CA    1 
ATOM   12768 C  C     . PRO   B 1 1196 ? 141.030 182.985 120.655 1.00 26.02  ? 1196 PRO   B C     1 
ATOM   12769 O  O     . PRO   B 1 1196 ? 140.022 182.994 121.364 1.00 27.95  ? 1196 PRO   B O     1 
ATOM   12770 C  CB    . PRO   B 1 1196 ? 142.888 183.880 122.114 1.00 28.29  ? 1196 PRO   B CB    1 
ATOM   12771 C  CG    . PRO   B 1 1196 ? 143.143 185.260 122.581 1.00 31.02  ? 1196 PRO   B CG    1 
ATOM   12772 C  CD    . PRO   B 1 1196 ? 141.985 186.093 122.124 1.00 33.34  ? 1196 PRO   B CD    1 
ATOM   12773 N  N     . ILE   B 1 1197 ? 141.239 182.067 119.716 1.00 29.66  ? 1197 ILE   B N     1 
ATOM   12774 C  CA    . ILE   B 1 1197 ? 140.215 181.093 119.370 1.00 26.15  ? 1197 ILE   B CA    1 
ATOM   12775 C  C     . ILE   B 1 1197 ? 140.841 179.715 119.220 1.00 25.97  ? 1197 ILE   B C     1 
ATOM   12776 O  O     . ILE   B 1 1197 ? 141.977 179.567 118.759 1.00 30.90  ? 1197 ILE   B O     1 
ATOM   12777 C  CB    . ILE   B 1 1197 ? 139.453 181.490 118.086 1.00 23.40  ? 1197 ILE   B CB    1 
ATOM   12778 C  CG1   . ILE   B 1 1197 ? 138.284 180.533 117.844 1.00 25.04  ? 1197 ILE   B CG1   1 
ATOM   12779 C  CG2   . ILE   B 1 1197 ? 140.391 181.517 116.896 1.00 21.66  ? 1197 ILE   B CG2   1 
ATOM   12780 C  CD1   . ILE   B 1 1197 ? 137.375 180.952 116.714 1.00 21.12  ? 1197 ILE   B CD1   1 
ATOM   12781 N  N     . LEU   B 1 1198 ? 140.084 178.704 119.633 1.00 22.78  ? 1198 LEU   B N     1 
ATOM   12782 C  CA    . LEU   B 1 1198 ? 140.478 177.306 119.517 1.00 18.01  ? 1198 LEU   B CA    1 
ATOM   12783 C  C     . LEU   B 1 1198 ? 139.392 176.574 118.743 1.00 24.50  ? 1198 LEU   B C     1 
ATOM   12784 O  O     . LEU   B 1 1198 ? 138.267 176.425 119.234 1.00 23.39  ? 1198 LEU   B O     1 
ATOM   12785 C  CB    . LEU   B 1 1198 ? 140.685 176.675 120.894 1.00 17.72  ? 1198 LEU   B CB    1 
ATOM   12786 C  CG    . LEU   B 1 1198 ? 142.071 176.815 121.526 1.00 27.36  ? 1198 LEU   B CG    1 
ATOM   12787 C  CD1   . LEU   B 1 1198 ? 142.337 178.253 121.928 1.00 30.54  ? 1198 LEU   B CD1   1 
ATOM   12788 C  CD2   . LEU   B 1 1198 ? 142.200 175.896 122.727 1.00 24.78  ? 1198 LEU   B CD2   1 
ATOM   12789 N  N     . LEU   B 1 1199 ? 139.725 176.124 117.537 1.00 25.04  ? 1199 LEU   B N     1 
ATOM   12790 C  CA    . LEU   B 1 1199 ? 138.838 175.273 116.753 1.00 17.89  ? 1199 LEU   B CA    1 
ATOM   12791 C  C     . LEU   B 1 1199 ? 139.151 173.830 117.121 1.00 20.10  ? 1199 LEU   B C     1 
ATOM   12792 O  O     . LEU   B 1 1199 ? 140.243 173.330 116.833 1.00 32.94  ? 1199 LEU   B O     1 
ATOM   12793 C  CB    . LEU   B 1 1199 ? 139.020 175.525 115.259 1.00 11.38  ? 1199 LEU   B CB    1 
ATOM   12794 C  CG    . LEU   B 1 1199 ? 139.066 176.996 114.842 1.00 20.89  ? 1199 LEU   B CG    1 
ATOM   12795 C  CD1   . LEU   B 1 1199 ? 139.298 177.135 113.347 1.00 21.44  ? 1199 LEU   B CD1   1 
ATOM   12796 C  CD2   . LEU   B 1 1199 ? 137.791 177.707 115.257 1.00 26.04  ? 1199 LEU   B CD2   1 
