data_8S7W
# 
_entry.id   8S7W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8S7W         pdb_00008s7w 10.2210/pdb8s7w/pdb 
WWPDB D_1292137024 ?            ?                   
# 
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 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-01-22 
3 'Structure model' 1 2 2025-02-05 
# 
_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' 'Database references' 
2 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 3 'Structure model' citation 
# 
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.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8S7W 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Mattevi 
_pdbx_contact_author.name_last          Andrea 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guerriere, T.B.' 1 0009-0003-3232-6822 
'Mattevi, A.'     2 0000-0002-9523-7128 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1046 
_citation.page_last                 1060 
_citation.title                     
'Dehydrogenase versus oxidase function: the interplay between substrate binding and flavin microenvironment.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c05944 
_citation.pdbx_database_id_PubMed   39781101 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guerriere, T.B.' 1  ? 
primary 'Vancheri, A.'    2  ? 
primary 'Ricotti, I.'     3  ? 
primary 'Serapian, S.A.'  4  ? 
primary 'Eggerichs, D.'   5  ? 
primary 'Tischler, D.'    6  ? 
primary 'Colombo, G.'     7  ? 
primary 'Mascotti, M.L.'  8  ? 
primary 'Fraaije, M.W.'   9  ? 
primary 'Mattevi, A.'     10 ? 
# 
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 Oxidoreductase                58247.816 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   2   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                35.453    5   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'       106.120   8   ? ? ? ? 
5 water       nat water                         18.015    589 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDVGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDVGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_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 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'CHLORIDE ION'                CL  
4 'DI(HYDROXYETHYL)ETHER'       PEG 
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   ALA n 
1 3   ALA n 
1 4   PRO n 
1 5   LEU n 
1 6   PRO n 
1 7   GLU n 
1 8   GLY n 
1 9   VAL n 
1 10  SER n 
1 11  ALA n 
1 12  GLU n 
1 13  ALA n 
1 14  MET n 
1 15  SER n 
1 16  SER n 
1 17  ALA n 
1 18  LEU n 
1 19  ASP n 
1 20  ARG n 
1 21  PHE n 
1 22  ALA n 
1 23  ARG n 
1 24  ILE n 
1 25  VAL n 
1 26  GLY n 
1 27  ALA n 
1 28  ASP n 
1 29  TRP n 
1 30  VAL n 
1 31  PHE n 
1 32  THR n 
1 33  GLU n 
1 34  ASP n 
1 35  LYS n 
1 36  ILE n 
1 37  THR n 
1 38  PRO n 
1 39  TYR n 
1 40  GLU n 
1 41  ASP n 
1 42  PRO n 
1 43  TYR n 
1 44  THR n 
1 45  ILE n 
1 46  SER n 
1 47  ASN n 
1 48  ASP n 
1 49  GLU n 
1 50  THR n 
1 51  GLU n 
1 52  HIS n 
1 53  ARG n 
1 54  PRO n 
1 55  TYR n 
1 56  ALA n 
1 57  ALA n 
1 58  VAL n 
1 59  ALA n 
1 60  PRO n 
1 61  ALA n 
1 62  SER n 
1 63  THR n 
1 64  GLU n 
1 65  GLU n 
1 66  VAL n 
1 67  GLN n 
1 68  GLU n 
1 69  ILE n 
1 70  VAL n 
1 71  ARG n 
1 72  VAL n 
1 73  ALA n 
1 74  ASN n 
1 75  GLU n 
1 76  PHE n 
1 77  GLY n 
1 78  VAL n 
1 79  PRO n 
1 80  LEU n 
1 81  TRP n 
1 82  PRO n 
1 83  VAL n 
1 84  SER n 
1 85  ARG n 
1 86  GLY n 
1 87  LYS n 
1 88  ASN n 
1 89  PHE n 
1 90  ALA n 
1 91  TYR n 
1 92  GLY n 
1 93  GLY n 
1 94  ALA n 
1 95  ALA n 
1 96  PRO n 
1 97  VAL n 
1 98  MET n 
1 99  SER n 
1 100 GLY n 
1 101 THR n 
1 102 VAL n 
1 103 VAL n 
1 104 LEU n 
1 105 ASP n 
1 106 MET n 
1 107 ASN n 
1 108 ARG n 
1 109 MET n 
1 110 ASN n 
1 111 ARG n 
1 112 ILE n 
1 113 LEU n 
1 114 GLU n 
1 115 VAL n 
1 116 ASN n 
1 117 GLU n 
1 118 GLU n 
1 119 PHE n 
1 120 GLY n 
1 121 TYR n 
1 122 ALA n 
1 123 LEU n 
1 124 VAL n 
1 125 GLU n 
1 126 PRO n 
1 127 GLY n 
1 128 VAL n 
1 129 SER n 
1 130 TYR n 
1 131 PHE n 
1 132 GLU n 
1 133 LEU n 
1 134 TYR n 
1 135 ASP n 
1 136 TYR n 
1 137 ILE n 
1 138 GLN n 
1 139 GLU n 
1 140 LYS n 
1 141 GLY n 
1 142 LEU n 
1 143 LYS n 
1 144 LEU n 
1 145 TRP n 
1 146 ILE n 
1 147 ASP n 
1 148 VAL n 
1 149 PRO n 
1 150 ASP n 
1 151 VAL n 
1 152 GLY n 
1 153 TRP n 
1 154 GLY n 
1 155 SER n 
1 156 VAL n 
1 157 VAL n 
1 158 GLY n 
1 159 ASN n 
1 160 ALA n 
1 161 LEU n 
1 162 ASP n 
1 163 HIS n 
1 164 GLY n 
1 165 ILE n 
1 166 GLY n 
1 167 TYR n 
1 168 THR n 
1 169 PRO n 
1 170 TYR n 
1 171 GLY n 
1 172 ASP n 
1 173 HIS n 
1 174 PHE n 
1 175 ALA n 
1 176 MET n 
1 177 GLN n 
1 178 CYS n 
1 179 GLY n 
1 180 MET n 
1 181 GLU n 
1 182 VAL n 
1 183 VAL n 
1 184 LEU n 
1 185 PRO n 
1 186 ASN n 
1 187 GLY n 
1 188 GLU n 
1 189 VAL n 
1 190 VAL n 
1 191 ARG n 
1 192 THR n 
1 193 GLY n 
1 194 MET n 
1 195 GLY n 
1 196 ALA n 
1 197 MET n 
1 198 PRO n 
1 199 GLY n 
1 200 ASN n 
1 201 ASN n 
1 202 THR n 
1 203 TRP n 
1 204 GLN n 
1 205 LEU n 
1 206 PHE n 
1 207 LYS n 
1 208 TYR n 
1 209 GLY n 
1 210 TYR n 
1 211 GLY n 
1 212 PRO n 
1 213 TYR n 
1 214 VAL n 
1 215 ASP n 
1 216 GLY n 
1 217 ILE n 
1 218 PHE n 
1 219 SER n 
1 220 GLN n 
1 221 SER n 
1 222 ASN n 
1 223 PHE n 
1 224 GLY n 
1 225 VAL n 
1 226 VAL n 
1 227 THR n 
1 228 LYS n 
1 229 MET n 
1 230 GLY n 
1 231 ILE n 
1 232 TRP n 
1 233 LEU n 
1 234 MET n 
1 235 PRO n 
1 236 GLU n 
1 237 PRO n 
1 238 ALA n 
1 239 GLY n 
1 240 TYR n 
1 241 ARG n 
1 242 PRO n 
1 243 TYR n 
1 244 LEU n 
1 245 ILE n 
1 246 THR n 
1 247 PHE n 
1 248 GLU n 
1 249 ASN n 
1 250 GLU n 
1 251 ASP n 
1 252 ASP n 
1 253 ILE n 
1 254 GLU n 
1 255 THR n 
1 256 VAL n 
1 257 THR n 
1 258 GLU n 
1 259 ARG n 
1 260 LEU n 
1 261 ARG n 
1 262 PRO n 
1 263 LEU n 
1 264 LYS n 
1 265 VAL n 
1 266 ALA n 
1 267 GLY n 
1 268 VAL n 
1 269 ILE n 
1 270 GLN n 
1 271 ASN n 
1 272 GLY n 
1 273 ALA n 
1 274 THR n 
1 275 VAL n 
1 276 ARG n 
1 277 SER n 
1 278 LEU n 
1 279 VAL n 
1 280 LEU n 
1 281 ASP n 
1 282 ALA n 
1 283 ALA n 
1 284 ILE n 
1 285 THR n 
1 286 ARG n 
1 287 THR n 
1 288 LYS n 
1 289 SER n 
1 290 GLN n 
1 291 TYR n 
1 292 TYR n 
1 293 ASP n 
1 294 GLY n 
1 295 ASP n 
1 296 GLY n 
1 297 PRO n 
1 298 ILE n 
1 299 PRO n 
1 300 PRO n 
1 301 SER n 
1 302 VAL n 
1 303 ALA n 
1 304 LYS n 
1 305 THR n 
1 306 MET n 
1 307 MET n 
1 308 ALA n 
1 309 ASP n 
1 310 LEU n 
1 311 ASP n 
1 312 LEU n 
1 313 GLY n 
1 314 MET n 
1 315 TRP n 
1 316 ASN n 
1 317 PHE n 
1 318 CYS n 
1 319 GLY n 
1 320 ALA n 
1 321 LEU n 
1 322 TYR n 
1 323 GLY n 
1 324 PRO n 
1 325 PRO n 
1 326 PRO n 
1 327 VAL n 
1 328 MET n 
1 329 ASP n 
1 330 THR n 
1 331 LEU n 
1 332 TRP n 
1 333 THR n 
1 334 ALA n 
1 335 ILE n 
1 336 ARG n 
1 337 ASP n 
1 338 SER n 
1 339 PHE n 
1 340 ALA n 
1 341 ASP n 
1 342 ILE n 
1 343 PRO n 
1 344 GLY n 
1 345 VAL n 
1 346 LYS n 
1 347 PHE n 
1 348 TYR n 
1 349 PHE n 
1 350 PRO n 
1 351 GLU n 
1 352 ASP n 
1 353 ARG n 
1 354 ARG n 
1 355 HIS n 
1 356 LYS n 
1 357 VAL n 
1 358 ASP n 
1 359 LEU n 
1 360 LEU n 
1 361 LEU n 
1 362 HIS n 
1 363 ARG n 
1 364 ALA n 
1 365 GLU n 
1 366 THR n 
1 367 MET n 
1 368 LYS n 
1 369 GLY n 
1 370 VAL n 
1 371 PRO n 
1 372 LYS n 
1 373 LEU n 
1 374 THR n 
1 375 GLU n 
1 376 PHE n 
1 377 ASN n 
1 378 PHE n 
1 379 LEU n 
1 380 ASN n 
1 381 TRP n 
1 382 ASP n 
1 383 GLY n 
1 384 GLY n 
1 385 GLY n 
1 386 GLY n 
1 387 HIS n 
1 388 VAL n 
1 389 GLY n 
1 390 PHE n 
1 391 SER n 
1 392 PRO n 
1 393 VAL n 
1 394 SER n 
1 395 PRO n 
1 396 ILE n 
1 397 THR n 
1 398 GLY n 
1 399 LYS n 
1 400 ASP n 
1 401 ALA n 
1 402 ILE n 
1 403 LYS n 
1 404 GLN n 
1 405 TYR n 
1 406 ASN n 
1 407 MET n 
1 408 VAL n 
1 409 SER n 
1 410 SER n 
1 411 ARG n 
1 412 VAL n 
1 413 ARG n 
1 414 GLU n 
1 415 TYR n 
1 416 GLY n 
1 417 PHE n 
1 418 ASP n 
1 419 TYR n 
1 420 MET n 
1 421 GLY n 
1 422 LEU n 
1 423 LEU n 
1 424 ALA n 
1 425 ILE n 
1 426 GLY n 
1 427 TRP n 
1 428 ARG n 
1 429 ASP n 
1 430 LEU n 
1 431 HIS n 
1 432 HIS n 
1 433 VAL n 
1 434 THR n 
1 435 VAL n 
1 436 ILE n 
1 437 VAL n 
1 438 TYR n 
1 439 ASP n 
1 440 LYS n 
1 441 THR n 
1 442 ASP n 
1 443 PRO n 
1 444 ASP n 
1 445 GLU n 
1 446 ARG n 
1 447 LYS n 
1 448 LYS n 
1 449 LEU n 
1 450 ASP n 
1 451 GLU n 
1 452 LEU n 
1 453 PHE n 
1 454 ASN n 
1 455 ILE n 
1 456 LEU n 
1 457 VAL n 
1 458 ASP n 
1 459 GLU n 
1 460 ALA n 
1 461 ALA n 
1 462 ALA n 
1 463 GLU n 
1 464 GLY n 
1 465 TYR n 
1 466 GLY n 
1 467 GLU n 
1 468 TYR n 
1 469 ARG n 
1 470 THR n 
1 471 HIS n 
1 472 ILE n 
1 473 ARG n 
1 474 TYR n 
1 475 MET n 
1 476 ASP n 
1 477 ARG n 
1 478 ILE n 
1 479 ALA n 
1 480 LYS n 
1 481 THR n 
1 482 TYR n 
1 483 SER n 
1 484 TRP n 
1 485 ASN n 
1 486 ASP n 
1 487 ASN n 
1 488 ALA n 
1 489 LEU n 
1 490 TRP n 
1 491 LYS n 
1 492 MET n 
1 493 HIS n 
1 494 GLU n 
1 495 THR n 
1 496 ILE n 
1 497 LYS n 
1 498 ASP n 
1 499 ALA n 
1 500 LEU n 
1 501 ASP n 
1 502 PRO n 
1 503 ASN n 
1 504 GLY n 
1 505 ILE n 
1 506 LEU n 
1 507 ALA n 
1 508 PRO n 
1 509 GLY n 
1 510 LYS n 
1 511 SER n 
1 512 GLY n 
1 513 ILE n 
1 514 TRP n 
1 515 GLY n 
1 516 LYS n 
1 517 ASN n 
1 518 ARG n 
1 519 ARG n 
1 520 LYS n 
1 521 ALA 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                   521 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CW354_13745 
_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      'Marinicaulis flavus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2058213 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
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 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'       ? 'C4 H10 O3'         106.120 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
# 
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   1   MET MET A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  MET 14  14  14  MET MET A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ASN 47  47  47  ASN ASN A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  TRP 81  81  81  TRP TRP A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  MET 98  98  98  MET MET A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 TRP 145 145 145 TRP TRP A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 MET 180 180 180 MET MET A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 MET 197 197 197 MET MET A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 TYR 210 210 210 TYR TYR A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ASN 222 222 222 ASN ASN A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 MET 229 229 229 MET MET A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 TRP 232 232 232 TRP TRP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 TYR 243 243 243 TYR TYR A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ARG 261 261 261 ARG ARG A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 GLN 290 290 290 GLN GLN A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 PRO 297 297 297 PRO PRO A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 MET 307 307 307 MET MET A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 TRP 315 315 315 TRP TRP A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 CYS 318 318 318 CYS CYS A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 MET 328 328 328 MET MET A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 THR 330 330 330 THR THR A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 THR 333 333 333 THR THR A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 PRO 343 343 343 PRO PRO A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 TYR 348 348 348 TYR TYR A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 ARG 353 353 353 ARG ARG A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 HIS 355 355 355 HIS HIS A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 VAL 357 357 357 VAL VAL A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 HIS 362 362 362 HIS HIS A . n 
A 1 363 ARG 363 363 363 ARG ARG A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 MET 367 367 367 MET MET A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 TRP 381 381 381 TRP TRP A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 HIS 387 387 387 HIS HIS A . n 
A 1 388 VAL 388 388 388 VAL VAL A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 PRO 395 395 395 PRO PRO A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 LYS 399 399 399 LYS LYS A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 ALA 401 401 401 ALA ALA A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 TYR 405 405 405 TYR TYR A . n 
A 1 406 ASN 406 406 406 ASN ASN A . n 
A 1 407 MET 407 407 407 MET MET A . n 
A 1 408 VAL 408 408 408 VAL VAL A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 ASP 418 418 418 ASP ASP A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLY 426 426 426 GLY GLY A . n 
A 1 427 TRP 427 427 427 TRP TRP A . n 
A 1 428 ARG 428 428 428 ARG ARG A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 HIS 431 431 431 HIS HIS A . n 
A 1 432 HIS 432 432 432 HIS HIS A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 THR 434 434 434 THR THR A . n 
A 1 435 VAL 435 435 435 VAL VAL 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 TYR 438 438 438 TYR TYR A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 THR 441 441 441 THR THR A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 PRO 443 443 443 PRO PRO A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 LYS 448 448 448 LYS LYS A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 ASP 450 450 450 ASP ASP A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 ASN 454 454 454 ASN ASN A . n 
A 1 455 ILE 455 455 455 ILE ILE A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 ASP 458 458 458 ASP ASP A . n 
A 1 459 GLU 459 459 459 GLU GLU A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ALA 462 462 462 ALA ALA A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 GLU 467 467 467 GLU GLU A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 THR 470 470 470 THR THR A . n 
A 1 471 HIS 471 471 471 HIS HIS A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 TYR 474 474 474 TYR TYR A . n 
A 1 475 MET 475 475 475 MET MET A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 ARG 477 477 477 ARG ARG A . n 
A 1 478 ILE 478 478 478 ILE ILE A . n 
A 1 479 ALA 479 479 479 ALA ALA A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 TYR 482 482 482 TYR TYR A . n 
A 1 483 SER 483 483 483 SER SER A . n 
A 1 484 TRP 484 484 484 TRP TRP A . n 
A 1 485 ASN 485 485 485 ASN ASN A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 ASN 487 487 487 ASN ASN A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 MET 492 492 492 MET MET A . n 
A 1 493 HIS 493 493 493 HIS HIS A . n 
A 1 494 GLU 494 494 494 GLU GLU A . n 
A 1 495 THR 495 495 495 THR THR A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 LYS 497 497 497 LYS LYS A . n 
A 1 498 ASP 498 498 498 ASP ASP A . n 
A 1 499 ALA 499 499 499 ALA ALA A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 ASP 501 501 501 ASP ASP A . n 
A 1 502 PRO 502 502 502 PRO PRO A . n 
A 1 503 ASN 503 503 503 ASN ASN A . n 
A 1 504 GLY 504 504 504 GLY GLY A . n 
A 1 505 ILE 505 505 505 ILE ILE A . n 
A 1 506 LEU 506 506 506 LEU LEU A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 PRO 508 508 508 PRO PRO A . n 
A 1 509 GLY 509 509 509 GLY GLY A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 SER 511 511 511 SER SER A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 ILE 513 513 513 ILE ILE A . n 
A 1 514 TRP 514 514 514 TRP TRP A . n 
A 1 515 GLY 515 515 515 GLY GLY A . n 
A 1 516 LYS 516 516 516 LYS LYS A . n 
A 1 517 ASN 517 517 517 ASN ASN A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 LYS 520 520 ?   ?   ?   A . n 
A 1 521 ALA 521 521 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   ALA 3   3   3   ALA ALA B . n 
B 1 4   PRO 4   4   4   PRO PRO B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  MET 14  14  14  MET MET B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  ARG 23  23  23  ARG ARG B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  GLU 33  33  33  GLU GLU B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  TYR 43  43  43  TYR TYR B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  ILE 45  45  45  ILE ILE B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ASN 47  47  47  ASN ASN B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  ARG 53  53  53  ARG ARG B . n 
B 1 54  PRO 54  54  54  PRO PRO B . n 
B 1 55  TYR 55  55  55  TYR TYR B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  GLU 68  68  68  GLU GLU B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  PRO 79  79  79  PRO PRO B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  TRP 81  81  81  TRP TRP B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  ARG 85  85  85  ARG ARG B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  MET 98  98  98  MET MET B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 THR 101 101 101 THR THR B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 MET 106 106 106 MET MET B . n 
B 1 107 ASN 107 107 107 ASN ASN B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 MET 109 109 109 MET MET B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 PRO 126 126 126 PRO PRO B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 TYR 130 130 130 TYR TYR B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 TYR 136 136 136 TYR TYR B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 TRP 145 145 145 TRP TRP B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 TRP 153 153 153 TRP TRP B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 VAL 156 156 156 VAL VAL B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ASP 172 172 172 ASP ASP B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 PHE 174 174 174 PHE PHE B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 GLN 177 177 177 GLN GLN B . n 
B 1 178 CYS 178 178 178 CYS CYS B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 MET 180 180 180 MET MET B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 GLU 188 188 188 GLU GLU B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ARG 191 191 191 ARG ARG B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 MET 194 194 194 MET MET B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 MET 197 197 197 MET MET B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 ASN 200 200 200 ASN ASN B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 TRP 203 203 203 TRP TRP B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 PHE 206 206 206 PHE PHE B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 TYR 210 210 210 TYR TYR B . n 
B 1 211 GLY 211 211 211 GLY GLY B . n 
B 1 212 PRO 212 212 212 PRO PRO B . n 
B 1 213 TYR 213 213 213 TYR TYR B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 GLY 216 216 216 GLY GLY B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 PHE 218 218 218 PHE PHE B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 GLN 220 220 220 GLN GLN B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 ASN 222 222 222 ASN ASN B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 MET 229 229 229 MET MET B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 TRP 232 232 232 TRP TRP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 TYR 243 243 243 TYR TYR B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 THR 246 246 246 THR THR B . n 
B 1 247 PHE 247 247 247 PHE PHE B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 GLU 250 250 250 GLU GLU B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 THR 255 255 255 THR THR B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 ARG 261 261 261 ARG ARG B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 ILE 269 269 269 ILE ILE B . n 
B 1 270 GLN 270 270 270 GLN GLN B . n 
B 1 271 ASN 271 271 271 ASN ASN B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 ARG 276 276 276 ARG ARG B . n 
B 1 277 SER 277 277 277 SER SER B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 ASP 281 281 281 ASP ASP B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 ALA 283 283 283 ALA ALA B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 THR 287 287 287 THR THR B . n 
B 1 288 LYS 288 288 288 LYS LYS B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 GLN 290 290 290 GLN GLN B . n 
B 1 291 TYR 291 291 291 TYR TYR B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 GLY 294 294 294 GLY GLY B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 PRO 297 297 297 PRO PRO B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 PRO 300 300 300 PRO PRO B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 ALA 303 303 303 ALA ALA B . n 
B 1 304 LYS 304 304 304 LYS LYS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 MET 306 306 306 MET MET B . n 
B 1 307 MET 307 307 307 MET MET B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 ASP 309 309 309 ASP ASP B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 GLY 313 313 313 GLY GLY B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 TRP 315 315 315 TRP TRP B . n 
B 1 316 ASN 316 316 316 ASN ASN B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 CYS 318 318 318 CYS CYS B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 TYR 322 322 322 TYR TYR B . n 
B 1 323 GLY 323 323 323 GLY GLY B . n 
B 1 324 PRO 324 324 324 PRO PRO B . n 
B 1 325 PRO 325 325 325 PRO PRO B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 MET 328 328 328 MET MET B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 THR 330 330 330 THR THR B . n 
B 1 331 LEU 331 331 331 LEU LEU B . n 
B 1 332 TRP 332 332 332 TRP TRP B . n 
B 1 333 THR 333 333 333 THR THR B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 ILE 335 335 335 ILE ILE B . n 
B 1 336 ARG 336 336 336 ARG ARG B . n 
B 1 337 ASP 337 337 337 ASP ASP B . n 
B 1 338 SER 338 338 338 SER SER B . n 
B 1 339 PHE 339 339 339 PHE PHE B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 ASP 341 341 341 ASP ASP B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 PRO 343 343 343 PRO PRO B . n 
B 1 344 GLY 344 344 344 GLY GLY B . n 
B 1 345 VAL 345 345 345 VAL VAL B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 TYR 348 348 348 TYR TYR B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 ARG 353 353 353 ARG ARG B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 HIS 355 355 355 HIS HIS B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 VAL 357 357 357 VAL VAL B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 LEU 359 359 359 LEU LEU B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 HIS 362 362 362 HIS HIS B . n 
B 1 363 ARG 363 363 363 ARG ARG B . n 
B 1 364 ALA 364 364 364 ALA ALA B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 MET 367 367 367 MET MET B . n 
B 1 368 LYS 368 368 368 LYS LYS B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 VAL 370 370 370 VAL VAL B . n 
B 1 371 PRO 371 371 371 PRO PRO B . n 
B 1 372 LYS 372 372 372 LYS LYS B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 GLU 375 375 375 GLU GLU B . n 
B 1 376 PHE 376 376 376 PHE PHE B . n 
B 1 377 ASN 377 377 377 ASN ASN B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 TRP 381 381 381 TRP TRP B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 GLY 383 383 383 GLY GLY B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 GLY 386 386 386 GLY GLY B . n 
B 1 387 HIS 387 387 387 HIS HIS B . n 
B 1 388 VAL 388 388 388 VAL VAL B . n 
B 1 389 GLY 389 389 389 GLY GLY B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 SER 391 391 391 SER SER B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 VAL 393 393 393 VAL VAL B . n 
B 1 394 SER 394 394 394 SER SER B . n 
B 1 395 PRO 395 395 395 PRO PRO B . n 
B 1 396 ILE 396 396 396 ILE ILE B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLY 398 398 398 GLY GLY B . n 
B 1 399 LYS 399 399 399 LYS LYS B . n 
B 1 400 ASP 400 400 400 ASP ASP B . n 
B 1 401 ALA 401 401 401 ALA ALA B . n 
B 1 402 ILE 402 402 402 ILE ILE B . n 
B 1 403 LYS 403 403 403 LYS LYS B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 TYR 405 405 405 TYR TYR B . n 
B 1 406 ASN 406 406 406 ASN ASN B . n 
B 1 407 MET 407 407 407 MET MET B . n 
B 1 408 VAL 408 408 408 VAL VAL B . n 
B 1 409 SER 409 409 409 SER SER B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 VAL 412 412 412 VAL VAL B . n 
B 1 413 ARG 413 413 413 ARG ARG B . n 
B 1 414 GLU 414 414 414 GLU GLU B . n 
B 1 415 TYR 415 415 415 TYR TYR B . n 
B 1 416 GLY 416 416 416 GLY GLY B . n 
B 1 417 PHE 417 417 417 PHE PHE B . n 
B 1 418 ASP 418 418 418 ASP ASP B . n 
B 1 419 TYR 419 419 419 TYR TYR B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLY 421 421 421 GLY GLY B . n 
B 1 422 LEU 422 422 422 LEU LEU B . n 
B 1 423 LEU 423 423 423 LEU LEU B . n 
B 1 424 ALA 424 424 424 ALA ALA B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLY 426 426 426 GLY GLY B . n 
B 1 427 TRP 427 427 427 TRP TRP B . n 
B 1 428 ARG 428 428 428 ARG ARG B . n 
B 1 429 ASP 429 429 429 ASP ASP B . n 
B 1 430 LEU 430 430 430 LEU LEU B . n 
B 1 431 HIS 431 431 431 HIS HIS B . n 
B 1 432 HIS 432 432 432 HIS HIS B . n 
B 1 433 VAL 433 433 433 VAL VAL B . n 
B 1 434 THR 434 434 434 THR THR B . n 
B 1 435 VAL 435 435 435 VAL VAL 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 TYR 438 438 438 TYR TYR B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 THR 441 441 441 THR THR B . n 
B 1 442 ASP 442 442 442 ASP ASP B . n 
B 1 443 PRO 443 443 443 PRO PRO B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 LYS 448 448 448 LYS LYS B . n 
B 1 449 LEU 449 449 449 LEU LEU B . n 
B 1 450 ASP 450 450 450 ASP ASP B . n 
B 1 451 GLU 451 451 451 GLU GLU B . n 
B 1 452 LEU 452 452 452 LEU LEU B . n 
B 1 453 PHE 453 453 453 PHE PHE B . n 
B 1 454 ASN 454 454 454 ASN ASN B . n 
B 1 455 ILE 455 455 455 ILE ILE B . n 
B 1 456 LEU 456 456 456 LEU LEU B . n 
B 1 457 VAL 457 457 457 VAL VAL B . n 
B 1 458 ASP 458 458 458 ASP ASP B . n 
B 1 459 GLU 459 459 459 GLU GLU B . n 
B 1 460 ALA 460 460 460 ALA ALA B . n 
B 1 461 ALA 461 461 461 ALA ALA B . n 
B 1 462 ALA 462 462 462 ALA ALA B . n 
B 1 463 GLU 463 463 463 GLU GLU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 TYR 465 465 465 TYR TYR B . n 
B 1 466 GLY 466 466 466 GLY GLY B . n 
B 1 467 GLU 467 467 467 GLU GLU B . n 
B 1 468 TYR 468 468 468 TYR TYR B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 THR 470 470 470 THR THR B . n 
B 1 471 HIS 471 471 471 HIS HIS B . n 
B 1 472 ILE 472 472 472 ILE ILE B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 TYR 474 474 474 TYR TYR B . n 
B 1 475 MET 475 475 475 MET MET B . n 
B 1 476 ASP 476 476 476 ASP ASP B . n 
B 1 477 ARG 477 477 477 ARG ARG B . n 
B 1 478 ILE 478 478 478 ILE ILE B . n 
B 1 479 ALA 479 479 479 ALA ALA B . n 
B 1 480 LYS 480 480 480 LYS LYS B . n 
B 1 481 THR 481 481 481 THR THR B . n 
B 1 482 TYR 482 482 482 TYR TYR B . n 
B 1 483 SER 483 483 483 SER SER B . n 
B 1 484 TRP 484 484 484 TRP TRP B . n 
B 1 485 ASN 485 485 485 ASN ASN B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 ASN 487 487 487 ASN ASN B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 LEU 489 489 489 LEU LEU B . n 
B 1 490 TRP 490 490 490 TRP TRP B . n 
B 1 491 LYS 491 491 491 LYS LYS B . n 
B 1 492 MET 492 492 492 MET MET B . n 
B 1 493 HIS 493 493 493 HIS HIS B . n 
B 1 494 GLU 494 494 494 GLU GLU B . n 
B 1 495 THR 495 495 495 THR THR B . n 
B 1 496 ILE 496 496 496 ILE ILE B . n 
B 1 497 LYS 497 497 497 LYS LYS B . n 
B 1 498 ASP 498 498 498 ASP ASP B . n 
B 1 499 ALA 499 499 499 ALA ALA B . n 
B 1 500 LEU 500 500 500 LEU LEU B . n 
B 1 501 ASP 501 501 501 ASP ASP B . n 
B 1 502 PRO 502 502 502 PRO PRO B . n 
B 1 503 ASN 503 503 503 ASN ASN B . n 
B 1 504 GLY 504 504 504 GLY GLY B . n 
B 1 505 ILE 505 505 505 ILE ILE B . n 
B 1 506 LEU 506 506 506 LEU LEU B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 PRO 508 508 508 PRO PRO B . n 
B 1 509 GLY 509 509 509 GLY GLY B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 SER 511 511 511 SER SER B . n 
B 1 512 GLY 512 512 512 GLY GLY B . n 
B 1 513 ILE 513 513 513 ILE ILE B . n 
B 1 514 TRP 514 514 514 TRP TRP B . n 
B 1 515 GLY 515 515 515 GLY GLY B . n 
B 1 516 LYS 516 516 516 LYS LYS B . n 
B 1 517 ASN 517 517 517 ASN ASN B . n 
B 1 518 ARG 518 518 518 ARG ARG B . n 
B 1 519 ARG 519 519 519 ARG ARG B . n 
B 1 520 LYS 520 520 ?   ?   ?   B . n 
B 1 521 ALA 521 521 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_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 FAD 1   601  601 FAD FAD A . 
D 3 CL  1   602  605 CL  CL  A . 
E 3 CL  1   603  606 CL  CL  A . 
F 4 PEG 1   604  607 PEG PEG A . 
G 4 PEG 1   605  609 PEG PEG A . 
H 4 PEG 1   606  610 PEG PEG A . 
I 2 FAD 1   601  601 FAD FAD B . 
J 4 PEG 1   602  605 PEG PEG B . 
K 4 PEG 1   603  606 PEG PEG B . 
L 4 PEG 1   604  607 PEG PEG B . 
M 4 PEG 1   605  608 PEG PEG B . 
N 4 PEG 1   606  609 PEG PEG B . 
O 3 CL  1   607  610 CL  CL  B . 
P 3 CL  1   608  611 CL  CL  B . 
Q 3 CL  1   609  612 CL  CL  B . 
R 5 HOH 1   701  86  HOH HOH A . 
R 5 HOH 2   702  451 HOH HOH A . 
R 5 HOH 3   703  512 HOH HOH A . 
R 5 HOH 4   704  310 HOH HOH A . 
R 5 HOH 5   705  445 HOH HOH A . 
R 5 HOH 6   706  244 HOH HOH A . 
R 5 HOH 7   707  371 HOH HOH A . 
R 5 HOH 8   708  197 HOH HOH A . 
R 5 HOH 9   709  56  HOH HOH A . 
R 5 HOH 10  710  92  HOH HOH A . 
R 5 HOH 11  711  488 HOH HOH A . 
R 5 HOH 12  712  337 HOH HOH A . 
R 5 HOH 13  713  146 HOH HOH A . 
R 5 HOH 14  714  464 HOH HOH A . 
R 5 HOH 15  715  78  HOH HOH A . 
R 5 HOH 16  716  379 HOH HOH A . 
R 5 HOH 17  717  55  HOH HOH A . 
R 5 HOH 18  718  568 HOH HOH A . 
R 5 HOH 19  719  62  HOH HOH A . 
R 5 HOH 20  720  97  HOH HOH A . 
R 5 HOH 21  721  247 HOH HOH A . 
R 5 HOH 22  722  412 HOH HOH A . 
R 5 HOH 23  723  129 HOH HOH A . 
R 5 HOH 24  724  18  HOH HOH A . 
R 5 HOH 25  725  45  HOH HOH A . 
R 5 HOH 26  726  573 HOH HOH A . 
R 5 HOH 27  727  395 HOH HOH A . 
R 5 HOH 28  728  424 HOH HOH A . 
R 5 HOH 29  729  123 HOH HOH A . 
R 5 HOH 30  730  63  HOH HOH A . 
R 5 HOH 31  731  169 HOH HOH A . 
R 5 HOH 32  732  210 HOH HOH A . 
R 5 HOH 33  733  2   HOH HOH A . 
R 5 HOH 34  734  231 HOH HOH A . 
R 5 HOH 35  735  10  HOH HOH A . 
R 5 HOH 36  736  3   HOH HOH A . 
R 5 HOH 37  737  376 HOH HOH A . 
R 5 HOH 38  738  76  HOH HOH A . 
R 5 HOH 39  739  434 HOH HOH A . 
R 5 HOH 40  740  241 HOH HOH A . 
R 5 HOH 41  741  193 HOH HOH A . 
R 5 HOH 42  742  199 HOH HOH A . 
R 5 HOH 43  743  30  HOH HOH A . 
R 5 HOH 44  744  184 HOH HOH A . 
R 5 HOH 45  745  233 HOH HOH A . 
R 5 HOH 46  746  168 HOH HOH A . 
R 5 HOH 47  747  230 HOH HOH A . 
R 5 HOH 48  748  99  HOH HOH A . 
R 5 HOH 49  749  144 HOH HOH A . 
R 5 HOH 50  750  523 HOH HOH A . 
R 5 HOH 51  751  82  HOH HOH A . 
R 5 HOH 52  752  108 HOH HOH A . 
R 5 HOH 53  753  19  HOH HOH A . 
R 5 HOH 54  754  283 HOH HOH A . 
R 5 HOH 55  755  317 HOH HOH A . 
R 5 HOH 56  756  182 HOH HOH A . 
R 5 HOH 57  757  286 HOH HOH A . 
R 5 HOH 58  758  39  HOH HOH A . 
R 5 HOH 59  759  192 HOH HOH A . 
R 5 HOH 60  760  548 HOH HOH A . 
R 5 HOH 61  761  16  HOH HOH A . 
R 5 HOH 62  762  170 HOH HOH A . 
R 5 HOH 63  763  77  HOH HOH A . 
R 5 HOH 64  764  14  HOH HOH A . 
R 5 HOH 65  765  69  HOH HOH A . 
R 5 HOH 66  766  206 HOH HOH A . 
R 5 HOH 67  767  11  HOH HOH A . 
R 5 HOH 68  768  106 HOH HOH A . 
R 5 HOH 69  769  302 HOH HOH A . 
R 5 HOH 70  770  349 HOH HOH A . 
R 5 HOH 71  771  326 HOH HOH A . 
R 5 HOH 72  772  453 HOH HOH A . 
R 5 HOH 73  773  570 HOH HOH A . 
R 5 HOH 74  774  133 HOH HOH A . 
R 5 HOH 75  775  306 HOH HOH A . 
R 5 HOH 76  776  542 HOH HOH A . 
R 5 HOH 77  777  314 HOH HOH A . 
R 5 HOH 78  778  57  HOH HOH A . 
R 5 HOH 79  779  347 HOH HOH A . 
R 5 HOH 80  780  138 HOH HOH A . 
R 5 HOH 81  781  113 HOH HOH A . 
R 5 HOH 82  782  87  HOH HOH A . 
R 5 HOH 83  783  391 HOH HOH A . 
R 5 HOH 84  784  558 HOH HOH A . 
R 5 HOH 85  785  209 HOH HOH A . 
R 5 HOH 86  786  160 HOH HOH A . 
R 5 HOH 87  787  339 HOH HOH A . 
R 5 HOH 88  788  497 HOH HOH A . 
R 5 HOH 89  789  222 HOH HOH A . 
R 5 HOH 90  790  280 HOH HOH A . 
R 5 HOH 91  791  174 HOH HOH A . 
R 5 HOH 92  792  362 HOH HOH A . 
R 5 HOH 93  793  572 HOH HOH A . 
R 5 HOH 94  794  235 HOH HOH A . 
R 5 HOH 95  795  217 HOH HOH A . 
R 5 HOH 96  796  413 HOH HOH A . 
R 5 HOH 97  797  153 HOH HOH A . 
R 5 HOH 98  798  94  HOH HOH A . 
R 5 HOH 99  799  559 HOH HOH A . 
R 5 HOH 100 800  375 HOH HOH A . 
R 5 HOH 101 801  246 HOH HOH A . 
R 5 HOH 102 802  518 HOH HOH A . 
R 5 HOH 103 803  161 HOH HOH A . 
R 5 HOH 104 804  356 HOH HOH A . 
R 5 HOH 105 805  152 HOH HOH A . 
R 5 HOH 106 806  236 HOH HOH A . 
R 5 HOH 107 807  48  HOH HOH A . 
R 5 HOH 108 808  44  HOH HOH A . 
R 5 HOH 109 809  273 HOH HOH A . 
R 5 HOH 110 810  53  HOH HOH A . 
R 5 HOH 111 811  397 HOH HOH A . 
R 5 HOH 112 812  54  HOH HOH A . 
R 5 HOH 113 813  555 HOH HOH A . 
R 5 HOH 114 814  479 HOH HOH A . 
R 5 HOH 115 815  284 HOH HOH A . 
R 5 HOH 116 816  6   HOH HOH A . 
R 5 HOH 117 817  543 HOH HOH A . 
R 5 HOH 118 818  383 HOH HOH A . 
R 5 HOH 119 819  538 HOH HOH A . 
R 5 HOH 120 820  372 HOH HOH A . 
R 5 HOH 121 821  315 HOH HOH A . 
R 5 HOH 122 822  7   HOH HOH A . 
R 5 HOH 123 823  382 HOH HOH A . 
R 5 HOH 124 824  88  HOH HOH A . 
R 5 HOH 125 825  5   HOH HOH A . 
R 5 HOH 126 826  41  HOH HOH A . 
R 5 HOH 127 827  459 HOH HOH A . 
R 5 HOH 128 828  269 HOH HOH A . 
R 5 HOH 129 829  21  HOH HOH A . 
R 5 HOH 130 830  100 HOH HOH A . 
R 5 HOH 131 831  312 HOH HOH A . 
R 5 HOH 132 832  131 HOH HOH A . 
R 5 HOH 133 833  332 HOH HOH A . 
R 5 HOH 134 834  60  HOH HOH A . 
R 5 HOH 135 835  147 HOH HOH A . 
R 5 HOH 136 836  325 HOH HOH A . 
R 5 HOH 137 837  561 HOH HOH A . 
R 5 HOH 138 838  355 HOH HOH A . 
R 5 HOH 139 839  380 HOH HOH A . 
R 5 HOH 140 840  140 HOH HOH A . 
R 5 HOH 141 841  107 HOH HOH A . 
R 5 HOH 142 842  185 HOH HOH A . 
R 5 HOH 143 843  505 HOH HOH A . 
R 5 HOH 144 844  544 HOH HOH A . 
R 5 HOH 145 845  118 HOH HOH A . 
R 5 HOH 146 846  540 HOH HOH A . 
R 5 HOH 147 847  390 HOH HOH A . 
R 5 HOH 148 848  135 HOH HOH A . 
R 5 HOH 149 849  366 HOH HOH A . 
R 5 HOH 150 850  519 HOH HOH A . 
R 5 HOH 151 851  344 HOH HOH A . 
R 5 HOH 152 852  81  HOH HOH A . 
R 5 HOH 153 853  102 HOH HOH A . 
R 5 HOH 154 854  208 HOH HOH A . 
R 5 HOH 155 855  122 HOH HOH A . 
R 5 HOH 156 856  1   HOH HOH A . 
R 5 HOH 157 857  212 HOH HOH A . 
R 5 HOH 158 858  313 HOH HOH A . 
R 5 HOH 159 859  282 HOH HOH A . 
R 5 HOH 160 860  148 HOH HOH A . 
R 5 HOH 161 861  351 HOH HOH A . 
R 5 HOH 162 862  61  HOH HOH A . 
R 5 HOH 163 863  394 HOH HOH A . 
R 5 HOH 164 864  58  HOH HOH A . 
R 5 HOH 165 865  137 HOH HOH A . 
R 5 HOH 166 866  343 HOH HOH A . 
R 5 HOH 167 867  38  HOH HOH A . 
R 5 HOH 168 868  348 HOH HOH A . 
R 5 HOH 169 869  335 HOH HOH A . 
R 5 HOH 170 870  256 HOH HOH A . 
R 5 HOH 171 871  368 HOH HOH A . 
R 5 HOH 172 872  159 HOH HOH A . 
R 5 HOH 173 873  551 HOH HOH A . 
R 5 HOH 174 874  28  HOH HOH A . 
R 5 HOH 175 875  266 HOH HOH A . 
R 5 HOH 176 876  501 HOH HOH A . 
R 5 HOH 177 877  139 HOH HOH A . 
R 5 HOH 178 878  121 HOH HOH A . 
R 5 HOH 179 879  188 HOH HOH A . 
R 5 HOH 180 880  74  HOH HOH A . 
R 5 HOH 181 881  179 HOH HOH A . 
R 5 HOH 182 882  473 HOH HOH A . 
R 5 HOH 183 883  8   HOH HOH A . 
R 5 HOH 184 884  323 HOH HOH A . 
R 5 HOH 185 885  143 HOH HOH A . 
R 5 HOH 186 886  276 HOH HOH A . 
R 5 HOH 187 887  520 HOH HOH A . 
R 5 HOH 188 888  408 HOH HOH A . 
R 5 HOH 189 889  387 HOH HOH A . 
R 5 HOH 190 890  117 HOH HOH A . 
R 5 HOH 191 891  126 HOH HOH A . 
R 5 HOH 192 892  91  HOH HOH A . 
R 5 HOH 193 893  560 HOH HOH A . 
R 5 HOH 194 894  270 HOH HOH A . 
R 5 HOH 195 895  287 HOH HOH A . 
R 5 HOH 196 896  409 HOH HOH A . 
R 5 HOH 197 897  204 HOH HOH A . 
R 5 HOH 198 898  320 HOH HOH A . 
R 5 HOH 199 899  191 HOH HOH A . 
R 5 HOH 200 900  136 HOH HOH A . 
R 5 HOH 201 901  352 HOH HOH A . 
R 5 HOH 202 902  393 HOH HOH A . 
R 5 HOH 203 903  17  HOH HOH A . 
R 5 HOH 204 904  483 HOH HOH A . 
R 5 HOH 205 905  377 HOH HOH A . 
R 5 HOH 206 906  441 HOH HOH A . 
R 5 HOH 207 907  414 HOH HOH A . 
R 5 HOH 208 908  575 HOH HOH A . 
R 5 HOH 209 909  65  HOH HOH A . 
R 5 HOH 210 910  321 HOH HOH A . 
R 5 HOH 211 911  32  HOH HOH A . 
R 5 HOH 212 912  234 HOH HOH A . 
R 5 HOH 213 913  239 HOH HOH A . 
R 5 HOH 214 914  531 HOH HOH A . 
R 5 HOH 215 915  207 HOH HOH A . 
R 5 HOH 216 916  277 HOH HOH A . 
R 5 HOH 217 917  71  HOH HOH A . 
R 5 HOH 218 918  525 HOH HOH A . 
R 5 HOH 219 919  333 HOH HOH A . 
R 5 HOH 220 920  550 HOH HOH A . 
R 5 HOH 221 921  295 HOH HOH A . 
R 5 HOH 222 922  419 HOH HOH A . 
R 5 HOH 223 923  506 HOH HOH A . 
R 5 HOH 224 924  149 HOH HOH A . 
R 5 HOH 225 925  318 HOH HOH A . 
R 5 HOH 226 926  405 HOH HOH A . 
R 5 HOH 227 927  433 HOH HOH A . 
R 5 HOH 228 928  417 HOH HOH A . 
R 5 HOH 229 929  268 HOH HOH A . 
R 5 HOH 230 930  324 HOH HOH A . 
R 5 HOH 231 931  171 HOH HOH A . 
R 5 HOH 232 932  262 HOH HOH A . 
R 5 HOH 233 933  334 HOH HOH A . 
R 5 HOH 234 934  265 HOH HOH A . 
R 5 HOH 235 935  84  HOH HOH A . 
R 5 HOH 236 936  565 HOH HOH A . 
R 5 HOH 237 937  363 HOH HOH A . 
R 5 HOH 238 938  384 HOH HOH A . 
R 5 HOH 239 939  232 HOH HOH A . 
R 5 HOH 240 940  259 HOH HOH A . 
R 5 HOH 241 941  167 HOH HOH A . 
R 5 HOH 242 942  374 HOH HOH A . 
R 5 HOH 243 943  517 HOH HOH A . 
R 5 HOH 244 944  250 HOH HOH A . 
R 5 HOH 245 945  196 HOH HOH A . 
R 5 HOH 246 946  466 HOH HOH A . 
R 5 HOH 247 947  582 HOH HOH A . 
R 5 HOH 248 948  35  HOH HOH A . 
R 5 HOH 249 949  328 HOH HOH A . 
R 5 HOH 250 950  457 HOH HOH A . 
R 5 HOH 251 951  294 HOH HOH A . 
R 5 HOH 252 952  503 HOH HOH A . 
R 5 HOH 253 953  216 HOH HOH A . 
R 5 HOH 254 954  421 HOH HOH A . 
R 5 HOH 255 955  49  HOH HOH A . 
R 5 HOH 256 956  549 HOH HOH A . 
R 5 HOH 257 957  172 HOH HOH A . 
R 5 HOH 258 958  260 HOH HOH A . 
R 5 HOH 259 959  442 HOH HOH A . 
R 5 HOH 260 960  220 HOH HOH A . 
R 5 HOH 261 961  422 HOH HOH A . 
R 5 HOH 262 962  515 HOH HOH A . 
R 5 HOH 263 963  462 HOH HOH A . 
R 5 HOH 264 964  389 HOH HOH A . 
R 5 HOH 265 965  350 HOH HOH A . 
R 5 HOH 266 966  440 HOH HOH A . 
R 5 HOH 267 967  189 HOH HOH A . 
R 5 HOH 268 968  463 HOH HOH A . 
R 5 HOH 269 969  228 HOH HOH A . 
R 5 HOH 270 970  298 HOH HOH A . 
R 5 HOH 271 971  438 HOH HOH A . 
R 5 HOH 272 972  327 HOH HOH A . 
R 5 HOH 273 973  516 HOH HOH A . 
R 5 HOH 274 974  163 HOH HOH A . 
R 5 HOH 275 975  114 HOH HOH A . 
R 5 HOH 276 976  502 HOH HOH A . 
R 5 HOH 277 977  498 HOH HOH A . 
R 5 HOH 278 978  242 HOH HOH A . 
R 5 HOH 279 979  504 HOH HOH A . 
R 5 HOH 280 980  472 HOH HOH A . 
R 5 HOH 281 981  458 HOH HOH A . 
R 5 HOH 282 982  142 HOH HOH A . 
R 5 HOH 283 983  436 HOH HOH A . 
R 5 HOH 284 984  20  HOH HOH A . 
R 5 HOH 285 985  418 HOH HOH A . 
R 5 HOH 286 986  443 HOH HOH A . 
R 5 HOH 287 987  40  HOH HOH A . 
R 5 HOH 288 988  508 HOH HOH A . 
R 5 HOH 289 989  116 HOH HOH A . 
R 5 HOH 290 990  581 HOH HOH A . 
R 5 HOH 291 991  513 HOH HOH A . 
R 5 HOH 292 992  507 HOH HOH A . 
R 5 HOH 293 993  461 HOH HOH A . 
R 5 HOH 294 994  435 HOH HOH A . 
R 5 HOH 295 995  439 HOH HOH A . 
R 5 HOH 296 996  492 HOH HOH A . 
R 5 HOH 297 997  162 HOH HOH A . 
R 5 HOH 298 998  254 HOH HOH A . 
R 5 HOH 299 999  432 HOH HOH A . 
R 5 HOH 300 1000 484 HOH HOH A . 
R 5 HOH 301 1001 156 HOH HOH A . 
R 5 HOH 302 1002 437 HOH HOH A . 
R 5 HOH 303 1003 499 HOH HOH A . 
R 5 HOH 304 1004 467 HOH HOH A . 
R 5 HOH 305 1005 452 HOH HOH A . 
R 5 HOH 306 1006 173 HOH HOH A . 
R 5 HOH 307 1007 493 HOH HOH A . 
R 5 HOH 308 1008 237 HOH HOH A . 
R 5 HOH 309 1009 130 HOH HOH A . 
R 5 HOH 310 1010 487 HOH HOH A . 
R 5 HOH 311 1011 584 HOH HOH A . 
R 5 HOH 312 1012 446 HOH HOH A . 
R 5 HOH 313 1013 450 HOH HOH A . 
R 5 HOH 314 1014 195 HOH HOH A . 
R 5 HOH 315 1015 455 HOH HOH A . 
R 5 HOH 316 1016 253 HOH HOH A . 
R 5 HOH 317 1017 465 HOH HOH A . 
R 5 HOH 318 1018 454 HOH HOH A . 
R 5 HOH 319 1019 471 HOH HOH A . 
R 5 HOH 320 1020 25  HOH HOH A . 
R 5 HOH 321 1021 481 HOH HOH A . 
R 5 HOH 322 1022 215 HOH HOH A . 
R 5 HOH 323 1023 444 HOH HOH A . 
R 5 HOH 324 1024 474 HOH HOH A . 
S 5 HOH 1   701  511 HOH HOH B . 
S 5 HOH 2   702  509 HOH HOH B . 
S 5 HOH 3   703  299 HOH HOH B . 
S 5 HOH 4   704  311 HOH HOH B . 
S 5 HOH 5   705  535 HOH HOH B . 
S 5 HOH 6   706  316 HOH HOH B . 
S 5 HOH 7   707  510 HOH HOH B . 
S 5 HOH 8   708  415 HOH HOH B . 
S 5 HOH 9   709  26  HOH HOH B . 
S 5 HOH 10  710  345 HOH HOH B . 
S 5 HOH 11  711  158 HOH HOH B . 
S 5 HOH 12  712  103 HOH HOH B . 
S 5 HOH 13  713  9   HOH HOH B . 
S 5 HOH 14  714  496 HOH HOH B . 
S 5 HOH 15  715  456 HOH HOH B . 
S 5 HOH 16  716  426 HOH HOH B . 
S 5 HOH 17  717  304 HOH HOH B . 
S 5 HOH 18  718  381 HOH HOH B . 
S 5 HOH 19  719  67  HOH HOH B . 
S 5 HOH 20  720  13  HOH HOH B . 
S 5 HOH 21  721  553 HOH HOH B . 
S 5 HOH 22  722  85  HOH HOH B . 
S 5 HOH 23  723  470 HOH HOH B . 
S 5 HOH 24  724  164 HOH HOH B . 
S 5 HOH 25  725  289 HOH HOH B . 
S 5 HOH 26  726  354 HOH HOH B . 
S 5 HOH 27  727  43  HOH HOH B . 
S 5 HOH 28  728  521 HOH HOH B . 
S 5 HOH 29  729  110 HOH HOH B . 
S 5 HOH 30  730  225 HOH HOH B . 
S 5 HOH 31  731  176 HOH HOH B . 
S 5 HOH 32  732  75  HOH HOH B . 
S 5 HOH 33  733  154 HOH HOH B . 
S 5 HOH 34  734  223 HOH HOH B . 
S 5 HOH 35  735  403 HOH HOH B . 
S 5 HOH 36  736  79  HOH HOH B . 
S 5 HOH 37  737  552 HOH HOH B . 
S 5 HOH 38  738  357 HOH HOH B . 
S 5 HOH 39  739  322 HOH HOH B . 
S 5 HOH 40  740  562 HOH HOH B . 
S 5 HOH 41  741  416 HOH HOH B . 
S 5 HOH 42  742  132 HOH HOH B . 
S 5 HOH 43  743  373 HOH HOH B . 
S 5 HOH 44  744  539 HOH HOH B . 
S 5 HOH 45  745  141 HOH HOH B . 
S 5 HOH 46  746  128 HOH HOH B . 
S 5 HOH 47  747  336 HOH HOH B . 
S 5 HOH 48  748  300 HOH HOH B . 
S 5 HOH 49  749  202 HOH HOH B . 
S 5 HOH 50  750  178 HOH HOH B . 
S 5 HOH 51  751  112 HOH HOH B . 
S 5 HOH 52  752  252 HOH HOH B . 
S 5 HOH 53  753  104 HOH HOH B . 
S 5 HOH 54  754  120 HOH HOH B . 
S 5 HOH 55  755  23  HOH HOH B . 
S 5 HOH 56  756  340 HOH HOH B . 
S 5 HOH 57  757  22  HOH HOH B . 
S 5 HOH 58  758  261 HOH HOH B . 
S 5 HOH 59  759  534 HOH HOH B . 
S 5 HOH 60  760  411 HOH HOH B . 
S 5 HOH 61  761  574 HOH HOH B . 
S 5 HOH 62  762  528 HOH HOH B . 
S 5 HOH 63  763  124 HOH HOH B . 
S 5 HOH 64  764  15  HOH HOH B . 
S 5 HOH 65  765  155 HOH HOH B . 
S 5 HOH 66  766  227 HOH HOH B . 
S 5 HOH 67  767  73  HOH HOH B . 
S 5 HOH 68  768  307 HOH HOH B . 
S 5 HOH 69  769  240 HOH HOH B . 
S 5 HOH 70  770  301 HOH HOH B . 
S 5 HOH 71  771  80  HOH HOH B . 
S 5 HOH 72  772  24  HOH HOH B . 
S 5 HOH 73  773  90  HOH HOH B . 
S 5 HOH 74  774  125 HOH HOH B . 
S 5 HOH 75  775  329 HOH HOH B . 
S 5 HOH 76  776  367 HOH HOH B . 
S 5 HOH 77  777  401 HOH HOH B . 
S 5 HOH 78  778  309 HOH HOH B . 
S 5 HOH 79  779  308 HOH HOH B . 
S 5 HOH 80  780  181 HOH HOH B . 
S 5 HOH 81  781  541 HOH HOH B . 
S 5 HOH 82  782  468 HOH HOH B . 
S 5 HOH 83  783  275 HOH HOH B . 
S 5 HOH 84  784  187 HOH HOH B . 
S 5 HOH 85  785  101 HOH HOH B . 
S 5 HOH 86  786  566 HOH HOH B . 
S 5 HOH 87  787  546 HOH HOH B . 
S 5 HOH 88  788  59  HOH HOH B . 
S 5 HOH 89  789  186 HOH HOH B . 
S 5 HOH 90  790  400 HOH HOH B . 
S 5 HOH 91  791  491 HOH HOH B . 
S 5 HOH 92  792  278 HOH HOH B . 
S 5 HOH 93  793  205 HOH HOH B . 
S 5 HOH 94  794  213 HOH HOH B . 
S 5 HOH 95  795  360 HOH HOH B . 
S 5 HOH 96  796  291 HOH HOH B . 
S 5 HOH 97  797  95  HOH HOH B . 
S 5 HOH 98  798  296 HOH HOH B . 
S 5 HOH 99  799  211 HOH HOH B . 
S 5 HOH 100 800  564 HOH HOH B . 
S 5 HOH 101 801  274 HOH HOH B . 
S 5 HOH 102 802  406 HOH HOH B . 
S 5 HOH 103 803  330 HOH HOH B . 
S 5 HOH 104 804  96  HOH HOH B . 
S 5 HOH 105 805  50  HOH HOH B . 
S 5 HOH 106 806  70  HOH HOH B . 
S 5 HOH 107 807  150 HOH HOH B . 
S 5 HOH 108 808  396 HOH HOH B . 
S 5 HOH 109 809  554 HOH HOH B . 
S 5 HOH 110 810  285 HOH HOH B . 
S 5 HOH 111 811  93  HOH HOH B . 
S 5 HOH 112 812  547 HOH HOH B . 
S 5 HOH 113 813  342 HOH HOH B . 
S 5 HOH 114 814  388 HOH HOH B . 
S 5 HOH 115 815  571 HOH HOH B . 
S 5 HOH 116 816  201 HOH HOH B . 
S 5 HOH 117 817  98  HOH HOH B . 
S 5 HOH 118 818  556 HOH HOH B . 
S 5 HOH 119 819  279 HOH HOH B . 
S 5 HOH 120 820  27  HOH HOH B . 
S 5 HOH 121 821  175 HOH HOH B . 
S 5 HOH 122 822  66  HOH HOH B . 
S 5 HOH 123 823  359 HOH HOH B . 
S 5 HOH 124 824  119 HOH HOH B . 
S 5 HOH 125 825  115 HOH HOH B . 
S 5 HOH 126 826  46  HOH HOH B . 
S 5 HOH 127 827  134 HOH HOH B . 
S 5 HOH 128 828  536 HOH HOH B . 
S 5 HOH 129 829  569 HOH HOH B . 
S 5 HOH 130 830  258 HOH HOH B . 
S 5 HOH 131 831  200 HOH HOH B . 
S 5 HOH 132 832  165 HOH HOH B . 
S 5 HOH 133 833  353 HOH HOH B . 
S 5 HOH 134 834  52  HOH HOH B . 
S 5 HOH 135 835  293 HOH HOH B . 
S 5 HOH 136 836  249 HOH HOH B . 
S 5 HOH 137 837  425 HOH HOH B . 
S 5 HOH 138 838  545 HOH HOH B . 
S 5 HOH 139 839  370 HOH HOH B . 
S 5 HOH 140 840  37  HOH HOH B . 
S 5 HOH 141 841  51  HOH HOH B . 
S 5 HOH 142 842  29  HOH HOH B . 
S 5 HOH 143 843  109 HOH HOH B . 
S 5 HOH 144 844  12  HOH HOH B . 
S 5 HOH 145 845  180 HOH HOH B . 
S 5 HOH 146 846  229 HOH HOH B . 
S 5 HOH 147 847  72  HOH HOH B . 
S 5 HOH 148 848  532 HOH HOH B . 
S 5 HOH 149 849  563 HOH HOH B . 
S 5 HOH 150 850  341 HOH HOH B . 
S 5 HOH 151 851  288 HOH HOH B . 
S 5 HOH 152 852  364 HOH HOH B . 
S 5 HOH 153 853  31  HOH HOH B . 
S 5 HOH 154 854  33  HOH HOH B . 
S 5 HOH 155 855  407 HOH HOH B . 
S 5 HOH 156 856  369 HOH HOH B . 
S 5 HOH 157 857  529 HOH HOH B . 
S 5 HOH 158 858  83  HOH HOH B . 
S 5 HOH 159 859  305 HOH HOH B . 
S 5 HOH 160 860  385 HOH HOH B . 
S 5 HOH 161 861  398 HOH HOH B . 
S 5 HOH 162 862  34  HOH HOH B . 
S 5 HOH 163 863  42  HOH HOH B . 
S 5 HOH 164 864  272 HOH HOH B . 
S 5 HOH 165 865  530 HOH HOH B . 
S 5 HOH 166 866  522 HOH HOH B . 
S 5 HOH 167 867  290 HOH HOH B . 
S 5 HOH 168 868  365 HOH HOH B . 
S 5 HOH 169 869  358 HOH HOH B . 
S 5 HOH 170 870  410 HOH HOH B . 
S 5 HOH 171 871  477 HOH HOH B . 
S 5 HOH 172 872  533 HOH HOH B . 
S 5 HOH 173 873  579 HOH HOH B . 
S 5 HOH 174 874  214 HOH HOH B . 
S 5 HOH 175 875  166 HOH HOH B . 
S 5 HOH 176 876  271 HOH HOH B . 
S 5 HOH 177 877  263 HOH HOH B . 
S 5 HOH 178 878  267 HOH HOH B . 
S 5 HOH 179 879  319 HOH HOH B . 
S 5 HOH 180 880  386 HOH HOH B . 
S 5 HOH 181 881  151 HOH HOH B . 
S 5 HOH 182 882  198 HOH HOH B . 
S 5 HOH 183 883  475 HOH HOH B . 
S 5 HOH 184 884  257 HOH HOH B . 
S 5 HOH 185 885  292 HOH HOH B . 
S 5 HOH 186 886  537 HOH HOH B . 
S 5 HOH 187 887  194 HOH HOH B . 
S 5 HOH 188 888  64  HOH HOH B . 
S 5 HOH 189 889  127 HOH HOH B . 
S 5 HOH 190 890  331 HOH HOH B . 
S 5 HOH 191 891  281 HOH HOH B . 
S 5 HOH 192 892  402 HOH HOH B . 
S 5 HOH 193 893  526 HOH HOH B . 
S 5 HOH 194 894  490 HOH HOH B . 
S 5 HOH 195 895  219 HOH HOH B . 
S 5 HOH 196 896  420 HOH HOH B . 
S 5 HOH 197 897  303 HOH HOH B . 
S 5 HOH 198 898  68  HOH HOH B . 
S 5 HOH 199 899  494 HOH HOH B . 
S 5 HOH 200 900  404 HOH HOH B . 
S 5 HOH 201 901  245 HOH HOH B . 
S 5 HOH 202 902  346 HOH HOH B . 
S 5 HOH 203 903  399 HOH HOH B . 
S 5 HOH 204 904  264 HOH HOH B . 
S 5 HOH 205 905  177 HOH HOH B . 
S 5 HOH 206 906  361 HOH HOH B . 
S 5 HOH 207 907  577 HOH HOH B . 
S 5 HOH 208 908  527 HOH HOH B . 
S 5 HOH 209 909  557 HOH HOH B . 
S 5 HOH 210 910  218 HOH HOH B . 
S 5 HOH 211 911  586 HOH HOH B . 
S 5 HOH 212 912  576 HOH HOH B . 
S 5 HOH 213 913  583 HOH HOH B . 
S 5 HOH 214 914  392 HOH HOH B . 
S 5 HOH 215 915  89  HOH HOH B . 
S 5 HOH 216 916  297 HOH HOH B . 
S 5 HOH 217 917  476 HOH HOH B . 
S 5 HOH 218 918  428 HOH HOH B . 
S 5 HOH 219 919  431 HOH HOH B . 
S 5 HOH 220 920  524 HOH HOH B . 
S 5 HOH 221 921  111 HOH HOH B . 
S 5 HOH 222 922  486 HOH HOH B . 
S 5 HOH 223 923  338 HOH HOH B . 
S 5 HOH 224 924  427 HOH HOH B . 
S 5 HOH 225 925  429 HOH HOH B . 
S 5 HOH 226 926  495 HOH HOH B . 
S 5 HOH 227 927  145 HOH HOH B . 
S 5 HOH 228 928  500 HOH HOH B . 
S 5 HOH 229 929  460 HOH HOH B . 
S 5 HOH 230 930  469 HOH HOH B . 
S 5 HOH 231 931  449 HOH HOH B . 
S 5 HOH 232 932  489 HOH HOH B . 
S 5 HOH 233 933  447 HOH HOH B . 
S 5 HOH 234 934  224 HOH HOH B . 
S 5 HOH 235 935  430 HOH HOH B . 
S 5 HOH 236 936  105 HOH HOH B . 
S 5 HOH 237 937  47  HOH HOH B . 
S 5 HOH 238 938  221 HOH HOH B . 
S 5 HOH 239 939  567 HOH HOH B . 
S 5 HOH 240 940  226 HOH HOH B . 
S 5 HOH 241 941  585 HOH HOH B . 
S 5 HOH 242 942  243 HOH HOH B . 
S 5 HOH 243 943  251 HOH HOH B . 
S 5 HOH 244 944  482 HOH HOH B . 
S 5 HOH 245 945  589 HOH HOH B . 
S 5 HOH 246 946  478 HOH HOH B . 
S 5 HOH 247 947  255 HOH HOH B . 
S 5 HOH 248 948  183 HOH HOH B . 
S 5 HOH 249 949  485 HOH HOH B . 
S 5 HOH 250 950  248 HOH HOH B . 
S 5 HOH 251 951  588 HOH HOH B . 
S 5 HOH 252 952  203 HOH HOH B . 
S 5 HOH 253 953  580 HOH HOH B . 
S 5 HOH 254 954  190 HOH HOH B . 
S 5 HOH 255 955  448 HOH HOH B . 
S 5 HOH 256 956  514 HOH HOH B . 
S 5 HOH 257 957  238 HOH HOH B . 
S 5 HOH 258 958  587 HOH HOH B . 
S 5 HOH 259 959  36  HOH HOH B . 
S 5 HOH 260 960  378 HOH HOH B . 
S 5 HOH 261 961  157 HOH HOH B . 
S 5 HOH 262 962  423 HOH HOH B . 
S 5 HOH 263 963  4   HOH HOH B . 
S 5 HOH 264 964  480 HOH HOH B . 
S 5 HOH 265 965  578 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 B MET 1   ? CG  ? B MET 1   CG  
2 1 Y 1 B MET 1   ? SD  ? B MET 1   SD  
3 1 Y 1 B MET 1   ? CE  ? B MET 1   CE  
4 1 Y 1 B ARG 354 ? CG  ? B ARG 354 CG  
5 1 Y 1 B ARG 354 ? CD  ? B ARG 354 CD  
6 1 Y 1 B ARG 354 ? NE  ? B ARG 354 NE  
7 1 Y 1 B ARG 354 ? CZ  ? B ARG 354 CZ  
8 1 Y 1 B ARG 354 ? NH1 ? B ARG 354 NH1 
9 1 Y 1 B ARG 354 ? NH2 ? B ARG 354 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S7W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.621 
_cell.length_a_esd                 ? 
_cell.length_b                     114.641 
_cell.length_b_esd                 ? 
_cell.length_c                     130.709 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8S7W 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8S7W 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.99 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Ammonium chloride and 20% w/v PEG 3350.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.999990 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999990 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S7W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               57.32 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     87358 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.182 
_reflns.pdbx_Rpim_I_all                                0.084 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       373164 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.989 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.159 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.10 
_reflns_shell.d_res_low                                     2.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           18272 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4434 
_reflns_shell.percent_possible_obs                          99.1 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.1 
_reflns_shell.pdbx_chi_squared                              1.03 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.294 
_reflns_shell.pdbx_Rpim_I_all                               0.603 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.394 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.132 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.45 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.63 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.18 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.606 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8S7W 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             49.86 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     82986 
_refine.ls_number_reflns_R_free                  4338 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.40 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17351 
_refine.ls_R_factor_R_free                       0.20928 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17162 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.160 
_refine.pdbx_overall_ESU_R_Free                  0.147 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.623 
_refine.overall_SU_ML                            0.116 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        49.86 
_refine_hist.number_atoms_solvent             589 
_refine_hist.number_atoms_total               8925 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8169 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         167 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.013  8565  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  7848  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.562  1.646  11650 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.343  1.578  18087 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.955  5.000  1036  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 37.150 22.217 442   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.332 15.000 1316  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 19.016 15.000 51    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  1062  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  9685  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1973  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.942  2.620  4150  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.942  2.619  4149  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.770  3.923  5184  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.769  3.924  5185  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.886  2.931  4415  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.886  2.932  4416  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.428  4.266  6467  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.645  30.973 9868  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.638  30.823 9762  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.155 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             322 
_refine_ls_shell.number_reflns_R_work             6091 
_refine_ls_shell.percent_reflns_obs               98.84 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.280 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.333 
# 
_struct.entry_id                     8S7W 
_struct.title                        'Vanillyl-alcohol dehydrogenase from Marinicaulis flavus: P151V mutant' 
_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        8S7W 
_struct_keywords.text            'FAD, flavin, oxidase, alcohol, enzyme mechanism, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 2 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 5 ? 
S N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2S7K3M2_9PROT 
_struct_ref.pdbx_db_accession          A0A2S7K3M2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDPGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_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 8S7W A 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
2 1 8S7W B 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8S7W VAL A 151 ? UNP A0A2S7K3M2 PRO 151 'engineered mutation' 151 1 
2 8S7W VAL B 151 ? UNP A0A2S7K3M2 PRO 151 'engineered mutation' 151 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13270 ? 
1 MORE         -111  ? 
1 'SSA (A^2)'  33640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 26  ? SER A 10  GLY A 26  1 ? 17 
HELX_P HELX_P2  AA2 THR A 32  ? GLU A 40  ? THR A 32  GLU A 40  5 ? 9  
HELX_P HELX_P3  AA3 SER A 62  ? GLY A 77  ? SER A 62  GLY A 77  1 ? 16 
HELX_P HELX_P4  AA4 SER A 129 ? LYS A 140 ? SER A 129 LYS A 140 1 ? 12 
HELX_P HELX_P5  AA5 SER A 155 ? ASP A 162 ? SER A 155 ASP A 162 1 ? 8  
HELX_P HELX_P6  AA6 HIS A 173 ? ALA A 175 ? HIS A 173 ALA A 175 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 193 ? MET A 197 ? GLY A 193 MET A 197 5 ? 5  
HELX_P HELX_P8  AA8 VAL A 214 ? SER A 219 ? VAL A 214 SER A 219 5 ? 6  
HELX_P HELX_P9  AA9 ASN A 249 ? ASP A 251 ? ASN A 249 ASP A 251 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 252 ? ALA A 266 ? ASP A 252 ALA A 266 1 ? 15 
HELX_P HELX_P11 AB2 LEU A 278 ? ARG A 286 ? LEU A 278 ARG A 286 1 ? 9  
HELX_P HELX_P12 AB3 THR A 287 ? TYR A 291 ? THR A 287 TYR A 291 5 ? 5  
HELX_P HELX_P13 AB4 PRO A 299 ? ASP A 311 ? PRO A 299 ASP A 311 1 ? 13 
HELX_P HELX_P14 AB5 PRO A 324 ? ALA A 340 ? PRO A 324 ALA A 340 1 ? 17 
HELX_P HELX_P15 AB6 PHE A 349 ? ARG A 353 ? PHE A 349 ARG A 353 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 358 ? MET A 367 ? ASP A 358 MET A 367 1 ? 10 
HELX_P HELX_P17 AB8 LEU A 373 ? TRP A 381 ? LEU A 373 TRP A 381 5 ? 9  
HELX_P HELX_P18 AB9 THR A 397 ? TYR A 415 ? THR A 397 TYR A 415 1 ? 19 
HELX_P HELX_P19 AC1 ASP A 442 ? GLU A 463 ? ASP A 442 GLU A 463 1 ? 22 
HELX_P HELX_P20 AC2 HIS A 471 ? ARG A 473 ? HIS A 471 ARG A 473 5 ? 3  
HELX_P HELX_P21 AC3 TYR A 474 ? TYR A 482 ? TYR A 474 TYR A 482 1 ? 9  
HELX_P HELX_P22 AC4 SER A 483 ? ASP A 501 ? SER A 483 ASP A 501 1 ? 19 
HELX_P HELX_P23 AC5 GLY A 509 ? ILE A 513 ? GLY A 509 ILE A 513 5 ? 5  
HELX_P HELX_P24 AC6 SER B 10  ? GLY B 26  ? SER B 10  GLY B 26  1 ? 17 
HELX_P HELX_P25 AC7 THR B 32  ? GLU B 40  ? THR B 32  GLU B 40  5 ? 9  
HELX_P HELX_P26 AC8 SER B 62  ? GLY B 77  ? SER B 62  GLY B 77  1 ? 16 
HELX_P HELX_P27 AC9 SER B 129 ? GLY B 141 ? SER B 129 GLY B 141 1 ? 13 
HELX_P HELX_P28 AD1 SER B 155 ? ASP B 162 ? SER B 155 ASP B 162 1 ? 8  
HELX_P HELX_P29 AD2 HIS B 173 ? ALA B 175 ? HIS B 173 ALA B 175 5 ? 3  
HELX_P HELX_P30 AD3 GLY B 193 ? MET B 197 ? GLY B 193 MET B 197 5 ? 5  
HELX_P HELX_P31 AD4 VAL B 214 ? SER B 219 ? VAL B 214 SER B 219 5 ? 6  
HELX_P HELX_P32 AD5 ASN B 249 ? ASP B 251 ? ASN B 249 ASP B 251 5 ? 3  
HELX_P HELX_P33 AD6 ASP B 252 ? ALA B 266 ? ASP B 252 ALA B 266 1 ? 15 
HELX_P HELX_P34 AD7 LEU B 278 ? ALA B 283 ? LEU B 278 ALA B 283 1 ? 6  
HELX_P HELX_P35 AD8 THR B 287 ? TYR B 291 ? THR B 287 TYR B 291 5 ? 5  
HELX_P HELX_P36 AD9 PRO B 299 ? ASP B 311 ? PRO B 299 ASP B 311 1 ? 13 
HELX_P HELX_P37 AE1 PRO B 324 ? ALA B 340 ? PRO B 324 ALA B 340 1 ? 17 
HELX_P HELX_P38 AE2 PHE B 349 ? ARG B 353 ? PHE B 349 ARG B 353 5 ? 5  
HELX_P HELX_P39 AE3 ASP B 358 ? MET B 367 ? ASP B 358 MET B 367 1 ? 10 
HELX_P HELX_P40 AE4 LEU B 373 ? TRP B 381 ? LEU B 373 TRP B 381 5 ? 9  
HELX_P HELX_P41 AE5 THR B 397 ? TYR B 415 ? THR B 397 TYR B 415 1 ? 19 
HELX_P HELX_P42 AE6 ASP B 442 ? GLU B 463 ? ASP B 442 GLU B 463 1 ? 22 
HELX_P HELX_P43 AE7 HIS B 471 ? ARG B 473 ? HIS B 471 ARG B 473 5 ? 3  
HELX_P HELX_P44 AE8 TYR B 474 ? THR B 481 ? TYR B 474 THR B 481 1 ? 8  
HELX_P HELX_P45 AE9 SER B 483 ? ASP B 501 ? SER B 483 ASP B 501 1 ? 19 
HELX_P HELX_P46 AF1 GLY B 509 ? ILE B 513 ? GLY B 509 ILE B 513 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 30  ? PHE A 31  ? VAL A 30  PHE A 31  
AA1 2 ALA A 56  ? VAL A 58  ? ALA A 56  VAL A 58  
AA1 3 VAL A 102 ? ASP A 105 ? VAL A 102 ASP A 105 
AA1 4 LEU A 80  ? VAL A 83  ? LEU A 80  VAL A 83  
AA2 1 ILE A 112 ? ASN A 116 ? ILE A 112 ASN A 116 
AA2 2 TYR A 121 ? VAL A 124 ? TYR A 121 VAL A 124 
AA2 3 VAL A 225 ? TRP A 232 ? VAL A 225 TRP A 232 
AA2 4 GLN A 177 ? VAL A 183 ? GLN A 177 VAL A 183 
AA2 5 VAL A 189 ? ARG A 191 ? VAL A 189 ARG A 191 
AA3 1 LEU A 144 ? TRP A 145 ? LEU A 144 TRP A 145 
AA3 2 MET A 234 ? PRO A 235 ? MET A 234 PRO A 235 
AA4 1 LYS A 346 ? TYR A 348 ? LYS A 346 TYR A 348 
AA4 2 TYR A 240 ? PHE A 247 ? TYR A 240 PHE A 247 
AA4 3 TRP A 315 ? TYR A 322 ? TRP A 315 TYR A 322 
AA4 4 ALA A 273 ? SER A 277 ? ALA A 273 SER A 277 
AA4 5 GLY A 421 ? ILE A 425 ? GLY A 421 ILE A 425 
AA4 6 LEU A 430 ? TYR A 438 ? LEU A 430 TYR A 438 
AA4 7 GLY A 386 ? PHE A 390 ? GLY A 386 PHE A 390 
AA5 1 LYS A 346 ? TYR A 348 ? LYS A 346 TYR A 348 
AA5 2 TYR A 240 ? PHE A 247 ? TYR A 240 PHE A 247 
AA5 3 TRP A 315 ? TYR A 322 ? TRP A 315 TYR A 322 
AA5 4 ALA A 273 ? SER A 277 ? ALA A 273 SER A 277 
AA5 5 GLY A 421 ? ILE A 425 ? GLY A 421 ILE A 425 
AA5 6 LEU A 430 ? TYR A 438 ? LEU A 430 TYR A 438 
AA5 7 VAL A 393 ? SER A 394 ? VAL A 393 SER A 394 
AA6 1 VAL B 30  ? PHE B 31  ? VAL B 30  PHE B 31  
AA6 2 ALA B 57  ? VAL B 58  ? ALA B 57  VAL B 58  
AA6 3 VAL B 102 ? ASP B 105 ? VAL B 102 ASP B 105 
AA6 4 LEU B 80  ? VAL B 83  ? LEU B 80  VAL B 83  
AA7 1 ILE B 112 ? ASN B 116 ? ILE B 112 ASN B 116 
AA7 2 TYR B 121 ? VAL B 124 ? TYR B 121 VAL B 124 
AA7 3 VAL B 225 ? TRP B 232 ? VAL B 225 TRP B 232 
AA7 4 GLN B 177 ? VAL B 183 ? GLN B 177 VAL B 183 
AA7 5 VAL B 189 ? ARG B 191 ? VAL B 189 ARG B 191 
AA8 1 LEU B 144 ? TRP B 145 ? LEU B 144 TRP B 145 
AA8 2 MET B 234 ? PRO B 235 ? MET B 234 PRO B 235 
AA9 1 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AA9 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AA9 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AA9 4 ALA B 273 ? SER B 277 ? ALA B 273 SER B 277 
AA9 5 MET B 420 ? ILE B 425 ? MET B 420 ILE B 425 
AA9 6 LEU B 430 ? TYR B 438 ? LEU B 430 TYR B 438 
AA9 7 GLY B 386 ? PHE B 390 ? GLY B 386 PHE B 390 
AB1 1 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AB1 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AB1 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AB1 4 ALA B 273 ? SER B 277 ? ALA B 273 SER B 277 
AB1 5 MET B 420 ? ILE B 425 ? MET B 420 ILE B 425 
AB1 6 LEU B 430 ? TYR B 438 ? LEU B 430 TYR B 438 
AB1 7 VAL B 393 ? SER B 394 ? VAL B 393 SER B 394 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 31  ? N PHE A 31  O ALA A 57  ? O ALA A 57  
AA1 2 3 N VAL A 58  ? N VAL A 58  O ASP A 105 ? O ASP A 105 
AA1 3 4 O LEU A 104 ? O LEU A 104 N VAL A 83  ? N VAL A 83  
AA2 1 2 N ASN A 116 ? N ASN A 116 O TYR A 121 ? O TYR A 121 
AA2 2 3 N ALA A 122 ? N ALA A 122 O ILE A 231 ? O ILE A 231 
AA2 3 4 O VAL A 225 ? O VAL A 225 N VAL A 183 ? N VAL A 183 
AA2 4 5 N VAL A 182 ? N VAL A 182 O VAL A 190 ? O VAL A 190 
AA3 1 2 N TRP A 145 ? N TRP A 145 O MET A 234 ? O MET A 234 
AA4 1 2 O TYR A 348 ? O TYR A 348 N LEU A 244 ? N LEU A 244 
AA4 2 3 N ILE A 245 ? N ILE A 245 O PHE A 317 ? O PHE A 317 
AA4 3 4 O ASN A 316 ? O ASN A 316 N ARG A 276 ? N ARG A 276 
AA4 4 5 N VAL A 275 ? N VAL A 275 O LEU A 423 ? O LEU A 423 
AA4 5 6 N LEU A 422 ? N LEU A 422 O VAL A 433 ? O VAL A 433 
AA4 6 7 O THR A 434 ? O THR A 434 N PHE A 390 ? N PHE A 390 
AA5 1 2 O TYR A 348 ? O TYR A 348 N LEU A 244 ? N LEU A 244 
AA5 2 3 N ILE A 245 ? N ILE A 245 O PHE A 317 ? O PHE A 317 
AA5 3 4 O ASN A 316 ? O ASN A 316 N ARG A 276 ? N ARG A 276 
AA5 4 5 N VAL A 275 ? N VAL A 275 O LEU A 423 ? O LEU A 423 
AA5 5 6 N LEU A 422 ? N LEU A 422 O VAL A 433 ? O VAL A 433 
AA5 6 7 O LEU A 430 ? O LEU A 430 N SER A 394 ? N SER A 394 
AA6 1 2 N PHE B 31  ? N PHE B 31  O ALA B 57  ? O ALA B 57  
AA6 2 3 N VAL B 58  ? N VAL B 58  O VAL B 103 ? O VAL B 103 
AA6 3 4 O LEU B 104 ? O LEU B 104 N VAL B 83  ? N VAL B 83  
AA7 1 2 N ASN B 116 ? N ASN B 116 O TYR B 121 ? O TYR B 121 
AA7 2 3 N VAL B 124 ? N VAL B 124 O MET B 229 ? O MET B 229 
AA7 3 4 O VAL B 225 ? O VAL B 225 N VAL B 183 ? N VAL B 183 
AA7 4 5 N VAL B 182 ? N VAL B 182 O VAL B 190 ? O VAL B 190 
AA8 1 2 N TRP B 145 ? N TRP B 145 O MET B 234 ? O MET B 234 
AA9 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AA9 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AA9 3 4 O ASN B 316 ? O ASN B 316 N ARG B 276 ? N ARG B 276 
AA9 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AA9 5 6 N LEU B 422 ? N LEU B 422 O VAL B 433 ? O VAL B 433 
AA9 6 7 O THR B 434 ? O THR B 434 N PHE B 390 ? N PHE B 390 
AB1 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AB1 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AB1 3 4 O ASN B 316 ? O ASN B 316 N ARG B 276 ? N ARG B 276 
AB1 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AB1 5 6 N LEU B 422 ? N LEU B 422 O VAL B 433 ? O VAL B 433 
AB1 6 7 O LEU B 430 ? O LEU B 430 N SER B 394 ? N SER B 394 
# 
_pdbx_entry_details.entry_id                   8S7W 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 NE2 B HIS 387  ? ? C8M B FAD 601  ? ? 1.40 
2  1 NE2 A HIS 387  ? ? C8M A FAD 601  ? ? 1.45 
3  1 O   A HOH 714  ? ? O   A HOH 982  ? ? 1.77 
4  1 O   B HOH 926  ? ? O   B HOH 948  ? ? 1.97 
5  1 O   A HOH 1023 ? ? O   B HOH 964  ? ? 2.01 
6  1 O   A TRP 514  ? ? O   A HOH 701  ? ? 2.05 
7  1 O   A HOH 801  ? ? O   A HOH 1019 ? ? 2.07 
8  1 NE  B ARG 518  ? ? O   B HOH 701  ? ? 2.16 
9  1 OE2 B GLU 75   ? ? O   B HOH 702  ? ? 2.19 
10 1 O   B HOH 837  ? ? O   B HOH 904  ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     972 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     873 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_454 
_pdbx_validate_symm_contact.dist              2.09 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              418 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              418 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              418 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                124.29 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.99 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                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 GLU A 33  ? ? 59.94   -123.00 
2  1 TYR A 43  ? ? -111.87 61.81   
3  1 ASN A 88  ? ? -75.08  49.74   
4  1 ALA A 90  ? ? 93.09   -12.96  
5  1 PRO A 149 ? ? -61.98  -177.73 
6  1 CYS A 178 ? ? -160.03 101.30  
7  1 GLN A 220 ? ? 39.83   51.83   
8  1 TRP A 427 ? ? -141.29 -70.30  
9  1 TYR A 482 ? ? -92.98  56.45   
10 1 ALA A 507 ? ? 37.23   62.04   
11 1 GLU B 33  ? ? 50.56   -126.44 
12 1 TYR B 43  ? ? -117.00 60.68   
13 1 ILE B 45  ? ? -121.75 -59.27  
14 1 ALA B 90  ? ? 93.15   -10.09  
15 1 PRO B 149 ? ? -87.04  42.12   
16 1 ASP B 150 ? ? 59.10   10.16   
17 1 TYR B 170 ? ? -93.52  31.99   
18 1 TRP B 427 ? ? -140.37 -62.14  
19 1 ALA B 507 ? ? 33.17   65.26   
# 
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 LYS 520 ? A LYS 520 
2 1 Y 1 A ALA 521 ? A ALA 521 
3 1 Y 1 B LYS 520 ? B LYS 520 
4 1 Y 1 B ALA 521 ? B ALA 521 
# 
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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CL  CL     CL N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
FAD PA     P  N R 89  
FAD O1A    O  N N 90  
FAD O2A    O  N N 91  
FAD O5B    O  N N 92  
FAD C5B    C  N N 93  
FAD C4B    C  N R 94  
FAD O4B    O  N N 95  
FAD C3B    C  N S 96  
FAD O3B    O  N N 97  
FAD C2B    C  N R 98  
FAD O2B    O  N N 99  
FAD C1B    C  N R 100 
FAD N9A    N  Y N 101 
FAD C8A    C  Y N 102 
FAD N7A    N  Y N 103 
FAD C5A    C  Y N 104 
FAD C6A    C  Y N 105 
FAD N6A    N  N N 106 
FAD N1A    N  Y N 107 
FAD C2A    C  Y N 108 
FAD N3A    N  Y N 109 
FAD C4A    C  Y N 110 
FAD N1     N  N N 111 
FAD C2     C  N N 112 
FAD O2     O  N N 113 
FAD N3     N  N N 114 
FAD C4     C  N N 115 
FAD O4     O  N N 116 
FAD C4X    C  N N 117 
FAD N5     N  N N 118 
FAD C5X    C  Y N 119 
FAD C6     C  Y N 120 
FAD C7     C  Y N 121 
FAD C7M    C  N N 122 
FAD C8     C  Y N 123 
FAD C8M    C  N N 124 
FAD C9     C  Y N 125 
FAD C9A    C  Y N 126 
FAD N10    N  N N 127 
FAD C10    C  N N 128 
FAD "C1'"  C  N N 129 
FAD "C2'"  C  N S 130 
FAD "O2'"  O  N N 131 
FAD "C3'"  C  N S 132 
FAD "O3'"  O  N N 133 
FAD "C4'"  C  N R 134 
FAD "O4'"  O  N N 135 
FAD "C5'"  C  N N 136 
FAD "O5'"  O  N N 137 
FAD P      P  N R 138 
FAD O1P    O  N N 139 
FAD O2P    O  N N 140 
FAD O3P    O  N N 141 
FAD HOA2   H  N N 142 
FAD H51A   H  N N 143 
FAD H52A   H  N N 144 
FAD H4B    H  N N 145 
FAD H3B    H  N N 146 
FAD HO3A   H  N N 147 
FAD H2B    H  N N 148 
FAD HO2A   H  N N 149 
FAD H1B    H  N N 150 
FAD H8A    H  N N 151 
FAD H61A   H  N N 152 
FAD H62A   H  N N 153 
FAD H2A    H  N N 154 
FAD HN3    H  N N 155 
FAD H6     H  N N 156 
FAD HM71   H  N N 157 
FAD HM72   H  N N 158 
FAD HM73   H  N N 159 
FAD HM81   H  N N 160 
FAD HM82   H  N N 161 
FAD HM83   H  N N 162 
FAD H9     H  N N 163 
FAD "H1'1" H  N N 164 
FAD "H1'2" H  N N 165 
FAD "H2'"  H  N N 166 
FAD "HO2'" H  N N 167 
FAD "H3'"  H  N N 168 
FAD "HO3'" H  N N 169 
FAD "H4'"  H  N N 170 
FAD "HO4'" H  N N 171 
FAD "H5'1" H  N N 172 
FAD "H5'2" H  N N 173 
FAD HOP2   H  N N 174 
GLN N      N  N N 175 
GLN CA     C  N S 176 
GLN C      C  N N 177 
GLN O      O  N N 178 
GLN CB     C  N N 179 
GLN CG     C  N N 180 
GLN CD     C  N N 181 
GLN OE1    O  N N 182 
GLN NE2    N  N N 183 
GLN OXT    O  N N 184 
GLN H      H  N N 185 
GLN H2     H  N N 186 
GLN HA     H  N N 187 
GLN HB2    H  N N 188 
GLN HB3    H  N N 189 
GLN HG2    H  N N 190 
GLN HG3    H  N N 191 
GLN HE21   H  N N 192 
GLN HE22   H  N N 193 
GLN HXT    H  N N 194 
GLU N      N  N N 195 
GLU CA     C  N S 196 
GLU C      C  N N 197 
GLU O      O  N N 198 
GLU CB     C  N N 199 
GLU CG     C  N N 200 
GLU CD     C  N N 201 
GLU OE1    O  N N 202 
GLU OE2    O  N N 203 
GLU OXT    O  N N 204 
GLU H      H  N N 205 
GLU H2     H  N N 206 
GLU HA     H  N N 207 
GLU HB2    H  N N 208 
GLU HB3    H  N N 209 
GLU HG2    H  N N 210 
GLU HG3    H  N N 211 
GLU HE2    H  N N 212 
GLU HXT    H  N N 213 
GLY N      N  N N 214 
GLY CA     C  N N 215 
GLY C      C  N N 216 
GLY O      O  N N 217 
GLY OXT    O  N N 218 
GLY H      H  N N 219 
GLY H2     H  N N 220 
GLY HA2    H  N N 221 
GLY HA3    H  N N 222 
GLY HXT    H  N N 223 
HIS N      N  N N 224 
HIS CA     C  N S 225 
HIS C      C  N N 226 
HIS O      O  N N 227 
HIS CB     C  N N 228 
HIS CG     C  Y N 229 
HIS ND1    N  Y N 230 
HIS CD2    C  Y N 231 
HIS CE1    C  Y N 232 
HIS NE2    N  Y N 233 
HIS OXT    O  N N 234 
HIS H      H  N N 235 
HIS H2     H  N N 236 
HIS HA     H  N N 237 
HIS HB2    H  N N 238 
HIS HB3    H  N N 239 
HIS HD1    H  N N 240 
HIS HD2    H  N N 241 
HIS HE1    H  N N 242 
HIS HE2    H  N N 243 
HIS HXT    H  N N 244 
HOH O      O  N N 245 
HOH H1     H  N N 246 
HOH H2     H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
PEG C1     C  N N 337 
PEG O1     O  N N 338 
PEG C2     C  N N 339 
PEG O2     O  N N 340 
PEG C3     C  N N 341 
PEG C4     C  N N 342 
PEG O4     O  N N 343 
PEG H11    H  N N 344 
PEG H12    H  N N 345 
PEG HO1    H  N N 346 
PEG H21    H  N N 347 
PEG H22    H  N N 348 
PEG H31    H  N N 349 
PEG H32    H  N N 350 
PEG H41    H  N N 351 
PEG H42    H  N N 352 
PEG HO4    H  N N 353 
PHE N      N  N N 354 
PHE CA     C  N S 355 
PHE C      C  N N 356 
PHE O      O  N N 357 
PHE CB     C  N N 358 
PHE CG     C  Y N 359 
PHE CD1    C  Y N 360 
PHE CD2    C  Y N 361 
PHE CE1    C  Y N 362 
PHE CE2    C  Y N 363 
PHE CZ     C  Y N 364 
PHE OXT    O  N N 365 
PHE H      H  N N 366 
PHE H2     H  N N 367 
PHE HA     H  N N 368 
PHE HB2    H  N N 369 
PHE HB3    H  N N 370 
PHE HD1    H  N N 371 
PHE HD2    H  N N 372 
PHE HE1    H  N N 373 
PHE HE2    H  N N 374 
PHE HZ     H  N N 375 
PHE HXT    H  N N 376 
PRO N      N  N N 377 
PRO CA     C  N S 378 
PRO C      C  N N 379 
PRO O      O  N N 380 
PRO CB     C  N N 381 
PRO CG     C  N N 382 
PRO CD     C  N N 383 
PRO OXT    O  N N 384 
PRO H      H  N N 385 
PRO HA     H  N N 386 
PRO HB2    H  N N 387 
PRO HB3    H  N N 388 
PRO HG2    H  N N 389 
PRO HG3    H  N N 390 
PRO HD2    H  N N 391 
PRO HD3    H  N N 392 
PRO HXT    H  N N 393 
SER N      N  N N 394 
SER CA     C  N S 395 
SER C      C  N N 396 
SER O      O  N N 397 
SER CB     C  N N 398 
SER OG     O  N N 399 
SER OXT    O  N N 400 
SER H      H  N N 401 
SER H2     H  N N 402 
SER HA     H  N N 403 
SER HB2    H  N N 404 
SER HB3    H  N N 405 
SER HG     H  N N 406 
SER HXT    H  N N 407 
THR N      N  N N 408 
THR CA     C  N S 409 
THR C      C  N N 410 
THR O      O  N N 411 
THR CB     C  N R 412 
THR OG1    O  N N 413 
THR CG2    C  N N 414 
THR OXT    O  N N 415 
THR H      H  N N 416 
THR H2     H  N N 417 
THR HA     H  N N 418 
THR HB     H  N N 419 
THR HG1    H  N N 420 
THR HG21   H  N N 421 
THR HG22   H  N N 422 
THR HG23   H  N N 423 
THR HXT    H  N N 424 
TRP N      N  N N 425 
TRP CA     C  N S 426 
TRP C      C  N N 427 
TRP O      O  N N 428 
TRP CB     C  N N 429 
TRP CG     C  Y N 430 
TRP CD1    C  Y N 431 
TRP CD2    C  Y N 432 
TRP NE1    N  Y N 433 
TRP CE2    C  Y N 434 
TRP CE3    C  Y N 435 
TRP CZ2    C  Y N 436 
TRP CZ3    C  Y N 437 
TRP CH2    C  Y N 438 
TRP OXT    O  N N 439 
TRP H      H  N N 440 
TRP H2     H  N N 441 
TRP HA     H  N N 442 
TRP HB2    H  N N 443 
TRP HB3    H  N N 444 
TRP HD1    H  N N 445 
TRP HE1    H  N N 446 
TRP HE3    H  N N 447 
TRP HZ2    H  N N 448 
TRP HZ3    H  N N 449 
TRP HH2    H  N N 450 
TRP HXT    H  N N 451 
TYR N      N  N N 452 
TYR CA     C  N S 453 
TYR C      C  N N 454 
TYR O      O  N N 455 
TYR CB     C  N N 456 
TYR CG     C  Y N 457 
TYR CD1    C  Y N 458 
TYR CD2    C  Y N 459 
TYR CE1    C  Y N 460 
TYR CE2    C  Y N 461 
TYR CZ     C  Y N 462 
TYR OH     O  N N 463 
TYR OXT    O  N N 464 
TYR H      H  N N 465 
TYR H2     H  N N 466 
TYR HA     H  N N 467 
TYR HB2    H  N N 468 
TYR HB3    H  N N 469 
TYR HD1    H  N N 470 
TYR HD2    H  N N 471 
TYR HE1    H  N N 472 
TYR HE2    H  N N 473 
TYR HH     H  N N 474 
TYR HXT    H  N N 475 
VAL N      N  N N 476 
VAL CA     C  N S 477 
VAL C      C  N N 478 
VAL O      O  N N 479 
VAL CB     C  N N 480 
VAL CG1    C  N N 481 
VAL CG2    C  N N 482 
VAL OXT    O  N N 483 
VAL H      H  N N 484 
VAL H2     H  N N 485 
VAL HA     H  N N 486 
VAL HB     H  N N 487 
VAL HG11   H  N N 488 
VAL HG12   H  N N 489 
VAL HG13   H  N N 490 
VAL HG21   H  N N 491 
VAL HG22   H  N N 492 
VAL HG23   H  N N 493 
VAL HXT    H  N N 494 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PEG C1    O1     sing N N 328 
PEG C1    C2     sing N N 329 
PEG C1    H11    sing N N 330 
PEG C1    H12    sing N N 331 
PEG O1    HO1    sing N N 332 
PEG C2    O2     sing N N 333 
PEG C2    H21    sing N N 334 
PEG C2    H22    sing N N 335 
PEG O2    C3     sing N N 336 
PEG C3    C4     sing N N 337 
PEG C3    H31    sing N N 338 
PEG C3    H32    sing N N 339 
PEG C4    O4     sing N N 340 
PEG C4    H41    sing N N 341 
PEG C4    H42    sing N N 342 
PEG O4    HO4    sing N N 343 
PHE N     CA     sing N N 344 
PHE N     H      sing N N 345 
PHE N     H2     sing N N 346 
PHE CA    C      sing N N 347 
PHE CA    CB     sing N N 348 
PHE CA    HA     sing N N 349 
PHE C     O      doub N N 350 
PHE C     OXT    sing N N 351 
PHE CB    CG     sing N N 352 
PHE CB    HB2    sing N N 353 
PHE CB    HB3    sing N N 354 
PHE CG    CD1    doub Y N 355 
PHE CG    CD2    sing Y N 356 
PHE CD1   CE1    sing Y N 357 
PHE CD1   HD1    sing N N 358 
PHE CD2   CE2    doub Y N 359 
PHE CD2   HD2    sing N N 360 
PHE CE1   CZ     doub Y N 361 
PHE CE1   HE1    sing N N 362 
PHE CE2   CZ     sing Y N 363 
PHE CE2   HE2    sing N N 364 
PHE CZ    HZ     sing N N 365 
PHE OXT   HXT    sing N N 366 
PRO N     CA     sing N N 367 
PRO N     CD     sing N N 368 
PRO N     H      sing N N 369 
PRO CA    C      sing N N 370 
PRO CA    CB     sing N N 371 
PRO CA    HA     sing N N 372 
PRO C     O      doub N N 373 
PRO C     OXT    sing N N 374 
PRO CB    CG     sing N N 375 
PRO CB    HB2    sing N N 376 
PRO CB    HB3    sing N N 377 
PRO CG    CD     sing N N 378 
PRO CG    HG2    sing N N 379 
PRO CG    HG3    sing N N 380 
PRO CD    HD2    sing N N 381 
PRO CD    HD3    sing N N 382 
PRO OXT   HXT    sing N N 383 
SER N     CA     sing N N 384 
SER N     H      sing N N 385 
SER N     H2     sing N N 386 
SER CA    C      sing N N 387 
SER CA    CB     sing N N 388 
SER CA    HA     sing N N 389 
SER C     O      doub N N 390 
SER C     OXT    sing N N 391 
SER CB    OG     sing N N 392 
SER CB    HB2    sing N N 393 
SER CB    HB3    sing N N 394 
SER OG    HG     sing N N 395 
SER OXT   HXT    sing N N 396 
THR N     CA     sing N N 397 
THR N     H      sing N N 398 
THR N     H2     sing N N 399 
THR CA    C      sing N N 400 
THR CA    CB     sing N N 401 
THR CA    HA     sing N N 402 
THR C     O      doub N N 403 
THR C     OXT    sing N N 404 
THR CB    OG1    sing N N 405 
THR CB    CG2    sing N N 406 
THR CB    HB     sing N N 407 
THR OG1   HG1    sing N N 408 
THR CG2   HG21   sing N N 409 
THR CG2   HG22   sing N N 410 
THR CG2   HG23   sing N N 411 
THR OXT   HXT    sing N N 412 
TRP N     CA     sing N N 413 
TRP N     H      sing N N 414 
TRP N     H2     sing N N 415 
TRP CA    C      sing N N 416 
TRP CA    CB     sing N N 417 
TRP CA    HA     sing N N 418 
TRP C     O      doub N N 419 
TRP C     OXT    sing N N 420 
TRP CB    CG     sing N N 421 
TRP CB    HB2    sing N N 422 
TRP CB    HB3    sing N N 423 
TRP CG    CD1    doub Y N 424 
TRP CG    CD2    sing Y N 425 
TRP CD1   NE1    sing Y N 426 
TRP CD1   HD1    sing N N 427 
TRP CD2   CE2    doub Y N 428 
TRP CD2   CE3    sing Y N 429 
TRP NE1   CE2    sing Y N 430 
TRP NE1   HE1    sing N N 431 
TRP CE2   CZ2    sing Y N 432 
TRP CE3   CZ3    doub Y N 433 
TRP CE3   HE3    sing N N 434 
TRP CZ2   CH2    doub Y N 435 
TRP CZ2   HZ2    sing N N 436 
TRP CZ3   CH2    sing Y N 437 
TRP CZ3   HZ3    sing N N 438 
TRP CH2   HH2    sing N N 439 
TRP OXT   HXT    sing N N 440 
TYR N     CA     sing N N 441 
TYR N     H      sing N N 442 
TYR N     H2     sing N N 443 
TYR CA    C      sing N N 444 
TYR CA    CB     sing N N 445 
TYR CA    HA     sing N N 446 
TYR C     O      doub N N 447 
TYR C     OXT    sing N N 448 
TYR CB    CG     sing N N 449 
TYR CB    HB2    sing N N 450 
TYR CB    HB3    sing N N 451 
TYR CG    CD1    doub Y N 452 
TYR CG    CD2    sing Y N 453 
TYR CD1   CE1    sing Y N 454 
TYR CD1   HD1    sing N N 455 
TYR CD2   CE2    doub Y N 456 
TYR CD2   HD2    sing N N 457 
TYR CE1   CZ     doub Y N 458 
TYR CE1   HE1    sing N N 459 
TYR CE2   CZ     sing Y N 460 
TYR CE2   HE2    sing N N 461 
TYR CZ    OH     sing N N 462 
TYR OH    HH     sing N N 463 
TYR OXT   HXT    sing N N 464 
VAL N     CA     sing N N 465 
VAL N     H      sing N N 466 
VAL N     H2     sing N N 467 
VAL CA    C      sing N N 468 
VAL CA    CB     sing N N 469 
VAL CA    HA     sing N N 470 
VAL C     O      doub N N 471 
VAL C     OXT    sing N N 472 
VAL CB    CG1    sing N N 473 
VAL CB    CG2    sing N N 474 
VAL CB    HB     sing N N 475 
VAL CG1   HG11   sing N N 476 
VAL CG1   HG12   sing N N 477 
VAL CG1   HG13   sing N N 478 
VAL CG2   HG21   sing N N 479 
VAL CG2   HG22   sing N N 480 
VAL CG2   HG23   sing N N 481 
VAL OXT   HXT    sing N N 482 
# 
_pdbx_audit_support.funding_organization   'European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           'B-Ligzymes (GA 824017)' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S7W 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009938 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008723 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007651 
_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 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? -8.709  -28.388 -12.753 1.00 50.62 ? 1    MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? -9.232  -29.715 -12.341 1.00 46.14 ? 1    MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? -10.478 -29.481 -11.469 1.00 42.93 ? 1    MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? -10.376 -28.734 -10.477 1.00 39.90 ? 1    MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? -8.169  -30.486 -11.552 1.00 53.94 ? 1    MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? -8.464  -31.975 -11.400 1.00 61.03 ? 1    MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? -7.793  -32.660 -9.854  1.00 75.16 ? 1    MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? -9.110  -32.278 -8.690  1.00 72.79 ? 1    MET A CE    1 
ATOM   9    N  N     . ALA A 1 2   ? -11.613 -30.078 -11.839 1.00 37.38 ? 2    ALA A N     1 
ATOM   10   C  CA    . ALA A 1 2   ? -12.921 -29.920 -11.164 1.00 34.66 ? 2    ALA A CA    1 
ATOM   11   C  C     . ALA A 1 2   ? -12.851 -30.605 -9.797  1.00 33.79 ? 2    ALA A C     1 
ATOM   12   O  O     . ALA A 1 2   ? -11.999 -31.521 -9.621  1.00 31.78 ? 2    ALA A O     1 
ATOM   13   C  CB    . ALA A 1 2   ? -14.045 -30.472 -12.016 1.00 31.03 ? 2    ALA A CB    1 
ATOM   14   N  N     . ALA A 1 3   ? -13.676 -30.132 -8.853  1.00 30.48 ? 3    ALA A N     1 
ATOM   15   C  CA    . ALA A 1 3   ? -13.803 -30.708 -7.500  1.00 27.59 ? 3    ALA A CA    1 
ATOM   16   C  C     . ALA A 1 3   ? -14.252 -32.148 -7.668  1.00 27.66 ? 3    ALA A C     1 
ATOM   17   O  O     . ALA A 1 3   ? -15.105 -32.423 -8.500  1.00 26.73 ? 3    ALA A O     1 
ATOM   18   C  CB    . ALA A 1 3   ? -14.788 -29.923 -6.662  1.00 24.98 ? 3    ALA A CB    1 
ATOM   19   N  N     . PRO A 1 4   ? -13.740 -33.088 -6.855  1.00 26.25 ? 4    PRO A N     1 
ATOM   20   C  CA    . PRO A 1 4   ? -14.311 -34.417 -6.805  1.00 27.47 ? 4    PRO A CA    1 
ATOM   21   C  C     . PRO A 1 4   ? -15.603 -34.378 -5.985  1.00 31.16 ? 4    PRO A C     1 
ATOM   22   O  O     . PRO A 1 4   ? -15.764 -33.484 -5.153  1.00 31.16 ? 4    PRO A O     1 
ATOM   23   C  CB    . PRO A 1 4   ? -13.256 -35.266 -6.086  1.00 27.11 ? 4    PRO A CB    1 
ATOM   24   C  CG    . PRO A 1 4   ? -12.506 -34.271 -5.220  1.00 29.45 ? 4    PRO A CG    1 
ATOM   25   C  CD    . PRO A 1 4   ? -12.605 -32.930 -5.941  1.00 28.58 ? 4    PRO A CD    1 
ATOM   26   N  N     . LEU A 1 5   ? -16.426 -35.401 -6.187  1.00 28.99 ? 5    LEU A N     1 
ATOM   27   C  CA    . LEU A 1 5   ? -17.596 -35.722 -5.339  1.00 29.58 ? 5    LEU A CA    1 
ATOM   28   C  C     . LEU A 1 5   ? -17.115 -36.052 -3.933  1.00 30.64 ? 5    LEU A C     1 
ATOM   29   O  O     . LEU A 1 5   ? -16.046 -36.631 -3.753  1.00 28.20 ? 5    LEU A O     1 
ATOM   30   C  CB    . LEU A 1 5   ? -18.376 -36.892 -5.945  1.00 28.86 ? 5    LEU A CB    1 
ATOM   31   C  CG    . LEU A 1 5   ? -19.218 -36.534 -7.168  1.00 30.92 ? 5    LEU A CG    1 
ATOM   32   C  CD1   . LEU A 1 5   ? -19.658 -37.785 -7.927  1.00 31.54 ? 5    LEU A CD1   1 
ATOM   33   C  CD2   . LEU A 1 5   ? -20.427 -35.711 -6.745  1.00 31.77 ? 5    LEU A CD2   1 
ATOM   34   N  N     . PRO A 1 6   ? -17.920 -35.705 -2.903  1.00 29.31 ? 6    PRO A N     1 
ATOM   35   C  CA    . PRO A 1 6   ? -17.640 -36.155 -1.556  1.00 32.62 ? 6    PRO A CA    1 
ATOM   36   C  C     . PRO A 1 6   ? -17.817 -37.675 -1.553  1.00 34.58 ? 6    PRO A C     1 
ATOM   37   O  O     . PRO A 1 6   ? -18.685 -38.178 -2.261  1.00 40.24 ? 6    PRO A O     1 
ATOM   38   C  CB    . PRO A 1 6   ? -18.643 -35.375 -0.702  1.00 33.55 ? 6    PRO A CB    1 
ATOM   39   C  CG    . PRO A 1 6   ? -19.773 -35.030 -1.645  1.00 30.87 ? 6    PRO A CG    1 
ATOM   40   C  CD    . PRO A 1 6   ? -19.153 -34.915 -3.013  1.00 30.36 ? 6    PRO A CD    1 
ATOM   41   N  N     . GLU A 1 7   ? -16.940 -38.371 -0.843  1.00 36.09 ? 7    GLU A N     1 
ATOM   42   C  CA    . GLU A 1 7   ? -16.968 -39.842 -0.765  1.00 38.59 ? 7    GLU A CA    1 
ATOM   43   C  C     . GLU A 1 7   ? -18.305 -40.251 -0.146  1.00 37.35 ? 7    GLU A C     1 
ATOM   44   O  O     . GLU A 1 7   ? -18.720 -39.599 0.825   1.00 37.55 ? 7    GLU A O     1 
ATOM   45   C  CB    . GLU A 1 7   ? -15.799 -40.371 0.056   1.00 45.03 ? 7    GLU A CB    1 
ATOM   46   C  CG    . GLU A 1 7   ? -15.974 -41.840 0.390   1.00 54.00 ? 7    GLU A CG    1 
ATOM   47   C  CD    . GLU A 1 7   ? -14.688 -42.560 0.741   1.00 61.85 ? 7    GLU A CD    1 
ATOM   48   O  OE1   . GLU A 1 7   ? -13.742 -41.879 1.181   1.00 61.89 ? 7    GLU A OE1   1 
ATOM   49   O  OE2   . GLU A 1 7   ? -14.643 -43.799 0.578   1.00 65.27 ? 7    GLU A OE2   1 
ATOM   50   N  N     . GLY A 1 8   ? -18.957 -41.267 -0.722  1.00 35.77 ? 8    GLY A N     1 
ATOM   51   C  CA    . GLY A 1 8   ? -20.261 -41.784 -0.283  1.00 33.55 ? 8    GLY A CA    1 
ATOM   52   C  C     . GLY A 1 8   ? -21.406 -41.138 -1.018  1.00 32.56 ? 8    GLY A C     1 
ATOM   53   O  O     . GLY A 1 8   ? -22.515 -41.564 -0.799  1.00 41.30 ? 8    GLY A O     1 
ATOM   54   N  N     . VAL A 1 9   ? -21.161 -40.125 -1.842  1.00 34.70 ? 9    VAL A N     1 
ATOM   55   C  CA    . VAL A 1 9   ? -22.229 -39.443 -2.619  1.00 30.75 ? 9    VAL A CA    1 
ATOM   56   C  C     . VAL A 1 9   ? -22.000 -39.720 -4.099  1.00 31.20 ? 9    VAL A C     1 
ATOM   57   O  O     . VAL A 1 9   ? -20.945 -39.357 -4.629  1.00 29.98 ? 9    VAL A O     1 
ATOM   58   C  CB    . VAL A 1 9   ? -22.293 -37.920 -2.385  1.00 30.44 ? 9    VAL A CB    1 
ATOM   59   C  CG1   . VAL A 1 9   ? -23.370 -37.277 -3.277  1.00 27.77 ? 9    VAL A CG1   1 
ATOM   60   C  CG2   . VAL A 1 9   ? -22.509 -37.579 -0.926  1.00 33.34 ? 9    VAL A CG2   1 
ATOM   61   N  N     . SER A 1 10  ? -23.032 -40.227 -4.754  1.00 35.61 ? 10   SER A N     1 
ATOM   62   C  CA    . SER A 1 10  ? -23.046 -40.547 -6.197  1.00 32.70 ? 10   SER A CA    1 
ATOM   63   C  C     . SER A 1 10  ? -23.281 -39.276 -7.013  1.00 31.80 ? 10   SER A C     1 
ATOM   64   O  O     . SER A 1 10  ? -23.798 -38.277 -6.458  1.00 28.30 ? 10   SER A O     1 
ATOM   65   C  CB    . SER A 1 10  ? -24.088 -41.587 -6.458  1.00 34.63 ? 10   SER A CB    1 
ATOM   66   O  OG    . SER A 1 10  ? -25.391 -41.029 -6.380  1.00 35.49 ? 10   SER A OG    1 
ATOM   67   N  N     . ALA A 1 11  ? -22.901 -39.324 -8.287  1.00 30.05 ? 11   ALA A N     1 
ATOM   68   C  CA    . ALA A 1 11  ? -23.188 -38.298 -9.307  1.00 33.94 ? 11   ALA A CA    1 
ATOM   69   C  C     . ALA A 1 11  ? -24.687 -37.991 -9.305  1.00 34.70 ? 11   ALA A C     1 
ATOM   70   O  O     . ALA A 1 11  ? -25.068 -36.806 -9.394  1.00 38.23 ? 11   ALA A O     1 
ATOM   71   C  CB    . ALA A 1 11  ? -22.726 -38.789 -10.656 1.00 32.68 ? 11   ALA A CB    1 
ATOM   72   N  N     . GLU A 1 12  ? -25.517 -39.027 -9.226  1.00 35.71 ? 12   GLU A N     1 
ATOM   73   C  CA    . GLU A 1 12  ? -26.995 -38.885 -9.343  1.00 39.72 ? 12   GLU A CA    1 
ATOM   74   C  C     . GLU A 1 12  ? -27.519 -38.195 -8.077  1.00 32.38 ? 12   GLU A C     1 
ATOM   75   O  O     . GLU A 1 12  ? -28.315 -37.252 -8.230  1.00 33.39 ? 12   GLU A O     1 
ATOM   76   C  CB    . GLU A 1 12  ? -27.685 -40.230 -9.615  1.00 45.97 ? 12   GLU A CB    1 
ATOM   77   C  CG    . GLU A 1 12  ? -27.040 -41.025 -10.755 1.00 58.11 ? 12   GLU A CG    1 
ATOM   78   C  CD    . GLU A 1 12  ? -25.826 -41.881 -10.383 1.00 63.63 ? 12   GLU A CD    1 
ATOM   79   O  OE1   . GLU A 1 12  ? -26.004 -42.849 -9.619  1.00 70.52 ? 12   GLU A OE1   1 
ATOM   80   O  OE2   . GLU A 1 12  ? -24.700 -41.579 -10.845 1.00 61.36 ? 12   GLU A OE2   1 
ATOM   81   N  N     . ALA A 1 13  ? -27.075 -38.608 -6.882  1.00 27.55 ? 13   ALA A N     1 
ATOM   82   C  CA    . ALA A 1 13  ? -27.436 -37.948 -5.602  1.00 28.79 ? 13   ALA A CA    1 
ATOM   83   C  C     . ALA A 1 13  ? -27.034 -36.459 -5.638  1.00 27.89 ? 13   ALA A C     1 
ATOM   84   O  O     . ALA A 1 13  ? -27.879 -35.612 -5.283  1.00 29.11 ? 13   ALA A O     1 
ATOM   85   C  CB    . ALA A 1 13  ? -26.830 -38.688 -4.440  1.00 28.89 ? 13   ALA A CB    1 
ATOM   86   N  N     . MET A 1 14  ? -25.836 -36.127 -6.128  1.00 27.13 ? 14   MET A N     1 
ATOM   87   C  CA    . MET A 1 14  ? -25.319 -34.728 -6.166  1.00 28.34 ? 14   MET A CA    1 
ATOM   88   C  C     . MET A 1 14  ? -26.177 -33.923 -7.154  1.00 30.77 ? 14   MET A C     1 
ATOM   89   O  O     . MET A 1 14  ? -26.715 -32.864 -6.765  1.00 29.21 ? 14   MET A O     1 
ATOM   90   C  CB    . MET A 1 14  ? -23.844 -34.680 -6.590  1.00 27.11 ? 14   MET A CB    1 
ATOM   91   C  CG    . MET A 1 14  ? -23.207 -33.290 -6.597  1.00 26.33 ? 14   MET A CG    1 
ATOM   92   S  SD    . MET A 1 14  ? -23.421 -32.380 -5.011  1.00 26.83 ? 14   MET A SD    1 
ATOM   93   C  CE    . MET A 1 14  ? -21.978 -32.891 -4.079  1.00 26.54 ? 14   MET A CE    1 
ATOM   94   N  N     . SER A 1 15  ? -26.328 -34.427 -8.382  1.00 29.88 ? 15   SER A N     1 
ATOM   95   C  CA    . SER A 1 15  ? -27.165 -33.809 -9.437  1.00 29.28 ? 15   SER A CA    1 
ATOM   96   C  C     . SER A 1 15  ? -28.582 -33.541 -8.897  1.00 28.19 ? 15   SER A C     1 
ATOM   97   O  O     . SER A 1 15  ? -29.094 -32.398 -9.026  1.00 29.97 ? 15   SER A O     1 
ATOM   98   C  CB    . SER A 1 15  ? -27.155 -34.690 -10.644 1.00 34.41 ? 15   SER A CB    1 
ATOM   99   O  OG    . SER A 1 15  ? -27.803 -34.039 -11.708 1.00 39.14 ? 15   SER A OG    1 
ATOM   100  N  N     . SER A 1 16  ? -29.173 -34.512 -8.205  1.00 28.16 ? 16   SER A N     1 
ATOM   101  C  CA    . SER A 1 16  ? -30.517 -34.373 -7.580  1.00 27.70 ? 16   SER A CA    1 
ATOM   102  C  C     . SER A 1 16  ? -30.496 -33.299 -6.487  1.00 26.55 ? 16   SER A C     1 
ATOM   103  O  O     . SER A 1 16  ? -31.351 -32.363 -6.496  1.00 27.87 ? 16   SER A O     1 
ATOM   104  C  CB    . SER A 1 16  ? -30.990 -35.674 -7.044  1.00 28.53 ? 16   SER A CB    1 
ATOM   105  O  OG    . SER A 1 16  ? -31.405 -36.503 -8.122  1.00 32.71 ? 16   SER A OG    1 
ATOM   106  N  N     . ALA A 1 17  ? -29.560 -33.393 -5.554  1.00 24.73 ? 17   ALA A N     1 
ATOM   107  C  CA    . ALA A 1 17  ? -29.477 -32.395 -4.463  1.00 23.63 ? 17   ALA A CA    1 
ATOM   108  C  C     . ALA A 1 17  ? -29.314 -30.971 -5.041  1.00 20.87 ? 17   ALA A C     1 
ATOM   109  O  O     . ALA A 1 17  ? -30.033 -30.073 -4.589  1.00 20.55 ? 17   ALA A O     1 
ATOM   110  C  CB    . ALA A 1 17  ? -28.379 -32.790 -3.516  1.00 24.98 ? 17   ALA A CB    1 
ATOM   111  N  N     . LEU A 1 18  ? -28.446 -30.741 -6.031  1.00 20.22 ? 18   LEU A N     1 
ATOM   112  C  CA    . LEU A 1 18  ? -28.221 -29.352 -6.543  1.00 21.55 ? 18   LEU A CA    1 
ATOM   113  C  C     . LEU A 1 18  ? -29.471 -28.806 -7.247  1.00 21.26 ? 18   LEU A C     1 
ATOM   114  O  O     . LEU A 1 18  ? -29.788 -27.594 -7.053  1.00 21.15 ? 18   LEU A O     1 
ATOM   115  C  CB    . LEU A 1 18  ? -27.008 -29.299 -7.471  1.00 24.03 ? 18   LEU A CB    1 
ATOM   116  C  CG    . LEU A 1 18  ? -25.666 -29.690 -6.844  1.00 23.87 ? 18   LEU A CG    1 
ATOM   117  C  CD1   . LEU A 1 18  ? -24.560 -29.688 -7.881  1.00 23.72 ? 18   LEU A CD1   1 
ATOM   118  C  CD2   . LEU A 1 18  ? -25.314 -28.775 -5.672  1.00 25.40 ? 18   LEU A CD2   1 
ATOM   119  N  N     . ASP A 1 19  ? -30.196 -29.638 -8.004  1.00 25.24 ? 19   ASP A N     1 
ATOM   120  C  CA    . ASP A 1 19  ? -31.501 -29.251 -8.624  1.00 23.92 ? 19   ASP A CA    1 
ATOM   121  C  C     . ASP A 1 19  ? -32.535 -28.950 -7.516  1.00 22.54 ? 19   ASP A C     1 
ATOM   122  O  O     . ASP A 1 19  ? -33.243 -27.923 -7.594  1.00 22.41 ? 19   ASP A O     1 
ATOM   123  C  CB    . ASP A 1 19  ? -32.022 -30.310 -9.610  1.00 27.16 ? 19   ASP A CB    1 
ATOM   124  C  CG    . ASP A 1 19  ? -33.210 -29.801 -10.435 1.00 30.94 ? 19   ASP A CG    1 
ATOM   125  O  OD1   . ASP A 1 19  ? -33.013 -28.865 -11.209 1.00 32.16 ? 19   ASP A OD1   1 
ATOM   126  O  OD2   . ASP A 1 19  ? -34.348 -30.280 -10.238 1.00 36.40 ? 19   ASP A OD2   1 
ATOM   127  N  N     . ARG A 1 20  ? -32.629 -29.783 -6.485  1.00 21.84 ? 20   ARG A N     1 
ATOM   128  C  CA    . ARG A 1 20  ? -33.514 -29.492 -5.328  1.00 22.36 ? 20   ARG A CA    1 
ATOM   129  C  C     . ARG A 1 20  ? -33.110 -28.168 -4.646  1.00 24.04 ? 20   ARG A C     1 
ATOM   130  O  O     . ARG A 1 20  ? -34.011 -27.381 -4.244  1.00 23.91 ? 20   ARG A O     1 
ATOM   131  C  CB    . ARG A 1 20  ? -33.466 -30.665 -4.355  1.00 24.62 ? 20   ARG A CB    1 
ATOM   132  C  CG    . ARG A 1 20  ? -34.108 -31.932 -4.902  1.00 26.62 ? 20   ARG A CG    1 
ATOM   133  C  CD    . ARG A 1 20  ? -35.627 -31.914 -4.894  1.00 27.37 ? 20   ARG A CD    1 
ATOM   134  N  NE    . ARG A 1 20  ? -36.154 -31.801 -3.537  1.00 24.43 ? 20   ARG A NE    1 
ATOM   135  C  CZ    . ARG A 1 20  ? -36.207 -32.781 -2.656  1.00 25.19 ? 20   ARG A CZ    1 
ATOM   136  N  NH1   . ARG A 1 20  ? -35.802 -34.005 -2.956  1.00 27.35 ? 20   ARG A NH1   1 
ATOM   137  N  NH2   . ARG A 1 20  ? -36.701 -32.535 -1.453  1.00 28.31 ? 20   ARG A NH2   1 
ATOM   138  N  N     . PHE A 1 21  ? -31.805 -27.920 -4.475  1.00 24.11 ? 21   PHE A N     1 
ATOM   139  C  CA    . PHE A 1 21  ? -31.308 -26.627 -3.933  1.00 23.46 ? 21   PHE A CA    1 
ATOM   140  C  C     . PHE A 1 21  ? -31.815 -25.502 -4.838  1.00 24.99 ? 21   PHE A C     1 
ATOM   141  O  O     . PHE A 1 21  ? -32.358 -24.473 -4.319  1.00 21.58 ? 21   PHE A O     1 
ATOM   142  C  CB    . PHE A 1 21  ? -29.785 -26.607 -3.841  1.00 22.91 ? 21   PHE A CB    1 
ATOM   143  C  CG    . PHE A 1 21  ? -29.177 -27.510 -2.803  1.00 21.84 ? 21   PHE A CG    1 
ATOM   144  C  CD1   . PHE A 1 21  ? -29.902 -27.947 -1.703  1.00 21.84 ? 21   PHE A CD1   1 
ATOM   145  C  CD2   . PHE A 1 21  ? -27.851 -27.878 -2.899  1.00 21.74 ? 21   PHE A CD2   1 
ATOM   146  C  CE1   . PHE A 1 21  ? -29.328 -28.778 -0.758  1.00 21.75 ? 21   PHE A CE1   1 
ATOM   147  C  CE2   . PHE A 1 21  ? -27.269 -28.676 -1.926  1.00 22.63 ? 21   PHE A CE2   1 
ATOM   148  C  CZ    . PHE A 1 21  ? -28.008 -29.128 -0.861  1.00 20.37 ? 21   PHE A CZ    1 
ATOM   149  N  N     . ALA A 1 22  ? -31.687 -25.679 -6.155  1.00 23.67 ? 22   ALA A N     1 
ATOM   150  C  CA    . ALA A 1 22  ? -32.136 -24.631 -7.118  1.00 27.59 ? 22   ALA A CA    1 
ATOM   151  C  C     . ALA A 1 22  ? -33.651 -24.390 -6.995  1.00 25.40 ? 22   ALA A C     1 
ATOM   152  O  O     . ALA A 1 22  ? -34.039 -23.252 -7.152  1.00 29.04 ? 22   ALA A O     1 
ATOM   153  C  CB    . ALA A 1 22  ? -31.745 -24.962 -8.534  1.00 26.61 ? 22   ALA A CB    1 
ATOM   154  N  N     . ARG A 1 23  ? -34.465 -25.409 -6.715  1.00 25.65 ? 23   ARG A N     1 
ATOM   155  C  CA    . ARG A 1 23  ? -35.935 -25.243 -6.530  1.00 28.68 ? 23   ARG A CA    1 
ATOM   156  C  C     . ARG A 1 23  ? -36.214 -24.396 -5.284  1.00 29.03 ? 23   ARG A C     1 
ATOM   157  O  O     . ARG A 1 23  ? -37.276 -23.796 -5.247  1.00 27.97 ? 23   ARG A O     1 
ATOM   158  C  CB    . ARG A 1 23  ? -36.684 -26.563 -6.316  1.00 32.84 ? 23   ARG A CB    1 
ATOM   159  C  CG    . ARG A 1 23  ? -36.450 -27.645 -7.367  1.00 38.48 ? 23   ARG A CG    1 
ATOM   160  C  CD    . ARG A 1 23  ? -37.109 -27.335 -8.693  1.00 37.08 ? 23   ARG A CD    1 
ATOM   161  N  NE    . ARG A 1 23  ? -36.688 -28.109 -9.862  1.00 34.45 ? 23   ARG A NE    1 
ATOM   162  C  CZ    . ARG A 1 23  ? -37.241 -27.939 -11.066 1.00 34.17 ? 23   ARG A CZ    1 
ATOM   163  N  NH1   . ARG A 1 23  ? -36.829 -28.622 -12.114 1.00 37.73 ? 23   ARG A NH1   1 
ATOM   164  N  NH2   . ARG A 1 23  ? -38.249 -27.099 -11.213 1.00 33.55 ? 23   ARG A NH2   1 
ATOM   165  N  N     . ILE A 1 24  ? -35.349 -24.431 -4.262  1.00 28.72 ? 24   ILE A N     1 
ATOM   166  C  CA    . ILE A 1 24  ? -35.539 -23.673 -2.984  1.00 25.58 ? 24   ILE A CA    1 
ATOM   167  C  C     . ILE A 1 24  ? -35.099 -22.223 -3.218  1.00 25.72 ? 24   ILE A C     1 
ATOM   168  O  O     . ILE A 1 24  ? -35.875 -21.318 -2.885  1.00 26.98 ? 24   ILE A O     1 
ATOM   169  C  CB    . ILE A 1 24  ? -34.773 -24.345 -1.814  1.00 26.59 ? 24   ILE A CB    1 
ATOM   170  C  CG1   . ILE A 1 24  ? -35.323 -25.738 -1.500  1.00 26.55 ? 24   ILE A CG1   1 
ATOM   171  C  CG2   . ILE A 1 24  ? -34.765 -23.465 -0.573  1.00 27.56 ? 24   ILE A CG2   1 
ATOM   172  C  CD1   . ILE A 1 24  ? -34.357 -26.627 -0.744  1.00 27.82 ? 24   ILE A CD1   1 
ATOM   173  N  N     . VAL A 1 25  ? -33.913 -21.972 -3.777  1.00 24.10 ? 25   VAL A N     1 
ATOM   174  C  CA    . VAL A 1 25  ? -33.323 -20.592 -3.731  1.00 26.02 ? 25   VAL A CA    1 
ATOM   175  C  C     . VAL A 1 25  ? -33.484 -19.873 -5.072  1.00 27.26 ? 25   VAL A C     1 
ATOM   176  O  O     . VAL A 1 25  ? -33.283 -18.619 -5.088  1.00 25.19 ? 25   VAL A O     1 
ATOM   177  C  CB    . VAL A 1 25  ? -31.844 -20.595 -3.299  1.00 24.18 ? 25   VAL A CB    1 
ATOM   178  C  CG1   . VAL A 1 25  ? -31.685 -21.219 -1.922  1.00 23.24 ? 25   VAL A CG1   1 
ATOM   179  C  CG2   . VAL A 1 25  ? -30.943 -21.283 -4.330  1.00 24.98 ? 25   VAL A CG2   1 
ATOM   180  N  N     . GLY A 1 26  ? -33.769 -20.618 -6.139  1.00 26.05 ? 26   GLY A N     1 
ATOM   181  C  CA    . GLY A 1 26  ? -33.688 -20.116 -7.526  1.00 29.26 ? 26   GLY A CA    1 
ATOM   182  C  C     . GLY A 1 26  ? -32.449 -20.649 -8.235  1.00 29.85 ? 26   GLY A C     1 
ATOM   183  O  O     . GLY A 1 26  ? -31.367 -20.729 -7.612  1.00 29.37 ? 26   GLY A O     1 
ATOM   184  N  N     . ALA A 1 27  ? -32.573 -20.980 -9.513  1.00 29.36 ? 27   ALA A N     1 
ATOM   185  C  CA    . ALA A 1 27  ? -31.472 -21.506 -10.348 1.00 30.20 ? 27   ALA A CA    1 
ATOM   186  C  C     . ALA A 1 27  ? -30.307 -20.494 -10.353 1.00 29.21 ? 27   ALA A C     1 
ATOM   187  O  O     . ALA A 1 27  ? -29.142 -20.916 -10.439 1.00 30.58 ? 27   ALA A O     1 
ATOM   188  C  CB    . ALA A 1 27  ? -32.008 -21.794 -11.737 1.00 31.00 ? 27   ALA A CB    1 
ATOM   189  N  N     . ASP A 1 28  ? -30.589 -19.197 -10.205 1.00 28.73 ? 28   ASP A N     1 
ATOM   190  C  CA    . ASP A 1 28  ? -29.544 -18.139 -10.243 1.00 30.54 ? 28   ASP A CA    1 
ATOM   191  C  C     . ASP A 1 28  ? -28.710 -18.152 -8.953  1.00 29.91 ? 28   ASP A C     1 
ATOM   192  O  O     . ASP A 1 28  ? -27.715 -17.432 -8.926  1.00 26.99 ? 28   ASP A O     1 
ATOM   193  C  CB    . ASP A 1 28  ? -30.143 -16.740 -10.446 1.00 34.05 ? 28   ASP A CB    1 
ATOM   194  C  CG    . ASP A 1 28  ? -30.848 -16.546 -11.784 1.00 37.47 ? 28   ASP A CG    1 
ATOM   195  O  OD1   . ASP A 1 28  ? -30.670 -17.389 -12.684 1.00 41.38 ? 28   ASP A OD1   1 
ATOM   196  O  OD2   . ASP A 1 28  ? -31.571 -15.556 -11.915 1.00 42.90 ? 28   ASP A OD2   1 
ATOM   197  N  N     . TRP A 1 29  ? -29.098 -18.909 -7.913  1.00 29.38 ? 29   TRP A N     1 
ATOM   198  C  CA    . TRP A 1 29  ? -28.437 -18.835 -6.585  1.00 25.97 ? 29   TRP A CA    1 
ATOM   199  C  C     . TRP A 1 29  ? -27.796 -20.169 -6.210  1.00 25.32 ? 29   TRP A C     1 
ATOM   200  O  O     . TRP A 1 29  ? -27.470 -20.362 -5.026  1.00 23.34 ? 29   TRP A O     1 
ATOM   201  C  CB    . TRP A 1 29  ? -29.425 -18.286 -5.558  1.00 25.39 ? 29   TRP A CB    1 
ATOM   202  C  CG    . TRP A 1 29  ? -29.871 -16.907 -5.937  1.00 27.32 ? 29   TRP A CG    1 
ATOM   203  C  CD1   . TRP A 1 29  ? -31.114 -16.540 -6.361  1.00 27.32 ? 29   TRP A CD1   1 
ATOM   204  C  CD2   . TRP A 1 29  ? -29.055 -15.720 -6.022  1.00 26.59 ? 29   TRP A CD2   1 
ATOM   205  N  NE1   . TRP A 1 29  ? -31.141 -15.202 -6.629  1.00 27.60 ? 29   TRP A NE1   1 
ATOM   206  C  CE2   . TRP A 1 29  ? -29.893 -14.676 -6.471  1.00 25.10 ? 29   TRP A CE2   1 
ATOM   207  C  CE3   . TRP A 1 29  ? -27.706 -15.434 -5.777  1.00 26.03 ? 29   TRP A CE3   1 
ATOM   208  C  CZ2   . TRP A 1 29  ? -29.439 -13.368 -6.638  1.00 26.26 ? 29   TRP A CZ2   1 
ATOM   209  C  CZ3   . TRP A 1 29  ? -27.254 -14.141 -5.957  1.00 28.01 ? 29   TRP A CZ3   1 
ATOM   210  C  CH2   . TRP A 1 29  ? -28.110 -13.119 -6.380  1.00 25.91 ? 29   TRP A CH2   1 
ATOM   211  N  N     . VAL A 1 30  ? -27.561 -21.017 -7.207  1.00 25.89 ? 30   VAL A N     1 
ATOM   212  C  CA    . VAL A 1 30  ? -26.748 -22.260 -7.084  1.00 24.88 ? 30   VAL A CA    1 
ATOM   213  C  C     . VAL A 1 30  ? -25.608 -22.091 -8.083  1.00 26.00 ? 30   VAL A C     1 
ATOM   214  O  O     . VAL A 1 30  ? -25.901 -21.824 -9.249  1.00 24.15 ? 30   VAL A O     1 
ATOM   215  C  CB    . VAL A 1 30  ? -27.552 -23.554 -7.350  1.00 23.60 ? 30   VAL A CB    1 
ATOM   216  C  CG1   . VAL A 1 30  ? -26.679 -24.801 -7.273  1.00 23.27 ? 30   VAL A CG1   1 
ATOM   217  C  CG2   . VAL A 1 30  ? -28.719 -23.690 -6.387  1.00 24.38 ? 30   VAL A CG2   1 
ATOM   218  N  N     . PHE A 1 31  ? -24.368 -22.236 -7.622  1.00 27.38 ? 31   PHE A N     1 
ATOM   219  C  CA    . PHE A 1 31  ? -23.132 -21.917 -8.374  1.00 25.98 ? 31   PHE A CA    1 
ATOM   220  C  C     . PHE A 1 31  ? -22.343 -23.216 -8.557  1.00 27.60 ? 31   PHE A C     1 
ATOM   221  O  O     . PHE A 1 31  ? -22.055 -23.922 -7.540  1.00 23.77 ? 31   PHE A O     1 
ATOM   222  C  CB    . PHE A 1 31  ? -22.371 -20.812 -7.638  1.00 27.12 ? 31   PHE A CB    1 
ATOM   223  C  CG    . PHE A 1 31  ? -23.171 -19.554 -7.408  1.00 25.62 ? 31   PHE A CG    1 
ATOM   224  C  CD1   . PHE A 1 31  ? -23.585 -18.762 -8.463  1.00 29.17 ? 31   PHE A CD1   1 
ATOM   225  C  CD2   . PHE A 1 31  ? -23.521 -19.163 -6.137  1.00 27.43 ? 31   PHE A CD2   1 
ATOM   226  C  CE1   . PHE A 1 31  ? -24.341 -17.619 -8.238  1.00 32.63 ? 31   PHE A CE1   1 
ATOM   227  C  CE2   . PHE A 1 31  ? -24.257 -18.012 -5.911  1.00 27.64 ? 31   PHE A CE2   1 
ATOM   228  C  CZ    . PHE A 1 31  ? -24.673 -17.244 -6.961  1.00 27.40 ? 31   PHE A CZ    1 
ATOM   229  N  N     . THR A 1 32  ? -22.057 -23.551 -9.824  1.00 27.16 ? 32   THR A N     1 
ATOM   230  C  CA    . THR A 1 32  ? -21.220 -24.713 -10.241 1.00 30.50 ? 32   THR A CA    1 
ATOM   231  C  C     . THR A 1 32  ? -20.221 -24.252 -11.299 1.00 30.35 ? 32   THR A C     1 
ATOM   232  O  O     . THR A 1 32  ? -20.355 -23.114 -11.785 1.00 33.45 ? 32   THR A O     1 
ATOM   233  C  CB    . THR A 1 32  ? -22.086 -25.860 -10.790 1.00 30.85 ? 32   THR A CB    1 
ATOM   234  O  OG1   . THR A 1 32  ? -22.713 -25.388 -11.980 1.00 30.24 ? 32   THR A OG1   1 
ATOM   235  C  CG2   . THR A 1 32  ? -23.163 -26.321 -9.836  1.00 29.81 ? 32   THR A CG2   1 
ATOM   236  N  N     . GLU A 1 33  ? -19.298 -25.125 -11.682 1.00 40.20 ? 33   GLU A N     1 
ATOM   237  C  CA    . GLU A 1 33  ? -18.430 -24.952 -12.884 1.00 47.15 ? 33   GLU A CA    1 
ATOM   238  C  C     . GLU A 1 33  ? -17.624 -23.666 -12.705 1.00 45.33 ? 33   GLU A C     1 
ATOM   239  O  O     . GLU A 1 33  ? -16.997 -23.536 -11.644 1.00 49.20 ? 33   GLU A O     1 
ATOM   240  C  CB    . GLU A 1 33  ? -19.287 -24.950 -14.157 1.00 55.83 ? 33   GLU A CB    1 
ATOM   241  C  CG    . GLU A 1 33  ? -20.480 -25.899 -14.094 1.00 62.37 ? 33   GLU A CG    1 
ATOM   242  C  CD    . GLU A 1 33  ? -20.799 -26.672 -15.363 1.00 67.13 ? 33   GLU A CD    1 
ATOM   243  O  OE1   . GLU A 1 33  ? -21.748 -26.280 -16.075 1.00 70.35 ? 33   GLU A OE1   1 
ATOM   244  O  OE2   . GLU A 1 33  ? -20.114 -27.682 -15.620 1.00 73.94 ? 33   GLU A OE2   1 
ATOM   245  N  N     . ASP A 1 34  ? -17.726 -22.723 -13.640 1.00 44.64 ? 34   ASP A N     1 
ATOM   246  C  CA    . ASP A 1 34  ? -16.942 -21.460 -13.642 1.00 50.69 ? 34   ASP A CA    1 
ATOM   247  C  C     . ASP A 1 34  ? -17.326 -20.581 -12.441 1.00 48.46 ? 34   ASP A C     1 
ATOM   248  O  O     . ASP A 1 34  ? -16.433 -19.856 -11.920 1.00 46.51 ? 34   ASP A O     1 
ATOM   249  C  CB    . ASP A 1 34  ? -17.091 -20.735 -14.984 1.00 62.38 ? 34   ASP A CB    1 
ATOM   250  C  CG    . ASP A 1 34  ? -16.513 -21.512 -16.160 1.00 69.34 ? 34   ASP A CG    1 
ATOM   251  O  OD1   . ASP A 1 34  ? -15.853 -22.542 -15.917 1.00 74.03 ? 34   ASP A OD1   1 
ATOM   252  O  OD2   . ASP A 1 34  ? -16.738 -21.088 -17.313 1.00 83.27 ? 34   ASP A OD2   1 
ATOM   253  N  N     . LYS A 1 35  ? -18.571 -20.655 -11.970 1.00 41.54 ? 35   LYS A N     1 
ATOM   254  C  CA    . LYS A 1 35  ? -19.067 -19.765 -10.887 1.00 37.43 ? 35   LYS A CA    1 
ATOM   255  C  C     . LYS A 1 35  ? -18.627 -20.247 -9.488  1.00 33.05 ? 35   LYS A C     1 
ATOM   256  O  O     . LYS A 1 35  ? -19.016 -19.614 -8.490  1.00 33.85 ? 35   LYS A O     1 
ATOM   257  C  CB    . LYS A 1 35  ? -20.587 -19.684 -10.987 1.00 45.35 ? 35   LYS A CB    1 
ATOM   258  C  CG    . LYS A 1 35  ? -21.115 -19.124 -12.302 1.00 52.02 ? 35   LYS A CG    1 
ATOM   259  C  CD    . LYS A 1 35  ? -22.352 -18.256 -12.115 1.00 59.23 ? 35   LYS A CD    1 
ATOM   260  C  CE    . LYS A 1 35  ? -22.689 -17.444 -13.347 1.00 67.87 ? 35   LYS A CE    1 
ATOM   261  N  NZ    . LYS A 1 35  ? -23.052 -18.313 -14.494 1.00 70.36 ? 35   LYS A NZ    1 
ATOM   262  N  N     . ILE A 1 36  ? -17.843 -21.315 -9.369  1.00 29.63 ? 36   ILE A N     1 
ATOM   263  C  CA    . ILE A 1 36  ? -17.359 -21.782 -8.035  1.00 28.91 ? 36   ILE A CA    1 
ATOM   264  C  C     . ILE A 1 36  ? -16.056 -21.054 -7.665  1.00 27.27 ? 36   ILE A C     1 
ATOM   265  O  O     . ILE A 1 36  ? -15.660 -21.168 -6.514  1.00 28.00 ? 36   ILE A O     1 
ATOM   266  C  CB    . ILE A 1 36  ? -17.207 -23.323 -7.994  1.00 28.93 ? 36   ILE A CB    1 
ATOM   267  C  CG1   . ILE A 1 36  ? -17.278 -23.898 -6.580  1.00 31.28 ? 36   ILE A CG1   1 
ATOM   268  C  CG2   . ILE A 1 36  ? -15.911 -23.772 -8.641  1.00 31.15 ? 36   ILE A CG2   1 
ATOM   269  C  CD1   . ILE A 1 36  ? -18.513 -23.543 -5.812  1.00 32.60 ? 36   ILE A CD1   1 
ATOM   270  N  N     . THR A 1 37  ? -15.399 -20.359 -8.600  1.00 26.52 ? 37   THR A N     1 
ATOM   271  C  CA    . THR A 1 37  ? -13.993 -19.878 -8.469  1.00 29.03 ? 37   THR A CA    1 
ATOM   272  C  C     . THR A 1 37  ? -13.832 -19.036 -7.213  1.00 24.93 ? 37   THR A C     1 
ATOM   273  O  O     . THR A 1 37  ? -12.899 -19.243 -6.437  1.00 25.59 ? 37   THR A O     1 
ATOM   274  C  CB    . THR A 1 37  ? -13.528 -19.152 -9.742  1.00 30.37 ? 37   THR A CB    1 
ATOM   275  O  OG1   . THR A 1 37  ? -13.664 -20.140 -10.758 1.00 36.91 ? 37   THR A OG1   1 
ATOM   276  C  CG2   . THR A 1 37  ? -12.080 -18.729 -9.732  1.00 33.81 ? 37   THR A CG2   1 
ATOM   277  N  N     . PRO A 1 38  ? -14.744 -18.086 -6.944  1.00 24.44 ? 38   PRO A N     1 
ATOM   278  C  CA    . PRO A 1 38  ? -14.610 -17.242 -5.753  1.00 23.65 ? 38   PRO A CA    1 
ATOM   279  C  C     . PRO A 1 38  ? -14.705 -17.998 -4.408  1.00 23.58 ? 38   PRO A C     1 
ATOM   280  O  O     . PRO A 1 38  ? -14.434 -17.405 -3.392  1.00 23.22 ? 38   PRO A O     1 
ATOM   281  C  CB    . PRO A 1 38  ? -15.801 -16.264 -5.861  1.00 24.10 ? 38   PRO A CB    1 
ATOM   282  C  CG    . PRO A 1 38  ? -16.275 -16.336 -7.303  1.00 24.12 ? 38   PRO A CG    1 
ATOM   283  C  CD    . PRO A 1 38  ? -15.900 -17.722 -7.789  1.00 23.75 ? 38   PRO A CD    1 
ATOM   284  N  N     . TYR A 1 39  ? -15.146 -19.258 -4.403  1.00 21.33 ? 39   TYR A N     1 
ATOM   285  C  CA    . TYR A 1 39  ? -15.330 -20.043 -3.162  1.00 21.64 ? 39   TYR A CA    1 
ATOM   286  C  C     . TYR A 1 39  ? -14.071 -20.879 -2.894  1.00 22.47 ? 39   TYR A C     1 
ATOM   287  O  O     . TYR A 1 39  ? -13.968 -21.471 -1.787  1.00 24.36 ? 39   TYR A O     1 
ATOM   288  C  CB    . TYR A 1 39  ? -16.614 -20.876 -3.235  1.00 22.35 ? 39   TYR A CB    1 
ATOM   289  C  CG    . TYR A 1 39  ? -17.873 -20.056 -3.288  1.00 23.10 ? 39   TYR A CG    1 
ATOM   290  C  CD1   . TYR A 1 39  ? -18.483 -19.634 -2.117  1.00 22.18 ? 39   TYR A CD1   1 
ATOM   291  C  CD2   . TYR A 1 39  ? -18.485 -19.728 -4.498  1.00 23.57 ? 39   TYR A CD2   1 
ATOM   292  C  CE1   . TYR A 1 39  ? -19.647 -18.877 -2.138  1.00 21.69 ? 39   TYR A CE1   1 
ATOM   293  C  CE2   . TYR A 1 39  ? -19.636 -18.954 -4.537  1.00 21.35 ? 39   TYR A CE2   1 
ATOM   294  C  CZ    . TYR A 1 39  ? -20.223 -18.537 -3.350  1.00 22.91 ? 39   TYR A CZ    1 
ATOM   295  O  OH    . TYR A 1 39  ? -21.365 -17.801 -3.333  1.00 22.63 ? 39   TYR A OH    1 
ATOM   296  N  N     . GLU A 1 40  ? -13.135 -20.910 -3.846  1.00 19.94 ? 40   GLU A N     1 
ATOM   297  C  CA    . GLU A 1 40  ? -11.789 -21.481 -3.639  1.00 20.35 ? 40   GLU A CA    1 
ATOM   298  C  C     . GLU A 1 40  ? -11.064 -20.615 -2.597  1.00 19.51 ? 40   GLU A C     1 
ATOM   299  O  O     . GLU A 1 40  ? -11.285 -19.400 -2.559  1.00 18.18 ? 40   GLU A O     1 
ATOM   300  C  CB    . GLU A 1 40  ? -10.994 -21.502 -4.949  1.00 23.10 ? 40   GLU A CB    1 
ATOM   301  C  CG    . GLU A 1 40  ? -11.678 -22.248 -6.109  1.00 25.65 ? 40   GLU A CG    1 
ATOM   302  C  CD    . GLU A 1 40  ? -11.744 -23.756 -5.989  1.00 26.51 ? 40   GLU A CD    1 
ATOM   303  O  OE1   . GLU A 1 40  ? -11.135 -24.315 -5.056  1.00 28.81 ? 40   GLU A OE1   1 
ATOM   304  O  OE2   . GLU A 1 40  ? -12.391 -24.386 -6.838  1.00 31.44 ? 40   GLU A OE2   1 
ATOM   305  N  N     . ASP A 1 41  ? -10.161 -21.209 -1.829  1.00 19.34 ? 41   ASP A N     1 
ATOM   306  C  CA    . ASP A 1 41  ? -9.189  -20.438 -1.013  1.00 20.60 ? 41   ASP A CA    1 
ATOM   307  C  C     . ASP A 1 41  ? -8.376  -19.546 -1.952  1.00 20.12 ? 41   ASP A C     1 
ATOM   308  O  O     . ASP A 1 41  ? -7.734  -20.078 -2.835  1.00 19.34 ? 41   ASP A O     1 
ATOM   309  C  CB    . ASP A 1 41  ? -8.293  -21.402 -0.242  1.00 20.72 ? 41   ASP A CB    1 
ATOM   310  C  CG    . ASP A 1 41  ? -7.339  -20.734 0.728   1.00 20.36 ? 41   ASP A CG    1 
ATOM   311  O  OD1   . ASP A 1 41  ? -7.348  -19.482 0.805   1.00 20.54 ? 41   ASP A OD1   1 
ATOM   312  O  OD2   . ASP A 1 41  ? -6.581  -21.484 1.400   1.00 22.69 ? 41   ASP A OD2   1 
ATOM   313  N  N     . PRO A 1 42  ? -8.400  -18.191 -1.852  1.00 20.66 ? 42   PRO A N     1 
ATOM   314  C  CA    . PRO A 1 42  ? -7.530  -17.342 -2.671  1.00 19.62 ? 42   PRO A CA    1 
ATOM   315  C  C     . PRO A 1 42  ? -6.032  -17.526 -2.368  1.00 21.39 ? 42   PRO A C     1 
ATOM   316  O  O     . PRO A 1 42  ? -5.189  -17.164 -3.210  1.00 24.95 ? 42   PRO A O     1 
ATOM   317  C  CB    . PRO A 1 42  ? -7.956  -15.900 -2.308  1.00 21.15 ? 42   PRO A CB    1 
ATOM   318  C  CG    . PRO A 1 42  ? -8.566  -16.039 -0.903  1.00 21.71 ? 42   PRO A CG    1 
ATOM   319  C  CD    . PRO A 1 42  ? -9.235  -17.403 -0.929  1.00 20.25 ? 42   PRO A CD    1 
ATOM   320  N  N     . TYR A 1 43  ? -5.694  -18.065 -1.193  1.00 21.08 ? 43   TYR A N     1 
ATOM   321  C  CA    . TYR A 1 43  ? -4.292  -18.219 -0.727  1.00 21.35 ? 43   TYR A CA    1 
ATOM   322  C  C     . TYR A 1 43  ? -3.903  -19.700 -0.673  1.00 22.42 ? 43   TYR A C     1 
ATOM   323  O  O     . TYR A 1 43  ? -3.645  -20.249 0.423   1.00 26.17 ? 43   TYR A O     1 
ATOM   324  C  CB    . TYR A 1 43  ? -4.126  -17.525 0.622   1.00 22.65 ? 43   TYR A CB    1 
ATOM   325  C  CG    . TYR A 1 43  ? -4.568  -16.086 0.712   1.00 20.73 ? 43   TYR A CG    1 
ATOM   326  C  CD1   . TYR A 1 43  ? -4.629  -15.231 -0.385  1.00 21.87 ? 43   TYR A CD1   1 
ATOM   327  C  CD2   . TYR A 1 43  ? -4.887  -15.571 1.949   1.00 20.63 ? 43   TYR A CD2   1 
ATOM   328  C  CE1   . TYR A 1 43  ? -5.029  -13.900 -0.249  1.00 20.70 ? 43   TYR A CE1   1 
ATOM   329  C  CE2   . TYR A 1 43  ? -5.248  -14.245 2.110   1.00 21.42 ? 43   TYR A CE2   1 
ATOM   330  C  CZ    . TYR A 1 43  ? -5.330  -13.408 1.014   1.00 22.30 ? 43   TYR A CZ    1 
ATOM   331  O  OH    . TYR A 1 43  ? -5.706  -12.113 1.253   1.00 22.12 ? 43   TYR A OH    1 
ATOM   332  N  N     . THR A 1 44  ? -3.931  -20.361 -1.829  1.00 22.90 ? 44   THR A N     1 
ATOM   333  C  CA    . THR A 1 44  ? -3.715  -21.829 -1.968  1.00 23.86 ? 44   THR A CA    1 
ATOM   334  C  C     . THR A 1 44  ? -2.479  -22.246 -1.166  1.00 24.74 ? 44   THR A C     1 
ATOM   335  O  O     . THR A 1 44  ? -1.427  -21.556 -1.280  1.00 29.29 ? 44   THR A O     1 
ATOM   336  C  CB    . THR A 1 44  ? -3.461  -22.232 -3.423  1.00 23.52 ? 44   THR A CB    1 
ATOM   337  O  OG1   . THR A 1 44  ? -4.409  -21.522 -4.235  1.00 22.06 ? 44   THR A OG1   1 
ATOM   338  C  CG2   . THR A 1 44  ? -3.516  -23.733 -3.609  1.00 22.41 ? 44   THR A CG2   1 
ATOM   339  N  N     . ILE A 1 45  ? -2.581  -23.322 -0.391  1.00 23.78 ? 45   ILE A N     1 
ATOM   340  C  CA    . ILE A 1 45  ? -1.404  -23.898 0.314   1.00 23.34 ? 45   ILE A CA    1 
ATOM   341  C  C     . ILE A 1 45  ? -1.033  -25.242 -0.323  1.00 25.06 ? 45   ILE A C     1 
ATOM   342  O  O     . ILE A 1 45  ? 0.161   -25.449 -0.611  1.00 28.87 ? 45   ILE A O     1 
ATOM   343  C  CB    . ILE A 1 45  ? -1.659  -23.992 1.817   1.00 22.87 ? 45   ILE A CB    1 
ATOM   344  C  CG1   . ILE A 1 45  ? -1.896  -22.606 2.442   1.00 22.44 ? 45   ILE A CG1   1 
ATOM   345  C  CG2   . ILE A 1 45  ? -0.502  -24.703 2.509   1.00 25.01 ? 45   ILE A CG2   1 
ATOM   346  C  CD1   . ILE A 1 45  ? -2.085  -22.656 3.942   1.00 21.49 ? 45   ILE A CD1   1 
ATOM   347  N  N     . SER A 1 46  ? -1.994  -26.132 -0.503  1.00 25.00 ? 46   SER A N     1 
ATOM   348  C  CA    . SER A 1 46  ? -1.753  -27.510 -0.990  1.00 27.31 ? 46   SER A CA    1 
ATOM   349  C  C     . SER A 1 46  ? -1.223  -27.471 -2.432  1.00 26.58 ? 46   SER A C     1 
ATOM   350  O  O     . SER A 1 46  ? -1.675  -26.601 -3.237  1.00 21.28 ? 46   SER A O     1 
ATOM   351  C  CB    . SER A 1 46  ? -3.019  -28.324 -0.900  1.00 29.05 ? 46   SER A CB    1 
ATOM   352  O  OG    . SER A 1 46  ? -2.758  -29.657 -1.276  1.00 30.87 ? 46   SER A OG    1 
ATOM   353  N  N     . ASN A 1 47  ? -0.340  -28.411 -2.762  1.00 28.30 ? 47   ASN A N     1 
ATOM   354  C  CA    . ASN A 1 47  ? 0.068   -28.685 -4.167  1.00 30.00 ? 47   ASN A CA    1 
ATOM   355  C  C     . ASN A 1 47  ? -0.778  -29.830 -4.739  1.00 31.75 ? 47   ASN A C     1 
ATOM   356  O  O     . ASN A 1 47  ? -0.594  -30.147 -5.920  1.00 31.52 ? 47   ASN A O     1 
ATOM   357  C  CB    . ASN A 1 47  ? 1.570   -28.944 -4.238  1.00 28.59 ? 47   ASN A CB    1 
ATOM   358  C  CG    . ASN A 1 47  ? 2.354   -27.660 -4.096  1.00 27.50 ? 47   ASN A CG    1 
ATOM   359  O  OD1   . ASN A 1 47  ? 1.899   -26.604 -4.508  1.00 30.10 ? 47   ASN A OD1   1 
ATOM   360  N  ND2   . ASN A 1 47  ? 3.541   -27.728 -3.532  1.00 27.95 ? 47   ASN A ND2   1 
ATOM   361  N  N     . ASP A 1 48  ? -1.689  -30.400 -3.939  1.00 30.42 ? 48   ASP A N     1 
ATOM   362  C  CA    . ASP A 1 48  ? -2.668  -31.436 -4.369  1.00 29.09 ? 48   ASP A CA    1 
ATOM   363  C  C     . ASP A 1 48  ? -4.014  -30.768 -4.697  1.00 30.80 ? 48   ASP A C     1 
ATOM   364  O  O     . ASP A 1 48  ? -4.757  -30.450 -3.750  1.00 29.82 ? 48   ASP A O     1 
ATOM   365  C  CB    . ASP A 1 48  ? -2.829  -32.495 -3.280  1.00 28.46 ? 48   ASP A CB    1 
ATOM   366  C  CG    . ASP A 1 48  ? -3.751  -33.631 -3.685  1.00 28.42 ? 48   ASP A CG    1 
ATOM   367  O  OD1   . ASP A 1 48  ? -4.548  -33.429 -4.608  1.00 30.72 ? 48   ASP A OD1   1 
ATOM   368  O  OD2   . ASP A 1 48  ? -3.690  -34.695 -3.035  1.00 30.71 ? 48   ASP A OD2   1 
ATOM   369  N  N     . GLU A 1 49  ? -4.347  -30.664 -5.983  1.00 31.66 ? 49   GLU A N     1 
ATOM   370  C  CA    . GLU A 1 49  ? -5.530  -29.944 -6.525  1.00 32.68 ? 49   GLU A CA    1 
ATOM   371  C  C     . GLU A 1 49  ? -6.854  -30.639 -6.180  1.00 30.55 ? 49   GLU A C     1 
ATOM   372  O  O     . GLU A 1 49  ? -7.878  -30.035 -6.488  1.00 29.31 ? 49   GLU A O     1 
ATOM   373  C  CB    . GLU A 1 49  ? -5.398  -29.795 -8.036  1.00 35.01 ? 49   GLU A CB    1 
ATOM   374  C  CG    . GLU A 1 49  ? -4.386  -28.752 -8.426  1.00 40.27 ? 49   GLU A CG    1 
ATOM   375  C  CD    . GLU A 1 49  ? -4.583  -28.150 -9.810  1.00 48.54 ? 49   GLU A CD    1 
ATOM   376  O  OE1   . GLU A 1 49  ? -5.452  -28.635 -10.553 1.00 48.08 ? 49   GLU A OE1   1 
ATOM   377  O  OE2   . GLU A 1 49  ? -3.857  -27.186 -10.139 1.00 58.07 ? 49   GLU A OE2   1 
ATOM   378  N  N     . THR A 1 50  ? -6.832  -31.819 -5.546  1.00 27.80 ? 50   THR A N     1 
ATOM   379  C  CA    . THR A 1 50  ? -8.033  -32.548 -5.080  1.00 30.18 ? 50   THR A CA    1 
ATOM   380  C  C     . THR A 1 50  ? -8.409  -32.166 -3.635  1.00 31.29 ? 50   THR A C     1 
ATOM   381  O  O     . THR A 1 50  ? -9.382  -32.773 -3.116  1.00 31.80 ? 50   THR A O     1 
ATOM   382  C  CB    . THR A 1 50  ? -7.839  -34.073 -5.129  1.00 29.36 ? 50   THR A CB    1 
ATOM   383  O  OG1   . THR A 1 50  ? -6.872  -34.423 -4.129  1.00 31.79 ? 50   THR A OG1   1 
