data_8S7P
# 
_entry.id   8S7P 
# 
_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   8S7P         pdb_00008s7p 10.2210/pdb8s7p/pdb 
WWPDB D_1292137015 ?            ?                   
# 
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                        8S7P 
_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         Andrea 
_pdbx_contact_author.name_last          Mattevi 
_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                58245.801 3  ? ? ? ? 
2 non-polymer nat 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   3  ? ? ? ? 
3 water       nat water                         18.015    48 ? ? ? ? 
# 
_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
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDPGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDPGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_strand_id                 A,B,C 
_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 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 PRO 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               NEB10beta 
_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 
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 
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   ?   ?   ?   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 PRO 151 151 151 PRO PRO 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   ?   ?   ?   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 PRO 151 151 151 PRO PRO 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 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ALA 2   2   ?   ?   ?   C . n 
C 1 3   ALA 3   3   3   ALA ALA C . n 
C 1 4   PRO 4   4   4   PRO PRO C . n 
C 1 5   LEU 5   5   5   LEU LEU C . n 
C 1 6   PRO 6   6   6   PRO PRO C . n 
C 1 7   GLU 7   7   7   GLU GLU C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  SER 10  10  10  SER SER C . n 
C 1 11  ALA 11  11  11  ALA ALA C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ALA 13  13  13  ALA ALA C . n 
C 1 14  MET 14  14  14  MET MET C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  ALA 17  17  17  ALA ALA C . n 
C 1 18  LEU 18  18  18  LEU LEU C . n 
C 1 19  ASP 19  19  19  ASP ASP C . n 
C 1 20  ARG 20  20  20  ARG ARG C . n 
C 1 21  PHE 21  21  21  PHE PHE C . n 
C 1 22  ALA 22  22  22  ALA ALA C . n 
C 1 23  ARG 23  23  23  ARG ARG C . n 
C 1 24  ILE 24  24  24  ILE ILE C . n 
C 1 25  VAL 25  25  25  VAL VAL C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  ALA 27  27  27  ALA ALA C . n 
C 1 28  ASP 28  28  28  ASP ASP C . n 
C 1 29  TRP 29  29  29  TRP TRP C . n 
C 1 30  VAL 30  30  30  VAL VAL C . n 
C 1 31  PHE 31  31  31  PHE PHE C . n 
C 1 32  THR 32  32  32  THR THR C . n 
C 1 33  GLU 33  33  33  GLU GLU C . n 
C 1 34  ASP 34  34  34  ASP ASP C . n 
C 1 35  LYS 35  35  35  LYS LYS C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  THR 37  37  37  THR THR C . n 
C 1 38  PRO 38  38  38  PRO PRO C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  ASP 41  41  41  ASP ASP C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  TYR 43  43  43  TYR TYR C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  ILE 45  45  45  ILE ILE C . n 
C 1 46  SER 46  46  46  SER SER C . n 
C 1 47  ASN 47  47  47  ASN ASN C . n 
C 1 48  ASP 48  48  48  ASP ASP C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  THR 50  50  50  THR THR C . n 
C 1 51  GLU 51  51  51  GLU GLU C . n 
C 1 52  HIS 52  52  52  HIS HIS C . n 
C 1 53  ARG 53  53  53  ARG ARG C . n 
C 1 54  PRO 54  54  54  PRO PRO C . n 
C 1 55  TYR 55  55  55  TYR TYR C . n 
C 1 56  ALA 56  56  56  ALA ALA C . n 
C 1 57  ALA 57  57  57  ALA ALA C . n 
C 1 58  VAL 58  58  58  VAL VAL C . n 
C 1 59  ALA 59  59  59  ALA ALA C . n 
C 1 60  PRO 60  60  60  PRO PRO C . n 
C 1 61  ALA 61  61  61  ALA ALA C . n 
C 1 62  SER 62  62  62  SER SER C . n 
C 1 63  THR 63  63  63  THR THR C . n 
C 1 64  GLU 64  64  64  GLU GLU C . n 
C 1 65  GLU 65  65  65  GLU GLU C . n 
C 1 66  VAL 66  66  66  VAL VAL C . n 
C 1 67  GLN 67  67  67  GLN GLN C . n 
C 1 68  GLU 68  68  68  GLU GLU C . n 
C 1 69  ILE 69  69  69  ILE ILE C . n 
C 1 70  VAL 70  70  70  VAL VAL C . n 
C 1 71  ARG 71  71  71  ARG ARG C . n 
C 1 72  VAL 72  72  72  VAL VAL C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  ASN 74  74  74  ASN ASN C . n 
C 1 75  GLU 75  75  75  GLU GLU C . n 
C 1 76  PHE 76  76  76  PHE PHE C . n 
C 1 77  GLY 77  77  77  GLY GLY C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  PRO 79  79  79  PRO PRO C . n 
C 1 80  LEU 80  80  80  LEU LEU C . n 
C 1 81  TRP 81  81  81  TRP TRP C . n 
C 1 82  PRO 82  82  82  PRO PRO C . n 
C 1 83  VAL 83  83  83  VAL VAL C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  ARG 85  85  85  ARG ARG C . n 
C 1 86  GLY 86  86  86  GLY GLY C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  ASN 88  88  88  ASN ASN C . n 
C 1 89  PHE 89  89  89  PHE PHE C . n 
C 1 90  ALA 90  90  90  ALA ALA C . n 
C 1 91  TYR 91  91  91  TYR TYR C . n 
C 1 92  GLY 92  92  92  GLY GLY C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  ALA 94  94  94  ALA ALA C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  PRO 96  96  96  PRO PRO C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  MET 98  98  98  MET MET C . n 
C 1 99  SER 99  99  99  SER SER C . n 
C 1 100 GLY 100 100 100 GLY GLY C . n 
C 1 101 THR 101 101 101 THR THR C . n 
C 1 102 VAL 102 102 102 VAL VAL C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 ASP 105 105 105 ASP ASP C . n 
C 1 106 MET 106 106 106 MET MET C . n 
C 1 107 ASN 107 107 107 ASN ASN C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 MET 109 109 109 MET MET C . n 
C 1 110 ASN 110 110 110 ASN ASN C . n 
C 1 111 ARG 111 111 111 ARG ARG C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 LEU 113 113 113 LEU LEU C . n 
C 1 114 GLU 114 114 114 GLU GLU C . n 
C 1 115 VAL 115 115 115 VAL VAL C . n 
C 1 116 ASN 116 116 116 ASN ASN C . n 
C 1 117 GLU 117 117 117 GLU GLU C . n 
C 1 118 GLU 118 118 118 GLU GLU C . n 
C 1 119 PHE 119 119 119 PHE PHE C . n 
C 1 120 GLY 120 120 120 GLY GLY C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ALA 122 122 122 ALA ALA C . n 
C 1 123 LEU 123 123 123 LEU LEU C . n 
C 1 124 VAL 124 124 124 VAL VAL C . n 
C 1 125 GLU 125 125 125 GLU GLU C . n 
C 1 126 PRO 126 126 126 PRO PRO C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 VAL 128 128 128 VAL VAL C . n 
C 1 129 SER 129 129 129 SER SER C . n 
C 1 130 TYR 130 130 130 TYR TYR C . n 
C 1 131 PHE 131 131 131 PHE PHE C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 TYR 134 134 134 TYR TYR C . n 
C 1 135 ASP 135 135 135 ASP ASP C . n 
C 1 136 TYR 136 136 136 TYR TYR C . n 
C 1 137 ILE 137 137 137 ILE ILE C . n 
C 1 138 GLN 138 138 138 GLN GLN C . n 
C 1 139 GLU 139 139 139 GLU GLU C . n 
C 1 140 LYS 140 140 140 LYS LYS C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 LYS 143 143 143 LYS LYS C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 TRP 145 145 145 TRP TRP C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 ASP 147 147 147 ASP ASP C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 PRO 149 149 149 PRO PRO C . n 
C 1 150 ASP 150 150 150 ASP ASP C . n 
C 1 151 PRO 151 151 151 PRO PRO C . n 
C 1 152 GLY 152 152 152 GLY GLY C . n 
C 1 153 TRP 153 153 153 TRP TRP C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 SER 155 155 155 SER SER C . n 
C 1 156 VAL 156 156 156 VAL VAL C . n 
C 1 157 VAL 157 157 157 VAL VAL C . n 
C 1 158 GLY 158 158 158 GLY GLY C . n 
C 1 159 ASN 159 159 159 ASN ASN C . n 
C 1 160 ALA 160 160 160 ALA ALA C . n 
C 1 161 LEU 161 161 161 LEU LEU C . n 
C 1 162 ASP 162 162 162 ASP ASP C . n 
C 1 163 HIS 163 163 163 HIS HIS C . n 
C 1 164 GLY 164 164 164 GLY GLY C . n 
C 1 165 ILE 165 165 165 ILE ILE C . n 
C 1 166 GLY 166 166 166 GLY GLY C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 THR 168 168 168 THR THR C . n 
C 1 169 PRO 169 169 169 PRO PRO C . n 
C 1 170 TYR 170 170 170 TYR TYR C . n 
C 1 171 GLY 171 171 171 GLY GLY C . n 
C 1 172 ASP 172 172 172 ASP ASP C . n 
C 1 173 HIS 173 173 173 HIS HIS C . n 
C 1 174 PHE 174 174 174 PHE PHE C . n 
C 1 175 ALA 175 175 175 ALA ALA C . n 
C 1 176 MET 176 176 176 MET MET C . n 
C 1 177 GLN 177 177 177 GLN GLN C . n 
C 1 178 CYS 178 178 178 CYS CYS C . n 
C 1 179 GLY 179 179 179 GLY GLY C . n 
C 1 180 MET 180 180 180 MET MET C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 VAL 182 182 182 VAL VAL C . n 
C 1 183 VAL 183 183 183 VAL VAL C . n 
C 1 184 LEU 184 184 184 LEU LEU C . n 
C 1 185 PRO 185 185 185 PRO PRO C . n 
C 1 186 ASN 186 186 186 ASN ASN C . n 
C 1 187 GLY 187 187 187 GLY GLY C . n 
C 1 188 GLU 188 188 188 GLU GLU C . n 
C 1 189 VAL 189 189 189 VAL VAL C . n 
C 1 190 VAL 190 190 190 VAL VAL C . n 
C 1 191 ARG 191 191 191 ARG ARG C . n 
C 1 192 THR 192 192 192 THR THR C . n 
C 1 193 GLY 193 193 193 GLY GLY C . n 
C 1 194 MET 194 194 194 MET MET C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 ALA 196 196 196 ALA ALA C . n 
C 1 197 MET 197 197 197 MET MET C . n 
C 1 198 PRO 198 198 198 PRO PRO C . n 
C 1 199 GLY 199 199 199 GLY GLY C . n 
C 1 200 ASN 200 200 200 ASN ASN C . n 
C 1 201 ASN 201 201 201 ASN ASN C . n 
C 1 202 THR 202 202 202 THR THR C . n 
C 1 203 TRP 203 203 203 TRP TRP C . n 
C 1 204 GLN 204 204 204 GLN GLN C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 PHE 206 206 206 PHE PHE C . n 
C 1 207 LYS 207 207 207 LYS LYS C . n 
C 1 208 TYR 208 208 208 TYR TYR C . n 
C 1 209 GLY 209 209 209 GLY GLY C . n 
C 1 210 TYR 210 210 210 TYR TYR C . n 
C 1 211 GLY 211 211 211 GLY GLY C . n 
C 1 212 PRO 212 212 212 PRO PRO C . n 
C 1 213 TYR 213 213 213 TYR TYR C . n 
C 1 214 VAL 214 214 214 VAL VAL C . n 
C 1 215 ASP 215 215 215 ASP ASP C . n 
C 1 216 GLY 216 216 216 GLY GLY C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 PHE 218 218 218 PHE PHE C . n 
C 1 219 SER 219 219 219 SER SER C . n 
C 1 220 GLN 220 220 220 GLN GLN C . n 
C 1 221 SER 221 221 221 SER SER C . n 
C 1 222 ASN 222 222 222 ASN ASN C . n 
C 1 223 PHE 223 223 223 PHE PHE C . n 
C 1 224 GLY 224 224 224 GLY GLY C . n 
C 1 225 VAL 225 225 225 VAL VAL C . n 
C 1 226 VAL 226 226 226 VAL VAL C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 LYS 228 228 228 LYS LYS C . n 
C 1 229 MET 229 229 229 MET MET C . n 
C 1 230 GLY 230 230 230 GLY GLY C . n 
C 1 231 ILE 231 231 231 ILE ILE C . n 
C 1 232 TRP 232 232 232 TRP TRP C . n 
C 1 233 LEU 233 233 233 LEU LEU C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 PRO 235 235 235 PRO PRO C . n 
C 1 236 GLU 236 236 236 GLU GLU C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 ALA 238 238 238 ALA ALA C . n 
C 1 239 GLY 239 239 239 GLY GLY C . n 
C 1 240 TYR 240 240 240 TYR TYR C . n 
C 1 241 ARG 241 241 241 ARG ARG C . n 
C 1 242 PRO 242 242 242 PRO PRO C . n 
C 1 243 TYR 243 243 243 TYR TYR C . n 
C 1 244 LEU 244 244 244 LEU LEU C . n 
C 1 245 ILE 245 245 245 ILE ILE C . n 
C 1 246 THR 246 246 246 THR THR C . n 
C 1 247 PHE 247 247 247 PHE PHE C . n 
C 1 248 GLU 248 248 248 GLU GLU C . n 
C 1 249 ASN 249 249 249 ASN ASN C . n 
C 1 250 GLU 250 250 250 GLU GLU C . n 
C 1 251 ASP 251 251 251 ASP ASP C . n 
C 1 252 ASP 252 252 252 ASP ASP C . n 
C 1 253 ILE 253 253 253 ILE ILE C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 THR 255 255 255 THR THR C . n 
C 1 256 VAL 256 256 256 VAL VAL C . n 
C 1 257 THR 257 257 257 THR THR C . n 
C 1 258 GLU 258 258 258 GLU GLU C . n 
C 1 259 ARG 259 259 259 ARG ARG C . n 
C 1 260 LEU 260 260 260 LEU LEU C . n 
C 1 261 ARG 261 261 261 ARG ARG C . n 
C 1 262 PRO 262 262 262 PRO PRO C . n 
C 1 263 LEU 263 263 263 LEU LEU C . n 
C 1 264 LYS 264 264 264 LYS LYS C . n 
C 1 265 VAL 265 265 265 VAL VAL C . n 
C 1 266 ALA 266 266 266 ALA ALA C . n 
C 1 267 GLY 267 267 267 GLY GLY C . n 
C 1 268 VAL 268 268 268 VAL VAL C . n 
C 1 269 ILE 269 269 269 ILE ILE C . n 
C 1 270 GLN 270 270 270 GLN GLN C . n 
C 1 271 ASN 271 271 271 ASN ASN C . n 
C 1 272 GLY 272 272 272 GLY GLY C . n 
C 1 273 ALA 273 273 273 ALA ALA C . n 
C 1 274 THR 274 274 274 THR THR C . n 
C 1 275 VAL 275 275 275 VAL VAL C . n 
C 1 276 ARG 276 276 276 ARG ARG C . n 
C 1 277 SER 277 277 277 SER SER C . n 
C 1 278 LEU 278 278 278 LEU LEU C . n 
C 1 279 VAL 279 279 279 VAL VAL C . n 
C 1 280 LEU 280 280 280 LEU LEU C . n 
C 1 281 ASP 281 281 281 ASP ASP C . n 
C 1 282 ALA 282 282 282 ALA ALA C . n 
C 1 283 ALA 283 283 283 ALA ALA C . n 
C 1 284 ILE 284 284 284 ILE ILE C . n 
C 1 285 THR 285 285 285 THR THR C . n 
C 1 286 ARG 286 286 286 ARG ARG C . n 
C 1 287 THR 287 287 287 THR THR C . n 
C 1 288 LYS 288 288 288 LYS LYS C . n 
C 1 289 SER 289 289 289 SER SER C . n 
C 1 290 GLN 290 290 290 GLN GLN C . n 
C 1 291 TYR 291 291 291 TYR TYR C . n 
C 1 292 TYR 292 292 292 TYR TYR C . n 
C 1 293 ASP 293 293 293 ASP ASP C . n 
C 1 294 GLY 294 294 294 GLY GLY C . n 
C 1 295 ASP 295 295 295 ASP ASP C . n 
C 1 296 GLY 296 296 296 GLY GLY C . n 
C 1 297 PRO 297 297 297 PRO PRO C . n 
C 1 298 ILE 298 298 298 ILE ILE C . n 
C 1 299 PRO 299 299 299 PRO PRO C . n 
C 1 300 PRO 300 300 300 PRO PRO C . n 
C 1 301 SER 301 301 301 SER SER C . n 
C 1 302 VAL 302 302 302 VAL VAL C . n 
C 1 303 ALA 303 303 303 ALA ALA C . n 
C 1 304 LYS 304 304 304 LYS LYS C . n 
C 1 305 THR 305 305 305 THR THR C . n 
C 1 306 MET 306 306 306 MET MET C . n 
C 1 307 MET 307 307 307 MET MET C . n 
C 1 308 ALA 308 308 308 ALA ALA C . n 
C 1 309 ASP 309 309 309 ASP ASP C . n 
C 1 310 LEU 310 310 310 LEU LEU C . n 
C 1 311 ASP 311 311 311 ASP ASP C . n 
C 1 312 LEU 312 312 312 LEU LEU C . n 
C 1 313 GLY 313 313 313 GLY GLY C . n 
C 1 314 MET 314 314 314 MET MET C . n 
C 1 315 TRP 315 315 315 TRP TRP C . n 
C 1 316 ASN 316 316 316 ASN ASN C . n 
C 1 317 PHE 317 317 317 PHE PHE C . n 
C 1 318 CYS 318 318 318 CYS CYS C . n 
C 1 319 GLY 319 319 319 GLY GLY C . n 
C 1 320 ALA 320 320 320 ALA ALA C . n 
C 1 321 LEU 321 321 321 LEU LEU C . n 
C 1 322 TYR 322 322 322 TYR TYR C . n 
C 1 323 GLY 323 323 323 GLY GLY C . n 
C 1 324 PRO 324 324 324 PRO PRO C . n 
C 1 325 PRO 325 325 325 PRO PRO C . n 
C 1 326 PRO 326 326 326 PRO PRO C . n 
C 1 327 VAL 327 327 327 VAL VAL C . n 
C 1 328 MET 328 328 328 MET MET C . n 
C 1 329 ASP 329 329 329 ASP ASP C . n 
C 1 330 THR 330 330 330 THR THR C . n 
C 1 331 LEU 331 331 331 LEU LEU C . n 
C 1 332 TRP 332 332 332 TRP TRP C . n 
C 1 333 THR 333 333 333 THR THR C . n 
C 1 334 ALA 334 334 334 ALA ALA C . n 
C 1 335 ILE 335 335 335 ILE ILE C . n 
C 1 336 ARG 336 336 336 ARG ARG C . n 
C 1 337 ASP 337 337 337 ASP ASP C . n 
C 1 338 SER 338 338 338 SER SER C . n 
C 1 339 PHE 339 339 339 PHE PHE C . n 
C 1 340 ALA 340 340 340 ALA ALA C . n 
C 1 341 ASP 341 341 341 ASP ASP C . n 
C 1 342 ILE 342 342 342 ILE ILE C . n 
C 1 343 PRO 343 343 343 PRO PRO C . n 
C 1 344 GLY 344 344 344 GLY GLY C . n 
C 1 345 VAL 345 345 345 VAL VAL C . n 
C 1 346 LYS 346 346 346 LYS LYS C . n 
C 1 347 PHE 347 347 347 PHE PHE C . n 
C 1 348 TYR 348 348 348 TYR TYR C . n 
C 1 349 PHE 349 349 349 PHE PHE C . n 
C 1 350 PRO 350 350 350 PRO PRO C . n 
C 1 351 GLU 351 351 351 GLU GLU C . n 
C 1 352 ASP 352 352 352 ASP ASP C . n 
C 1 353 ARG 353 353 353 ARG ARG C . n 
C 1 354 ARG 354 354 354 ARG ARG C . n 
C 1 355 HIS 355 355 355 HIS HIS C . n 
C 1 356 LYS 356 356 356 LYS LYS C . n 
C 1 357 VAL 357 357 357 VAL VAL C . n 
C 1 358 ASP 358 358 358 ASP ASP C . n 
C 1 359 LEU 359 359 359 LEU LEU C . n 
C 1 360 LEU 360 360 360 LEU LEU C . n 
C 1 361 LEU 361 361 361 LEU LEU C . n 
C 1 362 HIS 362 362 362 HIS HIS C . n 
C 1 363 ARG 363 363 363 ARG ARG C . n 
C 1 364 ALA 364 364 364 ALA ALA C . n 
C 1 365 GLU 365 365 365 GLU GLU C . n 
C 1 366 THR 366 366 366 THR THR C . n 
C 1 367 MET 367 367 367 MET MET C . n 
C 1 368 LYS 368 368 368 LYS LYS C . n 
C 1 369 GLY 369 369 369 GLY GLY C . n 
C 1 370 VAL 370 370 370 VAL VAL C . n 
C 1 371 PRO 371 371 371 PRO PRO C . n 
C 1 372 LYS 372 372 372 LYS LYS C . n 
C 1 373 LEU 373 373 373 LEU LEU C . n 
C 1 374 THR 374 374 374 THR THR C . n 
C 1 375 GLU 375 375 375 GLU GLU C . n 
C 1 376 PHE 376 376 376 PHE PHE C . n 
C 1 377 ASN 377 377 377 ASN ASN C . n 
C 1 378 PHE 378 378 378 PHE PHE C . n 
C 1 379 LEU 379 379 379 LEU LEU C . n 
C 1 380 ASN 380 380 380 ASN ASN C . n 
C 1 381 TRP 381 381 381 TRP TRP C . n 
C 1 382 ASP 382 382 382 ASP ASP C . n 
C 1 383 GLY 383 383 383 GLY GLY C . n 
C 1 384 GLY 384 384 384 GLY GLY C . n 
C 1 385 GLY 385 385 385 GLY GLY C . n 
C 1 386 GLY 386 386 386 GLY GLY C . n 
C 1 387 HIS 387 387 387 HIS HIS C . n 
C 1 388 VAL 388 388 388 VAL VAL C . n 
C 1 389 GLY 389 389 389 GLY GLY C . n 
C 1 390 PHE 390 390 390 PHE PHE C . n 
C 1 391 SER 391 391 391 SER SER C . n 
C 1 392 PRO 392 392 392 PRO PRO C . n 
C 1 393 VAL 393 393 393 VAL VAL C . n 
C 1 394 SER 394 394 394 SER SER C . n 
C 1 395 PRO 395 395 395 PRO PRO C . n 
C 1 396 ILE 396 396 396 ILE ILE C . n 
C 1 397 THR 397 397 397 THR THR C . n 
C 1 398 GLY 398 398 398 GLY GLY C . n 
C 1 399 LYS 399 399 399 LYS LYS C . n 
C 1 400 ASP 400 400 400 ASP ASP C . n 
C 1 401 ALA 401 401 401 ALA ALA C . n 
C 1 402 ILE 402 402 402 ILE ILE C . n 
C 1 403 LYS 403 403 403 LYS LYS C . n 
C 1 404 GLN 404 404 404 GLN GLN C . n 
C 1 405 TYR 405 405 405 TYR TYR C . n 
C 1 406 ASN 406 406 406 ASN ASN C . n 
C 1 407 MET 407 407 407 MET MET C . n 
C 1 408 VAL 408 408 408 VAL VAL C . n 
C 1 409 SER 409 409 409 SER SER C . n 
C 1 410 SER 410 410 410 SER SER C . n 
C 1 411 ARG 411 411 411 ARG ARG C . n 
C 1 412 VAL 412 412 412 VAL VAL C . n 
C 1 413 ARG 413 413 413 ARG ARG C . n 
C 1 414 GLU 414 414 414 GLU GLU C . n 
C 1 415 TYR 415 415 415 TYR TYR C . n 
C 1 416 GLY 416 416 416 GLY GLY C . n 
C 1 417 PHE 417 417 417 PHE PHE C . n 
C 1 418 ASP 418 418 418 ASP ASP C . n 
C 1 419 TYR 419 419 419 TYR TYR C . n 
C 1 420 MET 420 420 420 MET MET C . n 
C 1 421 GLY 421 421 421 GLY GLY C . n 
C 1 422 LEU 422 422 422 LEU LEU C . n 
C 1 423 LEU 423 423 423 LEU LEU C . n 
C 1 424 ALA 424 424 424 ALA ALA C . n 
C 1 425 ILE 425 425 425 ILE ILE C . n 
C 1 426 GLY 426 426 426 GLY GLY C . n 
C 1 427 TRP 427 427 427 TRP TRP C . n 
C 1 428 ARG 428 428 428 ARG ARG C . n 
C 1 429 ASP 429 429 429 ASP ASP C . n 
C 1 430 LEU 430 430 430 LEU LEU C . n 
C 1 431 HIS 431 431 431 HIS HIS C . n 
C 1 432 HIS 432 432 432 HIS HIS C . n 
C 1 433 VAL 433 433 433 VAL VAL C . n 
C 1 434 THR 434 434 434 THR THR C . n 
C 1 435 VAL 435 435 435 VAL VAL C . n 
C 1 436 ILE 436 436 436 ILE ILE C . n 
C 1 437 VAL 437 437 437 VAL VAL C . n 
C 1 438 TYR 438 438 438 TYR TYR C . n 
C 1 439 ASP 439 439 439 ASP ASP C . n 
C 1 440 LYS 440 440 440 LYS LYS C . n 
C 1 441 THR 441 441 441 THR THR C . n 
C 1 442 ASP 442 442 442 ASP ASP C . n 
C 1 443 PRO 443 443 443 PRO PRO C . n 
C 1 444 ASP 444 444 444 ASP ASP C . n 
C 1 445 GLU 445 445 445 GLU GLU C . n 
C 1 446 ARG 446 446 446 ARG ARG C . n 
C 1 447 LYS 447 447 447 LYS LYS C . n 
C 1 448 LYS 448 448 448 LYS LYS C . n 
C 1 449 LEU 449 449 449 LEU LEU C . n 
C 1 450 ASP 450 450 450 ASP ASP C . n 
C 1 451 GLU 451 451 451 GLU GLU C . n 
C 1 452 LEU 452 452 452 LEU LEU C . n 
C 1 453 PHE 453 453 453 PHE PHE C . n 
C 1 454 ASN 454 454 454 ASN ASN C . n 
C 1 455 ILE 455 455 455 ILE ILE C . n 
C 1 456 LEU 456 456 456 LEU LEU C . n 
C 1 457 VAL 457 457 457 VAL VAL C . n 
C 1 458 ASP 458 458 458 ASP ASP C . n 
C 1 459 GLU 459 459 459 GLU GLU C . n 
C 1 460 ALA 460 460 460 ALA ALA C . n 
C 1 461 ALA 461 461 461 ALA ALA C . n 
C 1 462 ALA 462 462 462 ALA ALA C . n 
C 1 463 GLU 463 463 463 GLU GLU C . n 
C 1 464 GLY 464 464 464 GLY GLY C . n 
C 1 465 TYR 465 465 465 TYR TYR C . n 
C 1 466 GLY 466 466 466 GLY GLY C . n 
C 1 467 GLU 467 467 467 GLU GLU C . n 
C 1 468 TYR 468 468 468 TYR TYR C . n 
C 1 469 ARG 469 469 469 ARG ARG C . n 
C 1 470 THR 470 470 470 THR THR C . n 
C 1 471 HIS 471 471 471 HIS HIS C . n 
C 1 472 ILE 472 472 472 ILE ILE C . n 
C 1 473 ARG 473 473 473 ARG ARG C . n 
C 1 474 TYR 474 474 474 TYR TYR C . n 
C 1 475 MET 475 475 475 MET MET C . n 
C 1 476 ASP 476 476 476 ASP ASP C . n 
C 1 477 ARG 477 477 477 ARG ARG C . n 
C 1 478 ILE 478 478 478 ILE ILE C . n 
C 1 479 ALA 479 479 479 ALA ALA C . n 
C 1 480 LYS 480 480 480 LYS LYS C . n 
C 1 481 THR 481 481 481 THR THR C . n 
C 1 482 TYR 482 482 482 TYR TYR C . n 
C 1 483 SER 483 483 483 SER SER C . n 
C 1 484 TRP 484 484 484 TRP TRP C . n 
C 1 485 ASN 485 485 485 ASN ASN C . n 
C 1 486 ASP 486 486 486 ASP ASP C . n 
C 1 487 ASN 487 487 487 ASN ASN C . n 
C 1 488 ALA 488 488 488 ALA ALA C . n 
C 1 489 LEU 489 489 489 LEU LEU C . n 
C 1 490 TRP 490 490 490 TRP TRP C . n 
C 1 491 LYS 491 491 491 LYS LYS C . n 
C 1 492 MET 492 492 492 MET MET C . n 
C 1 493 HIS 493 493 493 HIS HIS C . n 
C 1 494 GLU 494 494 494 GLU GLU C . n 
C 1 495 THR 495 495 495 THR THR C . n 
C 1 496 ILE 496 496 496 ILE ILE C . n 
C 1 497 LYS 497 497 497 LYS LYS C . n 
C 1 498 ASP 498 498 498 ASP ASP C . n 
C 1 499 ALA 499 499 499 ALA ALA C . n 
C 1 500 LEU 500 500 500 LEU LEU C . n 
C 1 501 ASP 501 501 501 ASP ASP C . n 
C 1 502 PRO 502 502 502 PRO PRO C . n 
C 1 503 ASN 503 503 503 ASN ASN C . n 
C 1 504 GLY 504 504 504 GLY GLY C . n 
C 1 505 ILE 505 505 505 ILE ILE C . n 
C 1 506 LEU 506 506 506 LEU LEU C . n 
C 1 507 ALA 507 507 507 ALA ALA C . n 
C 1 508 PRO 508 508 508 PRO PRO C . n 
C 1 509 GLY 509 509 509 GLY GLY C . n 
C 1 510 LYS 510 510 510 LYS LYS C . n 
C 1 511 SER 511 511 511 SER SER C . n 
C 1 512 GLY 512 512 512 GLY GLY C . n 
C 1 513 ILE 513 513 513 ILE ILE C . n 
C 1 514 TRP 514 514 514 TRP TRP C . n 
C 1 515 GLY 515 515 515 GLY GLY C . n 
C 1 516 LYS 516 516 516 LYS LYS C . n 
C 1 517 ASN 517 517 517 ASN ASN C . n 
C 1 518 ARG 518 518 518 ARG ARG C . n 
C 1 519 ARG 519 519 519 ARG ARG C . n 
C 1 520 LYS 520 520 ?   ?   ?   C . n 
C 1 521 ALA 521 521 ?   ?   ?   C . 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 
D 2 FAD 1  601 601 FAD FAD A . 
E 2 FAD 1  601 601 FAD FAD B . 
F 2 FAD 1  601 601 FAD FAD C . 
G 3 HOH 1  701 48  HOH HOH A . 
G 3 HOH 2  702 51  HOH HOH A . 
G 3 HOH 3  703 31  HOH HOH A . 
G 3 HOH 4  704 35  HOH HOH A . 
G 3 HOH 5  705 50  HOH HOH A . 
G 3 HOH 6  706 43  HOH HOH A . 
G 3 HOH 7  707 42  HOH HOH A . 
G 3 HOH 8  708 8   HOH HOH A . 
G 3 HOH 9  709 26  HOH HOH A . 
G 3 HOH 10 710 39  HOH HOH A . 
G 3 HOH 11 711 27  HOH HOH A . 
G 3 HOH 12 712 57  HOH HOH A . 
G 3 HOH 13 713 30  HOH HOH A . 
G 3 HOH 14 714 2   HOH HOH A . 
G 3 HOH 15 715 4   HOH HOH A . 
G 3 HOH 16 716 52  HOH HOH A . 
H 3 HOH 1  701 44  HOH HOH B . 
H 3 HOH 2  702 56  HOH HOH B . 
H 3 HOH 3  703 55  HOH HOH B . 
H 3 HOH 4  704 37  HOH HOH B . 
H 3 HOH 5  705 22  HOH HOH B . 
H 3 HOH 6  706 49  HOH HOH B . 
H 3 HOH 7  707 47  HOH HOH B . 
H 3 HOH 8  708 40  HOH HOH B . 
H 3 HOH 9  709 23  HOH HOH B . 
H 3 HOH 10 710 38  HOH HOH B . 
H 3 HOH 11 711 3   HOH HOH B . 
H 3 HOH 12 712 6   HOH HOH B . 
H 3 HOH 13 713 18  HOH HOH B . 
I 3 HOH 1  701 46  HOH HOH C . 
I 3 HOH 2  702 25  HOH HOH C . 
I 3 HOH 3  703 11  HOH HOH C . 
I 3 HOH 4  704 29  HOH HOH C . 
I 3 HOH 5  705 41  HOH HOH C . 
I 3 HOH 6  706 36  HOH HOH C . 
I 3 HOH 7  707 7   HOH HOH C . 
I 3 HOH 8  708 24  HOH HOH C . 
I 3 HOH 9  709 28  HOH HOH C . 
I 3 HOH 10 710 32  HOH HOH C . 
I 3 HOH 11 711 53  HOH HOH C . 
I 3 HOH 12 712 9   HOH HOH C . 
I 3 HOH 13 713 45  HOH HOH C . 
I 3 HOH 14 714 20  HOH HOH C . 
I 3 HOH 15 715 33  HOH HOH C . 
I 3 HOH 16 716 10  HOH HOH C . 
I 3 HOH 17 717 17  HOH HOH C . 
I 3 HOH 18 718 1   HOH HOH C . 
I 3 HOH 19 719 5   HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 34  ? CG  ? A ASP 34  CG  
2  1 Y 1 A ASP 34  ? OD1 ? A ASP 34  OD1 
3  1 Y 1 A ASP 34  ? OD2 ? A ASP 34  OD2 
4  1 Y 1 A LYS 35  ? CG  ? A LYS 35  CG  
5  1 Y 1 A LYS 35  ? CD  ? A LYS 35  CD  
6  1 Y 1 A LYS 35  ? CE  ? A LYS 35  CE  
7  1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
8  1 Y 1 B ARG 23  ? CG  ? B ARG 23  CG  
9  1 Y 1 B ARG 23  ? CD  ? B ARG 23  CD  
10 1 Y 1 B ARG 23  ? NE  ? B ARG 23  NE  
11 1 Y 1 B ARG 23  ? CZ  ? B ARG 23  CZ  
12 1 Y 1 B ARG 23  ? NH1 ? B ARG 23  NH1 
13 1 Y 1 B ARG 23  ? NH2 ? B ARG 23  NH2 
14 1 Y 1 B GLU 33  ? CG  ? B GLU 33  CG  
15 1 Y 1 B GLU 33  ? CD  ? B GLU 33  CD  
16 1 Y 1 B GLU 33  ? OE1 ? B GLU 33  OE1 
17 1 Y 1 B GLU 33  ? OE2 ? B GLU 33  OE2 
18 1 Y 1 B LYS 35  ? CG  ? B LYS 35  CG  
19 1 Y 1 B LYS 35  ? CD  ? B LYS 35  CD  
20 1 Y 1 B LYS 35  ? CE  ? B LYS 35  CE  
21 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
22 1 Y 1 B GLU 49  ? CG  ? B GLU 49  CG  
23 1 Y 1 B GLU 49  ? CD  ? B GLU 49  CD  
24 1 Y 1 B GLU 49  ? OE1 ? B GLU 49  OE1 
25 1 Y 1 B GLU 49  ? OE2 ? B GLU 49  OE2 
26 1 Y 1 B ASP 295 ? CG  ? B ASP 295 CG  
27 1 Y 1 B ASP 295 ? OD1 ? B ASP 295 OD1 
28 1 Y 1 B ASP 295 ? OD2 ? B ASP 295 OD2 
29 1 Y 1 B GLU 375 ? CG  ? B GLU 375 CG  
30 1 Y 1 B GLU 375 ? CD  ? B GLU 375 CD  
31 1 Y 1 B GLU 375 ? OE1 ? B GLU 375 OE1 
32 1 Y 1 B GLU 375 ? OE2 ? B GLU 375 OE2 
33 1 Y 1 B LYS 516 ? CG  ? B LYS 516 CG  
34 1 Y 1 B LYS 516 ? CD  ? B LYS 516 CD  
35 1 Y 1 B LYS 516 ? CE  ? B LYS 516 CE  
36 1 Y 1 B LYS 516 ? NZ  ? B LYS 516 NZ  
37 1 Y 1 C ASP 34  ? CG  ? C ASP 34  CG  
38 1 Y 1 C ASP 34  ? OD1 ? C ASP 34  OD1 
39 1 Y 1 C ASP 34  ? OD2 ? C ASP 34  OD2 
40 1 Y 1 C LYS 35  ? CG  ? C LYS 35  CG  
41 1 Y 1 C LYS 35  ? CD  ? C LYS 35  CD  
42 1 Y 1 C LYS 35  ? CE  ? C LYS 35  CE  
43 1 Y 1 C LYS 35  ? NZ  ? C LYS 35  NZ  
44 1 Y 1 C GLU 49  ? CG  ? C GLU 49  CG  
45 1 Y 1 C GLU 49  ? CD  ? C GLU 49  CD  
46 1 Y 1 C GLU 49  ? OE1 ? C GLU 49  OE1 
47 1 Y 1 C GLU 49  ? OE2 ? C GLU 49  OE2 
48 1 Y 1 C GLU 375 ? CG  ? C GLU 375 CG  
49 1 Y 1 C GLU 375 ? CD  ? C GLU 375 CD  
50 1 Y 1 C GLU 375 ? OE1 ? C GLU 375 OE1 
51 1 Y 1 C GLU 375 ? OE2 ? C GLU 375 OE2 
52 1 Y 1 C PHE 376 ? CG  ? C PHE 376 CG  
53 1 Y 1 C PHE 376 ? CD1 ? C PHE 376 CD1 
54 1 Y 1 C PHE 376 ? CD2 ? C PHE 376 CD2 
55 1 Y 1 C PHE 376 ? CE1 ? C PHE 376 CE1 
56 1 Y 1 C PHE 376 ? CE2 ? C PHE 376 CE2 
57 1 Y 1 C PHE 376 ? CZ  ? C PHE 376 CZ  
# 
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  ? ? ? 5.8.0403 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                     8S7P 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.142 
_cell.length_a_esd                 ? 
_cell.length_b                     143.224 
_cell.length_b_esd                 ? 
_cell.length_c                     287.748 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         8S7P 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 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                   8S7P 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.66 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.72 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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 EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-16 
_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   0.967700 
_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-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.967700 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S7P 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               67.49 
_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                                     77772 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                21.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.92 
_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                                0.170 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.166 
_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                                    2.35 
_reflns_shell.d_res_low                                     2.40 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           72661 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4521 
_reflns_shell.percent_possible_obs                          99.6 
_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                               16.1 
_reflns_shell.pdbx_chi_squared                              0.84 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               3.403 
_reflns_shell.pdbx_Rpim_I_all                               0.836 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.488 
_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                                  3.295 
_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]                            0.69 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            2.66 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -3.35 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               56.108 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.910 
_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                                 8S7P 
_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                            2.35 
_refine.ls_d_res_low                             67.49 
_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                     73750 
_refine.ls_number_reflns_R_free                  3964 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.23056 
_refine.ls_R_factor_R_free                       0.27907 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22789 
_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                       0.390 
_refine.pdbx_overall_ESU_R_Free                  0.274 
_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                             11.831 
_refine.overall_SU_ML                            0.253 
_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                       2.35 
_refine_hist.d_res_low                        67.49 
_refine_hist.number_atoms_solvent             48 
_refine_hist.number_atoms_total               12389 
_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        12182 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         159 
_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' ? 0.008  0.012  12703 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  11575 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.546  1.651  17332 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.518  1.568  26659 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.878  5.000  1550  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.376  5.000  77    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.366 10.000 1938  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.072  0.200  1826  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  14878 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  2949  ? 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' ? 5.408  5.513  6209  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.408  5.513  6209  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 7.680  9.916  7756  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.680  9.916  7757  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.794  5.866  6494  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.789  5.866  6491  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.386  10.631 9577  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.871 54.11  14449 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.871 54.11  14450 ? 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                       2.350 
_refine_ls_shell.d_res_low                        2.411 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             287 
_refine_ls_shell.number_reflns_R_work             5360 
_refine_ls_shell.percent_reflns_obs               99.63 
_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                  0.556 
_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                  0.554 
# 
_struct.entry_id                     8S7P 
_struct.title                        'Vanillyl-alcohol dehydrogenase from Marinicaulis flavus' 
_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        8S7P 
_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 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
_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 8S7P A 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
2 1 8S7P B 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
3 1 8S7P C 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 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)' 9960  ? 
1 MORE         -84   ? 
1 'SSA (A^2)'  34330 ? 
2 'ABSA (A^2)' 9940  ? 
2 MORE         -85   ? 
2 'SSA (A^2)'  34140 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,B,D,E,G,H 
2 1,2 C,F,I       
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 ? GLY A 141 ? SER A 129 GLY A 141 1 ? 13 
HELX_P HELX_P5  AA5 SER A 155 ? ASP A 162 ? SER A 155 ASP A 162 1 ? 8  
HELX_P HELX_P6  AA6 GLY A 193 ? MET A 197 ? GLY A 193 MET A 197 5 ? 5  
HELX_P HELX_P7  AA7 VAL A 214 ? SER A 219 ? VAL A 214 SER A 219 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 249 ? ASP A 251 ? ASN A 249 ASP A 251 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 252 ? ALA A 266 ? ASP A 252 ALA A 266 1 ? 15 
HELX_P HELX_P10 AB1 LEU A 278 ? ALA A 283 ? LEU A 278 ALA A 283 1 ? 6  
HELX_P HELX_P11 AB2 THR A 287 ? TYR A 291 ? THR A 287 TYR A 291 5 ? 5  
HELX_P HELX_P12 AB3 PRO A 299 ? ASP A 311 ? PRO A 299 ASP A 311 1 ? 13 
HELX_P HELX_P13 AB4 PRO A 324 ? SER A 338 ? PRO A 324 SER A 338 1 ? 15 
HELX_P HELX_P14 AB5 PHE A 349 ? ARG A 353 ? PHE A 349 ARG A 353 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 358 ? MET A 367 ? ASP A 358 MET A 367 1 ? 10 
HELX_P HELX_P16 AB7 ASN A 377 ? TRP A 381 ? ASN A 377 TRP A 381 5 ? 5  
HELX_P HELX_P17 AB8 THR A 397 ? TYR A 415 ? THR A 397 TYR A 415 1 ? 19 
HELX_P HELX_P18 AB9 ASP A 442 ? ALA A 462 ? ASP A 442 ALA A 462 1 ? 21 
HELX_P HELX_P19 AC1 HIS A 471 ? ARG A 473 ? HIS A 471 ARG A 473 5 ? 3  
HELX_P HELX_P20 AC2 TYR A 474 ? THR A 481 ? TYR A 474 THR A 481 1 ? 8  
HELX_P HELX_P21 AC3 SER A 483 ? ASP A 501 ? SER A 483 ASP A 501 1 ? 19 
HELX_P HELX_P22 AC4 GLY A 509 ? ILE A 513 ? GLY A 509 ILE A 513 5 ? 5  
HELX_P HELX_P23 AC5 GLY A 515 ? ARG A 519 ? GLY A 515 ARG A 519 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  ? PHE B 76  ? SER B 62  PHE B 76  1 ? 15 
HELX_P HELX_P27 AC9 ASN B 88  ? GLY B 92  ? ASN B 88  GLY B 92  5 ? 5  
HELX_P HELX_P28 AD1 SER B 129 ? LYS B 140 ? SER B 129 LYS B 140 1 ? 12 
HELX_P HELX_P29 AD2 SER B 155 ? ASP B 162 ? SER B 155 ASP B 162 1 ? 8  
HELX_P HELX_P30 AD3 HIS B 173 ? ALA B 175 ? HIS B 173 ALA B 175 5 ? 3  
HELX_P HELX_P31 AD4 GLY B 193 ? MET B 197 ? GLY B 193 MET B 197 5 ? 5  
HELX_P HELX_P32 AD5 VAL B 214 ? SER B 219 ? VAL B 214 SER B 219 5 ? 6  
HELX_P HELX_P33 AD6 ASN B 249 ? ASP B 251 ? ASN B 249 ASP B 251 5 ? 3  
HELX_P HELX_P34 AD7 ASP B 252 ? ALA B 266 ? ASP B 252 ALA B 266 1 ? 15 
HELX_P HELX_P35 AD8 LEU B 278 ? ARG B 286 ? LEU B 278 ARG B 286 1 ? 9  
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 THR B 397 ? TYR B 415 ? THR B 397 TYR B 415 1 ? 19 
HELX_P HELX_P41 AE5 ASP B 442 ? GLU B 463 ? ASP B 442 GLU B 463 1 ? 22 
HELX_P HELX_P42 AE6 HIS B 471 ? ARG B 473 ? HIS B 471 ARG B 473 5 ? 3  
HELX_P HELX_P43 AE7 TYR B 474 ? THR B 481 ? TYR B 474 THR B 481 1 ? 8  
HELX_P HELX_P44 AE8 SER B 483 ? ASP B 501 ? SER B 483 ASP B 501 1 ? 19 
HELX_P HELX_P45 AE9 GLY B 509 ? ILE B 513 ? GLY B 509 ILE B 513 5 ? 5  
HELX_P HELX_P46 AF1 GLY B 515 ? ARG B 519 ? GLY B 515 ARG B 519 5 ? 5  
HELX_P HELX_P47 AF2 SER C 10  ? GLY C 26  ? SER C 10  GLY C 26  1 ? 17 
HELX_P HELX_P48 AF3 SER C 62  ? PHE C 76  ? SER C 62  PHE C 76  1 ? 15 
HELX_P HELX_P49 AF4 SER C 129 ? GLY C 141 ? SER C 129 GLY C 141 1 ? 13 
HELX_P HELX_P50 AF5 SER C 155 ? ASP C 162 ? SER C 155 ASP C 162 1 ? 8  
HELX_P HELX_P51 AF6 HIS C 173 ? ALA C 175 ? HIS C 173 ALA C 175 5 ? 3  
HELX_P HELX_P52 AF7 GLY C 193 ? MET C 197 ? GLY C 193 MET C 197 5 ? 5  
HELX_P HELX_P53 AF8 VAL C 214 ? SER C 219 ? VAL C 214 SER C 219 5 ? 6  
HELX_P HELX_P54 AF9 ASN C 249 ? ASP C 251 ? ASN C 249 ASP C 251 5 ? 3  
HELX_P HELX_P55 AG1 ASP C 252 ? ALA C 266 ? ASP C 252 ALA C 266 1 ? 15 
HELX_P HELX_P56 AG2 LEU C 278 ? ALA C 283 ? LEU C 278 ALA C 283 1 ? 6  
HELX_P HELX_P57 AG3 THR C 287 ? TYR C 291 ? THR C 287 TYR C 291 5 ? 5  
HELX_P HELX_P58 AG4 PRO C 299 ? ASP C 311 ? PRO C 299 ASP C 311 1 ? 13 
HELX_P HELX_P59 AG5 PRO C 324 ? ALA C 340 ? PRO C 324 ALA C 340 1 ? 17 
HELX_P HELX_P60 AG6 PHE C 349 ? ARG C 353 ? PHE C 349 ARG C 353 5 ? 5  
HELX_P HELX_P61 AG7 ASP C 358 ? MET C 367 ? ASP C 358 MET C 367 1 ? 10 
HELX_P HELX_P62 AG8 ASN C 377 ? TRP C 381 ? ASN C 377 TRP C 381 5 ? 5  
HELX_P HELX_P63 AG9 THR C 397 ? TYR C 415 ? THR C 397 TYR C 415 1 ? 19 
HELX_P HELX_P64 AH1 ASP C 442 ? GLU C 463 ? ASP C 442 GLU C 463 1 ? 22 
HELX_P HELX_P65 AH2 HIS C 471 ? ARG C 473 ? HIS C 471 ARG C 473 5 ? 3  
HELX_P HELX_P66 AH3 TYR C 474 ? THR C 481 ? TYR C 474 THR C 481 1 ? 8  
HELX_P HELX_P67 AH4 SER C 483 ? ASP C 501 ? SER C 483 ASP C 501 1 ? 19 
HELX_P HELX_P68 AH5 GLY C 509 ? ILE C 513 ? GLY C 509 ILE C 513 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASP 150 A . ? ASP 150 A PRO 151 A ? PRO 151 A 1 -7.41  
2 ASP 150 B . ? ASP 150 B PRO 151 B ? PRO 151 B 1 -12.76 
3 ASP 150 C . ? ASP 150 C PRO 151 C ? PRO 151 C 1 1.97   
# 
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 ? 7 ? 
AA9 ? 4 ? 
AB1 ? 5 ? 
AB2 ? 2 ? 
AB3 ? 7 ? 
AB4 ? 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 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB3 5 6 ? anti-parallel 
AB3 6 7 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB4 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 57  ? VAL A 58  ? ALA A 57  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 MET A 420 ? ILE A 425 ? MET A 420 ILE A 425 
AA4 6 ASP A 429 ? TYR A 438 ? ASP A 429 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 MET A 420 ? ILE A 425 ? MET A 420 ILE A 425 
AA5 6 ASP A 429 ? TYR A 438 ? ASP A 429 TYR A 438 
AA5 7 VAL A 393 ? PRO A 395 ? VAL A 393 PRO A 395 
AA6 1 VAL B 30  ? PHE B 31  ? VAL B 30  PHE B 31  
AA6 2 ALA B 56  ? VAL B 58  ? ALA B 56  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 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AA8 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AA8 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AA8 4 ALA B 273 ? SER B 277 ? ALA B 273 SER B 277 
AA8 5 GLY B 421 ? ILE B 425 ? GLY B 421 ILE B 425 
AA8 6 LEU B 430 ? ASP B 439 ? LEU B 430 ASP B 439 
AA8 7 GLY B 385 ? PHE B 390 ? GLY B 385 PHE B 390 
AA9 1 VAL C 30  ? PHE C 31  ? VAL C 30  PHE C 31  
AA9 2 ALA C 56  ? VAL C 58  ? ALA C 56  VAL C 58  
AA9 3 VAL C 102 ? ASP C 105 ? VAL C 102 ASP C 105 
AA9 4 LEU C 80  ? VAL C 83  ? LEU C 80  VAL C 83  
AB1 1 ILE C 112 ? ASN C 116 ? ILE C 112 ASN C 116 
AB1 2 TYR C 121 ? VAL C 124 ? TYR C 121 VAL C 124 
AB1 3 VAL C 225 ? TRP C 232 ? VAL C 225 TRP C 232 
AB1 4 GLN C 177 ? VAL C 183 ? GLN C 177 VAL C 183 
AB1 5 VAL C 189 ? ARG C 191 ? VAL C 189 ARG C 191 
AB2 1 LEU C 144 ? TRP C 145 ? LEU C 144 TRP C 145 
AB2 2 MET C 234 ? PRO C 235 ? MET C 234 PRO C 235 
AB3 1 LYS C 346 ? TYR C 348 ? LYS C 346 TYR C 348 
AB3 2 TYR C 240 ? PHE C 247 ? TYR C 240 PHE C 247 
AB3 3 TRP C 315 ? TYR C 322 ? TRP C 315 TYR C 322 
AB3 4 ALA C 273 ? SER C 277 ? ALA C 273 SER C 277 
AB3 5 MET C 420 ? ILE C 425 ? MET C 420 ILE C 425 
AB3 6 ASP C 429 ? TYR C 438 ? ASP C 429 TYR C 438 
AB3 7 GLY C 386 ? PHE C 390 ? GLY C 386 PHE C 390 
AB4 1 LYS C 346 ? TYR C 348 ? LYS C 346 TYR C 348 
AB4 2 TYR C 240 ? PHE C 247 ? TYR C 240 PHE C 247 
AB4 3 TRP C 315 ? TYR C 322 ? TRP C 315 TYR C 322 
AB4 4 ALA C 273 ? SER C 277 ? ALA C 273 SER C 277 
AB4 5 MET C 420 ? ILE C 425 ? MET C 420 ILE C 425 
AB4 6 ASP C 429 ? TYR C 438 ? ASP C 429 TYR C 438 
AB4 7 VAL C 393 ? PRO C 395 ? VAL C 393 PRO C 395 
# 
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 GLU A 114 ? N GLU A 114 O LEU A 123 ? O LEU A 123 
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 MET A 420 ? N MET A 420 O VAL A 435 ? O VAL A 435 
AA4 6 7 O TYR A 438 ? O TYR A 438 N GLY A 386 ? N GLY A 386 
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 MET A 420 ? N MET A 420 O VAL A 435 ? O VAL A 435 
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 ALA B 56  ? N ALA B 56  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 GLY B 230 ? O GLY B 230 N CYS B 178 ? N CYS B 178 
AA7 4 5 N VAL B 182 ? N VAL B 182 O VAL B 190 ? O VAL B 190 
AA8 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AA8 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AA8 3 4 O ASN B 316 ? O ASN B 316 N ARG B 276 ? N ARG B 276 
AA8 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AA8 5 6 N LEU B 422 ? N LEU B 422 O VAL B 433 ? O VAL B 433 
AA8 6 7 O ILE B 436 ? O ILE B 436 N VAL B 388 ? N VAL B 388 
AA9 1 2 N PHE C 31  ? N PHE C 31  O ALA C 57  ? O ALA C 57  
AA9 2 3 N VAL C 58  ? N VAL C 58  O VAL C 103 ? O VAL C 103 
AA9 3 4 O VAL C 102 ? O VAL C 102 N TRP C 81  ? N TRP C 81  
AB1 1 2 N GLU C 114 ? N GLU C 114 O LEU C 123 ? O LEU C 123 
AB1 2 3 N VAL C 124 ? N VAL C 124 O MET C 229 ? O MET C 229 
AB1 3 4 O VAL C 225 ? O VAL C 225 N VAL C 183 ? N VAL C 183 
AB1 4 5 N VAL C 182 ? N VAL C 182 O VAL C 190 ? O VAL C 190 
AB2 1 2 N TRP C 145 ? N TRP C 145 O MET C 234 ? O MET C 234 
AB3 1 2 O TYR C 348 ? O TYR C 348 N LEU C 244 ? N LEU C 244 
AB3 2 3 N ILE C 245 ? N ILE C 245 O PHE C 317 ? O PHE C 317 
AB3 3 4 O ASN C 316 ? O ASN C 316 N ARG C 276 ? N ARG C 276 
AB3 4 5 N SER C 277 ? N SER C 277 O GLY C 421 ? O GLY C 421 
AB3 5 6 N LEU C 422 ? N LEU C 422 O VAL C 433 ? O VAL C 433 
AB3 6 7 O THR C 434 ? O THR C 434 N PHE C 390 ? N PHE C 390 
AB4 1 2 O TYR C 348 ? O TYR C 348 N LEU C 244 ? N LEU C 244 
AB4 2 3 N ILE C 245 ? N ILE C 245 O PHE C 317 ? O PHE C 317 
AB4 3 4 O ASN C 316 ? O ASN C 316 N ARG C 276 ? N ARG C 276 
AB4 4 5 N SER C 277 ? N SER C 277 O GLY C 421 ? O GLY C 421 
AB4 5 6 N LEU C 422 ? N LEU C 422 O VAL C 433 ? O VAL C 433 
AB4 6 7 O LEU C 430 ? O LEU C 430 N SER C 394 ? N SER C 394 
# 
_pdbx_entry_details.entry_id                   8S7P 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 191 ? ? CZ A ARG 191 ? ? NH2 A ARG 191 ? ? 117.28 120.30 -3.02 0.50 N 
2 1 NE A ARG 428 ? ? CZ A ARG 428 ? ? NH1 A ARG 428 ? ? 116.84 120.30 -3.46 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 33  ? ? 56.70   -127.74 
2  1 ALA A 90  ? ? 97.56   -4.93   
3  1 ILE A 112 ? ? -68.48  99.42   
4  1 TRP A 153 ? ? -48.84  164.02  
5  1 TYR A 170 ? ? -96.41  39.72   
6  1 CYS A 178 ? ? -166.19 108.18  
7  1 GLN A 220 ? ? 33.33   56.96   
8  1 ARG A 261 ? ? -47.62  -72.10  
9  1 ASP A 358 ? ? -176.08 144.89  
10 1 LEU A 373 ? ? -118.57 78.20   
11 1 ASN A 377 ? ? -143.42 -152.37 
12 1 TRP A 427 ? ? -141.83 -67.74  
13 1 TYR A 482 ? ? -95.24  58.50   
14 1 ALA A 507 ? ? 35.16   56.13   
15 1 SER A 511 ? ? 54.23   18.87   
16 1 GLU B 33  ? ? 55.47   -118.33 
17 1 LYS B 87  ? ? -99.03  35.57   
18 1 TYR B 170 ? ? -86.80  31.83   
19 1 CYS B 178 ? ? -160.67 115.90  
20 1 GLN B 220 ? ? 30.68   55.98   
21 1 ARG B 261 ? ? -41.51  -70.95  
22 1 ASN B 377 ? ? 179.16  -171.90 
23 1 ASN B 380 ? ? 56.83   18.09   
24 1 TRP B 381 ? ? -99.62  -61.88  
25 1 TRP B 427 ? ? -122.89 -62.61  
26 1 TYR B 482 ? ? -100.19 69.87   
27 1 ASN B 485 ? ? 70.18   47.58   
28 1 SER B 511 ? ? 47.77   27.78   
29 1 GLU C 7   ? ? -38.75  119.26  
30 1 THR C 32  ? ? -115.17 -148.27 
31 1 GLU C 33  ? ? 51.11   -113.62 
32 1 TYR C 43  ? ? -104.51 77.89   
33 1 GLU C 49  ? ? -87.38  47.03   
34 1 LYS C 87  ? ? -101.49 42.79   
35 1 ALA C 90  ? ? 95.49   4.91    
36 1 GLN C 220 ? ? 31.11   56.25   
37 1 ASN C 377 ? ? -172.14 -177.90 
38 1 ARG C 428 ? ? 74.82   -8.19   
39 1 ASP C 486 ? ? 39.45   56.28   
40 1 ALA C 507 ? ? 33.19   63.11   
41 1 SER C 511 ? ? 53.34   18.84   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 GLY B 515 ? ? LYS B 516 ? ? -149.12 
2 1 ASP C 147 ? ? VAL C 148 ? ? -148.57 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 411 ? ? 0.109 'SIDE CHAIN' 
2 1 ARG A 428 ? ? 0.172 'SIDE CHAIN' 
3 1 ARG B 71  ? ? 0.078 'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     704 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A LYS 520 ? A LYS 520 
3  1 Y 1 A ALA 521 ? A ALA 521 
4  1 Y 1 B MET 1   ? B MET 1   
5  1 Y 1 B LYS 520 ? B LYS 520 
6  1 Y 1 B ALA 521 ? B ALA 521 
7  1 Y 1 C MET 1   ? C MET 1   
8  1 Y 1 C ALA 2   ? C ALA 2   
9  1 Y 1 C LYS 520 ? C LYS 520 
10 1 Y 1 C ALA 521 ? C 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  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MET N      N N N 316 
MET CA     C N S 317 
MET C      C N N 318 
MET O      O N N 319 
MET CB     C N N 320 
MET CG     C N N 321 
MET SD     S N N 322 
MET CE     C N N 323 
MET OXT    O N N 324 
MET H      H N N 325 
MET H2     H N N 326 
MET HA     H N N 327 
MET HB2    H N N 328 
MET HB3    H N N 329 
MET HG2    H N N 330 
MET HG3    H N N 331 
MET HE1    H N N 332 
MET HE2    H N N 333 
MET HE3    H N N 334 
MET HXT    H N N 335 
PHE N      N N N 336 
PHE CA     C N S 337 
PHE C      C N N 338 
PHE O      O N N 339 
PHE CB     C N N 340 
PHE CG     C Y N 341 
PHE CD1    C Y N 342 
PHE CD2    C Y N 343 
PHE CE1    C Y N 344 
PHE CE2    C Y N 345 
PHE CZ     C Y N 346 
PHE OXT    O N N 347 
PHE H      H N N 348 
PHE H2     H N N 349 
PHE HA     H N N 350 
PHE HB2    H N N 351 
PHE HB3    H N N 352 
PHE HD1    H N N 353 
PHE HD2    H N N 354 
PHE HE1    H N N 355 
PHE HE2    H N N 356 
PHE HZ     H N N 357 
PHE HXT    H N N 358 
PRO N      N N N 359 
PRO CA     C N S 360 
PRO C      C N N 361 
PRO O      O N N 362 
PRO CB     C N N 363 
PRO CG     C N N 364 
PRO CD     C N N 365 
PRO OXT    O N N 366 
PRO H      H N N 367 
PRO HA     H N N 368 
PRO HB2    H N N 369 
PRO HB3    H N N 370 
PRO HG2    H N N 371 
PRO HG3    H N N 372 
PRO HD2    H N N 373 
PRO HD3    H N N 374 
PRO HXT    H N N 375 
SER N      N N N 376 
SER CA     C N S 377 
SER C      C N N 378 
SER O      O N N 379 
SER CB     C N N 380 
SER OG     O N N 381 
SER OXT    O N N 382 
SER H      H N N 383 
SER H2     H N N 384 
SER HA     H N N 385 
SER HB2    H N N 386 
SER HB3    H N N 387 
SER HG     H N N 388 
SER HXT    H N N 389 
THR N      N N N 390 
THR CA     C N S 391 
THR C      C N N 392 
THR O      O N N 393 
THR CB     C N R 394 
THR OG1    O N N 395 
THR CG2    C N N 396 
THR OXT    O N N 397 
THR H      H N N 398 
THR H2     H N N 399 
THR HA     H N N 400 
THR HB     H N N 401 
THR HG1    H N N 402 
THR HG21   H N N 403 
THR HG22   H N N 404 
THR HG23   H N N 405 
THR HXT    H N N 406 
TRP N      N N N 407 
TRP CA     C N S 408 
TRP C      C N N 409 
TRP O      O N N 410 
TRP CB     C N N 411 
TRP CG     C Y N 412 
TRP CD1    C Y N 413 
TRP CD2    C Y N 414 
TRP NE1    N Y N 415 
TRP CE2    C Y N 416 
TRP CE3    C Y N 417 
TRP CZ2    C Y N 418 
TRP CZ3    C Y N 419 
TRP CH2    C Y N 420 
TRP OXT    O N N 421 
TRP H      H N N 422 
TRP H2     H N N 423 
TRP HA     H N N 424 
TRP HB2    H N N 425 
TRP HB3    H N N 426 
TRP HD1    H N N 427 
TRP HE1    H N N 428 
TRP HE3    H N N 429 
TRP HZ2    H N N 430 
TRP HZ3    H N N 431 
TRP HH2    H N N 432 
TRP HXT    H N N 433 
TYR N      N N N 434 
TYR CA     C N S 435 
TYR C      C N N 436 
TYR O      O N N 437 
TYR CB     C N N 438 
TYR CG     C Y N 439 
TYR CD1    C Y N 440 
TYR CD2    C Y N 441 
TYR CE1    C Y N 442 
TYR CE2    C Y N 443 
TYR CZ     C Y N 444 
TYR OH     O N N 445 
TYR OXT    O N N 446 
TYR H      H N N 447 
TYR H2     H N N 448 
TYR HA     H N N 449 
TYR HB2    H N N 450 
TYR HB3    H N N 451 
TYR HD1    H N N 452 
TYR HD2    H N N 453 
TYR HE1    H N N 454 
TYR HE2    H N N 455 
TYR HH     H N N 456 
TYR HXT    H N N 457 
VAL N      N N N 458 
VAL CA     C N S 459 
VAL C      C N N 460 
VAL O      O N N 461 
VAL CB     C N N 462 
VAL CG1    C N N 463 
VAL CG2    C N N 464 
VAL OXT    O N N 465 
VAL H      H N N 466 
VAL H2     H N N 467 
VAL HA     H N N 468 
VAL HB     H N N 469 
VAL HG11   H N N 470 
VAL HG12   H N N 471 
VAL HG13   H N N 472 
VAL HG21   H N N 473 
VAL HG22   H N N 474 
VAL HG23   H N N 475 
VAL HXT    H N N 476 
# 
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 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_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                    8S7P 
_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]   0.011094 
_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]   0.006982 
_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]   0.003475 
_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 
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     . ALA A 1 2   ? -9.182  10.300  19.447  1.00 92.51  ? 2   ALA A N     1 
ATOM   2     C CA    . ALA A 1 2   ? -9.536  9.450   20.614  1.00 107.56 ? 2   ALA A CA    1 
ATOM   3     C C     . ALA A 1 2   ? -8.586  8.253   20.686  1.00 103.31 ? 2   ALA A C     1 
ATOM   4     O O     . ALA A 1 2   ? -8.147  7.745   19.654  1.00 89.64  ? 2   ALA A O     1 
ATOM   5     C CB    . ALA A 1 2   ? -10.983 9.006   20.531  1.00 103.63 ? 2   ALA A CB    1 
ATOM   6     N N     . ALA A 1 3   ? -8.280  7.808   21.912  1.00 89.99  ? 3   ALA A N     1 
ATOM   7     C CA    . ALA A 1 3   ? -7.206  6.849   22.135  1.00 101.71 ? 3   ALA A CA    1 
ATOM   8     C C     . ALA A 1 3   ? -7.675  5.422   21.865  1.00 87.92  ? 3   ALA A C     1 
ATOM   9     O O     . ALA A 1 3   ? -8.844  5.091   22.061  1.00 78.88  ? 3   ALA A O     1 
ATOM   10    C CB    . ALA A 1 3   ? -6.682  6.976   23.548  1.00 114.32 ? 3   ALA A CB    1 
ATOM   11    N N     . PRO A 1 4   ? -6.763  4.522   21.439  1.00 87.35  ? 4   PRO A N     1 
ATOM   12    C CA    . PRO A 1 4   ? -7.112  3.107   21.278  1.00 89.87  ? 4   PRO A CA    1 
ATOM   13    C C     . PRO A 1 4   ? -7.236  2.390   22.627  1.00 82.57  ? 4   PRO A C     1 
ATOM   14    O O     . PRO A 1 4   ? -6.944  2.978   23.663  1.00 77.22  ? 4   PRO A O     1 
ATOM   15    C CB    . PRO A 1 4   ? -5.967  2.556   20.403  1.00 95.99  ? 4   PRO A CB    1 
ATOM   16    C CG    . PRO A 1 4   ? -4.783  3.506   20.618  1.00 97.19  ? 4   PRO A CG    1 
ATOM   17    C CD    . PRO A 1 4   ? -5.369  4.831   21.072  1.00 89.81  ? 4   PRO A CD    1 
ATOM   18    N N     . LEU A 1 5   ? -7.693  1.129   22.609  1.00 81.59  ? 5   LEU A N     1 
ATOM   19    C CA    . LEU A 1 5   ? -7.578  0.242   23.761  1.00 80.90  ? 5   LEU A CA    1 
ATOM   20    C C     . LEU A 1 5   ? -6.118  -0.163  23.927  1.00 79.47  ? 5   LEU A C     1 
ATOM   21    O O     . LEU A 1 5   ? -5.391  -0.222  22.943  1.00 89.34  ? 5   LEU A O     1 
ATOM   22    C CB    . LEU A 1 5   ? -8.405  -1.035  23.550  1.00 86.40  ? 5   LEU A CB    1 
ATOM   23    C CG    . LEU A 1 5   ? -9.926  -0.891  23.502  1.00 88.79  ? 5   LEU A CG    1 
ATOM   24    C CD1   . LEU A 1 5   ? -10.578 -2.260  23.592  1.00 87.91  ? 5   LEU A CD1   1 
ATOM   25    C CD2   . LEU A 1 5   ? -10.448 0.023   24.607  1.00 93.30  ? 5   LEU A CD2   1 
ATOM   26    N N     . PRO A 1 6   ? -5.648  -0.515  25.143  1.00 82.22  ? 6   PRO A N     1 
ATOM   27    C CA    . PRO A 1 6   ? -4.326  -1.127  25.287  1.00 91.14  ? 6   PRO A CA    1 
ATOM   28    C C     . PRO A 1 6   ? -4.365  -2.587  24.826  1.00 88.78  ? 6   PRO A C     1 
ATOM   29    O O     . PRO A 1 6   ? -5.357  -3.278  25.050  1.00 93.53  ? 6   PRO A O     1 
ATOM   30    C CB    . PRO A 1 6   ? -4.007  -0.964  26.783  1.00 97.47  ? 6   PRO A CB    1 
ATOM   31    C CG    . PRO A 1 6   ? -5.363  -0.823  27.475  1.00 92.85  ? 6   PRO A CG    1 
ATOM   32    C CD    . PRO A 1 6   ? -6.341  -0.333  26.426  1.00 84.77  ? 6   PRO A CD    1 
ATOM   33    N N     . GLU A 1 7   ? -3.291  -3.040  24.166  1.00 79.30  ? 7   GLU A N     1 
ATOM   34    C CA    . GLU A 1 7   ? -3.189  -4.405  23.667  1.00 87.27  ? 7   GLU A CA    1 
ATOM   35    C C     . GLU A 1 7   ? -3.357  -5.426  24.804  1.00 83.50  ? 7   GLU A C     1 
ATOM   36    O O     . GLU A 1 7   ? -2.532  -5.493  25.715  1.00 85.69  ? 7   GLU A O     1 
ATOM   37    C CB    . GLU A 1 7   ? -1.843  -4.596  22.959  1.00 98.94  ? 7   GLU A CB    1 
ATOM   38    C CG    . GLU A 1 7   ? -1.562  -6.041  22.559  1.00 111.70 ? 7   GLU A CG    1 
ATOM   39    C CD    . GLU A 1 7   ? -0.228  -6.303  21.878  1.00 121.61 ? 7   GLU A CD    1 
ATOM   40    O OE1   . GLU A 1 7   ? -0.234  -6.829  20.738  1.00 112.06 ? 7   GLU A OE1   1 
ATOM   41    O OE2   . GLU A 1 7   ? 0.818   -5.997  22.494  1.00 114.94 ? 7   GLU A OE2   1 
ATOM   42    N N     . GLY A 1 8   ? -4.407  -6.258  24.709  1.00 79.39  ? 8   GLY A N     1 
ATOM   43    C CA    . GLY A 1 8   ? -4.713  -7.300  25.684  1.00 84.76  ? 8   GLY A CA    1 
ATOM   44    C C     . GLY A 1 8   ? -6.078  -7.088  26.349  1.00 84.17  ? 8   GLY A C     1 
ATOM   45    O O     . GLY A 1 8   ? -6.698  -8.020  26.869  1.00 75.78  ? 8   GLY A O     1 
ATOM   46    N N     . VAL A 1 9   ? -6.539  -5.836  26.325  1.00 85.43  ? 9   VAL A N     1 
ATOM   47    C CA    . VAL A 1 9   ? -7.767  -5.443  26.988  1.00 93.65  ? 9   VAL A CA    1 
ATOM   48    C C     . VAL A 1 9   ? -8.858  -5.324  25.930  1.00 93.42  ? 9   VAL A C     1 
ATOM   49    O O     . VAL A 1 9   ? -8.918  -4.314  25.225  1.00 84.62  ? 9   VAL A O     1 
ATOM   50    C CB    . VAL A 1 9   ? -7.561  -4.113  27.733  1.00 98.54  ? 9   VAL A CB    1 
ATOM   51    C CG1   . VAL A 1 9   ? -8.843  -3.597  28.362  1.00 103.03 ? 9   VAL A CG1   1 
ATOM   52    C CG2   . VAL A 1 9   ? -6.464  -4.235  28.776  1.00 102.77 ? 9   VAL A CG2   1 
ATOM   53    N N     . SER A 1 10  ? -9.699  -6.364  25.838  1.00 94.00  ? 10  SER A N     1 
ATOM   54    C CA    . SER A 1 10  ? -10.927 -6.321  25.055  1.00 83.60  ? 10  SER A CA    1 
ATOM   55    C C     . SER A 1 10  ? -11.788 -5.123  25.461  1.00 91.85  ? 10  SER A C     1 
ATOM   56    O O     . SER A 1 10  ? -11.602 -4.550  26.533  1.00 97.94  ? 10  SER A O     1 
ATOM   57    C CB    . SER A 1 10  ? -11.697 -7.622  25.172  1.00 80.74  ? 10  SER A CB    1 
ATOM   58    O OG    . SER A 1 10  ? -11.602 -8.194  26.470  1.00 72.22  ? 10  SER A OG    1 
ATOM   59    N N     . ALA A 1 11  ? -12.733 -4.752  24.583  1.00 99.63  ? 11  ALA A N     1 
ATOM   60    C CA    . ALA A 1 11  ? -13.612 -3.606  24.796  1.00 82.24  ? 11  ALA A CA    1 
ATOM   61    C C     . ALA A 1 11  ? -14.605 -3.890  25.923  1.00 67.86  ? 11  ALA A C     1 
ATOM   62    O O     . ALA A 1 11  ? -15.036 -2.948  26.589  1.00 68.28  ? 11  ALA A O     1 
ATOM   63    C CB    . ALA A 1 11  ? -14.321 -3.232  23.508  1.00 72.05  ? 11  ALA A CB    1 
ATOM   64    N N     . GLU A 1 12  ? -14.951 -5.174  26.124  1.00 71.98  ? 12  GLU A N     1 
ATOM   65    C CA    . GLU A 1 12  ? -15.862 -5.580  27.186  1.00 94.64  ? 12  GLU A CA    1 
ATOM   66    C C     . GLU A 1 12  ? -15.160 -5.392  28.529  1.00 99.23  ? 12  GLU A C     1 
ATOM   67    O O     . GLU A 1 12  ? -15.670 -4.681  29.394  1.00 95.10  ? 12  GLU A O     1 
ATOM   68    C CB    . GLU A 1 12  ? -16.332 -7.038  27.069  1.00 104.30 ? 12  GLU A CB    1 
ATOM   69    C CG    . GLU A 1 12  ? -16.937 -7.406  25.723  1.00 117.26 ? 12  GLU A CG    1 
ATOM   70    C CD    . GLU A 1 12  ? -15.932 -7.871  24.676  1.00 124.59 ? 12  GLU A CD    1 
ATOM   71    O OE1   . GLU A 1 12  ? -15.855 -7.238  23.598  1.00 103.07 ? 12  GLU A OE1   1 
ATOM   72    O OE2   . GLU A 1 12  ? -15.217 -8.868  24.938  1.00 117.89 ? 12  GLU A OE2   1 
ATOM   73    N N     . ALA A 1 13  ? -13.986 -6.026  28.680  1.00 89.78  ? 13  ALA A N     1 
ATOM   74    C CA    . ALA A 1 13  ? -13.158 -5.891  29.870  1.00 86.44  ? 13  ALA A CA    1 
ATOM   75    C C     . ALA A 1 13  ? -13.020 -4.419  30.282  1.00 81.20  ? 13  ALA A C     1 
ATOM   76    O O     . ALA A 1 13  ? -13.295 -4.078  31.429  1.00 81.60  ? 13  ALA A O     1 
ATOM   77    C CB    . ALA A 1 13  ? -11.810 -6.536  29.636  1.00 88.70  ? 13  ALA A CB    1 
ATOM   78    N N     . MET A 1 14  ? -12.625 -3.533  29.356  1.00 76.41  ? 14  MET A N     1 
ATOM   79    C CA    . MET A 1 14  ? -12.487 -2.113  29.670  1.00 74.75  ? 14  MET A CA    1 
ATOM   80    C C     . MET A 1 14  ? -13.805 -1.560  30.211  1.00 77.74  ? 14  MET A C     1 
ATOM   81    O O     . MET A 1 14  ? -13.855 -1.086  31.342  1.00 73.93  ? 14  MET A O     1 
ATOM   82    C CB    . MET A 1 14  ? -12.065 -1.298  28.443  1.00 75.83  ? 14  MET A CB    1 
ATOM   83    C CG    . MET A 1 14  ? -12.224 0.215   28.608  1.00 83.53  ? 14  MET A CG    1 
ATOM   84    S SD    . MET A 1 14  ? -11.252 0.911   29.997  1.00 79.80  ? 14  MET A SD    1 
ATOM   85    C CE    . MET A 1 14  ? -9.605  0.916   29.285  1.00 72.36  ? 14  MET A CE    1 
ATOM   86    N N     . SER A 1 15  ? -14.867 -1.647  29.398  1.00 90.23  ? 15  SER A N     1 
ATOM   87    C CA    . SER A 1 15  ? -16.165 -1.062  29.717  1.00 96.56  ? 15  SER A CA    1 
ATOM   88    C C     . SER A 1 15  ? -16.787 -1.648  30.997  1.00 81.70  ? 15  SER A C     1 
ATOM   89    O O     . SER A 1 15  ? -17.520 -0.935  31.683  1.00 71.71  ? 15  SER A O     1 
ATOM   90    C CB    . SER A 1 15  ? -17.105 -1.180  28.529  1.00 93.84  ? 15  SER A CB    1 
ATOM   91    O OG    . SER A 1 15  ? -17.198 -2.525  28.089  1.00 90.46  ? 15  SER A OG    1 
ATOM   92    N N     . SER A 1 16  ? -16.525 -2.932  31.311  1.00 66.61  ? 16  SER A N     1 
ATOM   93    C CA    . SER A 1 16  ? -16.964 -3.528  32.564  1.00 71.50  ? 16  SER A CA    1 
ATOM   94    C C     . SER A 1 16  ? -16.273 -2.810  33.719  1.00 91.16  ? 16  SER A C     1 
ATOM   95    O O     . SER A 1 16  ? -16.924 -2.312  34.638  1.00 97.36  ? 16  SER A O     1 
ATOM   96    C CB    . SER A 1 16  ? -16.665 -5.012  32.632  1.00 81.76  ? 16  SER A CB    1 
ATOM   97    O OG    . SER A 1 16  ? -17.125 -5.701  31.478  1.00 86.89  ? 16  SER A OG    1 
ATOM   98    N N     . ALA A 1 17  ? -14.938 -2.744  33.623  1.00 97.95  ? 17  ALA A N     1 
ATOM   99    C CA    . ALA A 1 17  ? -14.093 -2.083  34.605  1.00 83.71  ? 17  ALA A CA    1 
ATOM   100   C C     . ALA A 1 17  ? -14.458 -0.605  34.758  1.00 70.57  ? 17  ALA A C     1 
ATOM   101   O O     . ALA A 1 17  ? -14.407 -0.082  35.863  1.00 73.05  ? 17  ALA A O     1 
ATOM   102   C CB    . ALA A 1 17  ? -12.646 -2.256  34.219  1.00 86.46  ? 17  ALA A CB    1 
ATOM   103   N N     . LEU A 1 18  ? -14.836 0.082   33.676  1.00 72.06  ? 18  LEU A N     1 
ATOM   104   C CA    . LEU A 1 18  ? -15.214 1.491   33.795  1.00 83.76  ? 18  LEU A CA    1 
ATOM   105   C C     . LEU A 1 18  ? -16.530 1.650   34.562  1.00 90.70  ? 18  LEU A C     1 
ATOM   106   O O     . LEU A 1 18  ? -16.815 2.725   35.095  1.00 96.04  ? 18  LEU A O     1 
ATOM   107   C CB    . LEU A 1 18  ? -15.334 2.138   32.409  1.00 69.78  ? 18  LEU A CB    1 
ATOM   108   C CG    . LEU A 1 18  ? -14.045 2.660   31.781  1.00 76.04  ? 18  LEU A CG    1 
ATOM   109   C CD1   . LEU A 1 18  ? -14.355 3.503   30.548  1.00 87.77  ? 18  LEU A CD1   1 
ATOM   110   C CD2   . LEU A 1 18  ? -13.222 3.478   32.772  1.00 79.81  ? 18  LEU A CD2   1 
ATOM   111   N N     . ASP A 1 19  ? -17.344 0.590   34.585  1.00 90.26  ? 19  ASP A N     1 
ATOM   112   C CA    . ASP A 1 19  ? -18.617 0.633   35.280  1.00 100.73 ? 19  ASP A CA    1 
ATOM   113   C C     . ASP A 1 19  ? -18.390 0.277   36.752  1.00 93.40  ? 19  ASP A C     1 
ATOM   114   O O     . ASP A 1 19  ? -18.933 0.907   37.666  1.00 85.38  ? 19  ASP A O     1 
ATOM   115   C CB    . ASP A 1 19  ? -19.636 -0.250  34.557  1.00 101.52 ? 19  ASP A CB    1 
ATOM   116   C CG    . ASP A 1 19  ? -21.017 -0.166  35.176  1.00 104.17 ? 19  ASP A CG    1 
ATOM   117   O OD1   . ASP A 1 19  ? -21.517 0.984   35.363  1.00 78.29  ? 19  ASP A OD1   1 
ATOM   118   O OD2   . ASP A 1 19  ? -21.563 -1.245  35.496  1.00 98.96  ? 19  ASP A OD2   1 
ATOM   119   N N     . ARG A 1 20  ? -17.526 -0.709  36.984  1.00 87.39  ? 20  ARG A N     1 
ATOM   120   C CA    . ARG A 1 20  ? -17.187 -1.121  38.337  1.00 78.05  ? 20  ARG A CA    1 
ATOM   121   C C     . ARG A 1 20  ? -16.376 -0.026  39.054  1.00 67.26  ? 20  ARG A C     1 
ATOM   122   O O     . ARG A 1 20  ? -16.485 0.094   40.269  1.00 62.96  ? 20  ARG A O     1 
ATOM   123   C CB    . ARG A 1 20  ? -16.514 -2.497  38.250  1.00 78.05  ? 20  ARG A CB    1 
ATOM   124   C CG    . ARG A 1 20  ? -16.900 -3.454  39.367  1.00 80.74  ? 20  ARG A CG    1 
ATOM   125   C CD    . ARG A 1 20  ? -16.654 -4.901  38.991  1.00 75.22  ? 20  ARG A CD    1 
ATOM   126   N NE    . ARG A 1 20  ? -16.314 -5.681  40.173  1.00 77.57  ? 20  ARG A NE    1 
ATOM   127   C CZ    . ARG A 1 20  ? -16.100 -6.993  40.191  1.00 91.96  ? 20  ARG A CZ    1 
ATOM   128   N NH1   . ARG A 1 20  ? -16.337 -7.728  39.120  1.00 98.42  ? 20  ARG A NH1   1 
ATOM   129   N NH2   . ARG A 1 20  ? -15.671 -7.579  41.295  1.00 95.45  ? 20  ARG A NH2   1 
ATOM   130   N N     . PHE A 1 21  ? -15.569 0.769   38.320  1.00 64.25  ? 21  PHE A N     1 
ATOM   131   C CA    . PHE A 1 21  ? -14.940 1.976   38.853  1.00 69.03  ? 21  PHE A CA    1 
ATOM   132   C C     . PHE A 1 21  ? -16.008 3.016   39.207  1.00 69.20  ? 21  PHE A C     1 
ATOM   133   O O     . PHE A 1 21  ? -15.865 3.761   40.178  1.00 65.69  ? 21  PHE A O     1 
ATOM   134   C CB    . PHE A 1 21  ? -13.919 2.607   37.889  1.00 66.82  ? 21  PHE A CB    1 
ATOM   135   C CG    . PHE A 1 21  ? -12.705 1.786   37.493  1.00 74.11  ? 21  PHE A CG    1 
ATOM   136   C CD1   . PHE A 1 21  ? -12.285 0.669   38.215  1.00 76.40  ? 21  PHE A CD1   1 
ATOM   137   C CD2   . PHE A 1 21  ? -11.985 2.111   36.347  1.00 70.73  ? 21  PHE A CD2   1 
ATOM   138   C CE1   . PHE A 1 21  ? -11.178 -0.078  37.820  1.00 68.44  ? 21  PHE A CE1   1 
ATOM   139   C CE2   . PHE A 1 21  ? -10.892 1.352   35.947  1.00 65.81  ? 21  PHE A CE2   1 
ATOM   140   C CZ    . PHE A 1 21  ? -10.492 0.255   36.679  1.00 61.35  ? 21  PHE A CZ    1 
ATOM   141   N N     . ALA A 1 22  ? -17.074 3.073   38.409  1.00 72.35  ? 22  ALA A N     1 
ATOM   142   C CA    . ALA A 1 22  ? -18.156 4.014   38.646  1.00 78.47  ? 22  ALA A CA    1 
ATOM   143   C C     . ALA A 1 22  ? -18.904 3.683   39.942  1.00 75.16  ? 22  ALA A C     1 
ATOM   144   O O     . ALA A 1 22  ? -19.314 4.579   40.676  1.00 62.29  ? 22  ALA A O     1 
ATOM   145   C CB    . ALA A 1 22  ? -19.084 4.029   37.457  1.00 78.56  ? 22  ALA A CB    1 
ATOM   146   N N     . ARG A 1 23  ? -19.091 2.394   40.230  1.00 80.18  ? 23  ARG A N     1 
ATOM   147   C CA    . ARG A 1 23  ? -19.672 1.982   41.499  1.00 95.93  ? 23  ARG A CA    1 
ATOM   148   C C     . ARG A 1 23  ? -18.877 2.554   42.674  1.00 101.26 ? 23  ARG A C     1 
ATOM   149   O O     . ARG A 1 23  ? -19.453 3.077   43.634  1.00 96.33  ? 23  ARG A O     1 
ATOM   150   C CB    . ARG A 1 23  ? -19.668 0.457   41.651  1.00 110.00 ? 23  ARG A CB    1 
ATOM   151   C CG    . ARG A 1 23  ? -20.697 -0.273  40.804  1.00 124.81 ? 23  ARG A CG    1 
ATOM   152   C CD    . ARG A 1 23  ? -21.077 -1.610  41.423  1.00 131.36 ? 23  ARG A CD    1 
ATOM   153   N NE    . ARG A 1 23  ? -22.232 -2.186  40.751  1.00 133.43 ? 23  ARG A NE    1 
ATOM   154   C CZ    . ARG A 1 23  ? -23.438 -1.620  40.686  1.00 125.27 ? 23  ARG A CZ    1 
ATOM   155   N NH1   . ARG A 1 23  ? -23.711 -0.511  41.353  1.00 106.59 ? 23  ARG A NH1   1 
ATOM   156   N NH2   . ARG A 1 23  ? -24.384 -2.177  39.953  1.00 131.37 ? 23  ARG A NH2   1 
ATOM   157   N N     . ILE A 1 24  ? -17.545 2.424   42.575  1.00 91.61  ? 24  ILE A N     1 
ATOM   158   C CA    . ILE A 1 24  ? -16.653 2.544   43.714  1.00 69.14  ? 24  ILE A CA    1 
ATOM   159   C C     . ILE A 1 24  ? -16.502 4.016   44.088  1.00 67.37  ? 24  ILE A C     1 
ATOM   160   O O     . ILE A 1 24  ? -16.516 4.307   45.281  1.00 76.34  ? 24  ILE A O     1 
ATOM   161   C CB    . ILE A 1 24  ? -15.332 1.789   43.436  1.00 78.86  ? 24  ILE A CB    1 
ATOM   162   C CG1   . ILE A 1 24  ? -15.548 0.271   43.544  1.00 89.55  ? 24  ILE A CG1   1 
ATOM   163   C CG2   . ILE A 1 24  ? -14.195 2.252   44.338  1.00 74.56  ? 24  ILE A CG2   1 
ATOM   164   C CD1   . ILE A 1 24  ? -14.477 -0.586  42.877  1.00 93.16  ? 24  ILE A CD1   1 
ATOM   165   N N     . VAL A 1 25  ? -16.475 4.939   43.105  1.00 62.74  ? 25  VAL A N     1 
ATOM   166   C CA    . VAL A 1 25  ? -16.191 6.348   43.379  1.00 71.95  ? 25  VAL A CA    1 
ATOM   167   C C     . VAL A 1 25  ? -17.340 7.255   42.938  1.00 80.56  ? 25  VAL A C     1 
ATOM   168   O O     . VAL A 1 25  ? -17.193 8.483   42.962  1.00 73.06  ? 25  VAL A O     1 
ATOM   169   C CB    . VAL A 1 25  ? -14.885 6.817   42.702  1.00 78.47  ? 25  VAL A CB    1 
ATOM   170   C CG1   . VAL A 1 25  ? -13.693 5.936   43.066  1.00 79.38  ? 25  VAL A CG1   1 
ATOM   171   C CG2   . VAL A 1 25  ? -15.041 6.916   41.190  1.00 77.31  ? 25  VAL A CG2   1 
ATOM   172   N N     . GLY A 1 26  ? -18.466 6.653   42.525  1.00 99.49  ? 26  GLY A N     1 
ATOM   173   C CA    . GLY A 1 26  ? -19.573 7.389   41.929  1.00 94.80  ? 26  GLY A CA    1 
ATOM   174   C C     . GLY A 1 26  ? -19.474 7.418   40.408  1.00 83.28  ? 26  GLY A C     1 
ATOM   175   O O     . GLY A 1 26  ? -18.512 6.923   39.832  1.00 88.81  ? 26  GLY A O     1 
ATOM   176   N N     . ALA A 1 27  ? -20.486 7.995   39.762  1.00 87.56  ? 27  ALA A N     1 
ATOM   177   C CA    . ALA A 1 27  ? -20.474 8.136   38.317  1.00 88.27  ? 27  ALA A CA    1 
ATOM   178   C C     . ALA A 1 27  ? -20.173 9.582   37.925  1.00 81.59  ? 27  ALA A C     1 
ATOM   179   O O     . ALA A 1 27  ? -20.266 9.926   36.754  1.00 92.86  ? 27  ALA A O     1 
ATOM   180   C CB    . ALA A 1 27  ? -21.784 7.659   37.734  1.00 83.66  ? 27  ALA A CB    1 
ATOM   181   N N     . ASP A 1 28  ? -19.784 10.429  38.881  1.00 78.95  ? 28  ASP A N     1 
ATOM   182   C CA    . ASP A 1 28  ? -19.393 11.783  38.518  1.00 82.88  ? 28  ASP A CA    1 
ATOM   183   C C     . ASP A 1 28  ? -17.872 11.918  38.508  1.00 81.56  ? 28  ASP A C     1 
ATOM   184   O O     . ASP A 1 28  ? -17.369 12.927  38.020  1.00 86.14  ? 28  ASP A O     1 
ATOM   185   C CB    . ASP A 1 28  ? -20.046 12.842  39.414  1.00 86.89  ? 28  ASP A CB    1 
ATOM   186   C CG    . ASP A 1 28  ? -21.564 12.917  39.294  1.00 95.80  ? 28  ASP A CG    1 
ATOM   187   O OD1   . ASP A 1 28  ? -22.095 12.631  38.203  1.00 81.38  ? 28  ASP A OD1   1 
ATOM   188   O OD2   . ASP A 1 28  ? -22.210 13.299  40.287  1.00 95.71  ? 28  ASP A OD2   1 
ATOM   189   N N     . TRP A 1 29  ? -17.147 10.907  39.013  1.00 83.36  ? 29  TRP A N     1 
ATOM   190   C CA    . TRP A 1 29  ? -15.693 10.991  39.123  1.00 90.29  ? 29  TRP A CA    1 
ATOM   191   C C     . TRP A 1 29  ? -14.995 9.912   38.283  1.00 82.17  ? 29  TRP A C     1 
ATOM   192   O O     . TRP A 1 29  ? -13.975 9.373   38.705  1.00 72.63  ? 29  TRP A O     1 
ATOM   193   C CB    . TRP A 1 29  ? -15.282 10.905  40.601  1.00 85.17  ? 29  TRP A CB    1 
ATOM   194   C CG    . TRP A 1 29  ? -15.956 11.907  41.491  1.00 79.20  ? 29  TRP A CG    1 
ATOM   195   C CD1   . TRP A 1 29  ? -16.878 11.635  42.461  1.00 70.17  ? 29  TRP A CD1   1 
ATOM   196   C CD2   . TRP A 1 29  ? -15.750 13.338  41.526  1.00 66.17  ? 29  TRP A CD2   1 
ATOM   197   N NE1   . TRP A 1 29  ? -17.254 12.793  43.094  1.00 66.20  ? 29  TRP A NE1   1 
ATOM   198   C CE2   . TRP A 1 29  ? -16.585 13.854  42.545  1.00 64.60  ? 29  TRP A CE2   1 
ATOM   199   C CE3   . TRP A 1 29  ? -14.932 14.232  40.825  1.00 63.42  ? 29  TRP A CE3   1 
ATOM   200   C CZ2   . TRP A 1 29  ? -16.631 15.215  42.868  1.00 68.69  ? 29  TRP A CZ2   1 
ATOM   201   C CZ3   . TRP A 1 29  ? -14.968 15.576  41.148  1.00 66.79  ? 29  TRP A CZ3   1 
ATOM   202   C CH2   . TRP A 1 29  ? -15.809 16.061  42.154  1.00 68.32  ? 29  TRP A CH2   1 
ATOM   203   N N     . VAL A 1 30  ? -15.573 9.581   37.118  1.00 72.13  ? 30  VAL A N     1 
ATOM   204   C CA    . VAL A 1 30  ? -14.971 8.714   36.114  1.00 69.57  ? 30  VAL A CA    1 
ATOM   205   C C     . VAL A 1 30  ? -15.111 9.434   34.782  1.00 73.44  ? 30  VAL A C     1 
ATOM   206   O O     . VAL A 1 30  ? -16.228 9.614   34.323  1.00 85.06  ? 30  VAL A O     1 
ATOM   207   C CB    . VAL A 1 30  ? -15.649 7.331   36.034  1.00 67.41  ? 30  VAL A CB    1 
ATOM   208   C CG1   . VAL A 1 30  ? -15.233 6.553   34.789  1.00 63.90  ? 30  VAL A CG1   1 
ATOM   209   C CG2   . VAL A 1 30  ? -15.424 6.495   37.285  1.00 64.81  ? 30  VAL A CG2   1 
ATOM   210   N N     . PHE A 1 31  ? -13.989 9.838   34.175  1.00 89.94  ? 31  PHE A N     1 
ATOM   211   C CA    . PHE A 1 31  ? -14.009 10.786  33.069  1.00 99.48  ? 31  PHE A CA    1 
ATOM   212   C C     . PHE A 1 31  ? -13.625 10.103  31.756  1.00 111.22 ? 31  PHE A C     1 
ATOM   213   O O     . PHE A 1 31  ? -12.666 9.329   31.713  1.00 114.59 ? 31  PHE A O     1 
ATOM   214   C CB    . PHE A 1 31  ? -13.067 11.960  33.348  1.00 94.98  ? 31  PHE A CB    1 
ATOM   215   C CG    . PHE A 1 31  ? -13.344 12.705  34.630  1.00 98.89  ? 31  PHE A CG    1 
ATOM   216   C CD1   . PHE A 1 31  ? -14.591 13.268  34.871  1.00 93.85  ? 31  PHE A CD1   1 
ATOM   217   C CD2   . PHE A 1 31  ? -12.360 12.834  35.601  1.00 92.48  ? 31  PHE A CD2   1 
ATOM   218   C CE1   . PHE A 1 31  ? -14.836 13.965  36.043  1.00 90.16  ? 31  PHE A CE1   1 
ATOM   219   C CE2   . PHE A 1 31  ? -12.608 13.528  36.773  1.00 84.51  ? 31  PHE A CE2   1 
ATOM   220   C CZ    . PHE A 1 31  ? -13.842 14.098  36.990  1.00 92.90  ? 31  PHE A CZ    1 
ATOM   221   N N     . THR A 1 32  ? -14.383 10.424  30.692  1.00 109.31 ? 32  THR A N     1 
ATOM   222   C CA    . THR A 1 32  ? -14.089 9.995   29.331  1.00 103.57 ? 32  THR A CA    1 
ATOM   223   C C     . THR A 1 32  ? -14.297 11.189  28.387  1.00 113.93 ? 32  THR A C     1 
ATOM   224   O O     . THR A 1 32  ? -14.617 12.290  28.849  1.00 104.11 ? 32  THR A O     1 
ATOM   225   C CB    . THR A 1 32  ? -14.912 8.746   28.957  1.00 96.47  ? 32  THR A CB    1 
ATOM   226   O OG1   . THR A 1 32  ? -16.308 8.997   29.124  1.00 110.34 ? 32  THR A OG1   1 
ATOM   227   C CG2   . THR A 1 32  ? -14.582 7.524   29.785  1.00 83.77  ? 32  THR A CG2   1 
ATOM   228   N N     . GLU A 1 33  ? -14.024 10.961  27.085  1.00 113.79 ? 33  GLU A N     1 
ATOM   229   C CA    . GLU A 1 33  ? -14.431 11.808  25.965  1.00 111.21 ? 33  GLU A CA    1 
ATOM   230   C C     . GLU A 1 33  ? -13.930 13.249  26.132  1.00 113.06 ? 33  GLU A C     1 
ATOM   231   O O     . GLU A 1 33  ? -12.737 13.454  26.336  1.00 110.48 ? 33  GLU A O     1 
ATOM   232   C CB    . GLU A 1 33  ? -15.944 11.692  25.748  1.00 107.77 ? 33  GLU A CB    1 
ATOM   233   C CG    . GLU A 1 33  ? -16.379 10.324  25.241  1.00 105.57 ? 33  GLU A CG    1 
ATOM   234   C CD    . GLU A 1 33  ? -17.853 10.237  24.878  1.00 111.14 ? 33  GLU A CD    1 
ATOM   235   O OE1   . GLU A 1 33  ? -18.257 9.233   24.247  1.00 93.87  ? 33  GLU A OE1   1 
ATOM   236   O OE2   . GLU A 1 33  ? -18.603 11.174  25.234  1.00 102.53 ? 33  GLU A OE2   1 
ATOM   237   N N     . ASP A 1 34  ? -14.828 14.246  26.025  1.00 119.04 ? 34  ASP A N     1 
ATOM   238   C CA    . ASP A 1 34  ? -14.455 15.655  25.934  1.00 121.91 ? 34  ASP A CA    1 
ATOM   239   C C     . ASP A 1 34  ? -13.998 16.196  27.291  1.00 123.51 ? 34  ASP A C     1 
ATOM   240   O O     . ASP A 1 34  ? -13.664 17.377  27.396  1.00 101.77 ? 34  ASP A O     1 
ATOM   241   C CB    . ASP A 1 34  ? -15.618 16.509  25.410  1.00 109.74 ? 34  ASP A CB    1 
ATOM   242   N N     . LYS A 1 35  ? -14.010 15.332  28.321  1.00 123.12 ? 35  LYS A N     1 
ATOM   243   C CA    . LYS A 1 35  ? -13.536 15.667  29.655  1.00 112.61 ? 35  LYS A CA    1 
ATOM   244   C C     . LYS A 1 35  ? -12.098 15.180  29.855  1.00 111.10 ? 35  LYS A C     1 
ATOM   245   O O     . LYS A 1 35  ? -11.487 15.530  30.858  1.00 104.51 ? 35  LYS A O     1 
ATOM   246   C CB    . LYS A 1 35  ? -14.475 15.065  30.708  1.00 100.65 ? 35  LYS A CB    1 
ATOM   247   N N     . ILE A 1 36  ? -11.554 14.418  28.888  1.00 116.52 ? 36  ILE A N     1 
ATOM   248   C CA    . ILE A 1 36  ? -10.275 13.721  29.027  1.00 112.59 ? 36  ILE A CA    1 
ATOM   249   C C     . ILE A 1 36  ? -9.082  14.657  28.763  1.00 112.75 ? 36  ILE A C     1 
ATOM   250   O O     . ILE A 1 36  ? -7.968  14.377  29.211  1.00 108.29 ? 36  ILE A O     1 
ATOM   251   C CB    . ILE A 1 36  ? -10.236 12.475  28.106  1.00 100.56 ? 36  ILE A CB    1 
ATOM   252   C CG1   . ILE A 1 36  ? -9.295  11.383  28.624  1.00 96.22  ? 36  ILE A CG1   1 
ATOM   253   C CG2   . ILE A 1 36  ? -9.899  12.842  26.663  1.00 106.71 ? 36  ILE A CG2   1 
ATOM   254   C CD1   . ILE A 1 36  ? -9.930  10.416  29.591  1.00 100.94 ? 36  ILE A CD1   1 
ATOM   255   N N     . THR A 1 37  ? -9.292  15.768  28.038  1.00 110.42 ? 37  THR A N     1 
ATOM   256   C CA    . THR A 1 37  ? -8.186  16.448  27.375  1.00 109.30 ? 37  THR A CA    1 
ATOM   257   C C     . THR A 1 37  ? -7.287  17.194  28.363  1.00 108.32 ? 37  THR A C     1 
ATOM   258   O O     . THR A 1 37  ? -6.109  17.379  28.070  1.00 99.00  ? 37  THR A O     1 
ATOM   259   C CB    . THR A 1 37  ? -8.650  17.362  26.230  1.00 101.24 ? 37  THR A CB    1 
ATOM   260   O OG1   . THR A 1 37  ? -9.442  18.411  26.785  1.00 93.56  ? 37  THR A OG1   1 
ATOM   261   C CG2   . THR A 1 37  ? -9.408  16.616  25.149  1.00 95.01  ? 37  THR A CG2   1 
ATOM   262   N N     . PRO A 1 38  ? -7.754  17.654  29.548  1.00 114.99 ? 38  PRO A N     1 
ATOM   263   C CA    . PRO A 1 38  ? -6.829  18.226  30.529  1.00 115.56 ? 38  PRO A CA    1 
ATOM   264   C C     . PRO A 1 38  ? -5.774  17.251  31.071  1.00 110.01 ? 38  PRO A C     1 
ATOM   265   O O     . PRO A 1 38  ? -4.871  17.690  31.781  1.00 98.77  ? 38  PRO A O     1 
ATOM   266   C CB    . PRO A 1 38  ? -7.757  18.739  31.646  1.00 115.90 ? 38  PRO A CB    1 
ATOM   267   C CG    . PRO A 1 38  ? -9.101  18.899  30.972  1.00 115.02 ? 38  PRO A CG    1 
ATOM   268   C CD    . PRO A 1 38  ? -9.157  17.757  29.979  1.00 110.85 ? 38  PRO A CD    1 
ATOM   269   N N     . TYR A 1 39  ? -5.881  15.947  30.742  1.00 109.45 ? 39  TYR A N     1 
ATOM   270   C CA    . TYR A 1 39  ? -4.905  14.944  31.162  1.00 108.53 ? 39  TYR A CA    1 
ATOM   271   C C     . TYR A 1 39  ? -4.038  14.469  29.990  1.00 111.95 ? 39  TYR A C     1 
ATOM   272   O O     . TYR A 1 39  ? -3.296  13.493  30.127  1.00 90.16  ? 39  TYR A O     1 
ATOM   273   C CB    . TYR A 1 39  ? -5.579  13.729  31.816  1.00 107.75 ? 39  TYR A CB    1 
ATOM   274   C CG    . TYR A 1 39  ? -6.426  14.029  33.029  1.00 108.66 ? 39  TYR A CG    1 
ATOM   275   C CD1   . TYR A 1 39  ? -5.981  14.876  34.040  1.00 109.98 ? 39  TYR A CD1   1 
ATOM   276   C CD2   . TYR A 1 39  ? -7.677  13.454  33.168  1.00 95.35  ? 39  TYR A CD2   1 
ATOM   277   C CE1   . TYR A 1 39  ? -6.767  15.162  35.144  1.00 105.66 ? 39  TYR A CE1   1 
ATOM   278   C CE2   . TYR A 1 39  ? -8.470  13.719  34.270  1.00 102.75 ? 39  TYR A CE2   1 
ATOM   279   C CZ    . TYR A 1 39  ? -8.016  14.577  35.257  1.00 108.72 ? 39  TYR A CZ    1 
ATOM   280   O OH    . TYR A 1 39  ? -8.829  14.836  36.328  1.00 105.05 ? 39  TYR A OH    1 
ATOM   281   N N     . GLU A 1 40  ? -4.131  15.159  28.842  1.00 124.31 ? 40  GLU A N     1 
ATOM   282   C CA    . GLU A 1 40  ? -3.208  14.944  27.732  1.00 117.41 ? 40  GLU A CA    1 
ATOM   283   C C     . GLU A 1 40  ? -1.897  15.661  28.070  1.00 101.25 ? 40  GLU A C     1 
ATOM   284   O O     . GLU A 1 40  ? -1.854  16.514  28.961  1.00 81.48  ? 40  GLU A O     1 
ATOM   285   C CB    . GLU A 1 40  ? -3.778  15.436  26.386  1.00 111.39 ? 40  GLU A CB    1 
ATOM   286   C CG    . GLU A 1 40  ? -5.167  14.902  26.002  1.00 109.20 ? 40  GLU A CG    1 
ATOM   287   C CD    . GLU A 1 40  ? -5.286  13.522  25.358  1.00 103.62 ? 40  GLU A CD    1 
ATOM   288   O OE1   . GLU A 1 40  ? -4.243  12.860  25.154  1.00 108.38 ? 40  GLU A OE1   1 
ATOM   289   O OE2   . GLU A 1 40  ? -6.437  13.097  25.063  1.00 80.76  ? 40  GLU A OE2   1 
ATOM   290   N N     . ASP A 1 41  ? -0.826  15.291  27.357  1.00 94.47  ? 41  ASP A N     1 
ATOM   291   C CA    . ASP A 1 41  ? 0.445   15.991  27.442  1.00 91.76  ? 41  ASP A CA    1 
ATOM   292   C C     . ASP A 1 41  ? 0.227   17.385  26.853  1.00 85.66  ? 41  ASP A C     1 
ATOM   293   O O     . ASP A 1 41  ? -0.113  17.498  25.674  1.00 72.59  ? 41  ASP A O     1 
ATOM   294   C CB    . ASP A 1 41  ? 1.548   15.171  26.752  1.00 94.43  ? 41  ASP A CB    1 
ATOM   295   C CG    . ASP A 1 41  ? 2.969   15.730  26.800  1.00 93.18  ? 41  ASP A CG    1 
ATOM   296   O OD1   . ASP A 1 41  ? 3.230   16.698  27.559  1.00 72.79  ? 41  ASP A OD1   1 
ATOM   297   O OD2   . ASP A 1 41  ? 3.819   15.188  26.054  1.00 106.53 ? 41  ASP A OD2   1 
ATOM   298   N N     . PRO A 1 42  ? 0.362   18.484  27.644  1.00 88.37  ? 42  PRO A N     1 
ATOM   299   C CA    . PRO A 1 42  ? 0.201   19.840  27.101  1.00 89.00  ? 42  PRO A CA    1 
ATOM   300   C C     . PRO A 1 42  ? 1.304   20.304  26.136  1.00 83.33  ? 42  PRO A C     1 
ATOM   301   O O     . PRO A 1 42  ? 1.078   21.243  25.374  1.00 74.72  ? 42  PRO A O     1 
ATOM   302   C CB    . PRO A 1 42  ? 0.147   20.734  28.359  1.00 80.77  ? 42  PRO A CB    1 
ATOM   303   C CG    . PRO A 1 42  ? 0.888   19.951  29.427  1.00 77.96  ? 42  PRO A CG    1 
ATOM   304   C CD    . PRO A 1 42  ? 0.667   18.488  29.088  1.00 81.79  ? 42  PRO A CD    1 
ATOM   305   N N     . TYR A 1 43  ? 2.488   19.657  26.181  1.00 88.57  ? 43  TYR A N     1 
ATOM   306   C CA    . TYR A 1 43  ? 3.647   20.008  25.357  1.00 100.10 ? 43  TYR A CA    1 
ATOM   307   C C     . TYR A 1 43  ? 4.070   18.800  24.519  1.00 95.19  ? 43  TYR A C     1 
ATOM   308   O O     . TYR A 1 43  ? 5.139   18.226  24.743  1.00 95.44  ? 43  TYR A O     1 
ATOM   309   C CB    . TYR A 1 43  ? 4.856   20.445  26.203  1.00 97.06  ? 43  TYR A CB    1 
ATOM   310   C CG    . TYR A 1 43  ? 4.599   21.505  27.249  1.00 100.65 ? 43  TYR A CG    1 
ATOM   311   C CD1   . TYR A 1 43  ? 3.569   22.426  27.109  1.00 102.81 ? 43  TYR A CD1   1 
ATOM   312   C CD2   . TYR A 1 43  ? 5.368   21.565  28.405  1.00 89.41  ? 43  TYR A CD2   1 
ATOM   313   C CE1   . TYR A 1 43  ? 3.319   23.385  28.077  1.00 99.39  ? 43  TYR A CE1   1 
ATOM   314   C CE2   . TYR A 1 43  ? 5.130   22.518  29.381  1.00 86.15  ? 43  TYR A CE2   1 
ATOM   315   C CZ    . TYR A 1 43  ? 4.098   23.428  29.217  1.00 90.65  ? 43  TYR A CZ    1 
ATOM   316   O OH    . TYR A 1 43  ? 3.817   24.387  30.153  1.00 94.70  ? 43  TYR A OH    1 
ATOM   317   N N     . THR A 1 44  ? 3.229   18.427  23.547  1.00 86.16  ? 44  THR A N     1 
ATOM   318   C CA    . THR A 1 44  ? 3.409   17.180  22.821  1.00 91.21  ? 44  THR A CA    1 
ATOM   319   C C     . THR A 1 44  ? 4.714   17.259  22.019  1.00 81.80  ? 44  THR A C     1 
ATOM   320   O O     . THR A 1 44  ? 5.097   18.346  21.577  1.00 70.43  ? 44  THR A O     1 
ATOM   321   C CB    . THR A 1 44  ? 2.130   16.844  22.033  1.00 89.65  ? 44  THR A CB    1 
ATOM   322   O OG1   . THR A 1 44  ? 1.062   16.718  22.982  1.00 83.71  ? 44  THR A OG1   1 
ATOM   323   C CG2   . THR A 1 44  ? 2.229   15.565  21.226  1.00 81.74  ? 44  THR A CG2   1 
ATOM   324   N N     . ILE A 1 45  ? 5.410   16.105  21.910  1.00 67.19  ? 45  ILE A N     1 
ATOM   325   C CA    . ILE A 1 45  ? 6.641   15.966  21.142  1.00 69.89  ? 45  ILE A CA    1 
ATOM   326   C C     . ILE A 1 45  ? 6.418   15.030  19.945  1.00 66.09  ? 45  ILE A C     1 
ATOM   327   O O     . ILE A 1 45  ? 6.988   15.240  18.866  1.00 62.69  ? 45  ILE A O     1 
ATOM   328   C CB    . ILE A 1 45  ? 7.804   15.461  22.033  1.00 76.99  ? 45  ILE A CB    1 
ATOM   329   C CG1   . ILE A 1 45  ? 7.990   16.280  23.313  1.00 80.02  ? 45  ILE A CG1   1 
ATOM   330   C CG2   . ILE A 1 45  ? 9.106   15.392  21.244  1.00 75.59  ? 45  ILE A CG2   1 
ATOM   331   C CD1   . ILE A 1 45  ? 8.665   15.510  24.439  1.00 81.40  ? 45  ILE A CD1   1 
ATOM   332   N N     . SER A 1 46  ? 5.633   13.962  20.151  1.00 64.06  ? 46  SER A N     1 
ATOM   333   C CA    . SER A 1 46  ? 5.381   12.972  19.107  1.00 77.59  ? 46  SER A CA    1 
ATOM   334   C C     . SER A 1 46  ? 4.426   13.538  18.055  1.00 83.21  ? 46  SER A C     1 
ATOM   335   O O     . SER A 1 46  ? 3.424   14.174  18.394  1.00 90.87  ? 46  SER A O     1 
ATOM   336   C CB    . SER A 1 46  ? 4.831   11.676  19.681  1.00 78.94  ? 46  SER A CB    1 
ATOM   337   O OG    . SER A 1 46  ? 4.956   10.606  18.758  1.00 75.79  ? 46  SER A OG    1 
ATOM   338   N N     . ASN A 1 47  ? 4.745   13.270  16.781  1.00 81.18  ? 47  ASN A N     1 
ATOM   339   C CA    . ASN A 1 47  ? 3.912   13.665  15.656  1.00 76.63  ? 47  ASN A CA    1 
ATOM   340   C C     . ASN A 1 47  ? 2.880   12.576  15.340  1.00 78.45  ? 47  ASN A C     1 
ATOM   341   O O     . ASN A 1 47  ? 1.856   12.887  14.739  1.00 77.13  ? 47  ASN A O     1 