ATOM   12797 N  N     . VAL   B 1 1200 ? 138.203 173.167 117.776 1.00 19.55  ? 1200 VAL   B N     1 
ATOM   12798 C  CA    . VAL   B 1 1200 ? 138.417 171.849 118.356 1.00 19.28  ? 1200 VAL   B CA    1 
ATOM   12799 C  C     . VAL   B 1 1200 ? 137.503 170.854 117.661 1.00 22.05  ? 1200 VAL   B C     1 
ATOM   12800 O  O     . VAL   B 1 1200 ? 136.291 171.078 117.561 1.00 30.22  ? 1200 VAL   B O     1 
ATOM   12801 C  CB    . VAL   B 1 1200 ? 138.164 171.851 119.875 1.00 19.83  ? 1200 VAL   B CB    1 
ATOM   12802 C  CG1   . VAL   B 1 1200 ? 138.312 170.448 120.435 1.00 19.40  ? 1200 VAL   B CG1   1 
ATOM   12803 C  CG2   . VAL   B 1 1200 ? 139.114 172.811 120.567 1.00 21.10  ? 1200 VAL   B CG2   1 
ATOM   12804 N  N     . ARG   B 1 1201 ? 138.087 169.759 117.185 1.00 17.95  ? 1201 ARG   B N     1 
ATOM   12805 C  CA    . ARG   B 1 1201 ? 137.355 168.624 116.633 1.00 15.87  ? 1201 ARG   B CA    1 
ATOM   12806 C  C     . ARG   B 1 1201 ? 137.825 167.401 117.410 1.00 19.02  ? 1201 ARG   B C     1 
ATOM   12807 O  O     . ARG   B 1 1201 ? 138.938 166.915 117.194 1.00 30.32  ? 1201 ARG   B O     1 
ATOM   12808 C  CB    . ARG   B 1 1201 ? 137.604 168.467 115.138 1.00 30.12  ? 1201 ARG   B CB    1 
ATOM   12809 C  CG    . ARG   B 1 1201 ? 137.100 167.156 114.558 1.00 30.71  ? 1201 ARG   B CG    1 
ATOM   12810 C  CD    . ARG   B 1 1201 ? 135.607 167.005 114.757 1.00 20.31  ? 1201 ARG   B CD    1 
ATOM   12811 N  NE    . ARG   B 1 1201 ? 134.868 168.075 114.099 1.00 34.85  ? 1201 ARG   B NE    1 
ATOM   12812 C  CZ    . ARG   B 1 1201 ? 133.552 168.088 113.937 1.00 37.10  ? 1201 ARG   B CZ    1 
ATOM   12813 N  NH1   . ARG   B 1 1201 ? 132.793 167.091 114.360 1.00 34.71  ? 1201 ARG   B NH1   1 
ATOM   12814 N  NH2   . ARG   B 1 1201 ? 132.984 169.130 113.337 1.00 33.33  ? 1201 ARG   B NH2   1 
ATOM   12815 N  N     . GLY   B 1 1202 ? 136.991 166.921 118.323 1.00 25.56  ? 1202 GLY   B N     1 
ATOM   12816 C  CA    . GLY   B 1 1202 ? 137.355 165.788 119.140 1.00 9.01   ? 1202 GLY   B CA    1 
ATOM   12817 C  C     . GLY   B 1 1202 ? 137.394 164.505 118.336 1.00 23.13  ? 1202 GLY   B C     1 
ATOM   12818 O  O     . GLY   B 1 1202 ? 137.042 164.445 117.157 1.00 35.09  ? 1202 GLY   B O     1 
ATOM   12819 N  N     . ASN   B 1 1203 ? 137.835 163.445 119.009 1.00 22.66  ? 1203 ASN   B N     1 
ATOM   12820 C  CA    . ASN   B 1 1203 ? 137.984 162.143 118.375 1.00 25.74  ? 1203 ASN   B CA    1 
ATOM   12821 C  C     . ASN   B 1 1203 ? 136.645 161.470 118.101 1.00 29.28  ? 1203 ASN   B C     1 
ATOM   12822 O  O     . ASN   B 1 1203 ? 136.616 160.446 117.410 1.00 31.47  ? 1203 ASN   B O     1 
ATOM   12823 C  CB    . ASN   B 1 1203 ? 138.858 161.249 119.260 1.00 29.65  ? 1203 ASN   B CB    1 
ATOM   12824 C  CG    . ASN   B 1 1203 ? 139.056 159.861 118.689 1.00 35.37  ? 1203 ASN   B CG    1 