ATOM   384  C  CG2   . THR A 1 50  ? -7.421  -34.577 -6.497  1.00 29.91 ? 50   THR A CG2   1 
ATOM   385  N  N     . GLU A 1 51  ? -7.680  -31.263 -2.975  1.00 27.02 ? 51   GLU A N     1 
ATOM   386  C  CA    . GLU A 1 51  ? -7.918  -30.960 -1.532  1.00 26.79 ? 51   GLU A CA    1 
ATOM   387  C  C     . GLU A 1 51  ? -8.599  -29.592 -1.377  1.00 25.29 ? 51   GLU A C     1 
ATOM   388  O  O     . GLU A 1 51  ? -8.251  -28.649 -2.124  1.00 21.84 ? 51   GLU A O     1 
ATOM   389  C  CB    . GLU A 1 51  ? -6.612  -30.947 -0.743  1.00 28.10 ? 51   GLU A CB    1 
ATOM   390  C  CG    . GLU A 1 51  ? -5.931  -32.287 -0.663  1.00 30.70 ? 51   GLU A CG    1 
ATOM   391  C  CD    . GLU A 1 51  ? -4.756  -32.332 0.303   1.00 31.68 ? 51   GLU A CD    1 
ATOM   392  O  OE1   . GLU A 1 51  ? -3.866  -31.460 0.235   1.00 28.61 ? 51   GLU A OE1   1 
ATOM   393  O  OE2   . GLU A 1 51  ? -4.720  -33.259 1.096   1.00 36.34 ? 51   GLU A OE2   1 
ATOM   394  N  N     . HIS A 1 52  ? -9.534  -29.499 -0.429  1.00 26.11 ? 52   HIS A N     1 
ATOM   395  C  CA    . HIS A 1 52  ? -10.199 -28.239 -0.001  1.00 26.00 ? 52   HIS A CA    1 
ATOM   396  C  C     . HIS A 1 52  ? -10.981 -27.635 -1.160  1.00 22.99 ? 52   HIS A C     1 
ATOM   397  O  O     . HIS A 1 52  ? -10.957 -26.429 -1.290  1.00 23.62 ? 52   HIS A O     1 
ATOM   398  C  CB    . HIS A 1 52  ? -9.161  -27.241 0.533   1.00 26.96 ? 52   HIS A CB    1 
ATOM   399  C  CG    . HIS A 1 52  ? -8.204  -27.860 1.485   1.00 30.00 ? 52   HIS A CG    1 
ATOM   400  N  ND1   . HIS A 1 52  ? -8.641  -28.610 2.556   1.00 30.90 ? 52   HIS A ND1   1 
ATOM   401  C  CD2   . HIS A 1 52  ? -6.847  -27.880 1.503   1.00 30.26 ? 52   HIS A CD2   1 
ATOM   402  C  CE1   . HIS A 1 52  ? -7.582  -29.067 3.205   1.00 32.63 ? 52   HIS A CE1   1 
ATOM   403  N  NE2   . HIS A 1 52  ? -6.464  -28.638 2.571   1.00 30.94 ? 52   HIS A NE2   1 
ATOM   404  N  N     . ARG A 1 53  ? -11.592 -28.461 -1.993  1.00 22.64 ? 53   ARG A N     1 
ATOM   405  C  CA    . ARG A 1 53  ? -12.274 -28.028 -3.246  1.00 21.86 ? 53   ARG A CA    1 
ATOM   406  C  C     . ARG A 1 53  ? -13.777 -28.025 -2.989  1.00 23.32 ? 53   ARG A C     1 
ATOM   407  O  O     . ARG A 1 53  ? -14.383 -29.072 -2.761  1.00 22.43 ? 53   ARG A O     1 
ATOM   408  C  CB    . ARG A 1 53  ? -11.958 -28.985 -4.402  1.00 22.57 ? 53   ARG A CB    1 
ATOM   409  C  CG    . ARG A 1 53  ? -10.483 -29.075 -4.769  1.00 23.08 ? 53   ARG A CG    1 
ATOM   410  C  CD    . ARG A 1 53  ? -9.820  -27.741 -5.087  1.00 22.31 ? 53   ARG A CD    1 
ATOM   411  N  NE    . ARG A 1 53  ? -10.433 -27.047 -6.210  1.00 23.63 ? 53   ARG A NE    1 
ATOM   412  C  CZ    . ARG A 1 53  ? -10.372 -27.448 -7.483  1.00 24.91 ? 53   ARG A CZ    1 
ATOM   413  N  NH1   . ARG A 1 53  ? -9.750  -28.567 -7.830  1.00 26.06 ? 53   ARG A NH1   1 
ATOM   414  N  NH2   . ARG A 1 53  ? -10.974 -26.743 -8.414  1.00 25.59 ? 53   ARG A NH2   1 
ATOM   415  N  N     . PRO A 1 54  ? -14.430 -26.854 -3.005  1.00 20.93 ? 54   PRO A N     1 
ATOM   416  C  CA    . PRO A 1 54  ? -15.889 -26.813 -2.923  1.00 23.40 ? 54   PRO A CA    1 
ATOM   417  C  C     . PRO A 1 54  ? -16.499 -27.310 -4.234  1.00 24.03 ? 54   PRO A C     1 
ATOM   418  O  O     . PRO A 1 54  ? -15.968 -27.004 -5.334  1.00 25.75 ? 54   PRO A O     1 
ATOM   419  C  CB    . PRO A 1 54  ? -16.198 -25.331 -2.706  1.00 20.96 ? 54   PRO A CB    1 
ATOM   420  C  CG    . PRO A 1 54  ? -15.036 -24.641 -3.385  1.00 21.42 ? 54   PRO A CG    1 
ATOM   421  C  CD    . PRO A 1 54  ? -13.831 -25.526 -3.133  1.00 20.22 ? 54   PRO A CD    1 
ATOM   422  N  N     . TYR A 1 55  ? -17.552 -28.111 -4.114  1.00 25.42 ? 55   TYR A N     1 
ATOM   423  C  CA    . TYR A 1 55  ? -18.219 -28.733 -5.284  1.00 24.23 ? 55   TYR A CA    1 
ATOM   424  C  C     . TYR A 1 55  ? -19.192 -27.747 -5.930  1.00 23.01 ? 55   TYR A C     1 
ATOM   425  O  O     . TYR A 1 55  ? -19.353 -27.788 -7.123  1.00 21.62 ? 55   TYR A O     1 
ATOM   426  C  CB    . TYR A 1 55  ? -18.960 -29.996 -4.868  1.00 27.07 ? 55   TYR A CB    1 
ATOM   427  C  CG    . TYR A 1 55  ? -19.315 -30.801 -6.077  1.00 29.19 ? 55   TYR A CG    1 
ATOM   428  C  CD1   . TYR A 1 55  ? -18.444 -31.761 -6.567  1.00 31.20 ? 55   TYR A CD1   1 
ATOM   429  C  CD2   . TYR A 1 55  ? -20.470 -30.523 -6.788  1.00 29.23 ? 55   TYR A CD2   1 
ATOM   430  C  CE1   . TYR A 1 55  ? -18.745 -32.478 -7.716  1.00 31.36 ? 55   TYR A CE1   1 
ATOM   431  C  CE2   . TYR A 1 55  ? -20.780 -31.222 -7.944  1.00 32.75 ? 55   TYR A CE2   1 
ATOM   432  C  CZ    . TYR A 1 55  ? -19.916 -32.201 -8.404  1.00 31.87 ? 55   TYR A CZ    1 
ATOM   433  O  OH    . TYR A 1 55  ? -20.230 -32.887 -9.529  1.00 30.90 ? 55   TYR A OH    1 
ATOM   434  N  N     . ALA A 1 56  ? -19.876 -26.944 -5.115  1.00 21.71 ? 56   ALA A N     1 
ATOM   435  C  CA    . ALA A 1 56  ? -20.871 -25.931 -5.507  1.00 21.78 ? 56   ALA A CA    1 
ATOM   436  C  C     . ALA A 1 56  ? -21.132 -25.008 -4.312  1.00 20.64 ? 56   ALA A C     1 
ATOM   437  O  O     . ALA A 1 56  ? -20.608 -25.266 -3.196  1.00 19.41 ? 56   ALA A O     1 
ATOM   438  C  CB    . ALA A 1 56  ? -22.145 -26.612 -5.969  1.00 23.70 ? 56   ALA A CB    1 
ATOM   439  N  N     . ALA A 1 57  ? -21.877 -23.943 -4.555  1.00 20.07 ? 57   ALA A N     1 
ATOM   440  C  CA    . ALA A 1 57  ? -22.388 -23.047 -3.512  1.00 20.98 ? 57   ALA A CA    1 
ATOM   441  C  C     . ALA A 1 57  ? -23.889 -22.825 -3.713  1.00 21.17 ? 57   ALA A C     1 
ATOM   442  O  O     . ALA A 1 57  ? -24.349 -22.809 -4.841  1.00 25.51 ? 57   ALA A O     1 
ATOM   443  C  CB    . ALA A 1 57  ? -21.614 -21.756 -3.520  1.00 20.79 ? 57   ALA A CB    1 
ATOM   444  N  N     . VAL A 1 58  ? -24.603 -22.625 -2.624  1.00 21.32 ? 58   VAL A N     1 
ATOM   445  C  CA    . VAL A 1 58  ? -26.049 -22.262 -2.600  1.00 22.95 ? 58   VAL A CA    1 
ATOM   446  C  C     . VAL A 1 58  ? -26.162 -21.006 -1.724  1.00 21.24 ? 58   VAL A C     1 
ATOM   447  O  O     . VAL A 1 58  ? -25.531 -20.970 -0.628  1.00 21.72 ? 58   VAL A O     1 
ATOM   448  C  CB    . VAL A 1 58  ? -26.919 -23.448 -2.126  1.00 24.00 ? 58   VAL A CB    1 
ATOM   449  C  CG1   . VAL A 1 58  ? -26.443 -24.036 -0.815  1.00 28.03 ? 58   VAL A CG1   1 
ATOM   450  C  CG2   . VAL A 1 58  ? -28.394 -23.085 -2.007  1.00 23.89 ? 58   VAL A CG2   1 
ATOM   451  N  N     . ALA A 1 59  ? -26.867 -19.992 -2.213  1.00 19.57 ? 59   ALA A N     1 
ATOM   452  C  CA    . ALA A 1 59  ? -26.994 -18.658 -1.589  1.00 20.01 ? 59   ALA A CA    1 
ATOM   453  C  C     . ALA A 1 59  ? -28.460 -18.389 -1.260  1.00 21.81 ? 59   ALA A C     1 
ATOM   454  O  O     . ALA A 1 59  ? -29.172 -17.761 -2.043  1.00 24.51 ? 59   ALA A O     1 
ATOM   455  C  CB    . ALA A 1 59  ? -26.446 -17.591 -2.489  1.00 20.70 ? 59   ALA A CB    1 
ATOM   456  N  N     . PRO A 1 60  ? -28.937 -18.842 -0.082  1.00 19.92 ? 60   PRO A N     1 
ATOM   457  C  CA    . PRO A 1 60  ? -30.303 -18.584 0.360   1.00 20.54 ? 60   PRO A CA    1 
ATOM   458  C  C     . PRO A 1 60  ? -30.577 -17.141 0.814   1.00 21.48 ? 60   PRO A C     1 
ATOM   459  O  O     . PRO A 1 60  ? -29.649 -16.434 1.160   1.00 20.78 ? 60   PRO A O     1 
ATOM   460  C  CB    . PRO A 1 60  ? -30.479 -19.504 1.564   1.00 19.64 ? 60   PRO A CB    1 
ATOM   461  C  CG    . PRO A 1 60  ? -29.073 -19.657 2.118   1.00 19.64 ? 60   PRO A CG    1 
ATOM   462  C  CD    . PRO A 1 60  ? -28.177 -19.656 0.886   1.00 19.91 ? 60   PRO A CD    1 
ATOM   463  N  N     . ALA A 1 61  ? -31.868 -16.796 0.838   1.00 23.48 ? 61   ALA A N     1 
ATOM   464  C  CA    . ALA A 1 61  ? -32.411 -15.443 1.100   1.00 24.04 ? 61   ALA A CA    1 
ATOM   465  C  C     . ALA A 1 61  ? -33.047 -15.381 2.489   1.00 22.56 ? 61   ALA A C     1 
ATOM   466  O  O     . ALA A 1 61  ? -33.442 -14.282 2.914   1.00 25.11 ? 61   ALA A O     1 
ATOM   467  C  CB    . ALA A 1 61  ? -33.432 -15.094 0.033   1.00 26.37 ? 61   ALA A CB    1 
ATOM   468  N  N     . SER A 1 62  ? -33.201 -16.502 3.186   1.00 22.00 ? 62   SER A N     1 
ATOM   469  C  CA    . SER A 1 62  ? -33.950 -16.490 4.460   1.00 21.43 ? 62   SER A CA    1 
ATOM   470  C  C     . SER A 1 62  ? -33.649 -17.738 5.295   1.00 21.89 ? 62   SER A C     1 
ATOM   471  O  O     . SER A 1 62  ? -33.218 -18.765 4.712   1.00 20.99 ? 62   SER A O     1 
ATOM   472  C  CB    . SER A 1 62  ? -35.432 -16.411 4.143   1.00 22.40 ? 62   SER A CB    1 
ATOM   473  O  OG    . SER A 1 62  ? -35.856 -17.669 3.630   1.00 20.70 ? 62   SER A OG    1 
ATOM   474  N  N     . THR A 1 63  ? -34.013 -17.682 6.577   1.00 20.20 ? 63   THR A N     1 
ATOM   475  C  CA    . THR A 1 63  ? -33.925 -18.805 7.532   1.00 22.35 ? 63   THR A CA    1 
ATOM   476  C  C     . THR A 1 63  ? -34.714 -19.989 6.968   1.00 22.14 ? 63   THR A C     1 
ATOM   477  O  O     . THR A 1 63  ? -34.236 -21.121 7.048   1.00 21.67 ? 63   THR A O     1 
ATOM   478  C  CB    . THR A 1 63  ? -34.386 -18.371 8.934   1.00 23.46 ? 63   THR A CB    1 
ATOM   479  O  OG1   . THR A 1 63  ? -33.523 -17.333 9.399   1.00 24.51 ? 63   THR A OG1   1 
ATOM   480  C  CG2   . THR A 1 63  ? -34.352 -19.498 9.942   1.00 24.44 ? 63   THR A CG2   1 
ATOM   481  N  N     . GLU A 1 64  ? -35.866 -19.724 6.373   1.00 23.33 ? 64   GLU A N     1 
ATOM   482  C  CA    . GLU A 1 64  ? -36.757 -20.787 5.842   1.00 24.98 ? 64   GLU A CA    1 
ATOM   483  C  C     . GLU A 1 64  ? -36.053 -21.501 4.681   1.00 21.38 ? 64   GLU A C     1 
ATOM   484  O  O     . GLU A 1 64  ? -36.182 -22.735 4.609   1.00 21.11 ? 64   GLU A O     1 
ATOM   485  C  CB    . GLU A 1 64  ? -38.127 -20.202 5.469   1.00 27.66 ? 64   GLU A CB    1 
ATOM   486  C  CG    . GLU A 1 64  ? -38.913 -19.700 6.681   1.00 32.65 ? 64   GLU A CG    1 
ATOM   487  C  CD    . GLU A 1 64  ? -38.769 -18.242 7.148   1.00 36.90 ? 64   GLU A CD    1 
ATOM   488  O  OE1   . GLU A 1 64  ? -37.827 -17.491 6.712   1.00 34.76 ? 64   GLU A OE1   1 
ATOM   489  O  OE2   . GLU A 1 64  ? -39.618 -17.849 7.991   1.00 44.91 ? 64   GLU A OE2   1 
ATOM   490  N  N     . GLU A 1 65  ? -35.319 -20.787 3.824   1.00 18.94 ? 65   GLU A N     1 
ATOM   491  C  CA    . GLU A 1 65  ? -34.573 -21.453 2.730   1.00 19.29 ? 65   GLU A CA    1 
ATOM   492  C  C     . GLU A 1 65  ? -33.440 -22.295 3.345   1.00 20.29 ? 65   GLU A C     1 
ATOM   493  O  O     . GLU A 1 65  ? -33.317 -23.458 2.983   1.00 20.82 ? 65   GLU A O     1 
ATOM   494  C  CB    . GLU A 1 65  ? -34.149 -20.410 1.701   1.00 22.60 ? 65   GLU A CB    1 
ATOM   495  C  CG    . GLU A 1 65  ? -35.344 -19.832 0.943   1.00 22.96 ? 65   GLU A CG    1 
ATOM   496  C  CD    . GLU A 1 65  ? -35.042 -18.844 -0.170  1.00 25.21 ? 65   GLU A CD    1 
ATOM   497  O  OE1   . GLU A 1 65  ? -33.859 -18.685 -0.521  1.00 27.57 ? 65   GLU A OE1   1 
ATOM   498  O  OE2   . GLU A 1 65  ? -36.015 -18.242 -0.690  1.00 27.97 ? 65   GLU A OE2   1 
ATOM   499  N  N     . VAL A 1 66  ? -32.722 -21.778 4.345   1.00 19.79 ? 66   VAL A N     1 
ATOM   500  C  CA    . VAL A 1 66  ? -31.639 -22.522 5.044   1.00 18.86 ? 66   VAL A CA    1 
ATOM   501  C  C     . VAL A 1 66  ? -32.229 -23.833 5.596   1.00 19.39 ? 66   VAL A C     1 
ATOM   502  O  O     . VAL A 1 66  ? -31.610 -24.924 5.422   1.00 19.33 ? 66   VAL A O     1 
ATOM   503  C  CB    . VAL A 1 66  ? -31.006 -21.672 6.168   1.00 17.27 ? 66   VAL A CB    1 
ATOM   504  C  CG1   . VAL A 1 66  ? -30.086 -22.523 7.021   1.00 16.46 ? 66   VAL A CG1   1 
ATOM   505  C  CG2   . VAL A 1 66  ? -30.279 -20.431 5.638   1.00 17.59 ? 66   VAL A CG2   1 
ATOM   506  N  N     . GLN A 1 67  ? -33.380 -23.753 6.253   1.00 18.79 ? 67   GLN A N     1 
ATOM   507  C  CA    . GLN A 1 67  ? -34.045 -24.956 6.807   1.00 20.85 ? 67   GLN A CA    1 
ATOM   508  C  C     . GLN A 1 67  ? -34.307 -25.979 5.691   1.00 21.11 ? 67   GLN A C     1 
ATOM   509  O  O     . GLN A 1 67  ? -34.013 -27.191 5.904   1.00 20.37 ? 67   GLN A O     1 
ATOM   510  C  CB    . GLN A 1 67  ? -35.316 -24.533 7.537   1.00 22.48 ? 67   GLN A CB    1 
ATOM   511  C  CG    . GLN A 1 67  ? -35.041 -23.847 8.869   1.00 22.58 ? 67   GLN A CG    1 
ATOM   512  C  CD    . GLN A 1 67  ? -36.375 -23.513 9.475   1.00 23.53 ? 67   GLN A CD    1 
ATOM   513  O  OE1   . GLN A 1 67  ? -36.982 -22.493 9.176   1.00 26.36 ? 67   GLN A OE1   1 
ATOM   514  N  NE2   . GLN A 1 67  ? -36.856 -24.411 10.308  1.00 25.06 ? 67   GLN A NE2   1 
ATOM   515  N  N     . GLU A 1 68  ? -34.849 -25.537 4.551   1.00 23.01 ? 68   GLU A N     1 
ATOM   516  C  CA    . GLU A 1 68  ? -35.177 -26.444 3.411   1.00 25.16 ? 68   GLU A CA    1 
ATOM   517  C  C     . GLU A 1 68  ? -33.881 -27.044 2.862   1.00 22.65 ? 68   GLU A C     1 
ATOM   518  O  O     . GLU A 1 68  ? -33.830 -28.252 2.618   1.00 24.50 ? 68   GLU A O     1 
ATOM   519  C  CB    . GLU A 1 68  ? -35.935 -25.694 2.306   1.00 29.55 ? 68   GLU A CB    1 
ATOM   520  C  CG    . GLU A 1 68  ? -37.308 -25.168 2.727   1.00 37.06 ? 68   GLU A CG    1 
ATOM   521  C  CD    . GLU A 1 68  ? -38.031 -24.349 1.651   1.00 48.48 ? 68   GLU A CD    1 
ATOM   522  O  OE1   . GLU A 1 68  ? -37.641 -23.165 1.422   1.00 53.31 ? 68   GLU A OE1   1 
ATOM   523  O  OE2   . GLU A 1 68  ? -38.965 -24.899 0.997   1.00 51.97 ? 68   GLU A OE2   1 
ATOM   524  N  N     . ILE A 1 69  ? -32.846 -26.226 2.691   1.00 20.46 ? 69   ILE A N     1 
ATOM   525  C  CA    . ILE A 1 69  ? -31.533 -26.684 2.160   1.00 20.33 ? 69   ILE A CA    1 
ATOM   526  C  C     . ILE A 1 69  ? -31.012 -27.796 3.069   1.00 22.14 ? 69   ILE A C     1 
ATOM   527  O  O     . ILE A 1 69  ? -30.606 -28.855 2.535   1.00 22.52 ? 69   ILE A O     1 
ATOM   528  C  CB    . ILE A 1 69  ? -30.560 -25.503 2.006   1.00 19.77 ? 69   ILE A CB    1 
ATOM   529  C  CG1   . ILE A 1 69  ? -31.003 -24.580 0.861   1.00 19.97 ? 69   ILE A CG1   1 
ATOM   530  C  CG2   . ILE A 1 69  ? -29.146 -26.005 1.788   1.00 20.74 ? 69   ILE A CG2   1 
ATOM   531  C  CD1   . ILE A 1 69  ? -30.384 -23.199 0.911   1.00 20.59 ? 69   ILE A CD1   1 
ATOM   532  N  N     . VAL A 1 70  ? -31.058 -27.570 4.389   1.00 23.33 ? 70   VAL A N     1 
ATOM   533  C  CA    . VAL A 1 70  ? -30.503 -28.502 5.402   1.00 23.05 ? 70   VAL A CA    1 
ATOM   534  C  C     . VAL A 1 70  ? -31.250 -29.841 5.271   1.00 24.78 ? 70   VAL A C     1 
ATOM   535  O  O     . VAL A 1 70  ? -30.598 -30.909 5.371   1.00 26.58 ? 70   VAL A O     1 
ATOM   536  C  CB    . VAL A 1 70  ? -30.594 -27.902 6.817   1.00 22.83 ? 70   VAL A CB    1 
ATOM   537  C  CG1   . VAL A 1 70  ? -30.416 -28.967 7.893   1.00 22.39 ? 70   VAL A CG1   1 
ATOM   538  C  CG2   . VAL A 1 70  ? -29.593 -26.757 7.007   1.00 23.65 ? 70   VAL A CG2   1 
ATOM   539  N  N     . ARG A 1 71  ? -32.568 -29.802 5.088   1.00 24.75 ? 71   ARG A N     1 
ATOM   540  C  CA    . ARG A 1 71  ? -33.400 -31.030 4.957   1.00 24.18 ? 71   ARG A CA    1 
ATOM   541  C  C     . ARG A 1 71  ? -33.000 -31.788 3.687   1.00 20.51 ? 71   ARG A C     1 
ATOM   542  O  O     . ARG A 1 71  ? -32.883 -32.972 3.775   1.00 21.28 ? 71   ARG A O     1 
ATOM   543  C  CB    . ARG A 1 71  ? -34.876 -30.670 4.916   1.00 25.90 ? 71   ARG A CB    1 
ATOM   544  C  CG    . ARG A 1 71  ? -35.420 -30.209 6.250   1.00 30.19 ? 71   ARG A CG    1 
ATOM   545  C  CD    . ARG A 1 71  ? -36.901 -29.876 6.161   1.00 34.10 ? 71   ARG A CD    1 
ATOM   546  N  NE    . ARG A 1 71  ? -37.283 -29.179 7.385   1.00 37.09 ? 71   ARG A NE    1 
ATOM   547  C  CZ    . ARG A 1 71  ? -37.811 -27.963 7.444   1.00 37.50 ? 71   ARG A CZ    1 
ATOM   548  N  NH1   . ARG A 1 71  ? -38.066 -27.300 6.328   1.00 35.42 ? 71   ARG A NH1   1 
ATOM   549  N  NH2   . ARG A 1 71  ? -38.098 -27.429 8.626   1.00 37.69 ? 71   ARG A NH2   1 
ATOM   550  N  N     . VAL A 1 72  ? -32.804 -31.112 2.552   1.00 20.53 ? 72   VAL A N     1 
ATOM   551  C  CA    . VAL A 1 72  ? -32.327 -31.748 1.283   1.00 20.92 ? 72   VAL A CA    1 
ATOM   552  C  C     . VAL A 1 72  ? -30.917 -32.351 1.491   1.00 21.79 ? 72   VAL A C     1 
ATOM   553  O  O     . VAL A 1 72  ? -30.652 -33.454 0.981   1.00 21.38 ? 72   VAL A O     1 
ATOM   554  C  CB    . VAL A 1 72  ? -32.408 -30.741 0.118   1.00 21.54 ? 72   VAL A CB    1 
ATOM   555  C  CG1   . VAL A 1 72  ? -31.719 -31.246 -1.125  1.00 21.80 ? 72   VAL A CG1   1 
ATOM   556  C  CG2   . VAL A 1 72  ? -33.851 -30.346 -0.195  1.00 22.25 ? 72   VAL A CG2   1 
ATOM   557  N  N     . ALA A 1 73  ? -30.039 -31.706 2.266   1.00 21.64 ? 73   ALA A N     1 
ATOM   558  C  CA    . ALA A 1 73  ? -28.663 -32.193 2.514   1.00 21.63 ? 73   ALA A CA    1 
ATOM   559  C  C     . ALA A 1 73  ? -28.753 -33.529 3.246   1.00 22.12 ? 73   ALA A C     1 
ATOM   560  O  O     . ALA A 1 73  ? -28.053 -34.473 2.835   1.00 23.81 ? 73   ALA A O     1 
ATOM   561  C  CB    . ALA A 1 73  ? -27.856 -31.165 3.293   1.00 22.70 ? 73   ALA A CB    1 
ATOM   562  N  N     . ASN A 1 74  ? -29.624 -33.608 4.255   1.00 19.71 ? 74   ASN A N     1 
ATOM   563  C  CA    . ASN A 1 74  ? -29.905 -34.865 4.983   1.00 20.61 ? 74   ASN A CA    1 
ATOM   564  C  C     . ASN A 1 74  ? -30.482 -35.902 4.016   1.00 22.09 ? 74   ASN A C     1 
ATOM   565  O  O     . ASN A 1 74  ? -30.028 -37.028 4.058   1.00 19.52 ? 74   ASN A O     1 
ATOM   566  C  CB    . ASN A 1 74  ? -30.867 -34.676 6.151   1.00 20.33 ? 74   ASN A CB    1 
ATOM   567  C  CG    . ASN A 1 74  ? -30.170 -34.130 7.379   1.00 21.69 ? 74   ASN A CG    1 
ATOM   568  O  OD1   . ASN A 1 74  ? -29.474 -34.858 8.068   1.00 17.81 ? 74   ASN A OD1   1 
ATOM   569  N  ND2   . ASN A 1 74  ? -30.323 -32.837 7.621   1.00 20.61 ? 74   ASN A ND2   1 
ATOM   570  N  N     . GLU A 1 75  ? -31.455 -35.539 3.183   1.00 24.00 ? 75   GLU A N     1 
ATOM   571  C  CA    . GLU A 1 75  ? -32.063 -36.512 2.230   1.00 27.07 ? 75   GLU A CA    1 
ATOM   572  C  C     . GLU A 1 75  ? -30.963 -37.178 1.378   1.00 25.69 ? 75   GLU A C     1 
ATOM   573  O  O     . GLU A 1 75  ? -31.026 -38.392 1.238   1.00 23.88 ? 75   GLU A O     1 
ATOM   574  C  CB    . GLU A 1 75  ? -33.140 -35.810 1.409   1.00 29.50 ? 75   GLU A CB    1 
ATOM   575  C  CG    . GLU A 1 75  ? -33.937 -36.750 0.551   1.00 32.45 ? 75   GLU A CG    1 
ATOM   576  C  CD    . GLU A 1 75  ? -35.084 -36.100 -0.207  1.00 34.00 ? 75   GLU A CD    1 
ATOM   577  O  OE1   . GLU A 1 75  ? -35.531 -36.740 -1.198  1.00 38.05 ? 75   GLU A OE1   1 
ATOM   578  O  OE2   . GLU A 1 75  ? -35.542 -34.971 0.195   1.00 32.62 ? 75   GLU A OE2   1 
ATOM   579  N  N     . PHE A 1 76  ? -29.967 -36.437 0.863   1.00 24.85 ? 76   PHE A N     1 
ATOM   580  C  CA    . PHE A 1 76  ? -28.969 -36.978 -0.106  1.00 24.53 ? 76   PHE A CA    1 
ATOM   581  C  C     . PHE A 1 76  ? -27.593 -37.257 0.514   1.00 24.80 ? 76   PHE A C     1 
ATOM   582  O  O     . PHE A 1 76  ? -26.726 -37.671 -0.257  1.00 23.62 ? 76   PHE A O     1 
ATOM   583  C  CB    . PHE A 1 76  ? -28.834 -36.049 -1.320  1.00 27.16 ? 76   PHE A CB    1 
ATOM   584  C  CG    . PHE A 1 76  ? -30.078 -35.985 -2.169  1.00 26.62 ? 76   PHE A CG    1 
ATOM   585  C  CD1   . PHE A 1 76  ? -30.389 -37.030 -3.024  1.00 29.06 ? 76   PHE A CD1   1 
ATOM   586  C  CD2   . PHE A 1 76  ? -31.008 -34.975 -2.001  1.00 25.87 ? 76   PHE A CD2   1 
ATOM   587  C  CE1   . PHE A 1 76  ? -31.562 -37.009 -3.757  1.00 28.90 ? 76   PHE A CE1   1 
ATOM   588  C  CE2   . PHE A 1 76  ? -32.180 -34.957 -2.739  1.00 27.48 ? 76   PHE A CE2   1 
ATOM   589  C  CZ    . PHE A 1 76  ? -32.448 -35.973 -3.619  1.00 27.32 ? 76   PHE A CZ    1 
ATOM   590  N  N     . GLY A 1 77  ? -27.375 -37.028 1.820   1.00 25.03 ? 77   GLY A N     1 
ATOM   591  C  CA    . GLY A 1 77  ? -26.041 -37.157 2.450   1.00 22.35 ? 77   GLY A CA    1 
ATOM   592  C  C     . GLY A 1 77  ? -25.066 -36.142 1.880   1.00 22.81 ? 77   GLY A C     1 
ATOM   593  O  O     . GLY A 1 77  ? -23.879 -36.426 1.826   1.00 23.12 ? 77   GLY A O     1 
ATOM   594  N  N     . VAL A 1 78  ? -25.542 -35.014 1.370   1.00 20.96 ? 78   VAL A N     1 
ATOM   595  C  CA    . VAL A 1 78  ? -24.641 -34.021 0.741   1.00 21.91 ? 78   VAL A CA    1 
ATOM   596  C  C     . VAL A 1 78  ? -24.249 -33.018 1.816   1.00 22.90 ? 78   VAL A C     1 
ATOM   597  O  O     . VAL A 1 78  ? -25.098 -32.288 2.333   1.00 23.72 ? 78   VAL A O     1 
ATOM   598  C  CB    . VAL A 1 78  ? -25.271 -33.342 -0.482  1.00 22.91 ? 78   VAL A CB    1 
ATOM   599  C  CG1   . VAL A 1 78  ? -24.463 -32.125 -0.887  1.00 25.57 ? 78   VAL A CG1   1 
ATOM   600  C  CG2   . VAL A 1 78  ? -25.433 -34.313 -1.650  1.00 25.01 ? 78   VAL A CG2   1 
ATOM   601  N  N     . PRO A 1 79  ? -22.950 -32.964 2.185   1.00 23.59 ? 79   PRO A N     1 
ATOM   602  C  CA    . PRO A 1 79  ? -22.492 -32.097 3.274   1.00 22.45 ? 79   PRO A CA    1 
ATOM   603  C  C     . PRO A 1 79  ? -22.388 -30.625 2.840   1.00 20.06 ? 79   PRO A C     1 
ATOM   604  O  O     . PRO A 1 79  ? -22.130 -30.379 1.685   1.00 18.56 ? 79   PRO A O     1 
ATOM   605  C  CB    . PRO A 1 79  ? -21.119 -32.686 3.646   1.00 22.64 ? 79   PRO A CB    1 
ATOM   606  C  CG    . PRO A 1 79  ? -20.616 -33.337 2.362   1.00 25.19 ? 79   PRO A CG    1 
ATOM   607  C  CD    . PRO A 1 79  ? -21.842 -33.695 1.538   1.00 24.06 ? 79   PRO A CD    1 
ATOM   608  N  N     . LEU A 1 80  ? -22.573 -29.710 3.806   1.00 19.83 ? 80   LEU A N     1 
ATOM   609  C  CA    . LEU A 1 80  ? -22.659 -28.232 3.634   1.00 19.77 ? 80   LEU A CA    1 
ATOM   610  C  C     . LEU A 1 80  ? -21.546 -27.562 4.452   1.00 20.41 ? 80   LEU A C     1 
ATOM   611  O  O     . LEU A 1 80  ? -21.281 -28.009 5.540   1.00 21.17 ? 80   LEU A O     1 
ATOM   612  C  CB    . LEU A 1 80  ? -24.014 -27.735 4.138   1.00 20.18 ? 80   LEU A CB    1 
ATOM   613  C  CG    . LEU A 1 80  ? -25.272 -28.308 3.473   1.00 20.52 ? 80   LEU A CG    1 
ATOM   614  C  CD1   . LEU A 1 80  ? -26.511 -27.905 4.271   1.00 19.77 ? 80   LEU A CD1   1 
ATOM   615  C  CD2   . LEU A 1 80  ? -25.412 -27.854 2.023   1.00 20.47 ? 80   LEU A CD2   1 
ATOM   616  N  N     . TRP A 1 81  ? -20.931 -26.520 3.924   1.00 19.43 ? 81   TRP A N     1 
ATOM   617  C  CA    . TRP A 1 81  ? -19.991 -25.631 4.641   1.00 17.94 ? 81   TRP A CA    1 
ATOM   618  C  C     . TRP A 1 81  ? -20.665 -24.269 4.807   1.00 17.41 ? 81   TRP A C     1 
ATOM   619  O  O     . TRP A 1 81  ? -20.722 -23.466 3.873   1.00 17.61 ? 81   TRP A O     1 
ATOM   620  C  CB    . TRP A 1 81  ? -18.662 -25.543 3.882   1.00 19.00 ? 81   TRP A CB    1 
ATOM   621  C  CG    . TRP A 1 81  ? -17.563 -24.944 4.699   1.00 20.03 ? 81   TRP A CG    1 
ATOM   622  C  CD1   . TRP A 1 81  ? -17.185 -23.630 4.728   1.00 22.03 ? 81   TRP A CD1   1 
ATOM   623  C  CD2   . TRP A 1 81  ? -16.703 -25.624 5.621   1.00 19.21 ? 81   TRP A CD2   1 
ATOM   624  N  NE1   . TRP A 1 81  ? -16.138 -23.445 5.590   1.00 19.89 ? 81   TRP A NE1   1 
ATOM   625  C  CE2   . TRP A 1 81  ? -15.826 -24.655 6.159   1.00 21.13 ? 81   TRP A CE2   1 
ATOM   626  C  CE3   . TRP A 1 81  ? -16.552 -26.952 6.003   1.00 19.41 ? 81   TRP A CE3   1 
ATOM   627  C  CZ2   . TRP A 1 81  ? -14.842 -24.978 7.094   1.00 20.63 ? 81   TRP A CZ2   1 
ATOM   628  C  CZ3   . TRP A 1 81  ? -15.576 -27.268 6.922   1.00 20.80 ? 81   TRP A CZ3   1 
ATOM   629  C  CH2   . TRP A 1 81  ? -14.728 -26.299 7.457   1.00 20.50 ? 81   TRP A CH2   1 
ATOM   630  N  N     . PRO A 1 82  ? -21.264 -23.979 5.984   1.00 15.92 ? 82   PRO A N     1 
ATOM   631  C  CA    . PRO A 1 82  ? -21.887 -22.682 6.211   1.00 17.17 ? 82   PRO A CA    1 
ATOM   632  C  C     . PRO A 1 82  ? -20.874 -21.541 6.343   1.00 18.55 ? 82   PRO A C     1 
ATOM   633  O  O     . PRO A 1 82  ? -19.911 -21.655 7.090   1.00 17.60 ? 82   PRO A O     1 
ATOM   634  C  CB    . PRO A 1 82  ? -22.635 -22.864 7.531   1.00 16.69 ? 82   PRO A CB    1 
ATOM   635  C  CG    . PRO A 1 82  ? -22.740 -24.350 7.642   1.00 17.04 ? 82   PRO A CG    1 
ATOM   636  C  CD    . PRO A 1 82  ? -21.444 -24.892 7.113   1.00 16.06 ? 82   PRO A CD    1 
ATOM   637  N  N     . VAL A 1 83  ? -21.103 -20.473 5.588   1.00 18.40 ? 83   VAL A N     1 
ATOM   638  C  CA    . VAL A 1 83  ? -20.316 -19.212 5.714   1.00 20.28 ? 83   VAL A CA    1 
ATOM   639  C  C     . VAL A 1 83  ? -21.310 -18.058 5.776   1.00 20.15 ? 83   VAL A C     1 
ATOM   640  O  O     . VAL A 1 83  ? -22.402 -18.201 5.178   1.00 19.75 ? 83   VAL A O     1 
ATOM   641  C  CB    . VAL A 1 83  ? -19.277 -19.057 4.588   1.00 18.93 ? 83   VAL A CB    1 
ATOM   642  C  CG1   . VAL A 1 83  ? -18.417 -20.311 4.472   1.00 20.14 ? 83   VAL A CG1   1 
ATOM   643  C  CG2   . VAL A 1 83  ? -19.916 -18.674 3.273   1.00 20.62 ? 83   VAL A CG2   1 
ATOM   644  N  N     . SER A 1 84  ? -20.978 -17.031 6.558   1.00 19.26 ? 84   SER A N     1 
ATOM   645  C  CA    . SER A 1 84  ? -21.821 -15.821 6.740   1.00 18.67 ? 84   SER A CA    1 
ATOM   646  C  C     . SER A 1 84  ? -21.563 -14.913 5.551   1.00 18.40 ? 84   SER A C     1 
ATOM   647  O  O     . SER A 1 84  ? -22.522 -14.637 4.812   1.00 20.50 ? 84   SER A O     1 
ATOM   648  C  CB    . SER A 1 84  ? -21.542 -15.113 8.029   1.00 17.71 ? 84   SER A CB    1 
ATOM   649  O  OG    . SER A 1 84  ? -21.983 -15.876 9.128   1.00 17.89 ? 84   SER A OG    1 
ATOM   650  N  N     . ARG A 1 85  ? -20.325 -14.461 5.378   1.00 17.56 ? 85   ARG A N     1 
ATOM   651  C  CA    . ARG A 1 85  ? -19.904 -13.787 4.127   1.00 18.94 ? 85   ARG A CA    1 
ATOM   652  C  C     . ARG A 1 85  ? -18.779 -14.554 3.396   1.00 20.31 ? 85   ARG A C     1 
ATOM   653  O  O     . ARG A 1 85  ? -18.558 -14.225 2.225   1.00 20.38 ? 85   ARG A O     1 
ATOM   654  C  CB    . ARG A 1 85  ? -19.554 -12.334 4.455   1.00 21.16 ? 85   ARG A CB    1 
ATOM   655  C  CG    . ARG A 1 85  ? -20.780 -11.470 4.734   1.00 20.19 ? 85   ARG A CG    1 
ATOM   656  C  CD    . ARG A 1 85  ? -20.372 -10.071 5.143   1.00 21.75 ? 85   ARG A CD    1 
ATOM   657  N  NE    . ARG A 1 85  ? -19.618 -9.417  4.082   1.00 23.22 ? 85   ARG A NE    1 
ATOM   658  C  CZ    . ARG A 1 85  ? -20.141 -8.852  2.996   1.00 24.49 ? 85   ARG A CZ    1 
ATOM   659  N  NH1   . ARG A 1 85  ? -21.443 -8.825  2.813   1.00 25.24 ? 85   ARG A NH1   1 
ATOM   660  N  NH2   . ARG A 1 85  ? -19.357 -8.296  2.098   1.00 26.24 ? 85   ARG A NH2   1 
ATOM   661  N  N     . GLY A 1 86  ? -18.046 -15.470 4.046   1.00 19.37 ? 86   GLY A N     1 
ATOM   662  C  CA    . GLY A 1 86  ? -17.023 -16.304 3.389   1.00 20.61 ? 86   GLY A CA    1 
ATOM   663  C  C     . GLY A 1 86  ? -15.773 -15.534 3.056   1.00 19.73 ? 86   GLY A C     1 
ATOM   664  O  O     . GLY A 1 86  ? -15.037 -15.919 2.118   1.00 20.30 ? 86   GLY A O     1 
ATOM   665  N  N     . LYS A 1 87  ? -15.489 -14.502 3.832   1.00 21.67 ? 87   LYS A N     1 
ATOM   666  C  CA    . LYS A 1 87  ? -14.254 -13.690 3.647   1.00 20.93 ? 87   LYS A CA    1 
ATOM   667  C  C     . LYS A 1 87  ? -13.160 -14.124 4.618   1.00 17.86 ? 87   LYS A C     1 
ATOM   668  O  O     . LYS A 1 87  ? -12.315 -13.289 4.912   1.00 17.95 ? 87   LYS A O     1 
ATOM   669  C  CB    . LYS A 1 87  ? -14.575 -12.212 3.849   1.00 23.38 ? 87   LYS A CB    1 
ATOM   670  C  CG    . LYS A 1 87  ? -15.724 -11.704 3.006   1.00 24.73 ? 87   LYS A CG    1 
ATOM   671  C  CD    . LYS A 1 87  ? -15.409 -11.727 1.554   1.00 27.44 ? 87   LYS A CD    1 
ATOM   672  C  CE    . LYS A 1 87  ? -16.329 -10.815 0.773   1.00 32.73 ? 87   LYS A CE    1 
ATOM   673  N  NZ    . LYS A 1 87  ? -16.655 -11.370 -0.556  1.00 32.81 ? 87   LYS A NZ    1 
ATOM   674  N  N     . ASN A 1 88  ? -13.153 -15.385 5.054   1.00 18.01 ? 88   ASN A N     1 
ATOM   675  C  CA    . ASN A 1 88  ? -12.183 -15.919 6.052   1.00 18.61 ? 88   ASN A CA    1 
ATOM   676  C  C     . ASN A 1 88  ? -10.805 -16.124 5.381   1.00 18.52 ? 88   ASN A C     1 
ATOM   677  O  O     . ASN A 1 88  ? -10.195 -17.194 5.546   1.00 17.40 ? 88   ASN A O     1 
ATOM   678  C  CB    . ASN A 1 88  ? -12.720 -17.184 6.741   1.00 18.13 ? 88   ASN A CB    1 
ATOM   679  C  CG    . ASN A 1 88  ? -12.229 -17.348 8.168   1.00 17.82 ? 88   ASN A CG    1 
ATOM   680  O  OD1   . ASN A 1 88  ? -11.758 -16.397 8.799   1.00 15.05 ? 88   ASN A OD1   1 
ATOM   681  N  ND2   . ASN A 1 88  ? -12.373 -18.554 8.699   1.00 17.66 ? 88   ASN A ND2   1 
ATOM   682  N  N     . PHE A 1 89  ? -10.313 -15.105 4.677   1.00 19.04 ? 89   PHE A N     1 
ATOM   683  C  CA    . PHE A 1 89  ? -8.970  -15.085 4.044   1.00 18.79 ? 89   PHE A CA    1 
ATOM   684  C  C     . PHE A 1 89  ? -7.908  -15.092 5.159   1.00 17.85 ? 89   PHE A C     1 
ATOM   685  O  O     . PHE A 1 89  ? -8.100  -14.369 6.176   1.00 17.29 ? 89   PHE A O     1 
ATOM   686  C  CB    . PHE A 1 89  ? -8.874  -13.911 3.065   1.00 21.15 ? 89   PHE A CB    1 
ATOM   687  C  CG    . PHE A 1 89  ? -10.010 -13.826 2.075   1.00 24.06 ? 89   PHE A CG    1 
ATOM   688  C  CD1   . PHE A 1 89  ? -10.632 -14.966 1.588   1.00 28.17 ? 89   PHE A CD1   1 
ATOM   689  C  CD2   . PHE A 1 89  ? -10.461 -12.606 1.614   1.00 28.19 ? 89   PHE A CD2   1 
ATOM   690  C  CE1   . PHE A 1 89  ? -11.673 -14.888 0.671   1.00 30.07 ? 89   PHE A CE1   1 
ATOM   691  C  CE2   . PHE A 1 89  ? -11.511 -12.531 0.706   1.00 30.28 ? 89   PHE A CE2   1 
ATOM   692  C  CZ    . PHE A 1 89  ? -12.119 -13.669 0.244   1.00 27.54 ? 89   PHE A CZ    1 
ATOM   693  N  N     . ALA A 1 90  ? -6.874  -15.930 4.962   1.00 16.31 ? 90   ALA A N     1 
ATOM   694  C  CA    . ALA A 1 90  ? -5.839  -16.395 5.917   1.00 16.82 ? 90   ALA A CA    1 
ATOM   695  C  C     . ALA A 1 90  ? -6.250  -17.716 6.575   1.00 16.98 ? 90   ALA A C     1 
ATOM   696  O  O     . ALA A 1 90  ? -5.361  -18.341 7.171   1.00 18.20 ? 90   ALA A O     1 
ATOM   697  C  CB    . ALA A 1 90  ? -5.497  -15.369 6.961   1.00 17.41 ? 90   ALA A CB    1 
ATOM   698  N  N     . TYR A 1 91  ? -7.513  -18.136 6.447   1.00 16.55 ? 91   TYR A N     1 
ATOM   699  C  CA    . TYR A 1 91  ? -8.051  -19.364 7.088   1.00 17.08 ? 91   TYR A CA    1 
ATOM   700  C  C     . TYR A 1 91  ? -8.710  -20.308 6.072   1.00 16.27 ? 91   TYR A C     1 
ATOM   701  O  O     . TYR A 1 91  ? -9.291  -21.308 6.522   1.00 15.28 ? 91   TYR A O     1 
ATOM   702  C  CB    . TYR A 1 91  ? -9.018  -18.957 8.204   1.00 18.88 ? 91   TYR A CB    1 
ATOM   703  C  CG    . TYR A 1 91  ? -8.353  -18.248 9.358   1.00 21.24 ? 91   TYR A CG    1 
ATOM   704  C  CD1   . TYR A 1 91  ? -7.570  -18.934 10.267  1.00 22.83 ? 91   TYR A CD1   1 
ATOM   705  C  CD2   . TYR A 1 91  ? -8.444  -16.880 9.508   1.00 20.37 ? 91   TYR A CD2   1 
ATOM   706  C  CE1   . TYR A 1 91  ? -6.945  -18.279 11.318  1.00 23.04 ? 91   TYR A CE1   1 
ATOM   707  C  CE2   . TYR A 1 91  ? -7.819  -16.209 10.543  1.00 20.28 ? 91   TYR A CE2   1 
ATOM   708  C  CZ    . TYR A 1 91  ? -7.075  -16.911 11.460  1.00 21.13 ? 91   TYR A CZ    1 
ATOM   709  O  OH    . TYR A 1 91  ? -6.452  -16.257 12.472  1.00 21.21 ? 91   TYR A OH    1 
ATOM   710  N  N     . GLY A 1 92  ? -8.652  -19.993 4.772   1.00 17.45 ? 92   GLY A N     1 
ATOM   711  C  CA    . GLY A 1 92  ? -9.248  -20.825 3.706   1.00 18.27 ? 92   GLY A CA    1 
ATOM   712  C  C     . GLY A 1 92  ? -10.286 -20.098 2.864   1.00 18.90 ? 92   GLY A C     1 
ATOM   713  O  O     . GLY A 1 92  ? -10.743 -20.708 1.885   1.00 21.57 ? 92   GLY A O     1 
ATOM   714  N  N     . GLY A 1 93  ? -10.618 -18.835 3.174   1.00 19.13 ? 93   GLY A N     1 
ATOM   715  C  CA    . GLY A 1 93  ? -11.763 -18.118 2.572   1.00 17.85 ? 93   GLY A CA    1 
ATOM   716  C  C     . GLY A 1 93  ? -13.046 -18.904 2.796   1.00 18.39 ? 93   GLY A C     1 
ATOM   717  O  O     . GLY A 1 93  ? -13.290 -19.315 3.962   1.00 18.54 ? 93   GLY A O     1 
ATOM   718  N  N     . ALA A 1 94  ? -13.808 -19.184 1.732   1.00 16.81 ? 94   ALA A N     1 
ATOM   719  C  CA    . ALA A 1 94  ? -15.104 -19.894 1.795   1.00 18.37 ? 94   ALA A CA    1 
ATOM   720  C  C     . ALA A 1 94  ? -14.930 -21.402 1.590   1.00 18.99 ? 94   ALA A C     1 
ATOM   721  O  O     . ALA A 1 94  ? -15.971 -22.076 1.572   1.00 19.53 ? 94   ALA A O     1 
ATOM   722  C  CB    . ALA A 1 94  ? -16.085 -19.355 0.787   1.00 19.73 ? 94   ALA A CB    1 
ATOM   723  N  N     . ALA A 1 95  ? -13.692 -21.892 1.478   1.00 18.27 ? 95   ALA A N     1 
ATOM   724  C  CA    . ALA A 1 95  ? -13.400 -23.281 1.085   1.00 18.19 ? 95   ALA A CA    1 
ATOM   725  C  C     . ALA A 1 95  ? -13.568 -24.219 2.275   1.00 17.78 ? 95   ALA A C     1 
ATOM   726  O  O     . ALA A 1 95  ? -13.185 -23.900 3.400   1.00 16.69 ? 95   ALA A O     1 
ATOM   727  C  CB    . ALA A 1 95  ? -12.022 -23.391 0.492   1.00 18.63 ? 95   ALA A CB    1 
ATOM   728  N  N     . PRO A 1 96  ? -14.093 -25.441 2.025   1.00 18.25 ? 96   PRO A N     1 
ATOM   729  C  CA    . PRO A 1 96  ? -14.257 -26.449 3.059   1.00 17.82 ? 96   PRO A CA    1 
ATOM   730  C  C     . PRO A 1 96  ? -13.004 -27.289 3.300   1.00 18.85 ? 96   PRO A C     1 
ATOM   731  O  O     . PRO A 1 96  ? -12.142 -27.357 2.447   1.00 20.60 ? 96   PRO A O     1 
ATOM   732  C  CB    . PRO A 1 96  ? -15.310 -27.372 2.461   1.00 19.04 ? 96   PRO A CB    1 
ATOM   733  C  CG    . PRO A 1 96  ? -14.940 -27.368 0.969   1.00 19.78 ? 96   PRO A CG    1 
ATOM   734  C  CD    . PRO A 1 96  ? -14.526 -25.932 0.700   1.00 19.44 ? 96   PRO A CD    1 
ATOM   735  N  N     . VAL A 1 97  ? -12.980 -27.969 4.434   1.00 17.95 ? 97   VAL A N     1 
ATOM   736  C  CA    . VAL A 1 97  ? -11.902 -28.910 4.787   1.00 18.51 ? 97   VAL A CA    1 
ATOM   737  C  C     . VAL A 1 97  ? -11.961 -30.038 3.775   1.00 19.53 ? 97   VAL A C     1 
ATOM   738  O  O     . VAL A 1 97  ? -10.899 -30.351 3.227   1.00 20.51 ? 97   VAL A O     1 
ATOM   739  C  CB    . VAL A 1 97  ? -12.014 -29.453 6.220   1.00 19.40 ? 97   VAL A CB    1 
ATOM   740  C  CG1   . VAL A 1 97  ? -11.038 -30.604 6.415   1.00 19.80 ? 97   VAL A CG1   1 
ATOM   741  C  CG2   . VAL A 1 97  ? -11.788 -28.373 7.275   1.00 19.32 ? 97   VAL A CG2   1 
ATOM   742  N  N     . MET A 1 98  ? -13.145 -30.621 3.591   1.00 19.95 ? 98   MET A N     1 
ATOM   743  C  CA    . MET A 1 98  ? -13.344 -31.851 2.782   1.00 21.03 ? 98   MET A CA    1 
ATOM   744  C  C     . MET A 1 98  ? -13.830 -31.523 1.363   1.00 21.80 ? 98   MET A C     1 
ATOM   745  O  O     . MET A 1 98  ? -14.944 -30.974 1.213   1.00 23.17 ? 98   MET A O     1 
ATOM   746  C  CB    . MET A 1 98  ? -14.381 -32.753 3.441   1.00 21.41 ? 98   MET A CB    1 
ATOM   747  C  CG    . MET A 1 98  ? -14.349 -34.150 2.853   1.00 21.76 ? 98   MET A CG    1 
ATOM   748  S  SD    . MET A 1 98  ? -15.661 -35.172 3.454   1.00 24.39 ? 98   MET A SD    1 
ATOM   749  C  CE    . MET A 1 98  ? -17.104 -34.406 2.722   1.00 22.91 ? 98   MET A CE    1 
ATOM   750  N  N     . SER A 1 99  ? -13.044 -31.860 0.347   1.00 22.20 ? 99   SER A N     1 
ATOM   751  C  CA    . SER A 1 99  ? -13.433 -31.703 -1.082  1.00 21.94 ? 99   SER A CA    1 
ATOM   752  C  C     . SER A 1 99  ? -14.812 -32.330 -1.324  1.00 22.14 ? 99   SER A C     1 
ATOM   753  O  O     . SER A 1 99  ? -15.130 -33.379 -0.734  1.00 21.04 ? 99   SER A O     1 
ATOM   754  C  CB    . SER A 1 99  ? -12.382 -32.267 -2.007  1.00 21.34 ? 99   SER A CB    1 
ATOM   755  O  OG    . SER A 1 99  ? -11.222 -31.447 -1.996  1.00 22.47 ? 99   SER A OG    1 
ATOM   756  N  N     . GLY A 1 100 ? -15.620 -31.675 -2.145  1.00 22.68 ? 100  GLY A N     1 
ATOM   757  C  CA    . GLY A 1 100 ? -16.971 -32.151 -2.493  1.00 23.83 ? 100  GLY A CA    1 
ATOM   758  C  C     . GLY A 1 100 ? -18.039 -31.531 -1.610  1.00 24.83 ? 100  GLY A C     1 
ATOM   759  O  O     . GLY A 1 100 ? -19.215 -31.712 -1.923  1.00 25.90 ? 100  GLY A O     1 
ATOM   760  N  N     . THR A 1 101 ? -17.659 -30.892 -0.499  1.00 22.12 ? 101  THR A N     1 
ATOM   761  C  CA    . THR A 1 101 ? -18.611 -30.164 0.373   1.00 19.67 ? 101  THR A CA    1 
ATOM   762  C  C     . THR A 1 101 ? -19.206 -29.023 -0.458  1.00 18.80 ? 101  THR A C     1 
ATOM   763  O  O     . THR A 1 101 ? -18.495 -28.452 -1.285  1.00 18.61 ? 101  THR A O     1 
ATOM   764  C  CB    . THR A 1 101 ? -17.969 -29.675 1.679   1.00 18.89 ? 101  THR A CB    1 
ATOM   765  O  OG1   . THR A 1 101 ? -17.386 -30.780 2.377   1.00 16.91 ? 101  THR A OG1   1 
ATOM   766  C  CG2   . THR A 1 101 ? -18.989 -29.020 2.593   1.00 19.22 ? 101  THR A CG2   1 
ATOM   767  N  N     . VAL A 1 102 ? -20.496 -28.785 -0.285  1.00 18.48 ? 102  VAL A N     1 
ATOM   768  C  CA    . VAL A 1 102 ? -21.232 -27.654 -0.897  1.00 18.99 ? 102  VAL A CA    1 
ATOM   769  C  C     . VAL A 1 102 ? -21.263 -26.468 0.081   1.00 17.99 ? 102  VAL A C     1 
ATOM   770  O  O     . VAL A 1 102 ? -21.755 -26.650 1.213   1.00 19.77 ? 102  VAL A O     1 
ATOM   771  C  CB    . VAL A 1 102 ? -22.641 -28.105 -1.295  1.00 19.44 ? 102  VAL A CB    1 
ATOM   772  C  CG1   . VAL A 1 102 ? -23.503 -26.910 -1.685  1.00 20.47 ? 102  VAL A CG1   1 
ATOM   773  C  CG2   . VAL A 1 102 ? -22.565 -29.133 -2.417  1.00 20.72 ? 102  VAL A CG2   1 
ATOM   774  N  N     . VAL A 1 103 ? -20.796 -25.296 -0.354  1.00 16.96 ? 103  VAL A N     1 
ATOM   775  C  CA    . VAL A 1 103 ? -20.839 -24.052 0.461   1.00 18.39 ? 103  VAL A CA    1 
ATOM   776  C  C     . VAL A 1 103 ? -22.302 -23.556 0.567   1.00 19.70 ? 103  VAL A C     1 
ATOM   777  O  O     . VAL A 1 103 ? -22.988 -23.367 -0.455  1.00 18.77 ? 103  VAL A O     1 
ATOM   778  C  CB    . VAL A 1 103 ? -19.920 -22.962 -0.116  1.00 18.16 ? 103  VAL A CB    1 
ATOM   779  C  CG1   . VAL A 1 103 ? -20.022 -21.683 0.711   1.00 18.31 ? 103  VAL A CG1   1 
ATOM   780  C  CG2   . VAL A 1 103 ? -18.473 -23.444 -0.218  1.00 19.38 ? 103  VAL A CG2   1 
ATOM   781  N  N     . LEU A 1 104 ? -22.752 -23.328 1.793   1.00 19.56 ? 104  LEU A N     1 
ATOM   782  C  CA    . LEU A 1 104 ? -23.985 -22.597 2.129   1.00 18.51 ? 104  LEU A CA    1 
ATOM   783  C  C     . LEU A 1 104 ? -23.579 -21.156 2.462   1.00 20.13 ? 104  LEU A C     1 
ATOM   784  O  O     . LEU A 1 104 ? -23.067 -20.910 3.553   1.00 19.30 ? 104  LEU A O     1 
ATOM   785  C  CB    . LEU A 1 104 ? -24.640 -23.317 3.300   1.00 19.43 ? 104  LEU A CB    1 
ATOM   786  C  CG    . LEU A 1 104 ? -25.874 -22.634 3.867   1.00 22.49 ? 104  LEU A CG    1 
ATOM   787  C  CD1   . LEU A 1 104 ? -26.977 -22.608 2.846   1.00 22.66 ? 104  LEU A CD1   1 
ATOM   788  C  CD2   . LEU A 1 104 ? -26.316 -23.330 5.138   1.00 23.74 ? 104  LEU A CD2   1 
ATOM   789  N  N     . ASP A 1 105 ? -23.747 -20.267 1.493   1.00 20.66 ? 105  ASP A N     1 
ATOM   790  C  CA    . ASP A 1 105 ? -23.320 -18.859 1.535   1.00 21.03 ? 105  ASP A CA    1 
ATOM   791  C  C     . ASP A 1 105 ? -24.516 -18.033 1.976   1.00 21.92 ? 105  ASP A C     1 
ATOM   792  O  O     . ASP A 1 105 ? -25.480 -17.895 1.182   1.00 22.92 ? 105  ASP A O     1 
ATOM   793  C  CB    . ASP A 1 105 ? -22.830 -18.468 0.148   1.00 22.13 ? 105  ASP A CB    1 
ATOM   794  C  CG    . ASP A 1 105 ? -22.318 -17.048 0.068   1.00 23.03 ? 105  ASP A CG    1 
ATOM   795  O  OD1   . ASP A 1 105 ? -22.425 -16.310 1.085   1.00 21.12 ? 105  ASP A OD1   1 
ATOM   796  O  OD2   . ASP A 1 105 ? -21.803 -16.720 -1.008  1.00 24.92 ? 105  ASP A OD2   1 
ATOM   797  N  N     . MET A 1 106 ? -24.470 -17.478 3.179   1.00 21.64 ? 106  MET A N     1 
ATOM   798  C  CA    . MET A 1 106 ? -25.609 -16.685 3.692   1.00 22.53 ? 106  MET A CA    1 
ATOM   799  C  C     . MET A 1 106 ? -25.423 -15.173 3.444   1.00 22.99 ? 106  MET A C     1 
ATOM   800  O  O     . MET A 1 106 ? -26.135 -14.383 4.104   1.00 23.08 ? 106  MET A O     1 
ATOM   801  C  CB    . MET A 1 106 ? -25.825 -17.059 5.151   1.00 22.96 ? 106  MET A CB    1 
ATOM   802  C  CG    . MET A 1 106 ? -26.494 -18.435 5.211   1.00 23.14 ? 106  MET A CG    1 
ATOM   803  S  SD    . MET A 1 106 ? -26.745 -19.022 6.864   1.00 25.33 ? 106  MET A SD    1 
ATOM   804  C  CE    . MET A 1 106 ? -25.078 -19.458 7.337   1.00 25.99 ? 106  MET A CE    1 
ATOM   805  N  N     . ASN A 1 107 ? -24.610 -14.791 2.447   1.00 21.88 ? 107  ASN A N     1 
ATOM   806  C  CA    . ASN A 1 107 ? -24.354 -13.373 2.048   1.00 24.40 ? 107  ASN A CA    1 
ATOM   807  C  C     . ASN A 1 107 ? -25.655 -12.586 1.852   1.00 22.31 ? 107  ASN A C     1 
ATOM   808  O  O     . ASN A 1 107 ? -25.692 -11.423 2.238   1.00 19.74 ? 107  ASN A O     1 
ATOM   809  C  CB    . ASN A 1 107 ? -23.564 -13.267 0.734   1.00 29.89 ? 107  ASN A CB    1 
ATOM   810  C  CG    . ASN A 1 107 ? -22.112 -12.959 1.013   1.00 35.11 ? 107  ASN A CG    1 
ATOM   811  O  OD1   . ASN A 1 107 ? -21.221 -13.805 0.859   1.00 44.52 ? 107  ASN A OD1   1 
ATOM   812  N  ND2   . ASN A 1 107 ? -21.861 -11.737 1.444   1.00 42.50 ? 107  ASN A ND2   1 
ATOM   813  N  N     . ARG A 1 108 ? -26.695 -13.191 1.289   1.00 20.09 ? 108  ARG A N     1 
ATOM   814  C  CA    . ARG A 1 108 ? -27.905 -12.437 0.878   1.00 21.04 ? 108  ARG A CA    1 
ATOM   815  C  C     . ARG A 1 108 ? -28.804 -12.188 2.087   1.00 22.49 ? 108  ARG A C     1 
ATOM   816  O  O     . ARG A 1 108 ? -29.613 -11.284 1.988   1.00 21.53 ? 108  ARG A O     1 
ATOM   817  C  CB    . ARG A 1 108 ? -28.621 -13.193 -0.235  1.00 22.18 ? 108  ARG A CB    1 
ATOM   818  C  CG    . ARG A 1 108 ? -27.709 -13.395 -1.444  1.00 21.50 ? 108  ARG A CG    1 
ATOM   819  C  CD    . ARG A 1 108 ? -28.370 -14.341 -2.423  1.00 24.36 ? 108  ARG A CD    1 
ATOM   820  N  NE    . ARG A 1 108 ? -29.625 -13.783 -2.892  1.00 23.98 ? 108  ARG A NE    1 
ATOM   821  C  CZ    . ARG A 1 108 ? -30.770 -14.445 -3.085  1.00 24.89 ? 108  ARG A CZ    1 
ATOM   822  N  NH1   . ARG A 1 108 ? -30.863 -15.743 -2.857  1.00 24.95 ? 108  ARG A NH1   1 
ATOM   823  N  NH2   . ARG A 1 108 ? -31.846 -13.776 -3.483  1.00 26.27 ? 108  ARG A NH2   1 
ATOM   824  N  N     . MET A 1 109 ? -28.629 -12.930 3.186   1.00 20.67 ? 109  MET A N     1 
ATOM   825  C  CA    . MET A 1 109 ? -29.342 -12.698 4.468   1.00 20.34 ? 109  MET A CA    1 
ATOM   826  C  C     . MET A 1 109 ? -28.602 -11.587 5.195   1.00 20.78 ? 109  MET A C     1 
ATOM   827  O  O     . MET A 1 109 ? -27.809 -11.858 6.111   1.00 20.65 ? 109  MET A O     1 
ATOM   828  C  CB    . MET A 1 109 ? -29.428 -13.969 5.305   1.00 20.69 ? 109  MET A CB    1 
ATOM   829  C  CG    . MET A 1 109 ? -30.261 -15.038 4.588   1.00 21.66 ? 109  MET A CG    1 
ATOM   830  S  SD    . MET A 1 109 ? -30.058 -16.696 5.274   1.00 24.13 ? 109  MET A SD    1 
ATOM   831  C  CE    . MET A 1 109 ? -30.639 -16.347 6.937   1.00 22.97 ? 109  MET A CE    1 
ATOM   832  N  N     . ASN A 1 110 ? -28.819 -10.364 4.727   1.00 21.41 ? 110  ASN A N     1 
ATOM   833  C  CA    . ASN A 1 110 ? -28.059 -9.181  5.176   1.00 22.41 ? 110  ASN A CA    1 
ATOM   834  C  C     . ASN A 1 110 ? -28.977 -8.166  5.844   1.00 21.72 ? 110  ASN A C     1 
ATOM   835  O  O     . ASN A 1 110 ? -28.646 -6.992  5.750   1.00 22.46 ? 110  ASN A O     1 
ATOM   836  C  CB    . ASN A 1 110 ? -27.279 -8.571  4.018   1.00 23.74 ? 110  ASN A CB    1 
ATOM   837  C  CG    . ASN A 1 110 ? -28.144 -7.974  2.933   1.00 26.04 ? 110  ASN A CG    1 
ATOM   838  O  OD1   . ASN A 1 110 ? -29.344 -8.205  2.852   1.00 24.29 ? 110  ASN A OD1   1 
ATOM   839  N  ND2   . ASN A 1 110 ? -27.522 -7.142  2.123   1.00 32.97 ? 110  ASN A ND2   1 
ATOM   840  N  N     . ARG A 1 111 ? -30.034 -8.581  6.534   1.00 23.33 ? 111  ARG A N     1 
ATOM   841  C  CA    . ARG A 1 111 ? -30.897 -7.609  7.269   1.00 24.78 ? 111  ARG A CA    1 
ATOM   842  C  C     . ARG A 1 111 ? -30.260 -7.207  8.619   1.00 23.85 ? 111  ARG A C     1 
ATOM   843  O  O     . ARG A 1 111 ? -29.813 -8.065  9.379   1.00 22.31 ? 111  ARG A O     1 
ATOM   844  C  CB    . ARG A 1 111 ? -32.303 -8.145  7.511   1.00 27.33 ? 111  ARG A CB    1 
ATOM   845  C  CG    . ARG A 1 111 ? -33.115 -8.545  6.284   1.00 32.36 ? 111  ARG A CG    1 
ATOM   846  C  CD    . ARG A 1 111 ? -34.137 -9.606  6.711   1.00 39.59 ? 111  ARG A CD    1 
ATOM   847  N  NE    . ARG A 1 111 ? -34.829 -10.316 5.635   1.00 49.96 ? 111  ARG A NE    1 
ATOM   848  C  CZ    . ARG A 1 111 ? -34.335 -11.305 4.867   1.00 54.40 ? 111  ARG A CZ    1 
ATOM   849  N  NH1   . ARG A 1 111 ? -33.085 -11.732 4.983   1.00 49.37 ? 111  ARG A NH1   1 
ATOM   850  N  NH2   . ARG A 1 111 ? -35.119 -11.862 3.957   1.00 56.43 ? 111  ARG A NH2   1 
ATOM   851  N  N     . ILE A 1 112 ? -30.217 -5.902  8.886   1.00 24.29 ? 112  ILE A N     1 
ATOM   852  C  CA    . ILE A 1 112 ? -29.927 -5.324  10.216  1.00 22.63 ? 112  ILE A CA    1 
ATOM   853  C  C     . ILE A 1 112 ? -31.260 -5.290  10.943  1.00 23.41 ? 112  ILE A C     1 
ATOM   854  O  O     . ILE A 1 112 ? -32.071 -4.412  10.640  1.00 26.46 ? 112  ILE A O     1 
ATOM   855  C  CB    . ILE A 1 112 ? -29.251 -3.957  10.071  1.00 21.75 ? 112  ILE A CB    1 
ATOM   856  C  CG1   . ILE A 1 112 ? -27.944 -4.096  9.287   1.00 22.48 ? 112  ILE A CG1   1 
ATOM   857  C  CG2   . ILE A 1 112 ? -29.019 -3.356  11.440  1.00 22.52 ? 112  ILE A CG2   1 
ATOM   858  C  CD1   . ILE A 1 112 ? -27.155 -2.822  9.091   1.00 21.79 ? 112  ILE A CD1   1 
ATOM   859  N  N     . LEU A 1 113 ? -31.538 -6.286  11.770  1.00 23.09 ? 113  LEU A N     1 
ATOM   860  C  CA    . LEU A 1 113 ? -32.903 -6.464  12.339  1.00 23.82 ? 113  LEU A CA    1 
ATOM   861  C  C     . LEU A 1 113 ? -33.172 -5.378  13.385  1.00 24.56 ? 113  LEU A C     1 
ATOM   862  O  O     . LEU A 1 113 ? -34.326 -4.896  13.474  1.00 26.08 ? 113  LEU A O     1 
ATOM   863  C  CB    . LEU A 1 113 ? -33.039 -7.878  12.897  1.00 22.65 ? 113  LEU A CB    1 
ATOM   864  C  CG    . LEU A 1 113 ? -32.840 -8.975  11.850  1.00 26.66 ? 113  LEU A CG    1 
ATOM   865  C  CD1   . LEU A 1 113 ? -32.716 -10.349 12.483  1.00 24.50 ? 113  LEU A CD1   1 
ATOM   866  C  CD2   . LEU A 1 113 ? -33.970 -8.960  10.821  1.00 27.47 ? 113  LEU A CD2   1 
ATOM   867  N  N     . GLU A 1 114 ? -32.160 -5.004  14.165  1.00 24.81 ? 114  GLU A N     1 
ATOM   868  C  CA    . GLU A 1 114 ? -32.281 -3.923  15.172  1.00 24.34 ? 114  GLU A CA    1 
ATOM   869  C  C     . GLU A 1 114 ? -30.900 -3.343  15.449  1.00 22.97 ? 114  GLU A C     1 
ATOM   870  O  O     . GLU A 1 114 ? -29.945 -4.143  15.543  1.00 23.91 ? 114  GLU A O     1 
ATOM   871  C  CB    . GLU A 1 114 ? -32.924 -4.465  16.455  1.00 25.41 ? 114  GLU A CB    1 
ATOM   872  C  CG    . GLU A 1 114 ? -33.552 -3.343  17.255  1.00 28.28 ? 114  GLU A CG    1 
ATOM   873  C  CD    . GLU A 1 114 ? -33.971 -3.583  18.697  1.00 31.61 ? 114  GLU A CD    1 
ATOM   874  O  OE1   . GLU A 1 114 ? -34.097 -4.770  19.104  1.00 33.02 ? 114  GLU A OE1   1 
ATOM   875  O  OE2   . GLU A 1 114 ? -34.185 -2.563  19.416  1.00 30.25 ? 114  GLU A OE2   1 
ATOM   876  N  N     . VAL A 1 115 ? -30.799 -2.022  15.601  1.00 19.69 ? 115  VAL A N     1 
ATOM   877  C  CA    . VAL A 1 115 ? -29.676 -1.341  16.286  1.00 21.36 ? 115  VAL A CA    1 
ATOM   878  C  C     . VAL A 1 115 ? -30.301 -0.519  17.411  1.00 24.31 ? 115  VAL A C     1 
ATOM   879  O  O     . VAL A 1 115 ? -31.138 0.304   17.115  1.00 23.75 ? 115  VAL A O     1 
ATOM   880  C  CB    . VAL A 1 115 ? -28.812 -0.485  15.346  1.00 23.37 ? 115  VAL A CB    1 
ATOM   881  C  CG1   . VAL A 1 115 ? -27.640 0.108   16.093  1.00 24.80 ? 115  VAL A CG1   1 
ATOM   882  C  CG2   . VAL A 1 115 ? -28.313 -1.284  14.150  1.00 25.54 ? 115  VAL A CG2   1 
ATOM   883  N  N     . ASN A 1 116 ? -29.927 -0.791  18.661  1.00 23.83 ? 116  ASN A N     1 
ATOM   884  C  CA    . ASN A 1 116 ? -30.530 -0.179  19.859  1.00 21.44 ? 116  ASN A CA    1 
ATOM   885  C  C     . ASN A 1 116 ? -29.470 0.696   20.526  1.00 22.99 ? 116  ASN A C     1 
ATOM   886  O  O     . ASN A 1 116 ? -28.468 0.174   21.090  1.00 21.11 ? 116  ASN A O     1 
ATOM   887  C  CB    . ASN A 1 116 ? -31.159 -1.252  20.733  1.00 22.02 ? 116  ASN A CB    1 
ATOM   888  C  CG    . ASN A 1 116 ? -32.017 -0.666  21.835  1.00 20.50 ? 116  ASN A CG    1 
ATOM   889  O  OD1   . ASN A 1 116 ? -31.585 0.232   22.557  1.00 21.84 ? 116  ASN A OD1   1 
ATOM   890  N  ND2   . ASN A 1 116 ? -33.208 -1.213  21.994  1.00 19.96 ? 116  ASN A ND2   1 
ATOM   891  N  N     . GLU A 1 117 ? -29.695 2.011   20.471  1.00 22.45 ? 117  GLU A N     1 
ATOM   892  C  CA    . GLU A 1 117 ? -28.750 3.001   21.020  1.00 22.96 ? 117  GLU A CA    1 
ATOM   893  C  C     . GLU A 1 117 ? -28.780 2.981   22.556  1.00 24.02 ? 117  GLU A C     1 
ATOM   894  O  O     . GLU A 1 117 ? -27.687 2.956   23.187  1.00 23.70 ? 117  GLU A O     1 
ATOM   895  C  CB    . GLU A 1 117 ? -29.068 4.381   20.444  1.00 23.41 ? 117  GLU A CB    1 
ATOM   896  C  CG    . GLU A 1 117 ? -28.113 5.450   20.921  1.00 25.67 ? 117  GLU A CG    1 
ATOM   897  C  CD    . GLU A 1 117 ? -28.502 6.836   20.429  1.00 27.39 ? 117  GLU A CD    1 
ATOM   898  O  OE1   . GLU A 1 117 ? -29.659 7.201   20.649  1.00 35.57 ? 117  GLU A OE1   1 
ATOM   899  O  OE2   . GLU A 1 117 ? -27.681 7.509   19.785  1.00 24.46 ? 117  GLU A OE2   1 
ATOM   900  N  N     . GLU A 1 118 ? -29.955 3.051   23.171  1.00 25.17 ? 118  GLU A N     1 
ATOM   901  C  CA    . GLU A 1 118 ? -30.032 3.217   24.650  1.00 26.06 ? 118  GLU A CA    1 
ATOM   902  C  C     . GLU A 1 118 ? -29.492 1.938   25.336  1.00 24.80 ? 118  GLU A C     1 
ATOM   903  O  O     . GLU A 1 118 ? -28.940 2.072   26.447  1.00 23.95 ? 118  GLU A O     1 
ATOM   904  C  CB    . GLU A 1 118 ? -31.448 3.614   25.103  1.00 29.66 ? 118  GLU A CB    1 
ATOM   905  C  CG    . GLU A 1 118 ? -32.532 2.566   24.861  1.00 36.14 ? 118  GLU A CG    1 
ATOM   906  C  CD    . GLU A 1 118 ? -33.931 2.830   25.430  1.00 43.90 ? 118  GLU A CD    1 
ATOM   907  O  OE1   . GLU A 1 118 ? -34.102 3.811   26.200  1.00 49.93 ? 118  GLU A OE1   1 
ATOM   908  O  OE2   . GLU A 1 118 ? -34.870 2.038   25.110  1.00 49.15 ? 118  GLU A OE2   1 
ATOM   909  N  N     . PHE A 1 119 ? -29.600 0.754   24.722  1.00 21.90 ? 119  PHE A N     1 
ATOM   910  C  CA    . PHE A 1 119 ? -29.064 -0.505  25.317  1.00 24.00 ? 119  PHE A CA    1 
ATOM   911  C  C     . PHE A 1 119 ? -27.739 -0.939  24.666  1.00 21.82 ? 119  PHE A C     1 
ATOM   912  O  O     . PHE A 1 119 ? -27.135 -1.933  25.108  1.00 23.41 ? 119  PHE A O     1 
ATOM   913  C  CB    . PHE A 1 119 ? -30.114 -1.614  25.256  1.00 24.65 ? 119  PHE A CB    1 
ATOM   914  C  CG    . PHE A 1 119 ? -31.340 -1.346  26.087  1.00 27.14 ? 119  PHE A CG    1 
ATOM   915  C  CD1   . PHE A 1 119 ? -31.233 -0.953  27.411  1.00 31.73 ? 119  PHE A CD1   1 
ATOM   916  C  CD2   . PHE A 1 119 ? -32.602 -1.453  25.528  1.00 29.48 ? 119  PHE A CD2   1 
ATOM   917  C  CE1   . PHE A 1 119 ? -32.373 -0.659  28.147  1.00 31.78 ? 119  PHE A CE1   1 
ATOM   918  C  CE2   . PHE A 1 119 ? -33.738 -1.185  26.269  1.00 30.23 ? 119  PHE A CE2   1 
ATOM   919  C  CZ    . PHE A 1 119 ? -33.620 -0.780  27.576  1.00 29.97 ? 119  PHE A CZ    1 
ATOM   920  N  N     . GLY A 1 120 ? -27.276 -0.210  23.668  1.00 20.01 ? 120  GLY A N     1 
ATOM   921  C  CA    . GLY A 1 120 ? -26.017 -0.502  22.953  1.00 20.39 ? 120  GLY A CA    1 
ATOM   922  C  C     . GLY A 1 120 ? -25.948 -1.929  22.429  1.00 18.80 ? 120  GLY A C     1 
ATOM   923  O  O     . GLY A 1 120 ? -25.135 -2.722  22.917  1.00 16.31 ? 120  GLY A O     1 
ATOM   924  N  N     . TYR A 1 121 ? -26.758 -2.270  21.446  1.00 18.04 ? 121  TYR A N     1 
ATOM   925  C  CA    . TYR A 1 121 ? -26.608 -3.583  20.795  1.00 18.05 ? 121  TYR A CA    1 
ATOM   926  C  C     . TYR A 1 121 ? -27.145 -3.568  19.388  1.00 18.82 ? 121  TYR A C     1 
ATOM   927  O  O     . TYR A 1 121 ? -27.923 -2.649  19.047  1.00 18.55 ? 121  TYR A O     1 
ATOM   928  C  CB    . TYR A 1 121 ? -27.336 -4.648  21.600  1.00 17.75 ? 121  TYR A CB    1 
ATOM   929  C  CG    . TYR A 1 121 ? -28.834 -4.606  21.569  1.00 18.93 ? 121  TYR A CG    1 
ATOM   930  C  CD1   . TYR A 1 121 ? -29.547 -5.047  20.466  1.00 19.67 ? 121  TYR A CD1   1 
ATOM   931  C  CD2   . TYR A 1 121 ? -29.544 -4.210  22.698  1.00 19.91 ? 121  TYR A CD2   1 
ATOM   932  C  CE1   . TYR A 1 121 ? -30.925 -5.061  20.458  1.00 19.71 ? 121  TYR A CE1   1 
ATOM   933  C  CE2   . TYR A 1 121 ? -30.925 -4.247  22.723  1.00 19.66 ? 121  TYR A CE2   1 
ATOM   934  C  CZ    . TYR A 1 121 ? -31.611 -4.667  21.600  1.00 22.52 ? 121  TYR A CZ    1 
ATOM   935  O  OH    . TYR A 1 121 ? -32.976 -4.685  21.635  1.00 21.38 ? 121  TYR A OH    1 
ATOM   936  N  N     . ALA A 1 122 ? -26.802 -4.617  18.638  1.00 18.88 ? 122  ALA A N     1 
ATOM   937  C  CA    . ALA A 1 122 ? -27.380 -4.871  17.301  1.00 18.16 ? 122  ALA A CA    1 
ATOM   938  C  C     . ALA A 1 122 ? -27.788 -6.330  17.234  1.00 19.46 ? 122  ALA A C     1 
ATOM   939  O  O     . ALA A 1 122 ? -27.152 -7.152  17.939  1.00 19.25 ? 122  ALA A O     1 
ATOM   940  C  CB    . ALA A 1 122 ? -26.416 -4.532  16.208  1.00 17.49 ? 122  ALA A CB    1 
ATOM   941  N  N     . LEU A 1 123 ? -28.838 -6.597  16.458  1.00 18.06 ? 123  LEU A N     1 
ATOM   942  C  CA    . LEU A 1 123 ? -29.301 -7.943  16.098  1.00 18.95 ? 123  LEU A CA    1 
ATOM   943  C  C     . LEU A 1 123 ? -29.175 -8.025  14.585  1.00 20.06 ? 123  LEU A C     1 
ATOM   944  O  O     . LEU A 1 123 ? -29.813 -7.166  13.887  1.00 16.52 ? 123  LEU A O     1 
ATOM   945  C  CB    . LEU A 1 123 ? -30.747 -8.147  16.541  1.00 18.80 ? 123  LEU A CB    1 
ATOM   946  C  CG    . LEU A 1 123 ? -31.338 -9.491  16.127  1.00 19.66 ? 123  LEU A CG    1 
ATOM   947  C  CD1   . LEU A 1 123 ? -30.593 -10.632 16.820  1.00 18.33 ? 123  LEU A CD1   1 
ATOM   948  C  CD2   . LEU A 1 123 ? -32.844 -9.546  16.418  1.00 19.54 ? 123  LEU A CD2   1 
ATOM   949  N  N     . VAL A 1 124 ? -28.346 -8.953  14.105  1.00 19.94 ? 124  VAL A N     1 
ATOM   950  C  CA    . VAL A 1 124 ? -27.938 -8.998  12.672  1.00 21.38 ? 124  VAL A CA    1 
ATOM   951  C  C     . VAL A 1 124 ? -28.061 -10.418 12.100  1.00 21.74 ? 124  VAL A C     1 
ATOM   952  O  O     . VAL A 1 124 ? -27.811 -11.416 12.832  1.00 19.55 ? 124  VAL A O     1 
ATOM   953  C  CB    . VAL A 1 124 ? -26.508 -8.467  12.469  1.00 21.09 ? 124  VAL A CB    1 
ATOM   954  C  CG1   . VAL A 1 124 ? -26.407 -6.965  12.707  1.00 22.08 ? 124  VAL A CG1   1 
ATOM   955  C  CG2   . VAL A 1 124 ? -25.497 -9.242  13.298  1.00 20.50 ? 124  VAL A CG2   1 
ATOM   956  N  N     . GLU A 1 125 ? -28.311 -10.474 10.784  1.00 21.12 ? 125  GLU A N     1 
ATOM   957  C  CA    . GLU A 1 125 ? -28.238 -11.702 9.950   1.00 18.36 ? 125  GLU A CA    1 
ATOM   958  C  C     . GLU A 1 125 ? -26.807 -11.844 9.431   1.00 17.68 ? 125  GLU A C     1 
ATOM   959  O  O     . GLU A 1 125 ? -26.007 -10.898 9.442   1.00 15.74 ? 125  GLU A O     1 
ATOM   960  C  CB    . GLU A 1 125 ? -29.246 -11.604 8.801   1.00 20.17 ? 125  GLU A CB    1 
ATOM   961  C  CG    . GLU A 1 125 ? -30.719 -11.617 9.223   1.00 21.26 ? 125  GLU A CG    1 
ATOM   962  C  CD    . GLU A 1 125 ? -31.657 -11.820 8.040   1.00 21.44 ? 125  GLU A CD    1 
ATOM   963  O  OE1   . GLU A 1 125 ? -31.343 -11.262 6.949   1.00 22.28 ? 125  GLU A OE1   1 
ATOM   964  O  OE2   . GLU A 1 125 ? -32.581 -12.649 8.141   1.00 22.47 ? 125  GLU A OE2   1 
ATOM   965  N  N     . PRO A 1 126 ? -26.394 -13.065 9.020   1.00 17.60 ? 126  PRO A N     1 
ATOM   966  C  CA    . PRO A 1 126 ? -24.991 -13.343 8.765   1.00 18.00 ? 126  PRO A CA    1 
ATOM   967  C  C     . PRO A 1 126 ? -24.371 -12.517 7.646   1.00 18.50 ? 126  PRO A C     1 
ATOM   968  O  O     . PRO A 1 126 ? -23.192 -12.286 7.745   1.00 18.57 ? 126  PRO A O     1 
ATOM   969  C  CB    . PRO A 1 126 ? -24.989 -14.839 8.416   1.00 18.17 ? 126  PRO A CB    1 
ATOM   970  C  CG    . PRO A 1 126 ? -26.184 -15.364 9.125   1.00 17.49 ? 126  PRO A CG    1 
ATOM   971  C  CD    . PRO A 1 126 ? -27.216 -14.281 8.913   1.00 17.75 ? 126  PRO A CD    1 
ATOM   972  N  N     . GLY A 1 127 ? -25.148 -12.092 6.642   1.00 18.34 ? 127  GLY A N     1 
ATOM   973  C  CA    . GLY A 1 127 ? -24.604 -11.331 5.494   1.00 18.31 ? 127  GLY A CA    1 
ATOM   974  C  C     . GLY A 1 127 ? -24.226 -9.889  5.830   1.00 19.07 ? 127  GLY A C     1 
ATOM   975  O  O     . GLY A 1 127 ? -23.636 -9.222  4.985   1.00 17.70 ? 127  GLY A O     1 
ATOM   976  N  N     . VAL A 1 128 ? -24.530 -9.389  7.023   1.00 19.30 ? 128  VAL A N     1 
ATOM   977  C  CA    . VAL A 1 128 ? -24.219 -7.978  7.374   1.00 19.43 ? 128  VAL A CA    1 
ATOM   978  C  C     . VAL A 1 128 ? -22.715 -7.883  7.563   1.00 20.05 ? 128  VAL A C     1 
ATOM   979  O  O     . VAL A 1 128 ? -22.178 -8.624  8.418   1.00 20.05 ? 128  VAL A O     1 
ATOM   980  C  CB    . VAL A 1 128 ? -24.948 -7.485  8.641   1.00 22.05 ? 128  VAL A CB    1 
ATOM   981  C  CG1   . VAL A 1 128 ? -24.515 -6.064  8.973   1.00 24.02 ? 128  VAL A CG1   1 
ATOM   982  C  CG2   . VAL A 1 128 ? -26.458 -7.585  8.534   1.00 20.50 ? 128  VAL A CG2   1 
ATOM   983  N  N     . SER A 1 129 ? -22.090 -6.995  6.789   1.00 19.14 ? 129  SER A N     1 
ATOM   984  C  CA    . SER A 1 129 ? -20.673 -6.616  6.873   1.00 17.96 ? 129  SER A CA    1 
ATOM   985  C  C     . SER A 1 129 ? -20.494 -5.543  7.941   1.00 18.12 ? 129  SER A C     1 
ATOM   986  O  O     . SER A 1 129 ? -21.469 -4.802  8.288   1.00 19.89 ? 129  SER A O     1 
ATOM   987  C  CB    . SER A 1 129 ? -20.126 -6.161  5.521   1.00 18.69 ? 129  SER A CB    1 
ATOM   988  O  OG    . SER A 1 129 ? -20.556 -4.846  5.149   1.00 18.14 ? 129  SER A OG    1 
ATOM   989  N  N     . TYR A 1 130 ? -19.258 -5.389  8.377   1.00 17.96 ? 130  TYR A N     1 
ATOM   990  C  CA    . TYR A 1 130 ? -18.837 -4.281  9.263   1.00 18.68 ? 130  TYR A CA    1 
ATOM   991  C  C     . TYR A 1 130 ? -19.076 -2.958  8.531   1.00 20.36 ? 130  TYR A C     1 
ATOM   992  O  O     . TYR A 1 130 ? -19.612 -2.051  9.205   1.00 20.17 ? 130  TYR A O     1 
ATOM   993  C  CB    . TYR A 1 130 ? -17.392 -4.476  9.715   1.00 17.57 ? 130  TYR A CB    1 
ATOM   994  C  CG    . TYR A 1 130 ? -17.156 -5.685  10.585  1.00 17.18 ? 130  TYR A CG    1 
ATOM   995  C  CD1   . TYR A 1 130 ? -17.434 -5.650  11.944  1.00 17.08 ? 130  TYR A CD1   1 
ATOM   996  C  CD2   . TYR A 1 130 ? -16.632 -6.856  10.051  1.00 17.02 ? 130  TYR A CD2   1 
ATOM   997  C  CE1   . TYR A 1 130 ? -17.192 -6.746  12.764  1.00 17.12 ? 130  TYR A CE1   1 
ATOM   998  C  CE2   . TYR A 1 130 ? -16.384 -7.953  10.853  1.00 17.97 ? 130  TYR A CE2   1 
ATOM   999  C  CZ    . TYR A 1 130 ? -16.669 -7.898  12.212  1.00 17.18 ? 130  TYR A CZ    1 
ATOM   1000 O  OH    . TYR A 1 130 ? -16.402 -8.958  13.010  1.00 17.58 ? 130  TYR A OH    1 
ATOM   1001 N  N     . PHE A 1 131 ? -18.745 -2.859  7.232   1.00 22.08 ? 131  PHE A N     1 
ATOM   1002 C  CA    . PHE A 1 131 ? -19.039 -1.655  6.388   1.00 25.37 ? 131  PHE A CA    1 
ATOM   1003 C  C     . PHE A 1 131 ? -20.528 -1.305  6.530   1.00 22.32 ? 131  PHE A C     1 
ATOM   1004 O  O     . PHE A 1 131 ? -20.846 -0.135  6.828   1.00 21.45 ? 131  PHE A O     1 
ATOM   1005 C  CB    . PHE A 1 131 ? -18.668 -1.797  4.898   1.00 24.82 ? 131  PHE A CB    1 
ATOM   1006 C  CG    . PHE A 1 131 ? -17.195 -1.674  4.589   1.00 31.07 ? 131  PHE A CG    1 
ATOM   1007 C  CD1   . PHE A 1 131 ? -16.531 -0.447  4.634   1.00 31.25 ? 131  PHE A CD1   1 
ATOM   1008 C  CD2   . PHE A 1 131 ? -16.440 -2.789  4.221   1.00 31.47 ? 131  PHE A CD2   1 
ATOM   1009 C  CE1   . PHE A 1 131 ? -15.159 -0.381  4.373   1.00 32.13 ? 131  PHE A CE1   1 
ATOM   1010 C  CE2   . PHE A 1 131 ? -15.072 -2.696  3.974   1.00 25.91 ? 131  PHE A CE2   1 
ATOM   1011 C  CZ    . PHE A 1 131 ? -14.434 -1.510  4.058   1.00 23.39 ? 131  PHE A CZ    1 
ATOM   1012 N  N     . GLU A 1 132 ? -21.408 -2.276  6.299   1.00 22.22 ? 132  GLU A N     1 
ATOM   1013 C  CA    . GLU A 1 132 ? -22.875 -2.073  6.341   1.00 24.08 ? 132  GLU A CA    1 
ATOM   1014 C  C     . GLU A 1 132 ? -23.319 -1.620  7.738   1.00 23.36 ? 132  GLU A C     1 
ATOM   1015 O  O     . GLU A 1 132 ? -24.107 -0.664  7.824   1.00 20.97 ? 132  GLU A O     1 
ATOM   1016 C  CB    . GLU A 1 132 ? -23.602 -3.336  5.884   1.00 27.24 ? 132  GLU A CB    1 
ATOM   1017 C  CG    . GLU A 1 132 ? -23.465 -3.561  4.382   1.00 29.67 ? 132  GLU A CG    1 
ATOM   1018 C  CD    . GLU A 1 132 ? -24.045 -4.855  3.829   1.00 31.83 ? 132  GLU A CD    1 
ATOM   1019 O  OE1   . GLU A 1 132 ? -24.015 -5.920  4.511   1.00 27.26 ? 132  GLU A OE1   1 
ATOM   1020 O  OE2   . GLU A 1 132 ? -24.551 -4.789  2.711   1.00 38.76 ? 132  GLU A OE2   1 
ATOM   1021 N  N     . LEU A 1 133 ? -22.864 -2.268  8.810   1.00 22.33 ? 133  LEU A N     1 
ATOM   1022 C  CA    . LEU A 1 133 ? -23.353 -1.916  10.170  1.00 21.27 ? 133  LEU A CA    1 
ATOM   1023 C  C     . LEU A 1 133 ? -22.843 -0.512  10.506  1.00 20.38 ? 133  LEU A C     1 
ATOM   1024 O  O     . LEU A 1 133 ? -23.593 0.282   11.032  1.00 20.25 ? 133  LEU A O     1 
ATOM   1025 C  CB    . LEU A 1 133 ? -22.876 -2.948  11.197  1.00 21.79 ? 133  LEU A CB    1 
ATOM   1026 C  CG    . LEU A 1 133 ? -23.382 -2.736  12.623  1.00 21.33 ? 133  LEU A CG    1 
ATOM   1027 C  CD1   . LEU A 1 133 ? -24.908 -2.712  12.690  1.00 19.69 ? 133  LEU A CD1   1 
ATOM   1028 C  CD2   . LEU A 1 133 ? -22.848 -3.807  13.559  1.00 22.07 ? 133  LEU A CD2   1 
ATOM   1029 N  N     . TYR A 1 134 ? -21.607 -0.216  10.154  1.00 20.25 ? 134  TYR A N     1 
ATOM   1030 C  CA    . TYR A 1 134 ? -21.011 1.121   10.356  1.00 23.00 ? 134  TYR A CA    1 
ATOM   1031 C  C     . TYR A 1 134 ? -21.803 2.170   9.577   1.00 22.31 ? 134  TYR A C     1 
ATOM   1032 O  O     . TYR A 1 134 ? -22.153 3.174   10.184  1.00 21.61 ? 134  TYR A O     1 
ATOM   1033 C  CB    . TYR A 1 134 ? -19.550 1.142   9.920   1.00 22.15 ? 134  TYR A CB    1 
ATOM   1034 C  CG    . TYR A 1 134 ? -18.885 2.476   10.097  1.00 23.10 ? 134  TYR A CG    1 
ATOM   1035 C  CD1   . TYR A 1 134 ? -18.404 2.841   11.336  1.00 22.25 ? 134  TYR A CD1   1 
ATOM   1036 C  CD2   . TYR A 1 134 ? -18.688 3.337   9.023   1.00 22.96 ? 134  TYR A CD2   1 
ATOM   1037 C  CE1   . TYR A 1 134 ? -17.737 4.039   11.516  1.00 23.94 ? 134  TYR A CE1   1 
ATOM   1038 C  CE2   . TYR A 1 134 ? -18.034 4.551   9.183   1.00 24.48 ? 134  TYR A CE2   1 
ATOM   1039 C  CZ    . TYR A 1 134 ? -17.564 4.893   10.440  1.00 24.76 ? 134  TYR A CZ    1 
ATOM   1040 O  OH    . TYR A 1 134 ? -16.914 6.048   10.672  1.00 25.30 ? 134  TYR A OH    1 
ATOM   1041 N  N     . ASP A 1 135 ? -22.090 1.938   8.297   1.00 25.66 ? 135  ASP A N     1 
ATOM   1042 C  CA    . ASP A 1 135 ? -22.841 2.916   7.458   1.00 26.45 ? 135  ASP A CA    1 
ATOM   1043 C  C     . ASP A 1 135 ? -24.234 3.167   8.026   1.00 24.59 ? 135  ASP A C     1 
ATOM   1044 O  O     . ASP A 1 135 ? -24.660 4.314   8.058   1.00 27.04 ? 135  ASP A O     1 
ATOM   1045 C  CB    . ASP A 1 135 ? -22.981 2.446   6.028   1.00 30.48 ? 135  ASP A CB    1 
ATOM   1046 C  CG    . ASP A 1 135 ? -21.694 2.632   5.273   1.00 39.33 ? 135  ASP A CG    1 
ATOM   1047 O  OD1   . ASP A 1 135 ? -20.724 3.204   5.863   1.00 45.36 ? 135  ASP A OD1   1 
ATOM   1048 O  OD2   . ASP A 1 135 ? -21.655 2.187   4.126   1.00 42.84 ? 135  ASP A OD2   1 
ATOM   1049 N  N     . TYR A 1 136 ? -24.917 2.130   8.471   1.00 22.55 ? 136  TYR A N     1 
ATOM   1050 C  CA    . TYR A 1 136 ? -26.268 2.260   9.060   1.00 24.39 ? 136  TYR A CA    1 
ATOM   1051 C  C     . TYR A 1 136 ? -26.226 3.176   10.288  1.00 25.84 ? 136  TYR A C     1 
ATOM   1052 O  O     . TYR A 1 136 ? -27.101 4.076   10.410  1.00 26.38 ? 136  TYR A O     1 
ATOM   1053 C  CB    . TYR A 1 136 ? -26.821 0.876   9.371   1.00 26.26 ? 136  TYR A CB    1 
ATOM   1054 C  CG    . TYR A 1 136 ? -28.169 0.868   10.031  1.00 28.20 ? 136  TYR A CG    1 
ATOM   1055 C  CD1   . TYR A 1 136 ? -28.315 1.142   11.381  1.00 26.42 ? 136  TYR A CD1   1 
ATOM   1056 C  CD2   . TYR A 1 136 ? -29.300 0.561   9.294   1.00 31.14 ? 136  TYR A CD2   1 
ATOM   1057 C  CE1   . TYR A 1 136 ? -29.561 1.111   11.980  1.00 31.57 ? 136  TYR A CE1   1 
ATOM   1058 C  CE2   . TYR A 1 136 ? -30.553 0.514   9.881   1.00 33.54 ? 136  TYR A CE2   1 
ATOM   1059 C  CZ    . TYR A 1 136 ? -30.683 0.791   11.228  1.00 36.29 ? 136  TYR A CZ    1 
ATOM   1060 O  OH    . TYR A 1 136 ? -31.928 0.751   11.785  1.00 41.04 ? 136  TYR A OH    1 
ATOM   1061 N  N     . ILE A 1 137 ? -25.247 2.957   11.169  1.00 23.79 ? 137  ILE A N     1 
ATOM   1062 C  CA    . ILE A 1 137 ? -25.096 3.710   12.445  1.00 24.20 ? 137  ILE A CA    1 
ATOM   1063 C  C     . ILE A 1 137 ? -24.847 5.194   12.123  1.00 26.56 ? 137  ILE A C     1 
ATOM   1064 O  O     . ILE A 1 137 ? -25.540 6.065   12.732  1.00 23.77 ? 137  ILE A O     1 
ATOM   1065 C  CB    . ILE A 1 137 ? -23.966 3.106   13.299  1.00 21.91 ? 137  ILE A CB    1 
ATOM   1066 C  CG1   . ILE A 1 137 ? -24.432 1.793   13.933  1.00 22.38 ? 137  ILE A CG1   1 
ATOM   1067 C  CG2   . ILE A 1 137 ? -23.451 4.106   14.328  1.00 22.77 ? 137  ILE A CG2   1 
ATOM   1068 C  CD1   . ILE A 1 137 ? -23.356 1.044   14.663  1.00 22.16 ? 137  ILE A CD1   1 
ATOM   1069 N  N     . GLN A 1 138 ? -23.862 5.459   11.264  1.00 27.45 ? 138  GLN A N     1 
ATOM   1070 C  CA    . GLN A 1 138 ? -23.492 6.816   10.778  1.00 33.59 ? 138  GLN A CA    1 
ATOM   1071 C  C     . GLN A 1 138 ? -24.715 7.488   10.135  1.00 33.85 ? 138  GLN A C     1 
ATOM   1072 O  O     . GLN A 1 138 ? -25.074 8.568   10.562  1.00 36.32 ? 138  GLN A O     1 
ATOM   1073 C  CB    . GLN A 1 138 ? -22.329 6.710   9.792   1.00 37.79 ? 138  GLN A CB    1 
ATOM   1074 C  CG    . GLN A 1 138 ? -21.006 7.229   10.327  1.00 46.23 ? 138  GLN A CG    1 
ATOM   1075 C  CD    . GLN A 1 138 ? -20.656 6.753   11.718  1.00 49.96 ? 138  GLN A CD    1 
ATOM   1076 O  OE1   . GLN A 1 138 ? -20.835 5.584   12.099  1.00 58.50 ? 138  GLN A OE1   1 
ATOM   1077 N  NE2   . GLN A 1 138 ? -20.117 7.677   12.486  1.00 46.64 ? 138  GLN A NE2   1 
ATOM   1078 N  N     . GLU A 1 139 ? -25.333 6.844   9.151   1.00 39.29 ? 139  GLU A N     1 
ATOM   1079 C  CA    . GLU A 1 139 ? -26.545 7.332   8.449   1.00 40.40 ? 139  GLU A CA    1 
ATOM   1080 C  C     . GLU A 1 139 ? -27.602 7.736   9.484   1.00 39.41 ? 139  GLU A C     1 
ATOM   1081 O  O     . GLU A 1 139 ? -28.232 8.764   9.266   1.00 35.22 ? 139  GLU A O     1 
ATOM   1082 C  CB    . GLU A 1 139 ? -27.076 6.259   7.502   1.00 47.82 ? 139  GLU A CB    1 
ATOM   1083 C  CG    . GLU A 1 139 ? -28.383 6.619   6.818   1.00 59.72 ? 139  GLU A CG    1 
ATOM   1084 C  CD    . GLU A 1 139 ? -28.247 7.609   5.671   1.00 76.70 ? 139  GLU A CD    1 
ATOM   1085 O  OE1   . GLU A 1 139 ? -27.117 7.754   5.139   1.00 84.40 ? 139  GLU A OE1   1 
ATOM   1086 O  OE2   . GLU A 1 139 ? -29.276 8.224   5.299   1.00 86.93 ? 139  GLU A OE2   1 
ATOM   1087 N  N     . LYS A 1 140 ? -27.818 6.955   10.550  1.00 34.65 ? 140  LYS A N     1 
ATOM   1088 C  CA    . LYS A 1 140 ? -28.927 7.220   11.514  1.00 33.17 ? 140  LYS A CA    1 
ATOM   1089 C  C     . LYS A 1 140 ? -28.445 8.132   12.647  1.00 31.05 ? 140  LYS A C     1 
ATOM   1090 O  O     . LYS A 1 140 ? -29.245 8.373   13.538  1.00 37.29 ? 140  LYS A O     1 
ATOM   1091 C  CB    . LYS A 1 140 ? -29.521 5.935   12.093  1.00 37.80 ? 140  LYS A CB    1 
ATOM   1092 C  CG    . LYS A 1 140 ? -30.256 5.047   11.104  1.00 46.82 ? 140  LYS A CG    1 
ATOM   1093 C  CD    . LYS A 1 140 ? -31.395 5.736   10.379  1.00 54.90 ? 140  LYS A CD    1 
ATOM   1094 C  CE    . LYS A 1 140 ? -32.162 4.799   9.471   1.00 60.83 ? 140  LYS A CE    1 
ATOM   1095 N  NZ    . LYS A 1 140 ? -32.687 3.640   10.230  1.00 67.50 ? 140  LYS A NZ    1 
ATOM   1096 N  N     . GLY A 1 141 ? -27.198 8.616   12.614  1.00 26.96 ? 141  GLY A N     1 
ATOM   1097 C  CA    . GLY A 1 141 ? -26.571 9.384   13.702  1.00 26.92 ? 141  GLY A CA    1 
ATOM   1098 C  C     . GLY A 1 141 ? -26.633 8.702   15.072  1.00 28.48 ? 141  GLY A C     1 
ATOM   1099 O  O     . GLY A 1 141 ? -26.649 9.426   16.073  1.00 31.36 ? 141  GLY A O     1 
ATOM   1100 N  N     . LEU A 1 142 ? -26.557 7.370   15.180  1.00 27.39 ? 142  LEU A N     1 
ATOM   1101 C  CA    . LEU A 1 142 ? -26.573 6.712   16.518  1.00 25.82 ? 142  LEU A CA    1 
ATOM   1102 C  C     . LEU A 1 142 ? -25.198 6.870   17.187  1.00 25.20 ? 142  LEU A C     1 
ATOM   1103 O  O     . LEU A 1 142 ? -24.154 6.740   16.495  1.00 23.68 ? 142  LEU A O     1 
ATOM   1104 C  CB    . LEU A 1 142 ? -26.984 5.241   16.405  1.00 26.19 ? 142  LEU A CB    1 
ATOM   1105 C  CG    . LEU A 1 142 ? -28.335 4.945   15.753  1.00 27.17 ? 142  LEU A CG    1 
ATOM   1106 C  CD1   . LEU A 1 142 ? -28.616 3.456   15.749  1.00 27.26 ? 142  LEU A CD1   1 
ATOM   1107 C  CD2   . LEU A 1 142 ? -29.474 5.685   16.431  1.00 27.24 ? 142  LEU A CD2   1 
ATOM   1108 N  N     . LYS A 1 143 ? -25.182 7.101   18.502  1.00 24.40 ? 143  LYS A N     1 
ATOM   1109 C  CA    . LYS A 1 143 ? -23.920 7.314   19.252  1.00 27.26 ? 143  LYS A CA    1 
ATOM   1110 C  C     . LYS A 1 143 ? -23.354 5.958   19.706  1.00 25.04 ? 143  LYS A C     1 
ATOM   1111 O  O     . LYS A 1 143 ? -23.229 5.729   20.959  1.00 20.32 ? 143  LYS A O     1 
ATOM   1112 C  CB    . LYS A 1 143 ? -24.173 8.274   20.407  1.00 33.11 ? 143  LYS A CB    1 
ATOM   1113 C  CG    . LYS A 1 143 ? -24.641 9.664   19.987  1.00 39.40 ? 143  LYS A CG    1 
ATOM   1114 C  CD    . LYS A 1 143 ? -24.542 10.637  21.135  1.00 45.16 ? 143  LYS A CD    1 
ATOM   1115 C  CE    . LYS A 1 143 ? -25.819 11.406  21.390  1.00 53.71 ? 143  LYS A CE    1 
ATOM   1116 N  NZ    . LYS A 1 143 ? -25.953 12.527  20.432  1.00 60.74 ? 143  LYS A NZ    1 
ATOM   1117 N  N     . LEU A 1 144 ? -23.032 5.107   18.721  1.00 21.74 ? 144  LEU A N     1 
ATOM   1118 C  CA    . LEU A 1 144 ? -22.472 3.746   18.925  1.00 21.97 ? 144  LEU A CA    1 
ATOM   1119 C  C     . LEU A 1 144 ? -21.238 3.545   18.054  1.00 22.82 ? 144  LEU A C     1 
ATOM   1120 O  O     . LEU A 1 144 ? -21.176 4.084   16.938  1.00 20.93 ? 144  LEU A O     1 
ATOM   1121 C  CB    . LEU A 1 144 ? -23.527 2.702   18.585  1.00 22.04 ? 144  LEU A CB    1 
ATOM   1122 C  CG    . LEU A 1 144 ? -24.817 2.761   19.392  1.00 22.33 ? 144  LEU A CG    1 
ATOM   1123 C  CD1   . LEU A 1 144 ? -25.801 1.757   18.822  1.00 23.98 ? 144  LEU A CD1   1 
ATOM   1124 C  CD2   . LEU A 1 144 ? -24.566 2.486   20.866  1.00 23.83 ? 144  LEU A CD2   1 
ATOM   1125 N  N     . TRP A 1 145 ? -20.299 2.761   18.567  1.00 22.05 ? 145  TRP A N     1 
ATOM   1126 C  CA    . TRP A 1 145 ? -19.118 2.272   17.823  1.00 21.65 ? 145  TRP A CA    1 
ATOM   1127 C  C     . TRP A 1 145 ? -19.296 0.786   17.559  1.00 20.64 ? 145  TRP A C     1 
ATOM   1128 O  O     . TRP A 1 145 ? -19.961 0.079   18.340  1.00 17.75 ? 145  TRP A O     1 
ATOM   1129 C  CB    . TRP A 1 145 ? -17.820 2.537   18.585  1.00 23.38 ? 145  TRP A CB    1 
ATOM   1130 C  CG    . TRP A 1 145 ? -17.354 3.956   18.543  1.00 23.76 ? 145  TRP A CG    1 
ATOM   1131 C  CD1   . TRP A 1 145 ? -18.039 5.030   18.057  1.00 25.04 ? 145  TRP A CD1   1 
ATOM   1132 C  CD2   . TRP A 1 145 ? -16.103 4.467   19.029  1.00 26.07 ? 145  TRP A CD2   1 
ATOM   1133 N  NE1   . TRP A 1 145 ? -17.294 6.163   18.191  1.00 24.84 ? 145  TRP A NE1   1 
ATOM   1134 C  CE2   . TRP A 1 145 ? -16.104 5.853   18.784  1.00 26.25 ? 145  TRP A CE2   1 
ATOM   1135 C  CE3   . TRP A 1 145 ? -14.985 3.891   19.642  1.00 29.70 ? 145  TRP A CE3   1 
ATOM   1136 C  CZ2   . TRP A 1 145 ? -15.034 6.673   19.128  1.00 28.82 ? 145  TRP A CZ2   1 
ATOM   1137 C  CZ3   . TRP A 1 145 ? -13.930 4.706   19.990  1.00 29.51 ? 145  TRP A CZ3   1 
ATOM   1138 C  CH2   . TRP A 1 145 ? -13.955 6.072   19.730  1.00 28.70 ? 145  TRP A CH2   1 
ATOM   1139 N  N     . ILE A 1 146 ? -18.709 0.342   16.462  1.00 20.34 ? 146  ILE A N     1 
ATOM   1140 C  CA    . ILE A 1 146 ? -18.539 -1.104  16.234  1.00 18.89 ? 146  ILE A CA    1 
ATOM   1141 C  C     . ILE A 1 146 ? -17.084 -1.455  16.556  1.00 20.00 ? 146  ILE A C     1 
ATOM   1142 O  O     . ILE A 1 146 ? -16.222 -0.532  16.791  1.00 17.88 ? 146  ILE A O     1 
ATOM   1143 C  CB    . ILE A 1 146 ? -19.001 -1.476  14.821  1.00 20.58 ? 146  ILE A CB    1 
ATOM   1144 C  CG1   . ILE A 1 146 ? -18.186 -0.797  13.719  1.00 21.28 ? 146  ILE A CG1   1 
ATOM   1145 C  CG2   . ILE A 1 146 ? -20.486 -1.194  14.663  1.00 21.52 ? 146  ILE A CG2   1 
ATOM   1146 C  CD1   . ILE A 1 146 ? -18.364 -1.478  12.380  1.00 22.88 ? 146  ILE A CD1   1 
ATOM   1147 N  N     . ASP A 1 147 ? -16.804 -2.754  16.570  1.00 18.91 ? 147  ASP A N     1 
ATOM   1148 C  CA    . ASP A 1 147 ? -15.426 -3.252  16.751  1.00 16.97 ? 147  ASP A CA    1 
ATOM   1149 C  C     . ASP A 1 147 ? -15.080 -4.100  15.532  1.00 16.91 ? 147  ASP A C     1 
ATOM   1150 O  O     . ASP A 1 147 ? -15.687 -5.154  15.365  1.00 17.10 ? 147  ASP A O     1 
ATOM   1151 C  CB    . ASP A 1 147 ? -15.290 -3.989  18.082  1.00 17.70 ? 147  ASP A CB    1 
ATOM   1152 C  CG    . ASP A 1 147 ? -13.850 -4.341  18.340  1.00 17.48 ? 147  ASP A CG    1 
ATOM   1153 O  OD1   . ASP A 1 147 ? -13.313 -5.165  17.539  1.00 17.86 ? 147  ASP A OD1   1 
ATOM   1154 O  OD2   . ASP A 1 147 ? -13.275 -3.760  19.293  1.00 16.35 ? 147  ASP A OD2   1 
ATOM   1155 N  N     . VAL A 1 148 ? -14.135 -3.638  14.732  1.00 16.99 ? 148  VAL A N     1 
ATOM   1156 C  CA    . VAL A 1 148 ? -13.833 -4.201  13.399  1.00 20.14 ? 148  VAL A CA    1 
ATOM   1157 C  C     . VAL A 1 148 ? -12.493 -4.937  13.463  1.00 21.55 ? 148  VAL A C     1 
ATOM   1158 O  O     . VAL A 1 148 ? -11.521 -4.443  14.048  1.00 17.89 ? 148  VAL A O     1 
ATOM   1159 C  CB    . VAL A 1 148 ? -13.792 -3.101  12.317  1.00 21.43 ? 148  VAL A CB    1 
ATOM   1160 C  CG1   . VAL A 1 148 ? -15.052 -2.258  12.333  1.00 24.61 ? 148  VAL A CG1   1 
ATOM   1161 C  CG2   . VAL A 1 148 ? -12.572 -2.189  12.434  1.00 21.77 ? 148  VAL A CG2   1 
ATOM   1162 N  N     . PRO A 1 149 ? -12.370 -6.068  12.733  1.00 21.12 ? 149  PRO A N     1 
ATOM   1163 C  CA    . PRO A 1 149 ? -11.057 -6.638  12.459  1.00 23.29 ? 149  PRO A CA    1 
ATOM   1164 C  C     . PRO A 1 149 ? -10.291 -5.583  11.649  1.00 23.56 ? 149  PRO A C     1 
ATOM   1165 O  O     . PRO A 1 149 ? -10.805 -4.561  11.401  1.00 25.48 ? 149  PRO A O     1 
ATOM   1166 C  CB    . PRO A 1 149 ? -11.339 -7.938  11.704  1.00 25.79 ? 149  PRO A CB    1 
ATOM   1167 C  CG    . PRO A 1 149 ? -12.873 -8.091  11.678  1.00 23.73 ? 149  PRO A CG    1 
ATOM   1168 C  CD    . PRO A 1 149 ? -13.465 -6.743  12.028  1.00 22.28 ? 149  PRO A CD    1 
ATOM   1169 N  N     . ASP A 1 150 ? -9.077  -5.833  11.213  1.00 31.72 ? 150  ASP A N     1 
ATOM   1170 C  CA    . ASP A 1 150 ? -8.345  -4.862  10.349  1.00 32.16 ? 150  ASP A CA    1 
ATOM   1171 C  C     . ASP A 1 150 ? -9.007  -4.721  8.963   1.00 33.35 ? 150  ASP A C     1 
ATOM   1172 O  O     . ASP A 1 150 ? -8.605  -3.816  8.212   1.00 37.97 ? 150  ASP A O     1 
ATOM   1173 C  CB    . ASP A 1 150 ? -6.883  -5.278  10.224  1.00 35.35 ? 150  ASP A CB    1 
ATOM   1174 C  CG    . ASP A 1 150 ? -6.093  -4.987  11.478  1.00 40.03 ? 150  ASP A CG    1 
ATOM   1175 O  OD1   . ASP A 1 150 ? -6.336  -3.908  12.073  1.00 41.27 ? 150  ASP A OD1   1 
ATOM   1176 O  OD2   . ASP A 1 150 ? -5.248  -5.848  11.846  1.00 44.61 ? 150  ASP A OD2   1 
ATOM   1177 N  N     . VAL A 1 151 ? -10.058 -5.487  8.694   1.00 28.92 ? 151  VAL A N     1 
ATOM   1178 C  CA    . VAL A 1 151 ? -10.609 -5.761  7.351   1.00 34.85 ? 151  VAL A CA    1 
ATOM   1179 C  C     . VAL A 1 151 ? -12.134 -5.667  7.473   1.00 31.59 ? 151  VAL A C     1 
ATOM   1180 O  O     . VAL A 1 151 ? -12.680 -6.321  8.349   1.00 39.06 ? 151  VAL A O     1 
ATOM   1181 C  CB    . VAL A 1 151 ? -10.034 -7.140  6.944   1.00 37.45 ? 151  VAL A CB    1 
ATOM   1182 C  CG1   . VAL A 1 151 ? -11.055 -8.157  6.505   1.00 40.37 ? 151  VAL A CG1   1 
ATOM   1183 C  CG2   . VAL A 1 151 ? -8.915  -6.963  5.949   1.00 43.51 ? 151  VAL A CG2   1 
ATOM   1184 N  N     . GLY A 1 152 ? -12.786 -4.815  6.690   1.00 25.72 ? 152  GLY A N     1 
ATOM   1185 C  CA    . GLY A 1 152 ? -14.172 -4.395  6.956   1.00 26.05 ? 152  GLY A CA    1 
ATOM   1186 C  C     . GLY A 1 152 ? -15.218 -5.102  6.115   1.00 23.75 ? 152  GLY A C     1 
ATOM   1187 O  O     . GLY A 1 152 ? -16.402 -4.948  6.418   1.00 20.68 ? 152  GLY A O     1 
ATOM   1188 N  N     . TRP A 1 153 ? -14.828 -5.862  5.093   1.00 22.79 ? 153  TRP A N     1 
ATOM   1189 C  CA    . TRP A 1 153 ? -15.810 -6.627  4.273   1.00 21.02 ? 153  TRP A CA    1 
ATOM   1190 C  C     . TRP A 1 153 ? -16.233 -7.926  4.955   1.00 19.61 ? 153  TRP A C     1 
ATOM   1191 O  O     . TRP A 1 153 ? -17.028 -8.650  4.381   1.00 21.41 ? 153  TRP A O     1 
ATOM   1192 C  CB    . TRP A 1 153 ? -15.265 -6.907  2.876   1.00 22.63 ? 153  TRP A CB    1 
ATOM   1193 C  CG    . TRP A 1 153 ? -13.987 -7.689  2.778   1.00 21.69 ? 153  TRP A CG    1 
ATOM   1194 C  CD1   . TRP A 1 153 ? -13.332 -8.404  3.740   1.00 20.35 ? 153  TRP A CD1   1 
ATOM   1195 C  CD2   . TRP A 1 153 ? -13.250 -7.881  1.558   1.00 22.29 ? 153  TRP A CD2   1 
ATOM   1196 N  NE1   . TRP A 1 153 ? -12.213 -8.985  3.213   1.00 22.32 ? 153  TRP A NE1   1 
ATOM   1197 C  CE2   . TRP A 1 153 ? -12.139 -8.700  1.870   1.00 21.67 ? 153  TRP A CE2   1 
ATOM   1198 C  CE3   . TRP A 1 153 ? -13.427 -7.437  0.236   1.00 22.74 ? 153  TRP A CE3   1 
ATOM   1199 C  CZ2   . TRP A 1 153 ? -11.209 -9.084  0.899   1.00 20.93 ? 153  TRP A CZ2   1 
ATOM   1200 C  CZ3   . TRP A 1 153 ? -12.478 -7.784  -0.715  1.00 22.42 ? 153  TRP A CZ3   1 
ATOM   1201 C  CH2   . TRP A 1 153 ? -11.397 -8.606  -0.387  1.00 21.00 ? 153  TRP A CH2   1 
ATOM   1202 N  N     . GLY A 1 154 ? -15.726 -8.238  6.139   1.00 19.09 ? 154  GLY A N     1 
ATOM   1203 C  CA    . GLY A 1 154 ? -16.107 -9.477  6.845   1.00 18.34 ? 154  GLY A CA    1 
ATOM   1204 C  C     . GLY A 1 154 ? -17.499 -9.402  7.420   1.00 17.70 ? 154  GLY A C     1 
ATOM   1205 O  O     . GLY A 1 154 ? -18.101 -8.317  7.342   1.00 18.85 ? 154  GLY A O     1 
ATOM   1206 N  N     . SER A 1 155 ? -17.948 -10.499 8.025   1.00 15.24 ? 155  SER A N     1 
ATOM   1207 C  CA    . SER A 1 155 ? -19.258 -10.659 8.698   1.00 16.78 ? 155  SER A CA    1 
ATOM   1208 C  C     . SER A 1 155 ? -19.185 -10.375 10.212  1.00 16.81 ? 155  SER A C     1 
ATOM   1209 O  O     . SER A 1 155 ? -18.351 -10.987 10.924  1.00 17.40 ? 155  SER A O     1 
ATOM   1210 C  CB    . SER A 1 155 ? -19.790 -12.057 8.469   1.00 15.44 ? 155  SER A CB    1 
ATOM   1211 O  OG    . SER A 1 155 ? -20.966 -12.221 9.233   1.00 15.04 ? 155  SER A OG    1 
ATOM   1212 N  N     . VAL A 1 156 ? -20.114 -9.588  10.730  1.00 17.49 ? 156  VAL A N     1 
ATOM   1213 C  CA    . VAL A 1 156 ? -20.223 -9.340  12.195  1.00 19.09 ? 156  VAL A CA    1 
ATOM   1214 C  C     . VAL A 1 156 ? -20.455 -10.693 12.888  1.00 19.21 ? 156  VAL A C     1 
ATOM   1215 O  O     . VAL A 1 156 ? -19.795 -10.934 13.885  1.00 18.16 ? 156  VAL A O     1 
ATOM   1216 C  CB    . VAL A 1 156 ? -21.326 -8.321  12.529  1.00 21.16 ? 156  VAL A CB    1 
ATOM   1217 C  CG1   . VAL A 1 156 ? -21.449 -8.152  14.047  1.00 21.48 ? 156  VAL A CG1   1 
ATOM   1218 C  CG2   . VAL A 1 156 ? -21.070 -6.985  11.822  1.00 19.88 ? 156  VAL A CG2   1 
ATOM   1219 N  N     . VAL A 1 157 ? -21.303 -11.552 12.307  1.00 18.07 ? 157  VAL A N     1 
ATOM   1220 C  CA    . VAL A 1 157 ? -21.572 -12.944 12.761  1.00 17.14 ? 157  VAL A CA    1 
ATOM   1221 C  C     . VAL A 1 157 ? -20.391 -13.898 12.501  1.00 16.99 ? 157  VAL A C     1 
ATOM   1222 O  O     . VAL A 1 157 ? -19.845 -14.471 13.478  1.00 16.83 ? 157  VAL A O     1 
ATOM   1223 C  CB    . VAL A 1 157 ? -22.872 -13.461 12.138  1.00 17.14 ? 157  VAL A CB    1 
ATOM   1224 C  CG1   . VAL A 1 157 ? -23.087 -14.941 12.475  1.00 16.99 ? 157  VAL A CG1   1 
ATOM   1225 C  CG2   . VAL A 1 157 ? -24.036 -12.621 12.614  1.00 17.36 ? 157  VAL A CG2   1 
ATOM   1226 N  N     . GLY A 1 158 ? -20.002 -14.110 11.242  1.00 18.85 ? 158  GLY A N     1 
ATOM   1227 C  CA    . GLY A 1 158 ? -18.968 -15.098 10.871  1.00 17.22 ? 158  GLY A CA    1 
ATOM   1228 C  C     . GLY A 1 158 ? -17.695 -14.881 11.674  1.00 16.23 ? 158  GLY A C     1 
ATOM   1229 O  O     . GLY A 1 158 ? -17.196 -15.810 12.314  1.00 13.15 ? 158  GLY A O     1 
ATOM   1230 N  N     . ASN A 1 159 ? -17.217 -13.652 11.693  1.00 16.25 ? 159  ASN A N     1 
ATOM   1231 C  CA    . ASN A 1 159 ? -15.958 -13.336 12.397  1.00 16.32 ? 159  ASN A CA    1 
ATOM   1232 C  C     . ASN A 1 159 ? -16.113 -13.726 13.880  1.00 16.84 ? 159  ASN A C     1 
ATOM   1233 O  O     . ASN A 1 159 ? -15.194 -14.402 14.448  1.00 16.65 ? 159  ASN A O     1 
ATOM   1234 C  CB    . ASN A 1 159 ? -15.568 -11.886 12.159  1.00 17.03 ? 159  ASN A CB    1 
ATOM   1235 C  CG    . ASN A 1 159 ? -14.406 -11.501 13.035  1.00 18.44 ? 159  ASN A CG    1 
ATOM   1236 O  OD1   . ASN A 1 159 ? -14.582 -11.314 14.245  1.00 18.37 ? 159  ASN A OD1   1 
ATOM   1237 N  ND2   . ASN A 1 159 ? -13.220 -11.482 12.447  1.00 18.91 ? 159  ASN A ND2   1 
ATOM   1238 N  N     . ALA A 1 160 ? -17.234 -13.362 14.502  1.00 16.30 ? 160  ALA A N     1 
ATOM   1239 C  CA    . ALA A 1 160 ? -17.460 -13.634 15.936  1.00 16.23 ? 160  ALA A CA    1 
ATOM   1240 C  C     . ALA A 1 160 ? -17.474 -15.144 16.189  1.00 15.74 ? 160  ALA A C     1 
ATOM   1241 O  O     . ALA A 1 160 ? -16.865 -15.584 17.197  1.00 13.43 ? 160  ALA A O     1 
ATOM   1242 C  CB    . ALA A 1 160 ? -18.728 -12.960 16.428  1.00 16.11 ? 160  ALA A CB    1 
ATOM   1243 N  N     . LEU A 1 161 ? -18.186 -15.904 15.352  1.00 16.30 ? 161  LEU A N     1 
ATOM   1244 C  CA    . LEU A 1 161 ? -18.287 -17.378 15.510  1.00 16.11 ? 161  LEU A CA    1 
ATOM   1245 C  C     . LEU A 1 161 ? -16.910 -18.026 15.364  1.00 15.71 ? 161  LEU A C     1 
ATOM   1246 O  O     . LEU A 1 161 ? -16.673 -19.017 16.058  1.00 15.41 ? 161  LEU A O     1 
ATOM   1247 C  CB    . LEU A 1 161 ? -19.258 -17.955 14.480  1.00 16.63 ? 161  LEU A CB    1 
ATOM   1248 C  CG    . LEU A 1 161 ? -20.708 -17.506 14.653  1.00 16.89 ? 161  LEU A CG    1 
ATOM   1249 C  CD1   . LEU A 1 161 ? -21.557 -18.037 13.529  1.00 17.93 ? 161  LEU A CD1   1 
ATOM   1250 C  CD2   . LEU A 1 161 ? -21.255 -17.948 16.004  1.00 17.01 ? 161  LEU A CD2   1 
ATOM   1251 N  N     . ASP A 1 162 ? -16.007 -17.467 14.552  1.00 15.82 ? 162  ASP A N     1 
ATOM   1252 C  CA    . ASP A 1 162 ? -14.625 -18.012 14.444  1.00 16.25 ? 162  ASP A CA    1 
ATOM   1253 C  C     . ASP A 1 162 ? -13.709 -17.451 15.566  1.00 16.00 ? 162  ASP A C     1 
ATOM   1254 O  O     . ASP A 1 162 ? -12.494 -17.690 15.474  1.00 16.39 ? 162  ASP A O     1 
ATOM   1255 C  CB    . ASP A 1 162 ? -14.068 -17.824 13.031  1.00 16.95 ? 162  ASP A CB    1 
ATOM   1256 C  CG    . ASP A 1 162 ? -13.197 -19.007 12.579  1.00 19.68 ? 162  ASP A CG    1 
ATOM   1257 O  OD1   . ASP A 1 162 ? -13.464 -20.165 13.029  1.00 20.68 ? 162  ASP A OD1   1 
ATOM   1258 O  OD2   . ASP A 1 162 ? -12.211 -18.769 11.849  1.00 17.28 ? 162  ASP A OD2   1 
ATOM   1259 N  N     . HIS A 1 163 ? -14.250 -16.797 16.609  1.00 14.34 ? 163  HIS A N     1 
ATOM   1260 C  CA    . HIS A 1 163 ? -13.511 -16.204 17.774  1.00 15.56 ? 163  HIS A CA    1 
ATOM   1261 C  C     . HIS A 1 163 ? -12.583 -15.088 17.283  1.00 17.03 ? 163  HIS A C     1 
ATOM   1262 O  O     . HIS A 1 163 ? -11.411 -15.031 17.722  1.00 16.55 ? 163  HIS A O     1 
ATOM   1263 C  CB    . HIS A 1 163 ? -12.774 -17.263 18.596  1.00 17.14 ? 163  HIS A CB    1 
ATOM   1264 C  CG    . HIS A 1 163 ? -13.646 -18.337 19.166  1.00 17.07 ? 163  HIS A CG    1 
ATOM   1265 N  ND1   . HIS A 1 163 ? -13.121 -19.520 19.679  1.00 17.83 ? 163  HIS A ND1   1 
ATOM   1266 C  CD2   . HIS A 1 163 ? -14.991 -18.432 19.298  1.00 16.80 ? 163  HIS A CD2   1 
ATOM   1267 C  CE1   . HIS A 1 163 ? -14.113 -20.288 20.072  1.00 17.11 ? 163  HIS A CE1   1 
ATOM   1268 N  NE2   . HIS A 1 163 ? -15.262 -19.665 19.840  1.00 16.24 ? 163  HIS A NE2   1 
ATOM   1269 N  N     . GLY A 1 164 ? -13.095 -14.265 16.339  1.00 17.46 ? 164  GLY A N     1 
ATOM   1270 C  CA    . GLY A 1 164 ? -12.429 -13.079 15.786  1.00 17.48 ? 164  GLY A CA    1 
ATOM   1271 C  C     . GLY A 1 164 ? -12.182 -12.025 16.843  1.00 17.87 ? 164  GLY A C     1 
ATOM   1272 O  O     . GLY A 1 164 ? -12.837 -12.077 17.925  1.00 15.93 ? 164  GLY A O     1 
ATOM   1273 N  N     . ILE A 1 165 ? -11.280 -11.092 16.530  1.00 18.05 ? 165  ILE A N     1 
ATOM   1274 C  CA    . ILE A 1 165 ? -10.846 -10.006 17.450  1.00 19.00 ? 165  ILE A CA    1 
ATOM   1275 C  C     . ILE A 1 165 ? -10.742 -8.684  16.685  1.00 18.35 ? 165  ILE A C     1 
ATOM   1276 O  O     . ILE A 1 165 ? -10.452 -8.711  15.487  1.00 17.19 ? 165  ILE A O     1 
ATOM   1277 C  CB    . ILE A 1 165 ? -9.503  -10.384 18.071  1.00 22.70 ? 165  ILE A CB    1 
ATOM   1278 C  CG1   . ILE A 1 165 ? -8.461  -10.556 16.963  1.00 27.28 ? 165  ILE A CG1   1 
ATOM   1279 C  CG2   . ILE A 1 165 ? -9.657  -11.626 18.938  1.00 22.32 ? 165  ILE A CG2   1 
ATOM   1280 C  CD1   . ILE A 1 165 ? -7.054  -10.826 17.461  1.00 33.97 ? 165  ILE A CD1   1 
ATOM   1281 N  N     . GLY A 1 166 ? -10.980 -7.580  17.381  1.00 16.44 ? 166  GLY A N     1 
ATOM   1282 C  CA    . GLY A 1 166 ? -10.636 -6.230  16.935  1.00 18.32 ? 166  GLY A CA    1 
ATOM   1283 C  C     . GLY A 1 166 ? -9.919  -5.436  18.019  1.00 18.90 ? 166  GLY A C     1 
ATOM   1284 O  O     . GLY A 1 166 ? -9.329  -6.049  18.926  1.00 16.64 ? 166  GLY A O     1 
ATOM   1285 N  N     . TYR A 1 167 ? -9.932  -4.111  17.916  1.00 19.98 ? 167  TYR A N     1 
ATOM   1286 C  CA    . TYR A 1 167 ? -8.902  -3.242  18.538  1.00 20.95 ? 167  TYR A CA    1 
ATOM   1287 C  C     . TYR A 1 167 ? -9.543  -2.127  19.380  1.00 20.98 ? 167  TYR A C     1 
ATOM   1288 O  O     . TYR A 1 167 ? -8.812  -1.137  19.604  1.00 21.64 ? 167  TYR A O     1 
ATOM   1289 C  CB    . TYR A 1 167 ? -7.985  -2.765  17.417  1.00 22.86 ? 167  TYR A CB    1 
ATOM   1290 C  CG    . TYR A 1 167 ? -7.409  -3.930  16.659  1.00 23.60 ? 167  TYR A CG    1 
ATOM   1291 C  CD1   . TYR A 1 167 ? -6.289  -4.606  17.112  1.00 26.60 ? 167  TYR A CD1   1 
ATOM   1292 C  CD2   . TYR A 1 167 ? -8.032  -4.398  15.527  1.00 24.05 ? 167  TYR A CD2   1 
ATOM   1293 C  CE1   . TYR A 1 167 ? -5.800  -5.723  16.447  1.00 27.03 ? 167  TYR A CE1   1 
ATOM   1294 C  CE2   . TYR A 1 167 ? -7.566  -5.514  14.861  1.00 24.92 ? 167  TYR A CE2   1 
ATOM   1295 C  CZ    . TYR A 1 167 ? -6.437  -6.168  15.303  1.00 26.44 ? 167  TYR A CZ    1 
ATOM   1296 O  OH    . TYR A 1 167 ? -6.011  -7.276  14.621  1.00 32.12 ? 167  TYR A OH    1 
ATOM   1297 N  N     . THR A 1 168 ? -10.803 -2.288  19.824  1.00 19.03 ? 168  THR A N     1 
ATOM   1298 C  CA    . THR A 1 168 ? -11.462 -1.428  20.862  1.00 19.48 ? 168  THR A CA    1 
ATOM   1299 C  C     . THR A 1 168 ? -11.649 -2.236  22.143  1.00 18.55 ? 168  THR A C     1 
ATOM   1300 O  O     . THR A 1 168 ? -11.343 -3.418  22.161  1.00 20.81 ? 168  THR A O     1 
ATOM   1301 C  CB    . THR A 1 168 ? -12.784 -0.808  20.373  1.00 18.32 ? 168  THR A CB    1 
ATOM   1302 O  OG1   . THR A 1 168 ? -13.898 -1.687  20.618  1.00 17.35 ? 168  THR A OG1   1 
ATOM   1303 C  CG2   . THR A 1 168 ? -12.709 -0.409  18.911  1.00 18.69 ? 168  THR A CG2   1 
ATOM   1304 N  N     . PRO A 1 169 ? -12.198 -1.651  23.233  1.00 19.40 ? 169  PRO A N     1 
ATOM   1305 C  CA    . PRO A 1 169 ? -12.495 -2.411  24.440  1.00 17.82 ? 169  PRO A CA    1 
ATOM   1306 C  C     . PRO A 1 169 ? -13.454 -3.570  24.163  1.00 18.53 ? 169  PRO A C     1 
ATOM   1307 O  O     . PRO A 1 169 ? -13.486 -4.487  24.977  1.00 17.55 ? 169  PRO A O     1 
ATOM   1308 C  CB    . PRO A 1 169 ? -13.113 -1.384  25.406  1.00 17.97 ? 169  PRO A CB    1 
ATOM   1309 C  CG    . PRO A 1 169 ? -12.584 -0.069  24.916  1.00 19.03 ? 169  PRO A CG    1 
ATOM   1310 C  CD    . PRO A 1 169 ? -12.455 -0.208  23.411  1.00 18.25 ? 169  PRO A CD    1 
ATOM   1311 N  N     . TYR A 1 170 ? -14.190 -3.525  23.049  1.00 16.76 ? 170  TYR A N     1 
ATOM   1312 C  CA    . TYR A 1 170 ? -15.118 -4.615  22.624  1.00 16.83 ? 170  TYR A CA    1 
ATOM   1313 C  C     . TYR A 1 170 ? -14.416 -5.586  21.644  1.00 16.97 ? 170  TYR A C     1 
ATOM   1314 O  O     . TYR A 1 170 ? -15.087 -6.216  20.808  1.00 16.42 ? 170  TYR A O     1 
ATOM   1315 C  CB    . TYR A 1 170 ? -16.406 -4.024  22.020  1.00 16.84 ? 170  TYR A CB    1 
ATOM   1316 C  CG    . TYR A 1 170 ? -17.421 -3.539  23.027  1.00 17.11 ? 170  TYR A CG    1 
ATOM   1317 C  CD1   . TYR A 1 170 ? -17.059 -2.679  24.071  1.00 16.96 ? 170  TYR A CD1   1 
ATOM   1318 C  CD2   . TYR A 1 170 ? -18.744 -3.920  22.929  1.00 15.96 ? 170  TYR A CD2   1 
ATOM   1319 C  CE1   . TYR A 1 170 ? -17.987 -2.252  25.009  1.00 18.53 ? 170  TYR A CE1   1 
ATOM   1320 C  CE2   . TYR A 1 170 ? -19.687 -3.476  23.846  1.00 17.09 ? 170  TYR A CE2   1 
ATOM   1321 C  CZ    . TYR A 1 170 ? -19.314 -2.630  24.884  1.00 18.31 ? 170  TYR A CZ    1 
ATOM   1322 O  OH    . TYR A 1 170 ? -20.252 -2.202  25.785  1.00 20.62 ? 170  TYR A OH    1 
ATOM   1323 N  N     . GLY A 1 171 ? -13.098 -5.731  21.743  1.00 16.75 ? 171  GLY A N     1 
ATOM   1324 C  CA    . GLY A 1 171 ? -12.286 -6.476  20.759  1.00 17.71 ? 171  GLY A CA    1 
ATOM   1325 C  C     . GLY A 1 171 ? -12.464 -7.991  20.795  1.00 17.04 ? 171  GLY A C     1 
ATOM   1326 O  O     . GLY A 1 171 ? -12.008 -8.617  19.826  1.00 17.52 ? 171  GLY A O     1 
ATOM   1327 N  N     . ASP A 1 172 ? -13.029 -8.583  21.855  1.00 15.94 ? 172  ASP A N     1 
ATOM   1328 C  CA    . ASP A 1 172 ? -13.312 -10.050 21.904  1.00 17.61 ? 172  ASP A CA    1 
ATOM   1329 C  C     . ASP A 1 172 ? -14.727 -10.261 21.354  1.00 17.00 ? 172  ASP A C     1 
ATOM   1330 O  O     . ASP A 1 172 ? -15.721 -10.165 22.133  1.00 15.54 ? 172  ASP A O     1 
ATOM   1331 C  CB    . ASP A 1 172 ? -13.080 -10.660 23.287  1.00 18.03 ? 172  ASP A CB    1 
ATOM   1332 C  CG    . ASP A 1 172 ? -13.277 -12.182 23.336  1.00 20.31 ? 172  ASP A CG    1 
ATOM   1333 O  OD1   . ASP A 1 172 ? -13.951 -12.736 22.447  1.00 20.37 ? 172  ASP A OD1   1 
ATOM   1334 O  OD2   . ASP A 1 172 ? -12.759 -12.809 24.270  1.00 20.25 ? 172  ASP A OD2   1 
ATOM   1335 N  N     . HIS A 1 173 ? -14.830 -10.453 20.028  1.00 17.36 ? 173  HIS A N     1 
ATOM   1336 C  CA    . HIS A 1 173 ? -16.136 -10.409 19.308  1.00 16.76 ? 173  HIS A CA    1 
ATOM   1337 C  C     . HIS A 1 173 ? -17.122 -11.413 19.901  1.00 16.30 ? 173  HIS A C     1 
ATOM   1338 O  O     . HIS A 1 173 ? -18.304 -11.032 20.140  1.00 17.54 ? 173  HIS A O     1 
ATOM   1339 C  CB    . HIS A 1 173 ? -15.936 -10.538 17.801  1.00 17.17 ? 173  HIS A CB    1 
ATOM   1340 C  CG    . HIS A 1 173 ? -15.244 -9.347  17.268  1.00 17.46 ? 173  HIS A CG    1 
ATOM   1341 N  ND1   . HIS A 1 173 ? -14.752 -9.311  16.021  1.00 16.05 ? 173  HIS A ND1   1 
ATOM   1342 C  CD2   . HIS A 1 173 ? -14.916 -8.162  17.853  1.00 18.19 ? 173  HIS A CD2   1 
ATOM   1343 C  CE1   . HIS A 1 173 ? -14.194 -8.135  15.807  1.00 16.74 ? 173  HIS A CE1   1 
ATOM   1344 N  NE2   . HIS A 1 173 ? -14.261 -7.412  16.921  1.00 16.96 ? 173  HIS A NE2   1 
ATOM   1345 N  N     . PHE A 1 174 ? -16.707 -12.657 20.141  1.00 16.39 ? 174  PHE A N     1 
ATOM   1346 C  CA    . PHE A 1 174 ? -17.650 -13.694 20.641  1.00 14.78 ? 174  PHE A CA    1 
ATOM   1347 C  C     . PHE A 1 174 ? -18.066 -13.382 22.093  1.00 14.93 ? 174  PHE A C     1 
ATOM   1348 O  O     . PHE A 1 174 ? -19.230 -13.690 22.450  1.00 14.11 ? 174  PHE A O     1 
ATOM   1349 C  CB    . PHE A 1 174 ? -17.120 -15.119 20.460  1.00 15.09 ? 174  PHE A CB    1 
ATOM   1350 C  CG    . PHE A 1 174 ? -18.250 -16.098 20.557  1.00 15.85 ? 174  PHE A CG    1 
ATOM   1351 C  CD1   . PHE A 1 174 ? -19.253 -16.089 19.597  1.00 16.86 ? 174  PHE A CD1   1 
ATOM   1352 C  CD2   . PHE A 1 174 ? -18.438 -16.856 21.700  1.00 16.36 ? 174  PHE A CD2   1 
ATOM   1353 C  CE1   . PHE A 1 174 ? -20.382 -16.886 19.740  1.00 16.94 ? 174  PHE A CE1   1 
ATOM   1354 C  CE2   . PHE A 1 174 ? -19.555 -17.666 21.837  1.00 17.80 ? 174  PHE A CE2   1 
ATOM   1355 C  CZ    . PHE A 1 174 ? -20.526 -17.681 20.860  1.00 17.74 ? 174  PHE A CZ    1 
ATOM   1356 N  N     . ALA A 1 175 ? -17.196 -12.771 22.920  1.00 13.97 ? 175  ALA A N     1 
ATOM   1357 C  CA    . ALA A 1 175 ? -17.536 -12.428 24.315  1.00 15.09 ? 175  ALA A CA    1 
ATOM   1358 C  C     . ALA A 1 175 ? -18.646 -11.376 24.312  1.00 16.88 ? 175  ALA A C     1 
ATOM   1359 O  O     . ALA A 1 175 ? -19.379 -11.331 25.297  1.00 18.17 ? 175  ALA A O     1 
ATOM   1360 C  CB    . ALA A 1 175 ? -16.334 -11.946 25.071  1.00 15.30 ? 175  ALA A CB    1 
ATOM   1361 N  N     . MET A 1 176 ? -18.720 -10.545 23.262  1.00 16.79 ? 176  MET A N     1 
ATOM   1362 C  CA    . MET A 1 176 ? -19.730 -9.476  23.119  1.00 18.02 ? 176  MET A CA    1 
ATOM   1363 C  C     . MET A 1 176 ? -21.020 -10.010 22.462  1.00 18.47 ? 176  MET A C     1 
ATOM   1364 O  O     . MET A 1 176 ? -21.973 -9.233  22.371  1.00 22.55 ? 176  MET A O     1 
ATOM   1365 C  CB    . MET A 1 176 ? -19.162 -8.302  22.313  1.00 18.14 ? 176  MET A CB    1 
ATOM   1366 C  CG    . MET A 1 176 ? -18.009 -7.566  22.973  1.00 18.72 ? 176  MET A CG    1 
ATOM   1367 S  SD    . MET A 1 176 ? -18.357 -6.881  24.641  1.00 21.74 ? 176  MET A SD    1 
ATOM   1368 C  CE    . MET A 1 176 ? -17.574 -8.106  25.692  1.00 21.07 ? 176  MET A CE    1 
ATOM   1369 N  N     . GLN A 1 177 ? -21.095 -11.284 22.081  1.00 17.29 ? 177  GLN A N     1 
ATOM   1370 C  CA    . GLN A 1 177 ? -22.314 -11.928 21.502  1.00 17.25 ? 177  GLN A CA    1 
ATOM   1371 C  C     . GLN A 1 177 ? -23.382 -12.132 22.588  1.00 17.28 ? 177  GLN A C     1 
ATOM   1372 O  O     . GLN A 1 177 ? -23.037 -12.365 23.758  1.00 16.66 ? 177  GLN A O     1 
ATOM   1373 C  CB    . GLN A 1 177 ? -21.962 -13.248 20.798  1.00 17.13 ? 177  GLN A CB    1 
ATOM   1374 C  CG    . GLN A 1 177 ? -23.138 -14.025 20.238  1.00 16.87 ? 177  GLN A CG    1 
ATOM   1375 C  CD    . GLN A 1 177 ? -23.713 -14.998 21.234  1.00 18.93 ? 177  GLN A CD    1 
ATOM   1376 O  OE1   . GLN A 1 177 ? -23.072 -15.380 22.216  1.00 21.80 ? 177  GLN A OE1   1 
ATOM   1377 N  NE2   . GLN A 1 177 ? -24.957 -15.396 21.013  1.00 20.68 ? 177  GLN A NE2   1 
ATOM   1378 N  N     . CYS A 1 178 ? -24.647 -12.047 22.205  1.00 16.66 ? 178  CYS A N     1 
ATOM   1379 C  CA    . CYS A 1 178 ? -25.795 -12.094 23.154  1.00 16.92 ? 178  CYS A CA    1 
ATOM   1380 C  C     . CYS A 1 178 ? -27.056 -12.468 22.380  1.00 16.13 ? 178  CYS A C     1 
ATOM   1381 O  O     . CYS A 1 178 ? -27.582 -11.640 21.643  1.00 17.89 ? 178  CYS A O     1 
ATOM   1382 C  CB    . CYS A 1 178 ? -25.939 -10.785 23.921  1.00 16.31 ? 178  CYS A CB    1 
ATOM   1383 S  SG    . CYS A 1 178 ? -27.069 -10.962 25.317  1.00 16.94 ? 178  CYS A SG    1 
ATOM   1384 N  N     . GLY A 1 179 ? -27.445 -13.731 22.486  1.00 16.90 ? 179  GLY A N     1 
ATOM   1385 C  CA    . GLY A 1 179 ? -28.585 -14.320 21.774  1.00 16.13 ? 179  GLY A CA    1 
ATOM   1386 C  C     . GLY A 1 179 ? -28.218 -14.752 20.368  1.00 16.21 ? 179  GLY A C     1 
ATOM   1387 O  O     . GLY A 1 179 ? -27.514 -14.009 19.623  1.00 15.37 ? 179  GLY A O     1 
ATOM   1388 N  N     . MET A 1 180 ? -28.682 -15.922 19.982  1.00 17.67 ? 180  MET A N     1 
ATOM   1389 C  CA    . MET A 1 180 ? -28.568 -16.351 18.570  1.00 19.41 ? 180  MET A CA    1 
ATOM   1390 C  C     . MET A 1 180 ? -29.759 -17.238 18.201  1.00 18.22 ? 180  MET A C     1 
ATOM   1391 O  O     . MET A 1 180 ? -30.397 -17.807 19.089  1.00 17.23 ? 180  MET A O     1 
ATOM   1392 C  CB    . MET A 1 180 ? -27.235 -17.062 18.303  1.00 18.22 ? 180  MET A CB    1 
ATOM   1393 C  CG    . MET A 1 180 ? -27.017 -18.271 19.163  1.00 18.66 ? 180  MET A CG    1 
ATOM   1394 S  SD    . MET A 1 180 ? -25.588 -19.270 18.586  1.00 18.39 ? 180  MET A SD    1 
ATOM   1395 C  CE    . MET A 1 180 ? -24.259 -18.088 18.799  1.00 17.73 ? 180  MET A CE    1 
ATOM   1396 N  N     . GLU A 1 181 ? -30.066 -17.251 16.914  1.00 17.27 ? 181  GLU A N     1 
ATOM   1397 C  CA    . GLU A 1 181 ? -30.980 -18.223 16.300  1.00 17.63 ? 181  GLU A CA    1 
ATOM   1398 C  C     . GLU A 1 181 ? -30.093 -19.185 15.525  1.00 17.24 ? 181  GLU A C     1 
ATOM   1399 O  O     . GLU A 1 181 ? -29.190 -18.718 14.816  1.00 17.62 ? 181  GLU A O     1 
ATOM   1400 C  CB    . GLU A 1 181 ? -32.003 -17.527 15.406  1.00 18.35 ? 181  GLU A CB    1 
ATOM   1401 C  CG    . GLU A 1 181 ? -33.042 -18.453 14.792  1.00 19.67 ? 181  GLU A CG    1 
ATOM   1402 C  CD    . GLU A 1 181 ? -33.997 -17.703 13.867  1.00 21.97 ? 181  GLU A CD    1 
ATOM   1403 O  OE1   . GLU A 1 181 ? -35.052 -17.246 14.381  1.00 24.19 ? 181  GLU A OE1   1 
ATOM   1404 O  OE2   . GLU A 1 181 ? -33.629 -17.453 12.661  1.00 23.75 ? 181  GLU A OE2   1 
ATOM   1405 N  N     . VAL A 1 182 ? -30.392 -20.471 15.653  1.00 17.18 ? 182  VAL A N     1 
ATOM   1406 C  CA    . VAL A 1 182 ? -29.627 -21.568 15.035  1.00 19.12 ? 182  VAL A CA    1 
ATOM   1407 C  C     . VAL A 1 182 ? -30.611 -22.487 14.333  1.00 19.90 ? 182  VAL A C     1 
ATOM   1408 O  O     . VAL A 1 182 ? -31.584 -22.937 14.988  1.00 22.98 ? 182  VAL A O     1 
ATOM   1409 C  CB    . VAL A 1 182 ? -28.815 -22.354 16.082  1.00 20.93 ? 182  VAL A CB    1 
ATOM   1410 C  CG1   . VAL A 1 182 ? -27.938 -23.402 15.402  1.00 22.49 ? 182  VAL A CG1   1 
ATOM   1411 C  CG2   . VAL A 1 182 ? -27.962 -21.431 16.954  1.00 20.91 ? 182  VAL A CG2   1 
ATOM   1412 N  N     . VAL A 1 183 ? -30.297 -22.825 13.089  1.00 18.20 ? 183  VAL A N     1 
ATOM   1413 C  CA    . VAL A 1 183 ? -30.860 -24.011 12.397  1.00 17.81 ? 183  VAL A CA    1 
ATOM   1414 C  C     . VAL A 1 183 ? -29.979 -25.202 12.749  1.00 17.21 ? 183  VAL A C     1 
ATOM   1415 O  O     . VAL A 1 183 ? -28.774 -25.215 12.374  1.00 17.81 ? 183  VAL A O     1 
ATOM   1416 C  CB    . VAL A 1 183 ? -30.957 -23.794 10.875  1.00 17.71 ? 183  VAL A CB    1 
ATOM   1417 C  CG1   . VAL A 1 183 ? -31.492 -25.031 10.154  1.00 18.55 ? 183  VAL A CG1   1 
ATOM   1418 C  CG2   . VAL A 1 183 ? -31.806 -22.582 10.554  1.00 17.53 ? 183  VAL A CG2   1 
ATOM   1419 N  N     . LEU A 1 184 ? -30.557 -26.191 13.414  1.00 17.50 ? 184  LEU A N     1 
ATOM   1420 C  CA    . LEU A 1 184 ? -29.845 -27.430 13.819  1.00 18.64 ? 184  LEU A CA    1 
ATOM   1421 C  C     . LEU A 1 184 ? -29.702 -28.321 12.593  1.00 21.47 ? 184  LEU A C     1 
ATOM   1422 O  O     . LEU A 1 184 ? -30.329 -28.070 11.549  1.00 21.49 ? 184  LEU A O     1 
ATOM   1423 C  CB    . LEU A 1 184 ? -30.610 -28.107 14.964  1.00 20.06 ? 184  LEU A CB    1 
ATOM   1424 C  CG    . LEU A 1 184 ? -30.681 -27.287 16.255  1.00 20.32 ? 184  LEU A CG    1 
ATOM   1425 C  CD1   . LEU A 1 184 ? -31.640 -27.900 17.267  1.00 23.11 ? 184  LEU A CD1   1 
ATOM   1426 C  CD2   . LEU A 1 184 ? -29.292 -27.178 16.846  1.00 21.97 ? 184  LEU A CD2   1 
ATOM   1427 N  N     . PRO A 1 185 ? -28.829 -29.348 12.663  1.00 21.87 ? 185  PRO A N     1 
ATOM   1428 C  CA    . PRO A 1 185 ? -28.528 -30.171 11.496  1.00 21.76 ? 185  PRO A CA    1 
ATOM   1429 C  C     . PRO A 1 185 ? -29.743 -30.974 11.027  1.00 22.17 ? 185  PRO A C     1 
ATOM   1430 O  O     . PRO A 1 185 ? -29.640 -31.524 9.949   1.00 23.39 ? 185  PRO A O     1 
ATOM   1431 C  CB    . PRO A 1 185 ? -27.421 -31.117 11.964  1.00 22.58 ? 185  PRO A CB    1 
ATOM   1432 C  CG    . PRO A 1 185 ? -26.835 -30.414 13.188  1.00 23.69 ? 185  PRO A CG    1 
ATOM   1433 C  CD    . PRO A 1 185 ? -28.015 -29.718 13.831  1.00 22.63 ? 185  PRO A CD    1 
ATOM   1434 N  N     . ASN A 1 186 ? -30.820 -31.042 11.802  1.00 20.97 ? 186  ASN A N     1 
ATOM   1435 C  CA    . ASN A 1 186 ? -32.078 -31.694 11.343  1.00 23.56 ? 186  ASN A CA    1 
ATOM   1436 C  C     . ASN A 1 186 ? -32.974 -30.687 10.609  1.00 24.13 ? 186  ASN A C     1 
ATOM   1437 O  O     . ASN A 1 186 ? -34.009 -31.105 10.106  1.00 25.32 ? 186  ASN A O     1 
ATOM   1438 C  CB    . ASN A 1 186 ? -32.896 -32.353 12.453  1.00 24.24 ? 186  ASN A CB    1 
ATOM   1439 C  CG    . ASN A 1 186 ? -33.349 -31.396 13.533  1.00 25.97 ? 186  ASN A CG    1 
ATOM   1440 O  OD1   . ASN A 1 186 ? -33.081 -30.202 13.494  1.00 26.39 ? 186  ASN A OD1   1 
ATOM   1441 N  ND2   . ASN A 1 186 ? -33.998 -31.928 14.542  1.00 28.87 ? 186  ASN A ND2   1 
ATOM   1442 N  N     . GLY A 1 187 ? -32.611 -29.410 10.554  1.00 23.40 ? 187  GLY A N     1 
ATOM   1443 C  CA    . GLY A 1 187 ? -33.412 -28.399 9.841   1.00 24.01 ? 187  GLY A CA    1 
ATOM   1444 C  C     . GLY A 1 187 ? -34.403 -27.656 10.727  1.00 24.07 ? 187  GLY A C     1 
ATOM   1445 O  O     . GLY A 1 187 ? -35.079 -26.738 10.180  1.00 27.03 ? 187  GLY A O     1 
ATOM   1446 N  N     . GLU A 1 188 ? -34.483 -27.998 12.017  1.00 22.92 ? 188  GLU A N     1 
ATOM   1447 C  CA    . GLU A 1 188 ? -35.366 -27.319 13.014  1.00 24.42 ? 188  GLU A CA    1 
ATOM   1448 C  C     . GLU A 1 188 ? -34.658 -26.084 13.580  1.00 23.99 ? 188  GLU A C     1 
ATOM   1449 O  O     . GLU A 1 188 ? -33.425 -26.045 13.584  1.00 24.02 ? 188  GLU A O     1 
ATOM   1450 C  CB    . GLU A 1 188 ? -35.723 -28.257 14.166  1.00 27.02 ? 188  GLU A CB    1 
ATOM   1451 C  CG    . GLU A 1 188 ? -36.572 -29.450 13.739  1.00 30.25 ? 188  GLU A CG    1 
ATOM   1452 C  CD    . GLU A 1 188 ? -37.932 -29.062 13.221  1.00 31.62 ? 188  GLU A CD    1 
ATOM   1453 O  OE1   . GLU A 1 188 ? -38.770 -28.683 14.053  1.00 41.05 ? 188  GLU A OE1   1 
ATOM   1454 O  OE2   . GLU A 1 188 ? -38.112 -29.040 11.994  1.00 38.95 ? 188  GLU A OE2   1 
ATOM   1455 N  N     . VAL A 1 189 ? -35.410 -25.116 14.086  1.00 22.38 ? 189  VAL A N     1 
ATOM   1456 C  CA    . VAL A 1 189 ? -34.850 -23.814 14.492  1.00 23.40 ? 189  VAL A CA    1 
ATOM   1457 C  C     . VAL A 1 189 ? -34.978 -23.641 16.003  1.00 23.34 ? 189  VAL A C     1 
ATOM   1458 O  O     . VAL A 1 189 ? -35.944 -24.120 16.603  1.00 25.96 ? 189  VAL A O     1 
ATOM   1459 C  CB    . VAL A 1 189 ? -35.426 -22.673 13.635  1.00 25.85 ? 189  VAL A CB    1 
ATOM   1460 C  CG1   . VAL A 1 189 ? -36.919 -22.463 13.783  1.00 28.92 ? 189  VAL A CG1   1 
ATOM   1461 C  CG2   . VAL A 1 189 ? -34.667 -21.389 13.892  1.00 27.18 ? 189  VAL A CG2   1 
ATOM   1462 N  N     . VAL A 1 190 ? -33.970 -23.030 16.615  1.00 22.93 ? 190  VAL A N     1 
ATOM   1463 C  CA    . VAL A 1 190 ? -33.913 -22.816 18.083  1.00 23.92 ? 190  VAL A CA    1 
ATOM   1464 C  C     . VAL A 1 190 ? -33.386 -21.403 18.318  1.00 23.05 ? 190  VAL A C     1 
ATOM   1465 O  O     . VAL A 1 190 ? -32.607 -20.859 17.465  1.00 20.70 ? 190  VAL A O     1 
ATOM   1466 C  CB    . VAL A 1 190 ? -33.069 -23.923 18.767  1.00 27.32 ? 190  VAL A CB    1 
ATOM   1467 C  CG1   . VAL A 1 190 ? -31.608 -23.837 18.376  1.00 28.49 ? 190  VAL A CG1   1 
ATOM   1468 C  CG2   . VAL A 1 190 ? -33.182 -23.890 20.282  1.00 29.44 ? 190  VAL A CG2   1 
ATOM   1469 N  N     . ARG A 1 191 ? -33.826 -20.781 19.405  1.00 21.46 ? 191  ARG A N     1 
ATOM   1470 C  CA    . ARG A 1 191 ? -33.195 -19.525 19.867  1.00 20.57 ? 191  ARG A CA    1 
ATOM   1471 C  C     . ARG A 1 191 ? -32.637 -19.739 21.278  1.00 20.97 ? 191  ARG A C     1 
ATOM   1472 O  O     . ARG A 1 191 ? -33.324 -20.350 22.145  1.00 24.32 ? 191  ARG A O     1 
ATOM   1473 C  CB    . ARG A 1 191 ? -34.204 -18.380 19.809  1.00 21.38 ? 191  ARG A CB    1 
ATOM   1474 C  CG    . ARG A 1 191 ? -34.638 -18.041 18.394  1.00 22.42 ? 191  ARG A CG    1 
ATOM   1475 C  CD    . ARG A 1 191 ? -35.699 -16.954 18.359  1.00 23.18 ? 191  ARG A CD    1 
ATOM   1476 N  NE    . ARG A 1 191 ? -35.891 -16.521 16.984  1.00 25.41 ? 191  ARG A NE    1 
ATOM   1477 C  CZ    . ARG A 1 191 ? -36.632 -15.480 16.605  1.00 27.17 ? 191  ARG A CZ    1 
ATOM   1478 N  NH1   . ARG A 1 191 ? -37.210 -14.705 17.510  1.00 29.52 ? 191  ARG A NH1   1 
ATOM   1479 N  NH2   . ARG A 1 191 ? -36.697 -15.158 15.329  1.00 25.93 ? 191  ARG A NH2   1 
ATOM   1480 N  N     . THR A 1 192 ? -31.476 -19.156 21.537  1.00 19.02 ? 192  THR A N     1 
ATOM   1481 C  CA    . THR A 1 192 ? -30.788 -19.244 22.851  1.00 18.79 ? 192  THR A CA    1 
ATOM   1482 C  C     . THR A 1 192 ? -31.223 -18.087 23.762  1.00 19.51 ? 192  THR A C     1 
ATOM   1483 O  O     . THR A 1 192 ? -31.768 -17.084 23.230  1.00 17.39 ? 192  THR A O     1 
ATOM   1484 C  CB    . THR A 1 192 ? -29.279 -19.213 22.644  1.00 16.77 ? 192  THR A CB    1 
ATOM   1485 O  OG1   . THR A 1 192 ? -28.984 -17.906 22.151  1.00 16.85 ? 192  THR A OG1   1 
ATOM   1486 C  CG2   . THR A 1 192 ? -28.842 -20.292 21.686  1.00 17.78 ? 192  THR A CG2   1 
ATOM   1487 N  N     . GLY A 1 193 ? -30.939 -18.227 25.063  1.00 19.65 ? 193  GLY A N     1 
ATOM   1488 C  CA    . GLY A 1 193 ? -31.048 -17.158 26.065  1.00 20.55 ? 193  GLY A CA    1 
ATOM   1489 C  C     . GLY A 1 193 ? -32.499 -16.730 26.217  1.00 21.40 ? 193  GLY A C     1 
ATOM   1490 O  O     . GLY A 1 193 ? -33.360 -17.603 26.238  1.00 21.25 ? 193  GLY A O     1 
ATOM   1491 N  N     . MET A 1 194 ? -32.753 -15.427 26.341  1.00 20.92 ? 194  MET A N     1 
ATOM   1492 C  CA    . MET A 1 194 ? -34.117 -14.872 26.563  1.00 21.33 ? 194  MET A CA    1 
ATOM   1493 C  C     . MET A 1 194 ? -34.918 -14.996 25.255  1.00 20.37 ? 194  MET A C     1 
ATOM   1494 O  O     . MET A 1 194 ? -36.142 -14.967 25.310  1.00 18.93 ? 194  MET A O     1 
ATOM   1495 C  CB    . MET A 1 194 ? -34.028 -13.419 27.034  1.00 22.09 ? 194  MET A CB    1 
ATOM   1496 C  CG    . MET A 1 194 ? -33.180 -13.247 28.302  1.00 23.55 ? 194  MET A CG    1 
ATOM   1497 S  SD    . MET A 1 194 ? -33.655 -14.312 29.701  1.00 25.67 ? 194  MET A SD    1 
ATOM   1498 C  CE    . MET A 1 194 ? -35.411 -14.043 29.841  1.00 27.44 ? 194  MET A CE    1 
ATOM   1499 N  N     . GLY A 1 195 ? -34.255 -15.261 24.124  1.00 19.76 ? 195  GLY A N     1 
ATOM   1500 C  CA    . GLY A 1 195 ? -34.939 -15.516 22.840  1.00 20.76 ? 195  GLY A CA    1 
ATOM   1501 C  C     . GLY A 1 195 ? -35.878 -16.719 22.920  1.00 21.89 ? 195  GLY A C     1 
ATOM   1502 O  O     . GLY A 1 195 ? -36.850 -16.775 22.154  1.00 21.56 ? 195  GLY A O     1 
ATOM   1503 N  N     . ALA A 1 196 ? -35.637 -17.663 23.829  1.00 22.78 ? 196  ALA A N     1 
ATOM   1504 C  CA    . ALA A 1 196 ? -36.531 -18.825 24.008  1.00 21.17 ? 196  ALA A CA    1 
ATOM   1505 C  C     . ALA A 1 196 ? -37.859 -18.383 24.641  1.00 22.37 ? 196  ALA A C     1 
ATOM   1506 O  O     . ALA A 1 196 ? -38.826 -19.173 24.575  1.00 21.85 ? 196  ALA A O     1 
ATOM   1507 C  CB    . ALA A 1 196 ? -35.831 -19.875 24.826  1.00 21.14 ? 196  ALA A CB    1 
ATOM   1508 N  N     . MET A 1 197 ? -37.924 -17.181 25.224  1.00 22.04 ? 197  MET A N     1 
ATOM   1509 C  CA    . MET A 1 197 ? -39.156 -16.703 25.905  1.00 24.82 ? 197  MET A CA    1 
ATOM   1510 C  C     . MET A 1 197 ? -39.993 -15.881 24.941  1.00 22.99 ? 197  MET A C     1 
ATOM   1511 O  O     . MET A 1 197 ? -39.589 -14.766 24.607  1.00 23.68 ? 197  MET A O     1 
ATOM   1512 C  CB    . MET A 1 197 ? -38.864 -15.814 27.119  1.00 25.93 ? 197  MET A CB    1 
ATOM   1513 C  CG    . MET A 1 197 ? -40.133 -15.138 27.618  1.00 28.63 ? 197  MET A CG    1 
ATOM   1514 S  SD    . MET A 1 197 ? -40.049 -14.630 29.306  1.00 32.25 ? 197  MET A SD    1 
ATOM   1515 C  CE    . MET A 1 197 ? -40.708 -16.097 30.088  1.00 29.75 ? 197  MET A CE    1 
ATOM   1516 N  N     . PRO A 1 198 ? -41.222 -16.314 24.588  1.00 24.38 ? 198  PRO A N     1 
ATOM   1517 C  CA    . PRO A 1 198 ? -42.076 -15.535 23.687  1.00 26.42 ? 198  PRO A CA    1 
ATOM   1518 C  C     . PRO A 1 198 ? -42.406 -14.187 24.350  1.00 25.35 ? 198  PRO A C     1 
ATOM   1519 O  O     . PRO A 1 198 ? -42.750 -14.191 25.518  1.00 24.71 ? 198  PRO A O     1 
ATOM   1520 C  CB    . PRO A 1 198 ? -43.375 -16.351 23.551  1.00 26.70 ? 198  PRO A CB    1 
ATOM   1521 C  CG    . PRO A 1 198 ? -43.071 -17.704 24.170  1.00 26.86 ? 198  PRO A CG    1 
ATOM   1522 C  CD    . PRO A 1 198 ? -41.940 -17.466 25.154  1.00 27.86 ? 198  PRO A CD    1 
ATOM   1523 N  N     . GLY A 1 199 ? -42.274 -13.095 23.609  1.00 25.88 ? 199  GLY A N     1 
ATOM   1524 C  CA    . GLY A 1 199 ? -42.619 -11.729 24.050  1.00 25.20 ? 199  GLY A CA    1 
ATOM   1525 C  C     . GLY A 1 199 ? -41.484 -11.052 24.817  1.00 26.42 ? 199  GLY A C     1 
ATOM   1526 O  O     . GLY A 1 199 ? -41.702 -9.934  25.331  1.00 21.61 ? 199  GLY A O     1 
ATOM   1527 N  N     . ASN A 1 200 ? -40.299 -11.671 24.881  1.00 23.98 ? 200  ASN A N     1 
ATOM   1528 C  CA    . ASN A 1 200 ? -39.156 -11.082 25.625  1.00 24.29 ? 200  ASN A CA    1 
ATOM   1529 C  C     . ASN A 1 200 ? -38.749 -9.793  24.927  1.00 22.02 ? 200  ASN A C     1 
ATOM   1530 O  O     . ASN A 1 200 ? -38.924 -9.716  23.721  1.00 22.03 ? 200  ASN A O     1 
ATOM   1531 C  CB    . ASN A 1 200 ? -37.939 -12.010 25.676  1.00 23.87 ? 200  ASN A CB    1 
ATOM   1532 C  CG    . ASN A 1 200 ? -37.217 -12.001 24.346  1.00 23.48 ? 200  ASN A CG    1 
ATOM   1533 O  OD1   . ASN A 1 200 ? -36.313 -11.182 24.133  1.00 20.83 ? 200  ASN A OD1   1 
ATOM   1534 N  ND2   . ASN A 1 200 ? -37.687 -12.841 23.424  1.00 22.59 ? 200  ASN A ND2   1 
ATOM   1535 N  N     . ASN A 1 201 ? -38.123 -8.874  25.646  1.00 23.57 ? 201  ASN A N     1 
ATOM   1536 C  CA    . ASN A 1 201 ? -37.415 -7.705  25.048  1.00 22.19 ? 201  ASN A CA    1 
ATOM   1537 C  C     . ASN A 1 201 ? -35.959 -7.743  25.528  1.00 21.78 ? 201  ASN A C     1 
ATOM   1538 O  O     . ASN A 1 201 ? -35.339 -6.681  25.642  1.00 20.95 ? 201  ASN A O     1 
ATOM   1539 C  CB    . ASN A 1 201 ? -38.161 -6.403  25.378  1.00 23.87 ? 201  ASN A CB    1 
ATOM   1540 C  CG    . ASN A 1 201 ? -39.470 -6.286  24.615  1.00 25.43 ? 201  ASN A CG    1 
ATOM   1541 O  OD1   . ASN A 1 201 ? -40.548 -6.547  25.148  1.00 27.68 ? 201  ASN A OD1   1 
ATOM   1542 N  ND2   . ASN A 1 201 ? -39.380 -6.026  23.329  1.00 23.63 ? 201  ASN A ND2   1 
ATOM   1543 N  N     . THR A 1 202 ? -35.431 -8.928  25.844  1.00 20.24 ? 202  THR A N     1 
ATOM   1544 C  CA    . THR A 1 202 ? -34.160 -9.064  26.603  1.00 20.99 ? 202  THR A CA    1 
ATOM   1545 C  C     . THR A 1 202 ? -33.167 -10.003 25.895  1.00 21.70 ? 202  THR A C     1 
ATOM   1546 O  O     . THR A 1 202 ? -32.091 -10.229 26.474  1.00 21.03 ? 202  THR A O     1 
ATOM   1547 C  CB    . THR A 1 202 ? -34.477 -9.555  28.018  1.00 21.61 ? 202  THR A CB    1 
ATOM   1548 O  OG1   . THR A 1 202 ? -35.389 -10.648 27.867  1.00 20.10 ? 202  THR A OG1   1 
ATOM   1549 C  CG2   . THR A 1 202 ? -35.050 -8.450  28.895  1.00 20.18 ? 202  THR A CG2   1 
ATOM   1550 N  N     . TRP A 1 203 ? -33.497 -10.509 24.700  1.00 19.65 ? 203  TRP A N     1 
ATOM   1551 C  CA    . TRP A 1 203 ? -32.626 -11.412 23.900  1.00 19.68 ? 203  TRP A CA    1 
ATOM   1552 C  C     . TRP A 1 203 ? -31.202 -10.858 23.811  1.00 19.60 ? 203  TRP A C     1 
ATOM   1553 O  O     . TRP A 1 203 ? -30.256 -11.653 23.929  1.00 19.06 ? 203  TRP A O     1 
ATOM   1554 C  CB    . TRP A 1 203 ? -33.206 -11.622 22.505  1.00 19.56 ? 203  TRP A CB    1 
ATOM   1555 C  CG    . TRP A 1 203 ? -32.741 -12.858 21.803  1.00 18.86 ? 203  TRP A CG    1 
ATOM   1556 C  CD1   . TRP A 1 203 ? -32.063 -13.925 22.328  1.00 19.36 ? 203  TRP A CD1   1 
ATOM   1557 C  CD2   . TRP A 1 203 ? -32.979 -13.169 20.416  1.00 17.94 ? 203  TRP A CD2   1 
ATOM   1558 N  NE1   . TRP A 1 203 ? -31.882 -14.883 21.361  1.00 18.11 ? 203  TRP A NE1   1 
ATOM   1559 C  CE2   . TRP A 1 203 ? -32.408 -14.440 20.174  1.00 18.48 ? 203  TRP A CE2   1 
ATOM   1560 C  CE3   . TRP A 1 203 ? -33.620 -12.502 19.364  1.00 18.05 ? 203  TRP A CE3   1 
ATOM   1561 C  CZ2   . TRP A 1 203 ? -32.475 -15.063 18.922  1.00 17.94 ? 203  TRP A CZ2   1 
ATOM   1562 C  CZ3   . TRP A 1 203 ? -33.698 -13.120 18.128  1.00 19.29 ? 203  TRP A CZ3   1 
ATOM   1563 C  CH2   . TRP A 1 203 ? -33.122 -14.378 17.915  1.00 19.14 ? 203  TRP A CH2   1 
ATOM   1564 N  N     . GLN A 1 204 ? -31.059 -9.542  23.646  1.00 18.55 ? 204  GLN A N     1 
ATOM   1565 C  CA    . GLN A 1 204 ? -29.740 -8.894  23.506  1.00 18.73 ? 204  GLN A CA    1 
ATOM   1566 C  C     . GLN A 1 204 ? -29.292 -8.207  24.805  1.00 18.04 ? 204  GLN A C     1 
ATOM   1567 O  O     . GLN A 1 204 ? -28.288 -7.484  24.742  1.00 18.08 ? 204  GLN A O     1 
ATOM   1568 C  CB    . GLN A 1 204 ? -29.752 -7.960  22.304  1.00 18.66 ? 204  GLN A CB    1 
ATOM   1569 C  CG    . GLN A 1 204 ? -29.364 -8.671  21.016  1.00 19.44 ? 204  GLN A CG    1 
ATOM   1570 C  CD    . GLN A 1 204 ? -30.413 -9.639  20.536  1.00 18.71 ? 204  GLN A CD    1 
ATOM   1571 O  OE1   . GLN A 1 204 ? -31.480 -9.249  20.098  1.00 20.41 ? 204  GLN A OE1   1 
ATOM   1572 N  NE2   . GLN A 1 204 ? -30.115 -10.927 20.584  1.00 20.43 ? 204  GLN A NE2   1 
ATOM   1573 N  N     . LEU A 1 205 ? -29.927 -8.468  25.948  1.00 18.42 ? 205  LEU A N     1 
ATOM   1574 C  CA    . LEU A 1 205 ? -29.600 -7.751  27.209  1.00 20.16 ? 205  LEU A CA    1 
ATOM   1575 C  C     . LEU A 1 205 ? -29.007 -8.713  28.261  1.00 20.70 ? 205  LEU A C     1 
ATOM   1576 O  O     . LEU A 1 205 ? -28.348 -8.206  29.176  1.00 21.30 ? 205  LEU A O     1 
ATOM   1577 C  CB    . LEU A 1 205 ? -30.851 -7.056  27.775  1.00 21.34 ? 205  LEU A CB    1 
ATOM   1578 C  CG    . LEU A 1 205 ? -31.591 -6.084  26.853  1.00 20.39 ? 205  LEU A CG    1 
ATOM   1579 C  CD1   . LEU A 1 205 ? -32.728 -5.420  27.616  1.00 20.87 ? 205  LEU A CD1   1 
ATOM   1580 C  CD2   . LEU A 1 205 ? -30.663 -5.033  26.279  1.00 20.88 ? 205  LEU A CD2   1 
ATOM   1581 N  N     . PHE A 1 206 ? -29.209 -10.020 28.130  1.00 17.74 ? 206  PHE A N     1 
ATOM   1582 C  CA    . PHE A 1 206 ? -28.835 -11.030 29.138  1.00 18.35 ? 206  PHE A CA    1 
ATOM   1583 C  C     . PHE A 1 206 ? -28.464 -12.322 28.400  1.00 18.63 ? 206  PHE A C     1 
ATOM   1584 O  O     . PHE A 1 206 ? -29.351 -12.903 27.718  1.00 18.62 ? 206  PHE A O     1 
ATOM   1585 C  CB    . PHE A 1 206 ? -30.000 -11.250 30.100  1.00 19.22 ? 206  PHE A CB    1 
ATOM   1586 C  CG    . PHE A 1 206 ? -29.667 -12.136 31.263  1.00 18.98 ? 206  PHE A CG    1 
ATOM   1587 C  CD1   . PHE A 1 206 ? -28.738 -11.734 32.200  1.00 19.69 ? 206  PHE A CD1   1 
ATOM   1588 C  CD2   . PHE A 1 206 ? -30.287 -13.373 31.430  1.00 21.52 ? 206  PHE A CD2   1 
ATOM   1589 C  CE1   . PHE A 1 206 ? -28.436 -12.535 33.291  1.00 19.30 ? 206  PHE A CE1   1 
ATOM   1590 C  CE2   . PHE A 1 206 ? -29.969 -14.185 32.515  1.00 19.96 ? 206  PHE A CE2   1 
ATOM   1591 C  CZ    . PHE A 1 206 ? -29.031 -13.770 33.431  1.00 19.92 ? 206  PHE A CZ    1 
ATOM   1592 N  N     . LYS A 1 207 ? -27.200 -12.728 28.487  1.00 17.56 ? 207  LYS A N     1 
ATOM   1593 C  CA    . LYS A 1 207 ? -26.634 -13.873 27.739  1.00 18.65 ? 207  LYS A CA    1 
ATOM   1594 C  C     . LYS A 1 207 ? -27.285 -15.206 28.126  1.00 19.20 ? 207  LYS A C     1 
ATOM   1595 O  O     . LYS A 1 207 ? -27.611 -15.995 27.208  1.00 19.31 ? 207  LYS A O     1 
ATOM   1596 C  CB    . LYS A 1 207 ? -25.140 -13.998 28.032  1.00 18.82 ? 207  LYS A CB    1 
ATOM   1597 C  CG    . LYS A 1 207 ? -24.240 -12.964 27.381  1.00 20.70 ? 207  LYS A CG    1 
ATOM   1598 C  CD    . LYS A 1 207 ? -22.815 -13.105 27.864  1.00 22.19 ? 207  LYS A CD    1 
ATOM   1599 C  CE    . LYS A 1 207 ? -21.807 -12.392 26.982  1.00 23.79 ? 207  LYS A CE    1 
ATOM   1600 N  NZ    . LYS A 1 207 ? -21.433 -13.207 25.808  1.00 23.96 ? 207  LYS A NZ    1 
ATOM   1601 N  N     . TYR A 1 208 ? -27.408 -15.502 29.416  1.00 19.66 ? 208  TYR A N     1 
ATOM   1602 C  CA    . TYR A 1 208 ? -27.623 -16.898 29.860  1.00 20.40 ? 208  TYR A CA    1 
ATOM   1603 C  C     . TYR A 1 208 ? -29.028 -17.399 29.529  1.00 21.60 ? 208  TYR A C     1 
ATOM   1604 O  O     . TYR A 1 208 ? -29.186 -18.589 29.116  1.00 18.93 ? 208  TYR A O     1 