ATOM   342   C CB    . ASN A 1 47  ? 4.765   14.049  14.443  1.00 78.17  ? 47  ASN A CB    1 
ATOM   343   C CG    . ASN A 1 47  ? 5.372   15.432  14.571  1.00 74.92  ? 47  ASN A CG    1 
ATOM   344   O OD1   . ASN A 1 47  ? 4.689   16.367  14.989  1.00 72.92  ? 47  ASN A OD1   1 
ATOM   345   N ND2   . ASN A 1 47  ? 6.635   15.582  14.203  1.00 70.12  ? 47  ASN A ND2   1 
ATOM   346   N N     . ASP A 1 48  ? 3.149   11.319  15.737  1.00 78.98  ? 48  ASP A N     1 
ATOM   347   C CA    . ASP A 1 48  ? 2.124   10.285  15.837  1.00 89.33  ? 48  ASP A CA    1 
ATOM   348   C C     . ASP A 1 48  ? 1.216   10.612  17.023  1.00 85.69  ? 48  ASP A C     1 
ATOM   349   O O     . ASP A 1 48  ? 1.720   10.717  18.133  1.00 84.46  ? 48  ASP A O     1 
ATOM   350   C CB    . ASP A 1 48  ? 2.748   8.893   16.006  1.00 93.04  ? 48  ASP A CB    1 
ATOM   351   C CG    . ASP A 1 48  ? 1.776   7.764   16.331  1.00 90.78  ? 48  ASP A CG    1 
ATOM   352   O OD1   . ASP A 1 48  ? 0.570   8.040   16.501  1.00 84.27  ? 48  ASP A OD1   1 
ATOM   353   O OD2   . ASP A 1 48  ? 2.237   6.610   16.426  1.00 88.07  ? 48  ASP A OD2   1 
ATOM   354   N N     . GLU A 1 49  ? -0.108  10.727  16.780  1.00 90.05  ? 49  GLU A N     1 
ATOM   355   C CA    . GLU A 1 49  ? -1.066  11.299  17.727  1.00 95.47  ? 49  GLU A CA    1 
ATOM   356   C C     . GLU A 1 49  ? -1.786  10.219  18.544  1.00 88.02  ? 49  GLU A C     1 
ATOM   357   O O     . GLU A 1 49  ? -2.739  10.534  19.255  1.00 78.34  ? 49  GLU A O     1 
ATOM   358   C CB    . GLU A 1 49  ? -2.180  12.086  17.025  1.00 106.18 ? 49  GLU A CB    1 
ATOM   359   C CG    . GLU A 1 49  ? -1.730  13.106  15.992  1.00 111.02 ? 49  GLU A CG    1 
ATOM   360   C CD    . GLU A 1 49  ? -2.881  13.549  15.101  1.00 109.68 ? 49  GLU A CD    1 
ATOM   361   O OE1   . GLU A 1 49  ? -3.810  14.192  15.631  1.00 101.38 ? 49  GLU A OE1   1 
ATOM   362   O OE2   . GLU A 1 49  ? -2.876  13.201  13.893  1.00 95.98  ? 49  GLU A OE2   1 
ATOM   363   N N     . THR A 1 50  ? -1.351  8.955   18.436  1.00 83.39  ? 50  THR A N     1 
ATOM   364   C CA    . THR A 1 50  ? -1.915  7.874   19.228  1.00 88.69  ? 50  THR A CA    1 
ATOM   365   C C     . THR A 1 50  ? -0.934  7.386   20.301  1.00 90.34  ? 50  THR A C     1 
ATOM   366   O O     . THR A 1 50  ? -1.146  6.305   20.848  1.00 89.60  ? 50  THR A O     1 
ATOM   367   C CB    . THR A 1 50  ? -2.362  6.712   18.326  1.00 103.11 ? 50  THR A CB    1 
ATOM   368   O OG1   . THR A 1 50  ? -1.213  6.273   17.594  1.00 82.17  ? 50  THR A OG1   1 
ATOM   369   C CG2   . THR A 1 50  ? -3.511  7.078   17.403  1.00 101.85 ? 50  THR A CG2   1 
ATOM   370   N N     . GLU A 1 51  ? 0.117   8.172   20.612  1.00 87.15  ? 51  GLU A N     1 
ATOM   371   C CA    . GLU A 1 51  ? 1.075   7.857   21.669  1.00 87.86  ? 51  GLU A CA    1 
ATOM   372   C C     . GLU A 1 51  ? 0.859   8.801   22.858  1.00 88.40  ? 51  GLU A C     1 
ATOM   373   O O     . GLU A 1 51  ? 0.690   10.009  22.660  1.00 81.17  ? 51  GLU A O     1 
ATOM   374   C CB    . GLU A 1 51  ? 2.511   7.971   21.145  1.00 96.93  ? 51  GLU A CB    1 
ATOM   375   C CG    . GLU A 1 51  ? 2.936   6.830   20.226  1.00 99.77  ? 51  GLU A CG    1 
ATOM   376   C CD    . GLU A 1 51  ? 4.278   7.008   19.524  1.00 97.80  ? 51  GLU A CD    1 
ATOM   377   O OE1   . GLU A 1 51  ? 4.866   8.102   19.633  1.00 81.06  ? 51  GLU A OE1   1 
ATOM   378   O OE2   . GLU A 1 51  ? 4.731   6.056   18.847  1.00 98.48  ? 51  GLU A OE2   1 
ATOM   379   N N     . HIS A 1 52  ? 0.883   8.243   24.087  1.00 81.81  ? 52  HIS A N     1 
ATOM   380   C CA    . HIS A 1 52  ? 0.597   8.977   25.320  1.00 71.91  ? 52  HIS A CA    1 
ATOM   381   C C     . HIS A 1 52  ? -0.832  9.542   25.336  1.00 70.71  ? 52  HIS A C     1 
ATOM   382   O O     . HIS A 1 52  ? -1.034  10.756  25.495  1.00 54.09  ? 52  HIS A O     1 
ATOM   383   C CB    . HIS A 1 52  ? 1.646   10.069  25.541  1.00 71.78  ? 52  HIS A CB    1 
ATOM   384   C CG    . HIS A 1 52  ? 3.003   9.605   25.181  1.00 76.47  ? 52  HIS A CG    1 
ATOM   385   N ND1   . HIS A 1 52  ? 3.381   8.297   25.383  1.00 75.18  ? 52  HIS A ND1   1 
ATOM   386   C CD2   . HIS A 1 52  ? 4.034   10.217  24.589  1.00 81.73  ? 52  HIS A CD2   1 
ATOM   387   C CE1   . HIS A 1 52  ? 4.627   8.142   24.959  1.00 81.14  ? 52  HIS A CE1   1 
ATOM   388   N NE2   . HIS A 1 52  ? 5.039   9.291   24.465  1.00 83.91  ? 52  HIS A NE2   1 
ATOM   389   N N     . ARG A 1 53  ? -1.809  8.623   25.191  1.00 71.14  ? 53  ARG A N     1 
ATOM   390   C CA    . ARG A 1 53  ? -3.236  8.921   25.092  1.00 76.85  ? 53  ARG A CA    1 
ATOM   391   C C     . ARG A 1 53  ? -3.986  8.158   26.191  1.00 70.45  ? 53  ARG A C     1 
ATOM   392   O O     . ARG A 1 53  ? -4.094  6.932   26.162  1.00 62.12  ? 53  ARG A O     1 
ATOM   393   C CB    . ARG A 1 53  ? -3.784  8.536   23.706  1.00 80.74  ? 53  ARG A CB    1 
ATOM   394   C CG    . ARG A 1 53  ? -2.960  9.022   22.517  1.00 76.89  ? 53  ARG A CG    1 
ATOM   395   C CD    . ARG A 1 53  ? -2.812  10.538  22.445  1.00 80.50  ? 53  ARG A CD    1 
ATOM   396   N NE    . ARG A 1 53  ? -4.082  11.252  22.576  1.00 93.27  ? 53  ARG A NE    1 
ATOM   397   C CZ    . ARG A 1 53  ? -5.060  11.286  21.666  1.00 85.67  ? 53  ARG A CZ    1 
ATOM   398   N NH1   . ARG A 1 53  ? -4.841  10.886  20.425  1.00 78.50  ? 53  ARG A NH1   1 
ATOM   399   N NH2   . ARG A 1 53  ? -6.249  11.772  21.993  1.00 77.07  ? 53  ARG A NH2   1 
ATOM   400   N N     . PRO A 1 54  ? -4.473  8.838   27.252  1.00 71.07  ? 54  PRO A N     1 
ATOM   401   C CA    . PRO A 1 54  ? -5.227  8.149   28.298  1.00 66.17  ? 54  PRO A CA    1 
ATOM   402   C C     . PRO A 1 54  ? -6.634  7.765   27.842  1.00 67.34  ? 54  PRO A C     1 
ATOM   403   O O     . PRO A 1 54  ? -7.327  8.588   27.265  1.00 64.03  ? 54  PRO A O     1 
ATOM   404   C CB    . PRO A 1 54  ? -5.266  9.192   29.423  1.00 64.70  ? 54  PRO A CB    1 
ATOM   405   C CG    . PRO A 1 54  ? -5.165  10.537  28.724  1.00 63.58  ? 54  PRO A CG    1 
ATOM   406   C CD    . PRO A 1 54  ? -4.270  10.273  27.534  1.00 67.51  ? 54  PRO A CD    1 
ATOM   407   N N     . TYR A 1 55  ? -7.061  6.529   28.131  1.00 74.02  ? 55  TYR A N     1 
ATOM   408   C CA    . TYR A 1 55  ? -8.393  6.084   27.753  1.00 75.18  ? 55  TYR A CA    1 
ATOM   409   C C     . TYR A 1 55  ? -9.474  6.684   28.650  1.00 81.21  ? 55  TYR A C     1 
ATOM   410   O O     . TYR A 1 55  ? -10.606 6.833   28.203  1.00 76.00  ? 55  TYR A O     1 
ATOM   411   C CB    . TYR A 1 55  ? -8.523  4.563   27.813  1.00 73.71  ? 55  TYR A CB    1 
ATOM   412   C CG    . TYR A 1 55  ? -9.731  4.040   27.080  1.00 88.54  ? 55  TYR A CG    1 
ATOM   413   C CD1   . TYR A 1 55  ? -9.776  4.046   25.692  1.00 95.73  ? 55  TYR A CD1   1 
ATOM   414   C CD2   . TYR A 1 55  ? -10.844 3.572   27.760  1.00 99.40  ? 55  TYR A CD2   1 
ATOM   415   C CE1   . TYR A 1 55  ? -10.880 3.577   24.998  1.00 99.78  ? 55  TYR A CE1   1 
ATOM   416   C CE2   . TYR A 1 55  ? -11.956 3.094   27.080  1.00 110.99 ? 55  TYR A CE2   1 
ATOM   417   C CZ    . TYR A 1 55  ? -11.974 3.094   25.694  1.00 108.47 ? 55  TYR A CZ    1 
ATOM   418   O OH    . TYR A 1 55  ? -13.065 2.626   24.999  1.00 95.05  ? 55  TYR A OH    1 
ATOM   419   N N     . ALA A 1 56  ? -9.138  6.966   29.919  1.00 88.71  ? 56  ALA A N     1 
ATOM   420   C CA    . ALA A 1 56  ? -10.120 7.342   30.928  1.00 80.40  ? 56  ALA A CA    1 
ATOM   421   C C     . ALA A 1 56  ? -9.404  7.817   32.187  1.00 85.91  ? 56  ALA A C     1 
ATOM   422   O O     . ALA A 1 56  ? -8.189  7.669   32.293  1.00 86.43  ? 56  ALA A O     1 
ATOM   423   C CB    . ALA A 1 56  ? -11.006 6.170   31.241  1.00 81.83  ? 56  ALA A CB    1 
ATOM   424   N N     . ALA A 1 57  ? -10.169 8.350   33.150  1.00 80.97  ? 57  ALA A N     1 
ATOM   425   C CA    . ALA A 1 57  ? -9.581  8.943   34.339  1.00 74.91  ? 57  ALA A CA    1 
ATOM   426   C C     . ALA A 1 57  ? -10.539 8.842   35.527  1.00 80.38  ? 57  ALA A C     1 
ATOM   427   O O     . ALA A 1 57  ? -11.351 9.740   35.737  1.00 84.18  ? 57  ALA A O     1 
ATOM   428   C CB    . ALA A 1 57  ? -9.195  10.372  34.049  1.00 65.33  ? 57  ALA A CB    1 
ATOM   429   N N     . VAL A 1 58  ? -10.401 7.749   36.301  1.00 75.80  ? 58  VAL A N     1 
ATOM   430   C CA    . VAL A 1 58  ? -11.069 7.553   37.584  1.00 71.25  ? 58  VAL A CA    1 
ATOM   431   C C     . VAL A 1 58  ? -10.405 8.418   38.662  1.00 75.41  ? 58  VAL A C     1 
ATOM   432   O O     . VAL A 1 58  ? -9.198  8.664   38.633  1.00 73.17  ? 58  VAL A O     1 
ATOM   433   C CB    . VAL A 1 58  ? -11.106 6.059   37.980  1.00 71.21  ? 58  VAL A CB    1 
ATOM   434   C CG1   . VAL A 1 58  ? -9.729  5.472   38.226  1.00 75.34  ? 58  VAL A CG1   1 
ATOM   435   C CG2   . VAL A 1 58  ? -11.987 5.804   39.189  1.00 65.11  ? 58  VAL A CG2   1 
ATOM   436   N N     . ALA A 1 59  ? -11.216 8.909   39.614  1.00 69.22  ? 59  ALA A N     1 
ATOM   437   C CA    . ALA A 1 59  ? -10.754 9.919   40.551  1.00 62.17  ? 59  ALA A CA    1 
ATOM   438   C C     . ALA A 1 59  ? -11.299 9.615   41.941  1.00 63.04  ? 59  ALA A C     1 
ATOM   439   O O     . ALA A 1 59  ? -12.307 10.180  42.344  1.00 70.29  ? 59  ALA A O     1 
ATOM   440   C CB    . ALA A 1 59  ? -11.142 11.294  40.077  1.00 54.08  ? 59  ALA A CB    1 
ATOM   441   N N     . PRO A 1 60  ? -10.635 8.728   42.722  1.00 71.32  ? 60  PRO A N     1 
ATOM   442   C CA    . PRO A 1 60  ? -11.085 8.388   44.069  1.00 64.66  ? 60  PRO A CA    1 
ATOM   443   C C     . PRO A 1 60  ? -10.861 9.497   45.086  1.00 63.65  ? 60  PRO A C     1 
ATOM   444   O O     . PRO A 1 60  ? -10.265 10.532  44.776  1.00 76.86  ? 60  PRO A O     1 
ATOM   445   C CB    . PRO A 1 60  ? -10.264 7.147   44.432  1.00 62.09  ? 60  PRO A CB    1 
ATOM   446   C CG    . PRO A 1 60  ? -9.011  7.298   43.637  1.00 66.64  ? 60  PRO A CG    1 
ATOM   447   C CD    . PRO A 1 60  ? -9.435  7.963   42.346  1.00 70.82  ? 60  PRO A CD    1 
ATOM   448   N N     . ALA A 1 61  ? -11.392 9.248   46.288  1.00 67.32  ? 61  ALA A N     1 
ATOM   449   C CA    . ALA A 1 61  ? -11.526 10.253  47.333  1.00 76.14  ? 61  ALA A CA    1 
ATOM   450   C C     . ALA A 1 61  ? -10.979 9.757   48.671  1.00 66.29  ? 61  ALA A C     1 
ATOM   451   O O     . ALA A 1 61  ? -10.911 10.561  49.600  1.00 50.04  ? 61  ALA A O     1 
ATOM   452   C CB    . ALA A 1 61  ? -12.981 10.643  47.474  1.00 73.28  ? 61  ALA A CB    1 
ATOM   453   N N     . SER A 1 62  ? -10.603 8.462   48.722  1.00 61.41  ? 62  SER A N     1 
ATOM   454   C CA    . SER A 1 62  ? -10.171 7.765   49.920  1.00 61.66  ? 62  SER A CA    1 
ATOM   455   C C     . SER A 1 62  ? -9.212  6.629   49.546  1.00 62.96  ? 62  SER A C     1 
ATOM   456   O O     . SER A 1 62  ? -9.221  6.089   48.441  1.00 61.24  ? 62  SER A O     1 
ATOM   457   C CB    . SER A 1 62  ? -11.344 7.195   50.671  1.00 62.34  ? 62  SER A CB    1 
ATOM   458   O OG    . SER A 1 62  ? -11.463 5.780   50.435  1.00 64.25  ? 62  SER A OG    1 
ATOM   459   N N     . THR A 1 63  ? -8.435  6.195   50.526  1.00 56.81  ? 63  THR A N     1 
ATOM   460   C CA    . THR A 1 63  ? -7.484  5.129   50.316  1.00 57.65  ? 63  THR A CA    1 
ATOM   461   C C     . THR A 1 63  ? -8.242  3.857   49.974  1.00 60.84  ? 63  THR A C     1 
ATOM   462   O O     . THR A 1 63  ? -7.748  3.059   49.182  1.00 64.99  ? 63  THR A O     1 
ATOM   463   C CB    . THR A 1 63  ? -6.556  5.010   51.540  1.00 56.46  ? 63  THR A CB    1 
ATOM   464   O OG1   . THR A 1 63  ? -5.814  6.232   51.622  1.00 58.33  ? 63  THR A OG1   1 
ATOM   465   C CG2   . THR A 1 63  ? -5.615  3.825   51.489  1.00 46.10  ? 63  THR A CG2   1 
ATOM   466   N N     . GLU A 1 64  ? -9.420  3.653   50.591  1.00 76.32  ? 64  GLU A N     1 
ATOM   467   C CA    . GLU A 1 64  ? -10.144 2.389   50.451  1.00 69.29  ? 64  GLU A CA    1 
ATOM   468   C C     . GLU A 1 64  ? -10.600 2.209   48.992  1.00 57.97  ? 64  GLU A C     1 
ATOM   469   O O     . GLU A 1 64  ? -10.618 1.093   48.466  1.00 39.13  ? 64  GLU A O     1 
ATOM   470   C CB    . GLU A 1 64  ? -11.317 2.293   51.438  1.00 73.88  ? 64  GLU A CB    1 
ATOM   471   C CG    . GLU A 1 64  ? -11.633 0.848   51.839  1.00 95.94  ? 64  GLU A CG    1 
ATOM   472   C CD    . GLU A 1 64  ? -13.033 0.482   52.343  1.00 109.96 ? 64  GLU A CD    1 
ATOM   473   O OE1   . GLU A 1 64  ? -13.987 1.280   52.141  1.00 101.77 ? 64  GLU A OE1   1 
ATOM   474   O OE2   . GLU A 1 64  ? -13.179 -0.631  52.947  1.00 88.96  ? 64  GLU A OE2   1 
ATOM   475   N N     . GLU A 1 65  ? -10.959 3.318   48.332  1.00 48.22  ? 65  GLU A N     1 
ATOM   476   C CA    . GLU A 1 65  ? -11.440 3.278   46.966  1.00 57.62  ? 65  GLU A CA    1 
ATOM   477   C C     . GLU A 1 65  ? -10.278 2.867   46.077  1.00 59.56  ? 65  GLU A C     1 
ATOM   478   O O     . GLU A 1 65  ? -10.395 1.925   45.285  1.00 52.91  ? 65  GLU A O     1 
ATOM   479   C CB    . GLU A 1 65  ? -12.060 4.624   46.571  1.00 64.08  ? 65  GLU A CB    1 
ATOM   480   C CG    . GLU A 1 65  ? -13.455 4.812   47.155  1.00 62.71  ? 65  GLU A CG    1 
ATOM   481   C CD    . GLU A 1 65  ? -14.027 6.225   47.187  1.00 71.85  ? 65  GLU A CD    1 
ATOM   482   O OE1   . GLU A 1 65  ? -13.478 7.147   46.491  1.00 59.51  ? 65  GLU A OE1   1 
ATOM   483   O OE2   . GLU A 1 65  ? -15.028 6.401   47.941  1.00 68.38  ? 65  GLU A OE2   1 
ATOM   484   N N     . VAL A 1 66  ? -9.157  3.570   46.290  1.00 59.38  ? 66  VAL A N     1 
ATOM   485   C CA    . VAL A 1 66  ? -7.910  3.256   45.633  1.00 49.04  ? 66  VAL A CA    1 
ATOM   486   C C     . VAL A 1 66  ? -7.710  1.747   45.629  1.00 50.83  ? 66  VAL A C     1 
ATOM   487   O O     . VAL A 1 66  ? -7.337  1.186   44.589  1.00 63.09  ? 66  VAL A O     1 
ATOM   488   C CB    . VAL A 1 66  ? -6.722  3.990   46.272  1.00 50.19  ? 66  VAL A CB    1 
ATOM   489   C CG1   . VAL A 1 66  ? -5.419  3.504   45.671  1.00 54.99  ? 66  VAL A CG1   1 
ATOM   490   C CG2   . VAL A 1 66  ? -6.825  5.498   46.113  1.00 50.17  ? 66  VAL A CG2   1 
ATOM   491   N N     . GLN A 1 67  ? -7.960  1.110   46.780  1.00 52.85  ? 67  GLN A N     1 
ATOM   492   C CA    . GLN A 1 67  ? -7.718  -0.320  46.963  1.00 61.98  ? 67  GLN A CA    1 
ATOM   493   C C     . GLN A 1 67  ? -8.638  -1.134  46.050  1.00 67.88  ? 67  GLN A C     1 
ATOM   494   O O     . GLN A 1 67  ? -8.182  -2.080  45.399  1.00 70.72  ? 67  GLN A O     1 
ATOM   495   C CB    . GLN A 1 67  ? -7.883  -0.785  48.422  1.00 63.39  ? 67  GLN A CB    1 
ATOM   496   C CG    . GLN A 1 67  ? -7.083  0.008   49.453  1.00 65.13  ? 67  GLN A CG    1 
ATOM   497   C CD    . GLN A 1 67  ? -6.967  -0.635  50.824  1.00 65.33  ? 67  GLN A CD    1 
ATOM   498   O OE1   . GLN A 1 67  ? -7.038  0.027   51.860  1.00 63.76  ? 67  GLN A OE1   1 
ATOM   499   N NE2   . GLN A 1 67  ? -6.696  -1.927  50.857  1.00 57.21  ? 67  GLN A NE2   1 
ATOM   500   N N     . GLU A 1 68  ? -9.931  -0.775  46.003  1.00 68.83  ? 68  GLU A N     1 
ATOM   501   C CA    . GLU A 1 68  ? -10.885 -1.546  45.212  1.00 85.18  ? 68  GLU A CA    1 
ATOM   502   C C     . GLU A 1 68  ? -10.570 -1.344  43.724  1.00 73.65  ? 68  GLU A C     1 
ATOM   503   O O     . GLU A 1 68  ? -10.358 -2.312  42.988  1.00 65.05  ? 68  GLU A O     1 
ATOM   504   C CB    . GLU A 1 68  ? -12.332 -1.208  45.611  1.00 92.82  ? 68  GLU A CB    1 
ATOM   505   C CG    . GLU A 1 68  ? -12.769 -1.810  46.951  1.00 100.40 ? 68  GLU A CG    1 
ATOM   506   C CD    . GLU A 1 68  ? -13.181 -3.282  46.954  1.00 105.60 ? 68  GLU A CD    1 
ATOM   507   O OE1   . GLU A 1 68  ? -12.559 -4.088  46.216  1.00 97.97  ? 68  GLU A OE1   1 
ATOM   508   O OE2   . GLU A 1 68  ? -14.110 -3.637  47.727  1.00 91.89  ? 68  GLU A OE2   1 
ATOM   509   N N     . ILE A 1 69  ? -10.480 -0.076  43.299  1.00 61.12  ? 69  ILE A N     1 
ATOM   510   C CA    . ILE A 1 69  ? -10.028 0.241   41.956  1.00 62.45  ? 69  ILE A CA    1 
ATOM   511   C C     . ILE A 1 69  ? -8.944  -0.747  41.538  1.00 61.99  ? 69  ILE A C     1 
ATOM   512   O O     . ILE A 1 69  ? -9.066  -1.376  40.494  1.00 68.74  ? 69  ILE A O     1 
ATOM   513   C CB    . ILE A 1 69  ? -9.504  1.684   41.851  1.00 65.61  ? 69  ILE A CB    1 
ATOM   514   C CG1   . ILE A 1 69  ? -10.585 2.717   42.181  1.00 60.59  ? 69  ILE A CG1   1 
ATOM   515   C CG2   . ILE A 1 69  ? -8.911  1.898   40.462  1.00 65.63  ? 69  ILE A CG2   1 
ATOM   516   C CD1   . ILE A 1 69  ? -10.090 4.142   42.265  1.00 60.34  ? 69  ILE A CD1   1 
ATOM   517   N N     . VAL A 1 70  ? -7.905  -0.871  42.375  1.00 53.01  ? 70  VAL A N     1 
ATOM   518   C CA    . VAL A 1 70  ? -6.722  -1.652  42.059  1.00 53.54  ? 70  VAL A CA    1 
ATOM   519   C C     . VAL A 1 70  ? -7.125  -3.130  42.003  1.00 58.13  ? 70  VAL A C     1 
ATOM   520   O O     . VAL A 1 70  ? -6.593  -3.906  41.201  1.00 65.30  ? 70  VAL A O     1 
ATOM   521   C CB    . VAL A 1 70  ? -5.568  -1.346  43.067  1.00 52.88  ? 70  VAL A CB    1 
ATOM   522   C CG1   . VAL A 1 70  ? -4.376  -2.292  42.960  1.00 44.68  ? 70  VAL A CG1   1 
ATOM   523   C CG2   . VAL A 1 70  ? -5.059  0.091   42.984  1.00 47.15  ? 70  VAL A CG2   1 
ATOM   524   N N     . ARG A 1 71  ? -8.065  -3.543  42.856  1.00 70.65  ? 71  ARG A N     1 
ATOM   525   C CA    . ARG A 1 71  ? -8.542  -4.921  42.820  1.00 75.91  ? 71  ARG A CA    1 
ATOM   526   C C     . ARG A 1 71  ? -9.328  -5.177  41.530  1.00 75.10  ? 71  ARG A C     1 
ATOM   527   O O     . ARG A 1 71  ? -9.205  -6.241  40.913  1.00 67.48  ? 71  ARG A O     1 
ATOM   528   C CB    . ARG A 1 71  ? -9.380  -5.248  44.059  1.00 75.24  ? 71  ARG A CB    1 
ATOM   529   C CG    . ARG A 1 71  ? -8.549  -5.446  45.318  1.00 86.30  ? 71  ARG A CG    1 
ATOM   530   C CD    . ARG A 1 71  ? -9.320  -6.200  46.384  1.00 91.21  ? 71  ARG A CD    1 
ATOM   531   N NE    . ARG A 1 71  ? -8.757  -6.011  47.711  1.00 88.31  ? 71  ARG A NE    1 
ATOM   532   C CZ    . ARG A 1 71  ? -9.125  -5.040  48.533  1.00 84.65  ? 71  ARG A CZ    1 
ATOM   533   N NH1   . ARG A 1 71  ? -9.911  -4.071  48.094  1.00 76.66  ? 71  ARG A NH1   1 
ATOM   534   N NH2   . ARG A 1 71  ? -8.673  -5.019  49.774  1.00 83.50  ? 71  ARG A NH2   1 
ATOM   535   N N     . VAL A 1 72  ? -10.114 -4.183  41.106  1.00 68.40  ? 72  VAL A N     1 
ATOM   536   C CA    . VAL A 1 72  ? -10.865 -4.290  39.863  1.00 81.56  ? 72  VAL A CA    1 
ATOM   537   C C     . VAL A 1 72  ? -9.910  -4.316  38.666  1.00 76.64  ? 72  VAL A C     1 
ATOM   538   O O     . VAL A 1 72  ? -10.066 -5.145  37.764  1.00 67.42  ? 72  VAL A O     1 
ATOM   539   C CB    . VAL A 1 72  ? -11.902 -3.156  39.753  1.00 79.10  ? 72  VAL A CB    1 
ATOM   540   C CG1   . VAL A 1 72  ? -12.488 -3.049  38.356  1.00 71.16  ? 72  VAL A CG1   1 
ATOM   541   C CG2   . VAL A 1 72  ? -12.996 -3.339  40.796  1.00 81.25  ? 72  VAL A CG2   1 
ATOM   542   N N     . ALA A 1 73  ? -8.953  -3.374  38.673  1.00 72.44  ? 73  ALA A N     1 
ATOM   543   C CA    . ALA A 1 73  ? -7.892  -3.305  37.687  1.00 67.20  ? 73  ALA A CA    1 
ATOM   544   C C     . ALA A 1 73  ? -7.252  -4.679  37.498  1.00 64.79  ? 73  ALA A C     1 
ATOM   545   O O     . ALA A 1 73  ? -6.989  -5.109  36.373  1.00 63.92  ? 73  ALA A O     1 
ATOM   546   C CB    . ALA A 1 73  ? -6.878  -2.289  38.124  1.00 70.67  ? 73  ALA A CB    1 
ATOM   547   N N     . ASN A 1 74  ? -7.011  -5.375  38.605  1.00 60.12  ? 74  ASN A N     1 
ATOM   548   C CA    . ASN A 1 74  ? -6.456  -6.714  38.536  1.00 63.81  ? 74  ASN A CA    1 
ATOM   549   C C     . ASN A 1 74  ? -7.409  -7.655  37.809  1.00 73.72  ? 74  ASN A C     1 
ATOM   550   O O     . ASN A 1 74  ? -6.990  -8.407  36.929  1.00 68.36  ? 74  ASN A O     1 
ATOM   551   C CB    . ASN A 1 74  ? -6.113  -7.244  39.927  1.00 60.53  ? 74  ASN A CB    1 
ATOM   552   C CG    . ASN A 1 74  ? -4.699  -6.873  40.292  1.00 64.57  ? 74  ASN A CG    1 
ATOM   553   O OD1   . ASN A 1 74  ? -3.759  -7.391  39.687  1.00 58.28  ? 74  ASN A OD1   1 
ATOM   554   N ND2   . ASN A 1 74  ? -4.550  -5.916  41.192  1.00 63.49  ? 74  ASN A ND2   1 
ATOM   555   N N     . GLU A 1 75  ? -8.690  -7.580  38.188  1.00 88.05  ? 75  GLU A N     1 
ATOM   556   C CA    . GLU A 1 75  ? -9.712  -8.524  37.760  1.00 90.07  ? 75  GLU A CA    1 
ATOM   557   C C     . GLU A 1 75  ? -9.841  -8.553  36.236  1.00 81.11  ? 75  GLU A C     1 
ATOM   558   O O     . GLU A 1 75  ? -9.953  -9.634  35.655  1.00 74.19  ? 75  GLU A O     1 
ATOM   559   C CB    . GLU A 1 75  ? -11.037 -8.142  38.421  1.00 98.93  ? 75  GLU A CB    1 
ATOM   560   C CG    . GLU A 1 75  ? -12.059 -9.258  38.429  1.00 98.93  ? 75  GLU A CG    1 
ATOM   561   C CD    . GLU A 1 75  ? -13.264 -8.961  39.300  1.00 96.37  ? 75  GLU A CD    1 
ATOM   562   O OE1   . GLU A 1 75  ? -14.229 -9.748  39.241  1.00 88.65  ? 75  GLU A OE1   1 
ATOM   563   O OE2   . GLU A 1 75  ? -13.232 -7.940  40.028  1.00 86.39  ? 75  GLU A OE2   1 
ATOM   564   N N     . PHE A 1 76  ? -9.790  -7.363  35.613  1.00 79.84  ? 76  PHE A N     1 
ATOM   565   C CA    . PHE A 1 76  ? -10.089 -7.189  34.200  1.00 83.86  ? 76  PHE A CA    1 
ATOM   566   C C     . PHE A 1 76  ? -8.841  -6.939  33.349  1.00 78.93  ? 76  PHE A C     1 
ATOM   567   O O     . PHE A 1 76  ? -8.957  -6.729  32.141  1.00 70.78  ? 76  PHE A O     1 
ATOM   568   C CB    . PHE A 1 76  ? -11.104 -6.056  34.071  1.00 86.85  ? 76  PHE A CB    1 
ATOM   569   C CG    . PHE A 1 76  ? -12.412 -6.356  34.758  1.00 96.16  ? 76  PHE A CG    1 
ATOM   570   C CD1   . PHE A 1 76  ? -13.074 -7.555  34.534  1.00 88.40  ? 76  PHE A CD1   1 
ATOM   571   C CD2   . PHE A 1 76  ? -12.992 -5.436  35.615  1.00 104.62 ? 76  PHE A CD2   1 
ATOM   572   C CE1   . PHE A 1 76  ? -14.277 -7.832  35.164  1.00 86.36  ? 76  PHE A CE1   1 
ATOM   573   C CE2   . PHE A 1 76  ? -14.205 -5.708  36.229  1.00 108.80 ? 76  PHE A CE2   1 
ATOM   574   C CZ    . PHE A 1 76  ? -14.844 -6.905  36.006  1.00 97.42  ? 76  PHE A CZ    1 
ATOM   575   N N     . GLY A 1 77  ? -7.655  -6.995  33.973  1.00 79.54  ? 77  GLY A N     1 
ATOM   576   C CA    . GLY A 1 77  ? -6.381  -6.889  33.274  1.00 63.96  ? 77  GLY A CA    1 
ATOM   577   C C     . GLY A 1 77  ? -6.121  -5.479  32.757  1.00 56.31  ? 77  GLY A C     1 
ATOM   578   O O     . GLY A 1 77  ? -5.348  -5.313  31.822  1.00 61.65  ? 77  GLY A O     1 
ATOM   579   N N     . VAL A 1 78  ? -6.757  -4.484  33.383  1.00 52.17  ? 78  VAL A N     1 
ATOM   580   C CA    . VAL A 1 78  ? -6.776  -3.113  32.895  1.00 56.62  ? 78  VAL A CA    1 
ATOM   581   C C     . VAL A 1 78  ? -5.728  -2.293  33.632  1.00 60.83  ? 78  VAL A C     1 
ATOM   582   O O     . VAL A 1 78  ? -5.773  -2.200  34.848  1.00 76.13  ? 78  VAL A O     1 
ATOM   583   C CB    . VAL A 1 78  ? -8.166  -2.500  33.125  1.00 56.44  ? 78  VAL A CB    1 
ATOM   584   C CG1   . VAL A 1 78  ? -8.195  -1.002  32.885  1.00 53.01  ? 78  VAL A CG1   1 
ATOM   585   C CG2   . VAL A 1 78  ? -9.207  -3.210  32.280  1.00 68.65  ? 78  VAL A CG2   1 
ATOM   586   N N     . PRO A 1 79  ? -4.780  -1.641  32.939  1.00 70.34  ? 79  PRO A N     1 
ATOM   587   C CA    . PRO A 1 79  ? -3.704  -0.923  33.622  1.00 70.01  ? 79  PRO A CA    1 
ATOM   588   C C     . PRO A 1 79  ? -4.074  0.504   34.019  1.00 59.48  ? 79  PRO A C     1 
ATOM   589   O O     . PRO A 1 79  ? -4.864  1.119   33.312  1.00 55.95  ? 79  PRO A O     1 
ATOM   590   C CB    . PRO A 1 79  ? -2.606  -0.968  32.550  1.00 73.90  ? 79  PRO A CB    1 
ATOM   591   C CG    . PRO A 1 79  ? -3.374  -0.847  31.242  1.00 78.17  ? 79  PRO A CG    1 
ATOM   592   C CD    . PRO A 1 79  ? -4.653  -1.618  31.474  1.00 79.58  ? 79  PRO A CD    1 
ATOM   593   N N     . LEU A 1 80  ? -3.464  0.993   35.127  1.00 59.67  ? 80  LEU A N     1 
ATOM   594   C CA    . LEU A 1 80  ? -3.702  2.306   35.727  1.00 56.38  ? 80  LEU A CA    1 
ATOM   595   C C     . LEU A 1 80  ? -2.429  3.154   35.709  1.00 54.32  ? 80  LEU A C     1 
ATOM   596   O O     . LEU A 1 80  ? -1.322  2.631   35.633  1.00 52.11  ? 80  LEU A O     1 
ATOM   597   C CB    . LEU A 1 80  ? -4.128  2.126   37.185  1.00 59.91  ? 80  LEU A CB    1 
ATOM   598   C CG    . LEU A 1 80  ? -5.389  1.298   37.430  1.00 68.79  ? 80  LEU A CG    1 
ATOM   599   C CD1   . LEU A 1 80  ? -5.656  1.166   38.921  1.00 68.51  ? 80  LEU A CD1   1 
ATOM   600   C CD2   . LEU A 1 80  ? -6.593  1.912   36.736  1.00 63.21  ? 80  LEU A CD2   1 
ATOM   601   N N     . TRP A 1 81  ? -2.587  4.474   35.842  1.00 53.18  ? 81  TRP A N     1 
ATOM   602   C CA    . TRP A 1 81  ? -1.451  5.372   35.791  1.00 53.17  ? 81  TRP A CA    1 
ATOM   603   C C     . TRP A 1 81  ? -1.629  6.468   36.824  1.00 53.91  ? 81  TRP A C     1 
ATOM   604   O O     . TRP A 1 81  ? -2.229  7.490   36.524  1.00 58.91  ? 81  TRP A O     1 
ATOM   605   C CB    . TRP A 1 81  ? -1.240  5.957   34.392  1.00 54.54  ? 81  TRP A CB    1 
ATOM   606   C CG    . TRP A 1 81  ? -0.056  6.870   34.295  1.00 52.74  ? 81  TRP A CG    1 
ATOM   607   C CD1   . TRP A 1 81  ? 0.008   8.185   34.653  1.00 56.65  ? 81  TRP A CD1   1 
ATOM   608   C CD2   . TRP A 1 81  ? 1.266   6.520   33.841  1.00 52.61  ? 81  TRP A CD2   1 
ATOM   609   N NE1   . TRP A 1 81  ? 1.267   8.686   34.429  1.00 59.27  ? 81  TRP A NE1   1 
ATOM   610   C CE2   . TRP A 1 81  ? 2.055   7.691   33.916  1.00 54.56  ? 81  TRP A CE2   1 
ATOM   611   C CE3   . TRP A 1 81  ? 1.843   5.347   33.346  1.00 55.61  ? 81  TRP A CE3   1 
ATOM   612   C CZ2   . TRP A 1 81  ? 3.393   7.713   33.532  1.00 62.15  ? 81  TRP A CZ2   1 
ATOM   613   C CZ3   . TRP A 1 81  ? 3.160   5.365   32.954  1.00 59.75  ? 81  TRP A CZ3   1 
ATOM   614   C CH2   . TRP A 1 81  ? 3.924   6.532   33.056  1.00 68.82  ? 81  TRP A CH2   1 
ATOM   615   N N     . PRO A 1 82  ? -1.056  6.295   38.036  1.00 52.66  ? 82  PRO A N     1 
ATOM   616   C CA    . PRO A 1 82  ? -1.279  7.206   39.147  1.00 50.91  ? 82  PRO A CA    1 
ATOM   617   C C     . PRO A 1 82  ? -0.584  8.536   38.973  1.00 54.42  ? 82  PRO A C     1 
ATOM   618   O O     . PRO A 1 82  ? 0.571   8.568   38.571  1.00 64.25  ? 82  PRO A O     1 
ATOM   619   C CB    . PRO A 1 82  ? -0.629  6.515   40.352  1.00 59.29  ? 82  PRO A CB    1 
ATOM   620   C CG    . PRO A 1 82  ? -0.447  5.077   39.913  1.00 62.63  ? 82  PRO A CG    1 
ATOM   621   C CD    . PRO A 1 82  ? -0.212  5.162   38.423  1.00 57.79  ? 82  PRO A CD    1 
ATOM   622   N N     . VAL A 1 83  ? -1.307  9.604   39.312  1.00 61.33  ? 83  VAL A N     1 
ATOM   623   C CA    . VAL A 1 83  ? -0.773  10.954  39.336  1.00 63.34  ? 83  VAL A CA    1 
ATOM   624   C C     . VAL A 1 83  ? -1.348  11.668  40.555  1.00 73.02  ? 83  VAL A C     1 
ATOM   625   O O     . VAL A 1 83  ? -2.531  11.538  40.882  1.00 79.59  ? 83  VAL A O     1 
ATOM   626   C CB    . VAL A 1 83  ? -1.113  11.718  38.045  1.00 76.04  ? 83  VAL A CB    1 
ATOM   627   C CG1   . VAL A 1 83  ? -1.260  10.772  36.857  1.00 79.66  ? 83  VAL A CG1   1 
ATOM   628   C CG2   . VAL A 1 83  ? -2.356  12.591  38.187  1.00 77.99  ? 83  VAL A CG2   1 
ATOM   629   N N     . SER A 1 84  ? -0.497  12.437  41.224  1.00 70.99  ? 84  SER A N     1 
ATOM   630   C CA    . SER A 1 84  ? -0.908  13.101  42.440  1.00 72.38  ? 84  SER A CA    1 
ATOM   631   C C     . SER A 1 84  ? -1.767  14.294  42.059  1.00 69.47  ? 84  SER A C     1 
ATOM   632   O O     . SER A 1 84  ? -2.860  14.443  42.573  1.00 67.20  ? 84  SER A O     1 
ATOM   633   C CB    . SER A 1 84  ? 0.279   13.475  43.290  1.00 67.12  ? 84  SER A CB    1 
ATOM   634   O OG    . SER A 1 84  ? 0.878   12.296  43.808  1.00 61.58  ? 84  SER A OG    1 
ATOM   635   N N     . ARG A 1 85  ? -1.264  15.127  41.151  1.00 71.16  ? 85  ARG A N     1 
ATOM   636   C CA    . ARG A 1 85  ? -2.017  16.281  40.681  1.00 76.60  ? 85  ARG A CA    1 
ATOM   637   C C     . ARG A 1 85  ? -1.926  16.424  39.164  1.00 82.07  ? 85  ARG A C     1 
ATOM   638   O O     . ARG A 1 85  ? -2.803  17.033  38.552  1.00 92.49  ? 85  ARG A O     1 
ATOM   639   C CB    . ARG A 1 85  ? -1.524  17.542  41.389  1.00 66.76  ? 85  ARG A CB    1 
ATOM   640   C CG    . ARG A 1 85  ? -2.276  17.816  42.679  1.00 70.72  ? 85  ARG A CG    1 
ATOM   641   C CD    . ARG A 1 85  ? -1.931  19.125  43.374  1.00 69.38  ? 85  ARG A CD    1 
ATOM   642   N NE    . ARG A 1 85  ? -1.618  20.215  42.463  1.00 77.28  ? 85  ARG A NE    1 
ATOM   643   C CZ    . ARG A 1 85  ? -2.374  21.292  42.265  1.00 83.88  ? 85  ARG A CZ    1 
ATOM   644   N NH1   . ARG A 1 85  ? -3.605  21.325  42.758  1.00 62.80  ? 85  ARG A NH1   1 
ATOM   645   N NH2   . ARG A 1 85  ? -1.894  22.306  41.549  1.00 80.74  ? 85  ARG A NH2   1 
ATOM   646   N N     . GLY A 1 86  ? -0.851  15.878  38.582  1.00 89.60  ? 86  GLY A N     1 
ATOM   647   C CA    . GLY A 1 86  ? -0.679  15.811  37.143  1.00 82.97  ? 86  GLY A CA    1 
ATOM   648   C C     . GLY A 1 86  ? -0.225  17.143  36.557  1.00 83.68  ? 86  GLY A C     1 
ATOM   649   O O     . GLY A 1 86  ? -0.529  17.415  35.394  1.00 97.53  ? 86  GLY A O     1 
ATOM   650   N N     . LYS A 1 87  ? 0.504   17.944  37.365  1.00 78.32  ? 87  LYS A N     1 
ATOM   651   C CA    . LYS A 1 87  ? 1.127   19.187  36.912  1.00 74.64  ? 87  LYS A CA    1 
ATOM   652   C C     . LYS A 1 87  ? 2.596   18.951  36.533  1.00 70.22  ? 87  LYS A C     1 
ATOM   653   O O     . LYS A 1 87  ? 3.404   19.889  36.572  1.00 65.08  ? 87  LYS A O     1 
ATOM   654   C CB    . LYS A 1 87  ? 1.037   20.292  37.976  1.00 74.07  ? 87  LYS A CB    1 
ATOM   655   C CG    . LYS A 1 87  ? -0.317  20.463  38.654  1.00 80.00  ? 87  LYS A CG    1 
ATOM   656   C CD    . LYS A 1 87  ? -1.487  20.885  37.758  1.00 81.21  ? 87  LYS A CD    1 
ATOM   657   C CE    . LYS A 1 87  ? -2.734  20.070  38.060  1.00 78.63  ? 87  LYS A CE    1 
ATOM   658   N NZ    . LYS A 1 87  ? -3.959  20.600  37.423  1.00 73.00  ? 87  LYS A NZ    1 
ATOM   659   N N     . ASN A 1 88  ? 2.910   17.710  36.106  1.00 64.78  ? 88  ASN A N     1 
ATOM   660   C CA    . ASN A 1 88  ? 4.257   17.287  35.764  1.00 68.77  ? 88  ASN A CA    1 
ATOM   661   C C     . ASN A 1 88  ? 4.599   17.751  34.343  1.00 67.26  ? 88  ASN A C     1 
ATOM   662   O O     . ASN A 1 88  ? 4.908   16.937  33.469  1.00 59.07  ? 88  ASN A O     1 
ATOM   663   C CB    . ASN A 1 88  ? 4.435   15.769  35.946  1.00 68.10  ? 88  ASN A CB    1 
ATOM   664   C CG    . ASN A 1 88  ? 5.882   15.333  36.166  1.00 72.16  ? 88  ASN A CG    1 
ATOM   665   O OD1   . ASN A 1 88  ? 6.776   16.140  36.467  1.00 53.93  ? 88  ASN A OD1   1 
ATOM   666   N ND2   . ASN A 1 88  ? 6.116   14.035  36.048  1.00 68.17  ? 88  ASN A ND2   1 
ATOM   667   N N     . PHE A 1 89  ? 4.610   19.076  34.149  1.00 66.54  ? 89  PHE A N     1 
ATOM   668   C CA    . PHE A 1 89  ? 4.856   19.676  32.847  1.00 76.03  ? 89  PHE A CA    1 
ATOM   669   C C     . PHE A 1 89  ? 6.353   19.567  32.508  1.00 76.88  ? 89  PHE A C     1 
ATOM   670   O O     . PHE A 1 89  ? 7.199   19.799  33.383  1.00 82.34  ? 89  PHE A O     1 
ATOM   671   C CB    . PHE A 1 89  ? 4.324   21.122  32.836  1.00 85.89  ? 89  PHE A CB    1 
ATOM   672   C CG    . PHE A 1 89  ? 2.865   21.336  33.195  1.00 89.54  ? 89  PHE A CG    1 
ATOM   673   C CD1   . PHE A 1 89  ? 1.871   20.444  32.803  1.00 97.59  ? 89  PHE A CD1   1 
ATOM   674   C CD2   . PHE A 1 89  ? 2.472   22.473  33.891  1.00 97.14  ? 89  PHE A CD2   1 
ATOM   675   C CE1   . PHE A 1 89  ? 0.539   20.658  33.143  1.00 97.50  ? 89  PHE A CE1   1 
ATOM   676   C CE2   . PHE A 1 89  ? 1.141   22.693  34.221  1.00 96.83  ? 89  PHE A CE2   1 
ATOM   677   C CZ    . PHE A 1 89  ? 0.174   21.785  33.848  1.00 96.06  ? 89  PHE A CZ    1 
ATOM   678   N N     . ALA A 1 90  ? 6.664   19.209  31.237  1.00 70.56  ? 90  ALA A N     1 
ATOM   679   C CA    . ALA A 1 90  ? 8.022   19.059  30.702  1.00 64.83  ? 90  ALA A CA    1 
ATOM   680   C C     . ALA A 1 90  ? 8.453   17.595  30.721  1.00 62.74  ? 90  ALA A C     1 
ATOM   681   O O     . ALA A 1 90  ? 9.539   17.255  30.217  1.00 57.79  ? 90  ALA A O     1 
ATOM   682   C CB    . ALA A 1 90  ? 9.038   19.888  31.453  1.00 66.34  ? 90  ALA A CB    1 
ATOM   683   N N     . TYR A 1 91  ? 7.562   16.779  31.309  1.00 60.36  ? 91  TYR A N     1 
ATOM   684   C CA    . TYR A 1 91  ? 7.784   15.378  31.610  1.00 64.09  ? 91  TYR A CA    1 
ATOM   685   C C     . TYR A 1 91  ? 6.600   14.559  31.101  1.00 57.77  ? 91  TYR A C     1 
ATOM   686   O O     . TYR A 1 91  ? 6.628   13.326  31.164  1.00 56.62  ? 91  TYR A O     1 
ATOM   687   C CB    . TYR A 1 91  ? 8.054   15.201  33.115  1.00 69.21  ? 91  TYR A CB    1 
ATOM   688   C CG    . TYR A 1 91  ? 9.312   15.881  33.621  1.00 75.70  ? 91  TYR A CG    1 
ATOM   689   C CD1   . TYR A 1 91  ? 10.585  15.432  33.274  1.00 74.74  ? 91  TYR A CD1   1 
ATOM   690   C CD2   . TYR A 1 91  ? 9.238   17.005  34.428  1.00 69.11  ? 91  TYR A CD2   1 
ATOM   691   C CE1   . TYR A 1 91  ? 11.738  16.071  33.718  1.00 69.83  ? 91  TYR A CE1   1 
ATOM   692   C CE2   . TYR A 1 91  ? 10.379  17.649  34.883  1.00 66.82  ? 91  TYR A CE2   1 
ATOM   693   C CZ    . TYR A 1 91  ? 11.637  17.184  34.535  1.00 63.07  ? 91  TYR A CZ    1 
ATOM   694   O OH    . TYR A 1 91  ? 12.751  17.846  35.017  1.00 54.18  ? 91  TYR A OH    1 
ATOM   695   N N     . GLY A 1 92  ? 5.597   15.255  30.539  1.00 65.90  ? 92  GLY A N     1 
ATOM   696   C CA    . GLY A 1 92  ? 4.403   14.627  29.990  1.00 61.11  ? 92  GLY A CA    1 
ATOM   697   C C     . GLY A 1 92  ? 3.117   15.116  30.651  1.00 62.46  ? 92  GLY A C     1 
ATOM   698   O O     . GLY A 1 92  ? 2.029   14.742  30.226  1.00 57.98  ? 92  GLY A O     1 
ATOM   699   N N     . GLY A 1 93  ? 3.234   15.940  31.698  1.00 66.24  ? 93  GLY A N     1 
ATOM   700   C CA    . GLY A 1 93  ? 2.078   16.292  32.509  1.00 68.94  ? 93  GLY A CA    1 
ATOM   701   C C     . GLY A 1 93  ? 1.406   15.049  33.094  1.00 69.62  ? 93  GLY A C     1 
ATOM   702   O O     . GLY A 1 93  ? 2.037   14.256  33.803  1.00 67.16  ? 93  GLY A O     1 
ATOM   703   N N     . ALA A 1 94  ? 0.139   14.854  32.716  1.00 64.76  ? 94  ALA A N     1 
ATOM   704   C CA    . ALA A 1 94  ? -0.697  13.824  33.302  1.00 62.94  ? 94  ALA A CA    1 
ATOM   705   C C     . ALA A 1 94  ? -0.639  12.518  32.506  1.00 61.06  ? 94  ALA A C     1 
ATOM   706   O O     . ALA A 1 94  ? -1.030  11.456  32.997  1.00 52.90  ? 94  ALA A O     1 
ATOM   707   C CB    . ALA A 1 94  ? -2.103  14.355  33.379  1.00 70.38  ? 94  ALA A CB    1 
ATOM   708   N N     . ALA A 1 95  ? -0.140  12.585  31.269  1.00 67.21  ? 95  ALA A N     1 
ATOM   709   C CA    . ALA A 1 95  ? -0.345  11.500  30.321  1.00 64.94  ? 95  ALA A CA    1 
ATOM   710   C C     . ALA A 1 95  ? 0.514   10.283  30.656  1.00 55.20  ? 95  ALA A C     1 
ATOM   711   O O     . ALA A 1 95  ? 1.640   10.408  31.132  1.00 72.88  ? 95  ALA A O     1 
ATOM   712   C CB    . ALA A 1 95  ? -0.079  11.990  28.913  1.00 67.29  ? 95  ALA A CB    1 
ATOM   713   N N     . PRO A 1 96  ? 0.033   9.064   30.335  1.00 58.56  ? 96  PRO A N     1 
ATOM   714   C CA    . PRO A 1 96  ? 0.850   7.848   30.427  1.00 64.24  ? 96  PRO A CA    1 
ATOM   715   C C     . PRO A 1 96  ? 1.858   7.612   29.294  1.00 72.48  ? 96  PRO A C     1 
ATOM   716   O O     . PRO A 1 96  ? 1.763   8.213   28.225  1.00 74.97  ? 96  PRO A O     1 
ATOM   717   C CB    . PRO A 1 96  ? -0.248  6.780   30.328  1.00 64.34  ? 96  PRO A CB    1 
ATOM   718   C CG    . PRO A 1 96  ? -1.204  7.362   29.321  1.00 58.45  ? 96  PRO A CG    1 
ATOM   719   C CD    . PRO A 1 96  ? -1.301  8.802   29.769  1.00 61.85  ? 96  PRO A CD    1 
ATOM   720   N N     . VAL A 1 97  ? 2.808   6.698   29.532  1.00 78.91  ? 97  VAL A N     1 
ATOM   721   C CA    . VAL A 1 97  ? 3.778   6.262   28.533  1.00 71.40  ? 97  VAL A CA    1 
ATOM   722   C C     . VAL A 1 97  ? 3.036   5.439   27.496  1.00 71.87  ? 97  VAL A C     1 
ATOM   723   O O     . VAL A 1 97  ? 3.212   5.585   26.282  1.00 67.30  ? 97  VAL A O     1 
ATOM   724   C CB    . VAL A 1 97  ? 4.884   5.404   29.178  1.00 74.73  ? 97  VAL A CB    1 
ATOM   725   C CG1   . VAL A 1 97  ? 5.599   4.518   28.168  1.00 70.44  ? 97  VAL A CG1   1 
ATOM   726   C CG2   . VAL A 1 97  ? 5.871   6.252   29.972  1.00 79.57  ? 97  VAL A CG2   1 
ATOM   727   N N     . MET A 1 98  ? 2.226   4.532   28.030  1.00 68.49  ? 98  MET A N     1 
ATOM   728   C CA    . MET A 1 98  ? 1.443   3.674   27.178  1.00 73.06  ? 98  MET A CA    1 
ATOM   729   C C     . MET A 1 98  ? 0.126   4.393   26.889  1.00 83.96  ? 98  MET A C     1 
ATOM   730   O O     . MET A 1 98  ? -0.368  5.149   27.729  1.00 77.62  ? 98  MET A O     1 
ATOM   731   C CB    . MET A 1 98  ? 1.228   2.329   27.872  1.00 64.05  ? 98  MET A CB    1 
ATOM   732   C CG    . MET A 1 98  ? 0.844   1.228   26.930  1.00 56.82  ? 98  MET A CG    1 
ATOM   733   S SD    . MET A 1 98  ? 0.320   -0.244  27.824  1.00 70.15  ? 98  MET A SD    1 
ATOM   734   C CE    . MET A 1 98  ? 1.308   -1.463  26.948  1.00 69.27  ? 98  MET A CE    1 
ATOM   735   N N     . SER A 1 99  ? -0.374  4.219   25.654  1.00 88.07  ? 99  SER A N     1 
ATOM   736   C CA    . SER A 1 99  ? -1.731  4.607   25.289  1.00 81.94  ? 99  SER A CA    1 
ATOM   737   C C     . SER A 1 99  ? -2.722  3.658   25.953  1.00 66.85  ? 99  SER A C     1 
ATOM   738   O O     . SER A 1 99  ? -2.456  2.463   26.057  1.00 69.38  ? 99  SER A O     1 
ATOM   739   C CB    . SER A 1 99  ? -1.938  4.630   23.779  1.00 78.75  ? 99  SER A CB    1 
ATOM   740   O OG    . SER A 1 99  ? -1.781  5.944   23.249  1.00 79.04  ? 99  SER A OG    1 
ATOM   741   N N     . GLY A 1 100 ? -3.858  4.203   26.395  1.00 65.28  ? 100 GLY A N     1 
ATOM   742   C CA    . GLY A 1 100 ? -4.992  3.381   26.791  1.00 73.53  ? 100 GLY A CA    1 
ATOM   743   C C     . GLY A 1 100 ? -5.090  3.205   28.302  1.00 73.14  ? 100 GLY A C     1 
ATOM   744   O O     . GLY A 1 100 ? -6.156  2.940   28.844  1.00 85.54  ? 100 GLY A O     1 
ATOM   745   N N     . THR A 1 101 ? -3.971  3.375   28.995  1.00 74.25  ? 101 THR A N     1 
ATOM   746   C CA    . THR A 1 101 ? -3.989  3.163   30.425  1.00 72.30  ? 101 THR A CA    1 
ATOM   747   C C     . THR A 1 101 ? -4.971  4.169   31.005  1.00 73.99  ? 101 THR A C     1 
ATOM   748   O O     . THR A 1 101 ? -5.062  5.293   30.496  1.00 58.48  ? 101 THR A O     1 
ATOM   749   C CB    . THR A 1 101 ? -2.607  3.326   31.065  1.00 68.09  ? 101 THR A CB    1 
ATOM   750   O OG1   . THR A 1 101 ? -2.522  4.689   31.474  1.00 76.03  ? 101 THR A OG1   1 
ATOM   751   C CG2   . THR A 1 101 ? -1.462  2.961   30.145  1.00 68.73  ? 101 THR A CG2   1 
ATOM   752   N N     . VAL A 1 102 ? -5.664  3.726   32.070  1.00 71.94  ? 102 VAL A N     1 
ATOM   753   C CA    . VAL A 1 102 ? -6.606  4.525   32.841  1.00 66.00  ? 102 VAL A CA    1 
ATOM   754   C C     . VAL A 1 102 ? -5.836  5.361   33.859  1.00 60.36  ? 102 VAL A C     1 
ATOM   755   O O     . VAL A 1 102 ? -5.269  4.790   34.783  1.00 70.34  ? 102 VAL A O     1 
ATOM   756   C CB    . VAL A 1 102 ? -7.608  3.605   33.565  1.00 71.05  ? 102 VAL A CB    1 
ATOM   757   C CG1   . VAL A 1 102 ? -8.632  4.403   34.369  1.00 75.61  ? 102 VAL A CG1   1 
ATOM   758   C CG2   . VAL A 1 102 ? -8.289  2.621   32.613  1.00 64.07  ? 102 VAL A CG2   1 
ATOM   759   N N     . VAL A 1 103 ? -5.801  6.692   33.685  1.00 50.74  ? 103 VAL A N     1 
ATOM   760   C CA    . VAL A 1 103 ? -5.274  7.581   34.713  1.00 49.42  ? 103 VAL A CA    1 
ATOM   761   C C     . VAL A 1 103 ? -6.033  7.360   36.024  1.00 55.87  ? 103 VAL A C     1 
ATOM   762   O O     . VAL A 1 103 ? -7.264  7.291   36.028  1.00 50.53  ? 103 VAL A O     1 
ATOM   763   C CB    . VAL A 1 103 ? -5.396  9.065   34.343  1.00 45.63  ? 103 VAL A CB    1 
ATOM   764   C CG1   . VAL A 1 103 ? -4.963  9.958   35.503  1.00 47.71  ? 103 VAL A CG1   1 
ATOM   765   C CG2   . VAL A 1 103 ? -4.622  9.404   33.096  1.00 47.70  ? 103 VAL A CG2   1 
ATOM   766   N N     . LEU A 1 104 ? -5.278  7.276   37.129  1.00 59.25  ? 104 LEU A N     1 
ATOM   767   C CA    . LEU A 1 104 ? -5.821  7.267   38.476  1.00 53.99  ? 104 LEU A CA    1 
ATOM   768   C C     . LEU A 1 104 ? -5.446  8.591   39.099  1.00 53.20  ? 104 LEU A C     1 
ATOM   769   O O     . LEU A 1 104 ? -4.281  8.791   39.434  1.00 63.74  ? 104 LEU A O     1 
ATOM   770   C CB    . LEU A 1 104 ? -5.234  6.102   39.278  1.00 61.68  ? 104 LEU A CB    1 
ATOM   771   C CG    . LEU A 1 104 ? -5.533  6.110   40.779  1.00 67.82  ? 104 LEU A CG    1 
ATOM   772   C CD1   . LEU A 1 104 ? -6.992  5.819   41.056  1.00 66.99  ? 104 LEU A CD1   1 
ATOM   773   C CD2   . LEU A 1 104 ? -4.671  5.095   41.506  1.00 75.63  ? 104 LEU A CD2   1 
ATOM   774   N N     . ASP A 1 105 ? -6.439  9.474   39.213  1.00 57.17  ? 105 ASP A N     1 
ATOM   775   C CA    . ASP A 1 105 ? -6.223  10.842  39.647  1.00 58.38  ? 105 ASP A CA    1 
ATOM   776   C C     . ASP A 1 105 ? -6.629  10.995  41.113  1.00 57.27  ? 105 ASP A C     1 
ATOM   777   O O     . ASP A 1 105 ? -7.708  10.548  41.539  1.00 58.15  ? 105 ASP A O     1 
ATOM   778   C CB    . ASP A 1 105 ? -7.013  11.829  38.781  1.00 56.17  ? 105 ASP A CB    1 
ATOM   779   C CG    . ASP A 1 105 ? -6.643  13.283  39.004  1.00 59.12  ? 105 ASP A CG    1 
ATOM   780   O OD1   . ASP A 1 105 ? -5.720  13.537  39.789  1.00 70.85  ? 105 ASP A OD1   1 
ATOM   781   O OD2   . ASP A 1 105 ? -7.271  14.154  38.383  1.00 66.11  ? 105 ASP A OD2   1 
ATOM   782   N N     . MET A 1 106 ? -5.780  11.741  41.832  1.00 53.05  ? 106 MET A N     1 
ATOM   783   C CA    . MET A 1 106 ? -5.857  11.837  43.276  1.00 52.35  ? 106 MET A CA    1 
ATOM   784   C C     . MET A 1 106 ? -5.788  13.294  43.737  1.00 54.09  ? 106 MET A C     1 
ATOM   785   O O     . MET A 1 106 ? -5.595  13.570  44.917  1.00 61.57  ? 106 MET A O     1 
ATOM   786   C CB    . MET A 1 106 ? -4.765  10.956  43.883  1.00 50.41  ? 106 MET A CB    1 
ATOM   787   C CG    . MET A 1 106 ? -4.811  9.585   43.249  1.00 53.15  ? 106 MET A CG    1 
ATOM   788   S SD    . MET A 1 106 ? -4.167  8.262   44.225  1.00 67.40  ? 106 MET A SD    1 
ATOM   789   C CE    . MET A 1 106 ? -2.558  8.913   44.663  1.00 77.21  ? 106 MET A CE    1 
ATOM   790   N N     . ASN A 1 107 ? -6.077  14.222  42.822  1.00 55.77  ? 107 ASN A N     1 
ATOM   791   C CA    . ASN A 1 107 ? -6.504  15.560  43.200  1.00 67.78  ? 107 ASN A CA    1 
ATOM   792   C C     . ASN A 1 107 ? -7.424  15.514  44.415  1.00 59.25  ? 107 ASN A C     1 
ATOM   793   O O     . ASN A 1 107 ? -7.343  16.405  45.248  1.00 66.86  ? 107 ASN A O     1 
ATOM   794   C CB    . ASN A 1 107 ? -7.254  16.292  42.075  1.00 76.69  ? 107 ASN A CB    1 
ATOM   795   C CG    . ASN A 1 107 ? -6.355  17.201  41.263  1.00 91.28  ? 107 ASN A CG    1 
ATOM   796   O OD1   . ASN A 1 107 ? -5.845  18.186  41.784  1.00 96.85  ? 107 ASN A OD1   1 
ATOM   797   N ND2   . ASN A 1 107 ? -6.145  16.886  39.995  1.00 104.78 ? 107 ASN A ND2   1 
ATOM   798   N N     . ARG A 1 108 ? -8.339  14.539  44.486  1.00 57.18  ? 108 ARG A N     1 
ATOM   799   C CA    . ARG A 1 108 ? -9.437  14.654  45.442  1.00 70.64  ? 108 ARG A CA    1 
ATOM   800   C C     . ARG A 1 108 ? -8.955  14.405  46.875  1.00 64.82  ? 108 ARG A C     1 
ATOM   801   O O     . ARG A 1 108 ? -9.458  15.015  47.815  1.00 56.24  ? 108 ARG A O     1 
ATOM   802   C CB    . ARG A 1 108 ? -10.578 13.713  45.050  1.00 71.88  ? 108 ARG A CB    1 
ATOM   803   C CG    . ARG A 1 108 ? -11.293 14.144  43.777  1.00 75.40  ? 108 ARG A CG    1 
ATOM   804   C CD    . ARG A 1 108 ? -12.488 13.269  43.441  1.00 68.94  ? 108 ARG A CD    1 
ATOM   805   N NE    . ARG A 1 108 ? -13.621 13.573  44.309  1.00 64.12  ? 108 ARG A NE    1 
ATOM   806   C CZ    . ARG A 1 108 ? -14.435 12.674  44.857  1.00 63.64  ? 108 ARG A CZ    1 
ATOM   807   N NH1   . ARG A 1 108 ? -14.316 11.376  44.611  1.00 54.67  ? 108 ARG A NH1   1 
ATOM   808   N NH2   . ARG A 1 108 ? -15.404 13.097  45.647  1.00 75.73  ? 108 ARG A NH2   1 
ATOM   809   N N     . MET A 1 109 ? -7.982  13.498  47.020  1.00 60.91  ? 109 MET A N     1 
ATOM   810   C CA    . MET A 1 109 ? -7.311  13.228  48.281  1.00 54.82  ? 109 MET A CA    1 
ATOM   811   C C     . MET A 1 109 ? -6.262  14.313  48.535  1.00 49.71  ? 109 MET A C     1 
ATOM   812   O O     . MET A 1 109 ? -5.085  14.102  48.269  1.00 58.81  ? 109 MET A O     1 
ATOM   813   C CB    . MET A 1 109 ? -6.655  11.848  48.199  1.00 54.47  ? 109 MET A CB    1 
ATOM   814   C CG    . MET A 1 109 ? -7.657  10.765  47.857  1.00 49.52  ? 109 MET A CG    1 
ATOM   815   S SD    . MET A 1 109 ? -6.949  9.155   47.478  1.00 63.19  ? 109 MET A SD    1 
ATOM   816   C CE    . MET A 1 109 ? -6.070  8.813   49.008  1.00 66.42  ? 109 MET A CE    1 
ATOM   817   N N     . ASN A 1 110 ? -6.726  15.467  49.043  1.00 52.55  ? 110 ASN A N     1 
ATOM   818   C CA    . ASN A 1 110 ? -5.946  16.677  49.249  1.00 51.31  ? 110 ASN A CA    1 
ATOM   819   C C     . ASN A 1 110 ? -6.026  17.149  50.710  1.00 51.77  ? 110 ASN A C     1 
ATOM   820   O O     . ASN A 1 110 ? -5.810  18.343  51.010  1.00 44.16  ? 110 ASN A O     1 
ATOM   821   C CB    . ASN A 1 110 ? -6.396  17.787  48.296  1.00 61.56  ? 110 ASN A CB    1 
ATOM   822   C CG    . ASN A 1 110 ? -7.813  18.292  48.530  1.00 68.33  ? 110 ASN A CG    1 
ATOM   823   O OD1   . ASN A 1 110 ? -8.738  17.506  48.731  1.00 66.68  ? 110 ASN A OD1   1 
ATOM   824   N ND2   . ASN A 1 110 ? -8.002  19.605  48.486  1.00 59.28  ? 110 ASN A ND2   1 
ATOM   825   N N     . ARG A 1 111 ? -6.256  16.201  51.635  1.00 47.90  ? 111 ARG A N     1 
ATOM   826   C CA    . ARG A 1 111 ? -6.297  16.550  53.058  1.00 63.12  ? 111 ARG A CA    1 
ATOM   827   C C     . ARG A 1 111 ? -4.870  16.695  53.602  1.00 60.27  ? 111 ARG A C     1 
ATOM   828   O O     . ARG A 1 111 ? -4.084  15.746  53.575  1.00 56.57  ? 111 ARG A O     1 
ATOM   829   C CB    . ARG A 1 111 ? -7.113  15.536  53.879  1.00 55.84  ? 111 ARG A CB    1 
ATOM   830   C CG    . ARG A 1 111 ? -8.061  16.169  54.889  1.00 65.19  ? 111 ARG A CG    1 
ATOM   831   C CD    . ARG A 1 111 ? -8.466  15.199  55.986  1.00 78.01  ? 111 ARG A CD    1 
ATOM   832   N NE    . ARG A 1 111 ? -8.866  13.880  55.481  1.00 88.87  ? 111 ARG A NE    1 
ATOM   833   C CZ    . ARG A 1 111 ? -8.797  12.727  56.161  1.00 87.65  ? 111 ARG A CZ    1 
ATOM   834   N NH1   . ARG A 1 111 ? -8.330  12.687  57.400  1.00 67.23  ? 111 ARG A NH1   1 
ATOM   835   N NH2   . ARG A 1 111 ? -9.181  11.598  55.587  1.00 94.71  ? 111 ARG A NH2   1 
ATOM   836   N N     . ILE A 1 112 ? -4.537  17.907  54.054  1.00 54.48  ? 112 ILE A N     1 
ATOM   837   C CA    . ILE A 1 112 ? -3.390  18.123  54.919  1.00 53.28  ? 112 ILE A CA    1 
ATOM   838   C C     . ILE A 1 112 ? -3.658  17.493  56.285  1.00 59.45  ? 112 ILE A C     1 
ATOM   839   O O     . ILE A 1 112 ? -4.288  18.113  57.134  1.00 61.52  ? 112 ILE A O     1 
ATOM   840   C CB    . ILE A 1 112 ? -3.116  19.627  55.073  1.00 52.28  ? 112 ILE A CB    1 
ATOM   841   C CG1   . ILE A 1 112 ? -2.878  20.291  53.711  1.00 51.47  ? 112 ILE A CG1   1 
ATOM   842   C CG2   . ILE A 1 112 ? -1.979  19.886  56.053  1.00 54.99  ? 112 ILE A CG2   1 
ATOM   843   C CD1   . ILE A 1 112 ? -2.534  21.761  53.806  1.00 50.15  ? 112 ILE A CD1   1 
ATOM   844   N N     . LEU A 1 113 ? -3.116  16.291  56.514  1.00 54.99  ? 113 LEU A N     1 
ATOM   845   C CA    . LEU A 1 113 ? -3.436  15.503  57.692  1.00 57.31  ? 113 LEU A CA    1 
ATOM   846   C C     . LEU A 1 113 ? -2.721  15.975  58.964  1.00 57.50  ? 113 LEU A C     1 
ATOM   847   O O     . LEU A 1 113 ? -3.156  15.633  60.065  1.00 49.36  ? 113 LEU A O     1 
ATOM   848   C CB    . LEU A 1 113 ? -3.038  14.061  57.404  1.00 56.19  ? 113 LEU A CB    1 
ATOM   849   C CG    . LEU A 1 113 ? -3.683  13.439  56.175  1.00 61.59  ? 113 LEU A CG    1 
ATOM   850   C CD1   . LEU A 1 113 ? -2.888  12.238  55.708  1.00 68.76  ? 113 LEU A CD1   1 
ATOM   851   C CD2   . LEU A 1 113 ? -5.115  13.027  56.457  1.00 63.49  ? 113 LEU A CD2   1 
ATOM   852   N N     . GLU A 1 114 ? -1.570  16.649  58.846  1.00 63.03  ? 114 GLU A N     1 
ATOM   853   C CA    . GLU A 1 114 ? -0.849  17.086  60.040  1.00 58.72  ? 114 GLU A CA    1 
ATOM   854   C C     . GLU A 1 114 ? 0.228   18.086  59.663  1.00 53.33  ? 114 GLU A C     1 
ATOM   855   O O     . GLU A 1 114 ? 0.931   17.922  58.681  1.00 59.50  ? 114 GLU A O     1 
ATOM   856   C CB    . GLU A 1 114 ? -0.175  15.937  60.798  1.00 53.34  ? 114 GLU A CB    1 
ATOM   857   C CG    . GLU A 1 114 ? 0.210   16.307  62.216  1.00 62.26  ? 114 GLU A CG    1 
ATOM   858   C CD    . GLU A 1 114 ? 0.871   15.221  63.060  1.00 70.00  ? 114 GLU A CD    1 
ATOM   859   O OE1   . GLU A 1 114 ? 0.908   14.024  62.627  1.00 59.22  ? 114 GLU A OE1   1 
ATOM   860   O OE2   . GLU A 1 114 ? 1.360   15.579  64.166  1.00 62.41  ? 114 GLU A OE2   1 
ATOM   861   N N     . VAL A 1 115 ? 0.347   19.135  60.461  1.00 57.66  ? 115 VAL A N     1 
ATOM   862   C CA    . VAL A 1 115 ? 1.494   20.006  60.356  1.00 55.20  ? 115 VAL A CA    1 
ATOM   863   C C     . VAL A 1 115 ? 1.941   20.333  61.774  1.00 61.85  ? 115 VAL A C     1 
ATOM   864   O O     . VAL A 1 115 ? 1.293   21.112  62.477  1.00 58.91  ? 115 VAL A O     1 
ATOM   865   C CB    . VAL A 1 115 ? 1.207   21.256  59.522  1.00 52.22  ? 115 VAL A CB    1 
ATOM   866   C CG1   . VAL A 1 115 ? 2.454   22.127  59.398  1.00 55.86  ? 115 VAL A CG1   1 
ATOM   867   C CG2   . VAL A 1 115 ? 0.685   20.869  58.149  1.00 57.93  ? 115 VAL A CG2   1 
ATOM   868   N N     . ASN A 1 116 ? 3.069   19.712  62.144  1.00 59.15  ? 116 ASN A N     1 
ATOM   869   C CA    . ASN A 1 116 ? 3.668   19.815  63.460  1.00 50.32  ? 116 ASN A CA    1 
ATOM   870   C C     . ASN A 1 116 ? 4.773   20.861  63.398  1.00 49.69  ? 116 ASN A C     1 
ATOM   871   O O     . ASN A 1 116 ? 5.723   20.710  62.644  1.00 51.02  ? 116 ASN A O     1 
ATOM   872   C CB    . ASN A 1 116 ? 4.154   18.435  63.878  1.00 47.56  ? 116 ASN A CB    1 
ATOM   873   C CG    . ASN A 1 116 ? 4.570   18.362  65.325  1.00 48.27  ? 116 ASN A CG    1 
ATOM   874   O OD1   . ASN A 1 116 ? 5.423   19.119  65.790  1.00 40.62  ? 116 ASN A OD1   1 
ATOM   875   N ND2   . ASN A 1 116 ? 4.005   17.409  66.035  1.00 53.75  ? 116 ASN A ND2   1 
ATOM   876   N N     . GLU A 1 117 ? 4.637   21.923  64.195  1.00 55.91  ? 117 GLU A N     1 
ATOM   877   C CA    . GLU A 1 117 ? 5.569   23.043  64.201  1.00 54.64  ? 117 GLU A CA    1 
ATOM   878   C C     . GLU A 1 117 ? 6.818   22.669  65.000  1.00 57.28  ? 117 GLU A C     1 
ATOM   879   O O     . GLU A 1 117 ? 7.938   22.969  64.587  1.00 55.92  ? 117 GLU A O     1 
ATOM   880   C CB    . GLU A 1 117 ? 4.885   24.269  64.822  1.00 54.55  ? 117 GLU A CB    1 
ATOM   881   C CG    . GLU A 1 117 ? 5.704   25.551  64.762  1.00 56.78  ? 117 GLU A CG    1 
ATOM   882   C CD    . GLU A 1 117 ? 5.126   26.749  65.506  1.00 60.70  ? 117 GLU A CD    1 
ATOM   883   O OE1   . GLU A 1 117 ? 4.326   26.537  66.437  1.00 67.71  ? 117 GLU A OE1   1 
ATOM   884   O OE2   . GLU A 1 117 ? 5.448   27.894  65.125  1.00 61.94  ? 117 GLU A OE2   1 
ATOM   885   N N     . GLU A 1 118 ? 6.615   22.025  66.157  1.00 55.00  ? 118 GLU A N     1 
ATOM   886   C CA    . GLU A 1 118 ? 7.693   21.846  67.124  1.00 61.95  ? 118 GLU A CA    1 
ATOM   887   C C     . GLU A 1 118 ? 8.700   20.816  66.600  1.00 54.59  ? 118 GLU A C     1 
ATOM   888   O O     . GLU A 1 118 ? 9.879   20.894  66.923  1.00 48.49  ? 118 GLU A O     1 
ATOM   889   C CB    . GLU A 1 118 ? 7.125   21.432  68.490  1.00 63.35  ? 118 GLU A CB    1 
ATOM   890   C CG    . GLU A 1 118 ? 6.526   20.034  68.493  1.00 74.01  ? 118 GLU A CG    1 
ATOM   891   C CD    . GLU A 1 118 ? 5.746   19.582  69.723  1.00 89.63  ? 118 GLU A CD    1 
ATOM   892   O OE1   . GLU A 1 118 ? 6.292   19.687  70.861  1.00 68.91  ? 118 GLU A OE1   1 
ATOM   893   O OE2   . GLU A 1 118 ? 4.603   19.061  69.528  1.00 88.34  ? 118 GLU A OE2   1 
ATOM   894   N N     . PHE A 1 119 ? 8.200   19.838  65.835  1.00 51.00  ? 119 PHE A N     1 
ATOM   895   C CA    . PHE A 1 119 ? 9.012   18.819  65.201  1.00 55.46  ? 119 PHE A CA    1 
ATOM   896   C C     . PHE A 1 119 ? 9.212   19.072  63.710  1.00 52.78  ? 119 PHE A C     1 
ATOM   897   O O     . PHE A 1 119 ? 9.836   18.258  63.064  1.00 45.40  ? 119 PHE A O     1 
ATOM   898   C CB    . PHE A 1 119 ? 8.361   17.444  65.293  1.00 56.70  ? 119 PHE A CB    1 
ATOM   899   C CG    . PHE A 1 119 ? 8.260   16.910  66.690  1.00 67.39  ? 119 PHE A CG    1 
ATOM   900   C CD1   . PHE A 1 119 ? 9.330   17.021  67.566  1.00 78.63  ? 119 PHE A CD1   1 
ATOM   901   C CD2   . PHE A 1 119 ? 7.102   16.280  67.115  1.00 63.88  ? 119 PHE A CD2   1 
ATOM   902   C CE1   . PHE A 1 119 ? 9.226   16.545  68.861  1.00 76.74  ? 119 PHE A CE1   1 
ATOM   903   C CE2   . PHE A 1 119 ? 6.998   15.804  68.409  1.00 66.35  ? 119 PHE A CE2   1 
ATOM   904   C CZ    . PHE A 1 119 ? 8.059   15.942  69.279  1.00 78.78  ? 119 PHE A CZ    1 
ATOM   905   N N     . GLY A 1 120 ? 8.660   20.147  63.154  1.00 50.77  ? 120 GLY A N     1 
ATOM   906   C CA    . GLY A 1 120 ? 8.992   20.549  61.791  1.00 53.55  ? 120 GLY A CA    1 
ATOM   907   C C     . GLY A 1 120 ? 8.674   19.497  60.724  1.00 46.89  ? 120 GLY A C     1 
ATOM   908   O O     . GLY A 1 120 ? 9.572   19.071  60.008  1.00 43.47  ? 120 GLY A O     1 
ATOM   909   N N     . TYR A 1 121 ? 7.401   19.114  60.590  1.00 40.27  ? 121 TYR A N     1 
ATOM   910   C CA    . TYR A 1 121 ? 7.009   18.266  59.487  1.00 49.18  ? 121 TYR A CA    1 
ATOM   911   C C     . TYR A 1 121 ? 5.542   18.469  59.084  1.00 51.47  ? 121 TYR A C     1 
ATOM   912   O O     . TYR A 1 121 ? 4.779   19.166  59.747  1.00 47.15  ? 121 TYR A O     1 
ATOM   913   C CB    . TYR A 1 121 ? 7.336   16.818  59.841  1.00 47.87  ? 121 TYR A CB    1 
ATOM   914   C CG    . TYR A 1 121 ? 6.410   16.173  60.831  1.00 47.19  ? 121 TYR A CG    1 
ATOM   915   C CD1   . TYR A 1 121 ? 5.114   15.818  60.489  1.00 55.84  ? 121 TYR A CD1   1 
ATOM   916   C CD2   . TYR A 1 121 ? 6.823   15.954  62.131  1.00 47.34  ? 121 TYR A CD2   1 
ATOM   917   C CE1   . TYR A 1 121 ? 4.266   15.229  61.418  1.00 62.92  ? 121 TYR A CE1   1 
ATOM   918   C CE2   . TYR A 1 121 ? 5.995   15.366  63.071  1.00 50.72  ? 121 TYR A CE2   1 
ATOM   919   C CZ    . TYR A 1 121 ? 4.710   15.003  62.716  1.00 58.46  ? 121 TYR A CZ    1 
ATOM   920   O OH    . TYR A 1 121 ? 3.925   14.418  63.668  1.00 56.15  ? 121 TYR A OH    1 
ATOM   921   N N     . ALA A 1 122 ? 5.187   17.871  57.933  1.00 48.10  ? 122 ALA A N     1 
ATOM   922   C CA    . ALA A 1 122 ? 3.805   17.724  57.516  1.00 43.08  ? 122 ALA A CA    1 
ATOM   923   C C     . ALA A 1 122 ? 3.508   16.277  57.163  1.00 42.12  ? 122 ALA A C     1 
ATOM   924   O O     . ALA A 1 122 ? 4.391   15.485  56.867  1.00 42.53  ? 122 ALA A O     1 
ATOM   925   C CB    . ALA A 1 122 ? 3.518   18.606  56.350  1.00 49.31  ? 122 ALA A CB    1 
ATOM   926   N N     . LEU A 1 123 ? 2.233   15.930  57.259  1.00 43.42  ? 123 LEU A N     1 
ATOM   927   C CA    . LEU A 1 123 ? 1.713   14.716  56.683  1.00 45.16  ? 123 LEU A CA    1 
ATOM   928   C C     . LEU A 1 123 ? 0.598   15.147  55.734  1.00 52.61  ? 123 LEU A C     1 
ATOM   929   O O     . LEU A 1 123 ? -0.296  15.883  56.136  1.00 58.74  ? 123 LEU A O     1 
ATOM   930   C CB    . LEU A 1 123 ? 1.220   13.823  57.820  1.00 46.95  ? 123 LEU A CB    1 
ATOM   931   C CG    . LEU A 1 123 ? 0.759   12.430  57.401  1.00 49.71  ? 123 LEU A CG    1 
ATOM   932   C CD1   . LEU A 1 123 ? 1.882   11.664  56.721  1.00 50.15  ? 123 LEU A CD1   1 
ATOM   933   C CD2   . LEU A 1 123 ? 0.228   11.653  58.591  1.00 48.05  ? 123 LEU A CD2   1 
ATOM   934   N N     . VAL A 1 124 ? 0.713   14.753  54.460  1.00 62.63  ? 124 VAL A N     1 
ATOM   935   C CA    . VAL A 1 124 ? -0.141  15.246  53.386  1.00 56.56  ? 124 VAL A CA    1 
ATOM   936   C C     . VAL A 1 124 ? -0.552  14.077  52.489  1.00 56.45  ? 124 VAL A C     1 
ATOM   937   O O     . VAL A 1 124 ? 0.154   13.078  52.368  1.00 56.56  ? 124 VAL A O     1 
ATOM   938   C CB    . VAL A 1 124 ? 0.553   16.358  52.575  1.00 52.76  ? 124 VAL A CB    1 
ATOM   939   C CG1   . VAL A 1 124 ? 0.583   17.672  53.329  1.00 53.77  ? 124 VAL A CG1   1 
ATOM   940   C CG2   . VAL A 1 124 ? 1.966   15.986  52.146  1.00 57.57  ? 124 VAL A CG2   1 
ATOM   941   N N     . GLU A 1 125 ? -1.730  14.212  51.879  1.00 58.52  ? 125 GLU A N     1 
ATOM   942   C CA    . GLU A 1 125 ? -2.160  13.313  50.821  1.00 55.13  ? 125 GLU A CA    1 
ATOM   943   C C     . GLU A 1 125 ? -1.730  13.873  49.460  1.00 42.56  ? 125 GLU A C     1 
ATOM   944   O O     . GLU A 1 125 ? -1.379  15.054  49.352  1.00 50.13  ? 125 GLU A O     1 
ATOM   945   C CB    . GLU A 1 125 ? -3.678  13.165  50.885  1.00 56.69  ? 125 GLU A CB    1 
ATOM   946   C CG    . GLU A 1 125 ? -4.219  12.709  52.224  1.00 53.61  ? 125 GLU A CG    1 
ATOM   947   C CD    . GLU A 1 125 ? -5.733  12.669  52.169  1.00 55.24  ? 125 GLU A CD    1 
ATOM   948   O OE1   . GLU A 1 125 ? -6.332  13.727  51.895  1.00 57.52  ? 125 GLU A OE1   1 
ATOM   949   O OE2   . GLU A 1 125 ? -6.296  11.589  52.324  1.00 52.46  ? 125 GLU A OE2   1 
ATOM   950   N N     . PRO A 1 126 ? -1.765  13.069  48.371  1.00 44.37  ? 126 PRO A N     1 
ATOM   951   C CA    . PRO A 1 126 ? -1.332  13.531  47.044  1.00 49.36  ? 126 PRO A CA    1 
ATOM   952   C C     . PRO A 1 126 ? -1.864  14.883  46.558  1.00 54.88  ? 126 PRO A C     1 
ATOM   953   O O     . PRO A 1 126 ? -1.078  15.707  46.101  1.00 62.72  ? 126 PRO A O     1 
ATOM   954   C CB    . PRO A 1 126 ? -1.815  12.385  46.164  1.00 51.86  ? 126 PRO A CB    1 
ATOM   955   C CG    . PRO A 1 126 ? -1.552  11.183  47.038  1.00 49.73  ? 126 PRO A CG    1 
ATOM   956   C CD    . PRO A 1 126 ? -2.130  11.644  48.353  1.00 49.58  ? 126 PRO A CD    1 
ATOM   957   N N     . GLY A 1 127 ? -3.168  15.151  46.729  1.00 47.55  ? 127 GLY A N     1 
ATOM   958   C CA    . GLY A 1 127 ? -3.780  16.354  46.179  1.00 44.64  ? 127 GLY A CA    1 
ATOM   959   C C     . GLY A 1 127 ? -3.224  17.656  46.759  1.00 51.57  ? 127 GLY A C     1 
ATOM   960   O O     . GLY A 1 127 ? -3.451  18.745  46.227  1.00 51.00  ? 127 GLY A O     1 
ATOM   961   N N     . VAL A 1 128 ? -2.502  17.574  47.878  1.00 53.67  ? 128 VAL A N     1 
ATOM   962   C CA    . VAL A 1 128 ? -2.105  18.803  48.533  1.00 57.20  ? 128 VAL A CA    1 
ATOM   963   C C     . VAL A 1 128 ? -1.079  19.483  47.626  1.00 60.50  ? 128 VAL A C     1 
ATOM   964   O O     . VAL A 1 128 ? -0.038  18.906  47.322  1.00 70.25  ? 128 VAL A O     1 
ATOM   965   C CB    . VAL A 1 128 ? -1.567  18.552  49.959  1.00 53.14  ? 128 VAL A CB    1 
ATOM   966   C CG1   . VAL A 1 128 ? -1.112  19.830  50.640  1.00 48.17  ? 128 VAL A CG1   1 
ATOM   967   C CG2   . VAL A 1 128 ? -2.572  17.829  50.833  1.00 56.17  ? 128 VAL A CG2   1 
ATOM   968   N N     . SER A 1 129 ? -1.394  20.707  47.201  1.00 59.29  ? 129 SER A N     1 
ATOM   969   C CA    . SER A 1 129 ? -0.476  21.500  46.406  1.00 57.82  ? 129 SER A CA    1 
ATOM   970   C C     . SER A 1 129 ? 0.445   22.314  47.305  1.00 58.63  ? 129 SER A C     1 
ATOM   971   O O     . SER A 1 129 ? 0.097   22.610  48.444  1.00 63.78  ? 129 SER A O     1 
ATOM   972   C CB    . SER A 1 129 ? -1.239  22.428  45.527  1.00 51.78  ? 129 SER A CB    1 
ATOM   973   O OG    . SER A 1 129 ? -1.708  23.500  46.311  1.00 48.16  ? 129 SER A OG    1 
ATOM   974   N N     . TYR A 1 130 ? 1.577   22.750  46.738  1.00 49.89  ? 130 TYR A N     1 
ATOM   975   C CA    . TYR A 1 130 ? 2.489   23.636  47.421  1.00 48.19  ? 130 TYR A CA    1 
ATOM   976   C C     . TYR A 1 130 ? 1.727   24.871  47.883  1.00 53.31  ? 130 TYR A C     1 
ATOM   977   O O     . TYR A 1 130 ? 1.915   25.334  49.017  1.00 55.90  ? 130 TYR A O     1 
ATOM   978   C CB    . TYR A 1 130 ? 3.686   23.966  46.523  1.00 51.08  ? 130 TYR A CB    1 
ATOM   979   C CG    . TYR A 1 130 ? 4.633   22.818  46.249  1.00 51.68  ? 130 TYR A CG    1 
ATOM   980   C CD1   . TYR A 1 130 ? 5.503   22.352  47.226  1.00 52.39  ? 130 TYR A CD1   1 
ATOM   981   C CD2   . TYR A 1 130 ? 4.698   22.214  45.004  1.00 53.54  ? 130 TYR A CD2   1 
ATOM   982   C CE1   . TYR A 1 130 ? 6.388   21.315  46.987  1.00 48.88  ? 130 TYR A CE1   1 
ATOM   983   C CE2   . TYR A 1 130 ? 5.567   21.160  44.750  1.00 58.40  ? 130 TYR A CE2   1 
ATOM   984   C CZ    . TYR A 1 130 ? 6.437   20.724  45.737  1.00 57.63  ? 130 TYR A CZ    1 
ATOM   985   O OH    . TYR A 1 130 ? 7.319   19.696  45.490  1.00 50.97  ? 130 TYR A OH    1 
ATOM   986   N N     . PHE A 1 131 ? 0.859   25.398  47.011  1.00 61.10  ? 131 PHE A N     1 
ATOM   987   C CA    . PHE A 1 131 ? 0.042   26.566  47.352  1.00 64.52  ? 131 PHE A CA    1 
ATOM   988   C C     . PHE A 1 131 ? -0.846  26.284  48.563  1.00 53.83  ? 131 PHE A C     1 
ATOM   989   O O     . PHE A 1 131 ? -0.912  27.097  49.484  1.00 53.46  ? 131 PHE A O     1 
ATOM   990   C CB    . PHE A 1 131 ? -0.811  27.010  46.161  1.00 61.21  ? 131 PHE A CB    1 
ATOM   991   C CG    . PHE A 1 131 ? 0.000   27.689  45.090  1.00 60.28  ? 131 PHE A CG    1 
ATOM   992   C CD1   . PHE A 1 131 ? 0.409   29.006  45.255  1.00 58.82  ? 131 PHE A CD1   1 
ATOM   993   C CD2   . PHE A 1 131 ? 0.427   26.987  43.968  1.00 54.70  ? 131 PHE A CD2   1 
ATOM   994   C CE1   . PHE A 1 131 ? 1.186   29.628  44.287  1.00 55.96  ? 131 PHE A CE1   1 
ATOM   995   C CE2   . PHE A 1 131 ? 1.206   27.608  43.008  1.00 54.06  ? 131 PHE A CE2   1 
ATOM   996   C CZ    . PHE A 1 131 ? 1.588   28.924  43.173  1.00 55.60  ? 131 PHE A CZ    1 
ATOM   997   N N     . GLU A 1 132 ? -1.497  25.118  48.564  1.00 48.79  ? 132 GLU A N     1 
ATOM   998   C CA    . GLU A 1 132 ? -2.405  24.751  49.640  1.00 53.97  ? 132 GLU A CA    1 
ATOM   999   C C     . GLU A 1 132 ? -1.612  24.636  50.941  1.00 56.30  ? 132 GLU A C     1 
ATOM   1000  O O     . GLU A 1 132 ? -2.016  25.194  51.959  1.00 56.78  ? 132 GLU A O     1 
ATOM   1001  C CB    . GLU A 1 132 ? -3.204  23.489  49.274  1.00 59.07  ? 132 GLU A CB    1 
ATOM   1002  C CG    . GLU A 1 132 ? -4.289  23.733  48.214  1.00 59.12  ? 132 GLU A CG    1 
ATOM   1003  C CD    . GLU A 1 132 ? -5.005  22.523  47.621  1.00 63.17  ? 132 GLU A CD    1 
ATOM   1004  O OE1   . GLU A 1 132 ? -4.585  21.345  47.836  1.00 54.57  ? 132 GLU A OE1   1 
ATOM   1005  O OE2   . GLU A 1 132 ? -6.006  22.764  46.947  1.00 63.78  ? 132 GLU A OE2   1 
ATOM   1006  N N     . LEU A 1 133 ? -0.459  23.950  50.893  1.00 63.45  ? 133 LEU A N     1 
ATOM   1007  C CA    . LEU A 1 133 ? 0.331   23.712  52.092  1.00 53.61  ? 133 LEU A CA    1 
ATOM   1008  C C     . LEU A 1 133 ? 0.957   25.012  52.574  1.00 51.18  ? 133 LEU A C     1 
ATOM   1009  O O     . LEU A 1 133 ? 0.983   25.251  53.778  1.00 50.73  ? 133 LEU A O     1 
ATOM   1010  C CB    . LEU A 1 133 ? 1.403   22.653  51.845  1.00 51.52  ? 133 LEU A CB    1 
ATOM   1011  C CG    . LEU A 1 133 ? 2.301   22.366  53.046  1.00 51.79  ? 133 LEU A CG    1 
ATOM   1012  C CD1   . LEU A 1 133 ? 1.469   21.811  54.186  1.00 60.05  ? 133 LEU A CD1   1 
ATOM   1013  C CD2   . LEU A 1 133 ? 3.436   21.410  52.705  1.00 44.96  ? 133 LEU A CD2   1 
ATOM   1014  N N     . TYR A 1 134 ? 1.463   25.845  51.655  1.00 52.95  ? 134 TYR A N     1 
ATOM   1015  C CA    . TYR A 1 134 ? 1.917   27.167  52.063  1.00 53.81  ? 134 TYR A CA    1 
ATOM   1016  C C     . TYR A 1 134 ? 0.811   27.825  52.876  1.00 62.34  ? 134 TYR A C     1 
ATOM   1017  O O     . TYR A 1 134 ? 1.028   28.234  54.013  1.00 63.96  ? 134 TYR A O     1 
ATOM   1018  C CB    . TYR A 1 134 ? 2.223   28.087  50.878  1.00 51.65  ? 134 TYR A CB    1 
ATOM   1019  C CG    . TYR A 1 134 ? 2.858   29.419  51.218  1.00 46.76  ? 134 TYR A CG    1 
ATOM   1020  C CD1   . TYR A 1 134 ? 4.140   29.476  51.760  1.00 47.51  ? 134 TYR A CD1   1 
ATOM   1021  C CD2   . TYR A 1 134 ? 2.211   30.626  50.962  1.00 49.12  ? 134 TYR A CD2   1 
ATOM   1022  C CE1   . TYR A 1 134 ? 4.744   30.688  52.070  1.00 50.62  ? 134 TYR A CE1   1 
ATOM   1023  C CE2   . TYR A 1 134 ? 2.806   31.853  51.252  1.00 51.21  ? 134 TYR A CE2   1 
ATOM   1024  C CZ    . TYR A 1 134 ? 4.081   31.878  51.812  1.00 56.38  ? 134 TYR A CZ    1 
ATOM   1025  O OH    . TYR A 1 134 ? 4.744   33.034  52.109  1.00 54.45  ? 134 TYR A OH    1 
ATOM   1026  N N     . ASP A 1 135 ? -0.383  27.900  52.268  1.00 69.90  ? 135 ASP A N     1 
ATOM   1027  C CA    . ASP A 1 135 ? -1.445  28.765  52.762  1.00 73.48  ? 135 ASP A CA    1 
ATOM   1028  C C     . ASP A 1 135 ? -1.853  28.319  54.173  1.00 65.74  ? 135 ASP A C     1 
ATOM   1029  O O     . ASP A 1 135 ? -1.851  29.140  55.091  1.00 69.51  ? 135 ASP A O     1 
ATOM   1030  C CB    . ASP A 1 135 ? -2.574  28.877  51.725  1.00 71.06  ? 135 ASP A CB    1 
ATOM   1031  C CG    . ASP A 1 135 ? -2.297  29.815  50.549  1.00 66.57  ? 135 ASP A CG    1 
ATOM   1032  O OD1   . ASP A 1 135 ? -1.341  30.621  50.604  1.00 62.95  ? 135 ASP A OD1   1 
ATOM   1033  O OD2   . ASP A 1 135 ? -3.040  29.729  49.569  1.00 66.20  ? 135 ASP A OD2   1 
ATOM   1034  N N     . TYR A 1 136 ? -2.120  27.016  54.352  1.00 59.97  ? 136 TYR A N     1 
ATOM   1035  C CA    . TYR A 1 136 ? -2.489  26.438  55.634  1.00 54.85  ? 136 TYR A CA    1 
ATOM   1036  C C     . TYR A 1 136 ? -1.486  26.806  56.732  1.00 64.04  ? 136 TYR A C     1 
ATOM   1037  O O     . TYR A 1 136 ? -1.912  27.175  57.826  1.00 69.49  ? 136 TYR A O     1 
ATOM   1038  C CB    . TYR A 1 136 ? -2.660  24.932  55.471  1.00 62.86  ? 136 TYR A CB    1 
ATOM   1039  C CG    . TYR A 1 136 ? -2.924  24.178  56.755  1.00 78.74  ? 136 TYR A CG    1 
ATOM   1040  C CD1   . TYR A 1 136 ? -1.955  24.100  57.746  1.00 77.03  ? 136 TYR A CD1   1 
ATOM   1041  C CD2   . TYR A 1 136 ? -4.128  23.516  56.973  1.00 72.86  ? 136 TYR A CD2   1 
ATOM   1042  C CE1   . TYR A 1 136 ? -2.178  23.395  58.918  1.00 83.35  ? 136 TYR A CE1   1 
ATOM   1043  C CE2   . TYR A 1 136 ? -4.360  22.794  58.134  1.00 70.93  ? 136 TYR A CE2   1 
ATOM   1044  C CZ    . TYR A 1 136 ? -3.380  22.735  59.110  1.00 75.80  ? 136 TYR A CZ    1 
ATOM   1045  O OH    . TYR A 1 136 ? -3.553  22.033  60.271  1.00 65.46  ? 136 TYR A OH    1 
ATOM   1046  N N     . ILE A 1 137 ? -0.172  26.710  56.440  1.00 64.67  ? 137 ILE A N     1 
ATOM   1047  C CA    . ILE A 1 137 ? 0.900   27.231  57.297  1.00 56.28  ? 137 ILE A CA    1 
ATOM   1048  C C     . ILE A 1 137 ? 0.734   28.741  57.548  1.00 54.93  ? 137 ILE A C     1 
ATOM   1049  O O     . ILE A 1 137 ? 0.862   29.196  58.686  1.00 61.95  ? 137 ILE A O     1 
ATOM   1050  C CB    . ILE A 1 137 ? 2.300   26.891  56.715  1.00 52.56  ? 137 ILE A CB    1 
ATOM   1051  C CG1   . ILE A 1 137 ? 2.679   25.422  56.928  1.00 51.87  ? 137 ILE A CG1   1 
ATOM   1052  C CG2   . ILE A 1 137 ? 3.390   27.810  57.251  1.00 46.42  ? 137 ILE A CG2   1 
ATOM   1053  C CD1   . ILE A 1 137 ? 3.631   24.867  55.883  1.00 50.84  ? 137 ILE A CD1   1 
ATOM   1054  N N     . GLN A 1 138 ? 0.486   29.558  56.518  1.00 52.12  ? 138 GLN A N     1 
ATOM   1055  C CA    . GLN A 1 138 ? 0.458   30.996  56.767  1.00 60.81  ? 138 GLN A CA    1 
ATOM   1056  C C     . GLN A 1 138 ? -0.776  31.373  57.593  1.00 68.19  ? 138 GLN A C     1 
ATOM   1057  O O     . GLN A 1 138 ? -0.674  32.246  58.457  1.00 66.21  ? 138 GLN A O     1 
ATOM   1058  C CB    . GLN A 1 138 ? 0.531   31.818  55.480  1.00 65.31  ? 138 GLN A CB    1 
ATOM   1059  C CG    . GLN A 1 138 ? 1.834   31.659  54.692  1.00 78.61  ? 138 GLN A CG    1 
ATOM   1060  C CD    . GLN A 1 138 ? 3.128   31.795  55.474  1.00 81.76  ? 138 GLN A CD    1 
ATOM   1061  O OE1   . GLN A 1 138 ? 3.393   32.801  56.133  1.00 74.08  ? 138 GLN A OE1   1 
ATOM   1062  N NE2   . GLN A 1 138 ? 3.985   30.788  55.359  1.00 78.51  ? 138 GLN A NE2   1 
ATOM   1063  N N     . GLU A 1 139 ? -1.922  30.716  57.329  1.00 66.16  ? 139 GLU A N     1 
ATOM   1064  C CA    . GLU A 1 139 ? -3.163  30.985  58.037  1.00 70.01  ? 139 GLU A CA    1 
ATOM   1065  C C     . GLU A 1 139 ? -2.977  30.668  59.522  1.00 75.80  ? 139 GLU A C     1 
ATOM   1066  O O     . GLU A 1 139 ? -3.390  31.453  60.365  1.00 77.36  ? 139 GLU A O     1 
ATOM   1067  C CB    . GLU A 1 139 ? -4.354  30.202  57.460  1.00 77.57  ? 139 GLU A CB    1 
ATOM   1068  C CG    . GLU A 1 139 ? -4.948  30.815  56.191  1.00 94.56  ? 139 GLU A CG    1 
ATOM   1069  C CD    . GLU A 1 139 ? -6.417  30.513  55.883  1.00 111.68 ? 139 GLU A CD    1 
ATOM   1070  O OE1   . GLU A 1 139 ? -6.749  30.231  54.695  1.00 106.73 ? 139 GLU A OE1   1 
ATOM   1071  O OE2   . GLU A 1 139 ? -7.248  30.579  56.820  1.00 103.40 ? 139 GLU A OE2   1 
ATOM   1072  N N     . LYS A 1 140 ? -2.330  29.544  59.859  1.00 71.88  ? 140 LYS A N     1 
ATOM   1073  C CA    . LYS A 1 140 ? -2.186  29.174  61.258  1.00 67.40  ? 140 LYS A CA    1 
ATOM   1074  C C     . LYS A 1 140 ? -1.003  29.909  61.899  1.00 60.89  ? 140 LYS A C     1 
ATOM   1075  O O     . LYS A 1 140 ? -0.742  29.744  63.089  1.00 62.99  ? 140 LYS A O     1 
ATOM   1076  C CB    . LYS A 1 140 ? -2.052  27.656  61.409  1.00 69.50  ? 140 LYS A CB    1 
ATOM   1077  C CG    . LYS A 1 140 ? -3.200  26.805  60.880  1.00 76.49  ? 140 LYS A CG    1 
ATOM   1078  C CD    . LYS A 1 140 ? -4.514  26.989  61.607  1.00 84.83  ? 140 LYS A CD    1 
ATOM   1079  C CE    . LYS A 1 140 ? -5.548  25.974  61.174  1.00 86.48  ? 140 LYS A CE    1 
ATOM   1080  N NZ    . LYS A 1 140 ? -6.914  26.424  61.512  1.00 90.18  ? 140 LYS A NZ    1 
ATOM   1081  N N     . GLY A 1 141 ? -0.302  30.738  61.121  1.00 59.30  ? 141 GLY A N     1 
ATOM   1082  C CA    . GLY A 1 141 ? 0.883   31.442  61.587  1.00 59.63  ? 141 GLY A CA    1 
ATOM   1083  C C     . GLY A 1 141 ? 2.017   30.526  62.082  1.00 62.36  ? 141 GLY A C     1 
ATOM   1084  O O     . GLY A 1 141 ? 2.807   30.973  62.913  1.00 53.86  ? 141 GLY A O     1 
ATOM   1085  N N     . LEU A 1 142 ? 2.125   29.271  61.583  1.00 54.32  ? 142 LEU A N     1 
ATOM   1086  C CA    . LEU A 1 142 ? 3.195   28.355  61.995  1.00 54.33  ? 142 LEU A CA    1 
ATOM   1087  C C     . LEU A 1 142 ? 4.559   28.765  61.419  1.00 53.52  ? 142 LEU A C     1 
ATOM   1088  O O     . LEU A 1 142 ? 4.658   29.074  60.244  1.00 62.09  ? 142 LEU A O     1 
ATOM   1089  C CB    . LEU A 1 142 ? 2.865   26.946  61.515  1.00 49.37  ? 142 LEU A CB    1 
ATOM   1090  C CG    . LEU A 1 142 ? 1.529   26.368  61.962  1.00 50.92  ? 142 LEU A CG    1 
ATOM   1091  C CD1   . LEU A 1 142 ? 1.295   25.026  61.310  1.00 53.45  ? 142 LEU A CD1   1 
ATOM   1092  C CD2   . LEU A 1 142 ? 1.440   26.214  63.471  1.00 51.51  ? 142 LEU A CD2   1 
ATOM   1093  N N     . LYS A 1 143 ? 5.625   28.725  62.227  1.00 59.97  ? 143 LYS A N     1 
ATOM   1094  C CA    . LYS A 1 143 ? 6.927   29.270  61.848  1.00 68.47  ? 143 LYS A CA    1 
ATOM   1095  C C     . LYS A 1 143 ? 7.740   28.250  61.040  1.00 62.99  ? 143 LYS A C     1 
ATOM   1096  O O     . LYS A 1 143 ? 8.855   27.904  61.409  1.00 58.11  ? 143 LYS A O     1 
ATOM   1097  C CB    . LYS A 1 143 ? 7.715   29.659  63.105  1.00 80.03  ? 143 LYS A CB    1 
ATOM   1098  C CG    . LYS A 1 143 ? 7.254   30.916  63.835  1.00 89.00  ? 143 LYS A CG    1 
ATOM   1099  C CD    . LYS A 1 143 ? 7.648   32.203  63.122  1.00 106.17 ? 143 LYS A CD    1 
ATOM   1100  C CE    . LYS A 1 143 ? 7.570   33.456  63.975  1.00 106.33 ? 143 LYS A CE    1 
ATOM   1101  N NZ    . LYS A 1 143 ? 6.178   33.779  64.365  1.00 102.65 ? 143 LYS A NZ    1 
ATOM   1102  N N     . LEU A 1 144 ? 7.186   27.791  59.914  1.00 56.85  ? 144 LEU A N     1 
ATOM   1103  C CA    . LEU A 1 144 ? 7.785   26.762  59.087  1.00 50.31  ? 144 LEU A CA    1 
ATOM   1104  C C     . LEU A 1 144 ? 7.880   27.250  57.659  1.00 51.17  ? 144 LEU A C     1 
ATOM   1105  O O     . LEU A 1 144 ? 6.936   27.854  57.178  1.00 51.06  ? 144 LEU A O     1 
ATOM   1106  C CB    . LEU A 1 144 ? 6.873   25.544  59.077  1.00 48.41  ? 144 LEU A CB    1 
ATOM   1107  C CG    . LEU A 1 144 ? 6.772   24.809  60.394  1.00 48.55  ? 144 LEU A CG    1 
ATOM   1108  C CD1   . LEU A 1 144 ? 5.887   23.593  60.229  1.00 48.63  ? 144 LEU A CD1   1 
ATOM   1109  C CD2   . LEU A 1 144 ? 8.165   24.432  60.887  1.00 49.97  ? 144 LEU A CD2   1 
ATOM   1110  N N     . TRP A 1 145 ? 8.985   26.914  56.983  1.00 52.60  ? 145 TRP A N     1 
ATOM   1111  C CA    . TRP A 1 145 ? 9.065   27.042  55.536  1.00 43.17  ? 145 TRP A CA    1 
ATOM   1112  C C     . TRP A 1 145 ? 8.844   25.710  54.822  1.00 45.32  ? 145 TRP A C     1 
ATOM   1113  O O     . TRP A 1 145 ? 9.065   24.628  55.367  1.00 48.13  ? 145 TRP A O     1 
ATOM   1114  C CB    . TRP A 1 145 ? 10.397  27.619  55.156  1.00 43.30  ? 145 TRP A CB    1 
ATOM   1115  C CG    . TRP A 1 145 ? 10.501  29.055  55.516  1.00 49.75  ? 145 TRP A CG    1 
ATOM   1116  C CD1   . TRP A 1 145 ? 9.584   29.843  56.149  1.00 49.56  ? 145 TRP A CD1   1 
ATOM   1117  C CD2   . TRP A 1 145 ? 11.639  29.874  55.234  1.00 52.92  ? 145 TRP A CD2   1 
ATOM   1118  N NE1   . TRP A 1 145 ? 10.103  31.101  56.315  1.00 53.23  ? 145 TRP A NE1   1 
ATOM   1119  C CE2   . TRP A 1 145 ? 11.349  31.154  55.744  1.00 49.78  ? 145 TRP A CE2   1 
ATOM   1120  C CE3   . TRP A 1 145 ? 12.873  29.632  54.615  1.00 56.10  ? 145 TRP A CE3   1 
ATOM   1121  C CZ2   . TRP A 1 145 ? 12.262  32.197  55.651  1.00 53.66  ? 145 TRP A CZ2   1 
ATOM   1122  C CZ3   . TRP A 1 145 ? 13.772  30.673  54.511  1.00 53.05  ? 145 TRP A CZ3   1 
ATOM   1123  C CH2   . TRP A 1 145 ? 13.459  31.938  55.013  1.00 54.44  ? 145 TRP A CH2   1 
ATOM   1124  N N     . ILE A 1 146 ? 8.339   25.798  53.587  1.00 43.72  ? 146 ILE A N     1 
ATOM   1125  C CA    . ILE A 1 146 ? 8.233   24.612  52.771  1.00 44.09  ? 146 ILE A CA    1 
ATOM   1126  C C     . ILE A 1 146 ? 9.295   24.793  51.705  1.00 45.94  ? 146 ILE A C     1 
ATOM   1127  O O     . ILE A 1 146 ? 9.926   25.858  51.709  1.00 43.37  ? 146 ILE A O     1 
ATOM   1128  C CB    . ILE A 1 146 ? 6.807   24.462  52.238  1.00 45.10  ? 146 ILE A CB    1 
ATOM   1129  C CG1   . ILE A 1 146 ? 6.466   25.566  51.241  1.00 45.45  ? 146 ILE A CG1   1 
ATOM   1130  C CG2   . ILE A 1 146 ? 5.856   24.421  53.421  1.00 42.11  ? 146 ILE A CG2   1 
ATOM   1131  C CD1   . ILE A 1 146 ? 5.161   25.351  50.573  1.00 53.24  ? 146 ILE A CD1   1 
ATOM   1132  N N     . ASP A 1 147 ? 9.527   23.760  50.872  1.00 41.74  ? 147 ASP A N     1 
ATOM   1133  C CA    . ASP A 1 147 ? 10.482  23.922  49.789  1.00 41.60  ? 147 ASP A CA    1 
ATOM   1134  C C     . ASP A 1 147 ? 9.822   23.626  48.438  1.00 39.39  ? 147 ASP A C     1 
ATOM   1135  O O     . ASP A 1 147 ? 9.275   22.552  48.234  1.00 37.89  ? 147 ASP A O     1 
ATOM   1136  C CB    . ASP A 1 147 ? 11.734  23.081  50.031  1.00 40.41  ? 147 ASP A CB    1 
ATOM   1137  C CG    . ASP A 1 147 ? 12.769  23.336  48.952  1.00 42.11  ? 147 ASP A CG    1 
ATOM   1138  O OD1   . ASP A 1 147 ? 12.530  22.874  47.817  1.00 39.05  ? 147 ASP A OD1   1 
ATOM   1139  O OD2   . ASP A 1 147 ? 13.755  24.060  49.234  1.00 48.20  ? 147 ASP A OD2   1 
ATOM   1140  N N     . VAL A 1 148 ? 10.030  24.530  47.474  1.00 43.44  ? 148 VAL A N     1 
ATOM   1141  C CA    . VAL A 1 148 ? 9.079   24.778  46.393  1.00 46.94  ? 148 VAL A CA    1 
ATOM   1142  C C     . VAL A 1 148 ? 9.754   24.755  45.007  1.00 43.81  ? 148 VAL A C     1 
ATOM   1143  O O     . VAL A 1 148 ? 10.849  25.273  44.815  1.00 46.08  ? 148 VAL A O     1 
ATOM   1144  C CB    . VAL A 1 148 ? 8.379   26.109  46.767  1.00 43.53  ? 148 VAL A CB    1 
ATOM   1145  C CG1   . VAL A 1 148 ? 8.675   27.286  45.851  1.00 40.89  ? 148 VAL A CG1   1 
ATOM   1146  C CG2   . VAL A 1 148 ? 6.898   25.907  47.006  1.00 44.29  ? 148 VAL A CG2   1 
ATOM   1147  N N     . PRO A 1 149 ? 9.131   24.175  43.957  1.00 52.05  ? 149 PRO A N     1 
ATOM   1148  C CA    . PRO A 1 149 ? 9.577   24.409  42.580  1.00 49.31  ? 149 PRO A CA    1 
ATOM   1149  C C     . PRO A 1 149 ? 9.226   25.807  42.076  1.00 50.89  ? 149 PRO A C     1 
ATOM   1150  O O     . PRO A 1 149 ? 8.483   26.527  42.722  1.00 55.70  ? 149 PRO A O     1 
ATOM   1151  C CB    . PRO A 1 149 ? 8.813   23.362  41.756  1.00 50.59  ? 149 PRO A CB    1 
ATOM   1152  C CG    . PRO A 1 149 ? 7.588   23.024  42.578  1.00 49.88  ? 149 PRO A CG    1 
ATOM   1153  C CD    . PRO A 1 149 ? 7.987   23.251  44.026  1.00 54.96  ? 149 PRO A CD    1 
ATOM   1154  N N     . ASP A 1 150 ? 9.748   26.172  40.900  1.00 63.25  ? 150 ASP A N     1 
ATOM   1155  C CA    . ASP A 1 150 ? 9.507   27.464  40.275  1.00 67.98  ? 150 ASP A CA    1 
ATOM   1156  C C     . ASP A 1 150 ? 9.063   27.230  38.830  1.00 70.50  ? 150 ASP A C     1 
ATOM   1157  O O     . ASP A 1 150 ? 9.847   26.712  38.050  1.00 59.10  ? 150 ASP A O     1 
ATOM   1158  C CB    . ASP A 1 150 ? 10.793  28.295  40.296  1.00 78.77  ? 150 ASP A CB    1 
ATOM   1159  C CG    . ASP A 1 150 ? 10.692  29.748  39.846  1.00 78.19  ? 150 ASP A CG    1 
ATOM   1160  O OD1   . ASP A 1 150 ? 9.560   30.243  39.628  1.00 70.05  ? 150 ASP A OD1   1 
ATOM   1161  O OD2   . ASP A 1 150 ? 11.767  30.382  39.747  1.00 74.49  ? 150 ASP A OD2   1 
ATOM   1162  N N     . PRO A 1 151 ? 7.810   27.553  38.422  1.00 80.18  ? 151 PRO A N     1 
ATOM   1163  C CA    . PRO A 1 151 ? 6.760   27.989  39.341  1.00 82.98  ? 151 PRO A CA    1 
ATOM   1164  C C     . PRO A 1 151 ? 6.380   26.829  40.264  1.00 66.31  ? 151 PRO A C     1 
ATOM   1165  O O     . PRO A 1 151 ? 6.785   25.695  40.042  1.00 57.10  ? 151 PRO A O     1 
ATOM   1166  C CB    . PRO A 1 151 ? 5.575   28.416  38.437  1.00 82.32  ? 151 PRO A CB    1 
ATOM   1167  C CG    . PRO A 1 151 ? 6.120   28.437  37.023  1.00 78.20  ? 151 PRO A CG    1 
ATOM   1168  C CD    . PRO A 1 151 ? 7.327   27.517  37.032  1.00 80.54  ? 151 PRO A CD    1 
ATOM   1169  N N     . GLY A 1 152 ? 5.565   27.132  41.273  1.00 66.99  ? 152 GLY A N     1 
ATOM   1170  C CA    . GLY A 1 152 ? 5.200   26.166  42.288  1.00 68.55  ? 152 GLY A CA    1 
ATOM   1171  C C     . GLY A 1 152 ? 3.891   25.457  41.982  1.00 61.51  ? 152 GLY A C     1 
ATOM   1172  O O     . GLY A 1 152 ? 3.100   25.232  42.888  1.00 67.05  ? 152 GLY A O     1 
ATOM   1173  N N     . TRP A 1 153 ? 3.679   25.115  40.706  1.00 76.65  ? 153 TRP A N     1 
ATOM   1174  C CA    . TRP A 1 153 ? 2.744   24.066  40.334  1.00 77.45  ? 153 TRP A CA    1 
ATOM   1175  C C     . TRP A 1 153 ? 3.041   22.858  41.196  1.00 62.75  ? 153 TRP A C     1 
ATOM   1176  O O     . TRP A 1 153 ? 4.137   22.756  41.738  1.00 82.31  ? 153 TRP A O     1 
ATOM   1177  C CB    . TRP A 1 153 ? 2.898   23.622  38.870  1.00 89.10  ? 153 TRP A CB    1 
ATOM   1178  C CG    . TRP A 1 153 ? 2.593   24.671  37.856  1.00 98.95  ? 153 TRP A CG    1 
ATOM   1179  C CD1   . TRP A 1 153 ? 1.482   25.459  37.794  1.00 116.43 ? 153 TRP A CD1   1 
ATOM   1180  C CD2   . TRP A 1 153 ? 3.410   25.027  36.732  1.00 108.16 ? 153 TRP A CD2   1 
ATOM   1181  N NE1   . TRP A 1 153 ? 1.561   26.299  36.718  1.00 121.08 ? 153 TRP A NE1   1 
ATOM   1182  C CE2   . TRP A 1 153 ? 2.732   26.060  36.047  1.00 118.82 ? 153 TRP A CE2   1 
ATOM   1183  C CE3   . TRP A 1 153 ? 4.643   24.585  36.245  1.00 101.43 ? 153 TRP A CE3   1 
ATOM   1184  C CZ2   . TRP A 1 153 ? 3.253   26.661  34.901  1.00 113.62 ? 153 TRP A CZ2   1 
ATOM   1185  C CZ3   . TRP A 1 153 ? 5.149   25.177  35.109  1.00 104.23 ? 153 TRP A CZ3   1 
ATOM   1186  C CH2   . TRP A 1 153 ? 4.468   26.201  34.449  1.00 105.46 ? 153 TRP A CH2   1 
ATOM   1187  N N     . GLY A 1 154 ? 2.090   21.933  41.229  1.00 49.29  ? 154 GLY A N     1 
ATOM   1188  C CA    . GLY A 1 154 ? 2.381   20.541  41.520  1.00 48.03  ? 154 GLY A CA    1 
ATOM   1189  C C     . GLY A 1 154 ? 2.031   20.150  42.952  1.00 44.61  ? 154 GLY A C     1 
ATOM   1190  O O     . GLY A 1 154 ? 1.600   20.993  43.745  1.00 39.58  ? 154 GLY A O     1 
ATOM   1191  N N     . SER A 1 155 ? 2.150   18.835  43.187  1.00 42.46  ? 155 SER A N     1 
ATOM   1192  C CA    . SER A 1 155 ? 1.867   18.143  44.432  1.00 44.89  ? 155 SER A CA    1 
ATOM   1193  C C     . SER A 1 155 ? 3.150   17.949  45.243  1.00 56.61  ? 155 SER A C     1 
ATOM   1194  O O     . SER A 1 155 ? 4.138   17.437  44.701  1.00 64.69  ? 155 SER A O     1 
ATOM   1195  C CB    . SER A 1 155 ? 1.302   16.799  44.089  1.00 48.37  ? 155 SER A CB    1 