ATOM   12825 O  OD1   . ASN   B 1 1203 ? 139.435 158.935 119.406 1.00 38.45  ? 1203 ASN   B OD1   1 
ATOM   12826 N  ND2   . ASN   B 1 1203 ? 138.826 159.711 117.389 1.00 41.20  ? 1203 ASN   B ND2   1 
ATOM   12827 N  N     . HIS   B 1 1204 ? 135.546 162.020 118.615 1.00 39.08  ? 1204 HIS   B N     1 
ATOM   12828 C  CA    . HIS   B 1 1204 ? 134.203 161.458 118.509 1.00 33.76  ? 1204 HIS   B CA    1 
ATOM   12829 C  C     . HIS   B 1 1204 ? 133.997 160.259 119.421 1.00 35.48  ? 1204 HIS   B C     1 
ATOM   12830 O  O     . HIS   B 1 1204 ? 132.971 159.576 119.314 1.00 41.44  ? 1204 HIS   B O     1 
ATOM   12831 C  CB    . HIS   B 1 1204 ? 133.854 161.081 117.066 1.00 30.69  ? 1204 HIS   B CB    1 
ATOM   12832 C  CG    . HIS   B 1 1204 ? 133.279 162.213 116.276 1.00 35.11  ? 1204 HIS   B CG    1 
ATOM   12833 N  ND1   . HIS   B 1 1204 ? 131.924 162.445 116.191 1.00 35.70  ? 1204 HIS   B ND1   1 
ATOM   12834 C  CD2   . HIS   B 1 1204 ? 133.874 163.190 115.552 1.00 37.93  ? 1204 HIS   B CD2   1 
ATOM   12835 C  CE1   . HIS   B 1 1204 ? 131.708 163.509 115.439 1.00 34.20  ? 1204 HIS   B CE1   1 
ATOM   12836 N  NE2   . HIS   B 1 1204 ? 132.875 163.980 115.039 1.00 38.37  ? 1204 HIS   B NE2   1 
ATOM   12837 N  N     . GLN   B 1 1205 ? 134.940 159.984 120.313 1.00 32.91  ? 1205 GLN   B N     1 
ATOM   12838 C  CA    . GLN   B 1 1205 ? 134.754 159.025 121.389 1.00 35.26  ? 1205 GLN   B CA    1 
ATOM   12839 C  C     . GLN   B 1 1205 ? 134.422 159.784 122.664 1.00 37.77  ? 1205 GLN   B C     1 
ATOM   12840 O  O     . GLN   B 1 1205 ? 134.938 160.881 122.896 1.00 41.67  ? 1205 GLN   B O     1 
ATOM   12841 C  CB    . GLN   B 1 1205 ? 136.005 158.169 121.588 1.00 36.77  ? 1205 GLN   B CB    1 
ATOM   12842 C  CG    . GLN   B 1 1205 ? 136.476 157.474 120.326 1.00 38.90  ? 1205 GLN   B CG    1 
ATOM   12843 C  CD    . GLN   B 1 1205 ? 135.454 156.494 119.788 1.00 43.63  ? 1205 GLN   B CD    1 
ATOM   12844 O  OE1   . GLN   B 1 1205 ? 134.542 156.077 120.501 1.00 44.09  ? 1205 GLN   B OE1   1 
ATOM   12845 N  NE2   . GLN   B 1 1205 ? 135.599 156.122 118.522 1.00 43.94  ? 1205 GLN   B NE2   1 
ATOM   12846 N  N     . SER   B 1 1206 ? 133.552 159.202 123.484 1.00 34.19  ? 1206 SER   B N     1 
ATOM   12847 C  CA    . SER   B 1 1206 ? 133.057 159.907 124.658 1.00 25.42  ? 1206 SER   B CA    1 
ATOM   12848 C  C     . SER   B 1 1206 ? 134.212 160.306 125.565 1.00 30.47  ? 1206 SER   B C     1 
ATOM   12849 O  O     . SER   B 1 1206 ? 134.988 159.457 126.013 1.00 37.34  ? 1206 SER   B O     1 
ATOM   12850 C  CB    . SER   B 1 1206 ? 132.058 159.033 125.412 1.00 35.92  ? 1206 SER   B CB    1 
ATOM   12851 O  OG    . SER   B 1 1206 ? 130.749 159.568 125.316 1.00 43.03  ? 1206 SER   B OG    1 
ATOM   12852 N  N     . VAL   B 1 1207 ? 134.323 161.605 125.828 1.00 26.66  ? 1207 VAL   B N     1 
ATOM   12853 C  CA    . VAL   B 1 1207 ? 135.362 162.131 126.700 1.00 24.11  ? 1207 VAL   B CA    1 