ATOM   1605 C  CB    . TYR A 1 208 ? -27.395 -17.076 31.354  1.00 21.48 ? 208  TYR A CB    1 
ATOM   1606 C  CG    . TYR A 1 208 ? -26.013 -16.716 31.830  1.00 21.37 ? 208  TYR A CG    1 
ATOM   1607 C  CD1   . TYR A 1 208 ? -24.889 -17.069 31.115  1.00 20.60 ? 208  TYR A CD1   1 
ATOM   1608 C  CD2   . TYR A 1 208 ? -25.841 -16.038 33.021  1.00 20.26 ? 208  TYR A CD2   1 
ATOM   1609 C  CE1   . TYR A 1 208 ? -23.624 -16.732 31.565  1.00 22.84 ? 208  TYR A CE1   1 
ATOM   1610 C  CE2   . TYR A 1 208 ? -24.584 -15.681 33.479  1.00 21.06 ? 208  TYR A CE2   1 
ATOM   1611 C  CZ    . TYR A 1 208 ? -23.459 -16.042 32.758  1.00 22.42 ? 208  TYR A CZ    1 
ATOM   1612 O  OH    . TYR A 1 208 ? -22.211 -15.697 33.201  1.00 20.59 ? 208  TYR A OH    1 
ATOM   1613 N  N     . GLY A 1 209 ? -30.032 -16.558 29.752  1.00 21.69 ? 209  GLY A N     1 
ATOM   1614 C  CA    . GLY A 1 209 ? -31.396 -17.085 29.915  1.00 21.81 ? 209  GLY A CA    1 
ATOM   1615 C  C     . GLY A 1 209 ? -31.385 -18.052 31.083  1.00 21.10 ? 209  GLY A C     1 
ATOM   1616 O  O     . GLY A 1 209 ? -30.759 -17.709 32.103  1.00 21.23 ? 209  GLY A O     1 
ATOM   1617 N  N     . TYR A 1 210 ? -31.989 -19.227 30.931  1.00 18.96 ? 210  TYR A N     1 
ATOM   1618 C  CA    . TYR A 1 210 ? -32.151 -20.210 32.027  1.00 20.16 ? 210  TYR A CA    1 
ATOM   1619 C  C     . TYR A 1 210 ? -31.598 -21.551 31.549  1.00 19.16 ? 210  TYR A C     1 
ATOM   1620 O  O     . TYR A 1 210 ? -31.747 -21.893 30.364  1.00 20.90 ? 210  TYR A O     1 
ATOM   1621 C  CB    . TYR A 1 210 ? -33.616 -20.271 32.482  1.00 19.95 ? 210  TYR A CB    1 
ATOM   1622 C  CG    . TYR A 1 210 ? -33.985 -21.383 33.446  1.00 19.52 ? 210  TYR A CG    1 
ATOM   1623 C  CD1   . TYR A 1 210 ? -33.534 -21.407 34.755  1.00 20.72 ? 210  TYR A CD1   1 
ATOM   1624 C  CD2   . TYR A 1 210 ? -34.786 -22.432 33.032  1.00 20.67 ? 210  TYR A CD2   1 
ATOM   1625 C  CE1   . TYR A 1 210 ? -33.895 -22.426 35.627  1.00 21.49 ? 210  TYR A CE1   1 
ATOM   1626 C  CE2   . TYR A 1 210 ? -35.137 -23.474 33.873  1.00 20.85 ? 210  TYR A CE2   1 
ATOM   1627 C  CZ    . TYR A 1 210 ? -34.706 -23.460 35.182  1.00 20.68 ? 210  TYR A CZ    1 
ATOM   1628 O  OH    . TYR A 1 210 ? -35.096 -24.481 35.987  1.00 20.63 ? 210  TYR A OH    1 
ATOM   1629 N  N     . GLY A 1 211 ? -30.968 -22.292 32.459  1.00 19.46 ? 211  GLY A N     1 
ATOM   1630 C  CA    . GLY A 1 211 ? -30.442 -23.642 32.168  1.00 20.17 ? 211  GLY A CA    1 
ATOM   1631 C  C     . GLY A 1 211 ? -29.061 -23.584 31.511  1.00 20.77 ? 211  GLY A C     1 
ATOM   1632 O  O     . GLY A 1 211 ? -28.355 -22.576 31.606  1.00 20.27 ? 211  GLY A O     1 
ATOM   1633 N  N     . PRO A 1 212 ? -28.639 -24.675 30.831  1.00 20.85 ? 212  PRO A N     1 
ATOM   1634 C  CA    . PRO A 1 212 ? -27.307 -24.739 30.235  1.00 20.16 ? 212  PRO A CA    1 
ATOM   1635 C  C     . PRO A 1 212 ? -27.055 -23.603 29.235  1.00 20.75 ? 212  PRO A C     1 
ATOM   1636 O  O     . PRO A 1 212 ? -27.915 -23.273 28.451  1.00 18.27 ? 212  PRO A O     1 
ATOM   1637 C  CB    . PRO A 1 212 ? -27.283 -26.114 29.553  1.00 19.28 ? 212  PRO A CB    1 
ATOM   1638 C  CG    . PRO A 1 212 ? -28.318 -26.930 30.324  1.00 19.61 ? 212  PRO A CG    1 
ATOM   1639 C  CD    . PRO A 1 212 ? -29.406 -25.925 30.626  1.00 20.14 ? 212  PRO A CD    1 
ATOM   1640 N  N     . TYR A 1 213 ? -25.846 -23.040 29.297  1.00 21.09 ? 213  TYR A N     1 
ATOM   1641 C  CA    . TYR A 1 213 ? -25.400 -21.911 28.450  1.00 19.75 ? 213  TYR A CA    1 
ATOM   1642 C  C     . TYR A 1 213 ? -24.778 -22.521 27.191  1.00 19.85 ? 213  TYR A C     1 
ATOM   1643 O  O     . TYR A 1 213 ? -23.673 -23.068 27.286  1.00 18.25 ? 213  TYR A O     1 
ATOM   1644 C  CB    . TYR A 1 213 ? -24.495 -21.000 29.292  1.00 20.17 ? 213  TYR A CB    1 
ATOM   1645 C  CG    . TYR A 1 213 ? -23.991 -19.795 28.545  1.00 22.99 ? 213  TYR A CG    1 
ATOM   1646 C  CD1   . TYR A 1 213 ? -24.781 -19.177 27.583  1.00 22.37 ? 213  TYR A CD1   1 
ATOM   1647 C  CD2   . TYR A 1 213 ? -22.739 -19.249 28.818  1.00 25.56 ? 213  TYR A CD2   1 
ATOM   1648 C  CE1   . TYR A 1 213 ? -24.334 -18.075 26.877  1.00 24.43 ? 213  TYR A CE1   1 
ATOM   1649 C  CE2   . TYR A 1 213 ? -22.286 -18.121 28.143  1.00 27.04 ? 213  TYR A CE2   1 
ATOM   1650 C  CZ    . TYR A 1 213 ? -23.084 -17.544 27.153  1.00 27.85 ? 213  TYR A CZ    1 
ATOM   1651 O  OH    . TYR A 1 213 ? -22.662 -16.463 26.435  1.00 26.07 ? 213  TYR A OH    1 
ATOM   1652 N  N     . VAL A 1 214 ? -25.486 -22.492 26.059  1.00 19.22 ? 214  VAL A N     1 
ATOM   1653 C  CA    . VAL A 1 214 ? -25.129 -23.319 24.863  1.00 19.57 ? 214  VAL A CA    1 
ATOM   1654 C  C     . VAL A 1 214 ? -24.626 -22.471 23.690  1.00 19.50 ? 214  VAL A C     1 
ATOM   1655 O  O     . VAL A 1 214 ? -24.129 -23.093 22.733  1.00 19.47 ? 214  VAL A O     1 
ATOM   1656 C  CB    . VAL A 1 214 ? -26.297 -24.236 24.438  1.00 21.87 ? 214  VAL A CB    1 
ATOM   1657 C  CG1   . VAL A 1 214 ? -26.592 -25.296 25.513  1.00 20.77 ? 214  VAL A CG1   1 
ATOM   1658 C  CG2   . VAL A 1 214 ? -27.536 -23.444 24.074  1.00 20.00 ? 214  VAL A CG2   1 
ATOM   1659 N  N     . ASP A 1 215 ? -24.691 -21.131 23.752  1.00 18.57 ? 215  ASP A N     1 
ATOM   1660 C  CA    . ASP A 1 215 ? -24.341 -20.268 22.587  1.00 19.79 ? 215  ASP A CA    1 
ATOM   1661 C  C     . ASP A 1 215 ? -22.955 -20.679 22.072  1.00 18.34 ? 215  ASP A C     1 
ATOM   1662 O  O     . ASP A 1 215 ? -22.741 -20.716 20.842  1.00 17.43 ? 215  ASP A O     1 
ATOM   1663 C  CB    . ASP A 1 215 ? -24.379 -18.769 22.935  1.00 18.39 ? 215  ASP A CB    1 
ATOM   1664 C  CG    . ASP A 1 215 ? -25.778 -18.249 23.244  1.00 19.93 ? 215  ASP A CG    1 
ATOM   1665 O  OD1   . ASP A 1 215 ? -26.357 -18.705 24.245  1.00 19.63 ? 215  ASP A OD1   1 
ATOM   1666 O  OD2   . ASP A 1 215 ? -26.289 -17.406 22.472  1.00 20.77 ? 215  ASP A OD2   1 
ATOM   1667 N  N     . GLY A 1 216 ? -22.039 -20.895 23.010  1.00 17.62 ? 216  GLY A N     1 
ATOM   1668 C  CA    . GLY A 1 216 ? -20.634 -21.229 22.736  1.00 18.15 ? 216  GLY A CA    1 
ATOM   1669 C  C     . GLY A 1 216 ? -20.453 -22.446 21.843  1.00 16.16 ? 216  GLY A C     1 
ATOM   1670 O  O     . GLY A 1 216 ? -19.470 -22.462 21.115  1.00 14.98 ? 216  GLY A O     1 
ATOM   1671 N  N     . ILE A 1 217 ? -21.339 -23.433 21.916  1.00 16.78 ? 217  ILE A N     1 
ATOM   1672 C  CA    . ILE A 1 217 ? -21.167 -24.706 21.173  1.00 17.10 ? 217  ILE A CA    1 
ATOM   1673 C  C     . ILE A 1 217 ? -21.385 -24.459 19.680  1.00 18.27 ? 217  ILE A C     1 
ATOM   1674 O  O     . ILE A 1 217 ? -20.998 -25.351 18.903  1.00 16.76 ? 217  ILE A O     1 
ATOM   1675 C  CB    . ILE A 1 217 ? -22.030 -25.865 21.705  1.00 17.64 ? 217  ILE A CB    1 
ATOM   1676 C  CG1   . ILE A 1 217 ? -23.449 -25.897 21.132  1.00 18.61 ? 217  ILE A CG1   1 
ATOM   1677 C  CG2   . ILE A 1 217 ? -22.032 -25.914 23.211  1.00 18.10 ? 217  ILE A CG2   1 
ATOM   1678 C  CD1   . ILE A 1 217 ? -24.297 -27.019 21.751  1.00 19.89 ? 217  ILE A CD1   1 
ATOM   1679 N  N     . PHE A 1 218 ? -21.929 -23.306 19.277  1.00 17.39 ? 218  PHE A N     1 
ATOM   1680 C  CA    . PHE A 1 218 ? -22.135 -23.019 17.839  1.00 18.25 ? 218  PHE A CA    1 
ATOM   1681 C  C     . PHE A 1 218 ? -21.045 -22.092 17.314  1.00 17.94 ? 218  PHE A C     1 
ATOM   1682 O  O     . PHE A 1 218 ? -21.180 -21.640 16.139  1.00 21.25 ? 218  PHE A O     1 
ATOM   1683 C  CB    . PHE A 1 218 ? -23.541 -22.464 17.624  1.00 18.98 ? 218  PHE A CB    1 
ATOM   1684 C  CG    . PHE A 1 218 ? -24.603 -23.432 18.062  1.00 19.82 ? 218  PHE A CG    1 
ATOM   1685 C  CD1   . PHE A 1 218 ? -24.853 -24.576 17.329  1.00 20.80 ? 218  PHE A CD1   1 
ATOM   1686 C  CD2   . PHE A 1 218 ? -25.330 -23.223 19.219  1.00 20.47 ? 218  PHE A CD2   1 
ATOM   1687 C  CE1   . PHE A 1 218 ? -25.815 -25.487 17.737  1.00 21.02 ? 218  PHE A CE1   1 
ATOM   1688 C  CE2   . PHE A 1 218 ? -26.305 -24.122 19.617  1.00 22.77 ? 218  PHE A CE2   1 
ATOM   1689 C  CZ    . PHE A 1 218 ? -26.542 -25.266 18.881  1.00 21.31 ? 218  PHE A CZ    1 
ATOM   1690 N  N     . SER A 1 219 ? -20.045 -21.770 18.140  1.00 15.56 ? 219  SER A N     1 
ATOM   1691 C  CA    . SER A 1 219 ? -18.817 -21.054 17.713  1.00 15.10 ? 219  SER A CA    1 
ATOM   1692 C  C     . SER A 1 219 ? -17.726 -22.087 17.381  1.00 15.62 ? 219  SER A C     1 
ATOM   1693 O  O     . SER A 1 219 ? -17.698 -23.168 18.019  1.00 14.07 ? 219  SER A O     1 
ATOM   1694 C  CB    . SER A 1 219 ? -18.373 -20.036 18.757  1.00 14.95 ? 219  SER A CB    1 
ATOM   1695 O  OG    . SER A 1 219 ? -17.871 -20.682 19.933  1.00 16.24 ? 219  SER A OG    1 
ATOM   1696 N  N     . GLN A 1 220 ? -16.893 -21.797 16.370  1.00 16.69 ? 220  GLN A N     1 
ATOM   1697 C  CA    . GLN A 1 220 ? -15.844 -22.697 15.809  1.00 17.02 ? 220  GLN A CA    1 
ATOM   1698 C  C     . GLN A 1 220 ? -16.371 -24.130 15.740  1.00 18.68 ? 220  GLN A C     1 
ATOM   1699 O  O     . GLN A 1 220 ? -15.686 -25.070 16.249  1.00 17.33 ? 220  GLN A O     1 
ATOM   1700 C  CB    . GLN A 1 220 ? -14.564 -22.605 16.632  1.00 16.34 ? 220  GLN A CB    1 
ATOM   1701 C  CG    . GLN A 1 220 ? -13.819 -21.287 16.421  1.00 16.10 ? 220  GLN A CG    1 
ATOM   1702 C  CD    . GLN A 1 220 ? -12.355 -21.338 16.811  1.00 15.70 ? 220  GLN A CD    1 
ATOM   1703 O  OE1   . GLN A 1 220 ? -11.857 -22.314 17.384  1.00 17.81 ? 220  GLN A OE1   1 
ATOM   1704 N  NE2   . GLN A 1 220 ? -11.630 -20.280 16.491  1.00 14.59 ? 220  GLN A NE2   1 
ATOM   1705 N  N     . SER A 1 221 ? -17.548 -24.293 15.127  1.00 20.14 ? 221  SER A N     1 
ATOM   1706 C  CA    . SER A 1 221 ? -18.405 -25.481 15.348  1.00 20.32 ? 221  SER A CA    1 
ATOM   1707 C  C     . SER A 1 221 ? -19.054 -25.949 14.048  1.00 19.90 ? 221  SER A C     1 
ATOM   1708 O  O     . SER A 1 221 ? -19.200 -25.170 13.098  1.00 17.34 ? 221  SER A O     1 
ATOM   1709 C  CB    . SER A 1 221 ? -19.467 -25.167 16.389  1.00 23.51 ? 221  SER A CB    1 
ATOM   1710 O  OG    . SER A 1 221 ? -20.329 -26.268 16.581  1.00 22.46 ? 221  SER A OG    1 
ATOM   1711 N  N     . ASN A 1 222 ? -19.450 -27.222 14.039  1.00 19.20 ? 222  ASN A N     1 
ATOM   1712 C  CA    . ASN A 1 222 ? -20.273 -27.799 12.955  1.00 18.45 ? 222  ASN A CA    1 
ATOM   1713 C  C     . ASN A 1 222 ? -21.496 -28.433 13.608  1.00 18.04 ? 222  ASN A C     1 
ATOM   1714 O  O     . ASN A 1 222 ? -21.957 -29.453 13.094  1.00 18.20 ? 222  ASN A O     1 
ATOM   1715 C  CB    . ASN A 1 222 ? -19.456 -28.719 12.039  1.00 17.86 ? 222  ASN A CB    1 
ATOM   1716 C  CG    . ASN A 1 222 ? -18.769 -29.867 12.748  1.00 17.16 ? 222  ASN A CG    1 
ATOM   1717 O  OD1   . ASN A 1 222 ? -18.998 -30.114 13.916  1.00 15.75 ? 222  ASN A OD1   1 
ATOM   1718 N  ND2   . ASN A 1 222 ? -17.904 -30.560 12.039  1.00 17.41 ? 222  ASN A ND2   1 
ATOM   1719 N  N     . PHE A 1 223 ? -22.012 -27.820 14.681  1.00 18.01 ? 223  PHE A N     1 
ATOM   1720 C  CA    . PHE A 1 223 ? -23.222 -28.288 15.401  1.00 17.47 ? 223  PHE A CA    1 
ATOM   1721 C  C     . PHE A 1 223 ? -24.483 -27.555 14.931  1.00 18.24 ? 223  PHE A C     1 
ATOM   1722 O  O     . PHE A 1 223 ? -25.553 -28.023 15.313  1.00 19.36 ? 223  PHE A O     1 
ATOM   1723 C  CB    . PHE A 1 223 ? -23.100 -28.115 16.913  1.00 17.22 ? 223  PHE A CB    1 
ATOM   1724 C  CG    . PHE A 1 223 ? -21.997 -28.896 17.553  1.00 16.91 ? 223  PHE A CG    1 
ATOM   1725 C  CD1   . PHE A 1 223 ? -21.382 -29.953 16.892  1.00 16.90 ? 223  PHE A CD1   1 
ATOM   1726 C  CD2   . PHE A 1 223 ? -21.511 -28.517 18.788  1.00 17.17 ? 223  PHE A CD2   1 
ATOM   1727 C  CE1   . PHE A 1 223 ? -20.353 -30.657 17.492  1.00 17.61 ? 223  PHE A CE1   1 
ATOM   1728 C  CE2   . PHE A 1 223 ? -20.474 -29.222 19.378  1.00 19.59 ? 223  PHE A CE2   1 
ATOM   1729 C  CZ    . PHE A 1 223 ? -19.901 -30.297 18.736  1.00 17.66 ? 223  PHE A CZ    1 
ATOM   1730 N  N     . GLY A 1 224 ? -24.365 -26.491 14.137  1.00 18.10 ? 224  GLY A N     1 
ATOM   1731 C  CA    . GLY A 1 224 ? -25.507 -25.642 13.777  1.00 18.42 ? 224  GLY A CA    1 
ATOM   1732 C  C     . GLY A 1 224 ? -25.198 -24.642 12.674  1.00 18.88 ? 224  GLY A C     1 
ATOM   1733 O  O     . GLY A 1 224 ? -24.032 -24.396 12.396  1.00 19.74 ? 224  GLY A O     1 
ATOM   1734 N  N     . VAL A 1 225 ? -26.243 -24.088 12.060  1.00 19.38 ? 225  VAL A N     1 
ATOM   1735 C  CA    . VAL A 1 225 ? -26.158 -22.903 11.180  1.00 18.48 ? 225  VAL A CA    1 
ATOM   1736 C  C     . VAL A 1 225 ? -26.811 -21.703 11.877  1.00 18.53 ? 225  VAL A C     1 
ATOM   1737 O  O     . VAL A 1 225 ? -28.057 -21.668 11.998  1.00 17.01 ? 225  VAL A O     1 
ATOM   1738 C  CB    . VAL A 1 225 ? -26.783 -23.166 9.804   1.00 20.60 ? 225  VAL A CB    1 
ATOM   1739 C  CG1   . VAL A 1 225 ? -26.618 -21.951 8.924   1.00 20.96 ? 225  VAL A CG1   1 
ATOM   1740 C  CG2   . VAL A 1 225 ? -26.193 -24.400 9.127   1.00 22.44 ? 225  VAL A CG2   1 
ATOM   1741 N  N     . VAL A 1 226 ? -25.982 -20.719 12.246  1.00 17.66 ? 226  VAL A N     1 
ATOM   1742 C  CA    . VAL A 1 226 ? -26.429 -19.479 12.917  1.00 18.96 ? 226  VAL A CA    1 
ATOM   1743 C  C     . VAL A 1 226 ? -27.073 -18.589 11.861  1.00 18.20 ? 226  VAL A C     1 
ATOM   1744 O  O     . VAL A 1 226 ? -26.425 -18.306 10.841  1.00 20.73 ? 226  VAL A O     1 
ATOM   1745 C  CB    . VAL A 1 226 ? -25.285 -18.795 13.688  1.00 20.45 ? 226  VAL A CB    1 
ATOM   1746 C  CG1   . VAL A 1 226 ? -25.750 -17.474 14.280  1.00 20.03 ? 226  VAL A CG1   1 
ATOM   1747 C  CG2   . VAL A 1 226 ? -24.735 -19.716 14.783  1.00 21.07 ? 226  VAL A CG2   1 
ATOM   1748 N  N     . THR A 1 227 ? -28.324 -18.188 12.092  1.00 18.45 ? 227  THR A N     1 
ATOM   1749 C  CA    . THR A 1 227 ? -29.118 -17.386 11.115  1.00 17.87 ? 227  THR A CA    1 
ATOM   1750 C  C     . THR A 1 227 ? -29.414 -15.980 11.637  1.00 18.85 ? 227  THR A C     1 
ATOM   1751 O  O     . THR A 1 227 ? -29.737 -15.112 10.805  1.00 18.88 ? 227  THR A O     1 
ATOM   1752 C  CB    . THR A 1 227 ? -30.370 -18.158 10.728  1.00 17.06 ? 227  THR A CB    1 
ATOM   1753 O  OG1   . THR A 1 227 ? -31.129 -18.467 11.903  1.00 19.28 ? 227  THR A OG1   1 
ATOM   1754 C  CG2   . THR A 1 227 ? -30.005 -19.425 9.987   1.00 17.00 ? 227  THR A CG2   1 
ATOM   1755 N  N     . LYS A 1 228 ? -29.365 -15.775 12.958  1.00 19.33 ? 228  LYS A N     1 
ATOM   1756 C  CA    . LYS A 1 228 ? -29.384 -14.424 13.584  1.00 18.40 ? 228  LYS A CA    1 
ATOM   1757 C  C     . LYS A 1 228 ? -28.467 -14.414 14.793  1.00 17.90 ? 228  LYS A C     1 
ATOM   1758 O  O     . LYS A 1 228 ? -28.377 -15.460 15.498  1.00 17.94 ? 228  LYS A O     1 
ATOM   1759 C  CB    . LYS A 1 228 ? -30.790 -14.021 14.043  1.00 19.18 ? 228  LYS A CB    1 
ATOM   1760 C  CG    . LYS A 1 228 ? -31.884 -14.170 13.003  1.00 19.42 ? 228  LYS A CG    1 
ATOM   1761 C  CD    . LYS A 1 228 ? -33.311 -14.057 13.565  1.00 21.89 ? 228  LYS A CD    1 
ATOM   1762 C  CE    . LYS A 1 228 ? -34.371 -13.902 12.477  1.00 20.84 ? 228  LYS A CE    1 
ATOM   1763 N  NZ    . LYS A 1 228 ? -34.354 -15.066 11.556  1.00 23.33 ? 228  LYS A NZ    1 
ATOM   1764 N  N     . MET A 1 229 ? -27.851 -13.259 15.057  1.00 17.56 ? 229  MET A N     1 
ATOM   1765 C  CA    . MET A 1 229 ? -26.984 -13.092 16.244  1.00 17.63 ? 229  MET A CA    1 
ATOM   1766 C  C     . MET A 1 229 ? -27.100 -11.662 16.774  1.00 17.80 ? 229  MET A C     1 
ATOM   1767 O  O     . MET A 1 229 ? -27.031 -10.718 15.960  1.00 15.82 ? 229  MET A O     1 
ATOM   1768 C  CB    . MET A 1 229 ? -25.536 -13.406 15.883  1.00 16.62 ? 229  MET A CB    1 
ATOM   1769 C  CG    . MET A 1 229 ? -24.665 -13.776 17.056  1.00 17.95 ? 229  MET A CG    1 
ATOM   1770 S  SD    . MET A 1 229 ? -22.884 -13.767 16.606  1.00 20.27 ? 229  MET A SD    1 
ATOM   1771 C  CE    . MET A 1 229 ? -22.578 -12.002 16.539  1.00 19.86 ? 229  MET A CE    1 
ATOM   1772 N  N     . GLY A 1 230 ? -27.200 -11.543 18.099  1.00 15.84 ? 230  GLY A N     1 
ATOM   1773 C  CA    . GLY A 1 230 ? -27.044 -10.268 18.815  1.00 16.69 ? 230  GLY A CA    1 
ATOM   1774 C  C     . GLY A 1 230 ? -25.595 -9.979  19.116  1.00 17.87 ? 230  GLY A C     1 
ATOM   1775 O  O     . GLY A 1 230 ? -24.780 -10.957 19.340  1.00 19.47 ? 230  GLY A O     1 
ATOM   1776 N  N     . ILE A 1 231 ? -25.236 -8.703  19.130  1.00 17.58 ? 231  ILE A N     1 
ATOM   1777 C  CA    . ILE A 1 231 ? -23.891 -8.298  19.592  1.00 18.64 ? 231  ILE A CA    1 
ATOM   1778 C  C     . ILE A 1 231 ? -23.994 -7.004  20.412  1.00 18.53 ? 231  ILE A C     1 
ATOM   1779 O  O     . ILE A 1 231 ? -24.692 -6.068  20.010  1.00 17.06 ? 231  ILE A O     1 
ATOM   1780 C  CB    . ILE A 1 231 ? -22.904 -8.194  18.411  1.00 19.91 ? 231  ILE A CB    1 
ATOM   1781 C  CG1   . ILE A 1 231 ? -21.463 -8.205  18.937  1.00 20.64 ? 231  ILE A CG1   1 
ATOM   1782 C  CG2   . ILE A 1 231 ? -23.209 -6.973  17.562  1.00 20.35 ? 231  ILE A CG2   1 
ATOM   1783 C  CD1   . ILE A 1 231 ? -20.403 -8.392  17.867  1.00 21.72 ? 231  ILE A CD1   1 
ATOM   1784 N  N     . TRP A 1 232 ? -23.272 -6.937  21.520  1.00 16.62 ? 232  TRP A N     1 
ATOM   1785 C  CA    . TRP A 1 232 ? -23.175 -5.664  22.270  1.00 17.29 ? 232  TRP A CA    1 
ATOM   1786 C  C     . TRP A 1 232 ? -22.285 -4.672  21.507  1.00 18.40 ? 232  TRP A C     1 
ATOM   1787 O  O     . TRP A 1 232 ? -21.239 -5.094  20.934  1.00 17.04 ? 232  TRP A O     1 
ATOM   1788 C  CB    . TRP A 1 232 ? -22.690 -5.925  23.680  1.00 17.36 ? 232  TRP A CB    1 
ATOM   1789 C  CG    . TRP A 1 232 ? -23.643 -6.762  24.474  1.00 17.73 ? 232  TRP A CG    1 
ATOM   1790 C  CD1   . TRP A 1 232 ? -24.982 -6.917  24.271  1.00 18.44 ? 232  TRP A CD1   1 
ATOM   1791 C  CD2   . TRP A 1 232 ? -23.326 -7.554  25.627  1.00 18.80 ? 232  TRP A CD2   1 
ATOM   1792 N  NE1   . TRP A 1 232 ? -25.523 -7.718  25.234  1.00 18.70 ? 232  TRP A NE1   1 
ATOM   1793 C  CE2   . TRP A 1 232 ? -24.529 -8.134  26.075  1.00 19.00 ? 232  TRP A CE2   1 
ATOM   1794 C  CE3   . TRP A 1 232 ? -22.148 -7.857  26.304  1.00 19.69 ? 232  TRP A CE3   1 
ATOM   1795 C  CZ2   . TRP A 1 232 ? -24.581 -8.996  27.161  1.00 18.93 ? 232  TRP A CZ2   1 
ATOM   1796 C  CZ3   . TRP A 1 232 ? -22.199 -8.710  27.382  1.00 19.23 ? 232  TRP A CZ3   1 
ATOM   1797 C  CH2   . TRP A 1 232 ? -23.406 -9.256  27.814  1.00 19.24 ? 232  TRP A CH2   1 
ATOM   1798 N  N     . LEU A 1 233 ? -22.694 -3.395  21.500  1.00 18.18 ? 233  LEU A N     1 
ATOM   1799 C  CA    . LEU A 1 233 ? -21.942 -2.277  20.859  1.00 19.41 ? 233  LEU A CA    1 
ATOM   1800 C  C     . LEU A 1 233 ? -21.550 -1.229  21.895  1.00 17.77 ? 233  LEU A C     1 
ATOM   1801 O  O     . LEU A 1 233 ? -22.374 -0.880  22.725  1.00 19.21 ? 233  LEU A O     1 
ATOM   1802 C  CB    . LEU A 1 233 ? -22.813 -1.629  19.782  1.00 19.54 ? 233  LEU A CB    1 
ATOM   1803 C  CG    . LEU A 1 233 ? -23.213 -2.529  18.621  1.00 20.48 ? 233  LEU A CG    1 
ATOM   1804 C  CD1   . LEU A 1 233 ? -24.210 -1.806  17.709  1.00 20.34 ? 233  LEU A CD1   1 
ATOM   1805 C  CD2   . LEU A 1 233 ? -21.978 -2.967  17.852  1.00 20.17 ? 233  LEU A CD2   1 
ATOM   1806 N  N     . MET A 1 234 ? -20.324 -0.750  21.840  1.00 17.97 ? 234  MET A N     1 
ATOM   1807 C  CA    . MET A 1 234 ? -19.835 0.260   22.787  1.00 19.66 ? 234  MET A CA    1 
ATOM   1808 C  C     . MET A 1 234 ? -20.548 1.599   22.540  1.00 22.13 ? 234  MET A C     1 
ATOM   1809 O  O     . MET A 1 234 ? -20.551 2.129   21.410  1.00 18.45 ? 234  MET A O     1 
ATOM   1810 C  CB    . MET A 1 234 ? -18.328 0.452   22.624  1.00 21.51 ? 234  MET A CB    1 
ATOM   1811 C  CG    . MET A 1 234 ? -17.720 1.158   23.805  1.00 21.44 ? 234  MET A CG    1 
ATOM   1812 S  SD    . MET A 1 234 ? -15.961 1.231   23.694  1.00 24.45 ? 234  MET A SD    1 
ATOM   1813 C  CE    . MET A 1 234 ? -15.732 2.127   22.166  1.00 25.97 ? 234  MET A CE    1 
ATOM   1814 N  N     . PRO A 1 235 ? -21.139 2.214   23.599  1.00 20.66 ? 235  PRO A N     1 
ATOM   1815 C  CA    . PRO A 1 235 ? -21.547 3.618   23.519  1.00 21.98 ? 235  PRO A CA    1 
ATOM   1816 C  C     . PRO A 1 235 ? -20.355 4.506   23.137  1.00 22.93 ? 235  PRO A C     1 
ATOM   1817 O  O     . PRO A 1 235 ? -19.250 4.274   23.591  1.00 20.96 ? 235  PRO A O     1 
ATOM   1818 C  CB    . PRO A 1 235 ? -22.072 3.954   24.922  1.00 22.31 ? 235  PRO A CB    1 
ATOM   1819 C  CG    . PRO A 1 235 ? -22.427 2.588   25.524  1.00 21.93 ? 235  PRO A CG    1 
ATOM   1820 C  CD    . PRO A 1 235 ? -21.424 1.625   24.915  1.00 21.01 ? 235  PRO A CD    1 
ATOM   1821 N  N     . GLU A 1 236 ? -20.601 5.476   22.254  1.00 23.54 ? 236  GLU A N     1 
ATOM   1822 C  CA    . GLU A 1 236 ? -19.564 6.429   21.808  1.00 25.69 ? 236  GLU A CA    1 
ATOM   1823 C  C     . GLU A 1 236 ? -18.929 7.007   23.061  1.00 22.15 ? 236  GLU A C     1 
ATOM   1824 O  O     . GLU A 1 236 ? -19.640 7.394   23.959  1.00 22.76 ? 236  GLU A O     1 
ATOM   1825 C  CB    . GLU A 1 236 ? -20.170 7.505   20.902  1.00 28.33 ? 236  GLU A CB    1 
ATOM   1826 C  CG    . GLU A 1 236 ? -19.184 8.577   20.482  1.00 31.44 ? 236  GLU A CG    1 
ATOM   1827 C  CD    . GLU A 1 236 ? -19.797 9.658   19.586  1.00 36.86 ? 236  GLU A CD    1 
ATOM   1828 O  OE1   . GLU A 1 236 ? -20.878 10.171  19.908  1.00 36.13 ? 236  GLU A OE1   1 
ATOM   1829 O  OE2   . GLU A 1 236 ? -19.191 9.966   18.563  1.00 47.06 ? 236  GLU A OE2   1 
ATOM   1830 N  N     . PRO A 1 237 ? -17.591 6.985   23.199  1.00 22.99 ? 237  PRO A N     1 
ATOM   1831 C  CA    . PRO A 1 237 ? -16.937 7.497   24.403  1.00 23.75 ? 237  PRO A CA    1 
ATOM   1832 C  C     . PRO A 1 237 ? -16.778 9.026   24.420  1.00 25.21 ? 237  PRO A C     1 
ATOM   1833 O  O     . PRO A 1 237 ? -16.804 9.655   23.366  1.00 22.02 ? 237  PRO A O     1 
ATOM   1834 C  CB    . PRO A 1 237 ? -15.561 6.808   24.342  1.00 24.32 ? 237  PRO A CB    1 
ATOM   1835 C  CG    . PRO A 1 237 ? -15.295 6.694   22.863  1.00 25.26 ? 237  PRO A CG    1 
ATOM   1836 C  CD    . PRO A 1 237 ? -16.647 6.340   22.276  1.00 23.16 ? 237  PRO A CD    1 
ATOM   1837 N  N     . ALA A 1 238 ? -16.569 9.578   25.614  1.00 27.21 ? 238  ALA A N     1 
ATOM   1838 C  CA    . ALA A 1 238 ? -16.431 11.037  25.830  1.00 28.78 ? 238  ALA A CA    1 
ATOM   1839 C  C     . ALA A 1 238 ? -15.093 11.531  25.262  1.00 28.66 ? 238  ALA A C     1 
ATOM   1840 O  O     . ALA A 1 238 ? -14.944 12.724  25.045  1.00 34.94 ? 238  ALA A O     1 
ATOM   1841 C  CB    . ALA A 1 238 ? -16.548 11.340  27.297  1.00 29.42 ? 238  ALA A CB    1 
ATOM   1842 N  N     . GLY A 1 239 ? -14.138 10.643  25.023  1.00 26.17 ? 239  GLY A N     1 
ATOM   1843 C  CA    . GLY A 1 239 ? -12.858 10.992  24.389  1.00 22.81 ? 239  GLY A CA    1 
ATOM   1844 C  C     . GLY A 1 239 ? -12.146 9.755   23.871  1.00 24.05 ? 239  GLY A C     1 
ATOM   1845 O  O     . GLY A 1 239 ? -12.553 8.614   24.228  1.00 21.94 ? 239  GLY A O     1 
ATOM   1846 N  N     . TYR A 1 240 ? -11.105 9.976   23.068  1.00 23.10 ? 240  TYR A N     1 
ATOM   1847 C  CA    . TYR A 1 240 ? -10.381 8.913   22.339  1.00 24.33 ? 240  TYR A CA    1 
ATOM   1848 C  C     . TYR A 1 240 ? -8.969  9.408   22.063  1.00 22.99 ? 240  TYR A C     1 
ATOM   1849 O  O     . TYR A 1 240 ? -8.808  10.384  21.346  1.00 21.50 ? 240  TYR A O     1 
ATOM   1850 C  CB    . TYR A 1 240 ? -11.111 8.563   21.032  1.00 22.91 ? 240  TYR A CB    1 
ATOM   1851 C  CG    . TYR A 1 240 ? -10.335 7.620   20.152  1.00 23.02 ? 240  TYR A CG    1 
ATOM   1852 C  CD1   . TYR A 1 240 ? -9.996  6.348   20.601  1.00 23.83 ? 240  TYR A CD1   1 
ATOM   1853 C  CD2   . TYR A 1 240 ? -9.952  7.981   18.868  1.00 22.57 ? 240  TYR A CD2   1 
ATOM   1854 C  CE1   . TYR A 1 240 ? -9.287  5.472   19.799  1.00 24.11 ? 240  TYR A CE1   1 
ATOM   1855 C  CE2   . TYR A 1 240 ? -9.256  7.106   18.044  1.00 22.46 ? 240  TYR A CE2   1 
ATOM   1856 C  CZ    . TYR A 1 240 ? -8.909  5.848   18.515  1.00 23.26 ? 240  TYR A CZ    1 
ATOM   1857 O  OH    . TYR A 1 240 ? -8.210  4.975   17.723  1.00 20.58 ? 240  TYR A OH    1 
ATOM   1858 N  N     . ARG A 1 241 ? -7.958  8.750   22.600  1.00 22.97 ? 241  ARG A N     1 
ATOM   1859 C  CA    . ARG A 1 241 ? -6.556  9.181   22.340  1.00 24.19 ? 241  ARG A CA    1 
ATOM   1860 C  C     . ARG A 1 241 ? -5.738  7.943   21.974  1.00 23.11 ? 241  ARG A C     1 
ATOM   1861 O  O     . ARG A 1 241 ? -5.340  7.189   22.861  1.00 21.22 ? 241  ARG A O     1 
ATOM   1862 C  CB    . ARG A 1 241 ? -5.973  9.953   23.532  1.00 26.65 ? 241  ARG A CB    1 
ATOM   1863 C  CG    . ARG A 1 241 ? -6.546  11.355  23.752  1.00 28.79 ? 241  ARG A CG    1 
ATOM   1864 C  CD    . ARG A 1 241 ? -6.002  12.396  22.764  1.00 32.86 ? 241  ARG A CD    1 
ATOM   1865 N  NE    . ARG A 1 241 ? -4.683  12.936  23.129  1.00 33.71 ? 241  ARG A NE    1 
ATOM   1866 C  CZ    . ARG A 1 241 ? -3.745  13.322  22.278  1.00 34.00 ? 241  ARG A CZ    1 
ATOM   1867 N  NH1   . ARG A 1 241 ? -3.917  13.215  20.973  1.00 41.78 ? 241  ARG A NH1   1 
ATOM   1868 N  NH2   . ARG A 1 241 ? -2.614  13.804  22.733  1.00 38.29 ? 241  ARG A NH2   1 
ATOM   1869 N  N     . PRO A 1 242 ? -5.490  7.703   20.665  1.00 22.43 ? 242  PRO A N     1 
ATOM   1870 C  CA    . PRO A 1 242 ? -4.659  6.585   20.216  1.00 24.35 ? 242  PRO A CA    1 
ATOM   1871 C  C     . PRO A 1 242 ? -3.161  6.893   20.333  1.00 23.92 ? 242  PRO A C     1 
ATOM   1872 O  O     . PRO A 1 242 ? -2.777  8.030   20.194  1.00 25.02 ? 242  PRO A O     1 
ATOM   1873 C  CB    . PRO A 1 242 ? -5.099  6.389   18.753  1.00 23.21 ? 242  PRO A CB    1 
ATOM   1874 C  CG    . PRO A 1 242 ? -5.494  7.761   18.293  1.00 23.06 ? 242  PRO A CG    1 
ATOM   1875 C  CD    . PRO A 1 242 ? -6.088  8.418   19.525  1.00 24.40 ? 242  PRO A CD    1 
ATOM   1876 N  N     . TYR A 1 243 ? -2.347  5.880   20.621  1.00 22.79 ? 243  TYR A N     1 
ATOM   1877 C  CA    . TYR A 1 243 ? -0.895  6.091   20.819  1.00 23.57 ? 243  TYR A CA    1 
ATOM   1878 C  C     . TYR A 1 243 ? -0.056  4.975   20.205  1.00 21.85 ? 243  TYR A C     1 
ATOM   1879 O  O     . TYR A 1 243 ? -0.495  3.800   20.072  1.00 21.84 ? 243  TYR A O     1 
ATOM   1880 C  CB    . TYR A 1 243 ? -0.599  6.266   22.309  1.00 22.75 ? 243  TYR A CB    1 
ATOM   1881 C  CG    . TYR A 1 243 ? -0.997  5.103   23.175  1.00 21.92 ? 243  TYR A CG    1 
ATOM   1882 C  CD1   . TYR A 1 243 ? -0.205  3.973   23.274  1.00 21.69 ? 243  TYR A CD1   1 
ATOM   1883 C  CD2   . TYR A 1 243 ? -2.138  5.164   23.954  1.00 22.35 ? 243  TYR A CD2   1 
ATOM   1884 C  CE1   . TYR A 1 243 ? -0.569  2.910   24.090  1.00 22.36 ? 243  TYR A CE1   1 
ATOM   1885 C  CE2   . TYR A 1 243 ? -2.518  4.114   24.769  1.00 21.89 ? 243  TYR A CE2   1 
ATOM   1886 C  CZ    . TYR A 1 243 ? -1.737  2.969   24.823  1.00 22.67 ? 243  TYR A CZ    1 
ATOM   1887 O  OH    . TYR A 1 243 ? -2.126  1.932   25.620  1.00 22.80 ? 243  TYR A OH    1 
ATOM   1888 N  N     . LEU A 1 244 ? 1.207   5.337   19.984  1.00 21.67 ? 244  LEU A N     1 
ATOM   1889 C  CA    . LEU A 1 244 ? 2.298   4.427   19.556  1.00 20.91 ? 244  LEU A CA    1 
ATOM   1890 C  C     . LEU A 1 244 ? 3.485   4.603   20.500  1.00 20.64 ? 244  LEU A C     1 
ATOM   1891 O  O     . LEU A 1 244 ? 3.930   5.756   20.677  1.00 20.85 ? 244  LEU A O     1 
ATOM   1892 C  CB    . LEU A 1 244 ? 2.660   4.752   18.104  1.00 20.60 ? 244  LEU A CB    1 
ATOM   1893 C  CG    . LEU A 1 244 ? 3.844   3.989   17.527  1.00 21.29 ? 244  LEU A CG    1 
ATOM   1894 C  CD1   . LEU A 1 244 ? 3.591   2.494   17.536  1.00 23.62 ? 244  LEU A CD1   1 
ATOM   1895 C  CD2   . LEU A 1 244 ? 4.138   4.480   16.129  1.00 21.21 ? 244  LEU A CD2   1 
ATOM   1896 N  N     . ILE A 1 245 ? 3.928   3.503   21.112  1.00 18.47 ? 245  ILE A N     1 
ATOM   1897 C  CA    . ILE A 1 245 ? 5.193   3.414   21.890  1.00 20.24 ? 245  ILE A CA    1 
ATOM   1898 C  C     . ILE A 1 245 ? 6.140   2.519   21.086  1.00 22.75 ? 245  ILE A C     1 
ATOM   1899 O  O     . ILE A 1 245 ? 5.738   1.382   20.767  1.00 24.23 ? 245  ILE A O     1 
ATOM   1900 C  CB    . ILE A 1 245 ? 4.916   2.874   23.311  1.00 20.12 ? 245  ILE A CB    1 
ATOM   1901 C  CG1   . ILE A 1 245 ? 3.694   3.566   23.925  1.00 21.33 ? 245  ILE A CG1   1 
ATOM   1902 C  CG2   . ILE A 1 245 ? 6.150   2.990   24.194  1.00 20.87 ? 245  ILE A CG2   1 
ATOM   1903 C  CD1   . ILE A 1 245 ? 3.486   3.273   25.397  1.00 22.51 ? 245  ILE A CD1   1 
ATOM   1904 N  N     . THR A 1 246 ? 7.313   3.028   20.712  1.00 22.27 ? 246  THR A N     1 
ATOM   1905 C  CA    . THR A 1 246 ? 8.296   2.283   19.887  1.00 23.40 ? 246  THR A CA    1 
ATOM   1906 C  C     . THR A 1 246 ? 9.501   1.916   20.747  1.00 24.77 ? 246  THR A C     1 
ATOM   1907 O  O     . THR A 1 246 ? 9.824   2.653   21.721  1.00 24.19 ? 246  THR A O     1 
ATOM   1908 C  CB    . THR A 1 246 ? 8.690   3.035   18.611  1.00 24.04 ? 246  THR A CB    1 
ATOM   1909 O  OG1   . THR A 1 246 ? 9.497   4.176   18.900  1.00 22.74 ? 246  THR A OG1   1 
ATOM   1910 C  CG2   . THR A 1 246 ? 7.474   3.462   17.820  1.00 23.86 ? 246  THR A CG2   1 
ATOM   1911 N  N     . PHE A 1 247 ? 10.105  0.780   20.430  1.00 21.30 ? 247  PHE A N     1 
ATOM   1912 C  CA    . PHE A 1 247 ? 11.253  0.238   21.189  1.00 23.45 ? 247  PHE A CA    1 
ATOM   1913 C  C     . PHE A 1 247 ? 12.318  -0.106  20.165  1.00 23.01 ? 247  PHE A C     1 
ATOM   1914 O  O     . PHE A 1 247 ? 11.992  -0.711  19.119  1.00 22.71 ? 247  PHE A O     1 
ATOM   1915 C  CB    . PHE A 1 247 ? 10.839  -0.937  22.071  1.00 22.29 ? 247  PHE A CB    1 
ATOM   1916 C  CG    . PHE A 1 247 ? 9.629   -0.675  22.922  1.00 23.17 ? 247  PHE A CG    1 
ATOM   1917 C  CD1   . PHE A 1 247 ? 9.756   -0.108  24.182  1.00 23.98 ? 247  PHE A CD1   1 
ATOM   1918 C  CD2   . PHE A 1 247 ? 8.363   -1.032  22.484  1.00 23.37 ? 247  PHE A CD2   1 
ATOM   1919 C  CE1   . PHE A 1 247 ? 8.644   0.122   24.976  1.00 24.57 ? 247  PHE A CE1   1 
ATOM   1920 C  CE2   . PHE A 1 247 ? 7.253   -0.801  23.286  1.00 25.95 ? 247  PHE A CE2   1 
ATOM   1921 C  CZ    . PHE A 1 247 ? 7.392   -0.213  24.527  1.00 25.54 ? 247  PHE A CZ    1 
ATOM   1922 N  N     . GLU A 1 248 ? 13.539  0.316   20.435  1.00 25.96 ? 248  GLU A N     1 
ATOM   1923 C  CA    . GLU A 1 248 ? 14.631  0.344   19.435  1.00 28.48 ? 248  GLU A CA    1 
ATOM   1924 C  C     . GLU A 1 248 ? 15.250  -1.054  19.312  1.00 27.28 ? 248  GLU A C     1 
ATOM   1925 O  O     . GLU A 1 248 ? 15.770  -1.287  18.236  1.00 25.31 ? 248  GLU A O     1 
ATOM   1926 C  CB    . GLU A 1 248 ? 15.657  1.436   19.761  1.00 36.96 ? 248  GLU A CB    1 
ATOM   1927 C  CG    . GLU A 1 248 ? 16.550  1.158   20.971  1.00 47.70 ? 248  GLU A CG    1 
ATOM   1928 C  CD    . GLU A 1 248 ? 17.785  2.057   21.152  1.00 54.75 ? 248  GLU A CD    1 
ATOM   1929 O  OE1   . GLU A 1 248 ? 17.961  3.013   20.340  1.00 45.75 ? 248  GLU A OE1   1 
ATOM   1930 O  OE2   . GLU A 1 248 ? 18.576  1.802   22.121  1.00 53.97 ? 248  GLU A OE2   1 
ATOM   1931 N  N     . ASN A 1 249 ? 15.145  -1.957  20.313  1.00 24.85 ? 249  ASN A N     1 
ATOM   1932 C  CA    . ASN A 1 249 ? 15.917  -3.243  20.316  1.00 28.07 ? 249  ASN A CA    1 
ATOM   1933 C  C     . ASN A 1 249 ? 14.993  -4.456  20.316  1.00 26.64 ? 249  ASN A C     1 
ATOM   1934 O  O     . ASN A 1 249 ? 14.001  -4.442  21.047  1.00 24.33 ? 249  ASN A O     1 
ATOM   1935 C  CB    . ASN A 1 249 ? 16.891  -3.377  21.486  1.00 28.94 ? 249  ASN A CB    1 
ATOM   1936 C  CG    . ASN A 1 249 ? 17.915  -2.268  21.438  1.00 36.00 ? 249  ASN A CG    1 
ATOM   1937 O  OD1   . ASN A 1 249 ? 18.703  -2.201  20.509  1.00 44.38 ? 249  ASN A OD1   1 
ATOM   1938 N  ND2   . ASN A 1 249 ? 17.869  -1.352  22.387  1.00 41.33 ? 249  ASN A ND2   1 
ATOM   1939 N  N     . GLU A 1 250 ? 15.345  -5.451  19.506  1.00 27.58 ? 250  GLU A N     1 
ATOM   1940 C  CA    . GLU A 1 250 ? 14.649  -6.755  19.401  1.00 30.51 ? 250  GLU A CA    1 
ATOM   1941 C  C     . GLU A 1 250 ? 14.482  -7.372  20.796  1.00 25.88 ? 250  GLU A C     1 
ATOM   1942 O  O     . GLU A 1 250 ? 13.406  -7.869  21.065  1.00 22.28 ? 250  GLU A O     1 
ATOM   1943 C  CB    . GLU A 1 250 ? 15.429  -7.710  18.504  1.00 36.87 ? 250  GLU A CB    1 
ATOM   1944 C  CG    . GLU A 1 250 ? 15.443  -7.295  17.043  1.00 46.85 ? 250  GLU A CG    1 
ATOM   1945 C  CD    . GLU A 1 250 ? 16.596  -7.914  16.258  1.00 58.01 ? 250  GLU A CD    1 
ATOM   1946 O  OE1   . GLU A 1 250 ? 16.948  -9.109  16.529  1.00 64.75 ? 250  GLU A OE1   1 
ATOM   1947 O  OE2   . GLU A 1 250 ? 17.162  -7.206  15.395  1.00 60.84 ? 250  GLU A OE2   1 
ATOM   1948 N  N     . ASP A 1 251 ? 15.493  -7.279  21.661  1.00 23.60 ? 251  ASP A N     1 
ATOM   1949 C  CA    . ASP A 1 251 ? 15.463  -7.879  23.014  1.00 24.94 ? 251  ASP A CA    1 
ATOM   1950 C  C     . ASP A 1 251 ? 14.538  -7.091  23.946  1.00 22.22 ? 251  ASP A C     1 
ATOM   1951 O  O     . ASP A 1 251 ? 14.230  -7.648  25.013  1.00 21.46 ? 251  ASP A O     1 
ATOM   1952 C  CB    . ASP A 1 251 ? 16.862  -7.993  23.626  1.00 28.25 ? 251  ASP A CB    1 
ATOM   1953 C  CG    . ASP A 1 251 ? 17.734  -9.047  22.969  1.00 36.92 ? 251  ASP A CG    1 
ATOM   1954 O  OD1   . ASP A 1 251 ? 17.215  -9.791  22.106  1.00 42.56 ? 251  ASP A OD1   1 
ATOM   1955 O  OD2   . ASP A 1 251 ? 18.942  -9.099  23.301  1.00 47.95 ? 251  ASP A OD2   1 
ATOM   1956 N  N     . ASP A 1 252 ? 14.132  -5.855  23.613  1.00 20.74 ? 252  ASP A N     1 
ATOM   1957 C  CA    . ASP A 1 252 ? 13.209  -5.043  24.466  1.00 20.33 ? 252  ASP A CA    1 
ATOM   1958 C  C     . ASP A 1 252 ? 11.876  -5.774  24.720  1.00 20.73 ? 252  ASP A C     1 
ATOM   1959 O  O     . ASP A 1 252 ? 11.230  -5.510  25.779  1.00 19.76 ? 252  ASP A O     1 
ATOM   1960 C  CB    . ASP A 1 252 ? 12.945  -3.676  23.832  1.00 22.70 ? 252  ASP A CB    1 
ATOM   1961 C  CG    . ASP A 1 252 ? 14.148  -2.735  23.903  1.00 23.29 ? 252  ASP A CG    1 
ATOM   1962 O  OD1   . ASP A 1 252 ? 14.995  -2.938  24.770  1.00 23.75 ? 252  ASP A OD1   1 
ATOM   1963 O  OD2   . ASP A 1 252 ? 14.194  -1.778  23.126  1.00 23.62 ? 252  ASP A OD2   1 
ATOM   1964 N  N     . ILE A 1 253 ? 11.442  -6.651  23.801  1.00 21.10 ? 253  ILE A N     1 
ATOM   1965 C  CA    . ILE A 1 253 ? 10.128  -7.353  23.918  1.00 21.87 ? 253  ILE A CA    1 
ATOM   1966 C  C     . ILE A 1 253 ? 10.036  -8.092  25.262  1.00 21.77 ? 253  ILE A C     1 
ATOM   1967 O  O     . ILE A 1 253 ? 8.936   -8.156  25.816  1.00 23.25 ? 253  ILE A O     1 
ATOM   1968 C  CB    . ILE A 1 253 ? 9.830   -8.259  22.704  1.00 21.25 ? 253  ILE A CB    1 
ATOM   1969 C  CG1   . ILE A 1 253 ? 8.352   -8.662  22.671  1.00 18.99 ? 253  ILE A CG1   1 
ATOM   1970 C  CG2   . ILE A 1 253 ? 10.734  -9.470  22.648  1.00 22.65 ? 253  ILE A CG2   1 
ATOM   1971 C  CD1   . ILE A 1 253 ? 7.428   -7.499  22.563  1.00 18.43 ? 253  ILE A CD1   1 
ATOM   1972 N  N     . GLU A 1 254 ? 11.148  -8.553  25.829  1.00 24.17 ? 254  GLU A N     1 
ATOM   1973 C  CA    . GLU A 1 254 ? 11.140  -9.256  27.139  1.00 24.14 ? 254  GLU A CA    1 
ATOM   1974 C  C     . GLU A 1 254 ? 10.639  -8.285  28.222  1.00 23.88 ? 254  GLU A C     1 
ATOM   1975 O  O     . GLU A 1 254 ? 9.631   -8.610  28.890  1.00 21.70 ? 254  GLU A O     1 
ATOM   1976 C  CB    . GLU A 1 254 ? 12.520  -9.837  27.471  1.00 24.41 ? 254  GLU A CB    1 
ATOM   1977 C  CG    . GLU A 1 254 ? 12.509  -10.632 28.755  1.00 25.59 ? 254  GLU A CG    1 
ATOM   1978 C  CD    . GLU A 1 254 ? 13.749  -11.469 29.055  1.00 30.19 ? 254  GLU A CD    1 
ATOM   1979 O  OE1   . GLU A 1 254 ? 14.668  -11.486 28.233  1.00 31.49 ? 254  GLU A OE1   1 
ATOM   1980 O  OE2   . GLU A 1 254 ? 13.773  -12.128 30.116  1.00 29.29 ? 254  GLU A OE2   1 
ATOM   1981 N  N     . THR A 1 255 ? 11.288  -7.131  28.409  1.00 22.09 ? 255  THR A N     1 
ATOM   1982 C  CA    . THR A 1 255 ? 10.913  -6.216  29.518  1.00 21.54 ? 255  THR A CA    1 
ATOM   1983 C  C     . THR A 1 255 ? 9.552   -5.575  29.192  1.00 19.03 ? 255  THR A C     1 
ATOM   1984 O  O     . THR A 1 255 ? 8.777   -5.345  30.123  1.00 18.62 ? 255  THR A O     1 
ATOM   1985 C  CB    . THR A 1 255 ? 12.015  -5.186  29.846  1.00 21.47 ? 255  THR A CB    1 
ATOM   1986 O  OG1   . THR A 1 255 ? 11.723  -4.592  31.120  1.00 22.54 ? 255  THR A OG1   1 
ATOM   1987 C  CG2   . THR A 1 255 ? 12.092  -4.059  28.856  1.00 21.58 ? 255  THR A CG2   1 
ATOM   1988 N  N     . VAL A 1 256 ? 9.277   -5.301  27.920  1.00 18.89 ? 256  VAL A N     1 
ATOM   1989 C  CA    . VAL A 1 256 ? 7.999   -4.685  27.465  1.00 19.47 ? 256  VAL A CA    1 
ATOM   1990 C  C     . VAL A 1 256 ? 6.835   -5.584  27.917  1.00 19.57 ? 256  VAL A C     1 
ATOM   1991 O  O     . VAL A 1 256 ? 5.878   -5.060  28.476  1.00 17.94 ? 256  VAL A O     1 
ATOM   1992 C  CB    . VAL A 1 256 ? 7.988   -4.461  25.943  1.00 20.92 ? 256  VAL A CB    1 
ATOM   1993 C  CG1   . VAL A 1 256 ? 6.567   -4.279  25.436  1.00 19.55 ? 256  VAL A CG1   1 
ATOM   1994 C  CG2   . VAL A 1 256 ? 8.878   -3.288  25.525  1.00 21.56 ? 256  VAL A CG2   1 
ATOM   1995 N  N     . THR A 1 257 ? 6.925   -6.896  27.694  1.00 19.23 ? 257  THR A N     1 
ATOM   1996 C  CA    . THR A 1 257 ? 5.845   -7.845  28.040  1.00 19.06 ? 257  THR A CA    1 
ATOM   1997 C  C     . THR A 1 257 ? 5.679   -7.899  29.562  1.00 20.70 ? 257  THR A C     1 
ATOM   1998 O  O     . THR A 1 257 ? 4.538   -7.964  30.018  1.00 18.56 ? 257  THR A O     1 
ATOM   1999 C  CB    . THR A 1 257 ? 6.104   -9.222  27.430  1.00 19.04 ? 257  THR A CB    1 
ATOM   2000 O  OG1   . THR A 1 257 ? 6.186   -9.049  26.018  1.00 21.68 ? 257  THR A OG1   1 
ATOM   2001 C  CG2   . THR A 1 257 ? 5.009   -10.205 27.753  1.00 19.71 ? 257  THR A CG2   1 
ATOM   2002 N  N     . GLU A 1 258 ? 6.778   -7.896  30.332  1.00 22.55 ? 258  GLU A N     1 
ATOM   2003 C  CA    . GLU A 1 258 ? 6.706   -7.859  31.814  1.00 20.64 ? 258  GLU A CA    1 
ATOM   2004 C  C     . GLU A 1 258 ? 5.890   -6.642  32.255  1.00 19.88 ? 258  GLU A C     1 
ATOM   2005 O  O     . GLU A 1 258 ? 5.164   -6.746  33.250  1.00 19.65 ? 258  GLU A O     1 
ATOM   2006 C  CB    . GLU A 1 258 ? 8.101   -7.749  32.426  1.00 22.97 ? 258  GLU A CB    1 
ATOM   2007 C  CG    . GLU A 1 258 ? 8.906   -9.025  32.344  1.00 23.45 ? 258  GLU A CG    1 
ATOM   2008 C  CD    . GLU A 1 258 ? 8.255   -10.146 33.133  1.00 24.97 ? 258  GLU A CD    1 
ATOM   2009 O  OE1   . GLU A 1 258 ? 8.177   -9.986  34.383  1.00 24.68 ? 258  GLU A OE1   1 
ATOM   2010 O  OE2   . GLU A 1 258 ? 7.804   -11.150 32.508  1.00 21.58 ? 258  GLU A OE2   1 
ATOM   2011 N  N     . ARG A 1 259 ? 6.075   -5.500  31.603  1.00 19.73 ? 259  ARG A N     1 
ATOM   2012 C  CA    . ARG A 1 259 ? 5.458   -4.218  32.039  1.00 20.87 ? 259  ARG A CA    1 
ATOM   2013 C  C     . ARG A 1 259 ? 3.999   -4.204  31.600  1.00 22.07 ? 259  ARG A C     1 
ATOM   2014 O  O     . ARG A 1 259 ? 3.160   -3.672  32.349  1.00 22.63 ? 259  ARG A O     1 
ATOM   2015 C  CB    . ARG A 1 259 ? 6.220   -3.043  31.435  1.00 22.57 ? 259  ARG A CB    1 
ATOM   2016 C  CG    . ARG A 1 259 ? 7.637   -2.930  31.982  1.00 26.91 ? 259  ARG A CG    1 
ATOM   2017 C  CD    . ARG A 1 259 ? 8.619   -2.336  30.991  1.00 28.40 ? 259  ARG A CD    1 
ATOM   2018 N  NE    . ARG A 1 259 ? 9.985   -2.384  31.494  1.00 31.40 ? 259  ARG A NE    1 
ATOM   2019 C  CZ    . ARG A 1 259 ? 10.666  -1.355  32.024  1.00 32.37 ? 259  ARG A CZ    1 
ATOM   2020 N  NH1   . ARG A 1 259 ? 10.136  -0.148  32.136  1.00 30.87 ? 259  ARG A NH1   1 
ATOM   2021 N  NH2   . ARG A 1 259 ? 11.909  -1.534  32.411  1.00 30.86 ? 259  ARG A NH2   1 
ATOM   2022 N  N     . LEU A 1 260 ? 3.698   -4.821  30.444  1.00 21.24 ? 260  LEU A N     1 
ATOM   2023 C  CA    . LEU A 1 260 ? 2.318   -4.907  29.906  1.00 19.16 ? 260  LEU A CA    1 
ATOM   2024 C  C     . LEU A 1 260 ? 1.440   -5.743  30.843  1.00 19.73 ? 260  LEU A C     1 
ATOM   2025 O  O     . LEU A 1 260 ? 0.248   -5.402  31.008  1.00 20.21 ? 260  LEU A O     1 
ATOM   2026 C  CB    . LEU A 1 260 ? 2.366   -5.492  28.491  1.00 20.19 ? 260  LEU A CB    1 
ATOM   2027 C  CG    . LEU A 1 260 ? 2.785   -4.533  27.376  1.00 18.97 ? 260  LEU A CG    1 
ATOM   2028 C  CD1   . LEU A 1 260 ? 2.963   -5.302  26.080  1.00 19.72 ? 260  LEU A CD1   1 
ATOM   2029 C  CD2   . LEU A 1 260 ? 1.773   -3.420  27.167  1.00 20.10 ? 260  LEU A CD2   1 
ATOM   2030 N  N     . ARG A 1 261 ? 1.998   -6.767  31.499  1.00 21.63 ? 261  ARG A N     1 
ATOM   2031 C  CA    . ARG A 1 261 ? 1.187   -7.755  32.253  1.00 20.90 ? 261  ARG A CA    1 
ATOM   2032 C  C     . ARG A 1 261 ? 0.260   -7.075  33.261  1.00 22.34 ? 261  ARG A C     1 
ATOM   2033 O  O     . ARG A 1 261 ? -0.958  -7.241  33.176  1.00 20.24 ? 261  ARG A O     1 
ATOM   2034 C  CB    . ARG A 1 261 ? 2.060   -8.780  32.971  1.00 22.83 ? 261  ARG A CB    1 
ATOM   2035 C  CG    . ARG A 1 261 ? 1.244   -9.724  33.836  1.00 23.52 ? 261  ARG A CG    1 
ATOM   2036 C  CD    . ARG A 1 261 ? 2.079   -10.828 34.435  1.00 25.48 ? 261  ARG A CD    1 
ATOM   2037 N  NE    . ARG A 1 261 ? 3.227   -10.335 35.168  1.00 25.54 ? 261  ARG A NE    1 
ATOM   2038 C  CZ    . ARG A 1 261 ? 4.495   -10.433 34.782  1.00 26.00 ? 261  ARG A CZ    1 
ATOM   2039 N  NH1   . ARG A 1 261 ? 4.846   -10.968 33.619  1.00 24.09 ? 261  ARG A NH1   1 
ATOM   2040 N  NH2   . ARG A 1 261 ? 5.434   -9.978  35.588  1.00 26.15 ? 261  ARG A NH2   1 
ATOM   2041 N  N     . PRO A 1 262 ? 0.758   -6.328  34.273  1.00 20.93 ? 262  PRO A N     1 
ATOM   2042 C  CA    . PRO A 1 262 ? -0.141  -5.772  35.290  1.00 21.16 ? 262  PRO A CA    1 
ATOM   2043 C  C     . PRO A 1 262 ? -1.115  -4.751  34.685  1.00 18.55 ? 262  PRO A C     1 
ATOM   2044 O  O     . PRO A 1 262 ? -2.189  -4.606  35.156  1.00 18.08 ? 262  PRO A O     1 
ATOM   2045 C  CB    . PRO A 1 262 ? 0.803   -5.148  36.336  1.00 20.60 ? 262  PRO A CB    1 
ATOM   2046 C  CG    . PRO A 1 262 ? 2.084   -4.880  35.583  1.00 21.67 ? 262  PRO A CG    1 
ATOM   2047 C  CD    . PRO A 1 262 ? 2.159   -5.958  34.511  1.00 22.27 ? 262  PRO A CD    1 
ATOM   2048 N  N     . LEU A 1 263 ? -0.714  -4.061  33.635  1.00 19.11 ? 263  LEU A N     1 
ATOM   2049 C  CA    . LEU A 1 263 ? -1.549  -2.997  33.031  1.00 19.05 ? 263  LEU A CA    1 
ATOM   2050 C  C     . LEU A 1 263 ? -2.745  -3.660  32.339  1.00 18.39 ? 263  LEU A C     1 
ATOM   2051 O  O     . LEU A 1 263 ? -3.862  -3.087  32.375  1.00 20.73 ? 263  LEU A O     1 
ATOM   2052 C  CB    . LEU A 1 263 ? -0.705  -2.195  32.043  1.00 20.77 ? 263  LEU A CB    1 
ATOM   2053 C  CG    . LEU A 1 263 ? 0.441   -1.357  32.626  1.00 22.53 ? 263  LEU A CG    1 
ATOM   2054 C  CD1   . LEU A 1 263 ? 1.296   -0.815  31.488  1.00 22.30 ? 263  LEU A CD1   1 
ATOM   2055 C  CD2   . LEU A 1 263 ? -0.084  -0.201  33.477  1.00 21.41 ? 263  LEU A CD2   1 
ATOM   2056 N  N     . LYS A 1 264 ? -2.548  -4.849  31.775  1.00 18.63 ? 264  LYS A N     1 
ATOM   2057 C  CA    . LYS A 1 264 ? -3.625  -5.596  31.067  1.00 17.99 ? 264  LYS A CA    1 
ATOM   2058 C  C     . LYS A 1 264 ? -4.493  -6.357  32.065  1.00 17.50 ? 264  LYS A C     1 
ATOM   2059 O  O     . LYS A 1 264 ? -5.724  -6.222  31.996  1.00 17.55 ? 264  LYS A O     1 
ATOM   2060 C  CB    . LYS A 1 264 ? -3.025  -6.500  29.991  1.00 18.54 ? 264  LYS A CB    1 
ATOM   2061 C  CG    . LYS A 1 264 ? -2.730  -5.808  28.667  1.00 20.10 ? 264  LYS A CG    1 
ATOM   2062 C  CD    . LYS A 1 264 ? -3.943  -5.158  28.029  1.00 22.22 ? 264  LYS A CD    1 
ATOM   2063 C  CE    . LYS A 1 264 ? -5.010  -6.106  27.525  1.00 23.54 ? 264  LYS A CE    1 
ATOM   2064 N  NZ    . LYS A 1 264 ? -6.316  -5.409  27.373  1.00 24.07 ? 264  LYS A NZ    1 
ATOM   2065 N  N     . VAL A 1 265 ? -3.896  -7.038  33.040  1.00 18.44 ? 265  VAL A N     1 
ATOM   2066 C  CA    . VAL A 1 265 ? -4.674  -7.803  34.049  1.00 20.05 ? 265  VAL A CA    1 
ATOM   2067 C  C     . VAL A 1 265 ? -5.628  -6.864  34.822  1.00 21.86 ? 265  VAL A C     1 
ATOM   2068 O  O     . VAL A 1 265 ? -6.817  -7.270  35.051  1.00 19.68 ? 265  VAL A O     1 
ATOM   2069 C  CB    . VAL A 1 265 ? -3.733  -8.611  34.951  1.00 20.97 ? 265  VAL A CB    1 
ATOM   2070 C  CG1   . VAL A 1 265 ? -4.489  -9.315  36.066  1.00 21.55 ? 265  VAL A CG1   1 
ATOM   2071 C  CG2   . VAL A 1 265 ? -2.940  -9.627  34.128  1.00 21.77 ? 265  VAL A CG2   1 
ATOM   2072 N  N     . ALA A 1 266 ? -5.161  -5.657  35.184  1.00 21.87 ? 266  ALA A N     1 
ATOM   2073 C  CA    . ALA A 1 266 ? -5.919  -4.633  35.947  1.00 23.05 ? 266  ALA A CA    1 
ATOM   2074 C  C     . ALA A 1 266 ? -6.902  -3.857  35.046  1.00 24.23 ? 266  ALA A C     1 
ATOM   2075 O  O     . ALA A 1 266 ? -7.862  -3.289  35.587  1.00 27.56 ? 266  ALA A O     1 
ATOM   2076 C  CB    . ALA A 1 266 ? -4.932  -3.690  36.628  1.00 23.81 ? 266  ALA A CB    1 
ATOM   2077 N  N     . GLY A 1 267 ? -6.719  -3.868  33.715  1.00 23.78 ? 267  GLY A N     1 
ATOM   2078 C  CA    . GLY A 1 267 ? -7.596  -3.134  32.774  1.00 22.32 ? 267  GLY A CA    1 
ATOM   2079 C  C     . GLY A 1 267 ? -7.198  -1.661  32.611  1.00 22.52 ? 267  GLY A C     1 
ATOM   2080 O  O     . GLY A 1 267 ? -8.021  -0.866  32.127  1.00 24.54 ? 267  GLY A O     1 
ATOM   2081 N  N     . VAL A 1 268 ? -5.957  -1.299  32.926  1.00 21.93 ? 268  VAL A N     1 
ATOM   2082 C  CA    . VAL A 1 268 ? -5.414  0.071   32.727  1.00 22.32 ? 268  VAL A CA    1 
ATOM   2083 C  C     . VAL A 1 268 ? -5.272  0.348   31.221  1.00 22.31 ? 268  VAL A C     1 
ATOM   2084 O  O     . VAL A 1 268 ? -5.635  1.443   30.771  1.00 21.85 ? 268  VAL A O     1 
ATOM   2085 C  CB    . VAL A 1 268 ? -4.086  0.240   33.480  1.00 22.81 ? 268  VAL A CB    1 
ATOM   2086 C  CG1   . VAL A 1 268 ? -3.503  1.615   33.235  1.00 22.10 ? 268  VAL A CG1   1 
ATOM   2087 C  CG2   . VAL A 1 268 ? -4.271  -0.012  34.973  1.00 24.80 ? 268  VAL A CG2   1 
ATOM   2088 N  N     . ILE A 1 269 ? -4.763  -0.620  30.459  1.00 22.37 ? 269  ILE A N     1 
ATOM   2089 C  CA    . ILE A 1 269 ? -4.840  -0.586  28.978  1.00 22.55 ? 269  ILE A CA    1 
ATOM   2090 C  C     . ILE A 1 269 ? -6.228  -1.105  28.622  1.00 23.23 ? 269  ILE A C     1 
ATOM   2091 O  O     . ILE A 1 269 ? -6.536  -2.250  28.978  1.00 23.41 ? 269  ILE A O     1 
ATOM   2092 C  CB    . ILE A 1 269 ? -3.700  -1.402  28.350  1.00 22.61 ? 269  ILE A CB    1 
ATOM   2093 C  CG1   . ILE A 1 269 ? -2.353  -0.755  28.662  1.00 23.06 ? 269  ILE A CG1   1 
ATOM   2094 C  CG2   . ILE A 1 269 ? -3.919  -1.572  26.869  1.00 22.50 ? 269  ILE A CG2   1 
ATOM   2095 C  CD1   . ILE A 1 269 ? -1.149  -1.635  28.434  1.00 24.56 ? 269  ILE A CD1   1 
ATOM   2096 N  N     . GLN A 1 270 ? -7.057  -0.267  27.995  1.00 21.77 ? 270  GLN A N     1 
ATOM   2097 C  CA    . GLN A 1 270 ? -8.511  -0.547  27.888  1.00 20.11 ? 270  GLN A CA    1 
ATOM   2098 C  C     . GLN A 1 270 ? -8.836  -1.424  26.671  1.00 19.43 ? 270  GLN A C     1 
ATOM   2099 O  O     . GLN A 1 270 ? -9.872  -2.026  26.689  1.00 19.12 ? 270  GLN A O     1 
ATOM   2100 C  CB    . GLN A 1 270 ? -9.257  0.769   27.822  1.00 20.92 ? 270  GLN A CB    1 
ATOM   2101 C  CG    . GLN A 1 270 ? -9.213  1.535   29.131  1.00 20.00 ? 270  GLN A CG    1 
ATOM   2102 C  CD    . GLN A 1 270 ? -9.503  2.983   28.817  1.00 19.77 ? 270  GLN A CD    1 
ATOM   2103 O  OE1   . GLN A 1 270 ? -8.710  3.675   28.176  1.00 19.59 ? 270  GLN A OE1   1 
ATOM   2104 N  NE2   . GLN A 1 270 ? -10.673 3.433   29.217  1.00 19.05 ? 270  GLN A NE2   1 
ATOM   2105 N  N     . ASN A 1 271 ? -8.012  -1.448  25.629  1.00 19.42 ? 271  ASN A N     1 
ATOM   2106 C  CA    . ASN A 1 271 ? -8.220  -2.343  24.462  1.00 20.86 ? 271  ASN A CA    1 
ATOM   2107 C  C     . ASN A 1 271 ? -7.137  -3.431  24.463  1.00 21.64 ? 271  ASN A C     1 
ATOM   2108 O  O     . ASN A 1 271 ? -6.287  -3.463  25.406  1.00 20.79 ? 271  ASN A O     1 
ATOM   2109 C  CB    . ASN A 1 271 ? -8.266  -1.557  23.155  1.00 19.76 ? 271  ASN A CB    1 
ATOM   2110 C  CG    . ASN A 1 271 ? -7.041  -0.712  22.903  1.00 21.53 ? 271  ASN A CG    1 
ATOM   2111 O  OD1   . ASN A 1 271 ? -6.265  -0.392  23.821  1.00 22.71 ? 271  ASN A OD1   1 
ATOM   2112 N  ND2   . ASN A 1 271 ? -6.900  -0.301  21.656  1.00 23.15 ? 271  ASN A ND2   1 
ATOM   2113 N  N     . GLY A 1 272 ? -7.164  -4.308  23.460  1.00 22.89 ? 272  GLY A N     1 
ATOM   2114 C  CA    . GLY A 1 272 ? -6.080  -5.274  23.221  1.00 21.24 ? 272  GLY A CA    1 
ATOM   2115 C  C     . GLY A 1 272 ? -4.782  -4.519  23.069  1.00 22.27 ? 272  GLY A C     1 
ATOM   2116 O  O     . GLY A 1 272 ? -4.825  -3.426  22.462  1.00 24.06 ? 272  GLY A O     1 
ATOM   2117 N  N     . ALA A 1 273 ? -3.708  -4.981  23.709  1.00 21.11 ? 273  ALA A N     1 
ATOM   2118 C  CA    . ALA A 1 273 ? -2.327  -4.491  23.492  1.00 21.25 ? 273  ALA A CA    1 
ATOM   2119 C  C     . ALA A 1 273 ? -1.740  -5.269  22.314  1.00 21.81 ? 273  ALA A C     1 
ATOM   2120 O  O     . ALA A 1 273 ? -1.790  -6.505  22.349  1.00 20.64 ? 273  ALA A O     1 
ATOM   2121 C  CB    . ALA A 1 273 ? -1.495  -4.676  24.728  1.00 21.87 ? 273  ALA A CB    1 
ATOM   2122 N  N     . THR A 1 274 ? -1.288  -4.564  21.284  1.00 20.86 ? 274  THR A N     1 
ATOM   2123 C  CA    . THR A 1 274 ? -0.660  -5.166  20.079  1.00 23.60 ? 274  THR A CA    1 
ATOM   2124 C  C     . THR A 1 274 ? 0.733   -4.567  19.930  1.00 19.63 ? 274  THR A C     1 
ATOM   2125 O  O     . THR A 1 274 ? 0.813   -3.330  19.817  1.00 18.83 ? 274  THR A O     1 
ATOM   2126 C  CB    . THR A 1 274 ? -1.440  -4.882  18.784  1.00 24.26 ? 274  THR A CB    1 
ATOM   2127 O  OG1   . THR A 1 274 ? -2.826  -5.008  19.041  1.00 28.30 ? 274  THR A OG1   1 
ATOM   2128 C  CG2   . THR A 1 274 ? -1.109  -5.867  17.697  1.00 28.15 ? 274  THR A CG2   1 
ATOM   2129 N  N     . VAL A 1 275 ? 1.758   -5.409  19.949  1.00 18.07 ? 275  VAL A N     1 
ATOM   2130 C  CA    . VAL A 1 275 ? 3.170   -4.984  19.789  1.00 20.71 ? 275  VAL A CA    1 
ATOM   2131 C  C     . VAL A 1 275 ? 3.720   -5.637  18.512  1.00 21.98 ? 275  VAL A C     1 
ATOM   2132 O  O     . VAL A 1 275 ? 4.014   -6.854  18.519  1.00 21.63 ? 275  VAL A O     1 
ATOM   2133 C  CB    . VAL A 1 275 ? 3.994   -5.296  21.052  1.00 19.87 ? 275  VAL A CB    1 
ATOM   2134 C  CG1   . VAL A 1 275 ? 5.365   -4.645  21.016  1.00 22.22 ? 275  VAL A CG1   1 
ATOM   2135 C  CG2   . VAL A 1 275 ? 3.260   -4.866  22.299  1.00 21.21 ? 275  VAL A CG2   1 
ATOM   2136 N  N     . ARG A 1 276 ? 3.829   -4.851  17.452  1.00 21.23 ? 276  ARG A N     1 
ATOM   2137 C  CA    . ARG A 1 276 ? 4.130   -5.362  16.095  1.00 23.90 ? 276  ARG A CA    1 
ATOM   2138 C  C     . ARG A 1 276 ? 5.617   -5.167  15.801  1.00 22.60 ? 276  ARG A C     1 
ATOM   2139 O  O     . ARG A 1 276 ? 6.203   -4.151  16.221  1.00 20.78 ? 276  ARG A O     1 
ATOM   2140 C  CB    . ARG A 1 276 ? 3.250   -4.646  15.074  1.00 25.61 ? 276  ARG A CB    1 
ATOM   2141 C  CG    . ARG A 1 276 ? 1.761   -4.952  15.170  1.00 27.93 ? 276  ARG A CG    1 
ATOM   2142 C  CD    . ARG A 1 276 ? 1.017   -4.360  13.974  1.00 31.66 ? 276  ARG A CD    1 
ATOM   2143 N  NE    . ARG A 1 276 ? -0.424  -4.498  14.092  1.00 34.99 ? 276  ARG A NE    1 
ATOM   2144 C  CZ    . ARG A 1 276 ? -1.174  -3.827  14.961  1.00 42.49 ? 276  ARG A CZ    1 
ATOM   2145 N  NH1   . ARG A 1 276 ? -0.628  -2.929  15.778  1.00 46.11 ? 276  ARG A NH1   1 
ATOM   2146 N  NH2   . ARG A 1 276 ? -2.482  -4.028  14.992  1.00 46.56 ? 276  ARG A NH2   1 
ATOM   2147 N  N     . SER A 1 277 ? 6.197   -6.142  15.117  1.00 19.10 ? 277  SER A N     1 
ATOM   2148 C  CA    . SER A 1 277 ? 7.584   -6.137  14.621  1.00 19.64 ? 277  SER A CA    1 
ATOM   2149 C  C     . SER A 1 277 ? 7.686   -5.113  13.510  1.00 20.79 ? 277  SER A C     1 
ATOM   2150 O  O     . SER A 1 277 ? 6.668   -4.843  12.823  1.00 20.44 ? 277  SER A O     1 
ATOM   2151 C  CB    . SER A 1 277 ? 8.002   -7.514  14.116  1.00 20.91 ? 277  SER A CB    1 
ATOM   2152 O  OG    . SER A 1 277 ? 7.381   -7.808  12.874  1.00 19.54 ? 277  SER A OG    1 
ATOM   2153 N  N     . LEU A 1 278 ? 8.896   -4.589  13.341  1.00 22.89 ? 278  LEU A N     1 
ATOM   2154 C  CA    . LEU A 1 278 ? 9.251   -3.571  12.329  1.00 22.23 ? 278  LEU A CA    1 
ATOM   2155 C  C     . LEU A 1 278 ? 8.642   -3.914  10.963  1.00 22.01 ? 278  LEU A C     1 
ATOM   2156 O  O     . LEU A 1 278 ? 7.909   -3.065  10.392  1.00 24.45 ? 278  LEU A O     1 
ATOM   2157 C  CB    . LEU A 1 278 ? 10.776  -3.518  12.269  1.00 22.15 ? 278  LEU A CB    1 
ATOM   2158 C  CG    . LEU A 1 278 ? 11.363  -2.667  11.149  1.00 23.27 ? 278  LEU A CG    1 
ATOM   2159 C  CD1   . LEU A 1 278 ? 10.926  -1.212  11.281  1.00 23.35 ? 278  LEU A CD1   1 
ATOM   2160 C  CD2   . LEU A 1 278 ? 12.873  -2.795  11.138  1.00 25.13 ? 278  LEU A CD2   1 
ATOM   2161 N  N     . VAL A 1 279 ? 8.934   -5.090  10.420  1.00 23.06 ? 279  VAL A N     1 
ATOM   2162 C  CA    . VAL A 1 279 ? 8.570   -5.381  9.002   1.00 23.48 ? 279  VAL A CA    1 
ATOM   2163 C  C     . VAL A 1 279 ? 7.041   -5.459  8.880   1.00 22.99 ? 279  VAL A C     1 
ATOM   2164 O  O     . VAL A 1 279 ? 6.517   -5.024  7.871   1.00 25.80 ? 279  VAL A O     1 
ATOM   2165 C  CB    . VAL A 1 279 ? 9.237   -6.667  8.488   1.00 25.30 ? 279  VAL A CB    1 
ATOM   2166 C  CG1   . VAL A 1 279 ? 8.788   -6.996  7.071   1.00 27.87 ? 279  VAL A CG1   1 
ATOM   2167 C  CG2   . VAL A 1 279 ? 10.745  -6.572  8.541   1.00 25.14 ? 279  VAL A CG2   1 
ATOM   2168 N  N     . LEU A 1 280 ? 6.341   -6.037  9.851   1.00 22.36 ? 280  LEU A N     1 
ATOM   2169 C  CA    . LEU A 1 280 ? 4.865   -6.099  9.825   1.00 22.69 ? 280  LEU A CA    1 
ATOM   2170 C  C     . LEU A 1 280 ? 4.296   -4.675  9.686   1.00 23.86 ? 280  LEU A C     1 
ATOM   2171 O  O     . LEU A 1 280 ? 3.409   -4.467  8.848   1.00 22.28 ? 280  LEU A O     1 
ATOM   2172 C  CB    . LEU A 1 280 ? 4.353   -6.799  11.090  1.00 23.03 ? 280  LEU A CB    1 
ATOM   2173 C  CG    . LEU A 1 280 ? 2.830   -6.983  11.158  1.00 23.34 ? 280  LEU A CG    1 
ATOM   2174 C  CD1   . LEU A 1 280 ? 2.313   -7.646  9.891   1.00 23.34 ? 280  LEU A CD1   1 
ATOM   2175 C  CD2   . LEU A 1 280 ? 2.435   -7.797  12.373  1.00 23.81 ? 280  LEU A CD2   1 
ATOM   2176 N  N     . ASP A 1 281 ? 4.802   -3.722  10.463  1.00 23.44 ? 281  ASP A N     1 
ATOM   2177 C  CA    . ASP A 1 281 ? 4.307   -2.319  10.450  1.00 26.51 ? 281  ASP A CA    1 
ATOM   2178 C  C     . ASP A 1 281 ? 4.780   -1.579  9.180   1.00 23.28 ? 281  ASP A C     1 
ATOM   2179 O  O     . ASP A 1 281 ? 3.964   -0.874  8.602   1.00 21.96 ? 281  ASP A O     1 
ATOM   2180 C  CB    . ASP A 1 281 ? 4.653   -1.617  11.764  1.00 29.71 ? 281  ASP A CB    1 
ATOM   2181 C  CG    . ASP A 1 281 ? 3.602   -1.822  12.857  1.00 36.20 ? 281  ASP A CG    1 
ATOM   2182 O  OD1   . ASP A 1 281 ? 2.412   -2.010  12.523  1.00 37.78 ? 281  ASP A OD1   1 
ATOM   2183 O  OD2   . ASP A 1 281 ? 3.973   -1.773  14.039  1.00 39.27 ? 281  ASP A OD2   1 
ATOM   2184 N  N     . ALA A 1 282 ? 6.022   -1.749  8.742   1.00 24.47 ? 282  ALA A N     1 
ATOM   2185 C  CA    . ALA A 1 282 ? 6.563   -1.110  7.517   1.00 25.24 ? 282  ALA A CA    1 
ATOM   2186 C  C     . ALA A 1 282 ? 5.742   -1.524  6.289   1.00 26.89 ? 282  ALA A C     1 
ATOM   2187 O  O     . ALA A 1 282 ? 5.595   -0.686  5.377   1.00 27.19 ? 282  ALA A O     1 
ATOM   2188 C  CB    . ALA A 1 282 ? 8.007   -1.512  7.328   1.00 27.24 ? 282  ALA A CB    1 
ATOM   2189 N  N     . ALA A 1 283 ? 5.309   -2.789  6.223   1.00 25.91 ? 283  ALA A N     1 
ATOM   2190 C  CA    . ALA A 1 283 ? 4.627   -3.388  5.050   1.00 27.58 ? 283  ALA A CA    1 
ATOM   2191 C  C     . ALA A 1 283 ? 3.296   -2.678  4.727   1.00 27.97 ? 283  ALA A C     1 
ATOM   2192 O  O     . ALA A 1 283 ? 2.800   -2.902  3.614   1.00 24.34 ? 283  ALA A O     1 
ATOM   2193 C  CB    . ALA A 1 283 ? 4.376   -4.858  5.273   1.00 27.20 ? 283  ALA A CB    1 
ATOM   2194 N  N     . ILE A 1 284 ? 2.701   -1.929  5.659   1.00 27.70 ? 284  ILE A N     1 
ATOM   2195 C  CA    . ILE A 1 284 ? 1.469   -1.118  5.384   1.00 35.44 ? 284  ILE A CA    1 
ATOM   2196 C  C     . ILE A 1 284 ? 1.807   -0.077  4.312   1.00 36.96 ? 284  ILE A C     1 
ATOM   2197 O  O     . ILE A 1 284 ? 1.178   -0.132  3.205   1.00 40.53 ? 284  ILE A O     1 
ATOM   2198 C  CB    . ILE A 1 284 ? 0.895   -0.472  6.666   1.00 38.52 ? 284  ILE A CB    1 
ATOM   2199 C  CG1   . ILE A 1 284 ? 0.453   -1.541  7.668   1.00 42.09 ? 284  ILE A CG1   1 
ATOM   2200 C  CG2   . ILE A 1 284 ? -0.260  0.474   6.347   1.00 39.66 ? 284  ILE A CG2   1 
ATOM   2201 C  CD1   . ILE A 1 284 ? -0.463  -2.612  7.056   1.00 40.85 ? 284  ILE A CD1   1 
ATOM   2202 N  N     . THR A 1 285 ? 2.854   0.716   4.570   1.00 37.40 ? 285  THR A N     1 
ATOM   2203 C  CA    . THR A 1 285 ? 3.224   1.921   3.774   1.00 36.45 ? 285  THR A CA    1 
ATOM   2204 C  C     . THR A 1 285 ? 4.411   1.674   2.841   1.00 35.60 ? 285  THR A C     1 
ATOM   2205 O  O     . THR A 1 285 ? 4.627   2.560   2.032   1.00 42.19 ? 285  THR A O     1 
ATOM   2206 C  CB    . THR A 1 285 ? 3.492   3.122   4.689   1.00 34.98 ? 285  THR A CB    1 
ATOM   2207 O  OG1   . THR A 1 285 ? 4.712   2.906   5.392   1.00 32.81 ? 285  THR A OG1   1 
ATOM   2208 C  CG2   . THR A 1 285 ? 2.381   3.360   5.694   1.00 35.05 ? 285  THR A CG2   1 
ATOM   2209 N  N     . ARG A 1 286 ? 5.145   0.552   2.917   1.00 35.54 ? 286  ARG A N     1 
ATOM   2210 C  CA    . ARG A 1 286 ? 6.404   0.362   2.137   1.00 32.18 ? 286  ARG A CA    1 
ATOM   2211 C  C     . ARG A 1 286 ? 6.530   -1.054  1.576   1.00 31.53 ? 286  ARG A C     1 
ATOM   2212 O  O     . ARG A 1 286 ? 5.886   -1.958  2.116   1.00 34.25 ? 286  ARG A O     1 
ATOM   2213 C  CB    . ARG A 1 286 ? 7.635   0.646   2.999   1.00 33.54 ? 286  ARG A CB    1 
ATOM   2214 C  CG    . ARG A 1 286 ? 7.778   2.092   3.435   1.00 34.04 ? 286  ARG A CG    1 
ATOM   2215 C  CD    . ARG A 1 286 ? 8.190   2.976   2.270   1.00 36.18 ? 286  ARG A CD    1 
ATOM   2216 N  NE    . ARG A 1 286 ? 8.409   4.334   2.744   1.00 37.74 ? 286  ARG A NE    1 
ATOM   2217 C  CZ    . ARG A 1 286 ? 7.448   5.207   2.998   1.00 37.96 ? 286  ARG A CZ    1 
ATOM   2218 N  NH1   . ARG A 1 286 ? 6.185   4.886   2.779   1.00 40.81 ? 286  ARG A NH1   1 
ATOM   2219 N  NH2   . ARG A 1 286 ? 7.750   6.415   3.441   1.00 36.41 ? 286  ARG A NH2   1 
ATOM   2220 N  N     . THR A 1 287 ? 7.377   -1.242  0.553   1.00 31.51 ? 287  THR A N     1 
ATOM   2221 C  CA    . THR A 1 287 ? 7.788   -2.582  0.039   1.00 31.93 ? 287  THR A CA    1 
ATOM   2222 C  C     . THR A 1 287 ? 9.283   -2.850  0.282   1.00 30.70 ? 287  THR A C     1 
ATOM   2223 O  O     . THR A 1 287 ? 10.085  -1.893  0.381   1.00 30.38 ? 287  THR A O     1 
ATOM   2224 C  CB    . THR A 1 287 ? 7.428   -2.771  -1.435  1.00 32.12 ? 287  THR A CB    1 
ATOM   2225 O  OG1   . THR A 1 287 ? 8.288   -1.934  -2.207  1.00 36.30 ? 287  THR A OG1   1 
ATOM   2226 C  CG2   . THR A 1 287 ? 5.974   -2.463  -1.700  1.00 33.43 ? 287  THR A CG2   1 
ATOM   2227 N  N     . LYS A 1 288 ? 9.649   -4.125  0.357   1.00 31.78 ? 288  LYS A N     1 
ATOM   2228 C  CA    . LYS A 1 288 ? 11.049  -4.550  0.641   1.00 35.99 ? 288  LYS A CA    1 
ATOM   2229 C  C     . LYS A 1 288 ? 11.993  -3.927  -0.404  1.00 36.34 ? 288  LYS A C     1 
ATOM   2230 O  O     . LYS A 1 288 ? 13.049  -3.408  0.003   1.00 35.15 ? 288  LYS A O     1 
ATOM   2231 C  CB    . LYS A 1 288 ? 11.180  -6.074  0.659   1.00 36.47 ? 288  LYS A CB    1 
ATOM   2232 C  CG    . LYS A 1 288 ? 12.507  -6.561  1.220   1.00 39.10 ? 288  LYS A CG    1 
ATOM   2233 C  CD    . LYS A 1 288 ? 12.649  -8.054  1.317   1.00 42.40 ? 288  LYS A CD    1 
ATOM   2234 C  CE    . LYS A 1 288 ? 12.613  -8.760  -0.025  1.00 49.18 ? 288  LYS A CE    1 
ATOM   2235 N  NZ    . LYS A 1 288 ? 12.860  -10.219 0.113   1.00 49.72 ? 288  LYS A NZ    1 
ATOM   2236 N  N     . SER A 1 289 ? 11.589  -3.924  -1.675  1.00 39.41 ? 289  SER A N     1 
ATOM   2237 C  CA    . SER A 1 289 ? 12.370  -3.414  -2.840  1.00 41.69 ? 289  SER A CA    1 
ATOM   2238 C  C     . SER A 1 289 ? 12.841  -1.967  -2.610  1.00 39.57 ? 289  SER A C     1 
ATOM   2239 O  O     . SER A 1 289 ? 13.875  -1.622  -3.160  1.00 39.81 ? 289  SER A O     1 
ATOM   2240 C  CB    . SER A 1 289 ? 11.569  -3.510  -4.102  1.00 41.16 ? 289  SER A CB    1 
ATOM   2241 O  OG    . SER A 1 289 ? 10.400  -2.721  -3.984  1.00 43.17 ? 289  SER A OG    1 
ATOM   2242 N  N     . GLN A 1 290 ? 12.151  -1.176  -1.784  1.00 36.58 ? 290  GLN A N     1 
ATOM   2243 C  CA    . GLN A 1 290 ? 12.473  0.254   -1.571  1.00 36.67 ? 290  GLN A CA    1 
ATOM   2244 C  C     . GLN A 1 290 ? 13.614  0.403   -0.553  1.00 38.94 ? 290  GLN A C     1 
ATOM   2245 O  O     . GLN A 1 290 ? 14.094  1.544   -0.374  1.00 39.95 ? 290  GLN A O     1 
ATOM   2246 C  CB    . GLN A 1 290 ? 11.267  1.032   -1.056  1.00 35.44 ? 290  GLN A CB    1 
ATOM   2247 C  CG    . GLN A 1 290 ? 10.011  0.901   -1.909  1.00 35.85 ? 290  GLN A CG    1 
ATOM   2248 C  CD    . GLN A 1 290 ? 8.913   1.746   -1.306  1.00 36.41 ? 290  GLN A CD    1 
ATOM   2249 O  OE1   . GLN A 1 290 ? 8.132   1.305   -0.471  1.00 35.45 ? 290  GLN A OE1   1 
ATOM   2250 N  NE2   . GLN A 1 290 ? 8.895   3.014   -1.661  1.00 36.40 ? 290  GLN A NE2   1 
ATOM   2251 N  N     . TYR A 1 291 ? 14.026  -0.668  0.121   1.00 36.32 ? 291  TYR A N     1 
ATOM   2252 C  CA    . TYR A 1 291 ? 15.181  -0.623  1.062   1.00 37.49 ? 291  TYR A CA    1 
ATOM   2253 C  C     . TYR A 1 291 ? 16.223  -1.722  0.766   1.00 36.57 ? 291  TYR A C     1 
ATOM   2254 O  O     . TYR A 1 291 ? 17.274  -1.630  1.382   1.00 42.39 ? 291  TYR A O     1 
ATOM   2255 C  CB    . TYR A 1 291 ? 14.722  -0.755  2.520   1.00 33.57 ? 291  TYR A CB    1 
ATOM   2256 C  CG    . TYR A 1 291 ? 13.737  0.284   2.983   1.00 31.98 ? 291  TYR A CG    1 
ATOM   2257 C  CD1   . TYR A 1 291 ? 14.148  1.561   3.322   1.00 32.94 ? 291  TYR A CD1   1 
ATOM   2258 C  CD2   . TYR A 1 291 ? 12.387  -0.013  3.100   1.00 31.15 ? 291  TYR A CD2   1 
ATOM   2259 C  CE1   . TYR A 1 291 ? 13.243  2.529   3.735   1.00 33.48 ? 291  TYR A CE1   1 
ATOM   2260 C  CE2   . TYR A 1 291 ? 11.463  0.948   3.488   1.00 31.32 ? 291  TYR A CE2   1 
ATOM   2261 C  CZ    . TYR A 1 291 ? 11.889  2.222   3.813   1.00 32.40 ? 291  TYR A CZ    1 
ATOM   2262 O  OH    . TYR A 1 291 ? 10.981  3.163   4.213   1.00 36.89 ? 291  TYR A OH    1 
ATOM   2263 N  N     . TYR A 1 292 ? 15.955  -2.747  -0.051  1.00 39.24 ? 292  TYR A N     1 
ATOM   2264 C  CA    . TYR A 1 292 ? 16.855  -3.926  -0.188  1.00 43.17 ? 292  TYR A CA    1 
ATOM   2265 C  C     . TYR A 1 292 ? 16.553  -4.697  -1.474  1.00 46.85 ? 292  TYR A C     1 
ATOM   2266 O  O     . TYR A 1 292 ? 15.358  -4.840  -1.819  1.00 52.75 ? 292  TYR A O     1 
ATOM   2267 C  CB    . TYR A 1 292 ? 16.752  -4.807  1.057   1.00 46.35 ? 292  TYR A CB    1 
ATOM   2268 C  CG    . TYR A 1 292 ? 17.571  -6.078  1.049   1.00 51.52 ? 292  TYR A CG    1 
ATOM   2269 C  CD1   . TYR A 1 292 ? 18.960  -6.058  0.991   1.00 52.77 ? 292  TYR A CD1   1 
ATOM   2270 C  CD2   . TYR A 1 292 ? 16.951  -7.320  1.129   1.00 54.62 ? 292  TYR A CD2   1 
ATOM   2271 C  CE1   . TYR A 1 292 ? 19.704  -7.233  1.001   1.00 52.18 ? 292  TYR A CE1   1 
ATOM   2272 C  CE2   . TYR A 1 292 ? 17.679  -8.500  1.128   1.00 57.37 ? 292  TYR A CE2   1 
ATOM   2273 C  CZ    . TYR A 1 292 ? 19.062  -8.457  1.074   1.00 56.55 ? 292  TYR A CZ    1 
ATOM   2274 O  OH    . TYR A 1 292 ? 19.762  -9.629  1.063   1.00 55.18 ? 292  TYR A OH    1 
ATOM   2275 N  N     . ASP A 1 293 ? 17.607  -5.204  -2.135  1.00 46.37 ? 293  ASP A N     1 
ATOM   2276 C  CA    . ASP A 1 293 ? 17.563  -5.783  -3.506  1.00 50.41 ? 293  ASP A CA    1 
ATOM   2277 C  C     . ASP A 1 293 ? 17.504  -7.308  -3.457  1.00 49.05 ? 293  ASP A C     1 
ATOM   2278 O  O     . ASP A 1 293 ? 17.075  -7.888  -4.461  1.00 47.99 ? 293  ASP A O     1 
ATOM   2279 C  CB    . ASP A 1 293 ? 18.774  -5.352  -4.343  1.00 57.34 ? 293  ASP A CB    1 
ATOM   2280 C  CG    . ASP A 1 293 ? 18.750  -3.875  -4.693  1.00 65.28 ? 293  ASP A CG    1 
ATOM   2281 O  OD1   . ASP A 1 293 ? 17.650  -3.294  -4.675  1.00 76.58 ? 293  ASP A OD1   1 
ATOM   2282 O  OD2   . ASP A 1 293 ? 19.827  -3.309  -4.956  1.00 68.29 ? 293  ASP A OD2   1 
ATOM   2283 N  N     . GLY A 1 294 ? 17.915  -7.936  -2.352  1.00 52.56 ? 294  GLY A N     1 
ATOM   2284 C  CA    . GLY A 1 294 ? 17.919  -9.410  -2.192  1.00 58.87 ? 294  GLY A CA    1 
ATOM   2285 C  C     . GLY A 1 294 ? 16.548  -10.053 -2.378  1.00 62.34 ? 294  GLY A C     1 
ATOM   2286 O  O     . GLY A 1 294 ? 15.522  -9.379  -2.107  1.00 60.57 ? 294  GLY A O     1 
ATOM   2287 N  N     . ASP A 1 295 ? 16.529  -11.318 -2.824  1.00 67.40 ? 295  ASP A N     1 
ATOM   2288 C  CA    . ASP A 1 295 ? 15.317  -12.181 -2.894  1.00 69.22 ? 295  ASP A CA    1 
ATOM   2289 C  C     . ASP A 1 295 ? 15.133  -12.901 -1.552  1.00 69.28 ? 295  ASP A C     1 
ATOM   2290 O  O     . ASP A 1 295 ? 14.079  -13.563 -1.380  1.00 72.25 ? 295  ASP A O     1 
ATOM   2291 C  CB    . ASP A 1 295 ? 15.398  -13.196 -4.037  1.00 72.07 ? 295  ASP A CB    1 
ATOM   2292 C  CG    . ASP A 1 295 ? 15.344  -12.578 -5.426  1.00 81.40 ? 295  ASP A CG    1 
ATOM   2293 O  OD1   . ASP A 1 295 ? 14.742  -11.486 -5.569  1.00 82.66 ? 295  ASP A OD1   1 
ATOM   2294 O  OD2   . ASP A 1 295 ? 15.901  -13.198 -6.362  1.00 82.79 ? 295  ASP A OD2   1 
ATOM   2295 N  N     . GLY A 1 296 ? 16.115  -12.785 -0.647  1.00 61.28 ? 296  GLY A N     1 
ATOM   2296 C  CA    . GLY A 1 296 ? 16.054  -13.348 0.715   1.00 57.63 ? 296  GLY A CA    1 
ATOM   2297 C  C     . GLY A 1 296 ? 15.392  -12.377 1.688   1.00 54.61 ? 296  GLY A C     1 
ATOM   2298 O  O     . GLY A 1 296 ? 15.050  -11.253 1.314   1.00 52.42 ? 296  GLY A O     1 
ATOM   2299 N  N     . PRO A 1 297 ? 15.164  -12.798 2.954   1.00 45.89 ? 297  PRO A N     1 
ATOM   2300 C  CA    . PRO A 1 297 ? 14.755  -11.876 4.014   1.00 42.06 ? 297  PRO A CA    1 
ATOM   2301 C  C     . PRO A 1 297 ? 15.834  -10.809 4.311   1.00 39.60 ? 297  PRO A C     1 
ATOM   2302 O  O     . PRO A 1 297 ? 16.978  -10.999 3.956   1.00 36.03 ? 297  PRO A O     1 
ATOM   2303 C  CB    . PRO A 1 297 ? 14.443  -12.768 5.235   1.00 44.02 ? 297  PRO A CB    1 
ATOM   2304 C  CG    . PRO A 1 297 ? 14.835  -14.193 4.857   1.00 45.53 ? 297  PRO A CG    1 
ATOM   2305 C  CD    . PRO A 1 297 ? 15.269  -14.193 3.405   1.00 46.29 ? 297  PRO A CD    1 
ATOM   2306 N  N     . ILE A 1 298 ? 15.431  -9.686  4.921   1.00 41.71 ? 298  ILE A N     1 
ATOM   2307 C  CA    . ILE A 1 298 ? 16.272  -8.460  5.056   1.00 41.05 ? 298  ILE A CA    1 
ATOM   2308 C  C     . ILE A 1 298 ? 17.423  -8.733  6.003   1.00 46.75 ? 298  ILE A C     1 
ATOM   2309 O  O     . ILE A 1 298 ? 17.306  -9.609  6.858   1.00 46.35 ? 298  ILE A O     1 
ATOM   2310 C  CB    . ILE A 1 298 ? 15.485  -7.210  5.500   1.00 41.31 ? 298  ILE A CB    1 
ATOM   2311 C  CG1   . ILE A 1 298 ? 14.872  -7.324  6.896   1.00 39.96 ? 298  ILE A CG1   1 
ATOM   2312 C  CG2   . ILE A 1 298 ? 14.447  -6.852  4.454   1.00 45.78 ? 298  ILE A CG2   1 
ATOM   2313 C  CD1   . ILE A 1 298 ? 14.596  -5.993  7.550   1.00 37.98 ? 298  ILE A CD1   1 
ATOM   2314 N  N     . PRO A 1 299 ? 18.546  -7.988  5.841   1.00 55.88 ? 299  PRO A N     1 
ATOM   2315 C  CA    . PRO A 1 299 ? 19.601  -7.880  6.851   1.00 57.51 ? 299  PRO A CA    1 
ATOM   2316 C  C     . PRO A 1 299 ? 19.421  -6.768  7.883   1.00 55.53 ? 299  PRO A C     1 
ATOM   2317 O  O     . PRO A 1 299 ? 18.690  -5.814  7.639   1.00 54.33 ? 299  PRO A O     1 
ATOM   2318 C  CB    . PRO A 1 299 ? 20.861  -7.517  6.045   1.00 58.13 ? 299  PRO A CB    1 
ATOM   2319 C  CG    . PRO A 1 299 ? 20.398  -7.315  4.601   1.00 57.54 ? 299  PRO A CG    1 
ATOM   2320 C  CD    . PRO A 1 299 ? 18.891  -7.234  4.628   1.00 56.11 ? 299  PRO A CD    1 
ATOM   2321 N  N     . PRO A 1 300 ? 20.148  -6.829  9.029   1.00 59.59 ? 300  PRO A N     1 
ATOM   2322 C  CA    . PRO A 1 300 ? 20.019  -5.845  10.107  1.00 57.90 ? 300  PRO A CA    1 
ATOM   2323 C  C     . PRO A 1 300 ? 20.316  -4.388  9.740   1.00 57.91 ? 300  PRO A C     1 
ATOM   2324 O  O     . PRO A 1 300 ? 19.786  -3.501  10.398  1.00 62.80 ? 300  PRO A O     1 
ATOM   2325 C  CB    . PRO A 1 300 ? 21.058  -6.287  11.155  1.00 57.34 ? 300  PRO A CB    1 
ATOM   2326 C  CG    . PRO A 1 300 ? 21.225  -7.768  10.898  1.00 58.15 ? 300  PRO A CG    1 
ATOM   2327 C  CD    . PRO A 1 300 ? 21.085  -7.911  9.394   1.00 59.38 ? 300  PRO A CD    1 
ATOM   2328 N  N     . SER A 1 301 ? 21.180  -4.152  8.761   1.00 54.12 ? 301  SER A N     1 
ATOM   2329 C  CA    . SER A 1 301 ? 21.571  -2.776  8.357   1.00 54.19 ? 301  SER A CA    1 
ATOM   2330 C  C     . SER A 1 301 ? 20.334  -2.079  7.789   1.00 50.64 ? 301  SER A C     1 
ATOM   2331 O  O     . SER A 1 301 ? 20.102  -0.897  8.108   1.00 51.61 ? 301  SER A O     1 
ATOM   2332 C  CB    . SER A 1 301 ? 22.693  -2.804  7.358   1.00 57.15 ? 301  SER A CB    1 
ATOM   2333 O  OG    . SER A 1 301 ? 22.503  -3.873  6.442   1.00 59.79 ? 301  SER A OG    1 
ATOM   2334 N  N     . VAL A 1 302 ? 19.539  -2.821  7.018   1.00 51.36 ? 302  VAL A N     1 
ATOM   2335 C  CA    . VAL A 1 302 ? 18.279  -2.307  6.400   1.00 52.52 ? 302  VAL A CA    1 
ATOM   2336 C  C     . VAL A 1 302 ? 17.353  -1.864  7.545   1.00 47.88 ? 302  VAL A C     1 
ATOM   2337 O  O     . VAL A 1 302 ? 16.933  -0.683  7.562   1.00 42.38 ? 302  VAL A O     1 
ATOM   2338 C  CB    . VAL A 1 302 ? 17.653  -3.377  5.484   1.00 52.75 ? 302  VAL A CB    1 
ATOM   2339 C  CG1   . VAL A 1 302 ? 16.250  -3.014  5.033   1.00 54.52 ? 302  VAL A CG1   1 
ATOM   2340 C  CG2   . VAL A 1 302 ? 18.549  -3.662  4.283   1.00 52.66 ? 302  VAL A CG2   1 
ATOM   2341 N  N     . ALA A 1 303 ? 17.148  -2.749  8.520   1.00 43.96 ? 303  ALA A N     1 
ATOM   2342 C  CA    . ALA A 1 303 ? 16.260  -2.537  9.684   1.00 44.70 ? 303  ALA A CA    1 
ATOM   2343 C  C     . ALA A 1 303 ? 16.504  -1.160  10.296  1.00 42.51 ? 303  ALA A C     1 
ATOM   2344 O  O     . ALA A 1 303 ? 15.502  -0.444  10.542  1.00 40.84 ? 303  ALA A O     1 
ATOM   2345 C  CB    . ALA A 1 303 ? 16.452  -3.641  10.690  1.00 47.14 ? 303  ALA A CB    1 
ATOM   2346 N  N     . LYS A 1 304 ? 17.772  -0.779  10.489  1.00 46.68 ? 304  LYS A N     1 
ATOM   2347 C  CA    . LYS A 1 304 ? 18.155  0.556   11.039  1.00 45.30 ? 304  LYS A CA    1 
ATOM   2348 C  C     . LYS A 1 304 ? 17.671  1.708   10.146  1.00 41.35 ? 304  LYS A C     1 
ATOM   2349 O  O     . LYS A 1 304 ? 17.246  2.724   10.711  1.00 43.71 ? 304  LYS A O     1 
ATOM   2350 C  CB    . LYS A 1 304 ? 19.665  0.640   11.280  1.00 48.29 ? 304  LYS A CB    1 
ATOM   2351 C  CG    . LYS A 1 304 ? 20.087  0.066   12.624  1.00 50.80 ? 304  LYS A CG    1 
ATOM   2352 C  CD    . LYS A 1 304 ? 21.402  0.599   13.125  1.00 57.57 ? 304  LYS A CD    1 
ATOM   2353 C  CE    . LYS A 1 304 ? 21.781  -0.016  14.454  1.00 59.47 ? 304  LYS A CE    1 
ATOM   2354 N  NZ    . LYS A 1 304 ? 23.108  -0.668  14.387  1.00 61.20 ? 304  LYS A NZ    1 
ATOM   2355 N  N     . THR A 1 305 ? 17.753  1.586   8.819   1.00 45.75 ? 305  THR A N     1 
ATOM   2356 C  CA    . THR A 1 305 ? 17.330  2.642   7.849   1.00 48.16 ? 305  THR A CA    1 
ATOM   2357 C  C     . THR A 1 305 ? 15.824  2.864   8.001   1.00 42.14 ? 305  THR A C     1 
ATOM   2358 O  O     . THR A 1 305 ? 15.385  4.031   8.254   1.00 41.64 ? 305  THR A O     1 
ATOM   2359 C  CB    . THR A 1 305 ? 17.651  2.271   6.392   1.00 50.05 ? 305  THR A CB    1 
ATOM   2360 O  OG1   . THR A 1 305 ? 18.992  1.795   6.291   1.00 55.32 ? 305  THR A OG1   1 
ATOM   2361 C  CG2   . THR A 1 305 ? 17.467  3.440   5.455   1.00 49.72 ? 305  THR A CG2   1 
ATOM   2362 N  N     . MET A 1 306 ? 15.079  1.763   7.874   1.00 42.44 ? 306  MET A N     1 
ATOM   2363 C  CA    . MET A 1 306 ? 13.598  1.712   7.979   1.00 39.17 ? 306  MET A CA    1 
ATOM   2364 C  C     . MET A 1 306 ? 13.179  2.384   9.285   1.00 35.18 ? 306  MET A C     1 
ATOM   2365 O  O     . MET A 1 306 ? 12.275  3.225   9.250   1.00 33.96 ? 306  MET A O     1 
ATOM   2366 C  CB    . MET A 1 306 ? 13.116  0.260   7.929   1.00 44.25 ? 306  MET A CB    1 
ATOM   2367 C  CG    . MET A 1 306 ? 13.257  -0.362  6.551   1.00 39.52 ? 306  MET A CG    1 
ATOM   2368 S  SD    . MET A 1 306 ? 12.953  -2.137  6.541   1.00 41.53 ? 306  MET A SD    1 
ATOM   2369 C  CE    . MET A 1 306 ? 11.212  -2.176  6.967   1.00 47.10 ? 306  MET A CE    1 
ATOM   2370 N  N     . MET A 1 307 ? 13.878  2.119   10.390  1.00 35.69 ? 307  MET A N     1 
ATOM   2371 C  CA    . MET A 1 307 ? 13.456  2.671   11.701  1.00 36.54 ? 307  MET A CA    1 
ATOM   2372 C  C     . MET A 1 307 ? 13.464  4.203   11.655  1.00 36.63 ? 307  MET A C     1 
ATOM   2373 O  O     . MET A 1 307 ? 12.434  4.815   12.068  1.00 31.63 ? 307  MET A O     1 
ATOM   2374 C  CB    . MET A 1 307 ? 14.349  2.184   12.840  1.00 38.17 ? 307  MET A CB    1 
ATOM   2375 C  CG    . MET A 1 307 ? 14.075  0.759   13.253  1.00 38.77 ? 307  MET A CG    1 
ATOM   2376 S  SD    . MET A 1 307 ? 15.322  0.143   14.422  1.00 42.77 ? 307  MET A SD    1 
ATOM   2377 C  CE    . MET A 1 307 ? 14.682  0.794   15.953  1.00 39.24 ? 307  MET A CE    1 
ATOM   2378 N  N     . ALA A 1 308 ? 14.565  4.808   11.195  1.00 37.98 ? 308  ALA A N     1 
ATOM   2379 C  CA    . ALA A 1 308 ? 14.746  6.283   11.212  1.00 40.88 ? 308  ALA A CA    1 
ATOM   2380 C  C     . ALA A 1 308 ? 13.805  6.899   10.182  1.00 38.04 ? 308  ALA A C     1 
ATOM   2381 O  O     . ALA A 1 308 ? 13.213  7.977   10.491  1.00 39.75 ? 308  ALA A O     1 
ATOM   2382 C  CB    . ALA A 1 308 ? 16.179  6.686   10.946  1.00 44.12 ? 308  ALA A CB    1 
ATOM   2383 N  N     . ASP A 1 309 ? 13.683  6.222   9.036   1.00 35.29 ? 309  ASP A N     1 
ATOM   2384 C  CA    . ASP A 1 309 ? 12.836  6.609   7.880   1.00 38.25 ? 309  ASP A CA    1 
ATOM   2385 C  C     . ASP A 1 309 ? 11.351  6.649   8.281   1.00 43.01 ? 309  ASP A C     1 
ATOM   2386 O  O     . ASP A 1 309 ? 10.656  7.638   7.933   1.00 40.21 ? 309  ASP A O     1 
ATOM   2387 C  CB    . ASP A 1 309 ? 13.048  5.631   6.721   1.00 41.45 ? 309  ASP A CB    1 
ATOM   2388 C  CG    . ASP A 1 309 ? 12.581  6.186   5.387   1.00 47.37 ? 309  ASP A CG    1 
ATOM   2389 O  OD1   . ASP A 1 309 ? 12.679  7.416   5.221   1.00 54.83 ? 309  ASP A OD1   1 
ATOM   2390 O  OD2   . ASP A 1 309 ? 12.124  5.399   4.527   1.00 44.90 ? 309  ASP A OD2   1 
ATOM   2391 N  N     . LEU A 1 310 ? 10.845  5.622   8.980   1.00 37.56 ? 310  LEU A N     1 
ATOM   2392 C  CA    . LEU A 1 310 ? 9.383   5.479   9.223   1.00 34.79 ? 310  LEU A CA    1 
ATOM   2393 C  C     . LEU A 1 310 ? 9.044   5.921   10.649  1.00 29.84 ? 310  LEU A C     1 
ATOM   2394 O  O     . LEU A 1 310 ? 7.864   5.968   10.983  1.00 28.14 ? 310  LEU A O     1 
ATOM   2395 C  CB    . LEU A 1 310 ? 8.999   4.019   8.954   1.00 34.16 ? 310  LEU A CB    1 
ATOM   2396 C  CG    . LEU A 1 310 ? 9.310   3.544   7.540   1.00 33.53 ? 310  LEU A CG    1 
ATOM   2397 C  CD1   . LEU A 1 310 ? 9.051   2.055   7.368   1.00 33.79 ? 310  LEU A CD1   1 
ATOM   2398 C  CD2   . LEU A 1 310 ? 8.490   4.337   6.532   1.00 34.88 ? 310  LEU A CD2   1 
ATOM   2399 N  N     . ASP A 1 311 ? 10.039  6.310   11.443  1.00 29.88 ? 311  ASP A N     1 
ATOM   2400 C  CA    . ASP A 1 311 ? 9.855   6.573   12.889  1.00 29.66 ? 311  ASP A CA    1 
ATOM   2401 C  C     . ASP A 1 311 ? 9.177   5.356   13.511  1.00 26.63 ? 311  ASP A C     1 
ATOM   2402 O  O     . ASP A 1 311 ? 8.083   5.492   14.097  1.00 28.14 ? 311  ASP A O     1 
ATOM   2403 C  CB    . ASP A 1 311 ? 9.010   7.824   13.134  1.00 36.00 ? 311  ASP A CB    1 
ATOM   2404 C  CG    . ASP A 1 311 ? 9.735   9.126   12.850  1.00 42.54 ? 311  ASP A CG    1 
ATOM   2405 O  OD1   . ASP A 1 311 ? 10.986  9.155   13.020  1.00 44.76 ? 311  ASP A OD1   1 
ATOM   2406 O  OD2   . ASP A 1 311 ? 9.034   10.106  12.484  1.00 48.62 ? 311  ASP A OD2   1 
ATOM   2407 N  N     . LEU A 1 312 ? 9.784   4.193   13.341  1.00 26.09 ? 312  LEU A N     1 
ATOM   2408 C  CA    . LEU A 1 312 ? 9.314   2.937   13.972  1.00 24.70 ? 312  LEU A CA    1 
ATOM   2409 C  C     . LEU A 1 312 ? 10.476  2.341   14.753  1.00 22.71 ? 312  LEU A C     1 
ATOM   2410 O  O     . LEU A 1 312 ? 11.618  2.630   14.408  1.00 22.00 ? 312  LEU A O     1 
ATOM   2411 C  CB    . LEU A 1 312 ? 8.830   1.954   12.895  1.00 23.45 ? 312  LEU A CB    1 
ATOM   2412 C  CG    . LEU A 1 312 ? 7.593   2.367   12.109  1.00 22.84 ? 312  LEU A CG    1 
ATOM   2413 C  CD1   . LEU A 1 312 ? 7.362   1.377   10.981  1.00 22.83 ? 312  LEU A CD1   1 
ATOM   2414 C  CD2   . LEU A 1 312 ? 6.364   2.457   13.005  1.00 23.98 ? 312  LEU A CD2   1 
ATOM   2415 N  N     . GLY A 1 313 ? 10.157  1.515   15.739  1.00 23.36 ? 313  GLY A N     1 
ATOM   2416 C  CA    . GLY A 1 313 ? 11.128  0.669   16.445  1.00 24.67 ? 313  GLY A CA    1 
ATOM   2417 C  C     . GLY A 1 313 ? 11.151  -0.731  15.843  1.00 25.43 ? 313  GLY A C     1 
ATOM   2418 O  O     . GLY A 1 313 ? 10.384  -0.996  14.889  1.00 24.72 ? 313  GLY A O     1 
ATOM   2419 N  N     . MET A 1 314 ? 11.960  -1.610  16.428  1.00 24.52 ? 314  MET A N     1 
ATOM   2420 C  CA    . MET A 1 314 ? 11.949  -3.065  16.140  1.00 25.89 ? 314  MET A CA    1 
ATOM   2421 C  C     . MET A 1 314 ? 10.621  -3.652  16.629  1.00 24.55 ? 314  MET A C     1 
ATOM   2422 O  O     . MET A 1 314 ? 10.218  -4.683  16.094  1.00 21.50 ? 314  MET A O     1 
ATOM   2423 C  CB    . MET A 1 314 ? 13.140  -3.758  16.817  1.00 26.89 ? 314  MET A CB    1 
ATOM   2424 C  CG    . MET A 1 314 ? 14.474  -3.351  16.205  1.00 29.03 ? 314  MET A CG    1 
ATOM   2425 S  SD    . MET A 1 314 ? 14.515  -3.559  14.410  1.00 33.74 ? 314  MET A SD    1 
ATOM   2426 C  CE    . MET A 1 314 ? 14.382  -5.337  14.310  1.00 29.70 ? 314  MET A CE    1 
ATOM   2427 N  N     . TRP A 1 315 ? 10.023  -3.008  17.637  1.00 22.82 ? 315  TRP A N     1 
ATOM   2428 C  CA    . TRP A 1 315 ? 8.743   -3.359  18.294  1.00 22.74 ? 315  TRP A CA    1 
ATOM   2429 C  C     . TRP A 1 315 ? 7.919   -2.078  18.430  1.00 23.47 ? 315  TRP A C     1 
ATOM   2430 O  O     . TRP A 1 315 ? 8.495   -1.021  18.873  1.00 23.81 ? 315  TRP A O     1 
ATOM   2431 C  CB    . TRP A 1 315 ? 8.976   -4.020  19.656  1.00 22.08 ? 315  TRP A CB    1 
ATOM   2432 C  CG    . TRP A 1 315 ? 9.591   -5.382  19.568  1.00 22.05 ? 315  TRP A CG    1 
ATOM   2433 C  CD1   . TRP A 1 315 ? 10.844  -5.728  19.967  1.00 21.32 ? 315  TRP A CD1   1 
ATOM   2434 C  CD2   . TRP A 1 315 ? 9.010   -6.573  19.001  1.00 22.63 ? 315  TRP A CD2   1 
ATOM   2435 N  NE1   . TRP A 1 315 ? 11.083  -7.040  19.694  1.00 20.42 ? 315  TRP A NE1   1 
ATOM   2436 C  CE2   . TRP A 1 315 ? 9.974   -7.597  19.132  1.00 22.61 ? 315  TRP A CE2   1 
ATOM   2437 C  CE3   . TRP A 1 315 ? 7.783   -6.881  18.390  1.00 22.45 ? 315  TRP A CE3   1 
ATOM   2438 C  CZ2   . TRP A 1 315 ? 9.752   -8.902  18.678  1.00 22.47 ? 315  TRP A CZ2   1 
ATOM   2439 C  CZ3   . TRP A 1 315 ? 7.553   -8.172  17.963  1.00 21.52 ? 315  TRP A CZ3   1 
ATOM   2440 C  CH2   . TRP A 1 315 ? 8.545   -9.155  18.070  1.00 21.17 ? 315  TRP A CH2   1 
ATOM   2441 N  N     . ASN A 1 316 ? 6.646   -2.166  18.060  1.00 21.12 ? 316  ASN A N     1 
ATOM   2442 C  CA    . ASN A 1 316 ? 5.749   -1.000  17.907  1.00 22.59 ? 316  ASN A CA    1 
ATOM   2443 C  C     . ASN A 1 316 ? 4.416   -1.284  18.599  1.00 24.02 ? 316  ASN A C     1 
ATOM   2444 O  O     . ASN A 1 316 ? 3.584   -2.013  18.011  1.00 26.94 ? 316  ASN A O     1 
ATOM   2445 C  CB    . ASN A 1 316 ? 5.600   -0.677  16.436  1.00 22.71 ? 316  ASN A CB    1 
ATOM   2446 C  CG    . ASN A 1 316 ? 6.942   -0.394  15.796  1.00 25.14 ? 316  ASN A CG    1 
ATOM   2447 O  OD1   . ASN A 1 316 ? 7.549   0.648   16.043  1.00 24.16 ? 316  ASN A OD1   1 
ATOM   2448 N  ND2   . ASN A 1 316 ? 7.439   -1.334  15.007  1.00 26.22 ? 316  ASN A ND2   1 
ATOM   2449 N  N     . PHE A 1 317 ? 4.230   -0.745  19.812  1.00 22.45 ? 317  PHE A N     1 
ATOM   2450 C  CA    . PHE A 1 317 ? 3.029   -0.976  20.653  1.00 20.84 ? 317  PHE A CA    1 
ATOM   2451 C  C     . PHE A 1 317 ? 1.968   0.078   20.327  1.00 22.97 ? 317  PHE A C     1 
ATOM   2452 O  O     . PHE A 1 317 ? 2.183   1.264   20.669  1.00 22.10 ? 317  PHE A O     1 
ATOM   2453 C  CB    . PHE A 1 317 ? 3.418   -0.952  22.125  1.00 20.39 ? 317  PHE A CB    1 
ATOM   2454 C  CG    . PHE A 1 317 ? 2.265   -0.910  23.090  1.00 19.76 ? 317  PHE A CG    1 
ATOM   2455 C  CD1   . PHE A 1 317 ? 1.043   -1.484  22.788  1.00 21.06 ? 317  PHE A CD1   1 
ATOM   2456 C  CD2   . PHE A 1 317 ? 2.402   -0.287  24.315  1.00 21.52 ? 317  PHE A CD2   1 
ATOM   2457 C  CE1   . PHE A 1 317 ? -0.018  -1.407  23.687  1.00 21.20 ? 317  PHE A CE1   1 
ATOM   2458 C  CE2   . PHE A 1 317 ? 1.343   -0.197  25.209  1.00 20.28 ? 317  PHE A CE2   1 
ATOM   2459 C  CZ    . PHE A 1 317 ? 0.135   -0.770  24.897  1.00 19.60 ? 317  PHE A CZ    1 
ATOM   2460 N  N     . CYS A 1 318 ? 0.888   -0.320  19.643  1.00 25.76 ? 318  CYS A N     1 
ATOM   2461 C  CA    . CYS A 1 318 ? -0.332  0.505   19.424  1.00 24.55 ? 318  CYS A CA    1 
ATOM   2462 C  C     . CYS A 1 318 ? -1.384  0.146   20.463  1.00 24.50 ? 318  CYS A C     1 
ATOM   2463 O  O     . CYS A 1 318 ? -1.628  -1.057  20.720  1.00 26.29 ? 318  CYS A O     1 
ATOM   2464 C  CB    . CYS A 1 318 ? -0.914  0.388   18.028  1.00 27.07 ? 318  CYS A CB    1 
ATOM   2465 S  SG    . CYS A 1 318 ? 0.071   1.318   16.824  1.00 33.79 ? 318  CYS A SG    1 
ATOM   2466 N  N     . GLY A 1 319 ? -1.943  1.180   21.084  1.00 23.06 ? 319  GLY A N     1 
ATOM   2467 C  CA    . GLY A 1 319 ? -3.071  1.059   22.026  1.00 22.59 ? 319  GLY A CA    1 
ATOM   2468 C  C     . GLY A 1 319 ? -3.850  2.348   21.987  1.00 21.50 ? 319  GLY A C     1 
ATOM   2469 O  O     . GLY A 1 319 ? -3.468  3.210   21.172  1.00 19.89 ? 319  GLY A O     1 
ATOM   2470 N  N     . ALA A 1 320 ? -4.881  2.482   22.811  1.00 19.76 ? 320  ALA A N     1 
ATOM   2471 C  CA    . ALA A 1 320 ? -5.678  3.717   22.826  1.00 22.13 ? 320  ALA A CA    1 
ATOM   2472 C  C     . ALA A 1 320 ? -6.358  3.911   24.178  1.00 22.85 ? 320  ALA A C     1 
ATOM   2473 O  O     . ALA A 1 320 ? -6.630  2.925   24.904  1.00 22.49 ? 320  ALA A O     1 
ATOM   2474 C  CB    . ALA A 1 320 ? -6.653  3.720   21.671  1.00 22.08 ? 320  ALA A CB    1 
ATOM   2475 N  N     . LEU A 1 321 ? -6.612  5.185   24.471  1.00 25.42 ? 321  LEU A N     1 
ATOM   2476 C  CA    . LEU A 1 321 ? -7.295  5.706   25.689  1.00 24.66 ? 321  LEU A CA    1 
ATOM   2477 C  C     . LEU A 1 321 ? -8.718  6.071   25.297  1.00 21.69 ? 321  LEU A C     1 
ATOM   2478 O  O     . LEU A 1 321 ? -8.876  6.662   24.255  1.00 19.10 ? 321  LEU A O     1 
ATOM   2479 C  CB    . LEU A 1 321 ? -6.555  6.952   26.199  1.00 24.14 ? 321  LEU A CB    1 
ATOM   2480 C  CG    . LEU A 1 321 ? -5.061  6.763   26.446  1.00 24.43 ? 321  LEU A CG    1 
ATOM   2481 C  CD1   . LEU A 1 321 ? -4.382  8.110   26.695  1.00 26.75 ? 321  LEU A CD1   1 
ATOM   2482 C  CD2   . LEU A 1 321 ? -4.823  5.834   27.625  1.00 25.44 ? 321  LEU A CD2   1 
ATOM   2483 N  N     . TYR A 1 322 ? -9.689  5.693   26.121  1.00 20.84 ? 322  TYR A N     1 
ATOM   2484 C  CA    . TYR A 1 322 ? -11.122 5.946   25.897  1.00 21.60 ? 322  TYR A CA    1 
ATOM   2485 C  C     . TYR A 1 322 ? -11.694 6.571   27.165  1.00 22.99 ? 322  TYR A C     1 
ATOM   2486 O  O     . TYR A 1 322 ? -11.343 6.123   28.293  1.00 23.19 ? 322  TYR A O     1 
ATOM   2487 C  CB    . TYR A 1 322 ? -11.831 4.643   25.546  1.00 20.12 ? 322  TYR A CB    1 
ATOM   2488 C  CG    . TYR A 1 322 ? -11.194 3.876   24.414  1.00 21.05 ? 322  TYR A CG    1 
ATOM   2489 C  CD1   . TYR A 1 322 ? -10.137 3.013   24.645  1.00 19.84 ? 322  TYR A CD1   1 
ATOM   2490 C  CD2   . TYR A 1 322 ? -11.699 3.960   23.116  1.00 20.52 ? 322  TYR A CD2   1 
ATOM   2491 C  CE1   . TYR A 1 322 ? -9.597  2.256   23.618  1.00 20.64 ? 322  TYR A CE1   1 
ATOM   2492 C  CE2   . TYR A 1 322 ? -11.143 3.235   22.073  1.00 20.09 ? 322  TYR A CE2   1 
ATOM   2493 C  CZ    . TYR A 1 322 ? -10.097 2.371   22.335  1.00 20.63 ? 322  TYR A CZ    1 
ATOM   2494 O  OH    . TYR A 1 322 ? -9.567  1.621   21.333  1.00 22.93 ? 322  TYR A OH    1 
ATOM   2495 N  N     . GLY A 1 323 ? -12.530 7.586   26.989  1.00 24.28 ? 323  GLY A N     1 
ATOM   2496 C  CA    . GLY A 1 323 ? -13.314 8.152   28.098  1.00 26.40 ? 323  GLY A CA    1 
ATOM   2497 C  C     . GLY A 1 323 ? -13.046 9.631   28.272  1.00 27.36 ? 323  GLY A C     1 
ATOM   2498 O  O     . GLY A 1 323 ? -12.382 10.243  27.442  1.00 27.11 ? 323  GLY A O     1 
ATOM   2499 N  N     . PRO A 1 324 ? -13.577 10.247  29.349  1.00 32.65 ? 324  PRO A N     1 
ATOM   2500 C  CA    . PRO A 1 324 ? -13.373 11.677  29.581  1.00 32.55 ? 324  PRO A CA    1 
ATOM   2501 C  C     . PRO A 1 324 ? -11.892 11.959  29.797  1.00 29.57 ? 324  PRO A C     1 
ATOM   2502 O  O     . PRO A 1 324 ? -11.183 11.133  30.357  1.00 32.68 ? 324  PRO A O     1 
ATOM   2503 C  CB    . PRO A 1 324 ? -14.216 11.972  30.830  1.00 33.72 ? 324  PRO A CB    1 
ATOM   2504 C  CG    . PRO A 1 324 ? -14.438 10.633  31.493  1.00 33.18 ? 324  PRO A CG    1 
ATOM   2505 C  CD    . PRO A 1 324 ? -14.409 9.611   30.379  1.00 33.47 ? 324  PRO A CD    1 
ATOM   2506 N  N     . PRO A 1 325 ? -11.373 13.127  29.367  1.00 32.06 ? 325  PRO A N     1 
ATOM   2507 C  CA    . PRO A 1 325 ? -9.951  13.462  29.539  1.00 32.07 ? 325  PRO A CA    1 
ATOM   2508 C  C     . PRO A 1 325 ? -9.304  13.151  30.895  1.00 31.47 ? 325  PRO A C     1 
ATOM   2509 O  O     . PRO A 1 325 ? -8.221  12.588  30.929  1.00 31.16 ? 325  PRO A O     1 
ATOM   2510 C  CB    . PRO A 1 325 ? -9.928  14.964  29.198  1.00 32.87 ? 325  PRO A CB    1 
ATOM   2511 C  CG    . PRO A 1 325 ? -10.994 15.089  28.140  1.00 31.67 ? 325  PRO A CG    1 
ATOM   2512 C  CD    . PRO A 1 325 ? -12.098 14.156  28.604  1.00 31.88 ? 325  PRO A CD    1 
ATOM   2513 N  N     . PRO A 1 326 ? -9.896  13.458  32.071  1.00 33.58 ? 326  PRO A N     1 
ATOM   2514 C  CA    . PRO A 1 326 ? -9.223  13.178  33.340  1.00 32.01 ? 326  PRO A CA    1 
ATOM   2515 C  C     . PRO A 1 326 ? -8.966  11.672  33.526  1.00 32.31 ? 326  PRO A C     1 
ATOM   2516 O  O     . PRO A 1 326 ? -8.012  11.291  34.170  1.00 30.61 ? 326  PRO A O     1 
ATOM   2517 C  CB    . PRO A 1 326 ? -10.197 13.691  34.424  1.00 31.11 ? 326  PRO A CB    1 
ATOM   2518 C  CG    . PRO A 1 326 ? -11.147 14.595  33.690  1.00 33.47 ? 326  PRO A CG    1 
ATOM   2519 C  CD    . PRO A 1 326 ? -11.207 14.096  32.261  1.00 33.76 ? 326  PRO A CD    1 
ATOM   2520 N  N     . VAL A 1 327 ? -9.847  10.827  32.993  1.00 33.14 ? 327  VAL A N     1 
ATOM   2521 C  CA    . VAL A 1 327 ? -9.629  9.349   33.028  1.00 32.55 ? 327  VAL A CA    1 
ATOM   2522 C  C     . VAL A 1 327 ? -8.463  9.019   32.079  1.00 29.83 ? 327  VAL A C     1 
ATOM   2523 O  O     . VAL A 1 327 ? -7.536  8.321   32.496  1.00 31.56 ? 327  VAL A O     1 
ATOM   2524 C  CB    . VAL A 1 327 ? -10.915 8.578   32.669  1.00 33.55 ? 327  VAL A CB    1 
ATOM   2525 C  CG1   . VAL A 1 327 ? -10.678 7.078   32.569  1.00 34.16 ? 327  VAL A CG1   1 
ATOM   2526 C  CG2   . VAL A 1 327 ? -12.022 8.866   33.659  1.00 35.80 ? 327  VAL A CG2   1 
ATOM   2527 N  N     . MET A 1 328 ? -8.502  9.516   30.844  1.00 28.53 ? 328  MET A N     1 
ATOM   2528 C  CA    . MET A 1 328 ? -7.471  9.224   29.821  1.00 27.23 ? 328  MET A CA    1 
ATOM   2529 C  C     . MET A 1 328 ? -6.107  9.681   30.351  1.00 27.69 ? 328  MET A C     1 
ATOM   2530 O  O     . MET A 1 328 ? -5.133  8.903   30.228  1.00 24.58 ? 328  MET A O     1 
ATOM   2531 C  CB    . MET A 1 328 ? -7.803  9.873   28.473  1.00 25.84 ? 328  MET A CB    1 
ATOM   2532 C  CG    . MET A 1 328 ? -8.970  9.198   27.786  1.00 26.71 ? 328  MET A CG    1 
ATOM   2533 S  SD    . MET A 1 328 ? -9.125  9.571   26.006  1.00 28.96 ? 328  MET A SD    1 
ATOM   2534 C  CE    . MET A 1 328 ? -9.380  11.349  26.037  1.00 32.28 ? 328  MET A CE    1 
ATOM   2535 N  N     . ASP A 1 329 ? -6.036  10.855  30.987  1.00 27.47 ? 329  ASP A N     1 
ATOM   2536 C  CA    . ASP A 1 329 ? -4.751  11.391  31.512  1.00 26.69 ? 329  ASP A CA    1 
ATOM   2537 C  C     . ASP A 1 329 ? -4.213  10.474  32.592  1.00 25.20 ? 329  ASP A C     1 
ATOM   2538 O  O     . ASP A 1 329 ? -2.979  10.277  32.608  1.00 26.58 ? 329  ASP A O     1 
ATOM   2539 C  CB    . ASP A 1 329 ? -4.865  12.803  32.100  1.00 29.36 ? 329  ASP A CB    1 
ATOM   2540 C  CG    . ASP A 1 329 ? -5.100  13.844  31.040  1.00 30.58 ? 329  ASP A CG    1 
ATOM   2541 O  OD1   . ASP A 1 329 ? -4.771  13.582  29.859  1.00 39.03 ? 329  ASP A OD1   1 
ATOM   2542 O  OD2   . ASP A 1 329 ? -5.663  14.863  31.383  1.00 39.08 ? 329  ASP A OD2   1 
ATOM   2543 N  N     . THR A 1 330 ? -5.084  9.978   33.476  1.00 24.12 ? 330  THR A N     1 
ATOM   2544 C  CA    . THR A 1 330 ? -4.658  9.149   34.631  1.00 26.14 ? 330  THR A CA    1 
ATOM   2545 C  C     . THR A 1 330 ? -4.121  7.808   34.125  1.00 28.08 ? 330  THR A C     1 
ATOM   2546 O  O     . THR A 1 330 ? -3.035  7.388   34.572  1.00 24.96 ? 330  THR A O     1 
ATOM   2547 C  CB    . THR A 1 330 ? -5.778  8.897   35.634  1.00 25.67 ? 330  THR A CB    1 
ATOM   2548 O  OG1   . THR A 1 330 ? -6.301  10.149  36.059  1.00 26.19 ? 330  THR A OG1   1 
ATOM   2549 C  CG2   . THR A 1 330 ? -5.283  8.123   36.832  1.00 27.89 ? 330  THR A CG2   1 
ATOM   2550 N  N     . LEU A 1 331 ? -4.849  7.155   33.217  1.00 26.34 ? 331  LEU A N     1 
ATOM   2551 C  CA    . LEU A 1 331 ? -4.406  5.846   32.672  1.00 24.76 ? 331  LEU A CA    1 
ATOM   2552 C  C     . LEU A 1 331 ? -3.087  6.067   31.928  1.00 23.14 ? 331  LEU A C     1 
ATOM   2553 O  O     . LEU A 1 331 ? -2.151  5.263   32.108  1.00 23.21 ? 331  LEU A O     1 
ATOM   2554 C  CB    . LEU A 1 331 ? -5.497  5.265   31.767  1.00 24.25 ? 331  LEU A CB    1 
ATOM   2555 C  CG    . LEU A 1 331 ? -6.849  5.050   32.444  1.00 24.73 ? 331  LEU A CG    1 
ATOM   2556 C  CD1   . LEU A 1 331 ? -7.849  4.464   31.480  1.00 25.12 ? 331  LEU A CD1   1 
ATOM   2557 C  CD2   . LEU A 1 331 ? -6.746  4.192   33.702  1.00 24.81 ? 331  LEU A CD2   1 
ATOM   2558 N  N     . TRP A 1 332 ? -2.976  7.163   31.180  1.00 24.27 ? 332  TRP A N     1 
ATOM   2559 C  CA    . TRP A 1 332 ? -1.776  7.417   30.351  1.00 25.37 ? 332  TRP A CA    1 
ATOM   2560 C  C     . TRP A 1 332 ? -0.526  7.542   31.235  1.00 25.21 ? 332  TRP A C     1 
ATOM   2561 O  O     . TRP A 1 332 ? 0.539   7.044   30.819  1.00 24.35 ? 332  TRP A O     1 
ATOM   2562 C  CB    . TRP A 1 332 ? -1.949  8.656   29.474  1.00 25.41 ? 332  TRP A CB    1 
ATOM   2563 C  CG    . TRP A 1 332 ? -0.707  8.934   28.694  1.00 27.32 ? 332  TRP A CG    1 
ATOM   2564 C  CD1   . TRP A 1 332 ? 0.096   10.032  28.807  1.00 26.96 ? 332  TRP A CD1   1 
ATOM   2565 C  CD2   . TRP A 1 332 ? -0.055  8.053   27.751  1.00 28.98 ? 332  TRP A CD2   1 
ATOM   2566 N  NE1   . TRP A 1 332 ? 1.169   9.915   27.968  1.00 26.91 ? 332  TRP A NE1   1 
ATOM   2567 C  CE2   . TRP A 1 332 ? 1.110   8.718   27.309  1.00 26.34 ? 332  TRP A CE2   1 
ATOM   2568 C  CE3   . TRP A 1 332 ? -0.350  6.795   27.199  1.00 28.64 ? 332  TRP A CE3   1 
ATOM   2569 C  CZ2   . TRP A 1 332 ? 1.959   8.173   26.346  1.00 26.57 ? 332  TRP A CZ2   1 
ATOM   2570 C  CZ3   . TRP A 1 332 ? 0.496   6.254   26.245  1.00 26.41 ? 332  TRP A CZ3   1 
ATOM   2571 C  CH2   . TRP A 1 332 ? 1.633   6.932   25.827  1.00 25.81 ? 332  TRP A CH2   1 
ATOM   2572 N  N     . THR A 1 333 ? -0.644  8.223   32.378  1.00 24.23 ? 333  THR A N     1 
ATOM   2573 C  CA    . THR A 1 333 ? 0.441   8.431   33.376  1.00 24.31 ? 333  THR A CA    1 
ATOM   2574 C  C     . THR A 1 333 ? 0.955   7.058   33.802  1.00 25.36 ? 333  THR A C     1 
ATOM   2575 O  O     . THR A 1 333 ? 2.185   6.842   33.785  1.00 26.87 ? 333  THR A O     1 
ATOM   2576 C  CB    . THR A 1 333 ? -0.075  9.265   34.563  1.00 23.96 ? 333  THR A CB    1 
ATOM   2577 O  OG1   . THR A 1 333 ? -0.283  10.593  34.072  1.00 24.62 ? 333  THR A OG1   1 
ATOM   2578 C  CG2   . THR A 1 333 ? 0.877   9.265   35.731  1.00 25.32 ? 333  THR A CG2   1 
ATOM   2579 N  N     . ALA A 1 334 ? 0.028   6.156   34.125  1.00 25.58 ? 334  ALA A N     1 
ATOM   2580 C  CA    . ALA A 1 334 ? 0.310   4.753   34.506  1.00 26.58 ? 334  ALA A CA    1 
ATOM   2581 C  C     . ALA A 1 334 ? 1.039   4.018   33.367  1.00 24.44 ? 334  ALA A C     1 
ATOM   2582 O  O     . ALA A 1 334 ? 2.062   3.361   33.634  1.00 23.19 ? 334  ALA A O     1 
ATOM   2583 C  CB    . ALA A 1 334 ? -0.978  4.067   34.905  1.00 26.59 ? 334  ALA A CB    1 
ATOM   2584 N  N     . ILE A 1 335 ? 0.576   4.157   32.123  1.00 25.36 ? 335  ILE A N     1 
ATOM   2585 C  CA    . ILE A 1 335 ? 1.125   3.408   30.946  1.00 23.76 ? 335  ILE A CA    1 
ATOM   2586 C  C     . ILE A 1 335 ? 2.499   3.976   30.591  1.00 23.79 ? 335  ILE A C     1 
ATOM   2587 O  O     . ILE A 1 335 ? 3.456   3.193   30.460  1.00 25.19 ? 335  ILE A O     1 
ATOM   2588 C  CB    . ILE A 1 335 ? 0.157   3.454   29.740  1.00 24.18 ? 335  ILE A CB    1 
ATOM   2589 C  CG1   . ILE A 1 335 ? -1.171  2.764   30.071  1.00 22.45 ? 335  ILE A CG1   1 
ATOM   2590 C  CG2   . ILE A 1 335 ? 0.806   2.859   28.501  1.00 23.51 ? 335  ILE A CG2   1 
ATOM   2591 C  CD1   . ILE A 1 335 ? -2.324  3.183   29.192  1.00 23.34 ? 335  ILE A CD1   1 
ATOM   2592 N  N     . ARG A 1 336 ? 2.599   5.287   30.411  1.00 24.11 ? 336  ARG A N     1 
ATOM   2593 C  CA    . ARG A 1 336 ? 3.869   5.959   30.034  1.00 24.71 ? 336  ARG A CA    1 
ATOM   2594 C  C     . ARG A 1 336 ? 4.960   5.677   31.081  1.00 23.62 ? 336  ARG A C     1 
ATOM   2595 O  O     . ARG A 1 336 ? 6.043   5.255   30.677  1.00 23.01 ? 336  ARG A O     1 
ATOM   2596 C  CB    . ARG A 1 336 ? 3.657   7.467   29.913  1.00 27.61 ? 336  ARG A CB    1 
ATOM   2597 C  CG    . ARG A 1 336 ? 4.846   8.175   29.298  1.00 30.09 ? 336  ARG A CG    1 
ATOM   2598 C  CD    . ARG A 1 336 ? 4.893   9.649   29.621  1.00 33.99 ? 336  ARG A CD    1 
ATOM   2599 N  NE    . ARG A 1 336 ? 6.227   10.043  29.183  1.00 37.67 ? 336  ARG A NE    1 
ATOM   2600 C  CZ    . ARG A 1 336 ? 6.503   10.634  28.043  1.00 38.13 ? 336  ARG A CZ    1 
ATOM   2601 N  NH1   . ARG A 1 336 ? 5.523   10.993  27.227  1.00 45.30 ? 336  ARG A NH1   1 
ATOM   2602 N  NH2   . ARG A 1 336 ? 7.761   10.893  27.732  1.00 39.29 ? 336  ARG A NH2   1 
ATOM   2603 N  N     . ASP A 1 337 ? 4.683   5.897   32.373  1.00 23.71 ? 337  ASP A N     1 
ATOM   2604 C  CA    . ASP A 1 337 ? 5.645   5.588   33.478  1.00 26.13 ? 337  ASP A CA    1 
ATOM   2605 C  C     . ASP A 1 337 ? 6.095   4.111   33.436  1.00 26.53 ? 337  ASP A C     1 
ATOM   2606 O  O     . ASP A 1 337 ? 7.217   3.826   33.915  1.00 25.51 ? 337  ASP A O     1 
ATOM   2607 C  CB    . ASP A 1 337 ? 5.058   5.894   34.861  1.00 27.65 ? 337  ASP A CB    1 
ATOM   2608 C  CG    . ASP A 1 337 ? 4.793   7.367   35.069  1.00 31.74 ? 337  ASP A CG    1 
ATOM   2609 O  OD1   . ASP A 1 337 ? 5.216   8.165   34.200  1.00 32.03 ? 337  ASP A OD1   1 
ATOM   2610 O  OD2   . ASP A 1 337 ? 4.104   7.699   36.043  1.00 36.68 ? 337  ASP A OD2   1 
ATOM   2611 N  N     . SER A 1 338 ? 5.276   3.187   32.915  1.00 25.97 ? 338  SER A N     1 
ATOM   2612 C  CA    . SER A 1 338 ? 5.614   1.738   32.846  1.00 25.79 ? 338  SER A CA    1 
ATOM   2613 C  C     . SER A 1 338 ? 6.751   1.508   31.857  1.00 25.28 ? 338  SER A C     1 
ATOM   2614 O  O     . SER A 1 338 ? 7.417   0.480   32.014  1.00 26.03 ? 338  SER A O     1 
ATOM   2615 C  CB    . SER A 1 338 ? 4.422   0.887   32.508  1.00 26.51 ? 338  SER A CB    1 
ATOM   2616 O  OG    . SER A 1 338 ? 3.372   1.158   33.425  1.00 26.62 ? 338  SER A OG    1 
ATOM   2617 N  N     . PHE A 1 339 ? 6.944   2.402   30.876  1.00 25.32 ? 339  PHE A N     1 
ATOM   2618 C  CA    . PHE A 1 339 ? 7.939   2.206   29.783  1.00 25.92 ? 339  PHE A CA    1 
ATOM   2619 C  C     . PHE A 1 339 ? 9.028   3.299   29.737  1.00 26.70 ? 339  PHE A C     1 
ATOM   2620 O  O     . PHE A 1 339 ? 9.945   3.108   28.941  1.00 27.20 ? 339  PHE A O     1 
ATOM   2621 C  CB    . PHE A 1 339 ? 7.212   2.101   28.437  1.00 23.96 ? 339  PHE A CB    1 
ATOM   2622 C  CG    . PHE A 1 339 ? 6.200   0.981   28.391  1.00 23.59 ? 339  PHE A CG    1 
ATOM   2623 C  CD1   . PHE A 1 339 ? 6.604   -0.341  28.231  1.00 21.95 ? 339  PHE A CD1   1 
ATOM   2624 C  CD2   . PHE A 1 339 ? 4.839   1.247   28.514  1.00 23.40 ? 339  PHE A CD2   1 
ATOM   2625 C  CE1   . PHE A 1 339 ? 5.670   -1.368  28.243  1.00 22.33 ? 339  PHE A CE1   1 
ATOM   2626 C  CE2   . PHE A 1 339 ? 3.902   0.227   28.473  1.00 23.37 ? 339  PHE A CE2   1 
ATOM   2627 C  CZ    . PHE A 1 339 ? 4.317   -1.079  28.352  1.00 24.18 ? 339  PHE A CZ    1 
ATOM   2628 N  N     . ALA A 1 340 ? 8.944   4.395   30.505  1.00 26.58 ? 340  ALA A N     1 
ATOM   2629 C  CA    . ALA A 1 340 ? 9.797   5.600   30.315  1.00 29.25 ? 340  ALA A CA    1 
ATOM   2630 C  C     . ALA A 1 340 ? 11.290  5.291   30.521  1.00 29.85 ? 340  ALA A C     1 
ATOM   2631 O  O     . ALA A 1 340 ? 12.102  5.865   29.762  1.00 31.99 ? 340  ALA A O     1 
ATOM   2632 C  CB    . ALA A 1 340 ? 9.359   6.734   31.202  1.00 29.78 ? 340  ALA A CB    1 
ATOM   2633 N  N     . ASP A 1 341 ? 11.653  4.357   31.404  1.00 27.93 ? 341  ASP A N     1 
ATOM   2634 C  CA    . ASP A 1 341 ? 13.075  4.078   31.727  1.00 28.60 ? 341  ASP A CA    1 
ATOM   2635 C  C     . ASP A 1 341 ? 13.695  3.091   30.730  1.00 28.30 ? 341  ASP A C     1 
ATOM   2636 O  O     . ASP A 1 341 ? 14.856  2.738   30.930  1.00 31.29 ? 341  ASP A O     1 
ATOM   2637 C  CB    . ASP A 1 341 ? 13.247  3.651   33.196  1.00 29.73 ? 341  ASP A CB    1 
ATOM   2638 C  CG    . ASP A 1 341 ? 12.810  2.229   33.494  1.00 34.13 ? 341  ASP A CG    1 
ATOM   2639 O  OD1   . ASP A 1 341 ? 12.506  1.478   32.538  1.00 35.91 ? 341  ASP A OD1   1 
ATOM   2640 O  OD2   . ASP A 1 341 ? 12.815  1.870   34.677  1.00 40.58 ? 341  ASP A OD2   1 
ATOM   2641 N  N     . ILE A 1 342 ? 13.001  2.627   29.691  1.00 27.78 ? 342  ILE A N     1 
ATOM   2642 C  CA    . ILE A 1 342 ? 13.647  1.716   28.700  1.00 26.57 ? 342  ILE A CA    1 
ATOM   2643 C  C     . ILE A 1 342 ? 14.506  2.563   27.754  1.00 28.48 ? 342  ILE A C     1 
ATOM   2644 O  O     . ILE A 1 342 ? 14.015  3.483   27.111  1.00 29.26 ? 342  ILE A O     1 
ATOM   2645 C  CB    . ILE A 1 342 ? 12.604  0.880   27.946  1.00 26.55 ? 342  ILE A CB    1 
ATOM   2646 C  CG1   . ILE A 1 342 ? 11.790  -0.006  28.896  1.00 28.84 ? 342  ILE A CG1   1 
ATOM   2647 C  CG2   . ILE A 1 342 ? 13.273  0.077   26.845  1.00 24.84 ? 342  ILE A CG2   1 
ATOM   2648 C  CD1   . ILE A 1 342 ? 10.482  -0.487  28.320  1.00 27.59 ? 342  ILE A CD1   1 
ATOM   2649 N  N     . PRO A 1 343 ? 15.822  2.302   27.636  1.00 29.88 ? 343  PRO A N     1 
ATOM   2650 C  CA    . PRO A 1 343 ? 16.650  3.059   26.702  1.00 32.35 ? 343  PRO A CA    1 
ATOM   2651 C  C     . PRO A 1 343 ? 16.105  2.973   25.260  1.00 32.37 ? 343  PRO A C     1 
ATOM   2652 O  O     . PRO A 1 343 ? 15.869  1.860   24.799  1.00 29.12 ? 343  PRO A O     1 
ATOM   2653 C  CB    . PRO A 1 343 ? 18.045  2.404   26.788  1.00 31.57 ? 343  PRO A CB    1 
ATOM   2654 C  CG    . PRO A 1 343 ? 18.029  1.587   28.076  1.00 33.03 ? 343  PRO A CG    1 
ATOM   2655 C  CD    . PRO A 1 343 ? 16.577  1.283   28.389  1.00 31.86 ? 343  PRO A CD    1 
ATOM   2656 N  N     . GLY A 1 344 ? 15.916  4.130   24.603  1.00 27.12 ? 344  GLY A N     1 
ATOM   2657 C  CA    . GLY A 1 344 ? 15.521  4.238   23.188  1.00 26.70 ? 344  GLY A CA    1 
ATOM   2658 C  C     . GLY A 1 344 ? 14.011  4.265   22.980  1.00 26.71 ? 344  GLY A C     1 
ATOM   2659 O  O     . GLY A 1 344 ? 13.612  4.402   21.832  1.00 30.80 ? 344  GLY A O     1 
ATOM   2660 N  N     . VAL A 1 345 ? 13.198  4.160   24.035  1.00 25.89 ? 345  VAL A N     1 
ATOM   2661 C  CA    . VAL A 1 345 ? 11.710  4.232   23.931  1.00 26.36 ? 345  VAL A CA    1 
ATOM   2662 C  C     . VAL A 1 345 ? 11.293  5.602   23.382  1.00 30.12 ? 345  VAL A C     1 
ATOM   2663 O  O     . VAL A 1 345 ? 11.915  6.621   23.764  1.00 31.82 ? 345  VAL A O     1 
ATOM   2664 C  CB    . VAL A 1 345 ? 11.004  3.967   25.274  1.00 26.20 ? 345  VAL A CB    1 
ATOM   2665 C  CG1   . VAL A 1 345 ? 11.228  5.092   26.301  1.00 26.18 ? 345  VAL A CG1   1 
ATOM   2666 C  CG2   . VAL A 1 345 ? 9.515   3.734   25.071  1.00 24.97 ? 345  VAL A CG2   1 
ATOM   2667 N  N     . LYS A 1 346 ? 10.232  5.618   22.577  1.00 29.08 ? 346  LYS A N     1 
ATOM   2668 C  CA    . LYS A 1 346 ? 9.590   6.846   22.043  1.00 29.52 ? 346  LYS A CA    1 
ATOM   2669 C  C     . LYS A 1 346 ? 8.080   6.712   22.160  1.00 25.67 ? 346  LYS A C     1 
ATOM   2670 O  O     . LYS A 1 346 ? 7.567   5.572   22.023  1.00 27.31 ? 346  LYS A O     1 
ATOM   2671 C  CB    . LYS A 1 346 ? 10.074  7.107   20.621  1.00 33.84 ? 346  LYS A CB    1 
ATOM   2672 C  CG    . LYS A 1 346 ? 11.552  7.436   20.615  1.00 39.32 ? 346  LYS A CG    1 
ATOM   2673 C  CD    . LYS A 1 346 ? 12.073  8.049   19.382  1.00 47.06 ? 346  LYS A CD    1 
ATOM   2674 C  CE    . LYS A 1 346 ? 13.565  8.263   19.499  1.00 51.66 ? 346  LYS A CE    1 
ATOM   2675 N  NZ    . LYS A 1 346 ? 14.264  7.005   19.859  1.00 54.52 ? 346  LYS A NZ    1 
ATOM   2676 N  N     . PHE A 1 347 ? 7.434   7.812   22.520  1.00 22.87 ? 347  PHE A N     1 
ATOM   2677 C  CA    . PHE A 1 347 ? 5.974   7.925   22.747  1.00 24.68 ? 347  PHE A CA    1 
ATOM   2678 C  C     . PHE A 1 347 ? 5.400   8.846   21.677  1.00 26.33 ? 347  PHE A C     1 
ATOM   2679 O  O     . PHE A 1 347 ? 5.964   9.912   21.430  1.00 25.40 ? 347  PHE A O     1 
ATOM   2680 C  CB    . PHE A 1 347 ? 5.672   8.431   24.153  1.00 25.90 ? 347  PHE A CB    1 
ATOM   2681 C  CG    . PHE A 1 347 ? 6.264   7.593   25.258  1.00 25.50 ? 347  PHE A CG    1 
ATOM   2682 C  CD1   . PHE A 1 347 ? 5.577   6.507   25.772  1.00 24.37 ? 347  PHE A CD1   1 
ATOM   2683 C  CD2   . PHE A 1 347 ? 7.515   7.885   25.777  1.00 25.81 ? 347  PHE A CD2   1 
ATOM   2684 C  CE1   . PHE A 1 347 ? 6.120   5.736   26.785  1.00 24.05 ? 347  PHE A CE1   1 
ATOM   2685 C  CE2   . PHE A 1 347 ? 8.046   7.128   26.813  1.00 27.49 ? 347  PHE A CE2   1 
ATOM   2686 C  CZ    . PHE A 1 347 ? 7.347   6.049   27.313  1.00 25.87 ? 347  PHE A CZ    1 
ATOM   2687 N  N     . TYR A 1 348 ? 4.347   8.413   20.995  1.00 23.81 ? 348  TYR A N     1 
ATOM   2688 C  CA    . TYR A 1 348 ? 3.719   9.265   19.958  1.00 24.11 ? 348  TYR A CA    1 
ATOM   2689 C  C     . TYR A 1 348 ? 2.202   9.248   20.076  1.00 23.69 ? 348  TYR A C     1 
ATOM   2690 O  O     . TYR A 1 348 ? 1.611   8.176   20.272  1.00 25.22 ? 348  TYR A O     1 
ATOM   2691 C  CB    . TYR A 1 348 ? 4.075   8.814   18.544  1.00 22.97 ? 348  TYR A CB    1 
ATOM   2692 C  CG    . TYR A 1 348 ? 5.531   8.654   18.193  1.00 22.90 ? 348  TYR A CG    1 
ATOM   2693 C  CD1   . TYR A 1 348 ? 6.167   7.432   18.369  1.00 22.52 ? 348  TYR A CD1   1 
ATOM   2694 C  CD2   . TYR A 1 348 ? 6.243   9.669   17.553  1.00 21.95 ? 348  TYR A CD2   1 
ATOM   2695 C  CE1   . TYR A 1 348 ? 7.477   7.233   17.958  1.00 22.77 ? 348  TYR A CE1   1 
ATOM   2696 C  CE2   . TYR A 1 348 ? 7.554   9.477   17.124  1.00 21.47 ? 348  TYR A CE2   1 
ATOM   2697 C  CZ    . TYR A 1 348 ? 8.183   8.260   17.340  1.00 23.75 ? 348  TYR A CZ    1 
ATOM   2698 O  OH    . TYR A 1 348 ? 9.475   8.043   16.934  1.00 24.14 ? 348  TYR A OH    1 
ATOM   2699 N  N     . PHE A 1 349 ? 1.606   10.433  19.955  1.00 24.28 ? 349  PHE A N     1 
ATOM   2700 C  CA    . PHE A 1 349 ? 0.164   10.666  19.685  1.00 25.30 ? 349  PHE A CA    1 
ATOM   2701 C  C     . PHE A 1 349 ? 0.057   11.111  18.231  1.00 23.00 ? 349  PHE A C     1 
ATOM   2702 O  O     . PHE A 1 349 ? 1.073   11.367  17.586  1.00 22.55 ? 349  PHE A O     1 
ATOM   2703 C  CB    . PHE A 1 349 ? -0.409  11.617  20.740  1.00 28.18 ? 349  PHE A CB    1 
ATOM   2704 C  CG    . PHE A 1 349 ? -0.628  10.948  22.074  1.00 27.94 ? 349  PHE A CG    1 
ATOM   2705 C  CD1   . PHE A 1 349 ? -1.759  10.192  22.307  1.00 29.94 ? 349  PHE A CD1   1 
ATOM   2706 C  CD2   . PHE A 1 349 ? 0.296   11.076  23.094  1.00 30.04 ? 349  PHE A CD2   1 
ATOM   2707 C  CE1   . PHE A 1 349 ? -1.964  9.575   23.534  1.00 30.50 ? 349  PHE A CE1   1 
ATOM   2708 C  CE2   . PHE A 1 349 ? 0.103   10.454  24.313  1.00 30.04 ? 349  PHE A CE2   1 
ATOM   2709 C  CZ    . PHE A 1 349 ? -1.027  9.694   24.530  1.00 30.30 ? 349  PHE A CZ    1 
ATOM   2710 N  N     . PRO A 1 350 ? -1.134  11.083  17.605  1.00 24.42 ? 350  PRO A N     1 
ATOM   2711 C  CA    . PRO A 1 350 ? -1.222  11.353  16.170  1.00 27.01 ? 350  PRO A CA    1 
ATOM   2712 C  C     . PRO A 1 350 ? -0.491  12.640  15.766  1.00 26.51 ? 350  PRO A C     1 
ATOM   2713 O  O     . PRO A 1 350 ? 0.257   12.583  14.830  1.00 30.09 ? 350  PRO A O     1 
ATOM   2714 C  CB    . PRO A 1 350 ? -2.733  11.427  15.928  1.00 25.78 ? 350  PRO A CB    1 
ATOM   2715 C  CG    . PRO A 1 350 ? -3.287  10.469  16.948  1.00 26.02 ? 350  PRO A CG    1 
ATOM   2716 C  CD    . PRO A 1 350 ? -2.432  10.700  18.187  1.00 26.94 ? 350  PRO A CD    1 
ATOM   2717 N  N     . GLU A 1 351 ? -0.692  13.737  16.495  1.00 27.65 ? 351  GLU A N     1 
ATOM   2718 C  CA    . GLU A 1 351 ? -0.120  15.079  16.172  1.00 29.01 ? 351  GLU A CA    1 
ATOM   2719 C  C     . GLU A 1 351 ? 1.424   15.031  16.228  1.00 32.42 ? 351  GLU A C     1 
ATOM   2720 O  O     . GLU A 1 351 ? 2.062   15.845  15.532  1.00 30.68 ? 351  GLU A O     1 
ATOM   2721 C  CB    . GLU A 1 351 ? -0.717  16.147  17.092  1.00 28.37 ? 351  GLU A CB    1 
ATOM   2722 C  CG    . GLU A 1 351 ? -0.413  15.973  18.576  1.00 31.20 ? 351  GLU A CG    1 
ATOM   2723 C  CD    . GLU A 1 351 ? -1.303  15.016  19.383  1.00 33.98 ? 351  GLU A CD    1 
ATOM   2724 O  OE1   . GLU A 1 351 ? -1.971  14.129  18.777  1.00 33.53 ? 351  GLU A OE1   1 
ATOM   2725 O  OE2   . GLU A 1 351 ? -1.316  15.133  20.633  1.00 35.29 ? 351  GLU A OE2   1 
ATOM   2726 N  N     . ASP A 1 352 ? 2.016   14.058  16.938  1.00 30.49 ? 352  ASP A N     1 
ATOM   2727 C  CA    . ASP A 1 352 ? 3.487   13.862  17.005  1.00 30.32 ? 352  ASP A CA    1 
ATOM   2728 C  C     . ASP A 1 352 ? 4.040   13.181  15.752  1.00 30.39 ? 352  ASP A C     1 
ATOM   2729 O  O     . ASP A 1 352 ? 5.253   13.145  15.672  1.00 31.12 ? 352  ASP A O     1 
ATOM   2730 C  CB    . ASP A 1 352 ? 3.911   13.043  18.225  1.00 32.34 ? 352  ASP A CB    1 
ATOM   2731 C  CG    . ASP A 1 352 ? 3.515   13.669  19.545  1.00 31.69 ? 352  ASP A CG    1 
ATOM   2732 O  OD1   . ASP A 1 352 ? 3.590   14.888  19.654  1.00 36.65 ? 352  ASP A OD1   1 
ATOM   2733 O  OD2   . ASP A 1 352 ? 3.118   12.931  20.449  1.00 36.61 ? 352  ASP A OD2   1 
ATOM   2734 N  N     . ARG A 1 353 ? 3.231   12.643  14.827  1.00 28.62 ? 353  ARG A N     1 
ATOM   2735 C  CA    . ARG A 1 353 ? 3.754   11.878  13.655  1.00 30.18 ? 353  ARG A CA    1 
ATOM   2736 C  C     . ARG A 1 353 ? 4.042   12.837  12.481  1.00 33.04 ? 353  ARG A C     1 
ATOM   2737 O  O     . ARG A 1 353 ? 3.149   13.578  12.063  1.00 45.70 ? 353  ARG A O     1 
ATOM   2738 C  CB    . ARG A 1 353 ? 2.776   10.770  13.235  1.00 29.29 ? 353  ARG A CB    1 
ATOM   2739 C  CG    . ARG A 1 353 ? 2.424   9.783   14.348  1.00 30.26 ? 353  ARG A CG    1 
ATOM   2740 C  CD    . ARG A 1 353 ? 3.592   8.927   14.801  1.00 27.09 ? 353  ARG A CD    1 
ATOM   2741 N  NE    . ARG A 1 353 ? 4.070   7.994   13.777  1.00 28.01 ? 353  ARG A NE    1 
ATOM   2742 C  CZ    . ARG A 1 353 ? 5.221   7.306   13.843  1.00 26.27 ? 353  ARG A CZ    1 
ATOM   2743 N  NH1   . ARG A 1 353 ? 6.016   7.431   14.893  1.00 27.25 ? 353  ARG A NH1   1 
ATOM   2744 N  NH2   . ARG A 1 353 ? 5.613   6.520   12.853  1.00 26.08 ? 353  ARG A NH2   1 
ATOM   2745 N  N     . ARG A 1 354 ? 5.216   12.753  11.891  1.00 33.08 ? 354  ARG A N     1 
ATOM   2746 C  CA    . ARG A 1 354 ? 5.670   13.704  10.853  1.00 40.60 ? 354  ARG A CA    1 
ATOM   2747 C  C     . ARG A 1 354 ? 5.344   13.222  9.425   1.00 41.20 ? 354  ARG A C     1 
ATOM   2748 O  O     . ARG A 1 354 ? 5.507   14.038  8.534   1.00 45.73 ? 354  ARG A O     1 
ATOM   2749 C  CB    . ARG A 1 354 ? 7.159   13.983  11.070  1.00 43.31 ? 354  ARG A CB    1 
ATOM   2750 C  CG    . ARG A 1 354 ? 8.094   12.852  10.692  1.00 50.67 ? 354  ARG A CG    1 
ATOM   2751 C  CD    . ARG A 1 354 ? 9.509   13.151  11.183  1.00 62.49 ? 354  ARG A CD    1 
ATOM   2752 N  NE    . ARG A 1 354 ? 10.330  11.948  11.335  1.00 70.92 ? 354  ARG A NE    1 
ATOM   2753 C  CZ    . ARG A 1 354 ? 10.827  11.214  10.331  1.00 70.87 ? 354  ARG A CZ    1 
ATOM   2754 N  NH1   . ARG A 1 354 ? 10.600  11.563  9.073   1.00 70.64 ? 354  ARG A NH1   1 
ATOM   2755 N  NH2   . ARG A 1 354 ? 11.543  10.128  10.595  1.00 68.15 ? 354  ARG A NH2   1 
ATOM   2756 N  N     . HIS A 1 355 ? 4.863   11.995  9.186   1.00 43.93 ? 355  HIS A N     1 
ATOM   2757 C  CA    . HIS A 1 355 ? 4.472   11.523  7.823   1.00 44.87 ? 355  HIS A CA    1 
ATOM   2758 C  C     . HIS A 1 355 ? 2.961   11.630  7.623   1.00 43.16 ? 355  HIS A C     1 
ATOM   2759 O  O     . HIS A 1 355 ? 2.220   11.341  8.563   1.00 42.10 ? 355  HIS A O     1 
ATOM   2760 C  CB    . HIS A 1 355 ? 4.830   10.060  7.546   1.00 50.15 ? 355  HIS A CB    1 
ATOM   2761 C  CG    . HIS A 1 355 ? 6.279   9.775   7.569   1.00 57.19 ? 355  HIS A CG    1 
ATOM   2762 N  ND1   . HIS A 1 355 ? 7.021   9.916   8.719   1.00 61.68 ? 355  HIS A ND1   1 
ATOM   2763 C  CD2   . HIS A 1 355 ? 7.110   9.325   6.606   1.00 63.13 ? 355  HIS A CD2   1 
ATOM   2764 C  CE1   . HIS A 1 355 ? 8.265   9.583   8.467   1.00 71.41 ? 355  HIS A CE1   1 
ATOM   2765 N  NE2   . HIS A 1 355 ? 8.346   9.215   7.171   1.00 72.14 ? 355  HIS A NE2   1 
ATOM   2766 N  N     . LYS A 1 356 ? 2.553   11.913  6.386   1.00 47.08 ? 356  LYS A N     1 
ATOM   2767 C  CA    . LYS A 1 356 ? 1.143   12.007  5.920   1.00 46.07 ? 356  LYS A CA    1 
ATOM   2768 C  C     . LYS A 1 356 ? 0.483   10.626  6.013   1.00 40.10 ? 356  LYS A C     1 
ATOM   2769 O  O     . LYS A 1 356 ? -0.624  10.522  6.592   1.00 41.03 ? 356  LYS A O     1 
ATOM   2770 C  CB    . LYS A 1 356 ? 1.135   12.494  4.466   1.00 51.35 ? 356  LYS A CB    1 
ATOM   2771 C  CG    . LYS A 1 356 ? -0.202  13.017  3.973   1.00 63.33 ? 356  LYS A CG    1 
ATOM   2772 C  CD    . LYS A 1 356 ? -0.723  14.176  4.810   1.00 66.39 ? 356  LYS A CD    1 
ATOM   2773 C  CE    . LYS A 1 356 ? -1.709  15.059  4.068   1.00 71.11 ? 356  LYS A CE    1 
ATOM   2774 N  NZ    . LYS A 1 356 ? -2.943  15.293  4.862   1.00 72.97 ? 356  LYS A NZ    1 
ATOM   2775 N  N     . VAL A 1 357 ? 1.151   9.630   5.433   1.00 33.25 ? 357  VAL A N     1 
ATOM   2776 C  CA    . VAL A 1 357 ? 0.730   8.205   5.397   1.00 35.02 ? 357  VAL A CA    1 
ATOM   2777 C  C     . VAL A 1 357 ? 1.552   7.505   6.463   1.00 35.72 ? 357  VAL A C     1 
ATOM   2778 O  O     . VAL A 1 357 ? 2.777   7.435   6.284   1.00 33.79 ? 357  VAL A O     1 
ATOM   2779 C  CB    . VAL A 1 357 ? 0.993   7.566   4.022   1.00 37.12 ? 357  VAL A CB    1 
ATOM   2780 C  CG1   . VAL A 1 357 ? 0.748   6.063   4.041   1.00 36.58 ? 357  VAL A CG1   1 
ATOM   2781 C  CG2   . VAL A 1 357 ? 0.194   8.259   2.928   1.00 37.79 ? 357  VAL A CG2   1 
ATOM   2782 N  N     . ASP A 1 358 ? 0.914   7.049   7.535   1.00 32.27 ? 358  ASP A N     1 
ATOM   2783 C  CA    . ASP A 1 358 ? 1.645   6.739   8.783   1.00 29.10 ? 358  ASP A CA    1 
ATOM   2784 C  C     . ASP A 1 358 ? 0.956   5.601   9.511   1.00 26.75 ? 358  ASP A C     1 
ATOM   2785 O  O     . ASP A 1 358 ? -0.281  5.581   9.532   1.00 26.33 ? 358  ASP A O     1 
ATOM   2786 C  CB    . ASP A 1 358 ? 1.697   7.967   9.687   1.00 33.12 ? 358  ASP A CB    1 
ATOM   2787 C  CG    . ASP A 1 358 ? 2.435   7.656   10.977  1.00 33.75 ? 358  ASP A CG    1 
ATOM   2788 O  OD1   . ASP A 1 358 ? 3.667   7.366   10.895  1.00 31.58 ? 358  ASP A OD1   1 
ATOM   2789 O  OD2   . ASP A 1 358 ? 1.763   7.645   12.036  1.00 38.98 ? 358  ASP A OD2   1 
ATOM   2790 N  N     . LEU A 1 359 ? 1.749   4.745   10.150  1.00 27.66 ? 359  LEU A N     1 
ATOM   2791 C  CA    . LEU A 1 359 ? 1.244   3.579   10.898  1.00 27.58 ? 359  LEU A CA    1 
ATOM   2792 C  C     . LEU A 1 359 ? 0.250   3.999   11.999  1.00 24.73 ? 359  LEU A C     1 
ATOM   2793 O  O     . LEU A 1 359 ? -0.762  3.311   12.147  1.00 23.45 ? 359  LEU A O     1 
ATOM   2794 C  CB    . LEU A 1 359 ? 2.418   2.800   11.485  1.00 31.13 ? 359  LEU A CB    1 
ATOM   2795 C  CG    . LEU A 1 359 ? 1.969   1.773   12.516  1.00 33.42 ? 359  LEU A CG    1 
ATOM   2796 C  CD1   . LEU A 1 359 ? 1.428   0.543   11.811  1.00 37.32 ? 359  LEU A CD1   1 
ATOM   2797 C  CD2   . LEU A 1 359 ? 3.082   1.425   13.463  1.00 39.46 ? 359  LEU A CD2   1 
ATOM   2798 N  N     . LEU A 1 360 ? 0.548   5.011   12.817  1.00 24.20 ? 360  LEU A N     1 
ATOM   2799 C  CA    . LEU A 1 360 ? -0.339  5.396   13.948  1.00 24.61 ? 360  LEU A CA    1 
ATOM   2800 C  C     . LEU A 1 360 ? -1.664  5.935   13.386  1.00 25.34 ? 360  LEU A C     1 
ATOM   2801 O  O     . LEU A 1 360 ? -2.738  5.538   13.890  1.00 26.54 ? 360  LEU A O     1 
ATOM   2802 C  CB    . LEU A 1 360 ? 0.350   6.420   14.863  1.00 25.26 ? 360  LEU A CB    1 
ATOM   2803 C  CG    . LEU A 1 360 ? -0.509  6.880   16.048  1.00 26.02 ? 360  LEU A CG    1 
ATOM   2804 C  CD1   . LEU A 1 360 ? -1.079  5.671   16.780  1.00 24.88 ? 360  LEU A CD1   1 
ATOM   2805 C  CD2   . LEU A 1 360 ? 0.262   7.806   17.004  1.00 22.90 ? 360  LEU A CD2   1 
ATOM   2806 N  N     . LEU A 1 361 ? -1.617  6.766   12.354  1.00 24.83 ? 361  LEU A N     1 
ATOM   2807 C  CA    . LEU A 1 361 ? -2.854  7.274   11.691  1.00 29.93 ? 361  LEU A CA    1 
ATOM   2808 C  C     . LEU A 1 361 ? -3.673  6.086   11.154  1.00 26.07 ? 361  LEU A C     1 
ATOM   2809 O  O     . LEU A 1 361 ? -4.901  6.072   11.337  1.00 25.32 ? 361  LEU A O     1 
ATOM   2810 C  CB    . LEU A 1 361 ? -2.493  8.242   10.558  1.00 31.54 ? 361  LEU A CB    1 
ATOM   2811 C  CG    . LEU A 1 361 ? -1.699  9.484   10.968  1.00 38.65 ? 361  LEU A CG    1 
ATOM   2812 C  CD1   . LEU A 1 361 ? -1.647  10.499  9.829   1.00 40.28 ? 361  LEU A CD1   1 
ATOM   2813 C  CD2   . LEU A 1 361 ? -2.270  10.119  12.222  1.00 40.12 ? 361  LEU A CD2   1 
ATOM   2814 N  N     . HIS A 1 362 ? -3.029  5.121   10.511  1.00 24.10 ? 362  HIS A N     1 
ATOM   2815 C  CA    . HIS A 1 362 ? -3.696  3.880   10.026  1.00 24.53 ? 362  HIS A CA    1 
ATOM   2816 C  C     . HIS A 1 362 ? -4.304  3.105   11.219  1.00 23.08 ? 362  HIS A C     1 
ATOM   2817 O  O     . HIS A 1 362 ? -5.529  2.854   11.220  1.00 23.74 ? 362  HIS A O     1 
ATOM   2818 C  CB    . HIS A 1 362 ? -2.720  3.097   9.143   1.00 27.06 ? 362  HIS A CB    1 
ATOM   2819 C  CG    . HIS A 1 362 ? -3.213  1.750   8.739   1.00 28.74 ? 362  HIS A CG    1 
ATOM   2820 N  ND1   . HIS A 1 362 ? -2.915  0.598   9.478   1.00 31.04 ? 362  HIS A ND1   1 
ATOM   2821 C  CD2   . HIS A 1 362 ? -3.945  1.347   7.684   1.00 29.86 ? 362  HIS A CD2   1 
ATOM   2822 C  CE1   . HIS A 1 362 ? -3.452  -0.444  8.876   1.00 30.44 ? 362  HIS A CE1   1 
ATOM   2823 N  NE2   . HIS A 1 362 ? -4.108  -0.015  7.784   1.00 29.02 ? 362  HIS A NE2   1 
ATOM   2824 N  N     . ARG A 1 363 ? -3.546  2.793   12.263  1.00 22.08 ? 363  ARG A N     1 