ATOM   1196  O OG    . SER A 1 155 ? 1.404   15.905  45.185  1.00 62.44  ? 155 SER A OG    1 
ATOM   1197  N N     . VAL A 1 156 ? 3.106   18.306  46.535  1.00 51.88  ? 156 VAL A N     1 
ATOM   1198  C CA    . VAL A 1 156 ? 4.155   18.004  47.507  1.00 48.15  ? 156 VAL A CA    1 
ATOM   1199  C C     . VAL A 1 156 ? 4.623   16.557  47.319  1.00 47.86  ? 156 VAL A C     1 
ATOM   1200  O O     . VAL A 1 156 ? 5.829   16.271  47.292  1.00 47.79  ? 156 VAL A O     1 
ATOM   1201  C CB    . VAL A 1 156 ? 3.657   18.226  48.955  1.00 47.89  ? 156 VAL A CB    1 
ATOM   1202  C CG1   . VAL A 1 156 ? 4.749   18.011  49.991  1.00 54.42  ? 156 VAL A CG1   1 
ATOM   1203  C CG2   . VAL A 1 156 ? 3.050   19.603  49.165  1.00 47.02  ? 156 VAL A CG2   1 
ATOM   1204  N N     . VAL A 1 157 ? 3.653   15.646  47.199  1.00 44.28  ? 157 VAL A N     1 
ATOM   1205  C CA    . VAL A 1 157 ? 3.943   14.228  47.061  1.00 50.23  ? 157 VAL A CA    1 
ATOM   1206  C C     . VAL A 1 157 ? 4.508   13.939  45.670  1.00 49.95  ? 157 VAL A C     1 
ATOM   1207  O O     . VAL A 1 157 ? 5.567   13.341  45.524  1.00 63.77  ? 157 VAL A O     1 
ATOM   1208  C CB    . VAL A 1 157 ? 2.688   13.376  47.334  1.00 50.36  ? 157 VAL A CB    1 
ATOM   1209  C CG1   . VAL A 1 157 ? 2.993   11.888  47.279  1.00 48.59  ? 157 VAL A CG1   1 
ATOM   1210  C CG2   . VAL A 1 157 ? 2.042   13.733  48.660  1.00 53.32  ? 157 VAL A CG2   1 
ATOM   1211  N N     . GLY A 1 158 ? 3.766   14.316  44.637  1.00 47.76  ? 158 GLY A N     1 
ATOM   1212  C CA    . GLY A 1 158 ? 4.103   13.918  43.285  1.00 49.27  ? 158 GLY A CA    1 
ATOM   1213  C C     . GLY A 1 158 ? 5.495   14.402  42.874  1.00 46.36  ? 158 GLY A C     1 
ATOM   1214  O O     . GLY A 1 158 ? 6.226   13.650  42.251  1.00 36.32  ? 158 GLY A O     1 
ATOM   1215  N N     . ASN A 1 159 ? 5.814   15.656  43.216  1.00 42.87  ? 159 ASN A N     1 
ATOM   1216  C CA    . ASN A 1 159 ? 7.108   16.246  42.926  1.00 52.70  ? 159 ASN A CA    1 
ATOM   1217  C C     . ASN A 1 159 ? 8.235   15.466  43.590  1.00 53.36  ? 159 ASN A C     1 
ATOM   1218  O O     . ASN A 1 159 ? 9.253   15.203  42.963  1.00 55.42  ? 159 ASN A O     1 
ATOM   1219  C CB    . ASN A 1 159 ? 7.222   17.663  43.466  1.00 49.41  ? 159 ASN A CB    1 
ATOM   1220  C CG    . ASN A 1 159 ? 8.524   18.316  43.083  1.00 50.03  ? 159 ASN A CG    1 
ATOM   1221  O OD1   . ASN A 1 159 ? 9.553   18.089  43.702  1.00 60.07  ? 159 ASN A OD1   1 
ATOM   1222  N ND2   . ASN A 1 159 ? 8.477   19.196  42.106  1.00 59.19  ? 159 ASN A ND2   1 
ATOM   1223  N N     . ALA A 1 160 ? 8.034   15.121  44.860  1.00 46.33  ? 160 ALA A N     1 
ATOM   1224  C CA    . ALA A 1 160 ? 9.015   14.373  45.625  1.00 51.34  ? 160 ALA A CA    1 
ATOM   1225  C C     . ALA A 1 160 ? 9.239   12.969  45.055  1.00 51.09  ? 160 ALA A C     1 
ATOM   1226  O O     . ALA A 1 160 ? 10.386  12.488  45.056  1.00 49.43  ? 160 ALA A O     1 
ATOM   1227  C CB    . ALA A 1 160 ? 8.586   14.286  47.077  1.00 46.50  ? 160 ALA A CB    1 
ATOM   1228  N N     . LEU A 1 161 ? 8.152   12.296  44.635  1.00 46.55  ? 161 LEU A N     1 
ATOM   1229  C CA    . LEU A 1 161 ? 8.257   10.911  44.192  1.00 46.42  ? 161 LEU A CA    1 
ATOM   1230  C C     . LEU A 1 161 ? 9.042   10.863  42.896  1.00 45.10  ? 161 LEU A C     1 
ATOM   1231  O O     . LEU A 1 161 ? 9.575   9.808   42.544  1.00 39.39  ? 161 LEU A O     1 
ATOM   1232  C CB    . LEU A 1 161 ? 6.880   10.284  43.978  1.00 47.90  ? 161 LEU A CB    1 
ATOM   1233  C CG    . LEU A 1 161 ? 6.073   10.033  45.250  1.00 53.75  ? 161 LEU A CG    1 
ATOM   1234  C CD1   . LEU A 1 161 ? 4.895   9.117   44.941  1.00 52.59  ? 161 LEU A CD1   1 
ATOM   1235  C CD2   . LEU A 1 161 ? 6.939   9.451   46.372  1.00 49.45  ? 161 LEU A CD2   1 
ATOM   1236  N N     . ASP A 1 162 ? 9.094   12.016  42.208  1.00 37.95  ? 162 ASP A N     1 
ATOM   1237  C CA    . ASP A 1 162 ? 9.768   12.062  40.934  1.00 43.64  ? 162 ASP A CA    1 
ATOM   1238  C C     . ASP A 1 162 ? 11.161  12.654  41.148  1.00 42.96  ? 162 ASP A C     1 
ATOM   1239  O O     . ASP A 1 162 ? 11.801  12.974  40.163  1.00 43.24  ? 162 ASP A O     1 
ATOM   1240  C CB    . ASP A 1 162 ? 8.903   12.776  39.888  1.00 47.71  ? 162 ASP A CB    1 
ATOM   1241  C CG    . ASP A 1 162 ? 9.199   12.373  38.451  1.00 52.92  ? 162 ASP A CG    1 
ATOM   1242  O OD1   . ASP A 1 162 ? 9.050   11.160  38.102  1.00 55.33  ? 162 ASP A OD1   1 
ATOM   1243  O OD2   . ASP A 1 162 ? 9.608   13.260  37.701  1.00 54.02  ? 162 ASP A OD2   1 
ATOM   1244  N N     . HIS A 1 163 ? 11.633  12.742  42.412  1.00 36.72  ? 163 HIS A N     1 
ATOM   1245  C CA    . HIS A 1 163 ? 12.985  13.166  42.750  1.00 38.23  ? 163 HIS A CA    1 
ATOM   1246  C C     . HIS A 1 163 ? 13.166  14.642  42.376  1.00 44.31  ? 163 HIS A C     1 
ATOM   1247  O O     . HIS A 1 163 ? 14.241  15.097  41.928  1.00 39.17  ? 163 HIS A O     1 
ATOM   1248  C CB    . HIS A 1 163 ? 14.069  12.258  42.151  1.00 34.71  ? 163 HIS A CB    1 
ATOM   1249  C CG    . HIS A 1 163 ? 14.016  10.808  42.575  1.00 38.60  ? 163 HIS A CG    1 
ATOM   1250  N ND1   . HIS A 1 163 ? 14.646  9.809   41.850  1.00 34.68  ? 163 HIS A ND1   1 
ATOM   1251  C CD2   . HIS A 1 163 ? 13.365  10.187  43.578  1.00 38.87  ? 163 HIS A CD2   1 
ATOM   1252  C CE1   . HIS A 1 163 ? 14.401  8.636   42.427  1.00 39.67  ? 163 HIS A CE1   1 
ATOM   1253  N NE2   . HIS A 1 163 ? 13.633  8.840   43.483  1.00 39.26  ? 163 HIS A NE2   1 
ATOM   1254  N N     . GLY A 1 164 ? 12.101  15.399  42.612  1.00 34.78  ? 164 GLY A N     1 
ATOM   1255  C CA    . GLY A 1 164 ? 12.112  16.809  42.274  1.00 41.86  ? 164 GLY A CA    1 
ATOM   1256  C C     . GLY A 1 164 ? 12.880  17.627  43.297  1.00 46.35  ? 164 GLY A C     1 
ATOM   1257  O O     . GLY A 1 164 ? 13.279  17.107  44.340  1.00 49.17  ? 164 GLY A O     1 
ATOM   1258  N N     . ILE A 1 165 ? 13.049  18.915  42.980  1.00 52.20  ? 165 ILE A N     1 
ATOM   1259  C CA    . ILE A 1 165 ? 14.016  19.741  43.674  1.00 52.94  ? 165 ILE A CA    1 
ATOM   1260  C C     . ILE A 1 165 ? 13.537  21.188  43.810  1.00 54.37  ? 165 ILE A C     1 
ATOM   1261  O O     . ILE A 1 165 ? 12.797  21.714  42.979  1.00 51.61  ? 165 ILE A O     1 
ATOM   1262  C CB    . ILE A 1 165 ? 15.376  19.660  42.964  1.00 58.71  ? 165 ILE A CB    1 
ATOM   1263  C CG1   . ILE A 1 165 ? 15.308  20.206  41.534  1.00 77.16  ? 165 ILE A CG1   1 
ATOM   1264  C CG2   . ILE A 1 165 ? 15.905  18.231  43.019  1.00 58.32  ? 165 ILE A CG2   1 
ATOM   1265  C CD1   . ILE A 1 165 ? 16.562  20.983  41.095  1.00 87.14  ? 165 ILE A CD1   1 
ATOM   1266  N N     . GLY A 1 166 ? 14.018  21.843  44.871  1.00 49.11  ? 166 GLY A N     1 
ATOM   1267  C CA    . GLY A 1 166 ? 13.702  23.235  45.125  1.00 47.55  ? 166 GLY A CA    1 
ATOM   1268  C C     . GLY A 1 166 ? 14.951  24.037  45.467  1.00 45.47  ? 166 GLY A C     1 
ATOM   1269  O O     . GLY A 1 166 ? 16.056  23.668  45.083  1.00 45.82  ? 166 GLY A O     1 
ATOM   1270  N N     . TYR A 1 167 ? 14.757  25.157  46.156  1.00 43.27  ? 167 TYR A N     1 
ATOM   1271  C CA    . TYR A 1 167 ? 15.737  26.228  46.119  1.00 42.57  ? 167 TYR A CA    1 
ATOM   1272  C C     . TYR A 1 167 ? 16.095  26.710  47.521  1.00 41.28  ? 167 TYR A C     1 
ATOM   1273  O O     . TYR A 1 167 ? 16.645  27.791  47.651  1.00 47.24  ? 167 TYR A O     1 
ATOM   1274  C CB    . TYR A 1 167 ? 15.213  27.323  45.186  1.00 47.12  ? 167 TYR A CB    1 
ATOM   1275  C CG    . TYR A 1 167 ? 15.075  26.838  43.765  1.00 54.90  ? 167 TYR A CG    1 
ATOM   1276  C CD1   . TYR A 1 167 ? 16.195  26.707  42.961  1.00 70.40  ? 167 TYR A CD1   1 
ATOM   1277  C CD2   . TYR A 1 167 ? 13.865  26.396  43.260  1.00 53.81  ? 167 TYR A CD2   1 
ATOM   1278  C CE1   . TYR A 1 167 ? 16.109  26.199  41.674  1.00 79.88  ? 167 TYR A CE1   1 
ATOM   1279  C CE2   . TYR A 1 167 ? 13.759  25.894  41.971  1.00 59.70  ? 167 TYR A CE2   1 
ATOM   1280  C CZ    . TYR A 1 167 ? 14.887  25.792  41.173  1.00 71.00  ? 167 TYR A CZ    1 
ATOM   1281  O OH    . TYR A 1 167 ? 14.857  25.282  39.900  1.00 75.98  ? 167 TYR A OH    1 
ATOM   1282  N N     . THR A 1 168 ? 15.807  25.896  48.549  1.00 46.25  ? 168 THR A N     1 
ATOM   1283  C CA    . THR A 1 168 ? 16.218  26.147  49.928  1.00 48.19  ? 168 THR A CA    1 
ATOM   1284  C C     . THR A 1 168 ? 17.051  24.960  50.433  1.00 49.30  ? 168 THR A C     1 
ATOM   1285  O O     . THR A 1 168 ? 17.182  23.936  49.757  1.00 45.26  ? 168 THR A O     1 
ATOM   1286  C CB    . THR A 1 168 ? 15.002  26.351  50.860  1.00 46.23  ? 168 THR A CB    1 
ATOM   1287  O OG1   . THR A 1 168 ? 14.614  25.132  51.506  1.00 37.18  ? 168 THR A OG1   1 
ATOM   1288  C CG2   . THR A 1 168 ? 13.813  26.956  50.148  1.00 41.99  ? 168 THR A CG2   1 
ATOM   1289  N N     . PRO A 1 169 ? 17.564  24.987  51.684  1.00 49.09  ? 169 PRO A N     1 
ATOM   1290  C CA    . PRO A 1 169 ? 18.276  23.822  52.215  1.00 44.49  ? 169 PRO A CA    1 
ATOM   1291  C C     . PRO A 1 169 ? 17.482  22.509  52.182  1.00 44.14  ? 169 PRO A C     1 
ATOM   1292  O O     . PRO A 1 169 ? 18.102  21.453  52.217  1.00 45.28  ? 169 PRO A O     1 
ATOM   1293  C CB    . PRO A 1 169 ? 18.631  24.268  53.641  1.00 42.13  ? 169 PRO A CB    1 
ATOM   1294  C CG    . PRO A 1 169 ? 18.706  25.788  53.542  1.00 46.89  ? 169 PRO A CG    1 
ATOM   1295  C CD    . PRO A 1 169 ? 17.551  26.131  52.620  1.00 49.45  ? 169 PRO A CD    1 
ATOM   1296  N N     . TYR A 1 170 ? 16.133  22.568  52.092  1.00 44.89  ? 170 TYR A N     1 
ATOM   1297  C CA    . TYR A 1 170 ? 15.279  21.385  51.958  1.00 41.71  ? 170 TYR A CA    1 
ATOM   1298  C C     . TYR A 1 170 ? 14.953  21.162  50.476  1.00 42.49  ? 170 TYR A C     1 
ATOM   1299  O O     . TYR A 1 170 ? 13.865  20.731  50.092  1.00 46.32  ? 170 TYR A O     1 
ATOM   1300  C CB    . TYR A 1 170 ? 14.044  21.488  52.870  1.00 42.04  ? 170 TYR A CB    1 
ATOM   1301  C CG    . TYR A 1 170 ? 14.277  21.290  54.357  1.00 44.91  ? 170 TYR A CG    1 
ATOM   1302  C CD1   . TYR A 1 170 ? 15.347  21.879  55.027  1.00 49.62  ? 170 TYR A CD1   1 
ATOM   1303  C CD2   . TYR A 1 170 ? 13.418  20.515  55.114  1.00 43.97  ? 170 TYR A CD2   1 
ATOM   1304  C CE1   . TYR A 1 170 ? 15.570  21.677  56.385  1.00 47.78  ? 170 TYR A CE1   1 
ATOM   1305  C CE2   . TYR A 1 170 ? 13.626  20.308  56.473  1.00 54.58  ? 170 TYR A CE2   1 
ATOM   1306  C CZ    . TYR A 1 170 ? 14.706  20.890  57.120  1.00 46.62  ? 170 TYR A CZ    1 
ATOM   1307  O OH    . TYR A 1 170 ? 14.886  20.697  58.474  1.00 47.13  ? 170 TYR A OH    1 
ATOM   1308  N N     . GLY A 1 171 ? 15.968  21.384  49.639  1.00 49.68  ? 171 GLY A N     1 
ATOM   1309  C CA    . GLY A 1 171 ? 15.828  21.335  48.198  1.00 50.53  ? 171 GLY A CA    1 
ATOM   1310  C C     . GLY A 1 171 ? 15.623  19.928  47.636  1.00 43.50  ? 171 GLY A C     1 
ATOM   1311  O O     . GLY A 1 171 ? 14.956  19.787  46.628  1.00 50.98  ? 171 GLY A O     1 
ATOM   1312  N N     . ASP A 1 172 ? 16.218  18.904  48.241  1.00 40.40  ? 172 ASP A N     1 
ATOM   1313  C CA    . ASP A 1 172 ? 16.112  17.533  47.744  1.00 36.45  ? 172 ASP A CA    1 
ATOM   1314  C C     . ASP A 1 172 ? 14.832  16.906  48.312  1.00 41.35  ? 172 ASP A C     1 
ATOM   1315  O O     . ASP A 1 172 ? 14.826  16.297  49.381  1.00 39.06  ? 172 ASP A O     1 
ATOM   1316  C CB    . ASP A 1 172 ? 17.405  16.827  48.122  1.00 32.69  ? 172 ASP A CB    1 
ATOM   1317  C CG    . ASP A 1 172 ? 17.611  15.408  47.637  1.00 39.98  ? 172 ASP A CG    1 
ATOM   1318  O OD1   . ASP A 1 172 ? 16.611  14.759  47.249  1.00 34.92  ? 172 ASP A OD1   1 
ATOM   1319  O OD2   . ASP A 1 172 ? 18.810  14.963  47.685  1.00 38.20  ? 172 ASP A OD2   1 
ATOM   1320  N N     . HIS A 1 173 ? 13.713  17.062  47.593  1.00 38.87  ? 173 HIS A N     1 
ATOM   1321  C CA    . HIS A 1 173 ? 12.396  16.851  48.172  1.00 31.61  ? 173 HIS A CA    1 
ATOM   1322  C C     . HIS A 1 173 ? 12.269  15.453  48.743  1.00 36.99  ? 173 HIS A C     1 
ATOM   1323  O O     . HIS A 1 173 ? 11.848  15.283  49.877  1.00 47.86  ? 173 HIS A O     1 
ATOM   1324  C CB    . HIS A 1 173 ? 11.319  17.195  47.161  1.00 31.78  ? 173 HIS A CB    1 
ATOM   1325  C CG    . HIS A 1 173 ? 11.254  18.642  46.869  1.00 32.86  ? 173 HIS A CG    1 
ATOM   1326  N ND1   . HIS A 1 173 ? 10.467  19.137  45.850  1.00 36.86  ? 173 HIS A ND1   1 
ATOM   1327  C CD2   . HIS A 1 173 ? 11.912  19.690  47.407  1.00 32.85  ? 173 HIS A CD2   1 
ATOM   1328  C CE1   . HIS A 1 173 ? 10.625  20.456  45.799  1.00 43.33  ? 173 HIS A CE1   1 
ATOM   1329  N NE2   . HIS A 1 173 ? 11.501  20.818  46.743  1.00 38.78  ? 173 HIS A NE2   1 
ATOM   1330  N N     . PHE A 1 174 ? 12.685  14.447  47.997  1.00 35.45  ? 174 PHE A N     1 
ATOM   1331  C CA    . PHE A 1 174 ? 12.574  13.086  48.491  1.00 37.00  ? 174 PHE A CA    1 
ATOM   1332  C C     . PHE A 1 174 ? 13.587  12.814  49.608  1.00 39.20  ? 174 PHE A C     1 
ATOM   1333  O O     . PHE A 1 174 ? 13.364  11.970  50.478  1.00 41.65  ? 174 PHE A O     1 
ATOM   1334  C CB    . PHE A 1 174 ? 12.773  12.074  47.366  1.00 34.20  ? 174 PHE A CB    1 
ATOM   1335  C CG    . PHE A 1 174 ? 12.306  10.703  47.740  1.00 34.63  ? 174 PHE A CG    1 
ATOM   1336  C CD1   . PHE A 1 174 ? 10.968  10.470  47.985  1.00 34.51  ? 174 PHE A CD1   1 
ATOM   1337  C CD2   . PHE A 1 174 ? 13.203  9.679   47.925  1.00 35.33  ? 174 PHE A CD2   1 
ATOM   1338  C CE1   . PHE A 1 174 ? 10.533  9.221   48.369  1.00 37.26  ? 174 PHE A CE1   1 
ATOM   1339  C CE2   . PHE A 1 174 ? 12.770  8.426   48.309  1.00 37.89  ? 174 PHE A CE2   1 
ATOM   1340  C CZ    . PHE A 1 174 ? 11.436  8.199   48.536  1.00 40.85  ? 174 PHE A CZ    1 
ATOM   1341  N N     . ALA A 1 175 ? 14.714  13.521  49.636  1.00 35.06  ? 175 ALA A N     1 
ATOM   1342  C CA    . ALA A 1 175 ? 15.596  13.337  50.793  1.00 37.98  ? 175 ALA A CA    1 
ATOM   1343  C C     . ALA A 1 175 ? 14.854  13.703  52.089  1.00 34.04  ? 175 ALA A C     1 
ATOM   1344  O O     . ALA A 1 175 ? 15.055  13.071  53.107  1.00 38.49  ? 175 ALA A O     1 
ATOM   1345  C CB    . ALA A 1 175 ? 16.900  14.134  50.637  1.00 36.73  ? 175 ALA A CB    1 
ATOM   1346  N N     . MET A 1 176 ? 14.009  14.737  52.041  1.00 40.32  ? 176 MET A N     1 
ATOM   1347  C CA    . MET A 1 176 ? 13.252  15.235  53.178  1.00 41.49  ? 176 MET A CA    1 
ATOM   1348  C C     . MET A 1 176 ? 12.002  14.407  53.422  1.00 35.98  ? 176 MET A C     1 
ATOM   1349  O O     . MET A 1 176 ? 11.287  14.665  54.369  1.00 48.46  ? 176 MET A O     1 
ATOM   1350  C CB    . MET A 1 176 ? 12.843  16.696  52.984  1.00 36.02  ? 176 MET A CB    1 
ATOM   1351  C CG    . MET A 1 176 ? 14.041  17.642  52.873  1.00 38.63  ? 176 MET A CG    1 
ATOM   1352  S SD    . MET A 1 176 ? 15.361  17.490  54.162  1.00 46.27  ? 176 MET A SD    1 
ATOM   1353  C CE    . MET A 1 176 ? 16.319  16.116  53.539  1.00 55.55  ? 176 MET A CE    1 
ATOM   1354  N N     . GLN A 1 177 ? 11.794  13.345  52.661  1.00 41.09  ? 177 GLN A N     1 
ATOM   1355  C CA    . GLN A 1 177 ? 10.617  12.531  52.889  1.00 39.38  ? 177 GLN A CA    1 
ATOM   1356  C C     . GLN A 1 177 ? 10.838  11.571  54.057  1.00 40.52  ? 177 GLN A C     1 
ATOM   1357  O O     . GLN A 1 177 ? 11.960  11.177  54.361  1.00 41.24  ? 177 GLN A O     1 
ATOM   1358  C CB    . GLN A 1 177 ? 10.209  11.847  51.595  1.00 34.36  ? 177 GLN A CB    1 
ATOM   1359  C CG    . GLN A 1 177 ? 9.063   10.866  51.799  1.00 43.16  ? 177 GLN A CG    1 
ATOM   1360  C CD    . GLN A 1 177 ? 9.566   9.482   52.157  1.00 42.44  ? 177 GLN A CD    1 
ATOM   1361  O OE1   . GLN A 1 177 ? 10.708  9.144   51.848  1.00 50.47  ? 177 GLN A OE1   1 
ATOM   1362  N NE2   . GLN A 1 177 ? 8.731   8.675   52.797  1.00 32.49  ? 177 GLN A NE2   1 
ATOM   1363  N N     . CYS A 1 178 ? 9.726   11.178  54.703  1.00 43.95  ? 178 CYS A N     1 
ATOM   1364  C CA    . CYS A 1 178 ? 9.772   10.401  55.927  1.00 37.99  ? 178 CYS A CA    1 
ATOM   1365  C C     . CYS A 1 178 ? 8.406   9.802   56.270  1.00 43.73  ? 178 CYS A C     1 
ATOM   1366  O O     . CYS A 1 178 ? 7.501   10.499  56.729  1.00 38.05  ? 178 CYS A O     1 
ATOM   1367  C CB    . CYS A 1 178 ? 10.219  11.316  57.055  1.00 39.14  ? 178 CYS A CB    1 
ATOM   1368  S SG    . CYS A 1 178 ? 10.636  10.396  58.544  1.00 42.55  ? 178 CYS A SG    1 
ATOM   1369  N N     . GLY A 1 179 ? 8.293   8.482   56.104  1.00 44.92  ? 179 GLY A N     1 
ATOM   1370  C CA    . GLY A 1 179 ? 7.038   7.781   56.252  1.00 39.59  ? 179 GLY A CA    1 
ATOM   1371  C C     . GLY A 1 179 ? 6.108   7.998   55.057  1.00 39.53  ? 179 GLY A C     1 
ATOM   1372  O O     . GLY A 1 179 ? 5.903   9.118   54.584  1.00 39.76  ? 179 GLY A O     1 
ATOM   1373  N N     . MET A 1 180 ? 5.515   6.910   54.573  1.00 40.27  ? 180 MET A N     1 
ATOM   1374  C CA    . MET A 1 180 ? 4.479   7.009   53.559  1.00 42.20  ? 180 MET A CA    1 
ATOM   1375  C C     . MET A 1 180 ? 3.552   5.813   53.712  1.00 42.26  ? 180 MET A C     1 
ATOM   1376  O O     . MET A 1 180 ? 3.954   4.776   54.280  1.00 37.19  ? 180 MET A O     1 
ATOM   1377  C CB    . MET A 1 180 ? 5.050   7.040   52.119  1.00 41.36  ? 180 MET A CB    1 
ATOM   1378  C CG    . MET A 1 180 ? 5.882   5.830   51.735  1.00 40.79  ? 180 MET A CG    1 
ATOM   1379  S SD    . MET A 1 180 ? 6.271   5.657   49.925  1.00 48.56  ? 180 MET A SD    1 
ATOM   1380  C CE    . MET A 1 180 ? 7.408   7.020   49.681  1.00 52.02  ? 180 MET A CE    1 
ATOM   1381  N N     . GLU A 1 181 ? 2.328   5.986   53.183  1.00 45.86  ? 181 GLU A N     1 
ATOM   1382  C CA    . GLU A 1 181 ? 1.392   4.887   52.991  1.00 44.51  ? 181 GLU A CA    1 
ATOM   1383  C C     . GLU A 1 181 ? 1.247   4.577   51.508  1.00 45.04  ? 181 GLU A C     1 
ATOM   1384  O O     . GLU A 1 181 ? 1.081   5.481   50.697  1.00 43.83  ? 181 GLU A O     1 
ATOM   1385  C CB    . GLU A 1 181 ? 0.010   5.264   53.491  1.00 47.83  ? 181 GLU A CB    1 
ATOM   1386  C CG    . GLU A 1 181 ? -0.980  4.109   53.482  1.00 50.08  ? 181 GLU A CG    1 
ATOM   1387  C CD    . GLU A 1 181 ? -2.325  4.557   54.028  1.00 61.62  ? 181 GLU A CD    1 
ATOM   1388  O OE1   . GLU A 1 181 ? -2.617  4.279   55.230  1.00 59.09  ? 181 GLU A OE1   1 
ATOM   1389  O OE2   . GLU A 1 181 ? -3.045  5.264   53.280  1.00 63.16  ? 181 GLU A OE2   1 
ATOM   1390  N N     . VAL A 1 182 ? 1.231   3.283   51.185  1.00 42.69  ? 182 VAL A N     1 
ATOM   1391  C CA    . VAL A 1 182 ? 1.334   2.841   49.810  1.00 49.65  ? 182 VAL A CA    1 
ATOM   1392  C C     . VAL A 1 182 ? 0.286   1.756   49.597  1.00 52.33  ? 182 VAL A C     1 
ATOM   1393  O O     . VAL A 1 182 ? 0.264   0.769   50.325  1.00 55.79  ? 182 VAL A O     1 
ATOM   1394  C CB    . VAL A 1 182 ? 2.755   2.318   49.480  1.00 50.78  ? 182 VAL A CB    1 
ATOM   1395  C CG1   . VAL A 1 182 ? 2.857   1.751   48.073  1.00 46.92  ? 182 VAL A CG1   1 
ATOM   1396  C CG2   . VAL A 1 182 ? 3.823   3.387   49.691  1.00 50.24  ? 182 VAL A CG2   1 
ATOM   1397  N N     . VAL A 1 183 ? -0.565  1.940   48.584  1.00 47.74  ? 183 VAL A N     1 
ATOM   1398  C CA    . VAL A 1 183 ? -1.424  0.871   48.143  1.00 47.99  ? 183 VAL A CA    1 
ATOM   1399  C C     . VAL A 1 183 ? -0.635  0.052   47.132  1.00 47.02  ? 183 VAL A C     1 
ATOM   1400  O O     . VAL A 1 183 ? -0.270  0.558   46.067  1.00 45.97  ? 183 VAL A O     1 
ATOM   1401  C CB    . VAL A 1 183 ? -2.734  1.393   47.540  1.00 48.13  ? 183 VAL A CB    1 
ATOM   1402  C CG1   . VAL A 1 183 ? -3.576  0.235   47.069  1.00 52.60  ? 183 VAL A CG1   1 
ATOM   1403  C CG2   . VAL A 1 183 ? -3.504  2.262   48.505  1.00 48.43  ? 183 VAL A CG2   1 
ATOM   1404  N N     . LEU A 1 184 ? -0.377  -1.205  47.499  1.00 43.39  ? 184 LEU A N     1 
ATOM   1405  C CA    . LEU A 1 184 ? 0.335   -2.133  46.644  1.00 54.69  ? 184 LEU A CA    1 
ATOM   1406  C C     . LEU A 1 184 ? -0.534  -2.553  45.448  1.00 63.75  ? 184 LEU A C     1 
ATOM   1407  O O     . LEU A 1 184 ? -1.765  -2.434  45.445  1.00 57.32  ? 184 LEU A O     1 
ATOM   1408  C CB    . LEU A 1 184 ? 0.768   -3.333  47.499  1.00 61.08  ? 184 LEU A CB    1 
ATOM   1409  C CG    . LEU A 1 184 ? 1.680   -3.026  48.699  1.00 60.62  ? 184 LEU A CG    1 
ATOM   1410  C CD1   . LEU A 1 184 ? 2.148   -4.314  49.367  1.00 64.62  ? 184 LEU A CD1   1 
ATOM   1411  C CD2   . LEU A 1 184 ? 2.889   -2.196  48.292  1.00 54.64  ? 184 LEU A CD2   1 
ATOM   1412  N N     . PRO A 1 185 ? 0.084   -3.106  44.384  1.00 63.48  ? 185 PRO A N     1 
ATOM   1413  C CA    . PRO A 1 185 ? -0.667  -3.539  43.211  1.00 64.21  ? 185 PRO A CA    1 
ATOM   1414  C C     . PRO A 1 185 ? -1.738  -4.588  43.499  1.00 67.00  ? 185 PRO A C     1 
ATOM   1415  O O     . PRO A 1 185 ? -2.701  -4.708  42.749  1.00 67.87  ? 185 PRO A O     1 
ATOM   1416  C CB    . PRO A 1 185 ? 0.409   -4.158  42.313  1.00 67.96  ? 185 PRO A CB    1 
ATOM   1417  C CG    . PRO A 1 185 ? 1.703   -3.543  42.787  1.00 64.69  ? 185 PRO A CG    1 
ATOM   1418  C CD    . PRO A 1 185 ? 1.519   -3.401  44.277  1.00 64.55  ? 185 PRO A CD    1 
ATOM   1419  N N     . ASN A 1 186 ? -1.597  -5.345  44.593  1.00 68.33  ? 186 ASN A N     1 
ATOM   1420  C CA    . ASN A 1 186 ? -2.546  -6.421  44.839  1.00 59.97  ? 186 ASN A CA    1 
ATOM   1421  C C     . ASN A 1 186 ? -3.761  -5.877  45.579  1.00 52.06  ? 186 ASN A C     1 
ATOM   1422  O O     . ASN A 1 186 ? -4.674  -6.645  45.828  1.00 53.56  ? 186 ASN A O     1 
ATOM   1423  C CB    . ASN A 1 186 ? -1.931  -7.619  45.567  1.00 57.66  ? 186 ASN A CB    1 
ATOM   1424  C CG    . ASN A 1 186 ? -1.485  -7.253  46.958  1.00 53.37  ? 186 ASN A CG    1 
ATOM   1425  O OD1   . ASN A 1 186 ? -1.639  -6.100  47.358  1.00 54.16  ? 186 ASN A OD1   1 
ATOM   1426  N ND2   . ASN A 1 186 ? -0.915  -8.208  47.675  1.00 47.15  ? 186 ASN A ND2   1 
ATOM   1427  N N     . GLY A 1 187 ? -3.787  -4.568  45.874  1.00 51.99  ? 187 GLY A N     1 
ATOM   1428  C CA    . GLY A 1 187 ? -4.874  -3.968  46.633  1.00 53.39  ? 187 GLY A CA    1 
ATOM   1429  C C     . GLY A 1 187 ? -4.543  -3.660  48.105  1.00 52.85  ? 187 GLY A C     1 
ATOM   1430  O O     . GLY A 1 187 ? -5.139  -2.746  48.686  1.00 55.20  ? 187 GLY A O     1 
ATOM   1431  N N     . GLU A 1 188 ? -3.573  -4.372  48.697  1.00 54.96  ? 188 GLU A N     1 
ATOM   1432  C CA    . GLU A 1 188 ? -3.231  -4.246  50.119  1.00 60.11  ? 188 GLU A CA    1 
ATOM   1433  C C     . GLU A 1 188 ? -2.555  -2.899  50.392  1.00 54.87  ? 188 GLU A C     1 
ATOM   1434  O O     . GLU A 1 188 ? -1.981  -2.302  49.487  1.00 64.30  ? 188 GLU A O     1 
ATOM   1435  C CB    . GLU A 1 188 ? -2.359  -5.423  50.586  1.00 56.41  ? 188 GLU A CB    1 
ATOM   1436  C CG    . GLU A 1 188 ? -3.100  -6.770  50.632  1.00 65.65  ? 188 GLU A CG    1 
ATOM   1437  C CD    . GLU A 1 188 ? -4.290  -6.862  51.589  1.00 79.11  ? 188 GLU A CD    1 
ATOM   1438  O OE1   . GLU A 1 188 ? -4.064  -7.099  52.801  1.00 76.39  ? 188 GLU A OE1   1 
ATOM   1439  O OE2   . GLU A 1 188 ? -5.449  -6.692  51.129  1.00 72.63  ? 188 GLU A OE2   1 
ATOM   1440  N N     . VAL A 1 189 ? -2.685  -2.396  51.631  1.00 49.57  ? 189 VAL A N     1 
ATOM   1441  C CA    . VAL A 1 189 ? -2.071  -1.136  52.035  1.00 53.44  ? 189 VAL A CA    1 
ATOM   1442  C C     . VAL A 1 189 ? -0.985  -1.428  53.078  1.00 49.53  ? 189 VAL A C     1 
ATOM   1443  O O     . VAL A 1 189 ? -1.028  -2.452  53.750  1.00 49.56  ? 189 VAL A O     1 
ATOM   1444  C CB    . VAL A 1 189 ? -3.107  -0.106  52.520  1.00 54.47  ? 189 VAL A CB    1 
ATOM   1445  C CG1   . VAL A 1 189 ? -4.008  -0.631  53.626  1.00 55.11  ? 189 VAL A CG1   1 
ATOM   1446  C CG2   . VAL A 1 189 ? -2.437  1.181   52.958  1.00 59.01  ? 189 VAL A CG2   1 
ATOM   1447  N N     . VAL A 1 190 ? 0.060   -0.599  53.103  1.00 48.95  ? 190 VAL A N     1 
ATOM   1448  C CA    . VAL A 1 190 ? 1.193   -0.771  54.007  1.00 49.66  ? 190 VAL A CA    1 
ATOM   1449  C C     . VAL A 1 190 ? 1.642   0.603   54.468  1.00 47.17  ? 190 VAL A C     1 
ATOM   1450  O O     . VAL A 1 190 ? 1.390   1.615   53.813  1.00 52.92  ? 190 VAL A O     1 
ATOM   1451  C CB    . VAL A 1 190 ? 2.386   -1.480  53.351  1.00 52.58  ? 190 VAL A CB    1 
ATOM   1452  C CG1   . VAL A 1 190 ? 2.038   -2.876  52.838  1.00 56.97  ? 190 VAL A CG1   1 
ATOM   1453  C CG2   . VAL A 1 190 ? 2.975   -0.627  52.236  1.00 46.37  ? 190 VAL A CG2   1 
ATOM   1454  N N     . ARG A 1 191 ? 2.275   0.629   55.626  1.00 50.13  ? 191 ARG A N     1 
ATOM   1455  C CA    . ARG A 1 191 ? 2.934   1.836   56.068  1.00 52.31  ? 191 ARG A CA    1 
ATOM   1456  C C     . ARG A 1 191 ? 4.383   1.475   56.318  1.00 49.03  ? 191 ARG A C     1 
ATOM   1457  O O     . ARG A 1 191 ? 4.678   0.395   56.836  1.00 54.33  ? 191 ARG A O     1 
ATOM   1458  C CB    . ARG A 1 191 ? 2.240   2.406   57.299  1.00 55.88  ? 191 ARG A CB    1 
ATOM   1459  C CG    . ARG A 1 191 ? 0.868   2.985   56.998  1.00 57.75  ? 191 ARG A CG    1 
ATOM   1460  C CD    . ARG A 1 191 ? 0.271   3.823   58.125  1.00 61.66  ? 191 ARG A CD    1 
ATOM   1461  N NE    . ARG A 1 191 ? -1.159  3.989   57.898  1.00 70.93  ? 191 ARG A NE    1 
ATOM   1462  C CZ    . ARG A 1 191 ? -1.972  4.878   58.465  1.00 70.76  ? 191 ARG A CZ    1 
ATOM   1463  N NH1   . ARG A 1 191 ? -1.537  5.966   59.084  1.00 60.41  ? 191 ARG A NH1   1 
ATOM   1464  N NH2   . ARG A 1 191 ? -3.265  4.709   58.292  1.00 81.62  ? 191 ARG A NH2   1 
ATOM   1465  N N     . THR A 1 192 ? 5.257   2.366   55.864  1.00 46.32  ? 192 THR A N     1 
ATOM   1466  C CA    . THR A 1 192 ? 6.699   2.192   56.005  1.00 43.75  ? 192 THR A CA    1 
ATOM   1467  C C     . THR A 1 192 ? 7.186   2.877   57.275  1.00 41.57  ? 192 THR A C     1 
ATOM   1468  O O     . THR A 1 192 ? 6.443   3.647   57.884  1.00 48.67  ? 192 THR A O     1 
ATOM   1469  C CB    . THR A 1 192 ? 7.463   2.807   54.829  1.00 39.32  ? 192 THR A CB    1 
ATOM   1470  O OG1   . THR A 1 192 ? 7.295   4.230   54.865  1.00 37.24  ? 192 THR A OG1   1 
ATOM   1471  C CG2   . THR A 1 192 ? 7.017   2.229   53.502  1.00 43.75  ? 192 THR A CG2   1 
ATOM   1472  N N     . GLY A 1 193 ? 8.449   2.631   57.617  1.00 40.06  ? 193 GLY A N     1 
ATOM   1473  C CA    . GLY A 1 193 ? 9.097   3.272   58.751  1.00 42.53  ? 193 GLY A CA    1 
ATOM   1474  C C     . GLY A 1 193 ? 8.378   2.933   60.055  1.00 46.57  ? 193 GLY A C     1 
ATOM   1475  O O     . GLY A 1 193 ? 7.958   1.790   60.293  1.00 44.04  ? 193 GLY A O     1 
ATOM   1476  N N     . MET A 1 194 ? 8.185   3.978   60.857  1.00 47.78  ? 194 MET A N     1 
ATOM   1477  C CA    . MET A 1 194 ? 7.611   3.837   62.178  1.00 51.82  ? 194 MET A CA    1 
ATOM   1478  C C     . MET A 1 194 ? 6.094   3.654   62.053  1.00 51.58  ? 194 MET A C     1 
ATOM   1479  O O     . MET A 1 194 ? 5.403   3.283   62.994  1.00 52.38  ? 194 MET A O     1 
ATOM   1480  C CB    . MET A 1 194 ? 7.960   5.069   63.022  1.00 51.84  ? 194 MET A CB    1 
ATOM   1481  C CG    . MET A 1 194 ? 9.464   5.206   63.382  1.00 48.90  ? 194 MET A CG    1 
ATOM   1482  S SD    . MET A 1 194 ? 10.310  3.662   63.878  1.00 49.49  ? 194 MET A SD    1 
ATOM   1483  C CE    . MET A 1 194 ? 9.288   3.085   65.233  1.00 54.84  ? 194 MET A CE    1 
ATOM   1484  N N     . GLY A 1 195 ? 5.568   3.841   60.851  1.00 49.90  ? 195 GLY A N     1 
ATOM   1485  C CA    . GLY A 1 195 ? 4.134   3.832   60.649  1.00 47.96  ? 195 GLY A CA    1 
ATOM   1486  C C     . GLY A 1 195 ? 3.599   2.412   60.620  1.00 46.49  ? 195 GLY A C     1 
ATOM   1487  O O     . GLY A 1 195 ? 2.378   2.213   60.592  1.00 51.34  ? 195 GLY A O     1 
ATOM   1488  N N     . ALA A 1 196 ? 4.530   1.447   60.597  1.00 38.58  ? 196 ALA A N     1 
ATOM   1489  C CA    . ALA A 1 196 ? 4.160   0.049   60.788  1.00 39.31  ? 196 ALA A CA    1 
ATOM   1490  C C     . ALA A 1 196 ? 4.088   -0.348  62.283  1.00 40.50  ? 196 ALA A C     1 
ATOM   1491  O O     . ALA A 1 196 ? 3.844   -1.516  62.581  1.00 36.42  ? 196 ALA A O     1 
ATOM   1492  C CB    . ALA A 1 196 ? 5.156   -0.821  60.037  1.00 34.86  ? 196 ALA A CB    1 
ATOM   1493  N N     . MET A 1 197 ? 4.400   0.573   63.216  1.00 39.74  ? 197 MET A N     1 
ATOM   1494  C CA    . MET A 1 197 ? 4.151   0.368   64.647  1.00 50.82  ? 197 MET A CA    1 
ATOM   1495  C C     . MET A 1 197 ? 2.768   0.899   65.029  1.00 48.41  ? 197 MET A C     1 
ATOM   1496  O O     . MET A 1 197 ? 2.486   2.094   64.879  1.00 44.59  ? 197 MET A O     1 
ATOM   1497  C CB    . MET A 1 197 ? 5.159   1.114   65.527  1.00 47.77  ? 197 MET A CB    1 
ATOM   1498  C CG    . MET A 1 197 ? 6.235   0.227   66.053  1.00 65.79  ? 197 MET A CG    1 
ATOM   1499  S SD    . MET A 1 197 ? 6.013   -0.144  67.795  1.00 62.13  ? 197 MET A SD    1 
ATOM   1500  C CE    . MET A 1 197 ? 6.312   1.507   68.398  1.00 60.49  ? 197 MET A CE    1 
ATOM   1501  N N     . PRO A 1 198 ? 1.852   0.047   65.528  1.00 46.08  ? 198 PRO A N     1 
ATOM   1502  C CA    . PRO A 1 198 ? 0.633   0.562   66.150  1.00 48.61  ? 198 PRO A CA    1 
ATOM   1503  C C     . PRO A 1 198 ? 0.993   1.560   67.242  1.00 45.74  ? 198 PRO A C     1 
ATOM   1504  O O     . PRO A 1 198 ? 1.896   1.304   68.025  1.00 54.48  ? 198 PRO A O     1 
ATOM   1505  C CB    . PRO A 1 198 ? -0.011  -0.698  66.719  1.00 50.77  ? 198 PRO A CB    1 
ATOM   1506  C CG    . PRO A 1 198 ? 0.474   -1.810  65.796  1.00 51.71  ? 198 PRO A CG    1 
ATOM   1507  C CD    . PRO A 1 198 ? 1.900   -1.425  65.461  1.00 46.93  ? 198 PRO A CD    1 
ATOM   1508  N N     . GLY A 1 199 ? 0.388   2.746   67.196  1.00 46.26  ? 199 GLY A N     1 
ATOM   1509  C CA    . GLY A 1 199 ? 0.456   3.680   68.306  1.00 47.58  ? 199 GLY A CA    1 
ATOM   1510  C C     . GLY A 1 199 ? 1.653   4.622   68.278  1.00 49.69  ? 199 GLY A C     1 
ATOM   1511  O O     . GLY A 1 199 ? 1.818   5.447   69.196  1.00 46.39  ? 199 GLY A O     1 
ATOM   1512  N N     . ASN A 1 200 ? 2.462   4.537   67.212  1.00 49.03  ? 200 ASN A N     1 
ATOM   1513  C CA    . ASN A 1 200 ? 3.642   5.391   67.088  1.00 43.79  ? 200 ASN A CA    1 
ATOM   1514  C C     . ASN A 1 200 ? 3.224   6.850   67.003  1.00 37.78  ? 200 ASN A C     1 
ATOM   1515  O O     . ASN A 1 200 ? 2.159   7.161   66.483  1.00 43.34  ? 200 ASN A O     1 
ATOM   1516  C CB    . ASN A 1 200 ? 4.451   5.128   65.814  1.00 48.34  ? 200 ASN A CB    1 
ATOM   1517  C CG    . ASN A 1 200 ? 3.692   5.573   64.573  1.00 42.30  ? 200 ASN A CG    1 
ATOM   1518  O OD1   . ASN A 1 200 ? 3.738   6.733   64.162  1.00 33.57  ? 200 ASN A OD1   1 
ATOM   1519  N ND2   . ASN A 1 200 ? 2.928   4.654   64.019  1.00 40.15  ? 200 ASN A ND2   1 
ATOM   1520  N N     . ASN A 1 201 ? 4.131   7.727   67.418  1.00 41.98  ? 201 ASN A N     1 
ATOM   1521  C CA    . ASN A 1 201 ? 4.010   9.160   67.226  1.00 39.67  ? 201 ASN A CA    1 
ATOM   1522  C C     . ASN A 1 201 ? 5.287   9.607   66.501  1.00 37.79  ? 201 ASN A C     1 
ATOM   1523  O O     . ASN A 1 201 ? 5.658   10.798  66.527  1.00 33.92  ? 201 ASN A O     1 
ATOM   1524  C CB    . ASN A 1 201 ? 3.710   9.860   68.560  1.00 51.44  ? 201 ASN A CB    1 
ATOM   1525  C CG    . ASN A 1 201 ? 2.310   9.562   69.091  1.00 58.48  ? 201 ASN A CG    1 
ATOM   1526  O OD1   . ASN A 1 201 ? 1.426   10.417  69.072  1.00 57.40  ? 201 ASN A OD1   1 
ATOM   1527  N ND2   . ASN A 1 201 ? 2.068   8.334   69.538  1.00 53.90  ? 201 ASN A ND2   1 
ATOM   1528  N N     . THR A 1 202 ? 5.886   8.643   65.758  1.00 40.33  ? 202 THR A N     1 
ATOM   1529  C CA    . THR A 1 202 ? 7.232   8.801   65.201  1.00 45.27  ? 202 THR A CA    1 
ATOM   1530  C C     . THR A 1 202 ? 7.332   8.579   63.686  1.00 43.72  ? 202 THR A C     1 
ATOM   1531  O O     . THR A 1 202 ? 8.437   8.643   63.162  1.00 50.58  ? 202 THR A O     1 
ATOM   1532  C CB    . THR A 1 202 ? 8.210   7.844   65.883  1.00 39.43  ? 202 THR A CB    1 
ATOM   1533  O OG1   . THR A 1 202 ? 7.601   6.559   65.877  1.00 37.08  ? 202 THR A OG1   1 
ATOM   1534  C CG2   . THR A 1 202 ? 8.534   8.265   67.295  1.00 38.59  ? 202 THR A CG2   1 
ATOM   1535  N N     . TRP A 1 203 ? 6.201   8.412   62.987  1.00 44.90  ? 203 TRP A N     1 
ATOM   1536  C CA    . TRP A 1 203 ? 6.169   8.206   61.539  1.00 50.12  ? 203 TRP A CA    1 
ATOM   1537  C C     . TRP A 1 203 ? 7.012   9.235   60.778  1.00 44.94  ? 203 TRP A C     1 
ATOM   1538  O O     . TRP A 1 203 ? 7.741   8.864   59.871  1.00 41.75  ? 203 TRP A O     1 
ATOM   1539  C CB    . TRP A 1 203 ? 4.728   8.242   61.011  1.00 53.37  ? 203 TRP A CB    1 
ATOM   1540  C CG    . TRP A 1 203 ? 4.483   7.473   59.743  1.00 61.91  ? 203 TRP A CG    1 
ATOM   1541  C CD1   . TRP A 1 203 ? 5.323   6.607   59.092  1.00 58.34  ? 203 TRP A CD1   1 
ATOM   1542  C CD2   . TRP A 1 203 ? 3.260   7.477   58.986  1.00 56.71  ? 203 TRP A CD2   1 
ATOM   1543  N NE1   . TRP A 1 203 ? 4.702   6.069   57.996  1.00 50.09  ? 203 TRP A NE1   1 
ATOM   1544  C CE2   . TRP A 1 203 ? 3.439   6.589   57.904  1.00 56.21  ? 203 TRP A CE2   1 
ATOM   1545  C CE3   . TRP A 1 203 ? 2.034   8.132   59.140  1.00 50.53  ? 203 TRP A CE3   1 
ATOM   1546  C CZ2   . TRP A 1 203 ? 2.433   6.361   56.970  1.00 63.88  ? 203 TRP A CZ2   1 
ATOM   1547  C CZ3   . TRP A 1 203 ? 1.041   7.902   58.227  1.00 57.94  ? 203 TRP A CZ3   1 
ATOM   1548  C CH2   . TRP A 1 203 ? 1.244   7.032   57.153  1.00 70.22  ? 203 TRP A CH2   1 
ATOM   1549  N N     . GLN A 1 204 ? 6.855   10.519  61.108  1.00 39.06  ? 204 GLN A N     1 
ATOM   1550  C CA    . GLN A 1 204 ? 7.558   11.586  60.438  1.00 38.57  ? 204 GLN A CA    1 
ATOM   1551  C C     . GLN A 1 204 ? 8.772   12.019  61.269  1.00 43.35  ? 204 GLN A C     1 
ATOM   1552  O O     . GLN A 1 204 ? 9.193   13.176  61.181  1.00 41.04  ? 204 GLN A O     1 
ATOM   1553  C CB    . GLN A 1 204 ? 6.611   12.771  60.197  1.00 37.34  ? 204 GLN A CB    1 
ATOM   1554  C CG    . GLN A 1 204 ? 5.655   12.593  59.006  1.00 38.33  ? 204 GLN A CG    1 
ATOM   1555  C CD    . GLN A 1 204 ? 4.729   11.404  59.101  1.00 38.63  ? 204 GLN A CD    1 
ATOM   1556  O OE1   . GLN A 1 204 ? 3.768   11.391  59.865  1.00 41.60  ? 204 GLN A OE1   1 
ATOM   1557  N NE2   . GLN A 1 204 ? 4.987   10.381  58.303  1.00 41.83  ? 204 GLN A NE2   1 
ATOM   1558  N N     . LEU A 1 205 ? 9.330   11.125  62.095  1.00 40.17  ? 205 LEU A N     1 
ATOM   1559  C CA    . LEU A 1 205 ? 10.428  11.544  62.966  1.00 45.68  ? 205 LEU A CA    1 
ATOM   1560  C C     . LEU A 1 205 ? 11.696  10.736  62.693  1.00 43.52  ? 205 LEU A C     1 
ATOM   1561  O O     . LEU A 1 205 ? 12.800  11.187  62.971  1.00 39.92  ? 205 LEU A O     1 
ATOM   1562  C CB    . LEU A 1 205 ? 10.007  11.421  64.434  1.00 45.78  ? 205 LEU A CB    1 
ATOM   1563  C CG    . LEU A 1 205 ? 8.971   12.430  64.929  1.00 45.98  ? 205 LEU A CG    1 
ATOM   1564  C CD1   . LEU A 1 205 ? 8.937   12.495  66.449  1.00 45.63  ? 205 LEU A CD1   1 
ATOM   1565  C CD2   . LEU A 1 205 ? 9.245   13.812  64.380  1.00 45.11  ? 205 LEU A CD2   1 
ATOM   1566  N N     . PHE A 1 206 ? 11.524  9.557   62.101  1.00 43.25  ? 206 PHE A N     1 
ATOM   1567  C CA    . PHE A 1 206 ? 12.633  8.661   61.877  1.00 42.20  ? 206 PHE A CA    1 
ATOM   1568  C C     . PHE A 1 206 ? 12.327  7.788   60.663  1.00 42.69  ? 206 PHE A C     1 
ATOM   1569  O O     . PHE A 1 206 ? 11.430  6.953   60.720  1.00 46.29  ? 206 PHE A O     1 
ATOM   1570  C CB    . PHE A 1 206 ? 12.855  7.863   63.164  1.00 39.53  ? 206 PHE A CB    1 
ATOM   1571  C CG    . PHE A 1 206 ? 13.869  6.765   63.034  1.00 36.97  ? 206 PHE A CG    1 
ATOM   1572  C CD1   . PHE A 1 206 ? 15.226  7.069   63.003  1.00 42.24  ? 206 PHE A CD1   1 
ATOM   1573  C CD2   . PHE A 1 206 ? 13.473  5.448   62.920  1.00 35.22  ? 206 PHE A CD2   1 
ATOM   1574  C CE1   . PHE A 1 206 ? 16.169  6.059   62.912  1.00 41.94  ? 206 PHE A CE1   1 
ATOM   1575  C CE2   . PHE A 1 206 ? 14.407  4.438   62.784  1.00 33.87  ? 206 PHE A CE2   1 
ATOM   1576  C CZ    . PHE A 1 206 ? 15.753  4.747   62.779  1.00 39.77  ? 206 PHE A CZ    1 
ATOM   1577  N N     . LYS A 1 207 ? 13.113  7.971   59.587  1.00 49.32  ? 207 LYS A N     1 
ATOM   1578  C CA    . LYS A 1 207 ? 12.850  7.396   58.272  1.00 42.16  ? 207 LYS A CA    1 
ATOM   1579  C C     . LYS A 1 207 ? 12.879  5.870   58.282  1.00 42.01  ? 207 LYS A C     1 
ATOM   1580  O O     . LYS A 1 207 ? 12.001  5.239   57.717  1.00 48.91  ? 207 LYS A O     1 
ATOM   1581  C CB    . LYS A 1 207 ? 13.918  7.825   57.272  1.00 42.43  ? 207 LYS A CB    1 
ATOM   1582  C CG    . LYS A 1 207 ? 13.906  9.269   56.798  1.00 44.24  ? 207 LYS A CG    1 
ATOM   1583  C CD    . LYS A 1 207 ? 15.208  9.588   56.017  1.00 50.33  ? 207 LYS A CD    1 
ATOM   1584  C CE    . LYS A 1 207 ? 15.243  10.896  55.242  1.00 48.91  ? 207 LYS A CE    1 
ATOM   1585  N NZ    . LYS A 1 207 ? 14.641  10.721  53.898  1.00 50.79  ? 207 LYS A NZ    1 
ATOM   1586  N N     . TYR A 1 208 ? 13.895  5.270   58.904  1.00 48.52  ? 208 TYR A N     1 
ATOM   1587  C CA    . TYR A 1 208 ? 14.205  3.859   58.675  1.00 50.04  ? 208 TYR A CA    1 
ATOM   1588  C C     . TYR A 1 208 ? 13.088  2.948   59.167  1.00 50.84  ? 208 TYR A C     1 
ATOM   1589  O O     . TYR A 1 208 ? 12.591  2.121   58.422  1.00 53.96  ? 208 TYR A O     1 
ATOM   1590  C CB    . TYR A 1 208 ? 15.532  3.461   59.334  1.00 45.32  ? 208 TYR A CB    1 
ATOM   1591  C CG    . TYR A 1 208 ? 16.738  4.170   58.777  1.00 53.07  ? 208 TYR A CG    1 
ATOM   1592  C CD1   . TYR A 1 208 ? 16.750  4.705   57.493  1.00 53.45  ? 208 TYR A CD1   1 
ATOM   1593  C CD2   . TYR A 1 208 ? 17.860  4.363   59.556  1.00 60.96  ? 208 TYR A CD2   1 
ATOM   1594  C CE1   . TYR A 1 208 ? 17.842  5.405   57.007  1.00 49.50  ? 208 TYR A CE1   1 
ATOM   1595  C CE2   . TYR A 1 208 ? 18.968  5.041   59.075  1.00 61.47  ? 208 TYR A CE2   1 
ATOM   1596  C CZ    . TYR A 1 208 ? 18.968  5.551   57.793  1.00 49.89  ? 208 TYR A CZ    1 
ATOM   1597  O OH    . TYR A 1 208 ? 20.084  6.204   57.343  1.00 49.79  ? 208 TYR A OH    1 
ATOM   1598  N N     . GLY A 1 209 ? 12.674  3.108   60.422  1.00 48.79  ? 209 GLY A N     1 
ATOM   1599  C CA    . GLY A 1 209 ? 11.989  2.027   61.084  1.00 39.88  ? 209 GLY A CA    1 
ATOM   1600  C C     . GLY A 1 209 ? 12.999  0.939   61.404  1.00 38.12  ? 209 GLY A C     1 
ATOM   1601  O O     . GLY A 1 209 ? 14.106  1.232   61.846  1.00 49.77  ? 209 GLY A O     1 
ATOM   1602  N N     . TYR A 1 210 ? 12.588  -0.295  61.146  1.00 36.89  ? 210 TYR A N     1 
ATOM   1603  C CA    . TYR A 1 210 ? 13.381  -1.491  61.356  1.00 39.49  ? 210 TYR A CA    1 
ATOM   1604  C C     . TYR A 1 210 ? 13.424  -2.269  60.042  1.00 39.08  ? 210 TYR A C     1 
ATOM   1605  O O     . TYR A 1 210 ? 12.400  -2.473  59.383  1.00 38.62  ? 210 TYR A O     1 
ATOM   1606  C CB    . TYR A 1 210 ? 12.787  -2.392  62.456  1.00 35.58  ? 210 TYR A CB    1 
ATOM   1607  C CG    . TYR A 1 210 ? 13.471  -3.727  62.671  1.00 37.67  ? 210 TYR A CG    1 
ATOM   1608  C CD1   . TYR A 1 210 ? 14.828  -3.801  62.972  1.00 39.36  ? 210 TYR A CD1   1 
ATOM   1609  C CD2   . TYR A 1 210 ? 12.777  -4.926  62.576  1.00 40.35  ? 210 TYR A CD2   1 
ATOM   1610  C CE1   . TYR A 1 210 ? 15.472  -5.014  63.175  1.00 36.76  ? 210 TYR A CE1   1 
ATOM   1611  C CE2   . TYR A 1 210 ? 13.399  -6.148  62.785  1.00 39.44  ? 210 TYR A CE2   1 
ATOM   1612  C CZ    . TYR A 1 210 ? 14.754  -6.191  63.082  1.00 43.71  ? 210 TYR A CZ    1 
ATOM   1613  O OH    . TYR A 1 210 ? 15.420  -7.382  63.282  1.00 49.39  ? 210 TYR A OH    1 
ATOM   1614  N N     . GLY A 1 211 ? 14.625  -2.728  59.687  1.00 44.45  ? 211 GLY A N     1 
ATOM   1615  C CA    . GLY A 1 211 ? 14.763  -3.682  58.598  1.00 48.26  ? 211 GLY A CA    1 
ATOM   1616  C C     . GLY A 1 211 ? 14.883  -2.977  57.260  1.00 39.74  ? 211 GLY A C     1 
ATOM   1617  O O     . GLY A 1 211 ? 15.169  -1.793  57.215  1.00 48.50  ? 211 GLY A O     1 
ATOM   1618  N N     . PRO A 1 212 ? 14.659  -3.684  56.141  1.00 44.96  ? 212 PRO A N     1 
ATOM   1619  C CA    . PRO A 1 212 ? 14.824  -3.103  54.810  1.00 40.18  ? 212 PRO A CA    1 
ATOM   1620  C C     . PRO A 1 212 ? 14.158  -1.751  54.642  1.00 38.74  ? 212 PRO A C     1 
ATOM   1621  O O     . PRO A 1 212 ? 12.933  -1.655  54.813  1.00 45.67  ? 212 PRO A O     1 
ATOM   1622  C CB    . PRO A 1 212 ? 14.097  -4.107  53.913  1.00 48.70  ? 212 PRO A CB    1 
ATOM   1623  C CG    . PRO A 1 212 ? 14.230  -5.430  54.625  1.00 52.06  ? 212 PRO A CG    1 
ATOM   1624  C CD    . PRO A 1 212 ? 14.238  -5.092  56.099  1.00 49.54  ? 212 PRO A CD    1 
ATOM   1625  N N     . TYR A 1 213 ? 14.965  -0.741  54.270  1.00 36.01  ? 213 TYR A N     1 
ATOM   1626  C CA    . TYR A 1 213 ? 14.465  0.606   53.991  1.00 35.35  ? 213 TYR A CA    1 
ATOM   1627  C C     . TYR A 1 213 ? 13.934  0.700   52.554  1.00 40.11  ? 213 TYR A C     1 
ATOM   1628  O O     . TYR A 1 213 ? 14.715  0.590   51.609  1.00 30.68  ? 213 TYR A O     1 
ATOM   1629  C CB    . TYR A 1 213 ? 15.595  1.598   54.197  1.00 33.82  ? 213 TYR A CB    1 
ATOM   1630  C CG    . TYR A 1 213 ? 15.237  3.049   54.011  1.00 39.93  ? 213 TYR A CG    1 
ATOM   1631  C CD1   . TYR A 1 213 ? 14.036  3.577   54.452  1.00 40.58  ? 213 TYR A CD1   1 
ATOM   1632  C CD2   . TYR A 1 213 ? 16.164  3.931   53.476  1.00 50.66  ? 213 TYR A CD2   1 
ATOM   1633  C CE1   . TYR A 1 213 ? 13.732  4.917   54.284  1.00 38.94  ? 213 TYR A CE1   1 
ATOM   1634  C CE2   . TYR A 1 213 ? 15.883  5.276   53.316  1.00 45.73  ? 213 TYR A CE2   1 
ATOM   1635  C CZ    . TYR A 1 213 ? 14.661  5.766   53.718  1.00 40.35  ? 213 TYR A CZ    1 
ATOM   1636  O OH    . TYR A 1 213 ? 14.419  7.099   53.569  1.00 54.24  ? 213 TYR A OH    1 
ATOM   1637  N N     . VAL A 1 214 ? 12.600  0.883   52.403  1.00 39.60  ? 214 VAL A N     1 
ATOM   1638  C CA    . VAL A 1 214 ? 11.924  0.649   51.141  1.00 33.24  ? 214 VAL A CA    1 
ATOM   1639  C C     . VAL A 1 214 ? 11.161  1.867   50.625  1.00 39.81  ? 214 VAL A C     1 
ATOM   1640  O O     . VAL A 1 214 ? 10.613  1.809   49.521  1.00 49.70  ? 214 VAL A O     1 
ATOM   1641  C CB    . VAL A 1 214 ? 10.988  -0.559  51.224  1.00 38.41  ? 214 VAL A CB    1 
ATOM   1642  C CG1   . VAL A 1 214 ? 11.772  -1.842  51.441  1.00 35.99  ? 214 VAL A CG1   1 
ATOM   1643  C CG2   . VAL A 1 214 ? 9.909   -0.373  52.283  1.00 43.91  ? 214 VAL A CG2   1 
ATOM   1644  N N     . ASP A 1 215 ? 11.175  3.002   51.331  1.00 36.71  ? 215 ASP A N     1 
ATOM   1645  C CA    . ASP A 1 215 ? 10.450  4.153   50.829  1.00 38.69  ? 215 ASP A CA    1 
ATOM   1646  C C     . ASP A 1 215 ? 10.850  4.458   49.385  1.00 44.04  ? 215 ASP A C     1 
ATOM   1647  O O     . ASP A 1 215 ? 10.009  4.823   48.546  1.00 42.38  ? 215 ASP A O     1 
ATOM   1648  C CB    . ASP A 1 215 ? 10.660  5.353   51.742  1.00 41.89  ? 215 ASP A CB    1 
ATOM   1649  C CG    . ASP A 1 215 ? 9.933   5.219   53.072  1.00 42.05  ? 215 ASP A CG    1 
ATOM   1650  O OD1   . ASP A 1 215 ? 10.247  4.277   53.830  1.00 42.51  ? 215 ASP A OD1   1 
ATOM   1651  O OD2   . ASP A 1 215 ? 9.074   6.076   53.335  1.00 40.72  ? 215 ASP A OD2   1 
ATOM   1652  N N     . GLY A 1 216 ? 12.159  4.345   49.125  1.00 41.51  ? 216 GLY A N     1 
ATOM   1653  C CA    . GLY A 1 216 ? 12.737  4.764   47.858  1.00 45.02  ? 216 GLY A CA    1 
ATOM   1654  C C     . GLY A 1 216 ? 12.233  4.004   46.625  1.00 37.06  ? 216 GLY A C     1 
ATOM   1655  O O     . GLY A 1 216 ? 12.171  4.587   45.548  1.00 40.57  ? 216 GLY A O     1 
ATOM   1656  N N     . ILE A 1 217 ? 11.904  2.718   46.774  1.00 35.06  ? 217 ILE A N     1 
ATOM   1657  C CA    . ILE A 1 217 ? 11.372  1.908   45.685  1.00 40.37  ? 217 ILE A CA    1 
ATOM   1658  C C     . ILE A 1 217 ? 10.010  2.417   45.177  1.00 44.81  ? 217 ILE A C     1 
ATOM   1659  O O     . ILE A 1 217 ? 9.584   2.026   44.092  1.00 52.57  ? 217 ILE A O     1 
ATOM   1660  C CB    . ILE A 1 217 ? 11.268  0.409   46.068  1.00 38.83  ? 217 ILE A CB    1 
ATOM   1661  C CG1   . ILE A 1 217 ? 9.933   0.073   46.740  1.00 36.07  ? 217 ILE A CG1   1 
ATOM   1662  C CG2   . ILE A 1 217 ? 12.480  -0.094  46.868  1.00 33.54  ? 217 ILE A CG2   1 
ATOM   1663  C CD1   . ILE A 1 217 ? 9.745   -1.429  46.972  1.00 39.98  ? 217 ILE A CD1   1 
ATOM   1664  N N     . PHE A 1 218 ? 9.285   3.233   45.941  1.00 43.89  ? 218 PHE A N     1 
ATOM   1665  C CA    . PHE A 1 218 ? 8.036   3.797   45.438  1.00 46.97  ? 218 PHE A CA    1 
ATOM   1666  C C     . PHE A 1 218 ? 8.241   5.181   44.826  1.00 44.35  ? 218 PHE A C     1 
ATOM   1667  O O     . PHE A 1 218 ? 7.257   5.872   44.578  1.00 46.09  ? 218 PHE A O     1 
ATOM   1668  C CB    . PHE A 1 218 ? 6.978   3.856   46.550  1.00 42.37  ? 218 PHE A CB    1 
ATOM   1669  C CG    . PHE A 1 218 ? 6.728   2.493   47.131  1.00 39.18  ? 218 PHE A CG    1 
ATOM   1670  C CD1   . PHE A 1 218 ? 6.055   1.535   46.407  1.00 36.98  ? 218 PHE A CD1   1 
ATOM   1671  C CD2   . PHE A 1 218 ? 7.277   2.130   48.352  1.00 40.72  ? 218 PHE A CD2   1 
ATOM   1672  C CE1   . PHE A 1 218 ? 5.905   0.252   46.913  1.00 40.08  ? 218 PHE A CE1   1 
ATOM   1673  C CE2   . PHE A 1 218 ? 7.122   0.848   48.855  1.00 38.97  ? 218 PHE A CE2   1 
ATOM   1674  C CZ    . PHE A 1 218 ? 6.432   -0.090  48.137  1.00 38.13  ? 218 PHE A CZ    1 
ATOM   1675  N N     . SER A 1 219 ? 9.498   5.607   44.625  1.00 45.11  ? 219 SER A N     1 
ATOM   1676  C CA    . SER A 1 219 ? 9.792   6.869   43.939  1.00 44.59  ? 219 SER A CA    1 
ATOM   1677  C C     . SER A 1 219 ? 10.291  6.549   42.525  1.00 36.71  ? 219 SER A C     1 
ATOM   1678  O O     . SER A 1 219 ? 10.866  5.503   42.313  1.00 34.10  ? 219 SER A O     1 
ATOM   1679  C CB    . SER A 1 219 ? 10.761  7.748   44.734  1.00 42.80  ? 219 SER A CB    1 
ATOM   1680  O OG    . SER A 1 219 ? 12.072  7.195   44.766  1.00 42.13  ? 219 SER A OG    1 
ATOM   1681  N N     . GLN A 1 220 ? 10.000  7.413   41.541  1.00 42.25  ? 220 GLN A N     1 
ATOM   1682  C CA    . GLN A 1 220 ? 10.170  7.122   40.112  1.00 34.80  ? 220 GLN A CA    1 
ATOM   1683  C C     . GLN A 1 220 ? 9.905   5.646   39.838  1.00 38.51  ? 220 GLN A C     1 
ATOM   1684  O O     . GLN A 1 220 ? 10.771  4.935   39.335  1.00 39.48  ? 220 GLN A O     1 
ATOM   1685  C CB    . GLN A 1 220 ? 11.551  7.572   39.639  1.00 34.31  ? 220 GLN A CB    1 
ATOM   1686  C CG    . GLN A 1 220 ? 11.748  9.097   39.603  1.00 31.94  ? 220 GLN A CG    1 
ATOM   1687  C CD    . GLN A 1 220 ? 12.982  9.513   38.845  1.00 30.95  ? 220 GLN A CD    1 
ATOM   1688  O OE1   . GLN A 1 220 ? 13.782  8.683   38.438  1.00 32.24  ? 220 GLN A OE1   1 
ATOM   1689  N NE2   . GLN A 1 220 ? 13.196  10.814  38.701  1.00 32.40  ? 220 GLN A NE2   1 
ATOM   1690  N N     . SER A 1 221 ? 8.698   5.194   40.217  1.00 40.59  ? 221 SER A N     1 
ATOM   1691  C CA    . SER A 1 221 ? 8.387   3.779   40.249  1.00 39.75  ? 221 SER A CA    1 
ATOM   1692  C C     . SER A 1 221 ? 6.931   3.513   39.858  1.00 42.26  ? 221 SER A C     1 
ATOM   1693  O O     . SER A 1 221 ? 6.091   4.394   39.933  1.00 32.30  ? 221 SER A O     1 
ATOM   1694  C CB    . SER A 1 221 ? 8.647   3.288   41.631  1.00 44.00  ? 221 SER A CB    1 
ATOM   1695  O OG    . SER A 1 221 ? 8.550   1.878   41.694  1.00 51.56  ? 221 SER A OG    1 
ATOM   1696  N N     . ASN A 1 222 ? 6.635   2.255   39.516  1.00 42.42  ? 222 ASN A N     1 
ATOM   1697  C CA    . ASN A 1 222 ? 5.280   1.775   39.346  1.00 44.20  ? 222 ASN A CA    1 
ATOM   1698  C C     . ASN A 1 222 ? 5.035   0.580   40.265  1.00 49.73  ? 222 ASN A C     1 
ATOM   1699  O O     . ASN A 1 222 ? 4.410   -0.407  39.869  1.00 58.42  ? 222 ASN A O     1 
ATOM   1700  C CB    . ASN A 1 222 ? 5.071   1.343   37.891  1.00 50.64  ? 222 ASN A CB    1 
ATOM   1701  C CG    . ASN A 1 222 ? 6.146   0.388   37.399  1.00 56.86  ? 222 ASN A CG    1 
ATOM   1702  O OD1   . ASN A 1 222 ? 7.091   0.070   38.124  1.00 52.96  ? 222 ASN A OD1   1 
ATOM   1703  N ND2   . ASN A 1 222 ? 6.028   -0.061  36.159  1.00 59.18  ? 222 ASN A ND2   1 
ATOM   1704  N N     . PHE A 1 223 ? 5.574   0.630   41.483  1.00 50.89  ? 223 PHE A N     1 
ATOM   1705  C CA    . PHE A 1 223 ? 5.527   -0.519  42.375  1.00 46.68  ? 223 PHE A CA    1 
ATOM   1706  C C     . PHE A 1 223 ? 4.354   -0.380  43.338  1.00 41.16  ? 223 PHE A C     1 
ATOM   1707  O O     . PHE A 1 223 ? 4.001   -1.348  44.009  1.00 39.76  ? 223 PHE A O     1 
ATOM   1708  C CB    . PHE A 1 223 ? 6.827   -0.674  43.167  1.00 46.16  ? 223 PHE A CB    1 
ATOM   1709  C CG    . PHE A 1 223 ? 8.039   -1.133  42.404  1.00 44.47  ? 223 PHE A CG    1 
ATOM   1710  C CD1   . PHE A 1 223 ? 7.958   -1.544  41.086  1.00 51.04  ? 223 PHE A CD1   1 
ATOM   1711  C CD2   . PHE A 1 223 ? 9.285   -1.131  43.013  1.00 49.17  ? 223 PHE A CD2   1 
ATOM   1712  C CE1   . PHE A 1 223 ? 9.086   -1.951  40.389  1.00 50.48  ? 223 PHE A CE1   1 
ATOM   1713  C CE2   . PHE A 1 223 ? 10.415  -1.534  42.315  1.00 55.76  ? 223 PHE A CE2   1 
ATOM   1714  C CZ    . PHE A 1 223 ? 10.318  -1.934  40.999  1.00 56.09  ? 223 PHE A CZ    1 
ATOM   1715  N N     . GLY A 1 224 ? 3.742   0.808   43.393  1.00 37.67  ? 224 GLY A N     1 
ATOM   1716  C CA    . GLY A 1 224 ? 2.602   1.022   44.261  1.00 33.81  ? 224 GLY A CA    1 
ATOM   1717  C C     . GLY A 1 224 ? 2.035   2.414   44.077  1.00 39.24  ? 224 GLY A C     1 
ATOM   1718  O O     . GLY A 1 224 ? 2.553   3.186   43.274  1.00 40.07  ? 224 GLY A O     1 
ATOM   1719  N N     . VAL A 1 225 ? 0.969   2.703   44.837  1.00 44.53  ? 225 VAL A N     1 
ATOM   1720  C CA    . VAL A 1 225 ? 0.269   3.972   44.760  1.00 44.68  ? 225 VAL A CA    1 
ATOM   1721  C C     . VAL A 1 225 ? 0.408   4.626   46.121  1.00 49.99  ? 225 VAL A C     1 
ATOM   1722  O O     . VAL A 1 225 ? 0.120   4.002   47.133  1.00 52.80  ? 225 VAL A O     1 
ATOM   1723  C CB    . VAL A 1 225 ? -1.237  3.830   44.438  1.00 44.96  ? 225 VAL A CB    1 
ATOM   1724  C CG1   . VAL A 1 225 ? -1.845  5.179   44.088  1.00 40.06  ? 225 VAL A CG1   1 
ATOM   1725  C CG2   . VAL A 1 225 ? -1.525  2.806   43.353  1.00 45.29  ? 225 VAL A CG2   1 
ATOM   1726  N N     . VAL A 1 226 ? 0.775   5.903   46.130  1.00 49.46  ? 226 VAL A N     1 
ATOM   1727  C CA    . VAL A 1 226 ? 1.110   6.518   47.385  1.00 49.39  ? 226 VAL A CA    1 
ATOM   1728  C C     . VAL A 1 226 ? -0.047  7.397   47.825  1.00 52.72  ? 226 VAL A C     1 
ATOM   1729  O O     . VAL A 1 226 ? -0.403  8.375   47.162  1.00 42.27  ? 226 VAL A O     1 
ATOM   1730  C CB    . VAL A 1 226 ? 2.432   7.289   47.287  1.00 49.68  ? 226 VAL A CB    1 
ATOM   1731  C CG1   . VAL A 1 226 ? 2.804   7.906   48.628  1.00 47.47  ? 226 VAL A CG1   1 
ATOM   1732  C CG2   . VAL A 1 226 ? 3.541   6.405   46.750  1.00 48.18  ? 226 VAL A CG2   1 
ATOM   1733  N N     . THR A 1 227 ? -0.566  7.066   49.010  1.00 57.10  ? 227 THR A N     1 
ATOM   1734  C CA    . THR A 1 227 ? -1.814  7.648   49.456  1.00 52.96  ? 227 THR A CA    1 
ATOM   1735  C C     . THR A 1 227 ? -1.577  8.602   50.611  1.00 48.90  ? 227 THR A C     1 
ATOM   1736  O O     . THR A 1 227 ? -2.380  9.507   50.793  1.00 46.10  ? 227 THR A O     1 
ATOM   1737  C CB    . THR A 1 227 ? -2.826  6.538   49.702  1.00 52.02  ? 227 THR A CB    1 
ATOM   1738  O OG1   . THR A 1 227 ? -2.276  5.653   50.672  1.00 57.26  ? 227 THR A OG1   1 
ATOM   1739  C CG2   . THR A 1 227 ? -3.131  5.781   48.427  1.00 52.00  ? 227 THR A CG2   1 
ATOM   1740  N N     . LYS A 1 228 ? -0.450  8.473   51.328  1.00 54.88  ? 228 LYS A N     1 
ATOM   1741  C CA    . LYS A 1 228 ? -0.025  9.530   52.243  1.00 45.13  ? 228 LYS A CA    1 
ATOM   1742  C C     . LYS A 1 228 ? 1.497   9.586   52.304  1.00 40.23  ? 228 LYS A C     1 
ATOM   1743  O O     . LYS A 1 228 ? 2.174   8.558   52.212  1.00 38.07  ? 228 LYS A O     1 
ATOM   1744  C CB    . LYS A 1 228 ? -0.488  9.291   53.681  1.00 51.64  ? 228 LYS A CB    1 
ATOM   1745  C CG    . LYS A 1 228 ? -1.761  8.494   53.890  1.00 58.40  ? 228 LYS A CG    1 
ATOM   1746  C CD    . LYS A 1 228 ? -2.458  8.817   55.201  1.00 63.42  ? 228 LYS A CD    1 
ATOM   1747  C CE    . LYS A 1 228 ? -3.897  8.349   55.178  1.00 58.33  ? 228 LYS A CE    1 
ATOM   1748  N NZ    . LYS A 1 228 ? -3.914  6.908   54.869  1.00 56.91  ? 228 LYS A NZ    1 
ATOM   1749  N N     . MET A 1 229 ? 2.017   10.784  52.546  1.00 35.61  ? 229 MET A N     1 
ATOM   1750  C CA    . MET A 1 229 ? 3.449   10.951  52.656  1.00 41.74  ? 229 MET A CA    1 
ATOM   1751  C C     . MET A 1 229 ? 3.776   12.079  53.625  1.00 41.45  ? 229 MET A C     1 
ATOM   1752  O O     . MET A 1 229 ? 3.216   13.165  53.550  1.00 37.43  ? 229 MET A O     1 
ATOM   1753  C CB    . MET A 1 229 ? 4.079   11.282  51.298  1.00 44.67  ? 229 MET A CB    1 
ATOM   1754  C CG    . MET A 1 229 ? 5.585   11.389  51.376  1.00 44.36  ? 229 MET A CG    1 
ATOM   1755  S SD    . MET A 1 229 ? 6.335   11.691  49.771  1.00 42.63  ? 229 MET A SD    1 
ATOM   1756  C CE    . MET A 1 229 ? 6.461   13.487  49.835  1.00 30.19  ? 229 MET A CE    1 
ATOM   1757  N N     . GLY A 1 230 ? 4.736   11.805  54.508  1.00 46.29  ? 230 GLY A N     1 
ATOM   1758  C CA    . GLY A 1 230 ? 5.253   12.819  55.395  1.00 42.49  ? 230 GLY A CA    1 
ATOM   1759  C C     . GLY A 1 230 ? 6.498   13.435  54.794  1.00 44.18  ? 230 GLY A C     1 
ATOM   1760  O O     . GLY A 1 230 ? 7.205   12.776  54.037  1.00 46.17  ? 230 GLY A O     1 
ATOM   1761  N N     . ILE A 1 231 ? 6.707   14.713  55.106  1.00 39.70  ? 231 ILE A N     1 
ATOM   1762  C CA    . ILE A 1 231 ? 7.902   15.400  54.685  1.00 45.13  ? 231 ILE A CA    1 
ATOM   1763  C C     . ILE A 1 231 ? 8.335   16.291  55.845  1.00 44.97  ? 231 ILE A C     1 
ATOM   1764  O O     . ILE A 1 231 ? 7.471   16.819  56.561  1.00 36.68  ? 231 ILE A O     1 
ATOM   1765  C CB    . ILE A 1 231 ? 7.656   16.186  53.385  1.00 48.45  ? 231 ILE A CB    1 
ATOM   1766  C CG1   . ILE A 1 231 ? 8.957   16.643  52.727  1.00 48.06  ? 231 ILE A CG1   1 
ATOM   1767  C CG2   . ILE A 1 231 ? 6.743   17.374  53.642  1.00 57.47  ? 231 ILE A CG2   1 
ATOM   1768  C CD1   . ILE A 1 231 ? 8.752   17.407  51.427  1.00 50.80  ? 231 ILE A CD1   1 
ATOM   1769  N N     . TRP A 1 232 ? 9.671   16.412  56.023  1.00 37.54  ? 232 TRP A N     1 
ATOM   1770  C CA    . TRP A 1 232 ? 10.235  17.366  56.960  1.00 36.77  ? 232 TRP A CA    1 
ATOM   1771  C C     . TRP A 1 232 ? 10.125  18.751  56.338  1.00 34.70  ? 232 TRP A C     1 
ATOM   1772  O O     . TRP A 1 232 ? 10.077  18.868  55.121  1.00 44.54  ? 232 TRP A O     1 
ATOM   1773  C CB    . TRP A 1 232 ? 11.689  17.019  57.311  1.00 38.00  ? 232 TRP A CB    1 
ATOM   1774  C CG    . TRP A 1 232 ? 11.855  15.665  57.922  1.00 42.58  ? 232 TRP A CG    1 
ATOM   1775  C CD1   . TRP A 1 232 ? 10.909  14.930  58.576  1.00 46.50  ? 232 TRP A CD1   1 
ATOM   1776  C CD2   . TRP A 1 232 ? 13.030  14.834  57.867  1.00 51.73  ? 232 TRP A CD2   1 
ATOM   1777  N NE1   . TRP A 1 232 ? 11.414  13.712  58.947  1.00 48.97  ? 232 TRP A NE1   1 
ATOM   1778  C CE2   . TRP A 1 232 ? 12.715  13.625  58.525  1.00 46.71  ? 232 TRP A CE2   1 
ATOM   1779  C CE3   . TRP A 1 232 ? 14.318  15.001  57.342  1.00 50.60  ? 232 TRP A CE3   1 
ATOM   1780  C CZ2   . TRP A 1 232 ? 13.640  12.596  58.670  1.00 48.14  ? 232 TRP A CZ2   1 
ATOM   1781  C CZ3   . TRP A 1 232 ? 15.218  13.971  57.464  1.00 50.45  ? 232 TRP A CZ3   1 
ATOM   1782  C CH2   . TRP A 1 232 ? 14.884  12.783  58.114  1.00 48.55  ? 232 TRP A CH2   1 
ATOM   1783  N N     . LEU A 1 233 ? 10.130  19.774  57.188  1.00 36.49  ? 233 LEU A N     1 
ATOM   1784  C CA    . LEU A 1 233 ? 9.895   21.169  56.830  1.00 38.70  ? 233 LEU A CA    1 
ATOM   1785  C C     . LEU A 1 233 ? 10.842  21.967  57.704  1.00 41.98  ? 233 LEU A C     1 
ATOM   1786  O O     . LEU A 1 233 ? 10.984  21.653  58.883  1.00 48.47  ? 233 LEU A O     1 
ATOM   1787  C CB    . LEU A 1 233 ? 8.455   21.617  57.153  1.00 44.24  ? 233 LEU A CB    1 
ATOM   1788  C CG    . LEU A 1 233 ? 7.310   20.753  56.612  1.00 46.68  ? 233 LEU A CG    1 
ATOM   1789  C CD1   . LEU A 1 233 ? 5.978   21.156  57.200  1.00 52.48  ? 233 LEU A CD1   1 
ATOM   1790  C CD2   . LEU A 1 233 ? 7.220   20.870  55.105  1.00 48.08  ? 233 LEU A CD2   1 
ATOM   1791  N N     . MET A 1 234 ? 11.438  22.998  57.120  1.00 46.64  ? 234 MET A N     1 
ATOM   1792  C CA    . MET A 1 234 ? 12.524  23.728  57.728  1.00 48.72  ? 234 MET A CA    1 
ATOM   1793  C C     . MET A 1 234 ? 11.942  24.720  58.715  1.00 55.63  ? 234 MET A C     1 
ATOM   1794  O O     . MET A 1 234 ? 11.026  25.461  58.373  1.00 66.71  ? 234 MET A O     1 
ATOM   1795  C CB    . MET A 1 234 ? 13.283  24.521  56.671  1.00 50.69  ? 234 MET A CB    1 
ATOM   1796  C CG    . MET A 1 234 ? 14.518  25.218  57.189  1.00 51.79  ? 234 MET A CG    1 
ATOM   1797  S SD    . MET A 1 234 ? 15.403  25.866  55.788  1.00 53.05  ? 234 MET A SD    1 
ATOM   1798  C CE    . MET A 1 234 ? 15.705  27.559  56.273  1.00 61.10  ? 234 MET A CE    1 
ATOM   1799  N N     . PRO A 1 235 ? 12.459  24.789  59.956  1.00 53.00  ? 235 PRO A N     1 
ATOM   1800  C CA    . PRO A 1 235 ? 12.067  25.854  60.871  1.00 51.79  ? 235 PRO A CA    1 
ATOM   1801  C C     . PRO A 1 235 ? 12.393  27.202  60.260  1.00 49.13  ? 235 PRO A C     1 
ATOM   1802  O O     . PRO A 1 235 ? 13.493  27.390  59.737  1.00 46.77  ? 235 PRO A O     1 
ATOM   1803  C CB    . PRO A 1 235 ? 12.927  25.604  62.115  1.00 50.89  ? 235 PRO A CB    1 
ATOM   1804  C CG    . PRO A 1 235 ? 13.187  24.115  62.056  1.00 55.58  ? 235 PRO A CG    1 
ATOM   1805  C CD    . PRO A 1 235 ? 13.353  23.811  60.579  1.00 51.62  ? 235 PRO A CD    1 
ATOM   1806  N N     . GLU A 1 236 ? 11.451  28.139  60.393  1.00 49.93  ? 236 GLU A N     1 
ATOM   1807  C CA    . GLU A 1 236 ? 11.709  29.504  59.979  1.00 50.06  ? 236 GLU A CA    1 
ATOM   1808  C C     . GLU A 1 236 ? 13.070  29.865  60.542  1.00 46.64  ? 236 GLU A C     1 
ATOM   1809  O O     . GLU A 1 236 ? 13.272  29.746  61.736  1.00 59.44  ? 236 GLU A O     1 
ATOM   1810  C CB    . GLU A 1 236 ? 10.622  30.455  60.466  1.00 58.77  ? 236 GLU A CB    1 
ATOM   1811  C CG    . GLU A 1 236 ? 10.732  31.861  59.883  1.00 72.66  ? 236 GLU A CG    1 
ATOM   1812  C CD    . GLU A 1 236 ? 9.532   32.767  60.146  1.00 81.65  ? 236 GLU A CD    1 
ATOM   1813  O OE1   . GLU A 1 236 ? 9.747   33.971  60.346  1.00 79.31  ? 236 GLU A OE1   1 
ATOM   1814  O OE2   . GLU A 1 236 ? 8.381   32.262  60.169  1.00 75.97  ? 236 GLU A OE2   1 
ATOM   1815  N N     . PRO A 1 237 ? 14.063  30.226  59.709  1.00 50.57  ? 237 PRO A N     1 
ATOM   1816  C CA    . PRO A 1 237 ? 15.366  30.663  60.212  1.00 54.33  ? 237 PRO A CA    1 
ATOM   1817  C C     . PRO A 1 237 ? 15.298  32.032  60.874  1.00 53.91  ? 237 PRO A C     1 
ATOM   1818  O O     . PRO A 1 237 ? 14.245  32.635  60.917  1.00 62.95  ? 237 PRO A O     1 
ATOM   1819  C CB    . PRO A 1 237 ? 16.222  30.764  58.946  1.00 57.95  ? 237 PRO A CB    1 
ATOM   1820  C CG    . PRO A 1 237 ? 15.199  31.085  57.872  1.00 55.73  ? 237 PRO A CG    1 
ATOM   1821  C CD    . PRO A 1 237 ? 13.984  30.258  58.238  1.00 50.31  ? 237 PRO A CD    1 
ATOM   1822  N N     . ALA A 1 238 ? 16.437  32.514  61.361  1.00 53.56  ? 238 ALA A N     1 
ATOM   1823  C CA    . ALA A 1 238 ? 16.490  33.734  62.134  1.00 56.92  ? 238 ALA A CA    1 
ATOM   1824  C C     . ALA A 1 238 ? 16.796  34.907  61.218  1.00 52.00  ? 238 ALA A C     1 
ATOM   1825  O O     . ALA A 1 238 ? 16.569  36.040  61.604  1.00 58.18  ? 238 ALA A O     1 
ATOM   1826  C CB    . ALA A 1 238 ? 17.534  33.600  63.224  1.00 63.57  ? 238 ALA A CB    1 
ATOM   1827  N N     . GLY A 1 239 ? 17.366  34.631  60.045  1.00 50.97  ? 239 GLY A N     1 
ATOM   1828  C CA    . GLY A 1 239 ? 17.655  35.645  59.041  1.00 49.93  ? 239 GLY A CA    1 
ATOM   1829  C C     . GLY A 1 239 ? 17.620  35.051  57.632  1.00 56.71  ? 239 GLY A C     1 
ATOM   1830  O O     . GLY A 1 239 ? 17.481  33.831  57.475  1.00 59.17  ? 239 GLY A O     1 
ATOM   1831  N N     . TYR A 1 240 ? 17.746  35.921  56.619  1.00 59.72  ? 240 TYR A N     1 
ATOM   1832  C CA    . TYR A 1 240 ? 17.652  35.532  55.212  1.00 59.80  ? 240 TYR A CA    1 
ATOM   1833  C C     . TYR A 1 240 ? 18.210  36.658  54.337  1.00 60.12  ? 240 TYR A C     1 
ATOM   1834  O O     . TYR A 1 240 ? 17.814  37.818  54.452  1.00 59.83  ? 240 TYR A O     1 
ATOM   1835  C CB    . TYR A 1 240 ? 16.202  35.186  54.856  1.00 61.89  ? 240 TYR A CB    1 
ATOM   1836  C CG    . TYR A 1 240 ? 15.950  34.794  53.420  1.00 64.77  ? 240 TYR A CG    1 
ATOM   1837  C CD1   . TYR A 1 240 ? 16.467  33.623  52.890  1.00 65.04  ? 240 TYR A CD1   1 
ATOM   1838  C CD2   . TYR A 1 240 ? 15.159  35.574  52.595  1.00 57.97  ? 240 TYR A CD2   1 
ATOM   1839  C CE1   . TYR A 1 240 ? 16.216  33.240  51.584  1.00 59.36  ? 240 TYR A CE1   1 
ATOM   1840  C CE2   . TYR A 1 240 ? 14.915  35.219  51.281  1.00 59.67  ? 240 TYR A CE2   1 
ATOM   1841  C CZ    . TYR A 1 240 ? 15.451  34.051  50.768  1.00 63.71  ? 240 TYR A CZ    1 
ATOM   1842  O OH    . TYR A 1 240 ? 15.181  33.687  49.472  1.00 56.13  ? 240 TYR A OH    1 
ATOM   1843  N N     . ARG A 1 241 ? 19.206  36.340  53.514  1.00 56.39  ? 241 ARG A N     1 
ATOM   1844  C CA    . ARG A 1 241 ? 19.749  37.334  52.607  1.00 59.53  ? 241 ARG A CA    1 
ATOM   1845  C C     . ARG A 1 241 ? 19.963  36.644  51.261  1.00 59.00  ? 241 ARG A C     1 
ATOM   1846  O O     . ARG A 1 241 ? 20.927  35.891  51.120  1.00 60.10  ? 241 ARG A O     1 
ATOM   1847  C CB    . ARG A 1 241 ? 21.017  37.974  53.202  1.00 64.80  ? 241 ARG A CB    1 
ATOM   1848  C CG    . ARG A 1 241 ? 20.767  38.821  54.444  1.00 72.77  ? 241 ARG A CG    1 
ATOM   1849  C CD    . ARG A 1 241 ? 21.745  39.955  54.725  1.00 76.62  ? 241 ARG A CD    1 
ATOM   1850  N NE    . ARG A 1 241 ? 22.992  39.586  55.395  1.00 77.04  ? 241 ARG A NE    1 
ATOM   1851  C CZ    . ARG A 1 241 ? 24.215  39.808  54.907  1.00 84.29  ? 241 ARG A CZ    1 
ATOM   1852  N NH1   . ARG A 1 241 ? 24.376  40.345  53.709  1.00 81.10  ? 241 ARG A NH1   1 
ATOM   1853  N NH2   . ARG A 1 241 ? 25.285  39.476  55.612  1.00 85.50  ? 241 ARG A NH2   1 
ATOM   1854  N N     . PRO A 1 242 ? 19.042  36.789  50.272  1.00 55.03  ? 242 PRO A N     1 
ATOM   1855  C CA    . PRO A 1 242 ? 19.294  36.322  48.900  1.00 48.74  ? 242 PRO A CA    1 
ATOM   1856  C C     . PRO A 1 242 ? 20.253  37.233  48.151  1.00 44.42  ? 242 PRO A C     1 
ATOM   1857  O O     . PRO A 1 242 ? 20.359  38.411  48.453  1.00 47.58  ? 242 PRO A O     1 
ATOM   1858  C CB    . PRO A 1 242 ? 17.908  36.325  48.249  1.00 44.33  ? 242 PRO A CB    1 
ATOM   1859  C CG    . PRO A 1 242 ? 17.137  37.357  49.019  1.00 46.44  ? 242 PRO A CG    1 
ATOM   1860  C CD    . PRO A 1 242 ? 17.674  37.304  50.434  1.00 49.74  ? 242 PRO A CD    1 
ATOM   1861  N N     . TYR A 1 243 ? 20.992  36.672  47.194  1.00 45.13  ? 243 TYR A N     1 
ATOM   1862  C CA    . TYR A 1 243 ? 21.994  37.446  46.490  1.00 41.72  ? 243 TYR A CA    1 
ATOM   1863  C C     . TYR A 1 243 ? 22.080  36.947  45.058  1.00 38.36  ? 243 TYR A C     1 
ATOM   1864  O O     . TYR A 1 243 ? 21.688  35.832  44.774  1.00 38.79  ? 243 TYR A O     1 
ATOM   1865  C CB    . TYR A 1 243 ? 23.345  37.347  47.217  1.00 48.07  ? 243 TYR A CB    1 
ATOM   1866  C CG    . TYR A 1 243 ? 23.906  35.952  47.349  1.00 49.61  ? 243 TYR A CG    1 
ATOM   1867  C CD1   . TYR A 1 243 ? 24.631  35.352  46.327  1.00 55.49  ? 243 TYR A CD1   1 
ATOM   1868  C CD2   . TYR A 1 243 ? 23.677  35.203  48.487  1.00 52.18  ? 243 TYR A CD2   1 
ATOM   1869  C CE1   . TYR A 1 243 ? 25.132  34.063  46.453  1.00 58.40  ? 243 TYR A CE1   1 
ATOM   1870  C CE2   . TYR A 1 243 ? 24.148  33.903  48.621  1.00 54.07  ? 243 TYR A CE2   1 
ATOM   1871  C CZ    . TYR A 1 243 ? 24.901  33.337  47.609  1.00 56.83  ? 243 TYR A CZ    1 
ATOM   1872  O OH    . TYR A 1 243 ? 25.354  32.051  47.773  1.00 55.50  ? 243 TYR A OH    1 
ATOM   1873  N N     . LEU A 1 244 ? 22.687  37.762  44.200  1.00 37.09  ? 244 LEU A N     1 
ATOM   1874  C CA    . LEU A 1 244 ? 23.056  37.399  42.851  1.00 39.15  ? 244 LEU A CA    1 
ATOM   1875  C C     . LEU A 1 244 ? 24.536  37.736  42.592  1.00 43.86  ? 244 LEU A C     1 
ATOM   1876  O O     . LEU A 1 244 ? 25.022  38.838  42.882  1.00 44.01  ? 244 LEU A O     1 
ATOM   1877  C CB    . LEU A 1 244 ? 22.117  38.185  41.925  1.00 41.71  ? 244 LEU A CB    1 
ATOM   1878  C CG    . LEU A 1 244 ? 22.495  38.189  40.440  1.00 44.78  ? 244 LEU A CG    1 
ATOM   1879  C CD1   . LEU A 1 244 ? 22.354  36.793  39.860  1.00 39.79  ? 244 LEU A CD1   1 
ATOM   1880  C CD2   . LEU A 1 244 ? 21.662  39.179  39.634  1.00 43.47  ? 244 LEU A CD2   1 
ATOM   1881  N N     . ILE A 1 245 ? 25.268  36.790  42.002  1.00 41.12  ? 245 ILE A N     1 
ATOM   1882  C CA    . ILE A 1 245 ? 26.593  37.090  41.476  1.00 44.97  ? 245 ILE A CA    1 
ATOM   1883  C C     . ILE A 1 245 ? 26.583  36.863  39.957  1.00 43.86  ? 245 ILE A C     1 
ATOM   1884  O O     . ILE A 1 245 ? 26.233  35.762  39.510  1.00 47.46  ? 245 ILE A O     1 
ATOM   1885  C CB    . ILE A 1 245 ? 27.654  36.217  42.179  1.00 46.45  ? 245 ILE A CB    1 
ATOM   1886  C CG1   . ILE A 1 245 ? 27.606  36.348  43.707  1.00 50.38  ? 245 ILE A CG1   1 
ATOM   1887  C CG2   . ILE A 1 245 ? 29.030  36.526  41.631  1.00 46.29  ? 245 ILE A CG2   1 
ATOM   1888  C CD1   . ILE A 1 245 ? 28.770  35.691  44.422  1.00 46.45  ? 245 ILE A CD1   1 
ATOM   1889  N N     . THR A 1 246 ? 26.982  37.880  39.172  1.00 36.80  ? 246 THR A N     1 
ATOM   1890  C CA    . THR A 1 246 ? 26.984  37.770  37.715  1.00 37.96  ? 246 THR A CA    1 
ATOM   1891  C C     . THR A 1 246 ? 28.425  37.677  37.222  1.00 38.12  ? 246 THR A C     1 
ATOM   1892  O O     . THR A 1 246 ? 29.322  38.193  37.879  1.00 44.58  ? 246 THR A O     1 
ATOM   1893  C CB    . THR A 1 246 ? 26.261  38.945  37.023  1.00 37.49  ? 246 THR A CB    1 
ATOM   1894  O OG1   . THR A 1 246 ? 27.017  40.122  37.287  1.00 42.77  ? 246 THR A OG1   1 
ATOM   1895  C CG2   . THR A 1 246 ? 24.850  39.167  37.501  1.00 34.14  ? 246 THR A CG2   1 
ATOM   1896  N N     . PHE A 1 247 ? 28.623  37.057  36.044  1.00 43.46  ? 247 PHE A N     1 
ATOM   1897  C CA    . PHE A 1 247 ? 29.921  36.978  35.376  1.00 41.98  ? 247 PHE A CA    1 
ATOM   1898  C C     . PHE A 1 247 ? 29.795  37.495  33.934  1.00 44.83  ? 247 PHE A C     1 
ATOM   1899  O O     . PHE A 1 247 ? 28.782  37.284  33.259  1.00 48.03  ? 247 PHE A O     1 
ATOM   1900  C CB    . PHE A 1 247 ? 30.410  35.526  35.507  1.00 44.79  ? 247 PHE A CB    1 
ATOM   1901  C CG    . PHE A 1 247 ? 30.345  35.008  36.929  1.00 41.16  ? 247 PHE A CG    1 
ATOM   1902  C CD1   . PHE A 1 247 ? 31.381  35.255  37.828  1.00 38.88  ? 247 PHE A CD1   1 
ATOM   1903  C CD2   . PHE A 1 247 ? 29.196  34.384  37.402  1.00 36.77  ? 247 PHE A CD2   1 
ATOM   1904  C CE1   . PHE A 1 247 ? 31.283  34.850  39.154  1.00 38.43  ? 247 PHE A CE1   1 
ATOM   1905  C CE2   . PHE A 1 247 ? 29.113  33.959  38.722  1.00 39.59  ? 247 PHE A CE2   1 
ATOM   1906  C CZ    . PHE A 1 247 ? 30.155  34.194  39.593  1.00 39.13  ? 247 PHE A CZ    1 
ATOM   1907  N N     . GLU A 1 248 ? 30.824  38.201  33.459  1.00 50.70  ? 248 GLU A N     1 
ATOM   1908  C CA    . GLU A 1 248 ? 30.790  38.834  32.147  1.00 54.35  ? 248 GLU A CA    1 
ATOM   1909  C C     . GLU A 1 248 ? 30.864  37.796  31.029  1.00 58.14  ? 248 GLU A C     1 
ATOM   1910  O O     . GLU A 1 248 ? 30.065  37.850  30.097  1.00 60.98  ? 248 GLU A O     1 
ATOM   1911  C CB    . GLU A 1 248 ? 31.948  39.827  31.981  1.00 66.79  ? 248 GLU A CB    1 
ATOM   1912  C CG    . GLU A 1 248 ? 31.585  41.253  32.363  1.00 75.64  ? 248 GLU A CG    1 
ATOM   1913  C CD    . GLU A 1 248 ? 30.371  41.754  31.594  1.00 82.88  ? 248 GLU A CD    1 
ATOM   1914  O OE1   . GLU A 1 248 ? 30.497  41.921  30.345  1.00 78.72  ? 248 GLU A OE1   1 
ATOM   1915  O OE2   . GLU A 1 248 ? 29.282  41.914  32.229  1.00 65.97  ? 248 GLU A OE2   1 
ATOM   1916  N N     . ASN A 1 249 ? 31.808  36.844  31.138  1.00 53.47  ? 249 ASN A N     1 
ATOM   1917  C CA    . ASN A 1 249 ? 32.269  36.078  29.989  1.00 56.94  ? 249 ASN A CA    1 
ATOM   1918  C C     . ASN A 1 249 ? 31.749  34.644  30.001  1.00 49.67  ? 249 ASN A C     1 
ATOM   1919  O O     . ASN A 1 249 ? 31.669  34.023  31.045  1.00 45.40  ? 249 ASN A O     1 
ATOM   1920  C CB    . ASN A 1 249 ? 33.795  36.068  29.924  1.00 64.87  ? 249 ASN A CB    1 
ATOM   1921  C CG    . ASN A 1 249 ? 34.375  37.467  29.921  1.00 62.68  ? 249 ASN A CG    1 
ATOM   1922  O OD1   . ASN A 1 249 ? 34.235  38.190  28.940  1.00 57.56  ? 249 ASN A OD1   1 
ATOM   1923  N ND2   . ASN A 1 249 ? 35.017  37.856  31.012  1.00 62.27  ? 249 ASN A ND2   1 
ATOM   1924  N N     . GLU A 1 250 ? 31.430  34.115  28.815  1.00 48.89  ? 250 GLU A N     1 
ATOM   1925  C CA    . GLU A 1 250 ? 30.896  32.772  28.709  1.00 52.59  ? 250 GLU A CA    1 
ATOM   1926  C C     . GLU A 1 250 ? 31.869  31.770  29.335  1.00 52.06  ? 250 GLU A C     1 
ATOM   1927  O O     . GLU A 1 250 ? 31.437  30.818  29.969  1.00 49.37  ? 250 GLU A O     1 
ATOM   1928  C CB    . GLU A 1 250 ? 30.554  32.445  27.253  1.00 60.78  ? 250 GLU A CB    1 
ATOM   1929  C CG    . GLU A 1 250 ? 31.723  32.534  26.281  1.00 67.97  ? 250 GLU A CG    1 
ATOM   1930  C CD    . GLU A 1 250 ? 31.439  31.957  24.898  1.00 79.26  ? 250 GLU A CD    1 
ATOM   1931  O OE1   . GLU A 1 250 ? 30.363  31.347  24.701  1.00 86.74  ? 250 GLU A OE1   1 
ATOM   1932  O OE2   . GLU A 1 250 ? 32.291  32.110  24.011  1.00 76.53  ? 250 GLU A OE2   1 
ATOM   1933  N N     . ASP A 1 251 ? 33.181  31.992  29.176  1.00 58.47  ? 251 ASP A N     1 
ATOM   1934  C CA    . ASP A 1 251 ? 34.206  31.045  29.604  1.00 53.43  ? 251 ASP A CA    1 
ATOM   1935  C C     . ASP A 1 251 ? 34.362  31.018  31.131  1.00 54.22  ? 251 ASP A C     1 
ATOM   1936  O O     . ASP A 1 251 ? 34.972  30.093  31.668  1.00 66.52  ? 251 ASP A O     1 
ATOM   1937  C CB    . ASP A 1 251 ? 35.560  31.355  28.955  1.00 52.97  ? 251 ASP A CB    1 
ATOM   1938  C CG    . ASP A 1 251 ? 35.762  30.805  27.547  1.00 59.97  ? 251 ASP A CG    1 
ATOM   1939  O OD1   . ASP A 1 251 ? 34.838  30.124  27.011  1.00 58.62  ? 251 ASP A OD1   1 
ATOM   1940  O OD2   . ASP A 1 251 ? 36.880  31.010  27.012  1.00 53.11  ? 251 ASP A OD2   1 
ATOM   1941  N N     . ASP A 1 252 ? 33.804  32.012  31.830  1.00 47.67  ? 252 ASP A N     1 
ATOM   1942  C CA    . ASP A 1 252 ? 33.946  32.136  33.271  1.00 47.73  ? 252 ASP A CA    1 
ATOM   1943  C C     . ASP A 1 252 ? 33.316  30.921  33.972  1.00 45.54  ? 252 ASP A C     1 
ATOM   1944  O O     . ASP A 1 252 ? 33.609  30.640  35.125  1.00 43.67  ? 252 ASP A O     1 
ATOM   1945  C CB    . ASP A 1 252 ? 33.331  33.447  33.808  1.00 47.11  ? 252 ASP A CB    1 
ATOM   1946  C CG    . ASP A 1 252 ? 34.047  34.776  33.559  1.00 51.35  ? 252 ASP A CG    1 
ATOM   1947  O OD1   . ASP A 1 252 ? 35.278  34.782  33.384  1.00 54.86  ? 252 ASP A OD1   1 
ATOM   1948  O OD2   . ASP A 1 252 ? 33.365  35.830  33.593  1.00 58.65  ? 252 ASP A OD2   1 
ATOM   1949  N N     . ILE A 1 253 ? 32.413  30.195  33.320  1.00 45.06  ? 253 ILE A N     1 
ATOM   1950  C CA    . ILE A 1 253 ? 31.733  29.100  34.007  1.00 44.63  ? 253 ILE A CA    1 
ATOM   1951  C C     . ILE A 1 253 ? 32.702  28.008  34.486  1.00 42.86  ? 253 ILE A C     1 
ATOM   1952  O O     . ILE A 1 253 ? 32.418  27.294  35.444  1.00 39.25  ? 253 ILE A O     1 
ATOM   1953  C CB    . ILE A 1 253 ? 30.628  28.503  33.116  1.00 41.29  ? 253 ILE A CB    1 
ATOM   1954  C CG1   . ILE A 1 253 ? 29.706  27.574  33.909  1.00 38.53  ? 253 ILE A CG1   1 
ATOM   1955  C CG2   . ILE A 1 253 ? 31.228  27.807  31.897  1.00 42.24  ? 253 ILE A CG2   1 
ATOM   1956  C CD1   . ILE A 1 253 ? 29.152  28.181  35.181  1.00 37.06  ? 253 ILE A CD1   1 
ATOM   1957  N N     . GLU A 1 254 ? 33.848  27.869  33.817  1.00 48.48  ? 254 GLU A N     1 
ATOM   1958  C CA    . GLU A 1 254 ? 34.883  26.938  34.227  1.00 43.68  ? 254 GLU A CA    1 
ATOM   1959  C C     . GLU A 1 254 ? 35.398  27.304  35.629  1.00 43.76  ? 254 GLU A C     1 
ATOM   1960  O O     . GLU A 1 254 ? 35.351  26.498  36.545  1.00 46.86  ? 254 GLU A O     1 
ATOM   1961  C CB    . GLU A 1 254 ? 35.953  26.886  33.135  1.00 46.23  ? 254 GLU A CB    1 
ATOM   1962  C CG    . GLU A 1 254 ? 37.068  25.906  33.437  1.00 56.54  ? 254 GLU A CG    1 
ATOM   1963  C CD    . GLU A 1 254 ? 38.093  25.589  32.358  1.00 57.30  ? 254 GLU A CD    1 
ATOM   1964  O OE1   . GLU A 1 254 ? 37.931  26.030  31.183  1.00 62.82  ? 254 GLU A OE1   1 
ATOM   1965  O OE2   . GLU A 1 254 ? 39.051  24.872  32.702  1.00 52.87  ? 254 GLU A OE2   1 
ATOM   1966  N N     . THR A 1 255 ? 35.873  28.527  35.846  1.00 51.75  ? 255 THR A N     1 
ATOM   1967  C CA    . THR A 1 255 ? 36.492  28.845  37.128  1.00 49.51  ? 255 THR A CA    1 
ATOM   1968  C C     . THR A 1 255 ? 35.413  28.931  38.212  1.00 44.82  ? 255 THR A C     1 
ATOM   1969  O O     . THR A 1 255 ? 35.654  28.628  39.382  1.00 43.75  ? 255 THR A O     1 
ATOM   1970  C CB    . THR A 1 255 ? 37.425  30.060  36.990  1.00 53.74  ? 255 THR A CB    1 
ATOM   1971  O OG1   . THR A 1 255 ? 38.188  30.225  38.186  1.00 55.78  ? 255 THR A OG1   1 
ATOM   1972  C CG2   . THR A 1 255 ? 36.688  31.346  36.704  1.00 62.15  ? 255 THR A CG2   1 
ATOM   1973  N N     . VAL A 1 256 ? 34.206  29.309  37.805  1.00 46.21  ? 256 VAL A N     1 
ATOM   1974  C CA    . VAL A 1 256 ? 33.097  29.484  38.716  1.00 39.78  ? 256 VAL A CA    1 
ATOM   1975  C C     . VAL A 1 256 ? 32.755  28.121  39.302  1.00 40.04  ? 256 VAL A C     1 
ATOM   1976  O O     . VAL A 1 256 ? 32.608  27.996  40.526  1.00 38.33  ? 256 VAL A O     1 
ATOM   1977  C CB    . VAL A 1 256 ? 31.922  30.163  37.998  1.00 44.49  ? 256 VAL A CB    1 
ATOM   1978  C CG1   . VAL A 1 256 ? 30.639  30.153  38.811  1.00 49.65  ? 256 VAL A CG1   1 
ATOM   1979  C CG2   . VAL A 1 256 ? 32.273  31.587  37.621  1.00 47.22  ? 256 VAL A CG2   1 
ATOM   1980  N N     . THR A 1 257 ? 32.713  27.083  38.446  1.00 40.90  ? 257 THR A N     1 
ATOM   1981  C CA    . THR A 1 257 ? 32.360  25.754  38.938  1.00 36.16  ? 257 THR A CA    1 
ATOM   1982  C C     . THR A 1 257 ? 33.463  25.248  39.881  1.00 37.35  ? 257 THR A C     1 
ATOM   1983  O O     . THR A 1 257 ? 33.155  24.687  40.928  1.00 36.44  ? 257 THR A O     1 
ATOM   1984  C CB    . THR A 1 257 ? 31.980  24.814  37.794  1.00 40.67  ? 257 THR A CB    1 
ATOM   1985  O OG1   . THR A 1 257 ? 30.820  25.272  37.075  1.00 47.66  ? 257 THR A OG1   1 
ATOM   1986  C CG2   . THR A 1 257 ? 31.721  23.416  38.307  1.00 43.43  ? 257 THR A CG2   1 
ATOM   1987  N N     . GLU A 1 258 ? 34.741  25.541  39.563  1.00 37.69  ? 258 GLU A N     1 
ATOM   1988  C CA    . GLU A 1 258 ? 35.875  25.174  40.404  1.00 38.19  ? 258 GLU A CA    1 
ATOM   1989  C C     . GLU A 1 258 ? 35.752  25.803  41.791  1.00 44.59  ? 258 GLU A C     1 
ATOM   1990  O O     . GLU A 1 258 ? 35.972  25.147  42.794  1.00 51.94  ? 258 GLU A O     1 
ATOM   1991  C CB    . GLU A 1 258 ? 37.203  25.599  39.771  1.00 38.45  ? 258 GLU A CB    1 
ATOM   1992  C CG    . GLU A 1 258 ? 37.648  24.711  38.622  1.00 38.36  ? 258 GLU A CG    1 
ATOM   1993  C CD    . GLU A 1 258 ? 38.046  23.292  39.004  1.00 38.71  ? 258 GLU A CD    1 
ATOM   1994  O OE1   . GLU A 1 258 ? 39.095  23.127  39.631  1.00 48.44  ? 258 GLU A OE1   1 
ATOM   1995  O OE2   . GLU A 1 258 ? 37.315  22.353  38.669  1.00 42.74  ? 258 GLU A OE2   1 
ATOM   1996  N N     . ARG A 1 259 ? 35.386  27.082  41.852  1.00 45.91  ? 259 ARG A N     1 
ATOM   1997  C CA    . ARG A 1 259 ? 35.230  27.759  43.115  1.00 41.27  ? 259 ARG A CA    1 
ATOM   1998  C C     . ARG A 1 259 ? 34.007  27.257  43.886  1.00 48.43  ? 259 ARG A C     1 
ATOM   1999  O O     . ARG A 1 259 ? 34.014  27.296  45.119  1.00 45.25  ? 259 ARG A O     1 
ATOM   2000  C CB    . ARG A 1 259 ? 35.145  29.249  42.814  1.00 48.09  ? 259 ARG A CB    1 
ATOM   2001  C CG    . ARG A 1 259 ? 36.421  29.794  42.196  1.00 52.77  ? 259 ARG A CG    1 
ATOM   2002  C CD    . ARG A 1 259 ? 36.146  30.929  41.243  1.00 53.71  ? 259 ARG A CD    1 
ATOM   2003  N NE    . ARG A 1 259 ? 37.392  31.320  40.625  1.00 55.78  ? 259 ARG A NE    1 
ATOM   2004  C CZ    . ARG A 1 259 ? 38.186  32.258  41.112  1.00 53.08  ? 259 ARG A CZ    1 
ATOM   2005  N NH1   . ARG A 1 259 ? 37.895  32.821  42.269  1.00 47.49  ? 259 ARG A NH1   1 
ATOM   2006  N NH2   . ARG A 1 259 ? 39.265  32.623  40.446  1.00 50.37  ? 259 ARG A NH2   1 
ATOM   2007  N N     . LEU A 1 260 ? 32.969  26.782  43.173  1.00 46.60  ? 260 LEU A N     1 
ATOM   2008  C CA    . LEU A 1 260 ? 31.712  26.422  43.815  1.00 42.06  ? 260 LEU A CA    1 
ATOM   2009  C C     . LEU A 1 260 ? 31.837  25.121  44.580  1.00 41.53  ? 260 LEU A C     1 
ATOM   2010  O O     . LEU A 1 260 ? 31.189  24.925  45.606  1.00 44.51  ? 260 LEU A O     1 
ATOM   2011  C CB    . LEU A 1 260 ? 30.594  26.306  42.775  1.00 45.36  ? 260 LEU A CB    1 
ATOM   2012  C CG    . LEU A 1 260 ? 29.851  27.612  42.462  1.00 45.66  ? 260 LEU A CG    1 
ATOM   2013  C CD1   . LEU A 1 260 ? 28.913  27.423  41.280  1.00 49.79  ? 260 LEU A CD1   1 
ATOM   2014  C CD2   . LEU A 1 260 ? 29.045  28.097  43.662  1.00 44.29  ? 260 LEU A CD2   1 
ATOM   2015  N N     . ARG A 1 261 ? 32.651  24.226  44.032  1.00 46.74  ? 261 ARG A N     1 
ATOM   2016  C CA    . ARG A 1 261 ? 32.830  22.889  44.565  1.00 44.56  ? 261 ARG A CA    1 
ATOM   2017  C C     . ARG A 1 261 ? 33.064  22.911  46.085  1.00 44.95  ? 261 ARG A C     1 
ATOM   2018  O O     . ARG A 1 261 ? 32.208  22.470  46.845  1.00 44.61  ? 261 ARG A O     1 
ATOM   2019  C CB    . ARG A 1 261 ? 33.983  22.219  43.811  1.00 42.81  ? 261 ARG A CB    1 
ATOM   2020  C CG    . ARG A 1 261 ? 34.488  20.955  44.486  1.00 44.27  ? 261 ARG A CG    1 
ATOM   2021  C CD    . ARG A 1 261 ? 35.406  20.131  43.628  1.00 41.02  ? 261 ARG A CD    1 
ATOM   2022  N NE    . ARG A 1 261 ? 36.674  20.809  43.482  1.00 37.05  ? 261 ARG A NE    1 
ATOM   2023  C CZ    . ARG A 1 261 ? 37.149  21.208  42.309  1.00 39.92  ? 261 ARG A CZ    1 
ATOM   2024  N NH1   . ARG A 1 261 ? 36.425  21.079  41.216  1.00 40.15  ? 261 ARG A NH1   1 
ATOM   2025  N NH2   . ARG A 1 261 ? 38.358  21.722  42.213  1.00 40.43  ? 261 ARG A NH2   1 
ATOM   2026  N N     . PRO A 1 262 ? 34.228  23.353  46.612  1.00 44.57  ? 262 PRO A N     1 
ATOM   2027  C CA    . PRO A 1 262 ? 34.488  23.265  48.059  1.00 44.93  ? 262 PRO A CA    1 
ATOM   2028  C C     . PRO A 1 262 ? 33.414  23.919  48.933  1.00 48.02  ? 262 PRO A C     1 
ATOM   2029  O O     . PRO A 1 262 ? 33.145  23.426  50.020  1.00 50.66  ? 262 PRO A O     1 
ATOM   2030  C CB    . PRO A 1 262 ? 35.841  23.957  48.262  1.00 35.16  ? 262 PRO A CB    1 
ATOM   2031  C CG    . PRO A 1 262 ? 36.007  24.796  47.015  1.00 43.69  ? 262 PRO A CG    1 
ATOM   2032  C CD    . PRO A 1 262 ? 35.337  24.004  45.900  1.00 45.93  ? 262 PRO A CD    1 
ATOM   2033  N N     . LEU A 1 263 ? 32.792  25.006  48.444  1.00 46.26  ? 263 LEU A N     1 
ATOM   2034  C CA    . LEU A 1 263 ? 31.731  25.689  49.172  1.00 43.97  ? 263 LEU A CA    1 
ATOM   2035  C C     . LEU A 1 263 ? 30.498  24.803  49.304  1.00 39.74  ? 263 LEU A C     1 
ATOM   2036  O O     . LEU A 1 263 ? 29.844  24.825  50.336  1.00 40.68  ? 263 LEU A O     1 
ATOM   2037  C CB    . LEU A 1 263 ? 31.347  26.981  48.446  1.00 44.65  ? 263 LEU A CB    1 
ATOM   2038  C CG    . LEU A 1 263 ? 32.473  27.985  48.257  1.00 38.17  ? 263 LEU A CG    1 
ATOM   2039  C CD1   . LEU A 1 263 ? 31.975  29.199  47.517  1.00 36.15  ? 263 LEU A CD1   1 
ATOM   2040  C CD2   . LEU A 1 263 ? 33.038  28.375  49.602  1.00 43.05  ? 263 LEU A CD2   1 
ATOM   2041  N N     . LYS A 1 264 ? 30.193  24.036  48.257  1.00 38.83  ? 264 LYS A N     1 
ATOM   2042  C CA    . LYS A 1 264 ? 29.062  23.123  48.259  1.00 43.40  ? 264 LYS A CA    1 
ATOM   2043  C C     . LYS A 1 264 ? 29.362  21.802  48.989  1.00 42.57  ? 264 LYS A C     1 
ATOM   2044  O O     . LYS A 1 264 ? 28.491  21.251  49.676  1.00 44.62  ? 264 LYS A O     1 
ATOM   2045  C CB    . LYS A 1 264 ? 28.629  22.848  46.814  1.00 45.37  ? 264 LYS A CB    1 
ATOM   2046  C CG    . LYS A 1 264 ? 27.697  23.886  46.210  1.00 47.34  ? 264 LYS A CG    1 
ATOM   2047  C CD    . LYS A 1 264 ? 26.432  24.105  47.003  1.00 46.07  ? 264 LYS A CD    1 
ATOM   2048  C CE    . LYS A 1 264 ? 25.568  22.884  47.188  1.00 48.52  ? 264 LYS A CE    1 
ATOM   2049  N NZ    . LYS A 1 264 ? 24.655  23.073  48.345  1.00 53.11  ? 264 LYS A NZ    1 
ATOM   2050  N N     . VAL A 1 265 ? 30.561  21.247  48.814  1.00 39.27  ? 265 VAL A N     1 