ATOM   12854 C  C     . VAL   B 1 1207 ? 134.813 162.582 128.047 1.00 29.39  ? 1207 VAL   B C     1 
ATOM   12855 O  O     . VAL   B 1 1207 ? 135.593 162.714 129.003 1.00 28.16  ? 1207 VAL   B O     1 
ATOM   12856 C  CB    . VAL   B 1 1207 ? 136.125 163.285 126.016 1.00 10.18  ? 1207 VAL   B CB    1 
ATOM   12857 C  CG1   . VAL   B 1 1207 ? 136.243 164.482 126.941 1.00 23.26  ? 1207 VAL   B CG1   1 
ATOM   12858 C  CG2   . VAL   B 1 1207 ? 137.493 162.815 125.559 1.00 12.87  ? 1207 VAL   B CG2   1 
ATOM   12859 N  N     . LEU   B 1 1208 ? 133.508 162.802 128.161 1.00 23.30  ? 1208 LEU   B N     1 
ATOM   12860 C  CA    . LEU   B 1 1208 ? 132.852 163.131 129.413 1.00 15.11  ? 1208 LEU   B CA    1 
ATOM   12861 C  C     . LEU   B 1 1208 ? 131.870 162.025 129.769 1.00 21.21  ? 1208 LEU   B C     1 
ATOM   12862 O  O     . LEU   B 1 1208 ? 131.487 161.205 128.931 1.00 32.01  ? 1208 LEU   B O     1 
ATOM   12863 C  CB    . LEU   B 1 1208 ? 132.126 164.479 129.321 1.00 17.27  ? 1208 LEU   B CB    1 
ATOM   12864 C  CG    . LEU   B 1 1208 ? 132.916 165.637 128.712 1.00 22.32  ? 1208 LEU   B CG    1 
ATOM   12865 C  CD1   . LEU   B 1 1208 ? 131.979 166.712 128.188 1.00 15.41  ? 1208 LEU   B CD1   1 
ATOM   12866 C  CD2   . LEU   B 1 1208 ? 133.876 166.217 129.736 1.00 18.14  ? 1208 LEU   B CD2   1 
ATOM   12867 N  N     . THR   B 1 1209 ? 131.469 162.003 131.036 1.00 29.05  ? 1209 THR   B N     1 
ATOM   12868 C  CA    . THR   B 1 1209 ? 130.476 161.048 131.502 1.00 31.20  ? 1209 THR   B CA    1 
ATOM   12869 C  C     . THR   B 1 1209 ? 129.810 161.612 132.747 1.00 27.35  ? 1209 THR   B C     1 
ATOM   12870 O  O     . THR   B 1 1209 ? 130.447 162.322 133.529 1.00 35.55  ? 1209 THR   B O     1 
ATOM   12871 C  CB    . THR   B 1 1209 ? 131.106 159.682 131.805 1.00 28.44  ? 1209 THR   B CB    1 
ATOM   12872 O  OG1   . THR   B 1 1209 ? 130.074 158.706 131.991 1.00 30.24  ? 1209 THR   B OG1   1 
ATOM   12873 C  CG2   . THR   B 1 1209 ? 131.952 159.752 133.058 1.00 26.36  ? 1209 THR   B CG2   1 
ATOM   12874 N  N     . PHE   B 1 1210 ? 128.527 161.304 132.917 1.00 27.82  ? 1210 PHE   B N     1 
ATOM   12875 C  CA    . PHE   B 1 1210 ? 127.806 161.652 134.132 1.00 28.91  ? 1210 PHE   B CA    1 
ATOM   12876 C  C     . PHE   B 1 1210 ? 127.527 160.436 135.003 1.00 29.51  ? 1210 PHE   B C     1 
ATOM   12877 O  O     . PHE   B 1 1210 ? 126.711 160.517 135.925 1.00 38.30  ? 1210 PHE   B O     1 
ATOM   12878 C  CB    . PHE   B 1 1210 ? 126.504 162.386 133.798 1.00 27.93  ? 1210 PHE   B CB    1 
ATOM   12879 C  CG    . PHE   B 1 1210 ? 125.810 161.877 132.570 1.00 27.64  ? 1210 PHE   B CG    1 
ATOM   12880 C  CD1   . PHE   B 1 1210 ? 125.305 160.592 132.524 1.00 25.96  ? 1210 PHE   B CD1   1 
ATOM   12881 C  CD2   . PHE   B 1 1210 ? 125.651 162.695 131.465 1.00 30.08  ? 1210 PHE   B CD2   1 