ATOM   2825 C  CA    . ARG A 1 363 ? -4.085  1.945   13.371  1.00 23.40 ? 363  ARG A CA    1 
ATOM   2826 C  C     . ARG A 1 363 ? -5.117  2.720   14.186  1.00 21.83 ? 363  ARG A C     1 
ATOM   2827 O  O     . ARG A 1 363 ? -5.995  2.081   14.802  1.00 21.77 ? 363  ARG A O     1 
ATOM   2828 C  CB    . ARG A 1 363 ? -2.963  1.451   14.289  1.00 26.08 ? 363  ARG A CB    1 
ATOM   2829 C  CG    . ARG A 1 363 ? -1.917  0.610   13.563  1.00 29.37 ? 363  ARG A CG    1 
ATOM   2830 C  CD    . ARG A 1 363 ? -2.188  -0.870  13.530  1.00 29.57 ? 363  ARG A CD    1 
ATOM   2831 N  NE    . ARG A 1 363 ? -1.108  -1.520  12.766  1.00 36.52 ? 363  ARG A NE    1 
ATOM   2832 C  CZ    . ARG A 1 363 ? -1.252  -2.294  11.656  1.00 37.31 ? 363  ARG A CZ    1 
ATOM   2833 N  NH1   . ARG A 1 363 ? -2.445  -2.579  11.159  1.00 32.10 ? 363  ARG A NH1   1 
ATOM   2834 N  NH2   . ARG A 1 363 ? -0.184  -2.829  11.084  1.00 40.48 ? 363  ARG A NH2   1 
ATOM   2835 N  N     . ALA A 1 364 ? -5.038  4.051   14.197  1.00 21.13 ? 364  ALA A N     1 
ATOM   2836 C  CA    . ALA A 1 364 ? -5.963  4.907   14.976  1.00 21.66 ? 364  ALA A CA    1 
ATOM   2837 C  C     . ALA A 1 364 ? -7.398  4.738   14.442  1.00 22.22 ? 364  ALA A C     1 
ATOM   2838 O  O     . ALA A 1 364 ? -8.346  4.892   15.255  1.00 23.90 ? 364  ALA A O     1 
ATOM   2839 C  CB    . ALA A 1 364 ? -5.511  6.349   14.928  1.00 21.40 ? 364  ALA A CB    1 
ATOM   2840 N  N     . GLU A 1 365 ? -7.571  4.456   13.143  1.00 22.83 ? 365  GLU A N     1 
ATOM   2841 C  CA    . GLU A 1 365 ? -8.912  4.242   12.518  1.00 24.08 ? 365  GLU A CA    1 
ATOM   2842 C  C     . GLU A 1 365 ? -9.529  2.948   13.061  1.00 21.56 ? 365  GLU A C     1 
ATOM   2843 O  O     . GLU A 1 365 ? -10.699 2.949   13.484  1.00 21.33 ? 365  GLU A O     1 
ATOM   2844 C  CB    . GLU A 1 365 ? -8.828  4.147   10.987  1.00 28.45 ? 365  GLU A CB    1 
ATOM   2845 C  CG    . GLU A 1 365 ? -8.458  5.463   10.305  1.00 34.26 ? 365  GLU A CG    1 
ATOM   2846 C  CD    . GLU A 1 365 ? -9.465  6.583   10.521  1.00 42.33 ? 365  GLU A CD    1 
ATOM   2847 O  OE1   . GLU A 1 365 ? -10.443 6.641   9.757   1.00 50.79 ? 365  GLU A OE1   1 
ATOM   2848 O  OE2   . GLU A 1 365 ? -9.271  7.405   11.459  1.00 51.52 ? 365  GLU A OE2   1 
ATOM   2849 N  N     . THR A 1 366 ? -8.752  1.877   13.058  1.00 20.08 ? 366  THR A N     1 
ATOM   2850 C  CA    . THR A 1 366 ? -9.186  0.554   13.553  1.00 21.32 ? 366  THR A CA    1 
ATOM   2851 C  C     . THR A 1 366 ? -9.519  0.600   15.049  1.00 20.17 ? 366  THR A C     1 
ATOM   2852 O  O     . THR A 1 366 ? -10.484 -0.022  15.443  1.00 20.71 ? 366  THR A O     1 
ATOM   2853 C  CB    . THR A 1 366 ? -8.114  -0.489  13.258  1.00 21.82 ? 366  THR A CB    1 
ATOM   2854 O  OG1   . THR A 1 366 ? -7.543  -0.136  11.992  1.00 24.41 ? 366  THR A OG1   1 
ATOM   2855 C  CG2   . THR A 1 366 ? -8.722  -1.864  13.237  1.00 21.35 ? 366  THR A CG2   1 
ATOM   2856 N  N     . MET A 1 367 ? -8.748  1.323   15.854  1.00 22.14 ? 367  MET A N     1 
ATOM   2857 C  CA    . MET A 1 367 ? -8.942  1.397   17.332  1.00 20.83 ? 367  MET A CA    1 
ATOM   2858 C  C     . MET A 1 367 ? -10.165 2.273   17.700  1.00 19.98 ? 367  MET A C     1 
ATOM   2859 O  O     . MET A 1 367 ? -10.570 2.276   18.894  1.00 19.80 ? 367  MET A O     1 
ATOM   2860 C  CB    . MET A 1 367 ? -7.645  1.874   18.000  1.00 21.52 ? 367  MET A CB    1 
ATOM   2861 C  CG    . MET A 1 367 ? -6.520  0.863   17.880  1.00 20.81 ? 367  MET A CG    1 
ATOM   2862 S  SD    . MET A 1 367 ? -5.048  1.150   18.925  1.00 21.63 ? 367  MET A SD    1 
ATOM   2863 C  CE    . MET A 1 367 ? -4.371  2.594   18.105  1.00 24.13 ? 367  MET A CE    1 
ATOM   2864 N  N     . LYS A 1 368 ? -10.831 2.909   16.735  1.00 18.77 ? 368  LYS A N     1 
ATOM   2865 C  CA    . LYS A 1 368 ? -12.168 3.492   16.994  1.00 22.67 ? 368  LYS A CA    1 
ATOM   2866 C  C     . LYS A 1 368 ? -13.222 2.878   16.058  1.00 21.69 ? 368  LYS A C     1 
ATOM   2867 O  O     . LYS A 1 368 ? -14.267 3.500   15.879  1.00 22.80 ? 368  LYS A O     1 
ATOM   2868 C  CB    . LYS A 1 368 ? -12.117 5.024   16.966  1.00 25.18 ? 368  LYS A CB    1 
ATOM   2869 C  CG    . LYS A 1 368 ? -11.911 5.663   15.618  1.00 28.17 ? 368  LYS A CG    1 
ATOM   2870 C  CD    . LYS A 1 368 ? -12.189 7.157   15.634  1.00 33.32 ? 368  LYS A CD    1 
ATOM   2871 C  CE    . LYS A 1 368 ? -11.712 7.820   14.360  1.00 39.80 ? 368  LYS A CE    1 
ATOM   2872 N  NZ    . LYS A 1 368 ? -12.023 9.265   14.365  1.00 48.57 ? 368  LYS A NZ    1 
ATOM   2873 N  N     . GLY A 1 369 ? -12.980 1.682   15.524  1.00 21.10 ? 369  GLY A N     1 
ATOM   2874 C  CA    . GLY A 1 369 ? -14.018 0.886   14.843  1.00 21.52 ? 369  GLY A CA    1 
ATOM   2875 C  C     . GLY A 1 369 ? -14.391 1.417   13.465  1.00 19.58 ? 369  GLY A C     1 
ATOM   2876 O  O     . GLY A 1 369 ? -15.514 1.214   13.083  1.00 19.88 ? 369  GLY A O     1 
ATOM   2877 N  N     . VAL A 1 370 ? -13.468 2.025   12.725  1.00 19.20 ? 370  VAL A N     1 
ATOM   2878 C  CA    . VAL A 1 370 ? -13.710 2.480   11.327  1.00 20.92 ? 370  VAL A CA    1 
ATOM   2879 C  C     . VAL A 1 370 ? -13.304 1.355   10.367  1.00 20.23 ? 370  VAL A C     1 
ATOM   2880 O  O     . VAL A 1 370 ? -12.141 1.023   10.280  1.00 19.88 ? 370  VAL A O     1 
ATOM   2881 C  CB    . VAL A 1 370 ? -12.989 3.812   11.031  1.00 21.60 ? 370  VAL A CB    1 
ATOM   2882 C  CG1   . VAL A 1 370 ? -13.179 4.237   9.577   1.00 22.05 ? 370  VAL A CG1   1 
ATOM   2883 C  CG2   . VAL A 1 370 ? -13.460 4.914   11.976  1.00 21.77 ? 370  VAL A CG2   1 
ATOM   2884 N  N     . PRO A 1 371 ? -14.247 0.717   9.632   1.00 19.64 ? 371  PRO A N     1 
ATOM   2885 C  CA    . PRO A 1 371 ? -13.903 -0.394  8.749   1.00 19.40 ? 371  PRO A CA    1 
ATOM   2886 C  C     . PRO A 1 371 ? -13.224 0.073   7.451   1.00 22.05 ? 371  PRO A C     1 
ATOM   2887 O  O     . PRO A 1 371 ? -13.725 1.009   6.841   1.00 23.32 ? 371  PRO A O     1 
ATOM   2888 C  CB    . PRO A 1 371 ? -15.259 -1.012  8.391   1.00 20.12 ? 371  PRO A CB    1 
ATOM   2889 C  CG    . PRO A 1 371 ? -16.273 0.121   8.581   1.00 20.29 ? 371  PRO A CG    1 
ATOM   2890 C  CD    . PRO A 1 371 ? -15.676 1.049   9.615   1.00 17.84 ? 371  PRO A CD    1 
ATOM   2891 N  N     . LYS A 1 372 ? -12.145 -0.596  7.041   1.00 22.73 ? 372  LYS A N     1 
ATOM   2892 C  CA    . LYS A 1 372 ? -11.370 -0.273  5.808   1.00 23.42 ? 372  LYS A CA    1 
ATOM   2893 C  C     . LYS A 1 372 ? -10.873 -1.567  5.161   1.00 22.34 ? 372  LYS A C     1 
ATOM   2894 O  O     . LYS A 1 372 ? -11.056 -2.636  5.750   1.00 18.75 ? 372  LYS A O     1 
ATOM   2895 C  CB    . LYS A 1 372 ? -10.233 0.685   6.174   1.00 26.88 ? 372  LYS A CB    1 
ATOM   2896 C  CG    . LYS A 1 372 ? -10.760 2.017   6.728   1.00 32.95 ? 372  LYS A CG    1 
ATOM   2897 C  CD    . LYS A 1 372 ? -9.767  3.153   6.843   1.00 35.72 ? 372  LYS A CD    1 
ATOM   2898 C  CE    . LYS A 1 372 ? -9.382  3.713   5.494   1.00 42.51 ? 372  LYS A CE    1 
ATOM   2899 N  NZ    . LYS A 1 372 ? -8.268  4.691   5.579   1.00 50.32 ? 372  LYS A NZ    1 
ATOM   2900 N  N     . LEU A 1 373 ? -10.227 -1.461  4.001   1.00 21.90 ? 373  LEU A N     1 
ATOM   2901 C  CA    . LEU A 1 373 ? -9.553  -2.613  3.352   1.00 22.88 ? 373  LEU A CA    1 
ATOM   2902 C  C     . LEU A 1 373 ? -8.096  -2.280  3.033   1.00 20.69 ? 373  LEU A C     1 
ATOM   2903 O  O     . LEU A 1 373 ? -7.492  -3.043  2.286   1.00 21.92 ? 373  LEU A O     1 
ATOM   2904 C  CB    . LEU A 1 373 ? -10.358 -3.049  2.114   1.00 22.71 ? 373  LEU A CB    1 
ATOM   2905 C  CG    . LEU A 1 373 ? -11.667 -3.755  2.454   1.00 23.27 ? 373  LEU A CG    1 
ATOM   2906 C  CD1   . LEU A 1 373 ? -12.590 -3.834  1.252   1.00 25.12 ? 373  LEU A CD1   1 
ATOM   2907 C  CD2   . LEU A 1 373 ? -11.410 -5.134  3.020   1.00 24.12 ? 373  LEU A CD2   1 
ATOM   2908 N  N     . THR A 1 374 ? -7.523  -1.258  3.659   1.00 21.11 ? 374  THR A N     1 
ATOM   2909 C  CA    . THR A 1 374 ? -6.109  -0.837  3.444   1.00 21.26 ? 374  THR A CA    1 
ATOM   2910 C  C     . THR A 1 374 ? -5.124  -1.910  3.952   1.00 22.33 ? 374  THR A C     1 
ATOM   2911 O  O     . THR A 1 374 ? -4.033  -1.983  3.426   1.00 23.62 ? 374  THR A O     1 
ATOM   2912 C  CB    . THR A 1 374 ? -5.852  0.509   4.133   1.00 22.68 ? 374  THR A CB    1 
ATOM   2913 O  OG1   . THR A 1 374 ? -6.451  0.459   5.428   1.00 21.02 ? 374  THR A OG1   1 
ATOM   2914 C  CG2   . THR A 1 374 ? -6.445  1.672   3.363   1.00 23.30 ? 374  THR A CG2   1 
ATOM   2915 N  N     . GLU A 1 375 ? -5.487  -2.719  4.955   1.00 23.45 ? 375  GLU A N     1 
ATOM   2916 C  CA    . GLU A 1 375 ? -4.578  -3.707  5.589   1.00 21.96 ? 375  GLU A CA    1 
ATOM   2917 C  C     . GLU A 1 375 ? -4.021  -4.679  4.546   1.00 22.33 ? 375  GLU A C     1 
ATOM   2918 O  O     . GLU A 1 375 ? -2.861  -5.100  4.715   1.00 20.01 ? 375  GLU A O     1 
ATOM   2919 C  CB    . GLU A 1 375 ? -5.280  -4.488  6.700   1.00 23.52 ? 375  GLU A CB    1 
ATOM   2920 C  CG    . GLU A 1 375 ? -4.300  -5.128  7.673   1.00 24.24 ? 375  GLU A CG    1 
ATOM   2921 C  CD    . GLU A 1 375 ? -3.655  -4.158  8.663   1.00 25.94 ? 375  GLU A CD    1 
ATOM   2922 O  OE1   . GLU A 1 375 ? -4.143  -3.002  8.814   1.00 24.79 ? 375  GLU A OE1   1 
ATOM   2923 O  OE2   . GLU A 1 375 ? -2.683  -4.559  9.296   1.00 26.43 ? 375  GLU A OE2   1 
ATOM   2924 N  N     . PHE A 1 376 ? -4.776  -4.983  3.482   1.00 22.14 ? 376  PHE A N     1 
ATOM   2925 C  CA    . PHE A 1 376 ? -4.341  -5.940  2.422   1.00 23.26 ? 376  PHE A CA    1 
ATOM   2926 C  C     . PHE A 1 376 ? -3.082  -5.462  1.690   1.00 22.56 ? 376  PHE A C     1 
ATOM   2927 O  O     . PHE A 1 376 ? -2.367  -6.342  1.107   1.00 22.84 ? 376  PHE A O     1 
ATOM   2928 C  CB    . PHE A 1 376 ? -5.455  -6.256  1.426   1.00 21.23 ? 376  PHE A CB    1 
ATOM   2929 C  CG    . PHE A 1 376 ? -6.483  -7.201  1.977   1.00 22.00 ? 376  PHE A CG    1 
ATOM   2930 C  CD1   . PHE A 1 376 ? -6.230  -8.564  2.034   1.00 22.72 ? 376  PHE A CD1   1 
ATOM   2931 C  CD2   . PHE A 1 376 ? -7.711  -6.735  2.420   1.00 23.14 ? 376  PHE A CD2   1 
ATOM   2932 C  CE1   . PHE A 1 376 ? -7.176  -9.442  2.542   1.00 21.68 ? 376  PHE A CE1   1 
ATOM   2933 C  CE2   . PHE A 1 376 ? -8.664  -7.623  2.908   1.00 21.66 ? 376  PHE A CE2   1 
ATOM   2934 C  CZ    . PHE A 1 376 ? -8.380  -8.963  2.994   1.00 21.12 ? 376  PHE A CZ    1 
ATOM   2935 N  N     . ASN A 1 377 ? -2.773  -4.173  1.751   1.00 21.90 ? 377  ASN A N     1 
ATOM   2936 C  CA    . ASN A 1 377 ? -1.536  -3.610  1.141   1.00 23.99 ? 377  ASN A CA    1 
ATOM   2937 C  C     . ASN A 1 377 ? -0.275  -4.234  1.730   1.00 22.82 ? 377  ASN A C     1 
ATOM   2938 O  O     . ASN A 1 377 ? 0.683   -4.290  0.996   1.00 25.46 ? 377  ASN A O     1 
ATOM   2939 C  CB    . ASN A 1 377 ? -1.525  -2.088  1.209   1.00 25.15 ? 377  ASN A CB    1 
ATOM   2940 C  CG    . ASN A 1 377 ? -2.486  -1.530  0.181   1.00 27.26 ? 377  ASN A CG    1 
ATOM   2941 O  OD1   . ASN A 1 377 ? -2.301  -1.765  -1.028  1.00 26.71 ? 377  ASN A OD1   1 
ATOM   2942 N  ND2   . ASN A 1 377 ? -3.523  -0.843  0.653   1.00 24.20 ? 377  ASN A ND2   1 
ATOM   2943 N  N     . PHE A 1 378 ? -0.298  -4.783  2.949   1.00 23.49 ? 378  PHE A N     1 
ATOM   2944 C  CA    . PHE A 1 378 ? 0.906   -5.370  3.593   1.00 22.38 ? 378  PHE A CA    1 
ATOM   2945 C  C     . PHE A 1 378 ? 1.365   -6.606  2.809   1.00 23.41 ? 378  PHE A C     1 
ATOM   2946 O  O     . PHE A 1 378 ? 2.563   -6.927  2.851   1.00 23.13 ? 378  PHE A O     1 
ATOM   2947 C  CB    . PHE A 1 378 ? 0.665   -5.632  5.081   1.00 22.54 ? 378  PHE A CB    1 
ATOM   2948 C  CG    . PHE A 1 378 ? 0.380   -7.062  5.448   1.00 22.86 ? 378  PHE A CG    1 
ATOM   2949 C  CD1   . PHE A 1 378 ? -0.862  -7.620  5.229   1.00 25.85 ? 378  PHE A CD1   1 
ATOM   2950 C  CD2   . PHE A 1 378 ? 1.368   -7.859  5.995   1.00 26.51 ? 378  PHE A CD2   1 
ATOM   2951 C  CE1   . PHE A 1 378 ? -1.127  -8.937  5.567   1.00 26.65 ? 378  PHE A CE1   1 
ATOM   2952 C  CE2   . PHE A 1 378 ? 1.109   -9.174  6.342   1.00 25.59 ? 378  PHE A CE2   1 
ATOM   2953 C  CZ    . PHE A 1 378 ? -0.136  -9.713  6.113   1.00 28.32 ? 378  PHE A CZ    1 
ATOM   2954 N  N     . LEU A 1 379 ? 0.457   -7.267  2.093   1.00 24.15 ? 379  LEU A N     1 
ATOM   2955 C  CA    . LEU A 1 379 ? 0.784   -8.467  1.275   1.00 25.49 ? 379  LEU A CA    1 
ATOM   2956 C  C     . LEU A 1 379 ? 1.736   -8.116  0.119   1.00 26.70 ? 379  LEU A C     1 
ATOM   2957 O  O     . LEU A 1 379 ? 2.199   -9.058  -0.548  1.00 28.61 ? 379  LEU A O     1 
ATOM   2958 C  CB    . LEU A 1 379 ? -0.503  -9.057  0.700   1.00 24.76 ? 379  LEU A CB    1 
ATOM   2959 C  CG    . LEU A 1 379 ? -1.498  -9.627  1.701   1.00 24.30 ? 379  LEU A CG    1 
ATOM   2960 C  CD1   . LEU A 1 379 ? -2.719  -10.160 0.963   1.00 23.52 ? 379  LEU A CD1   1 
ATOM   2961 C  CD2   . LEU A 1 379 ? -0.868  -10.717 2.561   1.00 26.51 ? 379  LEU A CD2   1 
ATOM   2962 N  N     . ASN A 1 380 ? 1.970   -6.836  -0.169  1.00 25.60 ? 380  ASN A N     1 
ATOM   2963 C  CA    . ASN A 1 380 ? 2.875   -6.406  -1.271  1.00 27.98 ? 380  ASN A CA    1 
ATOM   2964 C  C     . ASN A 1 380 ? 4.325   -6.250  -0.782  1.00 29.11 ? 380  ASN A C     1 
ATOM   2965 O  O     . ASN A 1 380 ? 5.176   -5.814  -1.589  1.00 29.54 ? 380  ASN A O     1 
ATOM   2966 C  CB    . ASN A 1 380 ? 2.361   -5.126  -1.954  1.00 27.56 ? 380  ASN A CB    1 
ATOM   2967 C  CG    . ASN A 1 380 ? 1.234   -5.406  -2.937  1.00 27.26 ? 380  ASN A CG    1 
ATOM   2968 O  OD1   . ASN A 1 380 ? 1.072   -6.524  -3.461  1.00 24.58 ? 380  ASN A OD1   1 
ATOM   2969 N  ND2   . ASN A 1 380 ? 0.406   -4.406  -3.136  1.00 27.62 ? 380  ASN A ND2   1 
ATOM   2970 N  N     . TRP A 1 381 ? 4.613   -6.553  0.484   1.00 28.25 ? 381  TRP A N     1 
ATOM   2971 C  CA    . TRP A 1 381 ? 5.984   -6.448  1.053   1.00 28.61 ? 381  TRP A CA    1 
ATOM   2972 C  C     . TRP A 1 381 ? 7.003   -7.072  0.092   1.00 30.22 ? 381  TRP A C     1 
ATOM   2973 O  O     . TRP A 1 381 ? 8.011   -6.403  -0.217  1.00 30.65 ? 381  TRP A O     1 
ATOM   2974 C  CB    . TRP A 1 381 ? 6.069   -7.112  2.427   1.00 29.06 ? 381  TRP A CB    1 
ATOM   2975 C  CG    . TRP A 1 381 ? 7.459   -7.065  2.959   1.00 26.64 ? 381  TRP A CG    1 
ATOM   2976 C  CD1   . TRP A 1 381 ? 8.313   -8.113  3.125   1.00 27.27 ? 381  TRP A CD1   1 
ATOM   2977 C  CD2   . TRP A 1 381 ? 8.190   -5.882  3.291   1.00 26.64 ? 381  TRP A CD2   1 
ATOM   2978 N  NE1   . TRP A 1 381 ? 9.514   -7.668  3.591   1.00 29.05 ? 381  TRP A NE1   1 
ATOM   2979 C  CE2   . TRP A 1 381 ? 9.472   -6.304  3.709   1.00 27.54 ? 381  TRP A CE2   1 
ATOM   2980 C  CE3   . TRP A 1 381 ? 7.878   -4.525  3.306   1.00 24.53 ? 381  TRP A CE3   1 
ATOM   2981 C  CZ2   . TRP A 1 381 ? 10.452  -5.411  4.123   1.00 25.07 ? 381  TRP A CZ2   1 
ATOM   2982 C  CZ3   . TRP A 1 381 ? 8.846   -3.636  3.712   1.00 27.96 ? 381  TRP A CZ3   1 
ATOM   2983 C  CH2   . TRP A 1 381 ? 10.117  -4.077  4.113   1.00 28.86 ? 381  TRP A CH2   1 
ATOM   2984 N  N     . ASP A 1 382 ? 6.715   -8.281  -0.386  1.00 31.79 ? 382  ASP A N     1 
ATOM   2985 C  CA    . ASP A 1 382 ? 7.666   -9.118  -1.158  1.00 37.94 ? 382  ASP A CA    1 
ATOM   2986 C  C     . ASP A 1 382 ? 7.094   -9.437  -2.540  1.00 35.86 ? 382  ASP A C     1 
ATOM   2987 O  O     . ASP A 1 382 ? 7.241   -10.566 -2.985  1.00 38.93 ? 382  ASP A O     1 
ATOM   2988 C  CB    . ASP A 1 382 ? 7.974   -10.409 -0.399  1.00 43.89 ? 382  ASP A CB    1 
ATOM   2989 C  CG    . ASP A 1 382 ? 9.261   -11.062 -0.865  1.00 51.38 ? 382  ASP A CG    1 
ATOM   2990 O  OD1   . ASP A 1 382 ? 10.189  -10.305 -1.273  1.00 50.85 ? 382  ASP A OD1   1 
ATOM   2991 O  OD2   . ASP A 1 382 ? 9.317   -12.313 -0.831  1.00 53.20 ? 382  ASP A OD2   1 
ATOM   2992 N  N     . GLY A 1 383 ? 6.424   -8.478  -3.169  1.00 36.73 ? 383  GLY A N     1 
ATOM   2993 C  CA    . GLY A 1 383 ? 5.981   -8.586  -4.567  1.00 38.37 ? 383  GLY A CA    1 
ATOM   2994 C  C     . GLY A 1 383 ? 4.518   -8.967  -4.722  1.00 36.66 ? 383  GLY A C     1 
ATOM   2995 O  O     . GLY A 1 383 ? 3.980   -8.774  -5.834  1.00 40.05 ? 383  GLY A O     1 
ATOM   2996 N  N     . GLY A 1 384 ? 3.874   -9.476  -3.677  1.00 33.00 ? 384  GLY A N     1 
ATOM   2997 C  CA    . GLY A 1 384 ? 2.446   -9.843  -3.738  1.00 29.28 ? 384  GLY A CA    1 
ATOM   2998 C  C     . GLY A 1 384 ? 2.270   -11.256 -3.249  1.00 30.24 ? 384  GLY A C     1 
ATOM   2999 O  O     . GLY A 1 384 ? 3.113   -12.106 -3.566  1.00 32.74 ? 384  GLY A O     1 
ATOM   3000 N  N     . GLY A 1 385 ? 1.224   -11.529 -2.484  1.00 30.30 ? 385  GLY A N     1 
ATOM   3001 C  CA    . GLY A 1 385 ? 0.995   -12.914 -2.035  1.00 28.03 ? 385  GLY A CA    1 
ATOM   3002 C  C     . GLY A 1 385 ? -0.220  -13.045 -1.159  1.00 27.14 ? 385  GLY A C     1 
ATOM   3003 O  O     . GLY A 1 385 ? -0.981  -12.072 -1.041  1.00 26.18 ? 385  GLY A O     1 
ATOM   3004 N  N     . GLY A 1 386 ? -0.395  -14.243 -0.611  1.00 22.97 ? 386  GLY A N     1 
ATOM   3005 C  CA    . GLY A 1 386 ? -1.381  -14.528 0.431   1.00 23.06 ? 386  GLY A CA    1 
ATOM   3006 C  C     . GLY A 1 386 ? -0.729  -14.464 1.787   1.00 21.88 ? 386  GLY A C     1 
ATOM   3007 O  O     . GLY A 1 386 ? 0.492   -14.184 1.875   1.00 20.54 ? 386  GLY A O     1 
ATOM   3008 N  N     . HIS A 1 387 ? -1.513  -14.689 2.822   1.00 19.58 ? 387  HIS A N     1 
ATOM   3009 C  CA    . HIS A 1 387 ? -0.971  -14.792 4.189   1.00 20.26 ? 387  HIS A CA    1 
ATOM   3010 C  C     . HIS A 1 387 ? -1.661  -15.917 4.945   1.00 19.51 ? 387  HIS A C     1 
ATOM   3011 O  O     . HIS A 1 387 ? -2.772  -16.333 4.547   1.00 18.28 ? 387  HIS A O     1 
ATOM   3012 C  CB    . HIS A 1 387 ? -1.043  -13.448 4.922   1.00 20.39 ? 387  HIS A CB    1 
ATOM   3013 C  CG    . HIS A 1 387 ? -2.392  -12.969 5.363   1.00 19.25 ? 387  HIS A CG    1 
ATOM   3014 N  ND1   . HIS A 1 387 ? -2.705  -12.871 6.688   1.00 18.11 ? 387  HIS A ND1   1 
ATOM   3015 C  CD2   . HIS A 1 387 ? -3.456  -12.474 4.673   1.00 19.50 ? 387  HIS A CD2   1 
ATOM   3016 C  CE1   . HIS A 1 387 ? -3.899  -12.328 6.820   1.00 19.25 ? 387  HIS A CE1   1 
ATOM   3017 N  NE2   . HIS A 1 387 ? -4.420  -12.067 5.571   1.00 19.88 ? 387  HIS A NE2   1 
ATOM   3018 N  N     . VAL A 1 388 ? -0.957  -16.431 5.941   1.00 18.52 ? 388  VAL A N     1 
ATOM   3019 C  CA    . VAL A 1 388 ? -1.500  -17.374 6.949   1.00 20.10 ? 388  VAL A CA    1 
ATOM   3020 C  C     . VAL A 1 388 ? -0.819  -17.002 8.261   1.00 20.06 ? 388  VAL A C     1 
ATOM   3021 O  O     . VAL A 1 388 ? 0.253   -16.395 8.225   1.00 21.27 ? 388  VAL A O     1 
ATOM   3022 C  CB    . VAL A 1 388 ? -1.295  -18.845 6.554   1.00 20.71 ? 388  VAL A CB    1 
ATOM   3023 C  CG1   . VAL A 1 388 ? 0.177   -19.274 6.620   1.00 22.42 ? 388  VAL A CG1   1 
ATOM   3024 C  CG2   . VAL A 1 388 ? -2.149  -19.751 7.415   1.00 21.06 ? 388  VAL A CG2   1 
ATOM   3025 N  N     . GLY A 1 389 ? -1.483  -17.240 9.374   1.00 22.08 ? 389  GLY A N     1 
ATOM   3026 C  CA    . GLY A 1 389 ? -1.001  -16.867 10.710  1.00 20.84 ? 389  GLY A CA    1 
ATOM   3027 C  C     . GLY A 1 389 ? -0.992  -18.065 11.613  1.00 21.54 ? 389  GLY A C     1 
ATOM   3028 O  O     . GLY A 1 389 ? -1.690  -19.061 11.320  1.00 21.99 ? 389  GLY A O     1 
ATOM   3029 N  N     . PHE A 1 390 ? -0.182  -17.973 12.657  1.00 20.63 ? 390  PHE A N     1 
ATOM   3030 C  CA    . PHE A 1 390 ? -0.081  -18.949 13.755  1.00 19.42 ? 390  PHE A CA    1 
ATOM   3031 C  C     . PHE A 1 390 ? -0.088  -18.124 15.038  1.00 18.81 ? 390  PHE A C     1 
ATOM   3032 O  O     . PHE A 1 390 ? 0.855   -17.332 15.220  1.00 18.52 ? 390  PHE A O     1 
ATOM   3033 C  CB    . PHE A 1 390 ? 1.193   -19.784 13.582  1.00 20.98 ? 390  PHE A CB    1 
ATOM   3034 C  CG    . PHE A 1 390 ? 1.344   -20.857 14.633  1.00 20.28 ? 390  PHE A CG    1 
ATOM   3035 C  CD1   . PHE A 1 390 ? 0.324   -21.774 14.831  1.00 20.54 ? 390  PHE A CD1   1 
ATOM   3036 C  CD2   . PHE A 1 390 ? 2.480   -20.944 15.423  1.00 21.06 ? 390  PHE A CD2   1 
ATOM   3037 C  CE1   . PHE A 1 390 ? 0.420   -22.747 15.820  1.00 22.42 ? 390  PHE A CE1   1 
ATOM   3038 C  CE2   . PHE A 1 390 ? 2.592   -21.940 16.381  1.00 22.46 ? 390  PHE A CE2   1 
ATOM   3039 C  CZ    . PHE A 1 390 ? 1.556   -22.833 16.582  1.00 21.67 ? 390  PHE A CZ    1 
ATOM   3040 N  N     . SER A 1 391 ? -1.109  -18.282 15.872  1.00 18.09 ? 391  SER A N     1 
ATOM   3041 C  CA    . SER A 1 391 ? -1.437  -17.354 16.981  1.00 18.67 ? 391  SER A CA    1 
ATOM   3042 C  C     . SER A 1 391 ? -1.656  -18.101 18.295  1.00 18.40 ? 391  SER A C     1 
ATOM   3043 O  O     . SER A 1 391 ? -2.614  -17.832 19.012  1.00 18.25 ? 391  SER A O     1 
ATOM   3044 C  CB    . SER A 1 391 ? -2.673  -16.591 16.605  1.00 21.05 ? 391  SER A CB    1 
ATOM   3045 O  OG    . SER A 1 391 ? -3.708  -17.503 16.263  1.00 21.15 ? 391  SER A OG    1 
ATOM   3046 N  N     . PRO A 1 392 ? -0.737  -19.001 18.720  1.00 18.55 ? 392  PRO A N     1 
ATOM   3047 C  CA    . PRO A 1 392 ? -0.945  -19.756 19.950  1.00 17.35 ? 392  PRO A CA    1 
ATOM   3048 C  C     . PRO A 1 392 ? -0.905  -18.903 21.232  1.00 17.56 ? 392  PRO A C     1 
ATOM   3049 O  O     . PRO A 1 392 ? -0.400  -17.799 21.237  1.00 16.93 ? 392  PRO A O     1 
ATOM   3050 C  CB    . PRO A 1 392 ? 0.213   -20.733 19.899  1.00 18.07 ? 392  PRO A CB    1 
ATOM   3051 C  CG    . PRO A 1 392 ? 1.293   -19.936 19.261  1.00 18.10 ? 392  PRO A CG    1 
ATOM   3052 C  CD    . PRO A 1 392 ? 0.587   -19.245 18.118  1.00 17.65 ? 392  PRO A CD    1 
ATOM   3053 N  N     . VAL A 1 393 ? -1.483  -19.440 22.284  1.00 16.97 ? 393  VAL A N     1 
ATOM   3054 C  CA    . VAL A 1 393 ? -1.711  -18.768 23.598  1.00 18.72 ? 393  VAL A CA    1 
ATOM   3055 C  C     . VAL A 1 393 ? -0.543  -19.129 24.512  1.00 17.80 ? 393  VAL A C     1 
ATOM   3056 O  O     . VAL A 1 393 ? -0.147  -20.312 24.512  1.00 17.35 ? 393  VAL A O     1 
ATOM   3057 C  CB    . VAL A 1 393 ? -3.015  -19.249 24.247  1.00 20.81 ? 393  VAL A CB    1 
ATOM   3058 C  CG1   . VAL A 1 393 ? -3.298  -18.502 25.544  1.00 23.48 ? 393  VAL A CG1   1 
ATOM   3059 C  CG2   . VAL A 1 393 ? -4.183  -19.139 23.286  1.00 21.20 ? 393  VAL A CG2   1 
ATOM   3060 N  N     . SER A 1 394 ? -0.047  -18.154 25.268  1.00 16.34 ? 394  SER A N     1 
ATOM   3061 C  CA    . SER A 1 394 ? 1.029   -18.349 26.272  1.00 17.54 ? 394  SER A CA    1 
ATOM   3062 C  C     . SER A 1 394 ? 0.756   -17.409 27.434  1.00 19.67 ? 394  SER A C     1 
ATOM   3063 O  O     . SER A 1 394 ? -0.062  -16.481 27.305  1.00 18.53 ? 394  SER A O     1 
ATOM   3064 C  CB    . SER A 1 394 ? 2.392   -18.075 25.673  1.00 16.96 ? 394  SER A CB    1 
ATOM   3065 O  OG    . SER A 1 394 ? 2.425   -16.778 25.079  1.00 17.27 ? 394  SER A OG    1 
ATOM   3066 N  N     . PRO A 1 395 ? 1.446   -17.605 28.580  1.00 19.35 ? 395  PRO A N     1 
ATOM   3067 C  CA    . PRO A 1 395 ? 1.347   -16.678 29.699  1.00 21.29 ? 395  PRO A CA    1 
ATOM   3068 C  C     . PRO A 1 395 ? 1.962   -15.328 29.317  1.00 20.43 ? 395  PRO A C     1 
ATOM   3069 O  O     . PRO A 1 395 ? 2.854   -15.327 28.498  1.00 21.36 ? 395  PRO A O     1 
ATOM   3070 C  CB    . PRO A 1 395 ? 2.144   -17.362 30.825  1.00 20.83 ? 395  PRO A CB    1 
ATOM   3071 C  CG    . PRO A 1 395 ? 2.183   -18.810 30.414  1.00 22.02 ? 395  PRO A CG    1 
ATOM   3072 C  CD    . PRO A 1 395 ? 2.302   -18.746 28.899  1.00 21.84 ? 395  PRO A CD    1 
ATOM   3073 N  N     . ILE A 1 396 ? 1.512   -14.231 29.935  1.00 21.27 ? 396  ILE A N     1 
ATOM   3074 C  CA    . ILE A 1 396 ? 2.089   -12.871 29.697  1.00 19.91 ? 396  ILE A CA    1 
ATOM   3075 C  C     . ILE A 1 396 ? 3.386   -12.740 30.531  1.00 20.26 ? 396  ILE A C     1 
ATOM   3076 O  O     . ILE A 1 396 ? 3.353   -12.139 31.625  1.00 19.51 ? 396  ILE A O     1 
ATOM   3077 C  CB    . ILE A 1 396 ? 1.097   -11.726 30.004  1.00 19.68 ? 396  ILE A CB    1 
ATOM   3078 C  CG1   . ILE A 1 396 ? -0.325  -12.010 29.514  1.00 20.18 ? 396  ILE A CG1   1 
ATOM   3079 C  CG2   . ILE A 1 396 ? 1.633   -10.392 29.439  1.00 19.46 ? 396  ILE A CG2   1 
ATOM   3080 C  CD1   . ILE A 1 396 ? -1.361  -11.085 30.129  1.00 20.43 ? 396  ILE A CD1   1 
ATOM   3081 N  N     . THR A 1 397 ? 4.496   -13.291 30.053  1.00 19.24 ? 397  THR A N     1 
ATOM   3082 C  CA    . THR A 1 397 ? 5.834   -13.078 30.659  1.00 19.20 ? 397  THR A CA    1 
ATOM   3083 C  C     . THR A 1 397 ? 6.795   -12.693 29.529  1.00 19.70 ? 397  THR A C     1 
ATOM   3084 O  O     . THR A 1 397 ? 6.598   -13.171 28.362  1.00 20.30 ? 397  THR A O     1 
ATOM   3085 C  CB    . THR A 1 397 ? 6.349   -14.306 31.434  1.00 18.64 ? 397  THR A CB    1 
ATOM   3086 O  OG1   . THR A 1 397 ? 6.784   -15.296 30.495  1.00 18.32 ? 397  THR A OG1   1 
ATOM   3087 C  CG2   . THR A 1 397 ? 5.321   -14.886 32.374  1.00 19.14 ? 397  THR A CG2   1 
ATOM   3088 N  N     . GLY A 1 398 ? 7.808   -11.910 29.878  1.00 19.02 ? 398  GLY A N     1 
ATOM   3089 C  CA    . GLY A 1 398 ? 8.979   -11.636 29.036  1.00 20.82 ? 398  GLY A CA    1 
ATOM   3090 C  C     . GLY A 1 398 ? 9.613   -12.916 28.530  1.00 22.84 ? 398  GLY A C     1 
ATOM   3091 O  O     . GLY A 1 398 ? 9.914   -12.987 27.319  1.00 22.01 ? 398  GLY A O     1 
ATOM   3092 N  N     . LYS A 1 399 ? 9.830   -13.896 29.414  1.00 26.19 ? 399  LYS A N     1 
ATOM   3093 C  CA    . LYS A 1 399 ? 10.500  -15.176 29.048  1.00 27.83 ? 399  LYS A CA    1 
ATOM   3094 C  C     . LYS A 1 399 ? 9.712   -15.854 27.906  1.00 26.14 ? 399  LYS A C     1 
ATOM   3095 O  O     . LYS A 1 399 ? 10.331  -16.295 26.929  1.00 23.70 ? 399  LYS A O     1 
ATOM   3096 C  CB    . LYS A 1 399 ? 10.660  -16.065 30.283  1.00 33.04 ? 399  LYS A CB    1 
ATOM   3097 C  CG    . LYS A 1 399 ? 11.036  -17.514 29.979  1.00 45.49 ? 399  LYS A CG    1 
ATOM   3098 C  CD    . LYS A 1 399 ? 10.908  -18.501 31.160  1.00 55.07 ? 399  LYS A CD    1 
ATOM   3099 C  CE    . LYS A 1 399 ? 9.475   -18.909 31.479  1.00 62.21 ? 399  LYS A CE    1 
ATOM   3100 N  NZ    . LYS A 1 399 ? 8.905   -19.791 30.430  1.00 64.76 ? 399  LYS A NZ    1 
ATOM   3101 N  N     . ASP A 1 400 ? 8.390   -15.957 28.032  1.00 25.33 ? 400  ASP A N     1 
ATOM   3102 C  CA    . ASP A 1 400 ? 7.527   -16.601 27.006  1.00 23.68 ? 400  ASP A CA    1 
ATOM   3103 C  C     . ASP A 1 400 ? 7.594   -15.795 25.708  1.00 22.81 ? 400  ASP A C     1 
ATOM   3104 O  O     . ASP A 1 400 ? 7.649   -16.407 24.648  1.00 21.68 ? 400  ASP A O     1 
ATOM   3105 C  CB    . ASP A 1 400 ? 6.109   -16.736 27.537  1.00 24.53 ? 400  ASP A CB    1 
ATOM   3106 C  CG    . ASP A 1 400 ? 5.985   -17.834 28.580  1.00 25.27 ? 400  ASP A CG    1 
ATOM   3107 O  OD1   . ASP A 1 400 ? 6.171   -18.990 28.217  1.00 25.26 ? 400  ASP A OD1   1 
ATOM   3108 O  OD2   . ASP A 1 400 ? 5.682   -17.515 29.740  1.00 27.03 ? 400  ASP A OD2   1 
ATOM   3109 N  N     . ALA A 1 401 ? 7.623   -14.458 25.787  1.00 21.81 ? 401  ALA A N     1 
ATOM   3110 C  CA    . ALA A 1 401 ? 7.560   -13.580 24.598  1.00 21.19 ? 401  ALA A CA    1 
ATOM   3111 C  C     . ALA A 1 401 ? 8.866   -13.699 23.813  1.00 22.56 ? 401  ALA A C     1 
ATOM   3112 O  O     . ALA A 1 401 ? 8.826   -13.825 22.569  1.00 21.61 ? 401  ALA A O     1 
ATOM   3113 C  CB    . ALA A 1 401 ? 7.285   -12.145 25.012  1.00 21.79 ? 401  ALA A CB    1 
ATOM   3114 N  N     . ILE A 1 402 ? 9.995   -13.602 24.503  1.00 20.81 ? 402  ILE A N     1 
ATOM   3115 C  CA    . ILE A 1 402 ? 11.313  -13.612 23.820  1.00 23.60 ? 402  ILE A CA    1 
ATOM   3116 C  C     . ILE A 1 402 ? 11.558  -15.032 23.315  1.00 22.34 ? 402  ILE A C     1 
ATOM   3117 O  O     . ILE A 1 402 ? 12.050  -15.163 22.202  1.00 22.91 ? 402  ILE A O     1 
ATOM   3118 C  CB    . ILE A 1 402 ? 12.463  -13.054 24.697  1.00 24.76 ? 402  ILE A CB    1 
ATOM   3119 C  CG1   . ILE A 1 402 ? 13.682  -12.755 23.828  1.00 25.74 ? 402  ILE A CG1   1 
ATOM   3120 C  CG2   . ILE A 1 402 ? 12.819  -13.958 25.862  1.00 23.54 ? 402  ILE A CG2   1 
ATOM   3121 C  CD1   . ILE A 1 402 ? 13.648  -11.405 23.242  1.00 29.17 ? 402  ILE A CD1   1 
ATOM   3122 N  N     . LYS A 1 403 ? 11.185  -16.061 24.070  1.00 23.10 ? 403  LYS A N     1 
ATOM   3123 C  CA    . LYS A 1 403 ? 11.364  -17.450 23.579  1.00 23.19 ? 403  LYS A CA    1 
ATOM   3124 C  C     . LYS A 1 403 ? 10.655  -17.628 22.213  1.00 21.94 ? 403  LYS A C     1 
ATOM   3125 O  O     . LYS A 1 403 ? 11.216  -18.262 21.288  1.00 19.22 ? 403  LYS A O     1 
ATOM   3126 C  CB    . LYS A 1 403 ? 10.818  -18.456 24.589  1.00 25.23 ? 403  LYS A CB    1 
ATOM   3127 C  CG    . LYS A 1 403 ? 11.155  -19.903 24.232  1.00 28.69 ? 403  LYS A CG    1 
ATOM   3128 C  CD    . LYS A 1 403 ? 10.231  -20.894 24.818  1.00 31.77 ? 403  LYS A CD    1 
ATOM   3129 C  CE    . LYS A 1 403 ? 10.191  -20.918 26.333  1.00 34.26 ? 403  LYS A CE    1 
ATOM   3130 N  NZ    . LYS A 1 403 ? 9.099   -21.820 26.784  1.00 34.98 ? 403  LYS A NZ    1 
ATOM   3131 N  N     . GLN A 1 404 ? 9.426   -17.145 22.086  1.00 21.66 ? 404  GLN A N     1 
ATOM   3132 C  CA    . GLN A 1 404 ? 8.615   -17.356 20.855  1.00 20.16 ? 404  GLN A CA    1 
ATOM   3133 C  C     . GLN A 1 404 ? 9.224   -16.524 19.733  1.00 19.59 ? 404  GLN A C     1 
ATOM   3134 O  O     . GLN A 1 404 ? 9.406   -17.084 18.653  1.00 17.45 ? 404  GLN A O     1 
ATOM   3135 C  CB    . GLN A 1 404 ? 7.140   -17.098 21.130  1.00 19.64 ? 404  GLN A CB    1 
ATOM   3136 C  CG    . GLN A 1 404 ? 6.533   -18.192 21.998  1.00 19.93 ? 404  GLN A CG    1 
ATOM   3137 C  CD    . GLN A 1 404 ? 5.132   -17.868 22.443  1.00 20.54 ? 404  GLN A CD    1 
ATOM   3138 O  OE1   . GLN A 1 404 ? 4.153   -18.203 21.785  1.00 20.07 ? 404  GLN A OE1   1 
ATOM   3139 N  NE2   . GLN A 1 404 ? 5.032   -17.151 23.552  1.00 22.08 ? 404  GLN A NE2   1 
ATOM   3140 N  N     . TYR A 1 405 ? 9.577   -15.264 19.980  1.00 19.49 ? 405  TYR A N     1 
ATOM   3141 C  CA    . TYR A 1 405 ? 10.241  -14.414 18.955  1.00 21.84 ? 405  TYR A CA    1 
ATOM   3142 C  C     . TYR A 1 405 ? 11.482  -15.163 18.422  1.00 23.94 ? 405  TYR A C     1 
ATOM   3143 O  O     . TYR A 1 405 ? 11.641  -15.311 17.186  1.00 23.39 ? 405  TYR A O     1 
ATOM   3144 C  CB    . TYR A 1 405 ? 10.573  -13.027 19.515  1.00 22.37 ? 405  TYR A CB    1 
ATOM   3145 C  CG    . TYR A 1 405 ? 11.579  -12.294 18.666  1.00 23.97 ? 405  TYR A CG    1 
ATOM   3146 C  CD1   . TYR A 1 405 ? 11.261  -11.889 17.377  1.00 26.08 ? 405  TYR A CD1   1 
ATOM   3147 C  CD2   . TYR A 1 405 ? 12.876  -12.115 19.094  1.00 25.42 ? 405  TYR A CD2   1 
ATOM   3148 C  CE1   . TYR A 1 405 ? 12.185  -11.268 16.558  1.00 26.94 ? 405  TYR A CE1   1 
ATOM   3149 C  CE2   . TYR A 1 405 ? 13.817  -11.494 18.291  1.00 26.52 ? 405  TYR A CE2   1 
ATOM   3150 C  CZ    . TYR A 1 405 ? 13.476  -11.074 17.020  1.00 29.85 ? 405  TYR A CZ    1 
ATOM   3151 O  OH    . TYR A 1 405 ? 14.418  -10.444 16.247  1.00 36.29 ? 405  TYR A OH    1 
ATOM   3152 N  N     . ASN A 1 406 ? 12.312  -15.700 19.324  1.00 23.65 ? 406  ASN A N     1 
ATOM   3153 C  CA    . ASN A 1 406 ? 13.576  -16.400 18.953  1.00 26.84 ? 406  ASN A CA    1 
ATOM   3154 C  C     . ASN A 1 406 ? 13.239  -17.671 18.153  1.00 26.49 ? 406  ASN A C     1 
ATOM   3155 O  O     . ASN A 1 406 ? 13.787  -17.824 17.071  1.00 28.85 ? 406  ASN A O     1 
ATOM   3156 C  CB    . ASN A 1 406 ? 14.460  -16.693 20.179  1.00 25.14 ? 406  ASN A CB    1 
ATOM   3157 C  CG    . ASN A 1 406 ? 15.134  -15.461 20.754  1.00 25.29 ? 406  ASN A CG    1 
ATOM   3158 O  OD1   . ASN A 1 406 ? 15.433  -14.527 20.040  1.00 27.99 ? 406  ASN A OD1   1 
ATOM   3159 N  ND2   . ASN A 1 406 ? 15.438  -15.466 22.035  1.00 25.86 ? 406  ASN A ND2   1 
ATOM   3160 N  N     . MET A 1 407 ? 12.345  -18.523 18.650  1.00 23.98 ? 407  MET A N     1 
ATOM   3161 C  CA    . MET A 1 407 ? 11.962  -19.797 17.981  1.00 28.01 ? 407  MET A CA    1 
ATOM   3162 C  C     . MET A 1 407 ? 11.434  -19.522 16.567  1.00 26.40 ? 407  MET A C     1 
ATOM   3163 O  O     . MET A 1 407 ? 11.634  -20.334 15.677  1.00 26.21 ? 407  MET A O     1 
ATOM   3164 C  CB    . MET A 1 407 ? 10.782  -20.485 18.667  1.00 27.22 ? 407  MET A CB    1 
ATOM   3165 C  CG    . MET A 1 407 ? 11.050  -21.026 19.979  1.00 33.60 ? 407  MET A CG    1 
ATOM   3166 S  SD    . MET A 1 407 ? 9.439   -21.391 20.730  1.00 30.38 ? 407  MET A SD    1 
ATOM   3167 C  CE    . MET A 1 407 ? 9.247   -23.086 20.191  1.00 30.13 ? 407  MET A CE    1 
ATOM   3168 N  N     . VAL A 1 408 ? 10.566  -18.533 16.446  1.00 25.91 ? 408  VAL A N     1 
ATOM   3169 C  CA    . VAL A 1 408 ? 9.753   -18.374 15.210  1.00 26.37 ? 408  VAL A CA    1 
ATOM   3170 C  C     . VAL A 1 408 ? 10.568  -17.643 14.143  1.00 26.24 ? 408  VAL A C     1 
ATOM   3171 O  O     . VAL A 1 408 ? 10.576  -18.148 12.991  1.00 25.39 ? 408  VAL A O     1 
ATOM   3172 C  CB    . VAL A 1 408 ? 8.405   -17.706 15.494  1.00 26.14 ? 408  VAL A CB    1 
ATOM   3173 C  CG1   . VAL A 1 408 ? 7.711   -17.322 14.189  1.00 26.84 ? 408  VAL A CG1   1 
ATOM   3174 C  CG2   . VAL A 1 408 ? 7.561   -18.629 16.369  1.00 24.56 ? 408  VAL A CG2   1 
ATOM   3175 N  N     . SER A 1 409 ? 11.183  -16.500 14.474  1.00 26.26 ? 409  SER A N     1 
ATOM   3176 C  CA    . SER A 1 409 ? 11.919  -15.688 13.468  1.00 26.83 ? 409  SER A CA    1 
ATOM   3177 C  C     . SER A 1 409 ? 13.023  -16.552 12.829  1.00 28.34 ? 409  SER A C     1 
ATOM   3178 O  O     . SER A 1 409 ? 13.186  -16.531 11.601  1.00 28.34 ? 409  SER A O     1 
ATOM   3179 C  CB    . SER A 1 409 ? 12.465  -14.429 14.059  1.00 27.05 ? 409  SER A CB    1 
ATOM   3180 O  OG    . SER A 1 409 ? 13.271  -14.744 15.159  1.00 29.49 ? 409  SER A OG    1 
ATOM   3181 N  N     . SER A 1 410 ? 13.715  -17.340 13.641  1.00 27.78 ? 410  SER A N     1 
ATOM   3182 C  CA    . SER A 1 410 ? 14.719  -18.352 13.226  1.00 28.33 ? 410  SER A CA    1 
ATOM   3183 C  C     . SER A 1 410 ? 14.137  -19.265 12.127  1.00 27.28 ? 410  SER A C     1 
ATOM   3184 O  O     . SER A 1 410 ? 14.734  -19.351 11.025  1.00 26.43 ? 410  SER A O     1 
ATOM   3185 C  CB    . SER A 1 410 ? 15.143  -19.132 14.448  1.00 26.74 ? 410  SER A CB    1 
ATOM   3186 O  OG    . SER A 1 410 ? 16.040  -20.133 14.087  1.00 35.45 ? 410  SER A OG    1 
ATOM   3187 N  N     . ARG A 1 411 ? 13.016  -19.930 12.415  1.00 25.70 ? 411  ARG A N     1 
ATOM   3188 C  CA    . ARG A 1 411 ? 12.389  -20.932 11.510  1.00 25.50 ? 411  ARG A CA    1 
ATOM   3189 C  C     . ARG A 1 411 ? 11.889  -20.266 10.225  1.00 25.22 ? 411  ARG A C     1 
ATOM   3190 O  O     . ARG A 1 411 ? 12.059  -20.845 9.138   1.00 23.05 ? 411  ARG A O     1 
ATOM   3191 C  CB    . ARG A 1 411 ? 11.220  -21.642 12.196  1.00 25.20 ? 411  ARG A CB    1 
ATOM   3192 C  CG    . ARG A 1 411 ? 11.668  -22.648 13.246  1.00 25.83 ? 411  ARG A CG    1 
ATOM   3193 C  CD    . ARG A 1 411 ? 12.581  -23.706 12.663  1.00 25.19 ? 411  ARG A CD    1 
ATOM   3194 N  NE    . ARG A 1 411 ? 12.930  -24.694 13.669  1.00 27.29 ? 411  ARG A NE    1 
ATOM   3195 C  CZ    . ARG A 1 411 ? 13.918  -25.576 13.556  1.00 27.81 ? 411  ARG A CZ    1 
ATOM   3196 N  NH1   . ARG A 1 411 ? 14.664  -25.640 12.463  1.00 28.79 ? 411  ARG A NH1   1 
ATOM   3197 N  NH2   . ARG A 1 411 ? 14.169  -26.393 14.554  1.00 26.88 ? 411  ARG A NH2   1 
ATOM   3198 N  N     . VAL A 1 412 ? 11.233  -19.122 10.361  1.00 24.92 ? 412  VAL A N     1 
ATOM   3199 C  CA    . VAL A 1 412 ? 10.563  -18.438 9.221   1.00 25.66 ? 412  VAL A CA    1 
ATOM   3200 C  C     . VAL A 1 412 ? 11.666  -18.021 8.242   1.00 23.77 ? 412  VAL A C     1 
ATOM   3201 O  O     . VAL A 1 412 ? 11.531  -18.291 7.042   1.00 23.05 ? 412  VAL A O     1 
ATOM   3202 C  CB    . VAL A 1 412 ? 9.682   -17.274 9.727   1.00 28.03 ? 412  VAL A CB    1 
ATOM   3203 C  CG1   . VAL A 1 412 ? 9.340   -16.292 8.630   1.00 32.16 ? 412  VAL A CG1   1 
ATOM   3204 C  CG2   . VAL A 1 412 ? 8.403   -17.793 10.392  1.00 25.34 ? 412  VAL A CG2   1 
ATOM   3205 N  N     . ARG A 1 413 ? 12.758  -17.463 8.755   1.00 25.63 ? 413  ARG A N     1 
ATOM   3206 C  CA    . ARG A 1 413 ? 13.901  -16.980 7.928   1.00 27.38 ? 413  ARG A CA    1 
ATOM   3207 C  C     . ARG A 1 413 ? 14.627  -18.185 7.310   1.00 28.26 ? 413  ARG A C     1 
ATOM   3208 O  O     . ARG A 1 413 ? 15.039  -18.070 6.160   1.00 30.51 ? 413  ARG A O     1 
ATOM   3209 C  CB    . ARG A 1 413 ? 14.794  -16.056 8.762   1.00 28.19 ? 413  ARG A CB    1 
ATOM   3210 C  CG    . ARG A 1 413 ? 14.111  -14.726 9.054   1.00 31.21 ? 413  ARG A CG    1 
ATOM   3211 C  CD    . ARG A 1 413 ? 14.834  -13.842 10.056  1.00 34.41 ? 413  ARG A CD    1 
ATOM   3212 N  NE    . ARG A 1 413 ? 16.198  -13.584 9.604   1.00 38.33 ? 413  ARG A NE    1 
ATOM   3213 C  CZ    . ARG A 1 413 ? 16.594  -12.558 8.850   1.00 42.11 ? 413  ARG A CZ    1 
ATOM   3214 N  NH1   . ARG A 1 413 ? 15.742  -11.647 8.404   1.00 46.83 ? 413  ARG A NH1   1 
ATOM   3215 N  NH2   . ARG A 1 413 ? 17.867  -12.452 8.526   1.00 43.18 ? 413  ARG A NH2   1 
ATOM   3216 N  N     . GLU A 1 414 ? 14.670  -19.320 8.009   1.00 28.37 ? 414  GLU A N     1 
ATOM   3217 C  CA    . GLU A 1 414 ? 15.229  -20.592 7.495   1.00 29.33 ? 414  GLU A CA    1 
ATOM   3218 C  C     . GLU A 1 414 ? 14.507  -21.007 6.203   1.00 28.55 ? 414  GLU A C     1 
ATOM   3219 O  O     . GLU A 1 414 ? 15.143  -21.677 5.334   1.00 26.36 ? 414  GLU A O     1 
ATOM   3220 C  CB    . GLU A 1 414 ? 15.146  -21.673 8.574   1.00 30.40 ? 414  GLU A CB    1 
ATOM   3221 C  CG    . GLU A 1 414 ? 15.515  -23.041 8.061   1.00 31.32 ? 414  GLU A CG    1 
ATOM   3222 C  CD    . GLU A 1 414 ? 15.457  -24.160 9.069   1.00 33.30 ? 414  GLU A CD    1 
ATOM   3223 O  OE1   . GLU A 1 414 ? 15.113  -23.871 10.217  1.00 33.33 ? 414  GLU A OE1   1 
ATOM   3224 O  OE2   . GLU A 1 414 ? 15.713  -25.332 8.670   1.00 35.82 ? 414  GLU A OE2   1 
ATOM   3225 N  N     . TYR A 1 415 ? 13.236  -20.632 6.044   1.00 26.24 ? 415  TYR A N     1 
ATOM   3226 C  CA    . TYR A 1 415 ? 12.416  -21.074 4.889   1.00 25.21 ? 415  TYR A CA    1 
ATOM   3227 C  C     . TYR A 1 415 ? 12.268  -19.939 3.875   1.00 27.48 ? 415  TYR A C     1 
ATOM   3228 O  O     . TYR A 1 415 ? 11.448  -20.117 2.954   1.00 28.25 ? 415  TYR A O     1 
ATOM   3229 C  CB    . TYR A 1 415 ? 11.093  -21.659 5.376   1.00 23.12 ? 415  TYR A CB    1 
ATOM   3230 C  CG    . TYR A 1 415 ? 11.239  -23.085 5.805   1.00 22.81 ? 415  TYR A CG    1 
ATOM   3231 C  CD1   . TYR A 1 415 ? 11.755  -23.380 7.051   1.00 21.99 ? 415  TYR A CD1   1 
ATOM   3232 C  CD2   . TYR A 1 415 ? 10.930  -24.140 4.950   1.00 22.11 ? 415  TYR A CD2   1 
ATOM   3233 C  CE1   . TYR A 1 415 ? 11.962  -24.685 7.446   1.00 21.20 ? 415  TYR A CE1   1 
ATOM   3234 C  CE2   . TYR A 1 415 ? 11.083  -25.453 5.357   1.00 22.02 ? 415  TYR A CE2   1 
ATOM   3235 C  CZ    . TYR A 1 415 ? 11.627  -25.717 6.598   1.00 21.16 ? 415  TYR A CZ    1 
ATOM   3236 O  OH    . TYR A 1 415 ? 11.809  -26.990 7.024   1.00 23.25 ? 415  TYR A OH    1 
ATOM   3237 N  N     . GLY A 1 416 ? 13.010  -18.831 4.032   1.00 28.48 ? 416  GLY A N     1 
ATOM   3238 C  CA    . GLY A 1 416 ? 13.100  -17.767 3.008   1.00 30.48 ? 416  GLY A CA    1 
ATOM   3239 C  C     . GLY A 1 416 ? 12.073  -16.634 3.154   1.00 31.82 ? 416  GLY A C     1 
ATOM   3240 O  O     . GLY A 1 416 ? 12.011  -15.810 2.238   1.00 34.86 ? 416  GLY A O     1 
ATOM   3241 N  N     . PHE A 1 417 ? 11.339  -16.541 4.266   1.00 28.08 ? 417  PHE A N     1 
ATOM   3242 C  CA    . PHE A 1 417 ? 10.243  -15.553 4.484   1.00 26.60 ? 417  PHE A CA    1 
ATOM   3243 C  C     . PHE A 1 417 ? 10.722  -14.487 5.475   1.00 26.18 ? 417  PHE A C     1 
ATOM   3244 O  O     . PHE A 1 417 ? 11.488  -14.886 6.402   1.00 25.85 ? 417  PHE A O     1 
ATOM   3245 C  CB    . PHE A 1 417 ? 9.001   -16.278 5.014   1.00 26.63 ? 417  PHE A CB    1 
ATOM   3246 C  CG    . PHE A 1 417 ? 8.435   -17.375 4.146   1.00 25.25 ? 417  PHE A CG    1 
ATOM   3247 C  CD1   . PHE A 1 417 ? 7.797   -17.080 2.952   1.00 25.26 ? 417  PHE A CD1   1 
ATOM   3248 C  CD2   . PHE A 1 417 ? 8.501   -18.704 4.548   1.00 25.49 ? 417  PHE A CD2   1 
ATOM   3249 C  CE1   . PHE A 1 417 ? 7.299   -18.097 2.155   1.00 23.82 ? 417  PHE A CE1   1 
ATOM   3250 C  CE2   . PHE A 1 417 ? 7.978   -19.720 3.764   1.00 25.10 ? 417  PHE A CE2   1 
ATOM   3251 C  CZ    . PHE A 1 417 ? 7.375   -19.413 2.567   1.00 25.35 ? 417  PHE A CZ    1 
ATOM   3252 N  N     . ASP A 1 418 ? 10.347  -13.205 5.323   1.00 25.64 ? 418  ASP A N     1 
ATOM   3253 C  CA    . ASP A 1 418 ? 10.696  -12.186 6.364   1.00 26.92 ? 418  ASP A CA    1 
ATOM   3254 C  C     . ASP A 1 418 ? 9.829   -12.547 7.586   1.00 24.74 ? 418  ASP A C     1 
ATOM   3255 O  O     . ASP A 1 418 ? 8.708   -13.084 7.425   1.00 25.01 ? 418  ASP A O     1 
ATOM   3256 C  CB    . ASP A 1 418 ? 10.616  -10.680 5.972   1.00 28.41 ? 418  ASP A CB    1 
ATOM   3257 C  CG    . ASP A 1 418 ? 11.726  -9.970  5.137   1.00 28.24 ? 418  ASP A CG    1 
ATOM   3258 O  OD1   . ASP A 1 418 ? 11.641  -10.182 3.923   1.00 40.14 ? 418  ASP A OD1   1 
ATOM   3259 O  OD2   . ASP A 1 418 ? 12.549  -9.047  5.619   1.00 15.84 ? 418  ASP A OD2   1 
ATOM   3260 N  N     . TYR A 1 419 ? 10.408  -12.414 8.771   1.00 23.40 ? 419  TYR A N     1 
ATOM   3261 C  CA    . TYR A 1 419 ? 9.710   -12.501 10.059  1.00 23.25 ? 419  TYR A CA    1 
ATOM   3262 C  C     . TYR A 1 419 ? 8.821   -11.276 10.156  1.00 23.34 ? 419  TYR A C     1 
ATOM   3263 O  O     . TYR A 1 419 ? 9.298   -10.133 9.985   1.00 23.12 ? 419  TYR A O     1 
ATOM   3264 C  CB    . TYR A 1 419 ? 10.679  -12.531 11.237  1.00 24.99 ? 419  TYR A CB    1 
ATOM   3265 C  CG    . TYR A 1 419 ? 9.970   -12.421 12.556  1.00 25.67 ? 419  TYR A CG    1 
ATOM   3266 C  CD1   . TYR A 1 419 ? 9.157   -13.440 13.023  1.00 24.23 ? 419  TYR A CD1   1 
ATOM   3267 C  CD2   . TYR A 1 419 ? 10.057  -11.267 13.301  1.00 26.22 ? 419  TYR A CD2   1 
ATOM   3268 C  CE1   . TYR A 1 419 ? 8.510   -13.335 14.240  1.00 25.02 ? 419  TYR A CE1   1 
ATOM   3269 C  CE2   . TYR A 1 419 ? 9.403   -11.143 14.512  1.00 26.57 ? 419  TYR A CE2   1 
ATOM   3270 C  CZ    . TYR A 1 419 ? 8.617   -12.175 14.981  1.00 25.55 ? 419  TYR A CZ    1 
ATOM   3271 O  OH    . TYR A 1 419 ? 7.980   -12.031 16.181  1.00 25.72 ? 419  TYR A OH    1 
ATOM   3272 N  N     . MET A 1 420 ? 7.543   -11.539 10.343  1.00 22.43 ? 420  MET A N     1 
ATOM   3273 C  CA    . MET A 1 420 ? 6.515   -10.540 10.670  1.00 24.83 ? 420  MET A CA    1 
ATOM   3274 C  C     . MET A 1 420 ? 5.751   -11.135 11.846  1.00 24.97 ? 420  MET A C     1 
ATOM   3275 O  O     . MET A 1 420 ? 5.158   -12.211 11.689  1.00 25.44 ? 420  MET A O     1 
ATOM   3276 C  CB    . MET A 1 420 ? 5.561   -10.303 9.501   1.00 25.54 ? 420  MET A CB    1 
ATOM   3277 C  CG    . MET A 1 420 ? 6.188   -9.637  8.297   1.00 28.03 ? 420  MET A CG    1 
ATOM   3278 S  SD    . MET A 1 420 ? 5.062   -9.782  6.871   1.00 28.81 ? 420  MET A SD    1 
ATOM   3279 C  CE    . MET A 1 420 ? 5.845   -8.727  5.654   1.00 30.54 ? 420  MET A CE    1 
ATOM   3280 N  N     . GLY A 1 421 ? 5.861   -10.499 12.996  1.00 23.80 ? 421  GLY A N     1 
ATOM   3281 C  CA    . GLY A 1 421 ? 5.331   -11.035 14.249  1.00 23.65 ? 421  GLY A CA    1 
ATOM   3282 C  C     . GLY A 1 421 ? 4.673   -9.938  15.041  1.00 22.05 ? 421  GLY A C     1 
ATOM   3283 O  O     . GLY A 1 421 ? 5.003   -8.765  14.832  1.00 21.43 ? 421  GLY A O     1 
ATOM   3284 N  N     . LEU A 1 422 ? 3.760   -10.315 15.917  1.00 21.93 ? 422  LEU A N     1 
ATOM   3285 C  CA    . LEU A 1 422 ? 3.322   -9.394  16.976  1.00 23.23 ? 422  LEU A CA    1 
ATOM   3286 C  C     . LEU A 1 422 ? 3.067   -10.188 18.253  1.00 23.32 ? 422  LEU A C     1 
ATOM   3287 O  O     . LEU A 1 422 ? 2.874   -11.445 18.192  1.00 20.37 ? 422  LEU A O     1 
ATOM   3288 C  CB    . LEU A 1 422 ? 2.099   -8.631  16.461  1.00 25.37 ? 422  LEU A CB    1 
ATOM   3289 C  CG    . LEU A 1 422 ? 0.887   -9.470  16.089  1.00 25.20 ? 422  LEU A CG    1 
ATOM   3290 C  CD1   . LEU A 1 422 ? 0.130   -9.855  17.340  1.00 25.55 ? 422  LEU A CD1   1 
ATOM   3291 C  CD2   . LEU A 1 422 ? -0.039  -8.712  15.134  1.00 27.89 ? 422  LEU A CD2   1 
ATOM   3292 N  N     . LEU A 1 423 ? 3.207   -9.490  19.373  1.00 23.51 ? 423  LEU A N     1 
ATOM   3293 C  CA    . LEU A 1 423 ? 2.807   -9.963  20.724  1.00 23.46 ? 423  LEU A CA    1 
ATOM   3294 C  C     . LEU A 1 423 ? 1.496   -9.234  21.003  1.00 23.72 ? 423  LEU A C     1 
ATOM   3295 O  O     . LEU A 1 423 ? 1.519   -7.978  20.958  1.00 24.84 ? 423  LEU A O     1 
ATOM   3296 C  CB    . LEU A 1 423 ? 3.890   -9.616  21.754  1.00 22.17 ? 423  LEU A CB    1 
ATOM   3297 C  CG    . LEU A 1 423 ? 5.171   -10.446 21.739  1.00 24.00 ? 423  LEU A CG    1 
ATOM   3298 C  CD1   . LEU A 1 423 ? 4.921   -11.931 22.019  1.00 24.93 ? 423  LEU A CD1   1 
ATOM   3299 C  CD2   . LEU A 1 423 ? 5.932   -10.290 20.436  1.00 25.05 ? 423  LEU A CD2   1 
ATOM   3300 N  N     . ALA A 1 424 ? 0.396   -9.981  21.133  1.00 23.68 ? 424  ALA A N     1 
ATOM   3301 C  CA    . ALA A 1 424 ? -0.984  -9.482  21.392  1.00 21.29 ? 424  ALA A CA    1 
ATOM   3302 C  C     . ALA A 1 424 ? -1.429  -9.950  22.785  1.00 21.01 ? 424  ALA A C     1 
ATOM   3303 O  O     . ALA A 1 424 ? -1.129  -11.070 23.136  1.00 19.04 ? 424  ALA A O     1 
ATOM   3304 C  CB    . ALA A 1 424 ? -1.941  -9.973  20.325  1.00 19.82 ? 424  ALA A CB    1 
ATOM   3305 N  N     . ILE A 1 425 ? -2.137  -9.101  23.530  1.00 21.80 ? 425  ILE A N     1 
ATOM   3306 C  CA    . ILE A 1 425 ? -2.727  -9.419  24.863  1.00 22.66 ? 425  ILE A CA    1 
ATOM   3307 C  C     . ILE A 1 425 ? -4.189  -8.996  24.832  1.00 21.33 ? 425  ILE A C     1 
ATOM   3308 O  O     . ILE A 1 425 ? -4.469  -7.794  24.581  1.00 20.15 ? 425  ILE A O     1 
ATOM   3309 C  CB    . ILE A 1 425 ? -1.976  -8.732  26.025  1.00 23.41 ? 425  ILE A CB    1 
ATOM   3310 C  CG1   . ILE A 1 425 ? -0.498  -9.121  26.064  1.00 22.75 ? 425  ILE A CG1   1 
ATOM   3311 C  CG2   . ILE A 1 425 ? -2.654  -9.024  27.352  1.00 23.46 ? 425  ILE A CG2   1 
ATOM   3312 C  CD1   . ILE A 1 425 ? 0.382   -8.117  26.736  1.00 23.02 ? 425  ILE A CD1   1 
ATOM   3313 N  N     . GLY A 1 426 ? -5.074  -9.951  25.090  1.00 21.91 ? 426  GLY A N     1 
ATOM   3314 C  CA    . GLY A 1 426 ? -6.533  -9.747  25.166  1.00 22.04 ? 426  GLY A CA    1 
ATOM   3315 C  C     . GLY A 1 426 ? -6.857  -9.202  26.537  1.00 21.87 ? 426  GLY A C     1 
ATOM   3316 O  O     . GLY A 1 426 ? -7.302  -8.033  26.638  1.00 23.01 ? 426  GLY A O     1 
ATOM   3317 N  N     . TRP A 1 427 ? -6.657  -10.031 27.551  1.00 21.32 ? 427  TRP A N     1 
ATOM   3318 C  CA    . TRP A 1 427 ? -6.819  -9.652  28.978  1.00 22.27 ? 427  TRP A CA    1 
ATOM   3319 C  C     . TRP A 1 427 ? -5.701  -10.334 29.793  1.00 21.17 ? 427  TRP A C     1 
ATOM   3320 O  O     . TRP A 1 427 ? -4.774  -9.621  30.224  1.00 20.30 ? 427  TRP A O     1 
ATOM   3321 C  CB    . TRP A 1 427 ? -8.254  -9.974  29.461  1.00 19.89 ? 427  TRP A CB    1 
ATOM   3322 C  CG    . TRP A 1 427 ? -8.619  -9.371  30.785  1.00 21.18 ? 427  TRP A CG    1 
ATOM   3323 C  CD1   . TRP A 1 427 ? -7.807  -8.612  31.584  1.00 22.38 ? 427  TRP A CD1   1 
ATOM   3324 C  CD2   . TRP A 1 427 ? -9.881  -9.457  31.482  1.00 21.33 ? 427  TRP A CD2   1 
ATOM   3325 N  NE1   . TRP A 1 427 ? -8.468  -8.240  32.724  1.00 21.07 ? 427  TRP A NE1   1 
ATOM   3326 C  CE2   . TRP A 1 427 ? -9.739  -8.737  32.695  1.00 20.84 ? 427  TRP A CE2   1 
ATOM   3327 C  CE3   . TRP A 1 427 ? -11.113 -10.071 31.219  1.00 22.11 ? 427  TRP A CE3   1 
ATOM   3328 C  CZ2   . TRP A 1 427 ? -10.767 -8.625  33.631  1.00 20.37 ? 427  TRP A CZ2   1 
ATOM   3329 C  CZ3   . TRP A 1 427 ? -12.129 -9.976  32.150  1.00 21.68 ? 427  TRP A CZ3   1 
ATOM   3330 C  CH2   . TRP A 1 427 ? -11.959 -9.242  33.333  1.00 21.29 ? 427  TRP A CH2   1 
ATOM   3331 N  N     . ARG A 1 428 ? -5.760  -11.663 29.952  1.00 19.12 ? 428  ARG A N     1 
ATOM   3332 C  CA    . ARG A 1 428 ? -4.762  -12.447 30.726  1.00 18.37 ? 428  ARG A CA    1 
ATOM   3333 C  C     . ARG A 1 428 ? -3.940  -13.331 29.787  1.00 18.28 ? 428  ARG A C     1 
ATOM   3334 O  O     . ARG A 1 428 ? -3.101  -14.101 30.281  1.00 16.74 ? 428  ARG A O     1 
ATOM   3335 C  CB    . ARG A 1 428 ? -5.463  -13.285 31.793  1.00 18.65 ? 428  ARG A CB    1 
ATOM   3336 C  CG    . ARG A 1 428 ? -5.992  -12.468 32.965  1.00 18.16 ? 428  ARG A CG    1 
ATOM   3337 C  CD    . ARG A 1 428 ? -6.775  -13.349 33.929  1.00 18.94 ? 428  ARG A CD    1 
ATOM   3338 N  NE    . ARG A 1 428 ? -7.029  -12.719 35.221  1.00 19.65 ? 428  ARG A NE    1 
ATOM   3339 C  CZ    . ARG A 1 428 ? -7.981  -11.806 35.456  1.00 17.99 ? 428  ARG A CZ    1 
ATOM   3340 N  NH1   . ARG A 1 428 ? -8.719  -11.343 34.470  1.00 17.54 ? 428  ARG A NH1   1 
ATOM   3341 N  NH2   . ARG A 1 428 ? -8.153  -11.327 36.667  1.00 17.99 ? 428  ARG A NH2   1 
ATOM   3342 N  N     . ASP A 1 429 ? -4.147  -13.194 28.477  1.00 17.76 ? 429  ASP A N     1 
ATOM   3343 C  CA    . ASP A 1 429 ? -3.612  -14.139 27.470  1.00 18.33 ? 429  ASP A CA    1 
ATOM   3344 C  C     . ASP A 1 429 ? -2.651  -13.402 26.529  1.00 18.69 ? 429  ASP A C     1 
ATOM   3345 O  O     . ASP A 1 429 ? -3.085  -12.442 25.821  1.00 19.94 ? 429  ASP A O     1 
ATOM   3346 C  CB    . ASP A 1 429 ? -4.741  -14.772 26.652  1.00 20.06 ? 429  ASP A CB    1 
ATOM   3347 C  CG    . ASP A 1 429 ? -5.636  -13.762 25.937  1.00 22.79 ? 429  ASP A CG    1 
ATOM   3348 O  OD1   . ASP A 1 429 ? -6.123  -12.791 26.589  1.00 22.64 ? 429  ASP A OD1   1 
ATOM   3349 O  OD2   . ASP A 1 429 ? -5.831  -13.931 24.745  1.00 20.82 ? 429  ASP A OD2   1 
ATOM   3350 N  N     . LEU A 1 430 ? -1.430  -13.905 26.430  1.00 17.40 ? 430  LEU A N     1 
ATOM   3351 C  CA    . LEU A 1 430 ? -0.457  -13.492 25.402  1.00 18.31 ? 430  LEU A CA    1 
ATOM   3352 C  C     . LEU A 1 430 ? -0.585  -14.394 24.175  1.00 17.03 ? 430  LEU A C     1 
ATOM   3353 O  O     . LEU A 1 430 ? -0.707  -15.614 24.327  1.00 17.73 ? 430  LEU A O     1 
ATOM   3354 C  CB    . LEU A 1 430 ? 0.945   -13.596 25.998  1.00 19.50 ? 430  LEU A CB    1 
ATOM   3355 C  CG    . LEU A 1 430 ? 2.078   -13.168 25.062  1.00 20.85 ? 430  LEU A CG    1 
ATOM   3356 C  CD1   . LEU A 1 430 ? 2.043   -11.666 24.812  1.00 21.94 ? 430  LEU A CD1   1 
ATOM   3357 C  CD2   . LEU A 1 430 ? 3.422   -13.594 25.626  1.00 21.59 ? 430  LEU A CD2   1 
ATOM   3358 N  N     . HIS A 1 431 ? -0.503  -13.804 22.992  1.00 17.06 ? 431  HIS A N     1 
ATOM   3359 C  CA    . HIS A 1 431 ? -0.312  -14.530 21.724  1.00 18.19 ? 431  HIS A CA    1 
ATOM   3360 C  C     . HIS A 1 431 ? 0.894   -13.933 21.012  1.00 17.80 ? 431  HIS A C     1 
ATOM   3361 O  O     . HIS A 1 431 ? 0.828   -12.735 20.634  1.00 17.30 ? 431  HIS A O     1 
ATOM   3362 C  CB    . HIS A 1 431 ? -1.537  -14.464 20.810  1.00 18.58 ? 431  HIS A CB    1 
ATOM   3363 C  CG    . HIS A 1 431 ? -2.825  -14.781 21.480  1.00 20.37 ? 431  HIS A CG    1 
ATOM   3364 N  ND1   . HIS A 1 431 ? -3.592  -15.868 21.094  1.00 19.89 ? 431  HIS A ND1   1 
ATOM   3365 C  CD2   . HIS A 1 431 ? -3.486  -14.153 22.486  1.00 19.36 ? 431  HIS A CD2   1 
ATOM   3366 C  CE1   . HIS A 1 431 ? -4.664  -15.908 21.871  1.00 23.96 ? 431  HIS A CE1   1 
ATOM   3367 N  NE2   . HIS A 1 431 ? -4.634  -14.840 22.708  1.00 20.01 ? 431  HIS A NE2   1 
ATOM   3368 N  N     . HIS A 1 432 ? 1.939   -14.735 20.814  1.00 18.28 ? 432  HIS A N     1 
ATOM   3369 C  CA    . HIS A 1 432 ? 2.938   -14.466 19.752  1.00 17.24 ? 432  HIS A CA    1 
ATOM   3370 C  C     . HIS A 1 432 ? 2.255   -14.862 18.453  1.00 18.34 ? 432  HIS A C     1 
ATOM   3371 O  O     . HIS A 1 432 ? 1.939   -16.061 18.293  1.00 20.69 ? 432  HIS A O     1 
ATOM   3372 C  CB    . HIS A 1 432 ? 4.269   -15.205 19.945  1.00 19.73 ? 432  HIS A CB    1 
ATOM   3373 C  CG    . HIS A 1 432 ? 5.208   -14.903 18.833  1.00 19.93 ? 432  HIS A CG    1 
ATOM   3374 N  ND1   . HIS A 1 432 ? 5.175   -15.580 17.633  1.00 21.42 ? 432  HIS A ND1   1 
ATOM   3375 C  CD2   . HIS A 1 432 ? 6.105   -13.905 18.678  1.00 22.05 ? 432  HIS A CD2   1 
ATOM   3376 C  CE1   . HIS A 1 432 ? 6.008   -15.005 16.777  1.00 21.61 ? 432  HIS A CE1   1 
ATOM   3377 N  NE2   . HIS A 1 432 ? 6.594   -13.972 17.398  1.00 20.85 ? 432  HIS A NE2   1 
ATOM   3378 N  N     . VAL A 1 433 ? 1.988   -13.908 17.578  1.00 17.69 ? 433  VAL A N     1 
ATOM   3379 C  CA    . VAL A 1 433 ? 1.301   -14.187 16.284  1.00 18.55 ? 433  VAL A CA    1 
ATOM   3380 C  C     . VAL A 1 433 ? 2.361   -14.125 15.197  1.00 19.30 ? 433  VAL A C     1 
ATOM   3381 O  O     . VAL A 1 433 ? 2.993   -13.046 15.051  1.00 19.89 ? 433  VAL A O     1 
ATOM   3382 C  CB    . VAL A 1 433 ? 0.172   -13.183 15.993  1.00 17.80 ? 433  VAL A CB    1 
ATOM   3383 C  CG1   . VAL A 1 433 ? -0.406  -13.381 14.593  1.00 17.81 ? 433  VAL A CG1   1 
ATOM   3384 C  CG2   . VAL A 1 433 ? -0.908  -13.254 17.062  1.00 16.50 ? 433  VAL A CG2   1 
ATOM   3385 N  N     . THR A 1 434 ? 2.538   -15.231 14.476  1.00 19.35 ? 434  THR A N     1 
ATOM   3386 C  CA    . THR A 1 434 ? 3.433   -15.326 13.314  1.00 20.17 ? 434  THR A CA    1 
ATOM   3387 C  C     . THR A 1 434 ? 2.586   -15.021 12.081  1.00 20.15 ? 434  THR A C     1 
ATOM   3388 O  O     . THR A 1 434 ? 1.559   -15.675 11.916  1.00 19.55 ? 434  THR A O     1 
ATOM   3389 C  CB    . THR A 1 434 ? 4.084   -16.712 13.226  1.00 21.48 ? 434  THR A CB    1 
ATOM   3390 O  OG1   . THR A 1 434 ? 4.707   -17.056 14.469  1.00 21.60 ? 434  THR A OG1   1 
ATOM   3391 C  CG2   . THR A 1 434 ? 5.066   -16.768 12.077  1.00 22.00 ? 434  THR A CG2   1 
ATOM   3392 N  N     . VAL A 1 435 ? 2.963   -14.023 11.300  1.00 18.53 ? 435  VAL A N     1 
ATOM   3393 C  CA    . VAL A 1 435 ? 2.255   -13.658 10.044  1.00 19.04 ? 435  VAL A CA    1 
ATOM   3394 C  C     . VAL A 1 435 ? 3.191   -13.994 8.890   1.00 19.98 ? 435  VAL A C     1 
ATOM   3395 O  O     . VAL A 1 435 ? 4.304   -13.428 8.864   1.00 20.79 ? 435  VAL A O     1 
ATOM   3396 C  CB    . VAL A 1 435 ? 1.869   -12.175 10.022  1.00 19.84 ? 435  VAL A CB    1 
ATOM   3397 C  CG1   . VAL A 1 435 ? 1.216   -11.801 8.698   1.00 20.11 ? 435  VAL A CG1   1 
ATOM   3398 C  CG2   . VAL A 1 435 ? 0.986   -11.816 11.212  1.00 20.23 ? 435  VAL A CG2   1 
ATOM   3399 N  N     . ILE A 1 436 ? 2.800   -14.924 8.029   1.00 18.59 ? 436  ILE A N     1 
ATOM   3400 C  CA    . ILE A 1 436 ? 3.665   -15.364 6.897   1.00 19.53 ? 436  ILE A CA    1 
ATOM   3401 C  C     . ILE A 1 436 ? 3.022   -14.955 5.573   1.00 19.91 ? 436  ILE A C     1 
ATOM   3402 O  O     . ILE A 1 436 ? 1.967   -15.487 5.262   1.00 18.24 ? 436  ILE A O     1 
ATOM   3403 C  CB    . ILE A 1 436 ? 3.908   -16.878 6.935   1.00 20.84 ? 436  ILE A CB    1 
ATOM   3404 C  CG1   . ILE A 1 436 ? 4.422   -17.340 8.296   1.00 22.21 ? 436  ILE A CG1   1 
ATOM   3405 C  CG2   . ILE A 1 436 ? 4.864   -17.284 5.818   1.00 22.08 ? 436  ILE A CG2   1 
ATOM   3406 C  CD1   . ILE A 1 436 ? 4.157   -18.783 8.551   1.00 24.14 ? 436  ILE A CD1   1 
ATOM   3407 N  N     . VAL A 1 437 ? 3.721   -14.158 4.766   1.00 22.26 ? 437  VAL A N     1 
ATOM   3408 C  CA    . VAL A 1 437 ? 3.277   -13.742 3.405   1.00 22.19 ? 437  VAL A CA    1 
ATOM   3409 C  C     . VAL A 1 437 ? 4.035   -14.606 2.400   1.00 23.24 ? 437  VAL A C     1 
ATOM   3410 O  O     . VAL A 1 437 ? 5.263   -14.653 2.506   1.00 24.96 ? 437  VAL A O     1 
ATOM   3411 C  CB    . VAL A 1 437 ? 3.544   -12.243 3.190   1.00 22.15 ? 437  VAL A CB    1 
ATOM   3412 C  CG1   . VAL A 1 437 ? 3.194   -11.752 1.793   1.00 22.58 ? 437  VAL A CG1   1 
ATOM   3413 C  CG2   . VAL A 1 437 ? 2.824   -11.421 4.238   1.00 21.92 ? 437  VAL A CG2   1 
ATOM   3414 N  N     . TYR A 1 438 ? 3.325   -15.249 1.474   1.00 21.39 ? 438  TYR A N     1 
ATOM   3415 C  CA    . TYR A 1 438 ? 3.877   -16.249 0.531   1.00 22.15 ? 438  TYR A CA    1 
ATOM   3416 C  C     . TYR A 1 438 ? 3.260   -16.056 -0.851  1.00 23.35 ? 438  TYR A C     1 
ATOM   3417 O  O     . TYR A 1 438 ? 2.115   -15.676 -0.909  1.00 24.49 ? 438  TYR A O     1 
ATOM   3418 C  CB    . TYR A 1 438 ? 3.629   -17.665 1.040   1.00 21.05 ? 438  TYR A CB    1 
ATOM   3419 C  CG    . TYR A 1 438 ? 2.192   -18.060 1.284   1.00 23.27 ? 438  TYR A CG    1 
ATOM   3420 C  CD1   . TYR A 1 438 ? 1.509   -17.649 2.426   1.00 21.17 ? 438  TYR A CD1   1 
ATOM   3421 C  CD2   . TYR A 1 438 ? 1.532   -18.935 0.422   1.00 24.24 ? 438  TYR A CD2   1 
ATOM   3422 C  CE1   . TYR A 1 438 ? 0.210   -18.052 2.676   1.00 21.01 ? 438  TYR A CE1   1 
ATOM   3423 C  CE2   . TYR A 1 438 ? 0.222   -19.339 0.654   1.00 22.51 ? 438  TYR A CE2   1 
ATOM   3424 C  CZ    . TYR A 1 438 ? -0.441  -18.895 1.783   1.00 22.17 ? 438  TYR A CZ    1 
ATOM   3425 O  OH    . TYR A 1 438 ? -1.719  -19.309 2.025   1.00 21.68 ? 438  TYR A OH    1 
ATOM   3426 N  N     . ASP A 1 439 ? 4.001   -16.381 -1.909  1.00 23.46 ? 439  ASP A N     1 
ATOM   3427 C  CA    . ASP A 1 439 ? 3.492   -16.457 -3.297  1.00 25.11 ? 439  ASP A CA    1 
ATOM   3428 C  C     . ASP A 1 439 ? 2.665   -17.738 -3.429  1.00 25.25 ? 439  ASP A C     1 
ATOM   3429 O  O     . ASP A 1 439 ? 3.220   -18.824 -3.637  1.00 25.93 ? 439  ASP A O     1 
ATOM   3430 C  CB    . ASP A 1 439 ? 4.616   -16.403 -4.331  1.00 26.65 ? 439  ASP A CB    1 
ATOM   3431 C  CG    . ASP A 1 439 ? 4.107   -16.427 -5.763  1.00 28.64 ? 439  ASP A CG    1 
ATOM   3432 O  OD1   . ASP A 1 439 ? 2.868   -16.471 -5.964  1.00 30.53 ? 439  ASP A OD1   1 
ATOM   3433 O  OD2   . ASP A 1 439 ? 4.954   -16.426 -6.664  1.00 32.37 ? 439  ASP A OD2   1 
ATOM   3434 N  N     . LYS A 1 440 ? 1.356   -17.587 -3.323  1.00 25.98 ? 440  LYS A N     1 
ATOM   3435 C  CA    . LYS A 1 440 ? 0.388   -18.692 -3.350  1.00 26.36 ? 440  LYS A CA    1 
ATOM   3436 C  C     . LYS A 1 440 ? 0.373   -19.293 -4.759  1.00 27.60 ? 440  LYS A C     1 
ATOM   3437 O  O     . LYS A 1 440 ? -0.151  -20.418 -4.889  1.00 26.02 ? 440  LYS A O     1 
ATOM   3438 C  CB    . LYS A 1 440 ? -0.965  -18.139 -2.881  1.00 28.30 ? 440  LYS A CB    1 
ATOM   3439 C  CG    . LYS A 1 440 ? -1.579  -17.087 -3.796  1.00 30.04 ? 440  LYS A CG    1 
ATOM   3440 C  CD    . LYS A 1 440 ? -2.398  -17.690 -4.910  1.00 34.30 ? 440  LYS A CD    1 
ATOM   3441 C  CE    . LYS A 1 440 ? -3.137  -16.656 -5.740  1.00 38.16 ? 440  LYS A CE    1 
ATOM   3442 N  NZ    . LYS A 1 440 ? -4.043  -17.341 -6.690  1.00 40.09 ? 440  LYS A NZ    1 
ATOM   3443 N  N     . THR A 1 441 ? 0.927   -18.606 -5.775  1.00 30.16 ? 441  THR A N     1 
ATOM   3444 C  CA    . THR A 1 441 ? 0.969   -19.135 -7.169  1.00 31.58 ? 441  THR A CA    1 
ATOM   3445 C  C     . THR A 1 441 ? 2.186   -20.042 -7.354  1.00 34.27 ? 441  THR A C     1 
ATOM   3446 O  O     . THR A 1 441 ? 2.236   -20.702 -8.388  1.00 38.81 ? 441  THR A O     1 
ATOM   3447 C  CB    . THR A 1 441 ? 0.938   -18.039 -8.246  1.00 31.84 ? 441  THR A CB    1 
ATOM   3448 O  OG1   . THR A 1 441 ? 2.171   -17.315 -8.264  1.00 34.59 ? 441  THR A OG1   1 
ATOM   3449 C  CG2   . THR A 1 441 ? -0.190  -17.057 -8.045  1.00 30.91 ? 441  THR A CG2   1 
ATOM   3450 N  N     . ASP A 1 442 ? 3.122   -20.105 -6.405  1.00 32.31 ? 442  ASP A N     1 
ATOM   3451 C  CA    . ASP A 1 442 ? 4.396   -20.839 -6.623  1.00 30.75 ? 442  ASP A CA    1 
ATOM   3452 C  C     . ASP A 1 442 ? 4.399   -22.154 -5.851  1.00 29.05 ? 442  ASP A C     1 
ATOM   3453 O  O     . ASP A 1 442 ? 4.439   -22.176 -4.628  1.00 27.89 ? 442  ASP A O     1 
ATOM   3454 C  CB    . ASP A 1 442 ? 5.586   -19.954 -6.290  1.00 33.48 ? 442  ASP A CB    1 
ATOM   3455 C  CG    . ASP A 1 442 ? 6.920   -20.652 -6.450  1.00 34.42 ? 442  ASP A CG    1 
ATOM   3456 O  OD1   . ASP A 1 442 ? 6.957   -21.905 -6.557  1.00 37.65 ? 442  ASP A OD1   1 
ATOM   3457 O  OD2   . ASP A 1 442 ? 7.905   -19.940 -6.403  1.00 42.62 ? 442  ASP A OD2   1 
ATOM   3458 N  N     . PRO A 1 443 ? 4.406   -23.301 -6.558  1.00 30.06 ? 443  PRO A N     1 
ATOM   3459 C  CA    . PRO A 1 443 ? 4.334   -24.608 -5.908  1.00 31.18 ? 443  PRO A CA    1 
ATOM   3460 C  C     . PRO A 1 443 ? 5.456   -24.865 -4.889  1.00 31.28 ? 443  PRO A C     1 
ATOM   3461 O  O     . PRO A 1 443 ? 5.240   -25.595 -3.935  1.00 26.50 ? 443  PRO A O     1 
ATOM   3462 C  CB    . PRO A 1 443 ? 4.507   -25.613 -7.053  1.00 32.19 ? 443  PRO A CB    1 
ATOM   3463 C  CG    . PRO A 1 443 ? 4.213   -24.848 -8.326  1.00 31.39 ? 443  PRO A CG    1 
ATOM   3464 C  CD    . PRO A 1 443 ? 4.467   -23.390 -8.027  1.00 30.80 ? 443  PRO A CD    1 
ATOM   3465 N  N     . ASP A 1 444 ? 6.643   -24.310 -5.151  1.00 32.42 ? 444  ASP A N     1 
ATOM   3466 C  CA    . ASP A 1 444 ? 7.822   -24.503 -4.273  1.00 33.75 ? 444  ASP A CA    1 
ATOM   3467 C  C     . ASP A 1 444 ? 7.646   -23.672 -2.992  1.00 28.92 ? 444  ASP A C     1 
ATOM   3468 O  O     . ASP A 1 444 ? 8.005   -24.181 -1.933  1.00 26.63 ? 444  ASP A O     1 
ATOM   3469 C  CB    . ASP A 1 444 ? 9.119   -24.180 -5.008  1.00 39.65 ? 444  ASP A CB    1 
ATOM   3470 C  CG    . ASP A 1 444 ? 10.325  -24.577 -4.181  1.00 50.88 ? 444  ASP A CG    1 
ATOM   3471 O  OD1   . ASP A 1 444 ? 10.407  -25.780 -3.809  1.00 58.17 ? 444  ASP A OD1   1 
ATOM   3472 O  OD2   . ASP A 1 444 ? 11.137  -23.670 -3.860  1.00 57.18 ? 444  ASP A OD2   1 
ATOM   3473 N  N     . GLU A 1 445 ? 7.145   -22.439 -3.091  1.00 27.26 ? 445  GLU A N     1 
ATOM   3474 C  CA    . GLU A 1 445 ? 6.837   -21.582 -1.925  1.00 27.61 ? 445  GLU A CA    1 
ATOM   3475 C  C     . GLU A 1 445 ? 5.744   -22.250 -1.081  1.00 27.55 ? 445  GLU A C     1 
ATOM   3476 O  O     . GLU A 1 445 ? 5.853   -22.208 0.159   1.00 25.40 ? 445  GLU A O     1 
ATOM   3477 C  CB    . GLU A 1 445 ? 6.354   -20.216 -2.386  1.00 33.81 ? 445  GLU A CB    1 
ATOM   3478 C  CG    . GLU A 1 445 ? 7.452   -19.266 -2.808  1.00 40.93 ? 445  GLU A CG    1 
ATOM   3479 C  CD    . GLU A 1 445 ? 7.835   -18.292 -1.708  1.00 46.80 ? 445  GLU A CD    1 
ATOM   3480 O  OE1   . GLU A 1 445 ? 8.908   -18.544 -1.141  1.00 54.24 ? 445  GLU A OE1   1 
ATOM   3481 O  OE2   . GLU A 1 445 ? 7.055   -17.294 -1.406  1.00 41.07 ? 445  GLU A OE2   1 
ATOM   3482 N  N     . ARG A 1 446 ? 4.727   -22.835 -1.729  1.00 24.39 ? 446  ARG A N     1 
ATOM   3483 C  CA    . ARG A 1 446 ? 3.584   -23.495 -1.047  1.00 24.70 ? 446  ARG A CA    1 
ATOM   3484 C  C     . ARG A 1 446 ? 4.101   -24.699 -0.254  1.00 23.83 ? 446  ARG A C     1 
ATOM   3485 O  O     . ARG A 1 446 ? 3.627   -24.952 0.895   1.00 20.49 ? 446  ARG A O     1 
ATOM   3486 C  CB    . ARG A 1 446 ? 2.515   -23.915 -2.067  1.00 26.62 ? 446  ARG A CB    1 
ATOM   3487 C  CG    . ARG A 1 446 ? 1.704   -22.772 -2.660  1.00 25.94 ? 446  ARG A CG    1 
ATOM   3488 C  CD    . ARG A 1 446 ? 0.386   -23.243 -3.247  1.00 27.89 ? 446  ARG A CD    1 
ATOM   3489 N  NE    . ARG A 1 446 ? 0.578   -24.233 -4.285  1.00 28.91 ? 446  ARG A NE    1 
ATOM   3490 C  CZ    . ARG A 1 446 ? 0.394   -24.051 -5.600  1.00 32.33 ? 446  ARG A CZ    1 
ATOM   3491 N  NH1   . ARG A 1 446 ? -0.005  -22.890 -6.091  1.00 32.10 ? 446  ARG A NH1   1 
ATOM   3492 N  NH2   . ARG A 1 446 ? 0.633   -25.049 -6.433  1.00 31.11 ? 446  ARG A NH2   1 
ATOM   3493 N  N     . LYS A 1 447 ? 5.028   -25.448 -0.845  1.00 23.92 ? 447  LYS A N     1 
ATOM   3494 C  CA    . LYS A 1 447 ? 5.633   -26.632 -0.189  1.00 24.33 ? 447  LYS A CA    1 
ATOM   3495 C  C     . LYS A 1 447 ? 6.448   -26.173 1.032   1.00 22.33 ? 447  LYS A C     1 
ATOM   3496 O  O     . LYS A 1 447 ? 6.330   -26.803 2.106   1.00 20.45 ? 447  LYS A O     1 
ATOM   3497 C  CB    . LYS A 1 447 ? 6.472   -27.378 -1.221  1.00 28.23 ? 447  LYS A CB    1 
ATOM   3498 C  CG    . LYS A 1 447 ? 7.129   -28.649 -0.723  1.00 31.74 ? 447  LYS A CG    1 
ATOM   3499 C  CD    . LYS A 1 447 ? 7.905   -29.367 -1.822  1.00 38.33 ? 447  LYS A CD    1 
ATOM   3500 C  CE    . LYS A 1 447 ? 8.097   -30.837 -1.521  1.00 41.63 ? 447  LYS A CE    1 
ATOM   3501 N  NZ    . LYS A 1 447 ? 8.957   -31.000 -0.332  1.00 46.23 ? 447  LYS A NZ    1 
ATOM   3502 N  N     . LYS A 1 448 ? 7.257   -25.130 0.881   1.00 23.08 ? 448  LYS A N     1 
ATOM   3503 C  CA    . LYS A 1 448 ? 8.083   -24.579 2.000   1.00 24.15 ? 448  LYS A CA    1 
ATOM   3504 C  C     . LYS A 1 448 ? 7.183   -24.062 3.136   1.00 25.17 ? 448  LYS A C     1 
ATOM   3505 O  O     . LYS A 1 448 ? 7.522   -24.303 4.343   1.00 21.68 ? 448  LYS A O     1 
ATOM   3506 C  CB    . LYS A 1 448 ? 8.972   -23.469 1.461   1.00 26.49 ? 448  LYS A CB    1 
ATOM   3507 C  CG    . LYS A 1 448 ? 10.193  -24.026 0.742   1.00 28.33 ? 448  LYS A CG    1 
ATOM   3508 C  CD    . LYS A 1 448 ? 10.884  -23.043 -0.126  1.00 30.90 ? 448  LYS A CD    1 
ATOM   3509 C  CE    . LYS A 1 448 ? 11.287  -21.821 0.635   1.00 32.30 ? 448  LYS A CE    1 
ATOM   3510 N  NZ    . LYS A 1 448 ? 11.814  -20.810 -0.292  1.00 36.07 ? 448  LYS A NZ    1 
ATOM   3511 N  N     . LEU A 1 449 ? 6.079   -23.401 2.763   1.00 25.11 ? 449  LEU A N     1 
ATOM   3512 C  CA    . LEU A 1 449 ? 5.087   -22.834 3.716   1.00 26.83 ? 449  LEU A CA    1 
ATOM   3513 C  C     . LEU A 1 449 ? 4.487   -23.956 4.568   1.00 24.51 ? 449  LEU A C     1 
ATOM   3514 O  O     . LEU A 1 449 ? 4.538   -23.869 5.808   1.00 24.70 ? 449  LEU A O     1 
ATOM   3515 C  CB    . LEU A 1 449 ? 3.972   -22.095 2.975   1.00 27.64 ? 449  LEU A CB    1 
ATOM   3516 C  CG    . LEU A 1 449 ? 2.877   -21.583 3.917   1.00 29.90 ? 449  LEU A CG    1 
ATOM   3517 C  CD1   . LEU A 1 449 ? 3.434   -20.523 4.856   1.00 29.48 ? 449  LEU A CD1   1 
ATOM   3518 C  CD2   . LEU A 1 449 ? 1.701   -21.041 3.147   1.00 32.04 ? 449  LEU A CD2   1 
ATOM   3519 N  N     . ASP A 1 450 ? 3.948   -24.978 3.920   1.00 24.22 ? 450  ASP A N     1 
ATOM   3520 C  CA    . ASP A 1 450 ? 3.340   -26.154 4.591   1.00 23.72 ? 450  ASP A CA    1 
ATOM   3521 C  C     . ASP A 1 450 ? 4.351   -26.783 5.555   1.00 24.91 ? 450  ASP A C     1 
ATOM   3522 O  O     . ASP A 1 450 ? 3.969   -27.141 6.671   1.00 22.57 ? 450  ASP A O     1 
ATOM   3523 C  CB    . ASP A 1 450 ? 2.836   -27.140 3.540   1.00 24.67 ? 450  ASP A CB    1 
ATOM   3524 C  CG    . ASP A 1 450 ? 1.759   -28.083 4.016   1.00 26.99 ? 450  ASP A CG    1 
ATOM   3525 O  OD1   . ASP A 1 450 ? 1.017   -27.747 4.956   1.00 31.02 ? 450  ASP A OD1   1 
ATOM   3526 O  OD2   . ASP A 1 450 ? 1.624   -29.117 3.404   1.00 34.31 ? 450  ASP A OD2   1 
ATOM   3527 N  N     . GLU A 1 451 ? 5.599   -26.966 5.125   1.00 23.97 ? 451  GLU A N     1 
ATOM   3528 C  CA    . GLU A 1 451 ? 6.622   -27.665 5.942   1.00 24.18 ? 451  GLU A CA    1 
ATOM   3529 C  C     . GLU A 1 451 ? 6.956   -26.770 7.145   1.00 22.17 ? 451  GLU A C     1 
ATOM   3530 O  O     . GLU A 1 451 ? 7.077   -27.283 8.266   1.00 22.71 ? 451  GLU A O     1 
ATOM   3531 C  CB    . GLU A 1 451 ? 7.818   -28.008 5.036   1.00 26.94 ? 451  GLU A CB    1 
ATOM   3532 C  CG    . GLU A 1 451 ? 9.018   -28.649 5.729   1.00 32.42 ? 451  GLU A CG    1 
ATOM   3533 C  CD    . GLU A 1 451 ? 10.146  -29.095 4.781   1.00 33.95 ? 451  GLU A CD    1 
ATOM   3534 O  OE1   . GLU A 1 451 ? 9.820   -29.596 3.711   1.00 36.32 ? 451  GLU A OE1   1 
ATOM   3535 O  OE2   . GLU A 1 451 ? 11.338  -28.850 5.069   1.00 31.13 ? 451  GLU A OE2   1 
ATOM   3536 N  N     . LEU A 1 452 ? 7.100   -25.465 6.916   1.00 19.99 ? 452  LEU A N     1 
ATOM   3537 C  CA    . LEU A 1 452 ? 7.350   -24.482 7.989   1.00 20.09 ? 452  LEU A CA    1 
ATOM   3538 C  C     . LEU A 1 452 ? 6.200   -24.511 8.999   1.00 19.66 ? 452  LEU A C     1 
ATOM   3539 O  O     . LEU A 1 452 ? 6.464   -24.579 10.199  1.00 21.03 ? 452  LEU A O     1 
ATOM   3540 C  CB    . LEU A 1 452 ? 7.523   -23.099 7.375   1.00 20.45 ? 452  LEU A CB    1 
ATOM   3541 C  CG    . LEU A 1 452 ? 7.440   -21.925 8.339   1.00 18.96 ? 452  LEU A CG    1 
ATOM   3542 C  CD1   . LEU A 1 452 ? 8.491   -22.008 9.439   1.00 21.04 ? 452  LEU A CD1   1 
ATOM   3543 C  CD2   . LEU A 1 452 ? 7.581   -20.646 7.569   1.00 19.79 ? 452  LEU A CD2   1 
ATOM   3544 N  N     . PHE A 1 453 ? 4.967   -24.454 8.528   1.00 19.82 ? 453  PHE A N     1 
ATOM   3545 C  CA    . PHE A 1 453 ? 3.798   -24.344 9.423   1.00 20.46 ? 453  PHE A CA    1 
ATOM   3546 C  C     . PHE A 1 453 ? 3.776   -25.535 10.389  1.00 20.76 ? 453  PHE A C     1 
ATOM   3547 O  O     . PHE A 1 453 ? 3.563   -25.330 11.594  1.00 19.10 ? 453  PHE A O     1 
ATOM   3548 C  CB    . PHE A 1 453 ? 2.516   -24.182 8.605   1.00 21.91 ? 453  PHE A CB    1 
ATOM   3549 C  CG    . PHE A 1 453 ? 1.373   -23.650 9.430   1.00 21.68 ? 453  PHE A CG    1 
ATOM   3550 C  CD1   . PHE A 1 453 ? 0.607   -24.509 10.195  1.00 20.52 ? 453  PHE A CD1   1 
ATOM   3551 C  CD2   . PHE A 1 453 ? 1.123   -22.292 9.491   1.00 22.93 ? 453  PHE A CD2   1 
ATOM   3552 C  CE1   . PHE A 1 453 ? -0.434  -24.019 10.964  1.00 22.01 ? 453  PHE A CE1   1 
ATOM   3553 C  CE2   . PHE A 1 453 ? 0.089   -21.803 10.272  1.00 23.95 ? 453  PHE A CE2   1 
ATOM   3554 C  CZ    . PHE A 1 453 ? -0.684  -22.669 11.006  1.00 22.47 ? 453  PHE A CZ    1 
ATOM   3555 N  N     . ASN A 1 454 ? 4.044   -26.743 9.880   1.00 23.29 ? 454  ASN A N     1 
ATOM   3556 C  CA    . ASN A 1 454 ? 4.045   -27.994 10.689  1.00 23.58 ? 454  ASN A CA    1 
ATOM   3557 C  C     . ASN A 1 454 ? 5.122   -27.941 11.797  1.00 20.67 ? 454  ASN A C     1 
ATOM   3558 O  O     . ASN A 1 454 ? 4.856   -28.428 12.918  1.00 17.99 ? 454  ASN A O     1 
ATOM   3559 C  CB    . ASN A 1 454 ? 4.165   -29.218 9.775   1.00 23.99 ? 454  ASN A CB    1 
ATOM   3560 C  CG    . ASN A 1 454 ? 2.835   -29.552 9.118   1.00 26.87 ? 454  ASN A CG    1 
ATOM   3561 O  OD1   . ASN A 1 454 ? 1.859   -29.867 9.785   1.00 31.59 ? 454  ASN A OD1   1 
ATOM   3562 N  ND2   . ASN A 1 454 ? 2.757   -29.448 7.803   1.00 28.85 ? 454  ASN A ND2   1 
ATOM   3563 N  N     . ILE A 1 455 ? 6.313   -27.422 11.505  1.00 20.01 ? 455  ILE A N     1 
ATOM   3564 C  CA    . ILE A 1 455 ? 7.394   -27.200 12.517  1.00 20.82 ? 455  ILE A CA    1 
ATOM   3565 C  C     . ILE A 1 455 ? 6.924   -26.179 13.586  1.00 21.15 ? 455  ILE A C     1 
ATOM   3566 O  O     . ILE A 1 455 ? 7.164   -26.417 14.817  1.00 21.69 ? 455  ILE A O     1 
ATOM   3567 C  CB    . ILE A 1 455 ? 8.688   -26.739 11.810  1.00 20.75 ? 455  ILE A CB    1 
ATOM   3568 C  CG1   . ILE A 1 455 ? 9.231   -27.811 10.866  1.00 21.83 ? 455  ILE A CG1   1 
ATOM   3569 C  CG2   . ILE A 1 455 ? 9.754   -26.311 12.810  1.00 20.35 ? 455  ILE A CG2   1 
ATOM   3570 C  CD1   . ILE A 1 455 ? 10.381  -27.309 10.000  1.00 21.73 ? 455  ILE A CD1   1 
ATOM   3571 N  N     . LEU A 1 456 ? 6.291   -25.072 13.184  1.00 20.29 ? 456  LEU A N     1 
ATOM   3572 C  CA    . LEU A 1 456 ? 5.834   -24.047 14.167  1.00 21.32 ? 456  LEU A CA    1 
ATOM   3573 C  C     . LEU A 1 456 ? 4.822   -24.690 15.137  1.00 21.00 ? 456  LEU A C     1 
ATOM   3574 O  O     . LEU A 1 456 ? 4.969   -24.522 16.368  1.00 18.93 ? 456  LEU A O     1 
ATOM   3575 C  CB    . LEU A 1 456 ? 5.249   -22.837 13.426  1.00 21.22 ? 456  LEU A CB    1 
ATOM   3576 C  CG    . LEU A 1 456 ? 6.222   -22.073 12.532  1.00 19.10 ? 456  LEU A CG    1 
ATOM   3577 C  CD1   . LEU A 1 456 ? 5.547   -20.864 11.899  1.00 20.03 ? 456  LEU A CD1   1 
ATOM   3578 C  CD2   . LEU A 1 456 ? 7.445   -21.643 13.324  1.00 19.47 ? 456  LEU A CD2   1 
ATOM   3579 N  N     . VAL A 1 457 ? 3.861   -25.457 14.620  1.00 21.28 ? 457  VAL A N     1 
ATOM   3580 C  CA    . VAL A 1 457 ? 2.827   -26.114 15.472  1.00 20.59 ? 457  VAL A CA    1 
ATOM   3581 C  C     . VAL A 1 457 ? 3.515   -27.034 16.480  1.00 21.40 ? 457  VAL A C     1 
ATOM   3582 O  O     . VAL A 1 457 ? 3.181   -26.945 17.671  1.00 20.91 ? 457  VAL A O     1 
ATOM   3583 C  CB    . VAL A 1 457 ? 1.809   -26.884 14.629  1.00 20.92 ? 457  VAL A CB    1 
ATOM   3584 C  CG1   . VAL A 1 457 ? 0.902   -27.750 15.487  1.00 21.26 ? 457  VAL A CG1   1 
ATOM   3585 C  CG2   . VAL A 1 457 ? 1.027   -25.937 13.733  1.00 23.13 ? 457  VAL A CG2   1 
ATOM   3586 N  N     . ASP A 1 458 ? 4.442   -27.882 16.016  1.00 21.61 ? 458  ASP A N     1 
ATOM   3587 C  CA    . ASP A 1 458 ? 5.071   -28.940 16.843  1.00 22.75 ? 458  ASP A CA    1 
ATOM   3588 C  C     . ASP A 1 458 ? 5.928   -28.295 17.941  1.00 21.72 ? 458  ASP A C     1 
ATOM   3589 O  O     . ASP A 1 458 ? 5.863   -28.760 19.085  1.00 19.61 ? 458  ASP A O     1 
ATOM   3590 C  CB    . ASP A 1 458 ? 5.949   -29.892 16.021  1.00 25.67 ? 458  ASP A CB    1 
ATOM   3591 C  CG    . ASP A 1 458 ? 5.186   -30.875 15.163  1.00 27.67 ? 458  ASP A CG    1 
ATOM   3592 O  OD1   . ASP A 1 458 ? 3.987   -31.070 15.384  1.00 29.31 ? 458  ASP A OD1   1 
ATOM   3593 O  OD2   . ASP A 1 458 ? 5.797   -31.386 14.252  1.00 35.26 ? 458  ASP A OD2   1 
ATOM   3594 N  N     . GLU A 1 459 ? 6.749   -27.311 17.584  1.00 21.50 ? 459  GLU A N     1 
ATOM   3595 C  CA    . GLU A 1 459 ? 7.668   -26.669 18.556  1.00 21.68 ? 459  GLU A CA    1 
ATOM   3596 C  C     . GLU A 1 459 ? 6.832   -25.882 19.571  1.00 20.86 ? 459  GLU A C     1 
ATOM   3597 O  O     . GLU A 1 459 ? 7.196   -25.935 20.732  1.00 19.32 ? 459  GLU A O     1 
ATOM   3598 C  CB    . GLU A 1 459 ? 8.727   -25.836 17.848  1.00 22.18 ? 459  GLU A CB    1 
ATOM   3599 C  CG    . GLU A 1 459 ? 9.613   -26.708 16.975  1.00 24.58 ? 459  GLU A CG    1 
ATOM   3600 C  CD    . GLU A 1 459 ? 10.832  -26.058 16.364  1.00 25.85 ? 459  GLU A CD    1 
ATOM   3601 O  OE1   . GLU A 1 459 ? 10.857  -24.810 16.197  1.00 23.69 ? 459  GLU A OE1   1 
ATOM   3602 O  OE2   . GLU A 1 459 ? 11.740  -26.828 16.026  1.00 32.35 ? 459  GLU A OE2   1 
ATOM   3603 N  N     . ALA A 1 460 ? 5.716   -25.261 19.157  1.00 20.19 ? 460  ALA A N     1 
ATOM   3604 C  CA    . ALA A 1 460 ? 4.844   -24.501 20.076  1.00 18.95 ? 460  ALA A CA    1 
ATOM   3605 C  C     . ALA A 1 460 ? 4.191   -25.477 21.064  1.00 19.11 ? 460  ALA A C     1 
ATOM   3606 O  O     . ALA A 1 460 ? 4.228   -25.215 22.274  1.00 16.80 ? 460  ALA A O     1 
ATOM   3607 C  CB    . ALA A 1 460 ? 3.849   -23.714 19.282  1.00 19.76 ? 460  ALA A CB    1 
ATOM   3608 N  N     . ALA A 1 461 ? 3.638   -26.592 20.568  1.00 19.70 ? 461  ALA A N     1 
ATOM   3609 C  CA    . ALA A 1 461 ? 2.945   -27.614 21.386  1.00 18.13 ? 461  ALA A CA    1 
ATOM   3610 C  C     . ALA A 1 461 ? 3.935   -28.202 22.411  1.00 20.60 ? 461  ALA A C     1 
ATOM   3611 O  O     . ALA A 1 461 ? 3.511   -28.447 23.559  1.00 20.54 ? 461  ALA A O     1 
ATOM   3612 C  CB    . ALA A 1 461 ? 2.309   -28.694 20.527  1.00 16.87 ? 461  ALA A CB    1 
ATOM   3613 N  N     . ALA A 1 462 ? 5.197   -28.396 22.036  1.00 20.75 ? 462  ALA A N     1 
ATOM   3614 C  CA    . ALA A 1 462 ? 6.248   -28.948 22.919  1.00 24.23 ? 462  ALA A CA    1 
ATOM   3615 C  C     . ALA A 1 462 ? 6.502   -27.997 24.091  1.00 24.95 ? 462  ALA A C     1 
ATOM   3616 O  O     . ALA A 1 462 ? 6.894   -28.491 25.150  1.00 25.92 ? 462  ALA A O     1 
ATOM   3617 C  CB    . ALA A 1 462 ? 7.524   -29.188 22.134  1.00 25.18 ? 462  ALA A CB    1 
ATOM   3618 N  N     . GLU A 1 463 ? 6.278   -26.690 23.916  1.00 22.94 ? 463  GLU A N     1 
ATOM   3619 C  CA    . GLU A 1 463 ? 6.352   -25.699 25.026  1.00 23.23 ? 463  GLU A CA    1 
ATOM   3620 C  C     . GLU A 1 463 ? 5.003   -25.511 25.749  1.00 21.59 ? 463  GLU A C     1 
ATOM   3621 O  O     . GLU A 1 463 ? 4.983   -24.698 26.696  1.00 21.82 ? 463  GLU A O     1 
ATOM   3622 C  CB    . GLU A 1 463 ? 6.806   -24.335 24.521  1.00 23.59 ? 463  GLU A CB    1 
ATOM   3623 C  CG    . GLU A 1 463 ? 8.049   -24.399 23.683  1.00 26.38 ? 463  GLU A CG    1 
ATOM   3624 C  CD    . GLU A 1 463 ? 9.235   -24.928 24.461  1.00 29.19 ? 463  GLU A CD    1 
ATOM   3625 O  OE1   . GLU A 1 463 ? 9.502   -24.399 25.566  1.00 29.33 ? 463  GLU A OE1   1 
ATOM   3626 O  OE2   . GLU A 1 463 ? 9.839   -25.900 23.986  1.00 32.89 ? 463  GLU A OE2   1 
ATOM   3627 N  N     . GLY A 1 464 ? 3.933   -26.212 25.360  1.00 18.35 ? 464  GLY A N     1 
ATOM   3628 C  CA    . GLY A 1 464 ? 2.599   -26.036 25.962  1.00 18.54 ? 464  GLY A CA    1 
ATOM   3629 C  C     . GLY A 1 464 ? 1.849   -24.813 25.431  1.00 18.24 ? 464  GLY A C     1 
ATOM   3630 O  O     . GLY A 1 464 ? 0.942   -24.344 26.111  1.00 17.66 ? 464  GLY A O     1 
ATOM   3631 N  N     . TYR A 1 465 ? 2.188   -24.342 24.231  1.00 17.88 ? 465  TYR A N     1 
ATOM   3632 C  CA    . TYR A 1 465 ? 1.548   -23.208 23.514  1.00 17.63 ? 465  TYR A CA    1 
ATOM   3633 C  C     . TYR A 1 465 ? 0.582   -23.769 22.435  1.00 17.52 ? 465  TYR A C     1 
ATOM   3634 O  O     . TYR A 1 465 ? 1.055   -24.386 21.459  1.00 16.66 ? 465  TYR A O     1 
ATOM   3635 C  CB    . TYR A 1 465 ? 2.638   -22.348 22.858  1.00 18.16 ? 465  TYR A CB    1 
ATOM   3636 C  CG    . TYR A 1 465 ? 3.710   -21.773 23.750  1.00 19.05 ? 465  TYR A CG    1 
ATOM   3637 C  CD1   . TYR A 1 465 ? 3.512   -21.478 25.097  1.00 18.99 ? 465  TYR A CD1   1 
ATOM   3638 C  CD2   . TYR A 1 465 ? 4.950   -21.467 23.204  1.00 20.32 ? 465  TYR A CD2   1 
ATOM   3639 C  CE1   . TYR A 1 465 ? 4.531   -20.931 25.881  1.00 20.72 ? 465  TYR A CE1   1 
ATOM   3640 C  CE2   . TYR A 1 465 ? 5.967   -20.916 23.966  1.00 20.22 ? 465  TYR A CE2   1 
ATOM   3641 C  CZ    . TYR A 1 465 ? 5.758   -20.625 25.303  1.00 21.19 ? 465  TYR A CZ    1 
ATOM   3642 O  OH    . TYR A 1 465 ? 6.813   -20.071 25.982  1.00 21.83 ? 465  TYR A OH    1 
ATOM   3643 N  N     . GLY A 1 466 ? -0.733  -23.591 22.620  1.00 17.55 ? 466  GLY A N     1 
ATOM   3644 C  CA    . GLY A 1 466 ? -1.789  -24.110 21.738  1.00 18.49 ? 466  GLY A CA    1 
ATOM   3645 C  C     . GLY A 1 466 ? -2.468  -23.039 20.889  1.00 18.77 ? 466  GLY A C     1 
ATOM   3646 O  O     . GLY A 1 466 ? -2.800  -21.951 21.417  1.00 19.01 ? 466  GLY A O     1 
ATOM   3647 N  N     . GLU A 1 467 ? -2.753  -23.377 19.632  1.00 18.21 ? 467  GLU A N     1 
ATOM   3648 C  CA    . GLU A 1 467 ? -3.463  -22.499 18.670  1.00 17.63 ? 467  GLU A CA    1 
ATOM   3649 C  C     . GLU A 1 467 ? -4.942  -22.435 19.060  1.00 17.43 ? 467  GLU A C     1 
ATOM   3650 O  O     . GLU A 1 467 ? -5.481  -23.471 19.524  1.00 15.82 ? 467  GLU A O     1 
ATOM   3651 C  CB    . GLU A 1 467 ? -3.321  -23.024 17.242  1.00 18.77 ? 467  GLU A CB    1 
ATOM   3652 C  CG    . GLU A 1 467 ? -4.050  -22.157 16.221  1.00 19.07 ? 467  GLU A CG    1 
ATOM   3653 C  CD    . GLU A 1 467 ? -3.616  -20.694 16.164  1.00 18.12 ? 467  GLU A CD    1 
ATOM   3654 O  OE1   . GLU A 1 467 ? -4.154  -19.868 16.925  1.00 16.82 ? 467  GLU A OE1   1 
ATOM   3655 O  OE2   . GLU A 1 467 ? -2.713  -20.376 15.354  1.00 19.55 ? 467  GLU A OE2   1 
ATOM   3656 N  N     . TYR A 1 468 ? -5.577  -21.279 18.850  1.00 15.38 ? 468  TYR A N     1 
ATOM   3657 C  CA    . TYR A 1 468 ? -7.021  -21.089 19.122  1.00 16.23 ? 468  TYR A CA    1 
ATOM   3658 C  C     . TYR A 1 468 ? -7.814  -20.894 17.829  1.00 15.15 ? 468  TYR A C     1 
ATOM   3659 O  O     . TYR A 1 468 ? -9.049  -20.947 17.939  1.00 14.80 ? 468  TYR A O     1 
ATOM   3660 C  CB    . TYR A 1 468 ? -7.265  -19.893 20.059  1.00 16.94 ? 468  TYR A CB    1 
ATOM   3661 C  CG    . TYR A 1 468 ? -7.232  -18.552 19.378  1.00 16.04 ? 468  TYR A CG    1 
ATOM   3662 C  CD1   . TYR A 1 468 ? -6.028  -17.919 19.140  1.00 18.06 ? 468  TYR A CD1   1 
ATOM   3663 C  CD2   . TYR A 1 468 ? -8.395  -17.890 19.038  1.00 16.57 ? 468  TYR A CD2   1 
ATOM   3664 C  CE1   . TYR A 1 468 ? -5.976  -16.685 18.515  1.00 17.40 ? 468  TYR A CE1   1 
ATOM   3665 C  CE2   . TYR A 1 468 ? -8.369  -16.639 18.436  1.00 17.68 ? 468  TYR A CE2   1 
ATOM   3666 C  CZ    . TYR A 1 468 ? -7.151  -16.037 18.171  1.00 18.36 ? 468  TYR A CZ    1 
ATOM   3667 O  OH    . TYR A 1 468 ? -7.074  -14.838 17.540  1.00 16.95 ? 468  TYR A OH    1 
ATOM   3668 N  N     . ARG A 1 469 ? -7.164  -20.616 16.696  1.00 14.60 ? 469  ARG A N     1 
ATOM   3669 C  CA    . ARG A 1 469 ? -7.857  -20.405 15.399  1.00 15.44 ? 469  ARG A CA    1 
ATOM   3670 C  C     . ARG A 1 469 ? -6.925  -20.787 14.261  1.00 16.00 ? 469  ARG A C     1 
ATOM   3671 O  O     . ARG A 1 469 ? -5.755  -20.336 14.284  1.00 16.62 ? 469  ARG A O     1 
ATOM   3672 C  CB    . ARG A 1 469 ? -8.268  -18.938 15.270  1.00 16.04 ? 469  ARG A CB    1 
ATOM   3673 C  CG    . ARG A 1 469 ? -9.292  -18.683 14.185  1.00 16.67 ? 469  ARG A CG    1 
ATOM   3674 C  CD    . ARG A 1 469 ? -9.606  -17.204 14.058  1.00 17.82 ? 469  ARG A CD    1 
ATOM   3675 N  NE    . ARG A 1 469 ? -10.466 -16.856 12.909  1.00 18.23 ? 469  ARG A NE    1 
ATOM   3676 C  CZ    . ARG A 1 469 ? -10.722 -15.603 12.511  1.00 18.39 ? 469  ARG A CZ    1 
ATOM   3677 N  NH1   . ARG A 1 469 ? -10.216 -14.567 13.179  1.00 19.06 ? 469  ARG A NH1   1 
ATOM   3678 N  NH2   . ARG A 1 469 ? -11.487 -15.385 11.458  1.00 18.00 ? 469  ARG A NH2   1 
ATOM   3679 N  N     . THR A 1 470 ? -7.393  -21.539 13.271  1.00 16.15 ? 470  THR A N     1 
ATOM   3680 C  CA    . THR A 1 470 ? -6.479  -22.005 12.199  1.00 17.05 ? 470  THR A CA    1 
ATOM   3681 C  C     . THR A 1 470 ? -7.193  -22.195 10.854  1.00 18.23 ? 470  THR A C     1 
ATOM   3682 O  O     . THR A 1 470 ? -8.437  -22.255 10.794  1.00 18.04 ? 470  THR A O     1 
ATOM   3683 C  CB    . THR A 1 470 ? -5.788  -23.291 12.656  1.00 17.97 ? 470  THR A CB    1 
ATOM   3684 O  OG1   . THR A 1 470 ? -4.613  -23.483 11.863  1.00 18.14 ? 470  THR A OG1   1 
ATOM   3685 C  CG2   . THR A 1 470 ? -6.709  -24.499 12.619  1.00 18.10 ? 470  THR A CG2   1 
ATOM   3686 N  N     . HIS A 1 471 ? -6.375  -22.314 9.820   1.00 17.71 ? 471  HIS A N     1 
ATOM   3687 C  CA    . HIS A 1 471 ? -6.748  -22.552 8.408   1.00 18.23 ? 471  HIS A CA    1 
ATOM   3688 C  C     . HIS A 1 471 ? -7.337  -23.966 8.297   1.00 17.86 ? 471  HIS A C     1 
ATOM   3689 O  O     . HIS A 1 471 ? -6.962  -24.870 9.117   1.00 18.80 ? 471  HIS A O     1 
ATOM   3690 C  CB    . HIS A 1 471 ? -5.493  -22.285 7.554   1.00 17.66 ? 471  HIS A CB    1 
ATOM   3691 C  CG    . HIS A 1 471 ? -5.691  -22.346 6.083   1.00 18.10 ? 471  HIS A CG    1 
ATOM   3692 N  ND1   . HIS A 1 471 ? -5.974  -23.532 5.426   1.00 17.41 ? 471  HIS A ND1   1 
ATOM   3693 C  CD2   . HIS A 1 471 ? -5.571  -21.395 5.136   1.00 16.68 ? 471  HIS A CD2   1 
ATOM   3694 C  CE1   . HIS A 1 471 ? -6.031  -23.290 4.127   1.00 18.36 ? 471  HIS A CE1   1 
ATOM   3695 N  NE2   . HIS A 1 471 ? -5.776  -21.985 3.926   1.00 17.28 ? 471  HIS A NE2   1 
ATOM   3696 N  N     . ILE A 1 472 ? -8.248  -24.141 7.341   1.00 17.37 ? 472  ILE A N     1 
ATOM   3697 C  CA    . ILE A 1 472 ? -8.959  -25.422 7.073   1.00 17.47 ? 472  ILE A CA    1 
ATOM   3698 C  C     . ILE A 1 472 ? -7.938  -26.558 6.948   1.00 17.79 ? 472  ILE A C     1 
ATOM   3699 O  O     . ILE A 1 472 ? -8.238  -27.691 7.418   1.00 18.09 ? 472  ILE A O     1 
ATOM   3700 C  CB    . ILE A 1 472 ? -9.855  -25.286 5.822   1.00 18.04 ? 472  ILE A CB    1 
ATOM   3701 C  CG1   . ILE A 1 472 ? -9.064  -24.762 4.620   1.00 18.89 ? 472  ILE A CG1   1 
ATOM   3702 C  CG2   . ILE A 1 472 ? -11.066 -24.427 6.156   1.00 17.52 ? 472  ILE A CG2   1 
ATOM   3703 C  CD1   . ILE A 1 472 ? -9.886  -24.560 3.368   1.00 20.44 ? 472  ILE A CD1   1 
ATOM   3704 N  N     . ARG A 1 473 ? -6.757  -26.279 6.384   1.00 17.30 ? 473  ARG A N     1 
ATOM   3705 C  CA    . ARG A 1 473 ? -5.739  -27.318 6.128   1.00 18.09 ? 473  ARG A CA    1 
ATOM   3706 C  C     . ARG A 1 473 ? -5.159  -27.854 7.437   1.00 16.68 ? 473  ARG A C     1 
ATOM   3707 O  O     . ARG A 1 473 ? -4.704  -28.986 7.412   1.00 15.74 ? 473  ARG A O     1 
ATOM   3708 C  CB    . ARG A 1 473 ? -4.645  -26.753 5.226   1.00 20.97 ? 473  ARG A CB    1 
ATOM   3709 C  CG    . ARG A 1 473 ? -3.535  -27.745 4.911   1.00 22.45 ? 473  ARG A CG    1 
ATOM   3710 C  CD    . ARG A 1 473 ? -2.713  -27.264 3.747   1.00 24.61 ? 473  ARG A CD    1 
ATOM   3711 N  NE    . ARG A 1 473 ? -1.689  -28.228 3.418   1.00 25.82 ? 473  ARG A NE    1 
ATOM   3712 C  CZ    . ARG A 1 473 ? -1.883  -29.373 2.777   1.00 28.93 ? 473  ARG A CZ    1 
ATOM   3713 N  NH1   . ARG A 1 473 ? -3.085  -29.749 2.383   1.00 28.92 ? 473  ARG A NH1   1 
ATOM   3714 N  NH2   . ARG A 1 473 ? -0.856  -30.166 2.556   1.00 31.06 ? 473  ARG A NH2   1 
ATOM   3715 N  N     . TYR A 1 474 ? -5.166  -27.087 8.537   1.00 17.42 ? 474  TYR A N     1 
ATOM   3716 C  CA    . TYR A 1 474 ? -4.508  -27.482 9.820   1.00 16.99 ? 474  TYR A CA    1 
ATOM   3717 C  C     . TYR A 1 474 ? -5.509  -27.783 10.945  1.00 16.06 ? 474  TYR A C     1 
ATOM   3718 O  O     . TYR A 1 474 ? -5.094  -28.079 12.057  1.00 16.96 ? 474  TYR A O     1 
ATOM   3719 C  CB    . TYR A 1 474 ? -3.492  -26.404 10.201  1.00 17.67 ? 474  TYR A CB    1 
ATOM   3720 C  CG    . TYR A 1 474 ? -2.512  -26.123 9.085   1.00 18.52 ? 474  TYR A CG    1 
ATOM   3721 C  CD1   . TYR A 1 474 ? -1.602  -27.084 8.669   1.00 18.77 ? 474  TYR A CD1   1 
ATOM   3722 C  CD2   . TYR A 1 474 ? -2.509  -24.906 8.428   1.00 18.56 ? 474  TYR A CD2   1 
ATOM   3723 C  CE1   . TYR A 1 474 ? -0.710  -26.840 7.631   1.00 18.26 ? 474  TYR A CE1   1 
ATOM   3724 C  CE2   . TYR A 1 474 ? -1.637  -24.656 7.381   1.00 20.87 ? 474  TYR A CE2   1 
ATOM   3725 C  CZ    . TYR A 1 474 ? -0.722  -25.618 6.990   1.00 19.56 ? 474  TYR A CZ    1 
ATOM   3726 O  OH    . TYR A 1 474 ? 0.120   -25.343 5.943   1.00 24.21 ? 474  TYR A OH    1 
ATOM   3727 N  N     . MET A 1 475 ? -6.804  -27.802 10.666  1.00 16.17 ? 475  MET A N     1 
ATOM   3728 C  CA    . MET A 1 475 ? -7.851  -27.965 11.718  1.00 16.17 ? 475  MET A CA    1 
ATOM   3729 C  C     . MET A 1 475 ? -7.681  -29.316 12.437  1.00 17.54 ? 475  MET A C     1 
ATOM   3730 O  O     . MET A 1 475 ? -7.798  -29.338 13.689  1.00 16.33 ? 475  MET A O     1 
ATOM   3731 C  CB    . MET A 1 475 ? -9.248  -27.827 11.110  1.00 16.36 ? 475  MET A CB    1 
ATOM   3732 C  CG    . MET A 1 475 ? -9.575  -26.356 10.832  1.00 16.55 ? 475  MET A CG    1 
ATOM   3733 S  SD    . MET A 1 475 ? -11.205 -26.083 10.146  1.00 16.65 ? 475  MET A SD    1 
ATOM   3734 C  CE    . MET A 1 475 ? -11.222 -24.278 10.117  1.00 16.75 ? 475  MET A CE    1 
ATOM   3735 N  N     . ASP A 1 476 ? -7.396  -30.401 11.700  1.00 17.52 ? 476  ASP A N     1 
ATOM   3736 C  CA    . ASP A 1 476 ? -7.095  -31.731 12.307  1.00 19.23 ? 476  ASP A CA    1 
ATOM   3737 C  C     . ASP A 1 476 ? -5.810  -31.640 13.146  1.00 18.85 ? 476  ASP A C     1 
ATOM   3738 O  O     . ASP A 1 476 ? -5.801  -32.090 14.300  1.00 18.00 ? 476  ASP A O     1 
ATOM   3739 C  CB    . ASP A 1 476 ? -6.973  -32.841 11.251  1.00 20.29 ? 476  ASP A CB    1 
ATOM   3740 C  CG    . ASP A 1 476 ? -8.275  -33.566 10.949  1.00 24.09 ? 476  ASP A CG    1 
ATOM   3741 O  OD1   . ASP A 1 476 ? -9.365  -33.119 11.405  1.00 25.49 ? 476  ASP A OD1   1 
ATOM   3742 O  OD2   . ASP A 1 476 ? -8.213  -34.580 10.256  1.00 31.86 ? 476  ASP A OD2   1 
ATOM   3743 N  N     . ARG A 1 477 ? -4.766  -31.042 12.591  1.00 19.77 ? 477  ARG A N     1 
ATOM   3744 C  CA    . ARG A 1 477 ? -3.463  -30.928 13.264  1.00 20.77 ? 477  ARG A CA    1 
ATOM   3745 C  C     . ARG A 1 477 ? -3.628  -30.243 14.622  1.00 19.68 ? 477  ARG A C     1 
ATOM   3746 O  O     . ARG A 1 477 ? -3.075  -30.766 15.642  1.00 19.54 ? 477  ARG A O     1 
ATOM   3747 C  CB    . ARG A 1 477 ? -2.488  -30.163 12.383  1.00 25.28 ? 477  ARG A CB    1 
ATOM   3748 C  CG    . ARG A 1 477 ? -1.050  -30.306 12.859  1.00 31.87 ? 477  ARG A CG    1 
ATOM   3749 C  CD    . ARG A 1 477 ? -0.450  -31.619 12.366  1.00 39.17 ? 477  ARG A CD    1 
ATOM   3750 N  NE    . ARG A 1 477 ? 0.954   -31.376 12.064  1.00 48.57 ? 477  ARG A NE    1 
ATOM   3751 C  CZ    . ARG A 1 477 ? 1.908   -31.258 12.983  1.00 52.38 ? 477  ARG A CZ    1 
ATOM   3752 N  NH1   . ARG A 1 477 ? 1.622   -31.406 14.274  1.00 53.42 ? 477  ARG A NH1   1 
ATOM   3753 N  NH2   . ARG A 1 477 ? 3.149   -31.020 12.600  1.00 52.94 ? 477  ARG A NH2   1 
ATOM   3754 N  N     . ILE A 1 478 ? -4.335  -29.112 14.661  1.00 18.86 ? 478  ILE A N     1 
ATOM   3755 C  CA    . ILE A 1 478 ? -4.506  -28.325 15.918  1.00 16.63 ? 478  ILE A CA    1 
ATOM   3756 C  C     . ILE A 1 478 ? -5.332  -29.151 16.899  1.00 17.81 ? 478  ILE A C     1 
ATOM   3757 O  O     . ILE A 1 478 ? -4.961  -29.202 18.109  1.00 16.30 ? 478  ILE A O     1 
ATOM   3758 C  CB    . ILE A 1 478 ? -5.093  -26.935 15.623  1.00 16.56 ? 478  ILE A CB    1 
ATOM   3759 C  CG1   . ILE A 1 478 ? -4.140  -26.144 14.719  1.00 16.07 ? 478  ILE A CG1   1 
ATOM   3760 C  CG2   . ILE A 1 478 ? -5.391  -26.193 16.927  1.00 15.56 ? 478  ILE A CG2   1 
ATOM   3761 C  CD1   . ILE A 1 478 ? -2.701  -26.122 15.238  1.00 16.76 ? 478  ILE A CD1   1 
ATOM   3762 N  N     . ALA A 1 479 ? -6.392  -29.806 16.427  1.00 18.44 ? 479  ALA A N     1 
ATOM   3763 C  CA    . ALA A 1 479 ? -7.254  -30.625 17.320  1.00 19.54 ? 479  ALA A CA    1 
ATOM   3764 C  C     . ALA A 1 479 ? -6.406  -31.700 18.025  1.00 18.99 ? 479  ALA A C     1 
ATOM   3765 O  O     . ALA A 1 479 ? -6.608  -31.957 19.250  1.00 20.08 ? 479  ALA A O     1 
ATOM   3766 C  CB    . ALA A 1 479 ? -8.391  -31.273 16.549  1.00 19.94 ? 479  ALA A CB    1 
ATOM   3767 N  N     . LYS A 1 480 ? -5.470  -32.309 17.310  1.00 19.74 ? 480  LYS A N     1 
ATOM   3768 C  CA    . LYS A 1 480 ? -4.619  -33.407 17.851  1.00 20.32 ? 480  LYS A CA    1 
ATOM   3769 C  C     . LYS A 1 480 ? -3.644  -32.889 18.914  1.00 18.77 ? 480  LYS A C     1 
ATOM   3770 O  O     . LYS A 1 480 ? -3.279  -33.711 19.778  1.00 20.73 ? 480  LYS A O     1 
ATOM   3771 C  CB    . LYS A 1 480 ? -3.904  -34.130 16.711  1.00 23.57 ? 480  LYS A CB    1 
ATOM   3772 C  CG    . LYS A 1 480 ? -4.825  -35.020 15.887  1.00 27.46 ? 480  LYS A CG    1 
ATOM   3773 C  CD    . LYS A 1 480 ? -4.163  -35.473 14.603  1.00 34.13 ? 480  LYS A CD    1 
ATOM   3774 C  CE    . LYS A 1 480 ? -5.133  -35.865 13.508  1.00 40.76 ? 480  LYS A CE    1 
ATOM   3775 N  NZ    . LYS A 1 480 ? -5.125  -37.327 13.300  1.00 46.18 ? 480  LYS A NZ    1 
ATOM   3776 N  N     . THR A 1 481 ? -3.318  -31.594 18.960  1.00 18.13 ? 481  THR A N     1 
ATOM   3777 C  CA    . THR A 1 481 ? -2.488  -30.999 20.043  1.00 17.13 ? 481  THR A CA    1 
ATOM   3778 C  C     . THR A 1 481 ? -3.258  -30.964 21.371  1.00 18.34 ? 481  THR A C     1 
ATOM   3779 O  O     . THR A 1 481 ? -2.576  -30.920 22.418  1.00 17.11 ? 481  THR A O     1 
ATOM   3780 C  CB    . THR A 1 481 ? -1.968  -29.608 19.683  1.00 18.47 ? 481  THR A CB    1 
ATOM   3781 O  OG1   . THR A 1 481 ? -2.992  -28.608 19.623  1.00 16.53 ? 481  THR A OG1   1 
ATOM   3782 C  CG2   . THR A 1 481 ? -1.227  -29.647 18.367  1.00 19.15 ? 481  THR A CG2   1 
ATOM   3783 N  N     . TYR A 1 482 ? -4.601  -31.026 21.341  1.00 17.76 ? 482  TYR A N     1 
ATOM   3784 C  CA    . TYR A 1 482 ? -5.476  -30.938 22.545  1.00 19.04 ? 482  TYR A CA    1 
ATOM   3785 C  C     . TYR A 1 482 ? -5.783  -32.346 23.077  1.00 19.27 ? 482  TYR A C     1 
ATOM   3786 O  O     . TYR A 1 482 ? -6.964  -32.663 23.306  1.00 19.07 ? 482  TYR A O     1 
ATOM   3787 C  CB    . TYR A 1 482 ? -6.714  -30.088 22.236  1.00 18.79 ? 482  TYR A CB    1 
ATOM   3788 C  CG    . TYR A 1 482 ? -6.367  -28.634 22.094  1.00 19.32 ? 482  TYR A CG    1 
ATOM   3789 C  CD1   . TYR A 1 482 ? -6.112  -27.864 23.220  1.00 21.03 ? 482  TYR A CD1   1 
ATOM   3790 C  CD2   . TYR A 1 482 ? -6.188  -28.042 20.851  1.00 19.83 ? 482  TYR A CD2   1 
ATOM   3791 C  CE1   . TYR A 1 482 ? -5.740  -26.533 23.112  1.00 19.96 ? 482  TYR A CE1   1 
ATOM   3792 C  CE2   . TYR A 1 482 ? -5.785  -26.718 20.730  1.00 18.52 ? 482  TYR A CE2   1 
ATOM   3793 C  CZ    . TYR A 1 482 ? -5.566  -25.960 21.866  1.00 18.61 ? 482  TYR A CZ    1 
ATOM   3794 O  OH    . TYR A 1 482 ? -5.167  -24.654 21.790  1.00 18.19 ? 482  TYR A OH    1 
ATOM   3795 N  N     . SER A 1 483 ? -4.721  -33.102 23.379  1.00 19.04 ? 483  SER A N     1 
ATOM   3796 C  CA    . SER A 1 483 ? -4.709  -34.589 23.503  1.00 20.21 ? 483  SER A CA    1 
ATOM   3797 C  C     . SER A 1 483 ? -4.834  -35.065 24.956  1.00 20.02 ? 483  SER A C     1 
ATOM   3798 O  O     . SER A 1 483 ? -4.788  -36.279 25.186  1.00 19.27 ? 483  SER A O     1 
ATOM   3799 C  CB    . SER A 1 483 ? -3.434  -35.158 22.892  1.00 19.90 ? 483  SER A CB    1 
ATOM   3800 O  OG    . SER A 1 483 ? -2.294  -34.702 23.628  1.00 21.04 ? 483  SER A OG    1 
ATOM   3801 N  N     . TRP A 1 484 ? -5.029  -34.174 25.925  1.00 20.70 ? 484  TRP A N     1 
ATOM   3802 C  CA    . TRP A 1 484 ? -5.127  -34.572 27.354  1.00 20.91 ? 484  TRP A CA    1 
ATOM   3803 C  C     . TRP A 1 484 ? -6.079  -35.775 27.525  1.00 21.00 ? 484  TRP A C     1 
ATOM   3804 O  O     . TRP A 1 484 ? -7.188  -35.774 26.954  1.00 19.08 ? 484  TRP A O     1 
ATOM   3805 C  CB    . TRP A 1 484 ? -5.549  -33.396 28.242  1.00 21.69 ? 484  TRP A CB    1 
ATOM   3806 C  CG    . TRP A 1 484 ? -5.460  -33.735 29.697  1.00 20.73 ? 484  TRP A CG    1 
ATOM   3807 C  CD1   . TRP A 1 484 ? -4.314  -33.819 30.430  1.00 22.09 ? 484  TRP A CD1   1 
ATOM   3808 C  CD2   . TRP A 1 484 ? -6.527  -34.152 30.571  1.00 20.21 ? 484  TRP A CD2   1 
ATOM   3809 N  NE1   . TRP A 1 484 ? -4.595  -34.216 31.705  1.00 20.46 ? 484  TRP A NE1   1 
ATOM   3810 C  CE2   . TRP A 1 484 ? -5.941  -34.439 31.827  1.00 20.27 ? 484  TRP A CE2   1 
ATOM   3811 C  CE3   . TRP A 1 484 ? -7.911  -34.314 30.427  1.00 20.02 ? 484  TRP A CE3   1 
ATOM   3812 C  CZ2   . TRP A 1 484 ? -6.689  -34.853 32.935  1.00 19.13 ? 484  TRP A CZ2   1 
ATOM   3813 C  CZ3   . TRP A 1 484 ? -8.647  -34.735 31.513  1.00 19.04 ? 484  TRP A CZ3   1 
ATOM   3814 C  CH2   . TRP A 1 484 ? -8.042  -35.004 32.748  1.00 18.67 ? 484  TRP A CH2   1 
ATOM   3815 N  N     . ASN A 1 485 ? -5.665  -36.749 28.342  1.00 20.26 ? 485  ASN A N     1 
ATOM   3816 C  CA    . ASN A 1 485 ? -6.457  -37.955 28.678  1.00 20.48 ? 485  ASN A CA    1 
ATOM   3817 C  C     . ASN A 1 485 ? -6.918  -38.688 27.418  1.00 19.24 ? 485  ASN A C     1 
ATOM   3818 O  O     . ASN A 1 485 ? -8.121  -39.026 27.303  1.00 22.03 ? 485  ASN A O     1 
ATOM   3819 C  CB    . ASN A 1 485 ? -7.635  -37.583 29.575  1.00 21.67 ? 485  ASN A CB    1 
ATOM   3820 C  CG    . ASN A 1 485 ? -8.258  -38.836 30.096  1.00 22.04 ? 485  ASN A CG    1 
ATOM   3821 O  OD1   . ASN A 1 485 ? -7.577  -39.842 30.130  1.00 22.99 ? 485  ASN A OD1   1 
ATOM   3822 N  ND2   . ASN A 1 485 ? -9.538  -38.801 30.413  1.00 25.72 ? 485  ASN A ND2   1 
ATOM   3823 N  N     . ASP A 1 486 ? -5.995  -38.931 26.493  1.00 21.99 ? 486  ASP A N     1 
ATOM   3824 C  CA    . ASP A 1 486 ? -6.219  -39.671 25.220  1.00 24.14 ? 486  ASP A CA    1 
ATOM   3825 C  C     . ASP A 1 486 ? -7.347  -39.002 24.418  1.00 21.27 ? 486  ASP A C     1 
ATOM   3826 O  O     . ASP A 1 486 ? -8.294  -39.691 23.963  1.00 20.18 ? 486  ASP A O     1 
ATOM   3827 C  CB    . ASP A 1 486 ? -6.489  -41.162 25.479  1.00 28.08 ? 486  ASP A CB    1 
ATOM   3828 C  CG    . ASP A 1 486 ? -6.435  -41.968 24.184  1.00 37.20 ? 486  ASP A CG    1 
ATOM   3829 O  OD1   . ASP A 1 486 ? -5.622  -41.604 23.296  1.00 42.13 ? 486  ASP A OD1   1 
ATOM   3830 O  OD2   . ASP A 1 486 ? -7.236  -42.924 24.037  1.00 46.13 ? 486  ASP A OD2   1 
ATOM   3831 N  N     . ASN A 1 487 ? -7.249  -37.695 24.221  1.00 20.73 ? 487  ASN A N     1 
ATOM   3832 C  CA    . ASN A 1 487 ? -8.157  -36.942 23.307  1.00 21.18 ? 487  ASN A CA    1 
ATOM   3833 C  C     . ASN A 1 487 ? -9.590  -36.938 23.854  1.00 19.38 ? 487  ASN A C     1 
ATOM   3834 O  O     . ASN A 1 487 ? -10.518 -36.983 23.031  1.00 18.15 ? 487  ASN A O     1 
ATOM   3835 C  CB    . ASN A 1 487 ? -8.133  -37.525 21.882  1.00 20.80 ? 487  ASN A CB    1 
ATOM   3836 C  CG    . ASN A 1 487 ? -6.729  -37.539 21.308  1.00 22.19 ? 487  ASN A CG    1 
ATOM   3837 O  OD1   . ASN A 1 487 ? -6.070  -38.576 21.317  1.00 25.22 ? 487  ASN A OD1   1 
ATOM   3838 N  ND2   . ASN A 1 487 ? -6.222  -36.395 20.897  1.00 20.02 ? 487  ASN A ND2   1 
ATOM   3839 N  N     . ALA A 1 488 ? -9.748  -36.870 25.182  1.00 20.45 ? 488  ALA A N     1 
ATOM   3840 C  CA    . ALA A 1 488 ? -11.049 -36.855 25.906  1.00 20.04 ? 488  ALA A CA    1 
ATOM   3841 C  C     . ALA A 1 488 ? -11.944 -35.736 25.352  1.00 20.04 ? 488  ALA A C     1 
ATOM   3842 O  O     . ALA A 1 488 ? -13.141 -35.982 25.198  1.00 21.28 ? 488  ALA A O     1 
ATOM   3843 C  CB    . ALA A 1 488 ? -10.824 -36.657 27.387  1.00 19.35 ? 488  ALA A CB    1 
ATOM   3844 N  N     . LEU A 1 489 ? -11.393 -34.544 25.094  1.00 19.28 ? 489  LEU A N     1 
ATOM   3845 C  CA    . LEU A 1 489 ? -12.263 -33.393 24.736  1.00 19.78 ? 489  LEU A CA    1 
ATOM   3846 C  C     . LEU A 1 489 ? -12.882 -33.644 23.368  1.00 19.82 ? 489  LEU A C     1 
ATOM   3847 O  O     . LEU A 1 489 ? -14.119 -33.411 23.239  1.00 19.87 ? 489  LEU A O     1 
ATOM   3848 C  CB    . LEU A 1 489 ? -11.485 -32.072 24.760  1.00 20.24 ? 489  LEU A CB    1 
ATOM   3849 C  CG    . LEU A 1 489 ? -12.306 -30.806 24.483  1.00 18.12 ? 489  LEU A CG    1 
ATOM   3850 C  CD1   . LEU A 1 489 ? -13.499 -30.751 25.387  1.00 20.45 ? 489  LEU A CD1   1 
ATOM   3851 C  CD2   . LEU A 1 489 ? -11.467 -29.558 24.674  1.00 19.80 ? 489  LEU A CD2   1 
ATOM   3852 N  N     . TRP A 1 490 ? -12.065 -34.055 22.376  1.00 19.65 ? 490  TRP A N     1 
ATOM   3853 C  CA    . TRP A 1 490 ? -12.576 -34.331 21.014  1.00 19.25 ? 490  TRP A CA    1 
ATOM   3854 C  C     . TRP A 1 490 ? -13.529 -35.533 21.036  1.00 19.33 ? 490  TRP A C     1 
ATOM   3855 O  O     . TRP A 1 490 ? -14.439 -35.546 20.215  1.00 18.07 ? 490  TRP A O     1 
ATOM   3856 C  CB    . TRP A 1 490 ? -11.474 -34.425 19.935  1.00 19.15 ? 490  TRP A CB    1 
ATOM   3857 C  CG    . TRP A 1 490 ? -11.419 -33.135 19.182  1.00 19.42 ? 490  TRP A CG    1 
ATOM   3858 C  CD1   . TRP A 1 490 ? -11.808 -32.912 17.892  1.00 20.01 ? 490  TRP A CD1   1 
ATOM   3859 C  CD2   . TRP A 1 490 ? -11.090 -31.841 19.734  1.00 19.69 ? 490  TRP A CD2   1 
ATOM   3860 N  NE1   . TRP A 1 490 ? -11.687 -31.579 17.585  1.00 19.02 ? 490  TRP A NE1   1 
ATOM   3861 C  CE2   . TRP A 1 490 ? -11.249 -30.899 18.689  1.00 19.31 ? 490  TRP A CE2   1 
ATOM   3862 C  CE3   . TRP A 1 490 ? -10.592 -31.403 20.976  1.00 18.78 ? 490  TRP A CE3   1 
ATOM   3863 C  CZ2   . TRP A 1 490 ? -10.980 -29.544 18.860  1.00 19.57 ? 490  TRP A CZ2   1 
ATOM   3864 C  CZ3   . TRP A 1 490 ? -10.371 -30.052 21.153  1.00 20.07 ? 490  TRP A CZ3   1 
ATOM   3865 C  CH2   . TRP A 1 490 ? -10.535 -29.141 20.103  1.00 19.56 ? 490  TRP A CH2   1 
ATOM   3866 N  N     . LYS A 1 491 ? -13.376 -36.481 21.958  1.00 19.84 ? 491  LYS A N     1 
ATOM   3867 C  CA    . LYS A 1 491 ? -14.347 -37.596 22.089  1.00 21.58 ? 491  LYS A CA    1 
ATOM   3868 C  C     . LYS A 1 491 ? -15.697 -37.007 22.516  1.00 20.50 ? 491  LYS A C     1 
ATOM   3869 O  O     . LYS A 1 491 ? -16.745 -37.449 22.016  1.00 18.00 ? 491  LYS A O     1 
ATOM   3870 C  CB    . LYS A 1 491 ? -13.812 -38.657 23.059  1.00 22.64 ? 491  LYS A CB    1 
ATOM   3871 C  CG    . LYS A 1 491 ? -12.605 -39.425 22.530  1.00 22.43 ? 491  LYS A CG    1 
ATOM   3872 C  CD    . LYS A 1 491 ? -12.118 -40.497 23.471  1.00 24.09 ? 491  LYS A CD    1 
ATOM   3873 C  CE    . LYS A 1 491 ? -10.932 -41.260 22.898  1.00 26.76 ? 491  LYS A CE    1 
ATOM   3874 N  NZ    . LYS A 1 491 ? -10.147 -41.896 23.983  1.00 27.93 ? 491  LYS A NZ    1 
ATOM   3875 N  N     . MET A 1 492 ? -15.684 -35.988 23.368  1.00 18.94 ? 492  MET A N     1 
ATOM   3876 C  CA    . MET A 1 492 ? -16.967 -35.387 23.816  1.00 19.58 ? 492  MET A CA    1 
ATOM   3877 C  C     . MET A 1 492 ? -17.578 -34.579 22.660  1.00 17.84 ? 492  MET A C     1 
ATOM   3878 O  O     . MET A 1 492 ? -18.762 -34.694 22.430  1.00 18.46 ? 492  MET A O     1 
ATOM   3879 C  CB    . MET A 1 492 ? -16.773 -34.531 25.063  1.00 19.49 ? 492  MET A CB    1 
ATOM   3880 C  CG    . MET A 1 492 ? -18.092 -34.085 25.631  1.00 22.46 ? 492  MET A CG    1 
ATOM   3881 S  SD    . MET A 1 492 ? -17.872 -32.832 26.893  1.00 23.16 ? 492  MET A SD    1 
ATOM   3882 C  CE    . MET A 1 492 ? -17.517 -31.439 25.834  1.00 22.91 ? 492  MET A CE    1 
ATOM   3883 N  N     . HIS A 1 493 ? -16.792 -33.813 21.923  1.00 17.99 ? 493  HIS A N     1 
ATOM   3884 C  CA    . HIS A 1 493 ? -17.285 -33.060 20.743  1.00 17.57 ? 493  HIS A CA    1 
ATOM   3885 C  C     . HIS A 1 493 ? -17.900 -34.042 19.751  1.00 17.72 ? 493  HIS A C     1 
ATOM   3886 O  O     . HIS A 1 493 ? -18.923 -33.703 19.185  1.00 18.20 ? 493  HIS A O     1 
ATOM   3887 C  CB    . HIS A 1 493 ? -16.174 -32.273 20.039  1.00 17.74 ? 493  HIS A CB    1 
ATOM   3888 C  CG    . HIS A 1 493 ? -15.661 -31.102 20.793  1.00 17.34 ? 493  HIS A CG    1 
ATOM   3889 N  ND1   . HIS A 1 493 ? -16.437 -30.389 21.655  1.00 17.92 ? 493  HIS A ND1   1 
ATOM   3890 C  CD2   . HIS A 1 493 ? -14.443 -30.541 20.822  1.00 18.53 ? 493  HIS A CD2   1 
ATOM   3891 C  CE1   . HIS A 1 493 ? -15.735 -29.422 22.189  1.00 17.50 ? 493  HIS A CE1   1 
ATOM   3892 N  NE2   . HIS A 1 493 ? -14.499 -29.486 21.682  1.00 18.48 ? 493  HIS A NE2   1 
ATOM   3893 N  N     . GLU A 1 494 ? -17.309 -35.230 19.592  1.00 20.35 ? 494  GLU A N     1 
ATOM   3894 C  CA    . GLU A 1 494 ? -17.783 -36.286 18.652  1.00 20.95 ? 494  GLU A CA    1 
ATOM   3895 C  C     . GLU A 1 494 ? -19.149 -36.832 19.124  1.00 21.67 ? 494  GLU A C     1 
ATOM   3896 O  O     . GLU A 1 494 ? -20.053 -37.100 18.263  1.00 19.98 ? 494  GLU A O     1 
ATOM   3897 C  CB    . GLU A 1 494 ? -16.706 -37.366 18.481  1.00 22.72 ? 494  GLU A CB    1 
ATOM   3898 C  CG    . GLU A 1 494 ? -15.459 -36.919 17.701  1.00 26.27 ? 494  GLU A CG    1 
ATOM   3899 C  CD    . GLU A 1 494 ? -14.146 -37.709 17.880  1.00 34.62 ? 494  GLU A CD    1 
ATOM   3900 O  OE1   . GLU A 1 494 ? -13.082 -37.218 17.405  1.00 40.39 ? 494  GLU A OE1   1 
ATOM   3901 O  OE2   . GLU A 1 494 ? -14.167 -38.827 18.455  1.00 40.69 ? 494  GLU A OE2   1 
ATOM   3902 N  N     . THR A 1 495 ? -19.325 -37.026 20.430  1.00 20.82 ? 495  THR A N     1 
ATOM   3903 C  CA    . THR A 1 495 ? -20.597 -37.498 21.009  1.00 20.74 ? 495  THR A CA    1 
ATOM   3904 C  C     . THR A 1 495 ? -21.682 -36.467 20.690  1.00 21.54 ? 495  THR A C     1 
ATOM   3905 O  O     . THR A 1 495 ? -22.756 -36.866 20.282  1.00 20.46 ? 495  THR A O     1 
ATOM   3906 C  CB    . THR A 1 495 ? -20.451 -37.673 22.518  1.00 21.87 ? 495  THR A CB    1 
ATOM   3907 O  OG1   . THR A 1 495 ? -19.407 -38.619 22.672  1.00 19.89 ? 495  THR A OG1   1 
ATOM   3908 C  CG2   . THR A 1 495 ? -21.717 -38.127 23.202  1.00 22.41 ? 495  THR A CG2   1 
ATOM   3909 N  N     . ILE A 1 496 ? -21.388 -35.172 20.854  1.00 22.16 ? 496  ILE A N     1 
ATOM   3910 C  CA    . ILE A 1 496 ? -22.373 -34.078 20.628  1.00 20.68 ? 496  ILE A CA    1 
ATOM   3911 C  C     . ILE A 1 496 ? -22.672 -33.967 19.132  1.00 21.21 ? 496  ILE A C     1 
ATOM   3912 O  O     . ILE A 1 496 ? -23.866 -33.814 18.780  1.00 22.03 ? 496  ILE A O     1 
ATOM   3913 C  CB    . ILE A 1 496 ? -21.877 -32.769 21.261  1.00 22.46 ? 496  ILE A CB    1 
ATOM   3914 C  CG1   . ILE A 1 496 ? -21.727 -32.922 22.781  1.00 23.43 ? 496  ILE A CG1   1 
ATOM   3915 C  CG2   . ILE A 1 496 ? -22.776 -31.608 20.885  1.00 22.83 ? 496  ILE A CG2   1 
ATOM   3916 C  CD1   . ILE A 1 496 ? -21.180 -31.713 23.458  1.00 23.91 ? 496  ILE A CD1   1 
ATOM   3917 N  N     . LYS A 1 497 ? -21.645 -34.041 18.274  1.00 21.06 ? 497  LYS A N     1 
ATOM   3918 C  CA    . LYS A 1 497 ? -21.827 -34.017 16.804  1.00 19.05 ? 497  LYS A CA    1 
ATOM   3919 C  C     . LYS A 1 497 ? -22.780 -35.144 16.380  1.00 19.35 ? 497  LYS A C     1 
ATOM   3920 O  O     . LYS A 1 497 ? -23.643 -34.922 15.514  1.00 19.41 ? 497  LYS A O     1 
ATOM   3921 C  CB    . LYS A 1 497 ? -20.466 -34.217 16.143  1.00 19.62 ? 497  LYS A CB    1 
ATOM   3922 C  CG    . LYS A 1 497 ? -20.476 -34.324 14.635  1.00 19.64 ? 497  LYS A CG    1 
ATOM   3923 C  CD    . LYS A 1 497 ? -21.002 -33.089 13.989  1.00 20.23 ? 497  LYS A CD    1 
ATOM   3924 C  CE    . LYS A 1 497 ? -20.631 -33.011 12.526  1.00 20.62 ? 497  LYS A CE    1 
ATOM   3925 N  NZ    . LYS A 1 497 ? -21.238 -31.826 11.887  1.00 19.13 ? 497  LYS A NZ    1 
ATOM   3926 N  N     . ASP A 1 498 ? -22.568 -36.355 16.896  1.00 19.88 ? 498  ASP A N     1 
ATOM   3927 C  CA    . ASP A 1 498 ? -23.354 -37.546 16.460  1.00 21.41 ? 498  ASP A CA    1 
ATOM   3928 C  C     . ASP A 1 498 ? -24.811 -37.373 16.924  1.00 21.47 ? 498  ASP A C     1 
ATOM   3929 O  O     . ASP A 1 498 ? -25.701 -37.697 16.139  1.00 20.07 ? 498  ASP A O     1 
ATOM   3930 C  CB    . ASP A 1 498 ? -22.704 -38.844 16.931  1.00 21.20 ? 498  ASP A CB    1 
ATOM   3931 C  CG    . ASP A 1 498 ? -21.424 -39.228 16.190  1.00 23.09 ? 498  ASP A CG    1 
ATOM   3932 O  OD1   . ASP A 1 498 ? -21.164 -38.696 15.052  1.00 24.46 ? 498  ASP A OD1   1 
ATOM   3933 O  OD2   . ASP A 1 498 ? -20.652 -40.028 16.769  1.00 22.89 ? 498  ASP A OD2   1 
ATOM   3934 N  N     . ALA A 1 499 ? -25.030 -36.768 18.104  1.00 21.33 ? 499  ALA A N     1 
ATOM   3935 C  CA    . ALA A 1 499 ? -26.377 -36.449 18.640  1.00 20.78 ? 499  ALA A CA    1 
ATOM   3936 C  C     . ALA A 1 499 ? -27.086 -35.395 17.775  1.00 21.44 ? 499  ALA A C     1 
ATOM   3937 O  O     . ALA A 1 499 ? -28.249 -35.608 17.427  1.00 22.52 ? 499  ALA A O     1 
ATOM   3938 C  CB    . ALA A 1 499 ? -26.279 -36.013 20.074  1.00 20.30 ? 499  ALA A CB    1 
ATOM   3939 N  N     . LEU A 1 500 ? -26.443 -34.277 17.435  1.00 21.82 ? 500  LEU A N     1 
ATOM   3940 C  CA    . LEU A 1 500 ? -27.144 -33.164 16.743  1.00 22.92 ? 500  LEU A CA    1 
ATOM   3941 C  C     . LEU A 1 500 ? -27.198 -33.420 15.229  1.00 22.96 ? 500  LEU A C     1 
ATOM   3942 O  O     . LEU A 1 500 ? -28.179 -32.988 14.604  1.00 23.68 ? 500  LEU A O     1 
ATOM   3943 C  CB    . LEU A 1 500 ? -26.438 -31.848 17.065  1.00 23.31 ? 500  LEU A CB    1 
ATOM   3944 C  CG    . LEU A 1 500 ? -26.464 -31.457 18.535  1.00 23.44 ? 500  LEU A CG    1 
ATOM   3945 C  CD1   . LEU A 1 500 ? -25.560 -30.260 18.785  1.00 25.90 ? 500  LEU A CD1   1 
ATOM   3946 C  CD2   . LEU A 1 500 ? -27.884 -31.152 18.955  1.00 24.37 ? 500  LEU A CD2   1 
ATOM   3947 N  N     . ASP A 1 501 ? -26.173 -34.074 14.677  1.00 22.79 ? 501  ASP A N     1 
ATOM   3948 C  CA    . ASP A 1 501 ? -25.946 -34.254 13.222  1.00 23.57 ? 501  ASP A CA    1 
ATOM   3949 C  C     . ASP A 1 501 ? -25.673 -35.720 12.925  1.00 24.60 ? 501  ASP A C     1 
ATOM   3950 O  O     . ASP A 1 501 ? -24.587 -36.055 12.457  1.00 24.44 ? 501  ASP A O     1 
ATOM   3951 C  CB    . ASP A 1 501 ? -24.780 -33.375 12.756  1.00 22.89 ? 501  ASP A CB    1 
ATOM   3952 C  CG    . ASP A 1 501 ? -24.631 -33.273 11.252  1.00 21.64 ? 501  ASP A CG    1 
ATOM   3953 O  OD1   . ASP A 1 501 ? -25.498 -33.798 10.533  1.00 20.29 ? 501  ASP A OD1   1 
ATOM   3954 O  OD2   . ASP A 1 501 ? -23.600 -32.703 10.814  1.00 22.03 ? 501  ASP A OD2   1 
ATOM   3955 N  N     . PRO A 1 502 ? -26.647 -36.633 13.153  1.00 26.33 ? 502  PRO A N     1 
ATOM   3956 C  CA    . PRO A 1 502 ? -26.429 -38.060 12.906  1.00 27.88 ? 502  PRO A CA    1 
ATOM   3957 C  C     . PRO A 1 502 ? -26.024 -38.392 11.460  1.00 25.24 ? 502  PRO A C     1 
ATOM   3958 O  O     . PRO A 1 502 ? -25.192 -39.240 11.316  1.00 23.44 ? 502  PRO A O     1 
ATOM   3959 C  CB    . PRO A 1 502 ? -27.761 -38.737 13.313  1.00 29.14 ? 502  PRO A CB    1 
ATOM   3960 C  CG    . PRO A 1 502 ? -28.772 -37.599 13.354  1.00 27.26 ? 502  PRO A CG    1 
ATOM   3961 C  CD    . PRO A 1 502 ? -27.981 -36.355 13.701  1.00 26.19 ? 502  PRO A CD    1 
ATOM   3962 N  N     . ASN A 1 503 ? -26.493 -37.642 10.454  1.00 26.56 ? 503  ASN A N     1 
ATOM   3963 C  CA    . ASN A 1 503 ? -26.077 -37.856 9.035   1.00 25.83 ? 503  ASN A CA    1 
ATOM   3964 C  C     . ASN A 1 503 ? -24.791 -37.108 8.658   1.00 26.65 ? 503  ASN A C     1 
ATOM   3965 O  O     . ASN A 1 503 ? -24.357 -37.301 7.519   1.00 22.43 ? 503  ASN A O     1 
ATOM   3966 C  CB    . ASN A 1 503 ? -27.182 -37.483 8.056   1.00 28.13 ? 503  ASN A CB    1 
ATOM   3967 C  CG    . ASN A 1 503 ? -28.431 -38.294 8.333   1.00 28.12 ? 503  ASN A CG    1 
ATOM   3968 O  OD1   . ASN A 1 503 ? -28.348 -39.492 8.598   1.00 29.38 ? 503  ASN A OD1   1 
ATOM   3969 N  ND2   . ASN A 1 503 ? -29.576 -37.646 8.332   1.00 24.23 ? 503  ASN A ND2   1 
ATOM   3970 N  N     . GLY A 1 504 ? -24.189 -36.297 9.545   1.00 23.25 ? 504  GLY A N     1 
ATOM   3971 C  CA    . GLY A 1 504 ? -22.888 -35.673 9.254   1.00 22.83 ? 504  GLY A CA    1 
ATOM   3972 C  C     . GLY A 1 504 ? -22.955 -34.731 8.064   1.00 24.64 ? 504  GLY A C     1 
ATOM   3973 O  O     . GLY A 1 504 ? -22.010 -34.741 7.247   1.00 27.06 ? 504  GLY A O     1 
ATOM   3974 N  N     . ILE A 1 505 ? -23.999 -33.909 7.942   1.00 22.83 ? 505  ILE A N     1 
ATOM   3975 C  CA    . ILE A 1 505 ? -24.111 -33.028 6.741   1.00 23.89 ? 505  ILE A CA    1 
ATOM   3976 C  C     . ILE A 1 505 ? -23.625 -31.581 7.008   1.00 23.89 ? 505  ILE A C     1 
ATOM   3977 O  O     . ILE A 1 505 ? -23.566 -30.807 6.028   1.00 23.11 ? 505  ILE A O     1 
ATOM   3978 C  CB    . ILE A 1 505 ? -25.513 -33.143 6.091   1.00 28.18 ? 505  ILE A CB    1 
ATOM   3979 C  CG1   . ILE A 1 505 ? -26.689 -32.864 7.022   1.00 27.78 ? 505  ILE A CG1   1 
ATOM   3980 C  CG2   . ILE A 1 505 ? -25.655 -34.532 5.473   1.00 29.41 ? 505  ILE A CG2   1 
ATOM   3981 C  CD1   . ILE A 1 505 ? -26.707 -31.474 7.583   1.00 28.30 ? 505  ILE A CD1   1 
ATOM   3982 N  N     . LEU A 1 506 ? -23.243 -31.200 8.236   1.00 20.29 ? 506  LEU A N     1 
ATOM   3983 C  CA    . LEU A 1 506 ? -22.663 -29.844 8.464   1.00 21.04 ? 506  LEU A CA    1 
ATOM   3984 C  C     . LEU A 1 506 ? -21.128 -29.914 8.584   1.00 19.27 ? 506  LEU A C     1 
ATOM   3985 O  O     . LEU A 1 506 ? -20.609 -30.630 9.519   1.00 16.79 ? 506  LEU A O     1 
ATOM   3986 C  CB    . LEU A 1 506 ? -23.261 -29.203 9.719   1.00 20.42 ? 506  LEU A CB    1 
ATOM   3987 C  CG    . LEU A 1 506 ? -24.744 -28.882 9.691   1.00 22.56 ? 506  LEU A CG    1 
ATOM   3988 C  CD1   . LEU A 1 506 ? -25.128 -28.031 10.898  1.00 24.28 ? 506  LEU A CD1   1 
ATOM   3989 C  CD2   . LEU A 1 506 ? -25.181 -28.202 8.398   1.00 24.65 ? 506  LEU A CD2   1 
ATOM   3990 N  N     . ALA A 1 507 ? -20.459 -29.195 7.678   1.00 17.53 ? 507  ALA A N     1 
ATOM   3991 C  CA    . ALA A 1 507 ? -19.027 -28.798 7.702   1.00 18.47 ? 507  ALA A CA    1 
ATOM   3992 C  C     . ALA A 1 507 ? -18.147 -29.901 8.277   1.00 19.31 ? 507  ALA A C     1 
ATOM   3993 O  O     . ALA A 1 507 ? -17.487 -29.718 9.290   1.00 17.98 ? 507  ALA A O     1 
ATOM   3994 C  CB    . ALA A 1 507 ? -18.872 -27.522 8.486   1.00 18.34 ? 507  ALA A CB    1 
ATOM   3995 N  N     . PRO A 1 508 ? -18.095 -31.089 7.635   1.00 21.38 ? 508  PRO A N     1 
ATOM   3996 C  CA    . PRO A 1 508 ? -17.150 -32.130 8.037   1.00 20.59 ? 508  PRO A CA    1 
ATOM   3997 C  C     . PRO A 1 508 ? -15.708 -31.594 8.145   1.00 20.56 ? 508  PRO A C     1 
ATOM   3998 O  O     . PRO A 1 508 ? -15.195 -30.957 7.227   1.00 18.47 ? 508  PRO A O     1 
ATOM   3999 C  CB    . PRO A 1 508 ? -17.270 -33.208 6.947   1.00 22.41 ? 508  PRO A CB    1 
ATOM   4000 C  CG    . PRO A 1 508 ? -18.592 -32.945 6.240   1.00 22.37 ? 508  PRO A CG    1 
ATOM   4001 C  CD    . PRO A 1 508 ? -18.925 -31.479 6.479   1.00 22.45 ? 508  PRO A CD    1 
ATOM   4002 N  N     . GLY A 1 509 ? -15.110 -31.833 9.314   1.00 19.76 ? 509  GLY A N     1 
ATOM   4003 C  CA    . GLY A 1 509 ? -13.722 -31.513 9.640   1.00 19.44 ? 509  GLY A CA    1 
ATOM   4004 C  C     . GLY A 1 509 ? -13.556 -30.135 10.253  1.00 18.72 ? 509  GLY A C     1 
ATOM   4005 O  O     . GLY A 1 509 ? -12.440 -29.823 10.619  1.00 18.11 ? 509  GLY A O     1 
ATOM   4006 N  N     . LYS A 1 510 ? -14.611 -29.324 10.366  1.00 18.51 ? 510  LYS A N     1 
ATOM   4007 C  CA    . LYS A 1 510 ? -14.488 -28.029 11.076  1.00 17.82 ? 510  LYS A CA    1 
ATOM   4008 C  C     . LYS A 1 510 ? -13.965 -28.302 12.502  1.00 17.97 ? 510  LYS A C     1 
ATOM   4009 O  O     . LYS A 1 510 ? -14.529 -29.163 13.219  1.00 17.15 ? 510  LYS A O     1 
ATOM   4010 C  CB    . LYS A 1 510 ? -15.820 -27.269 11.116  1.00 17.85 ? 510  LYS A CB    1 
ATOM   4011 C  CG    . LYS A 1 510 ? -15.785 -25.966 11.903  1.00 15.79 ? 510  LYS A CG    1 
ATOM   4012 C  CD    . LYS A 1 510 ? -14.822 -24.927 11.408  1.00 16.04 ? 510  LYS A CD    1 
ATOM   4013 C  CE    . LYS A 1 510 ? -14.988 -23.576 12.119  1.00 16.96 ? 510  LYS A CE    1 
ATOM   4014 N  NZ    . LYS A 1 510 ? -13.790 -22.687 11.979  1.00 17.78 ? 510  LYS A NZ    1 
ATOM   4015 N  N     . SER A 1 511 ? -12.904 -27.598 12.894  1.00 17.37 ? 511  SER A N     1 
ATOM   4016 C  CA    . SER A 1 511 ? -12.265 -27.718 14.227  1.00 18.28 ? 511  SER A CA    1 
ATOM   4017 C  C     . SER A 1 511 ? -11.805 -29.168 14.479  1.00 17.96 ? 511  SER A C     1 
ATOM   4018 O  O     . SER A 1 511 ? -11.717 -29.569 15.644  1.00 20.97 ? 511  SER A O     1 
ATOM   4019 C  CB    . SER A 1 511 ? -13.211 -27.211 15.299  1.00 18.10 ? 511  SER A CB    1 
ATOM   4020 O  OG    . SER A 1 511 ? -13.436 -25.822 15.156  1.00 19.28 ? 511  SER A OG    1 
ATOM   4021 N  N     . GLY A 1 512 ? -11.526 -29.940 13.436  1.00 17.04 ? 512  GLY A N     1 
ATOM   4022 C  CA    . GLY A 1 512 ? -11.148 -31.362 13.581  1.00 17.57 ? 512  GLY A CA    1 
ATOM   4023 C  C     . GLY A 1 512 ? -12.297 -32.248 14.030  1.00 18.39 ? 512  GLY A C     1 
ATOM   4024 O  O     . GLY A 1 512 ? -12.024 -33.347 14.489  1.00 19.25 ? 512  GLY A O     1 
ATOM   4025 N  N     . ILE A 1 513 ? -13.551 -31.801 13.911  1.00 18.53 ? 513  ILE A N     1 
ATOM   4026 C  CA    . ILE A 1 513 ? -14.745 -32.602 14.310  1.00 17.77 ? 513  ILE A CA    1 
ATOM   4027 C  C     . ILE A 1 513 ? -15.334 -33.264 13.066  1.00 20.30 ? 513  ILE A C     1 
ATOM   4028 O  O     . ILE A 1 513 ? -15.803 -32.557 12.125  1.00 19.75 ? 513  ILE A O     1 
ATOM   4029 C  CB    . ILE A 1 513 ? -15.795 -31.767 15.066  1.00 17.32 ? 513  ILE A CB    1 
ATOM   4030 C  CG1   . ILE A 1 513 ? -15.182 -31.104 16.299  1.00 16.85 ? 513  ILE A CG1   1 
ATOM   4031 C  CG2   . ILE A 1 513 ? -16.991 -32.636 15.428  1.00 17.08 ? 513  ILE A CG2   1 
ATOM   4032 C  CD1   . ILE A 1 513 ? -16.011 -29.990 16.914  1.00 17.54 ? 513  ILE A CD1   1 
ATOM   4033 N  N     . TRP A 1 514 ? -15.336 -34.599 13.087  1.00 21.24 ? 514  TRP A N     1 
ATOM   4034 C  CA    . TRP A 1 514 ? -15.896 -35.454 12.017  1.00 23.12 ? 514  TRP A CA    1 
ATOM   4035 C  C     . TRP A 1 514 ? -16.933 -36.376 12.653  1.00 25.16 ? 514  TRP A C     1 
ATOM   4036 O  O     . TRP A 1 514 ? -16.640 -36.956 13.726  1.00 29.60 ? 514  TRP A O     1 
ATOM   4037 C  CB    . TRP A 1 514 ? -14.782 -36.288 11.389  1.00 21.53 ? 514  TRP A CB    1 
ATOM   4038 C  CG    . TRP A 1 514 ? -13.680 -35.524 10.742  1.00 20.57 ? 514  TRP A CG    1 
ATOM   4039 C  CD1   . TRP A 1 514 ? -12.518 -35.106 11.329  1.00 19.88 ? 514  TRP A CD1   1 
ATOM   4040 C  CD2   . TRP A 1 514 ? -13.587 -35.188 9.351   1.00 19.02 ? 514  TRP A CD2   1 
ATOM   4041 N  NE1   . TRP A 1 514 ? -11.723 -34.517 10.384  1.00 21.31 ? 514  TRP A NE1   1 
ATOM   4042 C  CE2   . TRP A 1 514 ? -12.352 -34.546 9.168   1.00 20.05 ? 514  TRP A CE2   1 
ATOM   4043 C  CE3   . TRP A 1 514 ? -14.416 -35.373 8.242   1.00 21.93 ? 514  TRP A CE3   1 
ATOM   4044 C  CZ2   . TRP A 1 514 ? -11.923 -34.084 7.923   1.00 22.52 ? 514  TRP A CZ2   1 