ATOM   2051  C CA    . VAL A 1 265 ? 30.880  19.959  49.409  1.00 39.79  ? 265 VAL A CA    1 
ATOM   2052  C C     . VAL A 1 265 ? 30.874  20.119  50.931  1.00 42.44  ? 265 VAL A C     1 
ATOM   2053  O O     . VAL A 1 265 ? 30.491  19.211  51.667  1.00 47.01  ? 265 VAL A O     1 
ATOM   2054  C CB    . VAL A 1 265 ? 32.223  19.443  48.852  1.00 37.86  ? 265 VAL A CB    1 
ATOM   2055  C CG1   . VAL A 1 265 ? 32.785  18.277  49.639  1.00 36.03  ? 265 VAL A CG1   1 
ATOM   2056  C CG2   . VAL A 1 265 ? 32.086  19.068  47.382  1.00 39.89  ? 265 VAL A CG2   1 
ATOM   2057  N N     . ALA A 1 266 ? 31.242  21.313  51.410  1.00 40.58  ? 266 ALA A N     1 
ATOM   2058  C CA    . ALA A 1 266 ? 31.312  21.537  52.850  1.00 42.63  ? 266 ALA A CA    1 
ATOM   2059  C C     . ALA A 1 266 ? 30.006  22.091  53.414  1.00 41.94  ? 266 ALA A C     1 
ATOM   2060  O O     . ALA A 1 266 ? 29.893  22.193  54.610  1.00 42.43  ? 266 ALA A O     1 
ATOM   2061  C CB    . ALA A 1 266 ? 32.480  22.436  53.185  1.00 38.83  ? 266 ALA A CB    1 
ATOM   2062  N N     . GLY A 1 267 ? 29.028  22.478  52.588  1.00 49.38  ? 267 GLY A N     1 
ATOM   2063  C CA    . GLY A 1 267 ? 27.784  23.047  53.103  1.00 52.22  ? 267 GLY A CA    1 
ATOM   2064  C C     . GLY A 1 267 ? 27.860  24.551  53.410  1.00 47.42  ? 267 GLY A C     1 
ATOM   2065  O O     . GLY A 1 267 ? 26.966  25.085  54.044  1.00 48.19  ? 267 GLY A O     1 
ATOM   2066  N N     . VAL A 1 268 ? 28.906  25.233  52.945  1.00 48.22  ? 268 VAL A N     1 
ATOM   2067  C CA    . VAL A 1 268 ? 29.093  26.661  53.178  1.00 54.89  ? 268 VAL A CA    1 
ATOM   2068  C C     . VAL A 1 268 ? 27.985  27.454  52.489  1.00 52.62  ? 268 VAL A C     1 
ATOM   2069  O O     . VAL A 1 268 ? 27.405  28.351  53.098  1.00 66.56  ? 268 VAL A O     1 
ATOM   2070  C CB    . VAL A 1 268 ? 30.480  27.146  52.711  1.00 48.54  ? 268 VAL A CB    1 
ATOM   2071  C CG1   . VAL A 1 268 ? 30.614  28.645  52.864  1.00 48.02  ? 268 VAL A CG1   1 
ATOM   2072  C CG2   . VAL A 1 268 ? 31.606  26.423  53.440  1.00 50.57  ? 268 VAL A CG2   1 
ATOM   2073  N N     . ILE A 1 269 ? 27.737  27.147  51.210  1.00 48.72  ? 269 ILE A N     1 
ATOM   2074  C CA    . ILE A 1 269 ? 26.502  27.511  50.537  1.00 40.55  ? 269 ILE A CA    1 
ATOM   2075  C C     . ILE A 1 269 ? 25.418  26.542  51.018  1.00 43.01  ? 269 ILE A C     1 
ATOM   2076  O O     . ILE A 1 269 ? 25.551  25.327  50.891  1.00 48.98  ? 269 ILE A O     1 
ATOM   2077  C CB    . ILE A 1 269 ? 26.718  27.465  49.016  1.00 38.89  ? 269 ILE A CB    1 
ATOM   2078  C CG1   . ILE A 1 269 ? 27.639  28.588  48.554  1.00 37.88  ? 269 ILE A CG1   1 
ATOM   2079  C CG2   . ILE A 1 269 ? 25.379  27.501  48.301  1.00 43.62  ? 269 ILE A CG2   1 
ATOM   2080  C CD1   . ILE A 1 269 ? 28.146  28.467  47.119  1.00 42.16  ? 269 ILE A CD1   1 
ATOM   2081  N N     . GLN A 1 270 ? 24.337  27.055  51.605  1.00 44.07  ? 270 GLN A N     1 
ATOM   2082  C CA    . GLN A 1 270 ? 23.413  26.188  52.327  1.00 43.89  ? 270 GLN A CA    1 
ATOM   2083  C C     . GLN A 1 270 ? 22.298  25.633  51.443  1.00 43.51  ? 270 GLN A C     1 
ATOM   2084  O O     . GLN A 1 270 ? 21.679  24.619  51.766  1.00 52.10  ? 270 GLN A O     1 
ATOM   2085  C CB    . GLN A 1 270 ? 22.795  26.948  53.499  1.00 44.86  ? 270 GLN A CB    1 
ATOM   2086  C CG    . GLN A 1 270 ? 23.807  27.419  54.526  1.00 45.07  ? 270 GLN A CG    1 
ATOM   2087  C CD    . GLN A 1 270 ? 23.409  28.739  55.140  1.00 45.73  ? 270 GLN A CD    1 
ATOM   2088  O OE1   . GLN A 1 270 ? 23.466  29.798  54.517  1.00 42.35  ? 270 GLN A OE1   1 
ATOM   2089  N NE2   . GLN A 1 270 ? 23.006  28.677  56.391  1.00 50.18  ? 270 GLN A NE2   1 
ATOM   2090  N N     . ASN A 1 271 ? 21.967  26.311  50.355  1.00 43.24  ? 271 ASN A N     1 
ATOM   2091  C CA    . ASN A 1 271 ? 21.006  25.741  49.420  1.00 44.80  ? 271 ASN A CA    1 
ATOM   2092  C C     . ASN A 1 271 ? 21.702  25.368  48.125  1.00 38.96  ? 271 ASN A C     1 
ATOM   2093  O O     . ASN A 1 271 ? 22.910  25.505  48.043  1.00 45.24  ? 271 ASN A O     1 
ATOM   2094  C CB    . ASN A 1 271 ? 19.837  26.684  49.132  1.00 48.55  ? 271 ASN A CB    1 
ATOM   2095  C CG    . ASN A 1 271 ? 20.219  28.000  48.499  1.00 41.71  ? 271 ASN A CG    1 
ATOM   2096  O OD1   . ASN A 1 271 ? 21.356  28.501  48.562  1.00 43.32  ? 271 ASN A OD1   1 
ATOM   2097  N ND2   . ASN A 1 271 ? 19.192  28.594  47.940  1.00 42.03  ? 271 ASN A ND2   1 
ATOM   2098  N N     . GLY A 1 272 ? 20.935  24.825  47.173  1.00 41.63  ? 272 GLY A N     1 
ATOM   2099  C CA    . GLY A 1 272 ? 21.411  24.549  45.828  1.00 36.68  ? 272 GLY A CA    1 
ATOM   2100  C C     . GLY A 1 272 ? 22.017  25.797  45.202  1.00 40.62  ? 272 GLY A C     1 
ATOM   2101  O O     . GLY A 1 272 ? 21.535  26.893  45.412  1.00 39.90  ? 272 GLY A O     1 
ATOM   2102  N N     . ALA A 1 273 ? 23.145  25.621  44.522  1.00 50.78  ? 273 ALA A N     1 
ATOM   2103  C CA    . ALA A 1 273 ? 23.762  26.656  43.721  1.00 52.59  ? 273 ALA A CA    1 
ATOM   2104  C C     . ALA A 1 273 ? 23.236  26.497  42.298  1.00 53.51  ? 273 ALA A C     1 
ATOM   2105  O O     . ALA A 1 273 ? 23.246  25.391  41.772  1.00 60.37  ? 273 ALA A O     1 
ATOM   2106  C CB    . ALA A 1 273 ? 25.272  26.524  43.782  1.00 47.84  ? 273 ALA A CB    1 
ATOM   2107  N N     . THR A 1 274 ? 22.754  27.598  41.709  1.00 51.34  ? 274 THR A N     1 
ATOM   2108  C CA    . THR A 1 274 ? 22.247  27.609  40.348  1.00 48.71  ? 274 THR A CA    1 
ATOM   2109  C C     . THR A 1 274 ? 22.929  28.746  39.596  1.00 50.17  ? 274 THR A C     1 
ATOM   2110  O O     . THR A 1 274 ? 22.793  29.891  39.999  1.00 55.88  ? 274 THR A O     1 
ATOM   2111  C CB    . THR A 1 274 ? 20.719  27.754  40.312  1.00 55.07  ? 274 THR A CB    1 
ATOM   2112  O OG1   . THR A 1 274 ? 20.423  29.044  40.841  1.00 71.66  ? 274 THR A OG1   1 
ATOM   2113  C CG2   . THR A 1 274 ? 19.966  26.694  41.096  1.00 56.90  ? 274 THR A CG2   1 
ATOM   2114  N N     . VAL A 1 275 ? 23.691  28.418  38.541  1.00 43.68  ? 275 VAL A N     1 
ATOM   2115  C CA    . VAL A 1 275 ? 24.327  29.421  37.720  1.00 41.14  ? 275 VAL A CA    1 
ATOM   2116  C C     . VAL A 1 275 ? 23.669  29.373  36.341  1.00 49.58  ? 275 VAL A C     1 
ATOM   2117  O O     . VAL A 1 275 ? 23.737  28.375  35.613  1.00 45.18  ? 275 VAL A O     1 
ATOM   2118  C CB    . VAL A 1 275 ? 25.852  29.219  37.693  1.00 41.52  ? 275 VAL A CB    1 
ATOM   2119  C CG1   . VAL A 1 275 ? 26.551  30.318  36.937  1.00 42.42  ? 275 VAL A CG1   1 
ATOM   2120  C CG2   . VAL A 1 275 ? 26.429  29.146  39.092  1.00 44.49  ? 275 VAL A CG2   1 
ATOM   2121  N N     . ARG A 1 276 ? 22.970  30.461  36.002  1.00 47.04  ? 276 ARG A N     1 
ATOM   2122  C CA    . ARG A 1 276 ? 22.052  30.412  34.882  1.00 43.45  ? 276 ARG A CA    1 
ATOM   2123  C C     . ARG A 1 276 ? 22.611  31.279  33.761  1.00 43.77  ? 276 ARG A C     1 
ATOM   2124  O O     . ARG A 1 276 ? 23.226  32.310  34.042  1.00 41.65  ? 276 ARG A O     1 
ATOM   2125  C CB    . ARG A 1 276 ? 20.656  30.842  35.339  1.00 43.84  ? 276 ARG A CB    1 
ATOM   2126  C CG    . ARG A 1 276 ? 19.924  29.816  36.193  1.00 45.35  ? 276 ARG A CG    1 
ATOM   2127  C CD    . ARG A 1 276 ? 18.441  30.135  36.288  1.00 48.03  ? 276 ARG A CD    1 
ATOM   2128  N NE    . ARG A 1 276 ? 17.710  29.358  37.278  1.00 53.69  ? 276 ARG A NE    1 
ATOM   2129  C CZ    . ARG A 1 276 ? 17.702  29.595  38.593  1.00 64.41  ? 276 ARG A CZ    1 
ATOM   2130  N NH1   . ARG A 1 276 ? 18.349  30.632  39.114  1.00 62.18  ? 276 ARG A NH1   1 
ATOM   2131  N NH2   . ARG A 1 276 ? 17.015  28.785  39.387  1.00 69.13  ? 276 ARG A NH2   1 
ATOM   2132  N N     . SER A 1 277 ? 22.398  30.834  32.509  1.00 42.89  ? 277 SER A N     1 
ATOM   2133  C CA    . SER A 1 277 ? 22.853  31.573  31.342  1.00 41.14  ? 277 SER A CA    1 
ATOM   2134  C C     . SER A 1 277 ? 21.953  32.781  31.134  1.00 45.23  ? 277 SER A C     1 
ATOM   2135  O O     . SER A 1 277 ? 20.765  32.751  31.485  1.00 40.21  ? 277 SER A O     1 
ATOM   2136  C CB    . SER A 1 277 ? 22.860  30.743  30.095  1.00 37.89  ? 277 SER A CB    1 
ATOM   2137  O OG    . SER A 1 277 ? 21.589  30.145  29.890  1.00 37.97  ? 277 SER A OG    1 
ATOM   2138  N N     . LEU A 1 278 ? 22.563  33.798  30.513  1.00 43.55  ? 278 LEU A N     1 
ATOM   2139  C CA    . LEU A 1 278 ? 21.944  35.079  30.249  1.00 47.89  ? 278 LEU A CA    1 
ATOM   2140  C C     . LEU A 1 278 ? 20.490  34.936  29.784  1.00 44.25  ? 278 LEU A C     1 
ATOM   2141  O O     . LEU A 1 278 ? 19.600  35.597  30.316  1.00 48.25  ? 278 LEU A O     1 
ATOM   2142  C CB    . LEU A 1 278 ? 22.790  35.807  29.204  1.00 52.85  ? 278 LEU A CB    1 
ATOM   2143  C CG    . LEU A 1 278 ? 22.140  37.071  28.644  1.00 55.78  ? 278 LEU A CG    1 
ATOM   2144  C CD1   . LEU A 1 278 ? 21.847  38.049  29.765  1.00 55.94  ? 278 LEU A CD1   1 
ATOM   2145  C CD2   . LEU A 1 278 ? 23.007  37.717  27.576  1.00 56.23  ? 278 LEU A CD2   1 
ATOM   2146  N N     . VAL A 1 279 ? 20.245  34.078  28.802  1.00 40.05  ? 279 VAL A N     1 
ATOM   2147  C CA    . VAL A 1 279 ? 18.935  34.010  28.182  1.00 42.54  ? 279 VAL A CA    1 
ATOM   2148  C C     . VAL A 1 279 ? 17.916  33.318  29.086  1.00 51.51  ? 279 VAL A C     1 
ATOM   2149  O O     . VAL A 1 279 ? 16.700  33.548  28.984  1.00 50.65  ? 279 VAL A O     1 
ATOM   2150  C CB    . VAL A 1 279 ? 18.985  33.308  26.823  1.00 41.89  ? 279 VAL A CB    1 
ATOM   2151  C CG1   . VAL A 1 279 ? 17.583  32.992  26.329  1.00 45.25  ? 279 VAL A CG1   1 
ATOM   2152  C CG2   . VAL A 1 279 ? 19.765  34.126  25.796  1.00 42.95  ? 279 VAL A CG2   1 
ATOM   2153  N N     . LEU A 1 280 ? 18.384  32.435  29.956  1.00 48.41  ? 280 LEU A N     1 
ATOM   2154  C CA    . LEU A 1 280 ? 17.421  31.727  30.767  1.00 46.27  ? 280 LEU A CA    1 
ATOM   2155  C C     . LEU A 1 280 ? 16.922  32.665  31.865  1.00 43.38  ? 280 LEU A C     1 
ATOM   2156  O O     . LEU A 1 280 ? 15.723  32.691  32.142  1.00 40.53  ? 280 LEU A O     1 
ATOM   2157  C CB    . LEU A 1 280 ? 18.034  30.419  31.271  1.00 45.22  ? 280 LEU A CB    1 
ATOM   2158  C CG    . LEU A 1 280 ? 17.215  29.695  32.330  1.00 47.78  ? 280 LEU A CG    1 
ATOM   2159  C CD1   . LEU A 1 280 ? 15.868  29.238  31.771  1.00 45.12  ? 280 LEU A CD1   1 
ATOM   2160  C CD2   . LEU A 1 280 ? 18.014  28.534  32.903  1.00 48.31  ? 280 LEU A CD2   1 
ATOM   2161  N N     . ASP A 1 281 ? 17.808  33.506  32.413  1.00 49.53  ? 281 ASP A N     1 
ATOM   2162  C CA    . ASP A 1 281 ? 17.409  34.521  33.396  1.00 53.72  ? 281 ASP A CA    1 
ATOM   2163  C C     . ASP A 1 281 ? 16.775  35.749  32.739  1.00 46.65  ? 281 ASP A C     1 
ATOM   2164  O O     . ASP A 1 281 ? 15.785  36.267  33.236  1.00 45.71  ? 281 ASP A O     1 
ATOM   2165  C CB    . ASP A 1 281 ? 18.580  34.960  34.286  1.00 53.43  ? 281 ASP A CB    1 
ATOM   2166  C CG    . ASP A 1 281 ? 18.816  34.037  35.470  1.00 52.89  ? 281 ASP A CG    1 
ATOM   2167  O OD1   . ASP A 1 281 ? 17.838  33.283  35.836  1.00 48.46  ? 281 ASP A OD1   1 
ATOM   2168  O OD2   . ASP A 1 281 ? 19.972  34.068  36.023  1.00 50.66  ? 281 ASP A OD2   1 
ATOM   2169  N N     . ALA A 1 282 ? 17.323  36.212  31.616  1.00 45.08  ? 282 ALA A N     1 
ATOM   2170  C CA    . ALA A 1 282 ? 16.682  37.307  30.905  1.00 46.14  ? 282 ALA A CA    1 
ATOM   2171  C C     . ALA A 1 282 ? 15.221  36.977  30.653  1.00 46.69  ? 282 ALA A C     1 
ATOM   2172  O O     . ALA A 1 282 ? 14.394  37.883  30.621  1.00 52.41  ? 282 ALA A O     1 
ATOM   2173  C CB    . ALA A 1 282 ? 17.361  37.590  29.595  1.00 44.98  ? 282 ALA A CB    1 
ATOM   2174  N N     . ALA A 1 283 ? 14.922  35.687  30.454  1.00 50.80  ? 283 ALA A N     1 
ATOM   2175  C CA    . ALA A 1 283 ? 13.596  35.243  30.042  1.00 47.42  ? 283 ALA A CA    1 
ATOM   2176  C C     . ALA A 1 283 ? 12.612  35.327  31.198  1.00 49.91  ? 283 ALA A C     1 
ATOM   2177  O O     . ALA A 1 283 ? 11.467  34.915  31.052  1.00 55.51  ? 283 ALA A O     1 
ATOM   2178  C CB    . ALA A 1 283 ? 13.656  33.831  29.513  1.00 46.22  ? 283 ALA A CB    1 
ATOM   2179  N N     . ILE A 1 284 ? 13.071  35.808  32.354  1.00 51.88  ? 284 ILE A N     1 
ATOM   2180  C CA    . ILE A 1 284 ? 12.189  35.946  33.493  1.00 60.77  ? 284 ILE A CA    1 
ATOM   2181  C C     . ILE A 1 284 ? 11.412  37.250  33.350  1.00 64.51  ? 284 ILE A C     1 
ATOM   2182  O O     . ILE A 1 284 ? 10.313  37.348  33.894  1.00 58.54  ? 284 ILE A O     1 
ATOM   2183  C CB    . ILE A 1 284 ? 12.964  35.821  34.826  1.00 69.00  ? 284 ILE A CB    1 
ATOM   2184  C CG1   . ILE A 1 284 ? 13.416  34.377  35.069  1.00 72.18  ? 284 ILE A CG1   1 
ATOM   2185  C CG2   . ILE A 1 284 ? 12.129  36.309  36.003  1.00 64.84  ? 284 ILE A CG2   1 
ATOM   2186  C CD1   . ILE A 1 284 ? 12.256  33.393  35.246  1.00 74.80  ? 284 ILE A CD1   1 
ATOM   2187  N N     . THR A 1 285 ? 11.952  38.212  32.578  1.00 61.52  ? 285 THR A N     1 
ATOM   2188  C CA    . THR A 1 285 ? 11.336  39.528  32.479  1.00 56.99  ? 285 THR A CA    1 
ATOM   2189  C C     . THR A 1 285 ? 11.238  40.050  31.048  1.00 50.51  ? 285 THR A C     1 
ATOM   2190  O O     . THR A 1 285 ? 10.635  41.092  30.867  1.00 56.68  ? 285 THR A O     1 
ATOM   2191  C CB    . THR A 1 285 ? 12.078  40.546  33.352  1.00 59.06  ? 285 THR A CB    1 
ATOM   2192  O OG1   . THR A 1 285 ? 13.387  40.791  32.822  1.00 56.03  ? 285 THR A OG1   1 
ATOM   2193  C CG2   . THR A 1 285 ? 12.149  40.082  34.790  1.00 53.63  ? 285 THR A CG2   1 
ATOM   2194  N N     . ARG A 1 286 ? 11.807  39.354  30.051  1.00 54.78  ? 286 ARG A N     1 
ATOM   2195  C CA    . ARG A 1 286 ? 11.758  39.774  28.652  1.00 46.16  ? 286 ARG A CA    1 
ATOM   2196  C C     . ARG A 1 286 ? 11.421  38.597  27.736  1.00 46.56  ? 286 ARG A C     1 
ATOM   2197  O O     . ARG A 1 286 ? 11.425  37.432  28.146  1.00 49.99  ? 286 ARG A O     1 
ATOM   2198  C CB    . ARG A 1 286 ? 13.090  40.369  28.187  1.00 47.16  ? 286 ARG A CB    1 
ATOM   2199  C CG    . ARG A 1 286 ? 13.582  41.536  29.032  1.00 51.68  ? 286 ARG A CG    1 
ATOM   2200  C CD    . ARG A 1 286 ? 12.696  42.771  28.933  1.00 52.13  ? 286 ARG A CD    1 
ATOM   2201  N NE    . ARG A 1 286 ? 13.254  43.912  29.662  1.00 52.33  ? 286 ARG A NE    1 
ATOM   2202  C CZ    . ARG A 1 286 ? 12.921  44.262  30.907  1.00 48.30  ? 286 ARG A CZ    1 
ATOM   2203  N NH1   . ARG A 1 286 ? 12.117  43.503  31.625  1.00 45.64  ? 286 ARG A NH1   1 
ATOM   2204  N NH2   . ARG A 1 286 ? 13.424  45.354  31.451  1.00 50.81  ? 286 ARG A NH2   1 
ATOM   2205  N N     . THR A 1 287 ? 11.086  38.926  26.481  1.00 47.95  ? 287 THR A N     1 
ATOM   2206  C CA    . THR A 1 287 ? 10.943  37.932  25.433  1.00 46.06  ? 287 THR A CA    1 
ATOM   2207  C C     . THR A 1 287 ? 12.008  38.192  24.377  1.00 40.15  ? 287 THR A C     1 
ATOM   2208  O O     . THR A 1 287 ? 12.602  39.256  24.337  1.00 43.30  ? 287 THR A O     1 
ATOM   2209  C CB    . THR A 1 287 ? 9.540   37.923  24.809  1.00 49.91  ? 287 THR A CB    1 
ATOM   2210  O OG1   . THR A 1 287 ? 9.447   39.021  23.904  1.00 54.41  ? 287 THR A OG1   1 
ATOM   2211  C CG2   . THR A 1 287 ? 8.415   37.987  25.819  1.00 46.29  ? 287 THR A CG2   1 
ATOM   2212  N N     . LYS A 1 288 ? 12.189  37.219  23.491  1.00 45.02  ? 288 LYS A N     1 
ATOM   2213  C CA    . LYS A 1 288 ? 13.093  37.338  22.359  1.00 44.81  ? 288 LYS A CA    1 
ATOM   2214  C C     . LYS A 1 288 ? 12.738  38.493  21.427  1.00 41.62  ? 288 LYS A C     1 
ATOM   2215  O O     . LYS A 1 288 ? 13.659  39.126  20.937  1.00 51.65  ? 288 LYS A O     1 
ATOM   2216  C CB    . LYS A 1 288 ? 13.062  36.044  21.543  1.00 42.77  ? 288 LYS A CB    1 
ATOM   2217  C CG    . LYS A 1 288 ? 14.210  35.864  20.561  1.00 41.38  ? 288 LYS A CG    1 
ATOM   2218  C CD    . LYS A 1 288 ? 14.011  34.639  19.689  1.00 47.37  ? 288 LYS A CD    1 
ATOM   2219  C CE    . LYS A 1 288 ? 15.080  34.430  18.638  1.00 47.33  ? 288 LYS A CE    1 
ATOM   2220  N NZ    . LYS A 1 288 ? 14.635  33.420  17.649  1.00 44.97  ? 288 LYS A NZ    1 
ATOM   2221  N N     . SER A 1 289 ? 11.441  38.692  21.129  1.00 47.16  ? 289 SER A N     1 
ATOM   2222  C CA    . SER A 1 289 ? 10.929  39.655  20.151  1.00 51.04  ? 289 SER A CA    1 
ATOM   2223  C C     . SER A 1 289 ? 11.324  41.086  20.524  1.00 47.63  ? 289 SER A C     1 
ATOM   2224  O O     . SER A 1 289 ? 11.474  41.966  19.680  1.00 48.41  ? 289 SER A O     1 
ATOM   2225  C CB    . SER A 1 289 ? 9.418   39.601  20.062  1.00 53.03  ? 289 SER A CB    1 
ATOM   2226  O OG    . SER A 1 289 ? 8.901   38.427  20.655  1.00 67.88  ? 289 SER A OG    1 
ATOM   2227  N N     . GLN A 1 290 ? 11.464  41.301  21.819  1.00 42.46  ? 290 GLN A N     1 
ATOM   2228  C CA    . GLN A 1 290 ? 11.875  42.570  22.384  1.00 44.28  ? 290 GLN A CA    1 
ATOM   2229  C C     . GLN A 1 290 ? 13.368  42.832  22.168  1.00 48.81  ? 290 GLN A C     1 
ATOM   2230  O O     . GLN A 1 290 ? 13.796  43.997  22.288  1.00 45.09  ? 290 GLN A O     1 
ATOM   2231  C CB    . GLN A 1 290 ? 11.476  42.551  23.855  1.00 39.38  ? 290 GLN A CB    1 
ATOM   2232  C CG    . GLN A 1 290 ? 9.992   42.255  24.011  1.00 40.54  ? 290 GLN A CG    1 
ATOM   2233  C CD    . GLN A 1 290 ? 9.599   42.142  25.453  1.00 53.13  ? 290 GLN A CD    1 
ATOM   2234  O OE1   . GLN A 1 290 ? 10.447  42.038  26.339  1.00 57.68  ? 290 GLN A OE1   1 
ATOM   2235  N NE2   . GLN A 1 290 ? 8.300   42.184  25.693  1.00 61.71  ? 290 GLN A NE2   1 
ATOM   2236  N N     . TYR A 1 291 ? 14.156  41.794  21.799  1.00 39.93  ? 291 TYR A N     1 
ATOM   2237  C CA    . TYR A 1 291 ? 15.584  42.037  21.622  1.00 43.72  ? 291 TYR A CA    1 
ATOM   2238  C C     . TYR A 1 291 ? 16.103  41.703  20.226  1.00 43.13  ? 291 TYR A C     1 
ATOM   2239  O O     . TYR A 1 291 ? 17.180  42.190  19.919  1.00 49.12  ? 291 TYR A O     1 
ATOM   2240  C CB    . TYR A 1 291 ? 16.405  41.347  22.714  1.00 40.36  ? 291 TYR A CB    1 
ATOM   2241  C CG    . TYR A 1 291 ? 16.494  42.121  23.994  1.00 37.79  ? 291 TYR A CG    1 
ATOM   2242  C CD1   . TYR A 1 291 ? 17.320  43.228  24.120  1.00 49.84  ? 291 TYR A CD1   1 
ATOM   2243  C CD2   . TYR A 1 291 ? 15.724  41.780  25.078  1.00 46.20  ? 291 TYR A CD2   1 
ATOM   2244  C CE1   . TYR A 1 291 ? 17.407  43.955  25.305  1.00 49.66  ? 291 TYR A CE1   1 
ATOM   2245  C CE2   . TYR A 1 291 ? 15.773  42.510  26.261  1.00 48.63  ? 291 TYR A CE2   1 
ATOM   2246  C CZ    . TYR A 1 291 ? 16.617  43.594  26.383  1.00 47.13  ? 291 TYR A CZ    1 
ATOM   2247  O OH    . TYR A 1 291 ? 16.630  44.288  27.564  1.00 58.70  ? 291 TYR A OH    1 
ATOM   2248  N N     . TYR A 1 292 ? 15.377  40.910  19.414  1.00 51.95  ? 292 TYR A N     1 
ATOM   2249  C CA    . TYR A 1 292 ? 15.860  40.392  18.125  1.00 56.00  ? 292 TYR A CA    1 
ATOM   2250  C C     . TYR A 1 292 ? 14.695  39.855  17.264  1.00 56.40  ? 292 TYR A C     1 
ATOM   2251  O O     . TYR A 1 292 ? 13.813  39.166  17.757  1.00 49.82  ? 292 TYR A O     1 
ATOM   2252  C CB    . TYR A 1 292 ? 16.918  39.303  18.381  1.00 53.97  ? 292 TYR A CB    1 
ATOM   2253  C CG    . TYR A 1 292 ? 17.532  38.672  17.150  1.00 49.14  ? 292 TYR A CG    1 
ATOM   2254  C CD1   . TYR A 1 292 ? 18.266  39.413  16.230  1.00 49.44  ? 292 TYR A CD1   1 
ATOM   2255  C CD2   . TYR A 1 292 ? 17.356  37.327  16.896  1.00 49.78  ? 292 TYR A CD2   1 
ATOM   2256  C CE1   . TYR A 1 292 ? 18.811  38.834  15.095  1.00 47.49  ? 292 TYR A CE1   1 
ATOM   2257  C CE2   . TYR A 1 292 ? 17.877  36.728  15.763  1.00 50.81  ? 292 TYR A CE2   1 
ATOM   2258  C CZ    . TYR A 1 292 ? 18.619  37.478  14.874  1.00 55.77  ? 292 TYR A CZ    1 
ATOM   2259  O OH    . TYR A 1 292 ? 19.096  36.787  13.795  1.00 66.20  ? 292 TYR A OH    1 
ATOM   2260  N N     . ASP A 1 293 ? 14.678  40.128  15.951  1.00 68.49  ? 293 ASP A N     1 
ATOM   2261  C CA    . ASP A 1 293 ? 13.526  39.747  15.141  1.00 74.74  ? 293 ASP A CA    1 
ATOM   2262  C C     . ASP A 1 293 ? 13.776  38.476  14.336  1.00 68.45  ? 293 ASP A C     1 
ATOM   2263  O O     . ASP A 1 293 ? 12.812  37.931  13.821  1.00 73.83  ? 293 ASP A O     1 
ATOM   2264  C CB    . ASP A 1 293 ? 13.073  40.878  14.206  1.00 93.70  ? 293 ASP A CB    1 
ATOM   2265  C CG    . ASP A 1 293 ? 12.063  41.827  14.844  1.00 113.19 ? 293 ASP A CG    1 
ATOM   2266  O OD1   . ASP A 1 293 ? 11.346  41.382  15.769  1.00 117.95 ? 293 ASP A OD1   1 
ATOM   2267  O OD2   . ASP A 1 293 ? 12.019  43.020  14.448  1.00 104.95 ? 293 ASP A OD2   1 
ATOM   2268  N N     . GLY A 1 294 ? 15.031  38.009  14.223  1.00 66.76  ? 294 GLY A N     1 
ATOM   2269  C CA    . GLY A 1 294 ? 15.372  36.827  13.429  1.00 63.20  ? 294 GLY A CA    1 
ATOM   2270  C C     . GLY A 1 294 ? 14.759  35.526  13.962  1.00 62.20  ? 294 GLY A C     1 
ATOM   2271  O O     . GLY A 1 294 ? 14.334  35.434  15.109  1.00 58.25  ? 294 GLY A O     1 
ATOM   2272  N N     . ASP A 1 295 ? 14.698  34.497  13.113  1.00 75.72  ? 295 ASP A N     1 
ATOM   2273  C CA    . ASP A 1 295 ? 14.066  33.237  13.493  1.00 84.09  ? 295 ASP A CA    1 
ATOM   2274  C C     . ASP A 1 295 ? 15.053  32.399  14.296  1.00 80.83  ? 295 ASP A C     1 
ATOM   2275  O O     . ASP A 1 295 ? 14.626  31.510  15.047  1.00 77.87  ? 295 ASP A O     1 
ATOM   2276  C CB    . ASP A 1 295 ? 13.633  32.398  12.285  1.00 87.83  ? 295 ASP A CB    1 
ATOM   2277  C CG    . ASP A 1 295 ? 13.044  33.216  11.151  1.00 94.76  ? 295 ASP A CG    1 
ATOM   2278  O OD1   . ASP A 1 295 ? 11.889  33.662  11.313  1.00 86.10  ? 295 ASP A OD1   1 
ATOM   2279  O OD2   . ASP A 1 295 ? 13.765  33.427  10.132  1.00 86.13  ? 295 ASP A OD2   1 
ATOM   2280  N N     . GLY A 1 296 ? 16.353  32.683  14.051  1.00 72.40  ? 296 GLY A N     1 
ATOM   2281  C CA    . GLY A 1 296 ? 17.483  31.951  14.604  1.00 70.01  ? 296 GLY A CA    1 
ATOM   2282  C C     . GLY A 1 296 ? 17.783  32.353  16.043  1.00 60.74  ? 296 GLY A C     1 
ATOM   2283  O O     . GLY A 1 296 ? 17.017  33.066  16.675  1.00 53.94  ? 296 GLY A O     1 
ATOM   2284  N N     . PRO A 1 297 ? 18.925  31.927  16.608  1.00 58.94  ? 297 PRO A N     1 
ATOM   2285  C CA    . PRO A 1 297 ? 19.245  32.233  18.003  1.00 56.32  ? 297 PRO A CA    1 
ATOM   2286  C C     . PRO A 1 297 ? 19.834  33.636  18.097  1.00 50.84  ? 297 PRO A C     1 
ATOM   2287  O O     . PRO A 1 297 ? 20.312  34.152  17.095  1.00 55.41  ? 297 PRO A O     1 
ATOM   2288  C CB    . PRO A 1 297 ? 20.281  31.143  18.319  1.00 56.94  ? 297 PRO A CB    1 
ATOM   2289  C CG    . PRO A 1 297 ? 21.039  30.968  17.004  1.00 54.75  ? 297 PRO A CG    1 
ATOM   2290  C CD    . PRO A 1 297 ? 19.990  31.174  15.924  1.00 57.36  ? 297 PRO A CD    1 
ATOM   2291  N N     . ILE A 1 298 ? 19.892  34.206  19.306  1.00 53.33  ? 298 ILE A N     1 
ATOM   2292  C CA    . ILE A 1 298 ? 20.303  35.590  19.481  1.00 50.41  ? 298 ILE A CA    1 
ATOM   2293  C C     . ILE A 1 298 ? 21.799  35.748  19.211  1.00 56.06  ? 298 ILE A C     1 
ATOM   2294  O O     . ILE A 1 298 ? 22.605  34.952  19.678  1.00 58.73  ? 298 ILE A O     1 
ATOM   2295  C CB    . ILE A 1 298 ? 19.938  36.106  20.880  1.00 50.77  ? 298 ILE A CB    1 
ATOM   2296  C CG1   . ILE A 1 298 ? 20.753  35.430  21.976  1.00 47.55  ? 298 ILE A CG1   1 
ATOM   2297  C CG2   . ILE A 1 298 ? 18.442  35.972  21.128  1.00 55.25  ? 298 ILE A CG2   1 
ATOM   2298  C CD1   . ILE A 1 298 ? 20.773  36.227  23.242  1.00 49.24  ? 298 ILE A CD1   1 
ATOM   2299  N N     . PRO A 1 299 ? 22.214  36.775  18.436  1.00 59.98  ? 299 PRO A N     1 
ATOM   2300  C CA    . PRO A 1 299 ? 23.623  37.010  18.144  1.00 60.49  ? 299 PRO A CA    1 
ATOM   2301  C C     . PRO A 1 299 ? 24.339  37.650  19.322  1.00 60.21  ? 299 PRO A C     1 
ATOM   2302  O O     . PRO A 1 299 ? 23.705  38.272  20.158  1.00 55.93  ? 299 PRO A O     1 
ATOM   2303  C CB    . PRO A 1 299 ? 23.658  37.998  16.965  1.00 60.55  ? 299 PRO A CB    1 
ATOM   2304  C CG    . PRO A 1 299 ? 22.214  38.326  16.644  1.00 63.39  ? 299 PRO A CG    1 
ATOM   2305  C CD    . PRO A 1 299 ? 21.345  37.726  17.732  1.00 63.36  ? 299 PRO A CD    1 
ATOM   2306  N N     . PRO A 1 300 ? 25.673  37.488  19.431  1.00 66.89  ? 300 PRO A N     1 
ATOM   2307  C CA    . PRO A 1 300 ? 26.474  38.185  20.439  1.00 69.00  ? 300 PRO A CA    1 
ATOM   2308  C C     . PRO A 1 300 ? 26.088  39.621  20.767  1.00 61.66  ? 300 PRO A C     1 
ATOM   2309  O O     . PRO A 1 300 ? 26.015  39.998  21.934  1.00 59.60  ? 300 PRO A O     1 
ATOM   2310  C CB    . PRO A 1 300 ? 27.860  38.135  19.788  1.00 66.94  ? 300 PRO A CB    1 
ATOM   2311  C CG    . PRO A 1 300 ? 27.884  36.747  19.182  1.00 69.93  ? 300 PRO A CG    1 
ATOM   2312  C CD    . PRO A 1 300 ? 26.472  36.520  18.669  1.00 68.46  ? 300 PRO A CD    1 
ATOM   2313  N N     . SER A 1 301 ? 25.830  40.412  19.734  1.00 57.54  ? 301 SER A N     1 
ATOM   2314  C CA    . SER A 1 301 ? 25.647  41.837  19.930  1.00 59.64  ? 301 SER A CA    1 
ATOM   2315  C C     . SER A 1 301 ? 24.401  42.107  20.777  1.00 54.55  ? 301 SER A C     1 
ATOM   2316  O O     . SER A 1 301 ? 24.371  43.056  21.555  1.00 60.94  ? 301 SER A O     1 
ATOM   2317  C CB    . SER A 1 301 ? 25.582  42.521  18.601  1.00 61.82  ? 301 SER A CB    1 
ATOM   2318  O OG    . SER A 1 301 ? 24.518  41.992  17.827  1.00 73.09  ? 301 SER A OG    1 
ATOM   2319  N N     . VAL A 1 302 ? 23.373  41.271  20.595  1.00 48.31  ? 302 VAL A N     1 
ATOM   2320  C CA    . VAL A 1 302 ? 22.129  41.343  21.347  1.00 51.72  ? 302 VAL A CA    1 
ATOM   2321  C C     . VAL A 1 302 ? 22.309  40.846  22.784  1.00 56.52  ? 302 VAL A C     1 
ATOM   2322  O O     . VAL A 1 302 ? 21.629  41.332  23.677  1.00 62.56  ? 302 VAL A O     1 
ATOM   2323  C CB    . VAL A 1 302 ? 21.039  40.532  20.634  1.00 54.55  ? 302 VAL A CB    1 
ATOM   2324  C CG1   . VAL A 1 302 ? 19.779  40.378  21.465  1.00 51.44  ? 302 VAL A CG1   1 
ATOM   2325  C CG2   . VAL A 1 302 ? 20.741  41.127  19.272  1.00 60.16  ? 302 VAL A CG2   1 
ATOM   2326  N N     . ALA A 1 303 ? 23.177  39.852  23.019  1.00 56.29  ? 303 ALA A N     1 
ATOM   2327  C CA    . ALA A 1 303 ? 23.463  39.443  24.389  1.00 55.64  ? 303 ALA A CA    1 
ATOM   2328  C C     . ALA A 1 303 ? 24.034  40.620  25.175  1.00 49.77  ? 303 ALA A C     1 
ATOM   2329  O O     . ALA A 1 303 ? 23.508  40.928  26.241  1.00 50.30  ? 303 ALA A O     1 
ATOM   2330  C CB    . ALA A 1 303 ? 24.400  38.262  24.421  1.00 55.92  ? 303 ALA A CB    1 
ATOM   2331  N N     . LYS A 1 304 ? 25.086  41.264  24.635  1.00 44.88  ? 304 LYS A N     1 
ATOM   2332  C CA    . LYS A 1 304 ? 25.724  42.405  25.279  1.00 55.63  ? 304 LYS A CA    1 
ATOM   2333  C C     . LYS A 1 304 ? 24.702  43.457  25.687  1.00 51.22  ? 304 LYS A C     1 
ATOM   2334  O O     . LYS A 1 304 ? 24.858  44.113  26.702  1.00 55.15  ? 304 LYS A O     1 
ATOM   2335  C CB    . LYS A 1 304 ? 26.781  43.052  24.377  1.00 68.26  ? 304 LYS A CB    1 
ATOM   2336  C CG    . LYS A 1 304 ? 28.203  42.764  24.836  1.00 90.88  ? 304 LYS A CG    1 
ATOM   2337  C CD    . LYS A 1 304 ? 29.288  42.966  23.801  1.00 101.59 ? 304 LYS A CD    1 
ATOM   2338  C CE    . LYS A 1 304 ? 30.657  42.603  24.347  1.00 100.06 ? 304 LYS A CE    1 
ATOM   2339  N NZ    . LYS A 1 304 ? 31.608  42.267  23.263  1.00 96.15  ? 304 LYS A NZ    1 
ATOM   2340  N N     . THR A 1 305 ? 23.665  43.604  24.871  1.00 60.35  ? 305 THR A N     1 
ATOM   2341  C CA    . THR A 1 305 ? 22.622  44.592  25.065  1.00 55.52  ? 305 THR A CA    1 
ATOM   2342  C C     . THR A 1 305 ? 21.664  44.151  26.163  1.00 53.05  ? 305 THR A C     1 
ATOM   2343  O O     . THR A 1 305 ? 21.202  44.972  26.955  1.00 56.08  ? 305 THR A O     1 
ATOM   2344  C CB    . THR A 1 305 ? 21.939  44.804  23.717  1.00 56.77  ? 305 THR A CB    1 
ATOM   2345  O OG1   . THR A 1 305 ? 22.859  45.607  22.968  1.00 54.44  ? 305 THR A OG1   1 
ATOM   2346  C CG2   . THR A 1 305 ? 20.568  45.425  23.830  1.00 59.40  ? 305 THR A CG2   1 
ATOM   2347  N N     . MET A 1 306 ? 21.377  42.844  26.215  1.00 48.90  ? 306 MET A N     1 
ATOM   2348  C CA    . MET A 1 306 ? 20.521  42.304  27.254  1.00 44.83  ? 306 MET A CA    1 
ATOM   2349  C C     . MET A 1 306 ? 21.211  42.426  28.616  1.00 45.80  ? 306 MET A C     1 
ATOM   2350  O O     . MET A 1 306 ? 20.560  42.755  29.597  1.00 45.77  ? 306 MET A O     1 
ATOM   2351  C CB    . MET A 1 306 ? 20.185  40.849  26.937  1.00 50.69  ? 306 MET A CB    1 
ATOM   2352  C CG    . MET A 1 306 ? 19.204  40.714  25.780  1.00 50.71  ? 306 MET A CG    1 
ATOM   2353  S SD    . MET A 1 306 ? 19.016  39.005  25.231  1.00 48.65  ? 306 MET A SD    1 
ATOM   2354  C CE    . MET A 1 306 ? 17.860  38.438  26.468  1.00 53.81  ? 306 MET A CE    1 
ATOM   2355  N N     . MET A 1 307 ? 22.538  42.231  28.635  1.00 47.16  ? 307 MET A N     1 
ATOM   2356  C CA    . MET A 1 307 ? 23.374  42.251  29.829  1.00 44.86  ? 307 MET A CA    1 
ATOM   2357  C C     . MET A 1 307 ? 23.436  43.654  30.413  1.00 49.08  ? 307 MET A C     1 
ATOM   2358  O O     . MET A 1 307 ? 23.180  43.809  31.604  1.00 46.60  ? 307 MET A O     1 
ATOM   2359  C CB    . MET A 1 307 ? 24.802  41.796  29.500  1.00 51.33  ? 307 MET A CB    1 
ATOM   2360  C CG    . MET A 1 307 ? 24.971  40.263  29.533  1.00 53.18  ? 307 MET A CG    1 
ATOM   2361  S SD    . MET A 1 307 ? 26.366  39.715  28.524  1.00 53.30  ? 307 MET A SD    1 
ATOM   2362  C CE    . MET A 1 307 ? 27.684  40.521  29.439  1.00 48.87  ? 307 MET A CE    1 
ATOM   2363  N N     . ALA A 1 308 ? 23.748  44.666  29.573  1.00 57.01  ? 308 ALA A N     1 
ATOM   2364  C CA    . ALA A 1 308 ? 23.745  46.072  29.991  1.00 50.61  ? 308 ALA A CA    1 
ATOM   2365  C C     . ALA A 1 308 ? 22.367  46.489  30.498  1.00 52.55  ? 308 ALA A C     1 
ATOM   2366  O O     . ALA A 1 308 ? 22.236  46.995  31.613  1.00 48.96  ? 308 ALA A O     1 
ATOM   2367  C CB    . ALA A 1 308 ? 24.188  46.960  28.872  1.00 51.82  ? 308 ALA A CB    1 
ATOM   2368  N N     . ASP A 1 309 ? 21.338  46.217  29.685  1.00 49.56  ? 309 ASP A N     1 
ATOM   2369  C CA    . ASP A 1 309 ? 19.989  46.614  30.033  1.00 49.65  ? 309 ASP A CA    1 
ATOM   2370  C C     . ASP A 1 309 ? 19.572  46.053  31.381  1.00 47.97  ? 309 ASP A C     1 
ATOM   2371  O O     . ASP A 1 309 ? 18.918  46.773  32.133  1.00 54.22  ? 309 ASP A O     1 
ATOM   2372  C CB    . ASP A 1 309 ? 18.939  46.126  29.029  1.00 52.48  ? 309 ASP A CB    1 
ATOM   2373  C CG    . ASP A 1 309 ? 18.813  46.923  27.742  1.00 56.09  ? 309 ASP A CG    1 
ATOM   2374  O OD1   . ASP A 1 309 ? 19.700  47.770  27.456  1.00 52.24  ? 309 ASP A OD1   1 
ATOM   2375  O OD2   . ASP A 1 309 ? 17.826  46.677  27.035  1.00 58.56  ? 309 ASP A OD2   1 
ATOM   2376  N N     . LEU A 1 310 ? 19.837  44.752  31.622  1.00 48.12  ? 310 LEU A N     1 
ATOM   2377  C CA    . LEU A 1 310 ? 19.185  44.025  32.711  1.00 47.55  ? 310 LEU A CA    1 
ATOM   2378  C C     . LEU A 1 310 ? 20.115  43.805  33.907  1.00 42.90  ? 310 LEU A C     1 
ATOM   2379  O O     . LEU A 1 310 ? 19.675  43.310  34.941  1.00 44.82  ? 310 LEU A O     1 
ATOM   2380  C CB    . LEU A 1 310 ? 18.686  42.673  32.186  1.00 53.52  ? 310 LEU A CB    1 
ATOM   2381  C CG    . LEU A 1 310 ? 17.655  42.735  31.065  1.00 52.09  ? 310 LEU A CG    1 
ATOM   2382  C CD1   . LEU A 1 310 ? 17.470  41.359  30.438  1.00 51.81  ? 310 LEU A CD1   1 
ATOM   2383  C CD2   . LEU A 1 310 ? 16.331  43.266  31.597  1.00 53.61  ? 310 LEU A CD2   1 
ATOM   2384  N N     . ASP A 1 311 ? 21.396  44.176  33.782  1.00 48.48  ? 311 ASP A N     1 
ATOM   2385  C CA    . ASP A 1 311 ? 22.376  43.969  34.842  1.00 49.02  ? 311 ASP A CA    1 
ATOM   2386  C C     . ASP A 1 311 ? 22.452  42.471  35.166  1.00 50.51  ? 311 ASP A C     1 
ATOM   2387  O O     . ASP A 1 311 ? 22.451  42.076  36.334  1.00 49.75  ? 311 ASP A O     1 
ATOM   2388  C CB    . ASP A 1 311 ? 22.055  44.829  36.083  1.00 54.49  ? 311 ASP A CB    1 
ATOM   2389  C CG    . ASP A 1 311 ? 22.165  46.347  35.932  1.00 54.95  ? 311 ASP A CG    1 
ATOM   2390  O OD1   . ASP A 1 311 ? 22.681  46.818  34.879  1.00 50.75  ? 311 ASP A OD1   1 
ATOM   2391  O OD2   . ASP A 1 311 ? 21.710  47.059  36.877  1.00 50.67  ? 311 ASP A OD2   1 
ATOM   2392  N N     . LEU A 1 312 ? 22.434  41.644  34.111  1.00 48.95  ? 312 LEU A N     1 
ATOM   2393  C CA    . LEU A 1 312 ? 22.758  40.231  34.188  1.00 47.26  ? 312 LEU A CA    1 
ATOM   2394  C C     . LEU A 1 312 ? 24.120  40.004  33.532  1.00 49.51  ? 312 LEU A C     1 
ATOM   2395  O O     . LEU A 1 312 ? 24.671  40.881  32.867  1.00 44.75  ? 312 LEU A O     1 
ATOM   2396  C CB    . LEU A 1 312 ? 21.699  39.411  33.455  1.00 47.49  ? 312 LEU A CB    1 
ATOM   2397  C CG    . LEU A 1 312 ? 20.286  39.480  34.023  1.00 50.84  ? 312 LEU A CG    1 
ATOM   2398  C CD1   . LEU A 1 312 ? 19.329  38.733  33.124  1.00 49.97  ? 312 LEU A CD1   1 
ATOM   2399  C CD2   . LEU A 1 312 ? 20.229  38.925  35.433  1.00 50.37  ? 312 LEU A CD2   1 
ATOM   2400  N N     . GLY A 1 313 ? 24.658  38.808  33.759  1.00 46.89  ? 313 GLY A N     1 
ATOM   2401  C CA    . GLY A 1 313 ? 25.889  38.365  33.136  1.00 48.32  ? 313 GLY A CA    1 
ATOM   2402  C C     . GLY A 1 313 ? 25.578  37.290  32.107  1.00 41.34  ? 313 GLY A C     1 
ATOM   2403  O O     . GLY A 1 313 ? 24.425  36.879  31.990  1.00 44.34  ? 313 GLY A O     1 
ATOM   2404  N N     . MET A 1 314 ? 26.611  36.870  31.372  1.00 40.16  ? 314 MET A N     1 
ATOM   2405  C CA    . MET A 1 314 ? 26.574  35.624  30.610  1.00 44.26  ? 314 MET A CA    1 
ATOM   2406  C C     . MET A 1 314 ? 26.207  34.454  31.526  1.00 40.01  ? 314 MET A C     1 
ATOM   2407  O O     . MET A 1 314 ? 25.422  33.629  31.094  1.00 34.28  ? 314 MET A O     1 
ATOM   2408  C CB    . MET A 1 314 ? 27.917  35.355  29.919  1.00 44.04  ? 314 MET A CB    1 
ATOM   2409  C CG    . MET A 1 314 ? 28.131  36.252  28.712  1.00 49.77  ? 314 MET A CG    1 
ATOM   2410  S SD    . MET A 1 314 ? 26.845  36.032  27.420  1.00 61.59  ? 314 MET A SD    1 
ATOM   2411  C CE    . MET A 1 314 ? 26.976  34.291  26.998  1.00 69.13  ? 314 MET A CE    1 
ATOM   2412  N N     . TRP A 1 315 ? 26.791  34.409  32.757  1.00 45.79  ? 315 TRP A N     1 
ATOM   2413  C CA    . TRP A 1 315 ? 26.416  33.505  33.851  1.00 45.01  ? 315 TRP A CA    1 
ATOM   2414  C C     . TRP A 1 315 ? 25.952  34.308  35.072  1.00 46.52  ? 315 TRP A C     1 
ATOM   2415  O O     . TRP A 1 315 ? 26.468  35.392  35.362  1.00 53.37  ? 315 TRP A O     1 
ATOM   2416  C CB    . TRP A 1 315 ? 27.579  32.563  34.231  1.00 44.21  ? 315 TRP A CB    1 
ATOM   2417  C CG    . TRP A 1 315 ? 27.946  31.667  33.103  1.00 35.80  ? 315 TRP A CG    1 
ATOM   2418  C CD1   . TRP A 1 315 ? 29.012  31.781  32.259  1.00 31.55  ? 315 TRP A CD1   1 
ATOM   2419  C CD2   . TRP A 1 315 ? 27.156  30.577  32.626  1.00 34.10  ? 315 TRP A CD2   1 
ATOM   2420  N NE1   . TRP A 1 315 ? 28.934  30.828  31.285  1.00 33.47  ? 315 TRP A NE1   1 
ATOM   2421  C CE2   . TRP A 1 315 ? 27.825  30.054  31.504  1.00 36.70  ? 315 TRP A CE2   1 
ATOM   2422  C CE3   . TRP A 1 315 ? 25.967  29.985  33.047  1.00 35.56  ? 315 TRP A CE3   1 
ATOM   2423  C CZ2   . TRP A 1 315 ? 27.323  28.970  30.792  1.00 37.26  ? 315 TRP A CZ2   1 
ATOM   2424  C CZ3   . TRP A 1 315 ? 25.465  28.916  32.343  1.00 34.36  ? 315 TRP A CZ3   1 
ATOM   2425  C CH2   . TRP A 1 315 ? 26.131  28.425  31.219  1.00 37.87  ? 315 TRP A CH2   1 
ATOM   2426  N N     . ASN A 1 316 ? 25.017  33.708  35.814  1.00 47.13  ? 316 ASN A N     1 
ATOM   2427  C CA    . ASN A 1 316 ? 24.223  34.383  36.830  1.00 44.75  ? 316 ASN A CA    1 
ATOM   2428  C C     . ASN A 1 316 ? 23.988  33.447  38.006  1.00 38.55  ? 316 ASN A C     1 
ATOM   2429  O O     . ASN A 1 316 ? 23.113  32.601  37.940  1.00 45.67  ? 316 ASN A O     1 
ATOM   2430  C CB    . ASN A 1 316 ? 22.888  34.828  36.231  1.00 44.78  ? 316 ASN A CB    1 
ATOM   2431  C CG    . ASN A 1 316 ? 23.094  35.895  35.178  1.00 46.54  ? 316 ASN A CG    1 
ATOM   2432  O OD1   . ASN A 1 316 ? 23.536  36.984  35.506  1.00 46.67  ? 316 ASN A OD1   1 
ATOM   2433  N ND2   . ASN A 1 316 ? 22.844  35.593  33.915  1.00 48.76  ? 316 ASN A ND2   1 
ATOM   2434  N N     . PHE A 1 317 ? 24.752  33.638  39.079  1.00 39.89  ? 317 PHE A N     1 
ATOM   2435  C CA    . PHE A 1 317 ? 24.654  32.813  40.262  1.00 42.80  ? 317 PHE A CA    1 
ATOM   2436  C C     . PHE A 1 317 ? 23.751  33.449  41.310  1.00 47.47  ? 317 PHE A C     1 
ATOM   2437  O O     . PHE A 1 317 ? 24.171  34.385  42.010  1.00 45.20  ? 317 PHE A O     1 
ATOM   2438  C CB    . PHE A 1 317 ? 26.060  32.596  40.830  1.00 50.99  ? 317 PHE A CB    1 
ATOM   2439  C CG    . PHE A 1 317 ? 26.151  31.870  42.154  1.00 45.26  ? 317 PHE A CG    1 
ATOM   2440  C CD1   . PHE A 1 317 ? 25.158  30.992  42.577  1.00 50.03  ? 317 PHE A CD1   1 
ATOM   2441  C CD2   . PHE A 1 317 ? 27.232  32.095  43.000  1.00 44.74  ? 317 PHE A CD2   1 
ATOM   2442  C CE1   . PHE A 1 317 ? 25.237  30.372  43.820  1.00 45.96  ? 317 PHE A CE1   1 
ATOM   2443  C CE2   . PHE A 1 317 ? 27.308  31.485  44.243  1.00 42.44  ? 317 PHE A CE2   1 
ATOM   2444  C CZ    . PHE A 1 317 ? 26.306  30.627  44.650  1.00 41.41  ? 317 PHE A CZ    1 
ATOM   2445  N N     . CYS A 1 318 ? 22.555  32.849  41.440  1.00 52.73  ? 318 CYS A N     1 
ATOM   2446  C CA    . CYS A 1 318 ? 21.609  33.073  42.535  1.00 57.82  ? 318 CYS A CA    1 
ATOM   2447  C C     . CYS A 1 318 ? 21.796  32.088  43.683  1.00 55.22  ? 318 CYS A C     1 
ATOM   2448  O O     . CYS A 1 318 ? 21.857  30.875  43.472  1.00 58.11  ? 318 CYS A O     1 
ATOM   2449  C CB    . CYS A 1 318 ? 20.160  32.875  42.105  1.00 55.86  ? 318 CYS A CB    1 
ATOM   2450  S SG    . CYS A 1 318 ? 19.469  34.408  41.459  1.00 63.51  ? 318 CYS A SG    1 
ATOM   2451  N N     . GLY A 1 319 ? 21.795  32.628  44.904  1.00 55.50  ? 319 GLY A N     1 
ATOM   2452  C CA    . GLY A 1 319 ? 21.996  31.834  46.103  1.00 57.78  ? 319 GLY A CA    1 
ATOM   2453  C C     . GLY A 1 319 ? 21.377  32.531  47.302  1.00 53.22  ? 319 GLY A C     1 
ATOM   2454  O O     . GLY A 1 319 ? 20.959  33.684  47.188  1.00 41.93  ? 319 GLY A O     1 
ATOM   2455  N N     . ALA A 1 320 ? 21.331  31.833  48.446  1.00 49.53  ? 320 ALA A N     1 
ATOM   2456  C CA    . ALA A 1 320 ? 20.820  32.498  49.635  1.00 49.42  ? 320 ALA A CA    1 
ATOM   2457  C C     . ALA A 1 320 ? 21.532  32.023  50.896  1.00 42.32  ? 320 ALA A C     1 
ATOM   2458  O O     . ALA A 1 320 ? 21.853  30.840  51.036  1.00 45.76  ? 320 ALA A O     1 
ATOM   2459  C CB    . ALA A 1 320 ? 19.310  32.325  49.721  1.00 48.69  ? 320 ALA A CB    1 
ATOM   2460  N N     . LEU A 1 321 ? 21.734  32.991  51.795  1.00 41.68  ? 321 LEU A N     1 
ATOM   2461  C CA    . LEU A 1 321 ? 22.244  32.818  53.156  1.00 46.08  ? 321 LEU A CA    1 
ATOM   2462  C C     . LEU A 1 321 ? 21.070  32.713  54.126  1.00 47.89  ? 321 LEU A C     1 
ATOM   2463  O O     . LEU A 1 321 ? 20.066  33.397  53.957  1.00 57.80  ? 321 LEU A O     1 
ATOM   2464  C CB    . LEU A 1 321 ? 23.105  34.045  53.487  1.00 44.86  ? 321 LEU A CB    1 
ATOM   2465  C CG    . LEU A 1 321 ? 24.173  34.374  52.439  1.00 45.62  ? 321 LEU A CG    1 
ATOM   2466  C CD1   . LEU A 1 321 ? 24.890  35.696  52.711  1.00 45.12  ? 321 LEU A CD1   1 
ATOM   2467  C CD2   . LEU A 1 321 ? 25.173  33.238  52.368  1.00 47.32  ? 321 LEU A CD2   1 
ATOM   2468  N N     . TYR A 1 322 ? 21.207  31.856  55.136  1.00 49.65  ? 322 TYR A N     1 
ATOM   2469  C CA    . TYR A 1 322 ? 20.148  31.545  56.085  1.00 46.14  ? 322 TYR A CA    1 
ATOM   2470  C C     . TYR A 1 322 ? 20.732  31.542  57.494  1.00 57.00  ? 322 TYR A C     1 
ATOM   2471  O O     . TYR A 1 322 ? 21.953  31.468  57.653  1.00 55.38  ? 322 TYR A O     1 
ATOM   2472  C CB    . TYR A 1 322 ? 19.552  30.165  55.801  1.00 48.04  ? 322 TYR A CB    1 
ATOM   2473  C CG    . TYR A 1 322 ? 18.988  29.994  54.411  1.00 48.92  ? 322 TYR A CG    1 
ATOM   2474  C CD1   . TYR A 1 322 ? 19.818  29.719  53.332  1.00 50.76  ? 322 TYR A CD1   1 
ATOM   2475  C CD2   . TYR A 1 322 ? 17.631  30.125  54.164  1.00 43.85  ? 322 TYR A CD2   1 
ATOM   2476  C CE1   . TYR A 1 322 ? 19.317  29.562  52.048  1.00 49.16  ? 322 TYR A CE1   1 
ATOM   2477  C CE2   . TYR A 1 322 ? 17.108  29.964  52.894  1.00 40.96  ? 322 TYR A CE2   1 
ATOM   2478  C CZ    . TYR A 1 322 ? 17.957  29.695  51.829  1.00 49.61  ? 322 TYR A CZ    1 
ATOM   2479  O OH    . TYR A 1 322 ? 17.482  29.545  50.548  1.00 49.38  ? 322 TYR A OH    1 
ATOM   2480  N N     . GLY A 1 323 ? 19.855  31.636  58.506  1.00 61.51  ? 323 GLY A N     1 
ATOM   2481  C CA    . GLY A 1 323 ? 20.257  31.647  59.905  1.00 63.70  ? 323 GLY A CA    1 
ATOM   2482  C C     . GLY A 1 323 ? 20.596  33.050  60.416  1.00 66.86  ? 323 GLY A C     1 
ATOM   2483  O O     . GLY A 1 323 ? 20.269  34.046  59.781  1.00 63.75  ? 323 GLY A O     1 
ATOM   2484  N N     . PRO A 1 324 ? 21.250  33.171  61.595  1.00 67.71  ? 324 PRO A N     1 
ATOM   2485  C CA    . PRO A 1 324 ? 21.485  34.475  62.219  1.00 58.72  ? 324 PRO A CA    1 
ATOM   2486  C C     . PRO A 1 324 ? 22.522  35.337  61.501  1.00 61.60  ? 324 PRO A C     1 
ATOM   2487  O O     . PRO A 1 324 ? 23.389  34.782  60.819  1.00 61.53  ? 324 PRO A O     1 
ATOM   2488  C CB    . PRO A 1 324 ? 21.980  34.114  63.626  1.00 61.80  ? 324 PRO A CB    1 
ATOM   2489  C CG    . PRO A 1 324 ? 21.591  32.652  63.814  1.00 69.35  ? 324 PRO A CG    1 
ATOM   2490  C CD    . PRO A 1 324 ? 21.707  32.048  62.432  1.00 68.30  ? 324 PRO A CD    1 
ATOM   2491  N N     . PRO A 1 325 ? 22.425  36.700  61.606  1.00 56.23  ? 325 PRO A N     1 
ATOM   2492  C CA    . PRO A 1 325 ? 23.316  37.638  60.919  1.00 53.79  ? 325 PRO A CA    1 
ATOM   2493  C C     . PRO A 1 325 ? 24.814  37.442  61.066  1.00 61.14  ? 325 PRO A C     1 
ATOM   2494  O O     . PRO A 1 325 ? 25.534  37.612  60.091  1.00 73.89  ? 325 PRO A O     1 
ATOM   2495  C CB    . PRO A 1 325 ? 22.926  39.019  61.479  1.00 54.60  ? 325 PRO A CB    1 
ATOM   2496  C CG    . PRO A 1 325 ? 21.439  38.860  61.759  1.00 55.17  ? 325 PRO A CG    1 
ATOM   2497  C CD    . PRO A 1 325 ? 21.315  37.429  62.254  1.00 57.94  ? 325 PRO A CD    1 
ATOM   2498  N N     . PRO A 1 326 ? 25.353  37.164  62.269  1.00 71.12  ? 326 PRO A N     1 
ATOM   2499  C CA    . PRO A 1 326 ? 26.789  36.891  62.394  1.00 68.76  ? 326 PRO A CA    1 
ATOM   2500  C C     . PRO A 1 326 ? 27.240  35.657  61.603  1.00 73.19  ? 326 PRO A C     1 
ATOM   2501  O O     . PRO A 1 326 ? 28.389  35.626  61.135  1.00 58.85  ? 326 PRO A O     1 
ATOM   2502  C CB    . PRO A 1 326 ? 26.999  36.688  63.904  1.00 69.30  ? 326 PRO A CB    1 
ATOM   2503  C CG    . PRO A 1 326 ? 25.788  37.354  64.549  1.00 72.47  ? 326 PRO A CG    1 
ATOM   2504  C CD    . PRO A 1 326 ? 24.651  37.176  63.563  1.00 70.62  ? 326 PRO A CD    1 
ATOM   2505  N N     . VAL A 1 327 ? 26.335  34.654  61.473  1.00 58.14  ? 327 VAL A N     1 
ATOM   2506  C CA    . VAL A 1 327 ? 26.576  33.481  60.642  1.00 56.71  ? 327 VAL A CA    1 
ATOM   2507  C C     . VAL A 1 327 ? 26.517  33.892  59.165  1.00 58.86  ? 327 VAL A C     1 
ATOM   2508  O O     . VAL A 1 327 ? 27.472  33.675  58.420  1.00 61.49  ? 327 VAL A O     1 
ATOM   2509  C CB    . VAL A 1 327 ? 25.574  32.353  60.956  1.00 56.02  ? 327 VAL A CB    1 
ATOM   2510  C CG1   . VAL A 1 327 ? 25.749  31.146  60.056  1.00 59.94  ? 327 VAL A CG1   1 
ATOM   2511  C CG2   . VAL A 1 327 ? 25.666  31.907  62.395  1.00 58.26  ? 327 VAL A CG2   1 
ATOM   2512  N N     . MET A 1 328 ? 25.403  34.508  58.747  1.00 53.66  ? 328 MET A N     1 
ATOM   2513  C CA    . MET A 1 328 ? 25.257  34.977  57.374  1.00 53.31  ? 328 MET A CA    1 
ATOM   2514  C C     . MET A 1 328 ? 26.444  35.860  56.963  1.00 50.58  ? 328 MET A C     1 
ATOM   2515  O O     . MET A 1 328 ? 26.910  35.757  55.830  1.00 45.30  ? 328 MET A O     1 
ATOM   2516  C CB    . MET A 1 328 ? 23.934  35.733  57.167  1.00 50.54  ? 328 MET A CB    1 
ATOM   2517  C CG    . MET A 1 328 ? 22.688  34.841  57.206  1.00 51.45  ? 328 MET A CG    1 
ATOM   2518  S SD    . MET A 1 328 ? 21.101  35.617  56.656  1.00 61.07  ? 328 MET A SD    1 
ATOM   2519  C CE    . MET A 1 328 ? 21.126  37.120  57.635  1.00 57.36  ? 328 MET A CE    1 
ATOM   2520  N N     . ASP A 1 329 ? 26.988  36.690  57.867  1.00 58.86  ? 329 ASP A N     1 
ATOM   2521  C CA    . ASP A 1 329 ? 28.122  37.554  57.516  1.00 67.35  ? 329 ASP A CA    1 
ATOM   2522  C C     . ASP A 1 329 ? 29.384  36.747  57.211  1.00 59.15  ? 329 ASP A C     1 
ATOM   2523  O O     . ASP A 1 329 ? 30.148  37.094  56.321  1.00 66.42  ? 329 ASP A O     1 
ATOM   2524  C CB    . ASP A 1 329 ? 28.491  38.573  58.602  1.00 66.73  ? 329 ASP A CB    1 
ATOM   2525  C CG    . ASP A 1 329 ? 27.414  39.607  58.899  1.00 71.58  ? 329 ASP A CG    1 
ATOM   2526  O OD1   . ASP A 1 329 ? 26.411  39.659  58.154  1.00 74.25  ? 329 ASP A OD1   1 
ATOM   2527  O OD2   . ASP A 1 329 ? 27.576  40.333  59.892  1.00 67.84  ? 329 ASP A OD2   1 
ATOM   2528  N N     . THR A 1 330 ? 29.601  35.671  57.961  1.00 62.10  ? 330 THR A N     1 
ATOM   2529  C CA    . THR A 1 330 ? 30.792  34.853  57.814  1.00 59.97  ? 330 THR A CA    1 
ATOM   2530  C C     . THR A 1 330 ? 30.728  34.001  56.547  1.00 56.32  ? 330 THR A C     1 
ATOM   2531  O O     . THR A 1 330 ? 31.747  33.819  55.901  1.00 51.37  ? 330 THR A O     1 
ATOM   2532  C CB    . THR A 1 330 ? 30.994  33.988  59.062  1.00 61.04  ? 330 THR A CB    1 
ATOM   2533  O OG1   . THR A 1 330 ? 31.372  34.903  60.094  1.00 63.25  ? 330 THR A OG1   1 
ATOM   2534  C CG2   . THR A 1 330 ? 32.043  32.911  58.877  1.00 66.43  ? 330 THR A CG2   1 
ATOM   2535  N N     . LEU A 1 331 ? 29.556  33.428  56.233  1.00 50.83  ? 331 LEU A N     1 
ATOM   2536  C CA    . LEU A 1 331 ? 29.379  32.700  54.989  1.00 48.02  ? 331 LEU A CA    1 
ATOM   2537  C C     . LEU A 1 331 ? 29.579  33.669  53.801  1.00 45.73  ? 331 LEU A C     1 
ATOM   2538  O O     . LEU A 1 331 ? 30.395  33.435  52.904  1.00 43.54  ? 331 LEU A O     1 
ATOM   2539  C CB    . LEU A 1 331 ? 27.986  32.047  55.002  1.00 53.27  ? 331 LEU A CB    1 
ATOM   2540  C CG    . LEU A 1 331 ? 27.649  31.096  56.160  1.00 53.93  ? 331 LEU A CG    1 
ATOM   2541  C CD1   . LEU A 1 331 ? 26.390  30.286  55.873  1.00 53.23  ? 331 LEU A CD1   1 
ATOM   2542  C CD2   . LEU A 1 331 ? 28.782  30.127  56.489  1.00 49.13  ? 331 LEU A CD2   1 
ATOM   2543  N N     . TRP A 1 332 ? 28.866  34.806  53.789  1.00 47.14  ? 332 TRP A N     1 
ATOM   2544  C CA    . TRP A 1 332 ? 29.071  35.810  52.751  1.00 45.18  ? 332 TRP A CA    1 
ATOM   2545  C C     . TRP A 1 332 ? 30.557  36.104  52.529  1.00 48.75  ? 332 TRP A C     1 
ATOM   2546  O O     . TRP A 1 332 ? 31.020  36.141  51.383  1.00 47.96  ? 332 TRP A O     1 
ATOM   2547  C CB    . TRP A 1 332 ? 28.315  37.104  53.031  1.00 43.42  ? 332 TRP A CB    1 
ATOM   2548  C CG    . TRP A 1 332 ? 28.465  38.093  51.917  1.00 51.02  ? 332 TRP A CG    1 
ATOM   2549  C CD1   . TRP A 1 332 ? 28.969  39.360  51.981  1.00 56.97  ? 332 TRP A CD1   1 
ATOM   2550  C CD2   . TRP A 1 332 ? 28.148  37.860  50.533  1.00 53.95  ? 332 TRP A CD2   1 
ATOM   2551  N NE1   . TRP A 1 332 ? 28.961  39.942  50.740  1.00 60.73  ? 332 TRP A NE1   1 
ATOM   2552  C CE2   . TRP A 1 332 ? 28.471  39.042  49.833  1.00 52.88  ? 332 TRP A CE2   1 
ATOM   2553  C CE3   . TRP A 1 332 ? 27.605  36.778  49.827  1.00 50.74  ? 332 TRP A CE3   1 
ATOM   2554  C CZ2   . TRP A 1 332 ? 28.276  39.159  48.460  1.00 50.46  ? 332 TRP A CZ2   1 
ATOM   2555  C CZ3   . TRP A 1 332 ? 27.410  36.899  48.470  1.00 48.28  ? 332 TRP A CZ3   1 
ATOM   2556  C CH2   . TRP A 1 332 ? 27.742  38.076  47.802  1.00 47.64  ? 332 TRP A CH2   1 
ATOM   2557  N N     . THR A 1 333 ? 31.315  36.311  53.610  1.00 52.78  ? 333 THR A N     1 
ATOM   2558  C CA    . THR A 1 333 ? 32.715  36.687  53.463  1.00 52.07  ? 333 THR A CA    1 
ATOM   2559  C C     . THR A 1 333 ? 33.426  35.631  52.630  1.00 52.80  ? 333 THR A C     1 
ATOM   2560  O O     . THR A 1 333 ? 34.087  35.975  51.647  1.00 54.58  ? 333 THR A O     1 
ATOM   2561  C CB    . THR A 1 333 ? 33.359  36.931  54.827  1.00 56.19  ? 333 THR A CB    1 
ATOM   2562  O OG1   . THR A 1 333 ? 32.732  38.123  55.303  1.00 62.04  ? 333 THR A OG1   1 
ATOM   2563  C CG2   . THR A 1 333 ? 34.863  37.091  54.766  1.00 51.50  ? 333 THR A CG2   1 
ATOM   2564  N N     . ALA A 1 334 ? 33.198  34.354  52.995  1.00 47.90  ? 334 ALA A N     1 
ATOM   2565  C CA    . ALA A 1 334 ? 33.798  33.211  52.317  1.00 45.99  ? 334 ALA A CA    1 
ATOM   2566  C C     . ALA A 1 334 ? 33.338  33.080  50.856  1.00 45.75  ? 334 ALA A C     1 
ATOM   2567  O O     . ALA A 1 334 ? 34.162  32.908  49.950  1.00 39.80  ? 334 ALA A O     1 
ATOM   2568  C CB    . ALA A 1 334 ? 33.467  31.969  53.105  1.00 45.96  ? 334 ALA A CB    1 
ATOM   2569  N N     . ILE A 1 335 ? 32.013  33.130  50.629  1.00 41.45  ? 335 ILE A N     1 
ATOM   2570  C CA    . ILE A 1 335 ? 31.480  33.039  49.276  1.00 46.60  ? 335 ILE A CA    1 
ATOM   2571  C C     . ILE A 1 335 ? 32.000  34.183  48.405  1.00 44.33  ? 335 ILE A C     1 
ATOM   2572  O O     . ILE A 1 335 ? 32.537  33.928  47.337  1.00 46.87  ? 335 ILE A O     1 
ATOM   2573  C CB    . ILE A 1 335 ? 29.937  32.991  49.271  1.00 43.94  ? 335 ILE A CB    1 
ATOM   2574  C CG1   . ILE A 1 335 ? 29.398  31.684  49.868  1.00 36.96  ? 335 ILE A CG1   1 
ATOM   2575  C CG2   . ILE A 1 335 ? 29.424  33.195  47.855  1.00 39.95  ? 335 ILE A CG2   1 
ATOM   2576  C CD1   . ILE A 1 335 ? 27.985  31.817  50.453  1.00 36.76  ? 335 ILE A CD1   1 
ATOM   2577  N N     . ARG A 1 336 ? 31.812  35.435  48.849  1.00 48.62  ? 336 ARG A N     1 
ATOM   2578  C CA    . ARG A 1 336 ? 32.275  36.610  48.114  1.00 53.42  ? 336 ARG A CA    1 
ATOM   2579  C C     . ARG A 1 336 ? 33.766  36.488  47.773  1.00 56.65  ? 336 ARG A C     1 
ATOM   2580  O O     . ARG A 1 336 ? 34.153  36.750  46.639  1.00 58.26  ? 336 ARG A O     1 
ATOM   2581  C CB    . ARG A 1 336 ? 32.014  37.907  48.906  1.00 63.62  ? 336 ARG A CB    1 
ATOM   2582  C CG    . ARG A 1 336 ? 32.061  39.197  48.092  1.00 60.24  ? 336 ARG A CG    1 
ATOM   2583  C CD    . ARG A 1 336 ? 32.189  40.478  48.914  1.00 66.67  ? 336 ARG A CD    1 
ATOM   2584  N NE    . ARG A 1 336 ? 31.906  41.712  48.160  1.00 71.12  ? 336 ARG A NE    1 
ATOM   2585  C CZ    . ARG A 1 336 ? 32.691  42.280  47.233  1.00 63.15  ? 336 ARG A CZ    1 
ATOM   2586  N NH1   . ARG A 1 336 ? 33.924  41.854  47.003  1.00 59.31  ? 336 ARG A NH1   1 
ATOM   2587  N NH2   . ARG A 1 336 ? 32.242  43.312  46.543  1.00 60.12  ? 336 ARG A NH2   1 
ATOM   2588  N N     . ASP A 1 337 ? 34.618  36.100  48.737  1.00 54.07  ? 337 ASP A N     1 
ATOM   2589  C CA    . ASP A 1 337 ? 36.057  36.119  48.499  1.00 52.25  ? 337 ASP A CA    1 
ATOM   2590  C C     . ASP A 1 337 ? 36.453  34.985  47.548  1.00 50.48  ? 337 ASP A C     1 
ATOM   2591  O O     . ASP A 1 337 ? 37.522  35.037  46.932  1.00 43.11  ? 337 ASP A O     1 
ATOM   2592  C CB    . ASP A 1 337 ? 36.855  36.151  49.811  1.00 53.41  ? 337 ASP A CB    1 
ATOM   2593  C CG    . ASP A 1 337 ? 36.671  37.445  50.603  1.00 64.13  ? 337 ASP A CG    1 
ATOM   2594  O OD1   . ASP A 1 337 ? 35.999  38.371  50.089  1.00 75.25  ? 337 ASP A OD1   1 
ATOM   2595  O OD2   . ASP A 1 337 ? 37.161  37.517  51.750  1.00 69.04  ? 337 ASP A OD2   1 
ATOM   2596  N N     . SER A 1 338 ? 35.569  33.991  47.367  1.00 46.19  ? 338 SER A N     1 
ATOM   2597  C CA    . SER A 1 338 ? 35.828  32.948  46.388  1.00 45.27  ? 338 SER A CA    1 
ATOM   2598  C C     . SER A 1 338 ? 35.675  33.448  44.951  1.00 46.35  ? 338 SER A C     1 
ATOM   2599  O O     . SER A 1 338 ? 36.153  32.767  44.053  1.00 52.38  ? 338 SER A O     1 
ATOM   2600  C CB    . SER A 1 338 ? 34.941  31.758  46.587  1.00 45.41  ? 338 SER A CB    1 
ATOM   2601  O OG    . SER A 1 338 ? 35.160  31.149  47.843  1.00 43.79  ? 338 SER A OG    1 
ATOM   2602  N N     . PHE A 1 339 ? 34.998  34.583  44.712  1.00 45.91  ? 339 PHE A N     1 
ATOM   2603  C CA    . PHE A 1 339 ? 34.678  34.984  43.346  1.00 47.54  ? 339 PHE A CA    1 
ATOM   2604  C C     . PHE A 1 339 ? 35.273  36.338  42.982  1.00 47.21  ? 339 PHE A C     1 
ATOM   2605  O O     . PHE A 1 339 ? 35.374  36.659  41.796  1.00 49.26  ? 339 PHE A O     1 
ATOM   2606  C CB    . PHE A 1 339 ? 33.161  35.006  43.127  1.00 49.53  ? 339 PHE A CB    1 
ATOM   2607  C CG    . PHE A 1 339 ? 32.500  33.655  43.256  1.00 44.53  ? 339 PHE A CG    1 
ATOM   2608  C CD1   . PHE A 1 339 ? 32.722  32.675  42.319  1.00 42.35  ? 339 PHE A CD1   1 
ATOM   2609  C CD2   . PHE A 1 339 ? 31.679  33.357  44.325  1.00 47.87  ? 339 PHE A CD2   1 
ATOM   2610  C CE1   . PHE A 1 339 ? 32.153  31.420  42.454  1.00 47.77  ? 339 PHE A CE1   1 
ATOM   2611  C CE2   . PHE A 1 339 ? 31.079  32.109  44.438  1.00 51.60  ? 339 PHE A CE2   1 
ATOM   2612  C CZ    . PHE A 1 339 ? 31.337  31.134  43.520  1.00 48.59  ? 339 PHE A CZ    1 
ATOM   2613  N N     . ALA A 1 340 ? 35.713  37.099  43.987  1.00 53.36  ? 340 ALA A N     1 
ATOM   2614  C CA    . ALA A 1 340 ? 36.071  38.509  43.817  1.00 52.96  ? 340 ALA A CA    1 
ATOM   2615  C C     . ALA A 1 340 ? 37.103  38.755  42.713  1.00 54.13  ? 340 ALA A C     1 
ATOM   2616  O O     . ALA A 1 340 ? 36.959  39.738  41.986  1.00 58.98  ? 340 ALA A O     1 
ATOM   2617  C CB    . ALA A 1 340 ? 36.580  39.068  45.112  1.00 48.04  ? 340 ALA A CB    1 
ATOM   2618  N N     . ASP A 1 341 ? 38.118  37.882  42.568  1.00 56.86  ? 341 ASP A N     1 
ATOM   2619  C CA    . ASP A 1 341 ? 39.261  38.156  41.696  1.00 52.84  ? 341 ASP A CA    1 
ATOM   2620  C C     . ASP A 1 341 ? 38.986  37.853  40.216  1.00 52.62  ? 341 ASP A C     1 
ATOM   2621  O O     . ASP A 1 341 ? 39.931  37.920  39.420  1.00 45.42  ? 341 ASP A O     1 
ATOM   2622  C CB    . ASP A 1 341 ? 40.512  37.395  42.136  1.00 54.93  ? 341 ASP A CB    1 
ATOM   2623  C CG    . ASP A 1 341 ? 40.607  35.927  41.738  1.00 59.12  ? 341 ASP A CG    1 
ATOM   2624  O OD1   . ASP A 1 341 ? 39.605  35.353  41.299  1.00 62.47  ? 341 ASP A OD1   1 
ATOM   2625  O OD2   . ASP A 1 341 ? 41.711  35.374  41.845  1.00 59.96  ? 341 ASP A OD2   1 
ATOM   2626  N N     . ILE A 1 342 ? 37.724  37.522  39.844  1.00 48.43  ? 342 ILE A N     1 
ATOM   2627  C CA    . ILE A 1 342 ? 37.388  37.254  38.447  1.00 52.57  ? 342 ILE A CA    1 
ATOM   2628  C C     . ILE A 1 342 ? 37.090  38.573  37.732  1.00 55.47  ? 342 ILE A C     1 
ATOM   2629  O O     . ILE A 1 342 ? 36.209  39.348  38.134  1.00 54.98  ? 342 ILE A O     1 
ATOM   2630  C CB    . ILE A 1 342 ? 36.201  36.285  38.291  1.00 56.23  ? 342 ILE A CB    1 
ATOM   2631  C CG1   . ILE A 1 342 ? 36.401  34.954  39.025  1.00 55.38  ? 342 ILE A CG1   1 
ATOM   2632  C CG2   . ILE A 1 342 ? 35.900  36.053  36.815  1.00 55.65  ? 342 ILE A CG2   1 
ATOM   2633  C CD1   . ILE A 1 342 ? 35.101  34.191  39.249  1.00 53.41  ? 342 ILE A CD1   1 
ATOM   2634  N N     . PRO A 1 343 ? 37.812  38.883  36.638  1.00 52.78  ? 343 PRO A N     1 
ATOM   2635  C CA    . PRO A 1 343 ? 37.479  40.054  35.835  1.00 51.97  ? 343 PRO A CA    1 
ATOM   2636  C C     . PRO A 1 343 ? 36.010  40.018  35.415  1.00 57.72  ? 343 PRO A C     1 
ATOM   2637  O O     . PRO A 1 343 ? 35.568  39.054  34.770  1.00 59.49  ? 343 PRO A O     1 
ATOM   2638  C CB    . PRO A 1 343 ? 38.439  39.954  34.648  1.00 50.46  ? 343 PRO A CB    1 
ATOM   2639  C CG    . PRO A 1 343 ? 39.621  39.206  35.233  1.00 55.52  ? 343 PRO A CG    1 
ATOM   2640  C CD    . PRO A 1 343 ? 38.986  38.161  36.127  1.00 56.43  ? 343 PRO A CD    1 
ATOM   2641  N N     . GLY A 1 344 ? 35.285  41.064  35.863  1.00 53.88  ? 344 GLY A N     1 
ATOM   2642  C CA    . GLY A 1 344 ? 33.946  41.407  35.415  1.00 50.51  ? 344 GLY A CA    1 
ATOM   2643  C C     . GLY A 1 344 ? 32.860  41.038  36.425  1.00 52.36  ? 344 GLY A C     1 
ATOM   2644  O O     . GLY A 1 344 ? 31.667  41.256  36.180  1.00 49.93  ? 344 GLY A O     1 
ATOM   2645  N N     . VAL A 1 345 ? 33.267  40.441  37.549  1.00 52.66  ? 345 VAL A N     1 
ATOM   2646  C CA    . VAL A 1 345 ? 32.296  39.923  38.492  1.00 51.15  ? 345 VAL A CA    1 
ATOM   2647  C C     . VAL A 1 345 ? 31.612  41.104  39.153  1.00 50.91  ? 345 VAL A C     1 
ATOM   2648  O O     . VAL A 1 345 ? 32.278  42.090  39.483  1.00 47.58  ? 345 VAL A O     1 
ATOM   2649  C CB    . VAL A 1 345 ? 32.937  39.001  39.542  1.00 57.22  ? 345 VAL A CB    1 
ATOM   2650  C CG1   . VAL A 1 345 ? 33.884  39.740  40.485  1.00 52.72  ? 345 VAL A CG1   1 
ATOM   2651  C CG2   . VAL A 1 345 ? 31.877  38.251  40.326  1.00 57.34  ? 345 VAL A CG2   1 
ATOM   2652  N N     . LYS A 1 346 ? 30.287  40.969  39.318  1.00 55.99  ? 346 LYS A N     1 
ATOM   2653  C CA    . LYS A 1 346 ? 29.476  41.896  40.096  1.00 60.70  ? 346 LYS A CA    1 
ATOM   2654  C C     . LYS A 1 346 ? 28.694  41.105  41.141  1.00 51.84  ? 346 LYS A C     1 
ATOM   2655  O O     . LYS A 1 346 ? 28.338  39.958  40.912  1.00 51.71  ? 346 LYS A O     1 
ATOM   2656  C CB    . LYS A 1 346 ? 28.523  42.703  39.201  1.00 72.54  ? 346 LYS A CB    1 
ATOM   2657  C CG    . LYS A 1 346 ? 29.177  43.558  38.118  1.00 79.07  ? 346 LYS A CG    1 
ATOM   2658  C CD    . LYS A 1 346 ? 29.954  44.767  38.633  1.00 95.36  ? 346 LYS A CD    1 
ATOM   2659  C CE    . LYS A 1 346 ? 30.777  45.457  37.562  1.00 104.43 ? 346 LYS A CE    1 
ATOM   2660  N NZ    . LYS A 1 346 ? 29.996  45.629  36.312  1.00 104.63 ? 346 LYS A NZ    1 
ATOM   2661  N N     . PHE A 1 347 ? 28.461  41.735  42.295  1.00 51.59  ? 347 PHE A N     1 
ATOM   2662  C CA    . PHE A 1 347 ? 27.713  41.131  43.383  1.00 53.13  ? 347 PHE A CA    1 
ATOM   2663  C C     . PHE A 1 347 ? 26.497  41.996  43.677  1.00 46.09  ? 347 PHE A C     1 
ATOM   2664  O O     . PHE A 1 347 ? 26.602  43.205  43.637  1.00 40.49  ? 347 PHE A O     1 
ATOM   2665  C CB    . PHE A 1 347 ? 28.570  41.053  44.645  1.00 54.44  ? 347 PHE A CB    1 
ATOM   2666  C CG    . PHE A 1 347 ? 29.896  40.365  44.459  1.00 54.82  ? 347 PHE A CG    1 
ATOM   2667  C CD1   . PHE A 1 347 ? 30.998  41.063  43.993  1.00 50.49  ? 347 PHE A CD1   1 
ATOM   2668  C CD2   . PHE A 1 347 ? 30.028  39.004  44.716  1.00 54.37  ? 347 PHE A CD2   1 
ATOM   2669  C CE1   . PHE A 1 347 ? 32.217  40.422  43.826  1.00 52.95  ? 347 PHE A CE1   1 
ATOM   2670  C CE2   . PHE A 1 347 ? 31.242  38.360  44.528  1.00 45.92  ? 347 PHE A CE2   1 
ATOM   2671  C CZ    . PHE A 1 347 ? 32.331  39.064  44.082  1.00 48.16  ? 347 PHE A CZ    1 
ATOM   2672  N N     . TYR A 1 348 ? 25.365  41.379  44.014  1.00 44.98  ? 348 TYR A N     1 
ATOM   2673  C CA    . TYR A 1 348 ? 24.148  42.140  44.228  1.00 50.15  ? 348 TYR A CA    1 
ATOM   2674  C C     . TYR A 1 348 ? 23.305  41.504  45.321  1.00 54.89  ? 348 TYR A C     1 
ATOM   2675  O O     . TYR A 1 348 ? 22.973  40.322  45.200  1.00 47.81  ? 348 TYR A O     1 
ATOM   2676  C CB    . TYR A 1 348 ? 23.242  42.122  42.995  1.00 53.85  ? 348 TYR A CB    1 
ATOM   2677  C CG    . TYR A 1 348 ? 23.802  42.743  41.743  1.00 47.31  ? 348 TYR A CG    1 
ATOM   2678  C CD1   . TYR A 1 348 ? 24.397  41.960  40.770  1.00 46.95  ? 348 TYR A CD1   1 
ATOM   2679  C CD2   . TYR A 1 348 ? 23.653  44.092  41.492  1.00 48.04  ? 348 TYR A CD2   1 
ATOM   2680  C CE1   . TYR A 1 348 ? 24.884  42.513  39.598  1.00 50.85  ? 348 TYR A CE1   1 
ATOM   2681  C CE2   . TYR A 1 348 ? 24.141  44.661  40.332  1.00 48.96  ? 348 TYR A CE2   1 
ATOM   2682  C CZ    . TYR A 1 348 ? 24.751  43.868  39.384  1.00 48.39  ? 348 TYR A CZ    1 
ATOM   2683  O OH    . TYR A 1 348 ? 25.213  44.439  38.250  1.00 50.82  ? 348 TYR A OH    1 
ATOM   2684  N N     . PHE A 1 349 ? 22.927  42.316  46.327  1.00 55.10  ? 349 PHE A N     1 
ATOM   2685  C CA    . PHE A 1 349 ? 21.780  42.015  47.179  1.00 58.30  ? 349 PHE A CA    1 
ATOM   2686  C C     . PHE A 1 349 ? 20.546  42.653  46.538  1.00 49.20  ? 349 PHE A C     1 
ATOM   2687  O O     . PHE A 1 349 ? 20.690  43.482  45.642  1.00 56.95  ? 349 PHE A O     1 
ATOM   2688  C CB    . PHE A 1 349 ? 22.069  42.455  48.625  1.00 63.80  ? 349 PHE A CB    1 
ATOM   2689  C CG    . PHE A 1 349 ? 23.246  41.753  49.266  1.00 61.10  ? 349 PHE A CG    1 
ATOM   2690  C CD1   . PHE A 1 349 ? 23.173  40.403  49.595  1.00 58.62  ? 349 PHE A CD1   1 
ATOM   2691  C CD2   . PHE A 1 349 ? 24.441  42.431  49.486  1.00 59.99  ? 349 PHE A CD2   1 
ATOM   2692  C CE1   . PHE A 1 349 ? 24.265  39.752  50.144  1.00 55.86  ? 349 PHE A CE1   1 
ATOM   2693  C CE2   . PHE A 1 349 ? 25.532  41.780  50.036  1.00 61.58  ? 349 PHE A CE2   1 
ATOM   2694  C CZ    . PHE A 1 349 ? 25.440  40.439  50.361  1.00 63.58  ? 349 PHE A CZ    1 
ATOM   2695  N N     . PRO A 1 350 ? 19.305  42.333  46.974  1.00 45.03  ? 350 PRO A N     1 
ATOM   2696  C CA    . PRO A 1 350 ? 18.101  42.850  46.319  1.00 48.02  ? 350 PRO A CA    1 
ATOM   2697  C C     . PRO A 1 350 ? 18.117  44.371  46.198  1.00 61.14  ? 350 PRO A C     1 
ATOM   2698  O O     . PRO A 1 350 ? 17.777  44.929  45.156  1.00 59.87  ? 350 PRO A O     1 
ATOM   2699  C CB    . PRO A 1 350 ? 16.953  42.414  47.243  1.00 44.60  ? 350 PRO A CB    1 
ATOM   2700  C CG    . PRO A 1 350 ? 17.499  41.227  47.982  1.00 44.54  ? 350 PRO A CG    1 
ATOM   2701  C CD    . PRO A 1 350 ? 18.977  41.539  48.167  1.00 46.60  ? 350 PRO A CD    1 
ATOM   2702  N N     . GLU A 1 351 ? 18.564  45.037  47.267  1.00 62.96  ? 351 GLU A N     1 
ATOM   2703  C CA    . GLU A 1 351 ? 18.559  46.484  47.291  1.00 57.81  ? 351 GLU A CA    1 
ATOM   2704  C C     . GLU A 1 351 ? 19.591  47.067  46.324  1.00 55.96  ? 351 GLU A C     1 
ATOM   2705  O O     . GLU A 1 351 ? 19.623  48.280  46.159  1.00 67.60  ? 351 GLU A O     1 
ATOM   2706  C CB    . GLU A 1 351 ? 18.742  47.015  48.718  1.00 66.50  ? 351 GLU A CB    1 
ATOM   2707  C CG    . GLU A 1 351 ? 20.085  46.676  49.372  1.00 75.52  ? 351 GLU A CG    1 
ATOM   2708  C CD    . GLU A 1 351 ? 20.136  45.424  50.243  1.00 76.13  ? 351 GLU A CD    1 
ATOM   2709  O OE1   . GLU A 1 351 ? 19.069  44.780  50.433  1.00 63.54  ? 351 GLU A OE1   1 
ATOM   2710  O OE2   . GLU A 1 351 ? 21.253  45.095  50.741  1.00 62.12  ? 351 GLU A OE2   1 
ATOM   2711  N N     . ASP A 1 352 ? 20.430  46.264  45.657  1.00 58.52  ? 352 ASP A N     1 
ATOM   2712  C CA    . ASP A 1 352 ? 21.327  46.841  44.658  1.00 55.11  ? 352 ASP A CA    1 
ATOM   2713  C C     . ASP A 1 352 ? 20.743  46.675  43.251  1.00 56.51  ? 352 ASP A C     1 
ATOM   2714  O O     . ASP A 1 352 ? 21.431  46.955  42.261  1.00 51.05  ? 352 ASP A O     1 
ATOM   2715  C CB    . ASP A 1 352 ? 22.733  46.231  44.684  1.00 60.27  ? 352 ASP A CB    1 
ATOM   2716  C CG    . ASP A 1 352 ? 23.454  46.265  46.022  1.00 61.84  ? 352 ASP A CG    1 
ATOM   2717  O OD1   . ASP A 1 352 ? 23.882  47.389  46.467  1.00 53.11  ? 352 ASP A OD1   1 
ATOM   2718  O OD2   . ASP A 1 352 ? 23.594  45.161  46.593  1.00 49.06  ? 352 ASP A OD2   1 
ATOM   2719  N N     . ARG A 1 353 ? 19.480  46.222  43.150  1.00 50.77  ? 353 ARG A N     1 
ATOM   2720  C CA    . ARG A 1 353 ? 18.867  45.937  41.854  1.00 53.57  ? 353 ARG A CA    1 
ATOM   2721  C C     . ARG A 1 353 ? 18.031  47.126  41.365  1.00 53.19  ? 353 ARG A C     1 
ATOM   2722  O O     . ARG A 1 353 ? 16.940  47.379  41.864  1.00 61.91  ? 353 ARG A O     1 
ATOM   2723  C CB    . ARG A 1 353 ? 17.989  44.679  41.931  1.00 44.15  ? 353 ARG A CB    1 
ATOM   2724  C CG    . ARG A 1 353 ? 18.732  43.375  42.203  1.00 45.36  ? 353 ARG A CG    1 
ATOM   2725  C CD    . ARG A 1 353 ? 19.889  43.040  41.262  1.00 43.19  ? 353 ARG A CD    1 
ATOM   2726  N NE    . ARG A 1 353 ? 19.474  42.508  39.979  1.00 35.27  ? 353 ARG A NE    1 
ATOM   2727  C CZ    . ARG A 1 353 ? 20.276  42.448  38.934  1.00 37.44  ? 353 ARG A CZ    1 
ATOM   2728  N NH1   . ARG A 1 353 ? 21.570  42.658  39.087  1.00 35.13  ? 353 ARG A NH1   1 
ATOM   2729  N NH2   . ARG A 1 353 ? 19.782  42.200  37.732  1.00 39.69  ? 353 ARG A NH2   1 
ATOM   2730  N N     . ARG A 1 354 ? 18.503  47.831  40.338  1.00 54.64  ? 354 ARG A N     1 
ATOM   2731  C CA    . ARG A 1 354 ? 17.826  49.055  39.934  1.00 61.21  ? 354 ARG A CA    1 
ATOM   2732  C C     . ARG A 1 354 ? 16.413  48.786  39.406  1.00 59.11  ? 354 ARG A C     1 
ATOM   2733  O O     . ARG A 1 354 ? 15.560  49.649  39.544  1.00 55.80  ? 354 ARG A O     1 
ATOM   2734  C CB    . ARG A 1 354 ? 18.685  49.866  38.964  1.00 63.97  ? 354 ARG A CB    1 
ATOM   2735  C CG    . ARG A 1 354 ? 19.161  49.139  37.718  1.00 65.80  ? 354 ARG A CG    1 
ATOM   2736  C CD    . ARG A 1 354 ? 20.202  50.049  37.093  1.00 63.86  ? 354 ARG A CD    1 
ATOM   2737  N NE    . ARG A 1 354 ? 20.717  49.590  35.819  1.00 69.78  ? 354 ARG A NE    1 
ATOM   2738  C CZ    . ARG A 1 354 ? 20.005  49.448  34.712  1.00 75.88  ? 354 ARG A CZ    1 
ATOM   2739  N NH1   . ARG A 1 354 ? 18.722  49.746  34.694  1.00 84.27  ? 354 ARG A NH1   1 
ATOM   2740  N NH2   . ARG A 1 354 ? 20.578  48.982  33.618  1.00 94.63  ? 354 ARG A NH2   1 
ATOM   2741  N N     . HIS A 1 355 ? 16.144  47.580  38.892  1.00 57.53  ? 355 HIS A N     1 
ATOM   2742  C CA    . HIS A 1 355 ? 14.826  47.215  38.395  1.00 49.85  ? 355 HIS A CA    1 
ATOM   2743  C C     . HIS A 1 355 ? 13.944  46.629  39.493  1.00 56.91  ? 355 HIS A C     1 
ATOM   2744  O O     . HIS A 1 355 ? 14.412  45.900  40.361  1.00 57.89  ? 355 HIS A O     1 
ATOM   2745  C CB    . HIS A 1 355 ? 14.897  46.158  37.286  1.00 43.35  ? 355 HIS A CB    1 
ATOM   2746  C CG    . HIS A 1 355 ? 15.798  46.489  36.139  1.00 40.28  ? 355 HIS A CG    1 
ATOM   2747  N ND1   . HIS A 1 355 ? 15.345  46.739  34.856  1.00 37.55  ? 355 HIS A ND1   1 
ATOM   2748  C CD2   . HIS A 1 355 ? 17.150  46.564  36.093  1.00 41.48  ? 355 HIS A CD2   1 
ATOM   2749  C CE1   . HIS A 1 355 ? 16.398  46.997  34.080  1.00 44.73  ? 355 HIS A CE1   1 
ATOM   2750  N NE2   . HIS A 1 355 ? 17.509  46.897  34.808  1.00 39.12  ? 355 HIS A NE2   1 
ATOM   2751  N N     . LYS A 1 356 ? 12.642  46.917  39.381  1.00 64.64  ? 356 LYS A N     1 
ATOM   2752  C CA    . LYS A 1 356 ? 11.636  46.542  40.362  1.00 70.14  ? 356 LYS A CA    1 
ATOM   2753  C C     . LYS A 1 356 ? 10.969  45.241  39.923  1.00 67.54  ? 356 LYS A C     1 
ATOM   2754  O O     . LYS A 1 356 ? 10.328  44.564  40.735  1.00 62.47  ? 356 LYS A O     1 
ATOM   2755  C CB    . LYS A 1 356 ? 10.632  47.690  40.564  1.00 69.33  ? 356 LYS A CB    1 
ATOM   2756  C CG    . LYS A 1 356 ? 11.143  48.808  41.473  1.00 80.54  ? 356 LYS A CG    1 
ATOM   2757  C CD    . LYS A 1 356 ? 10.369  50.103  41.388  1.00 89.07  ? 356 LYS A CD    1 
ATOM   2758  C CE    . LYS A 1 356 ? 8.912   49.968  41.791  1.00 91.84  ? 356 LYS A CE    1 
ATOM   2759  N NZ    . LYS A 1 356 ? 8.716   50.237  43.236  1.00 93.33  ? 356 LYS A NZ    1 
ATOM   2760  N N     . VAL A 1 357 ? 11.111  44.925  38.629  1.00 53.68  ? 357 VAL A N     1 
ATOM   2761  C CA    . VAL A 1 357 ? 10.865  43.589  38.126  1.00 55.37  ? 357 VAL A CA    1 
ATOM   2762  C C     . VAL A 1 357 ? 12.199  43.060  37.617  1.00 58.26  ? 357 VAL A C     1 
ATOM   2763  O O     . VAL A 1 357 ? 12.909  43.770  36.910  1.00 58.34  ? 357 VAL A O     1 
ATOM   2764  C CB    . VAL A 1 357 ? 9.754   43.617  37.069  1.00 64.55  ? 357 VAL A CB    1 
ATOM   2765  C CG1   . VAL A 1 357 ? 9.295   42.217  36.670  1.00 66.85  ? 357 VAL A CG1   1 
ATOM   2766  C CG2   . VAL A 1 357 ? 8.573   44.431  37.581  1.00 65.70  ? 357 VAL A CG2   1 
ATOM   2767  N N     . ASP A 1 358 ? 12.599  41.871  38.098  1.00 62.77  ? 358 ASP A N     1 
ATOM   2768  C CA    . ASP A 1 358 ? 14.014  41.508  38.118  1.00 58.38  ? 358 ASP A CA    1 
ATOM   2769  C C     . ASP A 1 358 ? 14.212  40.077  38.618  1.00 54.62  ? 358 ASP A C     1 
ATOM   2770  O O     . ASP A 1 358 ? 13.493  39.600  39.490  1.00 55.20  ? 358 ASP A O     1 
ATOM   2771  C CB    . ASP A 1 358 ? 14.814  42.478  38.990  1.00 52.82  ? 358 ASP A CB    1 
ATOM   2772  C CG    . ASP A 1 358 ? 16.326  42.374  38.864  1.00 55.07  ? 358 ASP A CG    1 
ATOM   2773  O OD1   . ASP A 1 358 ? 16.881  42.825  37.817  1.00 52.69  ? 358 ASP A OD1   1 
ATOM   2774  O OD2   . ASP A 1 358 ? 16.944  41.875  39.836  1.00 50.48  ? 358 ASP A OD2   1 
ATOM   2775  N N     . LEU A 1 359 ? 15.212  39.414  38.037  1.00 58.40  ? 359 LEU A N     1 
ATOM   2776  C CA    . LEU A 1 359 ? 15.641  38.084  38.425  1.00 63.77  ? 359 LEU A CA    1 
ATOM   2777  C C     . LEU A 1 359 ? 15.622  37.908  39.946  1.00 60.89  ? 359 LEU A C     1 
ATOM   2778  O O     . LEU A 1 359 ? 14.966  37.021  40.478  1.00 48.58  ? 359 LEU A O     1 
ATOM   2779  C CB    . LEU A 1 359 ? 17.082  37.871  37.931  1.00 65.68  ? 359 LEU A CB    1 
ATOM   2780  C CG    . LEU A 1 359 ? 17.731  36.575  38.440  1.00 60.34  ? 359 LEU A CG    1 
ATOM   2781  C CD1   . LEU A 1 359 ? 17.209  35.387  37.651  1.00 60.31  ? 359 LEU A CD1   1 
ATOM   2782  C CD2   . LEU A 1 359 ? 19.242  36.621  38.405  1.00 57.75  ? 359 LEU A CD2   1 
ATOM   2783  N N     . LEU A 1 360 ? 16.429  38.715  40.632  1.00 56.57  ? 360 LEU A N     1 
ATOM   2784  C CA    . LEU A 1 360 ? 16.754  38.436  42.015  1.00 55.62  ? 360 LEU A CA    1 
ATOM   2785  C C     . LEU A 1 360 ? 15.509  38.566  42.886  1.00 53.88  ? 360 LEU A C     1 
ATOM   2786  O O     . LEU A 1 360 ? 15.384  37.870  43.885  1.00 54.03  ? 360 LEU A O     1 
ATOM   2787  C CB    . LEU A 1 360 ? 17.881  39.377  42.447  1.00 53.24  ? 360 LEU A CB    1 
ATOM   2788  C CG    . LEU A 1 360 ? 18.338  39.246  43.895  1.00 53.82  ? 360 LEU A CG    1 
ATOM   2789  C CD1   . LEU A 1 360 ? 18.798  37.833  44.206  1.00 54.34  ? 360 LEU A CD1   1 
ATOM   2790  C CD2   . LEU A 1 360 ? 19.447  40.249  44.199  1.00 52.03  ? 360 LEU A CD2   1 
ATOM   2791  N N     . LEU A 1 361 ? 14.575  39.441  42.509  1.00 61.07  ? 361 LEU A N     1 
ATOM   2792  C CA    . LEU A 1 361 ? 13.404  39.655  43.348  1.00 59.85  ? 361 LEU A CA    1 
ATOM   2793  C C     . LEU A 1 361 ? 12.430  38.505  43.137  1.00 51.59  ? 361 LEU A C     1 
ATOM   2794  O O     . LEU A 1 361 ? 11.697  38.142  44.044  1.00 55.12  ? 361 LEU A O     1 
ATOM   2795  C CB    . LEU A 1 361 ? 12.789  41.034  43.071  1.00 57.47  ? 361 LEU A CB    1 
ATOM   2796  C CG    . LEU A 1 361 ? 13.748  42.217  43.259  1.00 69.14  ? 361 LEU A CG    1 
ATOM   2797  C CD1   . LEU A 1 361 ? 12.992  43.531  43.306  1.00 74.68  ? 361 LEU A CD1   1 
ATOM   2798  C CD2   . LEU A 1 361 ? 14.594  42.073  44.523  1.00 80.78  ? 361 LEU A CD2   1 
ATOM   2799  N N     . HIS A 1 362 ? 12.473  37.883  41.962  1.00 52.76  ? 362 HIS A N     1 
ATOM   2800  C CA    . HIS A 1 362 ? 11.637  36.720  41.701  1.00 54.40  ? 362 HIS A CA    1 
ATOM   2801  C C     . HIS A 1 362 ? 12.241  35.493  42.379  1.00 51.90  ? 362 HIS A C     1 
ATOM   2802  O O     . HIS A 1 362 ? 11.496  34.695  42.924  1.00 55.76  ? 362 HIS A O     1 
ATOM   2803  C CB    . HIS A 1 362 ? 11.455  36.503  40.188  1.00 55.66  ? 362 HIS A CB    1 
ATOM   2804  C CG    . HIS A 1 362 ? 10.667  35.293  39.808  1.00 57.12  ? 362 HIS A CG    1 
ATOM   2805  N ND1   . HIS A 1 362 ? 11.250  34.058  39.634  1.00 63.92  ? 362 HIS A ND1   1 
ATOM   2806  C CD2   . HIS A 1 362 ? 9.355   35.102  39.618  1.00 79.55  ? 362 HIS A CD2   1 
ATOM   2807  C CE1   . HIS A 1 362 ? 10.323  33.161  39.319  1.00 67.23  ? 362 HIS A CE1   1 
ATOM   2808  N NE2   . HIS A 1 362 ? 9.161   33.774  39.305  1.00 83.83  ? 362 HIS A NE2   1 
ATOM   2809  N N     . ARG A 1 363 ? 13.579  35.341  42.299  1.00 55.93  ? 363 ARG A N     1 
ATOM   2810  C CA    . ARG A 1 363 ? 14.293  34.181  42.815  1.00 54.90  ? 363 ARG A CA    1 
ATOM   2811  C C     . ARG A 1 363 ? 14.302  34.168  44.347  1.00 53.78  ? 363 ARG A C     1 
ATOM   2812  O O     . ARG A 1 363 ? 14.170  33.119  44.972  1.00 53.08  ? 363 ARG A O     1 
ATOM   2813  C CB    . ARG A 1 363 ? 15.733  34.168  42.305  1.00 60.02  ? 363 ARG A CB    1 
ATOM   2814  C CG    . ARG A 1 363 ? 15.865  33.819  40.833  1.00 66.64  ? 363 ARG A CG    1 
ATOM   2815  C CD    . ARG A 1 363 ? 15.595  32.369  40.454  1.00 73.86  ? 363 ARG A CD    1 
ATOM   2816  N NE    . ARG A 1 363 ? 16.007  32.216  39.057  1.00 73.56  ? 363 ARG A NE    1 
ATOM   2817  C CZ    . ARG A 1 363 ? 15.224  31.818  38.060  1.00 66.63  ? 363 ARG A CZ    1 
ATOM   2818  N NH1   . ARG A 1 363 ? 14.029  31.328  38.319  1.00 66.47  ? 363 ARG A NH1   1 
ATOM   2819  N NH2   . ARG A 1 363 ? 15.652  31.879  36.806  1.00 80.23  ? 363 ARG A NH2   1 
ATOM   2820  N N     . ALA A 1 364 ? 14.457  35.341  44.953  1.00 51.60  ? 364 ALA A N     1 
ATOM   2821  C CA    . ALA A 1 364 ? 14.338  35.481  46.396  1.00 58.31  ? 364 ALA A CA    1 
ATOM   2822  C C     . ALA A 1 364 ? 13.046  34.852  46.936  1.00 60.59  ? 364 ALA A C     1 
ATOM   2823  O O     . ALA A 1 364 ? 13.056  34.289  48.033  1.00 57.99  ? 364 ALA A O     1 
ATOM   2824  C CB    . ALA A 1 364 ? 14.464  36.943  46.778  1.00 55.93  ? 364 ALA A CB    1 
ATOM   2825  N N     . GLU A 1 365 ? 11.937  34.919  46.183  1.00 60.16  ? 365 GLU A N     1 
ATOM   2826  C CA    . GLU A 1 365 ? 10.689  34.320  46.654  1.00 61.71  ? 365 GLU A CA    1 
ATOM   2827  C C     . GLU A 1 365 ? 10.820  32.788  46.674  1.00 52.30  ? 365 GLU A C     1 
ATOM   2828  O O     . GLU A 1 365 ? 10.238  32.133  47.535  1.00 55.54  ? 365 GLU A O     1 
ATOM   2829  C CB    . GLU A 1 365 ? 9.461   34.779  45.835  1.00 68.63  ? 365 GLU A CB    1 
ATOM   2830  C CG    . GLU A 1 365 ? 8.984   36.231  46.069  1.00 72.75  ? 365 GLU A CG    1 
ATOM   2831  C CD    . GLU A 1 365 ? 8.287   36.566  47.391  1.00 82.90  ? 365 GLU A CD    1 
ATOM   2832  O OE1   . GLU A 1 365 ? 7.033   36.594  47.408  1.00 85.45  ? 365 GLU A OE1   1 
ATOM   2833  O OE2   . GLU A 1 365 ? 8.982   36.853  48.404  1.00 77.48  ? 365 GLU A OE2   1 
ATOM   2834  N N     . THR A 1 366 ? 11.581  32.193  45.741  1.00 50.00  ? 366 THR A N     1 
ATOM   2835  C CA    . THR A 1 366 ? 11.658  30.734  45.645  1.00 50.72  ? 366 THR A CA    1 
ATOM   2836  C C     . THR A 1 366 ? 12.670  30.188  46.652  1.00 45.53  ? 366 THR A C     1 
ATOM   2837  O O     . THR A 1 366 ? 12.575  29.042  47.122  1.00 43.36  ? 366 THR A O     1 
ATOM   2838  C CB    . THR A 1 366 ? 11.963  30.281  44.210  1.00 51.89  ? 366 THR A CB    1 
ATOM   2839  O OG1   . THR A 1 366 ? 12.839  31.232  43.623  1.00 75.96  ? 366 THR A OG1   1 
ATOM   2840  C CG2   . THR A 1 366 ? 10.757  30.257  43.312  1.00 64.19  ? 366 THR A CG2   1 
ATOM   2841  N N     . MET A 1 367 ? 13.661  31.029  46.959  1.00 41.55  ? 367 MET A N     1 
ATOM   2842  C CA    . MET A 1 367 ? 14.741  30.629  47.825  1.00 38.88  ? 367 MET A CA    1 
ATOM   2843  C C     . MET A 1 367 ? 14.297  30.798  49.289  1.00 52.22  ? 367 MET A C     1 
ATOM   2844  O O     . MET A 1 367 ? 15.070  30.446  50.180  1.00 52.92  ? 367 MET A O     1 
ATOM   2845  C CB    . MET A 1 367 ? 16.002  31.437  47.493  1.00 33.52  ? 367 MET A CB    1 
ATOM   2846  C CG    . MET A 1 367 ? 16.600  31.112  46.144  1.00 35.14  ? 367 MET A CG    1 
ATOM   2847  S SD    . MET A 1 367 ? 18.341  31.584  45.881  1.00 39.08  ? 367 MET A SD    1 
ATOM   2848  C CE    . MET A 1 367 ? 18.261  33.370  45.949  1.00 35.44  ? 367 MET A CE    1 
ATOM   2849  N N     . LYS A 1 368 ? 13.059  31.294  49.540  1.00 54.03  ? 368 LYS A N     1 
ATOM   2850  C CA    . LYS A 1 368 ? 12.486  31.347  50.891  1.00 53.88  ? 368 LYS A CA    1 
ATOM   2851  C C     . LYS A 1 368 ? 11.192  30.539  50.962  1.00 47.34  ? 368 LYS A C     1 
ATOM   2852  O O     . LYS A 1 368 ? 10.465  30.578  51.949  1.00 52.58  ? 368 LYS A O     1 
ATOM   2853  C CB    . LYS A 1 368 ? 12.284  32.784  51.398  1.00 58.27  ? 368 LYS A CB    1 
ATOM   2854  C CG    . LYS A 1 368 ? 10.883  33.385  51.333  1.00 66.41  ? 368 LYS A CG    1 
ATOM   2855  C CD    . LYS A 1 368 ? 10.725  34.683  52.126  1.00 77.59  ? 368 LYS A CD    1 
ATOM   2856  C CE    . LYS A 1 368 ? 11.113  35.924  51.343  1.00 88.39  ? 368 LYS A CE    1 
ATOM   2857  N NZ    . LYS A 1 368 ? 11.126  37.153  52.176  1.00 87.97  ? 368 LYS A NZ    1 
ATOM   2858  N N     . GLY A 1 369 ? 10.936  29.737  49.941  1.00 46.45  ? 369 GLY A N     1 
ATOM   2859  C CA    . GLY A 1 369 ? 9.887   28.737  50.018  1.00 49.47  ? 369 GLY A CA    1 
ATOM   2860  C C     . GLY A 1 369 ? 8.503   29.260  49.629  1.00 50.50  ? 369 GLY A C     1 
ATOM   2861  O O     . GLY A 1 369 ? 7.496   28.708  50.066  1.00 59.47  ? 369 GLY A O     1 
ATOM   2862  N N     . VAL A 1 370 ? 8.456   30.304  48.796  1.00 51.67  ? 370 VAL A N     1 
ATOM   2863  C CA    . VAL A 1 370 ? 7.201   30.954  48.476  1.00 55.04  ? 370 VAL A CA    1 
ATOM   2864  C C     . VAL A 1 370 ? 6.783   30.540  47.074  1.00 54.02  ? 370 VAL A C     1 
ATOM   2865  O O     . VAL A 1 370 ? 7.440   30.848  46.081  1.00 55.48  ? 370 VAL A O     1 
ATOM   2866  C CB    . VAL A 1 370 ? 7.279   32.486  48.602  1.00 63.02  ? 370 VAL A CB    1 
ATOM   2867  C CG1   . VAL A 1 370 ? 5.951   33.118  48.198  1.00 59.48  ? 370 VAL A CG1   1 
ATOM   2868  C CG2   . VAL A 1 370 ? 7.710   32.939  50.005  1.00 56.66  ? 370 VAL A CG2   1 
ATOM   2869  N N     . PRO A 1 371 ? 5.652   29.832  46.943  1.00 58.89  ? 371 PRO A N     1 
ATOM   2870  C CA    . PRO A 1 371 ? 5.248   29.325  45.643  1.00 62.28  ? 371 PRO A CA    1 
ATOM   2871  C C     . PRO A 1 371 ? 4.678   30.520  44.892  1.00 62.74  ? 371 PRO A C     1 
ATOM   2872  O O     . PRO A 1 371 ? 3.794   31.186  45.408  1.00 58.46  ? 371 PRO A O     1 
ATOM   2873  C CB    . PRO A 1 371 ? 4.241   28.211  45.962  1.00 56.89  ? 371 PRO A CB    1 
ATOM   2874  C CG    . PRO A 1 371 ? 3.883   28.369  47.438  1.00 56.61  ? 371 PRO A CG    1 
ATOM   2875  C CD    . PRO A 1 371 ? 4.688   29.517  48.004  1.00 56.45  ? 371 PRO A CD    1 
ATOM   2876  N N     . LYS A 1 372 ? 5.261   30.814  43.725  1.00 74.36  ? 372 LYS A N     1 
ATOM   2877  C CA    . LYS A 1 372 ? 4.870   31.944  42.897  1.00 74.34  ? 372 LYS A CA    1 
ATOM   2878  C C     . LYS A 1 372 ? 4.550   31.443  41.497  1.00 70.22  ? 372 LYS A C     1 
ATOM   2879  O O     . LYS A 1 372 ? 5.281   30.626  40.933  1.00 61.60  ? 372 LYS A O     1 
ATOM   2880  C CB    . LYS A 1 372 ? 5.972   33.005  42.808  1.00 82.25  ? 372 LYS A CB    1 
ATOM   2881  C CG    . LYS A 1 372 ? 5.988   34.030  43.931  1.00 94.56  ? 372 LYS A CG    1 
ATOM   2882  C CD    . LYS A 1 372 ? 4.641   34.701  44.156  1.00 99.34  ? 372 LYS A CD    1 
ATOM   2883  C CE    . LYS A 1 372 ? 4.671   35.803  45.193  1.00 100.80 ? 372 LYS A CE    1 
ATOM   2884  N NZ    . LYS A 1 372 ? 3.299   36.153  45.624  1.00 103.26 ? 372 LYS A NZ    1 
ATOM   2885  N N     . LEU A 1 373 ? 3.468   31.998  40.953  1.00 70.88  ? 373 LEU A N     1 
ATOM   2886  C CA    . LEU A 1 373 ? 2.894   31.547  39.704  1.00 76.57  ? 373 LEU A CA    1 
ATOM   2887  C C     . LEU A 1 373 ? 2.945   32.689  38.702  1.00 78.41  ? 373 LEU A C     1 
ATOM   2888  O O     . LEU A 1 373 ? 1.946   33.361  38.504  1.00 86.40  ? 373 LEU A O     1 
ATOM   2889  C CB    . LEU A 1 373 ? 1.452   31.143  40.011  1.00 76.47  ? 373 LEU A CB    1 
ATOM   2890  C CG    . LEU A 1 373 ? 0.678   30.519  38.858  1.00 88.10  ? 373 LEU A CG    1 
ATOM   2891  C CD1   . LEU A 1 373 ? 1.242   29.143  38.526  1.00 87.66  ? 373 LEU A CD1   1 
ATOM   2892  C CD2   . LEU A 1 373 ? -0.810  30.441  39.195  1.00 95.93  ? 373 LEU A CD2   1 
ATOM   2893  N N     . THR A 1 374 ? 4.112   32.944  38.106  1.00 97.59  ? 374 THR A N     1 
ATOM   2894  C CA    . THR A 1 374 ? 4.212   34.025  37.135  1.00 115.21 ? 374 THR A CA    1 
ATOM   2895  C C     . THR A 1 374 ? 3.716   33.512  35.789  1.00 114.12 ? 374 THR A C     1 
ATOM   2896  O O     . THR A 1 374 ? 3.929   32.350  35.449  1.00 110.31 ? 374 THR A O     1 
ATOM   2897  C CB    . THR A 1 374 ? 5.630   34.600  36.998  1.00 127.89 ? 374 THR A CB    1 
ATOM   2898  O OG1   . THR A 1 374 ? 6.512   33.559  36.579  1.00 128.60 ? 374 THR A OG1   1 
ATOM   2899  C CG2   . THR A 1 374 ? 6.150   35.232  38.273  1.00 134.59 ? 374 THR A CG2   1 
ATOM   2900  N N     . GLU A 1 375 ? 3.057   34.401  35.042  1.00 124.07 ? 375 GLU A N     1 
ATOM   2901  C CA    . GLU A 1 375 ? 2.624   34.103  33.687  1.00 140.39 ? 375 GLU A CA    1 
ATOM   2902  C C     . GLU A 1 375 ? 3.715   34.538  32.714  1.00 133.91 ? 375 GLU A C     1 
ATOM   2903  O O     . GLU A 1 375 ? 3.515   34.524  31.499  1.00 132.71 ? 375 GLU A O     1 
ATOM   2904  C CB    . GLU A 1 375 ? 1.283   34.787  33.422  1.00 143.31 ? 375 GLU A CB    1 