ATOM   12882 C  CE1   . PHE   B 1 1210 ? 124.661 160.131 131.395 1.00 28.65  ? 1210 PHE   B CE1   1 
ATOM   12883 C  CE2   . PHE   B 1 1210 ? 125.009 162.237 130.335 1.00 30.82  ? 1210 PHE   B CE2   1 
ATOM   12884 C  CZ    . PHE   B 1 1210 ? 124.513 160.953 130.300 1.00 31.31  ? 1210 PHE   B CZ    1 
ATOM   12885 N  N     . TYR   B 1 1211 ? 128.184 159.314 134.731 1.00 29.69  ? 1211 TYR   B N     1 
ATOM   12886 C  CA    . TYR   B 1 1211 ? 128.140 158.147 135.596 1.00 27.68  ? 1211 TYR   B CA    1 
ATOM   12887 C  C     . TYR   B 1 1211 ? 129.409 158.073 136.436 1.00 35.24  ? 1211 TYR   B C     1 
ATOM   12888 O  O     . TYR   B 1 1211 ? 130.438 158.672 136.115 1.00 38.35  ? 1211 TYR   B O     1 
ATOM   12889 C  CB    . TYR   B 1 1211 ? 127.963 156.868 134.770 1.00 26.34  ? 1211 TYR   B CB    1 
ATOM   12890 C  CG    . TYR   B 1 1211 ? 126.762 156.907 133.857 1.00 31.92  ? 1211 TYR   B CG    1 
ATOM   12891 C  CD1   . TYR   B 1 1211 ? 125.476 156.828 134.370 1.00 34.08  ? 1211 TYR   B CD1   1 
ATOM   12892 C  CD2   . TYR   B 1 1211 ? 126.914 157.035 132.484 1.00 36.10  ? 1211 TYR   B CD2   1 
ATOM   12893 C  CE1   . TYR   B 1 1211 ? 124.374 156.869 133.543 1.00 31.55  ? 1211 TYR   B CE1   1 
ATOM   12894 C  CE2   . TYR   B 1 1211 ? 125.818 157.078 131.648 1.00 36.42  ? 1211 TYR   B CE2   1 
ATOM   12895 C  CZ    . TYR   B 1 1211 ? 124.550 156.994 132.183 1.00 40.26  ? 1211 TYR   B CZ    1 
ATOM   12896 O  OH    . TYR   B 1 1211 ? 123.452 157.035 131.356 1.00 47.18  ? 1211 TYR   B OH    1 
ATOM   12897 N  N     . SER   B 1 1212 ? 129.324 157.325 137.529 1.00 45.01  ? 1212 SER   B N     1 
ATOM   12898 C  CA    . SER   B 1 1212 ? 130.465 157.153 138.417 1.00 44.50  ? 1212 SER   B CA    1 
ATOM   12899 C  C     . SER   B 1 1212 ? 130.744 155.674 138.655 1.00 46.66  ? 1212 SER   B C     1 
ATOM   12900 O  O     . SER   B 1 1212 ? 131.448 155.033 137.875 1.00 52.43  ? 1212 SER   B O     1 
ATOM   12901 C  CB    . SER   B 1 1212 ? 130.225 157.870 139.746 1.00 38.12  ? 1212 SER   B CB    1 
ATOM   12902 O  OG    . SER   B 1 1212 ? 129.436 157.079 140.616 1.00 48.09  ? 1212 SER   B OG    1 
HETATM 12903 N  N1    . A1ATU C 2 .    ? 123.701 152.871 171.571 1.00 48.37  ? 1301 A1ATU A N1    1 
HETATM 12904 N  N3    . A1ATU C 2 .    ? 123.279 155.315 171.575 1.00 51.38  ? 1301 A1ATU A N3    1 
HETATM 12905 C  C4    . A1ATU C 2 .    ? 125.918 154.703 169.038 1.00 47.01  ? 1301 A1ATU A C4    1 
HETATM 12906 C  C5    . A1ATU C 2 .    ? 128.439 152.100 169.717 1.00 51.96  ? 1301 A1ATU A C5    1 
HETATM 12907 C  C6    . A1ATU C 2 .    ? 122.799 153.971 171.612 1.00 54.23  ? 1301 A1ATU A C6    1 
HETATM 12908 C  C10   . A1ATU C 2 .    ? 124.372 156.524 168.887 1.00 44.32  ? 1301 A1ATU A C10   1 
HETATM 12909 C  C15   . A1ATU C 2 .    ? 124.219 150.557 170.987 1.00 50.09  ? 1301 A1ATU A C15   1 
HETATM 12910 C  C1    . A1ATU C 2 .    ? 126.076 149.668 167.128 1.00 46.65  ? 1301 A1ATU A C1    1 