ATOM   4045 C  CZ3   . TRP A 1 514 ? -14.006 -34.901 7.016   1.00 20.97 ? 514  TRP A CZ3   1 
ATOM   4046 C  CH2   . TRP A 1 514 ? -12.772 -34.261 6.859   1.00 22.35 ? 514  TRP A CH2   1 
ATOM   4047 N  N     . GLY A 1 515 ? -18.089 -36.534 12.050  1.00 26.89 ? 515  GLY A N     1 
ATOM   4048 C  CA    . GLY A 1 515 ? -19.102 -37.440 12.635  1.00 26.95 ? 515  GLY A CA    1 
ATOM   4049 C  C     . GLY A 1 515 ? -18.784 -38.917 12.394  1.00 25.55 ? 515  GLY A C     1 
ATOM   4050 O  O     . GLY A 1 515 ? -17.781 -39.230 11.717  1.00 20.57 ? 515  GLY A O     1 
ATOM   4051 N  N     . LYS A 1 516 ? -19.628 -39.787 12.943  1.00 28.13 ? 516  LYS A N     1 
ATOM   4052 C  CA    . LYS A 1 516 ? -19.426 -41.262 12.971  1.00 30.78 ? 516  LYS A CA    1 
ATOM   4053 C  C     . LYS A 1 516 ? -19.322 -41.817 11.545  1.00 28.78 ? 516  LYS A C     1 
ATOM   4054 O  O     . LYS A 1 516 ? -18.538 -42.743 11.342  1.00 32.36 ? 516  LYS A O     1 
ATOM   4055 C  CB    . LYS A 1 516 ? -20.549 -41.952 13.750  1.00 36.05 ? 516  LYS A CB    1 
ATOM   4056 C  CG    . LYS A 1 516 ? -21.967 -41.798 13.204  1.00 45.34 ? 516  LYS A CG    1 
ATOM   4057 C  CD    . LYS A 1 516 ? -22.992 -42.549 14.070  1.00 51.29 ? 516  LYS A CD    1 
ATOM   4058 C  CE    . LYS A 1 516 ? -24.363 -41.902 14.144  1.00 54.48 ? 516  LYS A CE    1 
ATOM   4059 N  NZ    . LYS A 1 516 ? -25.053 -41.952 12.836  1.00 54.59 ? 516  LYS A NZ    1 
ATOM   4060 N  N     . ASN A 1 517 ? -20.014 -41.243 10.573  1.00 27.63 ? 517  ASN A N     1 
ATOM   4061 C  CA    . ASN A 1 517 ? -19.979 -41.740 9.178   1.00 29.92 ? 517  ASN A CA    1 
ATOM   4062 C  C     . ASN A 1 517 ? -18.603 -41.513 8.539   1.00 32.62 ? 517  ASN A C     1 
ATOM   4063 O  O     . ASN A 1 517 ? -18.289 -42.252 7.583   1.00 33.61 ? 517  ASN A O     1 
ATOM   4064 C  CB    . ASN A 1 517 ? -21.049 -41.088 8.314   1.00 31.36 ? 517  ASN A CB    1 
ATOM   4065 C  CG    . ASN A 1 517 ? -22.457 -41.517 8.677   1.00 36.07 ? 517  ASN A CG    1 
ATOM   4066 O  OD1   . ASN A 1 517 ? -22.649 -42.511 9.369   1.00 37.72 ? 517  ASN A OD1   1 
ATOM   4067 N  ND2   . ASN A 1 517 ? -23.452 -40.783 8.196   1.00 34.79 ? 517  ASN A ND2   1 
ATOM   4068 N  N     . ARG A 1 518 ? -17.817 -40.517 8.980   1.00 31.95 ? 518  ARG A N     1 
ATOM   4069 C  CA    . ARG A 1 518 ? -16.529 -40.190 8.312   1.00 28.95 ? 518  ARG A CA    1 
ATOM   4070 C  C     . ARG A 1 518 ? -15.320 -40.460 9.218   1.00 31.74 ? 518  ARG A C     1 
ATOM   4071 O  O     . ARG A 1 518 ? -14.222 -40.462 8.688   1.00 39.60 ? 518  ARG A O     1 
ATOM   4072 C  CB    . ARG A 1 518 ? -16.588 -38.761 7.777   1.00 28.86 ? 518  ARG A CB    1 
ATOM   4073 C  CG    . ARG A 1 518 ? -17.724 -38.552 6.787   1.00 27.55 ? 518  ARG A CG    1 
ATOM   4074 C  CD    . ARG A 1 518 ? -17.577 -37.290 5.965   1.00 31.65 ? 518  ARG A CD    1 
ATOM   4075 N  NE    . ARG A 1 518 ? -18.651 -37.084 4.993   1.00 31.70 ? 518  ARG A NE    1 
ATOM   4076 C  CZ    . ARG A 1 518 ? -18.638 -37.477 3.711   1.00 36.42 ? 518  ARG A CZ    1 
ATOM   4077 N  NH1   . ARG A 1 518 ? -17.591 -38.087 3.148   1.00 35.14 ? 518  ARG A NH1   1 
ATOM   4078 N  NH2   . ARG A 1 518 ? -19.699 -37.221 2.970   1.00 38.24 ? 518  ARG A NH2   1 
ATOM   4079 N  N     . ARG A 1 519 ? -15.472 -40.715 10.517  1.00 32.47 ? 519  ARG A N     1 
ATOM   4080 C  CA    . ARG A 1 519 ? -14.295 -40.826 11.427  1.00 34.54 ? 519  ARG A CA    1 
ATOM   4081 C  C     . ARG A 1 519 ? -13.450 -42.053 11.052  1.00 35.10 ? 519  ARG A C     1 
ATOM   4082 O  O     . ARG A 1 519 ? -14.105 -43.098 11.185  1.00 33.13 ? 519  ARG A O     1 
ATOM   4083 C  CB    . ARG A 1 519 ? -14.737 -40.944 12.888  1.00 35.10 ? 519  ARG A CB    1 
ATOM   4084 C  CG    . ARG A 1 519 ? -14.922 -39.603 13.571  1.00 34.61 ? 519  ARG A CG    1 
ATOM   4085 C  CD    . ARG A 1 519 ? -14.939 -39.710 15.083  1.00 34.70 ? 519  ARG A CD    1 
ATOM   4086 N  NE    . ARG A 1 519 ? -15.977 -40.603 15.599  1.00 34.86 ? 519  ARG A NE    1 
ATOM   4087 C  CZ    . ARG A 1 519 ? -17.254 -40.279 15.837  1.00 34.86 ? 519  ARG A CZ    1 
ATOM   4088 N  NH1   . ARG A 1 519 ? -17.725 -39.065 15.579  1.00 32.31 ? 519  ARG A NH1   1 
ATOM   4089 N  NH2   . ARG A 1 519 ? -18.079 -41.195 16.319  1.00 35.70 ? 519  ARG A NH2   1 
ATOM   4090 N  N     . MET B 1 1   ? -42.416 -40.621 56.136  1.00 49.41 ? 1    MET B N     1 
ATOM   4091 C  CA    . MET B 1 1   ? -41.462 -39.593 56.636  1.00 51.11 ? 1    MET B CA    1 
ATOM   4092 C  C     . MET B 1 1   ? -40.040 -39.878 56.111  1.00 52.80 ? 1    MET B C     1 
ATOM   4093 O  O     . MET B 1 1   ? -39.358 -38.898 55.783  1.00 58.56 ? 1    MET B O     1 
ATOM   4094 C  CB    . MET B 1 1   ? -41.453 -39.533 58.167  1.00 47.81 ? 1    MET B CB    1 
ATOM   4095 N  N     . ALA B 1 2   ? -39.573 -41.134 56.038  1.00 49.20 ? 2    ALA B N     1 
ATOM   4096 C  CA    . ALA B 1 2   ? -38.268 -41.474 55.400  1.00 46.79 ? 2    ALA B CA    1 
ATOM   4097 C  C     . ALA B 1 2   ? -38.437 -41.305 53.878  1.00 44.26 ? 2    ALA B C     1 
ATOM   4098 O  O     . ALA B 1 2   ? -39.576 -41.395 53.415  1.00 40.19 ? 2    ALA B O     1 
ATOM   4099 C  CB    . ALA B 1 2   ? -37.803 -42.867 55.768  1.00 43.52 ? 2    ALA B CB    1 
ATOM   4100 N  N     . ALA B 1 3   ? -37.364 -41.030 53.127  1.00 41.15 ? 3    ALA B N     1 
ATOM   4101 C  CA    . ALA B 1 3   ? -37.422 -40.792 51.663  1.00 40.36 ? 3    ALA B CA    1 
ATOM   4102 C  C     . ALA B 1 3   ? -37.841 -42.061 50.935  1.00 37.32 ? 3    ALA B C     1 
ATOM   4103 O  O     . ALA B 1 3   ? -37.402 -43.160 51.292  1.00 32.52 ? 3    ALA B O     1 
ATOM   4104 C  CB    . ALA B 1 3   ? -36.093 -40.307 51.136  1.00 42.19 ? 3    ALA B CB    1 
ATOM   4105 N  N     . PRO B 1 4   ? -38.648 -41.941 49.851  1.00 36.82 ? 4    PRO B N     1 
ATOM   4106 C  CA    . PRO B 1 4   ? -38.945 -43.080 48.980  1.00 37.62 ? 4    PRO B CA    1 
ATOM   4107 C  C     . PRO B 1 4   ? -37.756 -43.474 48.086  1.00 44.16 ? 4    PRO B C     1 
ATOM   4108 O  O     . PRO B 1 4   ? -36.903 -42.624 47.832  1.00 45.29 ? 4    PRO B O     1 
ATOM   4109 C  CB    . PRO B 1 4   ? -40.084 -42.584 48.080  1.00 37.01 ? 4    PRO B CB    1 
ATOM   4110 C  CG    . PRO B 1 4   ? -39.928 -41.081 48.066  1.00 37.94 ? 4    PRO B CG    1 
ATOM   4111 C  CD    . PRO B 1 4   ? -39.272 -40.698 49.381  1.00 36.30 ? 4    PRO B CD    1 
ATOM   4112 N  N     . LEU B 1 5   ? -37.716 -44.734 47.631  1.00 42.51 ? 5    LEU B N     1 
ATOM   4113 C  CA    . LEU B 1 5   ? -36.819 -45.161 46.529  1.00 40.66 ? 5    LEU B CA    1 
ATOM   4114 C  C     . LEU B 1 5   ? -37.209 -44.402 45.266  1.00 40.22 ? 5    LEU B C     1 
ATOM   4115 O  O     . LEU B 1 5   ? -38.384 -44.188 45.001  1.00 35.73 ? 5    LEU B O     1 
ATOM   4116 C  CB    . LEU B 1 5   ? -36.938 -46.665 46.262  1.00 40.99 ? 5    LEU B CB    1 
ATOM   4117 C  CG    . LEU B 1 5   ? -36.360 -47.596 47.325  1.00 41.46 ? 5    LEU B CG    1 
ATOM   4118 C  CD1   . LEU B 1 5   ? -36.764 -49.026 47.029  1.00 39.64 ? 5    LEU B CD1   1 
ATOM   4119 C  CD2   . LEU B 1 5   ? -34.849 -47.477 47.407  1.00 46.93 ? 5    LEU B CD2   1 
ATOM   4120 N  N     . PRO B 1 6   ? -36.234 -44.033 44.408  1.00 42.02 ? 6    PRO B N     1 
ATOM   4121 C  CA    . PRO B 1 6   ? -36.551 -43.418 43.128  1.00 40.89 ? 6    PRO B CA    1 
ATOM   4122 C  C     . PRO B 1 6   ? -37.242 -44.465 42.254  1.00 43.43 ? 6    PRO B C     1 
ATOM   4123 O  O     . PRO B 1 6   ? -36.873 -45.613 42.315  1.00 48.86 ? 6    PRO B O     1 
ATOM   4124 C  CB    . PRO B 1 6   ? -35.188 -42.982 42.593  1.00 41.39 ? 6    PRO B CB    1 
ATOM   4125 C  CG    . PRO B 1 6   ? -34.200 -43.902 43.263  1.00 43.77 ? 6    PRO B CG    1 
ATOM   4126 C  CD    . PRO B 1 6   ? -34.795 -44.231 44.611  1.00 40.83 ? 6    PRO B CD    1 
ATOM   4127 N  N     . GLU B 1 7   ? -38.260 -44.053 41.506  1.00 48.44 ? 7    GLU B N     1 
ATOM   4128 C  CA    . GLU B 1 7   ? -39.047 -44.965 40.637  1.00 50.31 ? 7    GLU B CA    1 
ATOM   4129 C  C     . GLU B 1 7   ? -38.081 -45.636 39.657  1.00 45.41 ? 7    GLU B C     1 
ATOM   4130 O  O     . GLU B 1 7   ? -37.183 -44.949 39.145  1.00 43.83 ? 7    GLU B O     1 
ATOM   4131 C  CB    . GLU B 1 7   ? -40.180 -44.209 39.934  1.00 56.61 ? 7    GLU B CB    1 
ATOM   4132 C  CG    . GLU B 1 7   ? -40.709 -44.906 38.688  1.00 60.42 ? 7    GLU B CG    1 
ATOM   4133 C  CD    . GLU B 1 7   ? -41.944 -44.260 38.077  1.00 69.34 ? 7    GLU B CD    1 
ATOM   4134 O  OE1   . GLU B 1 7   ? -42.133 -43.032 38.266  1.00 68.31 ? 7    GLU B OE1   1 
ATOM   4135 O  OE2   . GLU B 1 7   ? -42.724 -44.988 37.418  1.00 74.59 ? 7    GLU B OE2   1 
ATOM   4136 N  N     . GLY B 1 8   ? -38.243 -46.944 39.462  1.00 43.81 ? 8    GLY B N     1 
ATOM   4137 C  CA    . GLY B 1 8   ? -37.454 -47.773 38.532  1.00 42.21 ? 8    GLY B CA    1 
ATOM   4138 C  C     . GLY B 1 8   ? -36.311 -48.460 39.241  1.00 45.19 ? 8    GLY B C     1 
ATOM   4139 O  O     . GLY B 1 8   ? -35.680 -49.315 38.617  1.00 45.27 ? 8    GLY B O     1 
ATOM   4140 N  N     . VAL B 1 9   ? -36.050 -48.092 40.499  1.00 46.62 ? 9    VAL B N     1 
ATOM   4141 C  CA    . VAL B 1 9   ? -34.891 -48.589 41.296  1.00 46.03 ? 9    VAL B CA    1 
ATOM   4142 C  C     . VAL B 1 9   ? -35.418 -49.446 42.446  1.00 44.65 ? 9    VAL B C     1 
ATOM   4143 O  O     . VAL B 1 9   ? -36.150 -48.901 43.309  1.00 44.94 ? 9    VAL B O     1 
ATOM   4144 C  CB    . VAL B 1 9   ? -34.037 -47.429 41.844  1.00 44.12 ? 9    VAL B CB    1 
ATOM   4145 C  CG1   . VAL B 1 9   ? -32.896 -47.938 42.719  1.00 42.58 ? 9    VAL B CG1   1 
ATOM   4146 C  CG2   . VAL B 1 9   ? -33.517 -46.531 40.730  1.00 44.75 ? 9    VAL B CG2   1 
ATOM   4147 N  N     . SER B 1 10  ? -34.957 -50.693 42.521  1.00 43.63 ? 10   SER B N     1 
ATOM   4148 C  CA    . SER B 1 10  ? -35.344 -51.673 43.566  1.00 41.97 ? 10   SER B CA    1 
ATOM   4149 C  C     . SER B 1 10  ? -34.624 -51.348 44.881  1.00 45.33 ? 10   SER B C     1 
ATOM   4150 O  O     . SER B 1 10  ? -33.640 -50.575 44.863  1.00 45.13 ? 10   SER B O     1 
ATOM   4151 C  CB    . SER B 1 10  ? -35.044 -53.057 43.084  1.00 43.98 ? 10   SER B CB    1 
ATOM   4152 O  OG    . SER B 1 10  ? -33.652 -53.310 43.148  1.00 49.36 ? 10   SER B OG    1 
ATOM   4153 N  N     . ALA B 1 11  ? -35.083 -51.911 45.998  1.00 42.26 ? 11   ALA B N     1 
ATOM   4154 C  CA    . ALA B 1 11  ? -34.364 -51.854 47.289  1.00 42.28 ? 11   ALA B CA    1 
ATOM   4155 C  C     . ALA B 1 11  ? -32.989 -52.522 47.133  1.00 44.47 ? 11   ALA B C     1 
ATOM   4156 O  O     . ALA B 1 11  ? -32.049 -52.115 47.855  1.00 41.23 ? 11   ALA B O     1 
ATOM   4157 C  CB    . ALA B 1 11  ? -35.180 -52.524 48.364  1.00 44.79 ? 11   ALA B CB    1 
ATOM   4158 N  N     . GLU B 1 12  ? -32.871 -53.507 46.234  1.00 41.49 ? 12   GLU B N     1 
ATOM   4159 C  CA    . GLU B 1 12  ? -31.646 -54.344 46.095  1.00 46.58 ? 12   GLU B CA    1 
ATOM   4160 C  C     . GLU B 1 12  ? -30.598 -53.517 45.347  1.00 44.89 ? 12   GLU B C     1 
ATOM   4161 O  O     . GLU B 1 12  ? -29.475 -53.401 45.863  1.00 45.29 ? 12   GLU B O     1 
ATOM   4162 C  CB    . GLU B 1 12  ? -31.892 -55.666 45.354  1.00 47.59 ? 12   GLU B CB    1 
ATOM   4163 C  CG    . GLU B 1 12  ? -33.139 -56.412 45.799  1.00 58.28 ? 12   GLU B CG    1 
ATOM   4164 C  CD    . GLU B 1 12  ? -34.390 -56.051 45.004  1.00 66.00 ? 12   GLU B CD    1 
ATOM   4165 O  OE1   . GLU B 1 12  ? -35.397 -55.657 45.622  1.00 59.44 ? 12   GLU B OE1   1 
ATOM   4166 O  OE2   . GLU B 1 12  ? -34.349 -56.143 43.755  1.00 80.57 ? 12   GLU B OE2   1 
ATOM   4167 N  N     . ALA B 1 13  ? -30.974 -52.964 44.187  1.00 41.92 ? 13   ALA B N     1 
ATOM   4168 C  CA    . ALA B 1 13  ? -30.135 -52.057 43.373  1.00 41.94 ? 13   ALA B CA    1 
ATOM   4169 C  C     . ALA B 1 13  ? -29.590 -50.939 44.277  1.00 40.25 ? 13   ALA B C     1 
ATOM   4170 O  O     . ALA B 1 13  ? -28.350 -50.733 44.305  1.00 43.01 ? 13   ALA B O     1 
ATOM   4171 C  CB    . ALA B 1 13  ? -30.935 -51.528 42.207  1.00 42.15 ? 13   ALA B CB    1 
ATOM   4172 N  N     . MET B 1 14  ? -30.469 -50.287 45.044  1.00 37.84 ? 14   MET B N     1 
ATOM   4173 C  CA    . MET B 1 14  ? -30.102 -49.143 45.919  1.00 37.06 ? 14   MET B CA    1 
ATOM   4174 C  C     . MET B 1 14  ? -29.109 -49.629 46.976  1.00 39.76 ? 14   MET B C     1 
ATOM   4175 O  O     . MET B 1 14  ? -28.113 -48.932 47.234  1.00 43.00 ? 14   MET B O     1 
ATOM   4176 C  CB    . MET B 1 14  ? -31.336 -48.540 46.593  1.00 34.40 ? 14   MET B CB    1 
ATOM   4177 C  CG    . MET B 1 14  ? -31.033 -47.376 47.528  1.00 36.13 ? 14   MET B CG    1 
ATOM   4178 S  SD    . MET B 1 14  ? -30.083 -46.009 46.747  1.00 37.93 ? 14   MET B SD    1 
ATOM   4179 C  CE    . MET B 1 14  ? -31.402 -45.202 45.830  1.00 38.63 ? 14   MET B CE    1 
ATOM   4180 N  N     . SER B 1 15  ? -29.346 -50.801 47.562  1.00 41.48 ? 15   SER B N     1 
ATOM   4181 C  CA    . SER B 1 15  ? -28.555 -51.296 48.717  1.00 38.49 ? 15   SER B CA    1 
ATOM   4182 C  C     . SER B 1 15  ? -27.140 -51.677 48.253  1.00 33.35 ? 15   SER B C     1 
ATOM   4183 O  O     . SER B 1 15  ? -26.182 -51.438 49.030  1.00 31.50 ? 15   SER B O     1 
ATOM   4184 C  CB    . SER B 1 15  ? -29.255 -52.439 49.406  1.00 39.31 ? 15   SER B CB    1 
ATOM   4185 O  OG    . SER B 1 15  ? -28.755 -52.590 50.726  1.00 44.05 ? 15   SER B OG    1 
ATOM   4186 N  N     . SER B 1 16  ? -27.032 -52.270 47.063  1.00 32.79 ? 16   SER B N     1 
ATOM   4187 C  CA    . SER B 1 16  ? -25.755 -52.635 46.382  1.00 39.01 ? 16   SER B CA    1 
ATOM   4188 C  C     . SER B 1 16  ? -24.937 -51.382 46.045  1.00 38.16 ? 16   SER B C     1 
ATOM   4189 O  O     . SER B 1 16  ? -23.728 -51.347 46.365  1.00 39.99 ? 16   SER B O     1 
ATOM   4190 C  CB    . SER B 1 16  ? -25.994 -53.416 45.119  1.00 38.99 ? 16   SER B CB    1 
ATOM   4191 O  OG    . SER B 1 16  ? -26.873 -54.488 45.359  1.00 45.68 ? 16   SER B OG    1 
ATOM   4192 N  N     . ALA B 1 17  ? -25.564 -50.410 45.382  1.00 37.13 ? 17   ALA B N     1 
ATOM   4193 C  CA    . ALA B 1 17  ? -24.932 -49.112 45.082  1.00 33.73 ? 17   ALA B CA    1 
ATOM   4194 C  C     . ALA B 1 17  ? -24.365 -48.553 46.383  1.00 32.88 ? 17   ALA B C     1 
ATOM   4195 O  O     . ALA B 1 17  ? -23.135 -48.258 46.434  1.00 29.55 ? 17   ALA B O     1 
ATOM   4196 C  CB    . ALA B 1 17  ? -25.926 -48.170 44.465  1.00 34.22 ? 17   ALA B CB    1 
ATOM   4197 N  N     . LEU B 1 18  ? -25.209 -48.437 47.415  1.00 32.00 ? 18   LEU B N     1 
ATOM   4198 C  CA    . LEU B 1 18  ? -24.770 -47.827 48.700  1.00 32.42 ? 18   LEU B CA    1 
ATOM   4199 C  C     . LEU B 1 18  ? -23.585 -48.624 49.264  1.00 32.97 ? 18   LEU B C     1 
ATOM   4200 O  O     . LEU B 1 18  ? -22.631 -47.987 49.771  1.00 33.21 ? 18   LEU B O     1 
ATOM   4201 C  CB    . LEU B 1 18  ? -25.948 -47.734 49.677  1.00 34.68 ? 18   LEU B CB    1 
ATOM   4202 C  CG    . LEU B 1 18  ? -27.053 -46.751 49.283  1.00 36.49 ? 18   LEU B CG    1 
ATOM   4203 C  CD1   . LEU B 1 18  ? -28.131 -46.669 50.360  1.00 38.21 ? 18   LEU B CD1   1 
ATOM   4204 C  CD2   . LEU B 1 18  ? -26.498 -45.356 48.996  1.00 34.62 ? 18   LEU B CD2   1 
ATOM   4205 N  N     . ASP B 1 19  ? -23.613 -49.957 49.157  1.00 35.74 ? 19   ASP B N     1 
ATOM   4206 C  CA    . ASP B 1 19  ? -22.509 -50.838 49.636  1.00 37.52 ? 19   ASP B CA    1 
ATOM   4207 C  C     . ASP B 1 19  ? -21.242 -50.529 48.837  1.00 35.48 ? 19   ASP B C     1 
ATOM   4208 O  O     . ASP B 1 19  ? -20.190 -50.292 49.479  1.00 35.43 ? 19   ASP B O     1 
ATOM   4209 C  CB    . ASP B 1 19  ? -22.851 -52.329 49.552  1.00 40.07 ? 19   ASP B CB    1 
ATOM   4210 C  CG    . ASP B 1 19  ? -23.504 -52.885 50.808  1.00 45.70 ? 19   ASP B CG    1 
ATOM   4211 O  OD1   . ASP B 1 19  ? -23.562 -52.164 51.851  1.00 46.57 ? 19   ASP B OD1   1 
ATOM   4212 O  OD2   . ASP B 1 19  ? -23.959 -54.034 50.738  1.00 57.61 ? 19   ASP B OD2   1 
ATOM   4213 N  N     . ARG B 1 20  ? -21.335 -50.468 47.509  1.00 33.13 ? 20   ARG B N     1 
ATOM   4214 C  CA    . ARG B 1 20  ? -20.186 -50.015 46.663  1.00 38.84 ? 20   ARG B CA    1 
ATOM   4215 C  C     . ARG B 1 20  ? -19.732 -48.587 47.008  1.00 34.29 ? 20   ARG B C     1 
ATOM   4216 O  O     . ARG B 1 20  ? -18.535 -48.413 47.226  1.00 33.56 ? 20   ARG B O     1 
ATOM   4217 C  CB    . ARG B 1 20  ? -20.489 -50.283 45.194  1.00 38.81 ? 20   ARG B CB    1 
ATOM   4218 C  CG    . ARG B 1 20  ? -20.159 -51.738 44.937  1.00 44.04 ? 20   ARG B CG    1 
ATOM   4219 C  CD    . ARG B 1 20  ? -20.746 -52.376 43.726  1.00 54.26 ? 20   ARG B CD    1 
ATOM   4220 N  NE    . ARG B 1 20  ? -19.908 -52.089 42.579  1.00 55.56 ? 20   ARG B NE    1 
ATOM   4221 C  CZ    . ARG B 1 20  ? -19.892 -52.824 41.488  1.00 60.10 ? 20   ARG B CZ    1 
ATOM   4222 N  NH1   . ARG B 1 20  ? -20.617 -53.933 41.413  1.00 61.53 ? 20   ARG B NH1   1 
ATOM   4223 N  NH2   . ARG B 1 20  ? -19.134 -52.447 40.480  1.00 70.05 ? 20   ARG B NH2   1 
ATOM   4224 N  N     . PHE B 1 21  ? -20.630 -47.615 47.175  1.00 34.18 ? 21   PHE B N     1 
ATOM   4225 C  CA    . PHE B 1 21  ? -20.235 -46.231 47.552  1.00 30.79 ? 21   PHE B CA    1 
ATOM   4226 C  C     . PHE B 1 21  ? -19.361 -46.250 48.820  1.00 34.73 ? 21   PHE B C     1 
ATOM   4227 O  O     . PHE B 1 21  ? -18.333 -45.526 48.862  1.00 31.55 ? 21   PHE B O     1 
ATOM   4228 C  CB    . PHE B 1 21  ? -21.472 -45.351 47.742  1.00 31.64 ? 21   PHE B CB    1 
ATOM   4229 C  CG    . PHE B 1 21  ? -22.284 -45.095 46.496  1.00 28.81 ? 21   PHE B CG    1 
ATOM   4230 C  CD1   . PHE B 1 21  ? -21.741 -45.260 45.232  1.00 29.64 ? 21   PHE B CD1   1 
ATOM   4231 C  CD2   . PHE B 1 21  ? -23.596 -44.656 46.585  1.00 29.68 ? 21   PHE B CD2   1 
ATOM   4232 C  CE1   . PHE B 1 21  ? -22.496 -45.020 44.087  1.00 28.55 ? 21   PHE B CE1   1 
ATOM   4233 C  CE2   . PHE B 1 21  ? -24.347 -44.407 45.442  1.00 29.38 ? 21   PHE B CE2   1 
ATOM   4234 C  CZ    . PHE B 1 21  ? -23.794 -44.587 44.193  1.00 28.67 ? 21   PHE B CZ    1 
ATOM   4235 N  N     . ALA B 1 22  ? -19.734 -47.047 49.836  1.00 36.47 ? 22   ALA B N     1 
ATOM   4236 C  CA    . ALA B 1 22  ? -19.042 -47.127 51.152  1.00 38.40 ? 22   ALA B CA    1 
ATOM   4237 C  C     . ALA B 1 22  ? -17.594 -47.616 50.981  1.00 37.48 ? 22   ALA B C     1 
ATOM   4238 O  O     . ALA B 1 22  ? -16.703 -47.158 51.757  1.00 38.93 ? 22   ALA B O     1 
ATOM   4239 C  CB    . ALA B 1 22  ? -19.809 -48.022 52.108  1.00 40.77 ? 22   ALA B CB    1 
ATOM   4240 N  N     . ARG B 1 23  ? -17.353 -48.487 50.001  1.00 35.82 ? 23   ARG B N     1 
ATOM   4241 C  CA    . ARG B 1 23  ? -16.005 -49.047 49.750  1.00 43.13 ? 23   ARG B CA    1 
ATOM   4242 C  C     . ARG B 1 23  ? -15.198 -48.007 48.966  1.00 44.75 ? 23   ARG B C     1 
ATOM   4243 O  O     . ARG B 1 23  ? -13.974 -47.895 49.239  1.00 47.57 ? 23   ARG B O     1 
ATOM   4244 C  CB    . ARG B 1 23  ? -16.129 -50.442 49.123  1.00 45.27 ? 23   ARG B CB    1 
ATOM   4245 C  CG    . ARG B 1 23  ? -16.693 -51.452 50.121  1.00 48.77 ? 23   ARG B CG    1 
ATOM   4246 C  CD    . ARG B 1 23  ? -16.597 -52.906 49.724  1.00 47.79 ? 23   ARG B CD    1 
ATOM   4247 N  NE    . ARG B 1 23  ? -17.457 -53.239 48.598  1.00 43.60 ? 23   ARG B NE    1 
ATOM   4248 C  CZ    . ARG B 1 23  ? -18.698 -53.691 48.676  1.00 40.41 ? 23   ARG B CZ    1 
ATOM   4249 N  NH1   . ARG B 1 23  ? -19.294 -53.831 49.850  1.00 41.56 ? 23   ARG B NH1   1 
ATOM   4250 N  NH2   . ARG B 1 23  ? -19.353 -53.964 47.557  1.00 40.51 ? 23   ARG B NH2   1 
ATOM   4251 N  N     . ILE B 1 24  ? -15.859 -47.233 48.093  1.00 40.95 ? 24   ILE B N     1 
ATOM   4252 C  CA    . ILE B 1 24  ? -15.189 -46.151 47.309  1.00 36.07 ? 24   ILE B CA    1 
ATOM   4253 C  C     . ILE B 1 24  ? -14.695 -45.070 48.278  1.00 34.09 ? 24   ILE B C     1 
ATOM   4254 O  O     . ILE B 1 24  ? -13.513 -44.737 48.209  1.00 37.51 ? 24   ILE B O     1 
ATOM   4255 C  CB    . ILE B 1 24  ? -16.094 -45.592 46.193  1.00 35.73 ? 24   ILE B CB    1 
ATOM   4256 C  CG1   . ILE B 1 24  ? -16.368 -46.647 45.124  1.00 35.55 ? 24   ILE B CG1   1 
ATOM   4257 C  CG2   . ILE B 1 24  ? -15.479 -44.339 45.572  1.00 37.40 ? 24   ILE B CG2   1 
ATOM   4258 C  CD1   . ILE B 1 24  ? -17.518 -46.323 44.195  1.00 36.52 ? 24   ILE B CD1   1 
ATOM   4259 N  N     . VAL B 1 25  ? -15.538 -44.578 49.180  1.00 32.41 ? 25   VAL B N     1 
ATOM   4260 C  CA    . VAL B 1 25  ? -15.239 -43.357 49.983  1.00 33.94 ? 25   VAL B CA    1 
ATOM   4261 C  C     . VAL B 1 25  ? -15.037 -43.679 51.470  1.00 31.74 ? 25   VAL B C     1 
ATOM   4262 O  O     . VAL B 1 25  ? -14.573 -42.774 52.181  1.00 28.81 ? 25   VAL B O     1 
ATOM   4263 C  CB    . VAL B 1 25  ? -16.350 -42.303 49.806  1.00 34.97 ? 25   VAL B CB    1 
ATOM   4264 C  CG1   . VAL B 1 25  ? -16.661 -42.063 48.334  1.00 33.97 ? 25   VAL B CG1   1 
ATOM   4265 C  CG2   . VAL B 1 25  ? -17.612 -42.684 50.573  1.00 33.90 ? 25   VAL B CG2   1 
ATOM   4266 N  N     . GLY B 1 26  ? -15.412 -44.877 51.936  1.00 39.53 ? 26   GLY B N     1 
ATOM   4267 C  CA    . GLY B 1 26  ? -15.343 -45.263 53.363  1.00 42.32 ? 26   GLY B CA    1 
ATOM   4268 C  C     . GLY B 1 26  ? -16.681 -45.082 54.066  1.00 44.44 ? 26   GLY B C     1 
ATOM   4269 O  O     . GLY B 1 26  ? -17.429 -44.134 53.716  1.00 41.16 ? 26   GLY B O     1 
ATOM   4270 N  N     . ALA B 1 27  ? -16.979 -45.953 55.031  1.00 44.49 ? 27   ALA B N     1 
ATOM   4271 C  CA    . ALA B 1 27  ? -18.321 -46.131 55.629  1.00 41.45 ? 27   ALA B CA    1 
ATOM   4272 C  C     . ALA B 1 27  ? -18.745 -44.859 56.366  1.00 38.92 ? 27   ALA B C     1 
ATOM   4273 O  O     . ALA B 1 27  ? -19.968 -44.593 56.419  1.00 37.38 ? 27   ALA B O     1 
ATOM   4274 C  CB    . ALA B 1 27  ? -18.301 -47.329 56.552  1.00 47.33 ? 27   ALA B CB    1 
ATOM   4275 N  N     . ASP B 1 28  ? -17.776 -44.088 56.878  1.00 37.38 ? 28   ASP B N     1 
ATOM   4276 C  CA    . ASP B 1 28  ? -18.021 -42.809 57.597  1.00 40.82 ? 28   ASP B CA    1 
ATOM   4277 C  C     . ASP B 1 28  ? -18.525 -41.685 56.670  1.00 40.06 ? 28   ASP B C     1 
ATOM   4278 O  O     . ASP B 1 28  ? -18.919 -40.630 57.228  1.00 42.20 ? 28   ASP B O     1 
ATOM   4279 C  CB    . ASP B 1 28  ? -16.757 -42.308 58.299  1.00 47.17 ? 28   ASP B CB    1 
ATOM   4280 C  CG    . ASP B 1 28  ? -16.358 -43.123 59.520  1.00 49.71 ? 28   ASP B CG    1 
ATOM   4281 O  OD1   . ASP B 1 28  ? -17.255 -43.555 60.255  1.00 52.77 ? 28   ASP B OD1   1 
ATOM   4282 O  OD2   . ASP B 1 28  ? -15.156 -43.307 59.725  1.00 56.33 ? 28   ASP B OD2   1 
ATOM   4283 N  N     . TRP B 1 29  ? -18.515 -41.865 55.341  1.00 35.31 ? 29   TRP B N     1 
ATOM   4284 C  CA    . TRP B 1 29  ? -18.851 -40.802 54.344  1.00 38.21 ? 29   TRP B CA    1 
ATOM   4285 C  C     . TRP B 1 29  ? -19.966 -41.261 53.405  1.00 37.79 ? 29   TRP B C     1 
ATOM   4286 O  O     . TRP B 1 29  ? -20.064 -40.707 52.312  1.00 39.47 ? 29   TRP B O     1 
ATOM   4287 C  CB    . TRP B 1 29  ? -17.606 -40.377 53.547  1.00 35.63 ? 29   TRP B CB    1 
ATOM   4288 C  CG    . TRP B 1 29  ? -16.488 -39.958 54.445  1.00 32.44 ? 29   TRP B CG    1 
ATOM   4289 C  CD1   . TRP B 1 29  ? -15.326 -40.634 54.674  1.00 33.19 ? 29   TRP B CD1   1 
ATOM   4290 C  CD2   . TRP B 1 29  ? -16.454 -38.787 55.282  1.00 32.24 ? 29   TRP B CD2   1 
ATOM   4291 N  NE1   . TRP B 1 29  ? -14.575 -39.963 55.604  1.00 33.56 ? 29   TRP B NE1   1 
ATOM   4292 C  CE2   . TRP B 1 29  ? -15.240 -38.831 56.001  1.00 33.22 ? 29   TRP B CE2   1 
ATOM   4293 C  CE3   . TRP B 1 29  ? -17.330 -37.714 55.502  1.00 32.95 ? 29   TRP B CE3   1 
ATOM   4294 C  CZ2   . TRP B 1 29  ? -14.864 -37.830 56.899  1.00 34.63 ? 29   TRP B CZ2   1 
ATOM   4295 C  CZ3   . TRP B 1 29  ? -16.967 -36.735 56.406  1.00 33.35 ? 29   TRP B CZ3   1 
ATOM   4296 C  CH2   . TRP B 1 29  ? -15.749 -36.795 57.097  1.00 35.10 ? 29   TRP B CH2   1 
ATOM   4297 N  N     . VAL B 1 30  ? -20.746 -42.267 53.795  1.00 39.98 ? 30   VAL B N     1 
ATOM   4298 C  CA    . VAL B 1 30  ? -22.085 -42.549 53.202  1.00 39.08 ? 30   VAL B CA    1 
ATOM   4299 C  C     . VAL B 1 30  ? -23.103 -42.267 54.310  1.00 39.58 ? 30   VAL B C     1 
ATOM   4300 O  O     . VAL B 1 30  ? -22.960 -42.893 55.338  1.00 38.32 ? 30   VAL B O     1 
ATOM   4301 C  CB    . VAL B 1 30  ? -22.179 -43.984 52.666  1.00 36.90 ? 30   VAL B CB    1 
ATOM   4302 C  CG1   . VAL B 1 30  ? -23.564 -44.297 52.113  1.00 38.78 ? 30   VAL B CG1   1 
ATOM   4303 C  CG2   . VAL B 1 30  ? -21.113 -44.235 51.620  1.00 36.78 ? 30   VAL B CG2   1 
ATOM   4304 N  N     . PHE B 1 31  ? -24.006 -41.292 54.127  1.00 39.94 ? 31   PHE B N     1 
ATOM   4305 C  CA    . PHE B 1 31  ? -24.976 -40.809 55.151  1.00 40.98 ? 31   PHE B CA    1 
ATOM   4306 C  C     . PHE B 1 31  ? -26.394 -41.260 54.784  1.00 41.03 ? 31   PHE B C     1 
ATOM   4307 O  O     . PHE B 1 31  ? -26.879 -40.942 53.689  1.00 39.87 ? 31   PHE B O     1 
ATOM   4308 C  CB    . PHE B 1 31  ? -24.870 -39.289 55.320  1.00 41.27 ? 31   PHE B CB    1 
ATOM   4309 C  CG    . PHE B 1 31  ? -23.469 -38.812 55.611  1.00 44.01 ? 31   PHE B CG    1 
ATOM   4310 C  CD1   . PHE B 1 31  ? -22.939 -38.891 56.896  1.00 41.18 ? 31   PHE B CD1   1 
ATOM   4311 C  CD2   . PHE B 1 31  ? -22.667 -38.309 54.591  1.00 44.18 ? 31   PHE B CD2   1 
ATOM   4312 C  CE1   . PHE B 1 31  ? -21.643 -38.467 57.148  1.00 41.54 ? 31   PHE B CE1   1 
ATOM   4313 C  CE2   . PHE B 1 31  ? -21.380 -37.860 54.857  1.00 43.51 ? 31   PHE B CE2   1 
ATOM   4314 C  CZ    . PHE B 1 31  ? -20.864 -37.955 56.131  1.00 42.53 ? 31   PHE B CZ    1 
ATOM   4315 N  N     . THR B 1 32  ? -27.023 -42.010 55.688  1.00 40.96 ? 32   THR B N     1 
ATOM   4316 C  CA    . THR B 1 32  ? -28.398 -42.566 55.563  1.00 46.44 ? 32   THR B CA    1 
ATOM   4317 C  C     . THR B 1 32  ? -29.150 -42.263 56.868  1.00 48.03 ? 32   THR B C     1 
ATOM   4318 O  O     . THR B 1 32  ? -28.531 -41.649 57.771  1.00 49.60 ? 32   THR B O     1 
ATOM   4319 C  CB    . THR B 1 32  ? -28.339 -44.066 55.248  1.00 47.28 ? 32   THR B CB    1 
ATOM   4320 O  OG1   . THR B 1 32  ? -27.568 -44.625 56.310  1.00 46.21 ? 32   THR B OG1   1 
ATOM   4321 C  CG2   . THR B 1 32  ? -27.707 -44.382 53.911  1.00 44.09 ? 32   THR B CG2   1 
ATOM   4322 N  N     . GLU B 1 33  ? -30.429 -42.641 56.960  1.00 50.66 ? 33   GLU B N     1 
ATOM   4323 C  CA    . GLU B 1 33  ? -31.240 -42.519 58.205  1.00 54.84 ? 33   GLU B CA    1 
ATOM   4324 C  C     . GLU B 1 33  ? -31.124 -41.090 58.764  1.00 51.90 ? 33   GLU B C     1 
ATOM   4325 O  O     . GLU B 1 33  ? -31.337 -40.161 57.985  1.00 54.60 ? 33   GLU B O     1 
ATOM   4326 C  CB    . GLU B 1 33  ? -30.775 -43.580 59.205  1.00 62.70 ? 33   GLU B CB    1 
ATOM   4327 C  CG    . GLU B 1 33  ? -30.671 -44.968 58.597  1.00 68.58 ? 33   GLU B CG    1 
ATOM   4328 C  CD    . GLU B 1 33  ? -30.015 -45.998 59.498  1.00 71.32 ? 33   GLU B CD    1 
ATOM   4329 O  OE1   . GLU B 1 33  ? -30.602 -47.079 59.659  1.00 77.86 ? 33   GLU B OE1   1 
ATOM   4330 O  OE2   . GLU B 1 33  ? -28.916 -45.722 60.026  1.00 74.40 ? 33   GLU B OE2   1 
ATOM   4331 N  N     . ASP B 1 34  ? -30.749 -40.925 60.039  1.00 53.62 ? 34   ASP B N     1 
ATOM   4332 C  CA    . ASP B 1 34  ? -30.769 -39.636 60.791  1.00 58.06 ? 34   ASP B CA    1 
ATOM   4333 C  C     . ASP B 1 34  ? -29.739 -38.647 60.240  1.00 52.85 ? 34   ASP B C     1 
ATOM   4334 O  O     . ASP B 1 34  ? -29.876 -37.430 60.503  1.00 53.25 ? 34   ASP B O     1 
ATOM   4335 C  CB    . ASP B 1 34  ? -30.445 -39.834 62.273  1.00 66.49 ? 34   ASP B CB    1 
ATOM   4336 C  CG    . ASP B 1 34  ? -31.401 -40.780 62.977  1.00 76.62 ? 34   ASP B CG    1 
ATOM   4337 O  OD1   . ASP B 1 34  ? -32.624 -40.553 62.876  1.00 78.60 ? 34   ASP B OD1   1 
ATOM   4338 O  OD2   . ASP B 1 34  ? -30.915 -41.752 63.595  1.00 82.73 ? 34   ASP B OD2   1 
ATOM   4339 N  N     . LYS B 1 35  ? -28.718 -39.146 59.553  1.00 49.62 ? 35   LYS B N     1 
ATOM   4340 C  CA    . LYS B 1 35  ? -27.578 -38.318 59.098  1.00 51.58 ? 35   LYS B CA    1 
ATOM   4341 C  C     . LYS B 1 35  ? -27.917 -37.667 57.751  1.00 45.59 ? 35   LYS B C     1 
ATOM   4342 O  O     . LYS B 1 35  ? -27.103 -36.847 57.305  1.00 46.38 ? 35   LYS B O     1 
ATOM   4343 C  CB    . LYS B 1 35  ? -26.301 -39.160 59.071  1.00 55.64 ? 35   LYS B CB    1 
ATOM   4344 C  CG    . LYS B 1 35  ? -25.707 -39.450 60.442  1.00 57.39 ? 35   LYS B CG    1 
ATOM   4345 C  CD    . LYS B 1 35  ? -24.372 -40.163 60.372  1.00 64.42 ? 35   LYS B CD    1 
ATOM   4346 C  CE    . LYS B 1 35  ? -23.277 -39.448 61.138  1.00 66.91 ? 35   LYS B CE    1 
ATOM   4347 N  NZ    . LYS B 1 35  ? -21.991 -40.174 61.033  1.00 66.80 ? 35   LYS B NZ    1 
ATOM   4348 N  N     . ILE B 1 36  ? -29.078 -37.982 57.157  1.00 43.32 ? 36   ILE B N     1 
ATOM   4349 C  CA    . ILE B 1 36  ? -29.581 -37.317 55.912  1.00 44.34 ? 36   ILE B CA    1 
ATOM   4350 C  C     . ILE B 1 36  ? -30.167 -35.920 56.208  1.00 43.09 ? 36   ILE B C     1 
ATOM   4351 O  O     . ILE B 1 36  ? -30.318 -35.146 55.242  1.00 39.72 ? 36   ILE B O     1 
ATOM   4352 C  CB    . ILE B 1 36  ? -30.598 -38.202 55.163  1.00 45.78 ? 36   ILE B CB    1 
ATOM   4353 C  CG1   . ILE B 1 36  ? -30.671 -37.823 53.682  1.00 46.48 ? 36   ILE B CG1   1 
ATOM   4354 C  CG2   . ILE B 1 36  ? -31.972 -38.164 55.817  1.00 47.37 ? 36   ILE B CG2   1 
ATOM   4355 C  CD1   . ILE B 1 36  ? -29.325 -37.845 52.983  1.00 45.77 ? 36   ILE B CD1   1 
ATOM   4356 N  N     . THR B 1 37  ? -30.472 -35.578 57.466  1.00 41.56 ? 37   THR B N     1 
ATOM   4357 C  CA    . THR B 1 37  ? -31.214 -34.332 57.818  1.00 43.92 ? 37   THR B CA    1 
ATOM   4358 C  C     . THR B 1 37  ? -30.577 -33.118 57.136  1.00 40.74 ? 37   THR B C     1 
ATOM   4359 O  O     . THR B 1 37  ? -31.294 -32.311 56.537  1.00 37.73 ? 37   THR B O     1 
ATOM   4360 C  CB    . THR B 1 37  ? -31.356 -34.118 59.334  1.00 42.93 ? 37   THR B CB    1 
ATOM   4361 O  OG1   . THR B 1 37  ? -32.242 -35.107 59.846  1.00 43.67 ? 37   THR B OG1   1 
ATOM   4362 C  CG2   . THR B 1 37  ? -31.944 -32.769 59.692  1.00 43.62 ? 37   THR B CG2   1 
ATOM   4363 N  N     . PRO B 1 38  ? -29.237 -32.922 57.210  1.00 36.60 ? 38   PRO B N     1 
ATOM   4364 C  CA    . PRO B 1 38  ? -28.622 -31.697 56.690  1.00 35.25 ? 38   PRO B CA    1 
ATOM   4365 C  C     . PRO B 1 38  ? -28.850 -31.475 55.185  1.00 33.09 ? 38   PRO B C     1 
ATOM   4366 O  O     . PRO B 1 38  ? -28.682 -30.366 54.734  1.00 31.39 ? 38   PRO B O     1 
ATOM   4367 C  CB    . PRO B 1 38  ? -27.130 -31.879 57.006  1.00 35.50 ? 38   PRO B CB    1 
ATOM   4368 C  CG    . PRO B 1 38  ? -27.101 -32.867 58.148  1.00 35.92 ? 38   PRO B CG    1 
ATOM   4369 C  CD    . PRO B 1 38  ? -28.245 -33.812 57.832  1.00 36.12 ? 38   PRO B CD    1 
ATOM   4370 N  N     . TYR B 1 39  ? -29.267 -32.521 54.475  1.00 31.60 ? 39   TYR B N     1 
ATOM   4371 C  CA    . TYR B 1 39  ? -29.430 -32.546 53.008  1.00 35.28 ? 39   TYR B CA    1 
ATOM   4372 C  C     . TYR B 1 39  ? -30.877 -32.242 52.626  1.00 37.05 ? 39   TYR B C     1 
ATOM   4373 O  O     . TYR B 1 39  ? -31.122 -32.035 51.419  1.00 43.53 ? 39   TYR B O     1 
ATOM   4374 C  CB    . TYR B 1 39  ? -28.957 -33.887 52.449  1.00 33.71 ? 39   TYR B CB    1 
ATOM   4375 C  CG    . TYR B 1 39  ? -27.473 -34.080 52.628  1.00 36.55 ? 39   TYR B CG    1 
ATOM   4376 C  CD1   . TYR B 1 39  ? -26.568 -33.442 51.796  1.00 31.26 ? 39   TYR B CD1   1 
ATOM   4377 C  CD2   . TYR B 1 39  ? -26.963 -34.866 53.658  1.00 36.54 ? 39   TYR B CD2   1 
ATOM   4378 C  CE1   . TYR B 1 39  ? -25.206 -33.588 51.977  1.00 31.27 ? 39   TYR B CE1   1 
ATOM   4379 C  CE2   . TYR B 1 39  ? -25.596 -35.044 53.833  1.00 34.58 ? 39   TYR B CE2   1 
ATOM   4380 C  CZ    . TYR B 1 39  ? -24.715 -34.398 52.988  1.00 33.78 ? 39   TYR B CZ    1 
ATOM   4381 O  OH    . TYR B 1 39  ? -23.368 -34.567 53.139  1.00 35.60 ? 39   TYR B OH    1 
ATOM   4382 N  N     . GLU B 1 40  ? -31.800 -32.217 53.588  1.00 34.43 ? 40   GLU B N     1 
ATOM   4383 C  CA    . GLU B 1 40  ? -33.180 -31.705 53.359  1.00 33.70 ? 40   GLU B CA    1 
ATOM   4384 C  C     . GLU B 1 40  ? -33.076 -30.195 53.049  1.00 30.12 ? 40   GLU B C     1 
ATOM   4385 O  O     . GLU B 1 40  ? -32.147 -29.513 53.562  1.00 27.89 ? 40   GLU B O     1 
ATOM   4386 C  CB    . GLU B 1 40  ? -34.102 -31.923 54.570  1.00 34.80 ? 40   GLU B CB    1 
ATOM   4387 C  CG    . GLU B 1 40  ? -34.144 -33.342 55.116  1.00 35.04 ? 40   GLU B CG    1 
ATOM   4388 C  CD    . GLU B 1 40  ? -34.812 -34.361 54.219  1.00 37.16 ? 40   GLU B CD    1 
ATOM   4389 O  OE1   . GLU B 1 40  ? -35.494 -33.964 53.245  1.00 44.13 ? 40   GLU B OE1   1 
ATOM   4390 O  OE2   . GLU B 1 40  ? -34.636 -35.555 54.484  1.00 42.50 ? 40   GLU B OE2   1 
ATOM   4391 N  N     . ASP B 1 41  ? -33.998 -29.681 52.246  1.00 30.36 ? 41   ASP B N     1 
ATOM   4392 C  CA    . ASP B 1 41  ? -34.158 -28.221 52.024  1.00 30.13 ? 41   ASP B CA    1 
ATOM   4393 C  C     . ASP B 1 41  ? -34.463 -27.591 53.375  1.00 30.72 ? 41   ASP B C     1 
ATOM   4394 O  O     . ASP B 1 41  ? -35.414 -28.004 54.018  1.00 32.25 ? 41   ASP B O     1 
ATOM   4395 C  CB    . ASP B 1 41  ? -35.307 -27.954 51.051  1.00 29.41 ? 41   ASP B CB    1 
ATOM   4396 C  CG    . ASP B 1 41  ? -35.525 -26.475 50.766  1.00 29.06 ? 41   ASP B CG    1 
ATOM   4397 O  OD1   . ASP B 1 41  ? -34.773 -25.641 51.346  1.00 25.90 ? 41   ASP B OD1   1 
ATOM   4398 O  OD2   . ASP B 1 41  ? -36.438 -26.165 49.951  1.00 27.58 ? 41   ASP B OD2   1 
ATOM   4399 N  N     . PRO B 1 42  ? -33.652 -26.648 53.900  1.00 33.84 ? 42   PRO B N     1 
ATOM   4400 C  CA    . PRO B 1 42  ? -33.913 -26.108 55.229  1.00 31.70 ? 42   PRO B CA    1 
ATOM   4401 C  C     . PRO B 1 42  ? -35.131 -25.178 55.242  1.00 34.83 ? 42   PRO B C     1 
ATOM   4402 O  O     . PRO B 1 42  ? -35.636 -24.893 56.334  1.00 34.14 ? 42   PRO B O     1 
ATOM   4403 C  CB    . PRO B 1 42  ? -32.638 -25.327 55.568  1.00 34.65 ? 42   PRO B CB    1 
ATOM   4404 C  CG    . PRO B 1 42  ? -32.059 -24.955 54.220  1.00 33.84 ? 42   PRO B CG    1 
ATOM   4405 C  CD    . PRO B 1 42  ? -32.413 -26.109 53.307  1.00 33.32 ? 42   PRO B CD    1 
ATOM   4406 N  N     . TYR B 1 43  ? -35.572 -24.729 54.060  1.00 33.22 ? 43   TYR B N     1 
ATOM   4407 C  CA    . TYR B 1 43  ? -36.692 -23.762 53.895  1.00 32.22 ? 43   TYR B CA    1 
ATOM   4408 C  C     . TYR B 1 43  ? -37.839 -24.428 53.128  1.00 32.66 ? 43   TYR B C     1 
ATOM   4409 O  O     . TYR B 1 43  ? -38.180 -23.979 51.996  1.00 33.29 ? 43   TYR B O     1 
ATOM   4410 C  CB    . TYR B 1 43  ? -36.221 -22.488 53.189  1.00 28.56 ? 43   TYR B CB    1 
ATOM   4411 C  CG    . TYR B 1 43  ? -35.019 -21.774 53.746  1.00 27.73 ? 43   TYR B CG    1 
ATOM   4412 C  CD1   . TYR B 1 43  ? -34.655 -21.855 55.081  1.00 28.53 ? 43   TYR B CD1   1 
ATOM   4413 C  CD2   . TYR B 1 43  ? -34.256 -20.972 52.915  1.00 26.36 ? 43   TYR B CD2   1 
ATOM   4414 C  CE1   . TYR B 1 43  ? -33.553 -21.175 55.572  1.00 27.44 ? 43   TYR B CE1   1 
ATOM   4415 C  CE2   . TYR B 1 43  ? -33.163 -20.274 53.393  1.00 29.22 ? 43   TYR B CE2   1 
ATOM   4416 C  CZ    . TYR B 1 43  ? -32.809 -20.376 54.724  1.00 28.95 ? 43   TYR B CZ    1 
ATOM   4417 O  OH    . TYR B 1 43  ? -31.741 -19.669 55.181  1.00 30.43 ? 43   TYR B OH    1 
ATOM   4418 N  N     . THR B 1 44  ? -38.386 -25.507 53.696  1.00 34.19 ? 44   THR B N     1 
ATOM   4419 C  CA    . THR B 1 44  ? -39.438 -26.350 53.059  1.00 33.30 ? 44   THR B CA    1 
ATOM   4420 C  C     . THR B 1 44  ? -40.450 -25.437 52.375  1.00 33.79 ? 44   THR B C     1 
ATOM   4421 O  O     . THR B 1 44  ? -40.749 -24.372 52.964  1.00 36.92 ? 44   THR B O     1 
ATOM   4422 C  CB    . THR B 1 44  ? -40.217 -27.214 54.071  1.00 32.46 ? 44   THR B CB    1 
ATOM   4423 O  OG1   . THR B 1 44  ? -39.315 -27.694 55.065  1.00 32.17 ? 44   THR B OG1   1 
ATOM   4424 C  CG2   . THR B 1 44  ? -40.938 -28.378 53.426  1.00 31.82 ? 44   THR B CG2   1 
ATOM   4425 N  N     . ILE B 1 45  ? -40.998 -25.866 51.234  1.00 32.35 ? 45   ILE B N     1 
ATOM   4426 C  CA    . ILE B 1 45  ? -42.095 -25.152 50.516  1.00 34.02 ? 45   ILE B CA    1 
ATOM   4427 C  C     . ILE B 1 45  ? -43.285 -26.101 50.388  1.00 35.12 ? 45   ILE B C     1 
ATOM   4428 O  O     . ILE B 1 45  ? -44.370 -25.738 50.868  1.00 40.09 ? 45   ILE B O     1 
ATOM   4429 C  CB    . ILE B 1 45  ? -41.669 -24.610 49.137  1.00 32.63 ? 45   ILE B CB    1 
ATOM   4430 C  CG1   . ILE B 1 45  ? -40.465 -23.665 49.237  1.00 32.11 ? 45   ILE B CG1   1 
ATOM   4431 C  CG2   . ILE B 1 45  ? -42.878 -23.965 48.470  1.00 33.47 ? 45   ILE B CG2   1 
ATOM   4432 C  CD1   . ILE B 1 45  ? -40.177 -22.861 47.985  1.00 30.02 ? 45   ILE B CD1   1 
ATOM   4433 N  N     . SER B 1 46  ? -43.082 -27.243 49.738  1.00 35.39 ? 46   SER B N     1 
ATOM   4434 C  CA    . SER B 1 46  ? -44.065 -28.346 49.592  1.00 39.06 ? 46   SER B CA    1 
ATOM   4435 C  C     . SER B 1 46  ? -44.611 -28.775 50.971  1.00 41.53 ? 46   SER B C     1 
ATOM   4436 O  O     . SER B 1 46  ? -43.840 -28.854 51.961  1.00 43.38 ? 46   SER B O     1 
ATOM   4437 C  CB    . SER B 1 46  ? -43.432 -29.482 48.862  1.00 37.81 ? 46   SER B CB    1 
ATOM   4438 O  OG    . SER B 1 46  ? -44.276 -30.612 48.838  1.00 36.77 ? 46   SER B OG    1 
ATOM   4439 N  N     . ASN B 1 47  ? -45.923 -28.970 51.036  1.00 39.50 ? 47   ASN B N     1 
ATOM   4440 C  CA    . ASN B 1 47  ? -46.622 -29.621 52.170  1.00 42.09 ? 47   ASN B CA    1 
ATOM   4441 C  C     . ASN B 1 47  ? -46.679 -31.137 51.949  1.00 39.69 ? 47   ASN B C     1 
ATOM   4442 O  O     . ASN B 1 47  ? -47.157 -31.836 52.843  1.00 40.58 ? 47   ASN B O     1 
ATOM   4443 C  CB    . ASN B 1 47  ? -48.009 -29.009 52.368  1.00 39.44 ? 47   ASN B CB    1 
ATOM   4444 C  CG    . ASN B 1 47  ? -47.919 -27.712 53.134  1.00 42.77 ? 47   ASN B CG    1 
ATOM   4445 O  OD1   . ASN B 1 47  ? -47.130 -27.592 54.076  1.00 47.16 ? 47   ASN B OD1   1 
ATOM   4446 N  ND2   . ASN B 1 47  ? -48.704 -26.730 52.731  1.00 48.43 ? 47   ASN B ND2   1 
ATOM   4447 N  N     . ASP B 1 48  ? -46.210 -31.632 50.805  1.00 40.19 ? 48   ASP B N     1 
ATOM   4448 C  CA    . ASP B 1 48  ? -46.120 -33.090 50.540  1.00 39.27 ? 48   ASP B CA    1 
ATOM   4449 C  C     . ASP B 1 48  ? -44.711 -33.583 50.913  1.00 43.54 ? 48   ASP B C     1 
ATOM   4450 O  O     . ASP B 1 48  ? -43.740 -33.305 50.135  1.00 39.05 ? 48   ASP B O     1 
ATOM   4451 C  CB    . ASP B 1 48  ? -46.502 -33.406 49.102  1.00 38.49 ? 48   ASP B CB    1 
ATOM   4452 C  CG    . ASP B 1 48  ? -46.303 -34.876 48.822  1.00 41.85 ? 48   ASP B CG    1 
ATOM   4453 O  OD1   . ASP B 1 48  ? -45.632 -35.536 49.658  1.00 42.87 ? 48   ASP B OD1   1 
ATOM   4454 O  OD2   . ASP B 1 48  ? -46.797 -35.347 47.784  1.00 44.15 ? 48   ASP B OD2   1 
ATOM   4455 N  N     . GLU B 1 49  ? -44.620 -34.302 52.039  1.00 40.75 ? 49   GLU B N     1 
ATOM   4456 C  CA    . GLU B 1 49  ? -43.367 -34.778 52.685  1.00 45.17 ? 49   GLU B CA    1 
ATOM   4457 C  C     . GLU B 1 49  ? -42.647 -35.845 51.856  1.00 44.13 ? 49   GLU B C     1 
ATOM   4458 O  O     . GLU B 1 49  ? -41.522 -36.188 52.236  1.00 46.97 ? 49   GLU B O     1 
ATOM   4459 C  CB    . GLU B 1 49  ? -43.665 -35.439 54.028  1.00 50.93 ? 49   GLU B CB    1 
ATOM   4460 C  CG    . GLU B 1 49  ? -43.965 -34.460 55.137  1.00 61.16 ? 49   GLU B CG    1 
ATOM   4461 C  CD    . GLU B 1 49  ? -44.323 -35.173 56.426  1.00 63.80 ? 49   GLU B CD    1 
ATOM   4462 O  OE1   . GLU B 1 49  ? -44.452 -36.414 56.381  1.00 63.55 ? 49   GLU B OE1   1 
ATOM   4463 O  OE2   . GLU B 1 49  ? -44.469 -34.490 57.459  1.00 68.79 ? 49   GLU B OE2   1 
ATOM   4464 N  N     . THR B 1 50  ? -43.269 -36.385 50.805  1.00 44.42 ? 50   THR B N     1 
ATOM   4465 C  CA    . THR B 1 50  ? -42.638 -37.349 49.861  1.00 43.89 ? 50   THR B CA    1 
ATOM   4466 C  C     . THR B 1 50  ? -41.861 -36.619 48.744  1.00 42.04 ? 50   THR B C     1 
ATOM   4467 O  O     . THR B 1 50  ? -41.366 -37.331 47.865  1.00 41.03 ? 50   THR B O     1 
ATOM   4468 C  CB    . THR B 1 50  ? -43.684 -38.281 49.225  1.00 44.09 ? 50   THR B CB    1 
ATOM   4469 O  OG1   . THR B 1 50  ? -44.473 -37.495 48.325  1.00 43.18 ? 50   THR B OG1   1 
ATOM   4470 C  CG2   . THR B 1 50  ? -44.556 -38.973 50.257  1.00 43.02 ? 50   THR B CG2   1 
ATOM   4471 N  N     . GLU B 1 51  ? -41.796 -35.274 48.738  1.00 41.32 ? 51   GLU B N     1 
ATOM   4472 C  CA    . GLU B 1 51  ? -41.174 -34.470 47.639  1.00 40.43 ? 51   GLU B CA    1 
ATOM   4473 C  C     . GLU B 1 51  ? -39.781 -33.957 48.040  1.00 34.61 ? 51   GLU B C     1 
ATOM   4474 O  O     . GLU B 1 51  ? -39.575 -33.578 49.215  1.00 29.52 ? 51   GLU B O     1 
ATOM   4475 C  CB    . GLU B 1 51  ? -42.080 -33.307 47.207  1.00 42.90 ? 51   GLU B CB    1 
ATOM   4476 C  CG    . GLU B 1 51  ? -43.206 -33.730 46.277  1.00 42.71 ? 51   GLU B CG    1 
ATOM   4477 C  CD    . GLU B 1 51  ? -44.102 -32.605 45.777  1.00 44.74 ? 51   GLU B CD    1 
ATOM   4478 O  OE1   . GLU B 1 51  ? -44.264 -31.580 46.486  1.00 44.71 ? 51   GLU B OE1   1 
ATOM   4479 O  OE2   . GLU B 1 51  ? -44.647 -32.762 44.686  1.00 50.41 ? 51   GLU B OE2   1 
ATOM   4480 N  N     . HIS B 1 52  ? -38.846 -33.944 47.080  1.00 34.28 ? 52   HIS B N     1 
ATOM   4481 C  CA    . HIS B 1 52  ? -37.485 -33.352 47.222  1.00 30.43 ? 52   HIS B CA    1 
ATOM   4482 C  C     . HIS B 1 52  ? -36.736 -34.056 48.359  1.00 30.00 ? 52   HIS B C     1 
ATOM   4483 O  O     . HIS B 1 52  ? -35.989 -33.384 49.107  1.00 29.73 ? 52   HIS B O     1 
ATOM   4484 C  CB    . HIS B 1 52  ? -37.601 -31.832 47.409  1.00 29.58 ? 52   HIS B CB    1 
ATOM   4485 C  CG    . HIS B 1 52  ? -38.516 -31.156 46.442  1.00 32.61 ? 52   HIS B CG    1 
ATOM   4486 N  ND1   . HIS B 1 52  ? -38.350 -31.250 45.066  1.00 39.92 ? 52   HIS B ND1   1 
ATOM   4487 C  CD2   . HIS B 1 52  ? -39.588 -30.351 46.634  1.00 35.16 ? 52   HIS B CD2   1 
ATOM   4488 C  CE1   . HIS B 1 52  ? -39.298 -30.560 44.449  1.00 38.66 ? 52   HIS B CE1   1 
ATOM   4489 N  NE2   . HIS B 1 52  ? -40.076 -29.994 45.396  1.00 39.00 ? 52   HIS B NE2   1 
ATOM   4490 N  N     . ARG B 1 53  ? -36.961 -35.359 48.522  1.00 31.30 ? 53   ARG B N     1 
ATOM   4491 C  CA    . ARG B 1 53  ? -36.373 -36.147 49.637  1.00 33.77 ? 53   ARG B CA    1 
ATOM   4492 C  C     . ARG B 1 53  ? -35.161 -36.919 49.122  1.00 33.15 ? 53   ARG B C     1 
ATOM   4493 O  O     . ARG B 1 53  ? -35.309 -37.851 48.339  1.00 31.73 ? 53   ARG B O     1 
ATOM   4494 C  CB    . ARG B 1 53  ? -37.422 -37.086 50.248  1.00 34.90 ? 53   ARG B CB    1 
ATOM   4495 C  CG    . ARG B 1 53  ? -38.745 -36.405 50.589  1.00 34.46 ? 53   ARG B CG    1 
ATOM   4496 C  CD    . ARG B 1 53  ? -38.609 -35.319 51.655  1.00 36.13 ? 53   ARG B CD    1 
ATOM   4497 N  NE    . ARG B 1 53  ? -37.893 -35.774 52.843  1.00 36.08 ? 53   ARG B NE    1 
ATOM   4498 C  CZ    . ARG B 1 53  ? -38.376 -36.612 53.764  1.00 38.58 ? 53   ARG B CZ    1 
ATOM   4499 N  NH1   . ARG B 1 53  ? -39.600 -37.114 53.665  1.00 35.30 ? 53   ARG B NH1   1 
ATOM   4500 N  NH2   . ARG B 1 53  ? -37.609 -36.972 54.778  1.00 39.54 ? 53   ARG B NH2   1 
ATOM   4501 N  N     . PRO B 1 54  ? -33.929 -36.536 49.524  1.00 31.06 ? 54   PRO B N     1 
ATOM   4502 C  CA    . PRO B 1 54  ? -32.733 -37.292 49.161  1.00 34.28 ? 54   PRO B CA    1 
ATOM   4503 C  C     . PRO B 1 54  ? -32.763 -38.660 49.855  1.00 34.79 ? 54   PRO B C     1 
ATOM   4504 O  O     . PRO B 1 54  ? -33.154 -38.719 51.004  1.00 31.27 ? 54   PRO B O     1 
ATOM   4505 C  CB    . PRO B 1 54  ? -31.578 -36.436 49.701  1.00 32.13 ? 54   PRO B CB    1 
ATOM   4506 C  CG    . PRO B 1 54  ? -32.198 -35.640 50.822  1.00 34.75 ? 54   PRO B CG    1 
ATOM   4507 C  CD    . PRO B 1 54  ? -33.620 -35.378 50.372  1.00 34.01 ? 54   PRO B CD    1 
ATOM   4508 N  N     . TYR B 1 55  ? -32.369 -39.727 49.174  1.00 34.09 ? 55   TYR B N     1 
ATOM   4509 C  CA    . TYR B 1 55  ? -32.345 -41.069 49.811  1.00 38.02 ? 55   TYR B CA    1 
ATOM   4510 C  C     . TYR B 1 55  ? -31.124 -41.192 50.732  1.00 35.82 ? 55   TYR B C     1 
ATOM   4511 O  O     . TYR B 1 55  ? -31.212 -41.828 51.782  1.00 35.12 ? 55   TYR B O     1 
ATOM   4512 C  CB    . TYR B 1 55  ? -32.371 -42.195 48.787  1.00 35.66 ? 55   TYR B CB    1 
ATOM   4513 C  CG    . TYR B 1 55  ? -32.784 -43.516 49.378  1.00 41.24 ? 55   TYR B CG    1 
ATOM   4514 C  CD1   . TYR B 1 55  ? -34.126 -43.859 49.455  1.00 41.79 ? 55   TYR B CD1   1 
ATOM   4515 C  CD2   . TYR B 1 55  ? -31.848 -44.423 49.864  1.00 41.87 ? 55   TYR B CD2   1 
ATOM   4516 C  CE1   . TYR B 1 55  ? -34.534 -45.075 49.978  1.00 43.77 ? 55   TYR B CE1   1 
ATOM   4517 C  CE2   . TYR B 1 55  ? -32.240 -45.636 50.413  1.00 41.81 ? 55   TYR B CE2   1 
ATOM   4518 C  CZ    . TYR B 1 55  ? -33.588 -45.960 50.461  1.00 44.12 ? 55   TYR B CZ    1 
ATOM   4519 O  OH    . TYR B 1 55  ? -34.018 -47.143 50.969  1.00 47.92 ? 55   TYR B OH    1 
ATOM   4520 N  N     . ALA B 1 56  ? -30.002 -40.606 50.327  1.00 34.01 ? 56   ALA B N     1 
ATOM   4521 C  CA    . ALA B 1 56  ? -28.704 -40.742 51.012  1.00 33.24 ? 56   ALA B CA    1 
ATOM   4522 C  C     . ALA B 1 56  ? -27.745 -39.706 50.437  1.00 33.57 ? 56   ALA B C     1 
ATOM   4523 O  O     . ALA B 1 56  ? -28.113 -39.020 49.462  1.00 34.49 ? 56   ALA B O     1 
ATOM   4524 C  CB    . ALA B 1 56  ? -28.169 -42.137 50.809  1.00 32.89 ? 56   ALA B CB    1 
ATOM   4525 N  N     . ALA B 1 57  ? -26.560 -39.618 51.020  1.00 31.08 ? 57   ALA B N     1 
ATOM   4526 C  CA    . ALA B 1 57  ? -25.485 -38.712 50.575  1.00 33.16 ? 57   ALA B CA    1 
ATOM   4527 C  C     . ALA B 1 57  ? -24.169 -39.480 50.580  1.00 31.55 ? 57   ALA B C     1 
ATOM   4528 O  O     . ALA B 1 57  ? -23.941 -40.253 51.526  1.00 32.83 ? 57   ALA B O     1 
ATOM   4529 C  CB    . ALA B 1 57  ? -25.421 -37.502 51.470  1.00 34.95 ? 57   ALA B CB    1 
ATOM   4530 N  N     . VAL B 1 58  ? -23.345 -39.267 49.554  1.00 31.99 ? 58   VAL B N     1 
ATOM   4531 C  CA    . VAL B 1 58  ? -21.950 -39.773 49.514  1.00 30.33 ? 58   VAL B CA    1 
ATOM   4532 C  C     . VAL B 1 58  ? -21.024 -38.552 49.401  1.00 29.82 ? 58   VAL B C     1 
ATOM   4533 O  O     . VAL B 1 58  ? -21.304 -37.653 48.589  1.00 32.00 ? 58   VAL B O     1 
ATOM   4534 C  CB    . VAL B 1 58  ? -21.800 -40.850 48.423  1.00 32.92 ? 58   VAL B CB    1 
ATOM   4535 C  CG1   . VAL B 1 58  ? -22.421 -40.438 47.105  1.00 38.07 ? 58   VAL B CG1   1 
ATOM   4536 C  CG2   . VAL B 1 58  ? -20.353 -41.261 48.209  1.00 34.94 ? 58   VAL B CG2   1 
ATOM   4537 N  N     . ALA B 1 59  ? -19.970 -38.502 50.211  1.00 25.17 ? 59   ALA B N     1 
ATOM   4538 C  CA    . ALA B 1 59  ? -18.971 -37.420 50.257  1.00 25.84 ? 59   ALA B CA    1 
ATOM   4539 C  C     . ALA B 1 59  ? -17.595 -37.917 49.818  1.00 26.80 ? 59   ALA B C     1 
ATOM   4540 O  O     . ALA B 1 59  ? -16.757 -38.253 50.646  1.00 27.10 ? 59   ALA B O     1 
ATOM   4541 C  CB    . ALA B 1 59  ? -18.931 -36.872 51.650  1.00 28.71 ? 59   ALA B CB    1 
ATOM   4542 N  N     . PRO B 1 60  ? -17.281 -37.921 48.508  1.00 28.46 ? 60   PRO B N     1 
ATOM   4543 C  CA    . PRO B 1 60  ? -15.962 -38.345 48.044  1.00 25.73 ? 60   PRO B CA    1 
ATOM   4544 C  C     . PRO B 1 60  ? -14.835 -37.381 48.417  1.00 28.09 ? 60   PRO B C     1 
ATOM   4545 O  O     . PRO B 1 60  ? -15.095 -36.219 48.775  1.00 28.39 ? 60   PRO B O     1 
ATOM   4546 C  CB    . PRO B 1 60  ? -16.108 -38.394 46.520  1.00 26.87 ? 60   PRO B CB    1 
ATOM   4547 C  CG    . PRO B 1 60  ? -17.225 -37.438 46.200  1.00 24.71 ? 60   PRO B CG    1 
ATOM   4548 C  CD    . PRO B 1 60  ? -18.151 -37.499 47.398  1.00 26.95 ? 60   PRO B CD    1 
ATOM   4549 N  N     . ALA B 1 61  ? -13.597 -37.881 48.329  1.00 28.56 ? 61   ALA B N     1 
ATOM   4550 C  CA    . ALA B 1 61  ? -12.378 -37.139 48.728  1.00 28.05 ? 61   ALA B CA    1 
ATOM   4551 C  C     . ALA B 1 61  ? -11.577 -36.702 47.498  1.00 25.46 ? 61   ALA B C     1 
ATOM   4552 O  O     . ALA B 1 61  ? -10.638 -35.952 47.714  1.00 26.24 ? 61   ALA B O     1 
ATOM   4553 C  CB    . ALA B 1 61  ? -11.523 -37.968 49.660  1.00 26.62 ? 61   ALA B CB    1 
ATOM   4554 N  N     . SER B 1 62  ? -11.919 -37.137 46.280  1.00 24.80 ? 62   SER B N     1 
ATOM   4555 C  CA    . SER B 1 62  ? -11.065 -36.915 45.078  1.00 23.95 ? 62   SER B CA    1 
ATOM   4556 C  C     . SER B 1 62  ? -11.857 -37.131 43.786  1.00 23.98 ? 62   SER B C     1 
ATOM   4557 O  O     . SER B 1 62  ? -12.903 -37.798 43.838  1.00 24.56 ? 62   SER B O     1 
ATOM   4558 C  CB    . SER B 1 62  ? -9.878  -37.863 45.103  1.00 24.84 ? 62   SER B CB    1 
ATOM   4559 O  OG    . SER B 1 62  ? -10.305 -39.163 44.755  1.00 23.55 ? 62   SER B OG    1 
ATOM   4560 N  N     . THR B 1 63  ? -11.315 -36.684 42.651  1.00 24.15 ? 63   THR B N     1 
ATOM   4561 C  CA    . THR B 1 63  ? -11.925 -36.889 41.308  1.00 24.98 ? 63   THR B CA    1 
ATOM   4562 C  C     . THR B 1 63  ? -12.069 -38.386 40.993  1.00 23.31 ? 63   THR B C     1 
ATOM   4563 O  O     . THR B 1 63  ? -13.117 -38.783 40.416  1.00 21.89 ? 63   THR B O     1 
ATOM   4564 C  CB    . THR B 1 63  ? -11.112 -36.130 40.258  1.00 25.86 ? 63   THR B CB    1 
ATOM   4565 O  OG1   . THR B 1 63  ? -11.231 -34.760 40.652  1.00 26.01 ? 63   THR B OG1   1 
ATOM   4566 C  CG2   . THR B 1 63  ? -11.601 -36.374 38.845  1.00 26.22 ? 63   THR B CG2   1 
ATOM   4567 N  N     . GLU B 1 64  ? -11.068 -39.207 41.353  1.00 27.63 ? 64   GLU B N     1 
ATOM   4568 C  CA    . GLU B 1 64  ? -11.075 -40.688 41.138  1.00 28.57 ? 64   GLU B CA    1 
ATOM   4569 C  C     . GLU B 1 64  ? -12.273 -41.314 41.879  1.00 24.87 ? 64   GLU B C     1 
ATOM   4570 O  O     . GLU B 1 64  ? -12.982 -42.155 41.302  1.00 24.74 ? 64   GLU B O     1 
ATOM   4571 C  CB    . GLU B 1 64  ? -9.757  -41.286 41.625  1.00 32.69 ? 64   GLU B CB    1 
ATOM   4572 C  CG    . GLU B 1 64  ? -8.575  -40.917 40.741  1.00 40.15 ? 64   GLU B CG    1 
ATOM   4573 C  CD    . GLU B 1 64  ? -8.048  -39.477 40.791  1.00 45.15 ? 64   GLU B CD    1 
ATOM   4574 O  OE1   . GLU B 1 64  ? -8.258  -38.748 41.806  1.00 42.02 ? 64   GLU B OE1   1 
ATOM   4575 O  OE2   . GLU B 1 64  ? -7.432  -39.069 39.788  1.00 56.26 ? 64   GLU B OE2   1 
ATOM   4576 N  N     . GLU B 1 65  ? -12.540 -40.891 43.110  1.00 25.95 ? 65   GLU B N     1 
ATOM   4577 C  CA    . GLU B 1 65  ? -13.715 -41.396 43.876  1.00 26.20 ? 65   GLU B CA    1 
ATOM   4578 C  C     . GLU B 1 65  ? -14.993 -40.919 43.180  1.00 26.73 ? 65   GLU B C     1 
ATOM   4579 O  O     . GLU B 1 65  ? -15.916 -41.740 43.034  1.00 28.92 ? 65   GLU B O     1 
ATOM   4580 C  CB    . GLU B 1 65  ? -13.598 -40.975 45.342  1.00 27.17 ? 65   GLU B CB    1 
ATOM   4581 C  CG    . GLU B 1 65  ? -12.643 -41.853 46.123  1.00 26.76 ? 65   GLU B CG    1 
ATOM   4582 C  CD    . GLU B 1 65  ? -12.367 -41.423 47.541  1.00 28.16 ? 65   GLU B CD    1 
ATOM   4583 O  OE1   . GLU B 1 65  ? -13.212 -40.728 48.149  1.00 27.28 ? 65   GLU B OE1   1 
ATOM   4584 O  OE2   . GLU B 1 65  ? -11.300 -41.830 48.050  1.00 33.48 ? 65   GLU B OE2   1 
ATOM   4585 N  N     . VAL B 1 66  ? -15.042 -39.670 42.684  1.00 24.95 ? 66   VAL B N     1 
ATOM   4586 C  CA    . VAL B 1 66  ? -16.228 -39.203 41.894  1.00 23.43 ? 66   VAL B CA    1 
ATOM   4587 C  C     . VAL B 1 66  ? -16.415 -40.119 40.677  1.00 21.13 ? 66   VAL B C     1 
ATOM   4588 O  O     . VAL B 1 66  ? -17.551 -40.545 40.402  1.00 20.75 ? 66   VAL B O     1 
ATOM   4589 C  CB    . VAL B 1 66  ? -16.124 -37.727 41.464  1.00 21.29 ? 66   VAL B CB    1 
ATOM   4590 C  CG1   . VAL B 1 66  ? -17.230 -37.380 40.494  1.00 21.13 ? 66   VAL B CG1   1 
ATOM   4591 C  CG2   . VAL B 1 66  ? -16.124 -36.796 42.662  1.00 20.32 ? 66   VAL B CG2   1 
ATOM   4592 N  N     . GLN B 1 67  ? -15.353 -40.433 39.950  1.00 23.30 ? 67   GLN B N     1 
ATOM   4593 C  CA    . GLN B 1 67  ? -15.503 -41.252 38.713  1.00 23.14 ? 67   GLN B CA    1 
ATOM   4594 C  C     . GLN B 1 67  ? -16.080 -42.627 39.070  1.00 25.46 ? 67   GLN B C     1 
ATOM   4595 O  O     . GLN B 1 67  ? -16.952 -43.117 38.321  1.00 25.87 ? 67   GLN B O     1 
ATOM   4596 C  CB    . GLN B 1 67  ? -14.170 -41.399 37.991  1.00 24.43 ? 67   GLN B CB    1 
ATOM   4597 C  CG    . GLN B 1 67  ? -13.599 -40.092 37.460  1.00 23.56 ? 67   GLN B CG    1 
ATOM   4598 C  CD    . GLN B 1 67  ? -12.271 -40.342 36.781  1.00 23.79 ? 67   GLN B CD    1 
ATOM   4599 O  OE1   . GLN B 1 67  ? -11.197 -40.162 37.352  1.00 23.38 ? 67   GLN B OE1   1 
ATOM   4600 N  NE2   . GLN B 1 67  ? -12.336 -40.796 35.544  1.00 24.88 ? 67   GLN B NE2   1 
ATOM   4601 N  N     . GLU B 1 68  ? -15.616 -43.215 40.172  1.00 25.36 ? 68   GLU B N     1 
ATOM   4602 C  CA    . GLU B 1 68  ? -16.029 -44.573 40.626  1.00 30.66 ? 68   GLU B CA    1 
ATOM   4603 C  C     . GLU B 1 68  ? -17.504 -44.538 41.042  1.00 28.82 ? 68   GLU B C     1 
ATOM   4604 O  O     . GLU B 1 68  ? -18.278 -45.359 40.552  1.00 30.10 ? 68   GLU B O     1 
ATOM   4605 C  CB    . GLU B 1 68  ? -15.055 -45.044 41.718  1.00 32.00 ? 68   GLU B CB    1 
ATOM   4606 C  CG    . GLU B 1 68  ? -13.706 -45.416 41.106  1.00 34.41 ? 68   GLU B CG    1 
ATOM   4607 C  CD    . GLU B 1 68  ? -12.609 -45.818 42.065  1.00 42.55 ? 68   GLU B CD    1 
ATOM   4608 O  OE1   . GLU B 1 68  ? -12.813 -45.679 43.302  1.00 41.45 ? 68   GLU B OE1   1 
ATOM   4609 O  OE2   . GLU B 1 68  ? -11.538 -46.270 41.558  1.00 54.63 ? 68   GLU B OE2   1 
ATOM   4610 N  N     . ILE B 1 69  ? -17.902 -43.533 41.827  1.00 28.28 ? 69   ILE B N     1 
ATOM   4611 C  CA    . ILE B 1 69  ? -19.323 -43.324 42.234  1.00 25.63 ? 69   ILE B CA    1 
ATOM   4612 C  C     . ILE B 1 69  ? -20.192 -43.231 40.982  1.00 24.75 ? 69   ILE B C     1 
ATOM   4613 O  O     . ILE B 1 69  ? -21.247 -43.872 40.934  1.00 22.51 ? 69   ILE B O     1 
ATOM   4614 C  CB    . ILE B 1 69  ? -19.468 -42.076 43.121  1.00 26.66 ? 69   ILE B CB    1 
ATOM   4615 C  CG1   . ILE B 1 69  ? -18.747 -42.250 44.459  1.00 24.31 ? 69   ILE B CG1   1 
ATOM   4616 C  CG2   . ILE B 1 69  ? -20.937 -41.744 43.321  1.00 27.58 ? 69   ILE B CG2   1 
ATOM   4617 C  CD1   . ILE B 1 69  ? -18.419 -40.958 45.123  1.00 24.88 ? 69   ILE B CD1   1 
ATOM   4618 N  N     . VAL B 1 70  ? -19.757 -42.479 39.975  1.00 25.04 ? 70   VAL B N     1 
ATOM   4619 C  CA    . VAL B 1 70  ? -20.554 -42.310 38.723  1.00 25.08 ? 70   VAL B CA    1 
ATOM   4620 C  C     . VAL B 1 70  ? -20.664 -43.639 37.954  1.00 25.38 ? 70   VAL B C     1 
ATOM   4621 O  O     . VAL B 1 70  ? -21.744 -43.895 37.381  1.00 24.75 ? 70   VAL B O     1 
ATOM   4622 C  CB    . VAL B 1 70  ? -19.998 -41.157 37.858  1.00 23.05 ? 70   VAL B CB    1 
ATOM   4623 C  CG1   . VAL B 1 70  ? -20.636 -41.119 36.487  1.00 22.11 ? 70   VAL B CG1   1 
ATOM   4624 C  CG2   . VAL B 1 70  ? -20.197 -39.823 38.551  1.00 24.43 ? 70   VAL B CG2   1 
ATOM   4625 N  N     . ARG B 1 71  ? -19.599 -44.433 37.853  1.00 26.26 ? 71   ARG B N     1 
ATOM   4626 C  CA    . ARG B 1 71  ? -19.690 -45.779 37.212  1.00 28.93 ? 71   ARG B CA    1 
ATOM   4627 C  C     . ARG B 1 71  ? -20.673 -46.676 37.986  1.00 26.44 ? 71   ARG B C     1 
ATOM   4628 O  O     . ARG B 1 71  ? -21.506 -47.337 37.360  1.00 28.94 ? 71   ARG B O     1 
ATOM   4629 C  CB    . ARG B 1 71  ? -18.308 -46.430 37.144  1.00 31.52 ? 71   ARG B CB    1 
ATOM   4630 C  CG    . ARG B 1 71  ? -17.370 -45.781 36.139  1.00 34.67 ? 71   ARG B CG    1 
ATOM   4631 C  CD    . ARG B 1 71  ? -15.966 -46.312 36.357  1.00 37.97 ? 71   ARG B CD    1 
ATOM   4632 N  NE    . ARG B 1 71  ? -15.008 -45.463 35.676  1.00 43.54 ? 71   ARG B NE    1 
ATOM   4633 C  CZ    . ARG B 1 71  ? -13.833 -45.081 36.183  1.00 47.26 ? 71   ARG B CZ    1 
ATOM   4634 N  NH1   . ARG B 1 71  ? -13.471 -45.448 37.405  1.00 48.42 ? 71   ARG B NH1   1 
ATOM   4635 N  NH2   . ARG B 1 71  ? -13.028 -44.311 35.464  1.00 48.09 ? 71   ARG B NH2   1 
ATOM   4636 N  N     . VAL B 1 72  ? -20.599 -46.677 39.310  1.00 27.08 ? 72   VAL B N     1 
ATOM   4637 C  CA    . VAL B 1 72  ? -21.516 -47.475 40.172  1.00 29.09 ? 72   VAL B CA    1 
ATOM   4638 C  C     . VAL B 1 72  ? -22.945 -47.013 39.909  1.00 31.49 ? 72   VAL B C     1 
ATOM   4639 O  O     . VAL B 1 72  ? -23.803 -47.881 39.663  1.00 36.80 ? 72   VAL B O     1 
ATOM   4640 C  CB    . VAL B 1 72  ? -21.099 -47.366 41.642  1.00 30.58 ? 72   VAL B CB    1 
ATOM   4641 C  CG1   . VAL B 1 72  ? -22.142 -47.931 42.600  1.00 34.31 ? 72   VAL B CG1   1 
ATOM   4642 C  CG2   . VAL B 1 72  ? -19.759 -48.051 41.844  1.00 29.37 ? 72   VAL B CG2   1 
ATOM   4643 N  N     . ALA B 1 73  ? -23.180 -45.696 39.902  1.00 32.30 ? 73   ALA B N     1 
ATOM   4644 C  CA    . ALA B 1 73  ? -24.492 -45.089 39.570  1.00 30.55 ? 73   ALA B CA    1 
ATOM   4645 C  C     . ALA B 1 73  ? -25.002 -45.642 38.233  1.00 29.45 ? 73   ALA B C     1 
ATOM   4646 O  O     . ALA B 1 73  ? -26.200 -46.035 38.195  1.00 29.05 ? 73   ALA B O     1 
ATOM   4647 C  CB    . ALA B 1 73  ? -24.413 -43.586 39.578  1.00 29.84 ? 73   ALA B CB    1 
ATOM   4648 N  N     . ASN B 1 74  ? -24.173 -45.710 37.182  1.00 28.03 ? 74   ASN B N     1 
ATOM   4649 C  CA    . ASN B 1 74  ? -24.626 -46.291 35.889  1.00 27.45 ? 74   ASN B CA    1 
ATOM   4650 C  C     . ASN B 1 74  ? -24.928 -47.788 36.062  1.00 31.55 ? 74   ASN B C     1 
ATOM   4651 O  O     . ASN B 1 74  ? -25.897 -48.244 35.453  1.00 29.21 ? 74   ASN B O     1 
ATOM   4652 C  CB    . ASN B 1 74  ? -23.659 -46.093 34.731  1.00 27.71 ? 74   ASN B CB    1 
ATOM   4653 C  CG    . ASN B 1 74  ? -23.689 -44.684 34.184  1.00 29.08 ? 74   ASN B CG    1 
ATOM   4654 O  OD1   . ASN B 1 74  ? -24.481 -44.356 33.301  1.00 27.34 ? 74   ASN B OD1   1 
ATOM   4655 N  ND2   . ASN B 1 74  ? -22.867 -43.827 34.763  1.00 31.86 ? 74   ASN B ND2   1 
ATOM   4656 N  N     . GLU B 1 75  ? -24.148 -48.516 36.864  1.00 32.42 ? 75   GLU B N     1 
ATOM   4657 C  CA    . GLU B 1 75  ? -24.312 -49.988 37.030  1.00 36.64 ? 75   GLU B CA    1 
ATOM   4658 C  C     . GLU B 1 75  ? -25.709 -50.299 37.595  1.00 34.25 ? 75   GLU B C     1 
ATOM   4659 O  O     . GLU B 1 75  ? -26.395 -51.120 37.034  1.00 32.18 ? 75   GLU B O     1 
ATOM   4660 C  CB    . GLU B 1 75  ? -23.208 -50.559 37.917  1.00 40.16 ? 75   GLU B CB    1 
ATOM   4661 C  CG    . GLU B 1 75  ? -23.056 -52.072 37.783  1.00 46.82 ? 75   GLU B CG    1 
ATOM   4662 C  CD    . GLU B 1 75  ? -21.905 -52.686 38.569  1.00 53.19 ? 75   GLU B CD    1 
ATOM   4663 O  OE1   . GLU B 1 75  ? -21.890 -53.936 38.697  1.00 56.75 ? 75   GLU B OE1   1 
ATOM   4664 O  OE2   . GLU B 1 75  ? -21.016 -51.914 39.045  1.00 50.04 ? 75   GLU B OE2   1 
ATOM   4665 N  N     . PHE B 1 76  ? -26.162 -49.584 38.617  1.00 35.09 ? 76   PHE B N     1 
ATOM   4666 C  CA    . PHE B 1 76  ? -27.403 -49.914 39.356  1.00 33.70 ? 76   PHE B CA    1 
ATOM   4667 C  C     . PHE B 1 76  ? -28.573 -49.007 38.969  1.00 33.87 ? 76   PHE B C     1 
ATOM   4668 O  O     . PHE B 1 76  ? -29.663 -49.204 39.519  1.00 39.26 ? 76   PHE B O     1 
ATOM   4669 C  CB    . PHE B 1 76  ? -27.059 -49.911 40.840  1.00 34.22 ? 76   PHE B CB    1 
ATOM   4670 C  CG    . PHE B 1 76  ? -26.071 -50.996 41.190  1.00 34.70 ? 76   PHE B CG    1 
ATOM   4671 C  CD1   . PHE B 1 76  ? -26.463 -52.330 41.176  1.00 38.05 ? 76   PHE B CD1   1 
ATOM   4672 C  CD2   . PHE B 1 76  ? -24.742 -50.697 41.457  1.00 32.55 ? 76   PHE B CD2   1 
ATOM   4673 C  CE1   . PHE B 1 76  ? -25.558 -53.342 41.467  1.00 36.74 ? 76   PHE B CE1   1 
ATOM   4674 C  CE2   . PHE B 1 76  ? -23.839 -51.709 41.752  1.00 36.11 ? 76   PHE B CE2   1 
ATOM   4675 C  CZ    . PHE B 1 76  ? -24.249 -53.027 41.762  1.00 37.76 ? 76   PHE B CZ    1 
ATOM   4676 N  N     . GLY B 1 77  ? -28.372 -48.065 38.044  1.00 37.55 ? 77   GLY B N     1 
ATOM   4677 C  CA    . GLY B 1 77  ? -29.387 -47.069 37.634  1.00 33.05 ? 77   GLY B CA    1 
ATOM   4678 C  C     . GLY B 1 77  ? -29.781 -46.153 38.786  1.00 31.39 ? 77   GLY B C     1 
ATOM   4679 O  O     . GLY B 1 77  ? -30.962 -45.742 38.834  1.00 28.98 ? 77   GLY B O     1 
ATOM   4680 N  N     . VAL B 1 78  ? -28.839 -45.824 39.680  1.00 30.29 ? 78   VAL B N     1 
ATOM   4681 C  CA    . VAL B 1 78  ? -29.098 -44.967 40.875  1.00 31.14 ? 78   VAL B CA    1 
ATOM   4682 C  C     . VAL B 1 78  ? -28.739 -43.514 40.548  1.00 31.04 ? 78   VAL B C     1 
ATOM   4683 O  O     . VAL B 1 78  ? -27.596 -43.193 40.217  1.00 32.06 ? 78   VAL B O     1 
ATOM   4684 C  CB    . VAL B 1 78  ? -28.352 -45.477 42.118  1.00 33.60 ? 78   VAL B CB    1 
ATOM   4685 C  CG1   . VAL B 1 78  ? -28.432 -44.487 43.265  1.00 32.77 ? 78   VAL B CG1   1 
ATOM   4686 C  CG2   . VAL B 1 78  ? -28.867 -46.843 42.556  1.00 35.48 ? 78   VAL B CG2   1 
ATOM   4687 N  N     . PRO B 1 79  ? -29.708 -42.576 40.602  1.00 29.89 ? 79   PRO B N     1 
ATOM   4688 C  CA    . PRO B 1 79  ? -29.436 -41.189 40.221  1.00 29.17 ? 79   PRO B CA    1 
ATOM   4689 C  C     . PRO B 1 79  ? -28.749 -40.413 41.353  1.00 25.26 ? 79   PRO B C     1 
ATOM   4690 O  O     . PRO B 1 79  ? -28.985 -40.711 42.505  1.00 25.06 ? 79   PRO B O     1 
ATOM   4691 C  CB    . PRO B 1 79  ? -30.831 -40.652 39.854  1.00 29.72 ? 79   PRO B CB    1 
ATOM   4692 C  CG    . PRO B 1 79  ? -31.808 -41.476 40.682  1.00 29.81 ? 79   PRO B CG    1 
ATOM   4693 C  CD    . PRO B 1 79  ? -31.115 -42.791 40.983  1.00 31.58 ? 79   PRO B CD    1 
ATOM   4694 N  N     . LEU B 1 80  ? -27.881 -39.470 40.973  1.00 23.91 ? 80   LEU B N     1 
ATOM   4695 C  CA    . LEU B 1 80  ? -27.038 -38.627 41.859  1.00 23.70 ? 80   LEU B CA    1 
ATOM   4696 C  C     . LEU B 1 80  ? -27.448 -37.156 41.742  1.00 25.52 ? 80   LEU B C     1 
ATOM   4697 O  O     . LEU B 1 80  ? -27.889 -36.762 40.646  1.00 26.18 ? 80   LEU B O     1 
ATOM   4698 C  CB    . LEU B 1 80  ? -25.587 -38.756 41.409  1.00 25.95 ? 80   LEU B CB    1 
ATOM   4699 C  CG    . LEU B 1 80  ? -24.997 -40.165 41.403  1.00 24.93 ? 80   LEU B CG    1 
ATOM   4700 C  CD1   . LEU B 1 80  ? -23.604 -40.128 40.833  1.00 25.27 ? 80   LEU B CD1   1 
ATOM   4701 C  CD2   . LEU B 1 80  ? -24.957 -40.714 42.810  1.00 24.87 ? 80   LEU B CD2   1 
ATOM   4702 N  N     . TRP B 1 81  ? -27.243 -36.377 42.807  1.00 23.90 ? 81   TRP B N     1 
ATOM   4703 C  CA    . TRP B 1 81  ? -27.450 -34.910 42.836  1.00 25.63 ? 81   TRP B CA    1 
ATOM   4704 C  C     . TRP B 1 81  ? -26.145 -34.261 43.263  1.00 24.98 ? 81   TRP B C     1 
ATOM   4705 O  O     . TRP B 1 81  ? -25.828 -34.184 44.459  1.00 25.95 ? 81   TRP B O     1 
ATOM   4706 C  CB    . TRP B 1 81  ? -28.616 -34.513 43.758  1.00 28.89 ? 81   TRP B CB    1 
ATOM   4707 C  CG    . TRP B 1 81  ? -28.980 -33.065 43.646  1.00 27.05 ? 81   TRP B CG    1 
ATOM   4708 C  CD1   . TRP B 1 81  ? -28.554 -32.033 44.429  1.00 28.81 ? 81   TRP B CD1   1 
ATOM   4709 C  CD2   . TRP B 1 81  ? -29.867 -32.493 42.668  1.00 28.26 ? 81   TRP B CD2   1 
ATOM   4710 N  NE1   . TRP B 1 81  ? -29.089 -30.851 43.979  1.00 29.43 ? 81   TRP B NE1   1 
ATOM   4711 C  CE2   . TRP B 1 81  ? -29.903 -31.105 42.905  1.00 26.71 ? 81   TRP B CE2   1 
ATOM   4712 C  CE3   . TRP B 1 81  ? -30.652 -33.022 41.639  1.00 26.62 ? 81   TRP B CE3   1 
ATOM   4713 C  CZ2   . TRP B 1 81  ? -30.689 -30.252 42.135  1.00 25.92 ? 81   TRP B CZ2   1 
ATOM   4714 C  CZ3   . TRP B 1 81  ? -31.421 -32.172 40.876  1.00 25.52 ? 81   TRP B CZ3   1 
ATOM   4715 C  CH2   . TRP B 1 81  ? -31.426 -30.808 41.116  1.00 25.65 ? 81   TRP B CH2   1 
ATOM   4716 N  N     . PRO B 1 82  ? -25.326 -33.817 42.287  1.00 24.44 ? 82   PRO B N     1 
ATOM   4717 C  CA    . PRO B 1 82  ? -24.039 -33.209 42.590  1.00 25.65 ? 82   PRO B CA    1 
ATOM   4718 C  C     . PRO B 1 82  ? -24.211 -31.809 43.176  1.00 27.82 ? 82   PRO B C     1 
ATOM   4719 O  O     . PRO B 1 82  ? -24.887 -30.964 42.550  1.00 29.72 ? 82   PRO B O     1 
ATOM   4720 C  CB    . PRO B 1 82  ? -23.351 -33.113 41.227  1.00 25.70 ? 82   PRO B CB    1 
ATOM   4721 C  CG    . PRO B 1 82  ? -24.109 -34.070 40.356  1.00 25.56 ? 82   PRO B CG    1 
ATOM   4722 C  CD    . PRO B 1 82  ? -25.527 -33.993 40.842  1.00 25.68 ? 82   PRO B CD    1 
ATOM   4723 N  N     . VAL B 1 83  ? -23.567 -31.597 44.318  1.00 27.58 ? 83   VAL B N     1 
ATOM   4724 C  CA    . VAL B 1 83  ? -23.414 -30.274 44.979  1.00 28.08 ? 83   VAL B CA    1 
ATOM   4725 C  C     . VAL B 1 83  ? -21.933 -30.097 45.310  1.00 29.97 ? 83   VAL B C     1 
ATOM   4726 O  O     . VAL B 1 83  ? -21.258 -31.111 45.607  1.00 29.60 ? 83   VAL B O     1 
ATOM   4727 C  CB    . VAL B 1 83  ? -24.312 -30.167 46.228  1.00 26.42 ? 83   VAL B CB    1 
ATOM   4728 C  CG1   . VAL B 1 83  ? -25.720 -30.574 45.885  1.00 26.34 ? 83   VAL B CG1   1 
ATOM   4729 C  CG2   . VAL B 1 83  ? -23.808 -30.981 47.416  1.00 28.33 ? 83   VAL B CG2   1 
ATOM   4730 N  N     . SER B 1 84  ? -21.452 -28.856 45.253  1.00 29.13 ? 84   SER B N     1 
ATOM   4731 C  CA    . SER B 1 84  ? -20.070 -28.488 45.624  1.00 27.49 ? 84   SER B CA    1 
ATOM   4732 C  C     . SER B 1 84  ? -19.989 -28.339 47.147  1.00 28.09 ? 84   SER B C     1 
ATOM   4733 O  O     . SER B 1 84  ? -19.137 -29.026 47.772  1.00 26.00 ? 84   SER B O     1 
ATOM   4734 C  CB    . SER B 1 84  ? -19.652 -27.252 44.897  1.00 28.24 ? 84   SER B CB    1 
ATOM   4735 O  OG    . SER B 1 84  ? -19.619 -27.505 43.502  1.00 27.08 ? 84   SER B OG    1 
ATOM   4736 N  N     . ARG B 1 85  ? -20.830 -27.484 47.739  1.00 26.77 ? 85   ARG B N     1 
ATOM   4737 C  CA    . ARG B 1 85  ? -20.975 -27.430 49.220  1.00 28.44 ? 85   ARG B CA    1 
ATOM   4738 C  C     . ARG B 1 85  ? -22.437 -27.515 49.665  1.00 27.23 ? 85   ARG B C     1 
ATOM   4739 O  O     . ARG B 1 85  ? -22.656 -27.605 50.882  1.00 27.12 ? 85   ARG B O     1 
ATOM   4740 C  CB    . ARG B 1 85  ? -20.267 -26.191 49.770  1.00 27.62 ? 85   ARG B CB    1 
ATOM   4741 C  CG    . ARG B 1 85  ? -18.761 -26.227 49.564  1.00 29.30 ? 85   ARG B CG    1 
ATOM   4742 C  CD    . ARG B 1 85  ? -18.056 -25.005 50.110  1.00 30.42 ? 85   ARG B CD    1 
ATOM   4743 N  NE    . ARG B 1 85  ? -18.511 -24.643 51.449  1.00 32.09 ? 85   ARG B NE    1 
ATOM   4744 C  CZ    . ARG B 1 85  ? -18.022 -25.102 52.594  1.00 30.60 ? 85   ARG B CZ    1 
ATOM   4745 N  NH1   . ARG B 1 85  ? -17.047 -25.990 52.602  1.00 29.60 ? 85   ARG B NH1   1 
ATOM   4746 N  NH2   . ARG B 1 85  ? -18.508 -24.650 53.734  1.00 30.58 ? 85   ARG B NH2   1 
ATOM   4747 N  N     . GLY B 1 86  ? -23.396 -27.487 48.740  1.00 26.42 ? 86   GLY B N     1 
ATOM   4748 C  CA    . GLY B 1 86  ? -24.830 -27.646 49.064  1.00 28.68 ? 86   GLY B CA    1 
ATOM   4749 C  C     . GLY B 1 86  ? -25.407 -26.521 49.924  1.00 29.72 ? 86   GLY B C     1 
ATOM   4750 O  O     . GLY B 1 86  ? -26.423 -26.787 50.599  1.00 27.71 ? 86   GLY B O     1 
ATOM   4751 N  N     . LYS B 1 87  ? -24.855 -25.295 49.865  1.00 26.45 ? 87   LYS B N     1 
ATOM   4752 C  CA    . LYS B 1 87  ? -25.358 -24.135 50.638  1.00 28.18 ? 87   LYS B CA    1 
ATOM   4753 C  C     . LYS B 1 87  ? -26.378 -23.341 49.808  1.00 25.76 ? 87   LYS B C     1 
ATOM   4754 O  O     . LYS B 1 87  ? -26.514 -22.131 50.057  1.00 23.91 ? 87   LYS B O     1 
ATOM   4755 C  CB    . LYS B 1 87  ? -24.187 -23.260 51.087  1.00 28.96 ? 87   LYS B CB    1 
ATOM   4756 C  CG    . LYS B 1 87  ? -23.092 -24.006 51.832  1.00 31.73 ? 87   LYS B CG    1 
ATOM   4757 C  CD    . LYS B 1 87  ? -23.535 -24.651 53.140  1.00 33.23 ? 87   LYS B CD    1 
ATOM   4758 C  CE    . LYS B 1 87  ? -22.451 -25.536 53.717  1.00 33.70 ? 87   LYS B CE    1 
ATOM   4759 N  NZ    . LYS B 1 87  ? -22.985 -26.349 54.818  1.00 34.56 ? 87   LYS B NZ    1 
ATOM   4760 N  N     . ASN B 1 88  ? -27.100 -23.989 48.893  1.00 24.51 ? 88   ASN B N     1 
ATOM   4761 C  CA    . ASN B 1 88  ? -28.019 -23.304 47.948  1.00 25.44 ? 88   ASN B CA    1 
ATOM   4762 C  C     . ASN B 1 88  ? -29.349 -22.969 48.664  1.00 26.07 ? 88   ASN B C     1 
ATOM   4763 O  O     . ASN B 1 88  ? -30.429 -23.235 48.123  1.00 27.30 ? 88   ASN B O     1 
ATOM   4764 C  CB    . ASN B 1 88  ? -28.145 -24.087 46.633  1.00 27.06 ? 88   ASN B CB    1 
ATOM   4765 C  CG    . ASN B 1 88  ? -28.320 -23.201 45.403  1.00 29.65 ? 88   ASN B CG    1 
ATOM   4766 O  OD1   . ASN B 1 88  ? -28.024 -21.999 45.416  1.00 27.51 ? 88   ASN B OD1   1 
ATOM   4767 N  ND2   . ASN B 1 88  ? -28.864 -23.770 44.343  1.00 27.87 ? 88   ASN B ND2   1 
ATOM   4768 N  N     . PHE B 1 89  ? -29.272 -22.333 49.831  1.00 26.46 ? 89   PHE B N     1 
ATOM   4769 C  CA    . PHE B 1 89  ? -30.438 -21.839 50.617  1.00 28.75 ? 89   PHE B CA    1 
ATOM   4770 C  C     . PHE B 1 89  ? -31.241 -20.856 49.738  1.00 26.96 ? 89   PHE B C     1 
ATOM   4771 O  O     . PHE B 1 89  ? -30.612 -20.052 49.026  1.00 29.40 ? 89   PHE B O     1 
ATOM   4772 C  CB    . PHE B 1 89  ? -29.931 -21.305 51.966  1.00 32.48 ? 89   PHE B CB    1 
ATOM   4773 C  CG    . PHE B 1 89  ? -29.073 -22.287 52.744  1.00 34.74 ? 89   PHE B CG    1 
ATOM   4774 C  CD1   . PHE B 1 89  ? -29.342 -23.657 52.720  1.00 39.60 ? 89   PHE B CD1   1 
ATOM   4775 C  CD2   . PHE B 1 89  ? -27.961 -21.863 53.451  1.00 37.94 ? 89   PHE B CD2   1 
ATOM   4776 C  CE1   . PHE B 1 89  ? -28.540 -24.570 53.401  1.00 38.45 ? 89   PHE B CE1   1 
ATOM   4777 C  CE2   . PHE B 1 89  ? -27.165 -22.772 54.146  1.00 37.70 ? 89   PHE B CE2   1 
ATOM   4778 C  CZ    . PHE B 1 89  ? -27.457 -24.121 54.120  1.00 36.26 ? 89   PHE B CZ    1 
ATOM   4779 N  N     . ALA B 1 90  ? -32.564 -21.028 49.684  1.00 24.45 ? 90   ALA B N     1 
ATOM   4780 C  CA    . ALA B 1 90  ? -33.550 -20.244 48.887  1.00 27.74 ? 90   ALA B CA    1 
ATOM   4781 C  C     . ALA B 1 90  ? -33.798 -20.916 47.537  1.00 26.74 ? 90   ALA B C     1 
ATOM   4782 O  O     . ALA B 1 90  ? -34.748 -20.491 46.815  1.00 27.92 ? 90   ALA B O     1 
ATOM   4783 C  CB    . ALA B 1 90  ? -33.116 -18.805 48.701  1.00 28.61 ? 90   ALA B CB    1 
ATOM   4784 N  N     . TYR B 1 91  ? -32.979 -21.921 47.209  1.00 26.08 ? 91   TYR B N     1 
ATOM   4785 C  CA    . TYR B 1 91  ? -33.094 -22.706 45.958  1.00 25.92 ? 91   TYR B CA    1 
ATOM   4786 C  C     . TYR B 1 91  ? -33.214 -24.200 46.258  1.00 26.96 ? 91   TYR B C     1 
ATOM   4787 O  O     . TYR B 1 91  ? -33.180 -24.969 45.296  1.00 24.88 ? 91   TYR B O     1 
ATOM   4788 C  CB    . TYR B 1 91  ? -31.918 -22.398 45.039  1.00 26.20 ? 91   TYR B CB    1 
ATOM   4789 C  CG    . TYR B 1 91  ? -31.835 -20.950 44.623  1.00 28.36 ? 91   TYR B CG    1 
ATOM   4790 C  CD1   . TYR B 1 91  ? -32.706 -20.420 43.685  1.00 30.17 ? 91   TYR B CD1   1 
ATOM   4791 C  CD2   . TYR B 1 91  ? -30.864 -20.112 45.147  1.00 29.18 ? 91   TYR B CD2   1 
ATOM   4792 C  CE1   . TYR B 1 91  ? -32.614 -19.099 43.274  1.00 29.09 ? 91   TYR B CE1   1 
ATOM   4793 C  CE2   . TYR B 1 91  ? -30.767 -18.786 44.760  1.00 30.40 ? 91   TYR B CE2   1 
ATOM   4794 C  CZ    . TYR B 1 91  ? -31.643 -18.279 43.820  1.00 28.67 ? 91   TYR B CZ    1 
ATOM   4795 O  OH    . TYR B 1 91  ? -31.541 -16.971 43.464  1.00 26.59 ? 91   TYR B OH    1 
ATOM   4796 N  N     . GLY B 1 92  ? -33.391 -24.578 47.532  1.00 28.88 ? 92   GLY B N     1 
ATOM   4797 C  CA    . GLY B 1 92  ? -33.692 -25.956 47.964  1.00 28.20 ? 92   GLY B CA    1 
ATOM   4798 C  C     . GLY B 1 92  ? -32.545 -26.579 48.744  1.00 27.27 ? 92   GLY B C     1 
ATOM   4799 O  O     . GLY B 1 92  ? -32.634 -27.780 49.047  1.00 28.31 ? 92   GLY B O     1 
ATOM   4800 N  N     . GLY B 1 93  ? -31.494 -25.805 49.023  1.00 25.55 ? 93   GLY B N     1 
ATOM   4801 C  CA    . GLY B 1 93  ? -30.271 -26.298 49.681  1.00 28.67 ? 93   GLY B CA    1 
ATOM   4802 C  C     . GLY B 1 93  ? -29.588 -27.376 48.843  1.00 29.68 ? 93   GLY B C     1 
ATOM   4803 O  O     . GLY B 1 93  ? -29.366 -27.142 47.637  1.00 26.90 ? 93   GLY B O     1 
ATOM   4804 N  N     . ALA B 1 94  ? -29.309 -28.527 49.456  1.00 28.38 ? 94   ALA B N     1 
ATOM   4805 C  CA    . ALA B 1 94  ? -28.622 -29.685 48.840  1.00 28.11 ? 94   ALA B CA    1 
ATOM   4806 C  C     . ALA B 1 94  ? -29.658 -30.724 48.389  1.00 27.87 ? 94   ALA B C     1 
ATOM   4807 O  O     . ALA B 1 94  ? -29.275 -31.824 47.946  1.00 26.35 ? 94   ALA B O     1 
ATOM   4808 C  CB    . ALA B 1 94  ? -27.659 -30.259 49.849  1.00 31.38 ? 94   ALA B CB    1 
ATOM   4809 N  N     . ALA B 1 95  ? -30.941 -30.379 48.447  1.00 26.34 ? 95   ALA B N     1 
ATOM   4810 C  CA    . ALA B 1 95  ? -32.032 -31.335 48.174  1.00 27.40 ? 95   ALA B CA    1 
ATOM   4811 C  C     . ALA B 1 95  ? -32.208 -31.439 46.666  1.00 26.79 ? 95   ALA B C     1 
ATOM   4812 O  O     . ALA B 1 95  ? -32.052 -30.454 45.934  1.00 26.99 ? 95   ALA B O     1 
ATOM   4813 C  CB    . ALA B 1 95  ? -33.308 -30.908 48.890  1.00 27.73 ? 95   ALA B CB    1 
ATOM   4814 N  N     . PRO B 1 96  ? -32.547 -32.645 46.165  1.00 27.48 ? 96   PRO B N     1 
ATOM   4815 C  CA    . PRO B 1 96  ? -32.777 -32.855 44.741  1.00 27.79 ? 96   PRO B CA    1 
ATOM   4816 C  C     . PRO B 1 96  ? -34.206 -32.518 44.309  1.00 28.36 ? 96   PRO B C     1 
ATOM   4817 O  O     . PRO B 1 96  ? -35.113 -32.552 45.138  1.00 31.69 ? 96   PRO B O     1 
ATOM   4818 C  CB    . PRO B 1 96  ? -32.562 -34.358 44.595  1.00 28.47 ? 96   PRO B CB    1 
ATOM   4819 C  CG    . PRO B 1 96  ? -33.117 -34.901 45.901  1.00 30.20 ? 96   PRO B CG    1 
ATOM   4820 C  CD    . PRO B 1 96  ? -32.665 -33.893 46.940  1.00 30.29 ? 96   PRO B CD    1 
ATOM   4821 N  N     . VAL B 1 97  ? -34.390 -32.298 43.016  1.00 26.61 ? 97   VAL B N     1 
ATOM   4822 C  CA    . VAL B 1 97  ? -35.741 -32.223 42.408  1.00 29.34 ? 97   VAL B CA    1 
ATOM   4823 C  C     . VAL B 1 97  ? -36.529 -33.502 42.727  1.00 31.50 ? 97   VAL B C     1 
ATOM   4824 O  O     . VAL B 1 97  ? -37.695 -33.366 43.167  1.00 31.63 ? 97   VAL B O     1 
ATOM   4825 C  CB    . VAL B 1 97  ? -35.669 -31.973 40.900  1.00 30.17 ? 97   VAL B CB    1 
ATOM   4826 C  CG1   . VAL B 1 97  ? -37.063 -32.079 40.289  1.00 31.53 ? 97   VAL B CG1   1 
ATOM   4827 C  CG2   . VAL B 1 97  ? -35.018 -30.615 40.603  1.00 30.26 ? 97   VAL B CG2   1 
ATOM   4828 N  N     . MET B 1 98  ? -35.933 -34.682 42.513  1.00 30.26 ? 98   MET B N     1 
ATOM   4829 C  CA    . MET B 1 98  ? -36.657 -35.977 42.474  1.00 31.19 ? 98   MET B CA    1 
ATOM   4830 C  C     . MET B 1 98  ? -36.276 -36.782 43.714  1.00 32.68 ? 98   MET B C     1 
ATOM   4831 O  O     . MET B 1 98  ? -35.080 -37.056 43.897  1.00 35.50 ? 98   MET B O     1 
ATOM   4832 C  CB    . MET B 1 98  ? -36.314 -36.778 41.217  1.00 33.43 ? 98   MET B CB    1 
ATOM   4833 C  CG    . MET B 1 98  ? -37.190 -38.032 41.032  1.00 32.92 ? 98   MET B CG    1 
ATOM   4834 S  SD    . MET B 1 98  ? -36.576 -39.088 39.685  1.00 35.61 ? 98   MET B SD    1 
ATOM   4835 C  CE    . MET B 1 98  ? -35.082 -39.713 40.461  1.00 33.66 ? 98   MET B CE    1 
ATOM   4836 N  N     . SER B 1 99  ? -37.266 -37.110 44.539  1.00 31.43 ? 99   SER B N     1 
ATOM   4837 C  CA    . SER B 1 99  ? -37.127 -37.974 45.739  1.00 34.40 ? 99   SER B CA    1 
ATOM   4838 C  C     . SER B 1 99  ? -36.436 -39.287 45.377  1.00 31.34 ? 99   SER B C     1 
ATOM   4839 O  O     . SER B 1 99  ? -36.683 -39.835 44.284  1.00 30.22 ? 99   SER B O     1 
ATOM   4840 C  CB    . SER B 1 99  ? -38.463 -38.210 46.406  1.00 33.67 ? 99   SER B CB    1 
ATOM   4841 O  OG    . SER B 1 99  ? -38.820 -37.045 47.147  1.00 33.94 ? 99   SER B OG    1 
ATOM   4842 N  N     . GLY B 1 100 ? -35.561 -39.737 46.269  1.00 33.67 ? 100  GLY B N     1 
ATOM   4843 C  CA    . GLY B 1 100 ? -34.808 -40.995 46.113  1.00 34.26 ? 100  GLY B CA    1 
ATOM   4844 C  C     . GLY B 1 100 ? -33.508 -40.805 45.348  1.00 33.21 ? 100  GLY B C     1 
ATOM   4845 O  O     . GLY B 1 100 ? -32.766 -41.784 45.234  1.00 33.65 ? 100  GLY B O     1 
ATOM   4846 N  N     . THR B 1 101 ? -33.251 -39.607 44.815  1.00 30.27 ? 101  THR B N     1 
ATOM   4847 C  CA    . THR B 1 101 ? -31.934 -39.214 44.270  1.00 27.62 ? 101  THR B CA    1 
ATOM   4848 C  C     . THR B 1 101 ? -30.939 -39.219 45.436  1.00 28.63 ? 101  THR B C     1 
ATOM   4849 O  O     . THR B 1 101 ? -31.315 -38.800 46.533  1.00 28.41 ? 101  THR B O     1 
ATOM   4850 C  CB    . THR B 1 101 ? -31.996 -37.852 43.562  1.00 29.45 ? 101  THR B CB    1 
ATOM   4851 O  OG1   . THR B 1 101 ? -32.976 -37.908 42.515  1.00 26.39 ? 101  THR B OG1   1 
ATOM   4852 C  CG2   . THR B 1 101 ? -30.658 -37.463 42.966  1.00 29.87 ? 101  THR B CG2   1 
ATOM   4853 N  N     . VAL B 1 102 ? -29.719 -39.719 45.213  1.00 27.86 ? 102  VAL B N     1 
ATOM   4854 C  CA    . VAL B 1 102 ? -28.620 -39.704 46.215  1.00 25.41 ? 102  VAL B CA    1 
ATOM   4855 C  C     . VAL B 1 102 ? -27.768 -38.453 45.991  1.00 24.86 ? 102  VAL B C     1 
ATOM   4856 O  O     . VAL B 1 102 ? -27.291 -38.259 44.865  1.00 29.31 ? 102  VAL B O     1 
ATOM   4857 C  CB    . VAL B 1 102 ? -27.790 -40.995 46.095  1.00 25.63 ? 102  VAL B CB    1 
ATOM   4858 C  CG1   . VAL B 1 102 ? -26.549 -40.957 46.964  1.00 26.29 ? 102  VAL B CG1   1 
ATOM   4859 C  CG2   . VAL B 1 102 ? -28.632 -42.219 46.396  1.00 26.08 ? 102  VAL B CG2   1 
ATOM   4860 N  N     . VAL B 1 103 ? -27.485 -37.694 47.044  1.00 25.40 ? 103  VAL B N     1 
ATOM   4861 C  CA    . VAL B 1 103 ? -26.661 -36.458 46.965  1.00 25.42 ? 103  VAL B CA    1 
ATOM   4862 C  C     . VAL B 1 103 ? -25.189 -36.851 46.873  1.00 28.27 ? 103  VAL B C     1 
ATOM   4863 O  O     . VAL B 1 103 ? -24.681 -37.633 47.725  1.00 27.81 ? 103  VAL B O     1 
ATOM   4864 C  CB    . VAL B 1 103 ? -26.939 -35.483 48.126  1.00 26.76 ? 103  VAL B CB    1 
ATOM   4865 C  CG1   . VAL B 1 103 ? -26.033 -34.262 48.059  1.00 28.39 ? 103  VAL B CG1   1 
ATOM   4866 C  CG2   . VAL B 1 103 ? -28.389 -35.052 48.135  1.00 24.45 ? 103  VAL B CG2   1 
ATOM   4867 N  N     . LEU B 1 104 ? -24.522 -36.319 45.846  1.00 28.32 ? 104  LEU B N     1 
ATOM   4868 C  CA    . LEU B 1 104 ? -23.064 -36.426 45.663  1.00 25.42 ? 104  LEU B CA    1 
ATOM   4869 C  C     . LEU B 1 104 ? -22.460 -35.135 46.188  1.00 24.94 ? 104  LEU B C     1 
ATOM   4870 O  O     . LEU B 1 104 ? -22.460 -34.139 45.456  1.00 24.94 ? 104  LEU B O     1 
ATOM   4871 C  CB    . LEU B 1 104 ? -22.772 -36.678 44.178  1.00 28.46 ? 104  LEU B CB    1 
ATOM   4872 C  CG    . LEU B 1 104 ? -21.293 -36.729 43.807  1.00 28.38 ? 104  LEU B CG    1 
ATOM   4873 C  CD1   . LEU B 1 104 ? -20.498 -37.510 44.831  1.00 30.66 ? 104  LEU B CD1   1 
ATOM   4874 C  CD2   . LEU B 1 104 ? -21.096 -37.318 42.428  1.00 29.17 ? 104  LEU B CD2   1 
ATOM   4875 N  N     . ASP B 1 105 ? -21.985 -35.160 47.427  1.00 24.52 ? 105  ASP B N     1 
ATOM   4876 C  CA    . ASP B 1 105 ? -21.508 -33.976 48.173  1.00 24.08 ? 105  ASP B CA    1 
ATOM   4877 C  C     . ASP B 1 105 ? -19.981 -33.920 48.120  1.00 26.88 ? 105  ASP B C     1 
ATOM   4878 O  O     . ASP B 1 105 ? -19.294 -34.808 48.719  1.00 25.90 ? 105  ASP B O     1 
ATOM   4879 C  CB    . ASP B 1 105 ? -22.072 -34.019 49.586  1.00 28.27 ? 105  ASP B CB    1 
ATOM   4880 C  CG    . ASP B 1 105 ? -21.573 -32.938 50.519  1.00 30.89 ? 105  ASP B CG    1 
ATOM   4881 O  OD1   . ASP B 1 105 ? -20.853 -32.014 50.061  1.00 30.38 ? 105  ASP B OD1   1 
ATOM   4882 O  OD2   . ASP B 1 105 ? -21.926 -33.031 51.709  1.00 38.03 ? 105  ASP B OD2   1 
ATOM   4883 N  N     . MET B 1 106 ? -19.444 -32.894 47.451  1.00 25.44 ? 106  MET B N     1 
ATOM   4884 C  CA    . MET B 1 106 ? -17.993 -32.788 47.214  1.00 26.10 ? 106  MET B CA    1 
ATOM   4885 C  C     . MET B 1 106 ? -17.362 -31.775 48.158  1.00 24.05 ? 106  MET B C     1 
ATOM   4886 O  O     . MET B 1 106 ? -16.287 -31.315 47.823  1.00 23.98 ? 106  MET B O     1 
ATOM   4887 C  CB    . MET B 1 106 ? -17.733 -32.445 45.748  1.00 28.76 ? 106  MET B CB    1 
ATOM   4888 C  CG    . MET B 1 106 ? -18.148 -33.581 44.833  1.00 30.38 ? 106  MET B CG    1 
ATOM   4889 S  SD    . MET B 1 106 ? -17.822 -33.239 43.079  1.00 32.88 ? 106  MET B SD    1 
ATOM   4890 C  CE    . MET B 1 106 ? -19.295 -32.309 42.659  1.00 38.23 ? 106  MET B CE    1 
ATOM   4891 N  N     . ASN B 1 107 ? -17.933 -31.516 49.346  1.00 24.57 ? 107  ASN B N     1 
ATOM   4892 C  CA    . ASN B 1 107 ? -17.365 -30.479 50.255  1.00 25.99 ? 107  ASN B CA    1 
ATOM   4893 C  C     . ASN B 1 107 ? -15.954 -30.872 50.730  1.00 25.54 ? 107  ASN B C     1 
ATOM   4894 O  O     . ASN B 1 107 ? -15.111 -29.965 50.997  1.00 23.56 ? 107  ASN B O     1 
ATOM   4895 C  CB    . ASN B 1 107 ? -18.307 -30.161 51.417  1.00 32.01 ? 107  ASN B CB    1 
ATOM   4896 C  CG    . ASN B 1 107 ? -18.160 -31.154 52.539  1.00 34.78 ? 107  ASN B CG    1 
ATOM   4897 O  OD1   . ASN B 1 107 ? -17.386 -30.937 53.470  1.00 37.21 ? 107  ASN B OD1   1 
ATOM   4898 N  ND2   . ASN B 1 107 ? -18.858 -32.275 52.421  1.00 40.74 ? 107  ASN B ND2   1 
ATOM   4899 N  N     . ARG B 1 108 ? -15.655 -32.171 50.806  1.00 25.33 ? 108  ARG B N     1 
ATOM   4900 C  CA    . ARG B 1 108 ? -14.355 -32.664 51.314  1.00 25.12 ? 108  ARG B CA    1 
ATOM   4901 C  C     . ARG B 1 108 ? -13.290 -32.454 50.233  1.00 25.54 ? 108  ARG B C     1 
ATOM   4902 O  O     . ARG B 1 108 ? -12.120 -32.325 50.626  1.00 25.26 ? 108  ARG B O     1 
ATOM   4903 C  CB    . ARG B 1 108 ? -14.435 -34.139 51.721  1.00 28.39 ? 108  ARG B CB    1 
ATOM   4904 C  CG    . ARG B 1 108 ? -15.349 -34.390 52.913  1.00 30.67 ? 108  ARG B CG    1 
ATOM   4905 C  CD    . ARG B 1 108 ? -15.564 -35.865 53.165  1.00 32.83 ? 108  ARG B CD    1 
ATOM   4906 N  NE    . ARG B 1 108 ? -14.294 -36.443 53.582  1.00 34.51 ? 108  ARG B NE    1 
ATOM   4907 C  CZ    . ARG B 1 108 ? -13.723 -37.519 53.056  1.00 34.45 ? 108  ARG B CZ    1 
ATOM   4908 N  NH1   . ARG B 1 108 ? -14.317 -38.238 52.111  1.00 35.47 ? 108  ARG B NH1   1 
ATOM   4909 N  NH2   . ARG B 1 108 ? -12.546 -37.889 53.517  1.00 33.48 ? 108  ARG B NH2   1 
ATOM   4910 N  N     . MET B 1 109 ? -13.661 -32.363 48.949  1.00 24.21 ? 109  MET B N     1 
ATOM   4911 C  CA    . MET B 1 109 ? -12.703 -31.969 47.869  1.00 24.39 ? 109  MET B CA    1 
ATOM   4912 C  C     . MET B 1 109 ? -12.535 -30.451 47.935  1.00 24.80 ? 109  MET B C     1 
ATOM   4913 O  O     . MET B 1 109 ? -13.227 -29.719 47.176  1.00 22.35 ? 109  MET B O     1 
ATOM   4914 C  CB    . MET B 1 109 ? -13.195 -32.415 46.492  1.00 24.84 ? 109  MET B CB    1 
ATOM   4915 C  CG    . MET B 1 109 ? -13.290 -33.940 46.370  1.00 25.40 ? 109  MET B CG    1 
ATOM   4916 S  SD    . MET B 1 109 ? -14.201 -34.521 44.930  1.00 30.82 ? 109  MET B SD    1 
ATOM   4917 C  CE    . MET B 1 109 ? -13.150 -33.901 43.618  1.00 29.77 ? 109  MET B CE    1 
ATOM   4918 N  N     . ASN B 1 110 ? -11.682 -29.978 48.840  1.00 23.25 ? 110  ASN B N     1 
ATOM   4919 C  CA    . ASN B 1 110 ? -11.601 -28.533 49.187  1.00 25.00 ? 110  ASN B CA    1 
ATOM   4920 C  C     . ASN B 1 110 ? -10.183 -28.011 49.004  1.00 24.60 ? 110  ASN B C     1 
ATOM   4921 O  O     . ASN B 1 110 ? -9.791  -27.123 49.776  1.00 26.96 ? 110  ASN B O     1 
ATOM   4922 C  CB    . ASN B 1 110 ? -12.064 -28.262 50.619  1.00 28.15 ? 110  ASN B CB    1 
ATOM   4923 C  CG    . ASN B 1 110 ? -11.223 -28.960 51.677  1.00 30.17 ? 110  ASN B CG    1 
ATOM   4924 O  OD1   . ASN B 1 110 ? -10.390 -29.816 51.399  1.00 28.66 ? 110  ASN B OD1   1 
ATOM   4925 N  ND2   . ASN B 1 110 ? -11.415 -28.575 52.917  1.00 35.18 ? 110  ASN B ND2   1 
ATOM   4926 N  N     . ARG B 1 111 ? -9.417  -28.551 48.063  1.00 24.33 ? 111  ARG B N     1 
ATOM   4927 C  CA    . ARG B 1 111 ? -8.021  -28.105 47.850  1.00 26.23 ? 111  ARG B CA    1 
ATOM   4928 C  C     . ARG B 1 111 ? -8.039  -26.788 47.070  1.00 24.20 ? 111  ARG B C     1 
ATOM   4929 O  O     . ARG B 1 111 ? -8.700  -26.725 46.019  1.00 22.00 ? 111  ARG B O     1 
ATOM   4930 C  CB    . ARG B 1 111 ? -7.203  -29.159 47.099  1.00 32.19 ? 111  ARG B CB    1 
ATOM   4931 C  CG    . ARG B 1 111 ? -6.883  -30.415 47.900  1.00 38.93 ? 111  ARG B CG    1 
ATOM   4932 C  CD    . ARG B 1 111 ? -6.578  -31.578 46.971  1.00 46.56 ? 111  ARG B CD    1 
ATOM   4933 N  NE    . ARG B 1 111 ? -6.864  -32.901 47.531  1.00 61.10 ? 111  ARG B NE    1 
ATOM   4934 C  CZ    . ARG B 1 111 ? -8.075  -33.440 47.774  1.00 62.78 ? 111  ARG B CZ    1 
ATOM   4935 N  NH1   . ARG B 1 111 ? -9.198  -32.775 47.554  1.00 55.23 ? 111  ARG B NH1   1 
ATOM   4936 N  NH2   . ARG B 1 111 ? -8.152  -34.662 48.274  1.00 63.89 ? 111  ARG B NH2   1 
ATOM   4937 N  N     . ILE B 1 112 ? -7.334  -25.780 47.554  1.00 23.38 ? 112  ILE B N     1 
ATOM   4938 C  CA    . ILE B 1 112 ? -7.001  -24.584 46.726  1.00 24.09 ? 112  ILE B CA    1 
ATOM   4939 C  C     . ILE B 1 112 ? -5.791  -24.998 45.896  1.00 24.60 ? 112  ILE B C     1 
ATOM   4940 O  O     . ILE B 1 112 ? -4.731  -25.031 46.452  1.00 27.16 ? 112  ILE B O     1 
ATOM   4941 C  CB    . ILE B 1 112 ? -6.755  -23.331 47.589  1.00 24.23 ? 112  ILE B CB    1 
ATOM   4942 C  CG1   . ILE B 1 112 ? -8.016  -22.925 48.354  1.00 23.94 ? 112  ILE B CG1   1 
ATOM   4943 C  CG2   . ILE B 1 112 ? -6.206  -22.164 46.757  1.00 25.46 ? 112  ILE B CG2   1 
ATOM   4944 C  CD1   . ILE B 1 112 ? -7.769  -21.842 49.405  1.00 23.54 ? 112  ILE B CD1   1 
ATOM   4945 N  N     . LEU B 1 113 ? -5.985  -25.389 44.635  1.00 23.76 ? 113  LEU B N     1 
ATOM   4946 C  CA    . LEU B 1 113 ? -4.929  -25.980 43.775  1.00 22.01 ? 113  LEU B CA    1 
ATOM   4947 C  C     . LEU B 1 113 ? -3.915  -24.904 43.374  1.00 22.77 ? 113  LEU B C     1 
ATOM   4948 O  O     . LEU B 1 113 ? -2.737  -25.225 43.269  1.00 23.42 ? 113  LEU B O     1 
ATOM   4949 C  CB    . LEU B 1 113 ? -5.596  -26.652 42.572  1.00 22.99 ? 113  LEU B CB    1 
ATOM   4950 C  CG    . LEU B 1 113 ? -6.461  -27.863 42.910  1.00 26.46 ? 113  LEU B CG    1 
ATOM   4951 C  CD1   . LEU B 1 113 ? -7.278  -28.330 41.715  1.00 26.42 ? 113  LEU B CD1   1 
ATOM   4952 C  CD2   . LEU B 1 113 ? -5.607  -29.017 43.457  1.00 26.08 ? 113  LEU B CD2   1 
ATOM   4953 N  N     . GLU B 1 114 ? -4.330  -23.659 43.150  1.00 24.12 ? 114  GLU B N     1 
ATOM   4954 C  CA    . GLU B 1 114 ? -3.405  -22.549 42.778  1.00 24.33 ? 114  GLU B CA    1 
ATOM   4955 C  C     . GLU B 1 114 ? -4.104  -21.220 43.045  1.00 23.02 ? 114  GLU B C     1 
ATOM   4956 O  O     . GLU B 1 114 ? -5.330  -21.126 42.780  1.00 21.71 ? 114  GLU B O     1 
ATOM   4957 C  CB    . GLU B 1 114 ? -2.981  -22.597 41.295  1.00 27.60 ? 114  GLU B CB    1 
ATOM   4958 C  CG    . GLU B 1 114 ? -1.726  -21.772 41.029  1.00 31.01 ? 114  GLU B CG    1 
ATOM   4959 C  CD    . GLU B 1 114 ? -1.277  -21.454 39.596  1.00 33.31 ? 114  GLU B CD    1 
ATOM   4960 O  OE1   . GLU B 1 114 ? -1.793  -22.040 38.619  1.00 29.34 ? 114  GLU B OE1   1 
ATOM   4961 O  OE2   . GLU B 1 114 ? -0.390  -20.582 39.463  1.00 34.98 ? 114  GLU B OE2   1 
ATOM   4962 N  N     . VAL B 1 115 ? -3.364  -20.246 43.575  1.00 21.84 ? 115  VAL B N     1 
ATOM   4963 C  CA    . VAL B 1 115 ? -3.759  -18.823 43.555  1.00 22.57 ? 115  VAL B CA    1 
ATOM   4964 C  C     . VAL B 1 115 ? -2.589  -18.100 42.916  1.00 22.85 ? 115  VAL B C     1 
ATOM   4965 O  O     . VAL B 1 115 ? -1.493  -18.194 43.422  1.00 24.63 ? 115  VAL B O     1 
ATOM   4966 C  CB    . VAL B 1 115 ? -4.094  -18.229 44.932  1.00 24.37 ? 115  VAL B CB    1 
ATOM   4967 C  CG1   . VAL B 1 115 ? -4.584  -16.777 44.794  1.00 25.25 ? 115  VAL B CG1   1 
ATOM   4968 C  CG2   . VAL B 1 115 ? -5.125  -19.068 45.649  1.00 26.02 ? 115  VAL B CG2   1 
ATOM   4969 N  N     . ASN B 1 116 ? -2.825  -17.464 41.787  1.00 21.65 ? 116  ASN B N     1 
ATOM   4970 C  CA    . ASN B 1 116 ? -1.751  -16.819 41.011  1.00 21.15 ? 116  ASN B CA    1 
ATOM   4971 C  C     . ASN B 1 116 ? -1.937  -15.305 41.131  1.00 20.01 ? 116  ASN B C     1 
ATOM   4972 O  O     . ASN B 1 116 ? -2.960  -14.796 40.687  1.00 20.06 ? 116  ASN B O     1 
ATOM   4973 C  CB    . ASN B 1 116 ? -1.776  -17.337 39.577  1.00 20.39 ? 116  ASN B CB    1 
ATOM   4974 C  CG    . ASN B 1 116 ? -0.556  -16.871 38.842  1.00 22.20 ? 116  ASN B CG    1 
ATOM   4975 O  OD1   . ASN B 1 116 ? -0.312  -15.667 38.758  1.00 25.10 ? 116  ASN B OD1   1 
ATOM   4976 N  ND2   . ASN B 1 116 ? 0.233   -17.812 38.352  1.00 22.73 ? 116  ASN B ND2   1 
ATOM   4977 N  N     . GLU B 1 117 ? -0.996  -14.608 41.733  1.00 20.41 ? 117  GLU B N     1 
ATOM   4978 C  CA    . GLU B 1 117 ? -1.122  -13.152 41.969  1.00 21.42 ? 117  GLU B CA    1 
ATOM   4979 C  C     . GLU B 1 117 ? -0.865  -12.362 40.684  1.00 20.52 ? 117  GLU B C     1 
ATOM   4980 O  O     . GLU B 1 117 ? -1.623  -11.439 40.438  1.00 20.36 ? 117  GLU B O     1 
ATOM   4981 C  CB    . GLU B 1 117 ? -0.173  -12.703 43.079  1.00 23.26 ? 117  GLU B CB    1 
ATOM   4982 C  CG    . GLU B 1 117 ? -0.391  -11.253 43.465  1.00 25.79 ? 117  GLU B CG    1 
ATOM   4983 C  CD    . GLU B 1 117 ? 0.579   -10.831 44.555  1.00 28.89 ? 117  GLU B CD    1 
ATOM   4984 O  OE1   . GLU B 1 117 ? 1.792   -11.012 44.361  1.00 33.18 ? 117  GLU B OE1   1 
ATOM   4985 O  OE2   . GLU B 1 117 ? 0.117   -10.439 45.614  1.00 31.58 ? 117  GLU B OE2   1 
ATOM   4986 N  N     . GLU B 1 118 ? 0.187   -12.665 39.928  1.00 21.59 ? 118  GLU B N     1 
ATOM   4987 C  CA    . GLU B 1 118 ? 0.595   -11.854 38.747  1.00 25.62 ? 118  GLU B CA    1 
ATOM   4988 C  C     . GLU B 1 118 ? -0.441  -12.012 37.619  1.00 22.97 ? 118  GLU B C     1 
ATOM   4989 O  O     . GLU B 1 118 ? -0.588  -11.058 36.851  1.00 21.90 ? 118  GLU B O     1 
ATOM   4990 C  CB    . GLU B 1 118 ? 2.012   -12.210 38.270  1.00 30.87 ? 118  GLU B CB    1 
ATOM   4991 C  CG    . GLU B 1 118 ? 2.145   -13.633 37.754  1.00 36.46 ? 118  GLU B CG    1 
ATOM   4992 C  CD    . GLU B 1 118 ? 3.547   -14.100 37.403  1.00 44.69 ? 118  GLU B CD    1 
ATOM   4993 O  OE1   . GLU B 1 118 ? 4.354   -13.259 36.963  1.00 49.47 ? 118  GLU B OE1   1 
ATOM   4994 O  OE2   . GLU B 1 118 ? 3.817   -15.329 37.552  1.00 50.68 ? 118  GLU B OE2   1 
ATOM   4995 N  N     . PHE B 1 119 ? -1.159  -13.139 37.529  1.00 20.76 ? 119  PHE B N     1 
ATOM   4996 C  CA    . PHE B 1 119 ? -2.184  -13.347 36.473  1.00 21.93 ? 119  PHE B CA    1 
ATOM   4997 C  C     . PHE B 1 119 ? -3.587  -13.206 37.048  1.00 20.62 ? 119  PHE B C     1 
ATOM   4998 O  O     . PHE B 1 119 ? -4.534  -13.271 36.264  1.00 23.96 ? 119  PHE B O     1 
ATOM   4999 C  CB    . PHE B 1 119 ? -1.991  -14.690 35.767  1.00 23.08 ? 119  PHE B CB    1 
ATOM   5000 C  CG    . PHE B 1 119 ? -0.648  -14.837 35.101  1.00 24.86 ? 119  PHE B CG    1 
ATOM   5001 C  CD1   . PHE B 1 119 ? -0.180  -13.865 34.244  1.00 27.46 ? 119  PHE B CD1   1 
ATOM   5002 C  CD2   . PHE B 1 119 ? 0.124   -15.971 35.296  1.00 27.66 ? 119  PHE B CD2   1 
ATOM   5003 C  CE1   . PHE B 1 119 ? 1.045   -14.009 33.614  1.00 26.99 ? 119  PHE B CE1   1 
ATOM   5004 C  CE2   . PHE B 1 119 ? 1.343   -16.118 34.655  1.00 26.46 ? 119  PHE B CE2   1 
ATOM   5005 C  CZ    . PHE B 1 119 ? 1.813   -15.123 33.847  1.00 27.14 ? 119  PHE B CZ    1 
ATOM   5006 N  N     . GLY B 1 120 ? -3.717  -13.009 38.361  1.00 19.79 ? 120  GLY B N     1 
ATOM   5007 C  CA    . GLY B 1 120 ? -5.020  -12.818 39.033  1.00 17.95 ? 120  GLY B CA    1 
ATOM   5008 C  C     . GLY B 1 120 ? -5.998  -13.938 38.734  1.00 18.23 ? 120  GLY B C     1 
ATOM   5009 O  O     . GLY B 1 120 ? -7.008  -13.692 38.040  1.00 18.84 ? 120  GLY B O     1 
ATOM   5010 N  N     . TYR B 1 121 ? -5.761  -15.134 39.279  1.00 16.86 ? 121  TYR B N     1 
ATOM   5011 C  CA    . TYR B 1 121 ? -6.717  -16.251 39.141  1.00 18.07 ? 121  TYR B CA    1 
ATOM   5012 C  C     . TYR B 1 121 ? -6.555  -17.240 40.297  1.00 18.44 ? 121  TYR B C     1 
ATOM   5013 O  O     . TYR B 1 121 ? -5.519  -17.229 40.985  1.00 18.52 ? 121  TYR B O     1 
ATOM   5014 C  CB    . TYR B 1 121 ? -6.554  -16.919 37.765  1.00 18.11 ? 121  TYR B CB    1 
ATOM   5015 C  CG    . TYR B 1 121 ? -5.352  -17.807 37.559  1.00 19.01 ? 121  TYR B CG    1 
ATOM   5016 C  CD1   . TYR B 1 121 ? -5.275  -19.083 38.118  1.00 18.71 ? 121  TYR B CD1   1 
ATOM   5017 C  CD2   . TYR B 1 121 ? -4.319  -17.417 36.725  1.00 19.39 ? 121  TYR B CD2   1 
ATOM   5018 C  CE1   . TYR B 1 121 ? -4.187  -19.910 37.885  1.00 17.87 ? 121  TYR B CE1   1 
ATOM   5019 C  CE2   . TYR B 1 121 ? -3.243  -18.248 36.455  1.00 17.59 ? 121  TYR B CE2   1 
ATOM   5020 C  CZ    . TYR B 1 121 ? -3.172  -19.496 37.041  1.00 17.90 ? 121  TYR B CZ    1 
ATOM   5021 O  OH    . TYR B 1 121 ? -2.107  -20.325 36.780  1.00 19.02 ? 121  TYR B OH    1 
ATOM   5022 N  N     . ALA B 1 122 ? -7.548  -18.102 40.457  1.00 18.91 ? 122  ALA B N     1 
ATOM   5023 C  CA    . ALA B 1 122 ? -7.481  -19.265 41.365  1.00 20.92 ? 122  ALA B CA    1 
ATOM   5024 C  C     . ALA B 1 122 ? -8.016  -20.504 40.639  1.00 20.96 ? 122  ALA B C     1 
ATOM   5025 O  O     . ALA B 1 122 ? -8.926  -20.382 39.762  1.00 18.60 ? 122  ALA B O     1 
ATOM   5026 C  CB    . ALA B 1 122 ? -8.248  -19.007 42.633  1.00 20.62 ? 122  ALA B CB    1 
ATOM   5027 N  N     . LEU B 1 123 ? -7.446  -21.655 40.990  1.00 19.20 ? 123  LEU B N     1 
ATOM   5028 C  CA    . LEU B 1 123 ? -7.927  -22.969 40.512  1.00 18.89 ? 123  LEU B CA    1 
ATOM   5029 C  C     . LEU B 1 123 ? -8.356  -23.740 41.761  1.00 20.69 ? 123  LEU B C     1 
ATOM   5030 O  O     . LEU B 1 123 ? -7.513  -23.824 42.706  1.00 20.47 ? 123  LEU B O     1 
ATOM   5031 C  CB    . LEU B 1 123 ? -6.812  -23.651 39.731  1.00 18.18 ? 123  LEU B CB    1 
ATOM   5032 C  CG    . LEU B 1 123 ? -7.104  -25.085 39.329  1.00 18.63 ? 123  LEU B CG    1 
ATOM   5033 C  CD1   . LEU B 1 123 ? -8.306  -25.122 38.368  1.00 18.08 ? 123  LEU B CD1   1 
ATOM   5034 C  CD2   . LEU B 1 123 ? -5.845  -25.716 38.727  1.00 18.74 ? 123  LEU B CD2   1 
ATOM   5035 N  N     . VAL B 1 124 ? -9.641  -24.121 41.832  1.00 18.66 ? 124  VAL B N     1 
ATOM   5036 C  CA    . VAL B 1 124 ? -10.268 -24.601 43.097  1.00 20.23 ? 124  VAL B CA    1 
ATOM   5037 C  C     . VAL B 1 124 ? -11.075 -25.874 42.829  1.00 20.28 ? 124  VAL B C     1 
ATOM   5038 O  O     . VAL B 1 124 ? -11.582 -26.053 41.695  1.00 20.64 ? 124  VAL B O     1 
ATOM   5039 C  CB    . VAL B 1 124 ? -11.116 -23.485 43.759  1.00 19.51 ? 124  VAL B CB    1 
ATOM   5040 C  CG1   . VAL B 1 124 ? -10.228 -22.330 44.198  1.00 19.01 ? 124  VAL B CG1   1 
ATOM   5041 C  CG2   . VAL B 1 124 ? -12.220 -22.971 42.847  1.00 20.12 ? 124  VAL B CG2   1 
ATOM   5042 N  N     . GLU B 1 125 ? -11.141 -26.730 43.844  1.00 21.01 ? 125  GLU B N     1 
ATOM   5043 C  CA    . GLU B 1 125 ? -12.060 -27.890 43.916  1.00 22.20 ? 125  GLU B CA    1 
ATOM   5044 C  C     . GLU B 1 125 ? -13.390 -27.379 44.444  1.00 21.85 ? 125  GLU B C     1 
ATOM   5045 O  O     . GLU B 1 125 ? -13.454 -26.308 45.040  1.00 22.41 ? 125  GLU B O     1 
ATOM   5046 C  CB    . GLU B 1 125 ? -11.470 -28.980 44.816  1.00 23.49 ? 125  GLU B CB    1 
ATOM   5047 C  CG    . GLU B 1 125 ? -10.211 -29.599 44.209  1.00 26.15 ? 125  GLU B CG    1 
ATOM   5048 C  CD    . GLU B 1 125 ? -9.707  -30.836 44.948  1.00 26.49 ? 125  GLU B CD    1 
ATOM   5049 O  OE1   . GLU B 1 125 ? -9.744  -30.828 46.197  1.00 23.39 ? 125  GLU B OE1   1 
ATOM   5050 O  OE2   . GLU B 1 125 ? -9.306  -31.798 44.277  1.00 28.53 ? 125  GLU B OE2   1 
ATOM   5051 N  N     . PRO B 1 126 ? -14.482 -28.132 44.251  1.00 22.21 ? 126  PRO B N     1 
ATOM   5052 C  CA    . PRO B 1 126 ? -15.812 -27.656 44.623  1.00 24.21 ? 126  PRO B CA    1 
ATOM   5053 C  C     . PRO B 1 126 ? -16.068 -27.329 46.108  1.00 25.67 ? 126  PRO B C     1 
ATOM   5054 O  O     . PRO B 1 126 ? -16.992 -26.575 46.376  1.00 25.78 ? 126  PRO B O     1 
ATOM   5055 C  CB    . PRO B 1 126 ? -16.692 -28.841 44.184  1.00 24.15 ? 126  PRO B CB    1 
ATOM   5056 C  CG    . PRO B 1 126 ? -15.920 -29.504 43.064  1.00 22.37 ? 126  PRO B CG    1 
ATOM   5057 C  CD    . PRO B 1 126 ? -14.505 -29.433 43.557  1.00 22.50 ? 126  PRO B CD    1 
ATOM   5058 N  N     . GLY B 1 127 ? -15.296 -27.914 47.032  1.00 24.85 ? 127  GLY B N     1 
ATOM   5059 C  CA    . GLY B 1 127 ? -15.467 -27.760 48.483  1.00 23.07 ? 127  GLY B CA    1 
ATOM   5060 C  C     . GLY B 1 127 ? -14.831 -26.485 49.019  1.00 24.45 ? 127  GLY B C     1 
ATOM   5061 O  O     . GLY B 1 127 ? -15.045 -26.167 50.207  1.00 23.44 ? 127  GLY B O     1 
ATOM   5062 N  N     . VAL B 1 128 ? -14.093 -25.746 48.198  1.00 24.19 ? 128  VAL B N     1 
ATOM   5063 C  CA    . VAL B 1 128 ? -13.460 -24.481 48.649  1.00 23.68 ? 128  VAL B CA    1 
ATOM   5064 C  C     . VAL B 1 128 ? -14.598 -23.486 48.885  1.00 23.49 ? 128  VAL B C     1 
ATOM   5065 O  O     . VAL B 1 128 ? -15.399 -23.278 47.979  1.00 24.48 ? 128  VAL B O     1 
ATOM   5066 C  CB    . VAL B 1 128 ? -12.413 -23.961 47.651  1.00 23.72 ? 128  VAL B CB    1 
ATOM   5067 C  CG1   . VAL B 1 128 ? -11.925 -22.569 48.032  1.00 23.97 ? 128  VAL B CG1   1 
ATOM   5068 C  CG2   . VAL B 1 128 ? -11.234 -24.920 47.538  1.00 25.63 ? 128  VAL B CG2   1 
ATOM   5069 N  N     . SER B 1 129 ? -14.679 -22.933 50.086  1.00 22.19 ? 129  SER B N     1 
ATOM   5070 C  CA    . SER B 1 129 ? -15.630 -21.859 50.439  1.00 24.43 ? 129  SER B CA    1 
ATOM   5071 C  C     . SER B 1 129 ? -15.007 -20.488 50.148  1.00 24.09 ? 129  SER B C     1 
ATOM   5072 O  O     . SER B 1 129 ? -13.776 -20.356 50.120  1.00 23.05 ? 129  SER B O     1 
ATOM   5073 C  CB    . SER B 1 129 ? -16.084 -21.963 51.890  1.00 23.17 ? 129  SER B CB    1 
ATOM   5074 O  OG    . SER B 1 129 ? -15.025 -21.586 52.738  1.00 22.43 ? 129  SER B OG    1 
ATOM   5075 N  N     . TYR B 1 130 ? -15.855 -19.480 49.983  1.00 22.96 ? 130  TYR B N     1 
ATOM   5076 C  CA    . TYR B 1 130 ? -15.408 -18.069 49.944  1.00 21.93 ? 130  TYR B CA    1 
ATOM   5077 C  C     . TYR B 1 130 ? -14.572 -17.749 51.196  1.00 22.51 ? 130  TYR B C     1 
ATOM   5078 O  O     . TYR B 1 130 ? -13.539 -17.075 51.063  1.00 24.55 ? 130  TYR B O     1 
ATOM   5079 C  CB    . TYR B 1 130 ? -16.635 -17.172 49.793  1.00 21.79 ? 130  TYR B CB    1 
ATOM   5080 C  CG    . TYR B 1 130 ? -17.358 -17.369 48.492  1.00 21.50 ? 130  TYR B CG    1 
ATOM   5081 C  CD1   . TYR B 1 130 ? -16.826 -16.858 47.314  1.00 21.08 ? 130  TYR B CD1   1 
ATOM   5082 C  CD2   . TYR B 1 130 ? -18.555 -18.055 48.431  1.00 22.22 ? 130  TYR B CD2   1 
ATOM   5083 C  CE1   . TYR B 1 130 ? -17.464 -17.036 46.102  1.00 20.65 ? 130  TYR B CE1   1 
ATOM   5084 C  CE2   . TYR B 1 130 ? -19.205 -18.244 47.215  1.00 24.41 ? 130  TYR B CE2   1 
ATOM   5085 C  CZ    . TYR B 1 130 ? -18.653 -17.732 46.052  1.00 21.49 ? 130  TYR B CZ    1 
ATOM   5086 O  OH    . TYR B 1 130 ? -19.302 -17.851 44.861  1.00 23.32 ? 130  TYR B OH    1 
ATOM   5087 N  N     . PHE B 1 131 ? -15.004 -18.171 52.392  1.00 22.30 ? 131  PHE B N     1 
ATOM   5088 C  CA    . PHE B 1 131 ? -14.253 -17.974 53.668  1.00 23.18 ? 131  PHE B CA    1 
ATOM   5089 C  C     . PHE B 1 131 ? -12.840 -18.545 53.523  1.00 24.14 ? 131  PHE B C     1 
ATOM   5090 O  O     . PHE B 1 131 ? -11.855 -17.828 53.807  1.00 24.89 ? 131  PHE B O     1 
ATOM   5091 C  CB    . PHE B 1 131 ? -14.983 -18.603 54.869  1.00 24.31 ? 131  PHE B CB    1 
ATOM   5092 C  CG    . PHE B 1 131 ? -16.167 -17.807 55.371  1.00 25.50 ? 131  PHE B CG    1 
ATOM   5093 C  CD1   . PHE B 1 131 ? -16.033 -16.480 55.764  1.00 26.91 ? 131  PHE B CD1   1 
ATOM   5094 C  CD2   . PHE B 1 131 ? -17.426 -18.379 55.497  1.00 27.66 ? 131  PHE B CD2   1 
ATOM   5095 C  CE1   . PHE B 1 131 ? -17.128 -15.756 56.237  1.00 23.52 ? 131  PHE B CE1   1 
ATOM   5096 C  CE2   . PHE B 1 131 ? -18.514 -17.632 55.946  1.00 24.49 ? 131  PHE B CE2   1 
ATOM   5097 C  CZ    . PHE B 1 131 ? -18.372 -16.321 56.272  1.00 20.34 ? 131  PHE B CZ    1 
ATOM   5098 N  N     . GLU B 1 132 ? -12.729 -19.789 53.061  1.00 26.42 ? 132  GLU B N     1 
ATOM   5099 C  CA    . GLU B 1 132 ? -11.414 -20.481 52.908  1.00 29.66 ? 132  GLU B CA    1 
ATOM   5100 C  C     . GLU B 1 132 ? -10.540 -19.710 51.903  1.00 26.28 ? 132  GLU B C     1 
ATOM   5101 O  O     . GLU B 1 132 ? -9.367  -19.423 52.212  1.00 22.80 ? 132  GLU B O     1 
ATOM   5102 C  CB    . GLU B 1 132 ? -11.612 -21.959 52.523  1.00 33.39 ? 132  GLU B CB    1 
ATOM   5103 C  CG    . GLU B 1 132 ? -12.193 -22.826 53.656  1.00 35.26 ? 132  GLU B CG    1 
ATOM   5104 C  CD    . GLU B 1 132 ? -12.886 -24.123 53.235  1.00 42.57 ? 132  GLU B CD    1 
ATOM   5105 O  OE1   . GLU B 1 132 ? -12.803 -24.515 52.040  1.00 46.88 ? 132  GLU B OE1   1 
ATOM   5106 O  OE2   . GLU B 1 132 ? -13.525 -24.753 54.093  1.00 47.49 ? 132  GLU B OE2   1 
ATOM   5107 N  N     . LEU B 1 133 ? -11.069 -19.364 50.735  1.00 24.44 ? 133  LEU B N     1 
ATOM   5108 C  CA    . LEU B 1 133 ? -10.243 -18.702 49.679  1.00 22.96 ? 133  LEU B CA    1 
ATOM   5109 C  C     . LEU B 1 133 ? -9.816  -17.302 50.145  1.00 21.32 ? 133  LEU B C     1 
ATOM   5110 O  O     . LEU B 1 133 ? -8.636  -16.897 49.908  1.00 19.26 ? 133  LEU B O     1 
ATOM   5111 C  CB    . LEU B 1 133 ? -11.031 -18.625 48.367  1.00 24.86 ? 133  LEU B CB    1 
ATOM   5112 C  CG    . LEU B 1 133 ? -10.266 -17.987 47.208  1.00 24.33 ? 133  LEU B CG    1 
ATOM   5113 C  CD1   . LEU B 1 133 ? -8.991  -18.776 46.932  1.00 23.94 ? 133  LEU B CD1   1 
ATOM   5114 C  CD2   . LEU B 1 133 ? -11.146 -17.912 45.959  1.00 25.35 ? 133  LEU B CD2   1 
ATOM   5115 N  N     . TYR B 1 134 ? -10.714 -16.582 50.809  1.00 22.29 ? 134  TYR B N     1 
ATOM   5116 C  CA    . TYR B 1 134 ? -10.391 -15.240 51.370  1.00 24.65 ? 134  TYR B CA    1 
ATOM   5117 C  C     . TYR B 1 134 ? -9.301  -15.390 52.441  1.00 24.25 ? 134  TYR B C     1 
ATOM   5118 O  O     . TYR B 1 134 ? -8.281  -14.662 52.402  1.00 25.17 ? 134  TYR B O     1 
ATOM   5119 C  CB    . TYR B 1 134 ? -11.642 -14.557 51.914  1.00 24.37 ? 134  TYR B CB    1 
ATOM   5120 C  CG    . TYR B 1 134 ? -11.397 -13.202 52.530  1.00 25.93 ? 134  TYR B CG    1 
ATOM   5121 C  CD1   . TYR B 1 134 ? -11.327 -12.062 51.741  1.00 24.66 ? 134  TYR B CD1   1 
ATOM   5122 C  CD2   . TYR B 1 134 ? -11.237 -13.062 53.904  1.00 28.45 ? 134  TYR B CD2   1 
ATOM   5123 C  CE1   . TYR B 1 134 ? -11.131 -10.815 52.298  1.00 25.03 ? 134  TYR B CE1   1 
ATOM   5124 C  CE2   . TYR B 1 134 ? -11.032 -11.814 54.484  1.00 30.35 ? 134  TYR B CE2   1 
ATOM   5125 C  CZ    . TYR B 1 134 ? -10.984 -10.690 53.674  1.00 28.29 ? 134  TYR B CZ    1 
ATOM   5126 O  OH    . TYR B 1 134 ? -10.786 -9.469  54.231  1.00 30.90 ? 134  TYR B OH    1 
ATOM   5127 N  N     . ASP B 1 135 ? -9.463  -16.355 53.335  1.00 27.02 ? 135  ASP B N     1 
ATOM   5128 C  CA    . ASP B 1 135 ? -8.466  -16.587 54.421  1.00 29.16 ? 135  ASP B CA    1 
ATOM   5129 C  C     . ASP B 1 135 ? -7.106  -16.974 53.833  1.00 29.54 ? 135  ASP B C     1 
ATOM   5130 O  O     . ASP B 1 135 ? -6.100  -16.391 54.265  1.00 29.37 ? 135  ASP B O     1 
ATOM   5131 C  CB    . ASP B 1 135 ? -9.002  -17.606 55.413  1.00 29.44 ? 135  ASP B CB    1 
ATOM   5132 C  CG    . ASP B 1 135 ? -10.137 -17.024 56.217  1.00 31.51 ? 135  ASP B CG    1 
ATOM   5133 O  OD1   . ASP B 1 135 ? -10.296 -15.792 56.207  1.00 35.56 ? 135  ASP B OD1   1 
ATOM   5134 O  OD2   . ASP B 1 135 ? -10.846 -17.804 56.830  1.00 38.47 ? 135  ASP B OD2   1 
ATOM   5135 N  N     . TYR B 1 136 ? -7.071  -17.888 52.860  1.00 28.54 ? 136  TYR B N     1 
ATOM   5136 C  CA    . TYR B 1 136 ? -5.834  -18.227 52.104  1.00 28.46 ? 136  TYR B CA    1 
ATOM   5137 C  C     . TYR B 1 136 ? -5.182  -16.962 51.524  1.00 26.64 ? 136  TYR B C     1 
ATOM   5138 O  O     . TYR B 1 136 ? -4.000  -16.741 51.730  1.00 26.85 ? 136  TYR B O     1 
ATOM   5139 C  CB    . TYR B 1 136 ? -6.115  -19.248 50.997  1.00 29.96 ? 136  TYR B CB    1 
ATOM   5140 C  CG    . TYR B 1 136 ? -4.879  -19.719 50.282  1.00 33.42 ? 136  TYR B CG    1 
ATOM   5141 C  CD1   . TYR B 1 136 ? -4.312  -18.970 49.261  1.00 37.72 ? 136  TYR B CD1   1 
ATOM   5142 C  CD2   . TYR B 1 136 ? -4.229  -20.884 50.662  1.00 40.98 ? 136  TYR B CD2   1 
ATOM   5143 C  CE1   . TYR B 1 136 ? -3.177  -19.399 48.594  1.00 39.02 ? 136  TYR B CE1   1 
ATOM   5144 C  CE2   . TYR B 1 136 ? -3.086  -21.327 50.011  1.00 42.25 ? 136  TYR B CE2   1 
ATOM   5145 C  CZ    . TYR B 1 136 ? -2.555  -20.575 48.982  1.00 44.86 ? 136  TYR B CZ    1 
ATOM   5146 O  OH    . TYR B 1 136 ? -1.423  -20.995 48.349  1.00 55.14 ? 136  TYR B OH    1 
ATOM   5147 N  N     . ILE B 1 137 ? -5.921  -16.137 50.799  1.00 25.22 ? 137  ILE B N     1 
ATOM   5148 C  CA    . ILE B 1 137 ? -5.332  -14.914 50.184  1.00 25.92 ? 137  ILE B CA    1 
ATOM   5149 C  C     . ILE B 1 137 ? -4.776  -14.018 51.297  1.00 25.70 ? 137  ILE B C     1 
ATOM   5150 O  O     . ILE B 1 137 ? -3.630  -13.546 51.139  1.00 24.92 ? 137  ILE B O     1 
ATOM   5151 C  CB    . ILE B 1 137 ? -6.343  -14.190 49.266  1.00 24.48 ? 137  ILE B CB    1 
ATOM   5152 C  CG1   . ILE B 1 137 ? -6.570  -14.998 47.978  1.00 27.12 ? 137  ILE B CG1   1 
ATOM   5153 C  CG2   . ILE B 1 137 ? -5.891  -12.771 48.958  1.00 25.26 ? 137  ILE B CG2   1 
ATOM   5154 C  CD1   . ILE B 1 137 ? -7.980  -14.902 47.417  1.00 27.96 ? 137  ILE B CD1   1 
ATOM   5155 N  N     . GLN B 1 138 ? -5.543  -13.771 52.366  1.00 28.37 ? 138  GLN B N     1 
ATOM   5156 C  CA    . GLN B 1 138 ? -5.146  -12.817 53.440  1.00 32.35 ? 138  GLN B CA    1 
ATOM   5157 C  C     . GLN B 1 138 ? -3.864  -13.305 54.131  1.00 35.40 ? 138  GLN B C     1 
ATOM   5158 O  O     . GLN B 1 138 ? -2.939  -12.503 54.228  1.00 37.25 ? 138  GLN B O     1 
ATOM   5159 C  CB    . GLN B 1 138 ? -6.246  -12.625 54.487  1.00 33.73 ? 138  GLN B CB    1 
ATOM   5160 C  CG    . GLN B 1 138 ? -7.528  -12.003 53.949  1.00 37.66 ? 138  GLN B CG    1 
ATOM   5161 C  CD    . GLN B 1 138 ? -7.332  -10.879 52.959  1.00 38.95 ? 138  GLN B CD    1 
ATOM   5162 O  OE1   . GLN B 1 138 ? -6.870  -9.791  53.286  1.00 34.63 ? 138  GLN B OE1   1 
ATOM   5163 N  NE2   . GLN B 1 138 ? -7.707  -11.144 51.719  1.00 46.69 ? 138  GLN B NE2   1 
ATOM   5164 N  N     . GLU B 1 139 ? -3.814  -14.574 54.552  1.00 36.68 ? 139  GLU B N     1 
ATOM   5165 C  CA    . GLU B 1 139 ? -2.648  -15.192 55.238  1.00 39.60 ? 139  GLU B CA    1 
ATOM   5166 C  C     . GLU B 1 139 ? -1.378  -15.095 54.371  1.00 38.98 ? 139  GLU B C     1 
ATOM   5167 O  O     . GLU B 1 139 ? -0.350  -14.771 54.947  1.00 37.34 ? 139  GLU B O     1 
ATOM   5168 C  CB    . GLU B 1 139 ? -2.953  -16.632 55.633  1.00 43.50 ? 139  GLU B CB    1 
ATOM   5169 C  CG    . GLU B 1 139 ? -1.730  -17.373 56.134  1.00 54.76 ? 139  GLU B CG    1 
ATOM   5170 C  CD    . GLU B 1 139 ? -1.823  -18.886 56.053  1.00 64.80 ? 139  GLU B CD    1 
ATOM   5171 O  OE1   . GLU B 1 139 ? -2.944  -19.418 56.199  1.00 74.15 ? 139  GLU B OE1   1 
ATOM   5172 O  OE2   . GLU B 1 139 ? -0.776  -19.528 55.816  1.00 73.11 ? 139  GLU B OE2   1 
ATOM   5173 N  N     . LYS B 1 140 ? -1.426  -15.332 53.049  1.00 34.77 ? 140  LYS B N     1 
ATOM   5174 C  CA    . LYS B 1 140 ? -0.234  -15.218 52.157  1.00 33.26 ? 140  LYS B CA    1 
ATOM   5175 C  C     . LYS B 1 140 ? 0.018   -13.754 51.740  1.00 30.98 ? 140  LYS B C     1 
ATOM   5176 O  O     . LYS B 1 140 ? 1.044   -13.463 51.114  1.00 29.40 ? 140  LYS B O     1 
ATOM   5177 C  CB    . LYS B 1 140 ? -0.396  -16.136 50.950  1.00 38.08 ? 140  LYS B CB    1 
ATOM   5178 C  CG    . LYS B 1 140 ? -0.742  -17.583 51.283  1.00 44.62 ? 140  LYS B CG    1 
ATOM   5179 C  CD    . LYS B 1 140 ? 0.320   -18.589 50.900  1.00 51.54 ? 140  LYS B CD    1 
ATOM   5180 C  CE    . LYS B 1 140 ? 0.032   -19.986 51.421  1.00 57.95 ? 140  LYS B CE    1 
ATOM   5181 N  NZ    . LYS B 1 140 ? 0.115   -20.055 52.902  1.00 62.39 ? 140  LYS B NZ    1 
ATOM   5182 N  N     . GLY B 1 141 ? -0.861  -12.824 52.087  1.00 28.58 ? 141  GLY B N     1 
ATOM   5183 C  CA    . GLY B 1 141 ? -0.661  -11.412 51.724  1.00 28.58 ? 141  GLY B CA    1 
ATOM   5184 C  C     . GLY B 1 141 ? -0.765  -11.157 50.217  1.00 28.73 ? 141  GLY B C     1 
ATOM   5185 O  O     . GLY B 1 141 ? -0.165  -10.196 49.762  1.00 28.98 ? 141  GLY B O     1 
ATOM   5186 N  N     . LEU B 1 142 ? -1.510  -11.959 49.448  1.00 30.87 ? 142  LEU B N     1 
ATOM   5187 C  CA    . LEU B 1 142 ? -1.638  -11.749 47.969  1.00 29.81 ? 142  LEU B CA    1 
ATOM   5188 C  C     . LEU B 1 142 ? -2.547  -10.531 47.722  1.00 28.93 ? 142  LEU B C     1 
ATOM   5189 O  O     . LEU B 1 142 ? -3.581  -10.431 48.380  1.00 28.19 ? 142  LEU B O     1 
ATOM   5190 C  CB    . LEU B 1 142 ? -2.157  -13.032 47.313  1.00 27.94 ? 142  LEU B CB    1 
ATOM   5191 C  CG    . LEU B 1 142 ? -1.278  -14.254 47.588  1.00 28.22 ? 142  LEU B CG    1 
ATOM   5192 C  CD1   . LEU B 1 142 ? -1.920  -15.534 47.090  1.00 31.11 ? 142  LEU B CD1   1 
ATOM   5193 C  CD2   . LEU B 1 142 ? 0.113   -14.076 46.992  1.00 28.41 ? 142  LEU B CD2   1 
ATOM   5194 N  N     . LYS B 1 143 ? -2.158  -9.616  46.836  1.00 25.78 ? 143  LYS B N     1 
ATOM   5195 C  CA    . LYS B 1 143 ? -2.945  -8.398  46.516  1.00 27.17 ? 143  LYS B CA    1 
ATOM   5196 C  C     . LYS B 1 143 ? -4.065  -8.747  45.523  1.00 25.83 ? 143  LYS B C     1 
ATOM   5197 O  O     . LYS B 1 143 ? -4.115  -8.157  44.408  1.00 24.06 ? 143  LYS B O     1 
ATOM   5198 C  CB    . LYS B 1 143 ? -1.985  -7.313  46.027  1.00 30.68 ? 143  LYS B CB    1 
ATOM   5199 C  CG    . LYS B 1 143 ? -0.907  -6.964  47.055  1.00 35.52 ? 143  LYS B CG    1 
ATOM   5200 C  CD    . LYS B 1 143 ? 0.107   -5.913  46.594  1.00 44.29 ? 143  LYS B CD    1 
ATOM   5201 C  CE    . LYS B 1 143 ? 0.972   -6.322  45.411  1.00 54.26 ? 143  LYS B CE    1 
ATOM   5202 N  NZ    . LYS B 1 143 ? 1.763   -7.555  45.674  1.00 61.22 ? 143  LYS B NZ    1 
ATOM   5203 N  N     . LEU B 1 144 ? -4.973  -9.631  45.935  1.00 24.54 ? 144  LEU B N     1 
ATOM   5204 C  CA    . LEU B 1 144 ? -6.149  -10.013 45.112  1.00 23.66 ? 144  LEU B CA    1 
ATOM   5205 C  C     . LEU B 1 144 ? -7.424  -9.873  45.937  1.00 23.57 ? 144  LEU B C     1 
ATOM   5206 O  O     . LEU B 1 144 ? -7.384  -10.194 47.149  1.00 23.06 ? 144  LEU B O     1 
ATOM   5207 C  CB    . LEU B 1 144 ? -5.987  -11.461 44.638  1.00 23.11 ? 144  LEU B CB    1 
ATOM   5208 C  CG    . LEU B 1 144 ? -4.734  -11.759 43.816  1.00 23.35 ? 144  LEU B CG    1 
ATOM   5209 C  CD1   . LEU B 1 144 ? -4.542  -13.251 43.744  1.00 24.21 ? 144  LEU B CD1   1 
ATOM   5210 C  CD2   . LEU B 1 144 ? -4.796  -11.137 42.420  1.00 23.55 ? 144  LEU B CD2   1 
ATOM   5211 N  N     . TRP B 1 145 ? -8.528  -9.499  45.281  1.00 22.64 ? 145  TRP B N     1 
ATOM   5212 C  CA    . TRP B 1 145 ? -9.888  -9.621  45.860  1.00 23.02 ? 145  TRP B CA    1 
ATOM   5213 C  C     . TRP B 1 145 ? -10.625 -10.832 45.292  1.00 24.57 ? 145  TRP B C     1 
ATOM   5214 O  O     . TRP B 1 145 ? -10.426 -11.205 44.106  1.00 24.59 ? 145  TRP B O     1 
ATOM   5215 C  CB    . TRP B 1 145 ? -10.685 -8.344  45.620  1.00 25.48 ? 145  TRP B CB    1 
ATOM   5216 C  CG    . TRP B 1 145 ? -10.217 -7.182  46.430  1.00 25.54 ? 145  TRP B CG    1 
ATOM   5217 C  CD1   . TRP B 1 145 ? -9.136  -7.155  47.257  1.00 27.79 ? 145  TRP B CD1   1 
ATOM   5218 C  CD2   . TRP B 1 145 ? -10.765 -5.857  46.450  1.00 26.95 ? 145  TRP B CD2   1 
ATOM   5219 N  NE1   . TRP B 1 145 ? -8.985  -5.913  47.794  1.00 28.70 ? 145  TRP B NE1   1 
ATOM   5220 C  CE2   . TRP B 1 145 ? -9.972  -5.095  47.333  1.00 27.73 ? 145  TRP B CE2   1 
ATOM   5221 C  CE3   . TRP B 1 145 ? -11.841 -5.232  45.822  1.00 28.57 ? 145  TRP B CE3   1 
ATOM   5222 C  CZ2   . TRP B 1 145 ? -10.230 -3.755  47.626  1.00 28.42 ? 145  TRP B CZ2   1 
ATOM   5223 C  CZ3   . TRP B 1 145 ? -12.104 -3.908  46.112  1.00 28.73 ? 145  TRP B CZ3   1 
ATOM   5224 C  CH2   . TRP B 1 145 ? -11.296 -3.175  46.980  1.00 28.02 ? 145  TRP B CH2   1 
ATOM   5225 N  N     . ILE B 1 146 ? -11.508 -11.391 46.108  1.00 22.67 ? 146  ILE B N     1 
ATOM   5226 C  CA    . ILE B 1 146 ? -12.542 -12.353 45.641  1.00 23.48 ? 146  ILE B CA    1 
ATOM   5227 C  C     . ILE B 1 146 ? -13.843 -11.592 45.478  1.00 22.89 ? 146  ILE B C     1 
ATOM   5228 O  O     . ILE B 1 146 ? -13.887 -10.389 45.844  1.00 22.64 ? 146  ILE B O     1 
ATOM   5229 C  CB    . ILE B 1 146 ? -12.694 -13.564 46.575  1.00 24.92 ? 146  ILE B CB    1 
ATOM   5230 C  CG1   . ILE B 1 146 ? -13.167 -13.174 47.980  1.00 27.31 ? 146  ILE B CG1   1 
ATOM   5231 C  CG2   . ILE B 1 146 ? -11.388 -14.342 46.621  1.00 25.86 ? 146  ILE B CG2   1 
ATOM   5232 C  CD1   . ILE B 1 146 ? -13.583 -14.382 48.813  1.00 28.49 ? 146  ILE B CD1   1 
ATOM   5233 N  N     . ASP B 1 147 ? -14.822 -12.272 44.895  1.00 20.65 ? 147  ASP B N     1 
ATOM   5234 C  CA    . ASP B 1 147 ? -16.197 -11.756 44.726  1.00 21.18 ? 147  ASP B CA    1 
ATOM   5235 C  C     . ASP B 1 147 ? -17.134 -12.753 45.393  1.00 21.69 ? 147  ASP B C     1 
ATOM   5236 O  O     . ASP B 1 147 ? -17.128 -13.934 45.024  1.00 21.87 ? 147  ASP B O     1 
ATOM   5237 C  CB    . ASP B 1 147 ? -16.522 -11.483 43.260  1.00 20.01 ? 147  ASP B CB    1 
ATOM   5238 C  CG    . ASP B 1 147 ? -17.779 -10.648 43.097  1.00 19.97 ? 147  ASP B CG    1 
ATOM   5239 O  OD1   . ASP B 1 147 ? -18.845 -11.189 43.415  1.00 18.36 ? 147  ASP B OD1   1 
ATOM   5240 O  OD2   . ASP B 1 147 ? -17.681 -9.480  42.627  1.00 18.58 ? 147  ASP B OD2   1 
ATOM   5241 N  N     . VAL B 1 148 ? -17.860 -12.280 46.392  1.00 21.73 ? 148  VAL B N     1 
ATOM   5242 C  CA    . VAL B 1 148 ? -18.682 -13.148 47.276  1.00 25.82 ? 148  VAL B CA    1 
ATOM   5243 C  C     . VAL B 1 148 ? -20.149 -12.819 47.048  1.00 23.27 ? 148  VAL B C     1 
ATOM   5244 O  O     . VAL B 1 148 ? -20.535 -11.660 46.961  1.00 21.88 ? 148  VAL B O     1 
ATOM   5245 C  CB    . VAL B 1 148 ? -18.300 -12.996 48.758  1.00 26.75 ? 148  VAL B CB    1 
ATOM   5246 C  CG1   . VAL B 1 148 ? -16.825 -13.259 48.967  1.00 28.00 ? 148  VAL B CG1   1 
ATOM   5247 C  CG2   . VAL B 1 148 ? -18.658 -11.618 49.299  1.00 30.64 ? 148  VAL B CG2   1 
ATOM   5248 N  N     . PRO B 1 149 ? -21.002 -13.847 47.047  1.00 24.49 ? 149  PRO B N     1 
ATOM   5249 C  CA    . PRO B 1 149 ? -22.441 -13.661 46.934  1.00 27.69 ? 149  PRO B CA    1 
ATOM   5250 C  C     . PRO B 1 149 ? -23.076 -13.436 48.302  1.00 31.73 ? 149  PRO B C     1 
ATOM   5251 O  O     . PRO B 1 149 ? -24.061 -14.093 48.545  1.00 39.52 ? 149  PRO B O     1 
ATOM   5252 C  CB    . PRO B 1 149 ? -22.849 -15.037 46.386  1.00 27.95 ? 149  PRO B CB    1 
ATOM   5253 C  CG    . PRO B 1 149 ? -21.951 -15.992 47.150  1.00 26.70 ? 149  PRO B CG    1 
ATOM   5254 C  CD    . PRO B 1 149 ? -20.625 -15.263 47.189  1.00 25.19 ? 149  PRO B CD    1 
ATOM   5255 N  N     . ASP B 1 150 ? -22.459 -12.639 49.172  1.00 34.73 ? 150  ASP B N     1 
ATOM   5256 C  CA    . ASP B 1 150 ? -22.994 -12.344 50.533  1.00 46.05 ? 150  ASP B CA    1 
ATOM   5257 C  C     . ASP B 1 150 ? -23.181 -13.603 51.401  1.00 45.99 ? 150  ASP B C     1 
ATOM   5258 O  O     . ASP B 1 150 ? -23.783 -13.490 52.473  1.00 55.62 ? 150  ASP B O     1 
ATOM   5259 C  CB    . ASP B 1 150 ? -24.340 -11.619 50.426  1.00 49.67 ? 150  ASP B CB    1 
ATOM   5260 C  CG    . ASP B 1 150 ? -24.278 -10.175 50.887  1.00 53.12 ? 150  ASP B CG    1 
ATOM   5261 O  OD1   . ASP B 1 150 ? -23.542 -9.885  51.887  1.00 61.21 ? 150  ASP B OD1   1 
ATOM   5262 O  OD2   . ASP B 1 150 ? -24.973 -9.358  50.264  1.00 58.03 ? 150  ASP B OD2   1 
ATOM   5263 N  N     . VAL B 1 151 ? -22.684 -14.762 50.983  1.00 46.40 ? 151  VAL B N     1 
ATOM   5264 C  CA    . VAL B 1 151 ? -22.871 -16.039 51.721  1.00 47.09 ? 151  VAL B CA    1 