ATOM   2905  C CG    . GLU A 1 375 ? 0.194   34.260  34.334  1.00 141.61 ? 375 GLU A CG    1 
ATOM   2906  C CD    . GLU A 1 375 ? -1.153  34.935  34.196  1.00 135.59 ? 375 GLU A CD    1 
ATOM   2907  O OE1   . GLU A 1 375 ? -1.257  35.883  33.392  1.00 136.13 ? 375 GLU A OE1   1 
ATOM   2908  O OE2   . GLU A 1 375 ? -2.086  34.502  34.899  1.00 116.20 ? 375 GLU A OE2   1 
ATOM   2909  N N     . PHE A 1 376 ? 4.870   34.906  33.281  1.00 115.09 ? 376 PHE A N     1 
ATOM   2910  C CA    . PHE A 1 376 ? 6.022   35.322  32.510  1.00 105.58 ? 376 PHE A CA    1 
ATOM   2911  C C     . PHE A 1 376 ? 7.261   34.551  32.978  1.00 103.99 ? 376 PHE A C     1 
ATOM   2912  O O     . PHE A 1 376 ? 7.796   34.827  34.050  1.00 117.26 ? 376 PHE A O     1 
ATOM   2913  C CB    . PHE A 1 376 ? 6.153   36.841  32.622  1.00 108.50 ? 376 PHE A CB    1 
ATOM   2914  C CG    . PHE A 1 376 ? 7.093   37.415  31.604  1.00 115.87 ? 376 PHE A CG    1 
ATOM   2915  C CD1   . PHE A 1 376 ? 8.424   37.035  31.611  1.00 128.67 ? 376 PHE A CD1   1 
ATOM   2916  C CD2   . PHE A 1 376 ? 6.642   38.271  30.612  1.00 112.34 ? 376 PHE A CD2   1 
ATOM   2917  C CE1   . PHE A 1 376 ? 9.302   37.528  30.666  1.00 142.42 ? 376 PHE A CE1   1 
ATOM   2918  C CE2   . PHE A 1 376 ? 7.522   38.761  29.664  1.00 122.86 ? 376 PHE A CE2   1 
ATOM   2919  C CZ    . PHE A 1 376 ? 8.847   38.390  29.697  1.00 136.95 ? 376 PHE A CZ    1 
ATOM   2920  N N     . ASN A 1 377 ? 7.706   33.577  32.169  1.00 94.75  ? 377 ASN A N     1 
ATOM   2921  C CA    . ASN A 1 377 ? 8.903   32.790  32.442  1.00 93.85  ? 377 ASN A CA    1 
ATOM   2922  C C     . ASN A 1 377 ? 9.596   32.517  31.108  1.00 88.45  ? 377 ASN A C     1 
ATOM   2923  O O     . ASN A 1 377 ? 9.460   33.285  30.157  1.00 94.12  ? 377 ASN A O     1 
ATOM   2924  C CB    . ASN A 1 377 ? 8.593   31.510  33.240  1.00 96.19  ? 377 ASN A CB    1 
ATOM   2925  C CG    . ASN A 1 377 ? 7.556   30.610  32.595  1.00 97.86  ? 377 ASN A CG    1 
ATOM   2926  O OD1   . ASN A 1 377 ? 7.603   30.373  31.391  1.00 100.78 ? 377 ASN A OD1   1 
ATOM   2927  N ND2   . ASN A 1 377 ? 6.605   30.116  33.378  1.00 95.78  ? 377 ASN A ND2   1 
ATOM   2928  N N     . PHE A 1 378 ? 10.330  31.411  31.028  1.00 82.31  ? 378 PHE A N     1 
ATOM   2929  C CA    . PHE A 1 378 ? 11.083  31.118  29.823  1.00 81.43  ? 378 PHE A CA    1 
ATOM   2930  C C     . PHE A 1 378 ? 10.200  30.492  28.741  1.00 80.53  ? 378 PHE A C     1 
ATOM   2931  O O     . PHE A 1 378 ? 10.630  30.428  27.598  1.00 80.34  ? 378 PHE A O     1 
ATOM   2932  C CB    . PHE A 1 378 ? 12.307  30.260  30.159  1.00 74.80  ? 378 PHE A CB    1 
ATOM   2933  C CG    . PHE A 1 378 ? 12.016  28.983  30.905  1.00 66.77  ? 378 PHE A CG    1 
ATOM   2934  C CD1   . PHE A 1 378 ? 11.522  27.875  30.241  1.00 54.98  ? 378 PHE A CD1   1 
ATOM   2935  C CD2   . PHE A 1 378 ? 12.254  28.890  32.273  1.00 72.09  ? 378 PHE A CD2   1 
ATOM   2936  C CE1   . PHE A 1 378 ? 11.272  26.695  30.923  1.00 59.00  ? 378 PHE A CE1   1 
ATOM   2937  C CE2   . PHE A 1 378 ? 12.023  27.703  32.952  1.00 70.03  ? 378 PHE A CE2   1 
ATOM   2938  C CZ    . PHE A 1 378 ? 11.525  26.611  32.275  1.00 66.16  ? 378 PHE A CZ    1 
ATOM   2939  N N     . LEU A 1 379 ? 8.982   30.035  29.067  1.00 83.14  ? 379 LEU A N     1 
ATOM   2940  C CA    . LEU A 1 379 ? 8.094   29.472  28.052  1.00 81.48  ? 379 LEU A CA    1 
ATOM   2941  C C     . LEU A 1 379 ? 7.676   30.540  27.038  1.00 77.81  ? 379 LEU A C     1 
ATOM   2942  O O     . LEU A 1 379 ? 7.416   30.216  25.879  1.00 85.21  ? 379 LEU A O     1 
ATOM   2943  C CB    . LEU A 1 379 ? 6.852   28.870  28.715  1.00 86.62  ? 379 LEU A CB    1 
ATOM   2944  C CG    . LEU A 1 379 ? 6.966   27.417  29.165  1.00 95.46  ? 379 LEU A CG    1 
ATOM   2945  C CD1   . LEU A 1 379 ? 5.977   27.123  30.283  1.00 92.07  ? 379 LEU A CD1   1 
ATOM   2946  C CD2   . LEU A 1 379 ? 6.724   26.475  27.993  1.00 102.97 ? 379 LEU A CD2   1 
ATOM   2947  N N     . ASN A 1 380 ? 7.613   31.805  27.481  1.00 63.64  ? 380 ASN A N     1 
ATOM   2948  C CA    . ASN A 1 380 ? 7.129   32.893  26.653  1.00 67.13  ? 380 ASN A CA    1 
ATOM   2949  C C     . ASN A 1 380 ? 8.225   33.387  25.717  1.00 68.82  ? 380 ASN A C     1 
ATOM   2950  O O     . ASN A 1 380 ? 7.914   34.066  24.744  1.00 74.08  ? 380 ASN A O     1 
ATOM   2951  C CB    . ASN A 1 380 ? 6.567   34.038  27.503  1.00 81.06  ? 380 ASN A CB    1 
ATOM   2952  C CG    . ASN A 1 380 ? 5.347   33.619  28.305  1.00 90.97  ? 380 ASN A CG    1 
ATOM   2953  O OD1   . ASN A 1 380 ? 4.364   33.131  27.754  1.00 85.53  ? 380 ASN A OD1   1 
ATOM   2954  N ND2   . ASN A 1 380 ? 5.405   33.778  29.616  1.00 94.34  ? 380 ASN A ND2   1 
ATOM   2955  N N     . TRP A 1 381 ? 9.484   32.999  25.991  1.00 66.46  ? 381 TRP A N     1 
ATOM   2956  C CA    . TRP A 1 381 ? 10.661  33.540  25.326  1.00 56.12  ? 381 TRP A CA    1 
ATOM   2957  C C     . TRP A 1 381 ? 10.500  33.607  23.804  1.00 56.94  ? 381 TRP A C     1 
ATOM   2958  O O     . TRP A 1 381 ? 10.782  34.646  23.209  1.00 56.59  ? 381 TRP A O     1 
ATOM   2959  C CB    . TRP A 1 381 ? 11.922  32.758  25.720  1.00 46.20  ? 381 TRP A CB    1 
ATOM   2960  C CG    . TRP A 1 381 ? 13.155  33.184  24.980  1.00 41.44  ? 381 TRP A CG    1 
ATOM   2961  C CD1   . TRP A 1 381 ? 13.782  32.502  23.978  1.00 46.96  ? 381 TRP A CD1   1 
ATOM   2962  C CD2   . TRP A 1 381 ? 13.921  34.385  25.159  1.00 41.66  ? 381 TRP A CD2   1 
ATOM   2963  N NE1   . TRP A 1 381 ? 14.880  33.190  23.521  1.00 43.34  ? 381 TRP A NE1   1 
ATOM   2964  C CE2   . TRP A 1 381 ? 14.988  34.345  24.234  1.00 39.77  ? 381 TRP A CE2   1 
ATOM   2965  C CE3   . TRP A 1 381 ? 13.827  35.481  26.022  1.00 46.76  ? 381 TRP A CE3   1 
ATOM   2966  C CZ2   . TRP A 1 381 ? 15.927  35.357  24.131  1.00 43.51  ? 381 TRP A CZ2   1 
ATOM   2967  C CZ3   . TRP A 1 381 ? 14.760  36.488  25.922  1.00 48.04  ? 381 TRP A CZ3   1 
ATOM   2968  C CH2   . TRP A 1 381 ? 15.786  36.428  24.980  1.00 51.14  ? 381 TRP A CH2   1 
ATOM   2969  N N     . ASP A 1 382 ? 10.088  32.496  23.184  1.00 66.93  ? 382 ASP A N     1 
ATOM   2970  C CA    . ASP A 1 382 ? 10.095  32.358  21.732  1.00 72.89  ? 382 ASP A CA    1 
ATOM   2971  C C     . ASP A 1 382 ? 8.651   32.375  21.233  1.00 73.74  ? 382 ASP A C     1 
ATOM   2972  O O     . ASP A 1 382 ? 8.291   31.618  20.343  1.00 63.66  ? 382 ASP A O     1 
ATOM   2973  C CB    . ASP A 1 382 ? 10.811  31.064  21.315  1.00 76.95  ? 382 ASP A CB    1 
ATOM   2974  C CG    . ASP A 1 382 ? 11.474  31.074  19.943  1.00 76.21  ? 382 ASP A CG    1 
ATOM   2975  O OD1   . ASP A 1 382 ? 10.865  31.579  18.975  1.00 68.68  ? 382 ASP A OD1   1 
ATOM   2976  O OD2   . ASP A 1 382 ? 12.596  30.548  19.849  1.00 81.39  ? 382 ASP A OD2   1 
ATOM   2977  N N     . GLY A 1 383 ? 7.807   33.203  21.859  1.00 90.76  ? 383 GLY A N     1 
ATOM   2978  C CA    . GLY A 1 383 ? 6.416   33.345  21.452  1.00 98.24  ? 383 GLY A CA    1 
ATOM   2979  C C     . GLY A 1 383 ? 5.482   32.328  22.109  1.00 94.23  ? 383 GLY A C     1 
ATOM   2980  O O     . GLY A 1 383 ? 4.270   32.386  21.908  1.00 93.33  ? 383 GLY A O     1 
ATOM   2981  N N     . GLY A 1 384 ? 6.042   31.393  22.883  1.00 88.16  ? 384 GLY A N     1 
ATOM   2982  C CA    . GLY A 1 384 ? 5.232   30.417  23.590  1.00 85.31  ? 384 GLY A CA    1 
ATOM   2983  C C     . GLY A 1 384 ? 5.293   29.023  22.971  1.00 80.05  ? 384 GLY A C     1 
ATOM   2984  O O     . GLY A 1 384 ? 5.640   28.843  21.798  1.00 71.42  ? 384 GLY A O     1 
ATOM   2985  N N     . GLY A 1 385 ? 4.928   28.042  23.800  1.00 67.23  ? 385 GLY A N     1 
ATOM   2986  C CA    . GLY A 1 385 ? 4.743   26.675  23.354  1.00 73.55  ? 385 GLY A CA    1 
ATOM   2987  C C     . GLY A 1 385 ? 4.994   25.677  24.481  1.00 75.63  ? 385 GLY A C     1 
ATOM   2988  O O     . GLY A 1 385 ? 4.309   25.698  25.503  1.00 81.13  ? 385 GLY A O     1 
ATOM   2989  N N     . GLY A 1 386 ? 5.980   24.801  24.264  1.00 67.12  ? 386 GLY A N     1 
ATOM   2990  C CA    . GLY A 1 386 ? 6.315   23.753  25.207  1.00 67.69  ? 386 GLY A CA    1 
ATOM   2991  C C     . GLY A 1 386 ? 7.802   23.761  25.567  1.00 65.68  ? 386 GLY A C     1 
ATOM   2992  O O     . GLY A 1 386 ? 8.623   24.443  24.935  1.00 53.99  ? 386 GLY A O     1 
ATOM   2993  N N     . HIS A 1 387 ? 8.140   22.998  26.613  1.00 62.43  ? 387 HIS A N     1 
ATOM   2994  C CA    . HIS A 1 387 ? 9.535   22.838  26.962  1.00 61.40  ? 387 HIS A CA    1 
ATOM   2995  C C     . HIS A 1 387 ? 9.847   21.381  27.275  1.00 53.92  ? 387 HIS A C     1 
ATOM   2996  O O     . HIS A 1 387 ? 8.968   20.541  27.480  1.00 55.89  ? 387 HIS A O     1 
ATOM   2997  C CB    . HIS A 1 387 ? 9.945   23.879  28.005  1.00 65.56  ? 387 HIS A CB    1 
ATOM   2998  C CG    . HIS A 1 387 ? 9.681   23.494  29.409  1.00 75.05  ? 387 HIS A CG    1 
ATOM   2999  N ND1   . HIS A 1 387 ? 10.726  23.290  30.287  1.00 72.35  ? 387 HIS A ND1   1 
ATOM   3000  C CD2   . HIS A 1 387 ? 8.552   23.271  30.086  1.00 74.40  ? 387 HIS A CD2   1 
ATOM   3001  C CE1   . HIS A 1 387 ? 10.236  22.973  31.470  1.00 78.33  ? 387 HIS A CE1   1 
ATOM   3002  N NE2   . HIS A 1 387 ? 8.927   22.960  31.366  1.00 79.61  ? 387 HIS A NE2   1 
ATOM   3003  N N     . VAL A 1 388 ? 11.137  21.090  27.163  1.00 56.35  ? 388 VAL A N     1 
ATOM   3004  C CA    . VAL A 1 388 ? 11.710  19.839  27.623  1.00 58.05  ? 388 VAL A CA    1 
ATOM   3005  C C     . VAL A 1 388 ? 13.064  20.184  28.252  1.00 48.58  ? 388 VAL A C     1 
ATOM   3006  O O     . VAL A 1 388 ? 13.620  21.265  28.042  1.00 47.02  ? 388 VAL A O     1 
ATOM   3007  C CB    . VAL A 1 388 ? 11.774  18.806  26.473  1.00 60.90  ? 388 VAL A CB    1 
ATOM   3008  C CG1   . VAL A 1 388 ? 12.931  19.073  25.524  1.00 68.62  ? 388 VAL A CG1   1 
ATOM   3009  C CG2   . VAL A 1 388 ? 11.815  17.372  26.981  1.00 61.13  ? 388 VAL A CG2   1 
ATOM   3010  N N     . GLY A 1 389 ? 13.539  19.307  29.128  1.00 47.93  ? 389 GLY A N     1 
ATOM   3011  C CA    . GLY A 1 389 ? 14.743  19.598  29.875  1.00 41.03  ? 389 GLY A CA    1 
ATOM   3012  C C     . GLY A 1 389 ? 15.582  18.344  29.938  1.00 40.90  ? 389 GLY A C     1 
ATOM   3013  O O     . GLY A 1 389 ? 15.021  17.256  29.978  1.00 36.69  ? 389 GLY A O     1 
ATOM   3014  N N     . PHE A 1 390 ? 16.887  18.536  29.759  1.00 43.74  ? 390 PHE A N     1 
ATOM   3015  C CA    . PHE A 1 390 ? 17.865  17.486  29.908  1.00 43.31  ? 390 PHE A CA    1 
ATOM   3016  C C     . PHE A 1 390 ? 18.748  17.871  31.087  1.00 42.64  ? 390 PHE A C     1 
ATOM   3017  O O     . PHE A 1 390 ? 19.385  18.917  31.027  1.00 40.95  ? 390 PHE A O     1 
ATOM   3018  C CB    . PHE A 1 390 ? 18.632  17.365  28.596  1.00 40.51  ? 390 PHE A CB    1 
ATOM   3019  C CG    . PHE A 1 390 ? 19.619  16.237  28.560  1.00 38.86  ? 390 PHE A CG    1 
ATOM   3020  C CD1   . PHE A 1 390 ? 19.200  14.954  28.882  1.00 42.12  ? 390 PHE A CD1   1 
ATOM   3021  C CD2   . PHE A 1 390 ? 20.950  16.450  28.218  1.00 37.57  ? 390 PHE A CD2   1 
ATOM   3022  C CE1   . PHE A 1 390 ? 20.092  13.890  28.849  1.00 44.23  ? 390 PHE A CE1   1 
ATOM   3023  C CE2   . PHE A 1 390 ? 21.834  15.381  28.166  1.00 42.09  ? 390 PHE A CE2   1 
ATOM   3024  C CZ    . PHE A 1 390 ? 21.404  14.103  28.482  1.00 42.33  ? 390 PHE A CZ    1 
ATOM   3025  N N     . SER A 1 391 ? 18.783  17.050  32.149  1.00 44.89  ? 391 SER A N     1 
ATOM   3026  C CA    . SER A 1 391 ? 19.437  17.462  33.397  1.00 47.37  ? 391 SER A CA    1 
ATOM   3027  C C     . SER A 1 391 ? 20.413  16.400  33.943  1.00 41.39  ? 391 SER A C     1 
ATOM   3028  O O     . SER A 1 391 ? 20.366  15.957  35.087  1.00 34.60  ? 391 SER A O     1 
ATOM   3029  C CB    . SER A 1 391 ? 18.365  17.852  34.391  1.00 41.66  ? 391 SER A CB    1 
ATOM   3030  O OG    . SER A 1 391 ? 17.480  16.763  34.567  1.00 38.45  ? 391 SER A OG    1 
ATOM   3031  N N     . PRO A 1 392 ? 21.387  15.943  33.144  1.00 42.96  ? 392 PRO A N     1 
ATOM   3032  C CA    . PRO A 1 392 ? 22.205  14.795  33.537  1.00 40.04  ? 392 PRO A CA    1 
ATOM   3033  C C     . PRO A 1 392 ? 23.189  15.135  34.645  1.00 35.56  ? 392 PRO A C     1 
ATOM   3034  O O     . PRO A 1 392 ? 23.462  16.313  34.891  1.00 37.86  ? 392 PRO A O     1 
ATOM   3035  C CB    . PRO A 1 392 ? 22.928  14.485  32.233  1.00 38.68  ? 392 PRO A CB    1 
ATOM   3036  C CG    . PRO A 1 392 ? 23.084  15.848  31.605  1.00 39.82  ? 392 PRO A CG    1 
ATOM   3037  C CD    . PRO A 1 392 ? 21.728  16.470  31.824  1.00 43.37  ? 392 PRO A CD    1 
ATOM   3038  N N     . VAL A 1 393 ? 23.759  14.094  35.266  1.00 35.48  ? 393 VAL A N     1 
ATOM   3039  C CA    . VAL A 1 393 ? 24.672  14.265  36.398  1.00 36.83  ? 393 VAL A CA    1 
ATOM   3040  C C     . VAL A 1 393 ? 26.133  14.227  35.939  1.00 36.84  ? 393 VAL A C     1 
ATOM   3041  O O     . VAL A 1 393 ? 26.522  13.424  35.109  1.00 41.37  ? 393 VAL A O     1 
ATOM   3042  C CB    . VAL A 1 393 ? 24.476  13.178  37.461  1.00 41.27  ? 393 VAL A CB    1 
ATOM   3043  C CG1   . VAL A 1 393 ? 25.299  13.521  38.675  1.00 48.39  ? 393 VAL A CG1   1 
ATOM   3044  C CG2   . VAL A 1 393 ? 23.021  12.955  37.846  1.00 45.70  ? 393 VAL A CG2   1 
ATOM   3045  N N     . SER A 1 394 ? 26.963  15.010  36.610  1.00 37.73  ? 394 SER A N     1 
ATOM   3046  C CA    . SER A 1 394 ? 28.372  15.133  36.303  1.00 35.51  ? 394 SER A CA    1 
ATOM   3047  C C     . SER A 1 394 ? 29.138  15.524  37.571  1.00 31.95  ? 394 SER A C     1 
ATOM   3048  O O     . SER A 1 394 ? 28.588  16.052  38.515  1.00 31.61  ? 394 SER A O     1 
ATOM   3049  C CB    . SER A 1 394 ? 28.584  16.176  35.243  1.00 38.78  ? 394 SER A CB    1 
ATOM   3050  O OG    . SER A 1 394 ? 27.811  17.331  35.514  1.00 45.88  ? 394 SER A OG    1 
ATOM   3051  N N     . PRO A 1 395 ? 30.460  15.337  37.627  1.00 29.96  ? 395 PRO A N     1 
ATOM   3052  C CA    . PRO A 1 395 ? 31.252  15.815  38.757  1.00 32.60  ? 395 PRO A CA    1 
ATOM   3053  C C     . PRO A 1 395 ? 31.377  17.346  38.742  1.00 41.52  ? 395 PRO A C     1 
ATOM   3054  O O     . PRO A 1 395 ? 31.422  17.966  37.680  1.00 45.99  ? 395 PRO A O     1 
ATOM   3055  C CB    . PRO A 1 395 ? 32.613  15.131  38.550  1.00 31.32  ? 395 PRO A CB    1 
ATOM   3056  C CG    . PRO A 1 395 ? 32.381  14.054  37.500  1.00 34.39  ? 395 PRO A CG    1 
ATOM   3057  C CD    . PRO A 1 395 ? 31.250  14.594  36.645  1.00 35.70  ? 395 PRO A CD    1 
ATOM   3058  N N     . ILE A 1 396 ? 31.399  17.966  39.926  1.00 41.97  ? 396 ILE A N     1 
ATOM   3059  C CA    . ILE A 1 396 ? 31.498  19.414  40.024  1.00 37.99  ? 396 ILE A CA    1 
ATOM   3060  C C     . ILE A 1 396 ? 32.925  19.846  39.690  1.00 38.43  ? 396 ILE A C     1 
ATOM   3061  O O     . ILE A 1 396 ? 33.784  19.981  40.581  1.00 38.09  ? 396 ILE A O     1 
ATOM   3062  C CB    . ILE A 1 396 ? 31.119  19.951  41.420  1.00 33.15  ? 396 ILE A CB    1 
ATOM   3063  C CG1   . ILE A 1 396 ? 29.944  19.261  42.089  1.00 37.51  ? 396 ILE A CG1   1 
ATOM   3064  C CG2   . ILE A 1 396 ? 30.841  21.429  41.318  1.00 41.03  ? 396 ILE A CG2   1 
ATOM   3065  C CD1   . ILE A 1 396 ? 29.735  19.720  43.525  1.00 36.74  ? 396 ILE A CD1   1 
ATOM   3066  N N     . THR A 1 397 ? 33.147  20.125  38.410  1.00 42.66  ? 397 THR A N     1 
ATOM   3067  C CA    . THR A 1 397 ? 34.462  20.467  37.882  1.00 44.84  ? 397 THR A CA    1 
ATOM   3068  C C     . THR A 1 397 ? 34.291  21.501  36.780  1.00 43.54  ? 397 THR A C     1 
ATOM   3069  O O     . THR A 1 397 ? 33.345  21.405  36.000  1.00 46.29  ? 397 THR A O     1 
ATOM   3070  C CB    . THR A 1 397 ? 35.154  19.210  37.343  1.00 50.45  ? 397 THR A CB    1 
ATOM   3071  O OG1   . THR A 1 397 ? 35.748  18.520  38.448  1.00 48.70  ? 397 THR A OG1   1 
ATOM   3072  C CG2   . THR A 1 397 ? 36.231  19.499  36.331  1.00 59.30  ? 397 THR A CG2   1 
ATOM   3073  N N     . GLY A 1 398 ? 35.197  22.486  36.737  1.00 46.49  ? 398 GLY A N     1 
ATOM   3074  C CA    . GLY A 1 398 ? 35.295  23.445  35.640  1.00 42.69  ? 398 GLY A CA    1 
ATOM   3075  C C     . GLY A 1 398 ? 35.259  22.774  34.258  1.00 46.57  ? 398 GLY A C     1 
ATOM   3076  O O     . GLY A 1 398 ? 34.532  23.210  33.366  1.00 50.41  ? 398 GLY A O     1 
ATOM   3077  N N     . LYS A 1 399 ? 36.041  21.699  34.095  1.00 46.98  ? 399 LYS A N     1 
ATOM   3078  C CA    . LYS A 1 399 ? 36.210  21.018  32.819  1.00 46.46  ? 399 LYS A CA    1 
ATOM   3079  C C     . LYS A 1 399 ? 34.909  20.333  32.376  1.00 41.25  ? 399 LYS A C     1 
ATOM   3080  O O     . LYS A 1 399 ? 34.590  20.310  31.189  1.00 48.15  ? 399 LYS A O     1 
ATOM   3081  C CB    . LYS A 1 399 ? 37.405  20.070  32.959  1.00 52.41  ? 399 LYS A CB    1 
ATOM   3082  C CG    . LYS A 1 399 ? 37.786  19.275  31.710  1.00 71.25  ? 399 LYS A CG    1 
ATOM   3083  C CD    . LYS A 1 399 ? 38.519  17.935  31.954  1.00 75.15  ? 399 LYS A CD    1 
ATOM   3084  C CE    . LYS A 1 399 ? 37.698  16.882  32.679  1.00 83.34  ? 399 LYS A CE    1 
ATOM   3085  N NZ    . LYS A 1 399 ? 36.606  16.332  31.834  1.00 85.98  ? 399 LYS A NZ    1 
ATOM   3086  N N     . ASP A 1 400 ? 34.160  19.776  33.330  1.00 35.59  ? 400 ASP A N     1 
ATOM   3087  C CA    . ASP A 1 400 ? 32.932  19.055  33.077  1.00 39.49  ? 400 ASP A CA    1 
ATOM   3088  C C     . ASP A 1 400 ? 31.792  20.007  32.705  1.00 45.03  ? 400 ASP A C     1 
ATOM   3089  O O     . ASP A 1 400 ? 30.987  19.732  31.808  1.00 43.16  ? 400 ASP A O     1 
ATOM   3090  C CB    . ASP A 1 400 ? 32.563  18.244  34.311  1.00 43.00  ? 400 ASP A CB    1 
ATOM   3091  C CG    . ASP A 1 400 ? 33.323  16.938  34.408  1.00 46.04  ? 400 ASP A CG    1 
ATOM   3092  O OD1   . ASP A 1 400 ? 33.129  16.134  33.494  1.00 41.81  ? 400 ASP A OD1   1 
ATOM   3093  O OD2   . ASP A 1 400 ? 34.094  16.734  35.416  1.00 48.01  ? 400 ASP A OD2   1 
ATOM   3094  N N     . ALA A 1 401 ? 31.741  21.143  33.406  1.00 44.60  ? 401 ALA A N     1 
ATOM   3095  C CA    . ALA A 1 401 ? 30.814  22.212  33.085  1.00 40.31  ? 401 ALA A CA    1 
ATOM   3096  C C     . ALA A 1 401 ? 31.063  22.786  31.682  1.00 39.75  ? 401 ALA A C     1 
ATOM   3097  O O     . ALA A 1 401 ? 30.168  22.798  30.855  1.00 43.71  ? 401 ALA A O     1 
ATOM   3098  C CB    . ALA A 1 401 ? 30.958  23.259  34.147  1.00 46.41  ? 401 ALA A CB    1 
ATOM   3099  N N     . ILE A 1 402 ? 32.256  23.324  31.432  1.00 37.44  ? 402 ILE A N     1 
ATOM   3100  C CA    . ILE A 1 402 ? 32.560  23.971  30.179  1.00 43.37  ? 402 ILE A CA    1 
ATOM   3101  C C     . ILE A 1 402 ? 32.352  22.978  29.030  1.00 46.51  ? 402 ILE A C     1 
ATOM   3102  O O     . ILE A 1 402 ? 31.906  23.337  27.940  1.00 47.49  ? 402 ILE A O     1 
ATOM   3103  C CB    . ILE A 1 402 ? 33.998  24.521  30.211  1.00 52.96  ? 402 ILE A CB    1 
ATOM   3104  C CG1   . ILE A 1 402 ? 34.270  25.467  29.039  1.00 59.17  ? 402 ILE A CG1   1 
ATOM   3105  C CG2   . ILE A 1 402 ? 35.024  23.400  30.255  1.00 49.53  ? 402 ILE A CG2   1 
ATOM   3106  C CD1   . ILE A 1 402 ? 34.009  26.913  29.339  1.00 63.59  ? 402 ILE A CD1   1 
ATOM   3107  N N     . LYS A 1 403 ? 32.666  21.707  29.268  1.00 43.18  ? 403 LYS A N     1 
ATOM   3108  C CA    . LYS A 1 403 ? 32.528  20.738  28.213  1.00 41.91  ? 403 LYS A CA    1 
ATOM   3109  C C     . LYS A 1 403 ? 31.045  20.616  27.884  1.00 39.11  ? 403 LYS A C     1 
ATOM   3110  O O     . LYS A 1 403 ? 30.654  20.712  26.718  1.00 37.00  ? 403 LYS A O     1 
ATOM   3111  C CB    . LYS A 1 403 ? 33.144  19.399  28.622  1.00 49.93  ? 403 LYS A CB    1 
ATOM   3112  C CG    . LYS A 1 403 ? 33.158  18.340  27.524  1.00 53.77  ? 403 LYS A CG    1 
ATOM   3113  C CD    . LYS A 1 403 ? 33.216  16.930  28.061  1.00 62.89  ? 403 LYS A CD    1 
ATOM   3114  C CE    . LYS A 1 403 ? 34.481  16.607  28.834  1.00 71.51  ? 403 LYS A CE    1 
ATOM   3115  N NZ    . LYS A 1 403 ? 34.416  15.266  29.467  1.00 69.20  ? 403 LYS A NZ    1 
ATOM   3116  N N     . GLN A 1 404 ? 30.222  20.406  28.921  1.00 39.29  ? 404 GLN A N     1 
ATOM   3117  C CA    . GLN A 1 404 ? 28.790  20.252  28.707  1.00 40.96  ? 404 GLN A CA    1 
ATOM   3118  C C     . GLN A 1 404 ? 28.242  21.500  28.021  1.00 48.92  ? 404 GLN A C     1 
ATOM   3119  O O     . GLN A 1 404 ? 27.513  21.375  27.045  1.00 52.05  ? 404 GLN A O     1 
ATOM   3120  C CB    . GLN A 1 404 ? 28.077  19.910  30.007  1.00 41.41  ? 404 GLN A CB    1 
ATOM   3121  C CG    . GLN A 1 404 ? 28.053  18.413  30.275  1.00 38.94  ? 404 GLN A CG    1 
ATOM   3122  C CD    . GLN A 1 404 ? 27.643  18.187  31.704  1.00 39.93  ? 404 GLN A CD    1 
ATOM   3123  O OE1   . GLN A 1 404 ? 28.417  18.473  32.623  1.00 37.68  ? 404 GLN A OE1   1 
ATOM   3124  N NE2   . GLN A 1 404 ? 26.428  17.684  31.897  1.00 44.32  ? 404 GLN A NE2   1 
ATOM   3125  N N     . TYR A 1 405 ? 28.669  22.693  28.470  1.00 46.79  ? 405 TYR A N     1 
ATOM   3126  C CA    . TYR A 1 405 ? 28.197  23.936  27.887  1.00 45.35  ? 405 TYR A CA    1 
ATOM   3127  C C     . TYR A 1 405 ? 28.513  23.962  26.391  1.00 44.69  ? 405 TYR A C     1 
ATOM   3128  O O     . TYR A 1 405 ? 27.642  24.271  25.570  1.00 42.42  ? 405 TYR A O     1 
ATOM   3129  C CB    . TYR A 1 405 ? 28.794  25.130  28.636  1.00 48.97  ? 405 TYR A CB    1 
ATOM   3130  C CG    . TYR A 1 405 ? 28.733  26.427  27.868  1.00 58.41  ? 405 TYR A CG    1 
ATOM   3131  C CD1   . TYR A 1 405 ? 27.524  27.065  27.639  1.00 53.31  ? 405 TYR A CD1   1 
ATOM   3132  C CD2   . TYR A 1 405 ? 29.888  26.988  27.335  1.00 57.00  ? 405 TYR A CD2   1 
ATOM   3133  C CE1   . TYR A 1 405 ? 27.462  28.231  26.897  1.00 55.10  ? 405 TYR A CE1   1 
ATOM   3134  C CE2   . TYR A 1 405 ? 29.841  28.162  26.608  1.00 59.66  ? 405 TYR A CE2   1 
ATOM   3135  C CZ    . TYR A 1 405 ? 28.622  28.775  26.377  1.00 59.85  ? 405 TYR A CZ    1 
ATOM   3136  O OH    . TYR A 1 405 ? 28.594  29.928  25.635  1.00 56.99  ? 405 TYR A OH    1 
ATOM   3137  N N     . ASN A 1 406 ? 29.762  23.623  26.053  1.00 40.02  ? 406 ASN A N     1 
ATOM   3138  C CA    . ASN A 1 406 ? 30.226  23.716  24.675  1.00 39.30  ? 406 ASN A CA    1 
ATOM   3139  C C     . ASN A 1 406 ? 29.445  22.757  23.792  1.00 40.96  ? 406 ASN A C     1 
ATOM   3140  O O     . ASN A 1 406 ? 28.955  23.193  22.753  1.00 42.58  ? 406 ASN A O     1 
ATOM   3141  C CB    . ASN A 1 406 ? 31.731  23.513  24.560  1.00 39.29  ? 406 ASN A CB    1 
ATOM   3142  C CG    . ASN A 1 406 ? 32.496  24.750  24.982  1.00 44.05  ? 406 ASN A CG    1 
ATOM   3143  O OD1   . ASN A 1 406 ? 32.060  25.880  24.758  1.00 51.28  ? 406 ASN A OD1   1 
ATOM   3144  N ND2   . ASN A 1 406 ? 33.635  24.563  25.613  1.00 44.25  ? 406 ASN A ND2   1 
ATOM   3145  N N     . MET A 1 407 ? 29.265  21.507  24.260  1.00 40.35  ? 407 MET A N     1 
ATOM   3146  C CA    . MET A 1 407 ? 28.596  20.444  23.517  1.00 42.08  ? 407 MET A CA    1 
ATOM   3147  C C     . MET A 1 407 ? 27.133  20.798  23.229  1.00 42.64  ? 407 MET A C     1 
ATOM   3148  O O     . MET A 1 407 ? 26.629  20.539  22.135  1.00 48.25  ? 407 MET A O     1 
ATOM   3149  C CB    . MET A 1 407 ? 28.515  19.138  24.332  1.00 48.20  ? 407 MET A CB    1 
ATOM   3150  C CG    . MET A 1 407 ? 29.797  18.454  24.648  1.00 49.97  ? 407 MET A CG    1 
ATOM   3151  S SD    . MET A 1 407 ? 29.500  17.089  25.798  1.00 57.09  ? 407 MET A SD    1 
ATOM   3152  C CE    . MET A 1 407 ? 28.897  15.819  24.685  1.00 49.06  ? 407 MET A CE    1 
ATOM   3153  N N     . VAL A 1 408 ? 26.427  21.265  24.268  1.00 37.61  ? 408 VAL A N     1 
ATOM   3154  C CA    . VAL A 1 408 ? 24.997  21.516  24.195  1.00 46.07  ? 408 VAL A CA    1 
ATOM   3155  C C     . VAL A 1 408 ? 24.705  22.817  23.438  1.00 48.86  ? 408 VAL A C     1 
ATOM   3156  O O     . VAL A 1 408 ? 23.910  22.816  22.491  1.00 41.13  ? 408 VAL A O     1 
ATOM   3157  C CB    . VAL A 1 408 ? 24.373  21.533  25.599  1.00 44.51  ? 408 VAL A CB    1 
ATOM   3158  C CG1   . VAL A 1 408 ? 22.914  21.922  25.546  1.00 47.43  ? 408 VAL A CG1   1 
ATOM   3159  C CG2   . VAL A 1 408 ? 24.521  20.176  26.278  1.00 44.60  ? 408 VAL A CG2   1 
ATOM   3160  N N     . SER A 1 409 ? 25.350  23.921  23.847  1.00 43.95  ? 409 SER A N     1 
ATOM   3161  C CA    . SER A 1 409 ? 25.120  25.187  23.163  1.00 45.88  ? 409 SER A CA    1 
ATOM   3162  C C     . SER A 1 409 ? 25.407  25.071  21.656  1.00 46.01  ? 409 SER A C     1 
ATOM   3163  O O     . SER A 1 409 ? 24.647  25.592  20.871  1.00 44.27  ? 409 SER A O     1 
ATOM   3164  C CB    . SER A 1 409 ? 25.871  26.324  23.801  1.00 44.35  ? 409 SER A CB    1 
ATOM   3165  O OG    . SER A 1 409 ? 27.265  26.192  23.594  1.00 52.27  ? 409 SER A OG    1 
ATOM   3166  N N     . SER A 1 410 ? 26.446  24.351  21.228  1.00 48.97  ? 410 SER A N     1 
ATOM   3167  C CA    . SER A 1 410 ? 26.709  24.193  19.804  1.00 53.14  ? 410 SER A CA    1 
ATOM   3168  C C     . SER A 1 410 ? 25.530  23.541  19.095  1.00 49.98  ? 410 SER A C     1 
ATOM   3169  O O     . SER A 1 410 ? 25.105  24.000  18.044  1.00 47.62  ? 410 SER A O     1 
ATOM   3170  C CB    . SER A 1 410 ? 27.924  23.373  19.548  1.00 54.21  ? 410 SER A CB    1 
ATOM   3171  O OG    . SER A 1 410 ? 29.003  23.935  20.242  1.00 64.07  ? 410 SER A OG    1 
ATOM   3172  N N     . ARG A 1 411 ? 25.045  22.440  19.653  1.00 44.96  ? 411 ARG A N     1 
ATOM   3173  C CA    . ARG A 1 411 ? 24.053  21.660  18.954  1.00 44.66  ? 411 ARG A CA    1 
ATOM   3174  C C     . ARG A 1 411 ? 22.722  22.387  19.003  1.00 42.87  ? 411 ARG A C     1 
ATOM   3175  O O     . ARG A 1 411 ? 22.038  22.466  18.003  1.00 50.46  ? 411 ARG A O     1 
ATOM   3176  C CB    . ARG A 1 411 ? 23.977  20.244  19.538  1.00 48.21  ? 411 ARG A CB    1 
ATOM   3177  C CG    . ARG A 1 411 ? 25.169  19.380  19.141  1.00 46.75  ? 411 ARG A CG    1 
ATOM   3178  C CD    . ARG A 1 411 ? 24.725  17.987  18.765  1.00 48.38  ? 411 ARG A CD    1 
ATOM   3179  N NE    . ARG A 1 411 ? 25.782  17.152  18.214  1.00 51.09  ? 411 ARG A NE    1 
ATOM   3180  C CZ    . ARG A 1 411 ? 25.884  16.817  16.929  1.00 50.54  ? 411 ARG A CZ    1 
ATOM   3181  N NH1   . ARG A 1 411 ? 25.354  17.577  15.996  1.00 44.10  ? 411 ARG A NH1   1 
ATOM   3182  N NH2   . ARG A 1 411 ? 26.575  15.755  16.569  1.00 56.71  ? 411 ARG A NH2   1 
ATOM   3183  N N     . VAL A 1 412 ? 22.357  22.866  20.187  1.00 45.31  ? 412 VAL A N     1 
ATOM   3184  C CA    . VAL A 1 412 ? 21.113  23.586  20.403  1.00 45.89  ? 412 VAL A CA    1 
ATOM   3185  C C     . VAL A 1 412 ? 20.988  24.762  19.419  1.00 43.27  ? 412 VAL A C     1 
ATOM   3186  O O     . VAL A 1 412 ? 19.928  24.921  18.800  1.00 37.95  ? 412 VAL A O     1 
ATOM   3187  C CB    . VAL A 1 412 ? 21.025  24.034  21.875  1.00 42.31  ? 412 VAL A CB    1 
ATOM   3188  C CG1   . VAL A 1 412 ? 20.010  25.130  22.078  1.00 54.18  ? 412 VAL A CG1   1 
ATOM   3189  C CG2   . VAL A 1 412 ? 20.726  22.871  22.797  1.00 42.11  ? 412 VAL A CG2   1 
ATOM   3190  N N     . ARG A 1 413 ? 22.065  25.554  19.269  1.00 37.77  ? 413 ARG A N     1 
ATOM   3191  C CA    . ARG A 1 413 ? 22.087  26.699  18.368  1.00 44.28  ? 413 ARG A CA    1 
ATOM   3192  C C     . ARG A 1 413 ? 22.094  26.267  16.899  1.00 48.05  ? 413 ARG A C     1 
ATOM   3193  O O     . ARG A 1 413 ? 21.493  26.929  16.064  1.00 48.70  ? 413 ARG A O     1 
ATOM   3194  C CB    . ARG A 1 413 ? 23.249  27.642  18.696  1.00 43.70  ? 413 ARG A CB    1 
ATOM   3195  C CG    . ARG A 1 413 ? 22.992  28.479  19.945  1.00 51.46  ? 413 ARG A CG    1 
ATOM   3196  C CD    . ARG A 1 413 ? 24.188  29.181  20.569  1.00 51.53  ? 413 ARG A CD    1 
ATOM   3197  N NE    . ARG A 1 413 ? 24.641  30.252  19.689  1.00 68.18  ? 413 ARG A NE    1 
ATOM   3198  C CZ    . ARG A 1 413 ? 24.059  31.442  19.506  1.00 71.00  ? 413 ARG A CZ    1 
ATOM   3199  N NH1   . ARG A 1 413 ? 23.045  31.838  20.261  1.00 75.59  ? 413 ARG A NH1   1 
ATOM   3200  N NH2   . ARG A 1 413 ? 24.540  32.259  18.582  1.00 70.58  ? 413 ARG A NH2   1 
ATOM   3201  N N     . GLU A 1 414 ? 22.692  25.116  16.585  1.00 55.66  ? 414 GLU A N     1 
ATOM   3202  C CA    . GLU A 1 414 ? 22.726  24.666  15.205  1.00 53.15  ? 414 GLU A CA    1 
ATOM   3203  C C     . GLU A 1 414 ? 21.300  24.357  14.734  1.00 49.40  ? 414 GLU A C     1 
ATOM   3204  O O     . GLU A 1 414 ? 20.968  24.574  13.567  1.00 47.21  ? 414 GLU A O     1 
ATOM   3205  C CB    . GLU A 1 414 ? 23.659  23.471  15.037  1.00 53.43  ? 414 GLU A CB    1 
ATOM   3206  C CG    . GLU A 1 414 ? 24.114  23.301  13.592  1.00 67.00  ? 414 GLU A CG    1 
ATOM   3207  C CD    . GLU A 1 414 ? 24.463  21.887  13.155  1.00 71.93  ? 414 GLU A CD    1 
ATOM   3208  O OE1   . GLU A 1 414 ? 24.796  21.053  14.035  1.00 89.65  ? 414 GLU A OE1   1 
ATOM   3209  O OE2   . GLU A 1 414 ? 24.364  21.616  11.943  1.00 55.50  ? 414 GLU A OE2   1 
ATOM   3210  N N     . TYR A 1 415 ? 20.450  23.893  15.660  1.00 45.48  ? 415 TYR A N     1 
ATOM   3211  C CA    . TYR A 1 415 ? 19.075  23.527  15.342  1.00 43.33  ? 415 TYR A CA    1 
ATOM   3212  C C     . TYR A 1 415 ? 18.129  24.727  15.409  1.00 38.23  ? 415 TYR A C     1 
ATOM   3213  O O     . TYR A 1 415 ? 16.969  24.533  15.146  1.00 42.11  ? 415 TYR A O     1 
ATOM   3214  C CB    . TYR A 1 415 ? 18.581  22.399  16.247  1.00 41.04  ? 415 TYR A CB    1 
ATOM   3215  C CG    . TYR A 1 415 ? 19.037  21.022  15.850  1.00 36.90  ? 415 TYR A CG    1 
ATOM   3216  C CD1   . TYR A 1 415 ? 20.382  20.702  15.841  1.00 40.43  ? 415 TYR A CD1   1 
ATOM   3217  C CD2   . TYR A 1 415 ? 18.133  20.038  15.477  1.00 41.10  ? 415 TYR A CD2   1 
ATOM   3218  C CE1   . TYR A 1 415 ? 20.828  19.431  15.504  1.00 43.93  ? 415 TYR A CE1   1 
ATOM   3219  C CE2   . TYR A 1 415 ? 18.559  18.752  15.158  1.00 47.64  ? 415 TYR A CE2   1 
ATOM   3220  C CZ    . TYR A 1 415 ? 19.916  18.451  15.156  1.00 47.27  ? 415 TYR A CZ    1 
ATOM   3221  O OH    . TYR A 1 415 ? 20.405  17.212  14.805  1.00 55.70  ? 415 TYR A OH    1 
ATOM   3222  N N     . GLY A 1 416 ? 18.620  25.958  15.671  1.00 46.70  ? 416 GLY A N     1 
ATOM   3223  C CA    . GLY A 1 416 ? 17.818  27.174  15.555  1.00 48.39  ? 416 GLY A CA    1 
ATOM   3224  C C     . GLY A 1 416 ? 17.286  27.732  16.887  1.00 52.67  ? 416 GLY A C     1 
ATOM   3225  O O     . GLY A 1 416 ? 16.813  28.875  16.946  1.00 50.36  ? 416 GLY A O     1 
ATOM   3226  N N     . PHE A 1 417 ? 17.374  26.917  17.948  1.00 50.36  ? 417 PHE A N     1 
ATOM   3227  C CA    . PHE A 1 417 ? 16.901  27.236  19.284  1.00 44.94  ? 417 PHE A CA    1 
ATOM   3228  C C     . PHE A 1 417 ? 17.917  28.115  20.002  1.00 49.26  ? 417 PHE A C     1 
ATOM   3229  O O     . PHE A 1 417 ? 19.081  28.179  19.605  1.00 46.71  ? 417 PHE A O     1 
ATOM   3230  C CB    . PHE A 1 417 ? 16.710  25.944  20.077  1.00 43.73  ? 417 PHE A CB    1 
ATOM   3231  C CG    . PHE A 1 417 ? 15.761  24.935  19.472  1.00 42.93  ? 417 PHE A CG    1 
ATOM   3232  C CD1   . PHE A 1 417 ? 14.388  25.156  19.429  1.00 45.76  ? 417 PHE A CD1   1 
ATOM   3233  C CD2   . PHE A 1 417 ? 16.233  23.733  18.970  1.00 48.15  ? 417 PHE A CD2   1 
ATOM   3234  C CE1   . PHE A 1 417 ? 13.520  24.206  18.903  1.00 41.97  ? 417 PHE A CE1   1 
ATOM   3235  C CE2   . PHE A 1 417 ? 15.371  22.784  18.436  1.00 42.59  ? 417 PHE A CE2   1 
ATOM   3236  C CZ    . PHE A 1 417 ? 14.017  23.015  18.418  1.00 44.09  ? 417 PHE A CZ    1 
ATOM   3237  N N     . ASP A 1 418 ? 17.475  28.802  21.065  1.00 51.61  ? 418 ASP A N     1 
ATOM   3238  C CA    . ASP A 1 418 ? 18.418  29.519  21.911  1.00 47.09  ? 418 ASP A CA    1 
ATOM   3239  C C     . ASP A 1 418 ? 18.936  28.573  22.995  1.00 47.99  ? 418 ASP A C     1 
ATOM   3240  O O     . ASP A 1 418 ? 18.231  27.664  23.438  1.00 44.02  ? 418 ASP A O     1 
ATOM   3241  C CB    . ASP A 1 418 ? 17.826  30.784  22.526  1.00 48.18  ? 418 ASP A CB    1 
ATOM   3242  C CG    . ASP A 1 418 ? 17.900  32.031  21.663  1.00 49.09  ? 418 ASP A CG    1 
ATOM   3243  O OD1   . ASP A 1 418 ? 19.019  32.555  21.496  1.00 48.44  ? 418 ASP A OD1   1 
ATOM   3244  O OD2   . ASP A 1 418 ? 16.826  32.475  21.191  1.00 48.60  ? 418 ASP A OD2   1 
ATOM   3245  N N     . TYR A 1 419 ? 20.192  28.794  23.391  1.00 45.00  ? 419 TYR A N     1 
ATOM   3246  C CA    . TYR A 1 419 ? 20.786  28.077  24.496  1.00 43.84  ? 419 TYR A CA    1 
ATOM   3247  C C     . TYR A 1 419 ? 20.220  28.637  25.795  1.00 38.95  ? 419 TYR A C     1 
ATOM   3248  O O     . TYR A 1 419 ? 20.358  29.809  26.109  1.00 39.49  ? 419 TYR A O     1 
ATOM   3249  C CB    . TYR A 1 419 ? 22.317  28.161  24.464  1.00 42.44  ? 419 TYR A CB    1 
ATOM   3250  C CG    . TYR A 1 419 ? 22.943  27.562  25.692  1.00 44.53  ? 419 TYR A CG    1 
ATOM   3251  C CD1   . TYR A 1 419 ? 22.806  26.212  25.998  1.00 44.69  ? 419 TYR A CD1   1 
ATOM   3252  C CD2   . TYR A 1 419 ? 23.594  28.367  26.609  1.00 47.29  ? 419 TYR A CD2   1 
ATOM   3253  C CE1   . TYR A 1 419 ? 23.342  25.685  27.168  1.00 46.37  ? 419 TYR A CE1   1 
ATOM   3254  C CE2   . TYR A 1 419 ? 24.152  27.849  27.765  1.00 49.71  ? 419 TYR A CE2   1 
ATOM   3255  C CZ    . TYR A 1 419 ? 24.024  26.504  28.055  1.00 49.03  ? 419 TYR A CZ    1 
ATOM   3256  O OH    . TYR A 1 419 ? 24.615  26.047  29.225  1.00 52.10  ? 419 TYR A OH    1 
ATOM   3257  N N     . MET A 1 420 ? 19.519  27.778  26.521  1.00 45.61  ? 420 MET A N     1 
ATOM   3258  C CA    . MET A 1 420 ? 19.028  28.101  27.848  1.00 46.49  ? 420 MET A CA    1 
ATOM   3259  C C     . MET A 1 420 ? 19.607  27.057  28.798  1.00 41.33  ? 420 MET A C     1 
ATOM   3260  O O     . MET A 1 420 ? 19.150  25.930  28.853  1.00 38.52  ? 420 MET A O     1 
ATOM   3261  C CB    . MET A 1 420 ? 17.494  28.080  27.893  1.00 51.44  ? 420 MET A CB    1 
ATOM   3262  C CG    . MET A 1 420 ? 16.869  28.956  26.844  1.00 50.51  ? 420 MET A CG    1 
ATOM   3263  S SD    . MET A 1 420 ? 15.097  29.025  26.938  1.00 55.74  ? 420 MET A SD    1 
ATOM   3264  C CE    . MET A 1 420 ? 14.870  30.790  26.759  1.00 60.26  ? 420 MET A CE    1 
ATOM   3265  N N     . GLY A 1 421 ? 20.705  27.413  29.446  1.00 44.46  ? 421 GLY A N     1 
ATOM   3266  C CA    . GLY A 1 421 ? 21.393  26.461  30.280  1.00 48.39  ? 421 GLY A CA    1 
ATOM   3267  C C     . GLY A 1 421 ? 21.614  26.985  31.690  1.00 50.75  ? 421 GLY A C     1 
ATOM   3268  O O     . GLY A 1 421 ? 21.701  28.196  31.928  1.00 54.58  ? 421 GLY A O     1 
ATOM   3269  N N     . LEU A 1 422 ? 21.788  25.998  32.573  1.00 55.37  ? 422 LEU A N     1 
ATOM   3270  C CA    . LEU A 1 422 ? 21.849  26.128  34.019  1.00 53.78  ? 422 LEU A CA    1 
ATOM   3271  C C     . LEU A 1 422 ? 22.956  25.182  34.484  1.00 52.45  ? 422 LEU A C     1 
ATOM   3272  O O     . LEU A 1 422 ? 23.025  24.031  34.038  1.00 51.67  ? 422 LEU A O     1 
ATOM   3273  C CB    . LEU A 1 422 ? 20.475  25.664  34.530  1.00 59.30  ? 422 LEU A CB    1 
ATOM   3274  C CG    . LEU A 1 422 ? 20.073  26.071  35.935  1.00 67.89  ? 422 LEU A CG    1 
ATOM   3275  C CD1   . LEU A 1 422 ? 18.643  25.634  36.235  1.00 75.12  ? 422 LEU A CD1   1 
ATOM   3276  C CD2   . LEU A 1 422 ? 21.034  25.494  36.938  1.00 71.71  ? 422 LEU A CD2   1 
ATOM   3277  N N     . LEU A 1 423 ? 23.831  25.632  35.373  1.00 46.33  ? 423 LEU A N     1 
ATOM   3278  C CA    . LEU A 1 423 ? 24.597  24.668  36.142  1.00 45.43  ? 423 LEU A CA    1 
ATOM   3279  C C     . LEU A 1 423 ? 24.131  24.711  37.580  1.00 41.78  ? 423 LEU A C     1 
ATOM   3280  O O     . LEU A 1 423 ? 24.166  25.773  38.191  1.00 33.62  ? 423 LEU A O     1 
ATOM   3281  C CB    . LEU A 1 423 ? 26.104  24.891  36.004  1.00 43.50  ? 423 LEU A CB    1 
ATOM   3282  C CG    . LEU A 1 423 ? 26.573  24.423  34.629  1.00 49.22  ? 423 LEU A CG    1 
ATOM   3283  C CD1   . LEU A 1 423 ? 27.174  25.570  33.859  1.00 53.19  ? 423 LEU A CD1   1 
ATOM   3284  C CD2   . LEU A 1 423 ? 27.502  23.243  34.731  1.00 45.62  ? 423 LEU A CD2   1 
ATOM   3285  N N     . ALA A 1 424 ? 23.725  23.518  38.046  1.00 41.33  ? 424 ALA A N     1 
ATOM   3286  C CA    . ALA A 1 424 ? 23.096  23.305  39.331  1.00 42.85  ? 424 ALA A CA    1 
ATOM   3287  C C     . ALA A 1 424 ? 23.884  22.262  40.108  1.00 42.95  ? 424 ALA A C     1 
ATOM   3288  O O     . ALA A 1 424 ? 24.185  21.190  39.570  1.00 48.20  ? 424 ALA A O     1 
ATOM   3289  C CB    . ALA A 1 424 ? 21.663  22.839  39.134  1.00 43.40  ? 424 ALA A CB    1 
ATOM   3290  N N     . ILE A 1 425 ? 24.106  22.570  41.390  1.00 40.15  ? 425 ILE A N     1 
ATOM   3291  C CA    . ILE A 1 425 ? 24.785  21.690  42.326  1.00 41.82  ? 425 ILE A CA    1 
ATOM   3292  C C     . ILE A 1 425 ? 23.859  21.454  43.517  1.00 42.27  ? 425 ILE A C     1 
ATOM   3293  O O     . ILE A 1 425 ? 23.454  22.406  44.181  1.00 41.81  ? 425 ILE A O     1 
ATOM   3294  C CB    . ILE A 1 425 ? 26.122  22.308  42.789  1.00 38.77  ? 425 ILE A CB    1 
ATOM   3295  C CG1   . ILE A 1 425 ? 27.045  22.574  41.609  1.00 38.35  ? 425 ILE A CG1   1 
ATOM   3296  C CG2   . ILE A 1 425 ? 26.784  21.424  43.819  1.00 38.44  ? 425 ILE A CG2   1 
ATOM   3297  C CD1   . ILE A 1 425 ? 27.972  23.707  41.834  1.00 42.80  ? 425 ILE A CD1   1 
ATOM   3298  N N     . GLY A 1 426 ? 23.561  20.183  43.808  1.00 40.13  ? 426 GLY A N     1 
ATOM   3299  C CA    . GLY A 1 426 ? 22.785  19.842  44.982  1.00 43.19  ? 426 GLY A CA    1 
ATOM   3300  C C     . GLY A 1 426 ? 23.676  19.843  46.216  1.00 45.79  ? 426 GLY A C     1 
ATOM   3301  O O     . GLY A 1 426 ? 23.495  20.680  47.101  1.00 49.35  ? 426 GLY A O     1 
ATOM   3302  N N     . TRP A 1 427 ? 24.621  18.894  46.242  1.00 40.23  ? 427 TRP A N     1 
ATOM   3303  C CA    . TRP A 1 427 ? 25.602  18.816  47.301  1.00 41.50  ? 427 TRP A CA    1 
ATOM   3304  C C     . TRP A 1 427 ? 26.959  18.410  46.732  1.00 39.90  ? 427 TRP A C     1 
ATOM   3305  O O     . TRP A 1 427 ? 27.870  19.235  46.683  1.00 45.12  ? 427 TRP A O     1 
ATOM   3306  C CB    . TRP A 1 427 ? 25.108  17.872  48.395  1.00 43.62  ? 427 TRP A CB    1 
ATOM   3307  C CG    . TRP A 1 427 ? 25.915  17.917  49.656  1.00 42.35  ? 427 TRP A CG    1 
ATOM   3308  C CD1   . TRP A 1 427 ? 27.041  18.646  49.893  1.00 41.80  ? 427 TRP A CD1   1 
ATOM   3309  C CD2   . TRP A 1 427 ? 25.662  17.158  50.851  1.00 46.76  ? 427 TRP A CD2   1 
ATOM   3310  N NE1   . TRP A 1 427 ? 27.485  18.430  51.167  1.00 49.25  ? 427 TRP A NE1   1 
ATOM   3311  C CE2   . TRP A 1 427 ? 26.667  17.507  51.775  1.00 49.71  ? 427 TRP A CE2   1 
ATOM   3312  C CE3   . TRP A 1 427 ? 24.711  16.200  51.225  1.00 46.32  ? 427 TRP A CE3   1 
ATOM   3313  C CZ2   . TRP A 1 427 ? 26.733  16.929  53.043  1.00 47.96  ? 427 TRP A CZ2   1 
ATOM   3314  C CZ3   . TRP A 1 427 ? 24.773  15.642  52.486  1.00 40.64  ? 427 TRP A CZ3   1 
ATOM   3315  C CH2   . TRP A 1 427 ? 25.772  16.003  53.375  1.00 43.38  ? 427 TRP A CH2   1 
ATOM   3316  N N     . ARG A 1 428 ? 27.065  17.168  46.248  1.00 38.95  ? 428 ARG A N     1 
ATOM   3317  C CA    . ARG A 1 428 ? 28.265  16.705  45.567  1.00 40.34  ? 428 ARG A CA    1 
ATOM   3318  C C     . ARG A 1 428 ? 28.016  16.512  44.058  1.00 41.30  ? 428 ARG A C     1 
ATOM   3319  O O     . ARG A 1 428 ? 28.966  16.235  43.328  1.00 43.53  ? 428 ARG A O     1 
ATOM   3320  C CB    . ARG A 1 428 ? 28.781  15.438  46.258  1.00 38.66  ? 428 ARG A CB    1 
ATOM   3321  C CG    . ARG A 1 428 ? 29.387  15.686  47.631  1.00 40.33  ? 428 ARG A CG    1 
ATOM   3322  C CD    . ARG A 1 428 ? 30.284  14.636  48.284  1.00 38.30  ? 428 ARG A CD    1 
ATOM   3323  N NE    . ARG A 1 428 ? 29.662  14.403  49.542  1.00 44.81  ? 428 ARG A NE    1 
ATOM   3324  C CZ    . ARG A 1 428 ? 30.075  14.803  50.723  1.00 53.03  ? 428 ARG A CZ    1 
ATOM   3325  N NH1   . ARG A 1 428 ? 29.156  15.232  51.559  1.00 60.01  ? 428 ARG A NH1   1 
ATOM   3326  N NH2   . ARG A 1 428 ? 31.358  14.875  51.029  1.00 56.42  ? 428 ARG A NH2   1 
ATOM   3327  N N     . ASP A 1 429 ? 26.767  16.720  43.601  1.00 39.94  ? 429 ASP A N     1 
ATOM   3328  C CA    . ASP A 1 429 ? 26.331  16.509  42.217  1.00 42.74  ? 429 ASP A CA    1 
ATOM   3329  C C     . ASP A 1 429 ? 26.290  17.813  41.405  1.00 43.11  ? 429 ASP A C     1 
ATOM   3330  O O     . ASP A 1 429 ? 25.784  18.831  41.859  1.00 46.59  ? 429 ASP A O     1 
ATOM   3331  C CB    . ASP A 1 429 ? 24.937  15.888  42.158  1.00 39.37  ? 429 ASP A CB    1 
ATOM   3332  C CG    . ASP A 1 429 ? 23.875  16.547  43.030  1.00 40.70  ? 429 ASP A CG    1 
ATOM   3333  O OD1   . ASP A 1 429 ? 24.194  16.901  44.180  1.00 44.36  ? 429 ASP A OD1   1 
ATOM   3334  O OD2   . ASP A 1 429 ? 22.699  16.607  42.597  1.00 40.31  ? 429 ASP A OD2   1 
ATOM   3335  N N     . LEU A 1 430 ? 26.854  17.798  40.194  1.00 42.99  ? 430 LEU A N     1 
ATOM   3336  C CA    . LEU A 1 430 ? 26.669  18.879  39.231  1.00 40.91  ? 430 LEU A CA    1 
ATOM   3337  C C     . LEU A 1 430 ? 25.640  18.419  38.200  1.00 35.58  ? 430 LEU A C     1 
ATOM   3338  O O     . LEU A 1 430 ? 25.598  17.247  37.862  1.00 34.61  ? 430 LEU A O     1 
ATOM   3339  C CB    . LEU A 1 430 ? 28.011  19.237  38.574  1.00 36.69  ? 430 LEU A CB    1 
ATOM   3340  C CG    . LEU A 1 430 ? 27.928  20.350  37.524  1.00 45.56  ? 430 LEU A CG    1 
ATOM   3341  C CD1   . LEU A 1 430 ? 27.765  21.719  38.175  1.00 46.81  ? 430 LEU A CD1   1 
ATOM   3342  C CD2   . LEU A 1 430 ? 29.128  20.353  36.591  1.00 42.44  ? 430 LEU A CD2   1 
ATOM   3343  N N     . HIS A 1 431 ? 24.797  19.333  37.727  1.00 35.43  ? 431 HIS A N     1 
ATOM   3344  C CA    . HIS A 1 431 ? 23.848  19.037  36.652  1.00 33.50  ? 431 HIS A CA    1 
ATOM   3345  C C     . HIS A 1 431 ? 23.893  20.202  35.691  1.00 31.77  ? 431 HIS A C     1 
ATOM   3346  O O     . HIS A 1 431 ? 23.647  21.325  36.126  1.00 33.83  ? 431 HIS A O     1 
ATOM   3347  C CB    . HIS A 1 431 ? 22.396  18.974  37.136  1.00 34.57  ? 431 HIS A CB    1 
ATOM   3348  C CG    . HIS A 1 431 ? 22.078  17.871  38.055  1.00 36.25  ? 431 HIS A CG    1 
ATOM   3349  N ND1   . HIS A 1 431 ? 22.506  17.805  39.363  1.00 39.81  ? 431 HIS A ND1   1 
ATOM   3350  C CD2   . HIS A 1 431 ? 21.357  16.777  37.835  1.00 39.58  ? 431 HIS A CD2   1 
ATOM   3351  C CE1   . HIS A 1 431 ? 22.012  16.707  39.916  1.00 35.98  ? 431 HIS A CE1   1 
ATOM   3352  N NE2   . HIS A 1 431 ? 21.322  16.060  38.998  1.00 41.67  ? 431 HIS A NE2   1 
ATOM   3353  N N     . HIS A 1 432 ? 24.365  19.957  34.460  1.00 37.64  ? 432 HIS A N     1 
ATOM   3354  C CA    . HIS A 1 432 ? 24.139  20.874  33.358  1.00 36.26  ? 432 HIS A CA    1 
ATOM   3355  C C     . HIS A 1 432 ? 22.734  20.616  32.838  1.00 37.34  ? 432 HIS A C     1 
ATOM   3356  O O     . HIS A 1 432 ? 22.480  19.582  32.235  1.00 37.59  ? 432 HIS A O     1 
ATOM   3357  C CB    . HIS A 1 432 ? 25.146  20.712  32.225  1.00 37.45  ? 432 HIS A CB    1 
ATOM   3358  C CG    . HIS A 1 432 ? 24.869  21.608  31.077  1.00 41.08  ? 432 HIS A CG    1 
ATOM   3359  N ND1   . HIS A 1 432 ? 25.413  22.874  31.002  1.00 44.78  ? 432 HIS A ND1   1 
ATOM   3360  C CD2   . HIS A 1 432 ? 24.090  21.472  29.993  1.00 45.58  ? 432 HIS A CD2   1 
ATOM   3361  C CE1   . HIS A 1 432 ? 24.983  23.479  29.901  1.00 39.35  ? 432 HIS A CE1   1 
ATOM   3362  N NE2   . HIS A 1 432 ? 24.190  22.647  29.261  1.00 43.55  ? 432 HIS A NE2   1 
ATOM   3363  N N     . VAL A 1 433 ? 21.830  21.563  33.106  1.00 43.04  ? 433 VAL A N     1 
ATOM   3364  C CA    . VAL A 1 433 ? 20.431  21.451  32.720  1.00 41.01  ? 433 VAL A CA    1 
ATOM   3365  C C     . VAL A 1 433 ? 20.228  22.277  31.461  1.00 45.20  ? 433 VAL A C     1 
ATOM   3366  O O     . VAL A 1 433 ? 20.583  23.459  31.415  1.00 47.88  ? 433 VAL A O     1 
ATOM   3367  C CB    . VAL A 1 433 ? 19.508  21.951  33.836  1.00 37.59  ? 433 VAL A CB    1 
ATOM   3368  C CG1   . VAL A 1 433 ? 18.043  21.821  33.458  1.00 37.38  ? 433 VAL A CG1   1 
ATOM   3369  C CG2   . VAL A 1 433 ? 19.831  21.282  35.163  1.00 35.34  ? 433 VAL A CG2   1 
ATOM   3370  N N     . THR A 1 434 ? 19.674  21.616  30.445  1.00 49.49  ? 434 THR A N     1 
ATOM   3371  C CA    . THR A 1 434 ? 19.374  22.230  29.169  1.00 43.36  ? 434 THR A CA    1 
ATOM   3372  C C     . THR A 1 434 ? 17.871  22.400  29.105  1.00 39.02  ? 434 THR A C     1 
ATOM   3373  O O     . THR A 1 434 ? 17.136  21.427  29.242  1.00 37.19  ? 434 THR A O     1 
ATOM   3374  C CB    . THR A 1 434 ? 19.868  21.356  28.017  1.00 48.80  ? 434 THR A CB    1 
ATOM   3375  O OG1   . THR A 1 434 ? 21.270  21.160  28.185  1.00 48.54  ? 434 THR A OG1   1 
ATOM   3376  C CG2   . THR A 1 434 ? 19.577  21.953  26.659  1.00 49.23  ? 434 THR A CG2   1 
ATOM   3377  N N     . VAL A 1 435 ? 17.448  23.652  28.933  1.00 41.36  ? 435 VAL A N     1 
ATOM   3378  C CA    . VAL A 1 435 ? 16.067  23.985  28.657  1.00 45.63  ? 435 VAL A CA    1 
ATOM   3379  C C     . VAL A 1 435 ? 15.938  24.377  27.188  1.00 45.88  ? 435 VAL A C     1 
ATOM   3380  O O     . VAL A 1 435 ? 16.670  25.253  26.734  1.00 44.35  ? 435 VAL A O     1 
ATOM   3381  C CB    . VAL A 1 435 ? 15.613  25.118  29.583  1.00 50.06  ? 435 VAL A CB    1 
ATOM   3382  C CG1   . VAL A 1 435 ? 14.219  25.594  29.226  1.00 49.75  ? 435 VAL A CG1   1 
ATOM   3383  C CG2   . VAL A 1 435 ? 15.680  24.670  31.034  1.00 52.52  ? 435 VAL A CG2   1 
ATOM   3384  N N     . ILE A 1 436 ? 15.041  23.693  26.457  1.00 44.83  ? 436 ILE A N     1 
ATOM   3385  C CA    . ILE A 1 436 ? 14.730  24.062  25.085  1.00 46.35  ? 436 ILE A CA    1 
ATOM   3386  C C     . ILE A 1 436 ? 13.230  24.331  24.983  1.00 46.82  ? 436 ILE A C     1 
ATOM   3387  O O     . ILE A 1 436 ? 12.423  23.417  25.115  1.00 43.97  ? 436 ILE A O     1 
ATOM   3388  C CB    . ILE A 1 436 ? 15.146  22.980  24.069  1.00 49.05  ? 436 ILE A CB    1 
ATOM   3389  C CG1   . ILE A 1 436 ? 16.483  22.316  24.405  1.00 51.72  ? 436 ILE A CG1   1 
ATOM   3390  C CG2   . ILE A 1 436 ? 15.175  23.555  22.669  1.00 54.28  ? 436 ILE A CG2   1 
ATOM   3391  C CD1   . ILE A 1 436 ? 16.634  20.942  23.804  1.00 45.31  ? 436 ILE A CD1   1 
ATOM   3392  N N     . VAL A 1 437 ? 12.893  25.587  24.675  1.00 47.68  ? 437 VAL A N     1 
ATOM   3393  C CA    . VAL A 1 437 ? 11.532  25.980  24.371  1.00 50.17  ? 437 VAL A CA    1 
ATOM   3394  C C     . VAL A 1 437 ? 11.220  25.805  22.882  1.00 48.14  ? 437 VAL A C     1 
ATOM   3395  O O     . VAL A 1 437 ? 12.022  26.119  22.007  1.00 44.57  ? 437 VAL A O     1 
ATOM   3396  C CB    . VAL A 1 437 ? 11.340  27.428  24.812  1.00 57.42  ? 437 VAL A CB    1 
ATOM   3397  C CG1   . VAL A 1 437 ? 9.931   27.915  24.503  1.00 78.71  ? 437 VAL A CG1   1 
ATOM   3398  C CG2   . VAL A 1 437 ? 11.649  27.550  26.289  1.00 58.99  ? 437 VAL A CG2   1 
ATOM   3399  N N     . TYR A 1 438 ? 10.014  25.332  22.578  1.00 45.29  ? 438 TYR A N     1 
ATOM   3400  C CA    . TYR A 1 438 ? 9.684   24.997  21.202  1.00 53.56  ? 438 TYR A CA    1 
ATOM   3401  C C     . TYR A 1 438 ? 8.196   25.212  20.945  1.00 55.01  ? 438 TYR A C     1 
ATOM   3402  O O     . TYR A 1 438 ? 7.377   25.113  21.858  1.00 61.36  ? 438 TYR A O     1 
ATOM   3403  C CB    . TYR A 1 438 ? 10.076  23.544  20.884  1.00 57.46  ? 438 TYR A CB    1 
ATOM   3404  C CG    . TYR A 1 438 ? 9.430   22.472  21.733  1.00 53.79  ? 438 TYR A CG    1 
ATOM   3405  C CD1   . TYR A 1 438 ? 9.821   22.236  23.039  1.00 55.95  ? 438 TYR A CD1   1 
ATOM   3406  C CD2   . TYR A 1 438 ? 8.419   21.672  21.222  1.00 66.14  ? 438 TYR A CD2   1 
ATOM   3407  C CE1   . TYR A 1 438 ? 9.204   21.263  23.816  1.00 67.28  ? 438 TYR A CE1   1 
ATOM   3408  C CE2   . TYR A 1 438 ? 7.799   20.685  21.979  1.00 67.79  ? 438 TYR A CE2   1 
ATOM   3409  C CZ    . TYR A 1 438 ? 8.193   20.475  23.285  1.00 71.50  ? 438 TYR A CZ    1 
ATOM   3410  O OH    . TYR A 1 438 ? 7.563   19.479  24.001  1.00 73.13  ? 438 TYR A OH    1 
ATOM   3411  N N     . ASP A 1 439 ? 7.864   25.461  19.675  1.00 55.37  ? 439 ASP A N     1 
ATOM   3412  C CA    . ASP A 1 439 ? 6.487   25.587  19.229  1.00 59.94  ? 439 ASP A CA    1 
ATOM   3413  C C     . ASP A 1 439 ? 5.862   24.193  19.073  1.00 67.01  ? 439 ASP A C     1 
ATOM   3414  O O     . ASP A 1 439 ? 6.035   23.536  18.046  1.00 72.14  ? 439 ASP A O     1 
ATOM   3415  C CB    . ASP A 1 439 ? 6.451   26.420  17.943  1.00 53.65  ? 439 ASP A CB    1 
ATOM   3416  C CG    . ASP A 1 439 ? 5.068   26.614  17.362  1.00 58.40  ? 439 ASP A CG    1 
ATOM   3417  O OD1   . ASP A 1 439 ? 4.074   26.129  17.992  1.00 50.55  ? 439 ASP A OD1   1 
ATOM   3418  O OD2   . ASP A 1 439 ? 5.006   27.214  16.269  1.00 64.65  ? 439 ASP A OD2   1 
ATOM   3419  N N     . LYS A 1 440 ? 5.078   23.769  20.071  1.00 64.26  ? 440 LYS A N     1 
ATOM   3420  C CA    . LYS A 1 440 ? 4.542   22.418  20.089  1.00 74.31  ? 440 LYS A CA    1 
ATOM   3421  C C     . LYS A 1 440 ? 3.270   22.345  19.248  1.00 78.26  ? 440 LYS A C     1 
ATOM   3422  O O     . LYS A 1 440 ? 2.444   21.460  19.468  1.00 70.24  ? 440 LYS A O     1 
ATOM   3423  C CB    . LYS A 1 440 ? 4.293   21.930  21.525  1.00 78.84  ? 440 LYS A CB    1 
ATOM   3424  C CG    . LYS A 1 440 ? 3.524   22.885  22.435  1.00 93.47  ? 440 LYS A CG    1 
ATOM   3425  C CD    . LYS A 1 440 ? 2.007   22.723  22.438  1.00 98.13  ? 440 LYS A CD    1 
ATOM   3426  C CE    . LYS A 1 440 ? 1.280   24.010  22.785  1.00 93.93  ? 440 LYS A CE    1 
ATOM   3427  N NZ    . LYS A 1 440 ? -0.189  23.859  22.695  1.00 87.00  ? 440 LYS A NZ    1 
ATOM   3428  N N     . THR A 1 441 ? 3.105   23.254  18.278  1.00 76.21  ? 441 THR A N     1 
ATOM   3429  C CA    . THR A 1 441 ? 2.016   23.090  17.318  1.00 80.99  ? 441 THR A CA    1 
ATOM   3430  C C     . THR A 1 441 ? 2.604   22.857  15.929  1.00 72.06  ? 441 THR A C     1 
ATOM   3431  O O     . THR A 1 441 ? 1.894   22.401  15.042  1.00 75.15  ? 441 THR A O     1 
ATOM   3432  C CB    . THR A 1 441 ? 1.001   24.245  17.378  1.00 68.93  ? 441 THR A CB    1 
ATOM   3433  O OG1   . THR A 1 441 ? 1.577   25.420  16.812  1.00 64.36  ? 441 THR A OG1   1 
ATOM   3434  C CG2   . THR A 1 441 ? 0.544   24.566  18.785  1.00 66.11  ? 441 THR A CG2   1 
ATOM   3435  N N     . ASP A 1 442 ? 3.904   23.133  15.773  1.00 73.28  ? 442 ASP A N     1 
ATOM   3436  C CA    . ASP A 1 442 ? 4.585   23.004  14.496  1.00 69.98  ? 442 ASP A CA    1 
ATOM   3437  C C     . ASP A 1 442 ? 5.264   21.638  14.410  1.00 70.73  ? 442 ASP A C     1 
ATOM   3438  O O     . ASP A 1 442 ? 6.242   21.411  15.112  1.00 75.03  ? 442 ASP A O     1 
ATOM   3439  C CB    . ASP A 1 442 ? 5.592   24.140  14.318  1.00 62.52  ? 442 ASP A CB    1 
ATOM   3440  C CG    . ASP A 1 442 ? 6.332   24.065  12.996  1.00 61.69  ? 442 ASP A CG    1 
ATOM   3441  O OD1   . ASP A 1 442 ? 6.183   23.042  12.301  1.00 68.81  ? 442 ASP A OD1   1 
ATOM   3442  O OD2   . ASP A 1 442 ? 7.055   25.023  12.680  1.00 57.70  ? 442 ASP A OD2   1 
ATOM   3443  N N     . PRO A 1 443 ? 4.812   20.713  13.525  1.00 70.73  ? 443 PRO A N     1 
ATOM   3444  C CA    . PRO A 1 443 ? 5.386   19.366  13.431  1.00 67.80  ? 443 PRO A CA    1 
ATOM   3445  C C     . PRO A 1 443 ? 6.846   19.275  12.976  1.00 60.23  ? 443 PRO A C     1 
ATOM   3446  O O     . PRO A 1 443 ? 7.533   18.291  13.238  1.00 52.66  ? 443 PRO A O     1 
ATOM   3447  C CB    . PRO A 1 443 ? 4.509   18.678  12.368  1.00 71.39  ? 443 PRO A CB    1 
ATOM   3448  C CG    . PRO A 1 443 ? 3.246   19.491  12.331  1.00 68.67  ? 443 PRO A CG    1 
ATOM   3449  C CD    . PRO A 1 443 ? 3.715   20.907  12.567  1.00 64.91  ? 443 PRO A CD    1 
ATOM   3450  N N     . ASP A 1 444 ? 7.320   20.295  12.264  1.00 54.27  ? 444 ASP A N     1 
ATOM   3451  C CA    . ASP A 1 444 ? 8.699   20.289  11.815  1.00 64.46  ? 444 ASP A CA    1 
ATOM   3452  C C     . ASP A 1 444 ? 9.633   20.630  12.978  1.00 67.95  ? 444 ASP A C     1 
ATOM   3453  O O     . ASP A 1 444 ? 10.739  20.103  13.027  1.00 66.60  ? 444 ASP A O     1 
ATOM   3454  C CB    . ASP A 1 444 ? 8.906   21.228  10.621  1.00 72.16  ? 444 ASP A CB    1 
ATOM   3455  C CG    . ASP A 1 444 ? 7.992   20.937  9.439   1.00 76.69  ? 444 ASP A CG    1 
ATOM   3456  O OD1   . ASP A 1 444 ? 7.767   19.745  9.147   1.00 77.57  ? 444 ASP A OD1   1 
ATOM   3457  O OD2   . ASP A 1 444 ? 7.521   21.903  8.816   1.00 73.43  ? 444 ASP A OD2   1 
ATOM   3458  N N     . GLU A 1 445 ? 9.193   21.524  13.882  1.00 67.59  ? 445 GLU A N     1 
ATOM   3459  C CA    . GLU A 1 445 ? 9.952   21.906  15.069  1.00 64.31  ? 445 GLU A CA    1 
ATOM   3460  C C     . GLU A 1 445 ? 9.995   20.746  16.054  1.00 56.54  ? 445 GLU A C     1 
ATOM   3461  O O     . GLU A 1 445 ? 11.034  20.514  16.671  1.00 45.82  ? 445 GLU A O     1 
ATOM   3462  C CB    . GLU A 1 445 ? 9.342   23.109  15.790  1.00 62.18  ? 445 GLU A CB    1 
ATOM   3463  C CG    . GLU A 1 445 ? 9.499   24.407  15.024  1.00 69.87  ? 445 GLU A CG    1 
ATOM   3464  C CD    . GLU A 1 445 ? 10.825  25.116  15.231  1.00 76.66  ? 445 GLU A CD    1 
ATOM   3465  O OE1   . GLU A 1 445 ? 10.955  25.814  16.289  1.00 74.36  ? 445 GLU A OE1   1 
ATOM   3466  O OE2   . GLU A 1 445 ? 11.718  24.964  14.340  1.00 56.49  ? 445 GLU A OE2   1 
ATOM   3467  N N     . ARG A 1 446 ? 8.856   20.051  16.177  1.00 55.32  ? 446 ARG A N     1 
ATOM   3468  C CA    . ARG A 1 446 ? 8.728   18.851  16.995  1.00 58.28  ? 446 ARG A CA    1 
ATOM   3469  C C     . ARG A 1 446 ? 9.742   17.795  16.553  1.00 59.19  ? 446 ARG A C     1 
ATOM   3470  O O     . ARG A 1 446 ? 10.264  17.070  17.400  1.00 63.50  ? 446 ARG A O     1 
ATOM   3471  C CB    . ARG A 1 446 ? 7.303   18.277  16.935  1.00 54.70  ? 446 ARG A CB    1 
ATOM   3472  C CG    . ARG A 1 446 ? 6.228   19.214  17.488  1.00 61.04  ? 446 ARG A CG    1 
ATOM   3473  C CD    . ARG A 1 446 ? 4.979   18.576  18.117  1.00 63.79  ? 446 ARG A CD    1 
ATOM   3474  N NE    . ARG A 1 446 ? 4.109   17.829  17.204  1.00 69.65  ? 446 ARG A NE    1 
ATOM   3475  C CZ    . ARG A 1 446 ? 2.965   18.273  16.668  1.00 68.56  ? 446 ARG A CZ    1 
ATOM   3476  N NH1   . ARG A 1 446 ? 2.448   19.430  17.036  1.00 71.80  ? 446 ARG A NH1   1 
ATOM   3477  N NH2   . ARG A 1 446 ? 2.341   17.563  15.742  1.00 65.38  ? 446 ARG A NH2   1 
ATOM   3478  N N     . LYS A 1 447 ? 9.966   17.684  15.230  1.00 61.10  ? 447 LYS A N     1 
ATOM   3479  C CA    . LYS A 1 447 ? 10.930  16.746  14.668  1.00 58.80  ? 447 LYS A CA    1 
ATOM   3480  C C     . LYS A 1 447 ? 12.341  17.192  15.064  1.00 53.88  ? 447 LYS A C     1 
ATOM   3481  O O     . LYS A 1 447 ? 13.157  16.380  15.469  1.00 50.17  ? 447 LYS A O     1 
ATOM   3482  C CB    . LYS A 1 447 ? 10.785  16.630  13.142  1.00 58.85  ? 447 LYS A CB    1 
ATOM   3483  C CG    . LYS A 1 447 ? 11.750  15.670  12.447  1.00 61.05  ? 447 LYS A CG    1 
ATOM   3484  C CD    . LYS A 1 447 ? 11.226  14.236  12.310  1.00 71.04  ? 447 LYS A CD    1 
ATOM   3485  C CE    . LYS A 1 447 ? 12.299  13.162  12.203  1.00 62.20  ? 447 LYS A CE    1 
ATOM   3486  N NZ    . LYS A 1 447 ? 13.142  13.071  13.421  1.00 70.17  ? 447 LYS A NZ    1 
ATOM   3487  N N     . LYS A 1 448 ? 12.623  18.487  14.931  1.00 51.22  ? 448 LYS A N     1 
ATOM   3488  C CA    . LYS A 1 448 ? 13.928  19.031  15.255  1.00 52.59  ? 448 LYS A CA    1 
ATOM   3489  C C     . LYS A 1 448 ? 14.267  18.733  16.711  1.00 49.92  ? 448 LYS A C     1 
ATOM   3490  O O     . LYS A 1 448 ? 15.374  18.257  16.980  1.00 51.07  ? 448 LYS A O     1 
ATOM   3491  C CB    . LYS A 1 448 ? 13.971  20.540  14.985  1.00 53.88  ? 448 LYS A CB    1 
ATOM   3492  C CG    . LYS A 1 448 ? 13.963  20.908  13.505  1.00 56.33  ? 448 LYS A CG    1 
ATOM   3493  C CD    . LYS A 1 448 ? 13.763  22.374  13.218  1.00 57.92  ? 448 LYS A CD    1 
ATOM   3494  C CE    . LYS A 1 448 ? 14.972  23.202  13.589  1.00 65.37  ? 448 LYS A CE    1 
ATOM   3495  N NZ    . LYS A 1 448 ? 14.778  24.657  13.352  1.00 60.86  ? 448 LYS A NZ    1 
ATOM   3496  N N     . LEU A 1 449 ? 13.308  19.023  17.604  1.00 42.03  ? 449 LEU A N     1 
ATOM   3497  C CA    . LEU A 1 449 ? 13.490  18.903  19.037  1.00 43.45  ? 449 LEU A CA    1 
ATOM   3498  C C     . LEU A 1 449 ? 13.761  17.449  19.384  1.00 42.57  ? 449 LEU A C     1 
ATOM   3499  O O     . LEU A 1 449 ? 14.762  17.128  20.027  1.00 40.35  ? 449 LEU A O     1 
ATOM   3500  C CB    . LEU A 1 449 ? 12.228  19.367  19.764  1.00 45.81  ? 449 LEU A CB    1 
ATOM   3501  C CG    . LEU A 1 449 ? 12.332  19.239  21.282  1.00 49.91  ? 449 LEU A CG    1 
ATOM   3502  C CD1   . LEU A 1 449 ? 13.155  20.380  21.864  1.00 44.99  ? 449 LEU A CD1   1 
ATOM   3503  C CD2   . LEU A 1 449 ? 10.960  19.173  21.910  1.00 51.81  ? 449 LEU A CD2   1 
ATOM   3504  N N     . ASP A 1 450 ? 12.875  16.573  18.901  1.00 41.80  ? 450 ASP A N     1 
ATOM   3505  C CA    . ASP A 1 450 ? 12.957  15.163  19.221  1.00 41.93  ? 450 ASP A CA    1 
ATOM   3506  C C     . ASP A 1 450 ? 14.384  14.701  18.913  1.00 49.15  ? 450 ASP A C     1 
ATOM   3507  O O     . ASP A 1 450 ? 15.053  14.139  19.775  1.00 41.28  ? 450 ASP A O     1 
ATOM   3508  C CB    . ASP A 1 450 ? 11.862  14.371  18.514  1.00 43.66  ? 450 ASP A CB    1 
ATOM   3509  C CG    . ASP A 1 450 ? 11.687  12.946  19.032  1.00 54.87  ? 450 ASP A CG    1 
ATOM   3510  O OD1   . ASP A 1 450 ? 12.032  12.683  20.215  1.00 62.62  ? 450 ASP A OD1   1 
ATOM   3511  O OD2   . ASP A 1 450 ? 11.155  12.105  18.267  1.00 48.97  ? 450 ASP A OD2   1 
ATOM   3512  N N     . GLU A 1 451 ? 14.865  15.038  17.706  1.00 43.37  ? 451 GLU A N     1 
ATOM   3513  C CA    . GLU A 1 451 ? 16.155  14.595  17.208  1.00 37.74  ? 451 GLU A CA    1 
ATOM   3514  C C     . GLU A 1 451 ? 17.277  15.199  18.053  1.00 39.60  ? 451 GLU A C     1 
ATOM   3515  O O     . GLU A 1 451 ? 18.194  14.501  18.442  1.00 44.29  ? 451 GLU A O     1 
ATOM   3516  C CB    . GLU A 1 451 ? 16.250  14.953  15.712  1.00 38.71  ? 451 GLU A CB    1 
ATOM   3517  C CG    . GLU A 1 451 ? 17.629  14.881  15.091  1.00 38.33  ? 451 GLU A CG    1 
ATOM   3518  C CD    . GLU A 1 451 ? 17.649  15.282  13.624  1.00 45.05  ? 451 GLU A CD    1 
ATOM   3519  O OE1   . GLU A 1 451 ? 16.753  14.800  12.909  1.00 42.08  ? 451 GLU A OE1   1 
ATOM   3520  O OE2   . GLU A 1 451 ? 18.575  16.061  13.200  1.00 43.56  ? 451 GLU A OE2   1 
ATOM   3521  N N     . LEU A 1 452 ? 17.221  16.518  18.270  1.00 39.25  ? 452 LEU A N     1 
ATOM   3522  C CA    . LEU A 1 452 ? 18.234  17.216  19.007  1.00 34.68  ? 452 LEU A CA    1 
ATOM   3523  C C     . LEU A 1 452 ? 18.353  16.563  20.382  1.00 36.28  ? 452 LEU A C     1 
ATOM   3524  O O     . LEU A 1 452 ? 19.460  16.385  20.882  1.00 38.94  ? 452 LEU A O     1 
ATOM   3525  C CB    . LEU A 1 452 ? 17.847  18.698  19.062  1.00 35.83  ? 452 LEU A CB    1 
ATOM   3526  C CG    . LEU A 1 452 ? 18.514  19.517  20.175  1.00 38.07  ? 452 LEU A CG    1 
ATOM   3527  C CD1   . LEU A 1 452 ? 20.041  19.541  20.042  1.00 35.58  ? 452 LEU A CD1   1 
ATOM   3528  C CD2   . LEU A 1 452 ? 17.954  20.938  20.189  1.00 35.87  ? 452 LEU A CD2   1 
ATOM   3529  N N     . PHE A 1 453 ? 17.210  16.156  20.943  1.00 35.61  ? 453 PHE A N     1 
ATOM   3530  C CA    . PHE A 1 453 ? 17.158  15.631  22.295  1.00 35.71  ? 453 PHE A CA    1 
ATOM   3531  C C     . PHE A 1 453 ? 17.930  14.329  22.321  1.00 38.89  ? 453 PHE A C     1 
ATOM   3532  O O     . PHE A 1 453 ? 18.700  14.076  23.248  1.00 41.46  ? 453 PHE A O     1 
ATOM   3533  C CB    . PHE A 1 453 ? 15.723  15.395  22.782  1.00 29.78  ? 453 PHE A CB    1 
ATOM   3534  C CG    . PHE A 1 453 ? 15.630  14.962  24.225  1.00 32.54  ? 453 PHE A CG    1 
ATOM   3535  C CD1   . PHE A 1 453 ? 15.613  15.896  25.254  1.00 33.42  ? 453 PHE A CD1   1 
ATOM   3536  C CD2   . PHE A 1 453 ? 15.576  13.612  24.565  1.00 39.08  ? 453 PHE A CD2   1 
ATOM   3537  C CE1   . PHE A 1 453 ? 15.532  15.480  26.578  1.00 34.56  ? 453 PHE A CE1   1 
ATOM   3538  C CE2   . PHE A 1 453 ? 15.511  13.200  25.891  1.00 36.44  ? 453 PHE A CE2   1 
ATOM   3539  C CZ    . PHE A 1 453 ? 15.473  14.139  26.893  1.00 30.92  ? 453 PHE A CZ    1 
ATOM   3540  N N     . ASN A 1 454 ? 17.673  13.513  21.302  1.00 36.18  ? 454 ASN A N     1 
ATOM   3541  C CA    . ASN A 1 454 ? 18.213  12.173  21.256  1.00 38.47  ? 454 ASN A CA    1 
ATOM   3542  C C     . ASN A 1 454 ? 19.730  12.289  21.120  1.00 39.69  ? 454 ASN A C     1 
ATOM   3543  O O     . ASN A 1 454 ? 20.434  11.512  21.755  1.00 51.83  ? 454 ASN A O     1 
ATOM   3544  C CB    . ASN A 1 454 ? 17.528  11.303  20.202  1.00 37.10  ? 454 ASN A CB    1 
ATOM   3545  C CG    . ASN A 1 454 ? 16.251  10.642  20.704  1.00 38.05  ? 454 ASN A CG    1 
ATOM   3546  O OD1   . ASN A 1 454 ? 16.266  9.707   21.512  1.00 49.27  ? 454 ASN A OD1   1 
ATOM   3547  N ND2   . ASN A 1 454 ? 15.121  11.051  20.165  1.00 36.57  ? 454 ASN A ND2   1 
ATOM   3548  N N     . ILE A 1 455 ? 20.219  13.323  20.441  1.00 34.57  ? 455 ILE A N     1 
ATOM   3549  C CA    . ILE A 1 455 ? 21.654  13.473  20.188  1.00 42.51  ? 455 ILE A CA    1 
ATOM   3550  C C     . ILE A 1 455 ? 22.363  13.949  21.465  1.00 43.42  ? 455 ILE A C     1 
ATOM   3551  O O     . ILE A 1 455 ? 23.486  13.513  21.794  1.00 39.72  ? 455 ILE A O     1 
ATOM   3552  C CB    . ILE A 1 455 ? 21.936  14.391  18.966  1.00 35.68  ? 455 ILE A CB    1 
ATOM   3553  C CG1   . ILE A 1 455 ? 21.419  13.769  17.671  1.00 35.70  ? 455 ILE A CG1   1 
ATOM   3554  C CG2   . ILE A 1 455 ? 23.416  14.734  18.836  1.00 34.22  ? 455 ILE A CG2   1 
ATOM   3555  C CD1   . ILE A 1 455 ? 21.801  14.524  16.382  1.00 36.77  ? 455 ILE A CD1   1 
ATOM   3556  N N     . LEU A 1 456 ? 21.674  14.815  22.217  1.00 43.97  ? 456 LEU A N     1 
ATOM   3557  C CA    . LEU A 1 456 ? 22.195  15.315  23.480  1.00 43.87  ? 456 LEU A CA    1 
ATOM   3558  C C     . LEU A 1 456 ? 22.350  14.170  24.504  1.00 42.19  ? 456 LEU A C     1 
ATOM   3559  O O     . LEU A 1 456 ? 23.416  13.987  25.113  1.00 47.33  ? 456 LEU A O     1 
ATOM   3560  C CB    . LEU A 1 456 ? 21.284  16.454  23.952  1.00 42.18  ? 456 LEU A CB    1 
ATOM   3561  C CG    . LEU A 1 456 ? 21.398  17.784  23.197  1.00 39.63  ? 456 LEU A CG    1 
ATOM   3562  C CD1   . LEU A 1 456 ? 20.456  18.820  23.787  1.00 39.15  ? 456 LEU A CD1   1 
ATOM   3563  C CD2   . LEU A 1 456 ? 22.816  18.342  23.206  1.00 35.09  ? 456 LEU A CD2   1 
ATOM   3564  N N     . VAL A 1 457 ? 21.327  13.334  24.639  1.00 39.92  ? 457 VAL A N     1 
ATOM   3565  C CA    . VAL A 1 457 ? 21.404  12.142  25.489  1.00 42.30  ? 457 VAL A CA    1 
ATOM   3566  C C     . VAL A 1 457 ? 22.591  11.269  25.067  1.00 37.65  ? 457 VAL A C     1 
ATOM   3567  O O     . VAL A 1 457 ? 23.341  10.771  25.890  1.00 35.57  ? 457 VAL A O     1 
ATOM   3568  C CB    . VAL A 1 457 ? 20.091  11.326  25.490  1.00 38.40  ? 457 VAL A CB    1 
ATOM   3569  C CG1   . VAL A 1 457 ? 20.161  10.116  26.398  1.00 44.30  ? 457 VAL A CG1   1 
ATOM   3570  C CG2   . VAL A 1 457 ? 18.875  12.151  25.875  1.00 39.69  ? 457 VAL A CG2   1 
ATOM   3571  N N     . ASP A 1 458 ? 22.773  11.064  23.770  1.00 42.02  ? 458 ASP A N     1 
ATOM   3572  C CA    . ASP A 1 458 ? 23.771  10.124  23.297  1.00 35.60  ? 458 ASP A CA    1 
ATOM   3573  C C     . ASP A 1 458 ? 25.152  10.693  23.602  1.00 37.70  ? 458 ASP A C     1 
ATOM   3574  O O     . ASP A 1 458 ? 26.014  10.038  24.178  1.00 44.46  ? 458 ASP A O     1 
ATOM   3575  C CB    . ASP A 1 458 ? 23.585  9.857   21.805  1.00 39.46  ? 458 ASP A CB    1 
ATOM   3576  C CG    . ASP A 1 458 ? 22.332  9.089   21.403  1.00 42.21  ? 458 ASP A CG    1 
ATOM   3577  O OD1   . ASP A 1 458 ? 21.703  8.463   22.293  1.00 44.19  ? 458 ASP A OD1   1 
ATOM   3578  O OD2   . ASP A 1 458 ? 21.988  9.120   20.178  1.00 35.44  ? 458 ASP A OD2   1 
ATOM   3579  N N     . GLU A 1 459 ? 25.339  11.968  23.280  1.00 37.64  ? 459 GLU A N     1 
ATOM   3580  C CA    . GLU A 1 459 ? 26.664  12.539  23.363  1.00 35.25  ? 459 GLU A CA    1 
ATOM   3581  C C     . GLU A 1 459 ? 27.067  12.670  24.824  1.00 34.97  ? 459 GLU A C     1 
ATOM   3582  O O     . GLU A 1 459 ? 28.243  12.633  25.135  1.00 40.47  ? 459 GLU A O     1 
ATOM   3583  C CB    . GLU A 1 459 ? 26.675  13.832  22.549  1.00 37.30  ? 459 GLU A CB    1 
ATOM   3584  C CG    . GLU A 1 459 ? 26.630  13.532  21.048  1.00 39.13  ? 459 GLU A CG    1 
ATOM   3585  C CD    . GLU A 1 459 ? 26.785  14.650  20.029  1.00 41.91  ? 459 GLU A CD    1 
ATOM   3586  O OE1   . GLU A 1 459 ? 26.839  15.893  20.393  1.00 43.45  ? 459 GLU A OE1   1 
ATOM   3587  O OE2   . GLU A 1 459 ? 26.852  14.264  18.851  1.00 41.12  ? 459 GLU A OE2   1 
ATOM   3588  N N     . ALA A 1 460 ? 26.086  12.821  25.714  1.00 39.04  ? 460 ALA A N     1 
ATOM   3589  C CA    . ALA A 1 460 ? 26.352  13.071  27.123  1.00 37.89  ? 460 ALA A CA    1 
ATOM   3590  C C     . ALA A 1 460 ? 26.577  11.742  27.822  1.00 32.90  ? 460 ALA A C     1 
ATOM   3591  O O     . ALA A 1 460 ? 27.516  11.592  28.600  1.00 34.13  ? 460 ALA A O     1 
ATOM   3592  C CB    . ALA A 1 460 ? 25.195  13.813  27.726  1.00 42.38  ? 460 ALA A CB    1 
ATOM   3593  N N     . ALA A 1 461 ? 25.758  10.752  27.466  1.00 30.74  ? 461 ALA A N     1 
ATOM   3594  C CA    . ALA A 1 461 ? 26.019  9.401   27.938  1.00 29.72  ? 461 ALA A CA    1 
ATOM   3595  C C     . ALA A 1 461 ? 27.463  9.020   27.677  1.00 36.62  ? 461 ALA A C     1 
ATOM   3596  O O     . ALA A 1 461 ? 28.121  8.556   28.601  1.00 36.28  ? 461 ALA A O     1 
ATOM   3597  C CB    . ALA A 1 461 ? 25.103  8.431   27.340  1.00 27.39  ? 461 ALA A CB    1 
ATOM   3598  N N     . ALA A 1 462 ? 27.965  9.340   26.467  1.00 39.66  ? 462 ALA A N     1 
ATOM   3599  C CA    . ALA A 1 462 ? 29.285  8.916   26.039  1.00 38.24  ? 462 ALA A CA    1 
ATOM   3600  C C     . ALA A 1 462 ? 30.385  9.537   26.892  1.00 38.92  ? 462 ALA A C     1 
ATOM   3601  O O     . ALA A 1 462 ? 31.503  9.039   26.916  1.00 58.45  ? 462 ALA A O     1 
ATOM   3602  C CB    . ALA A 1 462 ? 29.458  9.305   24.589  1.00 41.10  ? 462 ALA A CB    1 
ATOM   3603  N N     . GLU A 1 463 ? 30.056  10.647  27.551  1.00 39.53  ? 463 GLU A N     1 
ATOM   3604  C CA    . GLU A 1 463 ? 30.977  11.380  28.387  1.00 38.21  ? 463 GLU A CA    1 
ATOM   3605  C C     . GLU A 1 463 ? 30.750  11.045  29.865  1.00 39.83  ? 463 GLU A C     1 
ATOM   3606  O O     . GLU A 1 463 ? 31.304  11.711  30.744  1.00 44.84  ? 463 GLU A O     1 
ATOM   3607  C CB    . GLU A 1 463 ? 30.782  12.857  28.064  1.00 37.74  ? 463 GLU A CB    1 
ATOM   3608  C CG    . GLU A 1 463 ? 31.125  13.228  26.632  1.00 42.87  ? 463 GLU A CG    1 
ATOM   3609  C CD    . GLU A 1 463 ? 32.598  13.230  26.229  1.00 45.53  ? 463 GLU A CD    1 
ATOM   3610  O OE1   . GLU A 1 463 ? 33.487  13.253  27.114  1.00 45.36  ? 463 GLU A OE1   1 
ATOM   3611  O OE2   . GLU A 1 463 ? 32.863  13.181  25.017  1.00 52.43  ? 463 GLU A OE2   1 
ATOM   3612  N N     . GLY A 1 464 ? 29.944  10.006  30.121  1.00 36.03  ? 464 GLY A N     1 
ATOM   3613  C CA    . GLY A 1 464 ? 29.616  9.545   31.462  1.00 43.36  ? 464 GLY A CA    1 
ATOM   3614  C C     . GLY A 1 464 ? 28.522  10.336  32.199  1.00 44.11  ? 464 GLY A C     1 
ATOM   3615  O O     . GLY A 1 464 ? 28.396  10.215  33.414  1.00 49.10  ? 464 GLY A O     1 
ATOM   3616  N N     . TYR A 1 465 ? 27.748  11.146  31.469  1.00 42.93  ? 465 TYR A N     1 
ATOM   3617  C CA    . TYR A 1 465 ? 26.698  11.957  32.048  1.00 42.95  ? 465 TYR A CA    1 
ATOM   3618  C C     . TYR A 1 465 ? 25.316  11.360  31.770  1.00 42.70  ? 465 TYR A C     1 
ATOM   3619  O O     . TYR A 1 465 ? 24.884  11.250  30.593  1.00 39.70  ? 465 TYR A O     1 
ATOM   3620  C CB    . TYR A 1 465 ? 26.737  13.373  31.475  1.00 42.01  ? 465 TYR A CB    1 
ATOM   3621  C CG    . TYR A 1 465 ? 28.087  14.019  31.398  1.00 38.84  ? 465 TYR A CG    1 
ATOM   3622  C CD1   . TYR A 1 465 ? 29.009  13.885  32.427  1.00 37.32  ? 465 TYR A CD1   1 
ATOM   3623  C CD2   . TYR A 1 465 ? 28.435  14.813  30.315  1.00 33.66  ? 465 TYR A CD2   1 
ATOM   3624  C CE1   . TYR A 1 465 ? 30.262  14.495  32.371  1.00 32.14  ? 465 TYR A CE1   1 
ATOM   3625  C CE2   . TYR A 1 465 ? 29.683  15.431  30.252  1.00 36.12  ? 465 TYR A CE2   1 
ATOM   3626  C CZ    . TYR A 1 465 ? 30.605  15.274  31.287  1.00 33.49  ? 465 TYR A CZ    1 
ATOM   3627  O OH    . TYR A 1 465 ? 31.834  15.941  31.270  1.00 35.28  ? 465 TYR A OH    1 
ATOM   3628  N N     . GLY A 1 466 ? 24.592  11.086  32.871  1.00 32.13  ? 466 GLY A N     1 
ATOM   3629  C CA    . GLY A 1 466 ? 23.295  10.428  32.785  1.00 34.18  ? 466 GLY A CA    1 
ATOM   3630  C C     . GLY A 1 466 ? 22.163  11.131  33.531  1.00 32.74  ? 466 GLY A C     1 
ATOM   3631  O O     . GLY A 1 466 ? 22.359  11.653  34.611  1.00 35.43  ? 466 GLY A O     1 
ATOM   3632  N N     . GLU A 1 467 ? 20.968  11.070  32.936  1.00 33.66  ? 467 GLU A N     1 
ATOM   3633  C CA    . GLU A 1 467 ? 19.762  11.765  33.353  1.00 32.35  ? 467 GLU A CA    1 
ATOM   3634  C C     . GLU A 1 467 ? 19.120  11.123  34.574  1.00 31.07  ? 467 GLU A C     1 
ATOM   3635  O O     . GLU A 1 467 ? 19.166  9.917   34.761  1.00 33.71  ? 467 GLU A O     1 
ATOM   3636  C CB    . GLU A 1 467 ? 18.740  11.690  32.215  1.00 34.02  ? 467 GLU A CB    1 
ATOM   3637  C CG    . GLU A 1 467 ? 17.406  12.379  32.491  1.00 36.41  ? 467 GLU A CG    1 
ATOM   3638  C CD    . GLU A 1 467 ? 17.526  13.858  32.822  1.00 39.31  ? 467 GLU A CD    1 
ATOM   3639  O OE1   . GLU A 1 467 ? 17.868  14.206  34.005  1.00 41.74  ? 467 GLU A OE1   1 
ATOM   3640  O OE2   . GLU A 1 467 ? 17.357  14.659  31.885  1.00 33.85  ? 467 GLU A OE2   1 
ATOM   3641  N N     . TYR A 1 468 ? 18.414  11.929  35.363  1.00 35.58  ? 468 TYR A N     1 
ATOM   3642  C CA    . TYR A 1 468 ? 17.838  11.424  36.604  1.00 40.24  ? 468 TYR A CA    1 
ATOM   3643  C C     . TYR A 1 468 ? 16.311  11.536  36.599  1.00 38.85  ? 468 TYR A C     1 
ATOM   3644  O O     . TYR A 1 468 ? 15.633  10.784  37.298  1.00 43.14  ? 468 TYR A O     1 
ATOM   3645  C CB    . TYR A 1 468 ? 18.520  12.107  37.794  1.00 36.32  ? 468 TYR A CB    1 
ATOM   3646  C CG    . TYR A 1 468 ? 18.058  13.511  38.095  1.00 38.77  ? 468 TYR A CG    1 
ATOM   3647  C CD1   . TYR A 1 468 ? 18.563  14.609  37.423  1.00 38.61  ? 468 TYR A CD1   1 
ATOM   3648  C CD2   . TYR A 1 468 ? 17.136  13.751  39.104  1.00 38.25  ? 468 TYR A CD2   1 
ATOM   3649  C CE1   . TYR A 1 468 ? 18.130  15.898  37.698  1.00 37.37  ? 468 TYR A CE1   1 
ATOM   3650  C CE2   . TYR A 1 468 ? 16.709  15.034  39.402  1.00 34.52  ? 468 TYR A CE2   1 
ATOM   3651  C CZ    . TYR A 1 468 ? 17.193  16.106  38.693  1.00 36.09  ? 468 TYR A CZ    1 
ATOM   3652  O OH    . TYR A 1 468 ? 16.757  17.345  39.034  1.00 37.75  ? 468 TYR A OH    1 
ATOM   3653  N N     . ARG A 1 469 ? 15.797  12.415  35.742  1.00 47.37  ? 469 ARG A N     1 
ATOM   3654  C CA    . ARG A 1 469 ? 14.383  12.732  35.622  1.00 48.18  ? 469 ARG A CA    1 
ATOM   3655  C C     . ARG A 1 469 ? 14.081  13.063  34.164  1.00 46.52  ? 469 ARG A C     1 
ATOM   3656  O O     . ARG A 1 469 ? 14.834  13.821  33.556  1.00 47.39  ? 469 ARG A O     1 
ATOM   3657  C CB    . ARG A 1 469 ? 14.104  13.953  36.501  1.00 52.54  ? 469 ARG A CB    1 
ATOM   3658  C CG    . ARG A 1 469 ? 12.689  14.003  37.049  1.00 58.03  ? 469 ARG A CG    1 
ATOM   3659  C CD    . ARG A 1 469 ? 12.373  15.335  37.691  1.00 57.95  ? 469 ARG A CD    1 
ATOM   3660  N NE    . ARG A 1 469 ? 10.953  15.415  37.964  1.00 54.42  ? 469 ARG A NE    1 
ATOM   3661  C CZ    . ARG A 1 469 ? 10.337  16.500  38.402  1.00 55.55  ? 469 ARG A CZ    1 
ATOM   3662  N NH1   . ARG A 1 469 ? 11.045  17.584  38.674  1.00 50.52  ? 469 ARG A NH1   1 
ATOM   3663  N NH2   . ARG A 1 469 ? 9.019   16.492  38.557  1.00 56.85  ? 469 ARG A NH2   1 
ATOM   3664  N N     . THR A 1 470 ? 13.004  12.514  33.590  1.00 43.08  ? 470 THR A N     1 
ATOM   3665  C CA    . THR A 1 470 ? 12.744  12.784  32.187  1.00 44.14  ? 470 THR A CA    1 
ATOM   3666  C C     . THR A 1 470 ? 11.261  12.683  31.842  1.00 45.90  ? 470 THR A C     1 
ATOM   3667  O O     . THR A 1 470 ? 10.466  12.271  32.667  1.00 47.95  ? 470 THR A O     1 
ATOM   3668  C CB    . THR A 1 470 ? 13.541  11.835  31.295  1.00 45.36  ? 470 THR A CB    1 
ATOM   3669  O OG1   . THR A 1 470 ? 13.478  12.392  29.991  1.00 42.25  ? 470 THR A OG1   1 
ATOM   3670  C CG2   . THR A 1 470 ? 13.005  10.421  31.262  1.00 49.29  ? 470 THR A CG2   1 
ATOM   3671  N N     . HIS A 1 471 ? 10.934  13.045  30.587  1.00 46.69  ? 471 HIS A N     1 
ATOM   3672  C CA    . HIS A 1 471 ? 9.599   12.980  30.015  1.00 41.24  ? 471 HIS A CA    1 
ATOM   3673  C C     . HIS A 1 471 ? 9.193   11.539  29.707  1.00 44.06  ? 471 HIS A C     1 
ATOM   3674  O O     . HIS A 1 471 ? 10.060  10.751  29.344  1.00 41.06  ? 471 HIS A O     1 
ATOM   3675  C CB    . HIS A 1 471 ? 9.588   13.867  28.768  1.00 49.10  ? 471 HIS A CB    1 
ATOM   3676  C CG    . HIS A 1 471 ? 8.285   14.027  28.034  1.00 60.02  ? 471 HIS A CG    1 
ATOM   3677  N ND1   . HIS A 1 471 ? 7.534   13.007  27.477  1.00 53.80  ? 471 HIS A ND1   1 
ATOM   3678  C CD2   . HIS A 1 471 ? 7.639   15.175  27.733  1.00 59.51  ? 471 HIS A CD2   1 
ATOM   3679  C CE1   . HIS A 1 471 ? 6.480   13.529  26.876  1.00 60.12  ? 471 HIS A CE1   1 
ATOM   3680  N NE2   . HIS A 1 471 ? 6.529   14.845  27.017  1.00 58.60  ? 471 HIS A NE2   1 
ATOM   3681  N N     . ILE A 1 472 ? 7.874   11.221  29.819  1.00 43.19  ? 472 ILE A N     1 
ATOM   3682  C CA    . ILE A 1 472 ? 7.306   9.901   29.527  1.00 44.25  ? 472 ILE A CA    1 
ATOM   3683  C C     . ILE A 1 472 ? 7.750   9.374   28.161  1.00 49.36  ? 472 ILE A C     1 
ATOM   3684  O O     . ILE A 1 472 ? 7.840   8.167   27.921  1.00 58.47  ? 472 ILE A O     1 
ATOM   3685  C CB    . ILE A 1 472 ? 5.762   9.925   29.576  1.00 51.17  ? 472 ILE A CB    1 
ATOM   3686  C CG1   . ILE A 1 472 ? 5.193   10.995  28.634  1.00 58.39  ? 472 ILE A CG1   1 
ATOM   3687  C CG2   . ILE A 1 472 ? 5.233   10.091  30.996  1.00 47.10  ? 472 ILE A CG2   1 
ATOM   3688  C CD1   . ILE A 1 472 ? 3.678   11.035  28.562  1.00 61.11  ? 472 ILE A CD1   1 
ATOM   3689  N N     . ARG A 1 473 ? 7.981   10.272  27.220  1.00 46.68  ? 473 ARG A N     1 
ATOM   3690  C CA    . ARG A 1 473 ? 8.376   9.843   25.893  1.00 57.46  ? 473 ARG A CA    1 
ATOM   3691  C C     . ARG A 1 473 ? 9.755   9.192   25.949  1.00 50.78  ? 473 ARG A C     1 
ATOM   3692  O O     . ARG A 1 473 ? 10.094  8.379   25.098  1.00 50.56  ? 473 ARG A O     1 
ATOM   3693  C CB    . ARG A 1 473 ? 8.328   11.045  24.935  1.00 65.91  ? 473 ARG A CB    1 
ATOM   3694  C CG    . ARG A 1 473 ? 9.104   10.859  23.636  1.00 65.84  ? 473 ARG A CG    1 
ATOM   3695  C CD    . ARG A 1 473 ? 8.725   11.899  22.591  1.00 67.91  ? 473 ARG A CD    1 
ATOM   3696  N NE    . ARG A 1 473 ? 9.038   11.475  21.227  1.00 69.33  ? 473 ARG A NE    1 
ATOM   3697  C CZ    . ARG A 1 473 ? 8.494   10.424  20.604  1.00 69.16  ? 473 ARG A CZ    1 
ATOM   3698  N NH1   . ARG A 1 473 ? 7.610   9.642   21.210  1.00 69.61  ? 473 ARG A NH1   1 
ATOM   3699  N NH2   . ARG A 1 473 ? 8.820   10.168  19.352  1.00 59.02  ? 473 ARG A NH2   1 
ATOM   3700  N N     . TYR A 1 474 ? 10.582  9.604   26.913  1.00 52.57  ? 474 TYR A N     1 
ATOM   3701  C CA    . TYR A 1 474 ? 11.997  9.286   26.858  1.00 46.31  ? 474 TYR A CA    1 
ATOM   3702  C C     . TYR A 1 474 ? 12.366  8.292   27.951  1.00 46.42  ? 474 TYR A C     1 
ATOM   3703  O O     . TYR A 1 474 ? 13.540  7.968   28.110  1.00 49.00  ? 474 TYR A O     1 
ATOM   3704  C CB    . TYR A 1 474 ? 12.814  10.564  26.966  1.00 43.43  ? 474 TYR A CB    1 
ATOM   3705  C CG    . TYR A 1 474 ? 12.648  11.515  25.815  1.00 42.28  ? 474 TYR A CG    1 
ATOM   3706  C CD1   . TYR A 1 474 ? 12.805  11.093  24.509  1.00 48.40  ? 474 TYR A CD1   1 
ATOM   3707  C CD2   . TYR A 1 474 ? 12.349  12.844  26.037  1.00 41.83  ? 474 TYR A CD2   1 
ATOM   3708  C CE1   . TYR A 1 474 ? 12.649  11.966  23.447  1.00 50.54  ? 474 TYR A CE1   1 
ATOM   3709  C CE2   . TYR A 1 474 ? 12.166  13.723  24.987  1.00 41.43  ? 474 TYR A CE2   1 
ATOM   3710  C CZ    . TYR A 1 474 ? 12.324  13.285  23.693  1.00 47.38  ? 474 TYR A CZ    1 
ATOM   3711  O OH    . TYR A 1 474 ? 12.143  14.155  22.658  1.00 56.80  ? 474 TYR A OH    1 
ATOM   3712  N N     . MET A 1 475 ? 11.353  7.759   28.639  1.00 39.50  ? 475 MET A N     1 
ATOM   3713  C CA    . MET A 1 475 ? 11.596  6.955   29.822  1.00 45.91  ? 475 MET A CA    1 
ATOM   3714  C C     . MET A 1 475 ? 12.368  5.681   29.490  1.00 42.24  ? 475 MET A C     1 
ATOM   3715  O O     . MET A 1 475 ? 13.208  5.255   30.287  1.00 44.52  ? 475 MET A O     1 
ATOM   3716  C CB    . MET A 1 475 ? 10.273  6.591   30.497  1.00 43.45  ? 475 MET A CB    1 
ATOM   3717  C CG    . MET A 1 475 ? 9.842   7.637   31.454  1.00 42.88  ? 475 MET A CG    1 
ATOM   3718  S SD    . MET A 1 475 ? 8.288   7.300   32.346  1.00 43.37  ? 475 MET A SD    1 
ATOM   3719  C CE    . MET A 1 475 ? 8.082   9.030   32.830  1.00 31.74  ? 475 MET A CE    1 
ATOM   3720  N N     . ASP A 1 476 ? 12.031  5.054   28.359  1.00 39.39  ? 476 ASP A N     1 
ATOM   3721  C CA    . ASP A 1 476 ? 12.696  3.823   27.932  1.00 47.24  ? 476 ASP A CA    1 
ATOM   3722  C C     . ASP A 1 476 ? 14.134  4.118   27.528  1.00 42.16  ? 476 ASP A C     1 
ATOM   3723  O O     . ASP A 1 476 ? 15.000  3.298   27.801  1.00 43.31  ? 476 ASP A O     1 
ATOM   3724  C CB    . ASP A 1 476 ? 12.011  3.119   26.760  1.00 49.38  ? 476 ASP A CB    1 
ATOM   3725  C CG    . ASP A 1 476 ? 10.986  2.099   27.201  1.00 55.65  ? 476 ASP A CG    1 
ATOM   3726  O OD1   . ASP A 1 476 ? 9.891   2.508   27.659  1.00 66.70  ? 476 ASP A OD1   1 
ATOM   3727  O OD2   . ASP A 1 476 ? 11.307  0.905   27.114  1.00 66.00  ? 476 ASP A OD2   1 
ATOM   3728  N N     . ARG A 1 477 ? 14.346  5.295   26.925  1.00 37.91  ? 477 ARG A N     1 
ATOM   3729  C CA    . ARG A 1 477 ? 15.642  5.746   26.465  1.00 42.03  ? 477 ARG A CA    1 
ATOM   3730  C C     . ARG A 1 477 ? 16.527  6.043   27.672  1.00 41.24  ? 477 ARG A C     1 
ATOM   3731  O O     . ARG A 1 477 ? 17.717  5.776   27.648  1.00 39.75  ? 477 ARG A O     1 
ATOM   3732  C CB    . ARG A 1 477 ? 15.491  6.968   25.545  1.00 44.76  ? 477 ARG A CB    1 
ATOM   3733  C CG    . ARG A 1 477 ? 16.802  7.560   25.034  1.00 50.89  ? 477 ARG A CG    1 
ATOM   3734  C CD    . ARG A 1 477 ? 17.686  6.659   24.158  1.00 52.61  ? 477 ARG A CD    1 
ATOM   3735  N NE    . ARG A 1 477 ? 19.093  7.071   23.993  1.00 42.75  ? 477 ARG A NE    1 
ATOM   3736  C CZ    . ARG A 1 477 ? 20.091  6.718   24.814  1.00 50.62  ? 477 ARG A CZ    1 
ATOM   3737  N NH1   . ARG A 1 477 ? 19.859  5.977   25.878  1.00 54.16  ? 477 ARG A NH1   1 
ATOM   3738  N NH2   . ARG A 1 477 ? 21.343  7.064   24.567  1.00 55.09  ? 477 ARG A NH2   1 
ATOM   3739  N N     . ILE A 1 478 ? 15.974  6.585   28.751  1.00 40.67  ? 478 ILE A N     1 
ATOM   3740  C CA    . ILE A 1 478 ? 16.855  6.928   29.850  1.00 40.06  ? 478 ILE A CA    1 
ATOM   3741  C C     . ILE A 1 478 ? 17.232  5.675   30.630  1.00 40.16  ? 478 ILE A C     1 
ATOM   3742  O O     . ILE A 1 478 ? 18.385  5.576   31.049  1.00 42.90  ? 478 ILE A O     1 
ATOM   3743  C CB    . ILE A 1 478 ? 16.279  8.052   30.721  1.00 37.81  ? 478 ILE A CB    1 
ATOM   3744  C CG1   . ILE A 1 478 ? 16.043  9.305   29.877  1.00 36.36  ? 478 ILE A CG1   1 
ATOM   3745  C CG2   . ILE A 1 478 ? 17.229  8.328   31.877  1.00 43.16  ? 478 ILE A CG2   1 
ATOM   3746  C CD1   . ILE A 1 478 ? 17.271  9.794   29.105  1.00 34.38  ? 478 ILE A CD1   1 
ATOM   3747  N N     . ALA A 1 479 ? 16.305  4.708   30.729  1.00 37.84  ? 479 ALA A N     1 
ATOM   3748  C CA    . ALA A 1 479 ? 16.582  3.387   31.291  1.00 40.03  ? 479 ALA A CA    1 
ATOM   3749  C C     . ALA A 1 479 ? 17.726  2.673   30.586  1.00 42.19  ? 479 ALA A C     1 
ATOM   3750  O O     . ALA A 1 479 ? 18.532  2.018   31.245  1.00 52.12  ? 479 ALA A O     1 
ATOM   3751  C CB    . ALA A 1 479 ? 15.358  2.505   31.264  1.00 39.01  ? 479 ALA A CB    1 
ATOM   3752  N N     . LYS A 1 480 ? 17.767  2.776   29.255  1.00 49.97  ? 480 LYS A N     1 
ATOM   3753  C CA    . LYS A 1 480 ? 18.795  2.148   28.433  1.00 51.29  ? 480 LYS A CA    1 
ATOM   3754  C C     . LYS A 1 480 ? 20.203  2.692   28.706  1.00 44.27  ? 480 LYS A C     1 
ATOM   3755  O O     . LYS A 1 480 ? 21.181  2.064   28.333  1.00 48.63  ? 480 LYS A O     1 
ATOM   3756  C CB    . LYS A 1 480 ? 18.508  2.410   26.948  1.00 66.12  ? 480 LYS A CB    1 
ATOM   3757  C CG    . LYS A 1 480 ? 17.508  1.495   26.241  1.00 77.07  ? 480 LYS A CG    1 
ATOM   3758  C CD    . LYS A 1 480 ? 17.048  2.046   24.850  1.00 95.82  ? 480 LYS A CD    1 
ATOM   3759  C CE    . LYS A 1 480 ? 18.139  2.426   23.851  1.00 91.42  ? 480 LYS A CE    1 