HETATM 12911 C  "C1'" . A1ATU C 2 .    ? 127.171 152.516 169.339 1.00 52.08  ? 1301 A1ATU A "C1'" 1 
HETATM 12912 C  C11   . A1ATU C 2 .    ? 125.273 155.652 166.931 1.00 47.46  ? 1301 A1ATU A C11   1 
HETATM 12913 C  C12   . A1ATU C 2 .    ? 126.012 154.729 167.658 1.00 45.84  ? 1301 A1ATU A C12   1 
HETATM 12914 C  C16   . A1ATU C 2 .    ? 122.905 151.111 173.049 1.00 47.08  ? 1301 A1ATU A C16   1 
HETATM 12915 C  C2    . A1ATU C 2 .    ? 123.214 151.505 171.616 1.00 47.61  ? 1301 A1ATU A C2    1 
HETATM 12916 C  "C2'" . A1ATU C 2 .    ? 126.407 151.724 168.501 1.00 45.54  ? 1301 A1ATU A "C2'" 1 
HETATM 12917 C  "C3'" . A1ATU C 2 .    ? 126.908 150.519 168.040 1.00 49.59  ? 1301 A1ATU A "C3'" 1 
HETATM 12918 C  "C4'" . A1ATU C 2 .    ? 128.176 150.102 168.415 1.00 49.17  ? 1301 A1ATU A "C4'" 1 
HETATM 12919 C  "C5'" . A1ATU C 2 .    ? 128.941 150.892 169.255 1.00 47.74  ? 1301 A1ATU A "C5'" 1 
HETATM 12920 C  C9    . A1ATU C 2 .    ? 125.101 155.628 169.660 1.00 51.00  ? 1301 A1ATU A C9    1 
HETATM 12921 N  N7    . A1ATU C 2 .    ? 124.477 156.521 167.560 1.00 47.52  ? 1301 A1ATU A N7    1 
HETATM 12922 N  N9    . A1ATU C 2 .    ? 126.676 153.773 169.838 1.00 49.66  ? 1301 A1ATU A N9    1 
HETATM 12923 O  O6    . A1ATU C 2 .    ? 121.609 153.755 171.697 1.00 59.96  ? 1301 A1ATU A O6    1 
HETATM 12924 O  OP1   . A1ATU C 2 .    ? 125.130 157.026 171.836 1.00 51.26  ? 1301 A1ATU A OP1   1 
HETATM 12925 O  OP3   . A1ATU C 2 .    ? 125.707 154.772 172.120 1.00 54.65  ? 1301 A1ATU A OP3   1 
HETATM 12926 S  S1    . A1ATU C 2 .    ? 124.895 155.691 171.393 1.00 53.32  ? 1301 A1ATU A S1    1 
HETATM 12927 H  H13   . A1ATU C 2 .    ? 124.694 153.030 171.509 1.00 47.69  ? 1301 A1ATU A H13   1 
HETATM 12928 H  H12   . A1ATU C 2 .    ? 122.632 156.076 171.584 1.00 48.09  ? 1301 A1ATU A H12   1 
HETATM 12929 H  H5    . A1ATU C 2 .    ? 129.036 152.717 170.374 1.00 46.74  ? 1301 A1ATU A H5    1 
HETATM 12930 H  H9    . A1ATU C 2 .    ? 123.719 157.240 169.372 1.00 45.37  ? 1301 A1ATU A H9    1 
HETATM 12931 H  H17   . A1ATU C 2 .    ? 124.295 150.758 169.954 1.00 48.11  ? 1301 A1ATU A H17   1 
HETATM 12932 H  H16   . A1ATU C 2 .    ? 123.896 149.557 171.130 1.00 47.42  ? 1301 A1ATU A H16   1 
HETATM 12933 H  H15   . A1ATU C 2 .    ? 125.163 150.691 171.445 1.00 47.81  ? 1301 A1ATU A H15   1 
HETATM 12934 H  H3    . A1ATU C 2 .    ? 125.503 150.292 166.496 1.00 46.98  ? 1301 A1ATU A H3    1 
HETATM 12935 H  H1    . A1ATU C 2 .    ? 125.431 149.055 167.700 1.00 47.73  ? 1301 A1ATU A H1    1 
HETATM 12936 H  H2    . A1ATU C 2 .    ? 126.714 149.060 166.540 1.00 46.78  ? 1301 A1ATU A H2    1 
HETATM 12937 H  H10   . A1ATU C 2 .    ? 125.342 155.668 165.851 1.00 47.15  ? 1301 A1ATU A H10   1 
HETATM 12938 H  H11   . A1ATU C 2 .    ? 126.657 154.029 167.145 1.00 47.19  ? 1301 A1ATU A H11   1 
HETATM 12939 H  H20   . A1ATU C 2 .    ? 122.618 150.093 173.079 1.00 47.26  ? 1301 A1ATU A H20   1 