ATOM   5265 C  C     . VAL B 1 151 ? -21.492 -16.686 51.756  1.00 45.09 ? 151  VAL B C     1 
ATOM   5266 O  O     . VAL B 1 151 ? -21.203 -17.576 50.911  1.00 52.60 ? 151  VAL B O     1 
ATOM   5267 C  CB    . VAL B 1 151 ? -23.943 -16.947 51.077  1.00 53.34 ? 151  VAL B CB    1 
ATOM   5268 C  CG1   . VAL B 1 151 ? -24.039 -18.302 51.770  1.00 54.71 ? 151  VAL B CG1   1 
ATOM   5269 C  CG2   . VAL B 1 151 ? -25.312 -16.284 51.019  1.00 50.76 ? 151  VAL B CG2   1 
ATOM   5270 N  N     . GLY B 1 152 ? -20.667 -16.213 52.681  1.00 36.86 ? 152  GLY B N     1 
ATOM   5271 C  CA    . GLY B 1 152 ? -19.291 -16.686 52.888  1.00 38.63 ? 152  GLY B CA    1 
ATOM   5272 C  C     . GLY B 1 152 ? -19.141 -18.203 52.918  1.00 35.88 ? 152  GLY B C     1 
ATOM   5273 O  O     . GLY B 1 152 ? -18.056 -18.655 52.479  1.00 37.00 ? 152  GLY B O     1 
ATOM   5274 N  N     . TRP B 1 153 ? -20.123 -18.973 53.423  1.00 35.87 ? 153  TRP B N     1 
ATOM   5275 C  CA    . TRP B 1 153 ? -20.000 -20.458 53.585  1.00 37.97 ? 153  TRP B CA    1 
ATOM   5276 C  C     . TRP B 1 153 ? -20.285 -21.220 52.274  1.00 33.15 ? 153  TRP B C     1 
ATOM   5277 O  O     . TRP B 1 153 ? -20.138 -22.450 52.268  1.00 28.17 ? 153  TRP B O     1 
ATOM   5278 C  CB    . TRP B 1 153 ? -20.821 -21.008 54.776  1.00 45.51 ? 153  TRP B CB    1 
ATOM   5279 C  CG    . TRP B 1 153 ? -22.305 -20.792 54.766  1.00 56.41 ? 153  TRP B CG    1 
ATOM   5280 C  CD1   . TRP B 1 153 ? -23.116 -20.636 53.680  1.00 64.10 ? 153  TRP B CD1   1 
ATOM   5281 C  CD2   . TRP B 1 153 ? -23.175 -20.742 55.919  1.00 65.33 ? 153  TRP B CD2   1 
ATOM   5282 N  NE1   . TRP B 1 153 ? -24.420 -20.476 54.071  1.00 69.45 ? 153  TRP B NE1   1 
ATOM   5283 C  CE2   . TRP B 1 153 ? -24.489 -20.536 55.441  1.00 68.26 ? 153  TRP B CE2   1 
ATOM   5284 C  CE3   . TRP B 1 153 ? -22.977 -20.824 57.305  1.00 69.53 ? 153  TRP B CE3   1 
ATOM   5285 C  CZ2   . TRP B 1 153 ? -25.588 -20.419 56.296  1.00 70.29 ? 153  TRP B CZ2   1 
ATOM   5286 C  CZ3   . TRP B 1 153 ? -24.065 -20.709 58.148  1.00 69.48 ? 153  TRP B CZ3   1 
ATOM   5287 C  CH2   . TRP B 1 153 ? -25.352 -20.504 57.648  1.00 67.29 ? 153  TRP B CH2   1 
ATOM   5288 N  N     . GLY B 1 154 ? -20.613 -20.527 51.180  1.00 30.67 ? 154  GLY B N     1 
ATOM   5289 C  CA    . GLY B 1 154 ? -20.905 -21.150 49.874  1.00 28.30 ? 154  GLY B CA    1 
ATOM   5290 C  C     . GLY B 1 154 ? -19.648 -21.531 49.084  1.00 24.71 ? 154  GLY B C     1 
ATOM   5291 O  O     . GLY B 1 154 ? -18.523 -21.173 49.502  1.00 25.25 ? 154  GLY B O     1 
ATOM   5292 N  N     . SER B 1 155 ? -19.844 -22.209 47.951  1.00 22.80 ? 155  SER B N     1 
ATOM   5293 C  CA    . SER B 1 155 ? -18.764 -22.714 47.050  1.00 22.87 ? 155  SER B CA    1 
ATOM   5294 C  C     . SER B 1 155 ? -18.443 -21.695 45.956  1.00 20.03 ? 155  SER B C     1 
ATOM   5295 O  O     . SER B 1 155 ? -19.359 -21.347 45.191  1.00 21.33 ? 155  SER B O     1 
ATOM   5296 C  CB    . SER B 1 155 ? -19.123 -24.048 46.421  1.00 21.58 ? 155  SER B CB    1 
ATOM   5297 O  OG    . SER B 1 155 ? -18.165 -24.385 45.422  1.00 21.62 ? 155  SER B OG    1 
ATOM   5298 N  N     . VAL B 1 156 ? -17.170 -21.337 45.812  1.00 20.18 ? 156  VAL B N     1 
ATOM   5299 C  CA    . VAL B 1 156 ? -16.658 -20.626 44.604  1.00 21.22 ? 156  VAL B CA    1 
ATOM   5300 C  C     . VAL B 1 156 ? -17.140 -21.338 43.338  1.00 22.52 ? 156  VAL B C     1 
ATOM   5301 O  O     . VAL B 1 156 ? -17.587 -20.659 42.415  1.00 22.07 ? 156  VAL B O     1 
ATOM   5302 C  CB    . VAL B 1 156 ? -15.139 -20.512 44.600  1.00 21.69 ? 156  VAL B CB    1 
ATOM   5303 C  CG1   . VAL B 1 156 ? -14.690 -19.756 43.363  1.00 21.71 ? 156  VAL B CG1   1 
ATOM   5304 C  CG2   . VAL B 1 156 ? -14.634 -19.842 45.886  1.00 23.87 ? 156  VAL B CG2   1 
ATOM   5305 N  N     . VAL B 1 157 ? -17.091 -22.669 43.299  1.00 22.64 ? 157  VAL B N     1 
ATOM   5306 C  CA    . VAL B 1 157 ? -17.499 -23.456 42.098  1.00 20.99 ? 157  VAL B CA    1 
ATOM   5307 C  C     . VAL B 1 157 ? -19.022 -23.452 42.002  1.00 20.74 ? 157  VAL B C     1 
ATOM   5308 O  O     . VAL B 1 157 ? -19.519 -22.978 40.984  1.00 21.50 ? 157  VAL B O     1 
ATOM   5309 C  CB    . VAL B 1 157 ? -16.927 -24.883 42.137  1.00 19.64 ? 157  VAL B CB    1 
ATOM   5310 C  CG1   . VAL B 1 157 ? -17.478 -25.792 41.051  1.00 17.64 ? 157  VAL B CG1   1 
ATOM   5311 C  CG2   . VAL B 1 157 ? -15.431 -24.804 42.064  1.00 21.38 ? 157  VAL B CG2   1 
ATOM   5312 N  N     . GLY B 1 158 ? -19.706 -24.026 42.996  1.00 19.61 ? 158  GLY B N     1 
ATOM   5313 C  CA    . GLY B 1 158 ? -21.157 -24.296 42.969  1.00 19.15 ? 158  GLY B CA    1 
ATOM   5314 C  C     . GLY B 1 158 ? -21.970 -23.057 42.612  1.00 19.59 ? 158  GLY B C     1 
ATOM   5315 O  O     . GLY B 1 158 ? -22.948 -23.149 41.806  1.00 18.80 ? 158  GLY B O     1 
ATOM   5316 N  N     . ASN B 1 159 ? -21.618 -21.927 43.210  1.00 19.80 ? 159  ASN B N     1 
ATOM   5317 C  CA    . ASN B 1 159 ? -22.323 -20.640 42.969  1.00 18.93 ? 159  ASN B CA    1 
ATOM   5318 C  C     . ASN B 1 159 ? -22.108 -20.235 41.503  1.00 17.69 ? 159  ASN B C     1 
ATOM   5319 O  O     . ASN B 1 159 ? -23.052 -19.840 40.828  1.00 19.42 ? 159  ASN B O     1 
ATOM   5320 C  CB    . ASN B 1 159 ? -21.867 -19.616 44.001  1.00 18.26 ? 159  ASN B CB    1 
ATOM   5321 C  CG    . ASN B 1 159 ? -22.477 -18.258 43.761  1.00 20.51 ? 159  ASN B CG    1 
ATOM   5322 O  OD1   . ASN B 1 159 ? -21.979 -17.502 42.924  1.00 20.60 ? 159  ASN B OD1   1 
ATOM   5323 N  ND2   . ASN B 1 159 ? -23.540 -17.939 44.495  1.00 19.94 ? 159  ASN B ND2   1 
ATOM   5324 N  N     . ALA B 1 160 ? -20.889 -20.303 41.002  1.00 16.92 ? 160  ALA B N     1 
ATOM   5325 C  CA    . ALA B 1 160 ? -20.605 -19.886 39.612  1.00 16.61 ? 160  ALA B CA    1 
ATOM   5326 C  C     . ALA B 1 160 ? -21.456 -20.738 38.676  1.00 17.52 ? 160  ALA B C     1 
ATOM   5327 O  O     . ALA B 1 160 ? -22.070 -20.181 37.767  1.00 18.51 ? 160  ALA B O     1 
ATOM   5328 C  CB    . ALA B 1 160 ? -19.128 -19.990 39.318  1.00 17.06 ? 160  ALA B CB    1 
ATOM   5329 N  N     . LEU B 1 161 ? -21.561 -22.033 38.945  1.00 17.29 ? 161  LEU B N     1 
ATOM   5330 C  CA    . LEU B 1 161 ? -22.246 -22.989 38.038  1.00 19.18 ? 161  LEU B CA    1 
ATOM   5331 C  C     . LEU B 1 161 ? -23.741 -22.711 38.025  1.00 19.62 ? 161  LEU B C     1 
ATOM   5332 O  O     . LEU B 1 161 ? -24.372 -22.928 36.982  1.00 19.96 ? 161  LEU B O     1 
ATOM   5333 C  CB    . LEU B 1 161 ? -21.962 -24.423 38.491  1.00 19.97 ? 161  LEU B CB    1 
ATOM   5334 C  CG    . LEU B 1 161 ? -20.521 -24.912 38.300  1.00 19.97 ? 161  LEU B CG    1 
ATOM   5335 C  CD1   . LEU B 1 161 ? -20.401 -26.367 38.720  1.00 20.92 ? 161  LEU B CD1   1 
ATOM   5336 C  CD2   . LEU B 1 161 ? -20.043 -24.764 36.863  1.00 19.37 ? 161  LEU B CD2   1 
ATOM   5337 N  N     . ASP B 1 162 ? -24.292 -22.195 39.123  1.00 22.45 ? 162  ASP B N     1 
ATOM   5338 C  CA    . ASP B 1 162 ? -25.739 -21.863 39.193  1.00 22.77 ? 162  ASP B CA    1 
ATOM   5339 C  C     . ASP B 1 162 ? -25.954 -20.418 38.720  1.00 22.40 ? 162  ASP B C     1 
ATOM   5340 O  O     . ASP B 1 162 ? -27.032 -19.898 38.978  1.00 23.28 ? 162  ASP B O     1 
ATOM   5341 C  CB    . ASP B 1 162 ? -26.312 -22.096 40.593  1.00 23.66 ? 162  ASP B CB    1 
ATOM   5342 C  CG    . ASP B 1 162 ? -27.753 -22.614 40.591  1.00 26.32 ? 162  ASP B CG    1 
ATOM   5343 O  OD1   . ASP B 1 162 ? -28.121 -23.286 39.593  1.00 25.12 ? 162  ASP B OD1   1 
ATOM   5344 O  OD2   . ASP B 1 162 ? -28.516 -22.342 41.588  1.00 26.15 ? 162  ASP B OD2   1 
ATOM   5345 N  N     . HIS B 1 163 ? -24.952 -19.801 38.101  1.00 19.45 ? 163  HIS B N     1 
ATOM   5346 C  CA    . HIS B 1 163 ? -24.999 -18.419 37.572  1.00 19.76 ? 163  HIS B CA    1 
ATOM   5347 C  C     . HIS B 1 163 ? -25.190 -17.417 38.717  1.00 19.63 ? 163  HIS B C     1 
ATOM   5348 O  O     . HIS B 1 163 ? -25.910 -16.413 38.508  1.00 21.10 ? 163  HIS B O     1 
ATOM   5349 C  CB    . HIS B 1 163 ? -26.084 -18.276 36.496  1.00 20.21 ? 163  HIS B CB    1 
ATOM   5350 C  CG    . HIS B 1 163 ? -25.902 -19.168 35.319  1.00 21.25 ? 163  HIS B CG    1 
ATOM   5351 N  ND1   . HIS B 1 163 ? -26.923 -19.392 34.409  1.00 21.52 ? 163  HIS B ND1   1 
ATOM   5352 C  CD2   . HIS B 1 163 ? -24.813 -19.842 34.858  1.00 22.04 ? 163  HIS B CD2   1 
ATOM   5353 C  CE1   . HIS B 1 163 ? -26.473 -20.215 33.458  1.00 22.49 ? 163  HIS B CE1   1 
ATOM   5354 N  NE2   . HIS B 1 163 ? -25.188 -20.525 33.723  1.00 20.93 ? 163  HIS B NE2   1 
ATOM   5355 N  N     . GLY B 1 164 ? -24.499 -17.623 39.833  1.00 19.98 ? 164  GLY B N     1 
ATOM   5356 C  CA    . GLY B 1 164 ? -24.538 -16.750 41.018  1.00 20.90 ? 164  GLY B CA    1 
ATOM   5357 C  C     . GLY B 1 164 ? -23.860 -15.410 40.776  1.00 23.26 ? 164  GLY B C     1 
ATOM   5358 O  O     . GLY B 1 164 ? -23.151 -15.265 39.746  1.00 21.85 ? 164  GLY B O     1 
ATOM   5359 N  N     . ILE B 1 165 ? -24.087 -14.454 41.680  1.00 22.72 ? 165  ILE B N     1 
ATOM   5360 C  CA    . ILE B 1 165 ? -23.706 -13.022 41.509  1.00 23.44 ? 165  ILE B CA    1 
ATOM   5361 C  C     . ILE B 1 165 ? -23.167 -12.475 42.833  1.00 22.49 ? 165  ILE B C     1 
ATOM   5362 O  O     . ILE B 1 165 ? -23.619 -12.917 43.901  1.00 24.54 ? 165  ILE B O     1 
ATOM   5363 C  CB    . ILE B 1 165 ? -24.905 -12.195 41.033  1.00 26.12 ? 165  ILE B CB    1 
ATOM   5364 C  CG1   . ILE B 1 165 ? -26.081 -12.371 42.000  1.00 30.02 ? 165  ILE B CG1   1 
ATOM   5365 C  CG2   . ILE B 1 165 ? -25.261 -12.561 39.607  1.00 27.20 ? 165  ILE B CG2   1 
ATOM   5366 C  CD1   . ILE B 1 165 ? -27.210 -11.379 41.822  1.00 33.35 ? 165  ILE B CD1   1 
ATOM   5367 N  N     . GLY B 1 166 ? -22.221 -11.550 42.745  1.00 20.85 ? 166  GLY B N     1 
ATOM   5368 C  CA    . GLY B 1 166 ? -21.717 -10.776 43.886  1.00 22.13 ? 166  GLY B CA    1 
ATOM   5369 C  C     . GLY B 1 166 ? -21.687 -9.308  43.544  1.00 20.47 ? 166  GLY B C     1 
ATOM   5370 O  O     . GLY B 1 166 ? -22.417 -8.931  42.649  1.00 21.43 ? 166  GLY B O     1 
ATOM   5371 N  N     . TYR B 1 167 ? -20.896 -8.517  44.258  1.00 20.84 ? 167  TYR B N     1 
ATOM   5372 C  CA    . TYR B 1 167 ? -21.106 -7.052  44.393  1.00 21.06 ? 167  TYR B CA    1 
ATOM   5373 C  C     . TYR B 1 167 ? -19.829 -6.284  44.072  1.00 19.75 ? 167  TYR B C     1 
ATOM   5374 O  O     . TYR B 1 167 ? -19.799 -5.120  44.414  1.00 20.66 ? 167  TYR B O     1 
ATOM   5375 C  CB    . TYR B 1 167 ? -21.721 -6.759  45.766  1.00 22.18 ? 167  TYR B CB    1 
ATOM   5376 C  CG    . TYR B 1 167 ? -23.000 -7.521  45.886  1.00 24.60 ? 167  TYR B CG    1 
ATOM   5377 C  CD1   . TYR B 1 167 ? -24.178 -7.052  45.328  1.00 27.78 ? 167  TYR B CD1   1 
ATOM   5378 C  CD2   . TYR B 1 167 ? -22.994 -8.796  46.432  1.00 26.66 ? 167  TYR B CD2   1 
ATOM   5379 C  CE1   . TYR B 1 167 ? -25.343 -7.811  45.366  1.00 28.90 ? 167  TYR B CE1   1 
ATOM   5380 C  CE2   . TYR B 1 167 ? -24.136 -9.566  46.466  1.00 27.37 ? 167  TYR B CE2   1 
ATOM   5381 C  CZ    . TYR B 1 167 ? -25.309 -9.084  45.916  1.00 28.77 ? 167  TYR B CZ    1 
ATOM   5382 O  OH    . TYR B 1 167 ? -26.408 -9.898  45.946  1.00 31.34 ? 167  TYR B OH    1 
ATOM   5383 N  N     . THR B 1 168 ? -18.862 -6.886  43.365  1.00 21.61 ? 168  THR B N     1 
ATOM   5384 C  CA    . THR B 1 168 ? -17.672 -6.181  42.807  1.00 20.70 ? 168  THR B CA    1 
ATOM   5385 C  C     . THR B 1 168 ? -17.774 -6.180  41.283  1.00 21.10 ? 168  THR B C     1 
ATOM   5386 O  O     . THR B 1 168 ? -18.735 -6.709  40.708  1.00 20.98 ? 168  THR B O     1 
ATOM   5387 C  CB    . THR B 1 168 ? -16.350 -6.782  43.312  1.00 23.40 ? 168  THR B CB    1 
ATOM   5388 O  OG1   . THR B 1 168 ? -15.895 -7.824  42.437  1.00 20.18 ? 168  THR B OG1   1 
ATOM   5389 C  CG2   . THR B 1 168 ? -16.446 -7.296  44.739  1.00 23.53 ? 168  THR B CG2   1 
ATOM   5390 N  N     . PRO B 1 169 ? -16.810 -5.542  40.590  1.00 18.53 ? 169  PRO B N     1 
ATOM   5391 C  CA    . PRO B 1 169 ? -16.794 -5.570  39.135  1.00 20.01 ? 169  PRO B CA    1 
ATOM   5392 C  C     . PRO B 1 169 ? -16.663 -7.015  38.600  1.00 21.99 ? 169  PRO B C     1 
ATOM   5393 O  O     . PRO B 1 169 ? -17.031 -7.243  37.461  1.00 21.59 ? 169  PRO B O     1 
ATOM   5394 C  CB    . PRO B 1 169 ? -15.617 -4.653  38.743  1.00 20.47 ? 169  PRO B CB    1 
ATOM   5395 C  CG    . PRO B 1 169 ? -15.286 -3.824  40.000  1.00 19.53 ? 169  PRO B CG    1 
ATOM   5396 C  CD    . PRO B 1 169 ? -15.760 -4.682  41.164  1.00 19.10 ? 169  PRO B CD    1 
ATOM   5397 N  N     . TYR B 1 170 ? -16.225 -7.980  39.419  1.00 20.15 ? 170  TYR B N     1 
ATOM   5398 C  CA    . TYR B 1 170 ? -16.187 -9.419  39.058  1.00 19.15 ? 170  TYR B CA    1 
ATOM   5399 C  C     . TYR B 1 170 ? -17.466 -10.137 39.519  1.00 19.87 ? 170  TYR B C     1 
ATOM   5400 O  O     . TYR B 1 170 ? -17.403 -11.355 39.819  1.00 17.65 ? 170  TYR B O     1 
ATOM   5401 C  CB    . TYR B 1 170 ? -14.942 -10.092 39.636  1.00 19.72 ? 170  TYR B CB    1 
ATOM   5402 C  CG    . TYR B 1 170 ? -13.648 -9.838  38.893  1.00 18.62 ? 170  TYR B CG    1 
ATOM   5403 C  CD1   . TYR B 1 170 ? -13.243 -8.549  38.535  1.00 17.80 ? 170  TYR B CD1   1 
ATOM   5404 C  CD2   . TYR B 1 170 ? -12.809 -10.898 38.579  1.00 16.82 ? 170  TYR B CD2   1 
ATOM   5405 C  CE1   . TYR B 1 170 ? -12.051 -8.334  37.849  1.00 19.76 ? 170  TYR B CE1   1 
ATOM   5406 C  CE2   . TYR B 1 170 ? -11.614 -10.688 37.904  1.00 18.35 ? 170  TYR B CE2   1 
ATOM   5407 C  CZ    . TYR B 1 170 ? -11.216 -9.407  37.556  1.00 17.54 ? 170  TYR B CZ    1 
ATOM   5408 O  OH    . TYR B 1 170 ? -10.018 -9.239  36.920  1.00 17.17 ? 170  TYR B OH    1 
ATOM   5409 N  N     . GLY B 1 171 ? -18.606 -9.433  39.533  1.00 20.53 ? 171  GLY B N     1 
ATOM   5410 C  CA    . GLY B 1 171 ? -19.860 -9.930  40.137  1.00 20.17 ? 171  GLY B CA    1 
ATOM   5411 C  C     . GLY B 1 171 ? -20.558 -11.021 39.342  1.00 20.33 ? 171  GLY B C     1 
ATOM   5412 O  O     . GLY B 1 171 ? -21.383 -11.759 39.944  1.00 19.65 ? 171  GLY B O     1 
ATOM   5413 N  N     . ASP B 1 172 ? -20.332 -11.124 38.030  1.00 20.05 ? 172  ASP B N     1 
ATOM   5414 C  CA    . ASP B 1 172 ? -20.924 -12.209 37.208  1.00 19.04 ? 172  ASP B CA    1 
ATOM   5415 C  C     . ASP B 1 172 ? -19.981 -13.417 37.355  1.00 18.70 ? 172  ASP B C     1 
ATOM   5416 O  O     . ASP B 1 172 ? -18.945 -13.492 36.645  1.00 14.45 ? 172  ASP B O     1 
ATOM   5417 C  CB    . ASP B 1 172 ? -21.192 -11.757 35.770  1.00 19.86 ? 172  ASP B CB    1 
ATOM   5418 C  CG    . ASP B 1 172 ? -21.901 -12.817 34.917  1.00 22.74 ? 172  ASP B CG    1 
ATOM   5419 O  OD1   . ASP B 1 172 ? -22.026 -14.002 35.379  1.00 20.15 ? 172  ASP B OD1   1 
ATOM   5420 O  OD2   . ASP B 1 172 ? -22.342 -12.452 33.790  1.00 22.96 ? 172  ASP B OD2   1 
ATOM   5421 N  N     . HIS B 1 173 ? -20.265 -14.288 38.335  1.00 18.64 ? 173  HIS B N     1 
ATOM   5422 C  CA    . HIS B 1 173 ? -19.302 -15.345 38.798  1.00 18.63 ? 173  HIS B CA    1 
ATOM   5423 C  C     . HIS B 1 173 ? -18.977 -16.300 37.628  1.00 19.65 ? 173  HIS B C     1 
ATOM   5424 O  O     . HIS B 1 173 ? -17.783 -16.556 37.355  1.00 18.44 ? 173  HIS B O     1 
ATOM   5425 C  CB    . HIS B 1 173 ? -19.845 -16.042 40.060  1.00 19.79 ? 173  HIS B CB    1 
ATOM   5426 C  CG    . HIS B 1 173 ? -19.849 -15.146 41.253  1.00 19.93 ? 173  HIS B CG    1 
ATOM   5427 N  ND1   . HIS B 1 173 ? -20.467 -15.483 42.435  1.00 21.49 ? 173  HIS B ND1   1 
ATOM   5428 C  CD2   . HIS B 1 173 ? -19.278 -13.940 41.456  1.00 21.78 ? 173  HIS B CD2   1 
ATOM   5429 C  CE1   . HIS B 1 173 ? -20.270 -14.528 43.314  1.00 23.16 ? 173  HIS B CE1   1 
ATOM   5430 N  NE2   . HIS B 1 173 ? -19.538 -13.563 42.745  1.00 22.68 ? 173  HIS B NE2   1 
ATOM   5431 N  N     . PHE B 1 174 ? -19.983 -16.745 36.875  1.00 18.18 ? 174  PHE B N     1 
ATOM   5432 C  CA    . PHE B 1 174 ? -19.731 -17.656 35.735  1.00 17.70 ? 174  PHE B CA    1 
ATOM   5433 C  C     . PHE B 1 174 ? -19.002 -16.940 34.580  1.00 17.15 ? 174  PHE B C     1 
ATOM   5434 O  O     . PHE B 1 174 ? -18.206 -17.607 33.861  1.00 17.78 ? 174  PHE B O     1 
ATOM   5435 C  CB    . PHE B 1 174 ? -20.989 -18.401 35.297  1.00 16.86 ? 174  PHE B CB    1 
ATOM   5436 C  CG    . PHE B 1 174 ? -20.634 -19.547 34.372  1.00 18.02 ? 174  PHE B CG    1 
ATOM   5437 C  CD1   . PHE B 1 174 ? -19.961 -20.664 34.859  1.00 17.44 ? 174  PHE B CD1   1 
ATOM   5438 C  CD2   . PHE B 1 174 ? -20.876 -19.464 33.004  1.00 16.02 ? 174  PHE B CD2   1 
ATOM   5439 C  CE1   . PHE B 1 174 ? -19.626 -21.717 34.017  1.00 17.20 ? 174  PHE B CE1   1 
ATOM   5440 C  CE2   . PHE B 1 174 ? -20.534 -20.513 32.166  1.00 16.36 ? 174  PHE B CE2   1 
ATOM   5441 C  CZ    . PHE B 1 174 ? -19.921 -21.639 32.671  1.00 17.69 ? 174  PHE B CZ    1 
ATOM   5442 N  N     . ALA B 1 175 ? -19.152 -15.623 34.424  1.00 17.62 ? 175  ALA B N     1 
ATOM   5443 C  CA    . ALA B 1 175 ? -18.410 -14.867 33.394  1.00 17.59 ? 175  ALA B CA    1 
ATOM   5444 C  C     . ALA B 1 175 ? -16.919 -14.875 33.731  1.00 18.07 ? 175  ALA B C     1 
ATOM   5445 O  O     . ALA B 1 175 ? -16.073 -14.809 32.787  1.00 17.95 ? 175  ALA B O     1 
ATOM   5446 C  CB    . ALA B 1 175 ? -18.970 -13.482 33.234  1.00 18.63 ? 175  ALA B CB    1 
ATOM   5447 N  N     . MET B 1 176 ? -16.577 -14.964 35.019  1.00 17.22 ? 176  MET B N     1 
ATOM   5448 C  CA    . MET B 1 176 ? -15.171 -14.917 35.464  1.00 17.53 ? 176  MET B CA    1 
ATOM   5449 C  C     . MET B 1 176 ? -14.589 -16.340 35.513  1.00 18.03 ? 176  MET B C     1 
ATOM   5450 O  O     . MET B 1 176 ? -13.408 -16.458 35.844  1.00 18.50 ? 176  MET B O     1 
ATOM   5451 C  CB    . MET B 1 176 ? -15.034 -14.226 36.828  1.00 18.92 ? 176  MET B CB    1 
ATOM   5452 C  CG    . MET B 1 176 ? -15.500 -12.756 36.834  1.00 20.86 ? 176  MET B CG    1 
ATOM   5453 S  SD    . MET B 1 176 ? -14.531 -11.699 35.691  1.00 22.92 ? 176  MET B SD    1 
ATOM   5454 C  CE    . MET B 1 176 ? -15.667 -11.585 34.312  1.00 24.36 ? 176  MET B CE    1 
ATOM   5455 N  N     . GLN B 1 177 ? -15.371 -17.376 35.197  1.00 17.88 ? 177  GLN B N     1 
ATOM   5456 C  CA    . GLN B 1 177 ? -14.892 -18.789 35.132  1.00 18.71 ? 177  GLN B CA    1 
ATOM   5457 C  C     . GLN B 1 177 ? -13.966 -18.984 33.907  1.00 17.78 ? 177  GLN B C     1 
ATOM   5458 O  O     . GLN B 1 177 ? -14.170 -18.352 32.825  1.00 17.04 ? 177  GLN B O     1 
ATOM   5459 C  CB    . GLN B 1 177 ? -16.071 -19.774 35.145  1.00 19.03 ? 177  GLN B CB    1 
ATOM   5460 C  CG    . GLN B 1 177 ? -15.644 -21.238 35.009  1.00 18.81 ? 177  GLN B CG    1 
ATOM   5461 C  CD    . GLN B 1 177 ? -15.501 -21.654 33.560  1.00 18.77 ? 177  GLN B CD    1 
ATOM   5462 O  OE1   . GLN B 1 177 ? -16.139 -21.112 32.682  1.00 19.67 ? 177  GLN B OE1   1 
ATOM   5463 N  NE2   . GLN B 1 177 ? -14.698 -22.665 33.298  1.00 20.28 ? 177  GLN B NE2   1 
ATOM   5464 N  N     . CYS B 1 178 ? -12.906 -19.776 34.079  1.00 17.43 ? 178  CYS B N     1 
ATOM   5465 C  CA    . CYS B 1 178 ? -11.904 -20.024 33.013  1.00 16.52 ? 178  CYS B CA    1 
ATOM   5466 C  C     . CYS B 1 178 ? -11.249 -21.390 33.262  1.00 16.41 ? 178  CYS B C     1 
ATOM   5467 O  O     . CYS B 1 178 ? -10.480 -21.525 34.206  1.00 15.06 ? 178  CYS B O     1 
ATOM   5468 C  CB    . CYS B 1 178 ? -10.906 -18.886 32.952  1.00 16.53 ? 178  CYS B CB    1 
ATOM   5469 S  SG    . CYS B 1 178 ? -9.796  -18.942 31.525  1.00 16.04 ? 178  CYS B SG    1 
ATOM   5470 N  N     . GLY B 1 179 ? -11.595 -22.364 32.431  1.00 15.58 ? 179  GLY B N     1 
ATOM   5471 C  CA    . GLY B 1 179 ? -11.125 -23.750 32.537  1.00 16.89 ? 179  GLY B CA    1 
ATOM   5472 C  C     . GLY B 1 179 ? -11.926 -24.528 33.559  1.00 16.90 ? 179  GLY B C     1 
ATOM   5473 O  O     . GLY B 1 179 ? -12.211 -23.976 34.631  1.00 15.30 ? 179  GLY B O     1 
ATOM   5474 N  N     . MET B 1 180 ? -12.282 -25.771 33.248  1.00 17.98 ? 180  MET B N     1 
ATOM   5475 C  CA    . MET B 1 180 ? -12.835 -26.694 34.275  1.00 17.60 ? 180  MET B CA    1 
ATOM   5476 C  C     . MET B 1 180 ? -12.436 -28.129 33.934  1.00 17.78 ? 180  MET B C     1 
ATOM   5477 O  O     . MET B 1 180 ? -12.126 -28.424 32.776  1.00 17.14 ? 180  MET B O     1 
ATOM   5478 C  CB    . MET B 1 180 ? -14.366 -26.606 34.399  1.00 17.83 ? 180  MET B CB    1 
ATOM   5479 C  CG    . MET B 1 180 ? -15.097 -26.813 33.126  1.00 18.96 ? 180  MET B CG    1 
ATOM   5480 S  SD    . MET B 1 180 ? -16.921 -26.816 33.251  1.00 20.96 ? 180  MET B SD    1 
ATOM   5481 C  CE    . MET B 1 180 ? -17.226 -25.149 33.864  1.00 20.22 ? 180  MET B CE    1 
ATOM   5482 N  N     . GLU B 1 181 ? -12.523 -28.996 34.925  1.00 17.35 ? 181  GLU B N     1 
ATOM   5483 C  CA    . GLU B 1 181 ? -12.464 -30.457 34.754  1.00 17.71 ? 181  GLU B CA    1 
ATOM   5484 C  C     . GLU B 1 181 ? -13.843 -31.001 35.121  1.00 18.11 ? 181  GLU B C     1 
ATOM   5485 O  O     . GLU B 1 181 ? -14.414 -30.571 36.160  1.00 17.42 ? 181  GLU B O     1 
ATOM   5486 C  CB    . GLU B 1 181 ? -11.356 -31.031 35.633  1.00 19.07 ? 181  GLU B CB    1 
ATOM   5487 C  CG    . GLU B 1 181 ? -11.267 -32.538 35.592  1.00 20.13 ? 181  GLU B CG    1 
ATOM   5488 C  CD    . GLU B 1 181 ? -10.201 -33.045 36.543  1.00 19.55 ? 181  GLU B CD    1 
ATOM   5489 O  OE1   . GLU B 1 181 ? -9.042  -33.080 36.144  1.00 21.31 ? 181  GLU B OE1   1 
ATOM   5490 O  OE2   . GLU B 1 181 ? -10.530 -33.268 37.701  1.00 18.17 ? 181  GLU B OE2   1 
ATOM   5491 N  N     . VAL B 1 182 ? -14.356 -31.870 34.262  1.00 17.65 ? 182  VAL B N     1 
ATOM   5492 C  CA    . VAL B 1 182 ? -15.712 -32.437 34.339  1.00 19.39 ? 182  VAL B CA    1 
ATOM   5493 C  C     . VAL B 1 182 ? -15.581 -33.954 34.270  1.00 21.65 ? 182  VAL B C     1 
ATOM   5494 O  O     . VAL B 1 182 ? -14.929 -34.453 33.326  1.00 19.42 ? 182  VAL B O     1 
ATOM   5495 C  CB    . VAL B 1 182 ? -16.600 -31.903 33.207  1.00 19.92 ? 182  VAL B CB    1 
ATOM   5496 C  CG1   . VAL B 1 182 ? -18.028 -32.370 33.384  1.00 19.48 ? 182  VAL B CG1   1 
ATOM   5497 C  CG2   . VAL B 1 182 ? -16.526 -30.385 33.112  1.00 20.70 ? 182  VAL B CG2   1 
ATOM   5498 N  N     . VAL B 1 183 ? -16.174 -34.632 35.250  1.00 20.81 ? 183  VAL B N     1 
ATOM   5499 C  CA    . VAL B 1 183 ? -16.527 -36.067 35.111  1.00 20.75 ? 183  VAL B CA    1 
ATOM   5500 C  C     . VAL B 1 183 ? -17.855 -36.150 34.351  1.00 20.37 ? 183  VAL B C     1 
ATOM   5501 O  O     . VAL B 1 183 ? -18.885 -35.721 34.868  1.00 21.87 ? 183  VAL B O     1 
ATOM   5502 C  CB    . VAL B 1 183 ? -16.543 -36.729 36.502  1.00 20.67 ? 183  VAL B CB    1 
ATOM   5503 C  CG1   . VAL B 1 183 ? -16.915 -38.195 36.441  1.00 19.96 ? 183  VAL B CG1   1 
ATOM   5504 C  CG2   . VAL B 1 183 ? -15.175 -36.554 37.146  1.00 20.85 ? 183  VAL B CG2   1 
ATOM   5505 N  N     . LEU B 1 184 ? -17.811 -36.711 33.157  1.00 19.86 ? 184  LEU B N     1 
ATOM   5506 C  CA    . LEU B 1 184 ? -18.981 -36.940 32.295  1.00 19.40 ? 184  LEU B CA    1 
ATOM   5507 C  C     . LEU B 1 184 ? -19.826 -38.062 32.877  1.00 20.46 ? 184  LEU B C     1 
ATOM   5508 O  O     . LEU B 1 184 ? -19.382 -38.791 33.770  1.00 20.33 ? 184  LEU B O     1 
ATOM   5509 C  CB    . LEU B 1 184 ? -18.512 -37.272 30.882  1.00 20.50 ? 184  LEU B CB    1 
ATOM   5510 C  CG    . LEU B 1 184 ? -17.728 -36.179 30.173  1.00 19.77 ? 184  LEU B CG    1 
ATOM   5511 C  CD1   . LEU B 1 184 ? -17.279 -36.656 28.801  1.00 21.33 ? 184  LEU B CD1   1 
ATOM   5512 C  CD2   . LEU B 1 184 ? -18.570 -34.928 30.076  1.00 20.92 ? 184  LEU B CD2   1 
ATOM   5513 N  N     . PRO B 1 185 ? -21.104 -38.144 32.457  1.00 20.40 ? 185  PRO B N     1 
ATOM   5514 C  CA    . PRO B 1 185 ? -22.043 -39.117 33.011  1.00 22.39 ? 185  PRO B CA    1 
ATOM   5515 C  C     . PRO B 1 185 ? -21.627 -40.593 32.845  1.00 24.71 ? 185  PRO B C     1 
ATOM   5516 O  O     . PRO B 1 185 ? -22.209 -41.399 33.553  1.00 27.06 ? 185  PRO B O     1 
ATOM   5517 C  CB    . PRO B 1 185 ? -23.371 -38.790 32.296  1.00 21.44 ? 185  PRO B CB    1 
ATOM   5518 C  CG    . PRO B 1 185 ? -23.228 -37.318 31.904  1.00 21.44 ? 185  PRO B CG    1 
ATOM   5519 C  CD    . PRO B 1 185 ? -21.767 -37.190 31.547  1.00 21.48 ? 185  PRO B CD    1 
ATOM   5520 N  N     . ASN B 1 186 ? -20.609 -40.916 32.036  1.00 23.05 ? 186  ASN B N     1 
ATOM   5521 C  CA    . ASN B 1 186 ? -20.042 -42.292 31.924  1.00 25.22 ? 186  ASN B CA    1 
ATOM   5522 C  C     . ASN B 1 186 ? -18.833 -42.476 32.844  1.00 24.90 ? 186  ASN B C     1 
ATOM   5523 O  O     . ASN B 1 186 ? -18.227 -43.565 32.784  1.00 27.32 ? 186  ASN B O     1 
ATOM   5524 C  CB    . ASN B 1 186 ? -19.593 -42.649 30.509  1.00 24.56 ? 186  ASN B CB    1 
ATOM   5525 C  CG    . ASN B 1 186 ? -18.508 -41.721 29.999  1.00 27.88 ? 186  ASN B CG    1 
ATOM   5526 O  OD1   . ASN B 1 186 ? -18.076 -40.790 30.688  1.00 25.81 ? 186  ASN B OD1   1 
ATOM   5527 N  ND2   . ASN B 1 186 ? -18.115 -41.921 28.755  1.00 28.60 ? 186  ASN B ND2   1 
ATOM   5528 N  N     . GLY B 1 187 ? -18.465 -41.459 33.626  1.00 22.46 ? 187  GLY B N     1 
ATOM   5529 C  CA    . GLY B 1 187 ? -17.363 -41.536 34.606  1.00 21.95 ? 187  GLY B CA    1 
ATOM   5530 C  C     . GLY B 1 187 ? -15.999 -41.208 34.004  1.00 22.49 ? 187  GLY B C     1 
ATOM   5531 O  O     . GLY B 1 187 ? -15.014 -41.255 34.754  1.00 24.52 ? 187  GLY B O     1 
ATOM   5532 N  N     . GLU B 1 188 ? -15.939 -40.890 32.712  1.00 21.08 ? 188  GLU B N     1 
ATOM   5533 C  CA    . GLU B 1 188 ? -14.716 -40.426 32.003  1.00 23.12 ? 188  GLU B CA    1 
ATOM   5534 C  C     . GLU B 1 188 ? -14.490 -38.937 32.341  1.00 22.72 ? 188  GLU B C     1 
ATOM   5535 O  O     . GLU B 1 188 ? -15.481 -38.203 32.601  1.00 21.79 ? 188  GLU B O     1 
ATOM   5536 C  CB    . GLU B 1 188 ? -14.877 -40.650 30.489  1.00 24.48 ? 188  GLU B CB    1 
ATOM   5537 C  CG    . GLU B 1 188 ? -14.867 -42.137 30.082  1.00 26.91 ? 188  GLU B CG    1 
ATOM   5538 C  CD    . GLU B 1 188 ? -13.615 -42.885 30.518  1.00 30.75 ? 188  GLU B CD    1 
ATOM   5539 O  OE1   . GLU B 1 188 ? -12.539 -42.581 29.969  1.00 33.31 ? 188  GLU B OE1   1 
ATOM   5540 O  OE2   . GLU B 1 188 ? -13.691 -43.671 31.485  1.00 32.30 ? 188  GLU B OE2   1 
ATOM   5541 N  N     . VAL B 1 189 ? -13.254 -38.486 32.297  1.00 20.12 ? 189  VAL B N     1 
ATOM   5542 C  CA    . VAL B 1 189 ? -12.913 -37.123 32.746  1.00 22.48 ? 189  VAL B CA    1 
ATOM   5543 C  C     . VAL B 1 189 ? -12.386 -36.338 31.543  1.00 22.79 ? 189  VAL B C     1 
ATOM   5544 O  O     . VAL B 1 189 ? -11.716 -36.907 30.642  1.00 18.92 ? 189  VAL B O     1 
ATOM   5545 C  CB    . VAL B 1 189 ? -11.961 -37.148 33.954  1.00 25.54 ? 189  VAL B CB    1 
ATOM   5546 C  CG1   . VAL B 1 189 ? -10.607 -37.727 33.590  1.00 26.45 ? 189  VAL B CG1   1 
ATOM   5547 C  CG2   . VAL B 1 189 ? -11.813 -35.766 34.559  1.00 25.94 ? 189  VAL B CG2   1 
ATOM   5548 N  N     . VAL B 1 190 ? -12.716 -35.048 31.529  1.00 22.65 ? 190  VAL B N     1 
ATOM   5549 C  CA    . VAL B 1 190 ? -12.376 -34.128 30.416  1.00 22.45 ? 190  VAL B CA    1 
ATOM   5550 C  C     . VAL B 1 190 ? -11.941 -32.785 31.010  1.00 20.51 ? 190  VAL B C     1 
ATOM   5551 O  O     . VAL B 1 190 ? -12.443 -32.404 32.101  1.00 19.93 ? 190  VAL B O     1 
ATOM   5552 C  CB    . VAL B 1 190 ? -13.565 -34.020 29.454  1.00 24.24 ? 190  VAL B CB    1 
ATOM   5553 C  CG1   . VAL B 1 190 ? -14.758 -33.358 30.119  1.00 24.57 ? 190  VAL B CG1   1 
ATOM   5554 C  CG2   . VAL B 1 190 ? -13.194 -33.293 28.184  1.00 27.79 ? 190  VAL B CG2   1 
ATOM   5555 N  N     . ARG B 1 191 ? -11.030 -32.105 30.334  1.00 18.79 ? 191  ARG B N     1 
ATOM   5556 C  CA    . ARG B 1 191 ? -10.639 -30.710 30.642  1.00 19.72 ? 191  ARG B CA    1 
ATOM   5557 C  C     . ARG B 1 191 ? -10.967 -29.785 29.462  1.00 19.82 ? 191  ARG B C     1 
ATOM   5558 O  O     . ARG B 1 191 ? -10.640 -30.132 28.282  1.00 17.91 ? 191  ARG B O     1 
ATOM   5559 C  CB    . ARG B 1 191 ? -9.155  -30.662 31.002  1.00 20.92 ? 191  ARG B CB    1 
ATOM   5560 C  CG    . ARG B 1 191 ? -8.913  -31.220 32.391  1.00 22.01 ? 191  ARG B CG    1 
ATOM   5561 C  CD    . ARG B 1 191 ? -7.468  -31.197 32.785  1.00 22.03 ? 191  ARG B CD    1 
ATOM   5562 N  NE    . ARG B 1 191 ? -7.352  -31.731 34.123  1.00 23.17 ? 191  ARG B NE    1 
ATOM   5563 C  CZ    . ARG B 1 191 ? -6.275  -31.614 34.874  1.00 26.23 ? 191  ARG B CZ    1 
ATOM   5564 N  NH1   . ARG B 1 191 ? -5.208  -30.984 34.402  1.00 27.25 ? 191  ARG B NH1   1 
ATOM   5565 N  NH2   . ARG B 1 191 ? -6.282  -32.094 36.099  1.00 26.66 ? 191  ARG B NH2   1 
ATOM   5566 N  N     . THR B 1 192 ? -11.604 -28.650 29.771  1.00 18.13 ? 192  THR B N     1 
ATOM   5567 C  CA    . THR B 1 192 ? -12.048 -27.658 28.755  1.00 17.78 ? 192  THR B CA    1 
ATOM   5568 C  C     . THR B 1 192 ? -10.918 -26.675 28.473  1.00 17.01 ? 192  THR B C     1 
ATOM   5569 O  O     . THR B 1 192 ? -10.007 -26.536 29.313  1.00 15.63 ? 192  THR B O     1 
ATOM   5570 C  CB    . THR B 1 192 ? -13.281 -26.877 29.218  1.00 18.40 ? 192  THR B CB    1 
ATOM   5571 O  OG1   . THR B 1 192 ? -12.859 -26.073 30.319  1.00 16.31 ? 192  THR B OG1   1 
ATOM   5572 C  CG2   . THR B 1 192 ? -14.424 -27.794 29.585  1.00 19.83 ? 192  THR B CG2   1 
ATOM   5573 N  N     . GLY B 1 193 ? -11.006 -25.979 27.347  1.00 16.93 ? 193  GLY B N     1 
ATOM   5574 C  CA    . GLY B 1 193 ? -10.078 -24.879 27.029  1.00 17.87 ? 193  GLY B CA    1 
ATOM   5575 C  C     . GLY B 1 193 ? -8.634  -25.334 26.904  1.00 17.96 ? 193  GLY B C     1 
ATOM   5576 O  O     . GLY B 1 193 ? -8.365  -26.416 26.328  1.00 17.47 ? 193  GLY B O     1 
ATOM   5577 N  N     . MET B 1 194 ? -7.716  -24.544 27.457  1.00 18.38 ? 194  MET B N     1 
ATOM   5578 C  CA    . MET B 1 194 ? -6.260  -24.770 27.312  1.00 17.72 ? 194  MET B CA    1 
ATOM   5579 C  C     . MET B 1 194 ? -5.857  -26.003 28.151  1.00 17.62 ? 194  MET B C     1 
ATOM   5580 O  O     . MET B 1 194 ? -4.776  -26.564 27.889  1.00 17.30 ? 194  MET B O     1 
ATOM   5581 C  CB    . MET B 1 194 ? -5.451  -23.527 27.706  1.00 17.95 ? 194  MET B CB    1 
ATOM   5582 C  CG    . MET B 1 194 ? -5.636  -22.285 26.795  1.00 18.20 ? 194  MET B CG    1 
ATOM   5583 S  SD    . MET B 1 194 ? -5.679  -22.631 25.014  1.00 20.53 ? 194  MET B SD    1 
ATOM   5584 C  CE    . MET B 1 194 ? -4.054  -23.333 24.780  1.00 20.25 ? 194  MET B CE    1 
ATOM   5585 N  N     . GLY B 1 195 ? -6.715  -26.443 29.075  1.00 18.21 ? 195  GLY B N     1 
ATOM   5586 C  CA    . GLY B 1 195 ? -6.468  -27.614 29.945  1.00 18.68 ? 195  GLY B CA    1 
ATOM   5587 C  C     . GLY B 1 195 ? -6.439  -28.907 29.131  1.00 19.73 ? 195  GLY B C     1 
ATOM   5588 O  O     . GLY B 1 195 ? -5.915  -29.907 29.652  1.00 19.56 ? 195  GLY B O     1 
ATOM   5589 N  N     . ALA B 1 196 ? -7.012  -28.916 27.914  1.00 18.14 ? 196  ALA B N     1 
ATOM   5590 C  CA    . ALA B 1 196 ? -6.962  -30.081 26.994  1.00 18.52 ? 196  ALA B CA    1 
ATOM   5591 C  C     . ALA B 1 196 ? -5.565  -30.192 26.375  1.00 18.39 ? 196  ALA B C     1 
ATOM   5592 O  O     . ALA B 1 196 ? -5.322  -31.211 25.749  1.00 19.07 ? 196  ALA B O     1 
ATOM   5593 C  CB    . ALA B 1 196 ? -8.019  -30.002 25.916  1.00 19.17 ? 196  ALA B CB    1 
ATOM   5594 N  N     . MET B 1 197 ? -4.682  -29.199 26.532  1.00 18.30 ? 197  MET B N     1 
ATOM   5595 C  CA    . MET B 1 197 ? -3.302  -29.284 25.978  1.00 20.45 ? 197  MET B CA    1 
ATOM   5596 C  C     . MET B 1 197 ? -2.328  -29.710 27.074  1.00 21.35 ? 197  MET B C     1 
ATOM   5597 O  O     . MET B 1 197 ? -2.088  -28.934 27.992  1.00 18.48 ? 197  MET B O     1 
ATOM   5598 C  CB    . MET B 1 197 ? -2.826  -27.963 25.358  1.00 21.71 ? 197  MET B CB    1 
ATOM   5599 C  CG    . MET B 1 197 ? -1.337  -27.946 25.145  1.00 24.56 ? 197  MET B CG    1 
ATOM   5600 S  SD    . MET B 1 197 ? -0.760  -26.720 23.996  1.00 28.42 ? 197  MET B SD    1 
ATOM   5601 C  CE    . MET B 1 197 ? -1.118  -27.562 22.457  1.00 29.94 ? 197  MET B CE    1 
ATOM   5602 N  N     . PRO B 1 198 ? -1.674  -30.903 26.958  1.00 23.29 ? 198  PRO B N     1 
ATOM   5603 C  CA    . PRO B 1 198 ? -0.617  -31.303 27.884  1.00 21.96 ? 198  PRO B CA    1 
ATOM   5604 C  C     . PRO B 1 198 ? 0.487   -30.243 27.957  1.00 19.29 ? 198  PRO B C     1 
ATOM   5605 O  O     . PRO B 1 198 ? 0.915   -29.686 26.912  1.00 19.40 ? 198  PRO B O     1 
ATOM   5606 C  CB    . PRO B 1 198 ? -0.042  -32.616 27.309  1.00 22.93 ? 198  PRO B CB    1 
ATOM   5607 C  CG    . PRO B 1 198 ? -1.112  -33.133 26.384  1.00 25.89 ? 198  PRO B CG    1 
ATOM   5608 C  CD    . PRO B 1 198 ? -1.873  -31.911 25.896  1.00 24.49 ? 198  PRO B CD    1 
ATOM   5609 N  N     . GLY B 1 199 ? 0.891   -29.951 29.186  1.00 19.37 ? 199  GLY B N     1 
ATOM   5610 C  CA    . GLY B 1 199 ? 1.962   -29.002 29.509  1.00 19.33 ? 199  GLY B CA    1 
ATOM   5611 C  C     . GLY B 1 199 ? 1.567   -27.537 29.372  1.00 19.95 ? 199  GLY B C     1 
ATOM   5612 O  O     . GLY B 1 199 ? 2.458   -26.718 29.469  1.00 22.19 ? 199  GLY B O     1 
ATOM   5613 N  N     . ASN B 1 200 ? 0.295   -27.195 29.181  1.00 20.18 ? 200  ASN B N     1 
ATOM   5614 C  CA    . ASN B 1 200 ? -0.143  -25.771 29.125  1.00 20.89 ? 200  ASN B CA    1 
ATOM   5615 C  C     . ASN B 1 200 ? 0.160   -25.099 30.466  1.00 20.55 ? 200  ASN B C     1 
ATOM   5616 O  O     . ASN B 1 200 ? 0.096   -25.790 31.515  1.00 21.42 ? 200  ASN B O     1 
ATOM   5617 C  CB    . ASN B 1 200 ? -1.649  -25.643 28.865  1.00 20.69 ? 200  ASN B CB    1 
ATOM   5618 C  CG    . ASN B 1 200 ? -2.479  -25.992 30.081  1.00 20.03 ? 200  ASN B CG    1 
ATOM   5619 O  OD1   . ASN B 1 200 ? -2.764  -25.125 30.910  1.00 18.80 ? 200  ASN B OD1   1 
ATOM   5620 N  ND2   . ASN B 1 200 ? -2.812  -27.267 30.238  1.00 20.56 ? 200  ASN B ND2   1 
ATOM   5621 N  N     . ASN B 1 201 ? 0.348   -23.788 30.463  1.00 20.28 ? 201  ASN B N     1 
ATOM   5622 C  CA    . ASN B 1 201 ? 0.252   -22.959 31.698  1.00 20.02 ? 201  ASN B CA    1 
ATOM   5623 C  C     . ASN B 1 201 ? -0.817  -21.874 31.467  1.00 19.77 ? 201  ASN B C     1 
ATOM   5624 O  O     . ASN B 1 201 ? -0.635  -20.751 31.958  1.00 17.98 ? 201  ASN B O     1 
ATOM   5625 C  CB    . ASN B 1 201 ? 1.627   -22.391 32.077  1.00 20.56 ? 201  ASN B CB    1 
ATOM   5626 C  CG    . ASN B 1 201 ? 2.622   -23.487 32.377  1.00 21.27 ? 201  ASN B CG    1 
ATOM   5627 O  OD1   . ASN B 1 201 ? 3.402   -23.914 31.528  1.00 25.04 ? 201  ASN B OD1   1 
ATOM   5628 N  ND2   . ASN B 1 201 ? 2.594   -23.966 33.586  1.00 20.04 ? 201  ASN B ND2   1 
ATOM   5629 N  N     . THR B 1 202 ? -1.882  -22.197 30.721  1.00 17.65 ? 202  THR B N     1 
ATOM   5630 C  CA    . THR B 1 202 ? -2.817  -21.202 30.165  1.00 18.62 ? 202  THR B CA    1 
ATOM   5631 C  C     . THR B 1 202 ? -4.269  -21.562 30.483  1.00 17.13 ? 202  THR B C     1 
ATOM   5632 O  O     . THR B 1 202 ? -5.142  -20.853 30.038  1.00 16.30 ? 202  THR B O     1 
ATOM   5633 C  CB    . THR B 1 202 ? -2.587  -21.024 28.659  1.00 18.32 ? 202  THR B CB    1 
ATOM   5634 O  OG1   . THR B 1 202 ? -2.503  -22.323 28.059  1.00 17.90 ? 202  THR B OG1   1 
ATOM   5635 C  CG2   . THR B 1 202 ? -1.339  -20.202 28.381  1.00 17.89 ? 202  THR B CG2   1 
ATOM   5636 N  N     . TRP B 1 203 ? -4.498  -22.613 31.242  1.00 17.05 ? 203  TRP B N     1 
ATOM   5637 C  CA    . TRP B 1 203 ? -5.854  -23.117 31.565  1.00 17.15 ? 203  TRP B CA    1 
ATOM   5638 C  C     . TRP B 1 203 ? -6.702  -21.975 32.135  1.00 17.13 ? 203  TRP B C     1 
ATOM   5639 O  O     . TRP B 1 203 ? -7.888  -21.869 31.762  1.00 17.07 ? 203  TRP B O     1 
ATOM   5640 C  CB    . TRP B 1 203 ? -5.759  -24.270 32.562  1.00 16.85 ? 203  TRP B CB    1 
ATOM   5641 C  CG    . TRP B 1 203 ? -6.964  -25.144 32.571  1.00 17.45 ? 203  TRP B CG    1 
ATOM   5642 C  CD1   . TRP B 1 203 ? -8.019  -25.167 31.702  1.00 16.60 ? 203  TRP B CD1   1 
ATOM   5643 C  CD2   . TRP B 1 203 ? -7.204  -26.175 33.542  1.00 18.24 ? 203  TRP B CD2   1 
ATOM   5644 N  NE1   . TRP B 1 203 ? -8.893  -26.163 32.051  1.00 16.95 ? 203  TRP B NE1   1 
ATOM   5645 C  CE2   . TRP B 1 203 ? -8.422  -26.791 33.188  1.00 19.20 ? 203  TRP B CE2   1 
ATOM   5646 C  CE3   . TRP B 1 203 ? -6.506  -26.617 34.672  1.00 18.40 ? 203  TRP B CE3   1 
ATOM   5647 C  CZ2   . TRP B 1 203 ? -8.948  -27.840 33.942  1.00 18.12 ? 203  TRP B CZ2   1 
ATOM   5648 C  CZ3   . TRP B 1 203 ? -7.011  -27.676 35.394  1.00 19.26 ? 203  TRP B CZ3   1 
ATOM   5649 C  CH2   . TRP B 1 203 ? -8.237  -28.252 35.047  1.00 18.84 ? 203  TRP B CH2   1 
ATOM   5650 N  N     . GLN B 1 204 ? -6.126  -21.147 33.010  1.00 18.51 ? 204  GLN B N     1 
ATOM   5651 C  CA    . GLN B 1 204 ? -6.862  -20.033 33.678  1.00 18.55 ? 204  GLN B CA    1 
ATOM   5652 C  C     . GLN B 1 204 ? -6.561  -18.690 33.004  1.00 17.52 ? 204  GLN B C     1 
ATOM   5653 O  O     . GLN B 1 204 ? -6.894  -17.653 33.598  1.00 18.20 ? 204  GLN B O     1 
ATOM   5654 C  CB    . GLN B 1 204 ? -6.527  -19.996 35.177  1.00 19.19 ? 204  GLN B CB    1 
ATOM   5655 C  CG    . GLN B 1 204 ? -7.385  -20.967 35.979  1.00 19.44 ? 204  GLN B CG    1 
ATOM   5656 C  CD    . GLN B 1 204 ? -7.142  -22.427 35.640  1.00 18.81 ? 204  GLN B CD    1 
ATOM   5657 O  OE1   . GLN B 1 204 ? -6.120  -23.002 35.960  1.00 20.20 ? 204  GLN B OE1   1 
ATOM   5658 N  NE2   . GLN B 1 204 ? -8.097  -23.069 35.005  1.00 17.81 ? 204  GLN B NE2   1 
ATOM   5659 N  N     . LEU B 1 205 ? -5.965  -18.675 31.826  1.00 17.66 ? 205  LEU B N     1 
ATOM   5660 C  CA    . LEU B 1 205 ? -5.611  -17.395 31.140  1.00 18.21 ? 205  LEU B CA    1 
ATOM   5661 C  C     . LEU B 1 205 ? -6.480  -17.143 29.900  1.00 17.64 ? 205  LEU B C     1 
ATOM   5662 O  O     . LEU B 1 205 ? -6.530  -15.969 29.452  1.00 16.80 ? 205  LEU B O     1 
ATOM   5663 C  CB    . LEU B 1 205 ? -4.129  -17.376 30.752  1.00 19.10 ? 205  LEU B CB    1 
ATOM   5664 C  CG    . LEU B 1 205 ? -3.145  -17.632 31.888  1.00 19.68 ? 205  LEU B CG    1 
ATOM   5665 C  CD1   . LEU B 1 205 ? -1.722  -17.450 31.413  1.00 20.11 ? 205  LEU B CD1   1 
ATOM   5666 C  CD2   . LEU B 1 205 ? -3.438  -16.719 33.069  1.00 21.24 ? 205  LEU B CD2   1 
ATOM   5667 N  N     . PHE B 1 206 ? -7.107  -18.163 29.329  1.00 17.01 ? 206  PHE B N     1 
ATOM   5668 C  CA    . PHE B 1 206 ? -7.787  -18.023 28.011  1.00 17.47 ? 206  PHE B CA    1 
ATOM   5669 C  C     . PHE B 1 206 ? -8.991  -18.959 28.012  1.00 17.08 ? 206  PHE B C     1 
ATOM   5670 O  O     . PHE B 1 206 ? -8.818  -20.179 28.204  1.00 17.65 ? 206  PHE B O     1 
ATOM   5671 C  CB    . PHE B 1 206 ? -6.779  -18.281 26.882  1.00 16.47 ? 206  PHE B CB    1 
ATOM   5672 C  CG    . PHE B 1 206 ? -7.331  -18.096 25.487  1.00 17.38 ? 206  PHE B CG    1 
ATOM   5673 C  CD1   . PHE B 1 206 ? -7.546  -16.826 24.976  1.00 17.64 ? 206  PHE B CD1   1 
ATOM   5674 C  CD2   . PHE B 1 206 ? -7.628  -19.187 24.679  1.00 17.02 ? 206  PHE B CD2   1 
ATOM   5675 C  CE1   . PHE B 1 206 ? -8.038  -16.648 23.689  1.00 18.23 ? 206  PHE B CE1   1 
ATOM   5676 C  CE2   . PHE B 1 206 ? -8.101  -19.008 23.386  1.00 17.65 ? 206  PHE B CE2   1 
ATOM   5677 C  CZ    . PHE B 1 206 ? -8.321  -17.739 22.894  1.00 18.37 ? 206  PHE B CZ    1 
ATOM   5678 N  N     . LYS B 1 207 ? -10.191 -18.428 27.865  1.00 17.13 ? 207  LYS B N     1 
ATOM   5679 C  CA    . LYS B 1 207 ? -11.400 -19.266 28.092  1.00 18.47 ? 207  LYS B CA    1 
ATOM   5680 C  C     . LYS B 1 207 ? -11.582 -20.304 26.986  1.00 18.93 ? 207  LYS B C     1 
ATOM   5681 O  O     . LYS B 1 207 ? -11.941 -21.451 27.323  1.00 18.31 ? 207  LYS B O     1 
ATOM   5682 C  CB    . LYS B 1 207 ? -12.667 -18.420 28.178  1.00 20.77 ? 207  LYS B CB    1 
ATOM   5683 C  CG    . LYS B 1 207 ? -12.837 -17.601 29.457  1.00 20.75 ? 207  LYS B CG    1 
ATOM   5684 C  CD    . LYS B 1 207 ? -13.911 -16.554 29.217  1.00 22.76 ? 207  LYS B CD    1 
ATOM   5685 C  CE    . LYS B 1 207 ? -14.666 -16.097 30.432  1.00 22.94 ? 207  LYS B CE    1 
ATOM   5686 N  NZ    . LYS B 1 207 ? -15.668 -17.083 30.873  1.00 25.20 ? 207  LYS B NZ    1 
ATOM   5687 N  N     . TYR B 1 208 ? -11.411 -19.921 25.714  1.00 17.51 ? 208  TYR B N     1 
ATOM   5688 C  CA    . TYR B 1 208 ? -11.971 -20.707 24.578  1.00 19.91 ? 208  TYR B CA    1 
ATOM   5689 C  C     . TYR B 1 208 ? -11.214 -22.034 24.384  1.00 19.50 ? 208  TYR B C     1 
ATOM   5690 O  O     . TYR B 1 208 ? -11.864 -23.044 24.078  1.00 19.90 ? 208  TYR B O     1 
ATOM   5691 C  CB    . TYR B 1 208 ? -11.975 -19.921 23.257  1.00 19.00 ? 208  TYR B CB    1 
ATOM   5692 C  CG    . TYR B 1 208 ? -12.807 -18.664 23.245  1.00 19.47 ? 208  TYR B CG    1 
ATOM   5693 C  CD1   . TYR B 1 208 ? -14.074 -18.624 23.796  1.00 20.79 ? 208  TYR B CD1   1 
ATOM   5694 C  CD2   . TYR B 1 208 ? -12.298 -17.484 22.717  1.00 21.40 ? 208  TYR B CD2   1 
ATOM   5695 C  CE1   . TYR B 1 208 ? -14.815 -17.450 23.793  1.00 22.69 ? 208  TYR B CE1   1 
ATOM   5696 C  CE2   . TYR B 1 208 ? -13.024 -16.300 22.714  1.00 21.54 ? 208  TYR B CE2   1 
ATOM   5697 C  CZ    . TYR B 1 208 ? -14.302 -16.292 23.225  1.00 21.52 ? 208  TYR B CZ    1 
ATOM   5698 O  OH    . TYR B 1 208 ? -15.007 -15.123 23.243  1.00 20.30 ? 208  TYR B OH    1 
ATOM   5699 N  N     . GLY B 1 209 ? -9.890  -22.030 24.510  1.00 17.11 ? 209  GLY B N     1 
ATOM   5700 C  CA    . GLY B 1 209 ? -9.077  -23.038 23.810  1.00 17.70 ? 209  GLY B CA    1 
ATOM   5701 C  C     . GLY B 1 209 ? -9.413  -23.024 22.336  1.00 17.49 ? 209  GLY B C     1 
ATOM   5702 O  O     . GLY B 1 209 ? -9.406  -21.926 21.742  1.00 18.66 ? 209  GLY B O     1 
ATOM   5703 N  N     . TYR B 1 210 ? -9.696  -24.191 21.765  1.00 15.79 ? 210  TYR B N     1 
ATOM   5704 C  CA    . TYR B 1 210 ? -9.894  -24.396 20.321  1.00 16.30 ? 210  TYR B CA    1 
ATOM   5705 C  C     . TYR B 1 210 ? -11.193 -25.163 20.138  1.00 15.13 ? 210  TYR B C     1 
ATOM   5706 O  O     . TYR B 1 210 ? -11.501 -26.080 20.931  1.00 16.28 ? 210  TYR B O     1 
ATOM   5707 C  CB    . TYR B 1 210 ? -8.687  -25.123 19.707  1.00 16.64 ? 210  TYR B CB    1 
ATOM   5708 C  CG    . TYR B 1 210 ? -8.834  -25.549 18.269  1.00 16.76 ? 210  TYR B CG    1 
ATOM   5709 C  CD1   . TYR B 1 210 ? -8.964  -24.635 17.237  1.00 17.93 ? 210  TYR B CD1   1 
ATOM   5710 C  CD2   . TYR B 1 210 ? -8.806  -26.884 17.929  1.00 18.79 ? 210  TYR B CD2   1 
ATOM   5711 C  CE1   . TYR B 1 210 ? -9.074  -25.034 15.911  1.00 19.38 ? 210  TYR B CE1   1 
ATOM   5712 C  CE2   . TYR B 1 210 ? -8.872  -27.303 16.613  1.00 19.16 ? 210  TYR B CE2   1 
ATOM   5713 C  CZ    . TYR B 1 210 ? -8.995  -26.375 15.598  1.00 19.35 ? 210  TYR B CZ    1 
ATOM   5714 O  OH    . TYR B 1 210 ? -9.098  -26.825 14.325  1.00 20.04 ? 210  TYR B OH    1 
ATOM   5715 N  N     . GLY B 1 211 ? -11.904 -24.836 19.069  1.00 15.66 ? 211  GLY B N     1 
ATOM   5716 C  CA    . GLY B 1 211 ? -13.133 -25.527 18.665  1.00 15.18 ? 211  GLY B CA    1 
ATOM   5717 C  C     . GLY B 1 211 ? -14.300 -24.993 19.496  1.00 17.02 ? 211  GLY B C     1 
ATOM   5718 O  O     . GLY B 1 211 ? -14.237 -23.848 20.001  1.00 16.20 ? 211  GLY B O     1 
ATOM   5719 N  N     . PRO B 1 212 ? -15.406 -25.762 19.607  1.00 15.55 ? 212  PRO B N     1 
ATOM   5720 C  CA    . PRO B 1 212 ? -16.599 -25.290 20.299  1.00 17.06 ? 212  PRO B CA    1 
ATOM   5721 C  C     . PRO B 1 212 ? -16.343 -24.946 21.777  1.00 17.52 ? 212  PRO B C     1 
ATOM   5722 O  O     . PRO B 1 212 ? -15.578 -25.618 22.478  1.00 16.99 ? 212  PRO B O     1 
ATOM   5723 C  CB    . PRO B 1 212 ? -17.606 -26.444 20.161  1.00 16.93 ? 212  PRO B CB    1 
ATOM   5724 C  CG    . PRO B 1 212 ? -17.066 -27.258 18.986  1.00 17.42 ? 212  PRO B CG    1 
ATOM   5725 C  CD    . PRO B 1 212 ? -15.570 -27.121 19.087  1.00 16.84 ? 212  PRO B CD    1 
ATOM   5726 N  N     . TYR B 1 213 ? -17.040 -23.911 22.235  1.00 17.99 ? 213  TYR B N     1 
ATOM   5727 C  CA    . TYR B 1 213 ? -16.930 -23.385 23.605  1.00 19.10 ? 213  TYR B CA    1 
ATOM   5728 C  C     . TYR B 1 213 ? -18.043 -24.015 24.448  1.00 18.52 ? 213  TYR B C     1 
ATOM   5729 O  O     . TYR B 1 213 ? -19.231 -23.670 24.273  1.00 17.95 ? 213  TYR B O     1 
ATOM   5730 C  CB    . TYR B 1 213 ? -16.943 -21.859 23.535  1.00 21.24 ? 213  TYR B CB    1 
ATOM   5731 C  CG    . TYR B 1 213 ? -16.788 -21.234 24.884  1.00 22.77 ? 213  TYR B CG    1 
ATOM   5732 C  CD1   . TYR B 1 213 ? -15.850 -21.705 25.784  1.00 23.18 ? 213  TYR B CD1   1 
ATOM   5733 C  CD2   . TYR B 1 213 ? -17.560 -20.155 25.249  1.00 29.88 ? 213  TYR B CD2   1 
ATOM   5734 C  CE1   . TYR B 1 213 ? -15.704 -21.142 27.037  1.00 25.38 ? 213  TYR B CE1   1 
ATOM   5735 C  CE2   . TYR B 1 213 ? -17.424 -19.567 26.495  1.00 34.60 ? 213  TYR B CE2   1 
ATOM   5736 C  CZ    . TYR B 1 213 ? -16.509 -20.079 27.403  1.00 31.60 ? 213  TYR B CZ    1 
ATOM   5737 O  OH    . TYR B 1 213 ? -16.385 -19.483 28.619  1.00 32.29 ? 213  TYR B OH    1 
ATOM   5738 N  N     . VAL B 1 214 ? -17.659 -24.940 25.325  1.00 17.68 ? 214  VAL B N     1 
ATOM   5739 C  CA    . VAL B 1 214 ? -18.565 -25.944 25.941  1.00 16.77 ? 214  VAL B CA    1 
ATOM   5740 C  C     . VAL B 1 214 ? -18.651 -25.727 27.461  1.00 17.26 ? 214  VAL B C     1 
ATOM   5741 O  O     . VAL B 1 214 ? -19.497 -26.380 28.078  1.00 18.30 ? 214  VAL B O     1 
ATOM   5742 C  CB    . VAL B 1 214 ? -18.141 -27.394 25.605  1.00 17.18 ? 214  VAL B CB    1 
ATOM   5743 C  CG1   . VAL B 1 214 ? -18.277 -27.708 24.134  1.00 17.32 ? 214  VAL B CG1   1 
ATOM   5744 C  CG2   . VAL B 1 214 ? -16.745 -27.753 26.077  1.00 18.00 ? 214  VAL B CG2   1 
ATOM   5745 N  N     . ASP B 1 215 ? -17.825 -24.876 28.076  1.00 17.41 ? 215  ASP B N     1 
ATOM   5746 C  CA    . ASP B 1 215 ? -17.848 -24.747 29.558  1.00 18.00 ? 215  ASP B CA    1 
ATOM   5747 C  C     . ASP B 1 215 ? -19.272 -24.427 30.024  1.00 18.59 ? 215  ASP B C     1 
ATOM   5748 O  O     . ASP B 1 215 ? -19.671 -24.955 31.085  1.00 18.81 ? 215  ASP B O     1 
ATOM   5749 C  CB    . ASP B 1 215 ? -16.887 -23.684 30.085  1.00 18.04 ? 215  ASP B CB    1 
ATOM   5750 C  CG    . ASP B 1 215 ? -15.421 -24.014 29.847  1.00 18.23 ? 215  ASP B CG    1 
ATOM   5751 O  OD1   . ASP B 1 215 ? -15.045 -24.110 28.657  1.00 17.35 ? 215  ASP B OD1   1 
ATOM   5752 O  OD2   . ASP B 1 215 ? -14.650 -24.080 30.859  1.00 17.47 ? 215  ASP B OD2   1 
ATOM   5753 N  N     . GLY B 1 216 ? -19.989 -23.588 29.262  1.00 18.17 ? 216  GLY B N     1 
ATOM   5754 C  CA    . GLY B 1 216 ? -21.346 -23.114 29.583  1.00 18.95 ? 216  GLY B CA    1 
ATOM   5755 C  C     . GLY B 1 216 ? -22.346 -24.233 29.749  1.00 18.47 ? 216  GLY B C     1 
ATOM   5756 O  O     . GLY B 1 216 ? -23.236 -24.071 30.582  1.00 17.50 ? 216  GLY B O     1 
ATOM   5757 N  N     . ILE B 1 217 ? -22.180 -25.357 29.051  1.00 16.79 ? 217  ILE B N     1 
ATOM   5758 C  CA    . ILE B 1 217 ? -23.183 -26.457 29.058  1.00 18.48 ? 217  ILE B CA    1 
ATOM   5759 C  C     . ILE B 1 217 ? -23.139 -27.205 30.392  1.00 19.02 ? 217  ILE B C     1 
ATOM   5760 O  O     . ILE B 1 217 ? -24.109 -27.921 30.663  1.00 18.99 ? 217  ILE B O     1 
ATOM   5761 C  CB    . ILE B 1 217 ? -23.059 -27.427 27.862  1.00 19.87 ? 217  ILE B CB    1 
ATOM   5762 C  CG1   . ILE B 1 217 ? -22.004 -28.519 28.082  1.00 20.76 ? 217  ILE B CG1   1 
ATOM   5763 C  CG2   . ILE B 1 217 ? -22.858 -26.641 26.564  1.00 20.30 ? 217  ILE B CG2   1 
ATOM   5764 C  CD1   . ILE B 1 217 ? -21.969 -29.577 26.983  1.00 21.02 ? 217  ILE B CD1   1 
ATOM   5765 N  N     . PHE B 1 218 ? -22.098 -27.008 31.205  1.00 18.95 ? 218  PHE B N     1 
ATOM   5766 C  CA    . PHE B 1 218 ? -21.969 -27.625 32.550  1.00 19.28 ? 218  PHE B CA    1 
ATOM   5767 C  C     . PHE B 1 218 ? -22.461 -26.650 33.640  1.00 19.20 ? 218  PHE B C     1 
ATOM   5768 O  O     . PHE B 1 218 ? -22.341 -26.962 34.820  1.00 21.84 ? 218  PHE B O     1 
ATOM   5769 C  CB    . PHE B 1 218 ? -20.526 -28.089 32.744  1.00 18.53 ? 218  PHE B CB    1 
ATOM   5770 C  CG    . PHE B 1 218 ? -20.107 -29.101 31.713  1.00 18.27 ? 218  PHE B CG    1 
ATOM   5771 C  CD1   . PHE B 1 218 ? -20.680 -30.370 31.699  1.00 19.14 ? 218  PHE B CD1   1 
ATOM   5772 C  CD2   . PHE B 1 218 ? -19.187 -28.776 30.728  1.00 17.74 ? 218  PHE B CD2   1 
ATOM   5773 C  CE1   . PHE B 1 218 ? -20.317 -31.309 30.741  1.00 19.48 ? 218  PHE B CE1   1 
ATOM   5774 C  CE2   . PHE B 1 218 ? -18.823 -29.713 29.771  1.00 18.14 ? 218  PHE B CE2   1 
ATOM   5775 C  CZ    . PHE B 1 218 ? -19.406 -30.967 29.768  1.00 19.16 ? 218  PHE B CZ    1 
ATOM   5776 N  N     . SER B 1 219 ? -22.941 -25.464 33.277  1.00 18.32 ? 219  SER B N     1 
ATOM   5777 C  CA    . SER B 1 219 ? -23.541 -24.503 34.244  1.00 17.45 ? 219  SER B CA    1 
ATOM   5778 C  C     . SER B 1 219 ? -25.056 -24.710 34.189  1.00 18.76 ? 219  SER B C     1 
ATOM   5779 O  O     . SER B 1 219 ? -25.574 -25.028 33.073  1.00 19.06 ? 219  SER B O     1 
ATOM   5780 C  CB    . SER B 1 219 ? -23.116 -23.066 33.981  1.00 17.21 ? 219  SER B CB    1 
ATOM   5781 O  OG    . SER B 1 219 ? -23.632 -22.571 32.743  1.00 15.99 ? 219  SER B OG    1 
ATOM   5782 N  N     . GLN B 1 220 ? -25.727 -24.621 35.341  1.00 18.36 ? 220  GLN B N     1 
ATOM   5783 C  CA    . GLN B 1 220 ? -27.189 -24.865 35.505  1.00 18.93 ? 220  GLN B CA    1 
ATOM   5784 C  C     . GLN B 1 220 ? -27.583 -26.124 34.734  1.00 18.59 ? 220  GLN B C     1 
ATOM   5785 O  O     . GLN B 1 220 ? -28.566 -26.102 33.959  1.00 17.37 ? 220  GLN B O     1 
ATOM   5786 C  CB    . GLN B 1 220 ? -28.013 -23.651 35.077  1.00 19.58 ? 220  GLN B CB    1 
ATOM   5787 C  CG    . GLN B 1 220 ? -27.987 -22.491 36.079  1.00 19.94 ? 220  GLN B CG    1 
ATOM   5788 C  CD    . GLN B 1 220 ? -29.146 -21.531 35.907  1.00 19.88 ? 220  GLN B CD    1 
ATOM   5789 O  OE1   . GLN B 1 220 ? -29.879 -21.556 34.927  1.00 20.00 ? 220  GLN B OE1   1 
ATOM   5790 N  NE2   . GLN B 1 220 ? -29.341 -20.671 36.888  1.00 20.42 ? 220  GLN B NE2   1 
ATOM   5791 N  N     . SER B 1 221 ? -26.846 -27.205 34.961  1.00 20.45 ? 221  SER B N     1 
ATOM   5792 C  CA    . SER B 1 221 ? -26.852 -28.371 34.050  1.00 20.91 ? 221  SER B CA    1 
ATOM   5793 C  C     . SER B 1 221 ? -26.827 -29.673 34.826  1.00 19.53 ? 221  SER B C     1 
ATOM   5794 O  O     . SER B 1 221 ? -26.281 -29.697 35.933  1.00 19.04 ? 221  SER B O     1 
ATOM   5795 C  CB    . SER B 1 221 ? -25.666 -28.323 33.114  1.00 21.96 ? 221  SER B CB    1 
ATOM   5796 O  OG    . SER B 1 221 ? -25.746 -29.394 32.196  1.00 24.06 ? 221  SER B OG    1 
ATOM   5797 N  N     . ASN B 1 222 ? -27.269 -30.742 34.162  1.00 19.53 ? 222  ASN B N     1 
ATOM   5798 C  CA    . ASN B 1 222 ? -27.027 -32.128 34.641  1.00 21.82 ? 222  ASN B CA    1 
ATOM   5799 C  C     . ASN B 1 222 ? -26.262 -32.881 33.539  1.00 20.51 ? 222  ASN B C     1 
ATOM   5800 O  O     . ASN B 1 222 ? -26.505 -34.069 33.352  1.00 20.06 ? 222  ASN B O     1 
ATOM   5801 C  CB    . ASN B 1 222 ? -28.346 -32.767 35.102  1.00 20.99 ? 222  ASN B CB    1 
ATOM   5802 C  CG    . ASN B 1 222 ? -29.436 -32.773 34.052  1.00 21.24 ? 222  ASN B CG    1 
ATOM   5803 O  OD1   . ASN B 1 222 ? -29.217 -32.443 32.883  1.00 23.07 ? 222  ASN B OD1   1 
ATOM   5804 N  ND2   . ASN B 1 222 ? -30.636 -33.160 34.450  1.00 22.83 ? 222  ASN B ND2   1 
ATOM   5805 N  N     . PHE B 1 223 ? -25.350 -32.212 32.832  1.00 21.22 ? 223  PHE B N     1 
ATOM   5806 C  CA    . PHE B 1 223 ? -24.534 -32.837 31.748  1.00 19.43 ? 223  PHE B CA    1 
ATOM   5807 C  C     . PHE B 1 223 ? -23.216 -33.397 32.303  1.00 19.87 ? 223  PHE B C     1 
ATOM   5808 O  O     . PHE B 1 223 ? -22.533 -34.133 31.543  1.00 18.08 ? 223  PHE B O     1 
ATOM   5809 C  CB    . PHE B 1 223 ? -24.271 -31.841 30.623  1.00 18.68 ? 223  PHE B CB    1 
ATOM   5810 C  CG    . PHE B 1 223 ? -25.495 -31.367 29.888  1.00 19.42 ? 223  PHE B CG    1 
ATOM   5811 C  CD1   . PHE B 1 223 ? -26.714 -32.001 30.019  1.00 18.94 ? 223  PHE B CD1   1 
ATOM   5812 C  CD2   . PHE B 1 223 ? -25.432 -30.255 29.063  1.00 21.50 ? 223  PHE B CD2   1 
ATOM   5813 C  CE1   . PHE B 1 223 ? -27.824 -31.553 29.326  1.00 19.23 ? 223  PHE B CE1   1 
ATOM   5814 C  CE2   . PHE B 1 223 ? -26.545 -29.820 28.358  1.00 21.46 ? 223  PHE B CE2   1 
ATOM   5815 C  CZ    . PHE B 1 223 ? -27.743 -30.462 28.503  1.00 19.48 ? 223  PHE B CZ    1 
ATOM   5816 N  N     . GLY B 1 224 ? -22.859 -33.053 33.546  1.00 18.99 ? 224  GLY B N     1 
ATOM   5817 C  CA    . GLY B 1 224 ? -21.552 -33.437 34.113  1.00 20.98 ? 224  GLY B CA    1 
ATOM   5818 C  C     . GLY B 1 224 ? -21.351 -33.035 35.561  1.00 20.20 ? 224  GLY B C     1 
ATOM   5819 O  O     . GLY B 1 224 ? -22.157 -32.260 36.113  1.00 20.01 ? 224  GLY B O     1 
ATOM   5820 N  N     . VAL B 1 225 ? -20.263 -33.533 36.145  1.00 20.89 ? 225  VAL B N     1 
ATOM   5821 C  CA    . VAL B 1 225 ? -19.828 -33.227 37.527  1.00 19.31 ? 225  VAL B CA    1 
ATOM   5822 C  C     . VAL B 1 225 ? -18.516 -32.443 37.476  1.00 20.18 ? 225  VAL B C     1 
ATOM   5823 O  O     . VAL B 1 225 ? -17.487 -32.998 37.044  1.00 22.50 ? 225  VAL B O     1 
ATOM   5824 C  CB    . VAL B 1 225 ? -19.681 -34.512 38.349  1.00 22.22 ? 225  VAL B CB    1 
ATOM   5825 C  CG1   . VAL B 1 225 ? -19.381 -34.159 39.794  1.00 23.17 ? 225  VAL B CG1   1 
ATOM   5826 C  CG2   . VAL B 1 225 ? -20.909 -35.402 38.231  1.00 21.84 ? 225  VAL B CG2   1 
ATOM   5827 N  N     . VAL B 1 226 ? -18.552 -31.174 37.871  1.00 18.03 ? 226  VAL B N     1 
ATOM   5828 C  CA    . VAL B 1 226 ? -17.347 -30.313 37.827  1.00 18.43 ? 226  VAL B CA    1 
ATOM   5829 C  C     . VAL B 1 226 ? -16.517 -30.683 39.045  1.00 17.39 ? 226  VAL B C     1 
ATOM   5830 O  O     . VAL B 1 226 ? -17.105 -30.744 40.119  1.00 17.58 ? 226  VAL B O     1 
ATOM   5831 C  CB    . VAL B 1 226 ? -17.719 -28.815 37.773  1.00 17.12 ? 226  VAL B CB    1 
ATOM   5832 C  CG1   . VAL B 1 226 ? -16.462 -27.976 37.713  1.00 16.79 ? 226  VAL B CG1   1 
ATOM   5833 C  CG2   . VAL B 1 226 ? -18.613 -28.544 36.564  1.00 17.00 ? 226  VAL B CG2   1 
ATOM   5834 N  N     . THR B 1 227 ? -15.233 -30.986 38.852  1.00 17.08 ? 227  THR B N     1 
ATOM   5835 C  CA    . THR B 1 227 ? -14.284 -31.388 39.924  1.00 16.68 ? 227  THR B CA    1 
ATOM   5836 C  C     . THR B 1 227 ? -13.159 -30.373 40.092  1.00 17.80 ? 227  THR B C     1 
ATOM   5837 O  O     . THR B 1 227 ? -12.502 -30.387 41.186  1.00 18.59 ? 227  THR B O     1 
ATOM   5838 C  CB    . THR B 1 227 ? -13.770 -32.808 39.666  1.00 17.01 ? 227  THR B CB    1 
ATOM   5839 O  OG1   . THR B 1 227 ? -13.103 -32.863 38.402  1.00 18.37 ? 227  THR B OG1   1 
ATOM   5840 C  CG2   . THR B 1 227 ? -14.909 -33.807 39.670  1.00 17.47 ? 227  THR B CG2   1 
ATOM   5841 N  N     . LYS B 1 228 ? -12.878 -29.550 39.077  1.00 18.96 ? 228  LYS B N     1 
ATOM   5842 C  CA    . LYS B 1 228 ? -11.922 -28.415 39.249  1.00 19.84 ? 228  LYS B CA    1 
ATOM   5843 C  C     . LYS B 1 228 ? -12.413 -27.256 38.390  1.00 19.39 ? 228  LYS B C     1 
ATOM   5844 O  O     . LYS B 1 228 ? -13.036 -27.501 37.348  1.00 20.00 ? 228  LYS B O     1 
ATOM   5845 C  CB    . LYS B 1 228 ? -10.478 -28.767 38.861  1.00 20.42 ? 228  LYS B CB    1 
ATOM   5846 C  CG    . LYS B 1 228 ? -9.853  -30.004 39.496  1.00 19.69 ? 228  LYS B CG    1 
ATOM   5847 C  CD    . LYS B 1 228 ? -8.530  -30.386 38.864  1.00 20.17 ? 228  LYS B CD    1 
ATOM   5848 C  CE    . LYS B 1 228 ? -7.831  -31.552 39.555  1.00 21.09 ? 228  LYS B CE    1 
ATOM   5849 N  NZ    . LYS B 1 228 ? -8.722  -32.742 39.714  1.00 21.03 ? 228  LYS B NZ    1 
ATOM   5850 N  N     . MET B 1 229 ? -12.181 -26.035 38.838  1.00 19.78 ? 229  MET B N     1 
ATOM   5851 C  CA    . MET B 1 229 ? -12.709 -24.868 38.124  1.00 19.53 ? 229  MET B CA    1 
ATOM   5852 C  C     . MET B 1 229 ? -11.763 -23.702 38.360  1.00 19.22 ? 229  MET B C     1 
ATOM   5853 O  O     . MET B 1 229 ? -11.327 -23.503 39.501  1.00 20.11 ? 229  MET B O     1 
ATOM   5854 C  CB    . MET B 1 229 ? -14.132 -24.527 38.560  1.00 20.24 ? 229  MET B CB    1 
ATOM   5855 C  CG    . MET B 1 229 ? -14.747 -23.470 37.659  1.00 20.94 ? 229  MET B CG    1 
ATOM   5856 S  SD    . MET B 1 229 ? -16.246 -22.708 38.270  1.00 21.28 ? 229  MET B SD    1 
ATOM   5857 C  CE    . MET B 1 229 ? -15.550 -21.388 39.264  1.00 23.97 ? 229  MET B CE    1 
ATOM   5858 N  N     . GLY B 1 230 ? -11.390 -23.030 37.280  1.00 17.63 ? 230  GLY B N     1 
ATOM   5859 C  CA    . GLY B 1 230 ? -10.621 -21.790 37.378  1.00 18.32 ? 230  GLY B CA    1 
ATOM   5860 C  C     . GLY B 1 230 ? -11.559 -20.609 37.502  1.00 17.51 ? 230  GLY B C     1 
ATOM   5861 O  O     . GLY B 1 230 ? -12.685 -20.665 36.963  1.00 16.68 ? 230  GLY B O     1 
ATOM   5862 N  N     . ILE B 1 231 ? -11.095 -19.542 38.136  1.00 17.77 ? 231  ILE B N     1 
ATOM   5863 C  CA    . ILE B 1 231 ? -11.861 -18.277 38.213  1.00 18.19 ? 231  ILE B CA    1 
ATOM   5864 C  C     . ILE B 1 231 ? -10.874 -17.120 38.262  1.00 18.03 ? 231  ILE B C     1 
ATOM   5865 O  O     . ILE B 1 231 ? -9.827  -17.213 38.961  1.00 17.18 ? 231  ILE B O     1 
ATOM   5866 C  CB    . ILE B 1 231 ? -12.824 -18.272 39.410  1.00 20.61 ? 231  ILE B CB    1 
ATOM   5867 C  CG1   . ILE B 1 231 ? -13.793 -17.087 39.322  1.00 20.91 ? 231  ILE B CG1   1 
ATOM   5868 C  CG2   . ILE B 1 231 ? -12.036 -18.274 40.723  1.00 20.64 ? 231  ILE B CG2   1 
ATOM   5869 C  CD1   . ILE B 1 231 ? -15.083 -17.276 40.058  1.00 21.64 ? 231  ILE B CD1   1 
ATOM   5870 N  N     . TRP B 1 232 ? -11.187 -16.079 37.494  1.00 16.68 ? 232  TRP B N     1 
ATOM   5871 C  CA    . TRP B 1 232 ? -10.406 -14.824 37.451  1.00 16.79 ? 232  TRP B CA    1 
ATOM   5872 C  C     . TRP B 1 232 ? -10.659 -14.051 38.741  1.00 17.49 ? 232  TRP B C     1 
ATOM   5873 O  O     . TRP B 1 232 ? -11.808 -14.111 39.240  1.00 15.38 ? 232  TRP B O     1 
ATOM   5874 C  CB    . TRP B 1 232 ? -10.792 -14.045 36.205  1.00 18.99 ? 232  TRP B CB    1 
ATOM   5875 C  CG    . TRP B 1 232 ? -10.362 -14.709 34.934  1.00 17.56 ? 232  TRP B CG    1 
ATOM   5876 C  CD1   . TRP B 1 232 ? -9.352  -15.604 34.778  1.00 18.70 ? 232  TRP B CD1   1 
ATOM   5877 C  CD2   . TRP B 1 232 ? -10.883 -14.472 33.614  1.00 18.45 ? 232  TRP B CD2   1 
ATOM   5878 N  NE1   . TRP B 1 232 ? -9.213  -15.944 33.461  1.00 17.59 ? 232  TRP B NE1   1 
ATOM   5879 C  CE2   . TRP B 1 232 ? -10.145 -15.277 32.721  1.00 17.99 ? 232  TRP B CE2   1 
ATOM   5880 C  CE3   . TRP B 1 232 ? -11.891 -13.655 33.095  1.00 19.65 ? 232  TRP B CE3   1 
ATOM   5881 C  CZ2   . TRP B 1 232 ? -10.404 -15.321 31.346  1.00 18.64 ? 232  TRP B CZ2   1 
ATOM   5882 C  CZ3   . TRP B 1 232 ? -12.179 -13.717 31.742  1.00 19.16 ? 232  TRP B CZ3   1 
ATOM   5883 C  CH2   . TRP B 1 232 ? -11.407 -14.500 30.872  1.00 20.04 ? 232  TRP B CH2   1 
ATOM   5884 N  N     . LEU B 1 233 ? -9.595  -13.464 39.295  1.00 19.50 ? 233  LEU B N     1 
ATOM   5885 C  CA    . LEU B 1 233 ? -9.615  -12.688 40.565  1.00 20.24 ? 233  LEU B CA    1 
ATOM   5886 C  C     . LEU B 1 233 ? -9.149  -11.271 40.260  1.00 19.97 ? 233  LEU B C     1 
ATOM   5887 O  O     . LEU B 1 233 ? -8.146  -11.119 39.554  1.00 20.99 ? 233  LEU B O     1 
ATOM   5888 C  CB    . LEU B 1 233 ? -8.681  -13.324 41.604  1.00 20.67 ? 233  LEU B CB    1 
ATOM   5889 C  CG    . LEU B 1 233 ? -9.078  -14.710 42.129  1.00 21.44 ? 233  LEU B CG    1 
ATOM   5890 C  CD1   . LEU B 1 233 ? -8.089  -15.172 43.181  1.00 21.08 ? 233  LEU B CD1   1 
ATOM   5891 C  CD2   . LEU B 1 233 ? -10.499 -14.720 42.690  1.00 20.80 ? 233  LEU B CD2   1 
ATOM   5892 N  N     . MET B 1 234 ? -9.839  -10.286 40.801  1.00 19.72 ? 234  MET B N     1 
ATOM   5893 C  CA    . MET B 1 234 ? -9.514  -8.861  40.586  1.00 20.97 ? 234  MET B CA    1 
ATOM   5894 C  C     . MET B 1 234 ? -8.240  -8.489  41.355  1.00 21.19 ? 234  MET B C     1 
ATOM   5895 O  O     . MET B 1 234 ? -8.117  -8.721  42.548  1.00 18.34 ? 234  MET B O     1 
ATOM   5896 C  CB    . MET B 1 234 ? -10.670 -7.982  41.060  1.00 21.57 ? 234  MET B CB    1 
ATOM   5897 C  CG    . MET B 1 234 ? -10.496 -6.536  40.636  1.00 22.86 ? 234  MET B CG    1 
ATOM   5898 S  SD    . MET B 1 234 ? -11.959 -5.534  40.995  1.00 25.87 ? 234  MET B SD    1 
ATOM   5899 C  CE    . MET B 1 234 ? -12.013 -5.742  42.766  1.00 30.63 ? 234  MET B CE    1 
ATOM   5900 N  N     . PRO B 1 235 ? -7.221  -7.906  40.707  1.00 19.41 ? 235  PRO B N     1 
ATOM   5901 C  CA    . PRO B 1 235 ? -6.124  -7.280  41.440  1.00 21.98 ? 235  PRO B CA    1 
ATOM   5902 C  C     . PRO B 1 235 ? -6.653  -6.225  42.423  1.00 22.74 ? 235  PRO B C     1 
ATOM   5903 O  O     . PRO B 1 235 ? -7.560  -5.483  42.074  1.00 20.60 ? 235  PRO B O     1 
ATOM   5904 C  CB    . PRO B 1 235 ? -5.267  -6.630  40.347  1.00 20.73 ? 235  PRO B CB    1 
ATOM   5905 C  CG    . PRO B 1 235 ? -5.602  -7.442  39.124  1.00 20.47 ? 235  PRO B CG    1 
ATOM   5906 C  CD    . PRO B 1 235 ? -7.062  -7.804  39.267  1.00 20.84 ? 235  PRO B CD    1 
ATOM   5907 N  N     . GLU B 1 236 ? -6.126  -6.220  43.637  1.00 21.53 ? 236  GLU B N     1 
ATOM   5908 C  CA    . GLU B 1 236 ? -6.417  -5.143  44.606  1.00 24.77 ? 236  GLU B CA    1 
ATOM   5909 C  C     . GLU B 1 236 ? -6.282  -3.814  43.876  1.00 22.31 ? 236  GLU B C     1 
ATOM   5910 O  O     . GLU B 1 236 ? -5.237  -3.514  43.329  1.00 22.10 ? 236  GLU B O     1 
ATOM   5911 C  CB    . GLU B 1 236 ? -5.437  -5.192  45.780  1.00 27.51 ? 236  GLU B CB    1 
ATOM   5912 C  CG    . GLU B 1 236 ? -5.772  -4.202  46.860  1.00 33.74 ? 236  GLU B CG    1 
ATOM   5913 C  CD    . GLU B 1 236 ? -4.804  -4.184  48.032  1.00 39.14 ? 236  GLU B CD    1 
ATOM   5914 O  OE1   . GLU B 1 236 ? -3.680  -4.709  47.886  1.00 41.81 ? 236  GLU B OE1   1 
ATOM   5915 O  OE2   . GLU B 1 236 ? -5.181  -3.619  49.078  1.00 43.91 ? 236  GLU B OE2   1 
ATOM   5916 N  N     . PRO B 1 237 ? -7.347  -3.002  43.804  1.00 23.54 ? 237  PRO B N     1 
ATOM   5917 C  CA    . PRO B 1 237 ? -7.282  -1.698  43.139  1.00 25.08 ? 237  PRO B CA    1 
ATOM   5918 C  C     . PRO B 1 237 ? -6.557  -0.601  43.938  1.00 26.38 ? 237  PRO B C     1 
ATOM   5919 O  O     . PRO B 1 237 ? -6.312  -0.751  45.128  1.00 26.88 ? 237  PRO B O     1 
ATOM   5920 C  CB    . PRO B 1 237 ? -8.765  -1.348  43.011  1.00 27.92 ? 237  PRO B CB    1 
ATOM   5921 C  CG    . PRO B 1 237 ? -9.386  -1.992  44.233  1.00 26.67 ? 237  PRO B CG    1 
ATOM   5922 C  CD    . PRO B 1 237 ? -8.672  -3.321  44.346  1.00 24.77 ? 237  PRO B CD    1 
ATOM   5923 N  N     . ALA B 1 238 ? -6.252  0.499   43.269  1.00 28.47 ? 238  ALA B N     1 
ATOM   5924 C  CA    . ALA B 1 238 ? -5.535  1.658   43.841  1.00 31.25 ? 238  ALA B CA    1 
ATOM   5925 C  C     . ALA B 1 238 ? -6.432  2.415   44.844  1.00 33.19 ? 238  ALA B C     1 
ATOM   5926 O  O     . ALA B 1 238 ? -5.901  3.223   45.629  1.00 34.59 ? 238  ALA B O     1 
ATOM   5927 C  CB    . ALA B 1 238 ? -5.093  2.546   42.702  1.00 31.11 ? 238  ALA B CB    1 
ATOM   5928 N  N     . GLY B 1 239 ? -7.746  2.193   44.816  1.00 30.09 ? 239  GLY B N     1 
ATOM   5929 C  CA    . GLY B 1 239 ? -8.686  2.842   45.748  1.00 30.49 ? 239  GLY B CA    1 
ATOM   5930 C  C     . GLY B 1 239 ? -10.068 2.220   45.677  1.00 29.45 ? 239  GLY B C     1 
ATOM   5931 O  O     . GLY B 1 239 ? -10.365 1.485   44.706  1.00 26.46 ? 239  GLY B O     1 
ATOM   5932 N  N     . TYR B 1 240 ? -10.853 2.464   46.720  1.00 27.25 ? 240  TYR B N     1 
ATOM   5933 C  CA    . TYR B 1 240 ? -12.184 1.864   46.961  1.00 27.34 ? 240  TYR B CA    1 
ATOM   5934 C  C     . TYR B 1 240 ? -13.051 2.875   47.727  1.00 26.30 ? 240  TYR B C     1 
ATOM   5935 O  O     . TYR B 1 240 ? -12.659 3.235   48.836  1.00 25.04 ? 240  TYR B O     1 
ATOM   5936 C  CB    . TYR B 1 240 ? -12.023 0.560   47.750  1.00 24.14 ? 240  TYR B CB    1 
ATOM   5937 C  CG    . TYR B 1 240 ? -13.336 -0.052  48.156  1.00 23.55 ? 240  TYR B CG    1 
ATOM   5938 C  CD1   . TYR B 1 240 ? -14.251 -0.425  47.182  1.00 24.59 ? 240  TYR B CD1   1 
ATOM   5939 C  CD2   . TYR B 1 240 ? -13.683 -0.251  49.494  1.00 22.34 ? 240  TYR B CD2   1 
ATOM   5940 C  CE1   . TYR B 1 240 ? -15.472 -0.993  47.518  1.00 23.87 ? 240  TYR B CE1   1 
ATOM   5941 C  CE2   . TYR B 1 240 ? -14.901 -0.832  49.848  1.00 22.70 ? 240  TYR B CE2   1 
ATOM   5942 C  CZ    . TYR B 1 240 ? -15.798 -1.210  48.850  1.00 23.59 ? 240  TYR B CZ    1 
ATOM   5943 O  OH    . TYR B 1 240 ? -17.015 -1.769  49.125  1.00 20.10 ? 240  TYR B OH    1 
ATOM   5944 N  N     . ARG B 1 241 ? -14.216 3.244   47.195  1.00 26.72 ? 241  ARG B N     1 
ATOM   5945 C  CA    . ARG B 1 241 ? -15.153 4.213   47.836  1.00 26.20 ? 241  ARG B CA    1 
ATOM   5946 C  C     . ARG B 1 241 ? -16.591 3.734   47.707  1.00 24.00 ? 241  ARG B C     1 
ATOM   5947 O  O     . ARG B 1 241 ? -17.245 4.029   46.708  1.00 23.56 ? 241  ARG B O     1 
ATOM   5948 C  CB    . ARG B 1 241 ? -14.999 5.594   47.190  1.00 29.44 ? 241  ARG B CB    1 
ATOM   5949 C  CG    . ARG B 1 241 ? -13.740 6.343   47.609  1.00 33.96 ? 241  ARG B CG    1 
ATOM   5950 C  CD    . ARG B 1 241 ? -13.749 6.690   49.087  1.00 41.05 ? 241  ARG B CD    1 
ATOM   5951 N  NE    . ARG B 1 241 ? -14.554 7.879   49.387  1.00 50.78 ? 241  ARG B NE    1 
ATOM   5952 C  CZ    . ARG B 1 241 ? -15.079 8.174   50.580  1.00 49.54 ? 241  ARG B CZ    1 
ATOM   5953 N  NH1   . ARG B 1 241 ? -14.919 7.351   51.604  1.00 51.64 ? 241  ARG B NH1   1 
ATOM   5954 N  NH2   . ARG B 1 241 ? -15.788 9.281   50.733  1.00 46.98 ? 241  ARG B NH2   1 
ATOM   5955 N  N     . PRO B 1 242 ? -17.135 3.036   48.725  1.00 22.49 ? 242  PRO B N     1 
ATOM   5956 C  CA    . PRO B 1 242 ? -18.505 2.550   48.703  1.00 23.26 ? 242  PRO B CA    1 
ATOM   5957 C  C     . PRO B 1 242 ? -19.429 3.720   49.063  1.00 25.86 ? 242  PRO B C     1 
ATOM   5958 O  O     . PRO B 1 242 ? -18.985 4.615   49.760  1.00 23.99 ? 242  PRO B O     1 
ATOM   5959 C  CB    . PRO B 1 242 ? -18.494 1.475   49.777  1.00 24.42 ? 242  PRO B CB    1 
ATOM   5960 C  CG    . PRO B 1 242 ? -17.541 2.018   50.803  1.00 24.10 ? 242  PRO B CG    1 
ATOM   5961 C  CD    . PRO B 1 242 ? -16.480 2.745   50.003  1.00 25.17 ? 242  PRO B CD    1 
ATOM   5962 N  N     . TYR B 1 243 ? -20.655 3.720   48.542  1.00 24.50 ? 243  TYR B N     1 
ATOM   5963 C  CA    . TYR B 1 243 ? -21.594 4.849   48.710  1.00 25.50 ? 243  TYR B CA    1 
ATOM   5964 C  C     . TYR B 1 243 ? -23.011 4.295   48.829  1.00 26.01 ? 243  TYR B C     1 
ATOM   5965 O  O     . TYR B 1 243 ? -23.267 3.173   48.354  1.00 25.40 ? 243  TYR B O     1 
ATOM   5966 C  CB    . TYR B 1 243 ? -21.404 5.864   47.573  1.00 26.24 ? 243  TYR B CB    1 
ATOM   5967 C  CG    . TYR B 1 243 ? -21.717 5.364   46.183  1.00 24.75 ? 243  TYR B CG    1 
ATOM   5968 C  CD1   . TYR B 1 243 ? -23.027 5.199   45.768  1.00 24.41 ? 243  TYR B CD1   1 
ATOM   5969 C  CD2   . TYR B 1 243 ? -20.708 5.045   45.285  1.00 24.55 ? 243  TYR B CD2   1 
ATOM   5970 C  CE1   . TYR B 1 243 ? -23.338 4.732   44.501  1.00 25.61 ? 243  TYR B CE1   1 
ATOM   5971 C  CE2   . TYR B 1 243 ? -20.999 4.560   44.011  1.00 25.40 ? 243  TYR B CE2   1 
ATOM   5972 C  CZ    . TYR B 1 243 ? -22.316 4.407   43.614  1.00 27.44 ? 243  TYR B CZ    1 
ATOM   5973 O  OH    . TYR B 1 243 ? -22.631 3.913   42.377  1.00 30.25 ? 243  TYR B OH    1 
ATOM   5974 N  N     . LEU B 1 244 ? -23.902 5.100   49.423  1.00 24.89 ? 244  LEU B N     1 
ATOM   5975 C  CA    . LEU B 1 244 ? -25.352 4.816   49.573  1.00 23.49 ? 244  LEU B CA    1 
ATOM   5976 C  C     . LEU B 1 244 ? -26.121 6.049   49.123  1.00 24.11 ? 244  LEU B C     1 
ATOM   5977 O  O     . LEU B 1 244 ? -25.809 7.136   49.635  1.00 25.32 ? 244  LEU B O     1 
ATOM   5978 C  CB    . LEU B 1 244 ? -25.685 4.518   51.029  1.00 25.71 ? 244  LEU B CB    1 
ATOM   5979 C  CG    . LEU B 1 244 ? -27.182 4.477   51.343  1.00 27.45 ? 244  LEU B CG    1 
ATOM   5980 C  CD1   . LEU B 1 244 ? -27.858 3.439   50.480  1.00 26.95 ? 244  LEU B CD1   1 
ATOM   5981 C  CD2   . LEU B 1 244 ? -27.424 4.185   52.819  1.00 26.32 ? 244  LEU B CD2   1 
ATOM   5982 N  N     . ILE B 1 245 ? -27.052 5.881   48.186  1.00 23.07 ? 245  ILE B N     1 
ATOM   5983 C  CA    . ILE B 1 245 ? -27.958 6.959   47.717  1.00 22.16 ? 245  ILE B CA    1 
ATOM   5984 C  C     . ILE B 1 245 ? -29.367 6.519   48.051  1.00 22.32 ? 245  ILE B C     1 
ATOM   5985 O  O     . ILE B 1 245 ? -29.779 5.418   47.556  1.00 22.88 ? 245  ILE B O     1 
ATOM   5986 C  CB    . ILE B 1 245 ? -27.775 7.235   46.221  1.00 25.29 ? 245  ILE B CB    1 
ATOM   5987 C  CG1   . ILE B 1 245 ? -26.297 7.443   45.856  1.00 25.88 ? 245  ILE B CG1   1 
ATOM   5988 C  CG2   . ILE B 1 245 ? -28.639 8.416   45.799  1.00 26.32 ? 245  ILE B CG2   1 
ATOM   5989 C  CD1   . ILE B 1 245 ? -26.073 7.660   44.371  1.00 25.03 ? 245  ILE B CD1   1 
ATOM   5990 N  N     . THR B 1 246 ? -30.052 7.299   48.894  1.00 20.98 ? 246  THR B N     1 
ATOM   5991 C  CA    . THR B 1 246 ? -31.437 7.003   49.346  1.00 21.04 ? 246  THR B CA    1 
ATOM   5992 C  C     . THR B 1 246 ? -32.416 7.917   48.607  1.00 22.56 ? 246  THR B C     1 
ATOM   5993 O  O     . THR B 1 246 ? -32.066 9.090   48.318  1.00 26.26 ? 246  THR B O     1 
ATOM   5994 C  CB    . THR B 1 246 ? -31.585 7.069   50.873  1.00 19.51 ? 246  THR B CB    1 
ATOM   5995 O  OG1   . THR B 1 246 ? -31.531 8.433   51.293  1.00 20.14 ? 246  THR B OG1   1 
ATOM   5996 C  CG2   . THR B 1 246 ? -30.500 6.287   51.591  1.00 19.19 ? 246  THR B CG2   1 
ATOM   5997 N  N     . PHE B 1 247 ? -33.578 7.345   48.309  1.00 23.44 ? 247  PHE B N     1 
ATOM   5998 C  CA    . PHE B 1 247 ? -34.759 7.966   47.670  1.00 27.80 ? 247  PHE B CA    1 
ATOM   5999 C  C     . PHE B 1 247 ? -35.934 7.884   48.654  1.00 26.97 ? 247  PHE B C     1 
ATOM   6000 O  O     . PHE B 1 247 ? -36.181 6.808   49.202  1.00 23.62 ? 247  PHE B O     1 
ATOM   6001 C  CB    . PHE B 1 247 ? -35.014 7.287   46.323  1.00 27.35 ? 247  PHE B CB    1 
ATOM   6002 C  CG    . PHE B 1 247 ? -33.767 7.284   45.483  1.00 30.41 ? 247  PHE B CG    1 
ATOM   6003 C  CD1   . PHE B 1 247 ? -33.329 8.448   44.870  1.00 31.71 ? 247  PHE B CD1   1 
ATOM   6004 C  CD2   . PHE B 1 247 ? -32.989 6.141   45.371  1.00 32.02 ? 247  PHE B CD2   1 
ATOM   6005 C  CE1   . PHE B 1 247 ? -32.157 8.457   44.129  1.00 33.93 ? 247  PHE B CE1   1 
ATOM   6006 C  CE2   . PHE B 1 247 ? -31.818 6.150   44.631  1.00 33.16 ? 247  PHE B CE2   1 
ATOM   6007 C  CZ    . PHE B 1 247 ? -31.396 7.313   44.022  1.00 35.63 ? 247  PHE B CZ    1 
ATOM   6008 N  N     . GLU B 1 248 ? -36.618 9.006   48.868  1.00 28.62 ? 248  GLU B N     1 
ATOM   6009 C  CA    . GLU B 1 248 ? -37.736 9.131   49.838  1.00 31.58 ? 248  GLU B CA    1 
ATOM   6010 C  C     . GLU B 1 248 ? -39.003 8.449   49.328  1.00 28.16 ? 248  GLU B C     1 
ATOM   6011 O  O     . GLU B 1 248 ? -39.761 7.961   50.168  1.00 27.97 ? 248  GLU B O     1 
ATOM   6012 C  CB    . GLU B 1 248 ? -38.067 10.598  50.109  1.00 37.73 ? 248  GLU B CB    1 
ATOM   6013 C  CG    . GLU B 1 248 ? -37.461 11.118  51.389  1.00 48.78 ? 248  GLU B CG    1 
ATOM   6014 C  CD    . GLU B 1 248 ? -37.972 12.499  51.752  1.00 54.67 ? 248  GLU B CD    1 
ATOM   6015 O  OE1   . GLU B 1 248 ? -37.181 13.304  52.307  1.00 70.09 ? 248  GLU B OE1   1 
ATOM   6016 O  OE2   . GLU B 1 248 ? -39.149 12.774  51.460  1.00 56.90 ? 248  GLU B OE2   1 
ATOM   6017 N  N     . ASN B 1 249 ? -39.263 8.468   48.025  1.00 25.75 ? 249  ASN B N     1 
ATOM   6018 C  CA    . ASN B 1 249 ? -40.590 8.090   47.477  1.00 27.94 ? 249  ASN B CA    1 
ATOM   6019 C  C     . ASN B 1 249 ? -40.478 6.768   46.723  1.00 28.71 ? 249  ASN B C     1 
ATOM   6020 O  O     . ASN B 1 249 ? -39.529 6.603   45.937  1.00 28.35 ? 249  ASN B O     1 
ATOM   6021 C  CB    . ASN B 1 249 ? -41.169 9.218   46.623  1.00 27.89 ? 249  ASN B CB    1 
ATOM   6022 C  CG    . ASN B 1 249 ? -41.262 10.486  47.443  1.00 32.72 ? 249  ASN B CG    1 
ATOM   6023 O  OD1   . ASN B 1 249 ? -42.056 10.556  48.364  1.00 29.14 ? 249  ASN B OD1   1 
ATOM   6024 N  ND2   . ASN B 1 249 ? -40.388 11.445  47.196  1.00 36.78 ? 249  ASN B ND2   1 
ATOM   6025 N  N     . GLU B 1 250 ? -41.444 5.883   46.932  1.00 28.67 ? 250  GLU B N     1 
ATOM   6026 C  CA    . GLU B 1 250 ? -41.486 4.574   46.250  1.00 33.80 ? 250  GLU B CA    1 
ATOM   6027 C  C     . GLU B 1 250 ? -41.570 4.790   44.741  1.00 35.09 ? 250  GLU B C     1 
ATOM   6028 O  O     . GLU B 1 250 ? -40.957 4.002   44.020  1.00 34.49 ? 250  GLU B O     1 
ATOM   6029 C  CB    . GLU B 1 250 ? -42.631 3.729   46.785  1.00 38.63 ? 250  GLU B CB    1 
ATOM   6030 C  CG    . GLU B 1 250 ? -43.990 4.369   46.671  1.00 46.85 ? 250  GLU B CG    1 
ATOM   6031 C  CD    . GLU B 1 250 ? -45.038 3.519   47.368  1.00 53.62 ? 250  GLU B CD    1 
ATOM   6032 O  OE1   . GLU B 1 250 ? -44.641 2.584   48.083  1.00 54.64 ? 250  GLU B OE1   1 
ATOM   6033 O  OE2   . GLU B 1 250 ? -46.240 3.780   47.180  1.00 65.80 ? 250  GLU B OE2   1 
ATOM   6034 N  N     . ASP B 1 251 ? -42.237 5.856   44.292  1.00 32.35 ? 251  ASP B N     1 
ATOM   6035 C  CA    . ASP B 1 251 ? -42.377 6.196   42.851  1.00 34.65 ? 251  ASP B CA    1 
ATOM   6036 C  C     . ASP B 1 251 ? -41.054 6.686   42.250  1.00 31.34 ? 251  ASP B C     1 
ATOM   6037 O  O     . ASP B 1 251 ? -40.996 6.722   41.009  1.00 33.18 ? 251  ASP B O     1 
ATOM   6038 C  CB    . ASP B 1 251 ? -43.496 7.217   42.611  1.00 37.85 ? 251  ASP B CB    1 
ATOM   6039 C  CG    . ASP B 1 251 ? -44.869 6.568   42.639  1.00 40.24 ? 251  ASP B CG    1 
ATOM   6040 O  OD1   . ASP B 1 251 ? -44.919 5.328   42.780  1.00 41.36 ? 251  ASP B OD1   1 
ATOM   6041 O  OD2   . ASP B 1 251 ? -45.878 7.304   42.493  1.00 53.02 ? 251  ASP B OD2   1 
ATOM   6042 N  N     . ASP B 1 252 ? -40.045 7.040   43.060  1.00 27.95 ? 252  ASP B N     1 
ATOM   6043 C  CA    . ASP B 1 252 ? -38.715 7.477   42.561  1.00 28.26 ? 252  ASP B CA    1 
ATOM   6044 C  C     . ASP B 1 252 ? -38.031 6.375   41.719  1.00 27.74 ? 252  ASP B C     1 
ATOM   6045 O  O     . ASP B 1 252 ? -37.159 6.711   40.897  1.00 27.59 ? 252  ASP B O     1 
ATOM   6046 C  CB    . ASP B 1 252 ? -37.801 7.902   43.711  1.00 30.34 ? 252  ASP B CB    1 
ATOM   6047 C  CG    . ASP B 1 252 ? -38.200 9.221   44.376  1.00 30.07 ? 252  ASP B CG    1 
ATOM   6048 O  OD1   . ASP B 1 252 ? -38.891 10.023  43.712  1.00 26.88 ? 252  ASP B OD1   1 
ATOM   6049 O  OD2   . ASP B 1 252 ? -37.775 9.449   45.536  1.00 28.39 ? 252  ASP B OD2   1 
ATOM   6050 N  N     . ILE B 1 253 ? -38.327 5.104   41.954  1.00 27.76 ? 253  ILE B N     1 
ATOM   6051 C  CA    . ILE B 1 253 ? -37.626 3.970   41.284  1.00 27.35 ? 253  ILE B CA    1 
ATOM   6052 C  C     . ILE B 1 253 ? -37.779 4.108   39.762  1.00 30.38 ? 253  ILE B C     1 
ATOM   6053 O  O     . ILE B 1 253 ? -36.887 3.686   39.037  1.00 31.98 ? 253  ILE B O     1 
ATOM   6054 C  CB    . ILE B 1 253 ? -38.180 2.635   41.807  1.00 26.91 ? 253  ILE B CB    1 
ATOM   6055 C  CG1   . ILE B 1 253 ? -37.219 1.471   41.556  1.00 25.70 ? 253  ILE B CG1   1 
ATOM   6056 C  CG2   . ILE B 1 253 ? -39.564 2.373   41.239  1.00 27.74 ? 253  ILE B CG2   1 
ATOM   6057 C  CD1   . ILE B 1 253 ? -35.770 1.808   41.822  1.00 24.62 ? 253  ILE B CD1   1 
ATOM   6058 N  N     . GLU B 1 254 ? -38.863 4.711   39.279  1.00 31.93 ? 254  GLU B N     1 
ATOM   6059 C  CA    . GLU B 1 254 ? -39.034 4.944   37.828  1.00 30.35 ? 254  GLU B CA    1 
ATOM   6060 C  C     . GLU B 1 254 ? -37.891 5.799   37.274  1.00 29.03 ? 254  GLU B C     1 
ATOM   6061 O  O     . GLU B 1 254 ? -37.216 5.342   36.335  1.00 30.52 ? 254  GLU B O     1 
ATOM   6062 C  CB    . GLU B 1 254 ? -40.363 5.613   37.510  1.00 32.90 ? 254  GLU B CB    1 
ATOM   6063 C  CG    . GLU B 1 254 ? -40.590 5.677   36.010  1.00 34.52 ? 254  GLU B CG    1 
ATOM   6064 C  CD    . GLU B 1 254 ? -41.991 6.042   35.565  1.00 36.94 ? 254  GLU B CD    1 
ATOM   6065 O  OE1   . GLU B 1 254 ? -42.884 6.202   36.435  1.00 32.10 ? 254  GLU B OE1   1 
ATOM   6066 O  OE2   . GLU B 1 254 ? -42.173 6.178   34.341  1.00 38.51 ? 254  GLU B OE2   1 
ATOM   6067 N  N     . THR B 1 255 ? -37.680 6.998   37.801  1.00 24.71 ? 255  THR B N     1 
ATOM   6068 C  CA    . THR B 1 255 ? -36.672 7.956   37.269  1.00 25.99 ? 255  THR B CA    1 
ATOM   6069 C  C     . THR B 1 255 ? -35.268 7.436   37.610  1.00 23.68 ? 255  THR B C     1 
ATOM   6070 O  O     . THR B 1 255 ? -34.332 7.664   36.828  1.00 24.01 ? 255  THR B O     1 
ATOM   6071 C  CB    . THR B 1 255 ? -36.941 9.393   37.746  1.00 25.20 ? 255  THR B CB    1 
ATOM   6072 O  OG1   . THR B 1 255 ? -36.075 10.260  37.020  1.00 25.24 ? 255  THR B OG1   1 
ATOM   6073 C  CG2   . THR B 1 255 ? -36.658 9.626   39.213  1.00 27.83 ? 255  THR B CG2   1 
ATOM   6074 N  N     . VAL B 1 256 ? -35.132 6.762   38.749  1.00 24.38 ? 256  VAL B N     1 
ATOM   6075 C  CA    . VAL B 1 256 ? -33.842 6.178   39.210  1.00 23.71 ? 256  VAL B CA    1 
ATOM   6076 C  C     . VAL B 1 256 ? -33.395 5.135   38.161  1.00 22.51 ? 256  VAL B C     1 
ATOM   6077 O  O     . VAL B 1 256 ? -32.269 5.215   37.773  1.00 20.80 ? 256  VAL B O     1 
ATOM   6078 C  CB    . VAL B 1 256 ? -33.930 5.602   40.636  1.00 23.24 ? 256  VAL B CB    1 
ATOM   6079 C  CG1   . VAL B 1 256 ? -32.711 4.755   40.961  1.00 23.27 ? 256  VAL B CG1   1 
ATOM   6080 C  CG2   . VAL B 1 256 ? -34.094 6.720   41.702  1.00 24.66 ? 256  VAL B CG2   1 
ATOM   6081 N  N     . THR B 1 257 ? -34.249 4.206   37.740  1.00 21.92 ? 257  THR B N     1 
ATOM   6082 C  CA    . THR B 1 257 ? -33.894 3.194   36.718  1.00 24.63 ? 257  THR B CA    1 
ATOM   6083 C  C     . THR B 1 257 ? -33.519 3.908   35.408  1.00 26.72 ? 257  THR B C     1 
ATOM   6084 O  O     . THR B 1 257 ? -32.538 3.486   34.769  1.00 26.20 ? 257  THR B O     1 
ATOM   6085 C  CB    . THR B 1 257 ? -35.000 2.151   36.543  1.00 24.41 ? 257  THR B CB    1 
ATOM   6086 O  OG1   . THR B 1 257 ? -35.225 1.569   37.823  1.00 23.95 ? 257  THR B OG1   1 
ATOM   6087 C  CG2   . THR B 1 257 ? -34.625 1.054   35.566  1.00 25.05 ? 257  THR B CG2   1 
ATOM   6088 N  N     . GLU B 1 258 ? -34.238 4.977   35.038  1.00 26.90 ? 258  GLU B N     1 
ATOM   6089 C  CA    . GLU B 1 258 ? -33.950 5.737   33.800  1.00 25.69 ? 258  GLU B CA    1 
ATOM   6090 C  C     . GLU B 1 258 ? -32.530 6.271   33.881  1.00 24.10 ? 258  GLU B C     1 
ATOM   6091 O  O     . GLU B 1 258 ? -31.840 6.157   32.873  1.00 24.64 ? 258  GLU B O     1 
ATOM   6092 C  CB    . GLU B 1 258 ? -34.952 6.861   33.523  1.00 24.91 ? 258  GLU B CB    1 
ATOM   6093 C  CG    . GLU B 1 258 ? -36.281 6.345   33.008  1.00 25.73 ? 258  GLU B CG    1 
ATOM   6094 C  CD    . GLU B 1 258 ? -36.172 5.658   31.652  1.00 28.91 ? 258  GLU B CD    1 
ATOM   6095 O  OE1   . GLU B 1 258 ? -35.792 6.358   30.656  1.00 26.67 ? 258  GLU B OE1   1 
ATOM   6096 O  OE2   . GLU B 1 258 ? -36.454 4.429   31.585  1.00 26.10 ? 258  GLU B OE2   1 
ATOM   6097 N  N     . ARG B 1 259 ? -32.103 6.814   35.021  1.00 24.30 ? 259  ARG B N     1 
ATOM   6098 C  CA    . ARG B 1 259 ? -30.779 7.468   35.117  1.00 23.85 ? 259  ARG B CA    1 
ATOM   6099 C  C     . ARG B 1 259 ? -29.705 6.388   35.253  1.00 23.76 ? 259  ARG B C     1 
ATOM   6100 O  O     . ARG B 1 259 ? -28.559 6.620   34.801  1.00 24.51 ? 259  ARG B O     1 
ATOM   6101 C  CB    . ARG B 1 259 ? -30.751 8.460   36.275  1.00 26.70 ? 259  ARG B CB    1 
ATOM   6102 C  CG    . ARG B 1 259 ? -31.817 9.550   36.157  1.00 29.19 ? 259  ARG B CG    1 
ATOM   6103 C  CD    . ARG B 1 259 ? -32.338 9.954   37.523  1.00 30.67 ? 259  ARG B CD    1 
ATOM   6104 N  NE    . ARG B 1 259 ? -33.470 10.874  37.451  1.00 32.27 ? 259  ARG B NE    1 
ATOM   6105 C  CZ    . ARG B 1 259 ? -33.391 12.199  37.598  1.00 31.10 ? 259  ARG B CZ    1 
ATOM   6106 N  NH1   . ARG B 1 259 ? -32.244 12.829  37.830  1.00 27.09 ? 259  ARG B NH1   1 
ATOM   6107 N  NH2   . ARG B 1 259 ? -34.501 12.893  37.528  1.00 31.81 ? 259  ARG B NH2   1 
ATOM   6108 N  N     . LEU B 1 260 ? -30.061 5.235   35.816  1.00 22.62 ? 260  LEU B N     1 
ATOM   6109 C  CA    . LEU B 1 260 ? -29.098 4.124   36.017  1.00 23.33 ? 260  LEU B CA    1 
ATOM   6110 C  C     . LEU B 1 260 ? -28.655 3.563   34.664  1.00 21.62 ? 260  LEU B C     1 
ATOM   6111 O  O     . LEU B 1 260 ? -27.492 3.245   34.578  1.00 23.24 ? 260  LEU B O     1 
ATOM   6112 C  CB    . LEU B 1 260 ? -29.694 3.031   36.901  1.00 24.10 ? 260  LEU B CB    1 
ATOM   6113 C  CG    . LEU B 1 260 ? -29.587 3.281   38.405  1.00 24.13 ? 260  LEU B CG    1 
ATOM   6114 C  CD1   . LEU B 1 260 ? -30.352 2.214   39.164  1.00 25.28 ? 260  LEU B CD1   1 
ATOM   6115 C  CD2   . LEU B 1 260 ? -28.151 3.378   38.875  1.00 24.46 ? 260  LEU B CD2   1 
ATOM   6116 N  N     . ARG B 1 261 ? -29.539 3.532   33.664  1.00 22.49 ? 261  ARG B N     1 
ATOM   6117 C  CA    . ARG B 1 261 ? -29.332 2.847   32.367  1.00 23.53 ? 261  ARG B CA    1 
ATOM   6118 C  C     . ARG B 1 261 ? -28.046 3.320   31.706  1.00 23.55 ? 261  ARG B C     1 
ATOM   6119 O  O     . ARG B 1 261 ? -27.190 2.480   31.493  1.00 25.82 ? 261  ARG B O     1 
ATOM   6120 C  CB    . ARG B 1 261 ? -30.497 3.012   31.392  1.00 25.07 ? 261  ARG B CB    1 
ATOM   6121 C  CG    . ARG B 1 261 ? -30.215 2.445   30.005  1.00 24.95 ? 261  ARG B CG    1 
ATOM   6122 C  CD    . ARG B 1 261 ? -31.418 2.480   29.089  1.00 24.01 ? 261  ARG B CD    1 
ATOM   6123 N  NE    . ARG B 1 261 ? -31.904 3.847   28.986  1.00 24.47 ? 261  ARG B NE    1 
ATOM   6124 C  CZ    . ARG B 1 261 ? -33.093 4.295   29.403  1.00 24.80 ? 261  ARG B CZ    1 
ATOM   6125 N  NH1   . ARG B 1 261 ? -33.993 3.505   29.971  1.00 24.05 ? 261  ARG B NH1   1 
ATOM   6126 N  NH2   . ARG B 1 261 ? -33.388 5.564   29.231  1.00 24.69 ? 261  ARG B NH2   1 
ATOM   6127 N  N     . PRO B 1 262 ? -27.864 4.609   31.308  1.00 23.34 ? 262  PRO B N     1 
ATOM   6128 C  CA    . PRO B 1 262 ? -26.666 4.969   30.558  1.00 23.41 ? 262  PRO B CA    1 
ATOM   6129 C  C     . PRO B 1 262 ? -25.421 4.751   31.418  1.00 24.24 ? 262  PRO B C     1 
ATOM   6130 O  O     . PRO B 1 262 ? -24.363 4.431   30.855  1.00 22.76 ? 262  PRO B O     1 
ATOM   6131 C  CB    . PRO B 1 262 ? -26.875 6.438   30.148  1.00 22.79 ? 262  PRO B CB    1 
ATOM   6132 C  CG    . PRO B 1 262 ? -27.956 6.948   31.110  1.00 22.15 ? 262  PRO B CG    1 
ATOM   6133 C  CD    . PRO B 1 262 ? -28.821 5.738   31.388  1.00 22.18 ? 262  PRO B CD    1 
ATOM   6134 N  N     . LEU B 1 263 ? -25.536 4.958   32.734  1.00 22.76 ? 263  LEU B N     1 
ATOM   6135 C  CA    . LEU B 1 263 ? -24.362 4.834   33.645  1.00 23.72 ? 263  LEU B CA    1 
ATOM   6136 C  C     . LEU B 1 263 ? -23.857 3.377   33.605  1.00 22.77 ? 263  LEU B C     1 
ATOM   6137 O  O     . LEU B 1 263 ? -22.622 3.188   33.666  1.00 23.36 ? 263  LEU B O     1 
ATOM   6138 C  CB    . LEU B 1 263 ? -24.757 5.266   35.065  1.00 25.68 ? 263  LEU B CB    1 
ATOM   6139 C  CG    . LEU B 1 263 ? -25.064 6.763   35.244  1.00 25.13 ? 263  LEU B CG    1 
ATOM   6140 C  CD1   . LEU B 1 263 ? -25.655 7.033   36.616  1.00 24.24 ? 263  LEU B CD1   1 
ATOM   6141 C  CD2   . LEU B 1 263 ? -23.820 7.607   35.067  1.00 25.27 ? 263  LEU B CD2   1 
ATOM   6142 N  N     . LYS B 1 264 ? -24.773 2.410   33.495  1.00 21.65 ? 264  LYS B N     1 
ATOM   6143 C  CA    . LYS B 1 264 ? -24.483 0.959   33.559  1.00 23.75 ? 264  LYS B CA    1 
ATOM   6144 C  C     . LYS B 1 264 ? -24.015 0.492   32.174  1.00 23.51 ? 264  LYS B C     1 
ATOM   6145 O  O     . LYS B 1 264 ? -22.962 -0.129  32.099  1.00 24.24 ? 264  LYS B O     1 
ATOM   6146 C  CB    . LYS B 1 264 ? -25.704 0.172   34.051  1.00 25.06 ? 264  LYS B CB    1 
ATOM   6147 C  CG    . LYS B 1 264 ? -25.825 -0.004  35.558  1.00 26.61 ? 264  LYS B CG    1 
ATOM   6148 C  CD    . LYS B 1 264 ? -24.574 -0.552  36.198  1.00 31.18 ? 264  LYS B CD    1 
ATOM   6149 C  CE    . LYS B 1 264 ? -24.252 -1.989  35.836  1.00 32.08 ? 264  LYS B CE    1 
ATOM   6150 N  NZ    . LYS B 1 264 ? -22.855 -2.313  36.203  1.00 32.39 ? 264  LYS B NZ    1 
ATOM   6151 N  N     . VAL B 1 265 ? -24.730 0.834   31.105  1.00 21.10 ? 265  VAL B N     1 
ATOM   6152 C  CA    . VAL B 1 265 ? -24.335 0.425   29.731  1.00 23.13 ? 265  VAL B CA    1 
ATOM   6153 C  C     . VAL B 1 265 ? -22.898 0.902   29.489  1.00 23.12 ? 265  VAL B C     1 
ATOM   6154 O  O     . VAL B 1 265 ? -22.081 0.112   29.024  1.00 23.40 ? 265  VAL B O     1 
ATOM   6155 C  CB    . VAL B 1 265 ? -25.343 0.931   28.681  1.00 24.17 ? 265  VAL B CB    1 
ATOM   6156 C  CG1   . VAL B 1 265 ? -24.926 0.558   27.268  1.00 24.85 ? 265  VAL B CG1   1 
ATOM   6157 C  CG2   . VAL B 1 265 ? -26.751 0.408   28.973  1.00 23.42 ? 265  VAL B CG2   1 
ATOM   6158 N  N     . ALA B 1 266 ? -22.572 2.136   29.848  1.00 20.52 ? 266  ALA B N     1 
ATOM   6159 C  CA    . ALA B 1 266 ? -21.242 2.706   29.561  1.00 21.58 ? 266  ALA B CA    1 
ATOM   6160 C  C     . ALA B 1 266 ? -20.203 2.219   30.580  1.00 20.71 ? 266  ALA B C     1 
ATOM   6161 O  O     . ALA B 1 266 ? -19.029 2.396   30.322  1.00 23.43 ? 266  ALA B O     1 
ATOM   6162 C  CB    . ALA B 1 266 ? -21.327 4.205   29.500  1.00 19.92 ? 266  ALA B CB    1 
ATOM   6163 N  N     . GLY B 1 267 ? -20.585 1.619   31.693  1.00 21.91 ? 267  GLY B N     1 
ATOM   6164 C  CA    . GLY B 1 267 ? -19.590 1.169   32.696  1.00 23.31 ? 267  GLY B CA    1 
ATOM   6165 C  C     . GLY B 1 267 ? -19.115 2.274   33.643  1.00 24.56 ? 267  GLY B C     1 
ATOM   6166 O  O     . GLY B 1 267 ? -18.074 2.095   34.311  1.00 26.60 ? 267  GLY B O     1 
ATOM   6167 N  N     . VAL B 1 268 ? -19.845 3.376   33.758  1.00 26.28 ? 268  VAL B N     1 
ATOM   6168 C  CA    . VAL B 1 268 ? -19.495 4.461   34.729  1.00 26.39 ? 268  VAL B CA    1 
ATOM   6169 C  C     . VAL B 1 268 ? -19.703 3.930   36.155  1.00 23.40 ? 268  VAL B C     1 
ATOM   6170 O  O     . VAL B 1 268 ? -18.856 4.192   37.019  1.00 24.05 ? 268  VAL B O     1 
ATOM   6171 C  CB    . VAL B 1 268 ? -20.308 5.737   34.452  1.00 26.02 ? 268  VAL B CB    1 
ATOM   6172 C  CG1   . VAL B 1 268 ? -20.073 6.798   35.526  1.00 27.11 ? 268  VAL B CG1   1 
ATOM   6173 C  CG2   . VAL B 1 268 ? -19.993 6.266   33.063  1.00 25.89 ? 268  VAL B CG2   1 
ATOM   6174 N  N     . ILE B 1 269 ? -20.783 3.186   36.382  1.00 20.64 ? 269  ILE B N     1 
ATOM   6175 C  CA    . ILE B 1 269 ? -20.949 2.348   37.593  1.00 21.36 ? 269  ILE B CA    1 
ATOM   6176 C  C     . ILE B 1 269 ? -20.237 1.017   37.310  1.00 25.19 ? 269  ILE B C     1 
ATOM   6177 O  O     . ILE B 1 269 ? -20.619 0.362   36.321  1.00 26.94 ? 269  ILE B O     1 
ATOM   6178 C  CB    . ILE B 1 269 ? -22.427 2.173   37.946  1.00 20.90 ? 269  ILE B CB    1 
ATOM   6179 C  CG1   . ILE B 1 269 ? -23.098 3.505   38.310  1.00 22.27 ? 269  ILE B CG1   1 
ATOM   6180 C  CG2   . ILE B 1 269 ? -22.578 1.165   39.070  1.00 22.74 ? 269  ILE B CG2   1 
ATOM   6181 C  CD1   . ILE B 1 269 ? -24.611 3.453   38.224  1.00 23.01 ? 269  ILE B CD1   1 
ATOM   6182 N  N     . GLN B 1 270 ? -19.226 0.671   38.126  1.00 24.23 ? 270  GLN B N     1 
ATOM   6183 C  CA    . GLN B 1 270 ? -18.233 -0.391  37.843  1.00 23.36 ? 270  GLN B CA    1 
ATOM   6184 C  C     . GLN B 1 270 ? -18.670 -1.735  38.418  1.00 22.18 ? 270  GLN B C     1 
ATOM   6185 O  O     . GLN B 1 270 ? -18.110 -2.737  37.973  1.00 22.08 ? 270  GLN B O     1 
ATOM   6186 C  CB    . GLN B 1 270 ? -16.861 -0.030  38.403  1.00 23.57 ? 270  GLN B CB    1 
ATOM   6187 C  CG    . GLN B 1 270 ? -16.277 1.226   37.794  1.00 24.30 ? 270  GLN B CG    1 
ATOM   6188 C  CD    . GLN B 1 270 ? -15.274 1.901   38.696  1.00 23.97 ? 270  GLN B CD    1 
ATOM   6189 O  OE1   . GLN B 1 270 ? -15.604 2.436   39.754  1.00 25.11 ? 270  GLN B OE1   1 
ATOM   6190 N  NE2   . GLN B 1 270 ? -14.021 1.860   38.290  1.00 23.60 ? 270  GLN B NE2   1 
ATOM   6191 N  N     . ASN B 1 271 ? -19.574 -1.761  39.404  1.00 22.67 ? 271  ASN B N     1 
ATOM   6192 C  CA    . ASN B 1 271 ? -20.106 -3.018  39.982  1.00 22.04 ? 271  ASN B CA    1 
ATOM   6193 C  C     . ASN B 1 271 ? -21.591 -3.136  39.616  1.00 23.82 ? 271  ASN B C     1 
ATOM   6194 O  O     . ASN B 1 271 ? -22.105 -2.246  38.950  1.00 25.41 ? 271  ASN B O     1 
ATOM   6195 C  CB    . ASN B 1 271 ? -19.801 -3.146  41.476  1.00 22.42 ? 271  ASN B CB    1 
ATOM   6196 C  CG    . ASN B 1 271 ? -20.356 -2.061  42.393  1.00 22.91 ? 271  ASN B CG    1 
ATOM   6197 O  OD1   . ASN B 1 271 ? -20.593 -0.914  42.000  1.00 22.17 ? 271  ASN B OD1   1 
ATOM   6198 N  ND2   . ASN B 1 271 ? -20.476 -2.399  43.668  1.00 22.17 ? 271  ASN B ND2   1 
ATOM   6199 N  N     . GLY B 1 272 ? -22.253 -4.216  40.011  1.00 23.79 ? 272  GLY B N     1 
ATOM   6200 C  CA    . GLY B 1 272 ? -23.721 -4.288  39.934  1.00 24.38 ? 272  GLY B CA    1 
ATOM   6201 C  C     . GLY B 1 272 ? -24.316 -3.096  40.666  1.00 25.22 ? 272  GLY B C     1 
ATOM   6202 O  O     . GLY B 1 272 ? -23.733 -2.697  41.660  1.00 19.44 ? 272  GLY B O     1 
ATOM   6203 N  N     . ALA B 1 273 ? -25.360 -2.473  40.118  1.00 27.71 ? 273  ALA B N     1 
ATOM   6204 C  CA    . ALA B 1 273 ? -26.193 -1.459  40.815  1.00 28.45 ? 273  ALA B CA    1 
ATOM   6205 C  C     . ALA B 1 273 ? -27.235 -2.259  41.601  1.00 28.68 ? 273  ALA B C     1 
ATOM   6206 O  O     . ALA B 1 273 ? -27.932 -3.101  40.956  1.00 31.08 ? 273  ALA B O     1 
ATOM   6207 C  CB    . ALA B 1 273 ? -26.846 -0.526  39.819  1.00 26.77 ? 273  ALA B CB    1 
ATOM   6208 N  N     . THR B 1 274 ? -27.306 -2.076  42.921  1.00 25.18 ? 274  THR B N     1 
ATOM   6209 C  CA    . THR B 1 274 ? -28.357 -2.713  43.760  1.00 27.23 ? 274  THR B CA    1 
ATOM   6210 C  C     . THR B 1 274 ? -29.219 -1.639  44.434  1.00 24.50 ? 274  THR B C     1 
ATOM   6211 O  O     . THR B 1 274 ? -28.674 -0.851  45.197  1.00 26.97 ? 274  THR B O     1 
ATOM   6212 C  CB    . THR B 1 274 ? -27.768 -3.670  44.802  1.00 28.03 ? 274  THR B CB    1 
ATOM   6213 O  OG1   . THR B 1 274 ? -26.802 -4.509  44.161  1.00 30.56 ? 274  THR B OG1   1 
ATOM   6214 C  CG2   . THR B 1 274 ? -28.858 -4.522  45.400  1.00 30.70 ? 274  THR B CG2   1 
ATOM   6215 N  N     . VAL B 1 275 ? -30.514 -1.626  44.139  1.00 23.71 ? 275  VAL B N     1 
ATOM   6216 C  CA    . VAL B 1 275 ? -31.483 -0.635  44.677  1.00 25.70 ? 275  VAL B CA    1 
ATOM   6217 C  C     . VAL B 1 275 ? -32.507 -1.414  45.500  1.00 25.47 ? 275  VAL B C     1 
ATOM   6218 O  O     . VAL B 1 275 ? -33.466 -1.958  44.916  1.00 27.25 ? 275  VAL B O     1 
ATOM   6219 C  CB    . VAL B 1 275 ? -32.142 0.222   43.580  1.00 24.47 ? 275  VAL B CB    1 
ATOM   6220 C  CG1   . VAL B 1 275 ? -32.802 1.452   44.182  1.00 23.15 ? 275  VAL B CG1   1 
ATOM   6221 C  CG2   . VAL B 1 275 ? -31.143 0.629   42.505  1.00 24.12 ? 275  VAL B CG2   1 
ATOM   6222 N  N     . ARG B 1 276 ? -32.273 -1.474  46.806  1.00 24.42 ? 276  ARG B N     1 
ATOM   6223 C  CA    . ARG B 1 276 ? -33.052 -2.309  47.748  1.00 27.11 ? 276  ARG B CA    1 
ATOM   6224 C  C     . ARG B 1 276 ? -34.167 -1.467  48.382  1.00 26.22 ? 276  ARG B C     1 
ATOM   6225 O  O     . ARG B 1 276 ? -33.942 -0.240  48.668  1.00 25.27 ? 276  ARG B O     1 
ATOM   6226 C  CB    . ARG B 1 276 ? -32.124 -2.872  48.821  1.00 31.16 ? 276  ARG B CB    1 
ATOM   6227 C  CG    . ARG B 1 276 ? -31.134 -3.908  48.327  1.00 34.43 ? 276  ARG B CG    1 
ATOM   6228 C  CD    . ARG B 1 276 ? -30.411 -4.550  49.495  1.00 40.18 ? 276  ARG B CD    1 
ATOM   6229 N  NE    . ARG B 1 276 ? -29.321 -5.404  49.060  1.00 46.15 ? 276  ARG B NE    1 
ATOM   6230 C  CZ    . ARG B 1 276 ? -28.147 -4.962  48.594  1.00 50.27 ? 276  ARG B CZ    1 
ATOM   6231 N  NH1   . ARG B 1 276 ? -27.224 -5.831  48.213  1.00 57.44 ? 276  ARG B NH1   1 
ATOM   6232 N  NH2   . ARG B 1 276 ? -27.891 -3.663  48.505  1.00 53.49 ? 276  ARG B NH2   1 
ATOM   6233 N  N     . SER B 1 277 ? -35.308 -2.120  48.591  1.00 24.08 ? 277  SER B N     1 
ATOM   6234 C  CA    . SER B 1 277 ? -36.518 -1.616  49.278  1.00 24.31 ? 277  SER B CA    1 
ATOM   6235 C  C     . SER B 1 277 ? -36.214 -1.403  50.765  1.00 25.86 ? 277  SER B C     1 
ATOM   6236 O  O     . SER B 1 277 ? -35.327 -2.080  51.318  1.00 27.92 ? 277  SER B O     1 
ATOM   6237 C  CB    . SER B 1 277 ? -37.688 -2.556  49.043  1.00 22.81 ? 277  SER B CB    1 
ATOM   6238 O  OG    . SER B 1 277 ? -37.586 -3.740  49.838  1.00 21.60 ? 277  SER B OG    1 
ATOM   6239 N  N     . LEU B 1 278 ? -36.954 -0.509  51.407  1.00 24.25 ? 278  LEU B N     1 
ATOM   6240 C  CA    . LEU B 1 278 ? -36.780 -0.150  52.839  1.00 23.65 ? 278  LEU B CA    1 
ATOM   6241 C  C     . LEU B 1 278 ? -36.674 -1.383  53.743  1.00 22.14 ? 278  LEU B C     1 
ATOM   6242 O  O     . LEU B 1 278 ? -35.693 -1.442  54.515  1.00 21.27 ? 278  LEU B O     1 
ATOM   6243 C  CB    . LEU B 1 278 ? -37.990 0.688   53.250  1.00 24.75 ? 278  LEU B CB    1 
ATOM   6244 C  CG    . LEU B 1 278 ? -38.084 1.031   54.729  1.00 24.52 ? 278  LEU B CG    1 
ATOM   6245 C  CD1   . LEU B 1 278 ? -36.840 1.743   55.188  1.00 23.60 ? 278  LEU B CD1   1 
ATOM   6246 C  CD2   . LEU B 1 278 ? -39.331 1.880   54.967  1.00 25.92 ? 278  LEU B CD2   1 
ATOM   6247 N  N     . VAL B 1 279 ? -37.677 -2.266  53.713  1.00 21.92 ? 279  VAL B N     1 
ATOM   6248 C  CA    . VAL B 1 279 ? -37.785 -3.433  54.631  1.00 24.47 ? 279  VAL B CA    1 
ATOM   6249 C  C     . VAL B 1 279 ? -36.580 -4.372  54.440  1.00 26.98 ? 279  VAL B C     1 
ATOM   6250 O  O     . VAL B 1 279 ? -36.033 -4.850  55.478  1.00 27.43 ? 279  VAL B O     1 
ATOM   6251 C  CB    . VAL B 1 279 ? -39.133 -4.169  54.500  1.00 25.86 ? 279  VAL B CB    1 
ATOM   6252 C  CG1   . VAL B 1 279 ? -39.215 -5.333  55.491  1.00 26.25 ? 279  VAL B CG1   1 
ATOM   6253 C  CG2   . VAL B 1 279 ? -40.319 -3.222  54.713  1.00 25.99 ? 279  VAL B CG2   1 
ATOM   6254 N  N     . LEU B 1 280 ? -36.121 -4.601  53.198  1.00 26.58 ? 280  LEU B N     1 
ATOM   6255 C  CA    . LEU B 1 280 ? -34.965 -5.499  52.953  1.00 25.51 ? 280  LEU B CA    1 
ATOM   6256 C  C     . LEU B 1 280 ? -33.742 -4.933  53.692  1.00 24.92 ? 280  LEU B C     1 
ATOM   6257 O  O     . LEU B 1 280 ? -33.056 -5.681  54.386  1.00 22.12 ? 280  LEU B O     1 
ATOM   6258 C  CB    . LEU B 1 280 ? -34.701 -5.609  51.450  1.00 28.67 ? 280  LEU B CB    1 
ATOM   6259 C  CG    . LEU B 1 280 ? -33.650 -6.638  51.054  1.00 28.59 ? 280  LEU B CG    1 
ATOM   6260 C  CD1   . LEU B 1 280 ? -33.965 -7.988  51.698  1.00 31.23 ? 280  LEU B CD1   1 
ATOM   6261 C  CD2   . LEU B 1 280 ? -33.581 -6.773  49.547  1.00 31.23 ? 280  LEU B CD2   1 
ATOM   6262 N  N     . ASP B 1 281 ? -33.494 -3.634  53.558  1.00 23.85 ? 281  ASP B N     1 
ATOM   6263 C  CA    . ASP B 1 281 ? -32.339 -2.945  54.188  1.00 26.89 ? 281  ASP B CA    1 
ATOM   6264 C  C     . ASP B 1 281 ? -32.547 -2.828  55.704  1.00 25.33 ? 281  ASP B C     1 
ATOM   6265 O  O     . ASP B 1 281 ? -31.565 -2.963  56.448  1.00 26.11 ? 281  ASP B O     1 
ATOM   6266 C  CB    . ASP B 1 281 ? -32.085 -1.606  53.485  1.00 29.51 ? 281  ASP B CB    1 
ATOM   6267 C  CG    . ASP B 1 281 ? -31.323 -1.809  52.174  1.00 37.47 ? 281  ASP B CG    1 
ATOM   6268 O  OD1   . ASP B 1 281 ? -30.582 -2.824  52.071  1.00 38.98 ? 281  ASP B OD1   1 
ATOM   6269 O  OD2   . ASP B 1 281 ? -31.479 -0.982  51.261  1.00 43.59 ? 281  ASP B OD2   1 
ATOM   6270 N  N     . ALA B 1 282 ? -33.776 -2.601  56.157  1.00 23.09 ? 282  ALA B N     1 
ATOM   6271 C  CA    . ALA B 1 282 ? -34.043 -2.368  57.585  1.00 22.73 ? 282  ALA B CA    1 
ATOM   6272 C  C     . ALA B 1 282 ? -33.856 -3.680  58.357  1.00 23.08 ? 282  ALA B C     1 
ATOM   6273 O  O     . ALA B 1 282 ? -33.310 -3.623  59.470  1.00 22.93 ? 282  ALA B O     1 
ATOM   6274 C  CB    . ALA B 1 282 ? -35.427 -1.792  57.774  1.00 22.88 ? 282  ALA B CB    1 
ATOM   6275 N  N     . ALA B 1 283 ? -34.254 -4.801  57.762  1.00 23.54 ? 283  ALA B N     1 
ATOM   6276 C  CA    . ALA B 1 283 ? -34.226 -6.145  58.373  1.00 23.80 ? 283  ALA B CA    1 
ATOM   6277 C  C     . ALA B 1 283 ? -32.795 -6.563  58.646  1.00 26.20 ? 283  ALA B C     1 
ATOM   6278 O  O     . ALA B 1 283 ? -32.621 -7.603  59.261  1.00 26.60 ? 283  ALA B O     1 
ATOM   6279 C  CB    . ALA B 1 283 ? -34.881 -7.141  57.459  1.00 24.63 ? 283  ALA B CB    1 
ATOM   6280 N  N     . ILE B 1 284 ? -31.811 -5.827  58.124  1.00 28.61 ? 284  ILE B N     1 
ATOM   6281 C  CA    . ILE B 1 284 ? -30.385 -6.122  58.415  1.00 31.04 ? 284  ILE B CA    1 
ATOM   6282 C  C     . ILE B 1 284 ? -30.086 -5.731  59.865  1.00 30.65 ? 284  ILE B C     1 
ATOM   6283 O  O     . ILE B 1 284 ? -29.336 -6.466  60.511  1.00 32.92 ? 284  ILE B O     1 
ATOM   6284 C  CB    . ILE B 1 284 ? -29.421 -5.467  57.396  1.00 32.94 ? 284  ILE B CB    1 
ATOM   6285 C  CG1   . ILE B 1 284 ? -29.609 -6.021  55.980  1.00 35.17 ? 284  ILE B CG1   1 
ATOM   6286 C  CG2   . ILE B 1 284 ? -27.973 -5.614  57.836  1.00 33.10 ? 284  ILE B CG2   1 
ATOM   6287 C  CD1   . ILE B 1 284 ? -29.333 -7.519  55.825  1.00 37.27 ? 284  ILE B CD1   1 
ATOM   6288 N  N     . THR B 1 285 ? -30.634 -4.643  60.390  1.00 29.32 ? 285  THR B N     1 
ATOM   6289 C  CA    . THR B 1 285 ? -30.288 -4.189  61.763  1.00 29.86 ? 285  THR B CA    1 
ATOM   6290 C  C     . THR B 1 285 ? -31.502 -4.146  62.710  1.00 29.56 ? 285  THR B C     1 
ATOM   6291 O  O     . THR B 1 285 ? -31.274 -3.912  63.922  1.00 27.69 ? 285  THR B O     1 
ATOM   6292 C  CB    . THR B 1 285 ? -29.587 -2.834  61.728  1.00 31.86 ? 285  THR B CB    1 
ATOM   6293 O  OG1   . THR B 1 285 ? -30.558 -1.862  61.348  1.00 33.50 ? 285  THR B OG1   1 
ATOM   6294 C  CG2   . THR B 1 285 ? -28.398 -2.809  60.789  1.00 32.77 ? 285  THR B CG2   1 
ATOM   6295 N  N     . ARG B 1 286 ? -32.718 -4.427  62.248  1.00 24.59 ? 286  ARG B N     1 
ATOM   6296 C  CA    . ARG B 1 286 ? -33.938 -4.276  63.077  1.00 25.37 ? 286  ARG B CA    1 
ATOM   6297 C  C     . ARG B 1 286 ? -34.893 -5.433  62.771  1.00 26.05 ? 286  ARG B C     1 
ATOM   6298 O  O     . ARG B 1 286 ? -34.734 -6.045  61.708  1.00 28.16 ? 286  ARG B O     1 
ATOM   6299 C  CB    . ARG B 1 286 ? -34.610 -2.926  62.794  1.00 26.37 ? 286  ARG B CB    1 
ATOM   6300 C  CG    . ARG B 1 286 ? -33.847 -1.695  63.270  1.00 29.39 ? 286  ARG B CG    1 
ATOM   6301 C  CD    . ARG B 1 286 ? -33.881 -1.536  64.781  1.00 34.07 ? 286  ARG B CD    1 
ATOM   6302 N  NE    . ARG B 1 286 ? -33.535 -0.190  65.232  1.00 38.64 ? 286  ARG B NE    1 
ATOM   6303 C  CZ    . ARG B 1 286 ? -32.292 0.236   65.383  1.00 41.94 ? 286  ARG B CZ    1 
ATOM   6304 N  NH1   . ARG B 1 286 ? -31.284 -0.565  65.071  1.00 44.50 ? 286  ARG B NH1   1 
ATOM   6305 N  NH2   . ARG B 1 286 ? -32.058 1.477   65.767  1.00 38.60 ? 286  ARG B NH2   1 
ATOM   6306 N  N     . THR B 1 287 ? -35.853 -5.699  63.666  1.00 25.83 ? 287  THR B N     1 
ATOM   6307 C  CA    . THR B 1 287 ? -37.005 -6.607  63.443  1.00 27.53 ? 287  THR B CA    1 
ATOM   6308 C  C     . THR B 1 287 ? -38.282 -5.778  63.351  1.00 26.33 ? 287  THR B C     1 
ATOM   6309 O  O     . THR B 1 287 ? -38.301 -4.657  63.900  1.00 24.38 ? 287  THR B O     1 
ATOM   6310 C  CB    . THR B 1 287 ? -37.143 -7.629  64.571  1.00 28.06 ? 287  THR B CB    1 
ATOM   6311 O  OG1   . THR B 1 287 ? -37.430 -6.901  65.766  1.00 26.76 ? 287  THR B OG1   1 
ATOM   6312 C  CG2   . THR B 1 287 ? -35.884 -8.450  64.709  1.00 29.28 ? 287  THR B CG2   1 
ATOM   6313 N  N     . LYS B 1 288 ? -39.316 -6.336  62.733  1.00 24.08 ? 288  LYS B N     1 
ATOM   6314 C  CA    . LYS B 1 288 ? -40.633 -5.673  62.578  1.00 25.84 ? 288  LYS B CA    1 
ATOM   6315 C  C     . LYS B 1 288 ? -41.174 -5.232  63.955  1.00 26.57 ? 288  LYS B C     1 
ATOM   6316 O  O     . LYS B 1 288 ? -41.755 -4.137  64.025  1.00 22.60 ? 288  LYS B O     1 
ATOM   6317 C  CB    . LYS B 1 288 ? -41.611 -6.594  61.855  1.00 27.27 ? 288  LYS B CB    1 
ATOM   6318 C  CG    . LYS B 1 288 ? -42.991 -5.985  61.686  1.00 29.51 ? 288  LYS B CG    1 
ATOM   6319 C  CD    . LYS B 1 288 ? -43.890 -6.675  60.699  1.00 32.49 ? 288  LYS B CD    1 
ATOM   6320 C  CE    . LYS B 1 288 ? -44.846 -7.657  61.332  1.00 37.24 ? 288  LYS B CE    1 
ATOM   6321 N  NZ    . LYS B 1 288 ? -46.016 -7.956  60.458  1.00 40.32 ? 288  LYS B NZ    1 
ATOM   6322 N  N     . SER B 1 289 ? -40.973 -6.047  64.996  1.00 24.45 ? 289  SER B N     1 
ATOM   6323 C  CA    . SER B 1 289 ? -41.544 -5.869  66.359  1.00 25.00 ? 289  SER B CA    1 
ATOM   6324 C  C     . SER B 1 289 ? -40.963 -4.617  67.039  1.00 22.88 ? 289  SER B C     1 
ATOM   6325 O  O     . SER B 1 289 ? -41.566 -4.148  67.973  1.00 21.22 ? 289  SER B O     1 
ATOM   6326 C  CB    . SER B 1 289 ? -41.276 -7.100  67.190  1.00 25.15 ? 289  SER B CB    1 
ATOM   6327 O  OG    . SER B 1 289 ? -39.875 -7.282  67.257  1.00 28.77 ? 289  SER B OG    1 
ATOM   6328 N  N     . GLN B 1 290 ? -39.830 -4.089  66.577  1.00 23.97 ? 290  GLN B N     1 
ATOM   6329 C  CA    . GLN B 1 290 ? -39.250 -2.831  67.116  1.00 23.85 ? 290  GLN B CA    1 
ATOM   6330 C  C     . GLN B 1 290 ? -40.161 -1.655  66.723  1.00 22.97 ? 290  GLN B C     1 
ATOM   6331 O  O     . GLN B 1 290 ? -40.098 -0.657  67.423  1.00 22.50 ? 290  GLN B O     1 
ATOM   6332 C  CB    . GLN B 1 290 ? -37.789 -2.658  66.689  1.00 27.17 ? 290  GLN B CB    1 
ATOM   6333 C  CG    . GLN B 1 290 ? -36.808 -3.465  67.560  1.00 35.13 ? 290  GLN B CG    1 
ATOM   6334 C  CD    . GLN B 1 290 ? -35.580 -4.002  66.836  1.00 41.71 ? 290  GLN B CD    1 
ATOM   6335 O  OE1   . GLN B 1 290 ? -35.519 -4.097  65.625  1.00 45.72 ? 290  GLN B OE1   1 
ATOM   6336 N  NE2   . GLN B 1 290 ? -34.562 -4.393  67.569  1.00 48.82 ? 290  GLN B NE2   1 
ATOM   6337 N  N     . TYR B 1 291 ? -41.049 -1.797  65.728  1.00 21.86 ? 291  TYR B N     1 
ATOM   6338 C  CA    . TYR B 1 291 ? -41.853 -0.682  65.160  1.00 21.34 ? 291  TYR B CA    1 
ATOM   6339 C  C     . TYR B 1 291 ? -43.352 -0.986  65.109  1.00 21.81 ? 291  TYR B C     1 
ATOM   6340 O  O     . TYR B 1 291 ? -44.150 -0.039  65.115  1.00 21.09 ? 291  TYR B O     1 
ATOM   6341 C  CB    . TYR B 1 291 ? -41.418 -0.388  63.724  1.00 22.67 ? 291  TYR B CB    1 
ATOM   6342 C  CG    . TYR B 1 291 ? -39.976 -0.015  63.553  1.00 21.31 ? 291  TYR B CG    1 
ATOM   6343 C  CD1   . TYR B 1 291 ? -39.541 1.279   63.791  1.00 20.82 ? 291  TYR B CD1   1 
ATOM   6344 C  CD2   . TYR B 1 291 ? -39.048 -0.945  63.117  1.00 22.13 ? 291  TYR B CD2   1 
ATOM   6345 C  CE1   . TYR B 1 291 ? -38.215 1.638   63.605  1.00 20.40 ? 291  TYR B CE1   1 
ATOM   6346 C  CE2   . TYR B 1 291 ? -37.719 -0.598  62.920  1.00 21.17 ? 291  TYR B CE2   1 
ATOM   6347 C  CZ    . TYR B 1 291 ? -37.297 0.695   63.172  1.00 20.31 ? 291  TYR B CZ    1 
ATOM   6348 O  OH    . TYR B 1 291 ? -35.979 1.033   63.021  1.00 20.60 ? 291  TYR B OH    1 
ATOM   6349 N  N     . TYR B 1 292 ? -43.740 -2.249  64.983  1.00 22.70 ? 292  TYR B N     1 
ATOM   6350 C  CA    . TYR B 1 292 ? -45.147 -2.607  64.707  1.00 26.29 ? 292  TYR B CA    1 
ATOM   6351 C  C     . TYR B 1 292 ? -45.435 -3.989  65.292  1.00 30.56 ? 292  TYR B C     1 
ATOM   6352 O  O     . TYR B 1 292 ? -44.663 -4.915  65.032  1.00 28.13 ? 292  TYR B O     1 
ATOM   6353 C  CB    . TYR B 1 292 ? -45.373 -2.492  63.203  1.00 28.13 ? 292  TYR B CB    1 
ATOM   6354 C  CG    . TYR B 1 292 ? -46.781 -2.724  62.737  1.00 28.99 ? 292  TYR B CG    1 
ATOM   6355 C  CD1   . TYR B 1 292 ? -47.782 -1.824  63.051  1.00 32.21 ? 292  TYR B CD1   1 
ATOM   6356 C  CD2   . TYR B 1 292 ? -47.101 -3.822  61.957  1.00 29.57 ? 292  TYR B CD2   1 
ATOM   6357 C  CE1   . TYR B 1 292 ? -49.081 -2.014  62.618  1.00 32.90 ? 292  TYR B CE1   1 
ATOM   6358 C  CE2   . TYR B 1 292 ? -48.390 -4.028  61.509  1.00 30.74 ? 292  TYR B CE2   1 
ATOM   6359 C  CZ    . TYR B 1 292 ? -49.379 -3.127  61.853  1.00 32.90 ? 292  TYR B CZ    1 
ATOM   6360 O  OH    . TYR B 1 292 ? -50.649 -3.294  61.423  1.00 37.94 ? 292  TYR B OH    1 
ATOM   6361 N  N     . ASP B 1 293 ? -46.508 -4.104  66.086  1.00 36.24 ? 293  ASP B N     1 
ATOM   6362 C  CA    . ASP B 1 293 ? -46.833 -5.327  66.871  1.00 39.07 ? 293  ASP B CA    1 
ATOM   6363 C  C     . ASP B 1 293 ? -47.871 -6.159  66.107  1.00 38.25 ? 293  ASP B C     1 
ATOM   6364 O  O     . ASP B 1 293 ? -48.024 -7.341  66.444  1.00 44.65 ? 293  ASP B O     1 
ATOM   6365 C  CB    . ASP B 1 293 ? -47.275 -4.978  68.300  1.00 38.93 ? 293  ASP B CB    1 
ATOM   6366 C  CG    . ASP B 1 293 ? -46.145 -4.606  69.258  1.00 45.74 ? 293  ASP B CG    1 
ATOM   6367 O  OD1   . ASP B 1 293 ? -45.038 -5.245  69.183  1.00 47.11 ? 293  ASP B OD1   1 
ATOM   6368 O  OD2   . ASP B 1 293 ? -46.364 -3.665  70.089  1.00 51.11 ? 293  ASP B OD2   1 
ATOM   6369 N  N     . GLY B 1 294 ? -48.557 -5.588  65.119  1.00 38.99 ? 294  GLY B N     1 
ATOM   6370 C  CA    . GLY B 1 294 ? -49.543 -6.323  64.301  1.00 44.31 ? 294  GLY B CA    1 
ATOM   6371 C  C     . GLY B 1 294 ? -48.887 -7.351  63.378  1.00 52.83 ? 294  GLY B C     1 
ATOM   6372 O  O     . GLY B 1 294 ? -47.677 -7.209  63.067  1.00 51.06 ? 294  GLY B O     1 
ATOM   6373 N  N     . ASP B 1 295 ? -49.662 -8.335  62.918  1.00 56.54 ? 295  ASP B N     1 
ATOM   6374 C  CA    . ASP B 1 295 ? -49.163 -9.516  62.158  1.00 64.41 ? 295  ASP B CA    1 
ATOM   6375 C  C     . ASP B 1 295 ? -49.167 -9.228  60.647  1.00 60.42 ? 295  ASP B C     1 
ATOM   6376 O  O     . ASP B 1 295 ? -48.457 -9.944  59.918  1.00 59.82 ? 295  ASP B O     1 
ATOM   6377 C  CB    . ASP B 1 295 ? -49.958 -10.778 62.512  1.00 70.40 ? 295  ASP B CB    1 
ATOM   6378 C  CG    . ASP B 1 295 ? -51.461 -10.587 62.449  1.00 82.20 ? 295  ASP B CG    1 
ATOM   6379 O  OD1   . ASP B 1 295 ? -51.902 -9.426  62.307  1.00 94.77 ? 295  ASP B OD1   1 
ATOM   6380 O  OD2   . ASP B 1 295 ? -52.180 -11.598 62.548  1.00 95.94 ? 295  ASP B OD2   1 
ATOM   6381 N  N     . GLY B 1 296 ? -49.916 -8.226  60.186  1.00 56.15 ? 296  GLY B N     1 
ATOM   6382 C  CA    . GLY B 1 296 ? -49.949 -7.846  58.761  1.00 55.12 ? 296  GLY B CA    1 
ATOM   6383 C  C     . GLY B 1 296 ? -48.657 -7.165  58.300  1.00 55.99 ? 296  GLY B C     1 
ATOM   6384 O  O     . GLY B 1 296 ? -47.749 -6.888  59.086  1.00 53.93 ? 296  GLY B O     1 
ATOM   6385 N  N     . PRO B 1 297 ? -48.523 -6.923  56.979  1.00 49.97 ? 297  PRO B N     1 
ATOM   6386 C  CA    . PRO B 1 297 ? -47.516 -6.010  56.437  1.00 46.14 ? 297  PRO B CA    1 
ATOM   6387 C  C     . PRO B 1 297 ? -47.511 -4.634  57.113  1.00 43.36 ? 297  PRO B C     1 
ATOM   6388 O  O     . PRO B 1 297 ? -48.553 -4.192  57.488  1.00 42.43 ? 297  PRO B O     1 
ATOM   6389 C  CB    . PRO B 1 297 ? -47.983 -5.858  54.982  1.00 47.53 ? 297  PRO B CB    1 
ATOM   6390 C  CG    . PRO B 1 297 ? -48.569 -7.213  54.654  1.00 49.78 ? 297  PRO B CG    1 
ATOM   6391 C  CD    . PRO B 1 297 ? -49.304 -7.588  55.924  1.00 51.74 ? 297  PRO B CD    1 
ATOM   6392 N  N     . ILE B 1 298 ? -46.356 -3.970  57.208  1.00 41.17 ? 298  ILE B N     1 
ATOM   6393 C  CA    . ILE B 1 298 ? -46.255 -2.639  57.875  1.00 35.09 ? 298  ILE B CA    1 
ATOM   6394 C  C     . ILE B 1 298 ? -47.117 -1.651  57.097  1.00 36.53 ? 298  ILE B C     1 
ATOM   6395 O  O     . ILE B 1 298 ? -47.248 -1.781  55.885  1.00 35.08 ? 298  ILE B O     1 
ATOM   6396 C  CB    . ILE B 1 298 ? -44.802 -2.151  58.004  1.00 33.30 ? 298  ILE B CB    1 
ATOM   6397 C  CG1   . ILE B 1 298 ? -44.141 -1.922  56.643  1.00 31.66 ? 298  ILE B CG1   1 
ATOM   6398 C  CG2   . ILE B 1 298 ? -44.004 -3.102  58.865  1.00 36.09 ? 298  ILE B CG2   1 
ATOM   6399 C  CD1   . ILE B 1 298 ? -42.924 -1.060  56.703  1.00 31.91 ? 298  ILE B CD1   1 
ATOM   6400 N  N     . PRO B 1 299 ? -47.757 -0.681  57.793  1.00 33.55 ? 299  PRO B N     1 
ATOM   6401 C  CA    . PRO B 1 299 ? -48.377 0.475   57.161  1.00 32.77 ? 299  PRO B CA    1 
ATOM   6402 C  C     . PRO B 1 299 ? -47.417 1.625   56.879  1.00 34.36 ? 299  PRO B C     1 
ATOM   6403 O  O     . PRO B 1 299 ? -46.290 1.604   57.359  1.00 33.38 ? 299  PRO B O     1 
ATOM   6404 C  CB    . PRO B 1 299 ? -49.352 0.970   58.233  1.00 32.71 ? 299  PRO B CB    1 
ATOM   6405 C  CG    . PRO B 1 299 ? -48.664 0.624   59.533  1.00 31.61 ? 299  PRO B CG    1 
ATOM   6406 C  CD    . PRO B 1 299 ? -47.971 -0.694  59.247  1.00 33.97 ? 299  PRO B CD    1 
ATOM   6407 N  N     . PRO B 1 300 ? -47.847 2.630   56.075  1.00 31.26 ? 300  PRO B N     1 
ATOM   6408 C  CA    . PRO B 1 300 ? -47.005 3.758   55.674  1.00 30.99 ? 300  PRO B CA    1 
ATOM   6409 C  C     . PRO B 1 300 ? -46.407 4.620   56.788  1.00 31.06 ? 300  PRO B C     1 
ATOM   6410 O  O     . PRO B 1 300 ? -45.294 5.091   56.612  1.00 29.14 ? 300  PRO B O     1 
ATOM   6411 C  CB    . PRO B 1 300 ? -47.964 4.655   54.852  1.00 32.27 ? 300  PRO B CB    1 
ATOM   6412 C  CG    . PRO B 1 300 ? -48.959 3.673   54.265  1.00 31.17 ? 300  PRO B CG    1 
ATOM   6413 C  CD    . PRO B 1 300 ? -49.127 2.621   55.344  1.00 31.21 ? 300  PRO B CD    1 
ATOM   6414 N  N     . SER B 1 301 ? -47.162 4.845   57.866  1.00 30.09 ? 301  SER B N     1 
ATOM   6415 C  CA    . SER B 1 301 ? -46.694 5.614   59.046  1.00 28.43 ? 301  SER B CA    1 
ATOM   6416 C  C     . SER B 1 301 ? -45.483 4.886   59.630  1.00 25.75 ? 301  SER B C     1 
ATOM   6417 O  O     . SER B 1 301 ? -44.507 5.557   60.045  1.00 27.62 ? 301  SER B O     1 
ATOM   6418 C  CB    . SER B 1 301 ? -47.793 5.816   60.070  1.00 26.47 ? 301  SER B CB    1 
ATOM   6419 O  OG    . SER B 1 301 ? -48.392 4.576   60.407  1.00 26.18 ? 301  SER B OG    1 
ATOM   6420 N  N     . VAL B 1 302 ? -45.525 3.557   59.650  1.00 24.61 ? 302  VAL B N     1 
ATOM   6421 C  CA    . VAL B 1 302 ? -44.399 2.758   60.209  1.00 25.03 ? 302  VAL B CA    1 
ATOM   6422 C  C     . VAL B 1 302 ? -43.192 2.906   59.257  1.00 25.00 ? 302  VAL B C     1 
ATOM   6423 O  O     . VAL B 1 302 ? -42.078 3.186   59.729  1.00 22.88 ? 302  VAL B O     1 
ATOM   6424 C  CB    . VAL B 1 302 ? -44.814 1.298   60.459  1.00 24.47 ? 302  VAL B CB    1 
ATOM   6425 C  CG1   . VAL B 1 302 ? -43.605 0.372   60.585  1.00 23.52 ? 302  VAL B CG1   1 
ATOM   6426 C  CG2   . VAL B 1 302 ? -45.738 1.188   61.686  1.00 25.36 ? 302  VAL B CG2   1 
ATOM   6427 N  N     . ALA B 1 303 ? -43.398 2.778   57.951  1.00 24.55 ? 303  ALA B N     1 
ATOM   6428 C  CA    . ALA B 1 303 ? -42.327 2.961   56.932  1.00 24.88 ? 303  ALA B CA    1 
ATOM   6429 C  C     . ALA B 1 303 ? -41.562 4.269   57.202  1.00 24.33 ? 303  ALA B C     1 
ATOM   6430 O  O     . ALA B 1 303 ? -40.318 4.243   57.164  1.00 23.96 ? 303  ALA B O     1 
ATOM   6431 C  CB    . ALA B 1 303 ? -42.927 2.954   55.547  1.00 23.54 ? 303  ALA B CB    1 
ATOM   6432 N  N     . LYS B 1 304 ? -42.275 5.360   57.516  1.00 24.63 ? 304  LYS B N     1 
ATOM   6433 C  CA    . LYS B 1 304 ? -41.693 6.721   57.700  1.00 25.68 ? 304  LYS B CA    1 
ATOM   6434 C  C     . LYS B 1 304 ? -40.912 6.803   59.013  1.00 22.70 ? 304  LYS B C     1 
ATOM   6435 O  O     . LYS B 1 304 ? -39.813 7.353   58.980  1.00 21.08 ? 304  LYS B O     1 
ATOM   6436 C  CB    . LYS B 1 304 ? -42.791 7.785   57.606  1.00 32.19 ? 304  LYS B CB    1 
ATOM   6437 C  CG    . LYS B 1 304 ? -43.222 8.033   56.165  1.00 38.43 ? 304  LYS B CG    1 
ATOM   6438 C  CD    . LYS B 1 304 ? -44.335 9.024   55.994  1.00 45.54 ? 304  LYS B CD    1 
ATOM   6439 C  CE    . LYS B 1 304 ? -44.848 9.014   54.568  1.00 51.68 ? 304  LYS B CE    1 
ATOM   6440 N  NZ    . LYS B 1 304 ? -46.093 9.804   54.452  1.00 55.77 ? 304  LYS B NZ    1 
ATOM   6441 N  N     . THR B 1 305 ? -41.427 6.237   60.110  1.00 21.37 ? 305  THR B N     1 
ATOM   6442 C  CA    . THR B 1 305 ? -40.665 6.078   61.376  1.00 21.05 ? 305  THR B CA    1 
ATOM   6443 C  C     . THR B 1 305 ? -39.357 5.316   61.082  1.00 22.14 ? 305  THR B C     1 
ATOM   6444 O  O     . THR B 1 305 ? -38.296 5.783   61.498  1.00 20.62 ? 305  THR B O     1 
ATOM   6445 C  CB    . THR B 1 305 ? -41.528 5.407   62.444  1.00 21.57 ? 305  THR B CB    1 
ATOM   6446 O  OG1   . THR B 1 305 ? -42.730 6.173   62.591  1.00 20.33 ? 305  THR B OG1   1 
ATOM   6447 C  CG2   . THR B 1 305 ? -40.805 5.287   63.766  1.00 21.50 ? 305  THR B CG2   1 
ATOM   6448 N  N     . MET B 1 306 ? -39.422 4.199   60.347  1.00 22.37 ? 306  MET B N     1 
ATOM   6449 C  CA    . MET B 1 306 ? -38.236 3.363   60.021  1.00 23.82 ? 306  MET B CA    1 
ATOM   6450 C  C     . MET B 1 306 ? -37.232 4.186   59.214  1.00 21.40 ? 306  MET B C     1 
ATOM   6451 O  O     . MET B 1 306 ? -36.035 4.129   59.547  1.00 20.23 ? 306  MET B O     1 
ATOM   6452 C  CB    . MET B 1 306 ? -38.613 2.098   59.231  1.00 24.03 ? 306  MET B CB    1 
ATOM   6453 C  CG    . MET B 1 306 ? -39.417 1.124   60.055  1.00 23.43 ? 306  MET B CG    1 
ATOM   6454 S  SD    . MET B 1 306 ? -40.100 -0.184  59.004  1.00 27.58 ? 306  MET B SD    1 
ATOM   6455 C  CE    . MET B 1 306 ? -38.576 -0.862  58.356  1.00 26.78 ? 306  MET B CE    1 
ATOM   6456 N  N     . MET B 1 307 ? -37.702 4.966   58.237  1.00 22.05 ? 307  MET B N     1 
ATOM   6457 C  CA    . MET B 1 307 ? -36.821 5.791   57.361  1.00 22.43 ? 307  MET B CA    1 
ATOM   6458 C  C     . MET B 1 307 ? -36.088 6.811   58.237  1.00 21.63 ? 307  MET B C     1 
ATOM   6459 O  O     . MET B 1 307 ? -34.883 6.937   58.106  1.00 21.01 ? 307  MET B O     1 
ATOM   6460 C  CB    . MET B 1 307 ? -37.611 6.533   56.274  1.00 23.72 ? 307  MET B CB    1 
ATOM   6461 C  CG    . MET B 1 307 ? -38.002 5.656   55.117  1.00 26.61 ? 307  MET B CG    1 
ATOM   6462 S  SD    . MET B 1 307 ? -39.246 6.463   54.064  1.00 29.26 ? 307  MET B SD    1 
ATOM   6463 C  CE    . MET B 1 307 ? -38.330 7.932   53.613  1.00 27.03 ? 307  MET B CE    1 
ATOM   6464 N  N     . ALA B 1 308 ? -36.808 7.495   59.126  1.00 21.63 ? 308  ALA B N     1 
ATOM   6465 C  CA    . ALA B 1 308 ? -36.228 8.544   59.993  1.00 21.72 ? 308  ALA B CA    1 
ATOM   6466 C  C     . ALA B 1 308 ? -35.292 7.880   61.015  1.00 22.54 ? 308  ALA B C     1 
ATOM   6467 O  O     . ALA B 1 308 ? -34.266 8.450   61.325  1.00 22.16 ? 308  ALA B O     1 
ATOM   6468 C  CB    . ALA B 1 308 ? -37.332 9.346   60.647  1.00 19.26 ? 308  ALA B CB    1 
ATOM   6469 N  N     . ASP B 1 309 ? -35.675 6.730   61.578  1.00 23.68 ? 309  ASP B N     1 
ATOM   6470 C  CA    . ASP B 1 309 ? -34.869 6.061   62.623  1.00 22.57 ? 309  ASP B CA    1 
ATOM   6471 C  C     . ASP B 1 309 ? -33.532 5.593   62.016  1.00 25.08 ? 309  ASP B C     1 
ATOM   6472 O  O     . ASP B 1 309 ? -32.513 5.712   62.734  1.00 23.11 ? 309  ASP B O     1 
ATOM   6473 C  CB    . ASP B 1 309 ? -35.639 4.893   63.262  1.00 23.59 ? 309  ASP B CB    1 
ATOM   6474 C  CG    . ASP B 1 309 ? -34.917 4.211   64.422  1.00 21.99 ? 309  ASP B CG    1 
ATOM   6475 O  OD1   . ASP B 1 309 ? -34.218 4.934   65.181  1.00 23.98 ? 309  ASP B OD1   1 
ATOM   6476 O  OD2   . ASP B 1 309 ? -35.053 2.978   64.556  1.00 21.30 ? 309  ASP B OD2   1 
ATOM   6477 N  N     . LEU B 1 310 ? -33.525 5.049   60.783  1.00 23.22 ? 310  LEU B N     1 
ATOM   6478 C  CA    . LEU B 1 310 ? -32.334 4.333   60.221  1.00 25.78 ? 310  LEU B CA    1 
ATOM   6479 C  C     . LEU B 1 310 ? -31.580 5.143   59.158  1.00 24.08 ? 310  LEU B C     1 
ATOM   6480 O  O     . LEU B 1 310 ? -30.575 4.625   58.695  1.00 26.81 ? 310  LEU B O     1 
ATOM   6481 C  CB    . LEU B 1 310 ? -32.796 3.002   59.621  1.00 25.99 ? 310  LEU B CB    1 
ATOM   6482 C  CG    . LEU B 1 310 ? -33.475 2.067   60.623  1.00 28.90 ? 310  LEU B CG    1 
ATOM   6483 C  CD1   . LEU B 1 310 ? -34.038 0.820   59.934  1.00 28.00 ? 310  LEU B CD1   1 
ATOM   6484 C  CD2   . LEU B 1 310 ? -32.515 1.697   61.763  1.00 29.40 ? 310  LEU B CD2   1 
ATOM   6485 N  N     . ASP B 1 311 ? -32.036 6.343   58.781  1.00 25.92 ? 311  ASP B N     1 