ATOM   3760  N NZ    . LYS A 1 480 ? 18.548  1.288   22.987  1.00 92.94  ? 480 LYS A NZ    1 
ATOM   3761  N N     . THR A 1 481 ? 20.331  3.895   29.263  1.00 41.45  ? 481 THR A N     1 
ATOM   3762  C CA    . THR A 1 481 ? 21.630  4.450   29.588  1.00 41.74  ? 481 THR A CA    1 
ATOM   3763  C C     . THR A 1 481 ? 22.207  3.773   30.834  1.00 39.50  ? 481 THR A C     1 
ATOM   3764  O O     . THR A 1 481 ? 23.404  3.840   31.046  1.00 38.67  ? 481 THR A O     1 
ATOM   3765  C CB    . THR A 1 481 ? 21.573  5.973   29.835  1.00 47.96  ? 481 THR A CB    1 
ATOM   3766  O OG1   . THR A 1 481 ? 20.680  6.265   30.894  1.00 58.34  ? 481 THR A OG1   1 
ATOM   3767  C CG2   . THR A 1 481 ? 21.048  6.791   28.687  1.00 49.62  ? 481 THR A CG2   1 
ATOM   3768  N N     . TYR A 1 482 ? 21.371  3.168   31.690  1.00 43.20  ? 482 TYR A N     1 
ATOM   3769  C CA    . TYR A 1 482 ? 21.840  2.564   32.940  1.00 43.21  ? 482 TYR A CA    1 
ATOM   3770  C C     . TYR A 1 482 ? 22.089  1.069   32.733  1.00 42.66  ? 482 TYR A C     1 
ATOM   3771  O O     . TYR A 1 482 ? 21.556  0.251   33.473  1.00 41.87  ? 482 TYR A O     1 
ATOM   3772  C CB    . TYR A 1 482 ? 20.858  2.884   34.088  1.00 41.55  ? 482 TYR A CB    1 
ATOM   3773  C CG    . TYR A 1 482 ? 20.956  4.324   34.516  1.00 36.03  ? 482 TYR A CG    1 
ATOM   3774  C CD1   . TYR A 1 482 ? 22.043  4.782   35.230  1.00 35.55  ? 482 TYR A CD1   1 
ATOM   3775  C CD2   . TYR A 1 482 ? 20.079  5.269   34.026  1.00 36.67  ? 482 TYR A CD2   1 
ATOM   3776  C CE1   . TYR A 1 482 ? 22.201  6.130   35.509  1.00 33.76  ? 482 TYR A CE1   1 
ATOM   3777  C CE2   . TYR A 1 482 ? 20.204  6.615   34.322  1.00 36.86  ? 482 TYR A CE2   1 
ATOM   3778  C CZ    . TYR A 1 482 ? 21.262  7.054   35.097  1.00 39.71  ? 482 TYR A CZ    1 
ATOM   3779  O OH    . TYR A 1 482 ? 21.448  8.420   35.372  1.00 45.57  ? 482 TYR A OH    1 
ATOM   3780  N N     . SER A 1 483 ? 22.983  0.746   31.779  1.00 43.16  ? 483 SER A N     1 
ATOM   3781  C CA    . SER A 1 483 ? 22.999  -0.541  31.099  1.00 43.11  ? 483 SER A CA    1 
ATOM   3782  C C     . SER A 1 483 ? 24.108  -1.488  31.573  1.00 38.85  ? 483 SER A C     1 
ATOM   3783  O O     . SER A 1 483 ? 24.314  -2.547  30.972  1.00 43.73  ? 483 SER A O     1 
ATOM   3784  C CB    . SER A 1 483 ? 23.088  -0.307  29.584  1.00 42.30  ? 483 SER A CB    1 
ATOM   3785  O OG    . SER A 1 483 ? 24.371  0.155   29.213  1.00 39.16  ? 483 SER A OG    1 
ATOM   3786  N N     . TRP A 1 484 ? 24.809  -1.151  32.660  1.00 39.39  ? 484 TRP A N     1 
ATOM   3787  C CA    . TRP A 1 484 ? 25.924  -1.970  33.106  1.00 40.78  ? 484 TRP A CA    1 
ATOM   3788  C C     . TRP A 1 484 ? 25.522  -3.442  33.292  1.00 47.70  ? 484 TRP A C     1 
ATOM   3789  O O     . TRP A 1 484 ? 24.436  -3.753  33.774  1.00 51.18  ? 484 TRP A O     1 
ATOM   3790  C CB    . TRP A 1 484 ? 26.528  -1.382  34.367  1.00 38.97  ? 484 TRP A CB    1 
ATOM   3791  C CG    . TRP A 1 484 ? 27.834  -2.018  34.731  1.00 41.70  ? 484 TRP A CG    1 
ATOM   3792  C CD1   . TRP A 1 484 ? 29.085  -1.764  34.225  1.00 35.48  ? 484 TRP A CD1   1 
ATOM   3793  C CD2   . TRP A 1 484 ? 27.997  -3.029  35.730  1.00 40.09  ? 484 TRP A CD2   1 
ATOM   3794  N NE1   . TRP A 1 484 ? 30.013  -2.548  34.863  1.00 35.36  ? 484 TRP A NE1   1 
ATOM   3795  C CE2   . TRP A 1 484 ? 29.378  -3.345  35.781  1.00 38.93  ? 484 TRP A CE2   1 
ATOM   3796  C CE3   . TRP A 1 484 ? 27.107  -3.689  36.577  1.00 39.32  ? 484 TRP A CE3   1 
ATOM   3797  C CZ2   . TRP A 1 484 ? 29.889  -4.307  36.654  1.00 37.05  ? 484 TRP A CZ2   1 
ATOM   3798  C CZ3   . TRP A 1 484 ? 27.614  -4.641  37.432  1.00 40.60  ? 484 TRP A CZ3   1 
ATOM   3799  C CH2   . TRP A 1 484 ? 28.983  -4.938  37.468  1.00 41.44  ? 484 TRP A CH2   1 
ATOM   3800  N N     . ASN A 1 485 ? 26.408  -4.344  32.847  1.00 45.78  ? 485 ASN A N     1 
ATOM   3801  C CA    . ASN A 1 485 ? 26.201  -5.790  32.882  1.00 46.48  ? 485 ASN A CA    1 
ATOM   3802  C C     . ASN A 1 485 ? 24.880  -6.204  32.226  1.00 43.69  ? 485 ASN A C     1 
ATOM   3803  O O     . ASN A 1 485 ? 24.058  -6.850  32.855  1.00 43.85  ? 485 ASN A O     1 
ATOM   3804  C CB    . ASN A 1 485 ? 26.312  -6.325  34.308  1.00 47.08  ? 485 ASN A CB    1 
ATOM   3805  C CG    . ASN A 1 485 ? 26.339  -7.828  34.336  1.00 46.87  ? 485 ASN A CG    1 
ATOM   3806  O OD1   . ASN A 1 485 ? 26.760  -8.443  33.368  1.00 50.12  ? 485 ASN A OD1   1 
ATOM   3807  N ND2   . ASN A 1 485 ? 25.857  -8.418  35.415  1.00 49.51  ? 485 ASN A ND2   1 
ATOM   3808  N N     . ASP A 1 486 ? 24.730  -5.908  30.925  1.00 43.16  ? 486 ASP A N     1 
ATOM   3809  C CA    . ASP A 1 486 ? 23.523  -6.210  30.167  1.00 43.11  ? 486 ASP A CA    1 
ATOM   3810  C C     . ASP A 1 486 ? 22.248  -5.868  30.962  1.00 38.78  ? 486 ASP A C     1 
ATOM   3811  O O     . ASP A 1 486 ? 21.383  -6.694  31.080  1.00 42.30  ? 486 ASP A O     1 
ATOM   3812  C CB    . ASP A 1 486 ? 23.519  -7.675  29.714  1.00 43.81  ? 486 ASP A CB    1 
ATOM   3813  C CG    . ASP A 1 486 ? 22.432  -7.984  28.703  1.00 47.90  ? 486 ASP A CG    1 
ATOM   3814  O OD1   . ASP A 1 486 ? 21.978  -7.032  28.017  1.00 55.60  ? 486 ASP A OD1   1 
ATOM   3815  O OD2   . ASP A 1 486 ? 21.991  -9.147  28.655  1.00 52.86  ? 486 ASP A OD2   1 
ATOM   3816  N N     . ASN A 1 487 ? 22.112  -4.648  31.496  1.00 38.55  ? 487 ASN A N     1 
ATOM   3817  C CA    . ASN A 1 487 ? 20.865  -4.168  32.086  1.00 41.51  ? 487 ASN A CA    1 
ATOM   3818  C C     . ASN A 1 487 ? 20.518  -4.913  33.387  1.00 35.27  ? 487 ASN A C     1 
ATOM   3819  O O     . ASN A 1 487 ? 19.363  -5.173  33.694  1.00 40.41  ? 487 ASN A O     1 
ATOM   3820  C CB    . ASN A 1 487 ? 19.754  -4.144  31.029  1.00 39.70  ? 487 ASN A CB    1 
ATOM   3821  C CG    . ASN A 1 487 ? 20.107  -3.210  29.890  1.00 39.45  ? 487 ASN A CG    1 
ATOM   3822  O OD1   . ASN A 1 487 ? 20.529  -3.681  28.849  1.00 45.24  ? 487 ASN A OD1   1 
ATOM   3823  N ND2   . ASN A 1 487 ? 20.046  -1.897  30.097  1.00 41.84  ? 487 ASN A ND2   1 
ATOM   3824  N N     . ALA A 1 488 ? 21.531  -5.184  34.203  1.00 32.62  ? 488 ALA A N     1 
ATOM   3825  C CA    . ALA A 1 488 ? 21.374  -5.970  35.407  1.00 37.32  ? 488 ALA A CA    1 
ATOM   3826  C C     . ALA A 1 488 ? 20.438  -5.270  36.387  1.00 42.51  ? 488 ALA A C     1 
ATOM   3827  O O     . ALA A 1 488 ? 19.606  -5.931  37.018  1.00 47.16  ? 488 ALA A O     1 
ATOM   3828  C CB    . ALA A 1 488 ? 22.723  -6.235  36.018  1.00 42.35  ? 488 ALA A CB    1 
ATOM   3829  N N     . LEU A 1 489 ? 20.579  -3.941  36.508  1.00 40.78  ? 489 LEU A N     1 
ATOM   3830  C CA    . LEU A 1 489 ? 19.759  -3.204  37.447  1.00 39.12  ? 489 LEU A CA    1 
ATOM   3831  C C     . LEU A 1 489 ? 18.291  -3.348  37.037  1.00 43.40  ? 489 LEU A C     1 
ATOM   3832  O O     . LEU A 1 489 ? 17.481  -3.653  37.916  1.00 33.76  ? 489 LEU A O     1 
ATOM   3833  C CB    . LEU A 1 489 ? 20.194  -1.737  37.591  1.00 33.17  ? 489 LEU A CB    1 
ATOM   3834  C CG    . LEU A 1 489 ? 19.488  -0.990  38.734  1.00 37.79  ? 489 LEU A CG    1 
ATOM   3835  C CD1   . LEU A 1 489 ? 19.644  -1.698  40.082  1.00 37.99  ? 489 LEU A CD1   1 
ATOM   3836  C CD2   . LEU A 1 489 ? 19.974  0.443   38.870  1.00 37.94  ? 489 LEU A CD2   1 
ATOM   3837  N N     . TRP A 1 490 ? 17.971  -3.181  35.727  1.00 42.88  ? 490 TRP A N     1 
ATOM   3838  C CA    . TRP A 1 490 ? 16.575  -3.179  35.278  1.00 40.83  ? 490 TRP A CA    1 
ATOM   3839  C C     . TRP A 1 490 ? 16.006  -4.598  35.313  1.00 44.00  ? 490 TRP A C     1 
ATOM   3840  O O     . TRP A 1 490 ? 14.825  -4.786  35.581  1.00 47.06  ? 490 TRP A O     1 
ATOM   3841  C CB    . TRP A 1 490 ? 16.361  -2.485  33.918  1.00 38.90  ? 490 TRP A CB    1 
ATOM   3842  C CG    . TRP A 1 490 ? 15.724  -1.128  34.039  1.00 39.73  ? 490 TRP A CG    1 
ATOM   3843  C CD1   . TRP A 1 490 ? 14.468  -0.755  33.632  1.00 44.44  ? 490 TRP A CD1   1 
ATOM   3844  C CD2   . TRP A 1 490 ? 16.278  0.023   34.694  1.00 35.41  ? 490 TRP A CD2   1 
ATOM   3845  N NE1   . TRP A 1 490 ? 14.226  0.558   33.958  1.00 39.76  ? 490 TRP A NE1   1 
ATOM   3846  C CE2   . TRP A 1 490 ? 15.318  1.049   34.621  1.00 37.95  ? 490 TRP A CE2   1 
ATOM   3847  C CE3   . TRP A 1 490 ? 17.508  0.287   35.307  1.00 41.09  ? 490 TRP A CE3   1 
ATOM   3848  C CZ2   . TRP A 1 490 ? 15.562  2.323   35.132  1.00 42.88  ? 490 TRP A CZ2   1 
ATOM   3849  C CZ3   . TRP A 1 490 ? 17.730  1.531   35.856  1.00 36.19  ? 490 TRP A CZ3   1 
ATOM   3850  C CH2   . TRP A 1 490 ? 16.772  2.533   35.763  1.00 41.19  ? 490 TRP A CH2   1 
ATOM   3851  N N     . LYS A 1 491 ? 16.869  -5.605  35.182  1.00 45.54  ? 491 LYS A N     1 
ATOM   3852  C CA    . LYS A 1 491 ? 16.448  -6.980  35.416  1.00 45.48  ? 491 LYS A CA    1 
ATOM   3853  C C     . LYS A 1 491 ? 15.951  -7.156  36.842  1.00 44.00  ? 491 LYS A C     1 
ATOM   3854  O O     . LYS A 1 491 ? 14.931  -7.800  37.062  1.00 46.90  ? 491 LYS A O     1 
ATOM   3855  C CB    . LYS A 1 491 ? 17.591  -7.944  35.091  1.00 44.37  ? 491 LYS A CB    1 
ATOM   3856  C CG    . LYS A 1 491 ? 17.661  -8.211  33.597  1.00 48.04  ? 491 LYS A CG    1 
ATOM   3857  C CD    . LYS A 1 491 ? 18.990  -8.670  33.072  1.00 53.66  ? 491 LYS A CD    1 
ATOM   3858  C CE    . LYS A 1 491 ? 19.015  -8.723  31.553  1.00 49.68  ? 491 LYS A CE    1 
ATOM   3859  N NZ    . LYS A 1 491 ? 20.207  -9.461  31.079  1.00 47.05  ? 491 LYS A NZ    1 
ATOM   3860  N N     . MET A 1 492 ? 16.653  -6.564  37.805  1.00 38.12  ? 492 MET A N     1 
ATOM   3861  C CA    . MET A 1 492 ? 16.204  -6.700  39.174  1.00 46.86  ? 492 MET A CA    1 
ATOM   3862  C C     . MET A 1 492 ? 14.835  -6.019  39.380  1.00 51.82  ? 492 MET A C     1 
ATOM   3863  O O     . MET A 1 492 ? 13.949  -6.608  40.017  1.00 50.26  ? 492 MET A O     1 
ATOM   3864  C CB    . MET A 1 492 ? 17.227  -6.115  40.146  1.00 44.05  ? 492 MET A CB    1 
ATOM   3865  C CG    . MET A 1 492 ? 16.770  -6.247  41.553  1.00 44.24  ? 492 MET A CG    1 
ATOM   3866  S SD    . MET A 1 492 ? 17.667  -5.228  42.643  1.00 50.40  ? 492 MET A SD    1 
ATOM   3867  C CE    . MET A 1 492 ? 16.970  -3.637  42.208  1.00 50.00  ? 492 MET A CE    1 
ATOM   3868  N N     . HIS A 1 493 ? 14.684  -4.781  38.858  1.00 45.62  ? 493 HIS A N     1 
ATOM   3869  C CA    . HIS A 1 493 ? 13.447  -4.023  38.932  1.00 50.03  ? 493 HIS A CA    1 
ATOM   3870  C C     . HIS A 1 493 ? 12.296  -4.868  38.383  1.00 45.43  ? 493 HIS A C     1 
ATOM   3871  O O     . HIS A 1 493 ? 11.193  -4.805  38.900  1.00 50.90  ? 493 HIS A O     1 
ATOM   3872  C CB    . HIS A 1 493 ? 13.527  -2.687  38.163  1.00 52.04  ? 493 HIS A CB    1 
ATOM   3873  C CG    . HIS A 1 493 ? 14.406  -1.617  38.721  1.00 46.20  ? 493 HIS A CG    1 
ATOM   3874  N ND1   . HIS A 1 493 ? 14.482  -1.314  40.057  1.00 49.08  ? 493 HIS A ND1   1 
ATOM   3875  C CD2   . HIS A 1 493 ? 15.243  -0.769  38.123  1.00 48.40  ? 493 HIS A CD2   1 
ATOM   3876  C CE1   . HIS A 1 493 ? 15.340  -0.319  40.246  1.00 44.84  ? 493 HIS A CE1   1 
ATOM   3877  N NE2   . HIS A 1 493 ? 15.843  0.004   39.098  1.00 45.20  ? 493 HIS A NE2   1 
ATOM   3878  N N     . GLU A 1 494 ? 12.550  -5.617  37.304  1.00 56.18  ? 494 GLU A N     1 
ATOM   3879  C CA    . GLU A 1 494 ? 11.514  -6.405  36.643  1.00 62.24  ? 494 GLU A CA    1 
ATOM   3880  C C     . GLU A 1 494 ? 11.189  -7.608  37.530  1.00 58.61  ? 494 GLU A C     1 
ATOM   3881  O O     . GLU A 1 494 ? 10.038  -8.020  37.617  1.00 56.83  ? 494 GLU A O     1 
ATOM   3882  C CB    . GLU A 1 494 ? 11.923  -6.832  35.223  1.00 58.93  ? 494 GLU A CB    1 
ATOM   3883  C CG    . GLU A 1 494 ? 12.190  -5.686  34.224  1.00 69.21  ? 494 GLU A CG    1 
ATOM   3884  C CD    . GLU A 1 494 ? 11.088  -5.138  33.305  1.00 91.08  ? 494 GLU A CD    1 
ATOM   3885  O OE1   . GLU A 1 494 ? 9.853   -5.437  33.508  1.00 81.31  ? 494 GLU A OE1   1 
ATOM   3886  O OE2   . GLU A 1 494 ? 11.463  -4.383  32.348  1.00 82.56  ? 494 GLU A OE2   1 
ATOM   3887  N N     . THR A 1 495 ? 12.199  -8.158  38.217  1.00 54.40  ? 495 THR A N     1 
ATOM   3888  C CA    . THR A 1 495 ? 11.948  -9.192  39.212  1.00 52.06  ? 495 THR A CA    1 
ATOM   3889  C C     . THR A 1 495 ? 10.979  -8.638  40.270  1.00 55.68  ? 495 THR A C     1 
ATOM   3890  O O     . THR A 1 495 ? 9.961   -9.252  40.579  1.00 54.88  ? 495 THR A O     1 
ATOM   3891  C CB    . THR A 1 495 ? 13.270  -9.759  39.753  1.00 48.03  ? 495 THR A CB    1 
ATOM   3892  O OG1   . THR A 1 495 ? 13.883  -10.568 38.746  1.00 46.81  ? 495 THR A OG1   1 
ATOM   3893  C CG2   . THR A 1 495 ? 13.116  -10.629 40.984  1.00 42.84  ? 495 THR A CG2   1 
ATOM   3894  N N     . ILE A 1 496 ? 11.253  -7.437  40.771  1.00 50.61  ? 496 ILE A N     1 
ATOM   3895  C CA    . ILE A 1 496 ? 10.421  -6.863  41.806  1.00 52.81  ? 496 ILE A CA    1 
ATOM   3896  C C     . ILE A 1 496 ? 9.047   -6.542  41.230  1.00 50.34  ? 496 ILE A C     1 
ATOM   3897  O O     . ILE A 1 496 ? 8.051   -6.635  41.943  1.00 56.29  ? 496 ILE A O     1 
ATOM   3898  C CB    . ILE A 1 496 ? 11.124  -5.655  42.458  1.00 48.64  ? 496 ILE A CB    1 
ATOM   3899  C CG1   . ILE A 1 496 ? 12.225  -6.121  43.406  1.00 55.33  ? 496 ILE A CG1   1 
ATOM   3900  C CG2   . ILE A 1 496 ? 10.157  -4.751  43.192  1.00 50.99  ? 496 ILE A CG2   1 
ATOM   3901  C CD1   . ILE A 1 496 ? 13.263  -5.057  43.711  1.00 59.71  ? 496 ILE A CD1   1 
ATOM   3902  N N     . LYS A 1 497 ? 8.994   -6.167  39.952  1.00 49.56  ? 497 LYS A N     1 
ATOM   3903  C CA    . LYS A 1 497 ? 7.744   -5.716  39.363  1.00 48.56  ? 497 LYS A CA    1 
ATOM   3904  C C     . LYS A 1 497 ? 6.792   -6.897  39.227  1.00 45.37  ? 497 LYS A C     1 
ATOM   3905  O O     . LYS A 1 497 ? 5.618   -6.765  39.522  1.00 53.96  ? 497 LYS A O     1 
ATOM   3906  C CB    . LYS A 1 497 ? 7.979   -5.069  38.001  1.00 51.06  ? 497 LYS A CB    1 
ATOM   3907  C CG    . LYS A 1 497 ? 6.704   -4.693  37.252  1.00 55.68  ? 497 LYS A CG    1 
ATOM   3908  C CD    . LYS A 1 497 ? 6.016   -3.426  37.727  1.00 56.31  ? 497 LYS A CD    1 
ATOM   3909  C CE    . LYS A 1 497 ? 4.735   -3.160  36.961  1.00 50.49  ? 497 LYS A CE    1 
ATOM   3910  N NZ    . LYS A 1 497 ? 3.891   -2.164  37.659  1.00 53.87  ? 497 LYS A NZ    1 
ATOM   3911  N N     . ASP A 1 498 ? 7.330   -8.045  38.802  1.00 47.53  ? 498 ASP A N     1 
ATOM   3912  C CA    . ASP A 1 498 ? 6.587   -9.272  38.576  1.00 47.37  ? 498 ASP A CA    1 
ATOM   3913  C C     . ASP A 1 498 ? 6.062   -9.862  39.881  1.00 51.93  ? 498 ASP A C     1 
ATOM   3914  O O     . ASP A 1 498 ? 5.118   -10.646 39.861  1.00 62.16  ? 498 ASP A O     1 
ATOM   3915  C CB    . ASP A 1 498 ? 7.455   -10.260 37.794  1.00 48.80  ? 498 ASP A CB    1 
ATOM   3916  C CG    . ASP A 1 498 ? 7.702   -9.803  36.353  1.00 55.99  ? 498 ASP A CG    1 
ATOM   3917  O OD1   . ASP A 1 498 ? 7.050   -8.808  35.897  1.00 42.57  ? 498 ASP A OD1   1 
ATOM   3918  O OD2   . ASP A 1 498 ? 8.565   -10.418 35.693  1.00 51.72  ? 498 ASP A OD2   1 
ATOM   3919  N N     . ALA A 1 499 ? 6.680   -9.500  41.005  1.00 54.04  ? 499 ALA A N     1 
ATOM   3920  C CA    . ALA A 1 499 ? 6.303   -10.013 42.311  1.00 54.87  ? 499 ALA A CA    1 
ATOM   3921  C C     . ALA A 1 499 ? 5.222   -9.128  42.937  1.00 53.74  ? 499 ALA A C     1 
ATOM   3922  O O     . ALA A 1 499 ? 4.221   -9.634  43.426  1.00 59.32  ? 499 ALA A O     1 
ATOM   3923  C CB    . ALA A 1 499 ? 7.535   -10.087 43.177  1.00 60.94  ? 499 ALA A CB    1 
ATOM   3924  N N     . LEU A 1 500 ? 5.413   -7.806  42.920  1.00 44.52  ? 500 LEU A N     1 
ATOM   3925  C CA    . LEU A 1 500 ? 4.448   -6.896  43.499  1.00 48.12  ? 500 LEU A CA    1 
ATOM   3926  C C     . LEU A 1 500 ? 3.214   -6.747  42.612  1.00 61.85  ? 500 LEU A C     1 
ATOM   3927  O O     . LEU A 1 500 ? 2.108   -6.564  43.120  1.00 59.43  ? 500 LEU A O     1 
ATOM   3928  C CB    . LEU A 1 500 ? 5.120   -5.533  43.675  1.00 49.87  ? 500 LEU A CB    1 
ATOM   3929  C CG    . LEU A 1 500 ? 6.147   -5.442  44.799  1.00 49.37  ? 500 LEU A CG    1 
ATOM   3930  C CD1   . LEU A 1 500 ? 6.682   -4.017  44.925  1.00 45.33  ? 500 LEU A CD1   1 
ATOM   3931  C CD2   . LEU A 1 500 ? 5.517   -5.900  46.113  1.00 53.13  ? 500 LEU A CD2   1 
ATOM   3932  N N     . ASP A 1 501 ? 3.443   -6.690  41.290  1.00 63.21  ? 501 ASP A N     1 
ATOM   3933  C CA    . ASP A 1 501 ? 2.397   -6.421  40.320  1.00 53.16  ? 501 ASP A CA    1 
ATOM   3934  C C     . ASP A 1 501 ? 2.445   -7.524  39.272  1.00 58.14  ? 501 ASP A C     1 
ATOM   3935  O O     . ASP A 1 501 ? 2.874   -7.298  38.143  1.00 63.70  ? 501 ASP A O     1 
ATOM   3936  C CB    . ASP A 1 501 ? 2.539   -5.024  39.709  1.00 53.85  ? 501 ASP A CB    1 
ATOM   3937  C CG    . ASP A 1 501 ? 1.403   -4.661  38.772  1.00 54.37  ? 501 ASP A CG    1 
ATOM   3938  O OD1   . ASP A 1 501 ? 0.519   -5.515  38.588  1.00 61.84  ? 501 ASP A OD1   1 
ATOM   3939  O OD2   . ASP A 1 501 ? 1.396   -3.517  38.270  1.00 63.27  ? 501 ASP A OD2   1 
ATOM   3940  N N     . PRO A 1 502 ? 2.023   -8.760  39.613  1.00 63.72  ? 502 PRO A N     1 
ATOM   3941  C CA    . PRO A 1 502 ? 2.058   -9.858  38.645  1.00 64.67  ? 502 PRO A CA    1 
ATOM   3942  C C     . PRO A 1 502 ? 1.197   -9.594  37.401  1.00 64.82  ? 502 PRO A C     1 
ATOM   3943  O O     . PRO A 1 502 ? 1.519   -10.114 36.336  1.00 53.71  ? 502 PRO A O     1 
ATOM   3944  C CB    . PRO A 1 502 ? 1.622   -11.083 39.479  1.00 58.35  ? 502 PRO A CB    1 
ATOM   3945  C CG    . PRO A 1 502 ? 0.853   -10.492 40.646  1.00 61.16  ? 502 PRO A CG    1 
ATOM   3946  C CD    . PRO A 1 502 ? 1.537   -9.179  40.939  1.00 61.98  ? 502 PRO A CD    1 
ATOM   3947  N N     . ASN A 1 503 ? 0.145   -8.758  37.506  1.00 65.46  ? 503 ASN A N     1 
ATOM   3948  C CA    . ASN A 1 503 ? -0.790  -8.571  36.398  1.00 69.59  ? 503 ASN A CA    1 
ATOM   3949  C C     . ASN A 1 503 ? -0.533  -7.264  35.656  1.00 70.98  ? 503 ASN A C     1 
ATOM   3950  O O     . ASN A 1 503 ? -1.384  -6.844  34.880  1.00 69.06  ? 503 ASN A O     1 
ATOM   3951  C CB    . ASN A 1 503 ? -2.264  -8.540  36.829  1.00 70.48  ? 503 ASN A CB    1 
ATOM   3952  C CG    . ASN A 1 503 ? -2.791  -9.869  37.340  1.00 67.26  ? 503 ASN A CG    1 
ATOM   3953  O OD1   . ASN A 1 503 ? -2.541  -10.927 36.758  1.00 58.65  ? 503 ASN A OD1   1 
ATOM   3954  N ND2   . ASN A 1 503 ? -3.499  -9.826  38.457  1.00 64.50  ? 503 ASN A ND2   1 
ATOM   3955  N N     . GLY A 1 504 ? 0.605   -6.616  35.941  1.00 69.68  ? 504 GLY A N     1 
ATOM   3956  C CA    . GLY A 1 504 ? 1.035   -5.402  35.259  1.00 63.81  ? 504 GLY A CA    1 
ATOM   3957  C C     . GLY A 1 504 ? -0.047  -4.334  35.091  1.00 58.11  ? 504 GLY A C     1 
ATOM   3958  O O     . GLY A 1 504 ? -0.209  -3.816  33.987  1.00 62.43  ? 504 GLY A O     1 
ATOM   3959  N N     . ILE A 1 505 ? -0.723  -3.956  36.187  1.00 50.87  ? 505 ILE A N     1 
ATOM   3960  C CA    . ILE A 1 505 ? -1.772  -2.944  36.144  1.00 55.43  ? 505 ILE A CA    1 
ATOM   3961  C C     . ILE A 1 505 ? -1.298  -1.580  36.651  1.00 57.77  ? 505 ILE A C     1 
ATOM   3962  O O     . ILE A 1 505 ? -2.078  -0.632  36.640  1.00 65.75  ? 505 ILE A O     1 
ATOM   3963  C CB    . ILE A 1 505 ? -3.035  -3.413  36.900  1.00 66.63  ? 505 ILE A CB    1 
ATOM   3964  C CG1   . ILE A 1 505 ? -2.744  -3.838  38.342  1.00 66.94  ? 505 ILE A CG1   1 
ATOM   3965  C CG2   . ILE A 1 505 ? -3.738  -4.518  36.123  1.00 75.60  ? 505 ILE A CG2   1 
ATOM   3966  C CD1   . ILE A 1 505 ? -2.624  -2.684  39.295  1.00 69.24  ? 505 ILE A CD1   1 
ATOM   3967  N N     . LEU A 1 506 ? -0.043  -1.448  37.109  1.00 63.40  ? 506 LEU A N     1 
ATOM   3968  C CA    . LEU A 1 506 ? 0.444   -0.141  37.530  1.00 61.89  ? 506 LEU A CA    1 
ATOM   3969  C C     . LEU A 1 506 ? 1.414   0.455   36.504  1.00 57.05  ? 506 LEU A C     1 
ATOM   3970  O O     . LEU A 1 506 ? 2.442   -0.141  36.198  1.00 57.90  ? 506 LEU A O     1 
ATOM   3971  C CB    . LEU A 1 506 ? 1.082   -0.239  38.919  1.00 66.58  ? 506 LEU A CB    1 
ATOM   3972  C CG    . LEU A 1 506 ? 0.144   -0.069  40.119  1.00 73.38  ? 506 LEU A CG    1 
ATOM   3973  C CD1   . LEU A 1 506 ? 0.901   0.435   41.340  1.00 79.13  ? 506 LEU A CD1   1 
ATOM   3974  C CD2   . LEU A 1 506 ? -1.008  0.873   39.818  1.00 78.68  ? 506 LEU A CD2   1 
ATOM   3975  N N     . ALA A 1 507 ? 1.024   1.630   35.977  1.00 54.70  ? 507 ALA A N     1 
ATOM   3976  C CA    . ALA A 1 507 ? 1.854   2.558   35.226  1.00 53.28  ? 507 ALA A CA    1 
ATOM   3977  C C     . ALA A 1 507 ? 2.876   1.827   34.365  1.00 56.43  ? 507 ALA A C     1 
ATOM   3978  O O     . ALA A 1 507 ? 4.074   2.099   34.423  1.00 50.43  ? 507 ALA A O     1 
ATOM   3979  C CB    . ALA A 1 507 ? 2.519   3.531   36.154  1.00 51.11  ? 507 ALA A CB    1 
ATOM   3980  N N     . PRO A 1 508 ? 2.419   0.919   33.484  1.00 60.72  ? 508 PRO A N     1 
ATOM   3981  C CA    . PRO A 1 508 ? 3.337   0.104   32.700  1.00 62.82  ? 508 PRO A CA    1 
ATOM   3982  C C     . PRO A 1 508 ? 4.222   1.062   31.905  1.00 54.87  ? 508 PRO A C     1 
ATOM   3983  O O     . PRO A 1 508 ? 3.774   2.057   31.335  1.00 55.12  ? 508 PRO A O     1 
ATOM   3984  C CB    . PRO A 1 508 ? 2.416   -0.814  31.888  1.00 68.74  ? 508 PRO A CB    1 
ATOM   3985  C CG    . PRO A 1 508 ? 1.118   -0.038  31.813  1.00 72.30  ? 508 PRO A CG    1 
ATOM   3986  C CD    . PRO A 1 508 ? 1.015   0.699   33.133  1.00 64.01  ? 508 PRO A CD    1 
ATOM   3987  N N     . GLY A 1 509 ? 5.525   0.818   32.023  1.00 62.83  ? 509 GLY A N     1 
ATOM   3988  C CA    . GLY A 1 509 ? 6.532   1.593   31.326  1.00 60.33  ? 509 GLY A CA    1 
ATOM   3989  C C     . GLY A 1 509 ? 7.056   2.792   32.104  1.00 47.96  ? 509 GLY A C     1 
ATOM   3990  O O     . GLY A 1 509 ? 7.831   3.551   31.533  1.00 45.31  ? 509 GLY A O     1 
ATOM   3991  N N     . LYS A 1 510 ? 6.639   2.983   33.367  1.00 47.13  ? 510 LYS A N     1 
ATOM   3992  C CA    . LYS A 1 510 ? 7.218   4.059   34.171  1.00 49.75  ? 510 LYS A CA    1 
ATOM   3993  C C     . LYS A 1 510 ? 8.688   3.713   34.406  1.00 39.83  ? 510 LYS A C     1 
ATOM   3994  O O     . LYS A 1 510 ? 9.019   2.551   34.651  1.00 39.21  ? 510 LYS A O     1 
ATOM   3995  C CB    . LYS A 1 510 ? 6.441   4.279   35.478  1.00 58.42  ? 510 LYS A CB    1 
ATOM   3996  C CG    . LYS A 1 510 ? 6.962   5.364   36.426  1.00 57.81  ? 510 LYS A CG    1 
ATOM   3997  C CD    . LYS A 1 510 ? 6.843   6.794   35.924  1.00 63.91  ? 510 LYS A CD    1 
ATOM   3998  C CE    . LYS A 1 510 ? 7.614   7.830   36.734  1.00 63.86  ? 510 LYS A CE    1 
ATOM   3999  N NZ    . LYS A 1 510 ? 9.033   7.974   36.309  1.00 62.81  ? 510 LYS A NZ    1 
ATOM   4000  N N     . SER A 1 511 ? 9.572   4.690   34.180  1.00 40.87  ? 511 SER A N     1 
ATOM   4001  C CA    . SER A 1 511 ? 11.017  4.525   34.342  1.00 40.95  ? 511 SER A CA    1 
ATOM   4002  C C     . SER A 1 511 ? 11.578  3.350   33.548  1.00 39.45  ? 511 SER A C     1 
ATOM   4003  O O     . SER A 1 511 ? 12.683  2.887   33.830  1.00 43.52  ? 511 SER A O     1 
ATOM   4004  C CB    . SER A 1 511 ? 11.380  4.374   35.802  1.00 37.69  ? 511 SER A CB    1 
ATOM   4005  O OG    . SER A 1 511 ? 10.922  5.505   36.544  1.00 39.60  ? 511 SER A OG    1 
ATOM   4006  N N     . GLY A 1 512 ? 10.838  2.874   32.543  1.00 38.69  ? 512 GLY A N     1 
ATOM   4007  C CA    . GLY A 1 512 ? 11.310  1.757   31.742  1.00 37.82  ? 512 GLY A CA    1 
ATOM   4008  C C     . GLY A 1 512 ? 10.954  0.384   32.300  1.00 40.51  ? 512 GLY A C     1 
ATOM   4009  O O     . GLY A 1 512 ? 11.466  -0.637  31.821  1.00 49.65  ? 512 GLY A O     1 
ATOM   4010  N N     . ILE A 1 513 ? 10.074  0.339   33.303  1.00 42.63  ? 513 ILE A N     1 
ATOM   4011  C CA    . ILE A 1 513 ? 9.769   -0.926  33.935  1.00 39.64  ? 513 ILE A CA    1 
ATOM   4012  C C     . ILE A 1 513 ? 8.449   -1.438  33.373  1.00 44.13  ? 513 ILE A C     1 
ATOM   4013  O O     . ILE A 1 513 ? 7.446   -0.740  33.500  1.00 48.37  ? 513 ILE A O     1 
ATOM   4014  C CB    . ILE A 1 513 ? 9.723   -0.731  35.457  1.00 43.11  ? 513 ILE A CB    1 
ATOM   4015  C CG1   . ILE A 1 513 ? 11.054  -0.192  35.997  1.00 45.52  ? 513 ILE A CG1   1 
ATOM   4016  C CG2   . ILE A 1 513 ? 9.311   -2.039  36.120  1.00 45.43  ? 513 ILE A CG2   1 
ATOM   4017  C CD1   . ILE A 1 513 ? 10.950  0.515   37.335  1.00 39.85  ? 513 ILE A CD1   1 
ATOM   4018  N N     . TRP A 1 514 ? 8.442   -2.650  32.785  1.00 50.28  ? 514 TRP A N     1 
ATOM   4019  C CA    . TRP A 1 514 ? 7.318   -3.040  31.948  1.00 59.63  ? 514 TRP A CA    1 
ATOM   4020  C C     . TRP A 1 514 ? 6.483   -4.176  32.555  1.00 64.17  ? 514 TRP A C     1 
ATOM   4021  O O     . TRP A 1 514 ? 5.246   -4.118  32.519  1.00 67.13  ? 514 TRP A O     1 
ATOM   4022  C CB    . TRP A 1 514 ? 7.780   -3.307  30.506  1.00 56.51  ? 514 TRP A CB    1 
ATOM   4023  C CG    . TRP A 1 514 ? 7.941   -2.048  29.700  1.00 51.89  ? 514 TRP A CG    1 
ATOM   4024  C CD1   . TRP A 1 514 ? 9.120   -1.422  29.449  1.00 49.56  ? 514 TRP A CD1   1 
ATOM   4025  C CD2   . TRP A 1 514 ? 6.930   -1.252  29.041  1.00 52.57  ? 514 TRP A CD2   1 
ATOM   4026  N NE1   . TRP A 1 514 ? 8.913   -0.292  28.709  1.00 55.06  ? 514 TRP A NE1   1 
ATOM   4027  C CE2   . TRP A 1 514 ? 7.582   -0.163  28.432  1.00 51.26  ? 514 TRP A CE2   1 
ATOM   4028  C CE3   . TRP A 1 514 ? 5.544   -1.345  28.880  1.00 58.64  ? 514 TRP A CE3   1 
ATOM   4029  C CZ2   . TRP A 1 514 ? 6.910   0.817   27.701  1.00 51.55  ? 514 TRP A CZ2   1 
ATOM   4030  C CZ3   . TRP A 1 514 ? 4.872   -0.371  28.171  1.00 54.25  ? 514 TRP A CZ3   1 
ATOM   4031  C CH2   . TRP A 1 514 ? 5.546   0.697   27.589  1.00 51.86  ? 514 TRP A CH2   1 
ATOM   4032  N N     . GLY A 1 515 ? 7.138   -5.206  33.093  1.00 59.71  ? 515 GLY A N     1 
ATOM   4033  C CA    . GLY A 1 515 ? 6.413   -6.361  33.611  1.00 58.15  ? 515 GLY A CA    1 
ATOM   4034  C C     . GLY A 1 515 ? 6.151   -7.423  32.542  1.00 53.21  ? 515 GLY A C     1 
ATOM   4035  O O     . GLY A 1 515 ? 5.770   -7.066  31.433  1.00 60.77  ? 515 GLY A O     1 
ATOM   4036  N N     . LYS A 1 516 ? 6.251   -8.709  32.935  1.00 53.79  ? 516 LYS A N     1 
ATOM   4037  C CA    . LYS A 1 516 ? 6.347   -9.881  32.062  1.00 58.90  ? 516 LYS A CA    1 
ATOM   4038  C C     . LYS A 1 516 ? 5.313   -9.911  30.933  1.00 57.64  ? 516 LYS A C     1 
ATOM   4039  O O     . LYS A 1 516 ? 5.615   -10.398 29.839  1.00 59.40  ? 516 LYS A O     1 
ATOM   4040  C CB    . LYS A 1 516 ? 6.169   -11.192 32.836  1.00 63.05  ? 516 LYS A CB    1 
ATOM   4041  C CG    . LYS A 1 516 ? 6.766   -12.416 32.149  1.00 77.44  ? 516 LYS A CG    1 
ATOM   4042  C CD    . LYS A 1 516 ? 6.257   -13.730 32.718  1.00 94.02  ? 516 LYS A CD    1 
ATOM   4043  C CE    . LYS A 1 516 ? 7.061   -14.942 32.285  1.00 95.56  ? 516 LYS A CE    1 
ATOM   4044  N NZ    . LYS A 1 516 ? 6.495   -16.189 32.857  1.00 96.07  ? 516 LYS A NZ    1 
ATOM   4045  N N     . ASN A 1 517 ? 4.091   -9.455  31.205  1.00 58.85  ? 517 ASN A N     1 
ATOM   4046  C CA    . ASN A 1 517 ? 3.019   -9.573  30.229  1.00 68.74  ? 517 ASN A CA    1 
ATOM   4047  C C     . ASN A 1 517 ? 3.330   -8.765  28.971  1.00 75.24  ? 517 ASN A C     1 
ATOM   4048  O O     . ASN A 1 517 ? 2.981   -9.204  27.880  1.00 76.00  ? 517 ASN A O     1 
ATOM   4049  C CB    . ASN A 1 517 ? 1.674   -9.130  30.803  1.00 71.08  ? 517 ASN A CB    1 
ATOM   4050  C CG    . ASN A 1 517 ? 1.135   -10.099 31.827  1.00 69.65  ? 517 ASN A CG    1 
ATOM   4051  O OD1   . ASN A 1 517 ? 1.444   -11.292 31.799  1.00 65.40  ? 517 ASN A OD1   1 
ATOM   4052  N ND2   . ASN A 1 517 ? 0.311   -9.582  32.719  1.00 70.38  ? 517 ASN A ND2   1 
ATOM   4053  N N     . ARG A 1 518 ? 3.961   -7.590  29.141  1.00 80.43  ? 518 ARG A N     1 
ATOM   4054  C CA    . ARG A 1 518 ? 4.195   -6.646  28.054  1.00 72.65  ? 518 ARG A CA    1 
ATOM   4055  C C     . ARG A 1 518 ? 5.682   -6.492  27.753  1.00 62.87  ? 518 ARG A C     1 
ATOM   4056  O O     . ARG A 1 518 ? 6.070   -5.483  27.190  1.00 56.97  ? 518 ARG A O     1 
ATOM   4057  C CB    . ARG A 1 518 ? 3.643   -5.271  28.428  1.00 66.59  ? 518 ARG A CB    1 
ATOM   4058  C CG    . ARG A 1 518 ? 2.192   -5.300  28.865  1.00 72.25  ? 518 ARG A CG    1 
ATOM   4059  C CD    . ARG A 1 518 ? 1.742   -3.911  29.239  1.00 82.50  ? 518 ARG A CD    1 
ATOM   4060  N NE    . ARG A 1 518 ? 0.332   -3.710  28.935  1.00 85.55  ? 518 ARG A NE    1 
ATOM   4061  C CZ    . ARG A 1 518 ? -0.639  -3.603  29.839  1.00 93.47  ? 518 ARG A CZ    1 
ATOM   4062  N NH1   . ARG A 1 518 ? -0.409  -3.874  31.118  1.00 86.98  ? 518 ARG A NH1   1 
ATOM   4063  N NH2   . ARG A 1 518 ? -1.858  -3.278  29.438  1.00 92.52  ? 518 ARG A NH2   1 
ATOM   4064  N N     . ARG A 1 519 ? 6.491   -7.485  28.140  1.00 68.40  ? 519 ARG A N     1 
ATOM   4065  C CA    . ARG A 1 519 ? 7.939   -7.450  28.003  1.00 65.83  ? 519 ARG A CA    1 
ATOM   4066  C C     . ARG A 1 519 ? 8.382   -8.780  27.383  1.00 62.84  ? 519 ARG A C     1 
ATOM   4067  O O     . ARG A 1 519 ? 8.716   -8.746  26.192  1.00 67.25  ? 519 ARG A O     1 
ATOM   4068  C CB    . ARG A 1 519 ? 8.587   -7.208  29.373  1.00 65.18  ? 519 ARG A CB    1 
ATOM   4069  C CG    . ARG A 1 519 ? 10.071  -7.532  29.435  1.00 66.95  ? 519 ARG A CG    1 
ATOM   4070  C CD    . ARG A 1 519 ? 10.594  -7.596  30.851  1.00 66.92  ? 519 ARG A CD    1 
ATOM   4071  N NE    . ARG A 1 519 ? 10.427  -8.913  31.464  1.00 61.33  ? 519 ARG A NE    1 
ATOM   4072  C CZ    . ARG A 1 519 ? 9.961   -9.146  32.689  1.00 53.41  ? 519 ARG A CZ    1 
ATOM   4073  N NH1   . ARG A 1 519 ? 9.505   -8.164  33.457  1.00 54.31  ? 519 ARG A NH1   1 
ATOM   4074  N NH2   . ARG A 1 519 ? 9.927   -10.388 33.136  1.00 55.54  ? 519 ARG A NH2   1 
ATOM   4075  N N     . ALA B 1 2   ? 29.390  -29.153 69.230  1.00 95.45  ? 2   ALA B N     1 
ATOM   4076  C CA    . ALA B 1 2   ? 29.355  -28.980 67.753  1.00 107.63 ? 2   ALA B CA    1 
ATOM   4077  C C     . ALA B 1 2   ? 27.945  -28.578 67.313  1.00 100.87 ? 2   ALA B C     1 
ATOM   4078  O O     . ALA B 1 2   ? 27.016  -28.617 68.121  1.00 80.75  ? 2   ALA B O     1 
ATOM   4079  C CB    . ALA B 1 2   ? 29.821  -30.250 67.067  1.00 110.25 ? 2   ALA B CB    1 
ATOM   4080  N N     . ALA B 1 3   ? 27.797  -28.222 66.026  1.00 97.41  ? 3   ALA B N     1 
ATOM   4081  C CA    . ALA B 1 3   ? 26.570  -27.627 65.509  1.00 104.97 ? 3   ALA B CA    1 
ATOM   4082  C C     . ALA B 1 3   ? 25.844  -28.546 64.512  1.00 101.43 ? 3   ALA B C     1 
ATOM   4083  O O     . ALA B 1 3   ? 26.446  -29.419 63.877  1.00 85.70  ? 3   ALA B O     1 
ATOM   4084  C CB    . ALA B 1 3   ? 26.899  -26.283 64.899  1.00 108.53 ? 3   ALA B CB    1 
ATOM   4085  N N     . PRO B 1 4   ? 24.505  -28.371 64.350  1.00 91.61  ? 4   PRO B N     1 
ATOM   4086  C CA    . PRO B 1 4   ? 23.693  -29.212 63.465  1.00 91.10  ? 4   PRO B CA    1 
ATOM   4087  C C     . PRO B 1 4   ? 23.440  -28.655 62.065  1.00 85.89  ? 4   PRO B C     1 
ATOM   4088  O O     . PRO B 1 4   ? 23.543  -27.449 61.861  1.00 87.50  ? 4   PRO B O     1 
ATOM   4089  C CB    . PRO B 1 4   ? 22.361  -29.204 64.231  1.00 89.81  ? 4   PRO B CB    1 
ATOM   4090  C CG    . PRO B 1 4   ? 22.251  -27.778 64.736  1.00 87.66  ? 4   PRO B CG    1 
ATOM   4091  C CD    . PRO B 1 4   ? 23.677  -27.372 65.056  1.00 83.75  ? 4   PRO B CD    1 
ATOM   4092  N N     . LEU B 1 5   ? 23.053  -29.540 61.132  1.00 87.53  ? 5   LEU B N     1 
ATOM   4093  C CA    . LEU B 1 5   ? 22.652  -29.149 59.785  1.00 80.52  ? 5   LEU B CA    1 
ATOM   4094  C C     . LEU B 1 5   ? 21.375  -28.330 59.881  1.00 79.54  ? 5   LEU B C     1 
ATOM   4095  O O     . LEU B 1 5   ? 20.554  -28.572 60.758  1.00 80.15  ? 5   LEU B O     1 
ATOM   4096  C CB    . LEU B 1 5   ? 22.379  -30.368 58.893  1.00 74.11  ? 5   LEU B CB    1 
ATOM   4097  C CG    . LEU B 1 5   ? 23.533  -31.347 58.682  1.00 81.80  ? 5   LEU B CG    1 
ATOM   4098  C CD1   . LEU B 1 5   ? 23.100  -32.518 57.804  1.00 86.05  ? 5   LEU B CD1   1 
ATOM   4099  C CD2   . LEU B 1 5   ? 24.742  -30.651 58.078  1.00 83.78  ? 5   LEU B CD2   1 
ATOM   4100  N N     . PRO B 1 6   ? 21.151  -27.380 58.949  1.00 78.24  ? 6   PRO B N     1 
ATOM   4101  C CA    . PRO B 1 6   ? 19.854  -26.729 58.823  1.00 78.90  ? 6   PRO B CA    1 
ATOM   4102  C C     . PRO B 1 6   ? 18.857  -27.796 58.406  1.00 72.61  ? 6   PRO B C     1 
ATOM   4103  O O     . PRO B 1 6   ? 19.270  -28.774 57.790  1.00 81.89  ? 6   PRO B O     1 
ATOM   4104  C CB    . PRO B 1 6   ? 20.009  -25.693 57.703  1.00 83.59  ? 6   PRO B CB    1 
ATOM   4105  C CG    . PRO B 1 6   ? 21.489  -25.695 57.337  1.00 85.57  ? 6   PRO B CG    1 
ATOM   4106  C CD    . PRO B 1 6   ? 22.109  -26.940 57.929  1.00 81.02  ? 6   PRO B CD    1 
ATOM   4107  N N     . GLU B 1 7   ? 17.575  -27.597 58.742  1.00 81.22  ? 7   GLU B N     1 
ATOM   4108  C CA    . GLU B 1 7   ? 16.526  -28.539 58.370  1.00 88.61  ? 7   GLU B CA    1 
ATOM   4109  C C     . GLU B 1 7   ? 16.290  -28.418 56.868  1.00 74.68  ? 7   GLU B C     1 
ATOM   4110  O O     . GLU B 1 7   ? 16.204  -27.313 56.369  1.00 70.62  ? 7   GLU B O     1 
ATOM   4111  C CB    . GLU B 1 7   ? 15.238  -28.296 59.168  1.00 90.00  ? 7   GLU B CB    1 
ATOM   4112  C CG    . GLU B 1 7   ? 14.076  -29.193 58.747  1.00 92.39  ? 7   GLU B CG    1 
ATOM   4113  C CD    . GLU B 1 7   ? 13.048  -29.490 59.830  1.00 100.66 ? 7   GLU B CD    1 
ATOM   4114  O OE1   . GLU B 1 7   ? 12.512  -28.533 60.431  1.00 103.52 ? 7   GLU B OE1   1 
ATOM   4115  O OE2   . GLU B 1 7   ? 12.779  -30.684 60.075  1.00 91.61  ? 7   GLU B OE2   1 
ATOM   4116  N N     . GLY B 1 8   ? 16.207  -29.555 56.165  1.00 75.30  ? 8   GLY B N     1 
ATOM   4117  C CA    . GLY B 1 8   ? 15.979  -29.578 54.724  1.00 79.17  ? 8   GLY B CA    1 
ATOM   4118  C C     . GLY B 1 8   ? 17.280  -29.662 53.926  1.00 76.18  ? 8   GLY B C     1 
ATOM   4119  O O     . GLY B 1 8   ? 17.261  -29.556 52.706  1.00 76.06  ? 8   GLY B O     1 
ATOM   4120  N N     . VAL B 1 9   ? 18.382  -29.908 54.643  1.00 69.02  ? 9   VAL B N     1 
ATOM   4121  C CA    . VAL B 1 9   ? 19.729  -29.905 54.113  1.00 75.16  ? 9   VAL B CA    1 
ATOM   4122  C C     . VAL B 1 9   ? 20.424  -31.179 54.602  1.00 87.96  ? 9   VAL B C     1 
ATOM   4123  O O     . VAL B 1 9   ? 20.842  -31.246 55.760  1.00 94.03  ? 9   VAL B O     1 
ATOM   4124  C CB    . VAL B 1 9   ? 20.472  -28.631 54.583  1.00 78.54  ? 9   VAL B CB    1 
ATOM   4125  C CG1   . VAL B 1 9   ? 21.899  -28.544 54.044  1.00 74.70  ? 9   VAL B CG1   1 
ATOM   4126  C CG2   . VAL B 1 9   ? 19.690  -27.362 54.256  1.00 72.10  ? 9   VAL B CG2   1 
ATOM   4127  N N     . SER B 1 10  ? 20.558  -32.184 53.721  1.00 84.22  ? 10  SER B N     1 
ATOM   4128  C CA    . SER B 1 10  ? 21.253  -33.417 54.067  1.00 85.75  ? 10  SER B CA    1 
ATOM   4129  C C     . SER B 1 10  ? 22.733  -33.132 54.306  1.00 83.23  ? 10  SER B C     1 
ATOM   4130  O O     . SER B 1 10  ? 23.195  -32.025 54.063  1.00 92.81  ? 10  SER B O     1 
ATOM   4131  C CB    . SER B 1 10  ? 21.072  -34.474 52.997  1.00 91.80  ? 10  SER B CB    1 
ATOM   4132  O OG    . SER B 1 10  ? 21.800  -34.161 51.819  1.00 86.24  ? 10  SER B OG    1 
ATOM   4133  N N     . ALA B 1 11  ? 23.471  -34.139 54.783  1.00 83.72  ? 11  ALA B N     1 
ATOM   4134  C CA    . ALA B 1 11  ? 24.923  -34.065 54.862  1.00 79.48  ? 11  ALA B CA    1 
ATOM   4135  C C     . ALA B 1 11  ? 25.538  -34.360 53.493  1.00 73.71  ? 11  ALA B C     1 
ATOM   4136  O O     . ALA B 1 11  ? 26.700  -34.054 53.267  1.00 73.05  ? 11  ALA B O     1 
ATOM   4137  C CB    . ALA B 1 11  ? 25.454  -35.012 55.920  1.00 71.78  ? 11  ALA B CB    1 
ATOM   4138  N N     . GLU B 1 12  ? 24.777  -34.964 52.576  1.00 89.85  ? 12  GLU B N     1 
ATOM   4139  C CA    . GLU B 1 12  ? 25.267  -35.174 51.218  1.00 101.13 ? 12  GLU B CA    1 
ATOM   4140  C C     . GLU B 1 12  ? 25.369  -33.813 50.532  1.00 95.74  ? 12  GLU B C     1 
ATOM   4141  O O     . GLU B 1 12  ? 26.392  -33.492 49.931  1.00 77.44  ? 12  GLU B O     1 
ATOM   4142  C CB    . GLU B 1 12  ? 24.359  -36.112 50.411  1.00 109.64 ? 12  GLU B CB    1 
ATOM   4143  C CG    . GLU B 1 12  ? 24.243  -37.521 50.983  1.00 119.91 ? 12  GLU B CG    1 
ATOM   4144  C CD    . GLU B 1 12  ? 23.213  -37.693 52.092  1.00 119.61 ? 12  GLU B CD    1 
ATOM   4145  O OE1   . GLU B 1 12  ? 22.001  -37.554 51.802  1.00 101.57 ? 12  GLU B OE1   1 
ATOM   4146  O OE2   . GLU B 1 12  ? 23.625  -37.956 53.251  1.00 103.57 ? 12  GLU B OE2   1 
ATOM   4147  N N     . ALA B 1 13  ? 24.290  -33.022 50.652  1.00 87.37  ? 13  ALA B N     1 
ATOM   4148  C CA    . ALA B 1 13  ? 24.232  -31.670 50.121  1.00 77.10  ? 13  ALA B CA    1 
ATOM   4149  C C     . ALA B 1 13  ? 25.324  -30.805 50.751  1.00 74.65  ? 13  ALA B C     1 
ATOM   4150  O O     . ALA B 1 13  ? 26.178  -30.274 50.040  1.00 63.48  ? 13  ALA B O     1 
ATOM   4151  C CB    . ALA B 1 13  ? 22.860  -31.082 50.355  1.00 70.54  ? 13  ALA B CB    1 
ATOM   4152  N N     . MET B 1 14  ? 25.306  -30.705 52.089  1.00 69.24  ? 14  MET B N     1 
ATOM   4153  C CA    . MET B 1 14  ? 26.191  -29.805 52.813  1.00 72.04  ? 14  MET B CA    1 
ATOM   4154  C C     . MET B 1 14  ? 27.649  -30.101 52.480  1.00 73.00  ? 14  MET B C     1 
ATOM   4155  O O     . MET B 1 14  ? 28.473  -29.191 52.438  1.00 80.93  ? 14  MET B O     1 
ATOM   4156  C CB    . MET B 1 14  ? 25.992  -29.928 54.324  1.00 75.24  ? 14  MET B CB    1 
ATOM   4157  C CG    . MET B 1 14  ? 26.964  -29.095 55.155  1.00 78.54  ? 14  MET B CG    1 
ATOM   4158  S SD    . MET B 1 14  ? 26.827  -27.298 54.885  1.00 75.38  ? 14  MET B SD    1 
ATOM   4159  C CE    . MET B 1 14  ? 25.547  -26.858 56.059  1.00 72.87  ? 14  MET B CE    1 
ATOM   4160  N N     . SER B 1 15  ? 27.953  -31.375 52.235  1.00 82.93  ? 15  SER B N     1 
ATOM   4161  C CA    . SER B 1 15  ? 29.325  -31.834 52.105  1.00 85.00  ? 15  SER B CA    1 
ATOM   4162  C C     . SER B 1 15  ? 29.870  -31.552 50.699  1.00 84.36  ? 15  SER B C     1 
ATOM   4163  O O     . SER B 1 15  ? 31.058  -31.254 50.544  1.00 72.46  ? 15  SER B O     1 
ATOM   4164  C CB    . SER B 1 15  ? 29.399  -33.296 52.481  1.00 76.47  ? 15  SER B CB    1 
ATOM   4165  O OG    . SER B 1 15  ? 30.717  -33.783 52.350  1.00 78.53  ? 15  SER B OG    1 
ATOM   4166  N N     . SER B 1 16  ? 28.998  -31.651 49.683  1.00 75.34  ? 16  SER B N     1 
ATOM   4167  C CA    . SER B 1 16  ? 29.356  -31.349 48.303  1.00 80.98  ? 16  SER B CA    1 
ATOM   4168  C C     . SER B 1 16  ? 29.427  -29.835 48.075  1.00 83.28  ? 16  SER B C     1 
ATOM   4169  O O     . SER B 1 16  ? 30.215  -29.363 47.255  1.00 78.11  ? 16  SER B O     1 
ATOM   4170  C CB    . SER B 1 16  ? 28.397  -32.007 47.327  1.00 80.86  ? 16  SER B CB    1 
ATOM   4171  O OG    . SER B 1 16  ? 28.660  -33.401 47.192  1.00 72.86  ? 16  SER B OG    1 
ATOM   4172  N N     . ALA B 1 17  ? 28.604  -29.072 48.805  1.00 82.32  ? 17  ALA B N     1 
ATOM   4173  C CA    . ALA B 1 17  ? 28.615  -27.620 48.718  1.00 75.26  ? 17  ALA B CA    1 
ATOM   4174  C C     . ALA B 1 17  ? 29.883  -27.048 49.350  1.00 77.71  ? 17  ALA B C     1 
ATOM   4175  O O     . ALA B 1 17  ? 30.322  -25.967 48.959  1.00 81.11  ? 17  ALA B O     1 
ATOM   4176  C CB    . ALA B 1 17  ? 27.387  -27.041 49.365  1.00 72.66  ? 17  ALA B CB    1 
ATOM   4177  N N     . LEU B 1 18  ? 30.456  -27.760 50.329  1.00 67.07  ? 18  LEU B N     1 
ATOM   4178  C CA    . LEU B 1 18  ? 31.663  -27.297 50.992  1.00 72.56  ? 18  LEU B CA    1 
ATOM   4179  C C     . LEU B 1 18  ? 32.886  -27.633 50.145  1.00 75.48  ? 18  LEU B C     1 
ATOM   4180  O O     . LEU B 1 18  ? 33.943  -27.049 50.331  1.00 73.33  ? 18  LEU B O     1 
ATOM   4181  C CB    . LEU B 1 18  ? 31.769  -27.935 52.380  1.00 83.41  ? 18  LEU B CB    1 
ATOM   4182  C CG    . LEU B 1 18  ? 30.853  -27.365 53.464  1.00 90.82  ? 18  LEU B CG    1 
ATOM   4183  C CD1   . LEU B 1 18  ? 31.008  -28.162 54.753  1.00 100.40 ? 18  LEU B CD1   1 
ATOM   4184  C CD2   . LEU B 1 18  ? 31.136  -25.887 53.721  1.00 87.25  ? 18  LEU B CD2   1 
ATOM   4185  N N     . ASP B 1 19  ? 32.740  -28.577 49.216  1.00 85.33  ? 19  ASP B N     1 
ATOM   4186  C CA    . ASP B 1 19  ? 33.829  -28.923 48.319  1.00 99.48  ? 19  ASP B CA    1 
ATOM   4187  C C     . ASP B 1 19  ? 33.958  -27.848 47.244  1.00 95.15  ? 19  ASP B C     1 
ATOM   4188  O O     . ASP B 1 19  ? 35.059  -27.373 46.967  1.00 96.24  ? 19  ASP B O     1 
ATOM   4189  C CB    . ASP B 1 19  ? 33.614  -30.303 47.687  1.00 103.80 ? 19  ASP B CB    1 
ATOM   4190  C CG    . ASP B 1 19  ? 33.842  -31.462 48.640  1.00 106.93 ? 19  ASP B CG    1 
ATOM   4191  O OD1   . ASP B 1 19  ? 34.091  -31.211 49.847  1.00 103.34 ? 19  ASP B OD1   1 
ATOM   4192  O OD2   . ASP B 1 19  ? 33.789  -32.605 48.162  1.00 109.18 ? 19  ASP B OD2   1 
ATOM   4193  N N     . ARG B 1 20  ? 32.817  -27.507 46.630  1.00 90.33  ? 20  ARG B N     1 
ATOM   4194  C CA    . ARG B 1 20  ? 32.750  -26.482 45.601  1.00 83.65  ? 20  ARG B CA    1 
ATOM   4195  C C     . ARG B 1 20  ? 33.253  -25.153 46.159  1.00 75.29  ? 20  ARG B C     1 
ATOM   4196  O O     . ARG B 1 20  ? 34.114  -24.541 45.532  1.00 72.74  ? 20  ARG B O     1 
ATOM   4197  C CB    . ARG B 1 20  ? 31.323  -26.359 45.064  1.00 79.26  ? 20  ARG B CB    1 
ATOM   4198  C CG    . ARG B 1 20  ? 30.940  -27.500 44.134  1.00 83.16  ? 20  ARG B CG    1 
ATOM   4199  C CD    . ARG B 1 20  ? 31.499  -27.313 42.733  1.00 85.09  ? 20  ARG B CD    1 
ATOM   4200  N NE    . ARG B 1 20  ? 30.576  -26.574 41.888  1.00 85.83  ? 20  ARG B NE    1 
ATOM   4201  C CZ    . ARG B 1 20  ? 29.402  -27.042 41.460  1.00 96.92  ? 20  ARG B CZ    1 
ATOM   4202  N NH1   . ARG B 1 20  ? 29.007  -28.265 41.775  1.00 90.26  ? 20  ARG B NH1   1 
ATOM   4203  N NH2   . ARG B 1 20  ? 28.618  -26.282 40.711  1.00 101.65 ? 20  ARG B NH2   1 
ATOM   4204  N N     . PHE B 1 21  ? 32.739  -24.748 47.338  1.00 60.62  ? 21  PHE B N     1 
ATOM   4205  C CA    . PHE B 1 21  ? 33.204  -23.549 48.022  1.00 52.98  ? 21  PHE B CA    1 
ATOM   4206  C C     . PHE B 1 21  ? 34.733  -23.519 48.019  1.00 60.76  ? 21  PHE B C     1 
ATOM   4207  O O     . PHE B 1 21  ? 35.349  -22.506 47.689  1.00 66.69  ? 21  PHE B O     1 
ATOM   4208  C CB    . PHE B 1 21  ? 32.728  -23.457 49.482  1.00 46.47  ? 21  PHE B CB    1 
ATOM   4209  C CG    . PHE B 1 21  ? 31.255  -23.214 49.752  1.00 43.87  ? 21  PHE B CG    1 
ATOM   4210  C CD1   . PHE B 1 21  ? 30.336  -23.002 48.744  1.00 40.18  ? 21  PHE B CD1   1 
ATOM   4211  C CD2   . PHE B 1 21  ? 30.780  -23.189 51.061  1.00 48.30  ? 21  PHE B CD2   1 
ATOM   4212  C CE1   . PHE B 1 21  ? 28.992  -22.786 49.028  1.00 45.00  ? 21  PHE B CE1   1 
ATOM   4213  C CE2   . PHE B 1 21  ? 29.432  -22.986 51.342  1.00 49.77  ? 21  PHE B CE2   1 
ATOM   4214  C CZ    . PHE B 1 21  ? 28.527  -22.803 50.320  1.00 44.10  ? 21  PHE B CZ    1 
ATOM   4215  N N     . ALA B 1 22  ? 35.352  -24.626 48.425  1.00 63.78  ? 22  ALA B N     1 
ATOM   4216  C CA    . ALA B 1 22  ? 36.793  -24.646 48.583  1.00 64.57  ? 22  ALA B CA    1 
ATOM   4217  C C     . ALA B 1 22  ? 37.437  -24.790 47.212  1.00 61.30  ? 22  ALA B C     1 
ATOM   4218  O O     . ALA B 1 22  ? 38.630  -24.513 47.084  1.00 58.90  ? 22  ALA B O     1 
ATOM   4219  C CB    . ALA B 1 22  ? 37.225  -25.739 49.529  1.00 62.21  ? 22  ALA B CB    1 
ATOM   4220  N N     . ARG B 1 23  ? 36.653  -25.220 46.208  1.00 59.84  ? 23  ARG B N     1 
ATOM   4221  C CA    . ARG B 1 23  ? 37.130  -25.176 44.828  1.00 67.07  ? 23  ARG B CA    1 
ATOM   4222  C C     . ARG B 1 23  ? 37.180  -23.702 44.395  1.00 64.47  ? 23  ARG B C     1 
ATOM   4223  O O     . ARG B 1 23  ? 38.190  -23.274 43.866  1.00 64.51  ? 23  ARG B O     1 
ATOM   4224  C CB    . ARG B 1 23  ? 36.310  -26.086 43.896  1.00 64.17  ? 23  ARG B CB    1 
ATOM   4225  N N     . ILE B 1 24  ? 36.142  -22.904 44.706  1.00 63.14  ? 24  ILE B N     1 
ATOM   4226  C CA    . ILE B 1 24  ? 36.072  -21.489 44.346  1.00 57.34  ? 24  ILE B CA    1 
ATOM   4227  C C     . ILE B 1 24  ? 37.164  -20.674 45.041  1.00 56.96  ? 24  ILE B C     1 
ATOM   4228  O O     . ILE B 1 24  ? 37.852  -19.886 44.390  1.00 62.02  ? 24  ILE B O     1 
ATOM   4229  C CB    . ILE B 1 24  ? 34.671  -20.915 44.649  1.00 57.39  ? 24  ILE B CB    1 
ATOM   4230  C CG1   . ILE B 1 24  ? 33.587  -21.585 43.803  1.00 52.70  ? 24  ILE B CG1   1 
ATOM   4231  C CG2   . ILE B 1 24  ? 34.629  -19.398 44.478  1.00 58.80  ? 24  ILE B CG2   1 
ATOM   4232  C CD1   . ILE B 1 24  ? 32.206  -21.451 44.385  1.00 55.83  ? 24  ILE B CD1   1 
ATOM   4233  N N     . VAL B 1 25  ? 37.314  -20.837 46.361  1.00 51.74  ? 25  VAL B N     1 
ATOM   4234  C CA    . VAL B 1 25  ? 38.084  -19.891 47.152  1.00 47.46  ? 25  VAL B CA    1 
ATOM   4235  C C     . VAL B 1 25  ? 39.435  -20.472 47.536  1.00 49.25  ? 25  VAL B C     1 
ATOM   4236  O O     . VAL B 1 25  ? 40.350  -19.718 47.853  1.00 51.44  ? 25  VAL B O     1 
ATOM   4237  C CB    . VAL B 1 25  ? 37.310  -19.447 48.408  1.00 53.16  ? 25  VAL B CB    1 
ATOM   4238  C CG1   . VAL B 1 25  ? 35.866  -19.078 48.096  1.00 56.88  ? 25  VAL B CG1   1 
ATOM   4239  C CG2   . VAL B 1 25  ? 37.354  -20.479 49.519  1.00 59.11  ? 25  VAL B CG2   1 
ATOM   4240  N N     . GLY B 1 26  ? 39.531  -21.803 47.571  1.00 51.69  ? 26  GLY B N     1 
ATOM   4241  C CA    . GLY B 1 26  ? 40.716  -22.466 48.081  1.00 62.50  ? 26  GLY B CA    1 
ATOM   4242  C C     . GLY B 1 26  ? 40.486  -23.075 49.464  1.00 74.88  ? 26  GLY B C     1 
ATOM   4243  O O     . GLY B 1 26  ? 39.881  -22.436 50.325  1.00 70.95  ? 26  GLY B O     1 
ATOM   4244  N N     . ALA B 1 27  ? 41.034  -24.290 49.658  1.00 81.95  ? 27  ALA B N     1 
ATOM   4245  C CA    . ALA B 1 27  ? 40.809  -25.118 50.833  1.00 81.91  ? 27  ALA B CA    1 
ATOM   4246  C C     . ALA B 1 27  ? 41.100  -24.358 52.127  1.00 75.55  ? 27  ALA B C     1 
ATOM   4247  O O     . ALA B 1 27  ? 40.383  -24.542 53.108  1.00 69.16  ? 27  ALA B O     1 
ATOM   4248  C CB    . ALA B 1 27  ? 41.652  -26.365 50.739  1.00 83.33  ? 27  ALA B CB    1 
ATOM   4249  N N     . ASP B 1 28  ? 42.113  -23.480 52.110  1.00 72.67  ? 28  ASP B N     1 
ATOM   4250  C CA    . ASP B 1 28  ? 42.564  -22.780 53.307  1.00 75.35  ? 28  ASP B CA    1 
ATOM   4251  C C     . ASP B 1 28  ? 41.580  -21.685 53.752  1.00 71.00  ? 28  ASP B C     1 
ATOM   4252  O O     . ASP B 1 28  ? 41.777  -21.126 54.839  1.00 65.39  ? 28  ASP B O     1 
ATOM   4253  C CB    . ASP B 1 28  ? 43.971  -22.194 53.104  1.00 82.97  ? 28  ASP B CB    1 
ATOM   4254  C CG    . ASP B 1 28  ? 45.053  -23.204 52.725  1.00 94.27  ? 28  ASP B CG    1 
ATOM   4255  O OD1   . ASP B 1 28  ? 44.749  -24.420 52.668  1.00 104.25 ? 28  ASP B OD1   1 
ATOM   4256  O OD2   . ASP B 1 28  ? 46.203  -22.773 52.478  1.00 86.97  ? 28  ASP B OD2   1 
ATOM   4257  N N     . TRP B 1 29  ? 40.546  -21.364 52.936  1.00 58.01  ? 29  TRP B N     1 
ATOM   4258  C CA    . TRP B 1 29  ? 39.586  -20.313 53.271  1.00 60.40  ? 29  TRP B CA    1 
ATOM   4259  C C     . TRP B 1 29  ? 38.171  -20.860 53.463  1.00 69.92  ? 29  TRP B C     1 
ATOM   4260  O O     . TRP B 1 29  ? 37.223  -20.075 53.402  1.00 67.63  ? 29  TRP B O     1 
ATOM   4261  C CB    . TRP B 1 29  ? 39.593  -19.176 52.230  1.00 57.51  ? 29  TRP B CB    1 
ATOM   4262  C CG    . TRP B 1 29  ? 40.936  -18.530 52.136  1.00 52.35  ? 29  TRP B CG    1 
ATOM   4263  C CD1   . TRP B 1 29  ? 41.832  -18.635 51.109  1.00 52.51  ? 29  TRP B CD1   1 
ATOM   4264  C CD2   . TRP B 1 29  ? 41.584  -17.774 53.170  1.00 46.98  ? 29  TRP B CD2   1 
ATOM   4265  N NE1   . TRP B 1 29  ? 42.985  -17.971 51.427  1.00 59.18  ? 29  TRP B NE1   1 
ATOM   4266  C CE2   . TRP B 1 29  ? 42.865  -17.432 52.686  1.00 52.26  ? 29  TRP B CE2   1 
ATOM   4267  C CE3   . TRP B 1 29  ? 41.201  -17.328 54.440  1.00 52.84  ? 29  TRP B CE3   1 
ATOM   4268  C CZ2   . TRP B 1 29  ? 43.770  -16.675 53.437  1.00 54.12  ? 29  TRP B CZ2   1 
ATOM   4269  C CZ3   . TRP B 1 29  ? 42.094  -16.573 55.181  1.00 58.12  ? 29  TRP B CZ3   1 
ATOM   4270  C CH2   . TRP B 1 29  ? 43.369  -16.261 54.691  1.00 56.07  ? 29  TRP B CH2   1 
ATOM   4271  N N     . VAL B 1 30  ? 38.032  -22.185 53.662  1.00 72.65  ? 30  VAL B N     1 
ATOM   4272  C CA    . VAL B 1 30  ? 36.844  -22.768 54.280  1.00 68.78  ? 30  VAL B CA    1 
ATOM   4273  C C     . VAL B 1 30  ? 37.208  -23.217 55.692  1.00 67.35  ? 30  VAL B C     1 
ATOM   4274  O O     . VAL B 1 30  ? 38.257  -23.814 55.892  1.00 64.65  ? 30  VAL B O     1 
ATOM   4275  C CB    . VAL B 1 30  ? 36.253  -23.948 53.488  1.00 67.47  ? 30  VAL B CB    1 
ATOM   4276  C CG1   . VAL B 1 30  ? 35.207  -24.682 54.303  1.00 67.21  ? 30  VAL B CG1   1 
ATOM   4277  C CG2   . VAL B 1 30  ? 35.658  -23.510 52.159  1.00 78.68  ? 30  VAL B CG2   1 
ATOM   4278  N N     . PHE B 1 31  ? 36.328  -22.918 56.653  1.00 68.46  ? 31  PHE B N     1 
ATOM   4279  C CA    . PHE B 1 31  ? 36.568  -23.193 58.056  1.00 70.78  ? 31  PHE B CA    1 
ATOM   4280  C C     . PHE B 1 31  ? 35.430  -24.062 58.588  1.00 75.93  ? 31  PHE B C     1 
ATOM   4281  O O     . PHE B 1 31  ? 34.271  -23.835 58.241  1.00 76.05  ? 31  PHE B O     1 
ATOM   4282  C CB    . PHE B 1 31  ? 36.697  -21.892 58.853  1.00 73.89  ? 31  PHE B CB    1 
ATOM   4283  C CG    . PHE B 1 31  ? 37.767  -20.924 58.400  1.00 81.83  ? 31  PHE B CG    1 
ATOM   4284  C CD1   . PHE B 1 31  ? 39.117  -21.252 58.456  1.00 92.13  ? 31  PHE B CD1   1 
ATOM   4285  C CD2   . PHE B 1 31  ? 37.424  -19.655 57.957  1.00 87.81  ? 31  PHE B CD2   1 
ATOM   4286  C CE1   . PHE B 1 31  ? 40.091  -20.345 58.055  1.00 95.32  ? 31  PHE B CE1   1 
ATOM   4287  C CE2   . PHE B 1 31  ? 38.398  -18.748 57.566  1.00 98.40  ? 31  PHE B CE2   1 
ATOM   4288  C CZ    . PHE B 1 31  ? 39.730  -19.093 57.610  1.00 98.39  ? 31  PHE B CZ    1 
ATOM   4289  N N     . THR B 1 32  ? 35.799  -25.070 59.404  1.00 89.14  ? 32  THR B N     1 
ATOM   4290  C CA    . THR B 1 32  ? 34.887  -25.983 60.089  1.00 85.16  ? 32  THR B CA    1 
ATOM   4291  C C     . THR B 1 32  ? 35.465  -26.331 61.467  1.00 96.94  ? 32  THR B C     1 
ATOM   4292  O O     . THR B 1 32  ? 36.342  -25.612 61.952  1.00 105.08 ? 32  THR B O     1 
ATOM   4293  C CB    . THR B 1 32  ? 34.641  -27.248 59.259  1.00 73.53  ? 32  THR B CB    1 
ATOM   4294  O OG1   . THR B 1 32  ? 35.921  -27.724 58.858  1.00 74.42  ? 32  THR B OG1   1 
ATOM   4295  C CG2   . THR B 1 32  ? 33.788  -27.030 58.032  1.00 78.85  ? 32  THR B CG2   1 
ATOM   4296  N N     . GLU B 1 33  ? 34.929  -27.393 62.107  1.00 99.92  ? 33  GLU B N     1 
ATOM   4297  C CA    . GLU B 1 33  ? 35.542  -28.059 63.257  1.00 96.44  ? 33  GLU B CA    1 
ATOM   4298  C C     . GLU B 1 33  ? 35.804  -27.032 64.362  1.00 91.96  ? 33  GLU B C     1 
ATOM   4299  O O     . GLU B 1 33  ? 34.853  -26.421 64.836  1.00 83.47  ? 33  GLU B O     1 
ATOM   4300  C CB    . GLU B 1 33  ? 36.783  -28.862 62.831  1.00 91.13  ? 33  GLU B CB    1 
ATOM   4301  N N     . ASP B 1 34  ? 37.077  -26.823 64.751  1.00 96.89  ? 34  ASP B N     1 
ATOM   4302  C CA    . ASP B 1 34  ? 37.421  -25.961 65.879  1.00 105.00 ? 34  ASP B CA    1 
ATOM   4303  C C     . ASP B 1 34  ? 37.788  -24.544 65.440  1.00 105.33 ? 34  ASP B C     1 
ATOM   4304  O O     . ASP B 1 34  ? 38.152  -23.734 66.292  1.00 95.39  ? 34  ASP B O     1 
ATOM   4305  C CB    . ASP B 1 34  ? 38.579  -26.526 66.715  1.00 104.32 ? 34  ASP B CB    1 
ATOM   4306  C CG    . ASP B 1 34  ? 38.256  -26.792 68.182  1.00 106.32 ? 34  ASP B CG    1 
ATOM   4307  O OD1   . ASP B 1 34  ? 37.168  -26.375 68.653  1.00 98.10  ? 34  ASP B OD1   1 
ATOM   4308  O OD2   . ASP B 1 34  ? 39.107  -27.405 68.857  1.00 105.41 ? 34  ASP B OD2   1 
ATOM   4309  N N     . LYS B 1 35  ? 37.682  -24.242 64.137  1.00 117.53 ? 35  LYS B N     1 
ATOM   4310  C CA    . LYS B 1 35  ? 38.023  -22.920 63.626  1.00 118.73 ? 35  LYS B CA    1 
ATOM   4311  C C     . LYS B 1 35  ? 36.755  -22.071 63.445  1.00 104.37 ? 35  LYS B C     1 
ATOM   4312  O O     . LYS B 1 35  ? 36.839  -20.945 62.963  1.00 88.62  ? 35  LYS B O     1 
ATOM   4313  C CB    . LYS B 1 35  ? 38.859  -23.053 62.343  1.00 105.86 ? 35  LYS B CB    1 
ATOM   4314  N N     . ILE B 1 36  ? 35.590  -22.585 63.875  1.00 93.27  ? 36  ILE B N     1 
ATOM   4315  C CA    . ILE B 1 36  ? 34.348  -21.824 63.855  1.00 89.77  ? 36  ILE B CA    1 
ATOM   4316  C C     . ILE B 1 36  ? 34.222  -20.984 65.127  1.00 81.40  ? 36  ILE B C     1 
ATOM   4317  O O     . ILE B 1 36  ? 33.358  -20.115 65.190  1.00 74.76  ? 36  ILE B O     1 
ATOM   4318  C CB    . ILE B 1 36  ? 33.131  -22.754 63.657  1.00 87.72  ? 36  ILE B CB    1 
ATOM   4319  C CG1   . ILE B 1 36  ? 33.176  -23.439 62.291  1.00 93.89  ? 36  ILE B CG1   1 
ATOM   4320  C CG2   . ILE B 1 36  ? 31.822  -22.001 63.838  1.00 88.98  ? 36  ILE B CG2   1 
ATOM   4321  C CD1   . ILE B 1 36  ? 32.187  -24.570 62.145  1.00 98.32  ? 36  ILE B CD1   1 
ATOM   4322  N N     . THR B 1 37  ? 35.101  -21.209 66.117  1.00 88.47  ? 37  THR B N     1 
ATOM   4323  C CA    . THR B 1 37  ? 34.973  -20.588 67.434  1.00 96.51  ? 37  THR B CA    1 
ATOM   4324  C C     . THR B 1 37  ? 34.883  -19.056 67.348  1.00 86.97  ? 37  THR B C     1 
ATOM   4325  O O     . THR B 1 37  ? 34.133  -18.471 68.121  1.00 77.61  ? 37  THR B O     1 
ATOM   4326  C CB    . THR B 1 37  ? 36.059  -21.073 68.421  1.00 101.45 ? 37  THR B CB    1 
ATOM   4327  O OG1   . THR B 1 37  ? 37.289  -21.324 67.741  1.00 93.58  ? 37  THR B OG1   1 
ATOM   4328  C CG2   . THR B 1 37  ? 35.682  -22.340 69.163  1.00 100.66 ? 37  THR B CG2   1 
ATOM   4329  N N     . PRO B 1 38  ? 35.582  -18.329 66.434  1.00 92.48  ? 38  PRO B N     1 
ATOM   4330  C CA    . PRO B 1 38  ? 35.443  -16.869 66.354  1.00 90.56  ? 38  PRO B CA    1 
ATOM   4331  C C     . PRO B 1 38  ? 34.164  -16.347 65.677  1.00 88.52  ? 38  PRO B C     1 
ATOM   4332  O O     . PRO B 1 38  ? 33.905  -15.138 65.703  1.00 82.09  ? 38  PRO B O     1 
ATOM   4333  C CB    . PRO B 1 38  ? 36.672  -16.399 65.544  1.00 87.44  ? 38  PRO B CB    1 
ATOM   4334  C CG    . PRO B 1 38  ? 37.467  -17.655 65.197  1.00 86.13  ? 38  PRO B CG    1 
ATOM   4335  C CD    . PRO B 1 38  ? 36.549  -18.835 65.447  1.00 94.12  ? 38  PRO B CD    1 
ATOM   4336  N N     . TYR B 1 39  ? 33.371  -17.245 65.064  1.00 68.02  ? 39  TYR B N     1 
ATOM   4337  C CA    . TYR B 1 39  ? 32.103  -16.864 64.456  1.00 74.94  ? 39  TYR B CA    1 
ATOM   4338  C C     . TYR B 1 39  ? 30.942  -17.110 65.428  1.00 77.18  ? 39  TYR B C     1 
ATOM   4339  O O     . TYR B 1 39  ? 29.798  -16.792 65.120  1.00 71.17  ? 39  TYR B O     1 
ATOM   4340  C CB    . TYR B 1 39  ? 31.943  -17.574 63.107  1.00 79.07  ? 39  TYR B CB    1 
ATOM   4341  C CG    . TYR B 1 39  ? 33.032  -17.237 62.110  1.00 88.04  ? 39  TYR B CG    1 
ATOM   4342  C CD1   . TYR B 1 39  ? 33.021  -16.048 61.393  1.00 83.34  ? 39  TYR B CD1   1 
ATOM   4343  C CD2   . TYR B 1 39  ? 34.114  -18.081 61.915  1.00 86.15  ? 39  TYR B CD2   1 
ATOM   4344  C CE1   . TYR B 1 39  ? 34.030  -15.725 60.500  1.00 73.98  ? 39  TYR B CE1   1 
ATOM   4345  C CE2   . TYR B 1 39  ? 35.129  -17.776 61.020  1.00 82.30  ? 39  TYR B CE2   1 
ATOM   4346  C CZ    . TYR B 1 39  ? 35.087  -16.596 60.303  1.00 77.58  ? 39  TYR B CZ    1 
ATOM   4347  O OH    . TYR B 1 39  ? 36.101  -16.321 59.412  1.00 64.33  ? 39  TYR B OH    1 
ATOM   4348  N N     . GLU B 1 40  ? 31.236  -17.641 66.624  1.00 80.55  ? 40  GLU B N     1 
ATOM   4349  C CA    . GLU B 1 40  ? 30.243  -17.758 67.683  1.00 81.83  ? 40  GLU B CA    1 
ATOM   4350  C C     . GLU B 1 40  ? 29.985  -16.378 68.293  1.00 73.38  ? 40  GLU B C     1 
ATOM   4351  O O     . GLU B 1 40  ? 30.906  -15.563 68.345  1.00 63.52  ? 40  GLU B O     1 
ATOM   4352  C CB    . GLU B 1 40  ? 30.735  -18.756 68.736  1.00 82.83  ? 40  GLU B CB    1 
ATOM   4353  C CG    . GLU B 1 40  ? 30.822  -20.188 68.218  1.00 79.12  ? 40  GLU B CG    1 
ATOM   4354  C CD    . GLU B 1 40  ? 29.481  -20.868 68.002  1.00 77.04  ? 40  GLU B CD    1 
ATOM   4355  O OE1   . GLU B 1 40  ? 28.441  -20.284 68.407  1.00 74.30  ? 40  GLU B OE1   1 
ATOM   4356  O OE2   . GLU B 1 40  ? 29.467  -21.980 67.418  1.00 80.56  ? 40  GLU B OE2   1 
ATOM   4357  N N     . ASP B 1 41  ? 28.726  -16.123 68.702  1.00 69.78  ? 41  ASP B N     1 
ATOM   4358  C CA    . ASP B 1 41  ? 28.351  -14.948 69.486  1.00 76.88  ? 41  ASP B CA    1 
ATOM   4359  C C     . ASP B 1 41  ? 29.327  -14.856 70.665  1.00 78.70  ? 41  ASP B C     1 
ATOM   4360  O O     . ASP B 1 41  ? 29.442  -15.809 71.440  1.00 69.04  ? 41  ASP B O     1 
ATOM   4361  C CB    . ASP B 1 41  ? 26.865  -15.047 69.888  1.00 75.79  ? 41  ASP B CB    1 
ATOM   4362  C CG    . ASP B 1 41  ? 26.185  -13.879 70.612  1.00 74.72  ? 41  ASP B CG    1 
ATOM   4363  O OD1   . ASP B 1 41  ? 26.733  -12.737 70.683  1.00 59.93  ? 41  ASP B OD1   1 
ATOM   4364  O OD2   . ASP B 1 41  ? 25.062  -14.119 71.106  1.00 77.89  ? 41  ASP B OD2   1 
ATOM   4365  N N     . PRO B 1 42  ? 30.126  -13.762 70.802  1.00 91.73  ? 42  PRO B N     1 
ATOM   4366  C CA    . PRO B 1 42  ? 31.032  -13.623 71.942  1.00 87.62  ? 42  PRO B CA    1 
ATOM   4367  C C     . PRO B 1 42  ? 30.256  -13.369 73.236  1.00 87.67  ? 42  PRO B C     1 
ATOM   4368  O O     . PRO B 1 42  ? 30.719  -13.780 74.296  1.00 92.88  ? 42  PRO B O     1 
ATOM   4369  C CB    . PRO B 1 42  ? 31.981  -12.461 71.580  1.00 79.07  ? 42  PRO B CB    1 
ATOM   4370  C CG    . PRO B 1 42  ? 31.265  -11.689 70.482  1.00 88.66  ? 42  PRO B CG    1 
ATOM   4371  C CD    . PRO B 1 42  ? 30.233  -12.623 69.869  1.00 95.40  ? 42  PRO B CD    1 
ATOM   4372  N N     . TYR B 1 43  ? 29.080  -12.721 73.131  1.00 86.53  ? 43  TYR B N     1 
ATOM   4373  C CA    . TYR B 1 43  ? 28.235  -12.379 74.273  1.00 89.55  ? 43  TYR B CA    1 
ATOM   4374  C C     . TYR B 1 43  ? 26.930  -13.186 74.225  1.00 86.32  ? 43  TYR B C     1 
ATOM   4375  O O     . TYR B 1 43  ? 25.892  -12.669 73.803  1.00 98.04  ? 43  TYR B O     1 
ATOM   4376  C CB    . TYR B 1 43  ? 27.910  -10.876 74.291  1.00 90.41  ? 43  TYR B CB    1 
ATOM   4377  C CG    . TYR B 1 43  ? 29.067  -9.900  74.259  1.00 93.44  ? 43  TYR B CG    1 
ATOM   4378  C CD1   . TYR B 1 43  ? 30.366  -10.256 74.622  1.00 88.35  ? 43  TYR B CD1   1 
ATOM   4379  C CD2   . TYR B 1 43  ? 28.849  -8.589  73.847  1.00 92.90  ? 43  TYR B CD2   1 
ATOM   4380  C CE1   . TYR B 1 43  ? 31.410  -9.339  74.579  1.00 82.79  ? 43  TYR B CE1   1 
ATOM   4381  C CE2   . TYR B 1 43  ? 29.879  -7.662  73.799  1.00 93.23  ? 43  TYR B CE2   1 
ATOM   4382  C CZ    . TYR B 1 43  ? 31.163  -8.037  74.164  1.00 89.89  ? 43  TYR B CZ    1 
ATOM   4383  O OH    . TYR B 1 43  ? 32.156  -7.088  74.102  1.00 79.53  ? 43  TYR B OH    1 
ATOM   4384  N N     . THR B 1 44  ? 26.985  -14.447 74.680  1.00 88.74  ? 44  THR B N     1 
ATOM   4385  C CA    . THR B 1 44  ? 25.865  -15.383 74.590  1.00 94.19  ? 44  THR B CA    1 
ATOM   4386  C C     . THR B 1 44  ? 24.692  -14.900 75.449  1.00 96.65  ? 44  THR B C     1 
ATOM   4387  O O     . THR B 1 44  ? 24.913  -14.323 76.516  1.00 98.41  ? 44  THR B O     1 
ATOM   4388  C CB    . THR B 1 44  ? 26.298  -16.795 75.024  1.00 90.12  ? 44  THR B CB    1 
ATOM   4389  O OG1   . THR B 1 44  ? 27.612  -17.046 74.518  1.00 89.99  ? 44  THR B OG1   1 
ATOM   4390  C CG2   . THR B 1 44  ? 25.342  -17.877 74.565  1.00 81.80  ? 44  THR B CG2   1 
ATOM   4391  N N     . ILE B 1 45  ? 23.455  -15.129 74.962  1.00 92.40  ? 45  ILE B N     1 
ATOM   4392  C CA    . ILE B 1 45  ? 22.224  -14.876 75.714  1.00 91.80  ? 45  ILE B CA    1 
ATOM   4393  C C     . ILE B 1 45  ? 21.470  -16.194 75.943  1.00 94.84  ? 45  ILE B C     1 
ATOM   4394  O O     . ILE B 1 45  ? 20.796  -16.377 76.962  1.00 99.50  ? 45  ILE B O     1 
ATOM   4395  C CB    . ILE B 1 45  ? 21.320  -13.830 75.012  1.00 93.94  ? 45  ILE B CB    1 
ATOM   4396  C CG1   . ILE B 1 45  ? 22.087  -12.576 74.563  1.00 89.86  ? 45  ILE B CG1   1 
ATOM   4397  C CG2   . ILE B 1 45  ? 20.126  -13.481 75.899  1.00 91.97  ? 45  ILE B CG2   1 
ATOM   4398  C CD1   . ILE B 1 45  ? 21.223  -11.467 73.979  1.00 80.81  ? 45  ILE B CD1   1 
ATOM   4399  N N     . SER B 1 46  ? 21.569  -17.106 74.969  1.00 97.75  ? 46  SER B N     1 
ATOM   4400  C CA    . SER B 1 46  ? 20.830  -18.356 74.988  1.00 92.30  ? 46  SER B CA    1 
ATOM   4401  C C     . SER B 1 46  ? 21.485  -19.328 75.966  1.00 90.59  ? 46  SER B C     1 
ATOM   4402  O O     . SER B 1 46  ? 22.717  -19.420 76.033  1.00 68.82  ? 46  SER B O     1 
ATOM   4403  C CB    . SER B 1 46  ? 20.732  -18.943 73.589  1.00 89.53  ? 46  SER B CB    1 
ATOM   4404  O OG    . SER B 1 46  ? 19.930  -20.119 73.566  1.00 79.32  ? 46  SER B OG    1 
ATOM   4405  N N     . ASN B 1 47  ? 20.622  -20.026 76.723  1.00 98.91  ? 47  ASN B N     1 
ATOM   4406  C CA    . ASN B 1 47  ? 21.001  -21.183 77.521  1.00 100.50 ? 47  ASN B CA    1 
ATOM   4407  C C     . ASN B 1 47  ? 20.908  -22.460 76.688  1.00 98.44  ? 47  ASN B C     1 
ATOM   4408  O O     . ASN B 1 47  ? 21.535  -23.465 77.024  1.00 99.09  ? 47  ASN B O     1 
ATOM   4409  C CB    . ASN B 1 47  ? 20.140  -21.310 78.782  1.00 97.44  ? 47  ASN B CB    1 
ATOM   4410  C CG    . ASN B 1 47  ? 20.459  -20.244 79.805  1.00 87.98  ? 47  ASN B CG    1 
ATOM   4411  O OD1   . ASN B 1 47  ? 21.622  -19.892 79.976  1.00 76.48  ? 47  ASN B OD1   1 
ATOM   4412  N ND2   . ASN B 1 47  ? 19.442  -19.700 80.458  1.00 88.74  ? 47  ASN B ND2   1 
ATOM   4413  N N     . ASP B 1 48  ? 20.112  -22.415 75.612  1.00 100.38 ? 48  ASP B N     1 
ATOM   4414  C CA    . ASP B 1 48  ? 20.004  -23.516 74.666  1.00 99.96  ? 48  ASP B CA    1 
ATOM   4415  C C     . ASP B 1 48  ? 21.241  -23.508 73.755  1.00 100.13 ? 48  ASP B C     1 
ATOM   4416  O O     . ASP B 1 48  ? 21.387  -22.603 72.922  1.00 89.04  ? 48  ASP B O     1 
ATOM   4417  C CB    . ASP B 1 48  ? 18.659  -23.396 73.937  1.00 87.40  ? 48  ASP B CB    1 
ATOM   4418  C CG    . ASP B 1 48  ? 18.196  -24.648 73.214  1.00 84.41  ? 48  ASP B CG    1 
ATOM   4419  O OD1   . ASP B 1 48  ? 19.055  -25.490 72.868  1.00 78.45  ? 48  ASP B OD1   1 
ATOM   4420  O OD2   . ASP B 1 48  ? 16.968  -24.769 73.007  1.00 88.19  ? 48  ASP B OD2   1 
ATOM   4421  N N     . GLU B 1 49  ? 22.125  -24.518 73.909  1.00 99.87  ? 49  GLU B N     1 
ATOM   4422  C CA    . GLU B 1 49  ? 23.437  -24.522 73.259  1.00 100.80 ? 49  GLU B CA    1 
ATOM   4423  C C     . GLU B 1 49  ? 23.339  -24.998 71.801  1.00 107.32 ? 49  GLU B C     1 
ATOM   4424  O O     . GLU B 1 49  ? 24.366  -25.236 71.169  1.00 95.45  ? 49  GLU B O     1 
ATOM   4425  C CB    . GLU B 1 49  ? 24.439  -25.378 74.047  1.00 83.89  ? 49  GLU B CB    1 
ATOM   4426  N N     . THR B 1 50  ? 22.110  -25.096 71.257  1.00 111.96 ? 50  THR B N     1 
ATOM   4427  C CA    . THR B 1 50  ? 21.864  -25.532 69.885  1.00 106.10 ? 50  THR B CA    1 
ATOM   4428  C C     . THR B 1 50  ? 21.578  -24.358 68.940  1.00 96.61  ? 50  THR B C     1 
ATOM   4429  O O     . THR B 1 50  ? 21.479  -24.574 67.736  1.00 89.74  ? 50  THR B O     1 
ATOM   4430  C CB    . THR B 1 50  ? 20.676  -26.510 69.820  1.00 105.30 ? 50  THR B CB    1 
ATOM   4431  O OG1   . THR B 1 50  ? 19.484  -25.890 70.327  1.00 73.94  ? 50  THR B OG1   1 
ATOM   4432  C CG2   . THR B 1 50  ? 20.946  -27.797 70.574  1.00 103.73 ? 50  THR B CG2   1 
ATOM   4433  N N     . GLU B 1 51  ? 21.438  -23.133 69.476  1.00 88.75  ? 51  GLU B N     1 
ATOM   4434  C CA    . GLU B 1 51  ? 20.880  -22.005 68.738  1.00 95.44  ? 51  GLU B CA    1 
ATOM   4435  C C     . GLU B 1 51  ? 21.978  -21.022 68.319  1.00 94.83  ? 51  GLU B C     1 
ATOM   4436  O O     . GLU B 1 51  ? 22.921  -20.790 69.069  1.00 85.67  ? 51  GLU B O     1 
ATOM   4437  C CB    . GLU B 1 51  ? 19.839  -21.265 69.585  1.00 92.80  ? 51  GLU B CB    1 
ATOM   4438  C CG    . GLU B 1 51  ? 18.538  -22.028 69.780  1.00 89.52  ? 51  GLU B CG    1 
ATOM   4439  C CD    . GLU B 1 51  ? 17.496  -21.302 70.618  1.00 88.68  ? 51  GLU B CD    1 
ATOM   4440  O OE1   . GLU B 1 51  ? 17.886  -20.382 71.392  1.00 79.94  ? 51  GLU B OE1   1 
ATOM   4441  O OE2   . GLU B 1 51  ? 16.296  -21.651 70.490  1.00 81.80  ? 51  GLU B OE2   1 
ATOM   4442  N N     . HIS B 1 52  ? 21.826  -20.434 67.118  1.00 90.63  ? 52  HIS B N     1 
ATOM   4443  C CA    . HIS B 1 52  ? 22.729  -19.412 66.602  1.00 81.81  ? 52  HIS B CA    1 
ATOM   4444  C C     . HIS B 1 52  ? 24.145  -19.980 66.441  1.00 91.41  ? 52  HIS B C     1 
ATOM   4445  O O     . HIS B 1 52  ? 25.125  -19.284 66.736  1.00 87.54  ? 52  HIS B O     1 
ATOM   4446  C CB    . HIS B 1 52  ? 22.654  -18.144 67.468  1.00 74.94  ? 52  HIS B CB    1 
ATOM   4447  C CG    . HIS B 1 52  ? 21.253  -17.759 67.835  1.00 85.26  ? 52  HIS B CG    1 
ATOM   4448  N ND1   . HIS B 1 52  ? 20.199  -17.810 66.939  1.00 87.89  ? 52  HIS B ND1   1 
ATOM   4449  C CD2   . HIS B 1 52  ? 20.725  -17.361 69.008  1.00 85.64  ? 52  HIS B CD2   1 
ATOM   4450  C CE1   . HIS B 1 52  ? 19.082  -17.432 67.548  1.00 90.32  ? 52  HIS B CE1   1 
ATOM   4451  N NE2   . HIS B 1 52  ? 19.377  -17.157 68.808  1.00 95.15  ? 52  HIS B NE2   1 
ATOM   4452  N N     . ARG B 1 53  ? 24.228  -21.233 65.943  1.00 91.40  ? 53  ARG B N     1 
ATOM   4453  C CA    . ARG B 1 53  ? 25.473  -21.987 65.812  1.00 94.02  ? 53  ARG B CA    1 
ATOM   4454  C C     . ARG B 1 53  ? 25.818  -22.194 64.336  1.00 89.89  ? 53  ARG B C     1 
ATOM   4455  O O     . ARG B 1 53  ? 25.160  -22.972 63.648  1.00 104.07 ? 53  ARG B O     1 
ATOM   4456  C CB    . ARG B 1 53  ? 25.343  -23.356 66.491  1.00 94.17  ? 53  ARG B CB    1 
ATOM   4457  C CG    . ARG B 1 53  ? 24.814  -23.290 67.917  1.00 97.87  ? 53  ARG B CG    1 
ATOM   4458  C CD    . ARG B 1 53  ? 25.655  -22.405 68.827  1.00 97.95  ? 53  ARG B CD    1 
ATOM   4459  N NE    . ARG B 1 53  ? 27.078  -22.733 68.803  1.00 99.96  ? 53  ARG B NE    1 
ATOM   4460  C CZ    . ARG B 1 53  ? 27.598  -23.916 69.130  1.00 87.78  ? 53  ARG B CZ    1 
ATOM   4461  N NH1   . ARG B 1 53  ? 26.811  -24.917 69.475  1.00 75.14  ? 53  ARG B NH1   1 
ATOM   4462  N NH2   . ARG B 1 53  ? 28.907  -24.101 69.113  1.00 80.98  ? 53  ARG B NH2   1 
ATOM   4463  N N     . PRO B 1 54  ? 26.861  -21.521 63.796  1.00 77.52  ? 54  PRO B N     1 
ATOM   4464  C CA    . PRO B 1 54  ? 27.173  -21.606 62.366  1.00 72.76  ? 54  PRO B CA    1 
ATOM   4465  C C     . PRO B 1 54  ? 27.871  -22.905 61.964  1.00 64.96  ? 54  PRO B C     1 
ATOM   4466  O O     . PRO B 1 54  ? 28.866  -23.278 62.582  1.00 70.35  ? 54  PRO B O     1 
ATOM   4467  C CB    . PRO B 1 54  ? 28.101  -20.396 62.148  1.00 76.04  ? 54  PRO B CB    1 
ATOM   4468  C CG    . PRO B 1 54  ? 28.768  -20.161 63.483  1.00 75.50  ? 54  PRO B CG    1 
ATOM   4469  C CD    . PRO B 1 54  ? 27.770  -20.622 64.523  1.00 75.26  ? 54  PRO B CD    1 
ATOM   4470  N N     . TYR B 1 55  ? 27.393  -23.554 60.892  1.00 57.31  ? 55  TYR B N     1 
ATOM   4471  C CA    . TYR B 1 55  ? 27.920  -24.856 60.520  1.00 61.85  ? 55  TYR B CA    1 
ATOM   4472  C C     . TYR B 1 55  ? 29.346  -24.741 59.985  1.00 69.95  ? 55  TYR B C     1 
ATOM   4473  O O     . TYR B 1 55  ? 30.151  -25.642 60.220  1.00 72.42  ? 55  TYR B O     1 
ATOM   4474  C CB    . TYR B 1 55  ? 27.044  -25.572 59.489  1.00 68.14  ? 55  TYR B CB    1 
ATOM   4475  C CG    . TYR B 1 55  ? 27.500  -26.983 59.205  1.00 82.82  ? 55  TYR B CG    1 
ATOM   4476  C CD1   . TYR B 1 55  ? 28.545  -27.238 58.330  1.00 94.92  ? 55  TYR B CD1   1 
ATOM   4477  C CD2   . TYR B 1 55  ? 26.940  -28.070 59.867  1.00 97.22  ? 55  TYR B CD2   1 
ATOM   4478  C CE1   . TYR B 1 55  ? 28.998  -28.528 58.089  1.00 103.11 ? 55  TYR B CE1   1 
ATOM   4479  C CE2   . TYR B 1 55  ? 27.384  -29.367 59.641  1.00 104.00 ? 55  TYR B CE2   1 
ATOM   4480  C CZ    . TYR B 1 55  ? 28.417  -29.598 58.746  1.00 103.61 ? 55  TYR B CZ    1 
ATOM   4481  O OH    . TYR B 1 55  ? 28.885  -30.866 58.493  1.00 95.65  ? 55  TYR B OH    1 
ATOM   4482  N N     . ALA B 1 56  ? 29.625  -23.681 59.206  1.00 70.45  ? 56  ALA B N     1 
ATOM   4483  C CA    . ALA B 1 56  ? 30.951  -23.449 58.653  1.00 64.72  ? 56  ALA B CA    1 
ATOM   4484  C C     . ALA B 1 56  ? 31.118  -21.983 58.274  1.00 68.34  ? 56  ALA B C     1 
ATOM   4485  O O     . ALA B 1 56  ? 30.180  -21.190 58.349  1.00 67.43  ? 56  ALA B O     1 
ATOM   4486  C CB    . ALA B 1 56  ? 31.168  -24.325 57.456  1.00 59.37  ? 56  ALA B CB    1 
ATOM   4487  N N     . ALA B 1 57  ? 32.336  -21.635 57.862  1.00 64.56  ? 57  ALA B N     1 
ATOM   4488  C CA    . ALA B 1 57  ? 32.578  -20.334 57.271  1.00 69.65  ? 57  ALA B CA    1 
ATOM   4489  C C     . ALA B 1 57  ? 33.239  -20.490 55.903  1.00 64.63  ? 57  ALA B C     1 
ATOM   4490  O O     . ALA B 1 57  ? 33.828  -21.521 55.600  1.00 67.91  ? 57  ALA B O     1 
ATOM   4491  C CB    . ALA B 1 57  ? 33.404  -19.508 58.214  1.00 68.53  ? 57  ALA B CB    1 
ATOM   4492  N N     . VAL B 1 58  ? 33.090  -19.467 55.056  1.00 62.79  ? 58  VAL B N     1 
ATOM   4493  C CA    . VAL B 1 58  ? 33.781  -19.411 53.774  1.00 55.01  ? 58  VAL B CA    1 
ATOM   4494  C C     . VAL B 1 58  ? 34.180  -17.956 53.546  1.00 56.53  ? 58  VAL B C     1 
ATOM   4495  O O     . VAL B 1 58  ? 33.382  -17.063 53.786  1.00 62.38  ? 58  VAL B O     1 
ATOM   4496  C CB    . VAL B 1 58  ? 32.922  -19.977 52.635  1.00 51.64  ? 58  VAL B CB    1 
ATOM   4497  C CG1   . VAL B 1 58  ? 31.523  -19.409 52.657  1.00 56.49  ? 58  VAL B CG1   1 
ATOM   4498  C CG2   . VAL B 1 58  ? 33.542  -19.761 51.259  1.00 57.54  ? 58  VAL B CG2   1 
ATOM   4499  N N     . ALA B 1 59  ? 35.433  -17.733 53.131  1.00 50.22  ? 59  ALA B N     1 
ATOM   4500  C CA    . ALA B 1 59  ? 36.026  -16.411 53.097  1.00 45.56  ? 59  ALA B CA    1 
ATOM   4501  C C     . ALA B 1 59  ? 36.513  -16.081 51.681  1.00 46.61  ? 59  ALA B C     1 
ATOM   4502  O O     . ALA B 1 59  ? 37.698  -16.171 51.342  1.00 49.55  ? 59  ALA B O     1 
ATOM   4503  C CB    . ALA B 1 59  ? 37.129  -16.324 54.123  1.00 44.44  ? 59  ALA B CB    1 
ATOM   4504  N N     . PRO B 1 60  ? 35.614  -15.596 50.815  1.00 44.59  ? 60  PRO B N     1 
ATOM   4505  C CA    . PRO B 1 60  ? 35.986  -15.230 49.445  1.00 41.80  ? 60  PRO B CA    1 
ATOM   4506  C C     . PRO B 1 60  ? 36.972  -14.078 49.330  1.00 39.84  ? 60  PRO B C     1 
ATOM   4507  O O     . PRO B 1 60  ? 37.113  -13.313 50.277  1.00 45.76  ? 60  PRO B O     1 
ATOM   4508  C CB    . PRO B 1 60  ? 34.659  -14.813 48.805  1.00 46.02  ? 60  PRO B CB    1 
ATOM   4509  C CG    . PRO B 1 60  ? 33.758  -14.470 49.995  1.00 53.06  ? 60  PRO B CG    1 
ATOM   4510  C CD    . PRO B 1 60  ? 34.206  -15.347 51.136  1.00 46.91  ? 60  PRO B CD    1 
ATOM   4511  N N     . ALA B 1 61  ? 37.666  -13.982 48.172  1.00 42.32  ? 61  ALA B N     1 
ATOM   4512  C CA    . ALA B 1 61  ? 38.670  -12.947 47.969  1.00 49.40  ? 61  ALA B CA    1 
ATOM   4513  C C     . ALA B 1 61  ? 38.133  -11.789 47.110  1.00 52.29  ? 61  ALA B C     1 
ATOM   4514  O O     . ALA B 1 61  ? 38.817  -10.779 46.952  1.00 46.74  ? 61  ALA B O     1 
ATOM   4515  C CB    . ALA B 1 61  ? 39.929  -13.549 47.377  1.00 51.99  ? 61  ALA B CB    1 
ATOM   4516  N N     . SER B 1 62  ? 36.920  -11.928 46.557  1.00 40.40  ? 62  SER B N     1 
ATOM   4517  C CA    . SER B 1 62  ? 36.463  -11.020 45.532  1.00 45.58  ? 62  SER B CA    1 
ATOM   4518  C C     . SER B 1 62  ? 34.965  -11.215 45.333  1.00 46.91  ? 62  SER B C     1 
ATOM   4519  O O     . SER B 1 62  ? 34.445  -12.275 45.680  1.00 49.69  ? 62  SER B O     1 
ATOM   4520  C CB    . SER B 1 62  ? 37.228  -11.229 44.232  1.00 45.70  ? 62  SER B CB    1 
ATOM   4521  O OG    . SER B 1 62  ? 36.938  -12.506 43.658  1.00 50.80  ? 62  SER B OG    1 
ATOM   4522  N N     . THR B 1 63  ? 34.325  -10.165 44.785  1.00 42.91  ? 63  THR B N     1 
ATOM   4523  C CA    . THR B 1 63  ? 32.927  -10.119 44.371  1.00 45.76  ? 63  THR B CA    1 
ATOM   4524  C C     . THR B 1 63  ? 32.531  -11.359 43.558  1.00 52.38  ? 63  THR B C     1 
ATOM   4525  O O     . THR B 1 63  ? 31.420  -11.877 43.703  1.00 47.30  ? 63  THR B O     1 
ATOM   4526  C CB    . THR B 1 63  ? 32.648  -8.854  43.524  1.00 41.50  ? 63  THR B CB    1 
ATOM   4527  O OG1   . THR B 1 63  ? 32.813  -7.658  44.298  1.00 44.52  ? 63  THR B OG1   1 
ATOM   4528  C CG2   . THR B 1 63  ? 31.247  -8.836  42.947  1.00 37.00  ? 63  THR B CG2   1 
ATOM   4529  N N     . GLU B 1 64  ? 33.424  -11.809 42.665  1.00 49.89  ? 64  GLU B N     1 
ATOM   4530  C CA    . GLU B 1 64  ? 33.040  -12.798 41.671  1.00 54.13  ? 64  GLU B CA    1 
ATOM   4531  C C     . GLU B 1 64  ? 33.067  -14.182 42.319  1.00 51.40  ? 64  GLU B C     1 
ATOM   4532  O O     . GLU B 1 64  ? 32.222  -15.025 41.986  1.00 44.46  ? 64  GLU B O     1 
ATOM   4533  C CB    . GLU B 1 64  ? 33.923  -12.718 40.415  1.00 50.49  ? 64  GLU B CB    1 
ATOM   4534  C CG    . GLU B 1 64  ? 33.261  -13.288 39.170  1.00 50.96  ? 64  GLU B CG    1 
ATOM   4535  C CD    . GLU B 1 64  ? 33.137  -14.806 39.134  1.00 49.68  ? 64  GLU B CD    1 
ATOM   4536  O OE1   . GLU B 1 64  ? 34.096  -15.474 39.582  1.00 46.86  ? 64  GLU B OE1   1 
ATOM   4537  O OE2   . GLU B 1 64  ? 32.117  -15.310 38.597  1.00 44.05  ? 64  GLU B OE2   1 
ATOM   4538  N N     . GLU B 1 65  ? 34.032  -14.394 43.233  1.00 47.65  ? 65  GLU B N     1 
ATOM   4539  C CA    . GLU B 1 65  ? 34.009  -15.569 44.097  1.00 49.03  ? 65  GLU B CA    1 
ATOM   4540  C C     . GLU B 1 65  ? 32.733  -15.535 44.938  1.00 50.21  ? 65  GLU B C     1 
ATOM   4541  O O     . GLU B 1 65  ? 32.099  -16.566 45.130  1.00 49.87  ? 65  GLU B O     1 
ATOM   4542  C CB    . GLU B 1 65  ? 35.255  -15.655 44.977  1.00 50.14  ? 65  GLU B CB    1 
ATOM   4543  C CG    . GLU B 1 65  ? 36.536  -15.955 44.198  1.00 45.23  ? 65  GLU B CG    1 
ATOM   4544  C CD    . GLU B 1 65  ? 37.788  -16.073 45.051  1.00 46.13  ? 65  GLU B CD    1 
ATOM   4545  O OE1   . GLU B 1 65  ? 37.674  -15.988 46.296  1.00 52.09  ? 65  GLU B OE1   1 
ATOM   4546  O OE2   . GLU B 1 65  ? 38.885  -16.216 44.478  1.00 49.85  ? 65  GLU B OE2   1 
ATOM   4547  N N     . VAL B 1 66  ? 32.305  -14.335 45.359  1.00 51.39  ? 66  VAL B N     1 
ATOM   4548  C CA    . VAL B 1 66  ? 31.071  -14.208 46.115  1.00 47.02  ? 66  VAL B CA    1 
ATOM   4549  C C     . VAL B 1 66  ? 29.910  -14.718 45.274  1.00 45.25  ? 66  VAL B C     1 
ATOM   4550  O O     . VAL B 1 66  ? 29.092  -15.483 45.782  1.00 41.62  ? 66  VAL B O     1 
ATOM   4551  C CB    . VAL B 1 66  ? 30.825  -12.772 46.618  1.00 50.21  ? 66  VAL B CB    1 
ATOM   4552  C CG1   . VAL B 1 66  ? 29.397  -12.585 47.117  1.00 46.87  ? 66  VAL B CG1   1 
ATOM   4553  C CG2   . VAL B 1 66  ? 31.824  -12.369 47.695  1.00 48.07  ? 66  VAL B CG2   1 
ATOM   4554  N N     . GLN B 1 67  ? 29.850  -14.292 43.998  1.00 48.54  ? 67  GLN B N     1 
ATOM   4555  C CA    . GLN B 1 67  ? 28.825  -14.758 43.062  1.00 44.83  ? 67  GLN B CA    1 
ATOM   4556  C C     . GLN B 1 67  ? 28.885  -16.275 42.883  1.00 46.76  ? 67  GLN B C     1 
ATOM   4557  O O     . GLN B 1 67  ? 27.845  -16.953 42.867  1.00 42.22  ? 67  GLN B O     1 
ATOM   4558  C CB    . GLN B 1 67  ? 29.001  -14.151 41.672  1.00 49.58  ? 67  GLN B CB    1 
ATOM   4559  C CG    . GLN B 1 67  ? 28.553  -12.697 41.566  1.00 52.34  ? 67  GLN B CG    1 
ATOM   4560  C CD    . GLN B 1 67  ? 28.989  -12.054 40.273  1.00 45.97  ? 67  GLN B CD    1 
ATOM   4561  O OE1   . GLN B 1 67  ? 28.225  -11.962 39.312  1.00 42.54  ? 67  GLN B OE1   1 
ATOM   4562  N NE2   . GLN B 1 67  ? 30.230  -11.596 40.254  1.00 42.74  ? 67  GLN B NE2   1 
ATOM   4563  N N     . GLU B 1 68  ? 30.113  -16.792 42.729  1.00 50.39  ? 68  GLU B N     1 
ATOM   4564  C CA    . GLU B 1 68  ? 30.317  -18.207 42.466  1.00 49.88  ? 68  GLU B CA    1 
ATOM   4565  C C     . GLU B 1 68  ? 29.680  -18.966 43.630  1.00 52.28  ? 68  GLU B C     1 
ATOM   4566  O O     . GLU B 1 68  ? 28.793  -19.796 43.405  1.00 49.50  ? 68  GLU B O     1 
ATOM   4567  C CB    . GLU B 1 68  ? 31.796  -18.500 42.191  1.00 46.01  ? 68  GLU B CB    1 
ATOM   4568  C CG    . GLU B 1 68  ? 32.201  -18.380 40.724  1.00 45.98  ? 68  GLU B CG    1 
ATOM   4569  C CD    . GLU B 1 68  ? 33.614  -18.840 40.365  1.00 49.12  ? 68  GLU B CD    1 
ATOM   4570  O OE1   . GLU B 1 68  ? 33.904  -20.050 40.429  1.00 50.89  ? 68  GLU B OE1   1 
ATOM   4571  O OE2   . GLU B 1 68  ? 34.439  -17.991 40.014  1.00 52.64  ? 68  GLU B OE2   1 
ATOM   4572  N N     . ILE B 1 69  ? 30.019  -18.552 44.865  1.00 47.23  ? 69  ILE B N     1 
ATOM   4573  C CA    . ILE B 1 69  ? 29.491  -19.189 46.067  1.00 45.86  ? 69  ILE B CA    1 
ATOM   4574  C C     . ILE B 1 69  ? 27.972  -19.104 46.078  1.00 47.28  ? 69  ILE B C     1 
ATOM   4575  O O     . ILE B 1 69  ? 27.296  -20.093 46.289  1.00 52.07  ? 69  ILE B O     1 
ATOM   4576  C CB    . ILE B 1 69  ? 30.059  -18.533 47.329  1.00 49.13  ? 69  ILE B CB    1 
ATOM   4577  C CG1   . ILE B 1 69  ? 31.560  -18.779 47.478  1.00 50.38  ? 69  ILE B CG1   1 
ATOM   4578  C CG2   . ILE B 1 69  ? 29.271  -18.988 48.543  1.00 61.41  ? 69  ILE B CG2   1 
ATOM   4579  C CD1   . ILE B 1 69  ? 32.259  -17.766 48.361  1.00 53.69  ? 69  ILE B CD1   1 
ATOM   4580  N N     . VAL B 1 70  ? 27.423  -17.913 45.858  1.00 45.29  ? 70  VAL B N     1 
ATOM   4581  C CA    . VAL B 1 70  ? 25.984  -17.788 45.970  1.00 45.77  ? 70  VAL B CA    1 
ATOM   4582  C C     . VAL B 1 70  ? 25.306  -18.759 45.001  1.00 47.18  ? 70  VAL B C     1 
ATOM   4583  O O     . VAL B 1 70  ? 24.173  -19.139 45.246  1.00 48.85  ? 70  VAL B O     1 
ATOM   4584  C CB    . VAL B 1 70  ? 25.522  -16.330 45.759  1.00 43.65  ? 70  VAL B CB    1 
ATOM   4585  C CG1   . VAL B 1 70  ? 24.004  -16.195 45.713  1.00 39.62  ? 70  VAL B CG1   1 
ATOM   4586  C CG2   . VAL B 1 70  ? 26.085  -15.404 46.817  1.00 44.59  ? 70  VAL B CG2   1 
ATOM   4587  N N     . ARG B 1 71  ? 25.931  -19.083 43.853  1.00 56.83  ? 71  ARG B N     1 
ATOM   4588  C CA    . ARG B 1 71  ? 25.267  -19.910 42.839  1.00 55.01  ? 71  ARG B CA    1 
ATOM   4589  C C     . ARG B 1 71  ? 25.218  -21.355 43.339  1.00 53.13  ? 71  ARG B C     1 
ATOM   4590  O O     . ARG B 1 71  ? 24.178  -21.999 43.327  1.00 44.72  ? 71  ARG B O     1 
ATOM   4591  C CB    . ARG B 1 71  ? 25.975  -19.835 41.474  1.00 53.86  ? 71  ARG B CB    1 
ATOM   4592  C CG    . ARG B 1 71  ? 25.698  -18.559 40.693  1.00 54.39  ? 71  ARG B CG    1 
ATOM   4593  C CD    . ARG B 1 71  ? 26.247  -18.464 39.276  1.00 51.95  ? 71  ARG B CD    1 
ATOM   4594  N NE    . ARG B 1 71  ? 25.878  -17.185 38.657  1.00 46.87  ? 71  ARG B NE    1 
ATOM   4595  C CZ    . ARG B 1 71  ? 26.757  -16.272 38.241  1.00 47.54  ? 71  ARG B CZ    1 
ATOM   4596  N NH1   . ARG B 1 71  ? 28.022  -16.606 38.057  1.00 48.36  ? 71  ARG B NH1   1 
ATOM   4597  N NH2   . ARG B 1 71  ? 26.374  -15.035 37.971  1.00 47.34  ? 71  ARG B NH2   1 
ATOM   4598  N N     . VAL B 1 72  ? 26.369  -21.821 43.825  1.00 60.71  ? 72  VAL B N     1 
ATOM   4599  C CA    . VAL B 1 72  ? 26.514  -23.094 44.514  1.00 67.04  ? 72  VAL B CA    1 
ATOM   4600  C C     . VAL B 1 72  ? 25.526  -23.245 45.672  1.00 65.15  ? 72  VAL B C     1 
ATOM   4601  O O     . VAL B 1 72  ? 25.014  -24.338 45.897  1.00 61.92  ? 72  VAL B O     1 
ATOM   4602  C CB    . VAL B 1 72  ? 27.963  -23.250 45.001  1.00 64.68  ? 72  VAL B CB    1 
ATOM   4603  C CG1   . VAL B 1 72  ? 28.067  -24.194 46.191  1.00 64.68  ? 72  VAL B CG1   1 
ATOM   4604  C CG2   . VAL B 1 72  ? 28.861  -23.681 43.845  1.00 65.13  ? 72  VAL B CG2   1 
ATOM   4605  N N     . ALA B 1 73  ? 25.291  -22.162 46.416  1.00 60.92  ? 73  ALA B N     1 
ATOM   4606  C CA    . ALA B 1 73  ? 24.395  -22.198 47.560  1.00 60.84  ? 73  ALA B CA    1 
ATOM   4607  C C     . ALA B 1 73  ? 22.944  -22.381 47.122  1.00 59.27  ? 73  ALA B C     1 
ATOM   4608  O O     . ALA B 1 73  ? 22.155  -22.908 47.885  1.00 69.03  ? 73  ALA B O     1 
ATOM   4609  C CB    . ALA B 1 73  ? 24.536  -20.943 48.371  1.00 56.69  ? 73  ALA B CB    1 
ATOM   4610  N N     . ASN B 1 74  ? 22.575  -21.904 45.933  1.00 61.47  ? 74  ASN B N     1 
ATOM   4611  C CA    . ASN B 1 74  ? 21.217  -22.094 45.453  1.00 64.27  ? 74  ASN B CA    1 
ATOM   4612  C C     . ASN B 1 74  ? 21.059  -23.567 45.076  1.00 68.46  ? 74  ASN B C     1 
ATOM   4613  O O     . ASN B 1 74  ? 20.013  -24.162 45.337  1.00 65.92  ? 74  ASN B O     1 