HETATM 12940 H  H19   . A1ATU C 2 .    ? 122.116 151.711 173.418 1.00 47.60  ? 1301 A1ATU A H19   1 
HETATM 12941 H  H18   . A1ATU C 2 .    ? 123.765 151.253 173.645 1.00 48.08  ? 1301 A1ATU A H18   1 
HETATM 12942 H  H14   . A1ATU C 2 .    ? 122.282 151.444 171.035 1.00 47.43  ? 1301 A1ATU A H14   1 
HETATM 12943 H  H4    . A1ATU C 2 .    ? 125.416 152.043 168.208 1.00 46.24  ? 1301 A1ATU A H4    1 
HETATM 12944 H  H7    . A1ATU C 2 .    ? 128.566 149.159 168.050 1.00 47.83  ? 1301 A1ATU A H7    1 
HETATM 12945 H  H6    . A1ATU C 2 .    ? 129.930 150.568 169.550 1.00 47.08  ? 1301 A1ATU A H6    1 
HETATM 12946 H  H8    . A1ATU C 2 .    ? 126.820 153.993 170.815 1.00 48.32  ? 1301 A1ATU A H8    1 
HETATM 12947 CL CL    . CL    D 3 .    ? 127.212 155.329 159.604 1.00 31.66  ? 1302 CL    A CL    1 
HETATM 12948 NA NA    . NA    E 4 .    ? 118.202 155.327 166.830 1.00 32.33  ? 1303 NA    A NA    1 
HETATM 12949 N  N1    . A1ATU F 2 .    ? 191.433 162.486 171.395 1.00 44.56  ? 1301 A1ATU B N1    1 
HETATM 12950 N  N3    . A1ATU F 2 .    ? 191.817 159.985 171.670 1.00 49.27  ? 1301 A1ATU B N3    1 
HETATM 12951 C  C4    . A1ATU F 2 .    ? 189.474 160.571 168.967 1.00 45.57  ? 1301 A1ATU B C4    1 
HETATM 12952 C  C5    . A1ATU F 2 .    ? 186.965 163.196 169.700 1.00 49.37  ? 1301 A1ATU B C5    1 
HETATM 12953 C  C6    . A1ATU F 2 .    ? 192.259 161.354 171.645 1.00 52.85  ? 1301 A1ATU B C6    1 
HETATM 12954 C  C10   . A1ATU F 2 .    ? 190.983 158.698 168.900 1.00 42.36  ? 1301 A1ATU B C10   1 
HETATM 12955 C  C15   . A1ATU F 2 .    ? 191.171 164.897 170.801 1.00 45.79  ? 1301 A1ATU B C15   1 
HETATM 12956 C  C1    . A1ATU F 2 .    ? 189.347 165.641 167.154 1.00 43.44  ? 1301 A1ATU B C1    1 
HETATM 12957 C  "C1'" . A1ATU F 2 .    ? 188.216 162.764 169.289 1.00 49.01  ? 1301 A1ATU B "C1'" 1 
HETATM 12958 C  C11   . A1ATU F 2 .    ? 190.269 159.642 166.907 1.00 44.22  ? 1301 A1ATU B C11   1 
HETATM 12959 C  C12   . A1ATU F 2 .    ? 189.497 160.572 167.588 1.00 41.55  ? 1301 A1ATU B C12   1 
HETATM 12960 C  C16   . A1ATU F 2 .    ? 192.370 164.178 172.838 1.00 47.61  ? 1301 A1ATU B C16   1 
HETATM 12961 C  C2    . A1ATU F 2 .    ? 192.034 163.813 171.411 1.00 45.25  ? 1301 A1ATU B C2    1 
HETATM 12962 C  "C2'" . A1ATU F 2 .    ? 188.983 163.566 168.466 1.00 43.28  ? 1301 A1ATU B "C2'" 1 
HETATM 12963 C  "C3'" . A1ATU F 2 .    ? 188.497 164.793 168.052 1.00 47.75  ? 1301 A1ATU B "C3'" 1 
HETATM 12964 C  "C4'" . A1ATU F 2 .    ? 187.246 165.228 168.455 1.00 45.86  ? 1301 A1ATU B "C4'" 1 
HETATM 12965 C  "C5'" . A1ATU F 2 .    ? 186.478 164.427 169.282 1.00 45.74  ? 1301 A1ATU B "C5'" 1 
HETATM 12966 C  C9    . A1ATU F 2 .    ? 190.212 159.603 169.617 1.00 47.97  ? 1301 A1ATU B C9    1 
HETATM 12967 N  N7    . A1ATU F 2 .    ? 190.990 158.732 167.573 1.00 44.18  ? 1301 A1ATU B N7    1 