ATOM   6486 C  CA    . ASP B 1 311 ? -31.474 7.116   57.638  1.00 26.63 ? 311  ASP B CA    1 
ATOM   6487 C  C     . ASP B 1 311 ? -31.508 6.249   56.370  1.00 24.93 ? 311  ASP B C     1 
ATOM   6488 O  O     . ASP B 1 311 ? -30.475 6.118   55.704  1.00 24.17 ? 311  ASP B O     1 
ATOM   6489 C  CB    . ASP B 1 311 ? -30.073 7.624   57.981  1.00 28.27 ? 311  ASP B CB    1 
ATOM   6490 C  CG    . ASP B 1 311 ? -30.088 8.567   59.172  1.00 29.75 ? 311  ASP B CG    1 
ATOM   6491 O  OD1   . ASP B 1 311 ? -30.950 9.464   59.187  1.00 34.70 ? 311  ASP B OD1   1 
ATOM   6492 O  OD2   . ASP B 1 311 ? -29.267 8.370   60.082  1.00 30.77 ? 311  ASP B OD2   1 
ATOM   6493 N  N     . LEU B 1 312 ? -32.665 5.662   56.076  1.00 23.77 ? 312  LEU B N     1 
ATOM   6494 C  CA    . LEU B 1 312 ? -32.914 4.879   54.844  1.00 24.69 ? 312  LEU B CA    1 
ATOM   6495 C  C     . LEU B 1 312 ? -34.059 5.543   54.092  1.00 24.70 ? 312  LEU B C     1 
ATOM   6496 O  O     . LEU B 1 312 ? -34.878 6.244   54.734  1.00 23.06 ? 312  LEU B O     1 
ATOM   6497 C  CB    . LEU B 1 312 ? -33.271 3.427   55.206  1.00 24.70 ? 312  LEU B CB    1 
ATOM   6498 C  CG    . LEU B 1 312 ? -32.150 2.625   55.868  1.00 25.80 ? 312  LEU B CG    1 
ATOM   6499 C  CD1   . LEU B 1 312 ? -32.628 1.240   56.298  1.00 24.63 ? 312  LEU B CD1   1 
ATOM   6500 C  CD2   . LEU B 1 312 ? -30.964 2.506   54.931  1.00 28.32 ? 312  LEU B CD2   1 
ATOM   6501 N  N     . GLY B 1 313 ? -34.145 5.297   52.780  1.00 23.07 ? 313  GLY B N     1 
ATOM   6502 C  CA    . GLY B 1 313 ? -35.286 5.763   51.977  1.00 22.60 ? 313  GLY B CA    1 
ATOM   6503 C  C     . GLY B 1 313 ? -36.180 4.598   51.644  1.00 20.81 ? 313  GLY B C     1 
ATOM   6504 O  O     . GLY B 1 313 ? -35.893 3.504   52.119  1.00 20.04 ? 313  GLY B O     1 
ATOM   6505 N  N     . MET B 1 314 ? -37.231 4.822   50.870  1.00 20.66 ? 314  MET B N     1 
ATOM   6506 C  CA    . MET B 1 314 ? -38.058 3.717   50.335  1.00 23.01 ? 314  MET B CA    1 
ATOM   6507 C  C     . MET B 1 314 ? -37.201 2.872   49.375  1.00 22.71 ? 314  MET B C     1 
ATOM   6508 O  O     . MET B 1 314 ? -37.477 1.682   49.265  1.00 21.75 ? 314  MET B O     1 
ATOM   6509 C  CB    . MET B 1 314 ? -39.300 4.256   49.631  1.00 24.55 ? 314  MET B CB    1 
ATOM   6510 C  CG    . MET B 1 314 ? -40.277 4.915   50.585  1.00 27.53 ? 314  MET B CG    1 
ATOM   6511 S  SD    . MET B 1 314 ? -40.805 3.794   51.924  1.00 31.00 ? 314  MET B SD    1 
ATOM   6512 C  CE    . MET B 1 314 ? -41.823 2.657   50.995  1.00 31.55 ? 314  MET B CE    1 
ATOM   6513 N  N     . TRP B 1 315 ? -36.196 3.476   48.736  1.00 21.16 ? 315  TRP B N     1 
ATOM   6514 C  CA    . TRP B 1 315 ? -35.248 2.802   47.800  1.00 23.74 ? 315  TRP B CA    1 
ATOM   6515 C  C     . TRP B 1 315 ? -33.831 3.202   48.205  1.00 22.83 ? 315  TRP B C     1 
ATOM   6516 O  O     . TRP B 1 315 ? -33.609 4.394   48.486  1.00 22.90 ? 315  TRP B O     1 
ATOM   6517 C  CB    . TRP B 1 315 ? -35.543 3.134   46.316  1.00 21.80 ? 315  TRP B CB    1 
ATOM   6518 C  CG    . TRP B 1 315 ? -36.855 2.595   45.834  1.00 21.54 ? 315  TRP B CG    1 
ATOM   6519 C  CD1   . TRP B 1 315 ? -37.975 3.304   45.525  1.00 21.17 ? 315  TRP B CD1   1 
ATOM   6520 C  CD2   . TRP B 1 315 ? -37.189 1.206   45.616  1.00 22.44 ? 315  TRP B CD2   1 
ATOM   6521 N  NE1   . TRP B 1 315 ? -38.987 2.453   45.171  1.00 21.98 ? 315  TRP B NE1   1 
ATOM   6522 C  CE2   . TRP B 1 315 ? -38.530 1.163   45.198  1.00 22.43 ? 315  TRP B CE2   1 
ATOM   6523 C  CE3   . TRP B 1 315 ? -36.492 0.005   45.747  1.00 22.45 ? 315  TRP B CE3   1 
ATOM   6524 C  CZ2   . TRP B 1 315 ? -39.172 -0.028  44.872  1.00 24.12 ? 315  TRP B CZ2   1 
ATOM   6525 C  CZ3   . TRP B 1 315 ? -37.119 -1.170  45.416  1.00 22.56 ? 315  TRP B CZ3   1 
ATOM   6526 C  CH2   . TRP B 1 315 ? -38.445 -1.187  44.985  1.00 23.61 ? 315  TRP B CH2   1 
ATOM   6527 N  N     . ASN B 1 316 ? -32.916 2.235   48.246  1.00 22.47 ? 316  ASN B N     1 
ATOM   6528 C  CA    . ASN B 1 316 ? -31.543 2.446   48.758  1.00 23.15 ? 316  ASN B CA    1 
ATOM   6529 C  C     . ASN B 1 316 ? -30.541 1.879   47.754  1.00 22.68 ? 316  ASN B C     1 
ATOM   6530 O  O     . ASN B 1 316 ? -30.417 0.654   47.636  1.00 23.58 ? 316  ASN B O     1 
ATOM   6531 C  CB    . ASN B 1 316 ? -31.392 1.848   50.165  1.00 24.30 ? 316  ASN B CB    1 
ATOM   6532 C  CG    . ASN B 1 316 ? -32.430 2.410   51.117  1.00 24.68 ? 316  ASN B CG    1 
ATOM   6533 O  OD1   . ASN B 1 316 ? -32.299 3.542   51.615  1.00 25.97 ? 316  ASN B OD1   1 
ATOM   6534 N  ND2   . ASN B 1 316 ? -33.497 1.658   51.318  1.00 23.22 ? 316  ASN B ND2   1 
ATOM   6535 N  N     . PHE B 1 317 ? -29.803 2.754   47.089  1.00 24.87 ? 317  PHE B N     1 
ATOM   6536 C  CA    . PHE B 1 317 ? -28.872 2.376   46.005  1.00 23.63 ? 317  PHE B CA    1 
ATOM   6537 C  C     . PHE B 1 317 ? -27.471 2.309   46.592  1.00 23.63 ? 317  PHE B C     1 
ATOM   6538 O  O     . PHE B 1 317 ? -26.928 3.355   46.930  1.00 24.69 ? 317  PHE B O     1 
ATOM   6539 C  CB    . PHE B 1 317 ? -29.008 3.329   44.807  1.00 24.92 ? 317  PHE B CB    1 
ATOM   6540 C  CG    . PHE B 1 317 ? -27.878 3.256   43.813  1.00 23.22 ? 317  PHE B CG    1 
ATOM   6541 C  CD1   . PHE B 1 317 ? -27.236 2.054   43.555  1.00 22.66 ? 317  PHE B CD1   1 
ATOM   6542 C  CD2   . PHE B 1 317 ? -27.415 4.402   43.186  1.00 23.95 ? 317  PHE B CD2   1 
ATOM   6543 C  CE1   . PHE B 1 317 ? -26.156 2.007   42.685  1.00 23.60 ? 317  PHE B CE1   1 
ATOM   6544 C  CE2   . PHE B 1 317 ? -26.343 4.352   42.306  1.00 23.38 ? 317  PHE B CE2   1 
ATOM   6545 C  CZ    . PHE B 1 317 ? -25.721 3.151   42.049  1.00 23.42 ? 317  PHE B CZ    1 
ATOM   6546 N  N     . CYS B 1 318 ? -26.921 1.099   46.706  1.00 24.90 ? 318  CYS B N     1 
ATOM   6547 C  CA    . CYS B 1 318 ? -25.507 0.846   47.088  1.00 28.66 ? 318  CYS B CA    1 
ATOM   6548 C  C     . CYS B 1 318 ? -24.682 0.517   45.840  1.00 25.58 ? 318  CYS B C     1 
ATOM   6549 O  O     . CYS B 1 318 ? -25.135 -0.279  45.019  1.00 27.50 ? 318  CYS B O     1 
ATOM   6550 C  CB    . CYS B 1 318 ? -25.394 -0.288  48.095  1.00 34.59 ? 318  CYS B CB    1 
ATOM   6551 S  SG    . CYS B 1 318 ? -25.887 0.204   49.769  1.00 39.39 ? 318  CYS B SG    1 
ATOM   6552 N  N     . GLY B 1 319 ? -23.548 1.188   45.699  1.00 24.35 ? 319  GLY B N     1 
ATOM   6553 C  CA    . GLY B 1 319 ? -22.550 0.991   44.630  1.00 24.93 ? 319  GLY B CA    1 
ATOM   6554 C  C     . GLY B 1 319 ? -21.194 1.344   45.194  1.00 25.72 ? 319  GLY B C     1 
ATOM   6555 O  O     . GLY B 1 319 ? -21.137 1.785   46.367  1.00 25.49 ? 319  GLY B O     1 
ATOM   6556 N  N     . ALA B 1 320 ? -20.122 1.094   44.452  1.00 24.27 ? 320  ALA B N     1 
ATOM   6557 C  CA    . ALA B 1 320 ? -18.771 1.466   44.892  1.00 22.88 ? 320  ALA B CA    1 
ATOM   6558 C  C     . ALA B 1 320 ? -17.991 1.951   43.688  1.00 22.23 ? 320  ALA B C     1 
ATOM   6559 O  O     . ALA B 1 320 ? -18.267 1.502   42.603  1.00 22.88 ? 320  ALA B O     1 
ATOM   6560 C  CB    . ALA B 1 320 ? -18.107 0.318   45.600  1.00 22.11 ? 320  ALA B CB    1 
ATOM   6561 N  N     . LEU B 1 321 ? -17.109 2.906   43.938  1.00 22.57 ? 321  LEU B N     1 
ATOM   6562 C  CA    . LEU B 1 321 ? -16.072 3.396   43.012  1.00 22.07 ? 321  LEU B CA    1 
ATOM   6563 C  C     . LEU B 1 321 ? -14.796 2.598   43.278  1.00 22.88 ? 321  LEU B C     1 
ATOM   6564 O  O     . LEU B 1 321 ? -14.525 2.282   44.469  1.00 19.49 ? 321  LEU B O     1 
ATOM   6565 C  CB    . LEU B 1 321 ? -15.839 4.881   43.300  1.00 25.00 ? 321  LEU B CB    1 
ATOM   6566 C  CG    . LEU B 1 321 ? -17.103 5.733   43.401  1.00 25.78 ? 321  LEU B CG    1 
ATOM   6567 C  CD1   . LEU B 1 321 ? -16.775 7.065   44.034  1.00 26.39 ? 321  LEU B CD1   1 
ATOM   6568 C  CD2   . LEU B 1 321 ? -17.749 5.927   42.037  1.00 28.74 ? 321  LEU B CD2   1 
ATOM   6569 N  N     . TYR B 1 322 ? -14.064 2.259   42.215  1.00 22.10 ? 322  TYR B N     1 
ATOM   6570 C  CA    . TYR B 1 322 ? -12.801 1.495   42.296  1.00 21.50 ? 322  TYR B CA    1 
ATOM   6571 C  C     . TYR B 1 322 ? -11.734 2.172   41.467  1.00 24.30 ? 322  TYR B C     1 
ATOM   6572 O  O     . TYR B 1 322 ? -12.022 2.615   40.342  1.00 23.07 ? 322  TYR B O     1 
ATOM   6573 C  CB    . TYR B 1 322 ? -12.994 0.073   41.772  1.00 21.48 ? 322  TYR B CB    1 
ATOM   6574 C  CG    . TYR B 1 322 ? -14.108 -0.692  42.437  1.00 18.44 ? 322  TYR B CG    1 
ATOM   6575 C  CD1   . TYR B 1 322 ? -15.410 -0.560  42.011  1.00 17.77 ? 322  TYR B CD1   1 
ATOM   6576 C  CD2   . TYR B 1 322 ? -13.848 -1.575  43.475  1.00 18.88 ? 322  TYR B CD2   1 
ATOM   6577 C  CE1   . TYR B 1 322 ? -16.444 -1.273  42.599  1.00 18.41 ? 322  TYR B CE1   1 
ATOM   6578 C  CE2   . TYR B 1 322 ? -14.871 -2.263  44.100  1.00 18.33 ? 322  TYR B CE2   1 
ATOM   6579 C  CZ    . TYR B 1 322 ? -16.171 -2.127  43.656  1.00 18.46 ? 322  TYR B CZ    1 
ATOM   6580 O  OH    . TYR B 1 322 ? -17.171 -2.860  44.242  1.00 19.84 ? 322  TYR B OH    1 
ATOM   6581 N  N     . GLY B 1 323 ? -10.522 2.226   42.003  1.00 26.69 ? 323  GLY B N     1 
ATOM   6582 C  CA    . GLY B 1 323 ? -9.365  2.694   41.229  1.00 30.02 ? 323  GLY B CA    1 
ATOM   6583 C  C     . GLY B 1 323 ? -8.726  3.936   41.828  1.00 29.76 ? 323  GLY B C     1 
ATOM   6584 O  O     . GLY B 1 323 ? -8.981  4.300   42.981  1.00 27.69 ? 323  GLY B O     1 
ATOM   6585 N  N     . PRO B 1 324 ? -7.822  4.587   41.062  1.00 36.70 ? 324  PRO B N     1 
ATOM   6586 C  CA    . PRO B 1 324 ? -7.077  5.738   41.596  1.00 35.75 ? 324  PRO B CA    1 
ATOM   6587 C  C     . PRO B 1 324 ? -8.046  6.891   41.870  1.00 33.02 ? 324  PRO B C     1 
ATOM   6588 O  O     . PRO B 1 324 ? -9.070  7.020   41.196  1.00 31.88 ? 324  PRO B O     1 
ATOM   6589 C  CB    . PRO B 1 324 ? -6.020  6.025   40.522  1.00 37.51 ? 324  PRO B CB    1 
ATOM   6590 C  CG    . PRO B 1 324 ? -6.517  5.338   39.250  1.00 37.30 ? 324  PRO B CG    1 
ATOM   6591 C  CD    . PRO B 1 324 ? -7.458  4.224   39.676  1.00 34.93 ? 324  PRO B CD    1 
ATOM   6592 N  N     . PRO B 1 325 ? -7.811  7.712   42.915  1.00 33.78 ? 325  PRO B N     1 
ATOM   6593 C  CA    . PRO B 1 325 ? -8.670  8.870   43.210  1.00 33.39 ? 325  PRO B CA    1 
ATOM   6594 C  C     . PRO B 1 325 ? -9.177  9.718   42.039  1.00 31.13 ? 325  PRO B C     1 
ATOM   6595 O  O     . PRO B 1 325 ? -10.356 10.033  41.987  1.00 33.14 ? 325  PRO B O     1 
ATOM   6596 C  CB    . PRO B 1 325 ? -7.755  9.665   44.148  1.00 33.24 ? 325  PRO B CB    1 
ATOM   6597 C  CG    . PRO B 1 325 ? -7.127  8.568   44.973  1.00 34.87 ? 325  PRO B CG    1 
ATOM   6598 C  CD    . PRO B 1 325 ? -6.780  7.509   43.948  1.00 34.56 ? 325  PRO B CD    1 
ATOM   6599 N  N     . PRO B 1 326 ? -8.351  10.133  41.056  1.00 31.01 ? 326  PRO B N     1 
ATOM   6600 C  CA    . PRO B 1 326 ? -8.841  10.988  39.982  1.00 33.50 ? 326  PRO B CA    1 
ATOM   6601 C  C     . PRO B 1 326 ? -9.869  10.252  39.116  1.00 33.55 ? 326  PRO B C     1 
ATOM   6602 O  O     . PRO B 1 326 ? -10.738 10.892  38.590  1.00 38.37 ? 326  PRO B O     1 
ATOM   6603 C  CB    . PRO B 1 326 ? -7.592  11.358  39.166  1.00 32.80 ? 326  PRO B CB    1 
ATOM   6604 C  CG    . PRO B 1 326 ? -6.439  11.034  40.083  1.00 31.71 ? 326  PRO B CG    1 
ATOM   6605 C  CD    . PRO B 1 326 ? -6.916  9.876   40.927  1.00 33.95 ? 326  PRO B CD    1 
ATOM   6606 N  N     . VAL B 1 327 ? -9.771  8.930   38.997  1.00 28.70 ? 327  VAL B N     1 
ATOM   6607 C  CA    . VAL B 1 327 ? -10.802 8.169   38.249  1.00 29.57 ? 327  VAL B CA    1 
ATOM   6608 C  C     . VAL B 1 327 ? -12.080 8.148   39.097  1.00 26.86 ? 327  VAL B C     1 
ATOM   6609 O  O     . VAL B 1 327 ? -13.140 8.446   38.558  1.00 26.25 ? 327  VAL B O     1 
ATOM   6610 C  CB    . VAL B 1 327 ? -10.331 6.748   37.894  1.00 30.18 ? 327  VAL B CB    1 
ATOM   6611 C  CG1   . VAL B 1 327 ? -11.493 5.930   37.344  1.00 28.88 ? 327  VAL B CG1   1 
ATOM   6612 C  CG2   . VAL B 1 327 ? -9.162  6.783   36.921  1.00 29.72 ? 327  VAL B CG2   1 
ATOM   6613 N  N     . MET B 1 328 ? -11.975 7.791   40.375  1.00 26.54 ? 328  MET B N     1 
ATOM   6614 C  CA    . MET B 1 328 ? -13.158 7.690   41.279  1.00 25.69 ? 328  MET B CA    1 
ATOM   6615 C  C     . MET B 1 328 ? -13.879 9.044   41.339  1.00 23.58 ? 328  MET B C     1 
ATOM   6616 O  O     . MET B 1 328 ? -15.113 9.082   41.188  1.00 24.04 ? 328  MET B O     1 
ATOM   6617 C  CB    . MET B 1 328 ? -12.733 7.215   42.667  1.00 26.22 ? 328  MET B CB    1 
ATOM   6618 C  CG    . MET B 1 328 ? -12.254 5.772   42.674  1.00 27.57 ? 328  MET B CG    1 
ATOM   6619 S  SD    . MET B 1 328 ? -12.164 5.049   44.319  1.00 28.33 ? 328  MET B SD    1 
ATOM   6620 C  CE    . MET B 1 328 ? -10.957 6.136   45.080  1.00 30.56 ? 328  MET B CE    1 
ATOM   6621 N  N     . ASP B 1 329 ? -13.152 10.145  41.443  1.00 26.18 ? 329  ASP B N     1 
ATOM   6622 C  CA    . ASP B 1 329 ? -13.787 11.493  41.448  1.00 26.74 ? 329  ASP B CA    1 
ATOM   6623 C  C     . ASP B 1 329 ? -14.557 11.715  40.150  1.00 28.01 ? 329  ASP B C     1 
ATOM   6624 O  O     . ASP B 1 329 ? -15.713 12.191  40.234  1.00 27.41 ? 329  ASP B O     1 
ATOM   6625 C  CB    . ASP B 1 329 ? -12.750 12.588  41.630  1.00 29.16 ? 329  ASP B CB    1 
ATOM   6626 C  CG    . ASP B 1 329 ? -12.137 12.572  43.012  1.00 33.27 ? 329  ASP B CG    1 
ATOM   6627 O  OD1   . ASP B 1 329 ? -12.720 11.933  43.922  1.00 36.80 ? 329  ASP B OD1   1 
ATOM   6628 O  OD2   . ASP B 1 329 ? -11.034 13.122  43.139  1.00 44.17 ? 329  ASP B OD2   1 
ATOM   6629 N  N     . THR B 1 330 ? -13.961 11.401  38.984  1.00 26.52 ? 330  THR B N     1 
ATOM   6630 C  CA    . THR B 1 330 ? -14.637 11.639  37.687  1.00 26.31 ? 330  THR B CA    1 
ATOM   6631 C  C     . THR B 1 330 ? -15.936 10.836  37.620  1.00 25.53 ? 330  THR B C     1 
ATOM   6632 O  O     . THR B 1 330 ? -16.962 11.432  37.210  1.00 26.51 ? 330  THR B O     1 
ATOM   6633 C  CB    . THR B 1 330 ? -13.765 11.339  36.473  1.00 29.34 ? 330  THR B CB    1 
ATOM   6634 O  OG1   . THR B 1 330 ? -12.526 11.991  36.689  1.00 32.50 ? 330  THR B OG1   1 
ATOM   6635 C  CG2   . THR B 1 330 ? -14.379 11.821  35.179  1.00 31.69 ? 330  THR B CG2   1 
ATOM   6636 N  N     . LEU B 1 331 ? -15.919 9.547   37.977  1.00 25.88 ? 331  LEU B N     1 
ATOM   6637 C  CA    . LEU B 1 331 ? -17.142 8.682   37.935  1.00 24.75 ? 331  LEU B CA    1 
ATOM   6638 C  C     . LEU B 1 331 ? -18.136 9.194   38.984  1.00 22.95 ? 331  LEU B C     1 
ATOM   6639 O  O     . LEU B 1 331 ? -19.336 9.210   38.695  1.00 27.07 ? 331  LEU B O     1 
ATOM   6640 C  CB    . LEU B 1 331 ? -16.793 7.210   38.197  1.00 26.41 ? 331  LEU B CB    1 
ATOM   6641 C  CG    . LEU B 1 331 ? -15.662 6.628   37.343  1.00 28.07 ? 331  LEU B CG    1 
ATOM   6642 C  CD1   . LEU B 1 331 ? -15.239 5.253   37.853  1.00 27.85 ? 331  LEU B CD1   1 
ATOM   6643 C  CD2   . LEU B 1 331 ? -16.076 6.567   35.883  1.00 28.33 ? 331  LEU B CD2   1 
ATOM   6644 N  N     . TRP B 1 332 ? -17.663 9.592   40.163  1.00 23.59 ? 332  TRP B N     1 
ATOM   6645 C  CA    . TRP B 1 332 ? -18.558 10.110  41.231  1.00 26.24 ? 332  TRP B CA    1 
ATOM   6646 C  C     . TRP B 1 332 ? -19.294 11.352  40.720  1.00 25.46 ? 332  TRP B C     1 
ATOM   6647 O  O     . TRP B 1 332 ? -20.520 11.423  40.865  1.00 25.51 ? 332  TRP B O     1 
ATOM   6648 C  CB    . TRP B 1 332 ? -17.821 10.395  42.545  1.00 29.01 ? 332  TRP B CB    1 
ATOM   6649 C  CG    . TRP B 1 332 ? -18.804 10.841  43.586  1.00 30.46 ? 332  TRP B CG    1 
ATOM   6650 C  CD1   . TRP B 1 332 ? -18.848 12.057  44.203  1.00 29.78 ? 332  TRP B CD1   1 
ATOM   6651 C  CD2   . TRP B 1 332 ? -19.958 10.111  44.042  1.00 28.29 ? 332  TRP B CD2   1 
ATOM   6652 N  NE1   . TRP B 1 332 ? -19.925 12.115  45.047  1.00 33.54 ? 332  TRP B NE1   1 
ATOM   6653 C  CE2   . TRP B 1 332 ? -20.630 10.940  44.967  1.00 31.18 ? 332  TRP B CE2   1 
ATOM   6654 C  CE3   . TRP B 1 332 ? -20.485 8.844   43.780  1.00 30.82 ? 332  TRP B CE3   1 
ATOM   6655 C  CZ2   . TRP B 1 332 ? -21.790 10.535  45.628  1.00 29.50 ? 332  TRP B CZ2   1 
ATOM   6656 C  CZ3   . TRP B 1 332 ? -21.640 8.442   44.424  1.00 31.40 ? 332  TRP B CZ3   1 
ATOM   6657 C  CH2   . TRP B 1 332 ? -22.288 9.284   45.332  1.00 31.41 ? 332  TRP B CH2   1 
ATOM   6658 N  N     . THR B 1 333 ? -18.611 12.262  40.033  1.00 25.70 ? 333  THR B N     1 
ATOM   6659 C  CA    . THR B 1 333 ? -19.278 13.477  39.505  1.00 24.92 ? 333  THR B CA    1 
ATOM   6660 C  C     . THR B 1 333 ? -20.440 13.064  38.617  1.00 25.51 ? 333  THR B C     1 
ATOM   6661 O  O     . THR B 1 333 ? -21.512 13.647  38.785  1.00 28.96 ? 333  THR B O     1 
ATOM   6662 C  CB    . THR B 1 333 ? -18.283 14.411  38.822  1.00 24.36 ? 333  THR B CB    1 
ATOM   6663 O  OG1   . THR B 1 333 ? -17.418 14.773  39.891  1.00 24.41 ? 333  THR B OG1   1 
ATOM   6664 C  CG2   . THR B 1 333 ? -18.934 15.616  38.184  1.00 26.35 ? 333  THR B CG2   1 
ATOM   6665 N  N     . ALA B 1 334 ? -20.254 12.105  37.708  1.00 25.20 ? 334  ALA B N     1 
ATOM   6666 C  CA    . ALA B 1 334 ? -21.305 11.673  36.759  1.00 22.86 ? 334  ALA B CA    1 
ATOM   6667 C  C     . ALA B 1 334 ? -22.444 10.976  37.502  1.00 23.14 ? 334  ALA B C     1 
ATOM   6668 O  O     . ALA B 1 334 ? -23.618 11.130  37.097  1.00 26.02 ? 334  ALA B O     1 
ATOM   6669 C  CB    . ALA B 1 334 ? -20.731 10.742  35.716  1.00 23.49 ? 334  ALA B CB    1 
ATOM   6670 N  N     . ILE B 1 335 ? -22.119 10.140  38.481  1.00 22.75 ? 335  ILE B N     1 
ATOM   6671 C  CA    . ILE B 1 335 ? -23.144 9.363   39.236  1.00 23.08 ? 335  ILE B CA    1 
ATOM   6672 C  C     . ILE B 1 335 ? -23.967 10.356  40.066  1.00 22.28 ? 335  ILE B C     1 
ATOM   6673 O  O     . ILE B 1 335 ? -25.188 10.335  39.964  1.00 22.91 ? 335  ILE B O     1 
ATOM   6674 C  CB    . ILE B 1 335 ? -22.498 8.253   40.102  1.00 22.51 ? 335  ILE B CB    1 
ATOM   6675 C  CG1   . ILE B 1 335 ? -21.851 7.184   39.216  1.00 23.90 ? 335  ILE B CG1   1 
ATOM   6676 C  CG2   . ILE B 1 335 ? -23.519 7.629   41.035  1.00 23.31 ? 335  ILE B CG2   1 
ATOM   6677 C  CD1   . ILE B 1 335 ? -20.921 6.267   39.952  1.00 24.25 ? 335  ILE B CD1   1 
ATOM   6678 N  N     . ARG B 1 336 ? -23.297 11.155  40.878  1.00 28.07 ? 336  ARG B N     1 
ATOM   6679 C  CA    . ARG B 1 336 ? -23.936 12.150  41.781  1.00 31.95 ? 336  ARG B CA    1 
ATOM   6680 C  C     . ARG B 1 336 ? -24.868 13.044  40.960  1.00 30.14 ? 336  ARG B C     1 
ATOM   6681 O  O     . ARG B 1 336 ? -26.065 13.131  41.286  1.00 31.75 ? 336  ARG B O     1 
ATOM   6682 C  CB    . ARG B 1 336 ? -22.869 12.969  42.509  1.00 34.82 ? 336  ARG B CB    1 
ATOM   6683 C  CG    . ARG B 1 336 ? -23.400 13.631  43.770  1.00 41.24 ? 336  ARG B CG    1 
ATOM   6684 C  CD    . ARG B 1 336 ? -22.567 14.780  44.283  1.00 48.59 ? 336  ARG B CD    1 
ATOM   6685 N  NE    . ARG B 1 336 ? -23.488 15.620  45.037  1.00 61.89 ? 336  ARG B NE    1 
ATOM   6686 C  CZ    . ARG B 1 336 ? -23.728 15.530  46.344  1.00 63.39 ? 336  ARG B CZ    1 
ATOM   6687 N  NH1   . ARG B 1 336 ? -23.078 14.650  47.093  1.00 68.26 ? 336  ARG B NH1   1 
ATOM   6688 N  NH2   . ARG B 1 336 ? -24.621 16.335  46.897  1.00 58.42 ? 336  ARG B NH2   1 
ATOM   6689 N  N     . ASP B 1 337 ? -24.351 13.652  39.899  1.00 29.58 ? 337  ASP B N     1 
ATOM   6690 C  CA    . ASP B 1 337 ? -25.130 14.610  39.074  1.00 29.08 ? 337  ASP B CA    1 
ATOM   6691 C  C     . ASP B 1 337 ? -26.312 13.893  38.435  1.00 27.81 ? 337  ASP B C     1 
ATOM   6692 O  O     . ASP B 1 337 ? -27.309 14.581  38.201  1.00 28.65 ? 337  ASP B O     1 
ATOM   6693 C  CB    . ASP B 1 337 ? -24.261 15.298  38.019  1.00 32.20 ? 337  ASP B CB    1 
ATOM   6694 C  CG    . ASP B 1 337 ? -23.202 16.190  38.647  1.00 35.42 ? 337  ASP B CG    1 
ATOM   6695 O  OD1   . ASP B 1 337 ? -23.209 16.360  39.895  1.00 41.88 ? 337  ASP B OD1   1 
ATOM   6696 O  OD2   . ASP B 1 337 ? -22.367 16.671  37.907  1.00 41.06 ? 337  ASP B OD2   1 
ATOM   6697 N  N     . SER B 1 338 ? -26.252 12.572  38.195  1.00 26.38 ? 338  SER B N     1 
ATOM   6698 C  CA    . SER B 1 338 ? -27.417 11.855  37.598  1.00 27.44 ? 338  SER B CA    1 
ATOM   6699 C  C     . SER B 1 338 ? -28.634 11.853  38.542  1.00 26.40 ? 338  SER B C     1 
ATOM   6700 O  O     . SER B 1 338 ? -29.746 11.678  38.042  1.00 25.88 ? 338  SER B O     1 
ATOM   6701 C  CB    . SER B 1 338 ? -27.067 10.441  37.159  1.00 29.51 ? 338  SER B CB    1 
ATOM   6702 O  OG    . SER B 1 338 ? -25.960 10.447  36.280  1.00 26.53 ? 338  SER B OG    1 
ATOM   6703 N  N     . PHE B 1 339 ? -28.437 11.996  39.860  1.00 27.52 ? 339  PHE B N     1 
ATOM   6704 C  CA    . PHE B 1 339 ? -29.513 11.835  40.877  1.00 28.88 ? 339  PHE B CA    1 
ATOM   6705 C  C     . PHE B 1 339 ? -29.761 13.119  41.694  1.00 29.83 ? 339  PHE B C     1 
ATOM   6706 O  O     . PHE B 1 339 ? -30.773 13.137  42.393  1.00 27.91 ? 339  PHE B O     1 
ATOM   6707 C  CB    . PHE B 1 339 ? -29.149 10.654  41.785  1.00 26.37 ? 339  PHE B CB    1 
ATOM   6708 C  CG    . PHE B 1 339 ? -29.032 9.346   41.036  1.00 23.76 ? 339  PHE B CG    1 
ATOM   6709 C  CD1   . PHE B 1 339 ? -30.162 8.653   40.649  1.00 23.78 ? 339  PHE B CD1   1 
ATOM   6710 C  CD2   . PHE B 1 339 ? -27.795 8.821   40.692  1.00 24.71 ? 339  PHE B CD2   1 
ATOM   6711 C  CE1   . PHE B 1 339 ? -30.057 7.451   39.960  1.00 27.11 ? 339  PHE B CE1   1 
ATOM   6712 C  CE2   . PHE B 1 339 ? -27.691 7.614   40.005  1.00 24.55 ? 339  PHE B CE2   1 
ATOM   6713 C  CZ    . PHE B 1 339 ? -28.820 6.932   39.641  1.00 24.72 ? 339  PHE B CZ    1 
ATOM   6714 N  N     . ALA B 1 340 ? -28.897 14.135  41.603  1.00 30.46 ? 340  ALA B N     1 
ATOM   6715 C  CA    . ALA B 1 340 ? -28.858 15.316  42.504  1.00 33.93 ? 340  ALA B CA    1 
ATOM   6716 C  C     . ALA B 1 340 ? -30.204 16.065  42.510  1.00 34.89 ? 340  ALA B C     1 
ATOM   6717 O  O     . ALA B 1 340 ? -30.564 16.606  43.569  1.00 36.33 ? 340  ALA B O     1 
ATOM   6718 C  CB    . ALA B 1 340 ? -27.716 16.219  42.119  1.00 31.19 ? 340  ALA B CB    1 
ATOM   6719 N  N     . ASP B 1 341 ? -30.940 16.050  41.402  1.00 36.25 ? 341  ASP B N     1 
ATOM   6720 C  CA    . ASP B 1 341 ? -32.144 16.892  41.193  1.00 39.68 ? 341  ASP B CA    1 
ATOM   6721 C  C     . ASP B 1 341 ? -33.418 16.125  41.597  1.00 39.62 ? 341  ASP B C     1 
ATOM   6722 O  O     . ASP B 1 341 ? -34.511 16.677  41.442  1.00 36.51 ? 341  ASP B O     1 
ATOM   6723 C  CB    . ASP B 1 341 ? -32.156 17.458  39.759  1.00 40.99 ? 341  ASP B CB    1 
ATOM   6724 C  CG    . ASP B 1 341 ? -32.720 16.547  38.675  1.00 44.95 ? 341  ASP B CG    1 
ATOM   6725 O  OD1   . ASP B 1 341 ? -33.086 15.416  38.989  1.00 47.77 ? 341  ASP B OD1   1 
ATOM   6726 O  OD2   . ASP B 1 341 ? -32.781 16.978  37.516  1.00 48.71 ? 341  ASP B OD2   1 
ATOM   6727 N  N     . ILE B 1 342 ? -33.327 14.899  42.108  1.00 35.31 ? 342  ILE B N     1 
ATOM   6728 C  CA    . ILE B 1 342 ? -34.547 14.166  42.554  1.00 33.76 ? 342  ILE B CA    1 
ATOM   6729 C  C     . ILE B 1 342 ? -34.908 14.672  43.946  1.00 33.61 ? 342  ILE B C     1 
ATOM   6730 O  O     . ILE B 1 342 ? -34.065 14.664  44.836  1.00 31.97 ? 342  ILE B O     1 
ATOM   6731 C  CB    . ILE B 1 342 ? -34.331 12.646  42.542  1.00 32.71 ? 342  ILE B CB    1 
ATOM   6732 C  CG1   . ILE B 1 342 ? -33.966 12.141  41.144  1.00 31.86 ? 342  ILE B CG1   1 
ATOM   6733 C  CG2   . ILE B 1 342 ? -35.553 11.943  43.113  1.00 31.01 ? 342  ILE B CG2   1 
ATOM   6734 C  CD1   . ILE B 1 342 ? -33.340 10.753  41.148  1.00 31.34 ? 342  ILE B CD1   1 
ATOM   6735 N  N     . PRO B 1 343 ? -36.138 15.178  44.176  1.00 35.04 ? 343  PRO B N     1 
ATOM   6736 C  CA    . PRO B 1 343 ? -36.494 15.715  45.497  1.00 32.98 ? 343  PRO B CA    1 
ATOM   6737 C  C     . PRO B 1 343 ? -36.347 14.619  46.563  1.00 30.27 ? 343  PRO B C     1 
ATOM   6738 O  O     . PRO B 1 343 ? -36.857 13.528  46.378  1.00 28.10 ? 343  PRO B O     1 
ATOM   6739 C  CB    . PRO B 1 343 ? -37.956 16.180  45.365  1.00 30.25 ? 343  PRO B CB    1 
ATOM   6740 C  CG    . PRO B 1 343 ? -38.202 16.276  43.859  1.00 34.10 ? 343  PRO B CG    1 
ATOM   6741 C  CD    . PRO B 1 343 ? -37.225 15.318  43.192  1.00 34.13 ? 343  PRO B CD    1 
ATOM   6742 N  N     . GLY B 1 344 ? -35.641 14.918  47.645  1.00 29.61 ? 344  GLY B N     1 
ATOM   6743 C  CA    . GLY B 1 344 ? -35.551 14.019  48.805  1.00 29.82 ? 344  GLY B CA    1 
ATOM   6744 C  C     . GLY B 1 344 ? -34.355 13.089  48.735  1.00 29.14 ? 344  GLY B C     1 
ATOM   6745 O  O     . GLY B 1 344 ? -34.107 12.400  49.749  1.00 30.86 ? 344  GLY B O     1 
ATOM   6746 N  N     . VAL B 1 345 ? -33.593 13.119  47.639  1.00 28.37 ? 345  VAL B N     1 
ATOM   6747 C  CA    . VAL B 1 345 ? -32.386 12.252  47.453  1.00 30.07 ? 345  VAL B CA    1 
ATOM   6748 C  C     . VAL B 1 345 ? -31.383 12.567  48.564  1.00 28.08 ? 345  VAL B C     1 
ATOM   6749 O  O     . VAL B 1 345 ? -31.258 13.723  48.958  1.00 27.60 ? 345  VAL B O     1 
ATOM   6750 C  CB    . VAL B 1 345 ? -31.759 12.386  46.047  1.00 30.80 ? 345  VAL B CB    1 
ATOM   6751 C  CG1   . VAL B 1 345 ? -31.173 13.774  45.792  1.00 30.45 ? 345  VAL B CG1   1 
ATOM   6752 C  CG2   . VAL B 1 345 ? -30.723 11.295  45.783  1.00 29.97 ? 345  VAL B CG2   1 
ATOM   6753 N  N     . LYS B 1 346 ? -30.680 11.559  49.061  1.00 28.56 ? 346  LYS B N     1 
ATOM   6754 C  CA    . LYS B 1 346 ? -29.549 11.772  49.997  1.00 26.97 ? 346  LYS B CA    1 
ATOM   6755 C  C     . LYS B 1 346 ? -28.369 10.891  49.572  1.00 28.94 ? 346  LYS B C     1 
ATOM   6756 O  O     . LYS B 1 346 ? -28.599 9.718   49.170  1.00 28.11 ? 346  LYS B O     1 
ATOM   6757 C  CB    . LYS B 1 346 ? -30.042 11.535  51.428  1.00 30.95 ? 346  LYS B CB    1 
ATOM   6758 C  CG    . LYS B 1 346 ? -31.037 12.587  51.927  1.00 36.22 ? 346  LYS B CG    1 
ATOM   6759 C  CD    . LYS B 1 346 ? -31.647 12.301  53.300  1.00 41.99 ? 346  LYS B CD    1 
ATOM   6760 C  CE    . LYS B 1 346 ? -32.807 13.214  53.663  1.00 47.71 ? 346  LYS B CE    1 
ATOM   6761 N  NZ    . LYS B 1 346 ? -34.062 12.873  52.935  1.00 54.92 ? 346  LYS B NZ    1 
ATOM   6762 N  N     . PHE B 1 347 ? -27.151 11.436  49.672  1.00 29.45 ? 347  PHE B N     1 
ATOM   6763 C  CA    . PHE B 1 347 ? -25.868 10.774  49.339  1.00 29.66 ? 347  PHE B CA    1 
ATOM   6764 C  C     . PHE B 1 347 ? -25.098 10.524  50.639  1.00 32.05 ? 347  PHE B C     1 
ATOM   6765 O  O     . PHE B 1 347 ? -24.929 11.468  51.418  1.00 33.14 ? 347  PHE B O     1 
ATOM   6766 C  CB    . PHE B 1 347 ? -25.063 11.641  48.362  1.00 29.73 ? 347  PHE B CB    1 
ATOM   6767 C  CG    . PHE B 1 347 ? -25.803 12.046  47.114  1.00 29.97 ? 347  PHE B CG    1 
ATOM   6768 C  CD1   . PHE B 1 347 ? -25.790 11.236  45.994  1.00 31.78 ? 347  PHE B CD1   1 
ATOM   6769 C  CD2   . PHE B 1 347 ? -26.552 13.215  47.074  1.00 31.44 ? 347  PHE B CD2   1 
ATOM   6770 C  CE1   . PHE B 1 347 ? -26.497 11.580  44.850  1.00 32.55 ? 347  PHE B CE1   1 
ATOM   6771 C  CE2   . PHE B 1 347 ? -27.212 13.589  45.910  1.00 33.64 ? 347  PHE B CE2   1 
ATOM   6772 C  CZ    . PHE B 1 347 ? -27.188 12.764  44.799  1.00 31.98 ? 347  PHE B CZ    1 
ATOM   6773 N  N     . TYR B 1 348 ? -24.612 9.300   50.860  1.00 30.60 ? 348  TYR B N     1 
ATOM   6774 C  CA    . TYR B 1 348 ? -23.768 8.957   52.034  1.00 29.12 ? 348  TYR B CA    1 
ATOM   6775 C  C     . TYR B 1 348 ? -22.522 8.198   51.590  1.00 29.64 ? 348  TYR B C     1 
ATOM   6776 O  O     . TYR B 1 348 ? -22.610 7.285   50.742  1.00 27.72 ? 348  TYR B O     1 
ATOM   6777 C  CB    . TYR B 1 348 ? -24.513 8.055   53.016  1.00 30.16 ? 348  TYR B CB    1 
ATOM   6778 C  CG    . TYR B 1 348 ? -25.826 8.583   53.527  1.00 32.17 ? 348  TYR B CG    1 
ATOM   6779 C  CD1   . TYR B 1 348 ? -25.898 9.315   54.707  1.00 33.95 ? 348  TYR B CD1   1 
ATOM   6780 C  CD2   . TYR B 1 348 ? -27.007 8.306   52.858  1.00 32.13 ? 348  TYR B CD2   1 
ATOM   6781 C  CE1   . TYR B 1 348 ? -27.113 9.764   55.208  1.00 35.41 ? 348  TYR B CE1   1 
ATOM   6782 C  CE2   . TYR B 1 348 ? -28.227 8.751   53.340  1.00 34.63 ? 348  TYR B CE2   1 
ATOM   6783 C  CZ    . TYR B 1 348 ? -28.285 9.480   54.522  1.00 34.25 ? 348  TYR B CZ    1 
ATOM   6784 O  OH    . TYR B 1 348 ? -29.491 9.931   54.983  1.00 31.22 ? 348  TYR B OH    1 
ATOM   6785 N  N     . PHE B 1 349 ? -21.401 8.505   52.221  1.00 32.50 ? 349  PHE B N     1 
ATOM   6786 C  CA    . PHE B 1 349 ? -20.191 7.647   52.249  1.00 33.59 ? 349  PHE B CA    1 
ATOM   6787 C  C     . PHE B 1 349 ? -20.106 7.063   53.656  1.00 33.90 ? 349  PHE B C     1 
ATOM   6788 O  O     . PHE B 1 349 ? -20.867 7.459   54.537  1.00 29.27 ? 349  PHE B O     1 
ATOM   6789 C  CB    . PHE B 1 349 ? -18.989 8.487   51.816  1.00 39.82 ? 349  PHE B CB    1 
ATOM   6790 C  CG    . PHE B 1 349 ? -18.990 8.804   50.346  1.00 44.14 ? 349  PHE B CG    1 
ATOM   6791 C  CD1   . PHE B 1 349 ? -18.655 7.828   49.417  1.00 49.85 ? 349  PHE B CD1   1 
ATOM   6792 C  CD2   . PHE B 1 349 ? -19.335 10.062  49.887  1.00 48.04 ? 349  PHE B CD2   1 
ATOM   6793 C  CE1   . PHE B 1 349 ? -18.669 8.105   48.055  1.00 52.04 ? 349  PHE B CE1   1 
ATOM   6794 C  CE2   . PHE B 1 349 ? -19.325 10.343  48.528  1.00 49.78 ? 349  PHE B CE2   1 
ATOM   6795 C  CZ    . PHE B 1 349 ? -19.001 9.364   47.612  1.00 51.02 ? 349  PHE B CZ    1 
ATOM   6796 N  N     . PRO B 1 350 ? -19.255 6.054   53.923  1.00 32.93 ? 350  PRO B N     1 
ATOM   6797 C  CA    . PRO B 1 350 ? -19.223 5.462   55.258  1.00 34.05 ? 350  PRO B CA    1 
ATOM   6798 C  C     . PRO B 1 350 ? -19.139 6.524   56.362  1.00 36.27 ? 350  PRO B C     1 
ATOM   6799 O  O     . PRO B 1 350 ? -19.903 6.427   57.295  1.00 40.04 ? 350  PRO B O     1 
ATOM   6800 C  CB    . PRO B 1 350 ? -17.998 4.542   55.180  1.00 33.93 ? 350  PRO B CB    1 
ATOM   6801 C  CG    . PRO B 1 350 ? -18.021 4.088   53.735  1.00 32.37 ? 350  PRO B CG    1 
ATOM   6802 C  CD    . PRO B 1 350 ? -18.359 5.360   52.977  1.00 32.13 ? 350  PRO B CD    1 
ATOM   6803 N  N     . GLU B 1 351 ? -18.302 7.546   56.202  1.00 35.65 ? 351  GLU B N     1 
ATOM   6804 C  CA    . GLU B 1 351 ? -18.029 8.532   57.283  1.00 36.48 ? 351  GLU B CA    1 
ATOM   6805 C  C     . GLU B 1 351 ? -19.263 9.405   57.556  1.00 37.00 ? 351  GLU B C     1 
ATOM   6806 O  O     . GLU B 1 351 ? -19.247 10.077  58.585  1.00 36.35 ? 351  GLU B O     1 
ATOM   6807 C  CB    . GLU B 1 351 ? -16.776 9.351   56.965  1.00 39.07 ? 351  GLU B CB    1 
ATOM   6808 C  CG    . GLU B 1 351 ? -16.883 10.163  55.690  1.00 43.06 ? 351  GLU B CG    1 
ATOM   6809 C  CD    . GLU B 1 351 ? -16.380 9.518   54.403  1.00 42.18 ? 351  GLU B CD    1 
ATOM   6810 O  OE1   . GLU B 1 351 ? -16.402 8.257   54.272  1.00 37.60 ? 351  GLU B OE1   1 
ATOM   6811 O  OE2   . GLU B 1 351 ? -16.018 10.298  53.504  1.00 43.69 ? 351  GLU B OE2   1 
ATOM   6812 N  N     . ASP B 1 352 ? -20.304 9.351   56.707  1.00 39.22 ? 352  ASP B N     1 
ATOM   6813 C  CA    . ASP B 1 352 ? -21.599 10.083  56.835  1.00 34.90 ? 352  ASP B CA    1 
ATOM   6814 C  C     . ASP B 1 352 ? -22.656 9.304   57.631  1.00 34.55 ? 352  ASP B C     1 
ATOM   6815 O  O     . ASP B 1 352 ? -23.719 9.874   57.876  1.00 40.62 ? 352  ASP B O     1 
ATOM   6816 C  CB    . ASP B 1 352 ? -22.181 10.392  55.455  1.00 35.27 ? 352  ASP B CB    1 
ATOM   6817 C  CG    . ASP B 1 352 ? -21.281 11.288  54.630  1.00 35.92 ? 352  ASP B CG    1 
ATOM   6818 O  OD1   . ASP B 1 352 ? -20.698 12.209  55.228  1.00 38.30 ? 352  ASP B OD1   1 
ATOM   6819 O  OD2   . ASP B 1 352 ? -21.159 11.052  53.411  1.00 34.42 ? 352  ASP B OD2   1 
ATOM   6820 N  N     . ARG B 1 353 ? -22.439 8.032   57.946  1.00 36.35 ? 353  ARG B N     1 
ATOM   6821 C  CA    . ARG B 1 353 ? -23.457 7.172   58.604  1.00 39.16 ? 353  ARG B CA    1 
ATOM   6822 C  C     . ARG B 1 353 ? -23.225 7.175   60.119  1.00 46.19 ? 353  ARG B C     1 
ATOM   6823 O  O     . ARG B 1 353 ? -22.095 6.848   60.518  1.00 49.06 ? 353  ARG B O     1 
ATOM   6824 C  CB    . ARG B 1 353 ? -23.391 5.737   58.083  1.00 36.85 ? 353  ARG B CB    1 
ATOM   6825 C  CG    . ARG B 1 353 ? -23.507 5.622   56.572  1.00 34.19 ? 353  ARG B CG    1 
ATOM   6826 C  CD    . ARG B 1 353 ? -24.876 6.043   56.102  1.00 32.15 ? 353  ARG B CD    1 
ATOM   6827 N  NE    . ARG B 1 353 ? -25.879 5.078   56.504  1.00 28.39 ? 353  ARG B NE    1 
ATOM   6828 C  CZ    . ARG B 1 353 ? -27.190 5.229   56.359  1.00 28.10 ? 353  ARG B CZ    1 
ATOM   6829 N  NH1   . ARG B 1 353 ? -27.664 6.335   55.808  1.00 29.06 ? 353  ARG B NH1   1 
ATOM   6830 N  NH2   . ARG B 1 353 ? -28.014 4.276   56.772  1.00 26.76 ? 353  ARG B NH2   1 
ATOM   6831 N  N     . ARG B 1 354 ? -24.272 7.493   60.899  1.00 51.22 ? 354  ARG B N     1 
ATOM   6832 C  CA    . ARG B 1 354 ? -24.239 7.742   62.371  1.00 57.25 ? 354  ARG B CA    1 
ATOM   6833 C  C     . ARG B 1 354 ? -24.312 6.389   63.093  1.00 61.94 ? 354  ARG B C     1 
ATOM   6834 O  O     . ARG B 1 354 ? -23.473 6.145   63.988  1.00 65.34 ? 354  ARG B O     1 
ATOM   6835 C  CB    . ARG B 1 354 ? -25.369 8.702   62.776  1.00 54.84 ? 354  ARG B CB    1 
ATOM   6836 N  N     . HIS B 1 355 ? -25.219 5.513   62.652  1.00 62.57 ? 355  HIS B N     1 
ATOM   6837 C  CA    . HIS B 1 355 ? -25.457 4.161   63.234  1.00 64.97 ? 355  HIS B CA    1 
ATOM   6838 C  C     . HIS B 1 355 ? -24.138 3.369   63.198  1.00 67.93 ? 355  HIS B C     1 
ATOM   6839 O  O     . HIS B 1 355 ? -23.377 3.525   62.214  1.00 71.45 ? 355  HIS B O     1 
ATOM   6840 C  CB    . HIS B 1 355 ? -26.637 3.476   62.509  1.00 64.26 ? 355  HIS B CB    1 
ATOM   6841 C  CG    . HIS B 1 355 ? -27.837 4.356   62.381  1.00 68.10 ? 355  HIS B CG    1 
ATOM   6842 N  ND1   . HIS B 1 355 ? -28.830 4.385   63.339  1.00 66.19 ? 355  HIS B ND1   1 
ATOM   6843 C  CD2   . HIS B 1 355 ? -28.179 5.278   61.448  1.00 72.23 ? 355  HIS B CD2   1 
ATOM   6844 C  CE1   . HIS B 1 355 ? -29.737 5.276   63.003  1.00 70.62 ? 355  HIS B CE1   1 
ATOM   6845 N  NE2   . HIS B 1 355 ? -29.365 5.840   61.840  1.00 69.99 ? 355  HIS B NE2   1 
ATOM   6846 N  N     . LYS B 1 356 ? -23.859 2.570   64.235  1.00 67.19 ? 356  LYS B N     1 
ATOM   6847 C  CA    . LYS B 1 356 ? -22.587 1.807   64.365  1.00 67.04 ? 356  LYS B CA    1 
ATOM   6848 C  C     . LYS B 1 356 ? -22.714 0.497   63.572  1.00 65.82 ? 356  LYS B C     1 
ATOM   6849 O  O     . LYS B 1 356 ? -21.735 0.131   62.887  1.00 58.22 ? 356  LYS B O     1 
ATOM   6850 C  CB    . LYS B 1 356 ? -22.242 1.615   65.844  1.00 67.12 ? 356  LYS B CB    1 
ATOM   6851 C  CG    . LYS B 1 356 ? -21.753 2.885   66.541  1.00 69.31 ? 356  LYS B CG    1 
ATOM   6852 C  CD    . LYS B 1 356 ? -21.605 2.747   68.049  1.00 69.30 ? 356  LYS B CD    1 
ATOM   6853 C  CE    . LYS B 1 356 ? -22.870 3.073   68.824  1.00 66.80 ? 356  LYS B CE    1 
ATOM   6854 N  NZ    . LYS B 1 356 ? -22.825 2.576   70.224  1.00 56.81 ? 356  LYS B NZ    1 
ATOM   6855 N  N     . VAL B 1 357 ? -23.872 -0.169  63.673  1.00 58.87 ? 357  VAL B N     1 
ATOM   6856 C  CA    . VAL B 1 357 ? -24.293 -1.322  62.818  1.00 55.33 ? 357  VAL B CA    1 
ATOM   6857 C  C     . VAL B 1 357 ? -25.206 -0.732  61.750  1.00 54.93 ? 357  VAL B C     1 
ATOM   6858 O  O     . VAL B 1 357 ? -26.275 -0.200  62.111  1.00 51.44 ? 357  VAL B O     1 
ATOM   6859 C  CB    . VAL B 1 357 ? -25.042 -2.425  63.596  1.00 54.45 ? 357  VAL B CB    1 
ATOM   6860 C  CG1   . VAL B 1 357 ? -25.091 -3.722  62.799  1.00 55.85 ? 357  VAL B CG1   1 
ATOM   6861 C  CG2   . VAL B 1 357 ? -24.462 -2.662  64.985  1.00 53.74 ? 357  VAL B CG2   1 
ATOM   6862 N  N     . ASP B 1 358 ? -24.811 -0.787  60.485  1.00 48.52 ? 358  ASP B N     1 
ATOM   6863 C  CA    . ASP B 1 358 ? -25.441 0.111   59.493  1.00 45.16 ? 358  ASP B CA    1 
ATOM   6864 C  C     . ASP B 1 358 ? -25.420 -0.544  58.120  1.00 40.06 ? 358  ASP B C     1 
ATOM   6865 O  O     . ASP B 1 358 ? -24.405 -1.144  57.744  1.00 39.72 ? 358  ASP B O     1 
ATOM   6866 C  CB    . ASP B 1 358 ? -24.745 1.473   59.550  1.00 47.75 ? 358  ASP B CB    1 
ATOM   6867 C  CG    . ASP B 1 358 ? -25.238 2.424   58.486  1.00 47.19 ? 358  ASP B CG    1 
ATOM   6868 O  OD1   . ASP B 1 358 ? -26.367 2.985   58.662  1.00 45.92 ? 358  ASP B OD1   1 
ATOM   6869 O  OD2   . ASP B 1 358 ? -24.518 2.543   57.472  1.00 39.12 ? 358  ASP B OD2   1 
ATOM   6870 N  N     . LEU B 1 359 ? -26.506 -0.399  57.384  1.00 39.75 ? 359  LEU B N     1 
ATOM   6871 C  CA    . LEU B 1 359 ? -26.583 -0.972  56.030  1.00 43.59 ? 359  LEU B CA    1 
ATOM   6872 C  C     . LEU B 1 359 ? -25.253 -0.753  55.290  1.00 43.06 ? 359  LEU B C     1 
ATOM   6873 O  O     . LEU B 1 359 ? -24.688 -1.747  54.777  1.00 39.45 ? 359  LEU B O     1 
ATOM   6874 C  CB    . LEU B 1 359 ? -27.729 -0.331  55.258  1.00 46.90 ? 359  LEU B CB    1 
ATOM   6875 C  CG    . LEU B 1 359 ? -27.883 -0.943  53.874  1.00 52.44 ? 359  LEU B CG    1 
ATOM   6876 C  CD1   . LEU B 1 359 ? -28.563 -2.301  54.003  1.00 60.01 ? 359  LEU B CD1   1 
ATOM   6877 C  CD2   . LEU B 1 359 ? -28.620 -0.012  52.931  1.00 52.10 ? 359  LEU B CD2   1 
ATOM   6878 N  N     . LEU B 1 360 ? -24.782 0.497   55.208  1.00 39.97 ? 360  LEU B N     1 
ATOM   6879 C  CA    . LEU B 1 360 ? -23.663 0.885   54.307  1.00 38.09 ? 360  LEU B CA    1 
ATOM   6880 C  C     . LEU B 1 360 ? -22.349 0.258   54.791  1.00 37.45 ? 360  LEU B C     1 
ATOM   6881 O  O     . LEU B 1 360 ? -21.524 -0.108  53.937  1.00 36.19 ? 360  LEU B O     1 
ATOM   6882 C  CB    . LEU B 1 360 ? -23.533 2.404   54.205  1.00 36.02 ? 360  LEU B CB    1 
ATOM   6883 C  CG    . LEU B 1 360 ? -22.365 2.867   53.332  1.00 35.94 ? 360  LEU B CG    1 
ATOM   6884 C  CD1   . LEU B 1 360 ? -22.450 2.233   51.946  1.00 37.27 ? 360  LEU B CD1   1 
ATOM   6885 C  CD2   . LEU B 1 360 ? -22.315 4.383   53.235  1.00 35.91 ? 360  LEU B CD2   1 
ATOM   6886 N  N     . LEU B 1 361 ? -22.176 0.094   56.098  1.00 38.13 ? 361  LEU B N     1 
ATOM   6887 C  CA    . LEU B 1 361 ? -20.946 -0.504  56.666  1.00 38.61 ? 361  LEU B CA    1 
ATOM   6888 C  C     . LEU B 1 361 ? -20.894 -2.006  56.315  1.00 36.35 ? 361  LEU B C     1 
ATOM   6889 O  O     . LEU B 1 361 ? -19.794 -2.466  55.926  1.00 35.85 ? 361  LEU B O     1 
ATOM   6890 C  CB    . LEU B 1 361 ? -20.900 -0.191  58.167  1.00 46.49 ? 361  LEU B CB    1 
ATOM   6891 C  CG    . LEU B 1 361 ? -21.087 1.297   58.508  1.00 54.43 ? 361  LEU B CG    1 
ATOM   6892 C  CD1   . LEU B 1 361 ? -20.987 1.554   60.007  1.00 54.98 ? 361  LEU B CD1   1 
ATOM   6893 C  CD2   . LEU B 1 361 ? -20.099 2.177   57.741  1.00 53.05 ? 361  LEU B CD2   1 
ATOM   6894 N  N     . HIS B 1 362 ? -22.020 -2.732  56.333  1.00 33.78 ? 362  HIS B N     1 
ATOM   6895 C  CA    . HIS B 1 362 ? -22.090 -4.154  55.892  1.00 34.54 ? 362  HIS B CA    1 
ATOM   6896 C  C     . HIS B 1 362 ? -21.893 -4.254  54.368  1.00 31.80 ? 362  HIS B C     1 
ATOM   6897 O  O     . HIS B 1 362 ? -21.058 -5.044  53.944  1.00 32.13 ? 362  HIS B O     1 
ATOM   6898 C  CB    . HIS B 1 362 ? -23.405 -4.841  56.288  1.00 39.21 ? 362  HIS B CB    1 
ATOM   6899 C  CG    . HIS B 1 362 ? -23.603 -6.123  55.549  1.00 43.84 ? 362  HIS B CG    1 
ATOM   6900 N  ND1   . HIS B 1 362 ? -24.768 -6.414  54.848  1.00 47.08 ? 362  HIS B ND1   1 
ATOM   6901 C  CD2   . HIS B 1 362 ? -22.757 -7.167  55.344  1.00 50.63 ? 362  HIS B CD2   1 
ATOM   6902 C  CE1   . HIS B 1 362 ? -24.641 -7.599  54.270  1.00 49.28 ? 362  HIS B CE1   1 
ATOM   6903 N  NE2   . HIS B 1 362 ? -23.412 -8.076  54.547  1.00 51.84 ? 362  HIS B NE2   1 
ATOM   6904 N  N     . ARG B 1 363 ? -22.626 -3.476  53.572  1.00 30.08 ? 363  ARG B N     1 
ATOM   6905 C  CA    . ARG B 1 363 ? -22.547 -3.503  52.082  1.00 33.44 ? 363  ARG B CA    1 
ATOM   6906 C  C     . ARG B 1 363 ? -21.151 -3.115  51.603  1.00 31.15 ? 363  ARG B C     1 
ATOM   6907 O  O     . ARG B 1 363 ? -20.763 -3.630  50.539  1.00 30.31 ? 363  ARG B O     1 
ATOM   6908 C  CB    . ARG B 1 363 ? -23.535 -2.548  51.408  1.00 36.55 ? 363  ARG B CB    1 
ATOM   6909 C  CG    . ARG B 1 363 ? -24.982 -2.839  51.752  1.00 42.19 ? 363  ARG B CG    1 
ATOM   6910 C  CD    . ARG B 1 363 ? -25.490 -4.099  51.117  1.00 47.59 ? 363  ARG B CD    1 
ATOM   6911 N  NE    . ARG B 1 363 ? -26.911 -4.247  51.413  1.00 58.93 ? 363  ARG B NE    1 
ATOM   6912 C  CZ    . ARG B 1 363 ? -27.472 -5.286  52.045  1.00 66.93 ? 363  ARG B CZ    1 
ATOM   6913 N  NH1   . ARG B 1 363 ? -26.731 -6.298  52.472  1.00 68.17 ? 363  ARG B NH1   1 
ATOM   6914 N  NH2   . ARG B 1 363 ? -28.786 -5.316  52.229  1.00 69.05 ? 363  ARG B NH2   1 
ATOM   6915 N  N     . ALA B 1 364 ? -20.461 -2.210  52.314  1.00 27.39 ? 364  ALA B N     1 
ATOM   6916 C  CA    . ALA B 1 364 ? -19.095 -1.759  51.965  1.00 26.23 ? 364  ALA B CA    1 
ATOM   6917 C  C     . ALA B 1 364 ? -18.131 -2.957  52.036  1.00 27.19 ? 364  ALA B C     1 
ATOM   6918 O  O     . ALA B 1 364 ? -17.111 -2.965  51.332  1.00 27.53 ? 364  ALA B O     1 
ATOM   6919 C  CB    . ALA B 1 364 ? -18.634 -0.641  52.872  1.00 24.63 ? 364  ALA B CB    1 
ATOM   6920 N  N     . GLU B 1 365 ? -18.401 -3.903  52.919  1.00 27.32 ? 365  GLU B N     1 
ATOM   6921 C  CA    . GLU B 1 365 ? -17.560 -5.113  53.064  1.00 29.18 ? 365  GLU B CA    1 
ATOM   6922 C  C     . GLU B 1 365 ? -17.834 -6.026  51.867  1.00 25.58 ? 365  GLU B C     1 
ATOM   6923 O  O     . GLU B 1 365 ? -16.854 -6.442  51.263  1.00 27.22 ? 365  GLU B O     1 
ATOM   6924 C  CB    . GLU B 1 365 ? -17.835 -5.814  54.395  1.00 32.44 ? 365  GLU B CB    1 
ATOM   6925 C  CG    . GLU B 1 365 ? -17.046 -5.197  55.531  1.00 40.68 ? 365  GLU B CG    1 
ATOM   6926 C  CD    . GLU B 1 365 ? -17.362 -5.839  56.871  1.00 53.38 ? 365  GLU B CD    1 
ATOM   6927 O  OE1   . GLU B 1 365 ? -18.442 -6.504  56.989  1.00 51.41 ? 365  GLU B OE1   1 
ATOM   6928 O  OE2   . GLU B 1 365 ? -16.520 -5.695  57.793  1.00 70.11 ? 365  GLU B OE2   1 
ATOM   6929 N  N     . THR B 1 366 ? -19.104 -6.295  51.540  1.00 23.46 ? 366  THR B N     1 
ATOM   6930 C  CA    . THR B 1 366 ? -19.489 -7.150  50.392  1.00 25.46 ? 366  THR B CA    1 
ATOM   6931 C  C     . THR B 1 366 ? -18.900 -6.593  49.082  1.00 24.94 ? 366  THR B C     1 
ATOM   6932 O  O     . THR B 1 366 ? -18.415 -7.397  48.253  1.00 23.57 ? 366  THR B O     1 
ATOM   6933 C  CB    . THR B 1 366 ? -21.008 -7.324  50.331  1.00 28.28 ? 366  THR B CB    1 
ATOM   6934 O  OG1   . THR B 1 366 ? -21.450 -7.534  51.667  1.00 31.06 ? 366  THR B OG1   1 
ATOM   6935 C  CG2   . THR B 1 366 ? -21.407 -8.522  49.505  1.00 31.01 ? 366  THR B CG2   1 
ATOM   6936 N  N     . MET B 1 367 ? -18.901 -5.268  48.901  1.00 23.30 ? 367  MET B N     1 
ATOM   6937 C  CA    . MET B 1 367 ? -18.539 -4.623  47.611  1.00 22.43 ? 367  MET B CA    1 
ATOM   6938 C  C     . MET B 1 367 ? -17.009 -4.524  47.496  1.00 23.44 ? 367  MET B C     1 
ATOM   6939 O  O     . MET B 1 367 ? -16.519 -4.035  46.441  1.00 23.10 ? 367  MET B O     1 
ATOM   6940 C  CB    . MET B 1 367 ? -19.225 -3.259  47.436  1.00 20.94 ? 367  MET B CB    1 
ATOM   6941 C  CG    . MET B 1 367 ? -20.708 -3.358  47.101  1.00 21.23 ? 367  MET B CG    1 
ATOM   6942 S  SD    . MET B 1 367 ? -21.584 -1.766  46.875  1.00 22.57 ? 367  MET B SD    1 
ATOM   6943 C  CE    . MET B 1 367 ? -21.153 -0.915  48.395  1.00 23.59 ? 367  MET B CE    1 
ATOM   6944 N  N     . LYS B 1 368 ? -16.264 -5.010  48.491  1.00 25.33 ? 368  LYS B N     1 
ATOM   6945 C  CA    . LYS B 1 368 ? -14.812 -5.277  48.305  1.00 31.27 ? 368  LYS B CA    1 
ATOM   6946 C  C     . LYS B 1 368 ? -14.501 -6.750  48.585  1.00 28.45 ? 368  LYS B C     1 
ATOM   6947 O  O     . LYS B 1 368 ? -13.322 -7.059  48.883  1.00 28.79 ? 368  LYS B O     1 
ATOM   6948 C  CB    . LYS B 1 368 ? -13.934 -4.323  49.125  1.00 34.84 ? 368  LYS B CB    1 
ATOM   6949 C  CG    . LYS B 1 368 ? -13.986 -4.456  50.628  1.00 37.58 ? 368  LYS B CG    1 
ATOM   6950 C  CD    . LYS B 1 368 ? -12.955 -3.552  51.255  1.00 44.39 ? 368  LYS B CD    1 
ATOM   6951 C  CE    . LYS B 1 368 ? -13.005 -3.581  52.765  1.00 52.89 ? 368  LYS B CE    1 
ATOM   6952 N  NZ    . LYS B 1 368 ? -12.013 -2.642  53.334  1.00 63.52 ? 368  LYS B NZ    1 
ATOM   6953 N  N     . GLY B 1 369 ? -15.510 -7.607  48.458  1.00 26.66 ? 369  GLY B N     1 
ATOM   6954 C  CA    . GLY B 1 369 ? -15.351 -9.073  48.460  1.00 26.77 ? 369  GLY B CA    1 
ATOM   6955 C  C     . GLY B 1 369 ? -14.874 -9.629  49.789  1.00 24.31 ? 369  GLY B C     1 
ATOM   6956 O  O     . GLY B 1 369 ? -14.125 -10.615 49.751  1.00 22.08 ? 369  GLY B O     1 
ATOM   6957 N  N     . VAL B 1 370 ? -15.318 -9.045  50.910  1.00 26.40 ? 370  VAL B N     1 
ATOM   6958 C  CA    . VAL B 1 370 ? -15.142 -9.616  52.280  1.00 28.21 ? 370  VAL B CA    1 
ATOM   6959 C  C     . VAL B 1 370 ? -16.335 -10.522 52.592  1.00 28.45 ? 370  VAL B C     1 
ATOM   6960 O  O     . VAL B 1 370 ? -17.455 -10.055 52.718  1.00 29.48 ? 370  VAL B O     1 
ATOM   6961 C  CB    . VAL B 1 370 ? -14.969 -8.521  53.350  1.00 29.25 ? 370  VAL B CB    1 
ATOM   6962 C  CG1   . VAL B 1 370 ? -14.864 -9.153  54.742  1.00 30.14 ? 370  VAL B CG1   1 
ATOM   6963 C  CG2   . VAL B 1 370 ? -13.757 -7.644  53.067  1.00 27.93 ? 370  VAL B CG2   1 
ATOM   6964 N  N     . PRO B 1 371 ? -16.147 -11.854 52.732  1.00 29.86 ? 371  PRO B N     1 
ATOM   6965 C  CA    . PRO B 1 371 ? -17.263 -12.757 53.016  1.00 29.95 ? 371  PRO B CA    1 
ATOM   6966 C  C     . PRO B 1 371 ? -17.797 -12.564 54.444  1.00 29.87 ? 371  PRO B C     1 
ATOM   6967 O  O     . PRO B 1 371 ? -17.039 -12.358 55.329  1.00 27.96 ? 371  PRO B O     1 
ATOM   6968 C  CB    . PRO B 1 371 ? -16.643 -14.151 52.833  1.00 28.20 ? 371  PRO B CB    1 
ATOM   6969 C  CG    . PRO B 1 371 ? -15.198 -13.946 53.215  1.00 28.03 ? 371  PRO B CG    1 
ATOM   6970 C  CD    . PRO B 1 371 ? -14.854 -12.554 52.721  1.00 28.96 ? 371  PRO B CD    1 
ATOM   6971 N  N     . LYS B 1 372 ? -19.113 -12.627 54.610  1.00 35.42 ? 372  LYS B N     1 
ATOM   6972 C  CA    . LYS B 1 372 ? -19.826 -12.460 55.904  1.00 38.16 ? 372  LYS B CA    1 
ATOM   6973 C  C     . LYS B 1 372 ? -21.032 -13.387 55.863  1.00 37.77 ? 372  LYS B C     1 
ATOM   6974 O  O     . LYS B 1 372 ? -21.271 -13.961 54.785  1.00 34.21 ? 372  LYS B O     1 
ATOM   6975 C  CB    . LYS B 1 372 ? -20.321 -11.022 56.093  1.00 41.46 ? 372  LYS B CB    1 
ATOM   6976 C  CG    . LYS B 1 372 ? -19.244 -9.975  56.320  1.00 47.68 ? 372  LYS B CG    1 
ATOM   6977 C  CD    . LYS B 1 372 ? -18.670 -10.010 57.726  1.00 53.52 ? 372  LYS B CD    1 
ATOM   6978 C  CE    . LYS B 1 372 ? -17.270 -9.437  57.821  1.00 57.02 ? 372  LYS B CE    1 
ATOM   6979 N  NZ    . LYS B 1 372 ? -16.605 -9.795  59.096  1.00 57.82 ? 372  LYS B NZ    1 
ATOM   6980 N  N     . LEU B 1 373 ? -21.768 -13.494 56.973  1.00 40.46 ? 373  LEU B N     1 
ATOM   6981 C  CA    . LEU B 1 373 ? -23.096 -14.161 57.032  1.00 39.80 ? 373  LEU B CA    1 
ATOM   6982 C  C     . LEU B 1 373 ? -24.173 -13.185 57.526  1.00 40.44 ? 373  LEU B C     1 
ATOM   6983 O  O     . LEU B 1 373 ? -25.326 -13.649 57.665  1.00 35.71 ? 373  LEU B O     1 
ATOM   6984 C  CB    . LEU B 1 373 ? -23.003 -15.405 57.919  1.00 42.49 ? 373  LEU B CB    1 
ATOM   6985 C  CG    . LEU B 1 373 ? -22.162 -16.554 57.346  1.00 44.61 ? 373  LEU B CG    1 
ATOM   6986 C  CD1   . LEU B 1 373 ? -21.906 -17.605 58.408  1.00 46.52 ? 373  LEU B CD1   1 
ATOM   6987 C  CD2   . LEU B 1 373 ? -22.804 -17.196 56.120  1.00 43.55 ? 373  LEU B CD2   1 
ATOM   6988 N  N     . THR B 1 374 ? -23.824 -11.891 57.682  1.00 39.36 ? 374  THR B N     1 
ATOM   6989 C  CA    . THR B 1 374 ? -24.700 -10.728 58.020  1.00 40.65 ? 374  THR B CA    1 
ATOM   6990 C  C     . THR B 1 374 ? -26.051 -10.774 57.287  1.00 42.55 ? 374  THR B C     1 
ATOM   6991 O  O     . THR B 1 374 ? -27.117 -10.472 57.924  1.00 43.55 ? 374  THR B O     1 
ATOM   6992 C  CB    . THR B 1 374 ? -24.019 -9.395  57.660  1.00 42.33 ? 374  THR B CB    1 
ATOM   6993 O  OG1   . THR B 1 374 ? -22.739 -9.323  58.290  1.00 42.54 ? 374  THR B OG1   1 
ATOM   6994 C  CG2   . THR B 1 374 ? -24.831 -8.178  58.060  1.00 42.38 ? 374  THR B CG2   1 
ATOM   6995 N  N     . GLU B 1 375 ? -26.029 -11.087 55.991  1.00 40.29 ? 375  GLU B N     1 
ATOM   6996 C  CA    . GLU B 1 375 ? -27.228 -10.977 55.121  1.00 41.73 ? 375  GLU B CA    1 
ATOM   6997 C  C     . GLU B 1 375 ? -28.372 -11.832 55.690  1.00 40.66 ? 375  GLU B C     1 
ATOM   6998 O  O     . GLU B 1 375 ? -29.531 -11.457 55.465  1.00 36.89 ? 375  GLU B O     1 
ATOM   6999 C  CB    . GLU B 1 375 ? -26.896 -11.366 53.678  1.00 43.02 ? 375  GLU B CB    1 
ATOM   7000 C  CG    . GLU B 1 375 ? -27.938 -10.935 52.666  1.00 41.49 ? 375  GLU B CG    1 
ATOM   7001 C  CD    . GLU B 1 375 ? -28.145 -9.429  52.572  1.00 43.99 ? 375  GLU B CD    1 
ATOM   7002 O  OE1   . GLU B 1 375 ? -27.274 -8.660  53.045  1.00 41.74 ? 375  GLU B OE1   1 
ATOM   7003 O  OE2   . GLU B 1 375 ? -29.198 -9.030  52.060  1.00 39.42 ? 375  GLU B OE2   1 
ATOM   7004 N  N     . PHE B 1 376 ? -28.070 -12.932 56.393  1.00 40.23 ? 376  PHE B N     1 
ATOM   7005 C  CA    . PHE B 1 376 ? -29.094 -13.861 56.945  1.00 38.72 ? 376  PHE B CA    1 
ATOM   7006 C  C     . PHE B 1 376 ? -29.951 -13.128 58.004  1.00 35.19 ? 376  PHE B C     1 
ATOM   7007 O  O     . PHE B 1 376 ? -31.067 -13.587 58.252  1.00 35.36 ? 376  PHE B O     1 
ATOM   7008 C  CB    . PHE B 1 376 ? -28.443 -15.175 57.418  1.00 38.83 ? 376  PHE B CB    1 
ATOM   7009 C  CG    . PHE B 1 376 ? -28.205 -16.196 56.324  1.00 39.24 ? 376  PHE B CG    1 
ATOM   7010 C  CD1   . PHE B 1 376 ? -29.187 -17.119 55.977  1.00 37.85 ? 376  PHE B CD1   1 
ATOM   7011 C  CD2   . PHE B 1 376 ? -27.007 -16.228 55.624  1.00 43.92 ? 376  PHE B CD2   1 
ATOM   7012 C  CE1   . PHE B 1 376 ? -28.985 -18.060 54.976  1.00 33.38 ? 376  PHE B CE1   1 
ATOM   7013 C  CE2   . PHE B 1 376 ? -26.800 -17.177 54.628  1.00 43.90 ? 376  PHE B CE2   1 
ATOM   7014 C  CZ    . PHE B 1 376 ? -27.797 -18.078 54.298  1.00 38.84 ? 376  PHE B CZ    1 
ATOM   7015 N  N     . ASN B 1 377 ? -29.508 -11.985 58.545  1.00 32.90 ? 377  ASN B N     1 
ATOM   7016 C  CA    . ASN B 1 377 ? -30.297 -11.177 59.519  1.00 31.74 ? 377  ASN B CA    1 
ATOM   7017 C  C     . ASN B 1 377 ? -31.716 -10.866 59.004  1.00 32.75 ? 377  ASN B C     1 
ATOM   7018 O  O     . ASN B 1 377 ? -32.637 -10.771 59.865  1.00 32.73 ? 377  ASN B O     1 
ATOM   7019 C  CB    . ASN B 1 377 ? -29.622 -9.861  59.890  1.00 30.87 ? 377  ASN B CB    1 
ATOM   7020 C  CG    . ASN B 1 377 ? -28.380 -10.027 60.736  1.00 31.23 ? 377  ASN B CG    1 
ATOM   7021 O  OD1   . ASN B 1 377 ? -28.107 -11.102 61.250  1.00 33.69 ? 377  ASN B OD1   1 
ATOM   7022 N  ND2   . ASN B 1 377 ? -27.593 -8.973  60.863  1.00 33.11 ? 377  ASN B ND2   1 
ATOM   7023 N  N     . PHE B 1 378 ? -31.938 -10.726 57.689  1.00 28.96 ? 378  PHE B N     1 
ATOM   7024 C  CA    . PHE B 1 378 ? -33.277 -10.310 57.183  1.00 30.88 ? 378  PHE B CA    1 
ATOM   7025 C  C     . PHE B 1 378 ? -34.314 -11.419 57.408  1.00 29.22 ? 378  PHE B C     1 
ATOM   7026 O  O     . PHE B 1 378 ? -35.510 -11.110 57.398  1.00 25.47 ? 378  PHE B O     1 
ATOM   7027 C  CB    . PHE B 1 378 ? -33.233 -9.780  55.743  1.00 30.64 ? 378  PHE B CB    1 
ATOM   7028 C  CG    . PHE B 1 378 ? -33.024 -10.755 54.611  1.00 32.31 ? 378  PHE B CG    1 
ATOM   7029 C  CD1   . PHE B 1 378 ? -34.006 -11.664 54.254  1.00 34.18 ? 378  PHE B CD1   1 
ATOM   7030 C  CD2   . PHE B 1 378 ? -31.895 -10.663 53.803  1.00 34.03 ? 378  PHE B CD2   1 
ATOM   7031 C  CE1   . PHE B 1 378 ? -33.818 -12.531 53.186  1.00 34.24 ? 378  PHE B CE1   1 
ATOM   7032 C  CE2   . PHE B 1 378 ? -31.725 -11.517 52.719  1.00 35.61 ? 378  PHE B CE2   1 
ATOM   7033 C  CZ    . PHE B 1 378 ? -32.688 -12.450 52.413  1.00 32.87 ? 378  PHE B CZ    1 
ATOM   7034 N  N     . LEU B 1 379 ? -33.871 -12.668 57.581  1.00 29.67 ? 379  LEU B N     1 
ATOM   7035 C  CA    . LEU B 1 379 ? -34.729 -13.818 57.985  1.00 30.13 ? 379  LEU B CA    1 
ATOM   7036 C  C     . LEU B 1 379 ? -35.413 -13.592 59.360  1.00 27.96 ? 379  LEU B C     1 
ATOM   7037 O  O     . LEU B 1 379 ? -36.445 -14.232 59.591  1.00 28.43 ? 379  LEU B O     1 
ATOM   7038 C  CB    . LEU B 1 379 ? -33.869 -15.096 57.971  1.00 30.25 ? 379  LEU B CB    1 
ATOM   7039 C  CG    . LEU B 1 379 ? -33.416 -15.589 56.589  1.00 30.96 ? 379  LEU B CG    1 
ATOM   7040 C  CD1   . LEU B 1 379 ? -32.791 -16.989 56.658  1.00 28.59 ? 379  LEU B CD1   1 
ATOM   7041 C  CD2   . LEU B 1 379 ? -34.573 -15.587 55.604  1.00 30.17 ? 379  LEU B CD2   1 
ATOM   7042 N  N     . ASN B 1 380 ? -34.907 -12.703 60.227  1.00 29.20 ? 380  ASN B N     1 
ATOM   7043 C  CA    . ASN B 1 380 ? -35.473 -12.413 61.576  1.00 30.76 ? 380  ASN B CA    1 
ATOM   7044 C  C     . ASN B 1 380 ? -36.528 -11.309 61.549  1.00 29.88 ? 380  ASN B C     1 
ATOM   7045 O  O     . ASN B 1 380 ? -37.021 -10.946 62.645  1.00 28.87 ? 380  ASN B O     1 
ATOM   7046 C  CB    . ASN B 1 380 ? -34.385 -11.984 62.558  1.00 35.65 ? 380  ASN B CB    1 
ATOM   7047 C  CG    . ASN B 1 380 ? -33.459 -13.131 62.891  1.00 41.62 ? 380  ASN B CG    1 
ATOM   7048 O  OD1   . ASN B 1 380 ? -33.892 -14.281 63.002  1.00 47.49 ? 380  ASN B OD1   1 
ATOM   7049 N  ND2   . ASN B 1 380 ? -32.182 -12.826 63.033  1.00 45.26 ? 380  ASN B ND2   1 
ATOM   7050 N  N     . TRP B 1 381 ? -36.857 -10.763 60.375  1.00 29.87 ? 381  TRP B N     1 
ATOM   7051 C  CA    . TRP B 1 381 ? -37.745 -9.578  60.284  1.00 27.57 ? 381  TRP B CA    1 
ATOM   7052 C  C     . TRP B 1 381 ? -39.017 -9.815  61.106  1.00 29.37 ? 381  TRP B C     1 
ATOM   7053 O  O     . TRP B 1 381 ? -39.399 -8.938  61.903  1.00 29.17 ? 381  TRP B O     1 
ATOM   7054 C  CB    . TRP B 1 381 ? -38.088 -9.270  58.835  1.00 25.29 ? 381  TRP B CB    1 
ATOM   7055 C  CG    . TRP B 1 381 ? -39.059 -8.141  58.700  1.00 23.87 ? 381  TRP B CG    1 
ATOM   7056 C  CD1   . TRP B 1 381 ? -40.314 -8.194  58.176  1.00 22.15 ? 381  TRP B CD1   1 
ATOM   7057 C  CD2   . TRP B 1 381 ? -38.863 -6.785  59.153  1.00 22.62 ? 381  TRP B CD2   1 
ATOM   7058 N  NE1   . TRP B 1 381 ? -40.900 -6.948  58.229  1.00 25.71 ? 381  TRP B NE1   1 
ATOM   7059 C  CE2   . TRP B 1 381 ? -40.034 -6.066  58.832  1.00 23.66 ? 381  TRP B CE2   1 
ATOM   7060 C  CE3   . TRP B 1 381 ? -37.819 -6.109  59.791  1.00 23.19 ? 381  TRP B CE3   1 
ATOM   7061 C  CZ2   . TRP B 1 381 ? -40.179 -4.708  59.119  1.00 23.73 ? 381  TRP B CZ2   1 
ATOM   7062 C  CZ3   . TRP B 1 381 ? -37.961 -4.762  60.068  1.00 23.75 ? 381  TRP B CZ3   1 
ATOM   7063 C  CH2   . TRP B 1 381 ? -39.128 -4.070  59.730  1.00 23.15 ? 381  TRP B CH2   1 
ATOM   7064 N  N     . ASP B 1 382 ? -39.685 -10.936 60.851  1.00 30.11 ? 382  ASP B N     1 
ATOM   7065 C  CA    . ASP B 1 382 ? -40.948 -11.343 61.519  1.00 35.34 ? 382  ASP B CA    1 
ATOM   7066 C  C     . ASP B 1 382 ? -40.717 -12.545 62.458  1.00 36.46 ? 382  ASP B C     1 
ATOM   7067 O  O     . ASP B 1 382 ? -41.597 -13.383 62.532  1.00 33.68 ? 382  ASP B O     1 
ATOM   7068 C  CB    . ASP B 1 382 ? -42.002 -11.614 60.446  1.00 40.82 ? 382  ASP B CB    1 
ATOM   7069 C  CG    . ASP B 1 382 ? -43.434 -11.582 60.943  1.00 45.13 ? 382  ASP B CG    1 
ATOM   7070 O  OD1   . ASP B 1 382 ? -43.723 -10.819 61.891  1.00 46.40 ? 382  ASP B OD1   1 
ATOM   7071 O  OD2   . ASP B 1 382 ? -44.248 -12.337 60.389  1.00 54.18 ? 382  ASP B OD2   1 
ATOM   7072 N  N     . GLY B 1 383 ? -39.566 -12.628 63.140  1.00 38.55 ? 383  GLY B N     1 
ATOM   7073 C  CA    . GLY B 1 383 ? -39.296 -13.594 64.229  1.00 43.07 ? 383  GLY B CA    1 
ATOM   7074 C  C     . GLY B 1 383 ? -38.449 -14.810 63.831  1.00 41.16 ? 383  GLY B C     1 
ATOM   7075 O  O     . GLY B 1 383 ? -38.032 -15.533 64.739  1.00 41.84 ? 383  GLY B O     1 
ATOM   7076 N  N     . GLY B 1 384 ? -38.171 -15.025 62.542  1.00 38.62 ? 384  GLY B N     1 
ATOM   7077 C  CA    . GLY B 1 384 ? -37.404 -16.181 62.036  1.00 36.81 ? 384  GLY B CA    1 
ATOM   7078 C  C     . GLY B 1 384 ? -38.170 -16.900 60.942  1.00 39.24 ? 384  GLY B C     1 
ATOM   7079 O  O     . GLY B 1 384 ? -39.364 -17.207 61.135  1.00 43.24 ? 384  GLY B O     1 
ATOM   7080 N  N     . GLY B 1 385 ? -37.547 -17.120 59.792  1.00 35.75 ? 385  GLY B N     1 
ATOM   7081 C  CA    . GLY B 1 385 ? -38.189 -17.889 58.711  1.00 36.41 ? 385  GLY B CA    1 
ATOM   7082 C  C     . GLY B 1 385 ? -37.178 -18.352 57.682  1.00 33.54 ? 385  GLY B C     1 
ATOM   7083 O  O     . GLY B 1 385 ? -35.998 -18.174 57.929  1.00 35.78 ? 385  GLY B O     1 
ATOM   7084 N  N     . GLY B 1 386 ? -37.644 -18.938 56.586  1.00 32.61 ? 386  GLY B N     1 
ATOM   7085 C  CA    . GLY B 1 386 ? -36.860 -19.145 55.356  1.00 34.24 ? 386  GLY B CA    1 
ATOM   7086 C  C     . GLY B 1 386 ? -37.137 -18.077 54.307  1.00 34.64 ? 386  GLY B C     1 
ATOM   7087 O  O     . GLY B 1 386 ? -37.962 -17.177 54.551  1.00 30.28 ? 386  GLY B O     1 
ATOM   7088 N  N     . HIS B 1 387 ? -36.455 -18.154 53.163  1.00 32.48 ? 387  HIS B N     1 
ATOM   7089 C  CA    . HIS B 1 387 ? -36.694 -17.229 52.030  1.00 32.37 ? 387  HIS B CA    1 
ATOM   7090 C  C     . HIS B 1 387 ? -36.716 -18.037 50.743  1.00 32.86 ? 387  HIS B C     1 
ATOM   7091 O  O     . HIS B 1 387 ? -36.070 -19.097 50.683  1.00 31.43 ? 387  HIS B O     1 
ATOM   7092 C  CB    . HIS B 1 387 ? -35.719 -16.027 52.034  1.00 32.58 ? 387  HIS B CB    1 
ATOM   7093 C  CG    . HIS B 1 387 ? -34.267 -16.301 51.739  1.00 32.94 ? 387  HIS B CG    1 
ATOM   7094 N  ND1   . HIS B 1 387 ? -33.664 -15.771 50.624  1.00 31.96 ? 387  HIS B ND1   1 
ATOM   7095 C  CD2   . HIS B 1 387 ? -33.291 -16.953 52.426  1.00 29.21 ? 387  HIS B CD2   1 
ATOM   7096 C  CE1   . HIS B 1 387 ? -32.384 -16.093 50.605  1.00 34.31 ? 387  HIS B CE1   1 
ATOM   7097 N  NE2   . HIS B 1 387 ? -32.107 -16.859 51.707  1.00 34.94 ? 387  HIS B NE2   1 
ATOM   7098 N  N     . VAL B 1 388 ? -37.546 -17.587 49.809  1.00 34.93 ? 388  VAL B N     1 
ATOM   7099 C  CA    . VAL B 1 388 ? -37.442 -17.922 48.363  1.00 35.26 ? 388  VAL B CA    1 
ATOM   7100 C  C     . VAL B 1 388 ? -37.447 -16.609 47.576  1.00 32.32 ? 388  VAL B C     1 
ATOM   7101 O  O     . VAL B 1 388 ? -37.975 -15.594 48.111  1.00 32.89 ? 388  VAL B O     1 
ATOM   7102 C  CB    . VAL B 1 388 ? -38.561 -18.871 47.918  1.00 32.58 ? 388  VAL B CB    1 
ATOM   7103 C  CG1   . VAL B 1 388 ? -39.918 -18.190 47.930  1.00 34.92 ? 388  VAL B CG1   1 
ATOM   7104 C  CG2   . VAL B 1 388 ? -38.247 -19.455 46.553  1.00 31.50 ? 388  VAL B CG2   1 
ATOM   7105 N  N     . GLY B 1 389 ? -36.889 -16.631 46.366  1.00 28.75 ? 389  GLY B N     1 
ATOM   7106 C  CA    . GLY B 1 389 ? -36.669 -15.424 45.540  1.00 27.40 ? 389  GLY B CA    1 
ATOM   7107 C  C     . GLY B 1 389 ? -37.252 -15.590 44.157  1.00 26.05 ? 389  GLY B C     1 
ATOM   7108 O  O     . GLY B 1 389 ? -37.335 -16.732 43.677  1.00 23.71 ? 389  GLY B O     1 
ATOM   7109 N  N     . PHE B 1 390 ? -37.691 -14.490 43.552  1.00 28.12 ? 390  PHE B N     1 
ATOM   7110 C  CA    . PHE B 1 390 ? -38.143 -14.445 42.140  1.00 27.03 ? 390  PHE B CA    1 
ATOM   7111 C  C     . PHE B 1 390 ? -37.393 -13.297 41.473  1.00 27.26 ? 390  PHE B C     1 
ATOM   7112 O  O     . PHE B 1 390 ? -37.554 -12.120 41.892  1.00 26.58 ? 390  PHE B O     1 
ATOM   7113 C  CB    . PHE B 1 390 ? -39.667 -14.300 42.052  1.00 28.54 ? 390  PHE B CB    1 
ATOM   7114 C  CG    . PHE B 1 390 ? -40.207 -14.382 40.644  1.00 29.91 ? 390  PHE B CG    1 
ATOM   7115 C  CD1   . PHE B 1 390 ? -39.945 -15.489 39.852  1.00 29.22 ? 390  PHE B CD1   1 
ATOM   7116 C  CD2   . PHE B 1 390 ? -40.956 -13.346 40.102  1.00 31.37 ? 390  PHE B CD2   1 
ATOM   7117 C  CE1   . PHE B 1 390 ? -40.426 -15.563 38.554  1.00 33.03 ? 390  PHE B CE1   1 
ATOM   7118 C  CE2   . PHE B 1 390 ? -41.443 -13.420 38.806  1.00 31.42 ? 390  PHE B CE2   1 
ATOM   7119 C  CZ    . PHE B 1 390 ? -41.173 -14.525 38.033  1.00 32.96 ? 390  PHE B CZ    1 
ATOM   7120 N  N     . SER B 1 391 ? -36.588 -13.613 40.465  1.00 25.32 ? 391  SER B N     1 
ATOM   7121 C  CA    . SER B 1 391 ? -35.560 -12.685 39.948  1.00 26.60 ? 391  SER B CA    1 
ATOM   7122 C  C     . SER B 1 391 ? -35.604 -12.605 38.424  1.00 23.75 ? 391  SER B C     1 
ATOM   7123 O  O     . SER B 1 391 ? -34.586 -12.667 37.766  1.00 24.43 ? 391  SER B O     1 
ATOM   7124 C  CB    . SER B 1 391 ? -34.234 -13.139 40.485  1.00 27.94 ? 391  SER B CB    1 
ATOM   7125 O  OG    . SER B 1 391 ? -34.073 -14.517 40.187  1.00 32.55 ? 391  SER B OG    1 
ATOM   7126 N  N     . PRO B 1 392 ? -36.759 -12.378 37.779  1.00 25.10 ? 392  PRO B N     1 
ATOM   7127 C  CA    . PRO B 1 392 ? -36.791 -12.379 36.312  1.00 24.12 ? 392  PRO B CA    1 
ATOM   7128 C  C     . PRO B 1 392 ? -36.015 -11.206 35.689  1.00 25.03 ? 392  PRO B C     1 
ATOM   7129 O  O     . PRO B 1 392 ? -35.723 -10.244 36.397  1.00 26.80 ? 392  PRO B O     1 
ATOM   7130 C  CB    . PRO B 1 392 ? -38.286 -12.298 36.032  1.00 25.75 ? 392  PRO B CB    1 
ATOM   7131 C  CG    . PRO B 1 392 ? -38.804 -11.479 37.207  1.00 26.46 ? 392  PRO B CG    1 
ATOM   7132 C  CD    . PRO B 1 392 ? -38.063 -12.066 38.392  1.00 25.65 ? 392  PRO B CD    1 
ATOM   7133 N  N     . VAL B 1 393 ? -35.679 -11.326 34.398  1.00 24.48 ? 393  VAL B N     1 
ATOM   7134 C  CA    . VAL B 1 393 ? -34.868 -10.348 33.621  1.00 25.03 ? 393  VAL B CA    1 
ATOM   7135 C  C     . VAL B 1 393 ? -35.799 -9.403  32.856  1.00 22.81 ? 393  VAL B C     1 
ATOM   7136 O  O     . VAL B 1 393 ? -36.754 -9.887  32.236  1.00 23.51 ? 393  VAL B O     1 
ATOM   7137 C  CB    . VAL B 1 393 ? -33.958 -11.080 32.613  1.00 29.28 ? 393  VAL B CB    1 
ATOM   7138 C  CG1   . VAL B 1 393 ? -32.972 -10.132 31.978  1.00 32.99 ? 393  VAL B CG1   1 
ATOM   7139 C  CG2   . VAL B 1 393 ? -33.239 -12.241 33.259  1.00 35.39 ? 393  VAL B CG2   1 
ATOM   7140 N  N     . SER B 1 394 ? -35.449 -8.133  32.774  1.00 21.63 ? 394  SER B N     1 
ATOM   7141 C  CA    . SER B 1 394 ? -36.243 -7.094  32.065  1.00 23.50 ? 394  SER B CA    1 
ATOM   7142 C  C     . SER B 1 394 ? -35.281 -6.055  31.512  1.00 21.42 ? 394  SER B C     1 
ATOM   7143 O  O     . SER B 1 394 ? -34.129 -6.032  31.948  1.00 20.70 ? 394  SER B O     1 
ATOM   7144 C  CB    . SER B 1 394 ? -37.270 -6.458  33.006  1.00 23.68 ? 394  SER B CB    1 
ATOM   7145 O  OG    . SER B 1 394 ? -36.607 -5.899  34.130  1.00 27.03 ? 394  SER B OG    1 
ATOM   7146 N  N     . PRO B 1 395 ? -35.710 -5.195  30.552  1.00 20.88 ? 395  PRO B N     1 
ATOM   7147 C  CA    . PRO B 1 395 ? -34.911 -4.047  30.141  1.00 21.44 ? 395  PRO B CA    1 
ATOM   7148 C  C     . PRO B 1 395 ? -34.751 -3.024  31.272  1.00 23.21 ? 395  PRO B C     1 
ATOM   7149 O  O     . PRO B 1 395 ? -35.644 -2.942  32.108  1.00 22.60 ? 395  PRO B O     1 
ATOM   7150 C  CB    . PRO B 1 395 ? -35.659 -3.455  28.925  1.00 22.92 ? 395  PRO B CB    1 
ATOM   7151 C  CG    . PRO B 1 395 ? -36.621 -4.570  28.481  1.00 22.47 ? 395  PRO B CG    1 
ATOM   7152 C  CD    . PRO B 1 395 ? -36.947 -5.335  29.752  1.00 22.17 ? 395  PRO B CD    1 
ATOM   7153 N  N     . ILE B 1 396 ? -33.628 -2.291  31.266  1.00 23.14 ? 396  ILE B N     1 
ATOM   7154 C  CA    . ILE B 1 396 ? -33.344 -1.204  32.243  1.00 24.99 ? 396  ILE B CA    1 
ATOM   7155 C  C     . ILE B 1 396 ? -34.138 0.020   31.802  1.00 24.03 ? 396  ILE B C     1 
ATOM   7156 O  O     . ILE B 1 396 ? -33.566 0.880   31.133  1.00 23.71 ? 396  ILE B O     1 
ATOM   7157 C  CB    . ILE B 1 396 ? -31.855 -0.865  32.356  1.00 25.97 ? 396  ILE B CB    1 
ATOM   7158 C  CG1   . ILE B 1 396 ? -30.972 -2.106  32.473  1.00 25.36 ? 396  ILE B CG1   1 
ATOM   7159 C  CG2   . ILE B 1 396 ? -31.670 0.095   33.524  1.00 24.05 ? 396  ILE B CG2   1 
ATOM   7160 C  CD1   . ILE B 1 396 ? -29.525 -1.833  32.156  1.00 25.77 ? 396  ILE B CD1   1 
ATOM   7161 N  N     . THR B 1 397 ? -35.416 0.027   32.165  1.00 23.12 ? 397  THR B N     1 
ATOM   7162 C  CA    . THR B 1 397 ? -36.436 1.068   31.886  1.00 26.71 ? 397  THR B CA    1 
ATOM   7163 C  C     . THR B 1 397 ? -37.158 1.388   33.211  1.00 26.70 ? 397  THR B C     1 
ATOM   7164 O  O     . THR B 1 397 ? -37.551 0.458   33.953  1.00 21.72 ? 397  THR B O     1 
ATOM   7165 C  CB    . THR B 1 397 ? -37.280 0.487   30.739  1.00 29.28 ? 397  THR B CB    1 
ATOM   7166 O  OG1   . THR B 1 397 ? -36.774 0.908   29.467  1.00 31.60 ? 397  THR B OG1   1 
ATOM   7167 C  CG2   . THR B 1 397 ? -38.744 0.772   30.818  1.00 26.01 ? 397  THR B CG2   1 
ATOM   7168 N  N     . GLY B 1 398 ? -37.363 2.672   33.485  1.00 29.24 ? 398  GLY B N     1 
ATOM   7169 C  CA    . GLY B 1 398 ? -38.282 3.128   34.536  1.00 28.58 ? 398  GLY B CA    1 
ATOM   7170 C  C     . GLY B 1 398 ? -39.619 2.437   34.427  1.00 28.12 ? 398  GLY B C     1 
ATOM   7171 O  O     . GLY B 1 398 ? -40.159 2.025   35.468  1.00 29.88 ? 398  GLY B O     1 
ATOM   7172 N  N     . LYS B 1 399 ? -40.185 2.368   33.221  1.00 28.99 ? 399  LYS B N     1 
ATOM   7173 C  CA    . LYS B 1 399 ? -41.535 1.773   33.021  1.00 32.25 ? 399  LYS B CA    1 
ATOM   7174 C  C     . LYS B 1 399 ? -41.502 0.293   33.461  1.00 29.67 ? 399  LYS B C     1 
ATOM   7175 O  O     . LYS B 1 399 ? -42.462 -0.138  34.097  1.00 27.94 ? 399  LYS B O     1 
ATOM   7176 C  CB    . LYS B 1 399 ? -41.990 2.063   31.587  1.00 37.27 ? 399  LYS B CB    1 
ATOM   7177 C  CG    . LYS B 1 399 ? -43.131 1.217   31.046  1.00 47.13 ? 399  LYS B CG    1 
ATOM   7178 C  CD    . LYS B 1 399 ? -43.160 1.148   29.512  1.00 52.74 ? 399  LYS B CD    1 
ATOM   7179 C  CE    . LYS B 1 399 ? -42.110 0.220   28.921  1.00 58.12 ? 399  LYS B CE    1 
ATOM   7180 N  NZ    . LYS B 1 399 ? -42.371 -1.209  29.244  1.00 63.99 ? 399  LYS B NZ    1 
ATOM   7181 N  N     . ASP B 1 400 ? -40.426 -0.457  33.187  1.00 26.73 ? 400  ASP B N     1 
ATOM   7182 C  CA    . ASP B 1 400 ? -40.325 -1.900  33.555  1.00 26.46 ? 400  ASP B CA    1 
ATOM   7183 C  C     . ASP B 1 400 ? -40.098 -2.010  35.067  1.00 25.82 ? 400  ASP B C     1 
ATOM   7184 O  O     . ASP B 1 400 ? -40.735 -2.818  35.672  1.00 27.40 ? 400  ASP B O     1 
ATOM   7185 C  CB    . ASP B 1 400 ? -39.224 -2.631  32.792  1.00 25.11 ? 400  ASP B CB    1 
ATOM   7186 C  CG    . ASP B 1 400 ? -39.537 -2.832  31.320  1.00 25.74 ? 400  ASP B CG    1 
ATOM   7187 O  OD1   . ASP B 1 400 ? -40.377 -3.656  31.020  1.00 28.03 ? 400  ASP B OD1   1 
ATOM   7188 O  OD2   . ASP B 1 400 ? -38.946 -2.138  30.494  1.00 31.03 ? 400  ASP B OD2   1 
ATOM   7189 N  N     . ALA B 1 401 ? -39.218 -1.203  35.649  1.00 24.21 ? 401  ALA B N     1 
ATOM   7190 C  CA    . ALA B 1 401 ? -38.976 -1.210  37.101  1.00 26.89 ? 401  ALA B CA    1 
ATOM   7191 C  C     . ALA B 1 401 ? -40.293 -0.940  37.853  1.00 26.20 ? 401  ALA B C     1 
ATOM   7192 O  O     . ALA B 1 401 ? -40.639 -1.732  38.730  1.00 24.97 ? 401  ALA B O     1 
ATOM   7193 C  CB    . ALA B 1 401 ? -37.898 -0.215  37.416  1.00 27.14 ? 401  ALA B CB    1 
ATOM   7194 N  N     . ILE B 1 402 ? -41.038 0.111   37.509  1.00 25.98 ? 402  ILE B N     1 
ATOM   7195 C  CA    . ILE B 1 402 ? -42.204 0.521   38.347  1.00 27.89 ? 402  ILE B CA    1 
ATOM   7196 C  C     . ILE B 1 402 ? -43.353 -0.463  38.129  1.00 28.55 ? 402  ILE B C     1 
ATOM   7197 O  O     . ILE B 1 402 ? -44.067 -0.772  39.122  1.00 26.24 ? 402  ILE B O     1 
ATOM   7198 C  CB    . ILE B 1 402 ? -42.637 1.977   38.106  1.00 28.18 ? 402  ILE B CB    1 
ATOM   7199 C  CG1   . ILE B 1 402 ? -43.565 2.399   39.246  1.00 30.75 ? 402  ILE B CG1   1 
ATOM   7200 C  CG2   . ILE B 1 402 ? -43.280 2.187   36.733  1.00 27.58 ? 402  ILE B CG2   1 
ATOM   7201 C  CD1   . ILE B 1 402 ? -43.163 3.679   39.854  1.00 32.42 ? 402  ILE B CD1   1 
ATOM   7202 N  N     . LYS B 1 403 ? -43.514 -0.945  36.891  1.00 28.31 ? 403  LYS B N     1 
ATOM   7203 C  CA    . LYS B 1 403 ? -44.477 -2.023  36.564  1.00 29.07 ? 403  LYS B CA    1 
ATOM   7204 C  C     . LYS B 1 403 ? -44.223 -3.204  37.509  1.00 30.59 ? 403  LYS B C     1 
ATOM   7205 O  O     . LYS B 1 403 ? -45.161 -3.676  38.169  1.00 32.71 ? 403  LYS B O     1 
ATOM   7206 C  CB    . LYS B 1 403 ? -44.368 -2.517  35.119  1.00 30.94 ? 403  LYS B CB    1 
ATOM   7207 C  CG    . LYS B 1 403 ? -45.578 -3.344  34.709  1.00 33.48 ? 403  LYS B CG    1 
ATOM   7208 C  CD    . LYS B 1 403 ? -45.379 -4.251  33.550  1.00 35.24 ? 403  LYS B CD    1 
ATOM   7209 C  CE    . LYS B 1 403 ? -45.086 -3.508  32.269  1.00 37.87 ? 403  LYS B CE    1 
ATOM   7210 N  NZ    . LYS B 1 403 ? -44.881 -4.465  31.154  1.00 37.46 ? 403  LYS B NZ    1 
ATOM   7211 N  N     . GLN B 1 404 ? -42.997 -3.699  37.565  1.00 29.05 ? 404  GLN B N     1 
ATOM   7212 C  CA    . GLN B 1 404 ? -42.711 -4.916  38.367  1.00 30.88 ? 404  GLN B CA    1 
ATOM   7213 C  C     . GLN B 1 404 ? -42.896 -4.583  39.857  1.00 28.74 ? 404  GLN B C     1 
ATOM   7214 O  O     . GLN B 1 404 ? -43.505 -5.383  40.566  1.00 27.78 ? 404  GLN B O     1 
ATOM   7215 C  CB    . GLN B 1 404 ? -41.337 -5.482  38.012  1.00 28.83 ? 404  GLN B CB    1 
ATOM   7216 C  CG    . GLN B 1 404 ? -41.354 -6.242  36.699  1.00 28.12 ? 404  GLN B CG    1 
ATOM   7217 C  CD    . GLN B 1 404 ? -39.952 -6.583  36.270  1.00 26.60 ? 404  GLN B CD    1 
ATOM   7218 O  OE1   . GLN B 1 404 ? -39.475 -7.691  36.495  1.00 27.61 ? 404  GLN B OE1   1 
ATOM   7219 N  NE2   . GLN B 1 404 ? -39.265 -5.600  35.709  1.00 25.77 ? 404  GLN B NE2   1 
ATOM   7220 N  N     . TYR B 1 405 ? -42.431 -3.429  40.311  1.00 29.31 ? 405  TYR B N     1 
ATOM   7221 C  CA    . TYR B 1 405 ? -42.611 -3.026  41.724  1.00 32.46 ? 405  TYR B CA    1 
ATOM   7222 C  C     . TYR B 1 405 ? -44.096 -3.071  42.080  1.00 33.10 ? 405  TYR B C     1 
ATOM   7223 O  O     . TYR B 1 405 ? -44.421 -3.705  43.072  1.00 34.16 ? 405  TYR B O     1 
ATOM   7224 C  CB    . TYR B 1 405 ? -42.071 -1.636  42.015  1.00 33.48 ? 405  TYR B CB    1 
ATOM   7225 C  CG    . TYR B 1 405 ? -42.553 -1.104  43.334  1.00 35.17 ? 405  TYR B CG    1 
ATOM   7226 C  CD1   . TYR B 1 405 ? -42.185 -1.706  44.525  1.00 37.87 ? 405  TYR B CD1   1 
ATOM   7227 C  CD2   . TYR B 1 405 ? -43.407 -0.017  43.393  1.00 41.41 ? 405  TYR B CD2   1 
ATOM   7228 C  CE1   . TYR B 1 405 ? -42.615 -1.216  45.750  1.00 39.50 ? 405  TYR B CE1   1 
ATOM   7229 C  CE2   . TYR B 1 405 ? -43.863 0.476   44.607  1.00 43.20 ? 405  TYR B CE2   1 
ATOM   7230 C  CZ    . TYR B 1 405 ? -43.473 -0.130  45.788  1.00 41.81 ? 405  TYR B CZ    1 
ATOM   7231 O  OH    . TYR B 1 405 ? -43.933 0.354   46.975  1.00 42.87 ? 405  TYR B OH    1 
ATOM   7232 N  N     . ASN B 1 406 ? -44.952 -2.434  41.282  1.00 33.83 ? 406  ASN B N     1 
ATOM   7233 C  CA    . ASN B 1 406 ? -46.408 -2.360  41.575  1.00 36.50 ? 406  ASN B CA    1 
ATOM   7234 C  C     . ASN B 1 406 ? -47.031 -3.752  41.487  1.00 33.15 ? 406  ASN B C     1 
ATOM   7235 O  O     . ASN B 1 406 ? -47.827 -4.074  42.376  1.00 32.06 ? 406  ASN B O     1 
ATOM   7236 C  CB    . ASN B 1 406 ? -47.146 -1.360  40.684  1.00 35.73 ? 406  ASN B CB    1 
ATOM   7237 C  CG    . ASN B 1 406 ? -46.734 0.058   40.999  1.00 39.04 ? 406  ASN B CG    1 
ATOM   7238 O  OD1   . ASN B 1 406 ? -46.368 0.363   42.132  1.00 45.55 ? 406  ASN B OD1   1 
ATOM   7239 N  ND2   . ASN B 1 406 ? -46.731 0.920   39.995  1.00 41.45 ? 406  ASN B ND2   1 
ATOM   7240 N  N     . MET B 1 407 ? -46.740 -4.541  40.452  1.00 33.56 ? 407  MET B N     1 
ATOM   7241 C  CA    . MET B 1 407 ? -47.465 -5.826  40.254  1.00 35.43 ? 407  MET B CA    1 
ATOM   7242 C  C     . MET B 1 407 ? -47.017 -6.853  41.311  1.00 37.70 ? 407  MET B C     1 
ATOM   7243 O  O     . MET B 1 407 ? -47.829 -7.741  41.653  1.00 41.37 ? 407  MET B O     1 
ATOM   7244 C  CB    . MET B 1 407 ? -47.309 -6.386  38.833  1.00 38.36 ? 407  MET B CB    1 
ATOM   7245 C  CG    . MET B 1 407 ? -45.902 -6.799  38.428  1.00 43.15 ? 407  MET B CG    1 
ATOM   7246 S  SD    . MET B 1 407 ? -45.733 -6.979  36.614  1.00 41.79 ? 407  MET B SD    1 
ATOM   7247 C  CE    . MET B 1 407 ? -46.625 -8.504  36.312  1.00 41.36 ? 407  MET B CE    1 
ATOM   7248 N  N     . VAL B 1 408 ? -45.800 -6.733  41.846  1.00 34.46 ? 408  VAL B N     1 
ATOM   7249 C  CA    . VAL B 1 408 ? -45.261 -7.708  42.846  1.00 36.87 ? 408  VAL B CA    1 
ATOM   7250 C  C     . VAL B 1 408 ? -45.613 -7.251  44.282  1.00 35.02 ? 408  VAL B C     1 
ATOM   7251 O  O     . VAL B 1 408 ? -46.061 -8.092  45.076  1.00 34.08 ? 408  VAL B O     1 
ATOM   7252 C  CB    . VAL B 1 408 ? -43.744 -7.926  42.674  1.00 32.61 ? 408  VAL B CB    1 
ATOM   7253 C  CG1   . VAL B 1 408 ? -43.163 -8.718  43.852  1.00 33.16 ? 408  VAL B CG1   1 
ATOM   7254 C  CG2   . VAL B 1 408 ? -43.426 -8.611  41.356  1.00 32.06 ? 408  VAL B CG2   1 
ATOM   7255 N  N     . SER B 1 409 ? -45.360 -5.990  44.622  1.00 36.97 ? 409  SER B N     1 
ATOM   7256 C  CA    . SER B 1 409 ? -45.542 -5.456  45.995  1.00 40.73 ? 409  SER B CA    1 
ATOM   7257 C  C     . SER B 1 409 ? -46.999 -5.679  46.389  1.00 41.64 ? 409  SER B C     1 
ATOM   7258 O  O     . SER B 1 409 ? -47.238 -6.163  47.506  1.00 39.99 ? 409  SER B O     1 
ATOM   7259 C  CB    . SER B 1 409 ? -45.097 -4.002  46.135  1.00 41.63 ? 409  SER B CB    1 
ATOM   7260 O  OG    . SER B 1 409 ? -45.843 -3.123  45.299  1.00 41.62 ? 409  SER B OG    1 
ATOM   7261 N  N     . SER B 1 410 ? -47.918 -5.403  45.467  1.00 39.76 ? 410  SER B N     1 
ATOM   7262 C  CA    . SER B 1 410 ? -49.372 -5.561  45.682  1.00 41.67 ? 410  SER B CA    1 
ATOM   7263 C  C     . SER B 1 410 ? -49.691 -7.030  45.983  1.00 40.42 ? 410  SER B C     1 
ATOM   7264 O  O     . SER B 1 410 ? -50.467 -7.281  46.932  1.00 38.39 ? 410  SER B O     1 
ATOM   7265 C  CB    . SER B 1 410 ? -50.169 -5.017  44.508  1.00 42.26 ? 410  SER B CB    1 
ATOM   7266 O  OG    . SER B 1 410 ? -49.695 -5.553  43.291  1.00 44.88 ? 410  SER B OG    1 
ATOM   7267 N  N     . ARG B 1 411 ? -49.142 -7.970  45.213  1.00 37.58 ? 411  ARG B N     1 
ATOM   7268 C  CA    . ARG B 1 411 ? -49.474 -9.416  45.349  1.00 37.87 ? 411  ARG B CA    1 
ATOM   7269 C  C     . ARG B 1 411 ? -48.916 -9.999  46.649  1.00 36.58 ? 411  ARG B C     1 
ATOM   7270 O  O     . ARG B 1 411 ? -49.597 -10.789 47.292  1.00 34.77 ? 411  ARG B O     1 
ATOM   7271 C  CB    . ARG B 1 411 ? -48.880 -10.233 44.206  1.00 39.04 ? 411  ARG B CB    1 
ATOM   7272 C  CG    . ARG B 1 411 ? -49.641 -10.094 42.907  1.00 39.30 ? 411  ARG B CG    1 
ATOM   7273 C  CD    . ARG B 1 411 ? -50.985 -10.763 43.027  1.00 39.58 ? 411  ARG B CD    1 
ATOM   7274 N  NE    . ARG B 1 411 ? -51.684 -10.664 41.765  1.00 40.86 ? 411  ARG B NE    1 
ATOM   7275 C  CZ    . ARG B 1 411 ? -52.948 -10.990 41.582  1.00 45.06 ? 411  ARG B CZ    1 
ATOM   7276 N  NH1   . ARG B 1 411 ? -53.681 -11.421 42.595  1.00 48.65 ? 411  ARG B NH1   1 
ATOM   7277 N  NH2   . ARG B 1 411 ? -53.483 -10.870 40.385  1.00 43.38 ? 411  ARG B NH2   1 
ATOM   7278 N  N     . VAL B 1 412 ? -47.675 -9.672  46.971  1.00 38.08 ? 412  VAL B N     1 
ATOM   7279 C  CA    . VAL B 1 412 ? -46.947 -10.232 48.146  1.00 36.95 ? 412  VAL B CA    1 
ATOM   7280 C  C     . VAL B 1 412 ? -47.667 -9.753  49.422  1.00 37.77 ? 412  VAL B C     1 
ATOM   7281 O  O     . VAL B 1 412 ? -47.934 -10.601 50.316  1.00 34.76 ? 412  VAL B O     1 
ATOM   7282 C  CB    . VAL B 1 412 ? -45.470 -9.792  48.100  1.00 38.60 ? 412  VAL B CB    1 
ATOM   7283 C  CG1   . VAL B 1 412 ? -44.753 -10.019 49.422  1.00 41.46 ? 412  VAL B CG1   1 
ATOM   7284 C  CG2   . VAL B 1 412 ? -44.702 -10.443 46.954  1.00 36.37 ? 412  VAL B CG2   1 
ATOM   7285 N  N     . ARG B 1 413 ? -47.973 -8.444  49.483  1.00 35.73 ? 413  ARG B N     1 
ATOM   7286 C  CA    . ARG B 1 413 ? -48.742 -7.775  50.571  1.00 35.75 ? 413  ARG B CA    1 
ATOM   7287 C  C     . ARG B 1 413 ? -50.132 -8.415  50.641  1.00 37.48 ? 413  ARG B C     1 
ATOM   7288 O  O     . ARG B 1 413 ? -50.501 -8.838  51.737  1.00 38.63 ? 413  ARG B O     1 
ATOM   7289 C  CB    . ARG B 1 413 ? -48.703 -6.253  50.412  1.00 33.88 ? 413  ARG B CB    1 
ATOM   7290 C  CG    . ARG B 1 413 ? -47.334 -5.675  50.773  1.00 35.33 ? 413  ARG B CG    1 
ATOM   7291 C  CD    . ARG B 1 413 ? -47.155 -4.170  50.642  1.00 34.15 ? 413  ARG B CD    1 
ATOM   7292 N  NE    . ARG B 1 413 ? -48.116 -3.459  51.482  1.00 37.14 ? 413  ARG B NE    1 
ATOM   7293 C  CZ    . ARG B 1 413 ? -47.928 -3.032  52.742  1.00 37.66 ? 413  ARG B CZ    1 
ATOM   7294 N  NH1   . ARG B 1 413 ? -46.791 -3.198  53.397  1.00 35.49 ? 413  ARG B NH1   1 
ATOM   7295 N  NH2   . ARG B 1 413 ? -48.915 -2.412  53.358  1.00 44.68 ? 413  ARG B NH2   1 
ATOM   7296 N  N     . GLU B 1 414 ? -50.777 -8.643  49.495  1.00 40.87 ? 414  GLU B N     1 
ATOM   7297 C  CA    . GLU B 1 414 ? -52.086 -9.342  49.391  1.00 40.72 ? 414  GLU B CA    1 
ATOM   7298 C  C     . GLU B 1 414 ? -52.040 -10.681 50.140  1.00 41.20 ? 414  GLU B C     1 
ATOM   7299 O  O     . GLU B 1 414 ? -53.029 -10.959 50.826  1.00 41.23 ? 414  GLU B O     1 
ATOM   7300 C  CB    . GLU B 1 414 ? -52.508 -9.517  47.925  1.00 42.35 ? 414  GLU B CB    1 
ATOM   7301 C  CG    . GLU B 1 414 ? -53.734 -10.399 47.719  1.00 43.33 ? 414  GLU B CG    1 
ATOM   7302 C  CD    . GLU B 1 414 ? -54.054 -10.729 46.263  1.00 49.38 ? 414  GLU B CD    1 
ATOM   7303 O  OE1   . GLU B 1 414 ? -53.380 -10.177 45.371  1.00 46.59 ? 414  GLU B OE1   1 
ATOM   7304 O  OE2   . GLU B 1 414 ? -54.974 -11.560 46.015  1.00 50.72 ? 414  GLU B OE2   1 
ATOM   7305 N  N     . TYR B 1 415 ? -50.967 -11.480 50.006  1.00 40.79 ? 415  TYR B N     1 
ATOM   7306 C  CA    . TYR B 1 415 ? -50.819 -12.828 50.635  1.00 36.27 ? 415  TYR B CA    1 
ATOM   7307 C  C     . TYR B 1 415 ? -50.228 -12.720 52.057  1.00 36.04 ? 415  TYR B C     1 
ATOM   7308 O  O     . TYR B 1 415 ? -49.921 -13.761 52.637  1.00 42.49 ? 415  TYR B O     1 
ATOM   7309 C  CB    . TYR B 1 415 ? -50.033 -13.764 49.708  1.00 35.39 ? 415  TYR B CB    1 
ATOM   7310 C  CG    . TYR B 1 415 ? -50.883 -14.329 48.593  1.00 36.21 ? 415  TYR B CG    1 
ATOM   7311 C  CD1   . TYR B 1 415 ? -51.226 -13.557 47.496  1.00 36.47 ? 415  TYR B CD1   1 
ATOM   7312 C  CD2   . TYR B 1 415 ? -51.374 -15.622 48.646  1.00 35.43 ? 415  TYR B CD2   1 
ATOM   7313 C  CE1   . TYR B 1 415 ? -52.037 -14.048 46.484  1.00 36.54 ? 415  TYR B CE1   1 
ATOM   7314 C  CE2   . TYR B 1 415 ? -52.196 -16.130 47.650  1.00 37.21 ? 415  TYR B CE2   1 
ATOM   7315 C  CZ    . TYR B 1 415 ? -52.529 -15.337 46.565  1.00 37.50 ? 415  TYR B CZ    1 
ATOM   7316 O  OH    . TYR B 1 415 ? -53.338 -15.814 45.578  1.00 40.56 ? 415  TYR B OH    1 
ATOM   7317 N  N     . GLY B 1 416 ? -50.061 -11.510 52.598  1.00 36.64 ? 416  GLY B N     1 
ATOM   7318 C  CA    . GLY B 1 416 ? -49.759 -11.257 54.022  1.00 37.18 ? 416  GLY B CA    1 
ATOM   7319 C  C     . GLY B 1 416 ? -48.276 -11.117 54.353  1.00 39.24 ? 416  GLY B C     1 
ATOM   7320 O  O     . GLY B 1 416 ? -47.966 -11.054 55.571  1.00 41.61 ? 416  GLY B O     1 
ATOM   7321 N  N     . PHE B 1 417 ? -47.376 -11.091 53.360  1.00 34.63 ? 417  PHE B N     1 
ATOM   7322 C  CA    . PHE B 1 417 ? -45.907 -10.987 53.580  1.00 33.38 ? 417  PHE B CA    1 
ATOM   7323 C  C     . PHE B 1 417 ? -45.488 -9.531  53.434  1.00 32.99 ? 417  PHE B C     1 
ATOM   7324 O  O     . PHE B 1 417 ? -46.144 -8.838  52.644  1.00 38.28 ? 417  PHE B O     1 
ATOM   7325 C  CB    . PHE B 1 417 ? -45.125 -11.859 52.595  1.00 32.92 ? 417  PHE B CB    1 
ATOM   7326 C  CG    . PHE B 1 417 ? -45.548 -13.305 52.558  1.00 31.66 ? 417  PHE B CG    1 
ATOM   7327 C  CD1   . PHE B 1 417 ? -45.112 -14.200 53.519  1.00 33.69 ? 417  PHE B CD1   1 
ATOM   7328 C  CD2   . PHE B 1 417 ? -46.382 -13.780 51.567  1.00 32.44 ? 417  PHE B CD2   1 
ATOM   7329 C  CE1   . PHE B 1 417 ? -45.514 -15.531 53.494  1.00 30.99 ? 417  PHE B CE1   1 
ATOM   7330 C  CE2   . PHE B 1 417 ? -46.775 -15.116 51.538  1.00 31.25 ? 417  PHE B CE2   1 
ATOM   7331 C  CZ    . PHE B 1 417 ? -46.333 -15.990 52.497  1.00 29.04 ? 417  PHE B CZ    1 
ATOM   7332 N  N     . ASP B 1 418 ? -44.467 -9.063  54.164  1.00 31.38 ? 418  ASP B N     1 
ATOM   7333 C  CA    . ASP B 1 418 ? -43.911 -7.711  53.880  1.00 31.73 ? 418  ASP B CA    1 
ATOM   7334 C  C     . ASP B 1 418 ? -43.261 -7.825  52.489  1.00 36.92 ? 418  ASP B C     1 
ATOM   7335 O  O     . ASP B 1 418 ? -42.712 -8.925  52.130  1.00 37.18 ? 418  ASP B O     1 
ATOM   7336 C  CB    . ASP B 1 418 ? -43.021 -7.116  55.000  1.00 30.97 ? 418  ASP B CB    1 
ATOM   7337 C  CG    . ASP B 1 418 ? -43.729 -6.252  56.080  1.00 25.12 ? 418  ASP B CG    1 
ATOM   7338 O  OD1   . ASP B 1 418 ? -44.338 -5.302  55.786  1.00 17.54 ? 418  ASP B OD1   1 
ATOM   7339 O  OD2   . ASP B 1 418 ? -43.589 -6.551  57.224  1.00 27.89 ? 418  ASP B OD2   1 
ATOM   7340 N  N     . TYR B 1 419 ? -43.377 -6.763  51.694  1.00 33.33 ? 419  TYR B N     1 
ATOM   7341 C  CA    . TYR B 1 419 ? -42.612 -6.640  50.442  1.00 32.10 ? 419  TYR B CA    1 
ATOM   7342 C  C     . TYR B 1 419 ? -41.173 -6.346  50.826  1.00 31.19 ? 419  TYR B C     1 
ATOM   7343 O  O     . TYR B 1 419 ? -40.911 -5.358  51.520  1.00 31.04 ? 419  TYR B O     1 
ATOM   7344 C  CB    . TYR B 1 419 ? -43.164 -5.567  49.513  1.00 30.00 ? 419  TYR B CB    1 
ATOM   7345 C  CG    . TYR B 1 419 ? -42.261 -5.278  48.347  1.00 29.47 ? 419  TYR B CG    1 
ATOM   7346 C  CD1   . TYR B 1 419 ? -42.216 -6.100  47.229  1.00 29.27 ? 419  TYR B CD1   1 
ATOM   7347 C  CD2   . TYR B 1 419 ? -41.478 -4.143  48.344  1.00 29.54 ? 419  TYR B CD2   1 
ATOM   7348 C  CE1   . TYR B 1 419 ? -41.397 -5.809  46.143  1.00 29.70 ? 419  TYR B CE1   1 
ATOM   7349 C  CE2   . TYR B 1 419 ? -40.676 -3.828  47.266  1.00 31.49 ? 419  TYR B CE2   1 
ATOM   7350 C  CZ    . TYR B 1 419 ? -40.618 -4.671  46.172  1.00 31.15 ? 419  TYR B CZ    1 
ATOM   7351 O  OH    . TYR B 1 419 ? -39.779 -4.329  45.158  1.00 35.67 ? 419  TYR B OH    1 
ATOM   7352 N  N     . MET B 1 420 ? -40.282 -7.235  50.413  1.00 30.50 ? 420  MET B N     1 
ATOM   7353 C  CA    . MET B 1 420 ? -38.831 -6.976  50.392  1.00 31.15 ? 420  MET B CA    1 
ATOM   7354 C  C     . MET B 1 420 ? -38.375 -7.220  48.961  1.00 31.39 ? 420  MET B C     1 
ATOM   7355 O  O     . MET B 1 420 ? -38.694 -8.281  48.392  1.00 37.00 ? 420  MET B O     1 
ATOM   7356 C  CB    . MET B 1 420 ? -38.085 -7.905  51.336  1.00 33.04 ? 420  MET B CB    1 
ATOM   7357 C  CG    . MET B 1 420 ? -38.676 -7.963  52.719  1.00 34.79 ? 420  MET B CG    1 
ATOM   7358 S  SD    . MET B 1 420 ? -37.682 -9.150  53.628  1.00 37.53 ? 420  MET B SD    1 
ATOM   7359 C  CE    . MET B 1 420 ? -38.139 -8.780  55.323  1.00 37.71 ? 420  MET B CE    1 
ATOM   7360 N  N     . GLY B 1 421 ? -37.755 -6.224  48.369  1.00 30.84 ? 421  GLY B N     1 
ATOM   7361 C  CA    . GLY B 1 421 ? -37.464 -6.246  46.934  1.00 30.28 ? 421  GLY B CA    1 
ATOM   7362 C  C     . GLY B 1 421 ? -36.255 -5.418  46.606  1.00 28.94 ? 421  GLY B C     1 
ATOM   7363 O  O     . GLY B 1 421 ? -35.819 -4.601  47.444  1.00 27.38 ? 421  GLY B O     1 
ATOM   7364 N  N     . LEU B 1 422 ? -35.719 -5.636  45.412  1.00 30.02 ? 422  LEU B N     1 
ATOM   7365 C  CA    . LEU B 1 422 ? -34.646 -4.776  44.900  1.00 30.98 ? 422  LEU B CA    1 
ATOM   7366 C  C     . LEU B 1 422 ? -34.690 -4.778  43.376  1.00 27.53 ? 422  LEU B C     1 
ATOM   7367 O  O     . LEU B 1 422 ? -35.347 -5.649  42.813  1.00 28.55 ? 422  LEU B O     1 
ATOM   7368 C  CB    . LEU B 1 422 ? -33.332 -5.264  45.508  1.00 32.76 ? 422  LEU B CB    1 
ATOM   7369 C  CG    . LEU B 1 422 ? -32.862 -6.646  45.064  1.00 34.76 ? 422  LEU B CG    1 
ATOM   7370 C  CD1   . LEU B 1 422 ? -31.964 -6.533  43.841  1.00 37.67 ? 422  LEU B CD1   1 
ATOM   7371 C  CD2   . LEU B 1 422 ? -32.115 -7.334  46.189  1.00 33.44 ? 422  LEU B CD2   1 
ATOM   7372 N  N     . LEU B 1 423 ? -34.153 -3.718  42.779  1.00 27.00 ? 423  LEU B N     1 
ATOM   7373 C  CA    . LEU B 1 423 ? -33.855 -3.593  41.332  1.00 26.83 ? 423  LEU B CA    1 
ATOM   7374 C  C     . LEU B 1 423 ? -32.337 -3.753  41.261  1.00 28.56 ? 423  LEU B C     1 
ATOM   7375 O  O     . LEU B 1 423 ? -31.645 -2.949  41.897  1.00 30.15 ? 423  LEU B O     1 
ATOM   7376 C  CB    . LEU B 1 423 ? -34.303 -2.222  40.803  1.00 28.31 ? 423  LEU B CB    1 
ATOM   7377 C  CG    . LEU B 1 423 ? -35.807 -1.971  40.639  1.00 28.49 ? 423  LEU B CG    1 
ATOM   7378 C  CD1   . LEU B 1 423 ? -36.463 -2.952  39.695  1.00 29.26 ? 423  LEU B CD1   1 
ATOM   7379 C  CD2   . LEU B 1 423 ? -36.545 -1.989  41.972  1.00 29.23 ? 423  LEU B CD2   1 
ATOM   7380 N  N     . ALA B 1 424 ? -31.844 -4.821  40.631  1.00 29.21 ? 424  ALA B N     1 
ATOM   7381 C  CA    . ALA B 1 424 ? -30.402 -5.075  40.404  1.00 27.26 ? 424  ALA B CA    1 
ATOM   7382 C  C     . ALA B 1 424 ? -30.101 -4.952  38.902  1.00 27.74 ? 424  ALA B C     1 
ATOM   7383 O  O     . ALA B 1 424 ? -30.936 -5.391  38.042  1.00 29.57 ? 424  ALA B O     1 
ATOM   7384 C  CB    . ALA B 1 424 ? -30.032 -6.435  40.941  1.00 23.99 ? 424  ALA B CB    1 
ATOM   7385 N  N     . ILE B 1 425 ? -28.932 -4.406  38.580  1.00 28.65 ? 425  ILE B N     1 
ATOM   7386 C  CA    . ILE B 1 425 ? -28.448 -4.302  37.176  1.00 26.83 ? 425  ILE B CA    1 
ATOM   7387 C  C     . ILE B 1 425 ? -27.045 -4.911  37.095  1.00 25.58 ? 425  ILE B C     1 
ATOM   7388 O  O     . ILE B 1 425 ? -26.145 -4.439  37.803  1.00 23.83 ? 425  ILE B O     1 
ATOM   7389 C  CB    . ILE B 1 425 ? -28.489 -2.848  36.664  1.00 27.75 ? 425  ILE B CB    1 
ATOM   7390 C  CG1   . ILE B 1 425 ? -29.896 -2.251  36.711  1.00 30.76 ? 425  ILE B CG1   1 
ATOM   7391 C  CG2   . ILE B 1 425 ? -27.892 -2.746  35.265  1.00 30.12 ? 425  ILE B CG2   1 
ATOM   7392 C  CD1   . ILE B 1 425 ? -29.903 -0.738  36.601  1.00 31.57 ? 425  ILE B CD1   1 
ATOM   7393 N  N     . GLY B 1 426 ? -26.884 -5.894  36.202  1.00 25.80 ? 426  GLY B N     1 
ATOM   7394 C  CA    . GLY B 1 426 ? -25.598 -6.522  35.877  1.00 26.30 ? 426  GLY B CA    1 
ATOM   7395 C  C     . GLY B 1 426 ? -24.780 -5.592  35.013  1.00 27.67 ? 426  GLY B C     1 
ATOM   7396 O  O     . GLY B 1 426 ? -23.800 -5.019  35.552  1.00 29.03 ? 426  GLY B O     1 
ATOM   7397 N  N     . TRP B 1 427 ? -25.161 -5.489  33.731  1.00 26.25 ? 427  TRP B N     1 
ATOM   7398 C  CA    . TRP B 1 427 ? -24.521 -4.629  32.699  1.00 25.36 ? 427  TRP B CA    1 
ATOM   7399 C  C     . TRP B 1 427 ? -25.615 -4.006  31.819  1.00 22.38 ? 427  TRP B C     1 
ATOM   7400 O  O     . TRP B 1 427 ? -25.777 -2.784  31.850  1.00 24.48 ? 427  TRP B O     1 
ATOM   7401 C  CB    . TRP B 1 427 ? -23.472 -5.417  31.888  1.00 23.44 ? 427  TRP B CB    1 
ATOM   7402 C  CG    . TRP B 1 427 ? -22.615 -4.563  31.000  1.00 23.36 ? 427  TRP B CG    1 
ATOM   7403 C  CD1   . TRP B 1 427 ? -22.641 -3.197  30.898  1.00 23.18 ? 427  TRP B CD1   1 
ATOM   7404 C  CD2   . TRP B 1 427 ? -21.560 -4.990  30.113  1.00 23.82 ? 427  TRP B CD2   1 
ATOM   7405 N  NE1   . TRP B 1 427 ? -21.695 -2.757  30.018  1.00 21.84 ? 427  TRP B NE1   1 
ATOM   7406 C  CE2   . TRP B 1 427 ? -21.017 -3.827  29.517  1.00 22.74 ? 427  TRP B CE2   1 
ATOM   7407 C  CE3   . TRP B 1 427 ? -20.990 -6.224  29.792  1.00 24.66 ? 427  TRP B CE3   1 
ATOM   7408 C  CZ2   . TRP B 1 427 ? -19.960 -3.868  28.609  1.00 24.43 ? 427  TRP B CZ2   1 
ATOM   7409 C  CZ3   . TRP B 1 427 ? -19.945 -6.267  28.896  1.00 24.72 ? 427  TRP B CZ3   1 
ATOM   7410 C  CH2   . TRP B 1 427 ? -19.437 -5.103  28.314  1.00 25.46 ? 427  TRP B CH2   1 
ATOM   7411 N  N     . ARG B 1 428 ? -26.392 -4.819  31.110  1.00 21.95 ? 428  ARG B N     1 
ATOM   7412 C  CA    . ARG B 1 428 ? -27.515 -4.328  30.260  1.00 20.87 ? 428  ARG B CA    1 
ATOM   7413 C  C     . ARG B 1 428 ? -28.849 -4.881  30.773  1.00 19.49 ? 428  ARG B C     1 
ATOM   7414 O  O     . ARG B 1 428 ? -29.859 -4.688  30.114  1.00 19.18 ? 428  ARG B O     1 
ATOM   7415 C  CB    . ARG B 1 428 ? -27.241 -4.724  28.811  1.00 19.91 ? 428  ARG B CB    1 
ATOM   7416 C  CG    . ARG B 1 428 ? -26.215 -3.837  28.122  1.00 18.80 ? 428  ARG B CG    1 
ATOM   7417 C  CD    . ARG B 1 428 ? -25.895 -4.423  26.764  1.00 19.52 ? 428  ARG B CD    1 
ATOM   7418 N  NE    . ARG B 1 428 ? -25.114 -3.548  25.898  1.00 19.35 ? 428  ARG B NE    1 
ATOM   7419 C  CZ    . ARG B 1 428 ? -23.804 -3.363  25.963  1.00 19.23 ? 428  ARG B CZ    1 
ATOM   7420 N  NH1   . ARG B 1 428 ? -23.070 -3.980  26.873  1.00 19.62 ? 428  ARG B NH1   1 
ATOM   7421 N  NH2   . ARG B 1 428 ? -23.215 -2.558  25.097  1.00 20.45 ? 428  ARG B NH2   1 
ATOM   7422 N  N     . ASP B 1 429 ? -28.828 -5.583  31.899  1.00 20.13 ? 429  ASP B N     1 
ATOM   7423 C  CA    . ASP B 1 429 ? -29.941 -6.457  32.354  1.00 21.49 ? 429  ASP B CA    1 
ATOM   7424 C  C     . ASP B 1 429 ? -30.479 -5.884  33.663  1.00 22.15 ? 429  ASP B C     1 
ATOM   7425 O  O     . ASP B 1 429 ? -29.685 -5.670  34.589  1.00 23.98 ? 429  ASP B O     1 
ATOM   7426 C  CB    . ASP B 1 429 ? -29.507 -7.925  32.449  1.00 23.68 ? 429  ASP B CB    1 
ATOM   7427 C  CG    . ASP B 1 429 ? -28.371 -8.187  33.423  1.00 23.86 ? 429  ASP B CG    1 
ATOM   7428 O  OD1   . ASP B 1 429 ? -27.343 -7.505  33.302  1.00 22.24 ? 429  ASP B OD1   1 
ATOM   7429 O  OD2   . ASP B 1 429 ? -28.538 -9.070  34.291  1.00 24.87 ? 429  ASP B OD2   1 
ATOM   7430 N  N     . LEU B 1 430 ? -31.777 -5.597  33.690  1.00 26.65 ? 430  LEU B N     1 
ATOM   7431 C  CA    . LEU B 1 430 ? -32.541 -5.263  34.921  1.00 27.13 ? 430  LEU B CA    1 
ATOM   7432 C  C     . LEU B 1 430 ? -33.115 -6.546  35.512  1.00 27.78 ? 430  LEU B C     1 
ATOM   7433 O  O     . LEU B 1 430 ? -33.683 -7.360  34.765  1.00 26.52 ? 430  LEU B O     1 
ATOM   7434 C  CB    . LEU B 1 430 ? -33.681 -4.292  34.595  1.00 26.66 ? 430  LEU B CB    1 
ATOM   7435 C  CG    . LEU B 1 430 ? -34.489 -3.842  35.813  1.00 27.33 ? 430  LEU B CG    1 
ATOM   7436 C  CD1   . LEU B 1 430 ? -33.607 -3.046  36.777  1.00 28.03 ? 430  LEU B CD1   1 
ATOM   7437 C  CD2   . LEU B 1 430 ? -35.694 -3.022  35.399  1.00 28.14 ? 430  LEU B CD2   1 
ATOM   7438 N  N     . HIS B 1 431 ? -33.032 -6.668  36.833  1.00 27.52 ? 431  HIS B N     1 
ATOM   7439 C  CA    . HIS B 1 431 ? -33.779 -7.684  37.607  1.00 29.37 ? 431  HIS B CA    1 
ATOM   7440 C  C     . HIS B 1 431 ? -34.585 -6.982  38.703  1.00 27.81 ? 431  HIS B C     1 
ATOM   7441 O  O     . HIS B 1 431 ? -33.980 -6.316  39.561  1.00 26.80 ? 431  HIS B O     1 
ATOM   7442 C  CB    . HIS B 1 431 ? -32.814 -8.732  38.200  1.00 29.45 ? 431  HIS B CB    1 
ATOM   7443 C  CG    . HIS B 1 431 ? -31.947 -9.408  37.191  1.00 27.31 ? 431  HIS B CG    1 
ATOM   7444 N  ND1   . HIS B 1 431 ? -32.133 -10.729 36.829  1.00 29.24 ? 431  HIS B ND1   1 
ATOM   7445 C  CD2   . HIS B 1 431 ? -30.876 -8.980  36.493  1.00 29.68 ? 431  HIS B CD2   1 
ATOM   7446 C  CE1   . HIS B 1 431 ? -31.203 -11.082 35.950  1.00 27.65 ? 431  HIS B CE1   1 
ATOM   7447 N  NE2   . HIS B 1 431 ? -30.418 -10.033 35.724  1.00 26.60 ? 431  HIS B NE2   1 
ATOM   7448 N  N     . HIS B 1 432 ? -35.896 -7.137  38.684  1.00 27.26 ? 432  HIS B N     1 
ATOM   7449 C  CA    . HIS B 1 432 ? -36.728 -6.923  39.885  1.00 28.59 ? 432  HIS B CA    1 
ATOM   7450 C  C     . HIS B 1 432 ? -36.675 -8.221  40.666  1.00 26.80 ? 432  HIS B C     1 
ATOM   7451 O  O     . HIS B 1 432 ? -37.243 -9.223  40.165  1.00 27.15 ? 432  HIS B O     1 
ATOM   7452 C  CB    . HIS B 1 432 ? -38.182 -6.540  39.594  1.00 29.34 ? 432  HIS B CB    1 
ATOM   7453 C  CG    . HIS B 1 432 ? -38.969 -6.432  40.855  1.00 30.73 ? 432  HIS B CG    1 
ATOM   7454 N  ND1   . HIS B 1 432 ? -39.598 -7.518  41.436  1.00 32.06 ? 432  HIS B ND1   1 
ATOM   7455 C  CD2   . HIS B 1 432 ? -39.170 -5.388  41.690  1.00 34.82 ? 432  HIS B CD2   1 
ATOM   7456 C  CE1   . HIS B 1 432 ? -40.170 -7.141  42.561  1.00 33.85 ? 432  HIS B CE1   1 
ATOM   7457 N  NE2   . HIS B 1 432 ? -39.927 -5.832  42.736  1.00 32.01 ? 432  HIS B NE2   1 
ATOM   7458 N  N     . VAL B 1 433 ? -36.006 -8.192  41.814  1.00 25.82 ? 433  VAL B N     1 
ATOM   7459 C  CA    . VAL B 1 433 ? -35.843 -9.381  42.701  1.00 26.99 ? 433  VAL B CA    1 
ATOM   7460 C  C     . VAL B 1 433 ? -36.825 -9.245  43.866  1.00 28.21 ? 433  VAL B C     1 
ATOM   7461 O  O     . VAL B 1 433 ? -36.745 -8.250  44.621  1.00 26.89 ? 433  VAL B O     1 
ATOM   7462 C  CB    . VAL B 1 433 ? -34.385 -9.581  43.163  1.00 26.17 ? 433  VAL B CB    1 
ATOM   7463 C  CG1   . VAL B 1 433 ? -34.246 -10.817 44.047  1.00 24.31 ? 433  VAL B CG1   1 
ATOM   7464 C  CG2   . VAL B 1 433 ? -33.450 -9.687  41.965  1.00 24.84 ? 433  VAL B CG2   1 
ATOM   7465 N  N     . THR B 1 434 ? -37.752 -10.193 43.948  1.00 29.10 ? 434  THR B N     1 
ATOM   7466 C  CA    . THR B 1 434 ? -38.661 -10.403 45.091  1.00 29.83 ? 434  THR B CA    1 
ATOM   7467 C  C     . THR B 1 434 ? -38.031 -11.371 46.107  1.00 31.37 ? 434  THR B C     1 
ATOM   7468 O  O     . THR B 1 434 ? -37.783 -12.527 45.760  1.00 31.35 ? 434  THR B O     1 
ATOM   7469 C  CB    . THR B 1 434 ? -40.008 -10.928 44.601  1.00 35.03 ? 434  THR B CB    1 
ATOM   7470 O  OG1   . THR B 1 434 ? -40.423 -10.150 43.462  1.00 33.80 ? 434  THR B OG1   1 
ATOM   7471 C  CG2   . THR B 1 434 ? -41.035 -10.917 45.720  1.00 34.71 ? 434  THR B CG2   1 
ATOM   7472 N  N     . VAL B 1 435 ? -37.793 -10.892 47.332  1.00 30.87 ? 435  VAL B N     1 
ATOM   7473 C  CA    . VAL B 1 435 ? -37.374 -11.693 48.518  1.00 30.36 ? 435  VAL B CA    1 
ATOM   7474 C  C     . VAL B 1 435 ? -38.611 -11.916 49.402  1.00 31.33 ? 435  VAL B C     1 
ATOM   7475 O  O     . VAL B 1 435 ? -39.196 -10.909 49.910  1.00 32.69 ? 435  VAL B O     1 
ATOM   7476 C  CB    . VAL B 1 435 ? -36.264 -10.969 49.290  1.00 31.47 ? 435  VAL B CB    1 
ATOM   7477 C  CG1   . VAL B 1 435 ? -35.809 -11.781 50.504  1.00 32.81 ? 435  VAL B CG1   1 
ATOM   7478 C  CG2   . VAL B 1 435 ? -35.099 -10.632 48.378  1.00 32.07 ? 435  VAL B CG2   1 
ATOM   7479 N  N     . ILE B 1 436 ? -39.030 -13.168 49.548  1.00 28.43 ? 436  ILE B N     1 
ATOM   7480 C  CA    . ILE B 1 436 ? -40.209 -13.546 50.385  1.00 31.69 ? 436  ILE B CA    1 
ATOM   7481 C  C     . ILE B 1 436 ? -39.718 -14.338 51.606  1.00 31.10 ? 436  ILE B C     1 
ATOM   7482 O  O     . ILE B 1 436 ? -39.251 -15.506 51.416  1.00 32.45 ? 436  ILE B O     1 
ATOM   7483 C  CB    . ILE B 1 436 ? -41.232 -14.346 49.569  1.00 31.65 ? 436  ILE B CB    1 
ATOM   7484 C  CG1   . ILE B 1 436 ? -41.587 -13.643 48.258  1.00 31.66 ? 436  ILE B CG1   1 
ATOM   7485 C  CG2   . ILE B 1 436 ? -42.450 -14.626 50.431  1.00 34.51 ? 436  ILE B CG2   1 
ATOM   7486 C  CD1   . ILE B 1 436 ? -42.389 -14.488 47.307  1.00 32.36 ? 436  ILE B CD1   1 
ATOM   7487 N  N     . VAL B 1 437 ? -39.793 -13.717 52.785  1.00 27.47 ? 437  VAL B N     1 
ATOM   7488 C  CA    . VAL B 1 437 ? -39.475 -14.324 54.106  1.00 29.20 ? 437  VAL B CA    1 
ATOM   7489 C  C     . VAL B 1 437 ? -40.764 -14.939 54.649  1.00 31.25 ? 437  VAL B C     1 
ATOM   7490 O  O     . VAL B 1 437 ? -41.775 -14.229 54.739  1.00 33.31 ? 437  VAL B O     1 
ATOM   7491 C  CB    . VAL B 1 437 ? -38.890 -13.290 55.080  1.00 29.47 ? 437  VAL B CB    1 
ATOM   7492 C  CG1   . VAL B 1 437 ? -38.630 -13.902 56.441  1.00 30.41 ? 437  VAL B CG1   1 
ATOM   7493 C  CG2   . VAL B 1 437 ? -37.624 -12.633 54.542  1.00 29.73 ? 437  VAL B CG2   1 
ATOM   7494 N  N     . TYR B 1 438 ? -40.749 -16.225 54.967  1.00 32.97 ? 438  TYR B N     1 
ATOM   7495 C  CA    . TYR B 1 438 ? -41.952 -16.974 55.405  1.00 33.61 ? 438  TYR B CA    1 
ATOM   7496 C  C     . TYR B 1 438 ? -41.599 -17.948 56.529  1.00 35.79 ? 438  TYR B C     1 
ATOM   7497 O  O     . TYR B 1 438 ? -40.433 -18.427 56.616  1.00 35.42 ? 438  TYR B O     1 
ATOM   7498 C  CB    . TYR B 1 438 ? -42.552 -17.744 54.231  1.00 35.64 ? 438  TYR B CB    1 
ATOM   7499 C  CG    . TYR B 1 438 ? -41.648 -18.793 53.626  1.00 39.78 ? 438  TYR B CG    1 
ATOM   7500 C  CD1   . TYR B 1 438 ? -40.642 -18.429 52.742  1.00 37.76 ? 438  TYR B CD1   1 
ATOM   7501 C  CD2   . TYR B 1 438 ? -41.795 -20.148 53.926  1.00 42.38 ? 438  TYR B CD2   1 
ATOM   7502 C  CE1   . TYR B 1 438 ? -39.812 -19.370 52.156  1.00 39.26 ? 438  TYR B CE1   1 
ATOM   7503 C  CE2   . TYR B 1 438 ? -40.975 -21.108 53.342  1.00 42.19 ? 438  TYR B CE2   1 
ATOM   7504 C  CZ    . TYR B 1 438 ? -39.982 -20.713 52.455  1.00 42.69 ? 438  TYR B CZ    1 
ATOM   7505 O  OH    . TYR B 1 438 ? -39.136 -21.605 51.871  1.00 39.17 ? 438  TYR B OH    1 
ATOM   7506 N  N     . ASP B 1 439 ? -42.602 -18.302 57.328  1.00 37.34 ? 439  ASP B N     1 
ATOM   7507 C  CA    . ASP B 1 439 ? -42.471 -19.353 58.373  1.00 39.86 ? 439  ASP B CA    1 
ATOM   7508 C  C     . ASP B 1 439 ? -42.478 -20.736 57.699  1.00 39.29 ? 439  ASP B C     1 
ATOM   7509 O  O     . ASP B 1 439 ? -43.562 -21.235 57.353  1.00 35.98 ? 439  ASP B O     1 
ATOM   7510 C  CB    . ASP B 1 439 ? -43.588 -19.221 59.403  1.00 41.26 ? 439  ASP B CB    1 
ATOM   7511 C  CG    . ASP B 1 439 ? -43.403 -20.120 60.609  1.00 42.96 ? 439  ASP B CG    1 
ATOM   7512 O  OD1   . ASP B 1 439 ? -42.471 -20.939 60.594  1.00 43.27 ? 439  ASP B OD1   1 
ATOM   7513 O  OD2   . ASP B 1 439 ? -44.166 -19.942 61.567  1.00 47.22 ? 439  ASP B OD2   1 
ATOM   7514 N  N     . LYS B 1 440 ? -41.299 -21.326 57.494  1.00 41.47 ? 440  LYS B N     1 
ATOM   7515 C  CA    . LYS B 1 440 ? -41.133 -22.605 56.745  1.00 45.89 ? 440  LYS B CA    1 
ATOM   7516 C  C     . LYS B 1 440 ? -41.712 -23.788 57.551  1.00 43.61 ? 440  LYS B C     1 
ATOM   7517 O  O     . LYS B 1 440 ? -41.923 -24.861 56.967  1.00 43.18 ? 440  LYS B O     1 
ATOM   7518 C  CB    . LYS B 1 440 ? -39.655 -22.777 56.375  1.00 46.60 ? 440  LYS B CB    1 
ATOM   7519 C  CG    . LYS B 1 440 ? -38.679 -22.876 57.540  1.00 50.35 ? 440  LYS B CG    1 
ATOM   7520 C  CD    . LYS B 1 440 ? -38.546 -24.279 58.090  1.00 54.90 ? 440  LYS B CD    1 
ATOM   7521 C  CE    . LYS B 1 440 ? -37.465 -24.402 59.142  1.00 60.00 ? 440  LYS B CE    1 
ATOM   7522 N  NZ    . LYS B 1 440 ? -36.915 -25.780 59.184  1.00 62.77 ? 440  LYS B NZ    1 
ATOM   7523 N  N     . THR B 1 441 ? -41.956 -23.619 58.852  1.00 43.56 ? 441  THR B N     1 
ATOM   7524 C  CA    . THR B 1 441 ? -42.516 -24.683 59.729  1.00 44.95 ? 441  THR B CA    1 
ATOM   7525 C  C     . THR B 1 441 ? -44.049 -24.747 59.590  1.00 45.30 ? 441  THR B C     1 
ATOM   7526 O  O     . THR B 1 441 ? -44.627 -25.794 59.930  1.00 42.25 ? 441  THR B O     1 
ATOM   7527 C  CB    . THR B 1 441 ? -42.103 -24.461 61.190  1.00 44.76 ? 441  THR B CB    1 
ATOM   7528 O  OG1   . THR B 1 441 ? -42.800 -23.299 61.624  1.00 43.52 ? 441  THR B OG1   1 
ATOM   7529 C  CG2   . THR B 1 441 ? -40.619 -24.255 61.391  1.00 44.54 ? 441  THR B CG2   1 
ATOM   7530 N  N     . ASP B 1 442 ? -44.689 -23.678 59.109  1.00 45.42 ? 442  ASP B N     1 
ATOM   7531 C  CA    . ASP B 1 442 ? -46.168 -23.505 59.149  1.00 42.59 ? 442  ASP B CA    1 
ATOM   7532 C  C     . ASP B 1 442 ? -46.770 -23.907 57.806  1.00 42.12 ? 442  ASP B C     1 
ATOM   7533 O  O     . ASP B 1 442 ? -46.634 -23.189 56.821  1.00 40.05 ? 442  ASP B O     1 
ATOM   7534 C  CB    . ASP B 1 442 ? -46.519 -22.070 59.539  1.00 44.50 ? 442  ASP B CB    1 
ATOM   7535 C  CG    . ASP B 1 442 ? -48.012 -21.784 59.593  1.00 44.27 ? 442  ASP B CG    1 
ATOM   7536 O  OD1   . ASP B 1 442 ? -48.795 -22.576 59.027  1.00 44.29 ? 442  ASP B OD1   1 
ATOM   7537 O  OD2   . ASP B 1 442 ? -48.371 -20.752 60.180  1.00 48.36 ? 442  ASP B OD2   1 
ATOM   7538 N  N     . PRO B 1 443 ? -47.472 -25.058 57.727  1.00 41.71 ? 443  PRO B N     1 
ATOM   7539 C  CA    . PRO B 1 443 ? -48.100 -25.510 56.488  1.00 40.96 ? 443  PRO B CA    1 
ATOM   7540 C  C     . PRO B 1 443 ? -49.039 -24.502 55.812  1.00 42.07 ? 443  PRO B C     1 
ATOM   7541 O  O     . PRO B 1 443 ? -49.153 -24.541 54.603  1.00 42.95 ? 443  PRO B O     1 
ATOM   7542 C  CB    . PRO B 1 443 ? -48.930 -26.727 56.923  1.00 41.01 ? 443  PRO B CB    1 
ATOM   7543 C  CG    . PRO B 1 443 ? -48.183 -27.253 58.115  1.00 42.88 ? 443  PRO B CG    1 
ATOM   7544 C  CD    . PRO B 1 443 ? -47.654 -26.022 58.822  1.00 43.80 ? 443  PRO B CD    1 
ATOM   7545 N  N     . ASP B 1 444 ? -49.697 -23.640 56.587  1.00 41.27 ? 444  ASP B N     1 
ATOM   7546 C  CA    . ASP B 1 444 ? -50.625 -22.635 56.021  1.00 43.51 ? 444  ASP B CA    1 
ATOM   7547 C  C     . ASP B 1 444 ? -49.800 -21.590 55.266  1.00 41.84 ? 444  ASP B C     1 
ATOM   7548 O  O     . ASP B 1 444 ? -50.187 -21.255 54.133  1.00 45.25 ? 444  ASP B O     1 
ATOM   7549 C  CB    . ASP B 1 444 ? -51.511 -22.014 57.101  1.00 48.71 ? 444  ASP B CB    1 
ATOM   7550 C  CG    . ASP B 1 444 ? -52.642 -22.919 57.568  1.00 56.98 ? 444  ASP B CG    1 
ATOM   7551 O  OD1   . ASP B 1 444 ? -52.556 -24.153 57.381  1.00 61.06 ? 444  ASP B OD1   1 
ATOM   7552 O  OD2   . ASP B 1 444 ? -53.612 -22.380 58.118  1.00 67.70 ? 444  ASP B OD2   1 
ATOM   7553 N  N     . GLU B 1 445 ? -48.727 -21.077 55.877  1.00 40.02 ? 445  GLU B N     1 
ATOM   7554 C  CA    . GLU B 1 445 ? -47.829 -20.077 55.240  1.00 43.27 ? 445  GLU B CA    1 
ATOM   7555 C  C     . GLU B 1 445 ? -47.205 -20.676 53.963  1.00 43.27 ? 445  GLU B C     1 
ATOM   7556 O  O     . GLU B 1 445 ? -47.204 -19.981 52.925  1.00 38.62 ? 445  GLU B O     1 
ATOM   7557 C  CB    . GLU B 1 445 ? -46.768 -19.593 56.227  1.00 48.83 ? 445  GLU B CB    1 
ATOM   7558 C  CG    . GLU B 1 445 ? -47.317 -18.645 57.279  1.00 55.80 ? 445  GLU B CG    1 
ATOM   7559 C  CD    . GLU B 1 445 ? -47.914 -17.369 56.713  1.00 57.90 ? 445  GLU B CD    1 
ATOM   7560 O  OE1   . GLU B 1 445 ? -47.160 -16.584 56.106  1.00 65.57 ? 445  GLU B OE1   1 
ATOM   7561 O  OE2   . GLU B 1 445 ? -49.136 -17.180 56.855  1.00 60.61 ? 445  GLU B OE2   1 
ATOM   7562 N  N     . ARG B 1 446 ? -46.753 -21.936 54.014  1.00 40.95 ? 446  ARG B N     1 
ATOM   7563 C  CA    . ARG B 1 446 ? -46.132 -22.636 52.863  1.00 38.21 ? 446  ARG B CA    1 
ATOM   7564 C  C     . ARG B 1 446 ? -47.105 -22.613 51.684  1.00 41.60 ? 446  ARG B C     1 
ATOM   7565 O  O     . ARG B 1 446 ? -46.628 -22.398 50.528  1.00 34.40 ? 446  ARG B O     1 
ATOM   7566 C  CB    . ARG B 1 446 ? -45.693 -24.049 53.251  1.00 37.29 ? 446  ARG B CB    1 
ATOM   7567 C  CG    . ARG B 1 446 ? -44.455 -24.054 54.135  1.00 39.33 ? 446  ARG B CG    1 
ATOM   7568 C  CD    . ARG B 1 446 ? -43.713 -25.372 54.263  1.00 39.68 ? 446  ARG B CD    1 
ATOM   7569 N  NE    . ARG B 1 446 ? -44.564 -26.453 54.723  1.00 42.72 ? 446  ARG B NE    1 
ATOM   7570 C  CZ    . ARG B 1 446 ? -44.357 -27.213 55.797  1.00 44.73 ? 446  ARG B CZ    1 
ATOM   7571 N  NH1   . ARG B 1 446 ? -43.323 -27.022 56.606  1.00 43.00 ? 446  ARG B NH1   1 
ATOM   7572 N  NH2   . ARG B 1 446 ? -45.218 -28.178 56.058  1.00 44.74 ? 446  ARG B NH2   1 
ATOM   7573 N  N     . LYS B 1 447 ? -48.401 -22.824 51.955  1.00 42.03 ? 447  LYS B N     1 
ATOM   7574 C  CA    . LYS B 1 447 ? -49.445 -22.954 50.904  1.00 41.02 ? 447  LYS B CA    1 
ATOM   7575 C  C     . LYS B 1 447 ? -49.692 -21.574 50.289  1.00 41.48 ? 447  LYS B C     1 
ATOM   7576 O  O     . LYS B 1 447 ? -49.932 -21.470 49.061  1.00 35.44 ? 447  LYS B O     1 
ATOM   7577 C  CB    . LYS B 1 447 ? -50.732 -23.525 51.496  1.00 46.80 ? 447  LYS B CB    1 
ATOM   7578 C  CG    . LYS B 1 447 ? -51.933 -23.473 50.564  1.00 51.28 ? 447  LYS B CG    1 
ATOM   7579 C  CD    . LYS B 1 447 ? -53.168 -24.140 51.125  1.00 56.46 ? 447  LYS B CD    1 
ATOM   7580 C  CE    . LYS B 1 447 ? -54.438 -23.499 50.604  1.00 63.76 ? 447  LYS B CE    1 
ATOM   7581 N  NZ    . LYS B 1 447 ? -55.575 -24.448 50.655  1.00 70.10 ? 447  LYS B NZ    1 
ATOM   7582 N  N     . LYS B 1 448 ? -49.668 -20.532 51.115  1.00 39.74 ? 448  LYS B N     1 
ATOM   7583 C  CA    . LYS B 1 448 ? -49.926 -19.172 50.591  1.00 44.41 ? 448  LYS B CA    1 
ATOM   7584 C  C     . LYS B 1 448 ? -48.733 -18.818 49.702  1.00 44.37 ? 448  LYS B C     1 
ATOM   7585 O  O     . LYS B 1 448 ? -48.980 -18.243 48.626  1.00 36.27 ? 448  LYS B O     1 
ATOM   7586 C  CB    . LYS B 1 448 ? -50.136 -18.156 51.711  1.00 45.06 ? 448  LYS B CB    1 
ATOM   7587 C  CG    . LYS B 1 448 ? -51.458 -18.293 52.452  1.00 48.86 ? 448  LYS B CG    1 
ATOM   7588 C  CD    . LYS B 1 448 ? -51.718 -17.149 53.406  1.00 52.58 ? 448  LYS B CD    1 
ATOM   7589 C  CE    . LYS B 1 448 ? -50.483 -16.731 54.172  1.00 56.25 ? 448  LYS B CE    1 
ATOM   7590 N  NZ    . LYS B 1 448 ? -50.829 -15.871 55.327  1.00 62.68 ? 448  LYS B NZ    1 
ATOM   7591 N  N     . LEU B 1 449 ? -47.521 -19.196 50.152  1.00 40.14 ? 449  LEU B N     1 
ATOM   7592 C  CA    . LEU B 1 449 ? -46.229 -18.956 49.456  1.00 39.77 ? 449  LEU B CA    1 
ATOM   7593 C  C     . LEU B 1 449 ? -46.261 -19.591 48.066  1.00 36.44 ? 449  LEU B C     1 
ATOM   7594 O  O     . LEU B 1 449 ? -45.971 -18.896 47.097  1.00 35.22 ? 449  LEU B O     1 
ATOM   7595 C  CB    . LEU B 1 449 ? -45.052 -19.524 50.253  1.00 37.64 ? 449  LEU B CB    1 
ATOM   7596 C  CG    . LEU B 1 449 ? -43.712 -19.388 49.523  1.00 40.56 ? 449  LEU B CG    1 
ATOM   7597 C  CD1   . LEU B 1 449 ? -43.349 -17.918 49.366  1.00 39.90 ? 449  LEU B CD1   1 
ATOM   7598 C  CD2   . LEU B 1 449 ? -42.602 -20.155 50.225  1.00 42.54 ? 449  LEU B CD2   1 
ATOM   7599 N  N     . ASP B 1 450 ? -46.564 -20.880 47.987  1.00 40.06 ? 450  ASP B N     1 
ATOM   7600 C  CA    . ASP B 1 450 ? -46.581 -21.625 46.707  1.00 39.50 ? 450  ASP B CA    1 
ATOM   7601 C  C     . ASP B 1 450 ? -47.577 -20.959 45.750  1.00 41.68 ? 450  ASP B C     1 
ATOM   7602 O  O     . ASP B 1 450 ? -47.294 -20.821 44.529  1.00 41.06 ? 450  ASP B O     1 
ATOM   7603 C  CB    . ASP B 1 450 ? -46.894 -23.094 46.957  1.00 41.67 ? 450  ASP B CB    1 
ATOM   7604 C  CG    . ASP B 1 450 ? -46.691 -23.935 45.712  1.00 48.65 ? 450  ASP B CG    1 
ATOM   7605 O  OD1   . ASP B 1 450 ? -45.568 -23.912 45.158  1.00 55.25 ? 450  ASP B OD1   1 
ATOM   7606 O  OD2   . ASP B 1 450 ? -47.663 -24.564 45.279  1.00 51.92 ? 450  ASP B OD2   1 
ATOM   7607 N  N     . GLU B 1 451 ? -48.719 -20.551 46.280  1.00 38.71 ? 451  GLU B N     1 
ATOM   7608 C  CA    . GLU B 1 451 ? -49.796 -19.927 45.482  1.00 39.57 ? 451  GLU B CA    1 
ATOM   7609 C  C     . GLU B 1 451 ? -49.310 -18.587 44.928  1.00 37.20 ? 451  GLU B C     1 
ATOM   7610 O  O     . GLU B 1 451 ? -49.543 -18.303 43.722  1.00 37.96 ? 451  GLU B O     1 
ATOM   7611 C  CB    . GLU B 1 451 ? -51.015 -19.701 46.372  1.00 46.33 ? 451  GLU B CB    1 
ATOM   7612 C  CG    . GLU B 1 451 ? -52.257 -20.395 45.886  1.00 49.14 ? 451  GLU B CG    1 
ATOM   7613 C  CD    . GLU B 1 451 ? -53.370 -20.234 46.901  1.00 54.58 ? 451  GLU B CD    1 
ATOM   7614 O  OE1   . GLU B 1 451 ? -53.528 -21.155 47.750  1.00 49.18 ? 451  GLU B OE1   1 
ATOM   7615 O  OE2   . GLU B 1 451 ? -54.046 -19.164 46.843  1.00 50.69 ? 451  GLU B OE2   1 
ATOM   7616 N  N     . LEU B 1 452 ? -48.718 -17.767 45.799  1.00 33.00 ? 452  LEU B N     1 
ATOM   7617 C  CA    . LEU B 1 452 ? -48.207 -16.430 45.426  1.00 32.07 ? 452  LEU B CA    1 
ATOM   7618 C  C     . LEU B 1 452 ? -47.119 -16.603 44.350  1.00 34.99 ? 452  LEU B C     1 
ATOM   7619 O  O     . LEU B 1 452 ? -47.163 -15.890 43.321  1.00 31.17 ? 452  LEU B O     1 
ATOM   7620 C  CB    . LEU B 1 452 ? -47.669 -15.756 46.685  1.00 32.28 ? 452  LEU B CB    1 
ATOM   7621 C  CG    . LEU B 1 452 ? -46.818 -14.521 46.437  1.00 33.06 ? 452  LEU B CG    1 
ATOM   7622 C  CD1   . LEU B 1 452 ? -47.605 -13.463 45.680  1.00 36.32 ? 452  LEU B CD1   1 
ATOM   7623 C  CD2   . LEU B 1 452 ? -46.271 -13.982 47.740  1.00 36.12 ? 452  LEU B CD2   1 
ATOM   7624 N  N     . PHE B 1 453 ? -46.185 -17.531 44.581  1.00 31.47 ? 453  PHE B N     1 
ATOM   7625 C  CA    . PHE B 1 453 ? -45.004 -17.749 43.714  1.00 33.92 ? 453  PHE B CA    1 
ATOM   7626 C  C     . PHE B 1 453 ? -45.468 -18.024 42.275  1.00 31.98 ? 453  PHE B C     1 
ATOM   7627 O  O     . PHE B 1 453 ? -44.991 -17.350 41.351  1.00 32.01 ? 453  PHE B O     1 
ATOM   7628 C  CB    . PHE B 1 453 ? -44.121 -18.865 44.275  1.00 32.58 ? 453  PHE B CB    1 
ATOM   7629 C  CG    . PHE B 1 453 ? -42.780 -18.870 43.600  1.00 34.81 ? 453  PHE B CG    1 
ATOM   7630 C  CD1   . PHE B 1 453 ? -42.608 -19.530 42.391  1.00 33.79 ? 453  PHE B CD1   1 
ATOM   7631 C  CD2   . PHE B 1 453 ? -41.729 -18.119 44.113  1.00 36.01 ? 453  PHE B CD2   1 
ATOM   7632 C  CE1   . PHE B 1 453 ? -41.390 -19.478 41.729  1.00 35.19 ? 453  PHE B CE1   1 
ATOM   7633 C  CE2   . PHE B 1 453 ? -40.509 -18.084 43.448  1.00 36.71 ? 453  PHE B CE2   1 
ATOM   7634 C  CZ    . PHE B 1 453 ? -40.349 -18.757 42.256  1.00 31.92 ? 453  PHE B CZ    1 
ATOM   7635 N  N     . ASN B 1 454 ? -46.385 -18.979 42.110  1.00 29.66 ? 454  ASN B N     1 
ATOM   7636 C  CA    . ASN B 1 454 ? -46.980 -19.374 40.811  1.00 31.32 ? 454  ASN B CA    1 
ATOM   7637 C  C     . ASN B 1 454 ? -47.678 -18.203 40.113  1.00 35.11 ? 454  ASN B C     1 
ATOM   7638 O  O     . ASN B 1 454 ? -47.638 -18.145 38.889  1.00 34.93 ? 454  ASN B O     1 
ATOM   7639 C  CB    . ASN B 1 454 ? -47.946 -20.537 40.995  1.00 35.40 ? 454  ASN B CB    1 
ATOM   7640 C  CG    . ASN B 1 454 ? -47.190 -21.839 41.075  1.00 36.81 ? 454  ASN B CG    1 
ATOM   7641 O  OD1   . ASN B 1 454 ? -46.628 -22.292 40.082  1.00 45.84 ? 454  ASN B OD1   1 
ATOM   7642 N  ND2   . ASN B 1 454 ? -47.129 -22.417 42.257  1.00 40.62 ? 454  ASN B ND2   1 
ATOM   7643 N  N     . ILE B 1 455 ? -48.316 -17.310 40.858  1.00 33.48 ? 455  ILE B N     1 
ATOM   7644 C  CA    . ILE B 1 455 ? -48.937 -16.095 40.273  1.00 33.88 ? 455  ILE B CA    1 
ATOM   7645 C  C     . ILE B 1 455 ? -47.818 -15.174 39.804  1.00 32.32 ? 455  ILE B C     1 
ATOM   7646 O  O     . ILE B 1 455 ? -47.997 -14.527 38.755  1.00 30.68 ? 455  ILE B O     1 
ATOM   7647 C  CB    . ILE B 1 455 ? -49.861 -15.393 41.292  1.00 35.19 ? 455  ILE B CB    1 
ATOM   7648 C  CG1   . ILE B 1 455 ? -51.119 -16.235 41.538  1.00 37.52 ? 455  ILE B CG1   1 
ATOM   7649 C  CG2   . ILE B 1 455 ? -50.194 -13.980 40.841  1.00 32.88 ? 455  ILE B CG2   1 
ATOM   7650 C  CD1   . ILE B 1 455 ? -51.694 -16.076 42.915  1.00 38.35 ? 455  ILE B CD1   1 
ATOM   7651 N  N     . LEU B 1 456 ? -46.752 -15.043 40.591  1.00 30.46 ? 456  LEU B N     1 
ATOM   7652 C  CA    . LEU B 1 456 ? -45.645 -14.109 40.237  1.00 32.02 ? 456  LEU B CA    1 
ATOM   7653 C  C     . LEU B 1 456 ? -44.984 -14.564 38.917  1.00 28.89 ? 456  LEU B C     1 
ATOM   7654 O  O     . LEU B 1 456 ? -44.686 -13.708 38.099  1.00 26.36 ? 456  LEU B O     1 
ATOM   7655 C  CB    . LEU B 1 456 ? -44.625 -14.051 41.373  1.00 29.16 ? 456  LEU B CB    1 
ATOM   7656 C  CG    . LEU B 1 456 ? -45.083 -13.424 42.680  1.00 30.01 ? 456  LEU B CG    1 
ATOM   7657 C  CD1   . LEU B 1 456 ? -43.957 -13.529 43.681  1.00 31.39 ? 456  LEU B CD1   1 
ATOM   7658 C  CD2   . LEU B 1 456 ? -45.507 -11.969 42.516  1.00 29.29 ? 456  LEU B CD2   1 
ATOM   7659 N  N     . VAL B 1 457 ? -44.777 -15.875 38.743  1.00 30.82 ? 457  VAL B N     1 
ATOM   7660 C  CA    . VAL B 1 457 ? -44.204 -16.500 37.515  1.00 29.81 ? 457  VAL B CA    1 
ATOM   7661 C  C     . VAL B 1 457 ? -45.088 -16.154 36.312  1.00 31.73 ? 457  VAL B C     1 
ATOM   7662 O  O     . VAL B 1 457 ? -44.561 -15.498 35.400  1.00 29.79 ? 457  VAL B O     1 
ATOM   7663 C  CB    . VAL B 1 457 ? -44.021 -18.012 37.696  1.00 28.51 ? 457  VAL B CB    1 
ATOM   7664 C  CG1   . VAL B 1 457 ? -43.700 -18.710 36.376  1.00 29.20 ? 457  VAL B CG1   1 
ATOM   7665 C  CG2   . VAL B 1 457 ? -42.952 -18.289 38.730  1.00 28.54 ? 457  VAL B CG2   1 
ATOM   7666 N  N     . ASP B 1 458 ? -46.386 -16.492 36.353  1.00 33.67 ? 458  ASP B N     1 
ATOM   7667 C  CA    . ASP B 1 458 ? -47.338 -16.333 35.213  1.00 33.91 ? 458  ASP B CA    1 
ATOM   7668 C  C     . ASP B 1 458 ? -47.520 -14.877 34.826  1.00 29.87 ? 458  ASP B C     1 
ATOM   7669 O  O     . ASP B 1 458 ? -47.576 -14.593 33.625  1.00 31.40 ? 458  ASP B O     1 
ATOM   7670 C  CB    . ASP B 1 458 ? -48.714 -16.889 35.542  1.00 39.73 ? 458  ASP B CB    1 
ATOM   7671 C  CG    . ASP B 1 458 ? -48.638 -18.388 35.692  1.00 45.23 ? 458  ASP B CG    1 
ATOM   7672 O  OD1   . ASP B 1 458 ? -47.738 -18.981 35.064  1.00 47.45 ? 458  ASP B OD1   1 
ATOM   7673 O  OD2   . ASP B 1 458 ? -49.434 -18.934 36.465  1.00 47.32 ? 458  ASP B OD2   1 
ATOM   7674 N  N     . GLU B 1 459 ? -47.632 -13.993 35.811  1.00 31.64 ? 459  GLU B N     1 
ATOM   7675 C  CA    . GLU B 1 459 ? -47.825 -12.550 35.548  1.00 32.90 ? 459  GLU B CA    1 
ATOM   7676 C  C     . GLU B 1 459 ? -46.535 -11.989 34.937  1.00 31.94 ? 459  GLU B C     1 
ATOM   7677 O  O     . GLU B 1 459 ? -46.622 -11.070 34.082  1.00 29.20 ? 459  GLU B O     1 
ATOM   7678 C  CB    . GLU B 1 459 ? -48.228 -11.809 36.822  1.00 33.96 ? 459  GLU B CB    1 
ATOM   7679 C  CG    . GLU B 1 459 ? -49.605 -12.193 37.311  1.00 38.78 ? 459  GLU B CG    1 
ATOM   7680 C  CD    . GLU B 1 459 ? -50.207 -11.263 38.361  1.00 39.17 ? 459  GLU B CD    1 
ATOM   7681 O  OE1   . GLU B 1 459 ? -49.461 -10.589 39.083  1.00 41.41 ? 459  GLU B OE1   1 
ATOM   7682 O  OE2   . GLU B 1 459 ? -51.429 -11.210 38.428  1.00 38.11 ? 459  GLU B OE2   1 
ATOM   7683 N  N     . ALA B 1 460 ? -45.376 -12.491 35.364  1.00 29.86 ? 460  ALA B N     1 
ATOM   7684 C  CA    . ALA B 1 460 ? -44.079 -12.000 34.855  1.00 30.29 ? 460  ALA B CA    1 
ATOM   7685 C  C     . ALA B 1 460 ? -43.911 -12.457 33.394  1.00 26.43 ? 460  ALA B C     1 
ATOM   7686 O  O     . ALA B 1 460 ? -43.563 -11.621 32.535  1.00 26.00 ? 460  ALA B O     1 
ATOM   7687 C  CB    . ALA B 1 460 ? -42.964 -12.448 35.758  1.00 31.00 ? 460  ALA B CB    1 
ATOM   7688 N  N     . ALA B 1 461 ? -44.202 -13.715 33.106  1.00 26.63 ? 461  ALA B N     1 
ATOM   7689 C  CA    . ALA B 1 461 ? -44.053 -14.344 31.769  1.00 26.57 ? 461  ALA B CA    1 
ATOM   7690 C  C     . ALA B 1 461 ? -45.015 -13.679 30.773  1.00 29.19 ? 461  ALA B C     1 
ATOM   7691 O  O     . ALA B 1 461 ? -44.625 -13.503 29.591  1.00 26.86 ? 461  ALA B O     1 
ATOM   7692 C  CB    . ALA B 1 461 ? -44.318 -15.825 31.867  1.00 26.00 ? 461  ALA B CB    1 
ATOM   7693 N  N     . ALA B 1 462 ? -46.208 -13.275 31.229  1.00 31.78 ? 462  ALA B N     1 
ATOM   7694 C  CA    . ALA B 1 462 ? -47.220 -12.582 30.388  1.00 30.00 ? 462  ALA B CA    1 
ATOM   7695 C  C     . ALA B 1 462 ? -46.631 -11.260 29.906  1.00 30.37 ? 462  ALA B C     1 
ATOM   7696 O  O     . ALA B 1 462 ? -47.046 -10.805 28.829  1.00 33.53 ? 462  ALA B O     1 
ATOM   7697 C  CB    . ALA B 1 462 ? -48.514 -12.362 31.142  1.00 29.45 ? 462  ALA B CB    1 
ATOM   7698 N  N     . GLU B 1 463 ? -45.710 -10.657 30.668  1.00 29.22 ? 463  GLU B N     1 
ATOM   7699 C  CA    . GLU B 1 463 ? -45.013 -9.399  30.280  1.00 29.84 ? 463  GLU B CA    1 
ATOM   7700 C  C     . GLU B 1 463 ? -43.721 -9.699  29.489  1.00 26.80 ? 463  GLU B C     1 
ATOM   7701 O  O     . GLU B 1 463 ? -43.065 -8.737  29.069  1.00 28.45 ? 463  GLU B O     1 
ATOM   7702 C  CB    . GLU B 1 463 ? -44.659 -8.572  31.517  1.00 31.32 ? 463  GLU B CB    1 
ATOM   7703 C  CG    . GLU B 1 463 ? -45.852 -8.203  32.372  1.00 36.05 ? 463  GLU B CG    1 
ATOM   7704 C  CD    . GLU B 1 463 ? -46.904 -7.397  31.623  1.00 37.78 ? 463  GLU B CD    1 
ATOM   7705 O  OE1   . GLU B 1 463 ? -46.537 -6.354  31.027  1.00 35.60 ? 463  GLU B OE1   1 