ATOM   4614  C CB    . ASN B 1 74  ? 20.840  -21.162 44.285  1.00 57.28  ? 74  ASN B CB    1 
ATOM   4615  C CG    . ASN B 1 74  ? 20.342  -19.778 44.676  1.00 61.82  ? 74  ASN B CG    1 
ATOM   4616  O OD1   . ASN B 1 74  ? 19.141  -19.559 44.878  1.00 62.20  ? 74  ASN B OD1   1 
ATOM   4617  N ND2   . ASN B 1 74  ? 21.248  -18.809 44.707  1.00 56.03  ? 74  ASN B ND2   1 
ATOM   4618  N N     . GLU B 1 75  ? 22.102  -24.174 44.491  1.00 68.71  ? 75  GLU B N     1 
ATOM   4619  C CA    . GLU B 1 75  ? 21.888  -25.456 43.838  1.00 86.98  ? 75  GLU B CA    1 
ATOM   4620  C C     . GLU B 1 75  ? 21.960  -26.610 44.846  1.00 78.14  ? 75  GLU B C     1 
ATOM   4621  O O     . GLU B 1 75  ? 21.586  -27.716 44.489  1.00 79.31  ? 75  GLU B O     1 
ATOM   4622  C CB    . GLU B 1 75  ? 22.818  -25.641 42.632  1.00 100.53 ? 75  GLU B CB    1 
ATOM   4623  C CG    . GLU B 1 75  ? 24.187  -26.224 42.951  1.00 111.85 ? 75  GLU B CG    1 
ATOM   4624  C CD    . GLU B 1 75  ? 24.846  -26.968 41.795  1.00 115.21 ? 75  GLU B CD    1 
ATOM   4625  O OE1   . GLU B 1 75  ? 25.277  -28.132 42.006  1.00 116.60 ? 75  GLU B OE1   1 
ATOM   4626  O OE2   . GLU B 1 75  ? 24.919  -26.393 40.684  1.00 94.47  ? 75  GLU B OE2   1 
ATOM   4627  N N     . PHE B 1 76  ? 22.401  -26.357 46.091  1.00 78.58  ? 76  PHE B N     1 
ATOM   4628  C CA    . PHE B 1 76  ? 22.445  -27.360 47.153  1.00 73.16  ? 76  PHE B CA    1 
ATOM   4629  C C     . PHE B 1 76  ? 21.562  -26.983 48.350  1.00 71.60  ? 76  PHE B C     1 
ATOM   4630  O O     . PHE B 1 76  ? 21.542  -27.697 49.353  1.00 63.67  ? 76  PHE B O     1 
ATOM   4631  C CB    . PHE B 1 76  ? 23.894  -27.576 47.610  1.00 72.80  ? 76  PHE B CB    1 
ATOM   4632  C CG    . PHE B 1 76  ? 24.736  -28.339 46.621  1.00 81.46  ? 76  PHE B CG    1 
ATOM   4633  C CD1   . PHE B 1 76  ? 24.275  -29.527 46.063  1.00 93.71  ? 76  PHE B CD1   1 
ATOM   4634  C CD2   . PHE B 1 76  ? 25.988  -27.882 46.249  1.00 85.40  ? 76  PHE B CD2   1 
ATOM   4635  C CE1   . PHE B 1 76  ? 25.035  -30.226 45.139  1.00 92.12  ? 76  PHE B CE1   1 
ATOM   4636  C CE2   . PHE B 1 76  ? 26.754  -28.587 45.333  1.00 92.99  ? 76  PHE B CE2   1 
ATOM   4637  C CZ    . PHE B 1 76  ? 26.278  -29.758 44.782  1.00 99.23  ? 76  PHE B CZ    1 
ATOM   4638  N N     . GLY B 1 77  ? 20.843  -25.854 48.240  1.00 73.71  ? 77  GLY B N     1 
ATOM   4639  C CA    . GLY B 1 77  ? 19.907  -25.389 49.256  1.00 67.78  ? 77  GLY B CA    1 
ATOM   4640  C C     . GLY B 1 77  ? 20.572  -24.936 50.558  1.00 61.40  ? 77  GLY B C     1 
ATOM   4641  O O     . GLY B 1 77  ? 19.869  -24.743 51.547  1.00 64.17  ? 77  GLY B O     1 
ATOM   4642  N N     . VAL B 1 78  ? 21.904  -24.753 50.554  1.00 56.13  ? 78  VAL B N     1 
ATOM   4643  C CA    . VAL B 1 78  ? 22.656  -24.363 51.743  1.00 56.58  ? 78  VAL B CA    1 
ATOM   4644  C C     . VAL B 1 78  ? 22.559  -22.848 51.956  1.00 60.82  ? 78  VAL B C     1 
ATOM   4645  O O     . VAL B 1 78  ? 22.848  -22.097 51.033  1.00 73.55  ? 78  VAL B O     1 
ATOM   4646  C CB    . VAL B 1 78  ? 24.126  -24.795 51.598  1.00 52.42  ? 78  VAL B CB    1 
ATOM   4647  C CG1   . VAL B 1 78  ? 25.020  -24.177 52.651  1.00 48.33  ? 78  VAL B CG1   1 
ATOM   4648  C CG2   . VAL B 1 78  ? 24.262  -26.310 51.614  1.00 60.34  ? 78  VAL B CG2   1 
ATOM   4649  N N     . PRO B 1 79  ? 22.201  -22.342 53.162  1.00 55.19  ? 79  PRO B N     1 
ATOM   4650  C CA    . PRO B 1 79  ? 22.117  -20.910 53.429  1.00 60.40  ? 79  PRO B CA    1 
ATOM   4651  C C     . PRO B 1 79  ? 23.384  -20.239 53.950  1.00 64.25  ? 79  PRO B C     1 
ATOM   4652  O O     . PRO B 1 79  ? 24.219  -20.875 54.606  1.00 55.05  ? 79  PRO B O     1 
ATOM   4653  C CB    . PRO B 1 79  ? 21.049  -20.818 54.531  1.00 68.28  ? 79  PRO B CB    1 
ATOM   4654  C CG    . PRO B 1 79  ? 21.254  -22.082 55.330  1.00 63.76  ? 79  PRO B CG    1 
ATOM   4655  C CD    . PRO B 1 79  ? 21.764  -23.111 54.334  1.00 68.64  ? 79  PRO B CD    1 
ATOM   4656  N N     . LEU B 1 80  ? 23.456  -18.928 53.657  1.00 56.98  ? 80  LEU B N     1 
ATOM   4657  C CA    . LEU B 1 80  ? 24.646  -18.119 53.813  1.00 51.89  ? 80  LEU B CA    1 
ATOM   4658  C C     . LEU B 1 80  ? 24.316  -16.983 54.767  1.00 55.67  ? 80  LEU B C     1 
ATOM   4659  O O     . LEU B 1 80  ? 23.205  -16.458 54.710  1.00 49.79  ? 80  LEU B O     1 
ATOM   4660  C CB    . LEU B 1 80  ? 25.016  -17.519 52.459  1.00 54.98  ? 80  LEU B CB    1 
ATOM   4661  C CG    . LEU B 1 80  ? 25.555  -18.472 51.395  1.00 53.65  ? 80  LEU B CG    1 
ATOM   4662  C CD1   . LEU B 1 80  ? 26.110  -17.694 50.205  1.00 53.36  ? 80  LEU B CD1   1 
ATOM   4663  C CD2   . LEU B 1 80  ? 26.641  -19.348 51.964  1.00 51.26  ? 80  LEU B CD2   1 
ATOM   4664  N N     . TRP B 1 81  ? 25.288  -16.604 55.608  1.00 46.19  ? 81  TRP B N     1 
ATOM   4665  C CA    . TRP B 1 81  ? 25.109  -15.501 56.522  1.00 45.73  ? 81  TRP B CA    1 
ATOM   4666  C C     . TRP B 1 81  ? 26.220  -14.491 56.259  1.00 47.38  ? 81  TRP B C     1 
ATOM   4667  O O     . TRP B 1 81  ? 27.343  -14.643 56.718  1.00 49.41  ? 81  TRP B O     1 
ATOM   4668  C CB    . TRP B 1 81  ? 25.054  -15.984 57.980  1.00 45.50  ? 81  TRP B CB    1 
ATOM   4669  C CG    . TRP B 1 81  ? 24.651  -14.888 58.908  1.00 44.45  ? 81  TRP B CG    1 
ATOM   4670  C CD1   . TRP B 1 81  ? 25.451  -13.939 59.462  1.00 45.14  ? 81  TRP B CD1   1 
ATOM   4671  C CD2   . TRP B 1 81  ? 23.304  -14.532 59.267  1.00 45.71  ? 81  TRP B CD2   1 
ATOM   4672  N NE1   . TRP B 1 81  ? 24.699  -13.042 60.176  1.00 46.97  ? 81  TRP B NE1   1 
ATOM   4673  C CE2   . TRP B 1 81  ? 23.380  -13.387 60.078  1.00 45.11  ? 81  TRP B CE2   1 
ATOM   4674  C CE3   . TRP B 1 81  ? 22.057  -15.093 59.002  1.00 41.62  ? 81  TRP B CE3   1 
ATOM   4675  C CZ2   . TRP B 1 81  ? 22.252  -12.786 60.615  1.00 45.38  ? 81  TRP B CZ2   1 
ATOM   4676  C CZ3   . TRP B 1 81  ? 20.946  -14.512 59.540  1.00 43.11  ? 81  TRP B CZ3   1 
ATOM   4677  C CH2   . TRP B 1 81  ? 21.043  -13.356 60.309  1.00 44.10  ? 81  TRP B CH2   1 
ATOM   4678  N N     . PRO B 1 82  ? 25.957  -13.452 55.443  1.00 50.51  ? 82  PRO B N     1 
ATOM   4679  C CA    . PRO B 1 82  ? 26.994  -12.516 55.038  1.00 53.69  ? 82  PRO B CA    1 
ATOM   4680  C C     . PRO B 1 82  ? 27.453  -11.670 56.210  1.00 55.49  ? 82  PRO B C     1 
ATOM   4681  O O     . PRO B 1 82  ? 26.635  -11.082 56.897  1.00 53.71  ? 82  PRO B O     1 
ATOM   4682  C CB    . PRO B 1 82  ? 26.309  -11.611 54.011  1.00 53.61  ? 82  PRO B CB    1 
ATOM   4683  C CG    . PRO B 1 82  ? 25.084  -12.389 53.584  1.00 49.88  ? 82  PRO B CG    1 
ATOM   4684  C CD    . PRO B 1 82  ? 24.663  -13.143 54.824  1.00 52.60  ? 82  PRO B CD    1 
ATOM   4685  N N     . VAL B 1 83  ? 28.767  -11.599 56.400  1.00 57.74  ? 83  VAL B N     1 
ATOM   4686  C CA    . VAL B 1 83  ? 29.311  -10.635 57.333  1.00 58.02  ? 83  VAL B CA    1 
ATOM   4687  C C     . VAL B 1 83  ? 30.517  -9.940  56.700  1.00 63.25  ? 83  VAL B C     1 
ATOM   4688  O O     . VAL B 1 83  ? 31.297  -10.569 55.981  1.00 66.67  ? 83  VAL B O     1 
ATOM   4689  C CB    . VAL B 1 83  ? 29.636  -11.318 58.666  1.00 46.13  ? 83  VAL B CB    1 
ATOM   4690  C CG1   . VAL B 1 83  ? 28.417  -12.041 59.208  1.00 47.12  ? 83  VAL B CG1   1 
ATOM   4691  C CG2   . VAL B 1 83  ? 30.776  -12.286 58.527  1.00 48.54  ? 83  VAL B CG2   1 
ATOM   4692  N N     . SER B 1 84  ? 30.621  -8.629  56.961  1.00 51.78  ? 84  SER B N     1 
ATOM   4693  C CA    . SER B 1 84  ? 31.652  -7.795  56.388  1.00 56.77  ? 84  SER B CA    1 
ATOM   4694  C C     . SER B 1 84  ? 32.965  -8.033  57.126  1.00 56.95  ? 84  SER B C     1 
ATOM   4695  O O     . SER B 1 84  ? 33.909  -8.546  56.537  1.00 60.36  ? 84  SER B O     1 
ATOM   4696  C CB    . SER B 1 84  ? 31.246  -6.332  56.390  1.00 58.59  ? 84  SER B CB    1 
ATOM   4697  O OG    . SER B 1 84  ? 30.270  -6.050  55.393  1.00 53.85  ? 84  SER B OG    1 
ATOM   4698  N N     . ARG B 1 85  ? 33.013  -7.644  58.404  1.00 60.47  ? 85  ARG B N     1 
ATOM   4699  C CA    . ARG B 1 85  ? 34.102  -8.007  59.301  1.00 60.62  ? 85  ARG B CA    1 
ATOM   4700  C C     . ARG B 1 85  ? 33.565  -8.777  60.495  1.00 58.26  ? 85  ARG B C     1 
ATOM   4701  O O     . ARG B 1 85  ? 34.345  -9.385  61.223  1.00 64.00  ? 85  ARG B O     1 
ATOM   4702  C CB    . ARG B 1 85  ? 34.810  -6.775  59.854  1.00 60.34  ? 85  ARG B CB    1 
ATOM   4703  C CG    . ARG B 1 85  ? 35.668  -6.055  58.831  1.00 54.12  ? 85  ARG B CG    1 
ATOM   4704  C CD    . ARG B 1 85  ? 36.315  -4.838  59.449  1.00 48.27  ? 85  ARG B CD    1 
ATOM   4705  N NE    . ARG B 1 85  ? 37.317  -5.213  60.433  1.00 54.13  ? 85  ARG B NE    1 
ATOM   4706  C CZ    . ARG B 1 85  ? 38.521  -5.711  60.152  1.00 50.69  ? 85  ARG B CZ    1 
ATOM   4707  N NH1   . ARG B 1 85  ? 38.899  -5.900  58.896  1.00 49.18  ? 85  ARG B NH1   1 
ATOM   4708  N NH2   . ARG B 1 85  ? 39.329  -6.055  61.139  1.00 44.97  ? 85  ARG B NH2   1 
ATOM   4709  N N     . GLY B 1 86  ? 32.249  -8.672  60.710  1.00 57.02  ? 86  GLY B N     1 
ATOM   4710  C CA    . GLY B 1 86  ? 31.538  -9.513  61.654  1.00 55.26  ? 86  GLY B CA    1 
ATOM   4711  C C     . GLY B 1 86  ? 31.814  -9.113  63.097  1.00 58.86  ? 86  GLY B C     1 
ATOM   4712  O O     . GLY B 1 86  ? 31.779  -9.968  63.972  1.00 56.11  ? 86  GLY B O     1 
ATOM   4713  N N     . LYS B 1 87  ? 32.054  -7.813  63.328  1.00 73.00  ? 87  LYS B N     1 
ATOM   4714  C CA    . LYS B 1 87  ? 32.433  -7.304  64.641  1.00 80.32  ? 87  LYS B CA    1 
ATOM   4715  C C     . LYS B 1 87  ? 31.209  -6.712  65.356  1.00 72.59  ? 87  LYS B C     1 
ATOM   4716  O O     . LYS B 1 87  ? 31.342  -5.771  66.148  1.00 62.85  ? 87  LYS B O     1 
ATOM   4717  C CB    . LYS B 1 87  ? 33.588  -6.299  64.495  1.00 83.01  ? 87  LYS B CB    1 
ATOM   4718  C CG    . LYS B 1 87  ? 34.821  -6.813  63.756  1.00 85.94  ? 87  LYS B CG    1 
ATOM   4719  C CD    . LYS B 1 87  ? 35.603  -7.924  64.459  1.00 84.80  ? 87  LYS B CD    1 
ATOM   4720  C CE    . LYS B 1 87  ? 36.084  -8.990  63.490  1.00 89.06  ? 87  LYS B CE    1 
ATOM   4721  N NZ    . LYS B 1 87  ? 37.312  -9.677  63.945  1.00 81.43  ? 87  LYS B NZ    1 
ATOM   4722  N N     . ASN B 1 88  ? 30.035  -7.342  65.138  1.00 62.35  ? 88  ASN B N     1 
ATOM   4723  C CA    . ASN B 1 88  ? 28.739  -6.790  65.515  1.00 68.26  ? 88  ASN B CA    1 
ATOM   4724  C C     . ASN B 1 88  ? 28.399  -7.151  66.973  1.00 61.84  ? 88  ASN B C     1 
ATOM   4725  O O     . ASN B 1 88  ? 27.325  -7.690  67.238  1.00 52.78  ? 88  ASN B O     1 
ATOM   4726  C CB    . ASN B 1 88  ? 27.670  -7.265  64.512  1.00 59.86  ? 88  ASN B CB    1 
ATOM   4727  C CG    . ASN B 1 88  ? 26.477  -6.338  64.365  1.00 62.72  ? 88  ASN B CG    1 
ATOM   4728  O OD1   . ASN B 1 88  ? 26.552  -5.140  64.651  1.00 64.04  ? 88  ASN B OD1   1 
ATOM   4729  N ND2   . ASN B 1 88  ? 25.378  -6.874  63.860  1.00 64.01  ? 88  ASN B ND2   1 
ATOM   4730  N N     . PHE B 1 89  ? 29.265  -6.768  67.924  1.00 67.85  ? 89  PHE B N     1 
ATOM   4731  C CA    . PHE B 1 89  ? 29.405  -7.471  69.198  1.00 79.68  ? 89  PHE B CA    1 
ATOM   4732  C C     . PHE B 1 89  ? 28.140  -7.464  70.076  1.00 85.19  ? 89  PHE B C     1 
ATOM   4733  O O     . PHE B 1 89  ? 27.798  -8.483  70.692  1.00 88.20  ? 89  PHE B O     1 
ATOM   4734  C CB    . PHE B 1 89  ? 30.639  -6.948  69.938  1.00 78.78  ? 89  PHE B CB    1 
ATOM   4735  C CG    . PHE B 1 89  ? 31.951  -7.485  69.419  1.00 91.67  ? 89  PHE B CG    1 
ATOM   4736  C CD1   . PHE B 1 89  ? 32.084  -8.819  69.047  1.00 99.62  ? 89  PHE B CD1   1 
ATOM   4737  C CD2   . PHE B 1 89  ? 33.069  -6.670  69.339  1.00 95.24  ? 89  PHE B CD2   1 
ATOM   4738  C CE1   . PHE B 1 89  ? 33.293  -9.312  68.578  1.00 101.37 ? 89  PHE B CE1   1 
ATOM   4739  C CE2   . PHE B 1 89  ? 34.280  -7.168  68.880  1.00 93.82  ? 89  PHE B CE2   1 
ATOM   4740  C CZ    . PHE B 1 89  ? 34.393  -8.488  68.504  1.00 98.04  ? 89  PHE B CZ    1 
ATOM   4741  N N     . ALA B 1 90  ? 27.408  -6.349  70.123  1.00 80.35  ? 90  ALA B N     1 
ATOM   4742  C CA    . ALA B 1 90  ? 26.243  -6.261  70.998  1.00 78.12  ? 90  ALA B CA    1 
ATOM   4743  C C     . ALA B 1 90  ? 24.981  -6.822  70.344  1.00 67.02  ? 90  ALA B C     1 
ATOM   4744  O O     . ALA B 1 90  ? 23.896  -6.749  70.931  1.00 65.30  ? 90  ALA B O     1 
ATOM   4745  C CB    . ALA B 1 90  ? 26.019  -4.821  71.387  1.00 91.71  ? 90  ALA B CB    1 
ATOM   4746  N N     . TYR B 1 91  ? 25.114  -7.335  69.118  1.00 62.41  ? 91  TYR B N     1 
ATOM   4747  C CA    . TYR B 1 91  ? 23.974  -7.820  68.352  1.00 69.45  ? 91  TYR B CA    1 
ATOM   4748  C C     . TYR B 1 91  ? 24.173  -9.277  67.914  1.00 64.05  ? 91  TYR B C     1 
ATOM   4749  O O     . TYR B 1 91  ? 23.507  -9.750  66.999  1.00 54.07  ? 91  TYR B O     1 
ATOM   4750  C CB    . TYR B 1 91  ? 23.717  -6.900  67.152  1.00 66.48  ? 91  TYR B CB    1 
ATOM   4751  C CG    . TYR B 1 91  ? 23.569  -5.445  67.514  1.00 67.67  ? 91  TYR B CG    1 
ATOM   4752  C CD1   . TYR B 1 91  ? 24.658  -4.587  67.613  1.00 64.71  ? 91  TYR B CD1   1 
ATOM   4753  C CD2   . TYR B 1 91  ? 22.320  -4.942  67.823  1.00 66.55  ? 91  TYR B CD2   1 
ATOM   4754  C CE1   . TYR B 1 91  ? 24.493  -3.254  67.972  1.00 64.26  ? 91  TYR B CE1   1 
ATOM   4755  C CE2   . TYR B 1 91  ? 22.143  -3.620  68.187  1.00 62.88  ? 91  TYR B CE2   1 
ATOM   4756  C CZ    . TYR B 1 91  ? 23.226  -2.773  68.263  1.00 58.88  ? 91  TYR B CZ    1 
ATOM   4757  O OH    . TYR B 1 91  ? 22.948  -1.479  68.623  1.00 58.14  ? 91  TYR B OH    1 
ATOM   4758  N N     . GLY B 1 92  ? 25.061  -10.002 68.600  1.00 67.14  ? 92  GLY B N     1 
ATOM   4759  C CA    . GLY B 1 92  ? 25.243  -11.419 68.334  1.00 67.76  ? 92  GLY B CA    1 
ATOM   4760  C C     . GLY B 1 92  ? 26.490  -11.694 67.509  1.00 59.93  ? 92  GLY B C     1 
ATOM   4761  O O     . GLY B 1 92  ? 26.746  -12.848 67.178  1.00 53.12  ? 92  GLY B O     1 
ATOM   4762  N N     . GLY B 1 93  ? 27.227  -10.618 67.183  1.00 60.36  ? 93  GLY B N     1 
ATOM   4763  C CA    . GLY B 1 93  ? 28.502  -10.713 66.486  1.00 68.62  ? 93  GLY B CA    1 
ATOM   4764  C C     . GLY B 1 93  ? 28.370  -11.333 65.090  1.00 72.07  ? 93  GLY B C     1 
ATOM   4765  O O     . GLY B 1 93  ? 27.514  -10.922 64.296  1.00 74.16  ? 93  GLY B O     1 
ATOM   4766  N N     . ALA B 1 94  ? 29.192  -12.363 64.827  1.00 64.86  ? 94  ALA B N     1 
ATOM   4767  C CA    . ALA B 1 94  ? 29.310  -12.922 63.490  1.00 67.69  ? 94  ALA B CA    1 
ATOM   4768  C C     . ALA B 1 94  ? 28.350  -14.098 63.302  1.00 68.16  ? 94  ALA B C     1 
ATOM   4769  O O     . ALA B 1 94  ? 28.311  -14.685 62.227  1.00 60.18  ? 94  ALA B O     1 
ATOM   4770  C CB    . ALA B 1 94  ? 30.756  -13.308 63.215  1.00 65.28  ? 94  ALA B CB    1 
ATOM   4771  N N     . ALA B 1 95  ? 27.547  -14.430 64.325  1.00 79.93  ? 95  ALA B N     1 
ATOM   4772  C CA    . ALA B 1 95  ? 26.728  -15.638 64.277  1.00 78.61  ? 95  ALA B CA    1 
ATOM   4773  C C     . ALA B 1 95  ? 25.393  -15.380 63.577  1.00 66.68  ? 95  ALA B C     1 
ATOM   4774  O O     . ALA B 1 95  ? 24.887  -14.257 63.584  1.00 75.94  ? 95  ALA B O     1 
ATOM   4775  C CB    . ALA B 1 95  ? 26.504  -16.176 65.672  1.00 83.86  ? 95  ALA B CB    1 
ATOM   4776  N N     . PRO B 1 96  ? 24.770  -16.436 63.006  1.00 54.06  ? 96  PRO B N     1 
ATOM   4777  C CA    . PRO B 1 96  ? 23.449  -16.355 62.382  1.00 55.65  ? 96  PRO B CA    1 
ATOM   4778  C C     . PRO B 1 96  ? 22.241  -16.785 63.223  1.00 64.01  ? 96  PRO B C     1 
ATOM   4779  O O     . PRO B 1 96  ? 22.371  -17.659 64.068  1.00 79.09  ? 96  PRO B O     1 
ATOM   4780  C CB    . PRO B 1 96  ? 23.627  -17.445 61.328  1.00 59.21  ? 96  PRO B CB    1 
ATOM   4781  C CG    . PRO B 1 96  ? 24.311  -18.557 62.103  1.00 59.26  ? 96  PRO B CG    1 
ATOM   4782  C CD    . PRO B 1 96  ? 25.318  -17.799 62.943  1.00 56.91  ? 96  PRO B CD    1 
ATOM   4783  N N     . VAL B 1 97  ? 21.055  -16.235 62.913  1.00 66.39  ? 97  VAL B N     1 
ATOM   4784  C CA    . VAL B 1 97  ? 19.788  -16.593 63.541  1.00 68.49  ? 97  VAL B CA    1 
ATOM   4785  C C     . VAL B 1 97  ? 19.581  -18.106 63.501  1.00 73.48  ? 97  VAL B C     1 
ATOM   4786  O O     . VAL B 1 97  ? 19.273  -18.717 64.533  1.00 65.36  ? 97  VAL B O     1 
ATOM   4787  C CB    . VAL B 1 97  ? 18.598  -15.881 62.866  1.00 63.82  ? 97  VAL B CB    1 
ATOM   4788  C CG1   . VAL B 1 97  ? 17.282  -16.415 63.384  1.00 68.84  ? 97  VAL B CG1   1 
ATOM   4789  C CG2   . VAL B 1 97  ? 18.653  -14.364 63.036  1.00 69.27  ? 97  VAL B CG2   1 
ATOM   4790  N N     . MET B 1 98  ? 19.736  -18.686 62.301  1.00 72.77  ? 98  MET B N     1 
ATOM   4791  C CA    . MET B 1 98  ? 19.490  -20.106 62.093  1.00 77.32  ? 98  MET B CA    1 
ATOM   4792  C C     . MET B 1 98  ? 20.804  -20.878 62.180  1.00 79.31  ? 98  MET B C     1 
ATOM   4793  O O     . MET B 1 98  ? 21.761  -20.549 61.486  1.00 90.50  ? 98  MET B O     1 
ATOM   4794  C CB    . MET B 1 98  ? 18.826  -20.368 60.737  1.00 75.10  ? 98  MET B CB    1 
ATOM   4795  C CG    . MET B 1 98  ? 17.769  -21.460 60.782  1.00 72.41  ? 98  MET B CG    1 
ATOM   4796  S SD    . MET B 1 98  ? 17.146  -21.963 59.137  1.00 74.59  ? 98  MET B SD    1 
ATOM   4797  C CE    . MET B 1 98  ? 18.695  -22.309 58.300  1.00 63.84  ? 98  MET B CE    1 
ATOM   4798  N N     . SER B 1 99  ? 20.828  -21.889 63.063  1.00 76.06  ? 99  SER B N     1 
ATOM   4799  C CA    . SER B 1 99  ? 21.944  -22.810 63.203  1.00 66.94  ? 99  SER B CA    1 
ATOM   4800  C C     . SER B 1 99  ? 22.066  -23.642 61.940  1.00 63.22  ? 99  SER B C     1 
ATOM   4801  O O     . SER B 1 99  ? 21.059  -24.007 61.341  1.00 61.92  ? 99  SER B O     1 
ATOM   4802  C CB    . SER B 1 99  ? 21.763  -23.705 64.396  1.00 69.50  ? 99  SER B CB    1 
ATOM   4803  O OG    . SER B 1 99  ? 21.647  -22.930 65.576  1.00 72.28  ? 99  SER B OG    1 
ATOM   4804  N N     . GLY B 1 100 ? 23.305  -23.913 61.528  1.00 68.28  ? 100 GLY B N     1 
ATOM   4805  C CA    . GLY B 1 100 ? 23.543  -24.574 60.253  1.00 76.15  ? 100 GLY B CA    1 
ATOM   4806  C C     . GLY B 1 100 ? 23.879  -23.606 59.114  1.00 73.86  ? 100 GLY B C     1 
ATOM   4807  O O     . GLY B 1 100 ? 24.565  -23.990 58.171  1.00 70.56  ? 100 GLY B O     1 
ATOM   4808  N N     . THR B 1 101 ? 23.370  -22.366 59.189  1.00 74.24  ? 101 THR B N     1 
ATOM   4809  C CA    . THR B 1 101 ? 23.711  -21.317 58.239  1.00 64.38  ? 101 THR B CA    1 
ATOM   4810  C C     . THR B 1 101 ? 25.235  -21.217 58.142  1.00 62.11  ? 101 THR B C     1 
ATOM   4811  O O     . THR B 1 101 ? 25.913  -21.376 59.155  1.00 68.68  ? 101 THR B O     1 
ATOM   4812  C CB    . THR B 1 101 ? 23.027  -20.009 58.652  1.00 56.11  ? 101 THR B CB    1 
ATOM   4813  O OG1   . THR B 1 101 ? 21.658  -20.235 58.968  1.00 52.40  ? 101 THR B OG1   1 
ATOM   4814  C CG2   . THR B 1 101 ? 23.039  -18.970 57.565  1.00 66.47  ? 101 THR B CG2   1 
ATOM   4815  N N     . VAL B 1 102 ? 25.763  -21.022 56.916  1.00 63.09  ? 102 VAL B N     1 
ATOM   4816  C CA    . VAL B 1 102 ? 27.201  -20.885 56.663  1.00 55.91  ? 102 VAL B CA    1 
ATOM   4817  C C     . VAL B 1 102 ? 27.590  -19.408 56.676  1.00 54.11  ? 102 VAL B C     1 
ATOM   4818  O O     . VAL B 1 102 ? 26.991  -18.598 55.986  1.00 59.37  ? 102 VAL B O     1 
ATOM   4819  C CB    . VAL B 1 102 ? 27.610  -21.501 55.313  1.00 54.13  ? 102 VAL B CB    1 
ATOM   4820  C CG1   . VAL B 1 102 ? 29.104  -21.379 55.080  1.00 58.29  ? 102 VAL B CG1   1 
ATOM   4821  C CG2   . VAL B 1 102 ? 27.166  -22.944 55.179  1.00 63.56  ? 102 VAL B CG2   1 
ATOM   4822  N N     . VAL B 1 103 ? 28.604  -19.043 57.454  1.00 60.22  ? 103 VAL B N     1 
ATOM   4823  C CA    . VAL B 1 103 ? 28.989  -17.648 57.513  1.00 60.59  ? 103 VAL B CA    1 
ATOM   4824  C C     . VAL B 1 103 ? 29.742  -17.344 56.230  1.00 63.05  ? 103 VAL B C     1 
ATOM   4825  O O     . VAL B 1 103 ? 30.621  -18.096 55.833  1.00 69.54  ? 103 VAL B O     1 
ATOM   4826  C CB    . VAL B 1 103 ? 29.836  -17.329 58.756  1.00 68.34  ? 103 VAL B CB    1 
ATOM   4827  C CG1   . VAL B 1 103 ? 30.229  -15.860 58.805  1.00 73.86  ? 103 VAL B CG1   1 
ATOM   4828  C CG2   . VAL B 1 103 ? 29.111  -17.711 60.034  1.00 74.17  ? 103 VAL B CG2   1 
ATOM   4829  N N     . LEU B 1 104 ? 29.343  -16.265 55.565  1.00 65.78  ? 104 LEU B N     1 
ATOM   4830  C CA    . LEU B 1 104 ? 30.064  -15.755 54.416  1.00 56.89  ? 104 LEU B CA    1 
ATOM   4831  C C     . LEU B 1 104 ? 30.808  -14.519 54.901  1.00 54.42  ? 104 LEU B C     1 
ATOM   4832  O O     . LEU B 1 104 ? 30.214  -13.457 55.133  1.00 54.43  ? 104 LEU B O     1 
ATOM   4833  C CB    . LEU B 1 104 ? 29.073  -15.480 53.282  1.00 54.82  ? 104 LEU B CB    1 
ATOM   4834  C CG    . LEU B 1 104 ? 29.641  -14.841 52.017  1.00 54.30  ? 104 LEU B CG    1 
ATOM   4835  C CD1   . LEU B 1 104 ? 30.442  -15.837 51.208  1.00 55.15  ? 104 LEU B CD1   1 
ATOM   4836  C CD2   . LEU B 1 104 ? 28.515  -14.259 51.169  1.00 49.59  ? 104 LEU B CD2   1 
ATOM   4837  N N     . ASP B 1 105 ? 32.108  -14.736 55.119  1.00 50.28  ? 105 ASP B N     1 
ATOM   4838  C CA    . ASP B 1 105 ? 32.976  -13.797 55.795  1.00 52.37  ? 105 ASP B CA    1 
ATOM   4839  C C     . ASP B 1 105 ? 33.744  -13.012 54.737  1.00 52.32  ? 105 ASP B C     1 
ATOM   4840  O O     . ASP B 1 105 ? 34.623  -13.538 54.081  1.00 55.88  ? 105 ASP B O     1 
ATOM   4841  C CB    . ASP B 1 105 ? 33.917  -14.526 56.758  1.00 47.99  ? 105 ASP B CB    1 
ATOM   4842  C CG    . ASP B 1 105 ? 34.824  -13.617 57.585  1.00 53.93  ? 105 ASP B CG    1 
ATOM   4843  O OD1   . ASP B 1 105 ? 34.734  -12.386 57.425  1.00 58.33  ? 105 ASP B OD1   1 
ATOM   4844  O OD2   . ASP B 1 105 ? 35.630  -14.146 58.405  1.00 55.41  ? 105 ASP B OD2   1 
ATOM   4845  N N     . MET B 1 106 ? 33.468  -11.717 54.628  1.00 53.04  ? 106 MET B N     1 
ATOM   4846  C CA    . MET B 1 106 ? 34.041  -10.948 53.546  1.00 54.13  ? 106 MET B CA    1 
ATOM   4847  C C     . MET B 1 106 ? 35.182  -10.078 54.050  1.00 52.15  ? 106 MET B C     1 
ATOM   4848  O O     . MET B 1 106 ? 35.551  -9.113  53.393  1.00 52.41  ? 106 MET B O     1 
ATOM   4849  C CB    . MET B 1 106 ? 32.946  -10.135 52.852  1.00 56.05  ? 106 MET B CB    1 
ATOM   4850  C CG    . MET B 1 106 ? 32.353  -10.917 51.694  1.00 58.90  ? 106 MET B CG    1 
ATOM   4851  S SD    . MET B 1 106 ? 30.841  -10.262 51.030  1.00 60.36  ? 106 MET B SD    1 
ATOM   4852  C CE    . MET B 1 106 ? 29.894  -10.299 52.549  1.00 63.90  ? 106 MET B CE    1 
ATOM   4853  N N     . ASN B 1 107 ? 35.851  -10.505 55.123  1.00 53.56  ? 107 ASN B N     1 
ATOM   4854  C CA    . ASN B 1 107 ? 36.893  -9.663  55.684  1.00 55.34  ? 107 ASN B CA    1 
ATOM   4855  C C     . ASN B 1 107 ? 38.091  -9.597  54.725  1.00 45.52  ? 107 ASN B C     1 
ATOM   4856  O O     . ASN B 1 107 ? 38.672  -8.536  54.552  1.00 43.94  ? 107 ASN B O     1 
ATOM   4857  C CB    . ASN B 1 107 ? 37.246  -10.033 57.132  1.00 58.78  ? 107 ASN B CB    1 
ATOM   4858  C CG    . ASN B 1 107 ? 38.420  -10.977 57.194  1.00 74.10  ? 107 ASN B CG    1 
ATOM   4859  O OD1   . ASN B 1 107 ? 39.558  -10.532 57.338  1.00 74.55  ? 107 ASN B OD1   1 
ATOM   4860  N ND2   . ASN B 1 107 ? 38.158  -12.263 57.002  1.00 80.89  ? 107 ASN B ND2   1 
ATOM   4861  N N     . ARG B 1 108 ? 38.451  -10.681 54.043  1.00 49.71  ? 108 ARG B N     1 
ATOM   4862  C CA    . ARG B 1 108 ? 39.587  -10.630 53.116  1.00 56.01  ? 108 ARG B CA    1 
ATOM   4863  C C     . ARG B 1 108 ? 39.364  -9.619  51.980  1.00 52.34  ? 108 ARG B C     1 
ATOM   4864  O O     . ARG B 1 108 ? 40.318  -9.191  51.340  1.00 48.53  ? 108 ARG B O     1 
ATOM   4865  C CB    . ARG B 1 108 ? 39.853  -11.996 52.471  1.00 56.68  ? 108 ARG B CB    1 
ATOM   4866  C CG    . ARG B 1 108 ? 40.399  -13.048 53.427  1.00 53.41  ? 108 ARG B CG    1 
ATOM   4867  C CD    . ARG B 1 108 ? 40.468  -14.430 52.818  1.00 50.24  ? 108 ARG B CD    1 
ATOM   4868  N NE    . ARG B 1 108 ? 41.444  -14.493 51.725  1.00 53.63  ? 108 ARG B NE    1 
ATOM   4869  C CZ    . ARG B 1 108 ? 41.229  -15.080 50.549  1.00 49.49  ? 108 ARG B CZ    1 
ATOM   4870  N NH1   . ARG B 1 108 ? 40.134  -15.780 50.317  1.00 53.56  ? 108 ARG B NH1   1 
ATOM   4871  N NH2   . ARG B 1 108 ? 42.136  -15.010 49.609  1.00 48.94  ? 108 ARG B NH2   1 
ATOM   4872  N N     . MET B 1 109 ? 38.100  -9.278  51.705  1.00 51.41  ? 109 MET B N     1 
ATOM   4873  C CA    . MET B 1 109 ? 37.741  -8.289  50.703  1.00 51.61  ? 109 MET B CA    1 
ATOM   4874  C C     . MET B 1 109 ? 37.836  -6.916  51.356  1.00 46.42  ? 109 MET B C     1 
ATOM   4875  O O     . MET B 1 109 ? 36.820  -6.399  51.819  1.00 42.15  ? 109 MET B O     1 
ATOM   4876  C CB    . MET B 1 109 ? 36.312  -8.547  50.193  1.00 55.77  ? 109 MET B CB    1 
ATOM   4877  C CG    . MET B 1 109 ? 36.211  -9.800  49.295  1.00 58.69  ? 109 MET B CG    1 
ATOM   4878  S SD    . MET B 1 109 ? 34.511  -10.241 48.796  1.00 51.30  ? 109 MET B SD    1 
ATOM   4879  C CE    . MET B 1 109 ? 34.081  -8.678  48.040  1.00 44.00  ? 109 MET B CE    1 
ATOM   4880  N N     . ASN B 1 110 ? 39.069  -6.373  51.416  1.00 45.11  ? 110 ASN B N     1 
ATOM   4881  C CA    . ASN B 1 110 ? 39.375  -5.216  52.255  1.00 53.06  ? 110 ASN B CA    1 
ATOM   4882  C C     . ASN B 1 110 ? 40.020  -4.054  51.491  1.00 44.82  ? 110 ASN B C     1 
ATOM   4883  O O     . ASN B 1 110 ? 40.755  -3.278  52.086  1.00 39.52  ? 110 ASN B O     1 
ATOM   4884  C CB    . ASN B 1 110 ? 40.324  -5.582  53.403  1.00 53.52  ? 110 ASN B CB    1 
ATOM   4885  C CG    . ASN B 1 110 ? 41.662  -6.106  52.921  1.00 51.62  ? 110 ASN B CG    1 
ATOM   4886  O OD1   . ASN B 1 110 ? 41.889  -6.300  51.735  1.00 53.46  ? 110 ASN B OD1   1 
ATOM   4887  N ND2   . ASN B 1 110 ? 42.559  -6.383  53.842  1.00 64.45  ? 110 ASN B ND2   1 
ATOM   4888  N N     . ARG B 1 111 ? 39.749  -3.890  50.200  1.00 45.35  ? 111 ARG B N     1 
ATOM   4889  C CA    . ARG B 1 111 ? 40.434  -2.837  49.471  1.00 45.40  ? 111 ARG B CA    1 
ATOM   4890  C C     . ARG B 1 111 ? 39.709  -1.517  49.688  1.00 42.38  ? 111 ARG B C     1 
ATOM   4891  O O     . ARG B 1 111 ? 38.488  -1.467  49.816  1.00 46.70  ? 111 ARG B O     1 
ATOM   4892  C CB    . ARG B 1 111 ? 40.604  -3.239  48.011  1.00 54.26  ? 111 ARG B CB    1 
ATOM   4893  C CG    . ARG B 1 111 ? 41.771  -4.191  47.811  1.00 63.41  ? 111 ARG B CG    1 
ATOM   4894  C CD    . ARG B 1 111 ? 41.457  -5.339  46.884  1.00 74.24  ? 111 ARG B CD    1 
ATOM   4895  N NE    . ARG B 1 111 ? 41.485  -4.915  45.497  1.00 78.80  ? 111 ARG B NE    1 
ATOM   4896  C CZ    . ARG B 1 111 ? 40.446  -4.925  44.669  1.00 80.14  ? 111 ARG B CZ    1 
ATOM   4897  N NH1   . ARG B 1 111 ? 39.238  -5.242  45.110  1.00 76.30  ? 111 ARG B NH1   1 
ATOM   4898  N NH2   . ARG B 1 111 ? 40.625  -4.598  43.399  1.00 75.70  ? 111 ARG B NH2   1 
ATOM   4899  N N     . ILE B 1 112 ? 40.493  -0.461  49.869  1.00 42.34  ? 112 ILE B N     1 
ATOM   4900  C CA    . ILE B 1 112 ? 40.012  0.901   49.743  1.00 40.07  ? 112 ILE B CA    1 
ATOM   4901  C C     . ILE B 1 112 ? 40.115  1.254   48.267  1.00 39.56  ? 112 ILE B C     1 
ATOM   4902  O O     . ILE B 1 112 ? 41.208  1.487   47.769  1.00 43.69  ? 112 ILE B O     1 
ATOM   4903  C CB    . ILE B 1 112 ? 40.828  1.818   50.672  1.00 40.56  ? 112 ILE B CB    1 
ATOM   4904  C CG1   . ILE B 1 112 ? 40.513  1.499   52.132  1.00 43.07  ? 112 ILE B CG1   1 
ATOM   4905  C CG2   . ILE B 1 112 ? 40.591  3.289   50.390  1.00 46.15  ? 112 ILE B CG2   1 
ATOM   4906  C CD1   . ILE B 1 112 ? 41.407  2.186   53.136  1.00 48.51  ? 112 ILE B CD1   1 
ATOM   4907  N N     . LEU B 1 113 ? 38.977  1.235   47.554  1.00 42.24  ? 113 LEU B N     1 
ATOM   4908  C CA    . LEU B 1 113 ? 38.987  1.318   46.096  1.00 40.81  ? 113 LEU B CA    1 
ATOM   4909  C C     . LEU B 1 113 ? 39.287  2.745   45.674  1.00 39.60  ? 113 LEU B C     1 
ATOM   4910  O O     . LEU B 1 113 ? 40.007  2.951   44.708  1.00 48.51  ? 113 LEU B O     1 
ATOM   4911  C CB    . LEU B 1 113 ? 37.653  0.842   45.515  1.00 44.38  ? 113 LEU B CB    1 
ATOM   4912  C CG    . LEU B 1 113 ? 37.372  -0.648  45.695  1.00 49.51  ? 113 LEU B CG    1 
ATOM   4913  C CD1   . LEU B 1 113 ? 35.980  -1.011  45.216  1.00 50.06  ? 113 LEU B CD1   1 
ATOM   4914  C CD2   . LEU B 1 113 ? 38.406  -1.489  44.967  1.00 47.37  ? 113 LEU B CD2   1 
ATOM   4915  N N     . GLU B 1 114 ? 38.780  3.714   46.437  1.00 40.60  ? 114 GLU B N     1 
ATOM   4916  C CA    . GLU B 1 114 ? 39.060  5.122   46.193  1.00 39.90  ? 114 GLU B CA    1 
ATOM   4917  C C     . GLU B 1 114 ? 38.795  5.917   47.479  1.00 37.93  ? 114 GLU B C     1 
ATOM   4918  O O     . GLU B 1 114 ? 37.933  5.604   48.293  1.00 40.40  ? 114 GLU B O     1 
ATOM   4919  C CB    . GLU B 1 114 ? 38.236  5.588   44.989  1.00 44.37  ? 114 GLU B CB    1 
ATOM   4920  C CG    . GLU B 1 114 ? 38.551  6.989   44.501  1.00 50.29  ? 114 GLU B CG    1 
ATOM   4921  C CD    . GLU B 1 114 ? 37.630  7.505   43.393  1.00 57.10  ? 114 GLU B CD    1 
ATOM   4922  O OE1   . GLU B 1 114 ? 36.714  6.746   42.918  1.00 51.83  ? 114 GLU B OE1   1 
ATOM   4923  O OE2   . GLU B 1 114 ? 37.812  8.685   43.012  1.00 57.82  ? 114 GLU B OE2   1 
ATOM   4924  N N     . VAL B 1 115 ? 39.607  6.940   47.681  1.00 36.30  ? 115 VAL B N     1 
ATOM   4925  C CA    . VAL B 1 115 ? 39.249  8.016   48.568  1.00 39.85  ? 115 VAL B CA    1 
ATOM   4926  C C     . VAL B 1 115 ? 39.491  9.270   47.763  1.00 37.90  ? 115 VAL B C     1 
ATOM   4927  O O     . VAL B 1 115 ? 40.563  9.405   47.189  1.00 37.99  ? 115 VAL B O     1 
ATOM   4928  C CB    . VAL B 1 115 ? 40.085  8.041   49.857  1.00 40.73  ? 115 VAL B CB    1 
ATOM   4929  C CG1   . VAL B 1 115 ? 39.609  9.127   50.793  1.00 39.33  ? 115 VAL B CG1   1 
ATOM   4930  C CG2   . VAL B 1 115 ? 40.066  6.701   50.548  1.00 43.94  ? 115 VAL B CG2   1 
ATOM   4931  N N     . ASN B 1 116 ? 38.496  10.161  47.753  1.00 41.77  ? 116 ASN B N     1 
ATOM   4932  C CA    . ASN B 1 116 ? 38.542  11.363  46.936  1.00 41.94  ? 116 ASN B CA    1 
ATOM   4933  C C     . ASN B 1 116 ? 38.363  12.570  47.829  1.00 35.81  ? 116 ASN B C     1 
ATOM   4934  O O     . ASN B 1 116 ? 37.356  12.669  48.494  1.00 41.56  ? 116 ASN B O     1 
ATOM   4935  C CB    . ASN B 1 116 ? 37.457  11.384  45.859  1.00 40.14  ? 116 ASN B CB    1 
ATOM   4936  C CG    . ASN B 1 116 ? 37.574  12.573  44.936  1.00 38.05  ? 116 ASN B CG    1 
ATOM   4937  O OD1   . ASN B 1 116 ? 37.402  13.727  45.332  1.00 39.60  ? 116 ASN B OD1   1 
ATOM   4938  N ND2   . ASN B 1 116 ? 37.853  12.286  43.683  1.00 39.72  ? 116 ASN B ND2   1 
ATOM   4939  N N     . GLU B 1 117 ? 39.317  13.488  47.778  1.00 43.20  ? 117 GLU B N     1 
ATOM   4940  C CA    . GLU B 1 117 ? 39.364  14.641  48.659  1.00 46.39  ? 117 GLU B CA    1 
ATOM   4941  C C     . GLU B 1 117 ? 38.450  15.752  48.136  1.00 44.88  ? 117 GLU B C     1 
ATOM   4942  O O     . GLU B 1 117 ? 37.641  16.306  48.883  1.00 50.35  ? 117 GLU B O     1 
ATOM   4943  C CB    . GLU B 1 117 ? 40.818  15.097  48.765  1.00 43.75  ? 117 GLU B CB    1 
ATOM   4944  C CG    . GLU B 1 117 ? 41.096  16.070  49.906  1.00 51.16  ? 117 GLU B CG    1 
ATOM   4945  C CD    . GLU B 1 117 ? 42.545  16.558  49.961  1.00 53.54  ? 117 GLU B CD    1 
ATOM   4946  O OE1   . GLU B 1 117 ? 43.321  16.313  48.974  1.00 44.64  ? 117 GLU B OE1   1 
ATOM   4947  O OE2   . GLU B 1 117 ? 42.907  17.149  50.986  1.00 48.41  ? 117 GLU B OE2   1 
ATOM   4948  N N     . GLU B 1 118 ? 38.575  16.102  46.854  1.00 43.27  ? 118 GLU B N     1 
ATOM   4949  C CA    . GLU B 1 118 ? 37.863  17.263  46.329  1.00 41.08  ? 118 GLU B CA    1 
ATOM   4950  C C     . GLU B 1 118 ? 36.351  17.037  46.506  1.00 41.13  ? 118 GLU B C     1 
ATOM   4951  O O     . GLU B 1 118 ? 35.619  18.005  46.703  1.00 31.08  ? 118 GLU B O     1 
ATOM   4952  C CB    . GLU B 1 118 ? 38.255  17.544  44.866  1.00 42.67  ? 118 GLU B CB    1 
ATOM   4953  C CG    . GLU B 1 118 ? 38.108  16.342  43.928  1.00 52.22  ? 118 GLU B CG    1 
ATOM   4954  C CD    . GLU B 1 118 ? 38.409  16.545  42.440  1.00 60.69  ? 118 GLU B CD    1 
ATOM   4955  O OE1   . GLU B 1 118 ? 38.569  17.706  42.015  1.00 50.81  ? 118 GLU B OE1   1 
ATOM   4956  O OE2   . GLU B 1 118 ? 38.443  15.531  41.688  1.00 56.12  ? 118 GLU B OE2   1 
ATOM   4957  N N     . PHE B 1 119 ? 35.904  15.763  46.423  1.00 38.05  ? 119 PHE B N     1 
ATOM   4958  C CA    . PHE B 1 119 ? 34.497  15.420  46.398  1.00 40.64  ? 119 PHE B CA    1 
ATOM   4959  C C     . PHE B 1 119 ? 34.083  14.692  47.665  1.00 47.79  ? 119 PHE B C     1 
ATOM   4960  O O     . PHE B 1 119 ? 32.965  14.172  47.723  1.00 46.57  ? 119 PHE B O     1 
ATOM   4961  C CB    . PHE B 1 119 ? 34.130  14.517  45.222  1.00 35.97  ? 119 PHE B CB    1 
ATOM   4962  C CG    . PHE B 1 119 ? 34.417  15.089  43.874  1.00 36.45  ? 119 PHE B CG    1 
ATOM   4963  C CD1   . PHE B 1 119 ? 34.119  16.397  43.579  1.00 45.61  ? 119 PHE B CD1   1 
ATOM   4964  C CD2   . PHE B 1 119 ? 35.007  14.319  42.901  1.00 37.83  ? 119 PHE B CD2   1 
ATOM   4965  C CE1   . PHE B 1 119 ? 34.426  16.924  42.337  1.00 44.60  ? 119 PHE B CE1   1 
ATOM   4966  C CE2   . PHE B 1 119 ? 35.299  14.844  41.658  1.00 38.53  ? 119 PHE B CE2   1 
ATOM   4967  C CZ    . PHE B 1 119 ? 35.025  16.150  41.385  1.00 39.83  ? 119 PHE B CZ    1 
ATOM   4968  N N     . GLY B 1 120 ? 35.001  14.652  48.638  1.00 44.34  ? 120 GLY B N     1 
ATOM   4969  C CA    . GLY B 1 120 ? 34.717  14.137  49.966  1.00 40.48  ? 120 GLY B CA    1 
ATOM   4970  C C     . GLY B 1 120 ? 34.010  12.784  49.940  1.00 36.83  ? 120 GLY B C     1 
ATOM   4971  O O     . GLY B 1 120 ? 32.830  12.685  50.304  1.00 37.38  ? 120 GLY B O     1 
ATOM   4972  N N     . TYR B 1 121 ? 34.713  11.730  49.522  1.00 31.49  ? 121 TYR B N     1 
ATOM   4973  C CA    . TYR B 1 121 ? 34.054  10.432  49.520  1.00 34.03  ? 121 TYR B CA    1 
ATOM   4974  C C     . TYR B 1 121 ? 35.054  9.308   49.492  1.00 31.86  ? 121 TYR B C     1 
ATOM   4975  O O     . TYR B 1 121 ? 36.232  9.571   49.319  1.00 33.31  ? 121 TYR B O     1 
ATOM   4976  C CB    . TYR B 1 121 ? 33.105  10.293  48.333  1.00 35.72  ? 121 TYR B CB    1 
ATOM   4977  C CG    . TYR B 1 121 ? 33.693  10.066  46.965  1.00 36.16  ? 121 TYR B CG    1 
ATOM   4978  C CD1   . TYR B 1 121 ? 34.133  8.818   46.580  1.00 34.87  ? 121 TYR B CD1   1 
ATOM   4979  C CD2   . TYR B 1 121 ? 33.645  11.054  45.989  1.00 36.15  ? 121 TYR B CD2   1 
ATOM   4980  C CE1   . TYR B 1 121 ? 34.534  8.560   45.278  1.00 34.32  ? 121 TYR B CE1   1 
ATOM   4981  C CE2   . TYR B 1 121 ? 34.106  10.830  44.697  1.00 33.19  ? 121 TYR B CE2   1 
ATOM   4982  C CZ    . TYR B 1 121 ? 34.524  9.563   44.334  1.00 34.80  ? 121 TYR B CZ    1 
ATOM   4983  O OH    . TYR B 1 121 ? 34.939  9.253   43.067  1.00 36.53  ? 121 TYR B OH    1 
ATOM   4984  N N     . ALA B 1 122 ? 34.555  8.082   49.719  1.00 37.85  ? 122 ALA B N     1 
ATOM   4985  C CA    . ALA B 1 122 ? 35.386  6.889   49.657  1.00 36.63  ? 122 ALA B CA    1 
ATOM   4986  C C     . ALA B 1 122 ? 34.575  5.724   49.122  1.00 35.73  ? 122 ALA B C     1 
ATOM   4987  O O     . ALA B 1 122 ? 33.383  5.631   49.378  1.00 35.64  ? 122 ALA B O     1 
ATOM   4988  C CB    . ALA B 1 122 ? 35.928  6.555   51.015  1.00 39.40  ? 122 ALA B CB    1 
ATOM   4989  N N     . LEU B 1 123 ? 35.251  4.837   48.396  1.00 37.40  ? 123 LEU B N     1 
ATOM   4990  C CA    . LEU B 1 123 ? 34.631  3.610   47.929  1.00 39.91  ? 123 LEU B CA    1 
ATOM   4991  C C     . LEU B 1 123 ? 35.372  2.459   48.583  1.00 38.52  ? 123 LEU B C     1 
ATOM   4992  O O     . LEU B 1 123 ? 36.594  2.408   48.487  1.00 45.09  ? 123 LEU B O     1 
ATOM   4993  C CB    . LEU B 1 123 ? 34.744  3.538   46.399  1.00 38.71  ? 123 LEU B CB    1 
ATOM   4994  C CG    . LEU B 1 123 ? 34.080  2.341   45.731  1.00 32.32  ? 123 LEU B CG    1 
ATOM   4995  C CD1   . LEU B 1 123 ? 32.587  2.343   45.995  1.00 34.00  ? 123 LEU B CD1   1 
ATOM   4996  C CD2   . LEU B 1 123 ? 34.337  2.339   44.230  1.00 28.79  ? 123 LEU B CD2   1 
ATOM   4997  N N     . VAL B 1 124 ? 34.633  1.589   49.278  1.00 32.72  ? 124 VAL B N     1 
ATOM   4998  C CA    . VAL B 1 124 ? 35.252  0.600   50.130  1.00 32.00  ? 124 VAL B CA    1 
ATOM   4999  C C     . VAL B 1 124 ? 34.569  -0.754  49.931  1.00 34.57  ? 124 VAL B C     1 
ATOM   5000  O O     . VAL B 1 124 ? 33.400  -0.811  49.549  1.00 36.46  ? 124 VAL B O     1 
ATOM   5001  C CB    . VAL B 1 124 ? 35.249  1.050   51.602  1.00 31.31  ? 124 VAL B CB    1 
ATOM   5002  C CG1   . VAL B 1 124 ? 36.225  2.188   51.834  1.00 31.76  ? 124 VAL B CG1   1 
ATOM   5003  C CG2   . VAL B 1 124 ? 33.851  1.427   52.084  1.00 36.74  ? 124 VAL B CG2   1 
ATOM   5004  N N     . GLU B 1 125 ? 35.367  -1.818  50.115  1.00 38.00  ? 125 GLU B N     1 
ATOM   5005  C CA    . GLU B 1 125 ? 34.910  -3.195  50.186  1.00 44.23  ? 125 GLU B CA    1 
ATOM   5006  C C     . GLU B 1 125 ? 34.499  -3.464  51.629  1.00 46.69  ? 125 GLU B C     1 
ATOM   5007  O O     . GLU B 1 125 ? 34.861  -2.691  52.522  1.00 49.67  ? 125 GLU B O     1 
ATOM   5008  C CB    . GLU B 1 125 ? 36.018  -4.162  49.761  1.00 45.54  ? 125 GLU B CB    1 
ATOM   5009  C CG    . GLU B 1 125 ? 36.566  -3.893  48.368  1.00 48.71  ? 125 GLU B CG    1 
ATOM   5010  C CD    . GLU B 1 125 ? 37.237  -5.080  47.696  1.00 48.04  ? 125 GLU B CD    1 
ATOM   5011  O OE1   . GLU B 1 125 ? 38.288  -5.529  48.175  1.00 55.85  ? 125 GLU B OE1   1 
ATOM   5012  O OE2   . GLU B 1 125 ? 36.708  -5.543  46.685  1.00 54.92  ? 125 GLU B OE2   1 
ATOM   5013  N N     . PRO B 1 126 ? 33.696  -4.524  51.886  1.00 43.48  ? 126 PRO B N     1 
ATOM   5014  C CA    . PRO B 1 126 ? 33.187  -4.816  53.232  1.00 43.09  ? 126 PRO B CA    1 
ATOM   5015  C C     . PRO B 1 126 ? 34.232  -4.988  54.341  1.00 41.87  ? 126 PRO B C     1 
ATOM   5016  O O     . PRO B 1 126 ? 33.963  -4.698  55.504  1.00 41.25  ? 126 PRO B O     1 
ATOM   5017  C CB    . PRO B 1 126 ? 32.414  -6.135  53.048  1.00 41.84  ? 126 PRO B CB    1 
ATOM   5018  C CG    . PRO B 1 126 ? 31.989  -6.084  51.583  1.00 46.73  ? 126 PRO B CG    1 
ATOM   5019  C CD    . PRO B 1 126 ? 33.167  -5.450  50.878  1.00 42.85  ? 126 PRO B CD    1 
ATOM   5020  N N     . GLY B 1 127 ? 35.418  -5.487  54.000  1.00 43.87  ? 127 GLY B N     1 
ATOM   5021  C CA    . GLY B 1 127 ? 36.418  -5.773  55.021  1.00 50.02  ? 127 GLY B CA    1 
ATOM   5022  C C     . GLY B 1 127 ? 37.133  -4.539  55.572  1.00 48.00  ? 127 GLY B C     1 
ATOM   5023  O O     . GLY B 1 127 ? 37.911  -4.627  56.509  1.00 56.54  ? 127 GLY B O     1 
ATOM   5024  N N     . VAL B 1 128 ? 36.952  -3.389  54.940  1.00 49.98  ? 128 VAL B N     1 
ATOM   5025  C CA    . VAL B 1 128 ? 37.670  -2.207  55.363  1.00 45.16  ? 128 VAL B CA    1 
ATOM   5026  C C     . VAL B 1 128 ? 37.136  -1.783  56.729  1.00 51.78  ? 128 VAL B C     1 
ATOM   5027  O O     . VAL B 1 128 ? 35.931  -1.556  56.869  1.00 53.28  ? 128 VAL B O     1 
ATOM   5028  C CB    . VAL B 1 128 ? 37.519  -1.079  54.334  1.00 43.80  ? 128 VAL B CB    1 
ATOM   5029  C CG1   . VAL B 1 128 ? 38.238  0.167   54.780  1.00 40.99  ? 128 VAL B CG1   1 
ATOM   5030  C CG2   . VAL B 1 128 ? 37.969  -1.483  52.941  1.00 45.38  ? 128 VAL B CG2   1 
ATOM   5031  N N     . SER B 1 129 ? 38.048  -1.709  57.714  1.00 53.66  ? 129 SER B N     1 
ATOM   5032  C CA    . SER B 1 129 ? 37.724  -1.309  59.074  1.00 54.01  ? 129 SER B CA    1 
ATOM   5033  C C     . SER B 1 129 ? 37.796  0.210   59.175  1.00 50.70  ? 129 SER B C     1 
ATOM   5034  O O     . SER B 1 129 ? 38.416  0.853   58.338  1.00 43.22  ? 129 SER B O     1 
ATOM   5035  C CB    . SER B 1 129 ? 38.666  -1.937  60.076  1.00 56.90  ? 129 SER B CB    1 
ATOM   5036  O OG    . SER B 1 129 ? 39.991  -1.383  59.985  1.00 53.73  ? 129 SER B OG    1 
ATOM   5037  N N     . TYR B 1 130 ? 37.209  0.759   60.242  1.00 47.98  ? 130 TYR B N     1 
ATOM   5038  C CA    . TYR B 1 130 ? 37.325  2.177   60.503  1.00 45.85  ? 130 TYR B CA    1 
ATOM   5039  C C     . TYR B 1 130 ? 38.793  2.525   60.617  1.00 49.09  ? 130 TYR B C     1 
ATOM   5040  O O     . TYR B 1 130 ? 39.220  3.563   60.115  1.00 65.77  ? 130 TYR B O     1 
ATOM   5041  C CB    . TYR B 1 130 ? 36.506  2.567   61.725  1.00 42.49  ? 130 TYR B CB    1 
ATOM   5042  C CG    . TYR B 1 130 ? 35.021  2.571   61.454  1.00 40.90  ? 130 TYR B CG    1 
ATOM   5043  C CD1   . TYR B 1 130 ? 34.441  3.585   60.713  1.00 42.00  ? 130 TYR B CD1   1 
ATOM   5044  C CD2   . TYR B 1 130 ? 34.205  1.534   61.868  1.00 40.19  ? 130 TYR B CD2   1 
ATOM   5045  C CE1   . TYR B 1 130 ? 33.079  3.617   60.465  1.00 41.70  ? 130 TYR B CE1   1 
ATOM   5046  C CE2   . TYR B 1 130 ? 32.846  1.527   61.597  1.00 43.96  ? 130 TYR B CE2   1 
ATOM   5047  C CZ    . TYR B 1 130 ? 32.280  2.578   60.894  1.00 42.93  ? 130 TYR B CZ    1 
ATOM   5048  O OH    . TYR B 1 130 ? 30.949  2.612   60.610  1.00 45.22  ? 130 TYR B OH    1 
ATOM   5049  N N     . PHE B 1 131 ? 39.564  1.610   61.198  1.00 47.46  ? 131 PHE B N     1 
ATOM   5050  C CA    . PHE B 1 131 ? 40.963  1.891   61.482  1.00 49.01  ? 131 PHE B CA    1 
ATOM   5051  C C     . PHE B 1 131 ? 41.773  1.949   60.185  1.00 45.58  ? 131 PHE B C     1 
ATOM   5052  O O     . PHE B 1 131 ? 42.572  2.868   59.987  1.00 46.83  ? 131 PHE B O     1 
ATOM   5053  C CB    . PHE B 1 131 ? 41.523  0.858   62.459  1.00 52.96  ? 131 PHE B CB    1 
ATOM   5054  C CG    . PHE B 1 131 ? 41.281  1.150   63.920  1.00 58.42  ? 131 PHE B CG    1 
ATOM   5055  C CD1   . PHE B 1 131 ? 41.973  2.178   64.557  1.00 62.60  ? 131 PHE B CD1   1 
ATOM   5056  C CD2   . PHE B 1 131 ? 40.393  0.384   64.658  1.00 49.54  ? 131 PHE B CD2   1 
ATOM   5057  C CE1   . PHE B 1 131 ? 41.746  2.468   65.890  1.00 56.26  ? 131 PHE B CE1   1 
ATOM   5058  C CE2   . PHE B 1 131 ? 40.204  0.643   66.000  1.00 49.88  ? 131 PHE B CE2   1 
ATOM   5059  C CZ    . PHE B 1 131 ? 40.858  1.697   66.606  1.00 57.13  ? 131 PHE B CZ    1 
ATOM   5060  N N     . GLU B 1 132 ? 41.559  0.974   59.298  1.00 43.62  ? 132 GLU B N     1 
ATOM   5061  C CA    . GLU B 1 132 ? 42.190  0.997   57.978  1.00 45.79  ? 132 GLU B CA    1 
ATOM   5062  C C     . GLU B 1 132 ? 41.883  2.284   57.200  1.00 43.87  ? 132 GLU B C     1 
ATOM   5063  O O     . GLU B 1 132 ? 42.787  2.830   56.585  1.00 51.62  ? 132 GLU B O     1 
ATOM   5064  C CB    . GLU B 1 132 ? 41.796  -0.252  57.195  1.00 51.57  ? 132 GLU B CB    1 
ATOM   5065  C CG    . GLU B 1 132 ? 42.492  -1.504  57.718  1.00 54.68  ? 132 GLU B CG    1 
ATOM   5066  C CD    . GLU B 1 132 ? 41.774  -2.821  57.489  1.00 54.42  ? 132 GLU B CD    1 
ATOM   5067  O OE1   . GLU B 1 132 ? 40.631  -2.815  57.013  1.00 56.07  ? 132 GLU B OE1   1 
ATOM   5068  O OE2   . GLU B 1 132 ? 42.357  -3.851  57.830  1.00 66.67  ? 132 GLU B OE2   1 
ATOM   5069  N N     . LEU B 1 133 ? 40.638  2.787   57.248  1.00 45.17  ? 133 LEU B N     1 
ATOM   5070  C CA    . LEU B 1 133 ? 40.205  3.919   56.437  1.00 46.25  ? 133 LEU B CA    1 
ATOM   5071  C C     . LEU B 1 133 ? 40.770  5.214   57.021  1.00 42.13  ? 133 LEU B C     1 
ATOM   5072  O O     . LEU B 1 133 ? 41.270  6.056   56.284  1.00 44.94  ? 133 LEU B O     1 
ATOM   5073  C CB    . LEU B 1 133 ? 38.658  3.943   56.332  1.00 41.25  ? 133 LEU B CB    1 
ATOM   5074  C CG    . LEU B 1 133 ? 38.042  5.056   55.467  1.00 38.40  ? 133 LEU B CG    1 
ATOM   5075  C CD1   . LEU B 1 133 ? 38.509  5.016   54.001  1.00 38.74  ? 133 LEU B CD1   1 
ATOM   5076  C CD2   . LEU B 1 133 ? 36.519  5.009   55.493  1.00 42.40  ? 133 LEU B CD2   1 
ATOM   5077  N N     . TYR B 1 134 ? 40.690  5.373   58.347  1.00 42.10  ? 134 TYR B N     1 
ATOM   5078  C CA    . TYR B 1 134 ? 41.286  6.521   59.013  1.00 38.25  ? 134 TYR B CA    1 
ATOM   5079  C C     . TYR B 1 134 ? 42.803  6.598   58.788  1.00 42.74  ? 134 TYR B C     1 
ATOM   5080  O O     . TYR B 1 134 ? 43.346  7.704   58.645  1.00 40.47  ? 134 TYR B O     1 
ATOM   5081  C CB    . TYR B 1 134 ? 41.008  6.481   60.515  1.00 36.61  ? 134 TYR B CB    1 
ATOM   5082  C CG    . TYR B 1 134 ? 41.662  7.621   61.244  1.00 36.40  ? 134 TYR B CG    1 
ATOM   5083  C CD1   . TYR B 1 134 ? 41.137  8.893   61.156  1.00 36.42  ? 134 TYR B CD1   1 
ATOM   5084  C CD2   . TYR B 1 134 ? 42.846  7.452   61.962  1.00 40.76  ? 134 TYR B CD2   1 
ATOM   5085  C CE1   . TYR B 1 134 ? 41.733  9.971   61.787  1.00 41.22  ? 134 TYR B CE1   1 
ATOM   5086  C CE2   . TYR B 1 134 ? 43.429  8.510   62.652  1.00 41.66  ? 134 TYR B CE2   1 
ATOM   5087  C CZ    . TYR B 1 134 ? 42.876  9.777   62.544  1.00 45.26  ? 134 TYR B CZ    1 
ATOM   5088  O OH    . TYR B 1 134 ? 43.409  10.873  63.145  1.00 45.52  ? 134 TYR B OH    1 
ATOM   5089  N N     . ASP B 1 135 ? 43.481  5.435   58.775  1.00 41.16  ? 135 ASP B N     1 
ATOM   5090  C CA    . ASP B 1 135 ? 44.933  5.367   58.581  1.00 49.12  ? 135 ASP B CA    1 
ATOM   5091  C C     . ASP B 1 135 ? 45.305  5.670   57.126  1.00 48.56  ? 135 ASP B C     1 
ATOM   5092  O O     . ASP B 1 135 ? 46.266  6.401   56.891  1.00 49.57  ? 135 ASP B O     1 
ATOM   5093  C CB    . ASP B 1 135 ? 45.522  4.045   59.107  1.00 45.19  ? 135 ASP B CB    1 
ATOM   5094  C CG    . ASP B 1 135 ? 45.479  3.954   60.642  1.00 47.22  ? 135 ASP B CG    1 
ATOM   5095  O OD1   . ASP B 1 135 ? 45.398  5.020   61.305  1.00 38.91  ? 135 ASP B OD1   1 
ATOM   5096  O OD2   . ASP B 1 135 ? 45.423  2.828   61.174  1.00 41.38  ? 135 ASP B OD2   1 
ATOM   5097  N N     . TYR B 1 136 ? 44.509  5.167   56.168  1.00 47.49  ? 136 TYR B N     1 
ATOM   5098  C CA    . TYR B 1 136 ? 44.705  5.430   54.750  1.00 44.11  ? 136 TYR B CA    1 
ATOM   5099  C C     . TYR B 1 136 ? 44.677  6.931   54.519  1.00 45.26  ? 136 TYR B C     1 
ATOM   5100  O O     . TYR B 1 136 ? 45.577  7.508   53.904  1.00 41.50  ? 136 TYR B O     1 
ATOM   5101  C CB    . TYR B 1 136 ? 43.602  4.759   53.930  1.00 49.76  ? 136 TYR B CB    1 
ATOM   5102  C CG    . TYR B 1 136 ? 43.794  4.883   52.445  1.00 58.98  ? 136 TYR B CG    1 
ATOM   5103  C CD1   . TYR B 1 136 ? 43.490  6.053   51.777  1.00 56.49  ? 136 TYR B CD1   1 
ATOM   5104  C CD2   . TYR B 1 136 ? 44.338  3.841   51.714  1.00 67.41  ? 136 TYR B CD2   1 
ATOM   5105  C CE1   . TYR B 1 136 ? 43.710  6.179   50.415  1.00 58.86  ? 136 TYR B CE1   1 
ATOM   5106  C CE2   . TYR B 1 136 ? 44.559  3.952   50.352  1.00 64.80  ? 136 TYR B CE2   1 
ATOM   5107  C CZ    . TYR B 1 136 ? 44.264  5.134   49.704  1.00 59.22  ? 136 TYR B CZ    1 
ATOM   5108  O OH    . TYR B 1 136 ? 44.471  5.220   48.349  1.00 69.86  ? 136 TYR B OH    1 
ATOM   5109  N N     . ILE B 1 137 ? 43.645  7.550   55.091  1.00 45.02  ? 137 ILE B N     1 
ATOM   5110  C CA    . ILE B 1 137 ? 43.374  8.957   54.894  1.00 43.81  ? 137 ILE B CA    1 
ATOM   5111  C C     . ILE B 1 137 ? 44.571  9.777   55.393  1.00 50.16  ? 137 ILE B C     1 
ATOM   5112  O O     . ILE B 1 137 ? 44.963  10.786  54.765  1.00 43.76  ? 137 ILE B O     1 
ATOM   5113  C CB    . ILE B 1 137 ? 42.027  9.302   55.566  1.00 39.04  ? 137 ILE B CB    1 
ATOM   5114  C CG1   . ILE B 1 137 ? 40.856  8.803   54.708  1.00 42.15  ? 137 ILE B CG1   1 
ATOM   5115  C CG2   . ILE B 1 137 ? 41.925  10.801  55.866  1.00 38.51  ? 137 ILE B CG2   1 
ATOM   5116  C CD1   . ILE B 1 137 ? 39.478  8.823   55.369  1.00 39.78  ? 137 ILE B CD1   1 
ATOM   5117  N N     . GLN B 1 138 ? 45.125  9.337   56.540  1.00 50.75  ? 138 GLN B N     1 
ATOM   5118  C CA    . GLN B 1 138 ? 46.211  10.051  57.202  1.00 52.07  ? 138 GLN B CA    1 
ATOM   5119  C C     . GLN B 1 138 ? 47.507  9.849   56.411  1.00 46.29  ? 138 GLN B C     1 
ATOM   5120  O O     . GLN B 1 138 ? 48.104  10.825  55.980  1.00 49.71  ? 138 GLN B O     1 
ATOM   5121  C CB    . GLN B 1 138 ? 46.327  9.663   58.681  1.00 46.77  ? 138 GLN B CB    1 
ATOM   5122  C CG    . GLN B 1 138 ? 45.158  10.143  59.548  1.00 45.52  ? 138 GLN B CG    1 
ATOM   5123  C CD    . GLN B 1 138 ? 44.721  11.568  59.282  1.00 49.47  ? 138 GLN B CD    1 
ATOM   5124  O OE1   . GLN B 1 138 ? 45.536  12.468  59.127  1.00 53.92  ? 138 GLN B OE1   1 
ATOM   5125  N NE2   . GLN B 1 138 ? 43.420  11.813  59.256  1.00 50.05  ? 138 GLN B NE2   1 
ATOM   5126  N N     . GLU B 1 139 ? 47.902  8.604   56.145  1.00 47.61  ? 139 GLU B N     1 
ATOM   5127  C CA    . GLU B 1 139 ? 49.040  8.331   55.269  1.00 57.04  ? 139 GLU B CA    1 
ATOM   5128  C C     . GLU B 1 139 ? 49.072  9.297   54.077  1.00 60.42  ? 139 GLU B C     1 
ATOM   5129  O O     . GLU B 1 139 ? 50.131  9.823   53.749  1.00 64.34  ? 139 GLU B O     1 
ATOM   5130  C CB    . GLU B 1 139 ? 49.020  6.873   54.793  1.00 58.04  ? 139 GLU B CB    1 
ATOM   5131  C CG    . GLU B 1 139 ? 49.927  6.583   53.595  1.00 65.31  ? 139 GLU B CG    1 
ATOM   5132  C CD    . GLU B 1 139 ? 50.283  5.115   53.352  1.00 61.22  ? 139 GLU B CD    1 
ATOM   5133  O OE1   . GLU B 1 139 ? 51.036  4.819   52.400  1.00 66.43  ? 139 GLU B OE1   1 
ATOM   5134  O OE2   . GLU B 1 139 ? 49.844  4.272   54.123  1.00 55.43  ? 139 GLU B OE2   1 
ATOM   5135  N N     . LYS B 1 140 ? 47.911  9.553   53.454  1.00 56.08  ? 140 LYS B N     1 
ATOM   5136  C CA    . LYS B 1 140 ? 47.850  10.326  52.221  1.00 58.38  ? 140 LYS B CA    1 
ATOM   5137  C C     . LYS B 1 140 ? 47.693  11.826  52.517  1.00 51.81  ? 140 LYS B C     1 
ATOM   5138  O O     . LYS B 1 140 ? 47.743  12.637  51.593  1.00 49.49  ? 140 LYS B O     1 
ATOM   5139  C CB    . LYS B 1 140 ? 46.735  9.773   51.309  1.00 70.05  ? 140 LYS B CB    1 
ATOM   5140  C CG    . LYS B 1 140 ? 46.943  8.357   50.749  1.00 74.94  ? 140 LYS B CG    1 
ATOM   5141  C CD    . LYS B 1 140 ? 47.895  8.269   49.540  1.00 80.09  ? 140 LYS B CD    1 
ATOM   5142  C CE    . LYS B 1 140 ? 48.565  6.921   49.334  1.00 82.18  ? 140 LYS B CE    1 
ATOM   5143  N NZ    . LYS B 1 140 ? 47.732  6.003   48.521  1.00 81.71  ? 140 LYS B NZ    1 
ATOM   5144  N N     . GLY B 1 141 ? 47.497  12.214  53.788  1.00 47.33  ? 141 GLY B N     1 
ATOM   5145  C CA    . GLY B 1 141 ? 47.354  13.621  54.145  1.00 48.09  ? 141 GLY B CA    1 
ATOM   5146  C C     . GLY B 1 141 ? 46.091  14.270  53.555  1.00 46.56  ? 141 GLY B C     1 
ATOM   5147  O O     . GLY B 1 141 ? 46.050  15.482  53.355  1.00 35.20  ? 141 GLY B O     1 
ATOM   5148  N N     . LEU B 1 142 ? 45.045  13.460  53.321  1.00 47.54  ? 142 LEU B N     1 
ATOM   5149  C CA    . LEU B 1 142 ? 43.761  13.963  52.845  1.00 46.33  ? 142 LEU B CA    1 
ATOM   5150  C C     . LEU B 1 142 ? 43.010  14.669  53.980  1.00 42.52  ? 142 LEU B C     1 
ATOM   5151  O O     . LEU B 1 142 ? 42.870  14.143  55.064  1.00 44.34  ? 142 LEU B O     1 
ATOM   5152  C CB    . LEU B 1 142 ? 42.977  12.786  52.259  1.00 45.63  ? 142 LEU B CB    1 
ATOM   5153  C CG    . LEU B 1 142 ? 43.690  12.016  51.130  1.00 50.75  ? 142 LEU B CG    1 
ATOM   5154  C CD1   . LEU B 1 142 ? 42.771  10.994  50.478  1.00 43.22  ? 142 LEU B CD1   1 
ATOM   5155  C CD2   . LEU B 1 142 ? 44.248  12.953  50.058  1.00 51.35  ? 142 LEU B CD2   1 
ATOM   5156  N N     . LYS B 1 143 ? 42.548  15.885  53.718  1.00 43.72  ? 143 LYS B N     1 
ATOM   5157  C CA    . LYS B 1 143 ? 41.802  16.703  54.653  1.00 45.50  ? 143 LYS B CA    1 
ATOM   5158  C C     . LYS B 1 143 ? 40.344  16.243  54.735  1.00 42.32  ? 143 LYS B C     1 
ATOM   5159  O O     . LYS B 1 143 ? 39.445  16.985  54.373  1.00 45.00  ? 143 LYS B O     1 
ATOM   5160  C CB    . LYS B 1 143 ? 41.894  18.166  54.194  1.00 48.89  ? 143 LYS B CB    1 
ATOM   5161  C CG    . LYS B 1 143 ? 43.266  18.776  54.412  1.00 58.28  ? 143 LYS B CG    1 
ATOM   5162  C CD    . LYS B 1 143 ? 43.498  20.173  53.882  1.00 71.23  ? 143 LYS B CD    1 
ATOM   5163  C CE    . LYS B 1 143 ? 44.943  20.590  54.115  1.00 89.35  ? 143 LYS B CE    1 
ATOM   5164  N NZ    . LYS B 1 143 ? 45.222  21.999  53.734  1.00 100.87 ? 143 LYS B NZ    1 
ATOM   5165  N N     . LEU B 1 144 ? 40.122  15.020  55.233  1.00 45.27  ? 144 LEU B N     1 
ATOM   5166  C CA    . LEU B 1 144 ? 38.802  14.427  55.370  1.00 43.61  ? 144 LEU B CA    1 
ATOM   5167  C C     . LEU B 1 144 ? 38.664  13.854  56.771  1.00 40.99  ? 144 LEU B C     1 
ATOM   5168  O O     . LEU B 1 144 ? 39.657  13.447  57.329  1.00 37.88  ? 144 LEU B O     1 
ATOM   5169  C CB    . LEU B 1 144 ? 38.640  13.306  54.344  1.00 42.58  ? 144 LEU B CB    1 
ATOM   5170  C CG    . LEU B 1 144 ? 38.682  13.752  52.884  1.00 47.31  ? 144 LEU B CG    1 
ATOM   5171  C CD1   . LEU B 1 144 ? 38.517  12.564  51.962  1.00 47.06  ? 144 LEU B CD1   1 
ATOM   5172  C CD2   . LEU B 1 144 ? 37.601  14.781  52.590  1.00 50.03  ? 144 LEU B CD2   1 
ATOM   5173  N N     . TRP B 1 145 ? 37.438  13.833  57.322  1.00 42.74  ? 145 TRP B N     1 
ATOM   5174  C CA    . TRP B 1 145 ? 37.138  13.035  58.496  1.00 41.03  ? 145 TRP B CA    1 
ATOM   5175  C C     . TRP B 1 145 ? 36.233  11.870  58.128  1.00 37.63  ? 145 TRP B C     1 
ATOM   5176  O O     . TRP B 1 145 ? 35.476  11.934  57.172  1.00 40.66  ? 145 TRP B O     1 
ATOM   5177  C CB    . TRP B 1 145 ? 36.494  13.856  59.602  1.00 41.51  ? 145 TRP B CB    1 
ATOM   5178  C CG    . TRP B 1 145 ? 37.372  14.870  60.262  1.00 42.04  ? 145 TRP B CG    1 
ATOM   5179  C CD1   . TRP B 1 145 ? 38.695  15.114  60.061  1.00 45.07  ? 145 TRP B CD1   1 
ATOM   5180  C CD2   . TRP B 1 145 ? 36.930  15.821  61.241  1.00 44.34  ? 145 TRP B CD2   1 
ATOM   5181  N NE1   . TRP B 1 145 ? 39.101  16.163  60.841  1.00 46.32  ? 145 TRP B NE1   1 
ATOM   5182  C CE2   . TRP B 1 145 ? 38.044  16.608  61.580  1.00 42.66  ? 145 TRP B CE2   1 
ATOM   5183  C CE3   . TRP B 1 145 ? 35.701  16.068  61.870  1.00 46.99  ? 145 TRP B CE3   1 
ATOM   5184  C CZ2   . TRP B 1 145 ? 37.971  17.610  62.544  1.00 48.65  ? 145 TRP B CZ2   1 
ATOM   5185  C CZ3   . TRP B 1 145 ? 35.632  17.066  62.820  1.00 45.05  ? 145 TRP B CZ3   1 
ATOM   5186  C CH2   . TRP B 1 145 ? 36.754  17.820  63.151  1.00 43.37  ? 145 TRP B CH2   1 
ATOM   5187  N N     . ILE B 1 146 ? 36.367  10.791  58.896  1.00 37.59  ? 146 ILE B N     1 
ATOM   5188  C CA    . ILE B 1 146 ? 35.447  9.682   58.831  1.00 40.01  ? 146 ILE B CA    1 
ATOM   5189  C C     . ILE B 1 146 ? 34.503  9.866   60.010  1.00 41.29  ? 146 ILE B C     1 
ATOM   5190  O O     . ILE B 1 146 ? 34.639  10.825  60.767  1.00 40.18  ? 146 ILE B O     1 
ATOM   5191  C CB    . ILE B 1 146 ? 36.154  8.314   58.821  1.00 43.31  ? 146 ILE B CB    1 
ATOM   5192  C CG1   . ILE B 1 146 ? 36.961  8.065   60.094  1.00 41.96  ? 146 ILE B CG1   1 
ATOM   5193  C CG2   . ILE B 1 146 ? 37.023  8.157   57.571  1.00 45.31  ? 146 ILE B CG2   1 
ATOM   5194  C CD1   . ILE B 1 146 ? 37.514  6.667   60.168  1.00 40.73  ? 146 ILE B CD1   1 
ATOM   5195  N N     . ASP B 1 147 ? 33.477  9.019   60.059  1.00 37.22  ? 147 ASP B N     1 
ATOM   5196  C CA    . ASP B 1 147 ? 32.566  9.011   61.179  1.00 37.09  ? 147 ASP B CA    1 
ATOM   5197  C C     . ASP B 1 147 ? 32.519  7.595   61.750  1.00 38.73  ? 147 ASP B C     1 
ATOM   5198  O O     . ASP B 1 147 ? 32.276  6.631   61.034  1.00 46.27  ? 147 ASP B O     1 
ATOM   5199  C CB    . ASP B 1 147 ? 31.209  9.553   60.758  1.00 36.95  ? 147 ASP B CB    1 
ATOM   5200  C CG    . ASP B 1 147 ? 30.273  9.651   61.943  1.00 32.89  ? 147 ASP B CG    1 
ATOM   5201  O OD1   . ASP B 1 147 ? 29.845  8.548   62.406  1.00 33.75  ? 147 ASP B OD1   1 
ATOM   5202  O OD2   . ASP B 1 147 ? 30.028  10.797  62.404  1.00 22.75  ? 147 ASP B OD2   1 
ATOM   5203  N N     . VAL B 1 148 ? 32.747  7.501   63.061  1.00 44.19  ? 148 VAL B N     1 
ATOM   5204  C CA    . VAL B 1 148 ? 33.263  6.290   63.669  1.00 43.50  ? 148 VAL B CA    1 
ATOM   5205  C C     . VAL B 1 148 ? 32.403  5.955   64.879  1.00 46.84  ? 148 VAL B C     1 
ATOM   5206  O O     . VAL B 1 148 ? 31.919  6.872   65.548  1.00 45.95  ? 148 VAL B O     1 
ATOM   5207  C CB    . VAL B 1 148 ? 34.728  6.537   64.036  1.00 49.38  ? 148 VAL B CB    1 
ATOM   5208  C CG1   . VAL B 1 148 ? 34.896  7.018   65.472  1.00 49.42  ? 148 VAL B CG1   1 
ATOM   5209  C CG2   . VAL B 1 148 ? 35.569  5.317   63.782  1.00 65.06  ? 148 VAL B CG2   1 
ATOM   5210  N N     . PRO B 1 149 ? 32.131  4.655   65.145  1.00 50.43  ? 149 PRO B N     1 
ATOM   5211  C CA    . PRO B 1 149 ? 31.449  4.220   66.365  1.00 58.83  ? 149 PRO B CA    1 
ATOM   5212  C C     . PRO B 1 149 ? 32.444  4.175   67.532  1.00 63.91  ? 149 PRO B C     1 
ATOM   5213  O O     . PRO B 1 149 ? 33.656  4.295   67.308  1.00 64.84  ? 149 PRO B O     1 
ATOM   5214  C CB    . PRO B 1 149 ? 30.967  2.814   65.963  1.00 53.04  ? 149 PRO B CB    1 
ATOM   5215  C CG    . PRO B 1 149 ? 32.103  2.286   65.133  1.00 53.01  ? 149 PRO B CG    1 
ATOM   5216  C CD    . PRO B 1 149 ? 32.564  3.502   64.343  1.00 56.58  ? 149 PRO B CD    1 
ATOM   5217  N N     . ASP B 1 150 ? 31.941  3.990   68.764  1.00 61.50  ? 150 ASP B N     1 
ATOM   5218  C CA    . ASP B 1 150 ? 32.779  4.054   69.954  1.00 65.07  ? 150 ASP B CA    1 
ATOM   5219  C C     . ASP B 1 150 ? 32.564  2.803   70.786  1.00 66.18  ? 150 ASP B C     1 
ATOM   5220  O O     . ASP B 1 150 ? 31.490  2.670   71.370  1.00 60.41  ? 150 ASP B O     1 
ATOM   5221  C CB    . ASP B 1 150 ? 32.468  5.235   70.885  1.00 68.57  ? 150 ASP B CB    1 
ATOM   5222  C CG    . ASP B 1 150 ? 33.512  5.484   71.978  1.00 72.49  ? 150 ASP B CG    1 
ATOM   5223  O OD1   . ASP B 1 150 ? 34.630  4.956   71.870  1.00 71.81  ? 150 ASP B OD1   1 
ATOM   5224  O OD2   . ASP B 1 150 ? 33.210  6.206   72.937  1.00 70.07  ? 150 ASP B OD2   1 
ATOM   5225  N N     . PRO B 1 151 ? 33.585  1.912   70.914  1.00 79.74  ? 151 PRO B N     1 
ATOM   5226  C CA    . PRO B 1 151 ? 34.796  1.948   70.079  1.00 77.06  ? 151 PRO B CA    1 
ATOM   5227  C C     . PRO B 1 151 ? 34.588  1.561   68.610  1.00 69.24  ? 151 PRO B C     1 
ATOM   5228  O O     . PRO B 1 151 ? 33.501  1.100   68.214  1.00 54.90  ? 151 PRO B O     1 
ATOM   5229  C CB    . PRO B 1 151 ? 35.750  0.933   70.757  1.00 80.75  ? 151 PRO B CB    1 
ATOM   5230  C CG    . PRO B 1 151 ? 35.197  0.735   72.158  1.00 73.92  ? 151 PRO B CG    1 
ATOM   5231  C CD    . PRO B 1 151 ? 33.700  0.899   71.981  1.00 80.39  ? 151 PRO B CD    1 
ATOM   5232  N N     . GLY B 1 152 ? 35.681  1.711   67.836  1.00 76.45  ? 152 GLY B N     1 
ATOM   5233  C CA    . GLY B 1 152 ? 35.632  1.719   66.380  1.00 75.95  ? 152 GLY B CA    1 
ATOM   5234  C C     . GLY B 1 152 ? 36.320  0.531   65.708  1.00 67.66  ? 152 GLY B C     1 
ATOM   5235  O O     . GLY B 1 152 ? 37.136  0.726   64.808  1.00 67.60  ? 152 GLY B O     1 
ATOM   5236  N N     . TRP B 1 153 ? 35.881  -0.691  66.039  1.00 75.68  ? 153 TRP B N     1 
ATOM   5237  C CA    . TRP B 1 153 ? 36.581  -1.908  65.623  1.00 82.05  ? 153 TRP B CA    1 
ATOM   5238  C C     . TRP B 1 153 ? 36.038  -2.446  64.296  1.00 75.05  ? 153 TRP B C     1 
ATOM   5239  O O     . TRP B 1 153 ? 36.685  -3.301  63.667  1.00 66.28  ? 153 TRP B O     1 
ATOM   5240  C CB    . TRP B 1 153 ? 36.561  -3.002  66.723  1.00 83.23  ? 153 TRP B CB    1 
ATOM   5241  C CG    . TRP B 1 153 ? 35.294  -3.111  67.521  1.00 83.54  ? 153 TRP B CG    1 
ATOM   5242  C CD1   . TRP B 1 153 ? 34.030  -3.260  67.026  1.00 99.10  ? 153 TRP B CD1   1 
ATOM   5243  C CD2   . TRP B 1 153 ? 35.153  -3.058  68.959  1.00 84.55  ? 153 TRP B CD2   1 
ATOM   5244  N NE1   . TRP B 1 153 ? 33.112  -3.304  68.045  1.00 101.57 ? 153 TRP B NE1   1 
ATOM   5245  C CE2   . TRP B 1 153 ? 33.769  -3.185  69.243  1.00 91.74  ? 153 TRP B CE2   1 
ATOM   5246  C CE3   . TRP B 1 153 ? 36.046  -2.933  70.036  1.00 77.21  ? 153 TRP B CE3   1 
ATOM   5247  C CZ2   . TRP B 1 153 ? 33.267  -3.173  70.548  1.00 77.18  ? 153 TRP B CZ2   1 
ATOM   5248  C CZ3   . TRP B 1 153 ? 35.549  -2.926  71.329  1.00 76.51  ? 153 TRP B CZ3   1 
ATOM   5249  C CH2   . TRP B 1 153 ? 34.175  -3.036  71.579  1.00 75.40  ? 153 TRP B CH2   1 
ATOM   5250  N N     . GLY B 1 154 ? 34.850  -1.950  63.903  1.00 61.41  ? 154 GLY B N     1 
ATOM   5251  C CA    . GLY B 1 154 ? 34.006  -2.638  62.938  1.00 56.41  ? 154 GLY B CA    1 
ATOM   5252  C C     . GLY B 1 154 ? 34.217  -2.172  61.497  1.00 47.97  ? 154 GLY B C     1 
ATOM   5253  O O     . GLY B 1 154 ? 35.257  -1.617  61.161  1.00 54.48  ? 154 GLY B O     1 
ATOM   5254  N N     . SER B 1 155 ? 33.195  -2.422  60.670  1.00 44.27  ? 155 SER B N     1 
ATOM   5255  C CA    . SER B 1 155 ? 33.234  -2.292  59.221  1.00 42.84  ? 155 SER B CA    1 
ATOM   5256  C C     . SER B 1 155 ? 32.514  -1.024  58.743  1.00 44.97  ? 155 SER B C     1 
ATOM   5257  O O     . SER B 1 155 ? 31.320  -0.786  58.996  1.00 47.42  ? 155 SER B O     1 
ATOM   5258  C CB    . SER B 1 155 ? 32.627  -3.510  58.588  1.00 42.32  ? 155 SER B CB    1 
ATOM   5259  O OG    . SER B 1 155 ? 32.140  -3.199  57.284  1.00 50.70  ? 155 SER B OG    1 
ATOM   5260  N N     . VAL B 1 156 ? 33.230  -0.206  57.985  1.00 40.38  ? 156 VAL B N     1 
ATOM   5261  C CA    . VAL B 1 156 ? 32.578  0.917   57.346  1.00 44.00  ? 156 VAL B CA    1 
ATOM   5262  C C     . VAL B 1 156 ? 31.282  0.452   56.660  1.00 45.47  ? 156 VAL B C     1 
ATOM   5263  O O     . VAL B 1 156 ? 30.287  1.163   56.685  1.00 42.33  ? 156 VAL B O     1 
ATOM   5264  C CB    . VAL B 1 156 ? 33.523  1.592   56.345  1.00 41.85  ? 156 VAL B CB    1 
ATOM   5265  C CG1   . VAL B 1 156 ? 32.913  2.876   55.807  1.00 45.35  ? 156 VAL B CG1   1 
ATOM   5266  C CG2   . VAL B 1 156 ? 34.881  1.861   56.967  1.00 44.95  ? 156 VAL B CG2   1 
ATOM   5267  N N     . VAL B 1 157 ? 31.301  -0.734  56.034  1.00 44.59  ? 157 VAL B N     1 
ATOM   5268  C CA    . VAL B 1 157 ? 30.161  -1.201  55.266  1.00 43.47  ? 157 VAL B CA    1 
ATOM   5269  C C     . VAL B 1 157 ? 29.114  -1.843  56.174  1.00 50.33  ? 157 VAL B C     1 
ATOM   5270  O O     . VAL B 1 157 ? 27.939  -1.476  56.115  1.00 47.90  ? 157 VAL B O     1 
ATOM   5271  C CB    . VAL B 1 157 ? 30.569  -2.170  54.149  1.00 39.66  ? 157 VAL B CB    1 
ATOM   5272  C CG1   . VAL B 1 157 ? 29.358  -2.734  53.451  1.00 47.33  ? 157 VAL B CG1   1 
ATOM   5273  C CG2   . VAL B 1 157 ? 31.465  -1.504  53.134  1.00 41.06  ? 157 VAL B CG2   1 
ATOM   5274  N N     . GLY B 1 158 ? 29.521  -2.849  56.959  1.00 50.98  ? 158 GLY B N     1 
ATOM   5275  C CA    . GLY B 1 158 ? 28.558  -3.607  57.734  1.00 46.84  ? 158 GLY B CA    1 
ATOM   5276  C C     . GLY B 1 158 ? 27.822  -2.699  58.709  1.00 48.43  ? 158 GLY B C     1 
ATOM   5277  O O     . GLY B 1 158 ? 26.616  -2.805  58.917  1.00 43.56  ? 158 GLY B O     1 
ATOM   5278  N N     . ASN B 1 159 ? 28.564  -1.772  59.303  1.00 49.47  ? 159 ASN B N     1 
ATOM   5279  C CA    . ASN B 1 159 ? 27.960  -0.937  60.319  1.00 49.05  ? 159 ASN B CA    1 
ATOM   5280  C C     . ASN B 1 159 ? 26.885  -0.100  59.640  1.00 47.30  ? 159 ASN B C     1 
ATOM   5281  O O     . ASN B 1 159 ? 25.772  0.035   60.137  1.00 45.77  ? 159 ASN B O     1 
ATOM   5282  C CB    . ASN B 1 159 ? 29.038  -0.148  61.053  1.00 50.89  ? 159 ASN B CB    1 
ATOM   5283  C CG    . ASN B 1 159 ? 28.461  0.925   61.934  1.00 50.42  ? 159 ASN B CG    1 
ATOM   5284  O OD1   . ASN B 1 159 ? 28.115  2.000   61.449  1.00 50.26  ? 159 ASN B OD1   1 
ATOM   5285  N ND2   . ASN B 1 159 ? 28.417  0.662   63.228  1.00 50.24  ? 159 ASN B ND2   1 
ATOM   5286  N N     . ALA B 1 160 ? 27.244  0.434   58.471  1.00 46.18  ? 160 ALA B N     1 
ATOM   5287  C CA    . ALA B 1 160 ? 26.375  1.317   57.723  1.00 39.39  ? 160 ALA B CA    1 
ATOM   5288  C C     . ALA B 1 160 ? 25.128  0.558   57.295  1.00 36.97  ? 160 ALA B C     1 
ATOM   5289  O O     . ALA B 1 160 ? 24.025  1.101   57.389  1.00 36.12  ? 160 ALA B O     1 
ATOM   5290  C CB    . ALA B 1 160 ? 27.126  1.864   56.528  1.00 42.63  ? 160 ALA B CB    1 
ATOM   5291  N N     . LEU B 1 161 ? 25.306  -0.694  56.828  1.00 34.18  ? 161 LEU B N     1 
ATOM   5292  C CA    . LEU B 1 161 ? 24.168  -1.459  56.353  1.00 37.80  ? 161 LEU B CA    1 
ATOM   5293  C C     . LEU B 1 161 ? 23.198  -1.768  57.481  1.00 37.99  ? 161 LEU B C     1 
ATOM   5294  O O     . LEU B 1 161 ? 22.032  -2.014  57.227  1.00 44.05  ? 161 LEU B O     1 
ATOM   5295  C CB    . LEU B 1 161 ? 24.614  -2.761  55.698  1.00 37.92  ? 161 LEU B CB    1 
ATOM   5296  C CG    . LEU B 1 161 ? 25.196  -2.621  54.293  1.00 42.35  ? 161 LEU B CG    1 
ATOM   5297  C CD1   . LEU B 1 161 ? 25.381  -3.996  53.664  1.00 43.51  ? 161 LEU B CD1   1 
ATOM   5298  C CD2   . LEU B 1 161 ? 24.335  -1.737  53.407  1.00 44.18  ? 161 LEU B CD2   1 
ATOM   5299  N N     . ASP B 1 162 ? 23.689  -1.807  58.712  1.00 47.76  ? 162 ASP B N     1 
ATOM   5300  C CA    . ASP B 1 162 ? 22.874  -2.209  59.840  1.00 50.48  ? 162 ASP B CA    1 
ATOM   5301  C C     . ASP B 1 162 ? 22.329  -0.963  60.537  1.00 48.44  ? 162 ASP B C     1 
ATOM   5302  O O     . ASP B 1 162 ? 21.821  -1.069  61.640  1.00 54.44  ? 162 ASP B O     1 
ATOM   5303  C CB    . ASP B 1 162 ? 23.670  -3.165  60.733  1.00 56.62  ? 162 ASP B CB    1 
ATOM   5304  C CG    . ASP B 1 162 ? 22.797  -3.940  61.700  1.00 60.21  ? 162 ASP B CG    1 
ATOM   5305  O OD1   . ASP B 1 162 ? 21.964  -4.728  61.213  1.00 58.27  ? 162 ASP B OD1   1 
ATOM   5306  O OD2   . ASP B 1 162 ? 22.951  -3.725  62.925  1.00 59.42  ? 162 ASP B OD2   1 
ATOM   5307  N N     . HIS B 1 163 ? 22.393  0.197   59.857  1.00 46.30  ? 163 HIS B N     1 
ATOM   5308  C CA    . HIS B 1 163 ? 21.847  1.453   60.340  1.00 38.40  ? 163 HIS B CA    1 
ATOM   5309  C C     . HIS B 1 163 ? 22.633  1.939   61.548  1.00 41.51  ? 163 HIS B C     1 
ATOM   5310  O O     . HIS B 1 163 ? 22.066  2.413   62.516  1.00 49.16  ? 163 HIS B O     1 
ATOM   5311  C CB    . HIS B 1 163 ? 20.346  1.328   60.605  1.00 39.19  ? 163 HIS B CB    1 
ATOM   5312  C CG    . HIS B 1 163 ? 19.534  1.023   59.386  1.00 44.80  ? 163 HIS B CG    1 
ATOM   5313  N ND1   . HIS B 1 163 ? 18.177  0.761   59.443  1.00 53.00  ? 163 HIS B ND1   1 
ATOM   5314  C CD2   . HIS B 1 163 ? 19.880  0.948   58.085  1.00 37.80  ? 163 HIS B CD2   1 
ATOM   5315  C CE1   . HIS B 1 163 ? 17.737  0.540   58.209  1.00 48.38  ? 163 HIS B CE1   1 
ATOM   5316  N NE2   . HIS B 1 163 ? 18.748  0.670   57.374  1.00 39.98  ? 163 HIS B NE2   1 
ATOM   5317  N N     . GLY B 1 164 ? 23.960  1.869   61.458  1.00 45.15  ? 164 GLY B N     1 
ATOM   5318  C CA    . GLY B 1 164 ? 24.821  2.291   62.542  1.00 44.62  ? 164 GLY B CA    1 
ATOM   5319  C C     . GLY B 1 164 ? 24.837  3.809   62.699  1.00 49.53  ? 164 GLY B C     1 
ATOM   5320  O O     . GLY B 1 164 ? 24.434  4.523   61.788  1.00 49.67  ? 164 GLY B O     1 
ATOM   5321  N N     . ILE B 1 165 ? 25.344  4.269   63.855  1.00 53.66  ? 165 ILE B N     1 
ATOM   5322  C CA    . ILE B 1 165 ? 25.419  5.682   64.198  1.00 55.53  ? 165 ILE B CA    1 
ATOM   5323  C C     . ILE B 1 165 ? 26.805  5.994   64.763  1.00 53.36  ? 165 ILE B C     1 
ATOM   5324  O O     . ILE B 1 165 ? 27.517  5.089   65.217  1.00 45.16  ? 165 ILE B O     1 
ATOM   5325  C CB    . ILE B 1 165 ? 24.272  6.097   65.141  1.00 58.07  ? 165 ILE B CB    1 
ATOM   5326  C CG1   . ILE B 1 165 ? 24.141  5.201   66.382  1.00 68.89  ? 165 ILE B CG1   1 
ATOM   5327  C CG2   . ILE B 1 165 ? 22.970  6.130   64.350  1.00 58.40  ? 165 ILE B CG2   1 
ATOM   5328  C CD1   . ILE B 1 165 ? 25.174  5.441   67.471  1.00 72.87  ? 165 ILE B CD1   1 
ATOM   5329  N N     . GLY B 1 166 ? 27.178  7.279   64.660  1.00 42.11  ? 166 GLY B N     1 
ATOM   5330  C CA    . GLY B 1 166 ? 28.466  7.779   65.109  1.00 42.16  ? 166 GLY B CA    1 
ATOM   5331  C C     . GLY B 1 166 ? 28.299  9.187   65.656  1.00 42.69  ? 166 GLY B C     1 
ATOM   5332  O O     . GLY B 1 166 ? 27.149  9.604   65.844  1.00 40.54  ? 166 GLY B O     1 
ATOM   5333  N N     . TYR B 1 167 ? 29.409  9.936   65.852  1.00 43.14  ? 167 TYR B N     1 
ATOM   5334  C CA    . TYR B 1 167 ? 29.339  11.110  66.726  1.00 43.13  ? 167 TYR B CA    1 
ATOM   5335  C C     . TYR B 1 167 ? 29.733  12.425  66.046  1.00 43.87  ? 167 TYR B C     1 
ATOM   5336  O O     . TYR B 1 167 ? 29.923  13.436  66.734  1.00 45.12  ? 167 TYR B O     1 
ATOM   5337  C CB    . TYR B 1 167 ? 30.105  10.798  68.014  1.00 42.33  ? 167 TYR B CB    1 
ATOM   5338  C CG    . TYR B 1 167 ? 29.513  9.614   68.733  1.00 49.67  ? 167 TYR B CG    1 
ATOM   5339  C CD1   . TYR B 1 167 ? 29.778  8.318   68.307  1.00 53.17  ? 167 TYR B CD1   1 
ATOM   5340  C CD2   . TYR B 1 167 ? 28.600  9.781   69.770  1.00 47.56  ? 167 TYR B CD2   1 
ATOM   5341  C CE1   . TYR B 1 167 ? 29.189  7.219   68.923  1.00 55.82  ? 167 TYR B CE1   1 
ATOM   5342  C CE2   . TYR B 1 167 ? 27.991  8.692   70.373  1.00 49.77  ? 167 TYR B CE2   1 
ATOM   5343  C CZ    . TYR B 1 167 ? 28.286  7.406   69.950  1.00 50.88  ? 167 TYR B CZ    1 
ATOM   5344  O OH    . TYR B 1 167 ? 27.686  6.307   70.500  1.00 53.36  ? 167 TYR B OH    1 
ATOM   5345  N N     . THR B 1 168 ? 29.803  12.436  64.704  1.00 41.09  ? 168 THR B N     1 
ATOM   5346  C CA    . THR B 1 168 ? 30.015  13.660  63.938  1.00 42.39  ? 168 THR B CA    1 
ATOM   5347  C C     . THR B 1 168 ? 28.714  14.119  63.259  1.00 43.98  ? 168 THR B C     1 
ATOM   5348  O O     . THR B 1 168 ? 27.676  13.461  63.336  1.00 51.27  ? 168 THR B O     1 
ATOM   5349  C CB    . THR B 1 168 ? 31.168  13.456  62.933  1.00 46.26  ? 168 THR B CB    1 
ATOM   5350  O OG1   . THR B 1 168 ? 30.683  12.845  61.733  1.00 36.84  ? 168 THR B OG1   1 
ATOM   5351  C CG2   . THR B 1 168 ? 32.328  12.666  63.520  1.00 42.27  ? 168 THR B CG2   1 
ATOM   5352  N N     . PRO B 1 169 ? 28.693  15.254  62.526  1.00 43.76  ? 169 PRO B N     1 
ATOM   5353  C CA    . PRO B 1 169 ? 27.569  15.558  61.631  1.00 41.84  ? 169 PRO B CA    1 
ATOM   5354  C C     . PRO B 1 169 ? 27.240  14.478  60.591  1.00 38.40  ? 169 PRO B C     1 
ATOM   5355  O O     . PRO B 1 169 ? 26.085  14.325  60.197  1.00 38.94  ? 169 PRO B O     1 
ATOM   5356  C CB    . PRO B 1 169 ? 28.005  16.860  60.951  1.00 40.27  ? 169 PRO B CB    1 
ATOM   5357  C CG    . PRO B 1 169 ? 28.957  17.487  61.939  1.00 44.72  ? 169 PRO B CG    1 
ATOM   5358  C CD    . PRO B 1 169 ? 29.712  16.313  62.532  1.00 44.64  ? 169 PRO B CD    1 
ATOM   5359  N N     . TYR B 1 170 ? 28.237  13.684  60.198  1.00 31.48  ? 170 TYR B N     1 
ATOM   5360  C CA    . TYR B 1 170 ? 28.043  12.522  59.339  1.00 33.54  ? 170 TYR B CA    1 
ATOM   5361  C C     . TYR B 1 170 ? 27.697  11.305  60.192  1.00 31.28  ? 170 TYR B C     1 
ATOM   5362  O O     . TYR B 1 170 ? 28.003  10.172  59.843  1.00 34.02  ? 170 TYR B O     1 
ATOM   5363  C CB    . TYR B 1 170 ? 29.285  12.332  58.426  1.00 36.69  ? 170 TYR B CB    1 
ATOM   5364  C CG    . TYR B 1 170 ? 29.421  13.304  57.258  1.00 31.13  ? 170 TYR B CG    1 
ATOM   5365  C CD1   . TYR B 1 170 ? 29.294  14.665  57.449  1.00 29.27  ? 170 TYR B CD1   1 
ATOM   5366  C CD2   . TYR B 1 170 ? 29.666  12.874  55.952  1.00 32.02  ? 170 TYR B CD2   1 
ATOM   5367  C CE1   . TYR B 1 170 ? 29.422  15.583  56.415  1.00 32.26  ? 170 TYR B CE1   1 
ATOM   5368  C CE2   . TYR B 1 170 ? 29.819  13.773  54.899  1.00 27.76  ? 170 TYR B CE2   1 
ATOM   5369  C CZ    . TYR B 1 170 ? 29.693  15.135  55.125  1.00 32.94  ? 170 TYR B CZ    1 
ATOM   5370  O OH    . TYR B 1 170 ? 29.817  16.094  54.122  1.00 32.29  ? 170 TYR B OH    1 
ATOM   5371  N N     . GLY B 1 171 ? 27.009  11.524  61.319  1.00 44.48  ? 171 GLY B N     1 
ATOM   5372  C CA    . GLY B 1 171 ? 26.777  10.469  62.298  1.00 40.07  ? 171 GLY B CA    1 
ATOM   5373  C C     . GLY B 1 171 ? 25.814  9.379   61.811  1.00 46.02  ? 171 GLY B C     1 
ATOM   5374  O O     . GLY B 1 171 ? 25.885  8.246   62.302  1.00 43.80  ? 171 GLY B O     1 
ATOM   5375  N N     . ASP B 1 172 ? 24.898  9.711   60.874  1.00 40.07  ? 172 ASP B N     1 
ATOM   5376  C CA    . ASP B 1 172 ? 23.963  8.715   60.356  1.00 44.10  ? 172 ASP B CA    1 
ATOM   5377  C C     . ASP B 1 172 ? 24.617  8.034   59.153  1.00 42.69  ? 172 ASP B C     1 
ATOM   5378  O O     . ASP B 1 172 ? 24.687  8.597   58.070  1.00 44.31  ? 172 ASP B O     1 
ATOM   5379  C CB    . ASP B 1 172 ? 22.586  9.313   59.993  1.00 43.16  ? 172 ASP B CB    1 
ATOM   5380  C CG    . ASP B 1 172 ? 21.565  8.331   59.420  1.00 40.12  ? 172 ASP B CG    1 
ATOM   5381  O OD1   . ASP B 1 172 ? 21.942  7.128   59.129  1.00 35.14  ? 172 ASP B OD1   1 
ATOM   5382  O OD2   . ASP B 1 172 ? 20.381  8.742   59.296  1.00 38.21  ? 172 ASP B OD2   1 
ATOM   5383  N N     . HIS B 1 173 ? 25.062  6.799   59.346  1.00 40.66  ? 173 HIS B N     1 
ATOM   5384  C CA    . HIS B 1 173 ? 26.015  6.191   58.444  1.00 39.63  ? 173 HIS B CA    1 
ATOM   5385  C C     . HIS B 1 173 ? 25.322  5.885   57.114  1.00 41.09  ? 173 HIS B C     1 
ATOM   5386  O O     . HIS B 1 173 ? 25.815  6.265   56.033  1.00 35.77  ? 173 HIS B O     1 
ATOM   5387  C CB    . HIS B 1 173 ? 26.699  5.004   59.136  1.00 37.15  ? 173 HIS B CB    1 
ATOM   5388  C CG    . HIS B 1 173 ? 27.706  5.372   60.190  1.00 35.87  ? 173 HIS B CG    1 
ATOM   5389  N ND1   . HIS B 1 173 ? 28.281  4.416   61.009  1.00 33.53  ? 173 HIS B ND1   1 
ATOM   5390  C CD2   . HIS B 1 173 ? 28.189  6.560   60.619  1.00 37.59  ? 173 HIS B CD2   1 
ATOM   5391  C CE1   . HIS B 1 173 ? 29.138  5.011   61.837  1.00 42.30  ? 173 HIS B CE1   1 
ATOM   5392  N NE2   . HIS B 1 173 ? 29.106  6.316   61.630  1.00 37.91  ? 173 HIS B NE2   1 
ATOM   5393  N N     . PHE B 1 174 ? 24.191  5.175   57.192  1.00 39.86  ? 174 PHE B N     1 
ATOM   5394  C CA    . PHE B 1 174 ? 23.539  4.767   55.965  1.00 43.12  ? 174 PHE B CA    1 
ATOM   5395  C C     . PHE B 1 174 ? 23.020  5.990   55.224  1.00 43.09  ? 174 PHE B C     1 
ATOM   5396  O O     . PHE B 1 174 ? 23.021  6.004   53.994  1.00 44.81  ? 174 PHE B O     1 
ATOM   5397  C CB    . PHE B 1 174 ? 22.438  3.741   56.162  1.00 41.59  ? 174 PHE B CB    1 
ATOM   5398  C CG    . PHE B 1 174 ? 21.996  3.175   54.842  1.00 39.02  ? 174 PHE B CG    1 
ATOM   5399  C CD1   . PHE B 1 174 ? 22.888  2.501   54.040  1.00 37.21  ? 174 PHE B CD1   1 
ATOM   5400  C CD2   . PHE B 1 174 ? 20.700  3.350   54.384  1.00 48.06  ? 174 PHE B CD2   1 
ATOM   5401  C CE1   . PHE B 1 174 ? 22.485  1.968   52.827  1.00 47.38  ? 174 PHE B CE1   1 
ATOM   5402  C CE2   . PHE B 1 174 ? 20.309  2.859   53.145  1.00 52.58  ? 174 PHE B CE2   1 
ATOM   5403  C CZ    . PHE B 1 174 ? 21.201  2.161   52.369  1.00 48.82  ? 174 PHE B CZ    1 
ATOM   5404  N N     . ALA B 1 175 ? 22.711  7.061   55.959  1.00 41.70  ? 175 ALA B N     1 
ATOM   5405  C CA    . ALA B 1 175 ? 22.351  8.317   55.309  1.00 42.29  ? 175 ALA B CA    1 
ATOM   5406  C C     . ALA B 1 175 ? 23.431  8.769   54.338  1.00 37.81  ? 175 ALA B C     1 
ATOM   5407  O O     . ALA B 1 175 ? 23.114  9.214   53.250  1.00 46.17  ? 175 ALA B O     1 
ATOM   5408  C CB    . ALA B 1 175 ? 22.082  9.406   56.327  1.00 45.09  ? 175 ALA B CB    1 
ATOM   5409  N N     . MET B 1 176 ? 24.683  8.715   54.790  1.00 41.33  ? 176 MET B N     1 
ATOM   5410  C CA    . MET B 1 176 ? 25.843  9.202   54.071  1.00 37.00  ? 176 MET B CA    1 
ATOM   5411  C C     . MET B 1 176 ? 26.294  8.239   52.971  1.00 37.55  ? 176 MET B C     1 
ATOM   5412  O O     . MET B 1 176 ? 27.287  8.492   52.297  1.00 39.10  ? 176 MET B O     1 
ATOM   5413  C CB    . MET B 1 176 ? 26.989  9.366   55.065  1.00 32.21  ? 176 MET B CB    1 
ATOM   5414  C CG    . MET B 1 176 ? 26.774  10.507  56.030  1.00 35.26  ? 176 MET B CG    1 
ATOM   5415  S SD    . MET B 1 176 ? 26.335  12.096  55.284  1.00 41.00  ? 176 MET B SD    1 
ATOM   5416  C CE    . MET B 1 176 ? 24.560  12.001  55.498  1.00 39.59  ? 176 MET B CE    1 
ATOM   5417  N N     . GLN B 1 177 ? 25.635  7.096   52.841  1.00 36.11  ? 177 GLN B N     1 
ATOM   5418  C CA    . GLN B 1 177 ? 26.052  6.099   51.863  1.00 43.22  ? 177 GLN B CA    1 
ATOM   5419  C C     . GLN B 1 177 ? 25.586  6.508   50.468  1.00 38.69  ? 177 GLN B C     1 
ATOM   5420  O O     . GLN B 1 177 ? 24.563  7.138   50.343  1.00 38.58  ? 177 GLN B O     1 
ATOM   5421  C CB    . GLN B 1 177 ? 25.475  4.725   52.223  1.00 36.37  ? 177 GLN B CB    1 
ATOM   5422  C CG    . GLN B 1 177 ? 25.630  3.688   51.147  1.00 35.03  ? 177 GLN B CG    1 
ATOM   5423  C CD    . GLN B 1 177 ? 24.550  3.625   50.103  1.00 39.98  ? 177 GLN B CD    1 
ATOM   5424  O OE1   . GLN B 1 177 ? 23.361  3.720   50.391  1.00 49.11  ? 177 GLN B OE1   1 
ATOM   5425  N NE2   . GLN B 1 177 ? 24.949  3.319   48.878  1.00 45.82  ? 177 GLN B NE2   1 
ATOM   5426  N N     . CYS B 1 178 ? 26.315  6.102   49.427  1.00 40.17  ? 178 CYS B N     1 
ATOM   5427  C CA    . CYS B 1 178 ? 25.986  6.519   48.082  1.00 36.38  ? 178 CYS B CA    1 
ATOM   5428  C C     . CYS B 1 178 ? 26.617  5.597   47.046  1.00 29.79  ? 178 CYS B C     1 
ATOM   5429  O O     . CYS B 1 178 ? 27.826  5.469   46.988  1.00 35.77  ? 178 CYS B O     1 
ATOM   5430  C CB    . CYS B 1 178 ? 26.501  7.934   47.907  1.00 41.51  ? 178 CYS B CB    1 
ATOM   5431  S SG    . CYS B 1 178 ? 26.082  8.617   46.294  1.00 36.25  ? 178 CYS B SG    1 
ATOM   5432  N N     . GLY B 1 179 ? 25.810  4.893   46.273  1.00 30.29  ? 179 GLY B N     1 
ATOM   5433  C CA    . GLY B 1 179 ? 26.313  3.826   45.415  1.00 34.77  ? 179 GLY B CA    1 
ATOM   5434  C C     . GLY B 1 179 ? 26.683  2.523   46.152  1.00 34.37  ? 179 GLY B C     1 
ATOM   5435  O O     . GLY B 1 179 ? 27.306  2.558   47.222  1.00 33.11  ? 179 GLY B O     1 
ATOM   5436  N N     . MET B 1 180 ? 26.402  1.367   45.518  1.00 29.02  ? 180 MET B N     1 
ATOM   5437  C CA    . MET B 1 180 ? 26.883  0.091   46.034  1.00 31.89  ? 180 MET B CA    1 
ATOM   5438  C C     . MET B 1 180 ? 26.790  -0.924  44.920  1.00 34.49  ? 180 MET B C     1 
ATOM   5439  O O     . MET B 1 180 ? 26.073  -0.705  43.954  1.00 45.60  ? 180 MET B O     1 
ATOM   5440  C CB    . MET B 1 180 ? 26.106  -0.470  47.234  1.00 34.54  ? 180 MET B CB    1 
ATOM   5441  C CG    . MET B 1 180 ? 24.583  -0.450  47.058  1.00 36.90  ? 180 MET B CG    1 
ATOM   5442  S SD    . MET B 1 180 ? 23.661  -1.408  48.262  1.00 41.62  ? 180 MET B SD    1 
ATOM   5443  C CE    . MET B 1 180 ? 23.580  -0.349  49.701  1.00 41.65  ? 180 MET B CE    1 
ATOM   5444  N N     . GLU B 1 181 ? 27.580  -1.990  45.062  1.00 38.77  ? 181 GLU B N     1 
ATOM   5445  C CA    . GLU B 1 181 ? 27.530  -3.158  44.205  1.00 38.70  ? 181 GLU B CA    1 
ATOM   5446  C C     . GLU B 1 181 ? 26.907  -4.254  45.041  1.00 39.31  ? 181 GLU B C     1 
ATOM   5447  O O     . GLU B 1 181 ? 27.295  -4.438  46.198  1.00 41.77  ? 181 GLU B O     1 
ATOM   5448  C CB    . GLU B 1 181 ? 28.933  -3.544  43.744  1.00 40.33  ? 181 GLU B CB    1 
ATOM   5449  C CG    . GLU B 1 181 ? 28.973  -4.739  42.812  1.00 40.70  ? 181 GLU B CG    1 
ATOM   5450  C CD    . GLU B 1 181 ? 30.348  -5.015  42.227  1.00 42.85  ? 181 GLU B CD    1 
ATOM   5451  O OE1   . GLU B 1 181 ? 31.221  -5.505  42.952  1.00 47.97  ? 181 GLU B OE1   1 
ATOM   5452  O OE2   . GLU B 1 181 ? 30.558  -4.698  41.044  1.00 49.36  ? 181 GLU B OE2   1 
ATOM   5453  N N     . VAL B 1 182 ? 25.923  -4.932  44.449  1.00 44.40  ? 182 VAL B N     1 
ATOM   5454  C CA    . VAL B 1 182 ? 25.204  -5.983  45.147  1.00 41.93  ? 182 VAL B CA    1 
ATOM   5455  C C     . VAL B 1 182 ? 25.229  -7.264  44.316  1.00 39.43  ? 182 VAL B C     1 
ATOM   5456  O O     . VAL B 1 182 ? 24.966  -7.237  43.121  1.00 44.26  ? 182 VAL B O     1 
ATOM   5457  C CB    . VAL B 1 182 ? 23.772  -5.521  45.445  1.00 37.72  ? 182 VAL B CB    1 
ATOM   5458  C CG1   . VAL B 1 182 ? 23.011  -6.561  46.244  1.00 35.13  ? 182 VAL B CG1   1 
ATOM   5459  C CG2   . VAL B 1 182 ? 23.790  -4.185  46.161  1.00 38.71  ? 182 VAL B CG2   1 
ATOM   5460  N N     . VAL B 1 183 ? 25.605  -8.366  44.960  1.00 38.29  ? 183 VAL B N     1 
ATOM   5461  C CA    . VAL B 1 183 ? 25.351  -9.705  44.458  1.00 34.74  ? 183 VAL B CA    1 
ATOM   5462  C C     . VAL B 1 183 ? 23.988  -10.149 44.966  1.00 36.89  ? 183 VAL B C     1 
ATOM   5463  O O     . VAL B 1 183 ? 23.772  -10.344 46.165  1.00 39.62  ? 183 VAL B O     1 
ATOM   5464  C CB    . VAL B 1 183 ? 26.433  -10.693 44.913  1.00 34.01  ? 183 VAL B CB    1 
ATOM   5465  C CG1   . VAL B 1 183 ? 26.150  -12.077 44.375  1.00 32.26  ? 183 VAL B CG1   1 
ATOM   5466  C CG2   . VAL B 1 183 ? 27.830  -10.248 44.505  1.00 34.49  ? 183 VAL B CG2   1 
ATOM   5467  N N     . LEU B 1 184 ? 23.062  -10.310 44.035  1.00 37.04  ? 184 LEU B N     1 
ATOM   5468  C CA    . LEU B 1 184 ? 21.711  -10.674 44.388  1.00 38.65  ? 184 LEU B CA    1 