HETATM 12968 N  N9    . A1ATU F 2 .    ? 188.682 161.485 169.752 1.00 48.83  ? 1301 A1ATU B N9    1 
HETATM 12969 O  O6    . A1ATU F 2 .    ? 193.414 161.603 171.840 1.00 59.06  ? 1301 A1ATU B O6    1 
HETATM 12970 O  OP1   . A1ATU F 2 .    ? 190.076 158.160 171.752 1.00 53.64  ? 1301 A1ATU B OP1   1 
HETATM 12971 O  OP3   . A1ATU F 2 .    ? 189.351 160.377 172.053 1.00 52.50  ? 1301 A1ATU B OP3   1 
HETATM 12972 S  S1    . A1ATU F 2 .    ? 190.254 159.518 171.352 1.00 51.04  ? 1301 A1ATU B S1    1 
HETATM 12973 H  H13   . A1ATU F 2 .    ? 190.446 162.389 171.245 1.00 45.03  ? 1301 A1ATU B H13   1 
HETATM 12974 H  H12   . A1ATU F 2 .    ? 192.479 159.249 171.830 1.00 46.00  ? 1301 A1ATU B H12   1 
HETATM 12975 H  H5    . A1ATU F 2 .    ? 186.363 162.571 170.348 1.00 44.85  ? 1301 A1ATU B H5    1 
HETATM 12976 H  H9    . A1ATU F 2 .    ? 191.571 157.954 169.423 1.00 43.43  ? 1301 A1ATU B H9    1 
HETATM 12977 H  H17   . A1ATU F 2 .    ? 191.705 165.820 170.826 1.00 45.42  ? 1301 A1ATU B H17   1 
HETATM 12978 H  H16   . A1ATU F 2 .    ? 190.282 164.989 171.349 1.00 45.01  ? 1301 A1ATU B H16   1 
HETATM 12979 H  H15   . A1ATU F 2 .    ? 190.952 164.654 169.815 1.00 45.98  ? 1301 A1ATU B H15   1 
HETATM 12980 H  H3    . A1ATU F 2 .    ? 189.890 165.011 166.500 1.00 44.85  ? 1301 A1ATU B H3    1 
HETATM 12981 H  H1    . A1ATU F 2 .    ? 190.022 166.211 167.737 1.00 45.44  ? 1301 A1ATU B H1    1 
HETATM 12982 H  H2    . A1ATU F 2 .    ? 188.729 166.288 166.590 1.00 44.63  ? 1301 A1ATU B H2    1 
HETATM 12983 H  H10   . A1ATU F 2 .    ? 190.292 159.650 165.825 1.00 44.75  ? 1301 A1ATU B H10   1 
HETATM 12984 H  H11   . A1ATU F 2 .    ? 188.922 161.300 167.040 1.00 45.03  ? 1301 A1ATU B H11   1 
HETATM 12985 H  H20   . A1ATU F 2 .    ? 192.157 165.206 172.992 1.00 45.47  ? 1301 A1ATU B H20   1 
HETATM 12986 H  H19   . A1ATU F 2 .    ? 193.390 163.995 173.026 1.00 45.74  ? 1301 A1ATU B H19   1 
HETATM 12987 H  H18   . A1ATU F 2 .    ? 191.778 163.598 173.489 1.00 46.14  ? 1301 A1ATU B H18   1 
HETATM 12988 H  H14   . A1ATU F 2 .    ? 192.970 163.772 170.843 1.00 45.41  ? 1301 A1ATU B H14   1 
HETATM 12989 H  H4    . A1ATU F 2 .    ? 189.963 163.238 168.148 1.00 43.98  ? 1301 A1ATU B H4    1 
HETATM 12990 H  H7    . A1ATU F 2 .    ? 186.869 166.189 168.125 1.00 45.47  ? 1301 A1ATU B H7    1 
HETATM 12991 H  H6    . A1ATU F 2 .    ? 185.498 164.760 169.603 1.00 45.22  ? 1301 A1ATU B H6    1 
HETATM 12992 H  H8    . A1ATU F 2 .    ? 188.529 161.253 170.726 1.00 46.23  ? 1301 A1ATU B H8    1 
HETATM 12993 CL CL    . CL    G 3 .    ? 188.187 160.071 159.604 1.00 31.33  ? 1302 CL    B CL    1 
HETATM 12994 NA NA    . NA    H 4 .    ? 197.276 159.871 166.830 1.00 34.33  ? 1303 NA    B NA    1 
HETATM 12995 O  O     . HOH   I 5 .    ? 127.838 153.830 165.042 1.00 49.52  ? 1401 HOH   A O     1 
HETATM 12996 O  O     . HOH   J 5 .    ? 187.566 161.571 165.053 1.00 43.43  ? 1401 HOH   B O     1 
# 