ATOM   7706 O  OE2   . GLU B 1 463 ? -48.067 -7.831  31.613  1.00 37.94 ? 463  GLU B OE2   1 
ATOM   7707 N  N     . GLY B 1 464 ? -43.324 -10.956 29.342  1.00 23.82 ? 464  GLY B N     1 
ATOM   7708 C  CA    . GLY B 1 464 ? -42.042 -11.323 28.688  1.00 27.28 ? 464  GLY B CA    1 
ATOM   7709 C  C     . GLY B 1 464 ? -40.835 -11.186 29.621  1.00 25.83 ? 464  GLY B C     1 
ATOM   7710 O  O     . GLY B 1 464 ? -39.726 -10.867 29.153  1.00 26.59 ? 464  GLY B O     1 
ATOM   7711 N  N     . TYR B 1 465 ? -41.055 -11.378 30.914  1.00 24.98 ? 465  TYR B N     1 
ATOM   7712 C  CA    . TYR B 1 465 ? -40.010 -11.373 31.964  1.00 25.12 ? 465  TYR B CA    1 
ATOM   7713 C  C     . TYR B 1 465 ? -39.783 -12.815 32.399  1.00 23.05 ? 465  TYR B C     1 
ATOM   7714 O  O     . TYR B 1 465 ? -40.705 -13.414 32.962  1.00 21.11 ? 465  TYR B O     1 
ATOM   7715 C  CB    . TYR B 1 465 ? -40.426 -10.530 33.173  1.00 25.93 ? 465  TYR B CB    1 
ATOM   7716 C  CG    . TYR B 1 465 ? -40.817 -9.100  32.880  1.00 25.67 ? 465  TYR B CG    1 
ATOM   7717 C  CD1   . TYR B 1 465 ? -40.187 -8.347  31.899  1.00 25.99 ? 465  TYR B CD1   1 
ATOM   7718 C  CD2   . TYR B 1 465 ? -41.800 -8.476  33.642  1.00 25.53 ? 465  TYR B CD2   1 
ATOM   7719 C  CE1   . TYR B 1 465 ? -40.551 -7.025  31.658  1.00 26.14 ? 465  TYR B CE1   1 
ATOM   7720 C  CE2   . TYR B 1 465 ? -42.163 -7.156  33.427  1.00 25.98 ? 465  TYR B CE2   1 
ATOM   7721 C  CZ    . TYR B 1 465 ? -41.539 -6.427  32.434  1.00 26.72 ? 465  TYR B CZ    1 
ATOM   7722 O  OH    . TYR B 1 465 ? -41.901 -5.125  32.266  1.00 26.83 ? 465  TYR B OH    1 
ATOM   7723 N  N     . GLY B 1 466 ? -38.588 -13.337 32.125  1.00 22.63 ? 466  GLY B N     1 
ATOM   7724 C  CA    . GLY B 1 466 ? -38.216 -14.737 32.396  1.00 22.69 ? 466  GLY B CA    1 
ATOM   7725 C  C     . GLY B 1 466 ? -37.203 -14.851 33.519  1.00 22.01 ? 466  GLY B C     1 
ATOM   7726 O  O     . GLY B 1 466 ? -36.265 -14.020 33.597  1.00 19.96 ? 466  GLY B O     1 
ATOM   7727 N  N     . GLU B 1 467 ? -37.361 -15.880 34.341  1.00 21.04 ? 467  GLU B N     1 
ATOM   7728 C  CA    . GLU B 1 467 ? -36.446 -16.192 35.458  1.00 21.64 ? 467  GLU B CA    1 
ATOM   7729 C  C     . GLU B 1 467 ? -35.171 -16.819 34.899  1.00 20.49 ? 467  GLU B C     1 
ATOM   7730 O  O     . GLU B 1 467 ? -35.265 -17.605 33.941  1.00 20.75 ? 467  GLU B O     1 
ATOM   7731 C  CB    . GLU B 1 467 ? -37.153 -17.168 36.408  1.00 23.53 ? 467  GLU B CB    1 
ATOM   7732 C  CG    . GLU B 1 467 ? -36.360 -17.533 37.646  1.00 23.61 ? 467  GLU B CG    1 
ATOM   7733 C  CD    . GLU B 1 467 ? -35.933 -16.375 38.532  1.00 25.96 ? 467  GLU B CD    1 
ATOM   7734 O  OE1   . GLU B 1 467 ? -36.532 -16.222 39.655  1.00 24.26 ? 467  GLU B OE1   1 
ATOM   7735 O  OE2   . GLU B 1 467 ? -34.968 -15.655 38.141  1.00 26.53 ? 467  GLU B OE2   1 
ATOM   7736 N  N     . TYR B 1 468 ? -34.052 -16.572 35.561  1.00 19.80 ? 468  TYR B N     1 
ATOM   7737 C  CA    . TYR B 1 468 ? -32.731 -17.098 35.179  1.00 20.99 ? 468  TYR B CA    1 
ATOM   7738 C  C     . TYR B 1 468 ? -32.196 -18.085 36.230  1.00 22.06 ? 468  TYR B C     1 
ATOM   7739 O  O     . TYR B 1 468 ? -31.239 -18.801 35.890  1.00 20.92 ? 468  TYR B O     1 
ATOM   7740 C  CB    . TYR B 1 468 ? -31.783 -15.930 34.946  1.00 21.91 ? 468  TYR B CB    1 
ATOM   7741 C  CG    . TYR B 1 468 ? -31.185 -15.363 36.200  1.00 22.48 ? 468  TYR B CG    1 
ATOM   7742 C  CD1   . TYR B 1 468 ? -31.904 -14.484 36.992  1.00 23.97 ? 468  TYR B CD1   1 
ATOM   7743 C  CD2   . TYR B 1 468 ? -29.922 -15.743 36.614  1.00 21.77 ? 468  TYR B CD2   1 
ATOM   7744 C  CE1   . TYR B 1 468 ? -31.368 -13.970 38.162  1.00 24.14 ? 468  TYR B CE1   1 
ATOM   7745 C  CE2   . TYR B 1 468 ? -29.376 -15.262 37.791  1.00 22.82 ? 468  TYR B CE2   1 
ATOM   7746 C  CZ    . TYR B 1 468 ? -30.096 -14.360 38.561  1.00 25.11 ? 468  TYR B CZ    1 
ATOM   7747 O  OH    . TYR B 1 468 ? -29.532 -13.830 39.687  1.00 26.84 ? 468  TYR B OH    1 
ATOM   7748 N  N     . ARG B 1 469 ? -32.772 -18.131 37.438  1.00 20.29 ? 469  ARG B N     1 
ATOM   7749 C  CA    . ARG B 1 469 ? -32.332 -19.054 38.514  1.00 22.21 ? 469  ARG B CA    1 
ATOM   7750 C  C     . ARG B 1 469 ? -33.501 -19.315 39.472  1.00 23.27 ? 469  ARG B C     1 
ATOM   7751 O  O     . ARG B 1 469 ? -34.189 -18.354 39.847  1.00 21.40 ? 469  ARG B O     1 
ATOM   7752 C  CB    . ARG B 1 469 ? -31.138 -18.435 39.237  1.00 22.55 ? 469  ARG B CB    1 
ATOM   7753 C  CG    . ARG B 1 469 ? -30.479 -19.335 40.271  1.00 23.50 ? 469  ARG B CG    1 
ATOM   7754 C  CD    . ARG B 1 469 ? -29.337 -18.622 40.976  1.00 26.47 ? 469  ARG B CD    1 
ATOM   7755 N  NE    . ARG B 1 469 ? -28.682 -19.437 42.007  1.00 27.30 ? 469  ARG B NE    1 
ATOM   7756 C  CZ    . ARG B 1 469 ? -27.806 -18.972 42.886  1.00 28.89 ? 469  ARG B CZ    1 
ATOM   7757 N  NH1   . ARG B 1 469 ? -27.448 -17.698 42.820  1.00 26.92 ? 469  ARG B NH1   1 
ATOM   7758 N  NH2   . ARG B 1 469 ? -27.267 -19.778 43.802  1.00 27.74 ? 469  ARG B NH2   1 
ATOM   7759 N  N     . THR B 1 470 ? -33.753 -20.561 39.848  1.00 23.68 ? 470  THR B N     1 
ATOM   7760 C  CA    . THR B 1 470 ? -34.945 -20.862 40.676  1.00 24.69 ? 470  THR B CA    1 
ATOM   7761 C  C     . THR B 1 470 ? -34.729 -22.068 41.604  1.00 24.98 ? 470  THR B C     1 
ATOM   7762 O  O     . THR B 1 470 ? -33.665 -22.766 41.548  1.00 24.79 ? 470  THR B O     1 
ATOM   7763 C  CB    . THR B 1 470 ? -36.171 -21.020 39.770  1.00 25.98 ? 470  THR B CB    1 
ATOM   7764 O  OG1   . THR B 1 470 ? -37.324 -20.788 40.587  1.00 23.43 ? 470  THR B OG1   1 
ATOM   7765 C  CG2   . THR B 1 470 ? -36.198 -22.370 39.077  1.00 24.77 ? 470  THR B CG2   1 
ATOM   7766 N  N     . HIS B 1 471 ? -35.723 -22.294 42.442  1.00 23.37 ? 471  HIS B N     1 
ATOM   7767 C  CA    . HIS B 1 471 ? -35.710 -23.319 43.509  1.00 24.46 ? 471  HIS B CA    1 
ATOM   7768 C  C     . HIS B 1 471 ? -36.047 -24.643 42.838  1.00 22.38 ? 471  HIS B C     1 
ATOM   7769 O  O     . HIS B 1 471 ? -36.720 -24.606 41.782  1.00 21.33 ? 471  HIS B O     1 
ATOM   7770 C  CB    . HIS B 1 471 ? -36.659 -22.847 44.629  1.00 25.77 ? 471  HIS B CB    1 
ATOM   7771 C  CG    . HIS B 1 471 ? -36.810 -23.771 45.786  1.00 26.86 ? 471  HIS B CG    1 
ATOM   7772 N  ND1   . HIS B 1 471 ? -37.421 -25.004 45.663  1.00 25.58 ? 471  HIS B ND1   1 
ATOM   7773 C  CD2   . HIS B 1 471 ? -36.485 -23.618 47.093  1.00 25.81 ? 471  HIS B CD2   1 
ATOM   7774 C  CE1   . HIS B 1 471 ? -37.441 -25.592 46.857  1.00 26.45 ? 471  HIS B CE1   1 
ATOM   7775 N  NE2   . HIS B 1 471 ? -36.882 -24.752 47.748  1.00 25.93 ? 471  HIS B NE2   1 
ATOM   7776 N  N     . ILE B 1 472 ? -35.618 -25.759 43.428  1.00 22.07 ? 472  ILE B N     1 
ATOM   7777 C  CA    . ILE B 1 472 ? -35.831 -27.124 42.859  1.00 24.09 ? 472  ILE B CA    1 
ATOM   7778 C  C     . ILE B 1 472 ? -37.317 -27.368 42.591  1.00 25.27 ? 472  ILE B C     1 
ATOM   7779 O  O     . ILE B 1 472 ? -37.652 -28.067 41.566  1.00 22.26 ? 472  ILE B O     1 
ATOM   7780 C  CB    . ILE B 1 472 ? -35.235 -28.214 43.772  1.00 26.80 ? 472  ILE B CB    1 
ATOM   7781 C  CG1   . ILE B 1 472 ? -35.794 -28.168 45.203  1.00 29.56 ? 472  ILE B CG1   1 
ATOM   7782 C  CG2   . ILE B 1 472 ? -33.719 -28.132 43.755  1.00 24.60 ? 472  ILE B CG2   1 
ATOM   7783 C  CD1   . ILE B 1 472 ? -35.171 -29.198 46.156  1.00 29.26 ? 472  ILE B CD1   1 
ATOM   7784 N  N     . ARG B 1 473 ? -38.198 -26.813 43.436  1.00 27.63 ? 473  ARG B N     1 
ATOM   7785 C  CA    . ARG B 1 473 ? -39.668 -26.958 43.249  1.00 27.93 ? 473  ARG B CA    1 
ATOM   7786 C  C     . ARG B 1 473 ? -40.097 -26.395 41.880  1.00 25.99 ? 473  ARG B C     1 
ATOM   7787 O  O     . ARG B 1 473 ? -40.982 -26.992 41.231  1.00 24.66 ? 473  ARG B O     1 
ATOM   7788 C  CB    . ARG B 1 473 ? -40.411 -26.269 44.390  1.00 31.64 ? 473  ARG B CB    1 
ATOM   7789 C  CG    . ARG B 1 473 ? -41.912 -26.485 44.329  1.00 33.26 ? 473  ARG B CG    1 
ATOM   7790 C  CD    . ARG B 1 473 ? -42.604 -26.130 45.628  1.00 36.68 ? 473  ARG B CD    1 
ATOM   7791 N  NE    . ARG B 1 473 ? -44.027 -26.275 45.405  1.00 39.11 ? 473  ARG B NE    1 
ATOM   7792 C  CZ    . ARG B 1 473 ? -44.703 -27.425 45.457  1.00 43.64 ? 473  ARG B CZ    1 
ATOM   7793 N  NH1   . ARG B 1 473 ? -44.112 -28.572 45.761  1.00 42.84 ? 473  ARG B NH1   1 
ATOM   7794 N  NH2   . ARG B 1 473 ? -45.997 -27.409 45.205  1.00 50.24 ? 473  ARG B NH2   1 
ATOM   7795 N  N     . TYR B 1 474 ? -39.495 -25.302 41.425  1.00 24.82 ? 474  TYR B N     1 
ATOM   7796 C  CA    . TYR B 1 474 ? -40.040 -24.530 40.276  1.00 27.64 ? 474  TYR B CA    1 
ATOM   7797 C  C     . TYR B 1 474 ? -39.219 -24.756 38.992  1.00 25.86 ? 474  TYR B C     1 
ATOM   7798 O  O     . TYR B 1 474 ? -39.461 -24.082 37.989  1.00 22.79 ? 474  TYR B O     1 
ATOM   7799 C  CB    . TYR B 1 474 ? -40.145 -23.064 40.708  1.00 28.76 ? 474  TYR B CB    1 
ATOM   7800 C  CG    . TYR B 1 474 ? -41.030 -22.875 41.918  1.00 29.78 ? 474  TYR B CG    1 
ATOM   7801 C  CD1   . TYR B 1 474 ? -42.368 -23.237 41.876  1.00 28.78 ? 474  TYR B CD1   1 
ATOM   7802 C  CD2   . TYR B 1 474 ? -40.521 -22.387 43.114  1.00 32.70 ? 474  TYR B CD2   1 
ATOM   7803 C  CE1   . TYR B 1 474 ? -43.184 -23.099 42.987  1.00 31.86 ? 474  TYR B CE1   1 
ATOM   7804 C  CE2   . TYR B 1 474 ? -41.326 -22.233 44.234  1.00 35.93 ? 474  TYR B CE2   1 
ATOM   7805 C  CZ    . TYR B 1 474 ? -42.664 -22.596 44.169  1.00 32.90 ? 474  TYR B CZ    1 
ATOM   7806 O  OH    . TYR B 1 474 ? -43.459 -22.476 45.271  1.00 34.32 ? 474  TYR B OH    1 
ATOM   7807 N  N     . MET B 1 475 ? -38.283 -25.708 38.976  1.00 27.68 ? 475  MET B N     1 
ATOM   7808 C  CA    . MET B 1 475 ? -37.342 -25.808 37.821  1.00 25.12 ? 475  MET B CA    1 
ATOM   7809 C  C     . MET B 1 475 ? -38.106 -26.211 36.549  1.00 23.02 ? 475  MET B C     1 
ATOM   7810 O  O     . MET B 1 475 ? -37.809 -25.654 35.493  1.00 23.14 ? 475  MET B O     1 
ATOM   7811 C  CB    . MET B 1 475 ? -36.188 -26.766 38.125  1.00 25.53 ? 475  MET B CB    1 
ATOM   7812 C  CG    . MET B 1 475 ? -35.166 -26.155 39.068  1.00 25.46 ? 475  MET B CG    1 
ATOM   7813 S  SD    . MET B 1 475 ? -33.866 -27.320 39.529  1.00 23.84 ? 475  MET B SD    1 
ATOM   7814 C  CE    . MET B 1 475 ? -32.842 -26.256 40.550  1.00 23.11 ? 475  MET B CE    1 
ATOM   7815 N  N     . ASP B 1 476 ? -39.078 -27.110 36.639  1.00 24.03 ? 476  ASP B N     1 
ATOM   7816 C  CA    . ASP B 1 476 ? -39.939 -27.483 35.478  1.00 26.71 ? 476  ASP B CA    1 
ATOM   7817 C  C     . ASP B 1 476 ? -40.805 -26.292 35.069  1.00 27.32 ? 476  ASP B C     1 
ATOM   7818 O  O     . ASP B 1 476 ? -40.979 -26.056 33.849  1.00 27.40 ? 476  ASP B O     1 
ATOM   7819 C  CB    . ASP B 1 476 ? -40.875 -28.655 35.782  1.00 29.65 ? 476  ASP B CB    1 
ATOM   7820 C  CG    . ASP B 1 476 ? -40.269 -30.027 35.531  1.00 32.73 ? 476  ASP B CG    1 
ATOM   7821 O  OD1   . ASP B 1 476 ? -39.067 -30.113 35.218  1.00 33.16 ? 476  ASP B OD1   1 
ATOM   7822 O  OD2   . ASP B 1 476 ? -41.001 -30.993 35.650  1.00 39.57 ? 476  ASP B OD2   1 
ATOM   7823 N  N     . ARG B 1 477 ? -41.388 -25.607 36.051  1.00 26.79 ? 477  ARG B N     1 
ATOM   7824 C  CA    . ARG B 1 477 ? -42.251 -24.424 35.807  1.00 28.24 ? 477  ARG B CA    1 
ATOM   7825 C  C     . ARG B 1 477 ? -41.480 -23.345 35.018  1.00 24.35 ? 477  ARG B C     1 
ATOM   7826 O  O     . ARG B 1 477 ? -42.005 -22.803 34.050  1.00 21.07 ? 477  ARG B O     1 
ATOM   7827 C  CB    . ARG B 1 477 ? -42.755 -23.865 37.138  1.00 31.30 ? 477  ARG B CB    1 
ATOM   7828 C  CG    . ARG B 1 477 ? -43.861 -22.838 36.971  1.00 33.49 ? 477  ARG B CG    1 
ATOM   7829 C  CD    . ARG B 1 477 ? -45.165 -23.535 36.674  1.00 40.63 ? 477  ARG B CD    1 
ATOM   7830 N  NE    . ARG B 1 477 ? -46.250 -22.785 37.278  1.00 49.94 ? 477  ARG B NE    1 
ATOM   7831 C  CZ    . ARG B 1 477 ? -46.731 -21.641 36.806  1.00 58.78 ? 477  ARG B CZ    1 
ATOM   7832 N  NH1   . ARG B 1 477 ? -46.235 -21.098 35.699  1.00 55.97 ? 477  ARG B NH1   1 
ATOM   7833 N  NH2   . ARG B 1 477 ? -47.712 -21.045 37.461  1.00 61.31 ? 477  ARG B NH2   1 
ATOM   7834 N  N     . ILE B 1 478 ? -40.261 -23.019 35.411  1.00 23.59 ? 478  ILE B N     1 
ATOM   7835 C  CA    . ILE B 1 478 ? -39.461 -21.992 34.677  1.00 23.33 ? 478  ILE B CA    1 
ATOM   7836 C  C     . ILE B 1 478 ? -39.087 -22.495 33.266  1.00 23.43 ? 478  ILE B C     1 
ATOM   7837 O  O     . ILE B 1 478 ? -39.264 -21.712 32.291  1.00 23.12 ? 478  ILE B O     1 
ATOM   7838 C  CB    . ILE B 1 478 ? -38.248 -21.555 35.518  1.00 23.86 ? 478  ILE B CB    1 
ATOM   7839 C  CG1   . ILE B 1 478 ? -38.689 -20.951 36.856  1.00 25.58 ? 478  ILE B CG1   1 
ATOM   7840 C  CG2   . ILE B 1 478 ? -37.392 -20.578 34.723  1.00 25.43 ? 478  ILE B CG2   1 
ATOM   7841 C  CD1   . ILE B 1 478 ? -39.848 -19.945 36.739  1.00 24.82 ? 478  ILE B CD1   1 
ATOM   7842 N  N     . ALA B 1 479 ? -38.635 -23.747 33.129  1.00 22.17 ? 479  ALA B N     1 
ATOM   7843 C  CA    . ALA B 1 479 ? -38.263 -24.339 31.822  1.00 23.14 ? 479  ALA B CA    1 
ATOM   7844 C  C     . ALA B 1 479 ? -39.395 -24.106 30.830  1.00 23.27 ? 479  ALA B C     1 
ATOM   7845 O  O     . ALA B 1 479 ? -39.122 -23.724 29.682  1.00 24.34 ? 479  ALA B O     1 
ATOM   7846 C  CB    . ALA B 1 479 ? -37.957 -25.797 31.954  1.00 23.59 ? 479  ALA B CB    1 
ATOM   7847 N  N     . LYS B 1 480 ? -40.626 -24.333 31.280  1.00 24.96 ? 480  LYS B N     1 
ATOM   7848 C  CA    . LYS B 1 480 ? -41.839 -24.310 30.431  1.00 25.73 ? 480  LYS B CA    1 
ATOM   7849 C  C     . LYS B 1 480 ? -42.156 -22.885 29.968  1.00 23.60 ? 480  LYS B C     1 
ATOM   7850 O  O     . LYS B 1 480 ? -42.891 -22.770 28.989  1.00 22.76 ? 480  LYS B O     1 
ATOM   7851 C  CB    . LYS B 1 480 ? -43.024 -24.912 31.188  1.00 30.31 ? 480  LYS B CB    1 
ATOM   7852 C  CG    . LYS B 1 480 ? -43.027 -26.438 31.228  1.00 35.07 ? 480  LYS B CG    1 
ATOM   7853 C  CD    . LYS B 1 480 ? -44.071 -26.974 32.206  1.00 39.31 ? 480  LYS B CD    1 
ATOM   7854 C  CE    . LYS B 1 480 ? -43.803 -28.385 32.668  1.00 42.78 ? 480  LYS B CE    1 
ATOM   7855 N  NZ    . LYS B 1 480 ? -44.141 -29.346 31.599  1.00 46.66 ? 480  LYS B NZ    1 
ATOM   7856 N  N     . THR B 1 481 ? -41.619 -21.843 30.608  1.00 22.33 ? 481  THR B N     1 
ATOM   7857 C  CA    . THR B 1 481 ? -41.837 -20.447 30.147  1.00 23.36 ? 481  THR B CA    1 
ATOM   7858 C  C     . THR B 1 481 ? -40.963 -20.160 28.918  1.00 25.00 ? 481  THR B C     1 
ATOM   7859 O  O     . THR B 1 481 ? -41.235 -19.150 28.257  1.00 26.18 ? 481  THR B O     1 
ATOM   7860 C  CB    . THR B 1 481 ? -41.597 -19.423 31.265  1.00 23.01 ? 481  THR B CB    1 
ATOM   7861 O  OG1   . THR B 1 481 ? -40.219 -19.365 31.659  1.00 21.27 ? 481  THR B OG1   1 
ATOM   7862 C  CG2   . THR B 1 481 ? -42.453 -19.704 32.490  1.00 23.49 ? 481  THR B CG2   1 
ATOM   7863 N  N     . TYR B 1 482 ? -39.927 -20.963 28.644  1.00 22.38 ? 482  TYR B N     1 
ATOM   7864 C  CA    . TYR B 1 482 ? -39.007 -20.740 27.493  1.00 22.16 ? 482  TYR B CA    1 
ATOM   7865 C  C     . TYR B 1 482 ? -39.462 -21.593 26.305  1.00 22.18 ? 482  TYR B C     1 
ATOM   7866 O  O     . TYR B 1 482 ? -38.696 -22.422 25.766  1.00 23.42 ? 482  TYR B O     1 
ATOM   7867 C  CB    . TYR B 1 482 ? -37.564 -20.972 27.942  1.00 22.92 ? 482  TYR B CB    1 
ATOM   7868 C  CG    . TYR B 1 482 ? -37.068 -19.924 28.905  1.00 21.84 ? 482  TYR B CG    1 
ATOM   7869 C  CD1   . TYR B 1 482 ? -36.549 -18.738 28.425  1.00 22.98 ? 482  TYR B CD1   1 
ATOM   7870 C  CD2   . TYR B 1 482 ? -37.147 -20.090 30.281  1.00 19.71 ? 482  TYR B CD2   1 
ATOM   7871 C  CE1   . TYR B 1 482 ? -36.091 -17.751 29.277  1.00 22.37 ? 482  TYR B CE1   1 
ATOM   7872 C  CE2   . TYR B 1 482 ? -36.680 -19.115 31.142  1.00 21.19 ? 482  TYR B CE2   1 
ATOM   7873 C  CZ    . TYR B 1 482 ? -36.135 -17.942 30.641  1.00 21.92 ? 482  TYR B CZ    1 
ATOM   7874 O  OH    . TYR B 1 482 ? -35.714 -16.923 31.456  1.00 23.09 ? 482  TYR B OH    1 
ATOM   7875 N  N     . SER B 1 483 ? -40.683 -21.324 25.844  1.00 23.77 ? 483  SER B N     1 
ATOM   7876 C  CA    . SER B 1 483 ? -41.459 -22.211 24.947  1.00 24.74 ? 483  SER B CA    1 
ATOM   7877 C  C     . SER B 1 483 ? -41.401 -21.781 23.483  1.00 22.43 ? 483  SER B C     1 
ATOM   7878 O  O     . SER B 1 483 ? -42.143 -22.393 22.684  1.00 23.09 ? 483  SER B O     1 
ATOM   7879 C  CB    . SER B 1 483 ? -42.889 -22.264 25.395  1.00 26.98 ? 483  SER B CB    1 
ATOM   7880 O  OG    . SER B 1 483 ? -43.511 -21.024 25.097  1.00 27.92 ? 483  SER B OG    1 
ATOM   7881 N  N     . TRP B 1 484 ? -40.542 -20.835 23.093  1.00 24.63 ? 484  TRP B N     1 
ATOM   7882 C  CA    . TRP B 1 484 ? -40.441 -20.426 21.666  1.00 23.03 ? 484  TRP B CA    1 
ATOM   7883 C  C     . TRP B 1 484 ? -40.306 -21.675 20.787  1.00 23.70 ? 484  TRP B C     1 
ATOM   7884 O  O     . TRP B 1 484 ? -39.466 -22.563 21.095  1.00 23.84 ? 484  TRP B O     1 
ATOM   7885 C  CB    . TRP B 1 484 ? -39.320 -19.418 21.396  1.00 24.68 ? 484  TRP B CB    1 
ATOM   7886 C  CG    . TRP B 1 484 ? -39.358 -18.865 20.000  1.00 23.49 ? 484  TRP B CG    1 
ATOM   7887 C  CD1   . TRP B 1 484 ? -40.149 -17.845 19.542  1.00 24.37 ? 484  TRP B CD1   1 
ATOM   7888 C  CD2   . TRP B 1 484 ? -38.593 -19.306 18.865  1.00 22.75 ? 484  TRP B CD2   1 
ATOM   7889 N  NE1   . TRP B 1 484 ? -39.922 -17.615 18.209  1.00 25.79 ? 484  TRP B NE1   1 
ATOM   7890 C  CE2   . TRP B 1 484 ? -38.987 -18.511 17.759  1.00 24.08 ? 484  TRP B CE2   1 
ATOM   7891 C  CE3   . TRP B 1 484 ? -37.631 -20.298 18.672  1.00 22.35 ? 484  TRP B CE3   1 
ATOM   7892 C  CZ2   . TRP B 1 484 ? -38.422 -18.646 16.494  1.00 23.54 ? 484  TRP B CZ2   1 
ATOM   7893 C  CZ3   . TRP B 1 484 ? -37.119 -20.470 17.405  1.00 23.49 ? 484  TRP B CZ3   1 
ATOM   7894 C  CH2   . TRP B 1 484 ? -37.482 -19.632 16.340  1.00 22.66 ? 484  TRP B CH2   1 
ATOM   7895 N  N     . ASN B 1 485 ? -41.164 -21.730 19.771  1.00 24.12 ? 485  ASN B N     1 
ATOM   7896 C  CA    . ASN B 1 485 ? -41.228 -22.733 18.687  1.00 24.76 ? 485  ASN B CA    1 
ATOM   7897 C  C     . ASN B 1 485 ? -41.483 -24.118 19.288  1.00 25.90 ? 485  ASN B C     1 
ATOM   7898 O  O     . ASN B 1 485 ? -40.683 -25.038 19.022  1.00 23.21 ? 485  ASN B O     1 
ATOM   7899 C  CB    . ASN B 1 485 ? -39.977 -22.656 17.817  1.00 26.48 ? 485  ASN B CB    1 
ATOM   7900 C  CG    . ASN B 1 485 ? -40.070 -23.582 16.627  1.00 27.34 ? 485  ASN B CG    1 
ATOM   7901 O  OD1   . ASN B 1 485 ? -41.147 -23.784 16.105  1.00 29.35 ? 485  ASN B OD1   1 
ATOM   7902 N  ND2   . ASN B 1 485 ? -38.961 -24.155 16.201  1.00 27.37 ? 485  ASN B ND2   1 
ATOM   7903 N  N     . ASP B 1 486 ? -42.556 -24.257 20.076  1.00 24.49 ? 486  ASP B N     1 
ATOM   7904 C  CA    . ASP B 1 486 ? -42.968 -25.543 20.694  1.00 27.77 ? 486  ASP B CA    1 
ATOM   7905 C  C     . ASP B 1 486 ? -41.800 -26.137 21.496  1.00 25.39 ? 486  ASP B C     1 
ATOM   7906 O  O     . ASP B 1 486 ? -41.510 -27.354 21.369  1.00 27.98 ? 486  ASP B O     1 
ATOM   7907 C  CB    . ASP B 1 486 ? -43.515 -26.527 19.650  1.00 33.97 ? 486  ASP B CB    1 
ATOM   7908 C  CG    . ASP B 1 486 ? -44.230 -27.734 20.260  1.00 45.93 ? 486  ASP B CG    1 
ATOM   7909 O  OD1   . ASP B 1 486 ? -44.626 -27.656 21.450  1.00 58.66 ? 486  ASP B OD1   1 
ATOM   7910 O  OD2   . ASP B 1 486 ? -44.386 -28.763 19.556  1.00 61.29 ? 486  ASP B OD2   1 
ATOM   7911 N  N     . ASN B 1 487 ? -41.202 -25.333 22.363  1.00 24.86 ? 487  ASN B N     1 
ATOM   7912 C  CA    . ASN B 1 487 ? -40.188 -25.785 23.357  1.00 24.55 ? 487  ASN B CA    1 
ATOM   7913 C  C     . ASN B 1 487 ? -38.925 -26.296 22.636  1.00 21.92 ? 487  ASN B C     1 
ATOM   7914 O  O     . ASN B 1 487 ? -38.293 -27.220 23.138  1.00 21.90 ? 487  ASN B O     1 
ATOM   7915 C  CB    . ASN B 1 487 ? -40.773 -26.828 24.314  1.00 23.35 ? 487  ASN B CB    1 
ATOM   7916 C  CG    . ASN B 1 487 ? -42.021 -26.303 25.000  1.00 24.33 ? 487  ASN B CG    1 
ATOM   7917 O  OD1   . ASN B 1 487 ? -43.128 -26.596 24.557  1.00 29.61 ? 487  ASN B OD1   1 
ATOM   7918 N  ND2   . ASN B 1 487 ? -41.859 -25.493 26.026  1.00 21.32 ? 487  ASN B ND2   1 
ATOM   7919 N  N     . ALA B 1 488 ? -38.529 -25.659 21.547  1.00 22.47 ? 488  ALA B N     1 
ATOM   7920 C  CA    . ALA B 1 488 ? -37.348 -26.043 20.734  1.00 24.10 ? 488  ALA B CA    1 
ATOM   7921 C  C     . ALA B 1 488 ? -36.090 -26.152 21.619  1.00 23.93 ? 488  ALA B C     1 
ATOM   7922 O  O     . ALA B 1 488 ? -35.311 -27.130 21.452  1.00 23.35 ? 488  ALA B O     1 
ATOM   7923 C  CB    . ALA B 1 488 ? -37.180 -25.044 19.618  1.00 25.83 ? 488  ALA B CB    1 
ATOM   7924 N  N     . LEU B 1 489 ? -35.871 -25.201 22.531  1.00 22.67 ? 489  LEU B N     1 
ATOM   7925 C  CA    . LEU B 1 489 ? -34.588 -25.137 23.270  1.00 22.89 ? 489  LEU B CA    1 
ATOM   7926 C  C     . LEU B 1 489 ? -34.464 -26.346 24.199  1.00 22.69 ? 489  LEU B C     1 
ATOM   7927 O  O     . LEU B 1 489 ? -33.389 -26.976 24.208  1.00 20.78 ? 489  LEU B O     1 
ATOM   7928 C  CB    . LEU B 1 489 ? -34.453 -23.821 24.045  1.00 23.58 ? 489  LEU B CB    1 
ATOM   7929 C  CG    . LEU B 1 489 ? -33.096 -23.624 24.733  1.00 23.24 ? 489  LEU B CG    1 
ATOM   7930 C  CD1   . LEU B 1 489 ? -31.933 -23.901 23.794  1.00 23.22 ? 489  LEU B CD1   1 
ATOM   7931 C  CD2   . LEU B 1 489 ? -32.980 -22.228 25.331  1.00 24.96 ? 489  LEU B CD2   1 
ATOM   7932 N  N     . TRP B 1 490 ? -35.514 -26.693 24.939  1.00 22.33 ? 490  TRP B N     1 
ATOM   7933 C  CA    . TRP B 1 490 ? -35.460 -27.875 25.847  1.00 22.02 ? 490  TRP B CA    1 
ATOM   7934 C  C     . TRP B 1 490 ? -35.410 -29.196 25.055  1.00 20.93 ? 490  TRP B C     1 
ATOM   7935 O  O     . TRP B 1 490 ? -34.849 -30.184 25.568  1.00 24.16 ? 490  TRP B O     1 
ATOM   7936 C  CB    . TRP B 1 490 ? -36.566 -27.801 26.915  1.00 21.28 ? 490  TRP B CB    1 
ATOM   7937 C  CG    . TRP B 1 490 ? -36.016 -27.291 28.216  1.00 21.80 ? 490  TRP B CG    1 
ATOM   7938 C  CD1   . TRP B 1 490 ? -35.798 -28.014 29.351  1.00 21.26 ? 490  TRP B CD1   1 
ATOM   7939 C  CD2   . TRP B 1 490 ? -35.521 -25.962 28.488  1.00 21.95 ? 490  TRP B CD2   1 
ATOM   7940 N  NE1   . TRP B 1 490 ? -35.216 -27.231 30.314  1.00 21.58 ? 490  TRP B NE1   1 
ATOM   7941 C  CE2   . TRP B 1 490 ? -35.029 -25.967 29.809  1.00 22.41 ? 490  TRP B CE2   1 
ATOM   7942 C  CE3   . TRP B 1 490 ? -35.412 -24.786 27.739  1.00 22.72 ? 490  TRP B CE3   1 
ATOM   7943 C  CZ2   . TRP B 1 490 ? -34.458 -24.838 30.395  1.00 21.58 ? 490  TRP B CZ2   1 
ATOM   7944 C  CZ3   . TRP B 1 490 ? -34.837 -23.672 28.320  1.00 23.64 ? 490  TRP B CZ3   1 
ATOM   7945 C  CH2   . TRP B 1 490 ? -34.387 -23.695 29.643  1.00 22.41 ? 490  TRP B CH2   1 
ATOM   7946 N  N     . LYS B 1 491 ? -35.936 -29.246 23.836  1.00 21.93 ? 491  LYS B N     1 
ATOM   7947 C  CA    . LYS B 1 491 ? -35.796 -30.441 22.962  1.00 22.38 ? 491  LYS B CA    1 
ATOM   7948 C  C     . LYS B 1 491 ? -34.303 -30.625 22.637  1.00 20.59 ? 491  LYS B C     1 
ATOM   7949 O  O     . LYS B 1 491 ? -33.829 -31.774 22.617  1.00 17.56 ? 491  LYS B O     1 
ATOM   7950 C  CB    . LYS B 1 491 ? -36.661 -30.324 21.711  1.00 22.65 ? 491  LYS B CB    1 
ATOM   7951 C  CG    . LYS B 1 491 ? -38.139 -30.562 21.946  1.00 26.71 ? 491  LYS B CG    1 
ATOM   7952 C  CD    . LYS B 1 491 ? -38.996 -30.271 20.744  1.00 27.19 ? 491  LYS B CD    1 
ATOM   7953 C  CE    . LYS B 1 491 ? -40.465 -30.447 21.045  1.00 31.76 ? 491  LYS B CE    1 
ATOM   7954 N  NZ    . LYS B 1 491 ? -41.304 -29.880 19.959  1.00 35.84 ? 491  LYS B NZ    1 
ATOM   7955 N  N     . MET B 1 492 ? -33.579 -29.525 22.438  1.00 20.81 ? 492  MET B N     1 
ATOM   7956 C  CA    . MET B 1 492 ? -32.116 -29.586 22.173  1.00 21.11 ? 492  MET B CA    1 
ATOM   7957 C  C     . MET B 1 492 ? -31.374 -30.025 23.455  1.00 20.73 ? 492  MET B C     1 
ATOM   7958 O  O     . MET B 1 492 ? -30.566 -30.950 23.385  1.00 19.48 ? 492  MET B O     1 
ATOM   7959 C  CB    . MET B 1 492 ? -31.592 -28.242 21.672  1.00 20.83 ? 492  MET B CB    1 
ATOM   7960 C  CG    . MET B 1 492 ? -30.242 -28.383 21.002  1.00 23.46 ? 492  MET B CG    1 
ATOM   7961 S  SD    . MET B 1 492 ? -29.439 -26.823 20.720  1.00 26.09 ? 492  MET B SD    1 
ATOM   7962 C  CE    . MET B 1 492 ? -29.049 -26.251 22.376  1.00 25.65 ? 492  MET B CE    1 
ATOM   7963 N  N     . HIS B 1 493 ? -31.650 -29.415 24.607  1.00 20.62 ? 493  HIS B N     1 
ATOM   7964 C  CA    . HIS B 1 493 ? -31.043 -29.830 25.901  1.00 21.71 ? 493  HIS B CA    1 
ATOM   7965 C  C     . HIS B 1 493 ? -31.260 -31.341 26.099  1.00 22.64 ? 493  HIS B C     1 
ATOM   7966 O  O     . HIS B 1 493 ? -30.354 -32.006 26.619  1.00 21.40 ? 493  HIS B O     1 
ATOM   7967 C  CB    . HIS B 1 493 ? -31.631 -29.029 27.070  1.00 21.75 ? 493  HIS B CB    1 
ATOM   7968 C  CG    . HIS B 1 493 ? -31.280 -27.574 27.060  1.00 22.76 ? 493  HIS B CG    1 
ATOM   7969 N  ND1   . HIS B 1 493 ? -30.035 -27.113 26.686  1.00 23.62 ? 493  HIS B ND1   1 
ATOM   7970 C  CD2   . HIS B 1 493 ? -31.982 -26.482 27.440  1.00 24.71 ? 493  HIS B CD2   1 
ATOM   7971 C  CE1   . HIS B 1 493 ? -29.995 -25.802 26.816  1.00 24.71 ? 493  HIS B CE1   1 
ATOM   7972 N  NE2   . HIS B 1 493 ? -31.182 -25.379 27.266  1.00 22.95 ? 493  HIS B NE2   1 
ATOM   7973 N  N     . GLU B 1 494 ? -32.436 -31.851 25.731  1.00 23.63 ? 494  GLU B N     1 
ATOM   7974 C  CA    . GLU B 1 494 ? -32.817 -33.275 25.925  1.00 26.35 ? 494  GLU B CA    1 
ATOM   7975 C  C     . GLU B 1 494 ? -31.981 -34.169 25.002  1.00 24.98 ? 494  GLU B C     1 
ATOM   7976 O  O     . GLU B 1 494 ? -31.624 -35.274 25.450  1.00 24.35 ? 494  GLU B O     1 
ATOM   7977 C  CB    . GLU B 1 494 ? -34.322 -33.475 25.708  1.00 28.59 ? 494  GLU B CB    1 
ATOM   7978 C  CG    . GLU B 1 494 ? -35.142 -33.135 26.935  1.00 32.04 ? 494  GLU B CG    1 
ATOM   7979 C  CD    . GLU B 1 494 ? -36.582 -32.700 26.681  1.00 38.45 ? 494  GLU B CD    1 
ATOM   7980 O  OE1   . GLU B 1 494 ? -37.107 -32.933 25.556  1.00 40.16 ? 494  GLU B OE1   1 
ATOM   7981 O  OE2   . GLU B 1 494 ? -37.208 -32.164 27.635  1.00 44.87 ? 494  GLU B OE2   1 
ATOM   7982 N  N     . THR B 1 495 ? -31.694 -33.707 23.778  1.00 24.38 ? 495  THR B N     1 
ATOM   7983 C  CA    . THR B 1 495 ? -30.861 -34.420 22.781  1.00 23.78 ? 495  THR B CA    1 
ATOM   7984 C  C     . THR B 1 495 ? -29.442 -34.561 23.356  1.00 25.15 ? 495  THR B C     1 
ATOM   7985 O  O     . THR B 1 495 ? -28.891 -35.681 23.350  1.00 23.79 ? 495  THR B O     1 
ATOM   7986 C  CB    . THR B 1 495 ? -30.868 -33.687 21.440  1.00 23.84 ? 495  THR B CB    1 
ATOM   7987 O  OG1   . THR B 1 495 ? -32.210 -33.623 20.954  1.00 22.90 ? 495  THR B OG1   1 
ATOM   7988 C  CG2   . THR B 1 495 ? -29.981 -34.366 20.415  1.00 24.65 ? 495  THR B CG2   1 
ATOM   7989 N  N     . ILE B 1 496 ? -28.888 -33.465 23.881  1.00 22.24 ? 496  ILE B N     1 
ATOM   7990 C  CA    . ILE B 1 496 ? -27.541 -33.463 24.518  1.00 22.95 ? 496  ILE B CA    1 
ATOM   7991 C  C     . ILE B 1 496 ? -27.559 -34.329 25.790  1.00 20.80 ? 496  ILE B C     1 
ATOM   7992 O  O     . ILE B 1 496 ? -26.588 -35.096 25.981  1.00 19.97 ? 496  ILE B O     1 
ATOM   7993 C  CB    . ILE B 1 496 ? -27.045 -32.022 24.763  1.00 22.79 ? 496  ILE B CB    1 
ATOM   7994 C  CG1   . ILE B 1 496 ? -26.903 -31.272 23.431  1.00 25.38 ? 496  ILE B CG1   1 
ATOM   7995 C  CG2   . ILE B 1 496 ? -25.757 -32.034 25.562  1.00 21.28 ? 496  ILE B CG2   1 
ATOM   7996 C  CD1   . ILE B 1 496 ? -26.667 -29.776 23.579  1.00 27.45 ? 496  ILE B CD1   1 
ATOM   7997 N  N     . LYS B 1 497 ? -28.594 -34.216 26.624  1.00 19.37 ? 497  LYS B N     1 
ATOM   7998 C  CA    . LYS B 1 497 ? -28.756 -35.026 27.859  1.00 19.96 ? 497  LYS B CA    1 
ATOM   7999 C  C     . LYS B 1 497 ? -28.718 -36.523 27.505  1.00 21.99 ? 497  LYS B C     1 
ATOM   8000 O  O     . LYS B 1 497 ? -28.055 -37.297 28.224  1.00 22.81 ? 497  LYS B O     1 
ATOM   8001 C  CB    . LYS B 1 497 ? -30.079 -34.727 28.559  1.00 19.37 ? 497  LYS B CB    1 
ATOM   8002 C  CG    . LYS B 1 497 ? -30.344 -35.540 29.821  1.00 19.46 ? 497  LYS B CG    1 
ATOM   8003 C  CD    . LYS B 1 497 ? -29.418 -35.207 30.977  1.00 20.05 ? 497  LYS B CD    1 
ATOM   8004 C  CE    . LYS B 1 497 ? -29.744 -35.974 32.235  1.00 19.93 ? 497  LYS B CE    1 
ATOM   8005 N  NZ    . LYS B 1 497 ? -28.673 -35.878 33.265  1.00 20.65 ? 497  LYS B NZ    1 
ATOM   8006 N  N     . ASP B 1 498 ? -29.405 -36.925 26.442  1.00 21.63 ? 498  ASP B N     1 
ATOM   8007 C  CA    . ASP B 1 498 ? -29.542 -38.369 26.107  1.00 24.65 ? 498  ASP B CA    1 
ATOM   8008 C  C     . ASP B 1 498 ? -28.218 -38.876 25.521  1.00 25.04 ? 498  ASP B C     1 
ATOM   8009 O  O     . ASP B 1 498 ? -27.897 -40.049 25.737  1.00 28.44 ? 498  ASP B O     1 
ATOM   8010 C  CB    . ASP B 1 498 ? -30.748 -38.602 25.195  1.00 23.18 ? 498  ASP B CB    1 
ATOM   8011 C  CG    . ASP B 1 498 ? -32.082 -38.393 25.885  1.00 24.12 ? 498  ASP B CG    1 
ATOM   8012 O  OD1   . ASP B 1 498 ? -32.136 -38.439 27.159  1.00 26.85 ? 498  ASP B OD1   1 
ATOM   8013 O  OD2   . ASP B 1 498 ? -33.068 -38.207 25.161  1.00 24.94 ? 498  ASP B OD2   1 
ATOM   8014 N  N     . ALA B 1 499 ? -27.450 -38.005 24.872  1.00 26.36 ? 499  ALA B N     1 
ATOM   8015 C  CA    . ALA B 1 499 ? -26.134 -38.331 24.271  1.00 25.73 ? 499  ALA B CA    1 
ATOM   8016 C  C     . ALA B 1 499 ? -25.066 -38.450 25.368  1.00 25.27 ? 499  ALA B C     1 
ATOM   8017 O  O     . ALA B 1 499 ? -24.364 -39.456 25.373  1.00 21.79 ? 499  ALA B O     1 
ATOM   8018 C  CB    . ALA B 1 499 ? -25.776 -37.292 23.244  1.00 25.40 ? 499  ALA B CB    1 
ATOM   8019 N  N     . LEU B 1 500 ? -24.981 -37.502 26.308  1.00 23.58 ? 500  LEU B N     1 
ATOM   8020 C  CA    . LEU B 1 500 ? -23.968 -37.559 27.399  1.00 22.88 ? 500  LEU B CA    1 
ATOM   8021 C  C     . LEU B 1 500 ? -24.381 -38.541 28.505  1.00 21.98 ? 500  LEU B C     1 
ATOM   8022 O  O     . LEU B 1 500 ? -23.488 -39.150 29.089  1.00 19.12 ? 500  LEU B O     1 
ATOM   8023 C  CB    . LEU B 1 500 ? -23.735 -36.161 27.982  1.00 22.29 ? 500  LEU B CB    1 
ATOM   8024 C  CG    . LEU B 1 500 ? -23.180 -35.138 26.997  1.00 23.82 ? 500  LEU B CG    1 
ATOM   8025 C  CD1   . LEU B 1 500 ? -23.176 -33.759 27.616  1.00 24.84 ? 500  LEU B CD1   1 
ATOM   8026 C  CD2   . LEU B 1 500 ? -21.768 -35.481 26.534  1.00 26.16 ? 500  LEU B CD2   1 
ATOM   8027 N  N     . ASP B 1 501 ? -25.667 -38.602 28.856  1.00 23.30 ? 501  ASP B N     1 
ATOM   8028 C  CA    . ASP B 1 501 ? -26.170 -39.363 30.028  1.00 24.92 ? 501  ASP B CA    1 
ATOM   8029 C  C     . ASP B 1 501 ? -27.289 -40.312 29.577  1.00 26.40 ? 501  ASP B C     1 
ATOM   8030 O  O     . ASP B 1 501 ? -28.432 -40.181 30.004  1.00 27.68 ? 501  ASP B O     1 
ATOM   8031 C  CB    . ASP B 1 501 ? -26.592 -38.380 31.126  1.00 24.68 ? 501  ASP B CB    1 
ATOM   8032 C  CG    . ASP B 1 501 ? -26.908 -39.013 32.471  1.00 26.22 ? 501  ASP B CG    1 
ATOM   8033 O  OD1   . ASP B 1 501 ? -26.662 -40.249 32.627  1.00 24.29 ? 501  ASP B OD1   1 
ATOM   8034 O  OD2   . ASP B 1 501 ? -27.356 -38.258 33.387  1.00 26.24 ? 501  ASP B OD2   1 
ATOM   8035 N  N     . PRO B 1 502 ? -26.986 -41.344 28.757  1.00 28.97 ? 502  PRO B N     1 
ATOM   8036 C  CA    . PRO B 1 502 ? -28.018 -42.286 28.298  1.00 28.83 ? 502  PRO B CA    1 
ATOM   8037 C  C     . PRO B 1 502 ? -28.805 -42.984 29.438  1.00 28.26 ? 502  PRO B C     1 
ATOM   8038 O  O     . PRO B 1 502 ? -29.975 -43.184 29.285  1.00 28.86 ? 502  PRO B O     1 
ATOM   8039 C  CB    . PRO B 1 502 ? -27.254 -43.332 27.449  1.00 28.36 ? 502  PRO B CB    1 
ATOM   8040 C  CG    . PRO B 1 502 ? -25.806 -42.847 27.335  1.00 27.96 ? 502  PRO B CG    1 
ATOM   8041 C  CD    . PRO B 1 502 ? -25.622 -41.714 28.323  1.00 27.76 ? 502  PRO B CD    1 
ATOM   8042 N  N     . ASN B 1 503 ? -28.192 -43.295 30.583  1.00 27.72 ? 503  ASN B N     1 
ATOM   8043 C  CA    . ASN B 1 503 ? -28.930 -43.949 31.701  1.00 28.31 ? 503  ASN B CA    1 
ATOM   8044 C  C     . ASN B 1 503 ? -29.567 -42.931 32.655  1.00 29.32 ? 503  ASN B C     1 
ATOM   8045 O  O     . ASN B 1 503 ? -30.120 -43.392 33.646  1.00 30.48 ? 503  ASN B O     1 
ATOM   8046 C  CB    . ASN B 1 503 ? -28.047 -44.903 32.503  1.00 28.58 ? 503  ASN B CB    1 
ATOM   8047 C  CG    . ASN B 1 503 ? -27.373 -45.906 31.598  1.00 28.20 ? 503  ASN B CG    1 
ATOM   8048 O  OD1   . ASN B 1 503 ? -27.998 -46.420 30.684  1.00 29.55 ? 503  ASN B OD1   1 
ATOM   8049 N  ND2   . ASN B 1 503 ? -26.077 -46.079 31.761  1.00 29.10 ? 503  ASN B ND2   1 
ATOM   8050 N  N     . GLY B 1 504 ? -29.448 -41.619 32.397  1.00 28.74 ? 504  GLY B N     1 
ATOM   8051 C  CA    . GLY B 1 504 ? -30.111 -40.545 33.158  1.00 25.37 ? 504  GLY B CA    1 
ATOM   8052 C  C     . GLY B 1 504 ? -29.773 -40.620 34.626  1.00 28.16 ? 504  GLY B C     1 
ATOM   8053 O  O     . GLY B 1 504 ? -30.694 -40.524 35.448  1.00 32.97 ? 504  GLY B O     1 
ATOM   8054 N  N     . ILE B 1 505 ? -28.491 -40.763 34.972  1.00 27.79 ? 505  ILE B N     1 
ATOM   8055 C  CA    . ILE B 1 505 ? -28.090 -40.888 36.393  1.00 27.99 ? 505  ILE B CA    1 
ATOM   8056 C  C     . ILE B 1 505 ? -27.619 -39.537 36.958  1.00 27.46 ? 505  ILE B C     1 
ATOM   8057 O  O     . ILE B 1 505 ? -27.459 -39.501 38.165  1.00 30.98 ? 505  ILE B O     1 
ATOM   8058 C  CB    . ILE B 1 505 ? -27.097 -42.063 36.630  1.00 31.97 ? 505  ILE B CB    1 
ATOM   8059 C  CG1   . ILE B 1 505 ? -25.879 -42.084 35.702  1.00 33.71 ? 505  ILE B CG1   1 
ATOM   8060 C  CG2   . ILE B 1 505 ? -27.856 -43.386 36.556  1.00 32.55 ? 505  ILE B CG2   1 
ATOM   8061 C  CD1   . ILE B 1 505 ? -24.784 -41.121 36.068  1.00 35.69 ? 505  ILE B CD1   1 
ATOM   8062 N  N     . LEU B 1 506 ? -27.450 -38.452 36.189  1.00 25.35 ? 506  LEU B N     1 
ATOM   8063 C  CA    . LEU B 1 506 ? -27.074 -37.144 36.811  1.00 24.67 ? 506  LEU B CA    1 
ATOM   8064 C  C     . LEU B 1 506 ? -28.313 -36.242 37.020  1.00 24.62 ? 506  LEU B C     1 
ATOM   8065 O  O     . LEU B 1 506 ? -29.037 -35.900 36.033  1.00 22.43 ? 506  LEU B O     1 
ATOM   8066 C  CB    . LEU B 1 506 ? -26.018 -36.431 35.965  1.00 26.52 ? 506  LEU B CB    1 
ATOM   8067 C  CG    . LEU B 1 506 ? -24.618 -37.054 35.906  1.00 28.23 ? 506  LEU B CG    1 
ATOM   8068 C  CD1   . LEU B 1 506 ? -23.642 -36.041 35.321  1.00 29.15 ? 506  LEU B CD1   1 
ATOM   8069 C  CD2   . LEU B 1 506 ? -24.119 -37.518 37.270  1.00 28.32 ? 506  LEU B CD2   1 
ATOM   8070 N  N     . ALA B 1 507 ? -28.556 -35.881 38.280  1.00 23.97 ? 507  ALA B N     1 
ATOM   8071 C  CA    . ALA B 1 507 ? -29.498 -34.829 38.758  1.00 24.18 ? 507  ALA B CA    1 
ATOM   8072 C  C     . ALA B 1 507 ? -30.728 -34.723 37.852  1.00 24.16 ? 507  ALA B C     1 
ATOM   8073 O  O     . ALA B 1 507 ? -30.965 -33.697 37.197  1.00 23.16 ? 507  ALA B O     1 
ATOM   8074 C  CB    . ALA B 1 507 ? -28.757 -33.518 38.898  1.00 23.04 ? 507  ALA B CB    1 
ATOM   8075 N  N     . PRO B 1 508 ? -31.563 -35.785 37.804  1.00 23.72 ? 508  PRO B N     1 
ATOM   8076 C  CA    . PRO B 1 508 ? -32.791 -35.745 37.023  1.00 23.43 ? 508  PRO B CA    1 
ATOM   8077 C  C     . PRO B 1 508 ? -33.621 -34.522 37.435  1.00 24.14 ? 508  PRO B C     1 
ATOM   8078 O  O     . PRO B 1 508 ? -33.797 -34.298 38.629  1.00 23.41 ? 508  PRO B O     1 
ATOM   8079 C  CB    . PRO B 1 508 ? -33.513 -37.065 37.325  1.00 25.98 ? 508  PRO B CB    1 
ATOM   8080 C  CG    . PRO B 1 508 ? -32.433 -37.955 37.923  1.00 26.43 ? 508  PRO B CG    1 
ATOM   8081 C  CD    . PRO B 1 508 ? -31.402 -37.040 38.557  1.00 24.66 ? 508  PRO B CD    1 
ATOM   8082 N  N     . GLY B 1 509 ? -34.056 -33.742 36.441  1.00 22.76 ? 509  GLY B N     1 
ATOM   8083 C  CA    . GLY B 1 509 ? -34.933 -32.574 36.617  1.00 24.87 ? 509  GLY B CA    1 
ATOM   8084 C  C     . GLY B 1 509 ? -34.189 -31.260 36.848  1.00 26.46 ? 509  GLY B C     1 
ATOM   8085 O  O     . GLY B 1 509 ? -34.884 -30.222 36.878  1.00 24.63 ? 509  GLY B O     1 
ATOM   8086 N  N     . LYS B 1 510 ? -32.861 -31.261 37.012  1.00 24.72 ? 510  LYS B N     1 
ATOM   8087 C  CA    . LYS B 1 510 ? -32.103 -29.993 37.134  1.00 26.69 ? 510  LYS B CA    1 
ATOM   8088 C  C     . LYS B 1 510 ? -32.470 -29.130 35.920  1.00 25.49 ? 510  LYS B C     1 
ATOM   8089 O  O     . LYS B 1 510 ? -32.464 -29.669 34.806  1.00 24.78 ? 510  LYS B O     1 
ATOM   8090 C  CB    . LYS B 1 510 ? -30.600 -30.244 37.262  1.00 27.35 ? 510  LYS B CB    1 
ATOM   8091 C  CG    . LYS B 1 510 ? -29.731 -28.998 37.237  1.00 29.03 ? 510  LYS B CG    1 
ATOM   8092 C  CD    . LYS B 1 510 ? -29.984 -28.001 38.379  1.00 30.42 ? 510  LYS B CD    1 
ATOM   8093 C  CE    . LYS B 1 510 ? -29.095 -26.780 38.261  1.00 30.85 ? 510  LYS B CE    1 
ATOM   8094 N  NZ    . LYS B 1 510 ? -29.560 -25.645 39.102  1.00 32.89 ? 510  LYS B NZ    1 
ATOM   8095 N  N     . SER B 1 511 ? -32.919 -27.895 36.147  1.00 22.79 ? 511  SER B N     1 
ATOM   8096 C  CA    . SER B 1 511 ? -33.303 -26.937 35.074  1.00 24.93 ? 511  SER B CA    1 
ATOM   8097 C  C     . SER B 1 511 ? -34.427 -27.500 34.192  1.00 24.08 ? 511  SER B C     1 
ATOM   8098 O  O     . SER B 1 511 ? -34.490 -27.131 33.008  1.00 23.58 ? 511  SER B O     1 
ATOM   8099 C  CB    . SER B 1 511 ? -32.087 -26.574 34.245  1.00 24.57 ? 511  SER B CB    1 
ATOM   8100 O  OG    . SER B 1 511 ? -31.104 -25.946 35.054  1.00 25.16 ? 511  SER B OG    1 
ATOM   8101 N  N     . GLY B 1 512 ? -35.290 -28.362 34.736  1.00 22.54 ? 512  GLY B N     1 
ATOM   8102 C  CA    . GLY B 1 512 ? -36.334 -29.052 33.954  1.00 21.87 ? 512  GLY B CA    1 
ATOM   8103 C  C     . GLY B 1 512 ? -35.814 -29.991 32.861  1.00 23.12 ? 512  GLY B C     1 
ATOM   8104 O  O     . GLY B 1 512 ? -36.564 -30.230 31.869  1.00 24.66 ? 512  GLY B O     1 
ATOM   8105 N  N     . ILE B 1 513 ? -34.602 -30.526 32.999  1.00 22.40 ? 513  ILE B N     1 
ATOM   8106 C  CA    . ILE B 1 513 ? -34.009 -31.472 32.004  1.00 24.00 ? 513  ILE B CA    1 
ATOM   8107 C  C     . ILE B 1 513 ? -34.090 -32.887 32.595  1.00 24.14 ? 513  ILE B C     1 
ATOM   8108 O  O     . ILE B 1 513 ? -33.472 -33.136 33.654  1.00 23.59 ? 513  ILE B O     1 
ATOM   8109 C  CB    . ILE B 1 513 ? -32.563 -31.092 31.629  1.00 23.38 ? 513  ILE B CB    1 
ATOM   8110 C  CG1   . ILE B 1 513 ? -32.445 -29.651 31.107  1.00 23.77 ? 513  ILE B CG1   1 
ATOM   8111 C  CG2   . ILE B 1 513 ? -31.996 -32.095 30.647  1.00 23.54 ? 513  ILE B CG2   1 
ATOM   8112 C  CD1   . ILE B 1 513 ? -31.018 -29.185 30.919  1.00 22.71 ? 513  ILE B CD1   1 
ATOM   8113 N  N     . TRP B 1 514 ? -34.879 -33.732 31.947  1.00 26.28 ? 514  TRP B N     1 
ATOM   8114 C  CA    . TRP B 1 514 ? -35.098 -35.172 32.235  1.00 30.58 ? 514  TRP B CA    1 
ATOM   8115 C  C     . TRP B 1 514 ? -34.597 -35.958 31.010  1.00 33.26 ? 514  TRP B C     1 
ATOM   8116 O  O     . TRP B 1 514 ? -34.838 -35.530 29.811  1.00 39.18 ? 514  TRP B O     1 
ATOM   8117 C  CB    . TRP B 1 514 ? -36.586 -35.444 32.520  1.00 28.86 ? 514  TRP B CB    1 
ATOM   8118 C  CG    . TRP B 1 514 ? -37.183 -34.614 33.615  1.00 28.63 ? 514  TRP B CG    1 
ATOM   8119 C  CD1   . TRP B 1 514 ? -37.697 -33.352 33.506  1.00 28.19 ? 514  TRP B CD1   1 
ATOM   8120 C  CD2   . TRP B 1 514 ? -37.337 -34.988 34.999  1.00 25.90 ? 514  TRP B CD2   1 
ATOM   8121 N  NE1   . TRP B 1 514 ? -38.144 -32.917 34.723  1.00 28.10 ? 514  TRP B NE1   1 
ATOM   8122 C  CE2   . TRP B 1 514 ? -37.948 -33.897 35.658  1.00 27.05 ? 514  TRP B CE2   1 
ATOM   8123 C  CE3   . TRP B 1 514 ? -37.013 -36.125 35.742  1.00 25.62 ? 514  TRP B CE3   1 
ATOM   8124 C  CZ2   . TRP B 1 514 ? -38.230 -33.906 37.026  1.00 25.71 ? 514  TRP B CZ2   1 
ATOM   8125 C  CZ3   . TRP B 1 514 ? -37.290 -36.140 37.096  1.00 27.38 ? 514  TRP B CZ3   1 
ATOM   8126 C  CH2   . TRP B 1 514 ? -37.886 -35.041 37.730  1.00 26.72 ? 514  TRP B CH2   1 
ATOM   8127 N  N     . GLY B 1 515 ? -33.899 -37.045 31.256  1.00 31.70 ? 515  GLY B N     1 
ATOM   8128 C  CA    . GLY B 1 515 ? -33.495 -37.924 30.150  1.00 31.59 ? 515  GLY B CA    1 
ATOM   8129 C  C     . GLY B 1 515 ? -34.661 -38.738 29.607  1.00 31.14 ? 515  GLY B C     1 
ATOM   8130 O  O     . GLY B 1 515 ? -35.758 -38.675 30.182  1.00 27.37 ? 515  GLY B O     1 
ATOM   8131 N  N     . LYS B 1 516 ? -34.402 -39.511 28.549  1.00 32.06 ? 516  LYS B N     1 
ATOM   8132 C  CA    . LYS B 1 516 ? -35.415 -40.323 27.829  1.00 35.72 ? 516  LYS B CA    1 
ATOM   8133 C  C     . LYS B 1 516 ? -36.077 -41.337 28.787  1.00 36.73 ? 516  LYS B C     1 
ATOM   8134 O  O     . LYS B 1 516 ? -37.287 -41.623 28.598  1.00 35.67 ? 516  LYS B O     1 
ATOM   8135 C  CB    . LYS B 1 516 ? -34.802 -41.011 26.601  1.00 38.52 ? 516  LYS B CB    1 
ATOM   8136 C  CG    . LYS B 1 516 ? -33.498 -41.774 26.814  1.00 43.55 ? 516  LYS B CG    1 
ATOM   8137 C  CD    . LYS B 1 516 ? -33.324 -42.946 25.834  1.00 52.22 ? 516  LYS B CD    1 
ATOM   8138 C  CE    . LYS B 1 516 ? -31.900 -43.239 25.396  1.00 56.15 ? 516  LYS B CE    1 
ATOM   8139 N  NZ    . LYS B 1 516 ? -31.045 -43.696 26.517  1.00 61.03 ? 516  LYS B NZ    1 
ATOM   8140 N  N     . ASN B 1 517 ? -35.354 -41.856 29.780  1.00 31.95 ? 517  ASN B N     1 
ATOM   8141 C  CA    . ASN B 1 517 ? -35.917 -42.859 30.718  1.00 34.93 ? 517  ASN B CA    1 
ATOM   8142 C  C     . ASN B 1 517 ? -37.020 -42.243 31.590  1.00 36.07 ? 517  ASN B C     1 
ATOM   8143 O  O     . ASN B 1 517 ? -37.838 -43.014 32.057  1.00 38.97 ? 517  ASN B O     1 
ATOM   8144 C  CB    . ASN B 1 517 ? -34.860 -43.497 31.613  1.00 36.29 ? 517  ASN B CB    1 
ATOM   8145 C  CG    . ASN B 1 517 ? -33.815 -44.263 30.831  1.00 35.34 ? 517  ASN B CG    1 
ATOM   8146 O  OD1   . ASN B 1 517 ? -34.064 -44.715 29.723  1.00 38.63 ? 517  ASN B OD1   1 
ATOM   8147 N  ND2   . ASN B 1 517 ? -32.639 -44.413 31.406  1.00 35.56 ? 517  ASN B ND2   1 
ATOM   8148 N  N     . ARG B 1 518 ? -37.046 -40.925 31.830  1.00 37.36 ? 518  ARG B N     1 
ATOM   8149 C  CA    . ARG B 1 518 ? -38.008 -40.320 32.796  1.00 36.44 ? 518  ARG B CA    1 
ATOM   8150 C  C     . ARG B 1 518 ? -38.971 -39.327 32.133  1.00 35.34 ? 518  ARG B C     1 
ATOM   8151 O  O     . ARG B 1 518 ? -39.903 -38.898 32.820  1.00 41.27 ? 518  ARG B O     1 
ATOM   8152 C  CB    . ARG B 1 518 ? -37.241 -39.677 33.955  1.00 36.81 ? 518  ARG B CB    1 
ATOM   8153 C  CG    . ARG B 1 518 ? -36.408 -40.663 34.763  1.00 36.01 ? 518  ARG B CG    1 
ATOM   8154 C  CD    . ARG B 1 518 ? -36.051 -40.144 36.133  1.00 37.62 ? 518  ARG B CD    1 
ATOM   8155 N  NE    . ARG B 1 518 ? -35.293 -41.112 36.925  1.00 39.94 ? 518  ARG B NE    1 
ATOM   8156 C  CZ    . ARG B 1 518 ? -35.828 -42.091 37.661  1.00 49.94 ? 518  ARG B CZ    1 
ATOM   8157 N  NH1   . ARG B 1 518 ? -37.144 -42.256 37.744  1.00 51.14 ? 518  ARG B NH1   1 
ATOM   8158 N  NH2   . ARG B 1 518 ? -35.034 -42.916 38.321  1.00 49.38 ? 518  ARG B NH2   1 
ATOM   8159 N  N     . ARG B 1 519 ? -38.788 -38.969 30.868  1.00 37.65 ? 519  ARG B N     1 
ATOM   8160 C  CA    . ARG B 1 519 ? -39.480 -37.806 30.233  1.00 40.77 ? 519  ARG B CA    1 
ATOM   8161 C  C     . ARG B 1 519 ? -40.955 -38.146 29.983  1.00 41.72 ? 519  ARG B C     1 
ATOM   8162 O  O     . ARG B 1 519 ? -41.102 -39.260 29.486  1.00 41.11 ? 519  ARG B O     1 
ATOM   8163 C  CB    . ARG B 1 519 ? -38.754 -37.435 28.935  1.00 42.17 ? 519  ARG B CB    1 
ATOM   8164 C  CG    . ARG B 1 519 ? -38.746 -35.949 28.630  1.00 43.45 ? 519  ARG B CG    1 
ATOM   8165 C  CD    . ARG B 1 519 ? -37.701 -35.518 27.616  1.00 39.60 ? 519  ARG B CD    1 
ATOM   8166 N  NE    . ARG B 1 519 ? -37.292 -36.513 26.626  1.00 39.19 ? 519  ARG B NE    1 
ATOM   8167 C  CZ    . ARG B 1 519 ? -36.045 -36.977 26.429  1.00 35.83 ? 519  ARG B CZ    1 
ATOM   8168 N  NH1   . ARG B 1 519 ? -35.013 -36.577 27.156  1.00 36.18 ? 519  ARG B NH1   1 
ATOM   8169 N  NH2   . ARG B 1 519 ? -35.823 -37.857 25.476  1.00 34.79 ? 519  ARG B NH2   1 
HETATM 8170 P  PA    . FAD C 2 .   ? -16.951 -16.164 7.496   1.00 18.53 ? 601  FAD A PA    1 
HETATM 8171 O  O1A   . FAD C 2 .   ? -15.964 -16.571 6.444   1.00 16.24 ? 601  FAD A O1A   1 
HETATM 8172 O  O2A   . FAD C 2 .   ? -18.339 -15.915 7.006   1.00 17.91 ? 601  FAD A O2A   1 
HETATM 8173 O  O5B   . FAD C 2 .   ? -16.980 -17.197 8.710   1.00 18.25 ? 601  FAD A O5B   1 
HETATM 8174 C  C5B   . FAD C 2 .   ? -15.772 -17.883 9.135   1.00 18.78 ? 601  FAD A C5B   1 
HETATM 8175 C  C4B   . FAD C 2 .   ? -16.073 -19.315 9.512   1.00 19.01 ? 601  FAD A C4B   1 
HETATM 8176 O  O4B   . FAD C 2 .   ? -17.003 -19.371 10.638  1.00 20.08 ? 601  FAD A O4B   1 
HETATM 8177 C  C3B   . FAD C 2 .   ? -16.738 -20.163 8.422   1.00 18.89 ? 601  FAD A C3B   1 
HETATM 8178 O  O3B   . FAD C 2 .   ? -15.760 -20.728 7.557   1.00 20.76 ? 601  FAD A O3B   1 
HETATM 8179 C  C2B   . FAD C 2 .   ? -17.482 -21.217 9.249   1.00 19.57 ? 601  FAD A C2B   1 
HETATM 8180 O  O2B   . FAD C 2 .   ? -16.644 -22.202 9.768   1.00 19.51 ? 601  FAD A O2B   1 
HETATM 8181 C  C1B   . FAD C 2 .   ? -17.953 -20.410 10.454  1.00 19.28 ? 601  FAD A C1B   1 
HETATM 8182 N  N9A   . FAD C 2 .   ? -19.251 -19.803 10.249  1.00 22.76 ? 601  FAD A N9A   1 
HETATM 8183 C  C8A   . FAD C 2 .   ? -19.468 -18.570 9.677   1.00 22.42 ? 601  FAD A C8A   1 
HETATM 8184 N  N7A   . FAD C 2 .   ? -20.733 -18.241 9.632   1.00 21.79 ? 601  FAD A N7A   1 
HETATM 8185 C  C5A   . FAD C 2 .   ? -21.387 -19.318 10.214  1.00 23.44 ? 601  FAD A C5A   1 
HETATM 8186 C  C6A   . FAD C 2 .   ? -22.749 -19.551 10.478  1.00 21.98 ? 601  FAD A C6A   1 
HETATM 8187 N  N6A   . FAD C 2 .   ? -23.703 -18.659 10.213  1.00 22.64 ? 601  FAD A N6A   1 
HETATM 8188 N  N1A   . FAD C 2 .   ? -23.071 -20.710 11.103  1.00 20.80 ? 601  FAD A N1A   1 
HETATM 8189 C  C2A   . FAD C 2 .   ? -22.084 -21.576 11.388  1.00 23.23 ? 601  FAD A C2A   1 
HETATM 8190 N  N3A   . FAD C 2 .   ? -20.772 -21.459 11.193  1.00 23.34 ? 601  FAD A N3A   1 
HETATM 8191 C  C4A   . FAD C 2 .   ? -20.484 -20.294 10.593  1.00 22.19 ? 601  FAD A C4A   1 
HETATM 8192 N  N1    . FAD C 2 .   ? -9.412  -11.605 11.592  1.00 16.35 ? 601  FAD A N1    1 
HETATM 8193 C  C2    . FAD C 2 .   ? -9.650  -11.044 12.798  1.00 15.09 ? 601  FAD A C2    1 
HETATM 8194 O  O2    . FAD C 2 .   ? -10.405 -11.597 13.621  1.00 14.61 ? 601  FAD A O2    1 
HETATM 8195 N  N3    . FAD C 2 .   ? -9.039  -9.883  13.175  1.00 14.26 ? 601  FAD A N3    1 
HETATM 8196 C  C4    . FAD C 2 .   ? -8.289  -9.144  12.292  1.00 14.62 ? 601  FAD A C4    1 
HETATM 8197 O  O4    . FAD C 2 .   ? -7.813  -8.068  12.660  1.00 14.94 ? 601  FAD A O4    1 
HETATM 8198 C  C4X   . FAD C 2 .   ? -8.029  -9.684  11.025  1.00 15.00 ? 601  FAD A C4X   1 
HETATM 8199 N  N5    . FAD C 2 .   ? -7.293  -8.988  10.167  1.00 15.41 ? 601  FAD A N5    1 
HETATM 8200 C  C5X   . FAD C 2 .   ? -6.988  -9.588  8.965   1.00 16.24 ? 601  FAD A C5X   1 
HETATM 8201 C  C6    . FAD C 2 .   ? -6.135  -8.910  8.073   1.00 15.20 ? 601  FAD A C6    1 
HETATM 8202 C  C7    . FAD C 2 .   ? -5.774  -9.458  6.863   1.00 16.94 ? 601  FAD A C7    1 
HETATM 8203 C  C7M   . FAD C 2 .   ? -4.833  -8.729  5.938   1.00 16.23 ? 601  FAD A C7M   1 
HETATM 8204 C  C8    . FAD C 2 .   ? -6.230  -10.760 6.530   1.00 17.10 ? 601  FAD A C8    1 
HETATM 8205 C  C8M   . FAD C 2 .   ? -5.706  -11.465 5.297   1.00 19.67 ? 601  FAD A C8M   1 
HETATM 8206 C  C9    . FAD C 2 .   ? -7.119  -11.410 7.375   1.00 16.58 ? 601  FAD A C9    1 
HETATM 8207 C  C9A   . FAD C 2 .   ? -7.501  -10.863 8.606   1.00 15.65 ? 601  FAD A C9A   1 
HETATM 8208 N  N10   . FAD C 2 .   ? -8.375  -11.502 9.488   1.00 15.26 ? 601  FAD A N10   1 
HETATM 8209 C  C10   . FAD C 2 .   ? -8.656  -10.941 10.732  1.00 15.27 ? 601  FAD A C10   1 
HETATM 8210 C  "C1'" . FAD C 2 .   ? -8.914  -12.849 9.192   1.00 14.62 ? 601  FAD A "C1'" 1 
HETATM 8211 C  "C2'" . FAD C 2 .   ? -10.249 -12.891 8.408   1.00 14.92 ? 601  FAD A "C2'" 1 
HETATM 8212 O  "O2'" . FAD C 2 .   ? -10.051 -12.481 7.074   1.00 15.51 ? 601  FAD A "O2'" 1 
HETATM 8213 C  "C3'" . FAD C 2 .   ? -11.395 -12.115 9.060   1.00 15.32 ? 601  FAD A "C3'" 1 
HETATM 8214 O  "O3'" . FAD C 2 .   ? -11.545 -12.629 10.368  1.00 14.74 ? 601  FAD A "O3'" 1 
HETATM 8215 C  "C4'" . FAD C 2 .   ? -12.740 -12.180 8.327   1.00 16.12 ? 601  FAD A "C4'" 1 
HETATM 8216 O  "O4'" . FAD C 2 .   ? -13.640 -11.174 8.818   1.00 14.90 ? 601  FAD A "O4'" 1 
HETATM 8217 C  "C5'" . FAD C 2 .   ? -13.396 -13.542 8.436   1.00 16.62 ? 601  FAD A "C5'" 1 
HETATM 8218 O  "O5'" . FAD C 2 .   ? -14.350 -13.770 7.333   1.00 16.89 ? 601  FAD A "O5'" 1 
HETATM 8219 P  P     . FAD C 2 .   ? -15.905 -13.502 7.579   1.00 17.15 ? 601  FAD A P     1 
HETATM 8220 O  O1P   . FAD C 2 .   ? -16.075 -12.461 8.636   1.00 18.75 ? 601  FAD A O1P   1 
HETATM 8221 O  O2P   . FAD C 2 .   ? -16.470 -13.346 6.219   1.00 16.20 ? 601  FAD A O2P   1 
HETATM 8222 O  O3P   . FAD C 2 .   ? -16.456 -14.840 8.267   1.00 18.04 ? 601  FAD A O3P   1 
HETATM 8223 CL CL    . CL  D 3 .   ? -18.994 -35.088 9.462   1.00 10.35 ? 602  CL  A CL    1 
HETATM 8224 CL CL    . CL  E 3 .   ? -36.291 -11.170 14.807  1.00 34.11 ? 603  CL  A CL    1 
HETATM 8225 C  C1    . PEG F 4 .   ? -10.178 -6.422  26.215  1.00 45.32 ? 604  PEG A C1    1 
HETATM 8226 O  O1    . PEG F 4 .   ? -9.327  -5.393  25.793  1.00 40.81 ? 604  PEG A O1    1 
HETATM 8227 C  C2    . PEG F 4 .   ? -10.484 -7.381  25.109  1.00 49.86 ? 604  PEG A C2    1 
HETATM 8228 O  O2    . PEG F 4 .   ? -9.732  -7.063  23.938  1.00 53.25 ? 604  PEG A O2    1 
HETATM 8229 C  C3    . PEG F 4 .   ? -9.373  -8.218  23.167  1.00 56.77 ? 604  PEG A C3    1 
HETATM 8230 C  C4    . PEG F 4 .   ? -8.867  -7.811  21.800  1.00 51.33 ? 604  PEG A C4    1 
HETATM 8231 O  O4    . PEG F 4 .   ? -7.697  -8.487  21.405  1.00 50.66 ? 604  PEG A O4    1 
HETATM 8232 C  C1    . PEG G 4 .   ? -30.877 -31.800 16.318  1.00 45.20 ? 605  PEG A C1    1 
HETATM 8233 O  O1    . PEG G 4 .   ? -30.738 -32.312 14.994  1.00 39.84 ? 605  PEG A O1    1 
HETATM 8234 C  C2    . PEG G 4 .   ? -31.755 -32.637 17.236  1.00 42.54 ? 605  PEG A C2    1 
HETATM 8235 O  O2    . PEG G 4 .   ? -31.831 -31.977 18.504  1.00 38.76 ? 605  PEG A O2    1 
HETATM 8236 C  C3    . PEG G 4 .   ? -33.154 -31.859 19.028  1.00 45.33 ? 605  PEG A C3    1 
HETATM 8237 C  C4    . PEG G 4 .   ? -33.763 -30.547 18.685  1.00 44.56 ? 605  PEG A C4    1 
HETATM 8238 O  O4    . PEG G 4 .   ? -34.816 -30.640 17.731  1.00 50.36 ? 605  PEG A O4    1 
HETATM 8239 C  C1    . PEG H 4 .   ? -9.039  0.288   35.789  1.00 56.62 ? 606  PEG A C1    1 
HETATM 8240 O  O1    . PEG H 4 .   ? -10.050 -0.420  36.479  1.00 57.28 ? 606  PEG A O1    1 
HETATM 8241 C  C2    . PEG H 4 .   ? -9.491  0.722   34.421  1.00 57.69 ? 606  PEG A C2    1 
HETATM 8242 O  O2    . PEG H 4 .   ? -10.035 2.039   34.472  1.00 59.86 ? 606  PEG A O2    1 
HETATM 8243 C  C3    . PEG H 4 .   ? -11.092 2.291   33.544  1.00 53.69 ? 606  PEG A C3    1 
HETATM 8244 C  C4    . PEG H 4 .   ? -11.846 3.530   33.961  1.00 54.13 ? 606  PEG A C4    1 
HETATM 8245 O  O4    . PEG H 4 .   ? -13.266 3.405   33.814  1.00 54.00 ? 606  PEG A O4    1 
HETATM 8246 P  PA    . FAD I 2 .   ? -24.056 -25.564 45.670  1.00 26.53 ? 601  FAD B PA    1 
HETATM 8247 O  O1A   . FAD I 2 .   ? -25.295 -25.775 46.486  1.00 24.35 ? 601  FAD B O1A   1 
HETATM 8248 O  O2A   . FAD I 2 .   ? -22.910 -26.495 45.935  1.00 24.69 ? 601  FAD B O2A   1 
HETATM 8249 O  O5B   . FAD I 2 .   ? -24.418 -25.659 44.112  1.00 22.44 ? 601  FAD B O5B   1 
HETATM 8250 C  C5B   . FAD I 2 .   ? -25.630 -25.084 43.573  1.00 23.91 ? 601  FAD B C5B   1 
HETATM 8251 C  C4B   . FAD I 2 .   ? -26.155 -25.991 42.491  1.00 25.79 ? 601  FAD B C4B   1 
HETATM 8252 O  O4B   . FAD I 2 .   ? -25.215 -26.001 41.377  1.00 23.08 ? 601  FAD B O4B   1 
HETATM 8253 C  C3B   . FAD I 2 .   ? -26.337 -27.478 42.871  1.00 26.93 ? 601  FAD B C3B   1 
HETATM 8254 O  O3B   . FAD I 2 .   ? -27.613 -27.739 43.432  1.00 26.43 ? 601  FAD B O3B   1 
HETATM 8255 C  C2B   . FAD I 2 .   ? -26.171 -28.177 41.518  1.00 26.14 ? 601  FAD B C2B   1 
HETATM 8256 O  O2B   . FAD I 2 .   ? -27.380 -28.193 40.793  1.00 27.88 ? 601  FAD B O2B   1 
HETATM 8257 C  C1B   . FAD I 2 .   ? -25.073 -27.323 40.877  1.00 25.15 ? 601  FAD B C1B   1 
HETATM 8258 N  N9A   . FAD I 2 .   ? -23.701 -27.767 41.181  1.00 24.53 ? 601  FAD B N9A   1 
HETATM 8259 C  C8A   . FAD I 2 .   ? -22.883 -27.352 42.223  1.00 23.93 ? 601  FAD B C8A   1 
HETATM 8260 N  N7A   . FAD I 2 .   ? -21.698 -27.922 42.192  1.00 23.06 ? 601  FAD B N7A   1 
HETATM 8261 C  C5A   . FAD I 2 .   ? -21.720 -28.701 41.038  1.00 23.26 ? 601  FAD B C5A   1 
HETATM 8262 C  C6A   . FAD I 2 .   ? -20.750 -29.520 40.426  1.00 22.42 ? 601  FAD B C6A   1 
HETATM 8263 N  N6A   . FAD I 2 .   ? -19.514 -29.645 40.892  1.00 23.91 ? 601  FAD B N6A   1 
HETATM 8264 N  N1A   . FAD I 2 .   ? -21.086 -30.146 39.273  1.00 19.15 ? 601  FAD B N1A   1 
HETATM 8265 C  C2A   . FAD I 2 .   ? -22.308 -29.938 38.787  1.00 22.14 ? 601  FAD B C2A   1 
HETATM 8266 N  N3A   . FAD I 2 .   ? -23.315 -29.220 39.292  1.00 25.48 ? 601  FAD B N3A   1 
HETATM 8267 C  C4A   . FAD I 2 .   ? -22.944 -28.606 40.416  1.00 23.08 ? 601  FAD B C4A   1 
HETATM 8268 N  N1    . FAD I 2 .   ? -26.753 -16.279 45.894  1.00 27.96 ? 601  FAD B N1    1 
HETATM 8269 C  C2    . FAD I 2 .   ? -26.050 -15.401 45.137  1.00 27.07 ? 601  FAD B C2    1 
HETATM 8270 O  O2    . FAD I 2 .   ? -25.622 -15.716 44.015  1.00 23.53 ? 601  FAD B O2    1 
HETATM 8271 N  N3    . FAD I 2 .   ? -25.805 -14.114 45.561  1.00 27.45 ? 601  FAD B N3    1 
HETATM 8272 C  C4    . FAD I 2 .   ? -26.186 -13.660 46.804  1.00 29.15 ? 601  FAD B C4    1 
HETATM 8273 O  O4    . FAD I 2 .   ? -25.916 -12.495 47.144  1.00 25.46 ? 601  FAD B O4    1 
HETATM 8274 C  C4X   . FAD I 2 .   ? -26.944 -14.553 47.604  1.00 26.68 ? 601  FAD B C4X   1 
HETATM 8275 N  N5    . FAD I 2 .   ? -27.341 -14.135 48.771  1.00 29.10 ? 601  FAD B N5    1 
HETATM 8276 C  C5X   . FAD I 2 .   ? -28.137 -14.968 49.509  1.00 27.52 ? 601  FAD B C5X   1 
HETATM 8277 C  C6    . FAD I 2 .   ? -28.616 -14.474 50.734  1.00 27.34 ? 601  FAD B C6    1 
HETATM 8278 C  C7    . FAD I 2 .   ? -29.452 -15.212 51.540  1.00 28.36 ? 601  FAD B C7    1 
HETATM 8279 C  C7M   . FAD I 2 .   ? -29.935 -14.633 52.845  1.00 27.42 ? 601  FAD B C7M   1 
HETATM 8280 C  C8    . FAD I 2 .   ? -29.792 -16.535 51.147  1.00 27.69 ? 601  FAD B C8    1 
HETATM 8281 C  C8M   . FAD I 2 .   ? -30.809 -17.321 51.941  1.00 29.86 ? 601  FAD B C8M   1 
HETATM 8282 C  C9    . FAD I 2 .   ? -29.272 -17.057 49.943  1.00 25.60 ? 601  FAD B C9    1 
HETATM 8283 C  C9A   . FAD I 2 .   ? -28.459 -16.281 49.093  1.00 27.43 ? 601  FAD B C9A   1 
HETATM 8284 N  N10   . FAD I 2 .   ? -27.932 -16.734 47.863  1.00 26.17 ? 601  FAD B N10   1 
HETATM 8285 C  C10   . FAD I 2 .   ? -27.194 -15.871 47.070  1.00 27.34 ? 601  FAD B C10   1 
HETATM 8286 C  "C1'" . FAD I 2 .   ? -28.243 -18.091 47.342  1.00 25.28 ? 601  FAD B "C1'" 1 
HETATM 8287 C  "C2'" . FAD I 2 .   ? -27.248 -19.204 47.808  1.00 24.07 ? 601  FAD B "C2'" 1 
HETATM 8288 O  "O2'" . FAD I 2 .   ? -27.235 -19.324 49.252  1.00 27.89 ? 601  FAD B "O2'" 1 
HETATM 8289 C  "C3'" . FAD I 2 .   ? -25.791 -18.979 47.365  1.00 22.13 ? 601  FAD B "C3'" 1 
HETATM 8290 O  "O3'" . FAD I 2 .   ? -25.732 -18.703 45.960  1.00 19.93 ? 601  FAD B "O3'" 1 
HETATM 8291 C  "C4'" . FAD I 2 .   ? -24.857 -20.149 47.688  1.00 20.75 ? 601  FAD B "C4'" 1 
HETATM 8292 O  "O4'" . FAD I 2 .   ? -23.504 -19.722 47.557  1.00 19.54 ? 601  FAD B "O4'" 1 
HETATM 8293 C  "C5'" . FAD I 2 .   ? -25.070 -21.332 46.768  1.00 23.15 ? 601  FAD B "C5'" 1 
HETATM 8294 O  "O5'" . FAD I 2 .   ? -24.675 -22.606 47.385  1.00 24.13 ? 601  FAD B "O5'" 1 
HETATM 8295 P  P     . FAD I 2 .   ? -23.219 -23.210 47.099  1.00 24.63 ? 601  FAD B P     1 
HETATM 8296 O  O1P   . FAD I 2 .   ? -22.251 -22.137 46.745  1.00 20.75 ? 601  FAD B O1P   1 
HETATM 8297 O  O2P   . FAD I 2 .   ? -22.854 -24.142 48.239  1.00 23.38 ? 601  FAD B O2P   1 
HETATM 8298 O  O3P   . FAD I 2 .   ? -23.521 -24.058 45.783  1.00 21.97 ? 601  FAD B O3P   1 
HETATM 8299 C  C1    . PEG J 4 .   ? -17.324 -39.268 26.232  1.00 43.84 ? 602  PEG B C1    1 
HETATM 8300 O  O1    . PEG J 4 .   ? -16.058 -38.911 25.859  1.00 42.78 ? 602  PEG B O1    1 
HETATM 8301 C  C2    . PEG J 4 .   ? -18.309 -38.832 25.221  1.00 43.14 ? 602  PEG B C2    1 
HETATM 8302 O  O2    . PEG J 4 .   ? -19.557 -38.574 25.841  1.00 43.40 ? 602  PEG B O2    1 
HETATM 8303 C  C3    . PEG J 4 .   ? -20.119 -39.666 26.572  1.00 43.51 ? 602  PEG B C3    1 
HETATM 8304 C  C4    . PEG J 4 .   ? -20.351 -39.186 27.976  1.00 43.10 ? 602  PEG B C4    1 
HETATM 8305 O  O4    . PEG J 4 .   ? -20.593 -40.230 28.877  1.00 44.46 ? 602  PEG B O4    1 
HETATM 8306 C  C1    . PEG K 4 .   ? -12.130 -3.887  34.614  1.00 56.78 ? 603  PEG B C1    1 
HETATM 8307 O  O1    . PEG K 4 .   ? -12.021 -3.261  33.353  1.00 57.61 ? 603  PEG B O1    1 
HETATM 8308 C  C2    . PEG K 4 .   ? -12.625 -5.288  34.485  1.00 55.66 ? 603  PEG B C2    1 
HETATM 8309 O  O2    . PEG K 4 .   ? -13.971 -5.375  34.942  1.00 56.29 ? 603  PEG B O2    1 
HETATM 8310 C  C3    . PEG K 4 .   ? -14.555 -6.657  34.731  1.00 53.10 ? 603  PEG B C3    1 
HETATM 8311 C  C4    . PEG K 4 .   ? -15.989 -6.522  34.367  1.00 53.89 ? 603  PEG B C4    1 
HETATM 8312 O  O4    . PEG K 4 .   ? -16.197 -6.660  32.983  1.00 61.63 ? 603  PEG B O4    1 
HETATM 8313 C  C1    . PEG L 4 .   ? -16.498 -21.832 56.153  1.00 40.60 ? 604  PEG B C1    1 
HETATM 8314 O  O1    . PEG L 4 .   ? -15.705 -22.500 55.258  1.00 37.95 ? 604  PEG B O1    1 
HETATM 8315 C  C2    . PEG L 4 .   ? -17.933 -22.071 55.891  1.00 45.41 ? 604  PEG B C2    1 
HETATM 8316 O  O2    . PEG L 4 .   ? -18.638 -22.301 57.112  1.00 55.19 ? 604  PEG B O2    1 
HETATM 8317 C  C3    . PEG L 4 .   ? -18.943 -23.681 57.328  1.00 56.78 ? 604  PEG B C3    1 
HETATM 8318 C  C4    . PEG L 4 .   ? -20.349 -23.816 57.783  1.00 61.51 ? 604  PEG B C4    1 
HETATM 8319 O  O4    . PEG L 4 .   ? -21.066 -24.768 57.035  1.00 64.17 ? 604  PEG B O4    1 
HETATM 8320 C  C1    . PEG M 4 .   ? -15.511 -4.166  28.120  1.00 47.78 ? 605  PEG B C1    1 
HETATM 8321 O  O1    . PEG M 4 .   ? -15.074 -5.464  28.495  1.00 49.36 ? 605  PEG B O1    1 
HETATM 8322 C  C2    . PEG M 4 .   ? -14.885 -3.079  28.934  1.00 47.63 ? 605  PEG B C2    1 
HETATM 8323 O  O2    . PEG M 4 .   ? -15.831 -2.027  29.127  1.00 53.94 ? 605  PEG B O2    1 
HETATM 8324 C  C3    . PEG M 4 .   ? -15.523 -1.142  30.208  1.00 56.36 ? 605  PEG B C3    1 
HETATM 8325 C  C4    . PEG M 4 .   ? -16.370 -1.436  31.422  1.00 55.47 ? 605  PEG B C4    1 
HETATM 8326 O  O4    . PEG M 4 .   ? -17.375 -2.425  31.194  1.00 58.80 ? 605  PEG B O4    1 
HETATM 8327 C  C1    . PEG N 4 .   ? -40.073 -30.222 26.815  1.00 52.36 ? 606  PEG B C1    1 
HETATM 8328 O  O1    . PEG N 4 .   ? -38.808 -30.533 27.308  1.00 51.16 ? 606  PEG B O1    1 
HETATM 8329 C  C2    . PEG N 4 .   ? -40.195 -30.591 25.395  1.00 55.12 ? 606  PEG B C2    1 
HETATM 8330 O  O2    . PEG N 4 .   ? -40.954 -31.785 25.288  1.00 57.92 ? 606  PEG B O2    1 
HETATM 8331 C  C3    . PEG N 4 .   ? -40.192 -32.969 25.515  1.00 58.72 ? 606  PEG B C3    1 
HETATM 8332 C  C4    . PEG N 4 .   ? -39.731 -33.558 24.211  1.00 66.50 ? 606  PEG B C4    1 
HETATM 8333 O  O4    . PEG N 4 .   ? -40.754 -33.616 23.219  1.00 72.73 ? 606  PEG B O4    1 
HETATM 8334 CL CL    . CL  O 3 .   ? -6.518  0.022   39.527  1.00 30.01 ? 607  CL  B CL    1 
HETATM 8335 CL CL    . CL  P 3 .   ? -4.402  -29.704 38.846  1.00 40.00 ? 608  CL  B CL    1 
HETATM 8336 CL CL    . CL  Q 3 .   ? -32.789 -37.914 33.985  1.00 17.16 ? 609  CL  B CL    1 
HETATM 8337 O  O     . HOH R 5 .   ? -16.320 -36.417 15.678  1.00 48.88 ? 701  HOH A O     1 
HETATM 8338 O  O     . HOH R 5 .   ? 10.069  -11.100 2.569   1.00 39.20 ? 702  HOH A O     1 
HETATM 8339 O  O     . HOH R 5 .   ? -10.376 -1.065  38.635  1.00 43.03 ? 703  HOH A O     1 
HETATM 8340 O  O     . HOH R 5 .   ? 3.559   11.584  26.127  1.00 36.20 ? 704  HOH A O     1 
HETATM 8341 O  O     . HOH R 5 .   ? -15.396 3.676   32.910  1.00 40.21 ? 705  HOH A O     1 
HETATM 8342 O  O     . HOH R 5 .   ? -5.956  -10.735 -0.643  1.00 28.17 ? 706  HOH A O     1 
HETATM 8343 O  O     . HOH R 5 .   ? -2.874  -26.862 -5.280  1.00 30.81 ? 707  HOH A O     1 
HETATM 8344 O  O     . HOH R 5 .   ? 16.236  4.202   19.148  1.00 38.87 ? 708  HOH A O     1 
HETATM 8345 O  O     . HOH R 5 .   ? -13.635 -8.490  7.882   1.00 35.08 ? 709  HOH A O     1 
HETATM 8346 O  O     . HOH R 5 .   ? 10.170  5.691   16.779  1.00 23.18 ? 710  HOH A O     1 
HETATM 8347 O  O     . HOH R 5 .   ? -32.281 -38.756 -7.621  1.00 35.62 ? 711  HOH A O     1 
HETATM 8348 O  O     . HOH R 5 .   ? -25.673 4.028   24.184  1.00 27.66 ? 712  HOH A O     1 
HETATM 8349 O  O     . HOH R 5 .   ? -13.899 -26.478 -6.627  1.00 21.91 ? 713  HOH A O     1 
HETATM 8350 O  O     . HOH R 5 .   ? -4.824  -13.751 17.485  1.00 28.23 ? 714  HOH A O     1 
HETATM 8351 O  O     . HOH R 5 .   ? -17.859 -9.449  14.984  1.00 18.53 ? 715  HOH A O     1 
HETATM 8352 O  O     . HOH R 5 .   ? 4.475   -12.730 -1.546  1.00 34.64 ? 716  HOH A O     1 
HETATM 8353 O  O     . HOH R 5 .   ? -30.330 -13.925 25.636  1.00 15.56 ? 717  HOH A O     1 
HETATM 8354 O  O     . HOH R 5 .   ? -34.626 -4.565  24.475  1.00 40.04 ? 718  HOH A O     1 
HETATM 8355 O  O     . HOH R 5 .   ? -24.147 -15.415 24.678  1.00 22.65 ? 719  HOH A O     1 
HETATM 8356 O  O     . HOH R 5 .   ? -32.350 -14.681 9.634   1.00 24.89 ? 720  HOH A O     1 
HETATM 8357 O  O     . HOH R 5 .   ? -33.437 -17.335 -2.904  1.00 25.46 ? 721  HOH A O     1 
HETATM 8358 O  O     . HOH R 5 .   ? -28.755 -23.400 -10.811 1.00 39.59 ? 722  HOH A O     1 
HETATM 8359 O  O     . HOH R 5 .   ? -6.746  -22.352 -3.655  1.00 25.62 ? 723  HOH A O     1 
HETATM 8360 O  O     . HOH R 5 .   ? -13.878 -13.652 19.637  1.00 15.31 ? 724  HOH A O     1 
HETATM 8361 O  O     . HOH R 5 .   ? -13.515 -21.690 4.900   1.00 17.25 ? 725  HOH A O     1 
HETATM 8362 O  O     . HOH R 5 .   ? -13.735 -36.738 -2.636  1.00 38.92 ? 726  HOH A O     1 
HETATM 8363 O  O     . HOH R 5 .   ? 14.298  5.766   28.430  1.00 36.26 ? 727  HOH A O     1 
HETATM 8364 O  O     . HOH R 5 .   ? -6.024  -2.915  20.244  1.00 35.77 ? 728  HOH A O     1 
HETATM 8365 O  O     . HOH R 5 .   ? -7.831  -2.076  6.474   1.00 22.10 ? 729  HOH A O     1 
HETATM 8366 O  O     . HOH R 5 .   ? 13.783  0.767   23.184  1.00 22.73 ? 730  HOH A O     1 
HETATM 8367 O  O     . HOH R 5 .   ? -16.023 5.259   15.192  1.00 26.44 ? 731  HOH A O     1 
HETATM 8368 O  O     . HOH R 5 .   ? 17.067  -18.447 10.375  1.00 26.86 ? 732  HOH A O     1 
HETATM 8369 O  O     . HOH R 5 .   ? -10.701 -20.387 19.952  1.00 15.85 ? 733  HOH A O     1 
HETATM 8370 O  O     . HOH R 5 .   ? -10.813 -37.763 18.519  1.00 30.19 ? 734  HOH A O     1 
HETATM 8371 O  O     . HOH R 5 .   ? -23.264 -10.223 10.136  1.00 17.66 ? 735  HOH A O     1 
HETATM 8372 O  O     . HOH R 5 .   ? 1.771   -17.116 22.470  1.00 15.42 ? 736  HOH A O     1 
HETATM 8373 O  O     . HOH R 5 .   ? -0.677  -8.365  -2.945  1.00 37.44 ? 737  HOH A O     1 
HETATM 8374 O  O     . HOH R 5 .   ? -7.775  -34.200 19.829  1.00 18.89 ? 738  HOH A O     1 
HETATM 8375 O  O     . HOH R 5 .   ? 5.093   -31.203 19.514  1.00 38.34 ? 739  HOH A O     1 
HETATM 8376 O  O     . HOH R 5 .   ? -19.824 -24.313 10.725  1.00 28.69 ? 740  HOH A O     1 
HETATM 8377 O  O     . HOH R 5 .   ? -12.553 -23.425 -9.249  1.00 34.68 ? 741  HOH A O     1 
HETATM 8378 O  O     . HOH R 5 .   ? 5.526   -6.110  35.748  1.00 30.75 ? 742  HOH A O     1 
HETATM 8379 O  O     . HOH R 5 .   ? -9.212  -14.341 16.135  1.00 25.52 ? 743  HOH A O     1 
HETATM 8380 O  O     . HOH R 5 .   ? -3.540  -36.306 19.707  1.00 27.92 ? 744  HOH A O     1 
HETATM 8381 O  O     . HOH R 5 .   ? 11.187  -14.094 -1.220  1.00 36.54 ? 745  HOH A O     1 
HETATM 8382 O  O     . HOH R 5 .   ? -23.873 -39.215 20.532  1.00 26.98 ? 746  HOH A O     1 
HETATM 8383 O  O     . HOH R 5 .   ? -2.499  -6.673  -1.482  1.00 26.34 ? 747  HOH A O     1 
HETATM 8384 O  O     . HOH R 5 .   ? -9.059  -6.814  36.315  1.00 21.11 ? 748  HOH A O     1 
HETATM 8385 O  O     . HOH R 5 .   ? -26.111 -7.632  30.404  1.00 18.83 ? 749  HOH A O     1 
HETATM 8386 O  O     . HOH R 5 .   ? 10.482  -18.143 0.911   1.00 38.30 ? 750  HOH A O     1 
HETATM 8387 O  O     . HOH R 5 .   ? 9.692   -26.473 21.307  1.00 21.43 ? 751  HOH A O     1 
HETATM 8388 O  O     . HOH R 5 .   ? 1.533   -30.004 24.279  1.00 18.31 ? 752  HOH A O     1 
HETATM 8389 O  O     . HOH R 5 .   ? -4.819  1.878   26.487  1.00 20.84 ? 753  HOH A O     1 
HETATM 8390 O  O     . HOH R 5 .   ? 11.522  -29.229 14.990  1.00 36.99 ? 754  HOH A O     1 
HETATM 8391 O  O     . HOH R 5 .   ? -18.372 4.103   26.059  1.00 25.66 ? 755  HOH A O     1 
HETATM 8392 O  O     . HOH R 5 .   ? -37.773 -15.072 20.379  1.00 24.77 ? 756  HOH A O     1 
HETATM 8393 O  O     . HOH R 5 .   ? 12.224  -16.298 -0.337  1.00 42.50 ? 757  HOH A O     1 
HETATM 8394 O  O     . HOH R 5 .   ? -15.522 -19.027 5.564   1.00 17.51 ? 758  HOH A O     1 
HETATM 8395 O  O     . HOH R 5 .   ? 11.182  -7.133  16.080  1.00 26.32 ? 759  HOH A O     1 
HETATM 8396 O  O     . HOH R 5 .   ? 9.460   -8.223  35.862  1.00 43.75 ? 760  HOH A O     1 
HETATM 8397 O  O     . HOH R 5 .   ? -27.018 -15.848 0.559   1.00 17.26 ? 761  HOH A O     1 
HETATM 8398 O  O     . HOH R 5 .   ? -10.061 -24.260 -2.492  1.00 21.66 ? 762  HOH A O     1 
HETATM 8399 O  O     . HOH R 5 .   ? -20.976 -15.338 23.816  1.00 17.78 ? 763  HOH A O     1 
HETATM 8400 O  O     . HOH R 5 .   ? -11.560 -2.534  15.872  1.00 15.99 ? 764  HOH A O     1 
HETATM 8401 O  O     . HOH R 5 .   ? -26.859 -15.685 24.693  1.00 18.97 ? 765  HOH A O     1 
HETATM 8402 O  O     . HOH R 5 .   ? -0.964  -32.319 15.992  1.00 27.90 ? 766  HOH A O     1 
HETATM 8403 O  O     . HOH R 5 .   ? -1.098  -22.492 25.667  1.00 21.85 ? 767  HOH A O     1 
HETATM 8404 O  O     . HOH R 5 .   ? -19.200 -44.306 6.180   1.00 30.74 ? 768  HOH A O     1 
HETATM 8405 O  O     . HOH R 5 .   ? 6.768   -14.169 9.505   1.00 24.11 ? 769  HOH A O     1 
HETATM 8406 O  O     . HOH R 5 .   ? -6.084  8.399   11.851  1.00 32.89 ? 770  HOH A O     1 
HETATM 8407 O  O     . HOH R 5 .   ? 5.577   -19.197 31.800  1.00 35.54 ? 771  HOH A O     1 
HETATM 8408 O  O     . HOH R 5 .   ? 11.982  -6.596  32.853  1.00 37.75 ? 772  HOH A O     1 
HETATM 8409 O  O     . HOH R 5 .   ? 14.049  -6.925  -2.838  1.00 42.17 ? 773  HOH A O     1 
HETATM 8410 O  O     . HOH R 5 .   ? -30.586 -22.806 28.146  1.00 19.77 ? 774  HOH A O     1 
HETATM 8411 O  O     . HOH R 5 .   ? -9.223  -4.357  37.616  1.00 28.87 ? 775  HOH A O     1 
HETATM 8412 O  O     . HOH R 5 .   ? -28.212 9.962   18.868  1.00 45.54 ? 776  HOH A O     1 
HETATM 8413 O  O     . HOH R 5 .   ? -7.160  -5.236  29.903  1.00 33.60 ? 777  HOH A O     1 
HETATM 8414 O  O     . HOH R 5 .   ? -10.268 -31.134 9.766   1.00 19.05 ? 778  HOH A O     1 
HETATM 8415 O  O     . HOH R 5 .   ? -34.068 -29.039 -13.663 1.00 36.02 ? 779  HOH A O     1 
HETATM 8416 O  O     . HOH R 5 .   ? -9.010  -34.145 22.418  1.00 22.95 ? 780  HOH A O     1 
HETATM 8417 O  O     . HOH R 5 .   ? 3.692   -17.862 16.821  1.00 16.28 ? 781  HOH A O     1 
HETATM 8418 O  O     . HOH R 5 .   ? -27.538 -20.346 30.352  1.00 19.91 ? 782  HOH A O     1 
HETATM 8419 O  O     . HOH R 5 .   ? 1.942   -1.480  15.773  1.00 26.81 ? 783  HOH A O     1 
HETATM 8420 O  O     . HOH R 5 .   ? 1.877   -27.296 0.321   1.00 38.16 ? 784  HOH A O     1 
HETATM 8421 O  O     . HOH R 5 .   ? 14.217  -6.592  27.486  1.00 24.43 ? 785  HOH A O     1 
HETATM 8422 O  O     . HOH R 5 .   ? -24.426 6.227   23.318  1.00 23.48 ? 786  HOH A O     1 
HETATM 8423 O  O     . HOH R 5 .   ? 5.426   9.404   10.934  1.00 36.85 ? 787  HOH A O     1 
HETATM 8424 O  O     . HOH R 5 .   ? -18.522 -40.526 -4.776  1.00 38.21 ? 788  HOH A O     1 
HETATM 8425 O  O     . HOH R 5 .   ? 16.608  -0.730  24.942  1.00 27.73 ? 789  HOH A O     1 
HETATM 8426 O  O     . HOH R 5 .   ? -25.817 -0.508  5.740   1.00 30.53 ? 790  HOH A O     1 
HETATM 8427 O  O     . HOH R 5 .   ? -37.071 -11.232 29.898  1.00 25.86 ? 791  HOH A O     1 
HETATM 8428 O  O     . HOH R 5 .   ? -4.222  -17.740 9.548   1.00 26.10 ? 792  HOH A O     1 
HETATM 8429 O  O     . HOH R 5 .   ? -36.772 -12.849 20.879  1.00 38.54 ? 793  HOH A O     1 
HETATM 8430 O  O     . HOH R 5 .   ? -13.712 -35.622 -0.205  1.00 30.46 ? 794  HOH A O     1 
HETATM 8431 O  O     . HOH R 5 .   ? 4.699   -10.066 -0.799  1.00 28.91 ? 795  HOH A O     1 
HETATM 8432 O  O     . HOH R 5 .   ? -1.187  12.147  31.813  1.00 35.46 ? 796  HOH A O     1 
HETATM 8433 O  O     . HOH R 5 .   ? 9.422   -22.511 16.197  1.00 22.42 ? 797  HOH A O     1 
HETATM 8434 O  O     . HOH R 5 .   ? 7.511   -29.955 8.445   1.00 25.17 ? 798  HOH A O     1 
HETATM 8435 O  O     . HOH R 5 .   ? 5.436   -29.304 2.662   1.00 40.75 ? 799  HOH A O     1 
HETATM 8436 O  O     . HOH R 5 .   ? 12.807  -17.367 27.234  1.00 36.35 ? 800  HOH A O     1 
HETATM 8437 O  O     . HOH R 5 .   ? -11.678 -39.906 18.582  1.00 31.06 ? 801  HOH A O     1 
HETATM 8438 O  O     . HOH R 5 .   ? 5.031   -16.878 -9.341  1.00 42.05 ? 802  HOH A O     1 
HETATM 8439 O  O     . HOH R 5 .   ? -19.699 -0.285  27.629  1.00 20.58 ? 803  HOH A O     1 
HETATM 8440 O  O     . HOH R 5 .   ? -36.631 -30.086 9.864   1.00 29.62 ? 804  HOH A O     1 
HETATM 8441 O  O     . HOH R 5 .   ? -22.137 -37.251 12.962  1.00 23.55 ? 805  HOH A O     1 
HETATM 8442 O  O     . HOH R 5 .   ? 9.383   -5.782  -2.484  1.00 30.78 ? 806  HOH A O     1 
HETATM 8443 O  O     . HOH R 5 .   ? -3.860  -18.719 3.816   1.00 23.82 ? 807  HOH A O     1 
HETATM 8444 O  O     . HOH R 5 .   ? -18.622 -1.830  19.747  1.00 17.12 ? 808  HOH A O     1 
HETATM 8445 O  O     . HOH R 5 .   ? -28.197 -30.597 -10.862 1.00 30.99 ? 809  HOH A O     1 
HETATM 8446 O  O     . HOH R 5 .   ? -6.185  2.661   28.340  1.00 27.87 ? 810  HOH A O     1 
HETATM 8447 O  O     . HOH R 5 .   ? -1.698  -36.427 25.654  1.00 33.43 ? 811  HOH A O     1 
HETATM 8448 O  O     . HOH R 5 .   ? -20.051 -4.446  2.498   1.00 26.71 ? 812  HOH A O     1 
HETATM 8449 O  O     . HOH R 5 .   ? -26.317 -41.169 7.883   1.00 45.28 ? 813  HOH A O     1 
HETATM 8450 O  O     . HOH R 5 .   ? 5.250   -21.105 29.676  1.00 33.06 ? 814  HOH A O     1 
HETATM 8451 O  O     . HOH R 5 .   ? -6.546  -24.140 0.756   1.00 31.32 ? 815  HOH A O     1 
HETATM 8452 O  O     . HOH R 5 .   ? -9.099  -4.773  21.386  1.00 15.54 ? 816  HOH A O     1 
HETATM 8453 O  O     . HOH R 5 .   ? -27.695 -42.329 12.243  1.00 46.26 ? 817  HOH A O     1 
HETATM 8454 O  O     . HOH R 5 .   ? -40.278 -10.971 21.702  1.00 40.71 ? 818  HOH A O     1 
HETATM 8455 O  O     . HOH R 5 .   ? -18.733 -10.891 27.919  1.00 38.28 ? 819  HOH A O     1 
HETATM 8456 O  O     . HOH R 5 .   ? -1.230  -32.148 0.501   1.00 35.06 ? 820  HOH A O     1 
HETATM 8457 O  O     . HOH R 5 .   ? 0.240   -1.895  -2.054  1.00 33.87 ? 821  HOH A O     1 
HETATM 8458 O  O     . HOH R 5 .   ? -15.765 -29.935 4.749   1.00 19.48 ? 822  HOH A O     1 
HETATM 8459 O  O     . HOH R 5 .   ? -44.099 -8.618  25.531  1.00 37.13 ? 823  HOH A O     1 
HETATM 8460 O  O     . HOH R 5 .   ? 0.158   -31.133 22.500  1.00 18.50 ? 824  HOH A O     1 
HETATM 8461 O  O     . HOH R 5 .   ? -6.697  -18.338 3.219   1.00 19.24 ? 825  HOH A O     1 
HETATM 8462 O  O     . HOH R 5 .   ? -16.206 -0.492  19.719  1.00 14.27 ? 826  HOH A O     1 
HETATM 8463 O  O     . HOH R 5 .   ? -0.598  -30.791 8.961   1.00 33.36 ? 827  HOH A O     1 
HETATM 8464 O  O     . HOH R 5 .   ? -11.890 -24.399 13.379  1.00 18.87 ? 828  HOH A O     1 
HETATM 8465 O  O     . HOH R 5 .   ? -8.422  -33.648 25.704  1.00 14.02 ? 829  HOH A O     1 
HETATM 8466 O  O     . HOH R 5 .   ? -7.934  -30.216 8.490   1.00 18.16 ? 830  HOH A O     1 
HETATM 8467 O  O     . HOH R 5 .   ? -16.869 -40.011 20.996  1.00 33.67 ? 831  HOH A O     1 
HETATM 8468 O  O     . HOH R 5 .   ? -27.574 -20.596 25.846  1.00 24.30 ? 832  HOH A O     1 
HETATM 8469 O  O     . HOH R 5 .   ? 5.887   6.690   9.196   1.00 46.14 ? 833  HOH A O     1 
HETATM 8470 O  O     . HOH R 5 .   ? -3.064  -21.382 12.765  1.00 23.53 ? 834  HOH A O     1 
HETATM 8471 O  O     . HOH R 5 .   ? -32.916 -7.498  23.529  1.00 19.64 ? 835  HOH A O     1 
HETATM 8472 O  O     . HOH R 5 .   ? -24.836 -41.407 -3.021  1.00 36.93 ? 836  HOH A O     1 
HETATM 8473 O  O     . HOH R 5 .   ? 0.224   -30.577 -1.136  1.00 37.36 ? 837  HOH A O     1 
HETATM 8474 O  O     . HOH R 5 .   ? 11.325  8.181   28.463  1.00 32.54 ? 838  HOH A O     1 
HETATM 8475 O  O     . HOH R 5 .   ? -3.763  -2.448  19.518  1.00 32.81 ? 839  HOH A O     1 
HETATM 8476 O  O     . HOH R 5 .   ? -35.821 -21.365 21.506  1.00 21.83 ? 840  HOH A O     1 
HETATM 8477 O  O     . HOH R 5 .   ? 6.691   -22.438 16.974  1.00 23.27 ? 841  HOH A O     1 
HETATM 8478 O  O     . HOH R 5 .   ? -17.984 -24.303 8.557   1.00 38.10 ? 842  HOH A O     1 
HETATM 8479 O  O     . HOH R 5 .   ? -34.649 -34.401 5.362   1.00 46.16 ? 843  HOH A O     1 
HETATM 8480 O  O     . HOH R 5 .   ? 5.254   -29.227 27.261  1.00 46.08 ? 844  HOH A O     1 
HETATM 8481 O  O     . HOH R 5 .   ? -30.101 -20.321 27.148  1.00 21.65 ? 845  HOH A O     1 
HETATM 8482 O  O     . HOH R 5 .   ? 11.969  -11.463 32.121  1.00 41.96 ? 846  HOH A O     1 
HETATM 8483 O  O     . HOH R 5 .   ? 12.078  3.507   19.693  1.00 27.67 ? 847  HOH A O     1 
HETATM 8484 O  O     . HOH R 5 .   ? -27.999 -35.009 10.431  1.00 18.75 ? 848  HOH A O     1 
HETATM 8485 O  O     . HOH R 5 .   ? 9.793   2.922   33.365  1.00 35.56 ? 849  HOH A O     1 
HETATM 8486 O  O     . HOH R 5 .   ? -10.518 -13.924 23.043  1.00 36.33 ? 850  HOH A O     1 
HETATM 8487 O  O     . HOH R 5 .   ? -22.924 8.235   14.487  1.00 42.83 ? 851  HOH A O     1 
HETATM 8488 O  O     . HOH R 5 .   ? -19.037 -4.449  19.344  1.00 15.23 ? 852  HOH A O     1 
HETATM 8489 O  O     . HOH R 5 .   ? -22.054 -25.654 10.878  1.00 22.85 ? 853  HOH A O     1 
HETATM 8490 O  O     . HOH R 5 .   ? -12.987 -18.133 -0.737  1.00 22.99 ? 854  HOH A O     1 
HETATM 8491 O  O     . HOH R 5 .   ? 4.659   -19.008 19.147  1.00 22.47 ? 855  HOH A O     1 
HETATM 8492 O  O     . HOH R 5 .   ? -10.863 -10.889 4.859   1.00 15.49 ? 856  HOH A O     1 
HETATM 8493 O  O     . HOH R 5 .   ? 11.275  12.465  13.927  1.00 43.96 ? 857  HOH A O     1 
HETATM 8494 O  O     . HOH R 5 .   ? -38.501 -8.302  28.370  1.00 29.25 ? 858  HOH A O     1 
HETATM 8495 O  O     . HOH R 5 .   ? -10.050 -31.869 0.990   1.00 28.22 ? 859  HOH A O     1 
HETATM 8496 O  O     . HOH R 5 .   ? -37.168 -17.687 12.585  1.00 33.48 ? 860  HOH A O     1 
HETATM 8497 O  O     . HOH R 5 .   ? -6.217  -26.711 -2.213  1.00 28.86 ? 861  HOH A O     1 
HETATM 8498 O  O     . HOH R 5 .   ? 9.720   -13.197 32.298  1.00 23.88 ? 862  HOH A O     1 
HETATM 8499 O  O     . HOH R 5 .   ? 0.624   -4.861  8.839   1.00 43.80 ? 863  HOH A O     1 
HETATM 8500 O  O     . HOH R 5 .   ? -17.618 -6.859  16.496  1.00 14.31 ? 864  HOH A O     1 
HETATM 8501 O  O     . HOH R 5 .   ? -13.171 -35.892 14.925  1.00 30.22 ? 865  HOH A O     1 
HETATM 8502 O  O     . HOH R 5 .   ? -15.564 -15.923 -0.652  1.00 32.23 ? 866  HOH A O     1 
HETATM 8503 O  O     . HOH R 5 .   ? -17.348 2.425   14.850  1.00 18.65 ? 867  HOH A O     1 
HETATM 8504 O  O     . HOH R 5 .   ? -22.410 7.543   24.468  1.00 35.54 ? 868  HOH A O     1 
HETATM 8505 O  O     . HOH R 5 .   ? 7.587   -13.007 -4.358  1.00 45.63 ? 869  HOH A O     1 
HETATM 8506 O  O     . HOH R 5 .   ? -16.231 6.864   13.288  1.00 31.30 ? 870  HOH A O     1 
HETATM 8507 O  O     . HOH R 5 .   ? -34.371 -14.988 7.348   1.00 28.92 ? 871  HOH A O     1 
HETATM 8508 O  O     . HOH R 5 .   ? 0.978   -14.745 -4.767  1.00 35.49 ? 872  HOH A O     1 
HETATM 8509 O  O     . HOH R 5 .   ? 8.172   -12.458 3.679   1.00 36.93 ? 873  HOH A O     1 
HETATM 8510 O  O     . HOH R 5 .   ? -4.895  -30.780 9.593   1.00 16.56 ? 874  HOH A O     1 
HETATM 8511 O  O     . HOH R 5 .   ? -29.696 -9.622  -0.303  1.00 36.61 ? 875  HOH A O     1 
HETATM 8512 O  O     . HOH R 5 .   ? -15.064 -37.325 1.005   1.00 39.85 ? 876  HOH A O     1 
HETATM 8513 O  O     . HOH R 5 .   ? -11.023 -21.331 11.499  1.00 21.91 ? 877  HOH A O     1 
HETATM 8514 O  O     . HOH R 5 .   ? 12.792  -10.970 8.251   1.00 33.01 ? 878  HOH A O     1 
HETATM 8515 O  O     . HOH R 5 .   ? -10.264 -40.747 26.605  1.00 28.40 ? 879  HOH A O     1 
HETATM 8516 O  O     . HOH R 5 .   ? -19.049 -4.487  16.582  1.00 16.84 ? 880  HOH A O     1 
HETATM 8517 O  O     . HOH R 5 .   ? 9.856   -7.734  11.491  1.00 29.04 ? 881  HOH A O     1 
HETATM 8518 O  O     . HOH R 5 .   ? 0.182   -30.121 6.300   1.00 32.84 ? 882  HOH A O     1 
HETATM 8519 O  O     . HOH R 5 .   ? -1.977  -26.047 18.869  1.00 12.93 ? 883  HOH A O     1 
HETATM 8520 O  O     . HOH R 5 .   ? -13.621 -14.701 26.232  1.00 29.82 ? 884  HOH A O     1 
HETATM 8521 O  O     . HOH R 5 .   ? -1.930  -13.641 9.330   1.00 28.09 ? 885  HOH A O     1 
HETATM 8522 O  O     . HOH R 5 .   ? 6.200   -12.863 6.070   1.00 27.93 ? 886  HOH A O     1 
HETATM 8523 O  O     . HOH R 5 .   ? -15.180 3.266   5.856   1.00 37.54 ? 887  HOH A O     1 
HETATM 8524 O  O     . HOH R 5 .   ? 3.661   -3.323  0.918   1.00 29.38 ? 888  HOH A O     1 
HETATM 8525 O  O     . HOH R 5 .   ? -3.787  -21.128 -7.002  1.00 43.02 ? 889  HOH A O     1 
HETATM 8526 O  O     . HOH R 5 .   ? -12.086 -21.013 7.246   1.00 19.31 ? 890  HOH A O     1 
HETATM 8527 O  O     . HOH R 5 .   ? -6.832  2.042   8.787   1.00 32.26 ? 891  HOH A O     1 
HETATM 8528 O  O     . HOH R 5 .   ? -3.201  -37.117 29.782  1.00 31.34 ? 892  HOH A O     1 
HETATM 8529 O  O     . HOH R 5 .   ? -36.988 -6.118  21.724  1.00 42.09 ? 893  HOH A O     1 
HETATM 8530 O  O     . HOH R 5 .   ? -3.144  -38.568 26.740  1.00 30.32 ? 894  HOH A O     1 
HETATM 8531 O  O     . HOH R 5 .   ? -4.226  -17.954 13.458  1.00 28.96 ? 895  HOH A O     1 
HETATM 8532 O  O     . HOH R 5 .   ? -26.094 -19.928 -11.419 1.00 40.14 ? 896  HOH A O     1 
HETATM 8533 O  O     . HOH R 5 .   ? 18.122  -6.442  20.801  1.00 35.56 ? 897  HOH A O     1 
HETATM 8534 O  O     . HOH R 5 .   ? -19.947 3.299   14.440  1.00 30.43 ? 898  HOH A O     1 
HETATM 8535 O  O     . HOH R 5 .   ? -19.219 -21.903 14.019  1.00 20.80 ? 899  HOH A O     1 
HETATM 8536 O  O     . HOH R 5 .   ? -33.064 -19.762 28.291  1.00 24.24 ? 900  HOH A O     1 
HETATM 8537 O  O     . HOH R 5 .   ? 3.205   2.871   36.255  1.00 40.46 ? 901  HOH A O     1 
HETATM 8538 O  O     . HOH R 5 .   ? -27.950 -38.811 5.027   1.00 33.76 ? 902  HOH A O     1 
HETATM 8539 O  O     . HOH R 5 .   ? 0.782   -25.861 18.969  1.00 18.08 ? 903  HOH A O     1 
HETATM 8540 O  O     . HOH R 5 .   ? -15.056 -27.578 -9.037  1.00 35.38 ? 904  HOH A O     1 
HETATM 8541 O  O     . HOH R 5 .   ? 6.911   -23.202 28.281  1.00 39.79 ? 905  HOH A O     1 
HETATM 8542 O  O     . HOH R 5 .   ? -38.483 -28.200 3.589   1.00 46.57 ? 906  HOH A O     1 
HETATM 8543 O  O     . HOH R 5 .   ? 0.729   -6.667  -6.353  1.00 37.52 ? 907  HOH A O     1 
HETATM 8544 O  O     . HOH R 5 .   ? -34.359 -8.987  19.721  1.00 41.87 ? 908  HOH A O     1 
HETATM 8545 O  O     . HOH R 5 .   ? -13.914 -7.439  24.391  1.00 20.38 ? 909  HOH A O     1 
HETATM 8546 O  O     . HOH R 5 .   ? -27.445 -14.551 -9.326  1.00 38.08 ? 910  HOH A O     1 
HETATM 8547 O  O     . HOH R 5 .   ? -17.430 -6.732  19.139  1.00 14.58 ? 911  HOH A O     1 
HETATM 8548 O  O     . HOH R 5 .   ? -35.625 -9.011  22.292  1.00 37.31 ? 912  HOH A O     1 
HETATM 8549 O  O     . HOH R 5 .   ? 2.716   -8.713  37.555  1.00 30.20 ? 913  HOH A O     1 
HETATM 8550 O  O     . HOH R 5 .   ? -20.876 -15.110 30.651  1.00 43.08 ? 914  HOH A O     1 
HETATM 8551 O  O     . HOH R 5 .   ? -12.426 -11.242 26.734  1.00 35.26 ? 915  HOH A O     1 
HETATM 8552 O  O     . HOH R 5 .   ? -32.211 3.044   19.341  1.00 34.06 ? 916  HOH A O     1 
HETATM 8553 O  O     . HOH R 5 .   ? -13.685 -22.192 9.053   1.00 20.49 ? 917  HOH A O     1 
HETATM 8554 O  O     . HOH R 5 .   ? 10.699  -8.137  -3.207  1.00 42.48 ? 918  HOH A O     1 
HETATM 8555 O  O     . HOH R 5 .   ? -34.574 -14.869 -3.743  1.00 39.74 ? 919  HOH A O     1 
HETATM 8556 O  O     . HOH R 5 .   ? 17.658  -5.180  17.692  1.00 41.35 ? 920  HOH A O     1 
HETATM 8557 O  O     . HOH R 5 .   ? 3.734   12.544  23.311  1.00 42.33 ? 921  HOH A O     1 
HETATM 8558 O  O     . HOH R 5 .   ? -36.494 -28.712 -3.358  1.00 35.74 ? 922  HOH A O     1 
HETATM 8559 O  O     . HOH R 5 .   ? -33.539 -33.365 8.263   1.00 40.20 ? 923  HOH A O     1 
HETATM 8560 O  O     . HOH R 5 .   ? -11.069 -2.461  9.146   1.00 21.27 ? 924  HOH A O     1 
HETATM 8561 O  O     . HOH R 5 .   ? -10.496 -14.743 20.532  1.00 34.49 ? 925  HOH A O     1 
HETATM 8562 O  O     . HOH R 5 .   ? -38.062 -28.599 16.954  1.00 36.86 ? 926  HOH A O     1 
HETATM 8563 O  O     . HOH R 5 .   ? -33.233 -17.811 -9.994  1.00 34.56 ? 927  HOH A O     1 
HETATM 8564 O  O     . HOH R 5 .   ? 16.845  6.638   7.944   1.00 39.78 ? 928  HOH A O     1 
HETATM 8565 O  O     . HOH R 5 .   ? -25.385 -11.150 30.290  1.00 26.81 ? 929  HOH A O     1 
HETATM 8566 O  O     . HOH R 5 .   ? -21.264 -15.764 -5.544  1.00 37.83 ? 930  HOH A O     1 
HETATM 8567 O  O     . HOH R 5 .   ? 14.987  -17.463 24.248  1.00 30.70 ? 931  HOH A O     1 
HETATM 8568 O  O     . HOH R 5 .   ? -32.599 3.532   21.802  1.00 32.37 ? 932  HOH A O     1 
HETATM 8569 O  O     . HOH R 5 .   ? -38.240 -20.287 10.812  1.00 36.52 ? 933  HOH A O     1 
HETATM 8570 O  O     . HOH R 5 .   ? -37.178 -29.601 -0.896  1.00 35.80 ? 934  HOH A O     1 
HETATM 8571 O  O     . HOH R 5 .   ? -17.371 -14.264 -1.080  1.00 33.45 ? 935  HOH A O     1 
HETATM 8572 O  O     . HOH R 5 .   ? 17.938  0.777   3.105   1.00 42.31 ? 936  HOH A O     1 
HETATM 8573 O  O     . HOH R 5 .   ? -39.606 -24.170 11.580  1.00 32.11 ? 937  HOH A O     1 
HETATM 8574 O  O     . HOH R 5 .   ? 14.840  7.466   23.799  1.00 44.41 ? 938  HOH A O     1 
HETATM 8575 O  O     . HOH R 5 .   ? -21.998 -38.917 10.716  1.00 26.93 ? 939  HOH A O     1 
HETATM 8576 O  O     . HOH R 5 .   ? -33.489 -0.695  14.979  1.00 36.21 ? 940  HOH A O     1 
HETATM 8577 O  O     . HOH R 5 .   ? -9.222  -34.460 15.118  1.00 22.91 ? 941  HOH A O     1 
HETATM 8578 O  O     . HOH R 5 .   ? -3.152  -34.817 34.361  1.00 35.37 ? 942  HOH A O     1 
HETATM 8579 O  O     . HOH R 5 .   ? -39.617 -23.676 8.041   1.00 51.69 ? 943  HOH A O     1 
HETATM 8580 O  O     . HOH R 5 .   ? -12.359 -44.079 24.071  1.00 35.44 ? 944  HOH A O     1 
HETATM 8581 O  O     . HOH R 5 .   ? -20.100 -17.838 25.328  1.00 28.38 ? 945  HOH A O     1 
HETATM 8582 O  O     . HOH R 5 .   ? -8.995  -32.697 4.001   1.00 45.43 ? 946  HOH A O     1 
HETATM 8583 O  O     . HOH R 5 .   ? -35.395 -20.587 -10.794 1.00 40.92 ? 947  HOH A O     1 
HETATM 8584 O  O     . HOH R 5 .   ? -9.066  -12.449 31.555  1.00 25.86 ? 948  HOH A O     1 
HETATM 8585 O  O     . HOH R 5 .   ? -37.300 -15.688 10.675  1.00 38.66 ? 949  HOH A O     1 
HETATM 8586 O  O     . HOH R 5 .   ? -12.456 -2.120  37.578  1.00 43.69 ? 950  HOH A O     1 
HETATM 8587 O  O     . HOH R 5 .   ? -10.407 -22.244 13.830  1.00 20.21 ? 951  HOH A O     1 
HETATM 8588 O  O     . HOH R 5 .   ? -29.919 -40.887 11.001  1.00 43.32 ? 952  HOH A O     1 
HETATM 8589 O  O     . HOH R 5 .   ? -21.835 -20.181 26.121  1.00 29.91 ? 953  HOH A O     1 
HETATM 8590 O  O     . HOH R 5 .   ? 2.022   -1.273  0.331   1.00 36.85 ? 954  HOH A O     1 
HETATM 8591 O  O     . HOH R 5 .   ? -3.663  -1.738  16.908  1.00 28.25 ? 955  HOH A O     1 
HETATM 8592 O  O     . HOH R 5 .   ? -15.406 -37.497 -8.410  1.00 43.73 ? 956  HOH A O     1 
HETATM 8593 O  O     . HOH R 5 .   ? -5.548  -12.882 10.186  1.00 28.17 ? 957  HOH A O     1 
HETATM 8594 O  O     . HOH R 5 .   ? -19.869 -38.049 9.282   1.00 34.56 ? 958  HOH A O     1 
HETATM 8595 O  O     . HOH R 5 .   ? -36.861 -29.105 1.839   1.00 34.84 ? 959  HOH A O     1 
HETATM 8596 O  O     . HOH R 5 .   ? -10.600 13.159  22.671  1.00 30.76 ? 960  HOH A O     1 
HETATM 8597 O  O     . HOH R 5 .   ? -23.658 -21.574 -11.843 1.00 31.80 ? 961  HOH A O     1 
HETATM 8598 O  O     . HOH R 5 .   ? -2.287  6.624   7.173   1.00 40.22 ? 962  HOH A O     1 
HETATM 8599 O  O     . HOH R 5 .   ? -34.809 -35.010 13.881  1.00 40.06 ? 963  HOH A O     1 
HETATM 8600 O  O     . HOH R 5 .   ? -1.923  -30.677 7.100   1.00 40.57 ? 964  HOH A O     1 
HETATM 8601 O  O     . HOH R 5 .   ? -3.269  -15.518 12.902  1.00 28.22 ? 965  HOH A O     1 
HETATM 8602 O  O     . HOH R 5 .   ? -14.746 -39.122 4.479   1.00 38.40 ? 966  HOH A O     1 
HETATM 8603 O  O     . HOH R 5 .   ? -30.952 -3.658  6.569   1.00 30.88 ? 967  HOH A O     1 
HETATM 8604 O  O     . HOH R 5 .   ? -31.580 -35.460 14.245  1.00 46.06 ? 968  HOH A O     1 
HETATM 8605 O  O     . HOH R 5 .   ? 16.803  7.170   25.725  1.00 38.83 ? 969  HOH A O     1 
HETATM 8606 O  O     . HOH R 5 .   ? -7.454  -0.068  8.627   1.00 31.76 ? 970  HOH A O     1 
HETATM 8607 O  O     . HOH R 5 .   ? -8.770  -36.139 13.196  1.00 40.02 ? 971  HOH A O     1 
HETATM 8608 O  O     . HOH R 5 .   ? -0.875  1.305   0.787   1.00 51.68 ? 972  HOH A O     1 
HETATM 8609 O  O     . HOH R 5 .   ? -31.196 -34.551 -11.335 1.00 51.54 ? 973  HOH A O     1 
HETATM 8610 O  O     . HOH R 5 .   ? -6.235  12.467  18.525  1.00 25.64 ? 974  HOH A O     1 
HETATM 8611 O  O     . HOH R 5 .   ? -3.987  -14.959 10.367  1.00 21.92 ? 975  HOH A O     1 
HETATM 8612 O  O     . HOH R 5 .   ? -18.261 -45.603 8.608   1.00 47.52 ? 976  HOH A O     1 
HETATM 8613 O  O     . HOH R 5 .   ? 5.191   -19.432 -9.809  1.00 44.09 ? 977  HOH A O     1 
HETATM 8614 O  O     . HOH R 5 .   ? -8.107  -23.469 -6.649  1.00 33.72 ? 978  HOH A O     1 
HETATM 8615 O  O     . HOH R 5 .   ? -30.180 -40.852 5.900   1.00 47.80 ? 979  HOH A O     1 
HETATM 8616 O  O     . HOH R 5 .   ? 4.389   9.347   3.743   1.00 38.00 ? 980  HOH A O     1 
HETATM 8617 O  O     . HOH R 5 .   ? 5.741   -31.171 6.843   1.00 34.65 ? 981  HOH A O     1 
HETATM 8618 O  O     . HOH R 5 .   ? -4.529  -12.691 18.877  1.00 28.64 ? 982  HOH A O     1 
HETATM 8619 O  O     . HOH R 5 .   ? -0.078  -33.341 18.099  1.00 30.41 ? 983  HOH A O     1 
HETATM 8620 O  O     . HOH R 5 .   ? -17.185 7.378   28.445  1.00 20.56 ? 984  HOH A O     1 
HETATM 8621 O  O     . HOH R 5 .   ? -32.746 -35.213 9.632   1.00 30.21 ? 985  HOH A O     1 
HETATM 8622 O  O     . HOH R 5 .   ? -5.512  -11.486 21.507  1.00 39.35 ? 986  HOH A O     1 
HETATM 8623 O  O     . HOH R 5 .   ? -41.026 -14.092 20.296  1.00 22.62 ? 987  HOH A O     1 
HETATM 8624 O  O     . HOH R 5 .   ? -22.124 -44.337 6.210   1.00 49.05 ? 988  HOH A O     1 
HETATM 8625 O  O     . HOH R 5 .   ? -3.129  -34.242 11.752  1.00 36.74 ? 989  HOH A O     1 
HETATM 8626 O  O     . HOH R 5 .   ? -33.136 -9.113  2.373   1.00 50.77 ? 990  HOH A O     1 
HETATM 8627 O  O     . HOH R 5 .   ? -11.538 -39.111 10.844  1.00 40.93 ? 991  HOH A O     1 
HETATM 8628 O  O     . HOH R 5 .   ? -18.022 -41.790 3.920   1.00 38.28 ? 992  HOH A O     1 
HETATM 8629 O  O     . HOH R 5 .   ? -30.425 -34.838 11.668  1.00 28.82 ? 993  HOH A O     1 
HETATM 8630 O  O     . HOH R 5 .   ? 9.162   -30.494 18.559  1.00 36.29 ? 994  HOH A O     1 
HETATM 8631 O  O     . HOH R 5 .   ? -11.229 -38.132 8.525   1.00 47.74 ? 995  HOH A O     1 
HETATM 8632 O  O     . HOH R 5 .   ? -20.076 11.166  24.718  1.00 44.74 ? 996  HOH A O     1 
HETATM 8633 O  O     . HOH R 5 .   ? -6.223  -38.827 33.599  1.00 38.82 ? 997  HOH A O     1 
HETATM 8634 O  O     . HOH R 5 .   ? -3.252  12.118  26.624  1.00 34.85 ? 998  HOH A O     1 
HETATM 8635 O  O     . HOH R 5 .   ? -24.095 -14.655 -3.390  1.00 37.27 ? 999  HOH A O     1 
HETATM 8636 O  O     . HOH R 5 .   ? -3.061  -10.642 9.948   1.00 37.47 ? 1000 HOH A O     1 
HETATM 8637 O  O     . HOH R 5 .   ? -4.280  -13.795 14.741  1.00 29.90 ? 1001 HOH A O     1 
HETATM 8638 O  O     . HOH R 5 .   ? -11.652 -37.805 13.726  1.00 30.58 ? 1002 HOH A O     1 
HETATM 8639 O  O     . HOH R 5 .   ? -7.454  -24.497 -1.793  1.00 29.03 ? 1003 HOH A O     1 
HETATM 8640 O  O     . HOH R 5 .   ? -7.578  -32.195 7.056   1.00 34.66 ? 1004 HOH A O     1 
HETATM 8641 O  O     . HOH R 5 .   ? 12.716  -8.656  31.955  1.00 38.33 ? 1005 HOH A O     1 
HETATM 8642 O  O     . HOH R 5 .   ? -6.751  -25.266 -6.595  1.00 32.69 ? 1006 HOH A O     1 
HETATM 8643 O  O     . HOH R 5 .   ? -4.338  -38.244 32.571  1.00 39.18 ? 1007 HOH A O     1 
HETATM 8644 O  O     . HOH R 5 .   ? -10.708 -34.452 3.674   1.00 28.26 ? 1008 HOH A O     1 
HETATM 8645 O  O     . HOH R 5 .   ? 6.463   -21.206 19.553  1.00 23.08 ? 1009 HOH A O     1 
HETATM 8646 O  O     . HOH R 5 .   ? -30.906 -40.222 -6.137  1.00 38.15 ? 1010 HOH A O     1 
HETATM 8647 O  O     . HOH R 5 .   ? -36.399 -2.721  24.341  1.00 39.60 ? 1011 HOH A O     1 
HETATM 8648 O  O     . HOH R 5 .   ? -13.722 -12.678 28.403  1.00 39.17 ? 1012 HOH A O     1 
HETATM 8649 O  O     . HOH R 5 .   ? -0.891  -35.056 29.673  1.00 44.63 ? 1013 HOH A O     1 
HETATM 8650 O  O     . HOH R 5 .   ? -8.872  -35.377 17.648  1.00 23.52 ? 1014 HOH A O     1 
HETATM 8651 O  O     . HOH R 5 .   ? 9.882   -5.067  35.011  1.00 49.41 ? 1015 HOH A O     1 
HETATM 8652 O  O     . HOH R 5 .   ? 11.921  -7.917  13.696  1.00 32.53 ? 1016 HOH A O     1 
HETATM 8653 O  O     . HOH R 5 .   ? 1.633   -1.605  36.397  1.00 37.02 ? 1017 HOH A O     1 
HETATM 8654 O  O     . HOH R 5 .   ? 15.698  -2.044  30.060  1.00 40.88 ? 1018 HOH A O     1 
HETATM 8655 O  O     . HOH R 5 .   ? -9.628  -39.812 18.825  1.00 36.36 ? 1019 HOH A O     1 
HETATM 8656 O  O     . HOH R 5 .   ? -7.728  10.100  15.948  1.00 20.53 ? 1020 HOH A O     1 
HETATM 8657 O  O     . HOH R 5 .   ? 13.256  -22.263 23.056  1.00 46.14 ? 1021 HOH A O     1 
HETATM 8658 O  O     . HOH R 5 .   ? 14.068  -7.704  10.994  1.00 42.09 ? 1022 HOH A O     1 
HETATM 8659 O  O     . HOH R 5 .   ? -17.257 8.370   32.249  1.00 36.61 ? 1023 HOH A O     1 
HETATM 8660 O  O     . HOH R 5 .   ? -12.146 -12.059 -3.006  1.00 34.63 ? 1024 HOH A O     1 
HETATM 8661 O  O     . HOH S 5 .   ? -33.267 -41.198 36.170  1.00 38.01 ? 701  HOH B O     1 
HETATM 8662 O  O     . HOH S 5 .   ? -19.395 -50.806 38.080  1.00 47.71 ? 702  HOH B O     1 
HETATM 8663 O  O     . HOH S 5 .   ? -14.473 -37.607 26.685  1.00 24.90 ? 703  HOH B O     1 
HETATM 8664 O  O     . HOH S 5 .   ? -38.541 -40.314 42.994  1.00 39.72 ? 704  HOH B O     1 
HETATM 8665 O  O     . HOH S 5 .   ? -28.119 -47.667 34.766  1.00 41.97 ? 705  HOH B O     1 
HETATM 8666 O  O     . HOH S 5 .   ? -11.153 -7.439  49.833  1.00 33.08 ? 706  HOH B O     1 
HETATM 8667 O  O     . HOH S 5 .   ? -36.808 -32.435 30.025  1.00 34.79 ? 707  HOH B O     1 
HETATM 8668 O  O     . HOH S 5 .   ? -3.224  -4.711  42.630  1.00 33.87 ? 708  HOH B O     1 
HETATM 8669 O  O     . HOH S 5 .   ? -47.170 -10.151 39.872  1.00 29.78 ? 709  HOH B O     1 
HETATM 8670 O  O     . HOH S 5 .   ? -17.469 -1.794  56.415  1.00 32.55 ? 710  HOH B O     1 
HETATM 8671 O  O     . HOH S 5 .   ? -37.397 -18.146 40.943  1.00 27.98 ? 711  HOH B O     1 
HETATM 8672 O  O     . HOH S 5 .   ? -34.847 -18.441 45.430  1.00 33.64 ? 712  HOH B O     1 
HETATM 8673 O  O     . HOH S 5 .   ? -29.450 -18.345 34.237  1.00 20.01 ? 713  HOH B O     1 
HETATM 8674 O  O     . HOH S 5 .   ? -11.367 -32.503 52.995  1.00 32.12 ? 714  HOH B O     1 
HETATM 8675 O  O     . HOH S 5 .   ? -18.096 -4.249  32.739  1.00 50.52 ? 715  HOH B O     1 
HETATM 8676 O  O     . HOH S 5 .   ? -36.991 -34.203 23.403  1.00 42.65 ? 716  HOH B O     1 
HETATM 8677 O  O     . HOH S 5 .   ? -31.771 -29.188 56.019  1.00 32.81 ? 717  HOH B O     1 
HETATM 8678 O  O     . HOH S 5 .   ? -47.649 -37.609 47.087  1.00 45.11 ? 718  HOH B O     1 
HETATM 8679 O  O     . HOH S 5 .   ? -27.119 -27.458 46.067  1.00 25.44 ? 719  HOH B O     1 
HETATM 8680 O  O     . HOH S 5 .   ? -13.215 -27.001 22.528  1.00 13.47 ? 720  HOH B O     1 
HETATM 8681 O  O     . HOH S 5 .   ? -44.710 1.029   34.053  1.00 42.95 ? 721  HOH B O     1 
HETATM 8682 O  O     . HOH S 5 .   ? -37.721 -22.720 22.937  1.00 20.26 ? 722  HOH B O     1 
HETATM 8683 O  O     . HOH S 5 .   ? -10.663 -44.184 36.390  1.00 43.60 ? 723  HOH B O     1 
HETATM 8684 O  O     . HOH S 5 .   ? -22.632 -13.149 31.361  1.00 26.05 ? 724  HOH B O     1 
HETATM 8685 O  O     . HOH S 5 .   ? -10.425 -24.843 51.194  1.00 26.08 ? 725  HOH B O     1 
HETATM 8686 O  O     . HOH S 5 .   ? -38.924 -13.760 59.942  1.00 30.77 ? 726  HOH B O     1 
HETATM 8687 O  O     . HOH S 5 .   ? -4.384  -30.123 31.679  1.00 21.78 ? 727  HOH B O     1 
HETATM 8688 O  O     . HOH S 5 .   ? -51.593 -5.392  48.223  1.00 39.66 ? 728  HOH B O     1 
HETATM 8689 O  O     . HOH S 5 .   ? -14.678 -20.376 30.293  1.00 19.57 ? 729  HOH B O     1 
HETATM 8690 O  O     . HOH S 5 .   ? -33.633 9.774   50.745  1.00 22.59 ? 730  HOH B O     1 
HETATM 8691 O  O     . HOH S 5 .   ? -2.467  -7.403  42.603  1.00 27.29 ? 731  HOH B O     1 
HETATM 8692 O  O     . HOH S 5 .   ? -18.048 -17.909 42.632  1.00 16.97 ? 732  HOH B O     1 
HETATM 8693 O  O     . HOH S 5 .   ? -38.911 -28.795 39.460  1.00 20.27 ? 733  HOH B O     1 
HETATM 8694 O  O     . HOH S 5 .   ? -15.846 -44.513 32.971  1.00 31.12 ? 734  HOH B O     1 
HETATM 8695 O  O     . HOH S 5 .   ? -44.711 8.029   60.740  1.00 35.54 ? 735  HOH B O     1 
HETATM 8696 O  O     . HOH S 5 .   ? -8.844  -22.547 29.220  1.00 15.19 ? 736  HOH B O     1 
HETATM 8697 O  O     . HOH S 5 .   ? -27.256 -50.864 51.924  1.00 48.14 ? 737  HOH B O     1 
HETATM 8698 O  O     . HOH S 5 .   ? -21.021 -23.468 26.122  1.00 32.90 ? 738  HOH B O     1 
HETATM 8699 O  O     . HOH S 5 .   ? -37.640 -29.215 53.524  1.00 32.87 ? 739  HOH B O     1 
HETATM 8700 O  O     . HOH S 5 .   ? -29.154 -4.215  65.374  1.00 43.56 ? 740  HOH B O     1 
HETATM 8701 O  O     . HOH S 5 .   ? -27.320 -43.684 60.034  1.00 45.79 ? 741  HOH B O     1 
HETATM 8702 O  O     . HOH S 5 .   ? 0.035   -8.564  37.174  1.00 31.32 ? 742  HOH B O     1 
HETATM 8703 O  O     . HOH S 5 .   ? -39.582 -34.689 44.710  1.00 35.04 ? 743  HOH B O     1 
HETATM 8704 O  O     . HOH S 5 .   ? -9.892  -43.807 47.131  1.00 41.05 ? 744  HOH B O     1 
HETATM 8705 O  O     . HOH S 5 .   ? -39.622 -10.042 40.802  1.00 26.45 ? 745  HOH B O     1 
HETATM 8706 O  O     . HOH S 5 .   ? -44.807 -16.573 57.202  1.00 30.23 ? 746  HOH B O     1 
HETATM 8707 O  O     . HOH S 5 .   ? -29.330 -37.704 21.781  1.00 28.76 ? 747  HOH B O     1 
HETATM 8708 O  O     . HOH S 5 .   ? -41.386 -9.723  49.166  1.00 30.48 ? 748  HOH B O     1 
HETATM 8709 O  O     . HOH S 5 .   ? -29.970 -28.827 52.316  1.00 24.50 ? 749  HOH B O     1 
HETATM 8710 O  O     . HOH S 5 .   ? -2.705  -9.065  40.451  1.00 26.67 ? 750  HOH B O     1 
HETATM 8711 O  O     . HOH S 5 .   ? -13.907 -22.486 22.554  1.00 23.62 ? 751  HOH B O     1 
HETATM 8712 O  O     . HOH S 5 .   ? -35.927 -31.834 51.227  1.00 30.31 ? 752  HOH B O     1 
HETATM 8713 O  O     . HOH S 5 .   ? -38.793 12.520  44.915  1.00 33.38 ? 753  HOH B O     1 
HETATM 8714 O  O     . HOH S 5 .   ? -11.731 -9.987  48.865  1.00 19.63 ? 754  HOH B O     1 
HETATM 8715 O  O     . HOH S 5 .   ? -16.955 -34.624 49.922  1.00 27.97 ? 755  HOH B O     1 
HETATM 8716 O  O     . HOH S 5 .   ? -10.155 -7.447  52.659  1.00 31.86 ? 756  HOH B O     1 
HETATM 8717 O  O     . HOH S 5 .   ? -36.866 -7.734  36.074  1.00 23.35 ? 757  HOH B O     1 
HETATM 8718 O  O     . HOH S 5 .   ? -35.001 -28.188 19.047  1.00 31.28 ? 758  HOH B O     1 
HETATM 8719 O  O     . HOH S 5 .   ? -7.008  -34.750 39.962  1.00 38.76 ? 759  HOH B O     1 
HETATM 8720 O  O     . HOH S 5 .   ? -11.295 -48.486 40.120  1.00 33.36 ? 760  HOH B O     1 
HETATM 8721 O  O     . HOH S 5 .   ? -24.906 -35.698 58.253  1.00 43.28 ? 761  HOH B O     1 
HETATM 8722 O  O     . HOH S 5 .   ? 1.171   -19.589 41.367  1.00 40.46 ? 762  HOH B O     1 
HETATM 8723 O  O     . HOH S 5 .   ? -39.070 4.247   31.157  1.00 29.78 ? 763  HOH B O     1 
HETATM 8724 O  O     . HOH S 5 .   ? -30.895 -39.444 29.283  1.00 25.97 ? 764  HOH B O     1 
HETATM 8725 O  O     . HOH S 5 .   ? -37.525 -30.208 37.381  1.00 25.24 ? 765  HOH B O     1 
HETATM 8726 O  O     . HOH S 5 .   ? -31.600 8.628   54.019  1.00 22.80 ? 766  HOH B O     1 
HETATM 8727 O  O     . HOH S 5 .   ? -10.559 -32.271 41.978  1.00 17.12 ? 767  HOH B O     1 
HETATM 8728 O  O     . HOH S 5 .   ? -40.191 6.421   32.582  1.00 36.39 ? 768  HOH B O     1 
HETATM 8729 O  O     . HOH S 5 .   ? -43.760 -15.253 27.778  1.00 25.13 ? 769  HOH B O     1 
HETATM 8730 O  O     . HOH S 5 .   ? -30.173 -28.596 45.552  1.00 29.46 ? 770  HOH B O     1 
HETATM 8731 O  O     . HOH S 5 .   ? -21.374 -6.671  41.112  1.00 21.33 ? 771  HOH B O     1 
HETATM 8732 O  O     . HOH S 5 .   ? -18.969 -9.543  46.513  1.00 24.74 ? 772  HOH B O     1 
HETATM 8733 O  O     . HOH S 5 .   ? -17.645 -18.901 31.592  1.00 20.58 ? 773  HOH B O     1 
HETATM 8734 O  O     . HOH S 5 .   ? -25.424 -42.430 31.681  1.00 19.35 ? 774  HOH B O     1 
HETATM 8735 O  O     . HOH S 5 .   ? 5.113   -27.072 29.592  1.00 34.33 ? 775  HOH B O     1 
HETATM 8736 O  O     . HOH S 5 .   ? -34.924 -37.610 52.782  1.00 32.47 ? 776  HOH B O     1 
HETATM 8737 O  O     . HOH S 5 .   ? -44.849 -11.114 38.774  1.00 30.34 ? 777  HOH B O     1 
HETATM 8738 O  O     . HOH S 5 .   ? -39.961 -27.549 18.399  1.00 31.11 ? 778  HOH B O     1 
HETATM 8739 O  O     . HOH S 5 .   ? -8.910  -38.752 37.303  1.00 37.01 ? 779  HOH B O     1 
HETATM 8740 O  O     . HOH S 5 .   ? -44.206 -24.714 27.671  1.00 26.99 ? 780  HOH B O     1 
HETATM 8741 O  O     . HOH S 5 .   ? -44.641 -20.674 22.679  1.00 38.77 ? 781  HOH B O     1 
HETATM 8742 O  O     . HOH S 5 .   ? -44.450 4.275   63.419  1.00 28.71 ? 782  HOH B O     1 
HETATM 8743 O  O     . HOH S 5 .   ? -39.702 0.518   48.292  1.00 24.31 ? 783  HOH B O     1 
HETATM 8744 O  O     . HOH S 5 .   ? -27.375 9.132   34.391  1.00 28.96 ? 784  HOH B O     1 
HETATM 8745 O  O     . HOH S 5 .   ? -7.721  -13.554 29.221  1.00 18.80 ? 785  HOH B O     1 
HETATM 8746 O  O     . HOH S 5 .   ? -26.416 -9.996  35.690  1.00 38.01 ? 786  HOH B O     1 
HETATM 8747 O  O     . HOH S 5 .   ? -48.765 -9.464  33.688  1.00 44.88 ? 787  HOH B O     1 
HETATM 8748 O  O     . HOH S 5 .   ? -29.717 -26.902 41.946  1.00 23.50 ? 788  HOH B O     1 
HETATM 8749 O  O     . HOH S 5 .   ? -43.270 2.521   65.007  1.00 19.31 ? 789  HOH B O     1 
HETATM 8750 O  O     . HOH S 5 .   ? -17.783 13.237  35.364  1.00 32.09 ? 790  HOH B O     1 
HETATM 8751 O  O     . HOH S 5 .   ? -29.127 0.425   61.601  1.00 33.94 ? 791  HOH B O     1 
HETATM 8752 O  O     . HOH S 5 .   ? -21.479 -1.420  33.968  1.00 31.73 ? 792  HOH B O     1 
HETATM 8753 O  O     . HOH S 5 .   ? -39.671 -2.831  51.317  1.00 24.89 ? 793  HOH B O     1 
HETATM 8754 O  O     . HOH S 5 .   ? -7.916  -3.835  39.945  1.00 28.24 ? 794  HOH B O     1 
HETATM 8755 O  O     . HOH S 5 .   ? -46.697 -30.391 46.277  1.00 39.71 ? 795  HOH B O     1 
HETATM 8756 O  O     . HOH S 5 .   ? -14.165 -27.146 52.969  1.00 36.32 ? 796  HOH B O     1 
HETATM 8757 O  O     . HOH S 5 .   ? -16.196 -13.735 40.355  1.00 20.30 ? 797  HOH B O     1 
HETATM 8758 O  O     . HOH S 5 .   ? -23.535 -11.578 54.396  1.00 33.72 ? 798  HOH B O     1 
HETATM 8759 O  O     . HOH S 5 .   ? -12.630 -41.045 27.720  1.00 29.97 ? 799  HOH B O     1 
HETATM 8760 O  O     . HOH S 5 .   ? -43.067 6.841   39.081  1.00 43.14 ? 800  HOH B O     1 
HETATM 8761 O  O     . HOH S 5 .   ? -9.108  -47.124 42.478  1.00 28.98 ? 801  HOH B O     1 
HETATM 8762 O  O     . HOH S 5 .   ? -21.530 -10.082 32.691  1.00 40.79 ? 802  HOH B O     1 
HETATM 8763 O  O     . HOH S 5 .   ? -8.148  -21.336 53.743  1.00 37.01 ? 803  HOH B O     1 
HETATM 8764 O  O     . HOH S 5 .   ? -10.309 -15.696 27.704  1.00 21.70 ? 804  HOH B O     1 
HETATM 8765 O  O     . HOH S 5 .   ? -22.893 -15.948 37.101  1.00 14.59 ? 805  HOH B O     1 
HETATM 8766 O  O     . HOH S 5 .   ? -34.383 -23.303 49.966  1.00 23.98 ? 806  HOH B O     1 
HETATM 8767 O  O     . HOH S 5 .   ? -43.545 -17.700 28.560  1.00 24.83 ? 807  HOH B O     1 
HETATM 8768 O  O     . HOH S 5 .   ? -6.578  5.539   46.938  1.00 41.26 ? 808  HOH B O     1 
HETATM 8769 O  O     . HOH S 5 .   ? -44.989 -7.593  64.507  1.00 35.57 ? 809  HOH B O     1 
HETATM 8770 O  O     . HOH S 5 .   ? -13.176 -40.755 50.898  1.00 27.48 ? 810  HOH B O     1 
HETATM 8771 O  O     . HOH S 5 .   ? -12.785 -22.249 29.815  1.00 18.56 ? 811  HOH B O     1 
HETATM 8772 O  O     . HOH S 5 .   ? -35.077 -40.301 54.468  1.00 43.94 ? 812  HOH B O     1 
HETATM 8773 O  O     . HOH S 5 .   ? -32.772 7.257   65.461  1.00 30.01 ? 813  HOH B O     1 
HETATM 8774 O  O     . HOH S 5 .   ? -33.368 -42.326 53.418  1.00 47.42 ? 814  HOH B O     1 
HETATM 8775 O  O     . HOH S 5 .   ? -37.742 -52.638 45.860  1.00 44.93 ? 815  HOH B O     1 
HETATM 8776 O  O     . HOH S 5 .   ? -35.818 10.963  46.769  1.00 29.23 ? 816  HOH B O     1 
HETATM 8777 O  O     . HOH S 5 .   ? -31.780 -24.991 37.559  1.00 25.47 ? 817  HOH B O     1 
HETATM 8778 O  O     . HOH S 5 .   ? -16.033 -13.021 30.678  1.00 32.77 ? 818  HOH B O     1 
HETATM 8779 O  O     . HOH S 5 .   ? -30.527 -1.270  58.373  1.00 33.80 ? 819  HOH B O     1 
HETATM 8780 O  O     . HOH S 5 .   ? -41.681 -15.651 34.267  1.00 27.31 ? 820  HOH B O     1 
HETATM 8781 O  O     . HOH S 5 .   ? -37.987 -25.065 25.347  1.00 22.60 ? 821  HOH B O     1 
HETATM 8782 O  O     . HOH S 5 .   ? -12.391 -10.995 42.163  1.00 17.24 ? 822  HOH B O     1 
HETATM 8783 O  O     . HOH S 5 .   ? -32.789 17.099  45.187  1.00 35.37 ? 823  HOH B O     1 
HETATM 8784 O  O     . HOH S 5 .   ? -12.300 -25.742 24.905  1.00 20.45 ? 824  HOH B O     1 
HETATM 8785 O  O     . HOH S 5 .   ? -14.701 -25.045 26.064  1.00 22.07 ? 825  HOH B O     1 
HETATM 8786 O  O     . HOH S 5 .   ? -18.222 3.361   39.637  1.00 25.84 ? 826  HOH B O     1 
HETATM 8787 O  O     . HOH S 5 .   ? -13.516 -8.860  43.438  1.00 22.82 ? 827  HOH B O     1 
HETATM 8788 O  O     . HOH S 5 .   ? -27.750 -15.572 40.934  1.00 33.71 ? 828  HOH B O     1 
HETATM 8789 O  O     . HOH S 5 .   ? -11.295 -47.142 49.055  1.00 43.95 ? 829  HOH B O     1 
HETATM 8790 O  O     . HOH S 5 .   ? -30.956 -23.411 40.747  1.00 25.08 ? 830  HOH B O     1 
HETATM 8791 O  O     . HOH S 5 .   ? -43.169 -19.940 18.998  1.00 37.67 ? 831  HOH B O     1 
HETATM 8792 O  O     . HOH S 5 .   ? -44.223 -4.395  53.141  1.00 24.34 ? 832  HOH B O     1 
HETATM 8793 O  O     . HOH S 5 .   ? -40.574 -10.612 52.777  1.00 33.59 ? 833  HOH B O     1 
HETATM 8794 O  O     . HOH S 5 .   ? -9.440  -32.631 27.887  1.00 14.07 ? 834  HOH B O     1 
HETATM 8795 O  O     . HOH S 5 .   ? -9.179  -11.052 49.121  1.00 38.25 ? 835  HOH B O     1 
HETATM 8796 O  O     . HOH S 5 .   ? -39.523 -25.651 27.688  1.00 25.33 ? 836  HOH B O     1 
HETATM 8797 O  O     . HOH S 5 .   ? -17.611 -32.839 55.522  1.00 42.05 ? 837  HOH B O     1 
HETATM 8798 O  O     . HOH S 5 .   ? -29.915 11.875  56.967  1.00 47.49 ? 838  HOH B O     1 
HETATM 8799 O  O     . HOH S 5 .   ? 3.753   -22.888 28.935  1.00 31.54 ? 839  HOH B O     1 
HETATM 8800 O  O     . HOH S 5 .   ? -20.344 2.678   41.118  1.00 28.02 ? 840  HOH B O     1 
HETATM 8801 O  O     . HOH S 5 .   ? -14.025 -14.617 43.564  1.00 15.81 ? 841  HOH B O     1 
HETATM 8802 O  O     . HOH S 5 .   ? -15.185 -23.972 45.262  1.00 23.81 ? 842  HOH B O     1 
HETATM 8803 O  O     . HOH S 5 .   ? -13.626 -13.327 41.241  1.00 17.88 ? 843  HOH B O     1 
HETATM 8804 O  O     . HOH S 5 .   ? -29.157 -1.147  49.397  1.00 24.91 ? 844  HOH B O     1 
HETATM 8805 O  O     . HOH S 5 .   ? -41.681 -26.970 38.501  1.00 20.10 ? 845  HOH B O     1 
HETATM 8806 O  O     . HOH S 5 .   ? -44.443 -22.224 20.640  1.00 35.45 ? 846  HOH B O     1 
HETATM 8807 O  O     . HOH S 5 .   ? 1.349   -22.391 28.208  1.00 19.64 ? 847  HOH B O     1 
HETATM 8808 O  O     . HOH S 5 .   ? -55.256 -9.566  51.894  1.00 44.60 ? 848  HOH B O     1 
HETATM 8809 O  O     . HOH S 5 .   ? -25.700 -42.648 58.126  1.00 42.98 ? 849  HOH B O     1 
HETATM 8810 O  O     . HOH S 5 .   ? -40.635 -15.418 59.320  1.00 37.14 ? 850  HOH B O     1 
HETATM 8811 O  O     . HOH S 5 .   ? -0.044  -19.730 34.554  1.00 32.98 ? 851  HOH B O     1 
HETATM 8812 O  O     . HOH S 5 .   ? -13.052 -49.773 51.185  1.00 30.86 ? 852  HOH B O     1 
HETATM 8813 O  O     . HOH S 5 .   ? -39.670 -17.454 33.712  1.00 23.30 ? 853  HOH B O     1 
HETATM 8814 O  O     . HOH S 5 .   ? -33.275 -35.173 41.303  1.00 31.78 ? 854  HOH B O     1 
HETATM 8815 O  O     . HOH S 5 .   ? -23.294 -30.047 34.698  1.00 34.02 ? 855  HOH B O     1 
HETATM 8816 O  O     . HOH S 5 .   ? -24.686 -33.043 37.203  1.00 31.80 ? 856  HOH B O     1 
HETATM 8817 O  O     . HOH S 5 .   ? -11.429 -20.577 56.395  1.00 43.55 ? 857  HOH B O     1 
HETATM 8818 O  O     . HOH S 5 .   ? -9.572  -26.486 23.725  1.00 22.96 ? 858  HOH B O     1 
HETATM 8819 O  O     . HOH S 5 .   ? -18.208 1.893   27.614  1.00 31.13 ? 859  HOH B O     1 
HETATM 8820 O  O     . HOH S 5 .   ? -12.734 -14.529 57.062  1.00 43.37 ? 860  HOH B O     1 
HETATM 8821 O  O     . HOH S 5 .   ? -42.617 -9.581  64.240  1.00 35.09 ? 861  HOH B O     1 
HETATM 8822 O  O     . HOH S 5 .   ? -16.664 -15.484 42.645  1.00 17.74 ? 862  HOH B O     1 
HETATM 8823 O  O     . HOH S 5 .   ? -30.344 -11.119 40.207  1.00 29.82 ? 863  HOH B O     1 
HETATM 8824 O  O     . HOH S 5 .   ? -35.064 -34.306 21.950  1.00 40.57 ? 864  HOH B O     1 
HETATM 8825 O  O     . HOH S 5 .   ? -20.385 -27.362 55.944  1.00 40.93 ? 865  HOH B O     1 
HETATM 8826 O  O     . HOH S 5 .   ? -40.754 -7.282  28.096  1.00 37.41 ? 866  HOH B O     1 
HETATM 8827 O  O     . HOH S 5 .   ? -30.646 -26.057 44.293  1.00 25.04 ? 867  HOH B O     1 
HETATM 8828 O  O     . HOH S 5 .   ? -26.117 -14.424 36.402  1.00 31.49 ? 868  HOH B O     1 
HETATM 8829 O  O     . HOH S 5 .   ? -39.256 10.770  40.927  1.00 45.45 ? 869  HOH B O     1 
HETATM 8830 O  O     . HOH S 5 .   ? -0.940  -21.354 44.737  1.00 38.41 ? 870  HOH B O     1 
HETATM 8831 O  O     . HOH S 5 .   ? -11.835 9.587   45.398  1.00 42.53 ? 871  HOH B O     1 
HETATM 8832 O  O     . HOH S 5 .   ? -30.114 15.277  38.547  1.00 39.88 ? 872  HOH B O     1 
HETATM 8833 O  O     . HOH S 5 .   ? -47.814 -1.832  67.358  1.00 36.72 ? 873  HOH B O     1 
HETATM 8834 O  O     . HOH S 5 .   ? -9.991  -41.467 33.951  1.00 29.11 ? 874  HOH B O     1 
HETATM 8835 O  O     . HOH S 5 .   ? -47.151 4.237   63.023  1.00 26.12 ? 875  HOH B O     1 
HETATM 8836 O  O     . HOH S 5 .   ? -8.987  -34.940 42.847  1.00 30.65 ? 876  HOH B O     1 
HETATM 8837 O  O     . HOH S 5 .   ? -36.871 10.084  34.218  1.00 40.21 ? 877  HOH B O     1 
HETATM 8838 O  O     . HOH S 5 .   ? -24.382 -27.197 36.899  1.00 27.26 ? 878  HOH B O     1 
HETATM 8839 O  O     . HOH S 5 .   ? -46.689 0.376   53.991  1.00 42.12 ? 879  HOH B O     1 
HETATM 8840 O  O     . HOH S 5 .   ? -39.878 -28.182 57.897  1.00 45.10 ? 880  HOH B O     1 
HETATM 8841 O  O     . HOH S 5 .   ? -11.287 -40.747 31.889  1.00 20.63 ? 881  HOH B O     1 
HETATM 8842 O  O     . HOH S 5 .   ? -44.292 7.489   45.609  1.00 30.55 ? 882  HOH B O     1 
HETATM 8843 O  O     . HOH S 5 .   ? -32.080 8.807   63.254  1.00 36.65 ? 883  HOH B O     1 
HETATM 8844 O  O     . HOH S 5 .   ? -30.343 6.034   27.782  1.00 31.26 ? 884  HOH B O     1 
HETATM 8845 O  O     . HOH S 5 .   ? -40.427 -9.017  64.664  1.00 28.40 ? 885  HOH B O     1 
HETATM 8846 O  O     . HOH S 5 .   ? -23.880 -41.359 23.174  1.00 49.30 ? 886  HOH B O     1 
HETATM 8847 O  O     . HOH S 5 .   ? -39.713 -28.333 29.050  1.00 25.67 ? 887  HOH B O     1 
HETATM 8848 O  O     . HOH S 5 .   ? -36.646 -21.843 49.763  1.00 31.23 ? 888  HOH B O     1 
HETATM 8849 O  O     . HOH S 5 .   ? -18.352 -9.590  36.217  1.00 21.74 ? 889  HOH B O     1 
HETATM 8850 O  O     . HOH S 5 .   ? -31.799 -22.401 38.582  1.00 27.01 ? 890  HOH B O     1 
HETATM 8851 O  O     . HOH S 5 .   ? -5.667  -26.188 49.978  1.00 36.19 ? 891  HOH B O     1 
HETATM 8852 O  O     . HOH S 5 .   ? -25.956 -25.336 38.575  1.00 36.45 ? 892  HOH B O     1 
HETATM 8853 O  O     . HOH S 5 .   ? -20.004 14.466  46.873  1.00 39.78 ? 893  HOH B O     1 
HETATM 8854 O  O     . HOH S 5 .   ? -32.451 -41.514 30.353  1.00 33.90 ? 894  HOH B O     1 
HETATM 8855 O  O     . HOH S 5 .   ? -8.032  -35.768 36.952  1.00 32.05 ? 895  HOH B O     1 
HETATM 8856 O  O     . HOH S 5 .   ? -13.068 0.520   35.795  1.00 38.87 ? 896  HOH B O     1 
HETATM 8857 O  O     . HOH S 5 .   ? -50.223 4.425   58.049  1.00 37.00 ? 897  HOH B O     1 
HETATM 8858 O  O     . HOH S 5 .   ? -3.290  -21.275 33.967  1.00 16.78 ? 898  HOH B O     1 
HETATM 8859 O  O     . HOH S 5 .   ? -41.345 -15.781 16.296  1.00 37.48 ? 899  HOH B O     1 
HETATM 8860 O  O     . HOH S 5 .   ? -43.523 6.500   49.018  1.00 36.41 ? 900  HOH B O     1 
HETATM 8861 O  O     . HOH S 5 .   ? -27.335 14.309  50.572  1.00 28.62 ? 901  HOH B O     1 
HETATM 8862 O  O     . HOH S 5 .   ? -14.781 -44.300 56.572  1.00 42.54 ? 902  HOH B O     1 
HETATM 8863 O  O     . HOH S 5 .   ? -19.291 -19.059 29.316  1.00 34.67 ? 903  HOH B O     1 
HETATM 8864 O  O     . HOH S 5 .   ? -19.117 -34.215 54.723  1.00 33.78 ? 904  HOH B O     1 
HETATM 8865 O  O     . HOH S 5 .   ? -39.304 -29.032 31.394  1.00 27.46 ? 905  HOH B O     1 
HETATM 8866 O  O     . HOH S 5 .   ? -40.058 -46.476 48.440  1.00 40.79 ? 906  HOH B O     1 
HETATM 8867 O  O     . HOH S 5 .   ? -34.429 -14.334 48.061  1.00 42.34 ? 907  HOH B O     1 
HETATM 8868 O  O     . HOH S 5 .   ? -24.074 -24.130 56.604  1.00 53.04 ? 908  HOH B O     1 
HETATM 8869 O  O     . HOH S 5 .   ? -18.290 -16.944 29.294  1.00 43.07 ? 909  HOH B O     1 
HETATM 8870 O  O     . HOH S 5 .   ? 1.608   -16.176 42.451  1.00 37.71 ? 910  HOH B O     1 
HETATM 8871 O  O     . HOH S 5 .   ? -34.429 17.783  47.999  1.00 50.03 ? 911  HOH B O     1 
HETATM 8872 O  O     . HOH S 5 .   ? -19.724 -44.295 27.454  1.00 43.25 ? 912  HOH B O     1 
HETATM 8873 O  O     . HOH S 5 .   ? -28.639 16.965  46.041  1.00 40.69 ? 913  HOH B O     1 
HETATM 8874 O  O     . HOH S 5 .   ? 1.353   -21.425 36.973  1.00 51.77 ? 914  HOH B O     1 
HETATM 8875 O  O     . HOH S 5 .   ? -14.729 -4.062  31.796  1.00 29.32 ? 915  HOH B O     1 
HETATM 8876 O  O     . HOH S 5 .   ? -2.310  -23.695 33.730  1.00 36.92 ? 916  HOH B O     1 
HETATM 8877 O  O     . HOH S 5 .   ? -22.227 -42.775 27.824  1.00 40.60 ? 917  HOH B O     1 
HETATM 8878 O  O     . HOH S 5 .   ? 7.126   -13.587 35.390  1.00 48.54 ? 918  HOH B O     1 
HETATM 8879 O  O     . HOH S 5 .   ? -22.271 13.299  51.275  1.00 40.20 ? 919  HOH B O     1 
HETATM 8880 O  O     . HOH S 5 .   ? -25.227 -12.566 35.298  1.00 38.01 ? 920  HOH B O     1 
HETATM 8881 O  O     . HOH S 5 .   ? -28.257 6.308   65.930  1.00 20.33 ? 921  HOH B O     1 
HETATM 8882 O  O     . HOH S 5 .   ? -30.786 -15.388 46.882  1.00 30.82 ? 922  HOH B O     1 
HETATM 8883 O  O     . HOH S 5 .   ? -16.203 -15.363 26.360  1.00 34.42 ? 923  HOH B O     1 
HETATM 8884 O  O     . HOH S 5 .   ? -9.499  4.869   48.616  1.00 35.17 ? 924  HOH B O     1 
HETATM 8885 O  O     . HOH S 5 .   ? -6.211  -8.052  49.461  1.00 38.41 ? 925  HOH B O     1 
HETATM 8886 O  O     . HOH S 5 .   ? -20.702 -5.354  36.882  1.00 37.38 ? 926  HOH B O     1 
HETATM 8887 O  O     . HOH S 5 .   ? -47.355 0.375   36.703  1.00 30.54 ? 927  HOH B O     1 
HETATM 8888 O  O     . HOH S 5 .   ? -45.521 -21.349 30.636  1.00 42.01 ? 928  HOH B O     1 
HETATM 8889 O  O     . HOH S 5 .   ? -33.754 -14.366 43.879  1.00 31.77 ? 929  HOH B O     1 
HETATM 8890 O  O     . HOH S 5 .   ? -51.364 -3.670  65.797  1.00 32.33 ? 930  HOH B O     1 
HETATM 8891 O  O     . HOH S 5 .   ? -27.836 -11.989 37.032  1.00 39.71 ? 931  HOH B O     1 
HETATM 8892 O  O     . HOH S 5 .   ? -21.695 -45.710 31.677  1.00 35.75 ? 932  HOH B O     1 
HETATM 8893 O  O     . HOH S 5 .   ? -19.516 -13.665 59.664  1.00 26.15 ? 933  HOH B O     1 
HETATM 8894 O  O     . HOH S 5 .   ? -24.763 -29.121 53.362  1.00 43.66 ? 934  HOH B O     1 
HETATM 8895 O  O     . HOH S 5 .   ? -26.657 0.947   65.793  1.00 42.35 ? 935  HOH B O     1 
HETATM 8896 O  O     . HOH S 5 .   ? -32.068 -9.169  63.051  1.00 37.10 ? 936  HOH B O     1 
HETATM 8897 O  O     . HOH S 5 .   ? -1.321  -31.372 31.771  1.00 27.45 ? 937  HOH B O     1 
HETATM 8898 O  O     . HOH S 5 .   ? -44.668 -27.331 35.808  1.00 36.12 ? 938  HOH B O     1 
HETATM 8899 O  O     . HOH S 5 .   ? -7.828  0.085   48.428  1.00 41.10 ? 939  HOH B O     1 
HETATM 8900 O  O     . HOH S 5 .   ? -14.556 1.322   28.009  1.00 37.13 ? 940  HOH B O     1 
HETATM 8901 O  O     . HOH S 5 .   ? -19.863 14.054  34.506  1.00 42.09 ? 941  HOH B O     1 
HETATM 8902 O  O     . HOH S 5 .   ? -4.989  -35.639 36.220  1.00 40.72 ? 942  HOH B O     1 
HETATM 8903 O  O     . HOH S 5 .   ? -39.580 -33.384 30.318  1.00 31.63 ? 943  HOH B O     1 
HETATM 8904 O  O     . HOH S 5 .   ? -40.783 -35.280 32.147  1.00 40.20 ? 944  HOH B O     1 
HETATM 8905 O  O     . HOH S 5 .   ? -29.036 -55.614 42.251  1.00 42.56 ? 945  HOH B O     1 
HETATM 8906 O  O     . HOH S 5 .   ? -15.185 10.002  46.104  1.00 37.99 ? 946  HOH B O     1 
HETATM 8907 O  O     . HOH S 5 .   ? -41.759 -20.445 14.357  1.00 45.79 ? 947  HOH B O     1 
HETATM 8908 O  O     . HOH S 5 .   ? -21.080 -7.284  37.008  1.00 41.47 ? 948  HOH B O     1 
HETATM 8909 O  O     . HOH S 5 .   ? -36.332 -45.470 34.628  1.00 53.05 ? 949  HOH B O     1 
HETATM 8910 O  O     . HOH S 5 .   ? 4.352   -31.537 26.831  1.00 44.37 ? 950  HOH B O     1 
HETATM 8911 O  O     . HOH S 5 .   ? -44.730 -26.970 28.535  1.00 47.47 ? 951  HOH B O     1 
HETATM 8912 O  O     . HOH S 5 .   ? -23.006 8.204   30.995  1.00 31.68 ? 952  HOH B O     1 
HETATM 8913 O  O     . HOH S 5 .   ? -25.012 13.374  56.247  1.00 42.53 ? 953  HOH B O     1 
HETATM 8914 O  O     . HOH S 5 .   ? -39.551 -32.809 55.107  1.00 43.64 ? 954  HOH B O     1 
HETATM 8915 O  O     . HOH S 5 .   ? -43.523 -16.380 19.839  1.00 47.61 ? 955  HOH B O     1 
HETATM 8916 O  O     . HOH S 5 .   ? -31.232 -12.675 48.516  1.00 49.60 ? 956  HOH B O     1 
HETATM 8917 O  O     . HOH S 5 .   ? -38.053 -30.355 51.368  1.00 26.16 ? 957  HOH B O     1 
HETATM 8918 O  O     . HOH S 5 .   ? -19.084 -9.726  33.287  1.00 37.92 ? 958  HOH B O     1 
HETATM 8919 O  O     . HOH S 5 .   ? -43.531 -9.077  37.197  1.00 28.23 ? 959  HOH B O     1 
HETATM 8920 O  O     . HOH S 5 .   ? -41.087 -0.885  49.944  1.00 32.15 ? 960  HOH B O     1 
HETATM 8921 O  O     . HOH S 5 .   ? -43.222 -0.933  52.581  1.00 36.65 ? 961  HOH B O     1 
HETATM 8922 O  O     . HOH S 5 .   ? -20.556 -10.448 30.275  1.00 40.31 ? 962  HOH B O     1 
HETATM 8923 O  O     . HOH S 5 .   ? -14.717 0.929   53.345  1.00 16.48 ? 963  HOH B O     1 
HETATM 8924 O  O     . HOH S 5 .   ? -18.158 10.069  32.821  1.00 36.13 ? 964  HOH B O     1 
HETATM 8925 O  O     . HOH S 5 .   ? -25.718 12.168  61.993  1.00 42.50 ? 965  HOH B O     1 
# 