ATOM   5469  C C     . LEU B 1 184 ? 21.707  -12.122 44.854  1.00 42.57  ? 184 LEU B C     1 
ATOM   5470  O O     . LEU B 1 184 ? 22.708  -12.831 44.723  1.00 40.82  ? 184 LEU B O     1 
ATOM   5471  C CB    . LEU B 1 184 ? 20.810  -10.449 43.169  1.00 43.06  ? 184 LEU B CB    1 
ATOM   5472  C CG    . LEU B 1 184 ? 20.718  -9.002  42.664  1.00 40.73  ? 184 LEU B CG    1 
ATOM   5473  C CD1   . LEU B 1 184 ? 19.814  -8.911  41.449  1.00 37.98  ? 184 LEU B CD1   1 
ATOM   5474  C CD2   . LEU B 1 184 ? 20.230  -8.076  43.758  1.00 42.54  ? 184 LEU B CD2   1 
ATOM   5475  N N     . PRO B 1 185 ? 20.592  -12.582 45.463  1.00 46.91  ? 185 PRO B N     1 
ATOM   5476  C CA    . PRO B 1 185 ? 20.476  -13.979 45.884  1.00 43.97  ? 185 PRO B CA    1 
ATOM   5477  C C     . PRO B 1 185 ? 20.520  -15.014 44.754  1.00 46.02  ? 185 PRO B C     1 
ATOM   5478  O O     . PRO B 1 185 ? 20.638  -16.214 45.029  1.00 42.75  ? 185 PRO B O     1 
ATOM   5479  C CB    . PRO B 1 185 ? 19.121  -14.001 46.604  1.00 41.04  ? 185 PRO B CB    1 
ATOM   5480  C CG    . PRO B 1 185 ? 18.878  -12.550 47.018  1.00 41.59  ? 185 PRO B CG    1 
ATOM   5481  C CD    . PRO B 1 185 ? 19.420  -11.770 45.852  1.00 42.38  ? 185 PRO B CD    1 
ATOM   5482  N N     . ASN B 1 186 ? 20.438  -14.574 43.487  1.00 45.41  ? 186 ASN B N     1 
ATOM   5483  C CA    . ASN B 1 186 ? 20.496  -15.493 42.349  1.00 45.51  ? 186 ASN B CA    1 
ATOM   5484  C C     . ASN B 1 186 ? 21.895  -15.545 41.745  1.00 54.05  ? 186 ASN B C     1 
ATOM   5485  O O     . ASN B 1 186 ? 22.110  -16.327 40.823  1.00 57.06  ? 186 ASN B O     1 
ATOM   5486  C CB    . ASN B 1 186 ? 19.491  -15.152 41.249  1.00 46.45  ? 186 ASN B CB    1 
ATOM   5487  C CG    . ASN B 1 186 ? 19.615  -13.730 40.717  1.00 49.22  ? 186 ASN B CG    1 
ATOM   5488  O OD1   . ASN B 1 186 ? 20.578  -13.010 40.985  1.00 38.94  ? 186 ASN B OD1   1 
ATOM   5489  N ND2   . ASN B 1 186 ? 18.643  -13.313 39.930  1.00 44.03  ? 186 ASN B ND2   1 
ATOM   5490  N N     . GLY B 1 187 ? 22.835  -14.730 42.262  1.00 55.67  ? 187 GLY B N     1 
ATOM   5491  C CA    . GLY B 1 187 ? 24.224  -14.777 41.835  1.00 54.08  ? 187 GLY B CA    1 
ATOM   5492  C C     . GLY B 1 187 ? 24.580  -13.714 40.791  1.00 52.26  ? 187 GLY B C     1 
ATOM   5493  O O     . GLY B 1 187 ? 25.754  -13.558 40.463  1.00 48.92  ? 187 GLY B O     1 
ATOM   5494  N N     . GLU B 1 188 ? 23.572  -13.011 40.260  1.00 53.38  ? 188 GLU B N     1 
ATOM   5495  C CA    . GLU B 1 188 ? 23.775  -11.853 39.387  1.00 55.95  ? 188 GLU B CA    1 
ATOM   5496  C C     . GLU B 1 188 ? 24.315  -10.670 40.186  1.00 50.43  ? 188 GLU B C     1 
ATOM   5497  O O     . GLU B 1 188 ? 24.012  -10.540 41.367  1.00 55.84  ? 188 GLU B O     1 
ATOM   5498  C CB    . GLU B 1 188 ? 22.459  -11.399 38.751  1.00 52.32  ? 188 GLU B CB    1 
ATOM   5499  C CG    . GLU B 1 188 ? 21.758  -12.480 37.942  1.00 53.70  ? 188 GLU B CG    1 
ATOM   5500  C CD    . GLU B 1 188 ? 22.642  -12.970 36.810  1.00 55.49  ? 188 GLU B CD    1 
ATOM   5501  O OE1   . GLU B 1 188 ? 22.864  -12.179 35.897  1.00 55.14  ? 188 GLU B OE1   1 
ATOM   5502  O OE2   . GLU B 1 188 ? 23.150  -14.115 36.882  1.00 51.94  ? 188 GLU B OE2   1 
ATOM   5503  N N     . VAL B 1 189 ? 25.085  -9.788  39.536  1.00 44.09  ? 189 VAL B N     1 
ATOM   5504  C CA    . VAL B 1 189 ? 25.623  -8.622  40.222  1.00 42.44  ? 189 VAL B CA    1 
ATOM   5505  C C     . VAL B 1 189 ? 25.015  -7.364  39.621  1.00 38.03  ? 189 VAL B C     1 
ATOM   5506  O O     . VAL B 1 189 ? 24.747  -7.339  38.430  1.00 43.69  ? 189 VAL B O     1 
ATOM   5507  C CB    . VAL B 1 189 ? 27.170  -8.571  40.204  1.00 44.48  ? 189 VAL B CB    1 
ATOM   5508  C CG1   . VAL B 1 189 ? 27.750  -8.688  38.808  1.00 46.95  ? 189 VAL B CG1   1 
ATOM   5509  C CG2   . VAL B 1 189 ? 27.680  -7.309  40.874  1.00 40.26  ? 189 VAL B CG2   1 
ATOM   5510  N N     . VAL B 1 190 ? 24.819  -6.339  40.461  1.00 37.65  ? 190 VAL B N     1 
ATOM   5511  C CA    . VAL B 1 190 ? 24.252  -5.061  40.068  1.00 36.79  ? 190 VAL B CA    1 
ATOM   5512  C C     . VAL B 1 190 ? 25.019  -3.948  40.744  1.00 35.82  ? 190 VAL B C     1 
ATOM   5513  O O     . VAL B 1 190 ? 25.541  -4.106  41.853  1.00 49.05  ? 190 VAL B O     1 
ATOM   5514  C CB    . VAL B 1 190 ? 22.766  -4.883  40.443  1.00 39.78  ? 190 VAL B CB    1 
ATOM   5515  C CG1   . VAL B 1 190 ? 21.852  -5.707  39.582  1.00 41.45  ? 190 VAL B CG1   1 
ATOM   5516  C CG2   . VAL B 1 190 ? 22.493  -5.183  41.902  1.00 44.71  ? 190 VAL B CG2   1 
ATOM   5517  N N     . ARG B 1 191 ? 24.959  -2.796  40.096  1.00 36.06  ? 191 ARG B N     1 
ATOM   5518  C CA    . ARG B 1 191 ? 25.374  -1.534  40.668  1.00 38.20  ? 191 ARG B CA    1 
ATOM   5519  C C     . ARG B 1 191 ? 24.164  -0.622  40.718  1.00 39.08  ? 191 ARG B C     1 
ATOM   5520  O O     . ARG B 1 191 ? 23.295  -0.688  39.855  1.00 50.60  ? 191 ARG B O     1 
ATOM   5521  C CB    . ARG B 1 191 ? 26.550  -0.987  39.867  1.00 43.49  ? 191 ARG B CB    1 
ATOM   5522  C CG    . ARG B 1 191 ? 27.798  -1.827  40.093  1.00 42.56  ? 191 ARG B CG    1 
ATOM   5523  C CD    . ARG B 1 191 ? 29.028  -1.402  39.358  1.00 40.64  ? 191 ARG B CD    1 
ATOM   5524  N NE    . ARG B 1 191 ? 30.137  -2.315  39.611  1.00 47.34  ? 191 ARG B NE    1 
ATOM   5525  C CZ    . ARG B 1 191 ? 31.382  -2.109  39.182  1.00 46.32  ? 191 ARG B CZ    1 
ATOM   5526  N NH1   . ARG B 1 191 ? 31.630  -1.124  38.344  1.00 43.08  ? 191 ARG B NH1   1 
ATOM   5527  N NH2   . ARG B 1 191 ? 32.366  -2.895  39.565  1.00 41.71  ? 191 ARG B NH2   1 
ATOM   5528  N N     . THR B 1 192 ? 24.070  0.129   41.811  1.00 36.76  ? 192 THR B N     1 
ATOM   5529  C CA    . THR B 1 192 ? 22.983  1.056   42.032  1.00 39.98  ? 192 THR B CA    1 
ATOM   5530  C C     . THR B 1 192 ? 23.411  2.455   41.626  1.00 34.95  ? 192 THR B C     1 
ATOM   5531  O O     . THR B 1 192 ? 24.603  2.708   41.413  1.00 32.29  ? 192 THR B O     1 
ATOM   5532  C CB    . THR B 1 192 ? 22.571  1.110   43.509  1.00 43.97  ? 192 THR B CB    1 
ATOM   5533  O OG1   . THR B 1 192 ? 23.682  1.553   44.284  1.00 34.69  ? 192 THR B OG1   1 
ATOM   5534  C CG2   . THR B 1 192 ? 22.111  -0.229  44.017  1.00 51.56  ? 192 THR B CG2   1 
ATOM   5535  N N     . GLY B 1 193 ? 22.408  3.331   41.571  1.00 29.96  ? 193 GLY B N     1 
ATOM   5536  C CA    . GLY B 1 193 ? 22.640  4.746   41.363  1.00 32.20  ? 193 GLY B CA    1 
ATOM   5537  C C     . GLY B 1 193 ? 23.293  4.961   40.005  1.00 37.85  ? 193 GLY B C     1 
ATOM   5538  O O     . GLY B 1 193 ? 23.034  4.228   39.076  1.00 34.08  ? 193 GLY B O     1 
ATOM   5539  N N     . MET B 1 194 ? 24.243  5.893   39.970  1.00 47.45  ? 194 MET B N     1 
ATOM   5540  C CA    . MET B 1 194 ? 24.977  6.271   38.779  1.00 43.56  ? 194 MET B CA    1 
ATOM   5541  C C     . MET B 1 194 ? 25.955  5.176   38.368  1.00 38.88  ? 194 MET B C     1 
ATOM   5542  O O     . MET B 1 194 ? 26.438  5.200   37.236  1.00 41.75  ? 194 MET B O     1 
ATOM   5543  C CB    . MET B 1 194 ? 25.758  7.562   39.044  1.00 39.49  ? 194 MET B CB    1 
ATOM   5544  C CG    . MET B 1 194 ? 24.838  8.713   39.396  1.00 39.74  ? 194 MET B CG    1 
ATOM   5545  S SD    . MET B 1 194 ? 23.495  8.990   38.211  1.00 38.47  ? 194 MET B SD    1 
ATOM   5546  C CE    . MET B 1 194 ? 24.402  8.940   36.665  1.00 31.11  ? 194 MET B CE    1 
ATOM   5547  N N     . GLY B 1 195 ? 26.188  4.205   39.260  1.00 40.34  ? 195 GLY B N     1 
ATOM   5548  C CA    . GLY B 1 195 ? 27.050  3.062   38.987  1.00 40.91  ? 195 GLY B CA    1 
ATOM   5549  C C     . GLY B 1 195 ? 26.497  2.114   37.909  1.00 42.35  ? 195 GLY B C     1 
ATOM   5550  O O     . GLY B 1 195 ? 27.225  1.244   37.400  1.00 35.79  ? 195 GLY B O     1 
ATOM   5551  N N     . ALA B 1 196 ? 25.190  2.221   37.612  1.00 37.94  ? 196 ALA B N     1 
ATOM   5552  C CA    . ALA B 1 196 ? 24.581  1.346   36.624  1.00 39.54  ? 196 ALA B CA    1 
ATOM   5553  C C     . ALA B 1 196 ? 24.930  1.843   35.222  1.00 38.22  ? 196 ALA B C     1 
ATOM   5554  O O     . ALA B 1 196 ? 24.796  1.086   34.264  1.00 35.47  ? 196 ALA B O     1 
ATOM   5555  C CB    . ALA B 1 196 ? 23.077  1.235   36.819  1.00 41.24  ? 196 ALA B CB    1 
ATOM   5556  N N     . MET B 1 197 ? 25.342  3.124   35.124  1.00 40.30  ? 197 MET B N     1 
ATOM   5557  C CA    . MET B 1 197 ? 25.790  3.724   33.877  1.00 39.38  ? 197 MET B CA    1 
ATOM   5558  C C     . MET B 1 197 ? 27.290  3.486   33.708  1.00 41.49  ? 197 MET B C     1 
ATOM   5559  O O     . MET B 1 197 ? 28.113  3.965   34.490  1.00 40.95  ? 197 MET B O     1 
ATOM   5560  C CB    . MET B 1 197 ? 25.529  5.234   33.830  1.00 37.88  ? 197 MET B CB    1 
ATOM   5561  C CG    . MET B 1 197 ? 26.347  5.925   32.749  1.00 35.37  ? 197 MET B CG    1 
ATOM   5562  S SD    . MET B 1 197 ? 25.963  7.676   32.502  1.00 44.63  ? 197 MET B SD    1 
ATOM   5563  C CE    . MET B 1 197 ? 24.513  7.445   31.476  1.00 57.53  ? 197 MET B CE    1 
ATOM   5564  N N     . PRO B 1 198 ? 27.705  2.811   32.624  1.00 41.83  ? 198 PRO B N     1 
ATOM   5565  C CA    . PRO B 1 198 ? 29.124  2.593   32.379  1.00 43.65  ? 198 PRO B CA    1 
ATOM   5566  C C     . PRO B 1 198 ? 29.825  3.921   32.078  1.00 44.84  ? 198 PRO B C     1 
ATOM   5567  O O     . PRO B 1 198 ? 29.268  4.806   31.440  1.00 41.30  ? 198 PRO B O     1 
ATOM   5568  C CB    . PRO B 1 198 ? 29.135  1.619   31.186  1.00 44.71  ? 198 PRO B CB    1 
ATOM   5569  C CG    . PRO B 1 198 ? 27.706  1.136   31.015  1.00 41.52  ? 198 PRO B CG    1 
ATOM   5570  C CD    . PRO B 1 198 ? 26.842  2.238   31.582  1.00 41.62  ? 198 PRO B CD    1 
ATOM   5571  N N     . GLY B 1 199 ? 31.047  4.068   32.586  1.00 40.66  ? 199 GLY B N     1 
ATOM   5572  C CA    . GLY B 1 199 ? 31.834  5.258   32.334  1.00 41.80  ? 199 GLY B CA    1 
ATOM   5573  C C     . GLY B 1 199 ? 31.494  6.409   33.277  1.00 44.79  ? 199 GLY B C     1 
ATOM   5574  O O     . GLY B 1 199 ? 32.079  7.486   33.193  1.00 43.63  ? 199 GLY B O     1 
ATOM   5575  N N     . ASN B 1 200 ? 30.537  6.220   34.182  1.00 45.53  ? 200 ASN B N     1 
ATOM   5576  C CA    . ASN B 1 200 ? 30.207  7.311   35.083  1.00 42.42  ? 200 ASN B CA    1 
ATOM   5577  C C     . ASN B 1 200 ? 31.439  7.658   35.927  1.00 39.95  ? 200 ASN B C     1 
ATOM   5578  O O     . ASN B 1 200 ? 32.221  6.762   36.235  1.00 31.68  ? 200 ASN B O     1 
ATOM   5579  C CB    . ASN B 1 200 ? 29.047  6.942   36.001  1.00 37.05  ? 200 ASN B CB    1 
ATOM   5580  C CG    . ASN B 1 200 ? 29.500  6.008   37.091  1.00 37.54  ? 200 ASN B CG    1 
ATOM   5581  O OD1   . ASN B 1 200 ? 30.085  6.460   38.085  1.00 43.54  ? 200 ASN B OD1   1 
ATOM   5582  N ND2   . ASN B 1 200 ? 29.245  4.709   36.905  1.00 38.66  ? 200 ASN B ND2   1 
ATOM   5583  N N     . ASN B 1 201 ? 31.575  8.951   36.298  1.00 38.27  ? 201 ASN B N     1 
ATOM   5584  C CA    . ASN B 1 201 ? 32.436  9.373   37.389  1.00 37.74  ? 201 ASN B CA    1 
ATOM   5585  C C     . ASN B 1 201 ? 31.632  9.851   38.591  1.00 35.27  ? 201 ASN B C     1 
ATOM   5586  O O     . ASN B 1 201 ? 32.160  10.644  39.353  1.00 41.17  ? 201 ASN B O     1 
ATOM   5587  C CB    . ASN B 1 201 ? 33.420  10.448  36.931  1.00 39.99  ? 201 ASN B CB    1 
ATOM   5588  C CG    . ASN B 1 201 ? 34.455  9.837   36.019  1.00 39.51  ? 201 ASN B CG    1 
ATOM   5589  O OD1   . ASN B 1 201 ? 34.409  10.036  34.811  1.00 43.80  ? 201 ASN B OD1   1 
ATOM   5590  N ND2   . ASN B 1 201 ? 35.280  8.965   36.571  1.00 40.43  ? 201 ASN B ND2   1 
ATOM   5591  N N     . THR B 1 202 ? 30.376  9.391   38.738  1.00 34.69  ? 202 THR B N     1 
ATOM   5592  C CA    . THR B 1 202 ? 29.421  10.000  39.655  1.00 34.02  ? 202 THR B CA    1 
ATOM   5593  C C     . THR B 1 202 ? 28.723  8.987   40.577  1.00 30.37  ? 202 THR B C     1 
ATOM   5594  O O     . THR B 1 202 ? 27.698  9.315   41.157  1.00 28.76  ? 202 THR B O     1 
ATOM   5595  C CB    . THR B 1 202 ? 28.306  10.753  38.894  1.00 37.24  ? 202 THR B CB    1 
ATOM   5596  O OG1   . THR B 1 202 ? 27.581  9.826   38.103  1.00 30.16  ? 202 THR B OG1   1 
ATOM   5597  C CG2   . THR B 1 202 ? 28.805  11.882  38.027  1.00 38.92  ? 202 THR B CG2   1 
ATOM   5598  N N     . TRP B 1 203 ? 29.210  7.741   40.684  1.00 33.04  ? 203 TRP B N     1 
ATOM   5599  C CA    . TRP B 1 203 ? 28.607  6.740   41.565  1.00 33.79  ? 203 TRP B CA    1 
ATOM   5600  C C     . TRP B 1 203 ? 28.444  7.266   42.992  1.00 34.76  ? 203 TRP B C     1 
ATOM   5601  O O     . TRP B 1 203 ? 27.430  7.012   43.613  1.00 43.14  ? 203 TRP B O     1 
ATOM   5602  C CB    . TRP B 1 203 ? 29.491  5.506   41.596  1.00 32.52  ? 203 TRP B CB    1 
ATOM   5603  C CG    . TRP B 1 203 ? 28.831  4.206   41.914  1.00 29.26  ? 203 TRP B CG    1 
ATOM   5604  C CD1   . TRP B 1 203 ? 27.519  3.930   42.176  1.00 28.93  ? 203 TRP B CD1   1 
ATOM   5605  C CD2   . TRP B 1 203 ? 29.530  2.959   41.985  1.00 23.96  ? 203 TRP B CD2   1 
ATOM   5606  N NE1   . TRP B 1 203 ? 27.356  2.580   42.374  1.00 26.91  ? 203 TRP B NE1   1 
ATOM   5607  C CE2   . TRP B 1 203 ? 28.575  1.970   42.249  1.00 23.98  ? 203 TRP B CE2   1 
ATOM   5608  C CE3   . TRP B 1 203 ? 30.872  2.613   41.845  1.00 25.55  ? 203 TRP B CE3   1 
ATOM   5609  C CZ2   . TRP B 1 203 ? 28.930  0.636   42.348  1.00 29.73  ? 203 TRP B CZ2   1 
ATOM   5610  C CZ3   . TRP B 1 203 ? 31.233  1.299   41.994  1.00 24.98  ? 203 TRP B CZ3   1 
ATOM   5611  C CH2   . TRP B 1 203 ? 30.278  0.327   42.248  1.00 27.54  ? 203 TRP B CH2   1 
ATOM   5612  N N     . GLN B 1 204 ? 29.447  7.999   43.481  1.00 34.46  ? 204 GLN B N     1 
ATOM   5613  C CA    . GLN B 1 204 ? 29.540  8.452   44.869  1.00 33.85  ? 204 GLN B CA    1 
ATOM   5614  C C     . GLN B 1 204 ? 29.175  9.939   44.980  1.00 38.20  ? 204 GLN B C     1 
ATOM   5615  O O     . GLN B 1 204 ? 29.415  10.555  46.041  1.00 31.21  ? 204 GLN B O     1 
ATOM   5616  C CB    . GLN B 1 204 ? 30.977  8.282   45.400  1.00 29.88  ? 204 GLN B CB    1 
ATOM   5617  C CG    . GLN B 1 204 ? 31.302  6.908   45.964  1.00 30.26  ? 204 GLN B CG    1 
ATOM   5618  C CD    . GLN B 1 204 ? 31.208  5.787   44.965  1.00 29.51  ? 204 GLN B CD    1 
ATOM   5619  O OE1   . GLN B 1 204 ? 32.090  5.602   44.134  1.00 38.25  ? 204 GLN B OE1   1 
ATOM   5620  N NE2   . GLN B 1 204 ? 30.105  5.062   44.989  1.00 30.27  ? 204 GLN B NE2   1 
ATOM   5621  N N     . LEU B 1 205 ? 28.609  10.533  43.904  1.00 32.15  ? 205 LEU B N     1 
ATOM   5622  C CA    . LEU B 1 205 ? 28.210  11.923  44.028  1.00 32.05  ? 205 LEU B CA    1 
ATOM   5623  C C     . LEU B 1 205 ? 26.688  12.124  43.975  1.00 32.53  ? 205 LEU B C     1 
ATOM   5624  O O     . LEU B 1 205 ? 26.219  13.247  44.122  1.00 34.02  ? 205 LEU B O     1 
ATOM   5625  C CB    . LEU B 1 205 ? 28.887  12.741  42.928  1.00 35.58  ? 205 LEU B CB    1 
ATOM   5626  C CG    . LEU B 1 205 ? 30.401  12.649  42.775  1.00 38.30  ? 205 LEU B CG    1 
ATOM   5627  C CD1   . LEU B 1 205 ? 30.808  13.317  41.469  1.00 41.81  ? 205 LEU B CD1   1 
ATOM   5628  C CD2   . LEU B 1 205 ? 31.160  13.283  43.921  1.00 36.62  ? 205 LEU B CD2   1 
ATOM   5629  N N     . PHE B 1 206 ? 25.889  11.093  43.715  1.00 34.80  ? 206 PHE B N     1 
ATOM   5630  C CA    . PHE B 1 206 ? 24.456  11.316  43.525  1.00 34.84  ? 206 PHE B CA    1 
ATOM   5631  C C     . PHE B 1 206 ? 23.762  9.991   43.784  1.00 37.31  ? 206 PHE B C     1 
ATOM   5632  O O     . PHE B 1 206 ? 24.047  8.987   43.127  1.00 36.05  ? 206 PHE B O     1 
ATOM   5633  C CB    . PHE B 1 206 ? 24.156  11.844  42.117  1.00 39.11  ? 206 PHE B CB    1 
ATOM   5634  C CG    . PHE B 1 206 ? 22.706  12.122  41.795  1.00 37.24  ? 206 PHE B CG    1 
ATOM   5635  C CD1   . PHE B 1 206 ? 22.063  13.237  42.309  1.00 37.37  ? 206 PHE B CD1   1 
ATOM   5636  C CD2   . PHE B 1 206 ? 21.984  11.293  40.945  1.00 38.30  ? 206 PHE B CD2   1 
ATOM   5637  C CE1   . PHE B 1 206 ? 20.725  13.485  42.033  1.00 36.99  ? 206 PHE B CE1   1 
ATOM   5638  C CE2   . PHE B 1 206 ? 20.638  11.535  40.672  1.00 33.46  ? 206 PHE B CE2   1 
ATOM   5639  C CZ    . PHE B 1 206 ? 20.017  12.645  41.199  1.00 36.40  ? 206 PHE B CZ    1 
ATOM   5640  N N     . LYS B 1 207 ? 22.917  9.974   44.811  1.00 38.68  ? 207 LYS B N     1 
ATOM   5641  C CA    . LYS B 1 207 ? 22.382  8.707   45.280  1.00 41.68  ? 207 LYS B CA    1 
ATOM   5642  C C     . LYS B 1 207 ? 21.430  8.127   44.237  1.00 37.02  ? 207 LYS B C     1 
ATOM   5643  O O     . LYS B 1 207 ? 21.439  6.930   44.006  1.00 40.58  ? 207 LYS B O     1 
ATOM   5644  C CB    . LYS B 1 207 ? 21.579  8.863   46.582  1.00 42.84  ? 207 LYS B CB    1 
ATOM   5645  C CG    . LYS B 1 207 ? 22.374  9.168   47.844  1.00 41.81  ? 207 LYS B CG    1 
ATOM   5646  C CD    . LYS B 1 207 ? 21.509  9.703   48.972  1.00 39.61  ? 207 LYS B CD    1 
ATOM   5647  C CE    . LYS B 1 207 ? 22.155  9.652   50.338  1.00 36.76  ? 207 LYS B CE    1 
ATOM   5648  N NZ    . LYS B 1 207 ? 22.002  8.307   50.935  1.00 39.73  ? 207 LYS B NZ    1 
ATOM   5649  N N     . TYR B 1 208 ? 20.527  8.934   43.688  1.00 32.07  ? 208 TYR B N     1 
ATOM   5650  C CA    . TYR B 1 208 ? 19.336  8.340   43.079  1.00 38.42  ? 208 TYR B CA    1 
ATOM   5651  C C     . TYR B 1 208 ? 19.654  7.498   41.840  1.00 41.46  ? 208 TYR B C     1 
ATOM   5652  O O     . TYR B 1 208 ? 19.165  6.373   41.703  1.00 40.05  ? 208 TYR B O     1 
ATOM   5653  C CB    . TYR B 1 208 ? 18.257  9.380   42.759  1.00 34.48  ? 208 TYR B CB    1 
ATOM   5654  C CG    . TYR B 1 208 ? 17.693  10.065  43.978  1.00 38.94  ? 208 TYR B CG    1 
ATOM   5655  C CD1   . TYR B 1 208 ? 17.416  9.379   45.154  1.00 39.25  ? 208 TYR B CD1   1 
ATOM   5656  C CD2   . TYR B 1 208 ? 17.523  11.441  43.989  1.00 41.26  ? 208 TYR B CD2   1 
ATOM   5657  C CE1   . TYR B 1 208 ? 16.956  10.038  46.296  1.00 41.39  ? 208 TYR B CE1   1 
ATOM   5658  C CE2   . TYR B 1 208 ? 17.080  12.109  45.117  1.00 38.82  ? 208 TYR B CE2   1 
ATOM   5659  C CZ    . TYR B 1 208 ? 16.777  11.413  46.271  1.00 40.74  ? 208 TYR B CZ    1 
ATOM   5660  O OH    . TYR B 1 208 ? 16.295  12.155  47.336  1.00 44.30  ? 208 TYR B OH    1 
ATOM   5661  N N     . GLY B 1 209 ? 20.476  8.034   40.937  1.00 40.45  ? 209 GLY B N     1 
ATOM   5662  C CA    . GLY B 1 209 ? 20.454  7.567   39.564  1.00 38.29  ? 209 GLY B CA    1 
ATOM   5663  C C     . GLY B 1 209 ? 19.088  7.845   38.967  1.00 37.49  ? 209 GLY B C     1 
ATOM   5664  O O     . GLY B 1 209 ? 18.567  8.966   39.038  1.00 40.69  ? 209 GLY B O     1 
ATOM   5665  N N     . TYR B 1 210 ? 18.480  6.793   38.440  1.00 38.36  ? 210 TYR B N     1 
ATOM   5666  C CA    . TYR B 1 210 ? 17.258  6.957   37.685  1.00 37.55  ? 210 TYR B CA    1 
ATOM   5667  C C     . TYR B 1 210 ? 16.341  5.835   38.107  1.00 34.87  ? 210 TYR B C     1 
ATOM   5668  O O     . TYR B 1 210 ? 16.826  4.731   38.312  1.00 32.88  ? 210 TYR B O     1 
ATOM   5669  C CB    . TYR B 1 210 ? 17.543  6.936   36.175  1.00 42.67  ? 210 TYR B CB    1 
ATOM   5670  C CG    . TYR B 1 210 ? 16.291  6.904   35.337  1.00 43.75  ? 210 TYR B CG    1 
ATOM   5671  C CD1   . TYR B 1 210 ? 15.355  7.914   35.437  1.00 43.34  ? 210 TYR B CD1   1 
ATOM   5672  C CD2   . TYR B 1 210 ? 15.989  5.825   34.530  1.00 47.46  ? 210 TYR B CD2   1 
ATOM   5673  C CE1   . TYR B 1 210 ? 14.164  7.869   34.738  1.00 40.75  ? 210 TYR B CE1   1 
ATOM   5674  C CE2   . TYR B 1 210 ? 14.815  5.779   33.800  1.00 48.42  ? 210 TYR B CE2   1 
ATOM   5675  C CZ    . TYR B 1 210 ? 13.913  6.817   33.893  1.00 40.43  ? 210 TYR B CZ    1 
ATOM   5676  O OH    . TYR B 1 210 ? 12.776  6.813   33.155  1.00 48.32  ? 210 TYR B OH    1 
ATOM   5677  N N     . GLY B 1 211 ? 15.054  6.167   38.267  1.00 33.92  ? 211 GLY B N     1 
ATOM   5678  C CA    . GLY B 1 211 ? 14.025  5.210   38.611  1.00 37.01  ? 211 GLY B CA    1 
ATOM   5679  C C     . GLY B 1 211 ? 14.031  4.868   40.105  1.00 44.22  ? 211 GLY B C     1 
ATOM   5680  O O     . GLY B 1 211 ? 14.584  5.617   40.905  1.00 49.13  ? 211 GLY B O     1 
ATOM   5681  N N     . PRO B 1 212 ? 13.486  3.692   40.483  1.00 43.82  ? 212 PRO B N     1 
ATOM   5682  C CA    . PRO B 1 212 ? 13.285  3.339   41.883  1.00 46.18  ? 212 PRO B CA    1 
ATOM   5683  C C     . PRO B 1 212 ? 14.595  3.350   42.681  1.00 47.92  ? 212 PRO B C     1 
ATOM   5684  O O     . PRO B 1 212 ? 15.644  2.900   42.186  1.00 38.50  ? 212 PRO B O     1 
ATOM   5685  C CB    . PRO B 1 212 ? 12.670  1.913   41.834  1.00 52.49  ? 212 PRO B CB    1 
ATOM   5686  C CG    . PRO B 1 212 ? 12.253  1.658   40.403  1.00 50.12  ? 212 PRO B CG    1 
ATOM   5687  C CD    . PRO B 1 212 ? 13.069  2.616   39.559  1.00 46.60  ? 212 PRO B CD    1 
ATOM   5688  N N     . TYR B 1 213 ? 14.513  3.904   43.906  1.00 42.84  ? 213 TYR B N     1 
ATOM   5689  C CA    . TYR B 1 213 ? 15.665  4.058   44.786  1.00 41.86  ? 213 TYR B CA    1 
ATOM   5690  C C     . TYR B 1 213 ? 15.717  2.843   45.696  1.00 40.04  ? 213 TYR B C     1 
ATOM   5691  O O     . TYR B 1 213 ? 14.871  2.707   46.573  1.00 42.04  ? 213 TYR B O     1 
ATOM   5692  C CB    . TYR B 1 213 ? 15.577  5.339   45.612  1.00 40.38  ? 213 TYR B CB    1 
ATOM   5693  C CG    . TYR B 1 213 ? 16.775  5.601   46.482  1.00 48.47  ? 213 TYR B CG    1 
ATOM   5694  C CD1   . TYR B 1 213 ? 18.062  5.346   46.018  1.00 45.79  ? 213 TYR B CD1   1 
ATOM   5695  C CD2   . TYR B 1 213 ? 16.640  6.132   47.764  1.00 53.37  ? 213 TYR B CD2   1 
ATOM   5696  C CE1   . TYR B 1 213 ? 19.177  5.575   46.815  1.00 48.85  ? 213 TYR B CE1   1 
ATOM   5697  C CE2   . TYR B 1 213 ? 17.748  6.383   48.567  1.00 52.83  ? 213 TYR B CE2   1 
ATOM   5698  C CZ    . TYR B 1 213 ? 19.020  6.102   48.092  1.00 53.02  ? 213 TYR B CZ    1 
ATOM   5699  O OH    . TYR B 1 213 ? 20.133  6.322   48.856  1.00 54.24  ? 213 TYR B OH    1 
ATOM   5700  N N     . VAL B 1 214 ? 16.713  1.980   45.463  1.00 39.74  ? 214 VAL B N     1 
ATOM   5701  C CA    . VAL B 1 214 ? 16.715  0.625   45.984  1.00 38.33  ? 214 VAL B CA    1 
ATOM   5702  C C     . VAL B 1 214 ? 17.896  0.393   46.934  1.00 39.02  ? 214 VAL B C     1 
ATOM   5703  O O     . VAL B 1 214 ? 18.110  -0.751  47.345  1.00 37.37  ? 214 VAL B O     1 
ATOM   5704  C CB    . VAL B 1 214 ? 16.782  -0.412  44.847  1.00 39.78  ? 214 VAL B CB    1 
ATOM   5705  C CG1   . VAL B 1 214 ? 15.620  -0.317  43.875  1.00 47.52  ? 214 VAL B CG1   1 
ATOM   5706  C CG2   . VAL B 1 214 ? 18.085  -0.318  44.087  1.00 38.65  ? 214 VAL B CG2   1 
ATOM   5707  N N     . ASP B 1 215 ? 18.742  1.399   47.211  1.00 37.27  ? 215 ASP B N     1 
ATOM   5708  C CA    . ASP B 1 215 ? 19.914  1.095   48.028  1.00 44.13  ? 215 ASP B CA    1 
ATOM   5709  C C     . ASP B 1 215 ? 19.459  0.599   49.397  1.00 42.56  ? 215 ASP B C     1 
ATOM   5710  O O     . ASP B 1 215 ? 20.000  -0.385  49.899  1.00 51.39  ? 215 ASP B O     1 
ATOM   5711  C CB    . ASP B 1 215 ? 20.891  2.258   48.154  1.00 45.78  ? 215 ASP B CB    1 
ATOM   5712  C CG    . ASP B 1 215 ? 21.588  2.546   46.839  1.00 45.25  ? 215 ASP B CG    1 
ATOM   5713  O OD1   . ASP B 1 215 ? 20.845  2.828   45.875  1.00 43.81  ? 215 ASP B OD1   1 
ATOM   5714  O OD2   . ASP B 1 215 ? 22.864  2.490   46.804  1.00 39.07  ? 215 ASP B OD2   1 
ATOM   5715  N N     . GLY B 1 216 ? 18.387  1.215   49.910  1.00 40.00  ? 216 GLY B N     1 
ATOM   5716  C CA    . GLY B 1 216 ? 17.853  0.931   51.233  1.00 37.83  ? 216 GLY B CA    1 
ATOM   5717  C C     . GLY B 1 216 ? 17.468  -0.532  51.395  1.00 38.19  ? 216 GLY B C     1 
ATOM   5718  O O     . GLY B 1 216 ? 17.589  -1.087  52.478  1.00 44.45  ? 216 GLY B O     1 
ATOM   5719  N N     . ILE B 1 217 ? 17.056  -1.182  50.313  1.00 36.51  ? 217 ILE B N     1 
ATOM   5720  C CA    . ILE B 1 217 ? 16.506  -2.518  50.470  1.00 40.51  ? 217 ILE B CA    1 
ATOM   5721  C C     . ILE B 1 217 ? 17.612  -3.507  50.807  1.00 38.28  ? 217 ILE B C     1 
ATOM   5722  O O     . ILE B 1 217 ? 17.287  -4.599  51.258  1.00 42.54  ? 217 ILE B O     1 
ATOM   5723  C CB    . ILE B 1 217 ? 15.648  -3.019  49.281  1.00 40.81  ? 217 ILE B CB    1 
ATOM   5724  C CG1   . ILE B 1 217 ? 16.466  -3.456  48.059  1.00 37.96  ? 217 ILE B CG1   1 
ATOM   5725  C CG2   . ILE B 1 217 ? 14.587  -2.006  48.897  1.00 45.35  ? 217 ILE B CG2   1 
ATOM   5726  C CD1   . ILE B 1 217 ? 15.603  -4.124  46.998  1.00 33.97  ? 217 ILE B CD1   1 
ATOM   5727  N N     . PHE B 1 218 ? 18.890  -3.140  50.623  1.00 46.39  ? 218 PHE B N     1 
ATOM   5728  C CA    . PHE B 1 218 ? 19.986  -4.052  50.940  1.00 43.25  ? 218 PHE B CA    1 
ATOM   5729  C C     . PHE B 1 218 ? 20.593  -3.760  52.322  1.00 42.10  ? 218 PHE B C     1 
ATOM   5730  O O     . PHE B 1 218 ? 21.452  -4.516  52.758  1.00 50.41  ? 218 PHE B O     1 
ATOM   5731  C CB    . PHE B 1 218 ? 21.009  -4.050  49.804  1.00 42.12  ? 218 PHE B CB    1 
ATOM   5732  C CG    . PHE B 1 218 ? 20.408  -4.462  48.485  1.00 48.67  ? 218 PHE B CG    1 
ATOM   5733  C CD1   . PHE B 1 218 ? 20.016  -5.769  48.263  1.00 47.65  ? 218 PHE B CD1   1 
ATOM   5734  C CD2   . PHE B 1 218 ? 20.196  -3.535  47.481  1.00 43.34  ? 218 PHE B CD2   1 
ATOM   5735  C CE1   . PHE B 1 218 ? 19.436  -6.137  47.061  1.00 49.12  ? 218 PHE B CE1   1 
ATOM   5736  C CE2   . PHE B 1 218 ? 19.573  -3.901  46.304  1.00 48.10  ? 218 PHE B CE2   1 
ATOM   5737  C CZ    . PHE B 1 218 ? 19.196  -5.202  46.087  1.00 44.60  ? 218 PHE B CZ    1 
ATOM   5738  N N     . SER B 1 219 ? 20.103  -2.730  53.032  1.00 42.95  ? 219 SER B N     1 
ATOM   5739  C CA    . SER B 1 219 ? 20.454  -2.484  54.435  1.00 46.29  ? 219 SER B CA    1 
ATOM   5740  C C     . SER B 1 219 ? 19.477  -3.188  55.370  1.00 43.33  ? 219 SER B C     1 
ATOM   5741  O O     . SER B 1 219 ? 18.300  -3.277  55.049  1.00 45.76  ? 219 SER B O     1 
ATOM   5742  C CB    . SER B 1 219 ? 20.478  -0.994  54.759  1.00 46.39  ? 219 SER B CB    1 
ATOM   5743  O OG    . SER B 1 219 ? 19.161  -0.462  54.894  1.00 43.23  ? 219 SER B OG    1 
ATOM   5744  N N     . GLN B 1 220 ? 19.962  -3.562  56.562  1.00 44.93  ? 220 GLN B N     1 
ATOM   5745  C CA    . GLN B 1 220 ? 19.279  -4.453  57.489  1.00 41.11  ? 220 GLN B CA    1 
ATOM   5746  C C     . GLN B 1 220 ? 18.413  -5.459  56.741  1.00 48.89  ? 220 GLN B C     1 
ATOM   5747  O O     . GLN B 1 220 ? 17.207  -5.534  57.001  1.00 45.44  ? 220 GLN B O     1 
ATOM   5748  C CB    . GLN B 1 220 ? 18.421  -3.660  58.462  1.00 46.74  ? 220 GLN B CB    1 
ATOM   5749  C CG    . GLN B 1 220 ? 19.152  -3.267  59.726  1.00 54.73  ? 220 GLN B CG    1 
ATOM   5750  C CD    . GLN B 1 220 ? 18.297  -2.516  60.717  1.00 53.84  ? 220 GLN B CD    1 
ATOM   5751  O OE1   . GLN B 1 220 ? 17.077  -2.372  60.578  1.00 48.26  ? 220 GLN B OE1   1 
ATOM   5752  N NE2   . GLN B 1 220 ? 18.975  -2.013  61.732  1.00 49.86  ? 220 GLN B NE2   1 
ATOM   5753  N N     . SER B 1 221 ? 19.019  -6.230  55.811  1.00 49.44  ? 221 SER B N     1 
ATOM   5754  C CA    . SER B 1 221 ? 18.218  -7.124  54.991  1.00 45.63  ? 221 SER B CA    1 
ATOM   5755  C C     . SER B 1 221 ? 18.990  -8.368  54.598  1.00 40.22  ? 221 SER B C     1 
ATOM   5756  O O     . SER B 1 221 ? 20.183  -8.496  54.841  1.00 45.27  ? 221 SER B O     1 
ATOM   5757  C CB    . SER B 1 221 ? 17.664  -6.445  53.765  1.00 49.23  ? 221 SER B CB    1 
ATOM   5758  O OG    . SER B 1 221 ? 18.416  -6.763  52.611  1.00 59.31  ? 221 SER B OG    1 
ATOM   5759  N N     . ASN B 1 222 ? 18.247  -9.283  53.983  1.00 39.96  ? 222 ASN B N     1 
ATOM   5760  C CA    . ASN B 1 222 ? 18.826  -10.476 53.394  1.00 45.68  ? 222 ASN B CA    1 
ATOM   5761  C C     . ASN B 1 222 ? 18.461  -10.535 51.903  1.00 45.92  ? 222 ASN B C     1 
ATOM   5762  O O     . ASN B 1 222 ? 18.355  -11.626 51.349  1.00 40.30  ? 222 ASN B O     1 
ATOM   5763  C CB    . ASN B 1 222 ? 18.397  -11.728 54.159  1.00 41.79  ? 222 ASN B CB    1 
ATOM   5764  C CG    . ASN B 1 222 ? 16.899  -11.849 54.341  1.00 44.33  ? 222 ASN B CG    1 
ATOM   5765  O OD1   . ASN B 1 222 ? 16.110  -11.192 53.663  1.00 45.92  ? 222 ASN B OD1   1 
ATOM   5766  N ND2   . ASN B 1 222 ? 16.502  -12.719 55.252  1.00 48.01  ? 222 ASN B ND2   1 
ATOM   5767  N N     . PHE B 1 223 ? 18.304  -9.350  51.281  1.00 42.48  ? 223 PHE B N     1 
ATOM   5768  C CA    . PHE B 1 223 ? 17.939  -9.213  49.877  1.00 42.00  ? 223 PHE B CA    1 
ATOM   5769  C C     . PHE B 1 223 ? 19.155  -9.268  48.935  1.00 42.84  ? 223 PHE B C     1 
ATOM   5770  O O     . PHE B 1 223 ? 18.992  -9.431  47.730  1.00 35.20  ? 223 PHE B O     1 
ATOM   5771  C CB    . PHE B 1 223 ? 17.162  -7.911  49.720  1.00 42.00  ? 223 PHE B CB    1 
ATOM   5772  C CG    . PHE B 1 223 ? 15.773  -7.932  50.314  1.00 39.09  ? 223 PHE B CG    1 
ATOM   5773  C CD1   . PHE B 1 223 ? 15.190  -9.107  50.743  1.00 36.38  ? 223 PHE B CD1   1 
ATOM   5774  C CD2   . PHE B 1 223 ? 15.047  -6.763  50.438  1.00 37.61  ? 223 PHE B CD2   1 
ATOM   5775  C CE1   . PHE B 1 223 ? 13.923  -9.104  51.289  1.00 38.47  ? 223 PHE B CE1   1 
ATOM   5776  C CE2   . PHE B 1 223 ? 13.770  -6.765  50.972  1.00 40.03  ? 223 PHE B CE2   1 
ATOM   5777  C CZ    . PHE B 1 223 ? 13.221  -7.928  51.414  1.00 38.20  ? 223 PHE B CZ    1 
ATOM   5778  N N     . GLY B 1 224 ? 20.374  -9.182  49.492  1.00 39.87  ? 224 GLY B N     1 
ATOM   5779  C CA    . GLY B 1 224 ? 21.595  -9.326  48.728  1.00 36.68  ? 224 GLY B CA    1 
ATOM   5780  C C     . GLY B 1 224 ? 22.853  -9.199  49.585  1.00 37.68  ? 224 GLY B C     1 
ATOM   5781  O O     . GLY B 1 224 ? 22.825  -8.918  50.778  1.00 42.66  ? 224 GLY B O     1 
ATOM   5782  N N     . VAL B 1 225 ? 23.989  -9.343  48.914  1.00 43.48  ? 225 VAL B N     1 
ATOM   5783  C CA    . VAL B 1 225 ? 25.289  -9.248  49.550  1.00 40.10  ? 225 VAL B CA    1 
ATOM   5784  C C     . VAL B 1 225 ? 25.975  -8.023  48.962  1.00 41.28  ? 225 VAL B C     1 
ATOM   5785  O O     . VAL B 1 225 ? 26.260  -7.986  47.776  1.00 39.43  ? 225 VAL B O     1 
ATOM   5786  C CB    . VAL B 1 225 ? 26.104  -10.533 49.310  1.00 41.44  ? 225 VAL B CB    1 
ATOM   5787  C CG1   . VAL B 1 225 ? 27.427  -10.536 50.077  1.00 44.63  ? 225 VAL B CG1   1 
ATOM   5788  C CG2   . VAL B 1 225 ? 25.281  -11.789 49.610  1.00 38.71  ? 225 VAL B CG2   1 
ATOM   5789  N N     . VAL B 1 226 ? 26.269  -7.035  49.804  1.00 37.47  ? 226 VAL B N     1 
ATOM   5790  C CA    . VAL B 1 226 ? 26.940  -5.853  49.328  1.00 33.75  ? 226 VAL B CA    1 
ATOM   5791  C C     . VAL B 1 226 ? 28.443  -6.124  49.223  1.00 35.70  ? 226 VAL B C     1 
ATOM   5792  O O     . VAL B 1 226 ? 29.058  -6.503  50.207  1.00 39.94  ? 226 VAL B O     1 
ATOM   5793  C CB    . VAL B 1 226 ? 26.606  -4.704  50.276  1.00 30.61  ? 226 VAL B CB    1 
ATOM   5794  C CG1   . VAL B 1 226 ? 27.289  -3.429  49.851  1.00 35.63  ? 226 VAL B CG1   1 
ATOM   5795  C CG2   . VAL B 1 226 ? 25.108  -4.495  50.362  1.00 33.42  ? 226 VAL B CG2   1 
ATOM   5796  N N     . THR B 1 227 ? 29.050  -5.866  48.050  1.00 39.92  ? 227 THR B N     1 
ATOM   5797  C CA    . THR B 1 227 ? 30.464  -6.147  47.809  1.00 34.71  ? 227 THR B CA    1 
ATOM   5798  C C     . THR B 1 227 ? 31.268  -4.878  47.600  1.00 33.38  ? 227 THR B C     1 
ATOM   5799  O O     . THR B 1 227 ? 32.491  -4.872  47.743  1.00 39.76  ? 227 THR B O     1 
ATOM   5800  C CB    . THR B 1 227 ? 30.669  -7.025  46.576  1.00 40.32  ? 227 THR B CB    1 
ATOM   5801  O OG1   . THR B 1 227 ? 30.165  -6.315  45.450  1.00 37.81  ? 227 THR B OG1   1 
ATOM   5802  C CG2   . THR B 1 227 ? 29.966  -8.355  46.695  1.00 40.53  ? 227 THR B CG2   1 
ATOM   5803  N N     . LYS B 1 228 ? 30.583  -3.785  47.271  1.00 41.09  ? 228 LYS B N     1 
ATOM   5804  C CA    . LYS B 1 228 ? 31.204  -2.466  47.271  1.00 39.73  ? 228 LYS B CA    1 
ATOM   5805  C C     . LYS B 1 228 ? 30.177  -1.475  47.814  1.00 37.30  ? 228 LYS B C     1 
ATOM   5806  O O     . LYS B 1 228 ? 28.992  -1.675  47.595  1.00 35.88  ? 228 LYS B O     1 
ATOM   5807  C CB    . LYS B 1 228 ? 31.624  -2.035  45.853  1.00 37.59  ? 228 LYS B CB    1 
ATOM   5808  C CG    . LYS B 1 228 ? 32.583  -2.962  45.135  1.00 34.03  ? 228 LYS B CG    1 
ATOM   5809  C CD    . LYS B 1 228 ? 33.042  -2.421  43.797  1.00 38.28  ? 228 LYS B CD    1 
ATOM   5810  C CE    . LYS B 1 228 ? 34.178  -3.229  43.198  1.00 39.87  ? 228 LYS B CE    1 
ATOM   5811  N NZ    . LYS B 1 228 ? 33.837  -4.676  43.098  1.00 43.92  ? 228 LYS B NZ    1 
ATOM   5812  N N     . MET B 1 229 ? 30.651  -0.407  48.472  1.00 36.86  ? 229 MET B N     1 
ATOM   5813  C CA    . MET B 1 229 ? 29.801  0.670   48.933  1.00 37.82  ? 229 MET B CA    1 
ATOM   5814  C C     . MET B 1 229 ? 30.597  1.979   48.943  1.00 35.40  ? 229 MET B C     1 
ATOM   5815  O O     . MET B 1 229 ? 31.731  2.052   49.412  1.00 35.88  ? 229 MET B O     1 
ATOM   5816  C CB    . MET B 1 229 ? 29.282  0.347   50.341  1.00 38.08  ? 229 MET B CB    1 
ATOM   5817  C CG    . MET B 1 229 ? 28.193  1.258   50.842  1.00 37.66  ? 229 MET B CG    1 
ATOM   5818  S SD    . MET B 1 229 ? 27.773  0.977   52.643  1.00 41.59  ? 229 MET B SD    1 
ATOM   5819  C CE    . MET B 1 229 ? 28.698  2.354   53.316  1.00 45.54  ? 229 MET B CE    1 
ATOM   5820  N N     . GLY B 1 230 ? 29.992  3.032   48.398  1.00 37.07  ? 230 GLY B N     1 
ATOM   5821  C CA    . GLY B 1 230 ? 30.480  4.376   48.655  1.00 36.84  ? 230 GLY B CA    1 
ATOM   5822  C C     . GLY B 1 230 ? 29.852  4.992   49.903  1.00 37.15  ? 230 GLY B C     1 
ATOM   5823  O O     . GLY B 1 230 ? 28.668  4.768   50.205  1.00 33.41  ? 230 GLY B O     1 
ATOM   5824  N N     . ILE B 1 231 ? 30.638  5.847   50.558  1.00 37.89  ? 231 ILE B N     1 
ATOM   5825  C CA    . ILE B 1 231 ? 30.151  6.667   51.651  1.00 40.24  ? 231 ILE B CA    1 
ATOM   5826  C C     . ILE B 1 231 ? 30.749  8.075   51.535  1.00 36.77  ? 231 ILE B C     1 
ATOM   5827  O O     . ILE B 1 231 ? 31.905  8.255   51.153  1.00 39.07  ? 231 ILE B O     1 
ATOM   5828  C CB    . ILE B 1 231 ? 30.457  5.943   52.990  1.00 44.04  ? 231 ILE B CB    1 
ATOM   5829  C CG1   . ILE B 1 231 ? 29.813  6.640   54.190  1.00 42.74  ? 231 ILE B CG1   1 
ATOM   5830  C CG2   . ILE B 1 231 ? 31.955  5.763   53.173  1.00 43.57  ? 231 ILE B CG2   1 
ATOM   5831  C CD1   . ILE B 1 231 ? 29.991  5.929   55.493  1.00 40.81  ? 231 ILE B CD1   1 
ATOM   5832  N N     . TRP B 1 232 ? 29.939  9.084   51.871  1.00 38.50  ? 232 TRP B N     1 
ATOM   5833  C CA    . TRP B 1 232 ? 30.369  10.476  51.890  1.00 36.64  ? 232 TRP B CA    1 
ATOM   5834  C C     . TRP B 1 232 ? 31.152  10.749  53.171  1.00 35.18  ? 232 TRP B C     1 
ATOM   5835  O O     . TRP B 1 232 ? 30.901  10.130  54.190  1.00 46.25  ? 232 TRP B O     1 
ATOM   5836  C CB    . TRP B 1 232 ? 29.161  11.407  51.764  1.00 39.09  ? 232 TRP B CB    1 
ATOM   5837  C CG    . TRP B 1 232 ? 28.401  11.340  50.468  1.00 44.04  ? 232 TRP B CG    1 
ATOM   5838  C CD1   . TRP B 1 232 ? 28.903  10.988  49.253  1.00 41.57  ? 232 TRP B CD1   1 
ATOM   5839  C CD2   . TRP B 1 232 ? 27.015  11.691  50.245  1.00 43.71  ? 232 TRP B CD2   1 
ATOM   5840  N NE1   . TRP B 1 232 ? 27.940  11.098  48.301  1.00 48.34  ? 232 TRP B NE1   1 
ATOM   5841  C CE2   . TRP B 1 232 ? 26.769  11.529  48.871  1.00 44.67  ? 232 TRP B CE2   1 
ATOM   5842  C CE3   . TRP B 1 232 ? 25.948  12.105  51.065  1.00 41.81  ? 232 TRP B CE3   1 
ATOM   5843  C CZ2   . TRP B 1 232 ? 25.508  11.754  48.299  1.00 46.06  ? 232 TRP B CZ2   1 
ATOM   5844  C CZ3   . TRP B 1 232 ? 24.713  12.347  50.505  1.00 37.52  ? 232 TRP B CZ3   1 
ATOM   5845  C CH2   . TRP B 1 232 ? 24.491  12.174  49.131  1.00 41.39  ? 232 TRP B CH2   1 
ATOM   5846  N N     . LEU B 1 233 ? 32.088  11.698  53.107  1.00 32.79  ? 233 LEU B N     1 
ATOM   5847  C CA    . LEU B 1 233 ? 33.044  11.970  54.160  1.00 29.07  ? 233 LEU B CA    1 
ATOM   5848  C C     . LEU B 1 233 ? 33.131  13.476  54.375  1.00 31.95  ? 233 LEU B C     1 
ATOM   5849  O O     . LEU B 1 233 ? 33.371  14.241  53.449  1.00 31.26  ? 233 LEU B O     1 
ATOM   5850  C CB    . LEU B 1 233 ? 34.413  11.410  53.767  1.00 35.06  ? 233 LEU B CB    1 
ATOM   5851  C CG    . LEU B 1 233 ? 34.518  9.886   53.610  1.00 39.73  ? 233 LEU B CG    1 
ATOM   5852  C CD1   . LEU B 1 233 ? 35.912  9.472   53.167  1.00 40.55  ? 233 LEU B CD1   1 
ATOM   5853  C CD2   . LEU B 1 233 ? 34.175  9.159   54.885  1.00 35.91  ? 233 LEU B CD2   1 
ATOM   5854  N N     . MET B 1 234 ? 32.892  13.896  55.616  1.00 35.50  ? 234 MET B N     1 
ATOM   5855  C CA    . MET B 1 234 ? 32.949  15.302  55.960  1.00 44.11  ? 234 MET B CA    1 
ATOM   5856  C C     . MET B 1 234 ? 34.334  15.859  55.637  1.00 46.15  ? 234 MET B C     1 
ATOM   5857  O O     . MET B 1 234 ? 35.332  15.327  56.094  1.00 41.79  ? 234 MET B O     1 
ATOM   5858  C CB    . MET B 1 234 ? 32.668  15.502  57.453  1.00 43.95  ? 234 MET B CB    1 
ATOM   5859  C CG    . MET B 1 234 ? 32.363  16.936  57.813  1.00 42.08  ? 234 MET B CG    1 
ATOM   5860  S SD    . MET B 1 234 ? 31.976  17.039  59.574  1.00 48.72  ? 234 MET B SD    1 
ATOM   5861  C CE    . MET B 1 234 ? 32.159  18.805  59.819  1.00 55.90  ? 234 MET B CE    1 
ATOM   5862  N N     . PRO B 1 235 ? 34.434  16.952  54.851  1.00 46.49  ? 235 PRO B N     1 
ATOM   5863  C CA    . PRO B 1 235 ? 35.686  17.684  54.739  1.00 44.29  ? 235 PRO B CA    1 
ATOM   5864  C C     . PRO B 1 235 ? 36.053  18.270  56.098  1.00 47.31  ? 235 PRO B C     1 
ATOM   5865  O O     . PRO B 1 235 ? 35.177  18.653  56.859  1.00 43.94  ? 235 PRO B O     1 
ATOM   5866  C CB    . PRO B 1 235 ? 35.440  18.820  53.733  1.00 39.50  ? 235 PRO B CB    1 
ATOM   5867  C CG    . PRO B 1 235 ? 34.024  18.627  53.228  1.00 41.54  ? 235 PRO B CG    1 
ATOM   5868  C CD    . PRO B 1 235 ? 33.356  17.536  54.043  1.00 40.30  ? 235 PRO B CD    1 
ATOM   5869  N N     . GLU B 1 236 ? 37.362  18.400  56.324  1.00 45.51  ? 236 GLU B N     1 
ATOM   5870  C CA    . GLU B 1 236 ? 37.939  18.942  57.534  1.00 50.65  ? 236 GLU B CA    1 
ATOM   5871  C C     . GLU B 1 236 ? 37.348  20.315  57.848  1.00 56.31  ? 236 GLU B C     1 
ATOM   5872  O O     . GLU B 1 236 ? 37.451  21.249  57.058  1.00 53.57  ? 236 GLU B O     1 
ATOM   5873  C CB    . GLU B 1 236 ? 39.451  19.082  57.337  1.00 60.95  ? 236 GLU B CB    1 
ATOM   5874  C CG    . GLU B 1 236 ? 40.228  19.132  58.631  1.00 64.77  ? 236 GLU B CG    1 
ATOM   5875  C CD    . GLU B 1 236 ? 41.724  18.880  58.512  1.00 64.68  ? 236 GLU B CD    1 
ATOM   5876  O OE1   . GLU B 1 236 ? 42.439  19.574  59.220  1.00 60.14  ? 236 GLU B OE1   1 
ATOM   5877  O OE2   . GLU B 1 236 ? 42.166  17.961  57.756  1.00 62.26  ? 236 GLU B OE2   1 
ATOM   5878  N N     . PRO B 1 237 ? 36.696  20.516  59.011  1.00 51.46  ? 237 PRO B N     1 
ATOM   5879  C CA    . PRO B 1 237 ? 36.193  21.844  59.324  1.00 45.67  ? 237 PRO B CA    1 
ATOM   5880  C C     . PRO B 1 237 ? 37.330  22.761  59.729  1.00 51.80  ? 237 PRO B C     1 
ATOM   5881  O O     . PRO B 1 237 ? 38.435  22.321  60.022  1.00 44.95  ? 237 PRO B O     1 
ATOM   5882  C CB    . PRO B 1 237 ? 35.169  21.597  60.422  1.00 45.43  ? 237 PRO B CB    1 
ATOM   5883  C CG    . PRO B 1 237 ? 35.626  20.308  61.058  1.00 49.87  ? 237 PRO B CG    1 
ATOM   5884  C CD    . PRO B 1 237 ? 36.252  19.488  59.956  1.00 45.38  ? 237 PRO B CD    1 
ATOM   5885  N N     . ALA B 1 238 ? 37.010  24.053  59.698  1.00 58.07  ? 238 ALA B N     1 
ATOM   5886  C CA    . ALA B 1 238 ? 37.961  25.111  59.950  1.00 59.28  ? 238 ALA B CA    1 
ATOM   5887  C C     . ALA B 1 238 ? 38.239  25.238  61.445  1.00 61.84  ? 238 ALA B C     1 
ATOM   5888  O O     . ALA B 1 238 ? 39.169  25.941  61.832  1.00 66.06  ? 238 ALA B O     1 
ATOM   5889  C CB    . ALA B 1 238 ? 37.397  26.390  59.382  1.00 68.99  ? 238 ALA B CB    1 
ATOM   5890  N N     . GLY B 1 239 ? 37.406  24.582  62.263  1.00 61.99  ? 239 GLY B N     1 
ATOM   5891  C CA    . GLY B 1 239 ? 37.522  24.594  63.712  1.00 56.37  ? 239 GLY B CA    1 
ATOM   5892  C C     . GLY B 1 239 ? 36.606  23.555  64.375  1.00 55.10  ? 239 GLY B C     1 
ATOM   5893  O O     . GLY B 1 239 ? 35.570  23.149  63.818  1.00 50.28  ? 239 GLY B O     1 
ATOM   5894  N N     . TYR B 1 240 ? 36.980  23.165  65.598  1.00 48.84  ? 240 TYR B N     1 
ATOM   5895  C CA    . TYR B 1 240 ? 36.291  22.109  66.307  1.00 49.34  ? 240 TYR B CA    1 
ATOM   5896  C C     . TYR B 1 240 ? 36.413  22.338  67.806  1.00 46.81  ? 240 TYR B C     1 
ATOM   5897  O O     . TYR B 1 240 ? 37.524  22.477  68.290  1.00 49.63  ? 240 TYR B O     1 
ATOM   5898  C CB    . TYR B 1 240 ? 36.918  20.783  65.886  1.00 47.71  ? 240 TYR B CB    1 
ATOM   5899  C CG    . TYR B 1 240 ? 36.570  19.601  66.754  1.00 47.09  ? 240 TYR B CG    1 
ATOM   5900  C CD1   . TYR B 1 240 ? 35.278  19.115  66.800  1.00 48.24  ? 240 TYR B CD1   1 
ATOM   5901  C CD2   . TYR B 1 240 ? 37.531  18.964  67.520  1.00 46.88  ? 240 TYR B CD2   1 
ATOM   5902  C CE1   . TYR B 1 240 ? 34.941  18.025  67.584  1.00 50.63  ? 240 TYR B CE1   1 
ATOM   5903  C CE2   . TYR B 1 240 ? 37.213  17.864  68.304  1.00 54.83  ? 240 TYR B CE2   1 
ATOM   5904  C CZ    . TYR B 1 240 ? 35.907  17.407  68.354  1.00 50.99  ? 240 TYR B CZ    1 
ATOM   5905  O OH    . TYR B 1 240 ? 35.559  16.334  69.128  1.00 47.92  ? 240 TYR B OH    1 
ATOM   5906  N N     . ARG B 1 241 ? 35.284  22.333  68.525  1.00 49.91  ? 241 ARG B N     1 
ATOM   5907  C CA    . ARG B 1 241 ? 35.264  22.562  69.968  1.00 52.39  ? 241 ARG B CA    1 
ATOM   5908  C C     . ARG B 1 241 ? 34.285  21.607  70.654  1.00 52.17  ? 241 ARG B C     1 
ATOM   5909  O O     . ARG B 1 241 ? 33.091  21.883  70.744  1.00 50.99  ? 241 ARG B O     1 
ATOM   5910  C CB    . ARG B 1 241 ? 34.818  23.989  70.320  1.00 63.07  ? 241 ARG B CB    1 
ATOM   5911  C CG    . ARG B 1 241 ? 35.924  25.034  70.403  1.00 73.15  ? 241 ARG B CG    1 
ATOM   5912  C CD    . ARG B 1 241 ? 35.599  26.193  71.357  1.00 86.71  ? 241 ARG B CD    1 
ATOM   5913  N NE    . ARG B 1 241 ? 34.978  27.378  70.752  1.00 89.33  ? 241 ARG B NE    1 
ATOM   5914  C CZ    . ARG B 1 241 ? 35.619  28.296  70.021  1.00 96.05  ? 241 ARG B CZ    1 
ATOM   5915  N NH1   . ARG B 1 241 ? 36.923  28.211  69.815  1.00 93.82  ? 241 ARG B NH1   1 
ATOM   5916  N NH2   . ARG B 1 241 ? 34.956  29.313  69.497  1.00 98.67  ? 241 ARG B NH2   1 
ATOM   5917  N N     . PRO B 1 242 ? 34.747  20.480  71.234  1.00 51.09  ? 242 PRO B N     1 
ATOM   5918  C CA    . PRO B 1 242 ? 33.868  19.639  72.050  1.00 50.59  ? 242 PRO B CA    1 
ATOM   5919  C C     . PRO B 1 242 ? 33.530  20.267  73.406  1.00 55.60  ? 242 PRO B C     1 
ATOM   5920  O O     . PRO B 1 242 ? 34.369  20.964  73.969  1.00 55.84  ? 242 PRO B O     1 
ATOM   5921  C CB    . PRO B 1 242 ? 34.716  18.375  72.211  1.00 52.49  ? 242 PRO B CB    1 
ATOM   5922  C CG    . PRO B 1 242 ? 36.148  18.873  72.167  1.00 50.62  ? 242 PRO B CG    1 
ATOM   5923  C CD    . PRO B 1 242 ? 36.130  19.991  71.159  1.00 47.23  ? 242 PRO B CD    1 
ATOM   5924  N N     . TYR B 1 243 ? 32.307  20.020  73.910  1.00 56.61  ? 243 TYR B N     1 
ATOM   5925  C CA    . TYR B 1 243 ? 31.846  20.531  75.199  1.00 55.40  ? 243 TYR B CA    1 
ATOM   5926  C C     . TYR B 1 243 ? 31.146  19.448  76.003  1.00 55.00  ? 243 TYR B C     1 
ATOM   5927  O O     . TYR B 1 243 ? 30.722  18.447  75.437  1.00 54.24  ? 243 TYR B O     1 
ATOM   5928  C CB    . TYR B 1 243 ? 30.804  21.648  75.071  1.00 60.24  ? 243 TYR B CB    1 
ATOM   5929  C CG    . TYR B 1 243 ? 29.644  21.395  74.135  1.00 61.39  ? 243 TYR B CG    1 
ATOM   5930  C CD1   . TYR B 1 243 ? 29.800  21.560  72.770  1.00 60.37  ? 243 TYR B CD1   1 
ATOM   5931  C CD2   . TYR B 1 243 ? 28.374  21.049  74.588  1.00 63.67  ? 243 TYR B CD2   1 
ATOM   5932  C CE1   . TYR B 1 243 ? 28.752  21.363  71.880  1.00 63.68  ? 243 TYR B CE1   1 
ATOM   5933  C CE2   . TYR B 1 243 ? 27.310  20.853  73.706  1.00 58.08  ? 243 TYR B CE2   1 
ATOM   5934  C CZ    . TYR B 1 243 ? 27.500  21.006  72.340  1.00 58.23  ? 243 TYR B CZ    1 
ATOM   5935  O OH    . TYR B 1 243 ? 26.550  20.814  71.358  1.00 56.83  ? 243 TYR B OH    1 
ATOM   5936  N N     . LEU B 1 244 ? 31.042  19.664  77.325  1.00 56.24  ? 244 LEU B N     1 
ATOM   5937  C CA    . LEU B 1 244 ? 30.238  18.803  78.181  1.00 56.69  ? 244 LEU B CA    1 
ATOM   5938  C C     . LEU B 1 244 ? 29.402  19.654  79.129  1.00 53.76  ? 244 LEU B C     1 
ATOM   5939  O O     . LEU B 1 244 ? 29.919  20.565  79.760  1.00 48.91  ? 244 LEU B O     1 
ATOM   5940  C CB    . LEU B 1 244 ? 31.109  17.812  78.959  1.00 54.59  ? 244 LEU B CB    1 
ATOM   5941  C CG    . LEU B 1 244 ? 30.443  17.112  80.157  1.00 54.22  ? 244 LEU B CG    1 
ATOM   5942  C CD1   . LEU B 1 244 ? 29.487  16.016  79.737  1.00 52.65  ? 244 LEU B CD1   1 
ATOM   5943  C CD2   . LEU B 1 244 ? 31.492  16.516  81.084  1.00 52.82  ? 244 LEU B CD2   1 
ATOM   5944  N N     . ILE B 1 245 ? 28.110  19.313  79.196  1.00 54.54  ? 245 ILE B N     1 
ATOM   5945  C CA    . ILE B 1 245 ? 27.164  19.920  80.114  1.00 54.40  ? 245 ILE B CA    1 
ATOM   5946  C C     . ILE B 1 245 ? 26.563  18.813  80.986  1.00 59.09  ? 245 ILE B C     1 
ATOM   5947  O O     . ILE B 1 245 ? 26.093  17.800  80.460  1.00 59.14  ? 245 ILE B O     1 
ATOM   5948  C CB    . ILE B 1 245 ? 26.086  20.703  79.335  1.00 52.29  ? 245 ILE B CB    1 
ATOM   5949  C CG1   . ILE B 1 245 ? 26.690  21.500  78.175  1.00 53.51  ? 245 ILE B CG1   1 
ATOM   5950  C CG2   . ILE B 1 245 ? 25.264  21.597  80.255  1.00 51.79  ? 245 ILE B CG2   1 
ATOM   5951  C CD1   . ILE B 1 245 ? 25.670  22.223  77.331  1.00 47.81  ? 245 ILE B CD1   1 
ATOM   5952  N N     . THR B 1 246 ? 26.586  19.035  82.316  1.00 64.28  ? 246 THR B N     1 
ATOM   5953  C CA    . THR B 1 246 ? 26.163  18.066  83.327  1.00 59.44  ? 246 THR B CA    1 
ATOM   5954  C C     . THR B 1 246 ? 24.953  18.599  84.094  1.00 46.11  ? 246 THR B C     1 
ATOM   5955  O O     . THR B 1 246 ? 24.765  19.822  84.261  1.00 41.23  ? 246 THR B O     1 
ATOM   5956  C CB    . THR B 1 246 ? 27.319  17.733  84.291  1.00 62.34  ? 246 THR B CB    1 
ATOM   5957  O OG1   . THR B 1 246 ? 27.784  18.926  84.930  1.00 63.61  ? 246 THR B OG1   1 
ATOM   5958  C CG2   . THR B 1 246 ? 28.495  17.085  83.590  1.00 52.95  ? 246 THR B CG2   1 
ATOM   5959  N N     . PHE B 1 247 ? 24.143  17.653  84.572  1.00 44.20  ? 247 PHE B N     1 
ATOM   5960  C CA    . PHE B 1 247 ? 22.872  17.971  85.231  1.00 49.24  ? 247 PHE B CA    1 
ATOM   5961  C C     . PHE B 1 247 ? 22.760  17.223  86.567  1.00 50.08  ? 247 PHE B C     1 
ATOM   5962  O O     . PHE B 1 247 ? 22.872  16.002  86.610  1.00 49.39  ? 247 PHE B O     1 
ATOM   5963  C CB    . PHE B 1 247 ? 21.718  17.663  84.265  1.00 45.23  ? 247 PHE B CB    1 
ATOM   5964  C CG    . PHE B 1 247 ? 21.781  18.443  82.974  1.00 49.97  ? 247 PHE B CG    1 
ATOM   5965  C CD1   . PHE B 1 247 ? 21.574  19.818  82.961  1.00 52.01  ? 247 PHE B CD1   1 
ATOM   5966  C CD2   . PHE B 1 247 ? 22.143  17.825  81.786  1.00 51.13  ? 247 PHE B CD2   1 
ATOM   5967  C CE1   . PHE B 1 247 ? 21.669  20.536  81.774  1.00 51.16  ? 247 PHE B CE1   1 
ATOM   5968  C CE2   . PHE B 1 247 ? 22.239  18.545  80.604  1.00 49.62  ? 247 PHE B CE2   1 
ATOM   5969  C CZ    . PHE B 1 247 ? 21.983  19.893  80.599  1.00 48.44  ? 247 PHE B CZ    1 
ATOM   5970  N N     . GLU B 1 248 ? 22.521  17.968  87.653  1.00 62.15  ? 248 GLU B N     1 
ATOM   5971  C CA    . GLU B 1 248 ? 22.629  17.497  89.037  1.00 59.52  ? 248 GLU B CA    1 
ATOM   5972  C C     . GLU B 1 248 ? 21.589  16.409  89.340  1.00 56.25  ? 248 GLU B C     1 
ATOM   5973  O O     . GLU B 1 248 ? 21.897  15.360  89.908  1.00 51.30  ? 248 GLU B O     1 
ATOM   5974  C CB    . GLU B 1 248 ? 22.456  18.731  89.934  1.00 69.84  ? 248 GLU B CB    1 
ATOM   5975  C CG    . GLU B 1 248 ? 22.783  18.540  91.409  1.00 92.16  ? 248 GLU B CG    1 
ATOM   5976  C CD    . GLU B 1 248 ? 24.223  18.798  91.833  1.00 99.30  ? 248 GLU B CD    1 
ATOM   5977  O OE1   . GLU B 1 248 ? 24.434  19.021  93.041  1.00 107.70 ? 248 GLU B OE1   1 
ATOM   5978  O OE2   . GLU B 1 248 ? 25.137  18.739  90.973  1.00 91.19  ? 248 GLU B OE2   1 
ATOM   5979  N N     . ASN B 1 249 ? 20.349  16.635  88.894  1.00 56.29  ? 249 ASN B N     1 
ATOM   5980  C CA    . ASN B 1 249 ? 19.194  15.896  89.366  1.00 51.54  ? 249 ASN B CA    1 
ATOM   5981  C C     . ASN B 1 249 ? 18.748  14.951  88.274  1.00 59.04  ? 249 ASN B C     1 
ATOM   5982  O O     . ASN B 1 249 ? 18.810  15.331  87.109  1.00 66.21  ? 249 ASN B O     1 
ATOM   5983  C CB    . ASN B 1 249 ? 18.074  16.864  89.736  1.00 52.91  ? 249 ASN B CB    1 
ATOM   5984  C CG    . ASN B 1 249 ? 18.536  17.825  90.814  1.00 58.45  ? 249 ASN B CG    1 
ATOM   5985  O OD1   . ASN B 1 249 ? 18.616  19.042  90.617  1.00 54.55  ? 249 ASN B OD1   1 
ATOM   5986  N ND2   . ASN B 1 249 ? 18.921  17.265  91.949  1.00 55.08  ? 249 ASN B ND2   1 
ATOM   5987  N N     . GLU B 1 250 ? 18.281  13.759  88.668  1.00 62.01  ? 250 GLU B N     1 
ATOM   5988  C CA    . GLU B 1 250 ? 17.870  12.736  87.718  1.00 65.46  ? 250 GLU B CA    1 
ATOM   5989  C C     . GLU B 1 250 ? 16.626  13.203  86.954  1.00 65.51  ? 250 GLU B C     1 
ATOM   5990  O O     . GLU B 1 250 ? 16.401  12.769  85.826  1.00 72.76  ? 250 GLU B O     1 
ATOM   5991  C CB    . GLU B 1 250 ? 17.677  11.375  88.408  1.00 77.91  ? 250 GLU B CB    1 
ATOM   5992  C CG    . GLU B 1 250 ? 16.398  11.207  89.240  1.00 94.56  ? 250 GLU B CG    1 
ATOM   5993  C CD    . GLU B 1 250 ? 16.189  9.824   89.858  1.00 101.07 ? 250 GLU B CD    1 
ATOM   5994  O OE1   . GLU B 1 250 ? 17.195  9.226   90.298  1.00 109.46 ? 250 GLU B OE1   1 
ATOM   5995  O OE2   . GLU B 1 250 ? 15.021  9.343   89.922  1.00 89.15  ? 250 GLU B OE2   1 
ATOM   5996  N N     . ASP B 1 251 ? 15.825  14.097  87.549  1.00 58.03  ? 251 ASP B N     1 
ATOM   5997  C CA    . ASP B 1 251 ? 14.594  14.556  86.917  1.00 62.91  ? 251 ASP B CA    1 
ATOM   5998  C C     . ASP B 1 251 ? 14.896  15.635  85.862  1.00 63.67  ? 251 ASP B C     1 
ATOM   5999  O O     . ASP B 1 251 ? 14.008  16.003  85.076  1.00 48.06  ? 251 ASP B O     1 
ATOM   6000  C CB    . ASP B 1 251 ? 13.574  15.030  87.965  1.00 63.91  ? 251 ASP B CB    1 
ATOM   6001  C CG    . ASP B 1 251 ? 12.744  13.941  88.656  1.00 68.84  ? 251 ASP B CG    1 
ATOM   6002  O OD1   . ASP B 1 251 ? 13.092  12.740  88.591  1.00 61.69  ? 251 ASP B OD1   1 
ATOM   6003  O OD2   . ASP B 1 251 ? 11.729  14.301  89.261  1.00 74.67  ? 251 ASP B OD2   1 
ATOM   6004  N N     . ASP B 1 252 ? 16.160  16.107  85.824  1.00 59.47  ? 252 ASP B N     1 
ATOM   6005  C CA    . ASP B 1 252 ? 16.600  17.175  84.931  1.00 56.24  ? 252 ASP B CA    1 
ATOM   6006  C C     . ASP B 1 252 ? 16.364  16.800  83.466  1.00 48.31  ? 252 ASP B C     1 
ATOM   6007  O O     . ASP B 1 252 ? 16.156  17.660  82.611  1.00 40.28  ? 252 ASP B O     1 
ATOM   6008  C CB    . ASP B 1 252 ? 18.075  17.519  85.172  1.00 54.88  ? 252 ASP B CB    1 
ATOM   6009  C CG    . ASP B 1 252 ? 18.267  18.475  86.328  1.00 55.89  ? 252 ASP B CG    1 
ATOM   6010  O OD1   . ASP B 1 252 ? 17.219  18.954  86.822  1.00 55.94  ? 252 ASP B OD1   1 
ATOM   6011  O OD2   . ASP B 1 252 ? 19.458  18.770  86.697  1.00 61.78  ? 252 ASP B OD2   1 
ATOM   6012  N N     . ILE B 1 253 ? 16.329  15.502  83.203  1.00 44.84  ? 253 ILE B N     1 
ATOM   6013  C CA    . ILE B 1 253 ? 16.302  15.005  81.850  1.00 54.05  ? 253 ILE B CA    1 
ATOM   6014  C C     . ILE B 1 253 ? 15.055  15.487  81.106  1.00 64.36  ? 253 ILE B C     1 
ATOM   6015  O O     . ILE B 1 253 ? 15.080  15.586  79.877  1.00 68.19  ? 253 ILE B O     1 
ATOM   6016  C CB    . ILE B 1 253 ? 16.439  13.468  81.867  1.00 58.06  ? 253 ILE B CB    1 
ATOM   6017  C CG1   . ILE B 1 253 ? 16.864  12.954  80.500  1.00 62.99  ? 253 ILE B CG1   1 
ATOM   6018  C CG2   . ILE B 1 253 ? 15.176  12.769  82.333  1.00 65.00  ? 253 ILE B CG2   1 
ATOM   6019  C CD1   . ILE B 1 253 ? 18.066  13.685  79.917  1.00 67.54  ? 253 ILE B CD1   1 
ATOM   6020  N N     . GLU B 1 254 ? 13.970  15.763  81.842  1.00 67.89  ? 254 GLU B N     1 
ATOM   6021  C CA    . GLU B 1 254 ? 12.702  16.154  81.244  1.00 63.18  ? 254 GLU B CA    1 
ATOM   6022  C C     . GLU B 1 254 ? 12.865  17.499  80.547  1.00 53.09  ? 254 GLU B C     1 
ATOM   6023  O O     . GLU B 1 254 ? 12.706  17.608  79.330  1.00 50.35  ? 254 GLU B O     1 
ATOM   6024  C CB    . GLU B 1 254 ? 11.609  16.204  82.311  1.00 75.58  ? 254 GLU B CB    1 
ATOM   6025  C CG    . GLU B 1 254 ? 10.319  16.885  81.864  1.00 81.66  ? 254 GLU B CG    1 
ATOM   6026  C CD    . GLU B 1 254 ? 9.086   16.519  82.681  1.00 79.01  ? 254 GLU B CD    1 
ATOM   6027  O OE1   . GLU B 1 254 ? 9.234   15.754  83.659  1.00 78.85  ? 254 GLU B OE1   1 
ATOM   6028  O OE2   . GLU B 1 254 ? 7.976   16.962  82.316  1.00 64.36  ? 254 GLU B OE2   1 
ATOM   6029  N N     . THR B 1 255 ? 13.202  18.522  81.323  1.00 46.04  ? 255 THR B N     1 
ATOM   6030  C CA    . THR B 1 255 ? 13.341  19.848  80.758  1.00 49.40  ? 255 THR B CA    1 
ATOM   6031  C C     . THR B 1 255 ? 14.531  19.907  79.788  1.00 59.82  ? 255 THR B C     1 
ATOM   6032  O O     . THR B 1 255 ? 14.553  20.757  78.896  1.00 65.47  ? 255 THR B O     1 
ATOM   6033  C CB    . THR B 1 255 ? 13.479  20.899  81.864  1.00 50.05  ? 255 THR B CB    1 
ATOM   6034  O OG1   . THR B 1 255 ? 13.545  22.201  81.274  1.00 50.06  ? 255 THR B OG1   1 
ATOM   6035  C CG2   . THR B 1 255 ? 14.744  20.725  82.675  1.00 59.92  ? 255 THR B CG2   1 
ATOM   6036  N N     . VAL B 1 256 ? 15.544  19.043  79.974  1.00 56.15  ? 256 VAL B N     1 
ATOM   6037  C CA    . VAL B 1 256 ? 16.720  19.056  79.110  1.00 57.96  ? 256 VAL B CA    1 
ATOM   6038  C C     . VAL B 1 256 ? 16.317  18.640  77.685  1.00 54.31  ? 256 VAL B C     1 
ATOM   6039  O O     . VAL B 1 256 ? 16.645  19.324  76.714  1.00 48.18  ? 256 VAL B O     1 
ATOM   6040  C CB    . VAL B 1 256 ? 17.842  18.170  79.697  1.00 58.46  ? 256 VAL B CB    1 
ATOM   6041  C CG1   . VAL B 1 256 ? 18.855  17.719  78.653  1.00 63.17  ? 256 VAL B CG1   1 
ATOM   6042  C CG2   . VAL B 1 256 ? 18.559  18.866  80.841  1.00 54.79  ? 256 VAL B CG2   1 
ATOM   6043  N N     . THR B 1 257 ? 15.608  17.508  77.587  1.00 46.04  ? 257 THR B N     1 
ATOM   6044  C CA    . THR B 1 257 ? 15.021  17.018  76.357  1.00 48.77  ? 257 THR B CA    1 
ATOM   6045  C C     . THR B 1 257 ? 14.087  18.057  75.718  1.00 51.67  ? 257 THR B C     1 
ATOM   6046  O O     . THR B 1 257 ? 13.945  18.081  74.494  1.00 56.80  ? 257 THR B O     1 
ATOM   6047  C CB    . THR B 1 257 ? 14.319  15.680  76.609  1.00 45.47  ? 257 THR B CB    1 
ATOM   6048  O OG1   . THR B 1 257 ? 15.255  14.799  77.222  1.00 46.84  ? 257 THR B OG1   1 
ATOM   6049  C CG2   . THR B 1 257 ? 13.787  15.021  75.355  1.00 46.70  ? 257 THR B CG2   1 
ATOM   6050  N N     . GLU B 1 258 ? 13.443  18.915  76.518  1.00 54.60  ? 258 GLU B N     1 
ATOM   6051  C CA    . GLU B 1 258 ? 12.558  19.935  75.968  1.00 54.59  ? 258 GLU B CA    1 
ATOM   6052  C C     . GLU B 1 258 ? 13.379  20.993  75.254  1.00 53.65  ? 258 GLU B C     1 
ATOM   6053  O O     . GLU B 1 258 ? 12.876  21.648  74.345  1.00 58.55  ? 258 GLU B O     1 
ATOM   6054  C CB    . GLU B 1 258 ? 11.690  20.611  77.035  1.00 51.80  ? 258 GLU B CB    1 
ATOM   6055  C CG    . GLU B 1 258 ? 10.455  19.802  77.398  1.00 56.62  ? 258 GLU B CG    1 
ATOM   6056  C CD    . GLU B 1 258 ? 9.463   19.590  76.266  1.00 55.10  ? 258 GLU B CD    1 
ATOM   6057  O OE1   . GLU B 1 258 ? 8.865   20.578  75.863  1.00 56.85  ? 258 GLU B OE1   1 
ATOM   6058  O OE2   . GLU B 1 258 ? 9.305   18.438  75.779  1.00 55.74  ? 258 GLU B OE2   1 
ATOM   6059  N N     . ARG B 1 259 ? 14.607  21.206  75.731  1.00 55.46  ? 259 ARG B N     1 
ATOM   6060  C CA    . ARG B 1 259 ? 15.426  22.308  75.247  1.00 56.90  ? 259 ARG B CA    1 
ATOM   6061  C C     . ARG B 1 259 ? 16.281  21.860  74.056  1.00 54.38  ? 259 ARG B C     1 
ATOM   6062  O O     . ARG B 1 259 ? 16.695  22.691  73.256  1.00 54.86  ? 259 ARG B O     1 
ATOM   6063  C CB    . ARG B 1 259 ? 16.255  22.843  76.410  1.00 54.87  ? 259 ARG B CB    1 
ATOM   6064  C CG    . ARG B 1 259 ? 15.409  23.417  77.536  1.00 65.33  ? 259 ARG B CG    1 
ATOM   6065  C CD    . ARG B 1 259 ? 16.106  23.297  78.882  1.00 75.12  ? 259 ARG B CD    1 
ATOM   6066  N NE    . ARG B 1 259 ? 15.287  23.659  80.036  1.00 69.49  ? 259 ARG B NE    1 
ATOM   6067  C CZ    . ARG B 1 259 ? 15.509  24.708  80.825  1.00 72.85  ? 259 ARG B CZ    1 
ATOM   6068  N NH1   . ARG B 1 259 ? 16.418  25.616  80.512  1.00 73.38  ? 259 ARG B NH1   1 
ATOM   6069  N NH2   . ARG B 1 259 ? 14.803  24.851  81.930  1.00 72.99  ? 259 ARG B NH2   1 
ATOM   6070  N N     . LEU B 1 260 ? 16.519  20.548  73.948  1.00 45.74  ? 260 LEU B N     1 
ATOM   6071  C CA    . LEU B 1 260 ? 17.338  19.982  72.897  1.00 46.62  ? 260 LEU B CA    1 
ATOM   6072  C C     . LEU B 1 260 ? 16.540  19.958  71.598  1.00 48.40  ? 260 LEU B C     1 
ATOM   6073  O O     . LEU B 1 260 ? 17.117  20.242  70.550  1.00 48.93  ? 260 LEU B O     1 
ATOM   6074  C CB    . LEU B 1 260 ? 17.775  18.570  73.304  1.00 49.00  ? 260 LEU B CB    1 
ATOM   6075  C CG    . LEU B 1 260 ? 18.876  18.478  74.361  1.00 49.78  ? 260 LEU B CG    1 
ATOM   6076  C CD1   . LEU B 1 260 ? 18.953  17.080  74.913  1.00 53.89  ? 260 LEU B CD1   1 
ATOM   6077  C CD2   . LEU B 1 260 ? 20.229  18.873  73.804  1.00 50.37  ? 260 LEU B CD2   1 
ATOM   6078  N N     . ARG B 1 261 ? 15.229  19.655  71.693  1.00 42.48  ? 261 ARG B N     1 
ATOM   6079  C CA    . ARG B 1 261 ? 14.329  19.598  70.547  1.00 44.25  ? 261 ARG B CA    1 
ATOM   6080  C C     . ARG B 1 261 ? 14.607  20.760  69.590  1.00 42.24  ? 261 ARG B C     1 
ATOM   6081  O O     . ARG B 1 261 ? 15.145  20.554  68.513  1.00 44.36  ? 261 ARG B O     1 
ATOM   6082  C CB    . ARG B 1 261 ? 12.859  19.538  70.999  1.00 46.66  ? 261 ARG B CB    1 
ATOM   6083  C CG    . ARG B 1 261 ? 11.861  19.656  69.856  1.00 49.35  ? 261 ARG B CG    1 
ATOM   6084  C CD    . ARG B 1 261 ? 10.404  19.452  70.213  1.00 51.78  ? 261 ARG B CD    1 
ATOM   6085  N NE    . ARG B 1 261 ? 9.920   20.478  71.110  1.00 56.26  ? 261 ARG B NE    1 
ATOM   6086  C CZ    . ARG B 1 261 ? 9.692   20.295  72.407  1.00 61.26  ? 261 ARG B CZ    1 
ATOM   6087  N NH1   . ARG B 1 261 ? 9.739   19.085  72.934  1.00 61.27  ? 261 ARG B NH1   1 
ATOM   6088  N NH2   . ARG B 1 261 ? 9.448   21.330  73.188  1.00 57.92  ? 261 ARG B NH2   1 
ATOM   6089  N N     . PRO B 1 262 ? 14.291  22.036  69.902  1.00 46.71  ? 262 PRO B N     1 
ATOM   6090  C CA    . PRO B 1 262 ? 14.460  23.086  68.895  1.00 46.96  ? 262 PRO B CA    1 
ATOM   6091  C C     . PRO B 1 262 ? 15.901  23.202  68.395  1.00 49.36  ? 262 PRO B C     1 
ATOM   6092  O O     . PRO B 1 262 ? 16.117  23.509  67.229  1.00 48.36  ? 262 PRO B O     1 
ATOM   6093  C CB    . PRO B 1 262 ? 13.961  24.384  69.570  1.00 46.37  ? 262 PRO B CB    1 
ATOM   6094  C CG    . PRO B 1 262 ? 13.815  24.058  71.067  1.00 42.50  ? 262 PRO B CG    1 
ATOM   6095  C CD    . PRO B 1 262 ? 13.734  22.544  71.170  1.00 43.68  ? 262 PRO B CD    1 
ATOM   6096  N N     . LEU B 1 263 ? 16.887  22.991  69.276  1.00 52.55  ? 263 LEU B N     1 
ATOM   6097  C CA    . LEU B 1 263 ? 18.285  23.194  68.912  1.00 50.51  ? 263 LEU B CA    1 
ATOM   6098  C C     . LEU B 1 263 ? 18.742  22.148  67.900  1.00 48.49  ? 263 LEU B C     1 
ATOM   6099  O O     . LEU B 1 263 ? 19.678  22.367  67.128  1.00 52.31  ? 263 LEU B O     1 
ATOM   6100  C CB    . LEU B 1 263 ? 19.140  23.038  70.169  1.00 50.59  ? 263 LEU B CB    1 
ATOM   6101  C CG    . LEU B 1 263 ? 19.077  24.188  71.166  1.00 50.59  ? 263 LEU B CG    1 
ATOM   6102  C CD1   . LEU B 1 263 ? 19.797  23.805  72.468  1.00 50.48  ? 263 LEU B CD1   1 
ATOM   6103  C CD2   . LEU B 1 263 ? 19.654  25.453  70.550  1.00 47.94  ? 263 LEU B CD2   1 
ATOM   6104  N N     . LYS B 1 264 ? 18.122  20.975  68.002  1.00 41.22  ? 264 LYS B N     1 
ATOM   6105  C CA    . LYS B 1 264 ? 18.473  19.825  67.202  1.00 43.85  ? 264 LYS B CA    1 
ATOM   6106  C C     . LYS B 1 264 ? 17.759  19.919  65.850  1.00 56.88  ? 264 LYS B C     1 
ATOM   6107  O O     . LYS B 1 264 ? 18.335  19.686  64.787  1.00 55.78  ? 264 LYS B O     1 
ATOM   6108  C CB    . LYS B 1 264 ? 18.047  18.587  67.985  1.00 48.72  ? 264 LYS B CB    1 
ATOM   6109  C CG    . LYS B 1 264 ? 18.801  17.323  67.641  1.00 64.58  ? 264 LYS B CG    1 
ATOM   6110  C CD    . LYS B 1 264 ? 20.222  17.323  68.119  1.00 64.24  ? 264 LYS B CD    1 
ATOM   6111  C CE    . LYS B 1 264 ? 21.045  16.309  67.347  1.00 67.27  ? 264 LYS B CE    1 
ATOM   6112  N NZ    . LYS B 1 264 ? 21.239  16.656  65.906  1.00 54.42  ? 264 LYS B NZ    1 
ATOM   6113  N N     . VAL B 1 265 ? 16.478  20.294  65.905  1.00 60.96  ? 265 VAL B N     1 
ATOM   6114  C CA    . VAL B 1 265 ? 15.639  20.321  64.733  1.00 47.87  ? 265 VAL B CA    1 
ATOM   6115  C C     . VAL B 1 265 ? 16.102  21.398  63.766  1.00 43.60  ? 265 VAL B C     1 
ATOM   6116  O O     . VAL B 1 265 ? 16.113  21.163  62.567  1.00 49.57  ? 265 VAL B O     1 
ATOM   6117  C CB    . VAL B 1 265 ? 14.182  20.519  65.134  1.00 44.14  ? 265 VAL B CB    1 
ATOM   6118  C CG1   . VAL B 1 265 ? 13.350  20.963  63.948  1.00 46.28  ? 265 VAL B CG1   1 
ATOM   6119  C CG2   . VAL B 1 265 ? 13.641  19.251  65.762  1.00 44.63  ? 265 VAL B CG2   1 
ATOM   6120  N N     . ALA B 1 266 ? 16.487  22.565  64.268  1.00 38.38  ? 266 ALA B N     1 
ATOM   6121  C CA    . ALA B 1 266 ? 17.010  23.604  63.390  1.00 40.39  ? 266 ALA B CA    1 
ATOM   6122  C C     . ALA B 1 266 ? 18.487  23.352  63.040  1.00 46.95  ? 266 ALA B C     1 
ATOM   6123  O O     . ALA B 1 266 ? 19.097  24.196  62.388  1.00 41.63  ? 266 ALA B O     1 
ATOM   6124  C CB    . ALA B 1 266 ? 16.834  24.973  64.025  1.00 37.11  ? 266 ALA B CB    1 
ATOM   6125  N N     . GLY B 1 267 ? 19.072  22.235  63.511  1.00 52.35  ? 267 GLY B N     1 
ATOM   6126  C CA    . GLY B 1 267 ? 20.467  21.892  63.263  1.00 52.09  ? 267 GLY B CA    1 
ATOM   6127  C C     . GLY B 1 267 ? 21.476  22.819  63.959  1.00 56.62  ? 267 GLY B C     1 
ATOM   6128  O O     . GLY B 1 267 ? 22.576  23.021  63.447  1.00 51.75  ? 267 GLY B O     1 
ATOM   6129  N N     . VAL B 1 268 ? 21.119  23.387  65.124  1.00 57.79  ? 268 VAL B N     1 
ATOM   6130  C CA    . VAL B 1 268 ? 22.015  24.288  65.840  1.00 53.44  ? 268 VAL B CA    1 
ATOM   6131  C C     . VAL B 1 268 ? 23.098  23.453  66.529  1.00 52.73  ? 268 VAL B C     1 
ATOM   6132  O O     . VAL B 1 268 ? 24.296  23.770  66.508  1.00 45.92  ? 268 VAL B O     1 
ATOM   6133  C CB    . VAL B 1 268 ? 21.220  25.182  66.809  1.00 46.97  ? 268 VAL B CB    1 
ATOM   6134  C CG1   . VAL B 1 268 ? 22.119  25.972  67.736  1.00 49.47  ? 268 VAL B CG1   1 
ATOM   6135  C CG2   . VAL B 1 268 ? 20.312  26.121  66.041  1.00 46.14  ? 268 VAL B CG2   1 
ATOM   6136  N N     . ILE B 1 269 ? 22.649  22.348  67.116  1.00 48.68  ? 269 ILE B N     1 
ATOM   6137  C CA    . ILE B 1 269 ? 23.546  21.274  67.481  1.00 47.87  ? 269 ILE B CA    1 
ATOM   6138  C C     . ILE B 1 269 ? 23.839  20.487  66.211  1.00 52.04  ? 269 ILE B C     1 
ATOM   6139  O O     . ILE B 1 269 ? 22.919  19.932  65.613  1.00 52.51  ? 269 ILE B O     1 
ATOM   6140  C CB    . ILE B 1 269 ? 22.881  20.429  68.575  1.00 49.60  ? 269 ILE B CB    1 
ATOM   6141  C CG1   . ILE B 1 269 ? 22.810  21.207  69.891  1.00 52.27  ? 269 ILE B CG1   1 
ATOM   6142  C CG2   . ILE B 1 269 ? 23.573  19.094  68.747  1.00 56.84  ? 269 ILE B CG2   1 
ATOM   6143  C CD1   . ILE B 1 269 ? 21.880  20.602  70.919  1.00 54.34  ? 269 ILE B CD1   1 
ATOM   6144  N N     . GLN B 1 270 ? 25.112  20.451  65.803  1.00 56.44  ? 270 GLN B N     1 
ATOM   6145  C CA    . GLN B 1 270 ? 25.457  19.998  64.457  1.00 53.78  ? 270 GLN B CA    1 
ATOM   6146  C C     . GLN B 1 270 ? 25.750  18.500  64.402  1.00 53.72  ? 270 GLN B C     1 
ATOM   6147  O O     . GLN B 1 270 ? 25.851  17.968  63.305  1.00 47.14  ? 270 GLN B O     1 
ATOM   6148  C CB    . GLN B 1 270 ? 26.679  20.726  63.903  1.00 45.98  ? 270 GLN B CB    1 
ATOM   6149  C CG    . GLN B 1 270 ? 26.559  22.237  63.939  1.00 49.11  ? 270 GLN B CG    1 
ATOM   6150  C CD    . GLN B 1 270 ? 27.850  22.851  64.419  1.00 53.10  ? 270 GLN B CD    1 
ATOM   6151  O OE1   . GLN B 1 270 ? 28.205  22.764  65.599  1.00 53.46  ? 270 GLN B OE1   1 
ATOM   6152  N NE2   . GLN B 1 270 ? 28.579  23.437  63.483  1.00 50.19  ? 270 GLN B NE2   1 
ATOM   6153  N N     . ASN B 1 271 ? 25.935  17.822  65.546  1.00 50.63  ? 271 ASN B N     1 
ATOM   6154  C CA    . ASN B 1 271 ? 26.113  16.376  65.518  1.00 48.08  ? 271 ASN B CA    1 
ATOM   6155  C C     . ASN B 1 271 ? 24.986  15.741  66.313  1.00 46.05  ? 271 ASN B C     1 
ATOM   6156  O O     . ASN B 1 271 ? 24.088  16.457  66.724  1.00 45.37  ? 271 ASN B O     1 
ATOM   6157  C CB    . ASN B 1 271 ? 27.471  15.921  66.049  1.00 52.01  ? 271 ASN B CB    1 
ATOM   6158  C CG    . ASN B 1 271 ? 27.781  16.419  67.440  1.00 49.18  ? 271 ASN B CG    1 
ATOM   6159  O OD1   . ASN B 1 271 ? 27.296  17.459  67.866  1.00 61.03  ? 271 ASN B OD1   1 
ATOM   6160  N ND2   . ASN B 1 271 ? 28.632  15.701  68.137  1.00 46.94  ? 271 ASN B ND2   1 
ATOM   6161  N N     . GLY B 1 272 ? 25.033  14.414  66.479  1.00 44.63  ? 272 GLY B N     1 
ATOM   6162  C CA    . GLY B 1 272 ? 24.157  13.725  67.406  1.00 48.79  ? 272 GLY B CA    1 
ATOM   6163  C C     . GLY B 1 272 ? 24.316  14.240  68.835  1.00 53.35  ? 272 GLY B C     1 
ATOM   6164  O O     . GLY B 1 272 ? 25.429  14.523  69.277  1.00 54.79  ? 272 GLY B O     1 
ATOM   6165  N N     . ALA B 1 273 ? 23.177  14.381  69.531  1.00 60.16  ? 273 ALA B N     1 
ATOM   6166  C CA    . ALA B 1 273 ? 23.134  14.831  70.917  1.00 57.93  ? 273 ALA B CA    1 
ATOM   6167  C C     . ALA B 1 273 ? 22.961  13.611  71.795  1.00 62.53  ? 273 ALA B C     1 
ATOM   6168  O O     . ALA B 1 273 ? 21.895  12.997  71.684  1.00 52.97  ? 273 ALA B O     1 
ATOM   6169  C CB    . ALA B 1 273 ? 21.980  15.765  71.168  1.00 49.01  ? 273 ALA B CB    1 
ATOM   6170  N N     . THR B 1 274 ? 23.984  13.325  72.635  1.00 55.17  ? 274 THR B N     1 
ATOM   6171  C CA    . THR B 1 274 ? 23.953  12.219  73.585  1.00 60.41  ? 274 THR B CA    1 
ATOM   6172  C C     . THR B 1 274 ? 23.876  12.779  75.010  1.00 59.21  ? 274 THR B C     1 
ATOM   6173  O O     . THR B 1 274 ? 24.600  13.702  75.366  1.00 60.30  ? 274 THR B O     1 
ATOM   6174  C CB    . THR B 1 274 ? 25.155  11.284  73.359  1.00 70.62  ? 274 THR B CB    1 
ATOM   6175  O OG1   . THR B 1 274 ? 26.308  12.071  73.039  1.00 68.52  ? 274 THR B OG1   1 
ATOM   6176  C CG2   . THR B 1 274 ? 24.923  10.302  72.231  1.00 72.56  ? 274 THR B CG2   1 
ATOM   6177  N N     . VAL B 1 275 ? 22.957  12.243  75.813  1.00 53.96  ? 275 VAL B N     1 
ATOM   6178  C CA    . VAL B 1 275 ? 22.839  12.603  77.211  1.00 53.36  ? 275 VAL B CA    1 
ATOM   6179  C C     . VAL B 1 275 ? 22.890  11.307  78.007  1.00 57.13  ? 275 VAL B C     1 
ATOM   6180  O O     . VAL B 1 275 ? 21.926  10.556  77.955  1.00 60.19  ? 275 VAL B O     1 
ATOM   6181  C CB    . VAL B 1 275 ? 21.530  13.358  77.489  1.00 54.00  ? 275 VAL B CB    1 
ATOM   6182  C CG1   . VAL B 1 275 ? 21.525  13.936  78.892  1.00 56.95  ? 275 VAL B CG1   1 
ATOM   6183  C CG2   . VAL B 1 275 ? 21.267  14.459  76.470  1.00 57.55  ? 275 VAL B CG2   1 
ATOM   6184  N N     . ARG B 1 276 ? 24.003  11.071  78.725  1.00 56.76  ? 276 ARG B N     1 
ATOM   6185  C CA    . ARG B 1 276 ? 24.334  9.787   79.334  1.00 53.33  ? 276 ARG B CA    1 
ATOM   6186  C C     . ARG B 1 276 ? 24.054  9.777   80.846  1.00 51.06  ? 276 ARG B C     1 
ATOM   6187  O O     . ARG B 1 276 ? 24.129  10.826  81.508  1.00 45.12  ? 276 ARG B O     1 
ATOM   6188  C CB    . ARG B 1 276 ? 25.815  9.512   79.048  1.00 57.04  ? 276 ARG B CB    1 
ATOM   6189  C CG    . ARG B 1 276 ? 26.139  9.350   77.567  1.00 61.16  ? 276 ARG B CG    1 
ATOM   6190  C CD    . ARG B 1 276 ? 27.597  9.602   77.211  1.00 61.31  ? 276 ARG B CD    1 
ATOM   6191  N NE    . ARG B 1 276 ? 28.509  8.547   77.662  1.00 66.31  ? 276 ARG B NE    1 
ATOM   6192  C CZ    . ARG B 1 276 ? 28.666  7.344   77.087  1.00 70.14  ? 276 ARG B CZ    1 
ATOM   6193  N NH1   . ARG B 1 276 ? 27.975  7.001   76.004  1.00 71.13  ? 276 ARG B NH1   1 
ATOM   6194  N NH2   . ARG B 1 276 ? 29.510  6.468   77.616  1.00 60.70  ? 276 ARG B NH2   1 
ATOM   6195  N N     . SER B 1 277 ? 23.778  8.581   81.415  1.00 53.07  ? 277 SER B N     1 
ATOM   6196  C CA    . SER B 1 277 ? 23.523  8.468   82.858  1.00 53.33  ? 277 SER B CA    1 
ATOM   6197  C C     . SER B 1 277 ? 24.827  8.256   83.613  1.00 54.51  ? 277 SER B C     1 
ATOM   6198  O O     . SER B 1 277 ? 25.768  7.660   83.104  1.00 70.80  ? 277 SER B O     1 
ATOM   6199  C CB    . SER B 1 277 ? 22.495  7.416   83.255  1.00 50.45  ? 277 SER B CB    1 
ATOM   6200  O OG    . SER B 1 277 ? 22.858  6.090   82.880  1.00 49.03  ? 277 SER B OG    1 
ATOM   6201  N N     . LEU B 1 278 ? 24.866  8.779   84.833  1.00 61.33  ? 278 LEU B N     1 
ATOM   6202  C CA    . LEU B 1 278 ? 26.052  8.716   85.665  1.00 62.65  ? 278 LEU B CA    1 
ATOM   6203  C C     . LEU B 1 278 ? 26.636  7.301   85.619  1.00 52.64  ? 278 LEU B C     1 
ATOM   6204  O O     . LEU B 1 278 ? 27.834  7.137   85.425  1.00 49.17  ? 278 LEU B O     1 
ATOM   6205  C CB    . LEU B 1 278 ? 25.660  9.156   87.081  1.00 65.70  ? 278 LEU B CB    1 
ATOM   6206  C CG    . LEU B 1 278 ? 26.630  8.767   88.198  1.00 69.96  ? 278 LEU B CG    1 
ATOM   6207  C CD1   . LEU B 1 278 ? 27.875  9.638   88.196  1.00 67.58  ? 278 LEU B CD1   1 
ATOM   6208  C CD2   . LEU B 1 278 ? 25.936  8.819   89.551  1.00 68.24  ? 278 LEU B CD2   1 
ATOM   6209  N N     . VAL B 1 279 ? 25.788  6.275   85.754  1.00 52.60  ? 279 VAL B N     1 
ATOM   6210  C CA    . VAL B 1 279 ? 26.294  4.934   85.988  1.00 48.79  ? 279 VAL B CA    1 
ATOM   6211  C C     . VAL B 1 279 ? 26.929  4.380   84.725  1.00 58.92  ? 279 VAL B C     1 
ATOM   6212  O O     . VAL B 1 279 ? 27.892  3.629   84.824  1.00 63.74  ? 279 VAL B O     1 
ATOM   6213  C CB    . VAL B 1 279 ? 25.223  3.974   86.518  1.00 51.76  ? 279 VAL B CB    1 
ATOM   6214  C CG1   . VAL B 1 279 ? 25.767  2.566   86.726  1.00 50.12  ? 279 VAL B CG1   1 
ATOM   6215  C CG2   . VAL B 1 279 ? 24.628  4.496   87.813  1.00 59.63  ? 279 VAL B CG2   1 
ATOM   6216  N N     . LEU B 1 280 ? 26.391  4.727   83.552  1.00 58.59  ? 280 LEU B N     1 
ATOM   6217  C CA    . LEU B 1 280 ? 26.971  4.249   82.308  1.00 55.34  ? 280 LEU B CA    1 
ATOM   6218  C C     . LEU B 1 280 ? 28.448  4.644   82.178  1.00 57.53  ? 280 LEU B C     1 
ATOM   6219  O O     . LEU B 1 280 ? 29.212  3.826   81.687  1.00 58.11  ? 280 LEU B O     1 
ATOM   6220  C CB    . LEU B 1 280 ? 26.159  4.793   81.130  1.00 58.27  ? 280 LEU B CB    1 
ATOM   6221  C CG    . LEU B 1 280 ? 26.702  4.491   79.731  1.00 54.22  ? 280 LEU B CG    1 
ATOM   6222  C CD1   . LEU B 1 280 ? 26.754  2.991   79.438  1.00 48.80  ? 280 LEU B CD1   1 
ATOM   6223  C CD2   . LEU B 1 280 ? 25.852  5.195   78.692  1.00 66.10  ? 280 LEU B CD2   1 
ATOM   6224  N N     . ASP B 1 281 ? 28.854  5.872   82.562  1.00 56.48  ? 281 ASP B N     1 
ATOM   6225  C CA    . ASP B 1 281 ? 30.253  6.292   82.437  1.00 64.81  ? 281 ASP B CA    1 
ATOM   6226  C C     . ASP B 1 281 ? 31.141  5.781   83.577  1.00 60.53  ? 281 ASP B C     1 
ATOM   6227  O O     . ASP B 1 281 ? 32.232  5.271   83.353  1.00 59.85  ? 281 ASP B O     1 
ATOM   6228  C CB    . ASP B 1 281 ? 30.365  7.809   82.337  1.00 69.16  ? 281 ASP B CB    1 
ATOM   6229  C CG    . ASP B 1 281 ? 29.727  8.279   81.049  1.00 80.03  ? 281 ASP B CG    1 
ATOM   6230  O OD1   . ASP B 1 281 ? 29.978  7.610   80.013  1.00 74.85  ? 281 ASP B OD1   1 
ATOM   6231  O OD2   . ASP B 1 281 ? 28.975  9.283   81.095  1.00 97.49  ? 281 ASP B OD2   1 
ATOM   6232  N N     . ALA B 1 282 ? 30.683  5.924   84.811  1.00 60.25  ? 282 ALA B N     1 
ATOM   6233  C CA    . ALA B 1 282 ? 31.381  5.338   85.935  1.00 61.46  ? 282 ALA B CA    1 
ATOM   6234  C C     . ALA B 1 282 ? 31.789  3.891   85.661  1.00 64.85  ? 282 ALA B C     1 
ATOM   6235  O O     . ALA B 1 282 ? 32.889  3.494   86.034  1.00 81.47  ? 282 ALA B O     1 
ATOM   6236  C CB    . ALA B 1 282 ? 30.504  5.437   87.156  1.00 62.71  ? 282 ALA B CB    1 
ATOM   6237  N N     . ALA B 1 283 ? 30.920  3.096   85.021  1.00 69.79  ? 283 ALA B N     1 
ATOM   6238  C CA    . ALA B 1 283 ? 31.167  1.668   84.823  1.00 72.58  ? 283 ALA B CA    1 
ATOM   6239  C C     . ALA B 1 283 ? 32.103  1.394   83.640  1.00 76.12  ? 283 ALA B C     1 
ATOM   6240  O O     . ALA B 1 283 ? 32.399  0.229   83.360  1.00 72.24  ? 283 ALA B O     1 
ATOM   6241  C CB    . ALA B 1 283 ? 29.868  0.932   84.626  1.00 72.01  ? 283 ALA B CB    1 
ATOM   6242  N N     . ILE B 1 284 ? 32.552  2.455   82.951  1.00 64.87  ? 284 ILE B N     1 
ATOM   6243  C CA    . ILE B 1 284 ? 33.633  2.348   81.990  1.00 67.53  ? 284 ILE B CA    1 
ATOM   6244  C C     . ILE B 1 284 ? 34.961  2.587   82.707  1.00 67.34  ? 284 ILE B C     1 
ATOM   6245  O O     . ILE B 1 284 ? 35.912  1.831   82.506  1.00 59.56  ? 284 ILE B O     1 
ATOM   6246  C CB    . ILE B 1 284 ? 33.416  3.323   80.817  1.00 71.06  ? 284 ILE B CB    1 
ATOM   6247  C CG1   . ILE B 1 284 ? 32.096  3.029   80.098  1.00 71.30  ? 284 ILE B CG1   1 
ATOM   6248  C CG2   . ILE B 1 284 ? 34.601  3.291   79.853  1.00 71.51  ? 284 ILE B CG2   1 
ATOM   6249  C CD1   . ILE B 1 284 ? 31.610  4.172   79.235  1.00 72.41  ? 284 ILE B CD1   1 
ATOM   6250  N N     . THR B 1 285 ? 35.006  3.638   83.540  1.00 68.13  ? 285 THR B N     1 
ATOM   6251  C CA    . THR B 1 285 ? 36.253  4.099   84.125  1.00 66.01  ? 285 THR B CA    1 
ATOM   6252  C C     . THR B 1 285 ? 36.232  3.983   85.648  1.00 68.29  ? 285 THR B C     1 
ATOM   6253  O O     . THR B 1 285 ? 36.991  4.710   86.297  1.00 65.67  ? 285 THR B O     1 
ATOM   6254  C CB    . THR B 1 285 ? 36.591  5.542   83.699  1.00 68.79  ? 285 THR B CB    1 
ATOM   6255  O OG1   . THR B 1 285 ? 36.131  6.485   84.664  1.00 62.28  ? 285 THR B OG1   1 
ATOM   6256  C CG2   . THR B 1 285 ? 36.054  5.911   82.332  1.00 67.93  ? 285 THR B CG2   1 
ATOM   6257  N N     . ARG B 1 286 ? 35.411  3.064   86.208  1.00 65.21  ? 286 ARG B N     1 
ATOM   6258  C CA    . ARG B 1 286 ? 35.457  2.746   87.636  1.00 57.91  ? 286 ARG B CA    1 
ATOM   6259  C C     . ARG B 1 286 ? 34.986  1.312   87.898  1.00 60.51  ? 286 ARG B C     1 
ATOM   6260  O O     . ARG B 1 286 ? 34.693  0.567   86.962  1.00 67.03  ? 286 ARG B O     1 
ATOM   6261  C CB    . ARG B 1 286 ? 34.595  3.710   88.457  1.00 50.47  ? 286 ARG B CB    1 
ATOM   6262  C CG    . ARG B 1 286 ? 35.016  5.172   88.434  1.00 53.67  ? 286 ARG B CG    1 
ATOM   6263  C CD    . ARG B 1 286 ? 36.308  5.429   89.189  1.00 55.26  ? 286 ARG B CD    1 
ATOM   6264  N NE    . ARG B 1 286 ? 36.561  6.858   89.391  1.00 56.33  ? 286 ARG B NE    1 
ATOM   6265  C CZ    . ARG B 1 286 ? 37.132  7.665   88.501  1.00 52.72  ? 286 ARG B CZ    1 
ATOM   6266  N NH1   . ARG B 1 286 ? 37.592  7.171   87.359  1.00 45.05  ? 286 ARG B NH1   1 
ATOM   6267  N NH2   . ARG B 1 286 ? 37.273  8.954   88.780  1.00 51.47  ? 286 ARG B NH2   1 
ATOM   6268  N N     . THR B 1 287 ? 34.959  0.949   89.192  1.00 51.75  ? 287 THR B N     1 
ATOM   6269  C CA    . THR B 1 287 ? 34.427  -0.307  89.695  1.00 59.21  ? 287 THR B CA    1 
ATOM   6270  C C     . THR B 1 287 ? 33.272  -0.016  90.663  1.00 71.61  ? 287 THR B C     1 
ATOM   6271  O O     . THR B 1 287 ? 33.166  1.075   91.240  1.00 71.96  ? 287 THR B O     1 
ATOM   6272  C CB    . THR B 1 287 ? 35.482  -1.171  90.420  1.00 66.53  ? 287 THR B CB    1 
ATOM   6273  O OG1   . THR B 1 287 ? 35.649  -0.696  91.758  1.00 79.70  ? 287 THR B OG1   1 
ATOM   6274  C CG2   . THR B 1 287 ? 36.855  -1.186  89.777  1.00 72.69  ? 287 THR B CG2   1 
ATOM   6275  N N     . LYS B 1 288 ? 32.414  -1.031  90.844  1.00 77.61  ? 288 LYS B N     1 
ATOM   6276  C CA    . LYS B 1 288 ? 31.240  -0.950  91.698  1.00 67.74  ? 288 LYS B CA    1 
ATOM   6277  C C     . LYS B 1 288 ? 31.681  -1.030  93.163  1.00 71.36  ? 288 LYS B C     1 
ATOM   6278  O O     . LYS B 1 288 ? 31.112  -0.344  94.017  1.00 67.09  ? 288 LYS B O     1 
ATOM   6279  C CB    . LYS B 1 288 ? 30.275  -2.072  91.292  1.00 69.85  ? 288 LYS B CB    1 
ATOM   6280  C CG    . LYS B 1 288 ? 28.839  -1.991  91.810  1.00 70.18  ? 288 LYS B CG    1 
ATOM   6281  C CD    . LYS B 1 288 ? 27.991  -3.183  91.356  1.00 68.58  ? 288 LYS B CD    1 
ATOM   6282  C CE    . LYS B 1 288 ? 26.591  -3.233  91.944  1.00 71.00  ? 288 LYS B CE    1 
ATOM   6283  N NZ    . LYS B 1 288 ? 25.887  -4.498  91.597  1.00 66.88  ? 288 LYS B NZ    1 
ATOM   6284  N N     . SER B 1 289 ? 32.728  -1.827  93.440  1.00 73.76  ? 289 SER B N     1 
ATOM   6285  C CA    . SER B 1 289 ? 33.081  -2.202  94.805  1.00 77.90  ? 289 SER B CA    1 
ATOM   6286  C C     . SER B 1 289 ? 33.704  -1.032  95.561  1.00 76.35  ? 289 SER B C     1 
ATOM   6287  O O     . SER B 1 289 ? 33.640  -1.003  96.789  1.00 71.65  ? 289 SER B O     1 
ATOM   6288  C CB    . SER B 1 289 ? 33.979  -3.404  94.837  1.00 68.08  ? 289 SER B CB    1 
ATOM   6289  O OG    . SER B 1 289 ? 35.145  -3.158  94.071  1.00 69.56  ? 289 SER B OG    1 
ATOM   6290  N N     . GLN B 1 290 ? 34.274  -0.063  94.826  1.00 80.40  ? 290 GLN B N     1 
ATOM   6291  C CA    . GLN B 1 290 ? 34.886  1.109   95.445  1.00 78.95  ? 290 GLN B CA    1 
ATOM   6292  C C     . GLN B 1 290 ? 33.838  2.157   95.810  1.00 80.46  ? 290 GLN B C     1 
ATOM   6293  O O     . GLN B 1 290 ? 34.191  3.182   96.396  1.00 83.73  ? 290 GLN B O     1 
ATOM   6294  C CB    . GLN B 1 290 ? 35.899  1.767   94.514  1.00 72.22  ? 290 GLN B CB    1 
ATOM   6295  C CG    . GLN B 1 290 ? 35.293  2.137   93.179  1.00 74.47  ? 290 GLN B CG    1 
ATOM   6296  C CD    . GLN B 1 290 ? 36.204  3.048   92.404  1.00 84.64  ? 290 GLN B CD    1 
ATOM   6297  O OE1   . GLN B 1 290 ? 36.335  4.234   92.726  1.00 72.48  ? 290 GLN B OE1   1 
ATOM   6298  N NE2   . GLN B 1 290 ? 36.826  2.486   91.374  1.00 85.18  ? 290 GLN B NE2   1 
ATOM   6299  N N     . TYR B 1 291 ? 32.575  1.913   95.416  1.00 80.94  ? 291 TYR B N     1 
ATOM   6300  C CA    . TYR B 1 291 ? 31.455  2.789   95.735  1.00 69.44  ? 291 TYR B CA    1 
ATOM   6301  C C     . TYR B 1 291 ? 30.420  2.104   96.633  1.00 67.26  ? 291 TYR B C     1 
ATOM   6302  O O     . TYR B 1 291 ? 29.876  2.752   97.531  1.00 58.75  ? 291 TYR B O     1 
ATOM   6303  C CB    . TYR B 1 291 ? 30.803  3.260   94.443  1.00 59.82  ? 291 TYR B CB    1 
ATOM   6304  C CG    . TYR B 1 291 ? 31.624  4.215   93.616  1.00 60.10  ? 291 TYR B CG    1 
ATOM   6305  C CD1   . TYR B 1 291 ? 32.107  5.407   94.140  1.00 61.57  ? 291 TYR B CD1   1 
ATOM   6306  C CD2   . TYR B 1 291 ? 31.873  3.944   92.282  1.00 59.12  ? 291 TYR B CD2   1 
ATOM   6307  C CE1   . TYR B 1 291 ? 32.842  6.294   93.365  1.00 57.34  ? 291 TYR B CE1   1 
ATOM   6308  C CE2   . TYR B 1 291 ? 32.593  4.822   91.492  1.00 59.66  ? 291 TYR B CE2   1 
ATOM   6309  C CZ    . TYR B 1 291 ? 33.073  6.000   92.030  1.00 57.82  ? 291 TYR B CZ    1 
ATOM   6310  O OH    . TYR B 1 291 ? 33.777  6.822   91.195  1.00 52.95  ? 291 TYR B OH    1 
ATOM   6311  N N     . TYR B 1 292 ? 30.149  0.813   96.368  1.00 62.35  ? 292 TYR B N     1 
ATOM   6312  C CA    . TYR B 1 292 ? 29.164  0.038   97.102  1.00 67.41  ? 292 TYR B CA    1 
ATOM   6313  C C     . TYR B 1 292 ? 29.552  -1.445  97.075  1.00 72.30  ? 292 TYR B C     1 
ATOM   6314  O O     . TYR B 1 292 ? 29.925  -1.974  96.028  1.00 71.57  ? 292 TYR B O     1 
ATOM   6315  C CB    . TYR B 1 292 ? 27.780  0.338   96.509  1.00 74.11  ? 292 TYR B CB    1 
ATOM   6316  C CG    . TYR B 1 292 ? 26.673  -0.596  96.929  1.00 79.09  ? 292 TYR B CG    1 
ATOM   6317  C CD1   . TYR B 1 292 ? 25.975  -0.417  98.114  1.00 80.80  ? 292 TYR B CD1   1 
ATOM   6318  C CD2   . TYR B 1 292 ? 26.358  -1.698  96.149  1.00 83.51  ? 292 TYR B CD2   1 
ATOM   6319  C CE1   . TYR B 1 292 ? 24.963  -1.293  98.491  1.00 91.40  ? 292 TYR B CE1   1 
ATOM   6320  C CE2   . TYR B 1 292 ? 25.361  -2.586  96.516  1.00 86.94  ? 292 TYR B CE2   1 
ATOM   6321  C CZ    . TYR B 1 292 ? 24.655  -2.381  97.688  1.00 91.51  ? 292 TYR B CZ    1 
ATOM   6322  O OH    . TYR B 1 292 ? 23.669  -3.280  98.012  1.00 87.77  ? 292 TYR B OH    1 
ATOM   6323  N N     . ASP B 1 293 ? 29.429  -2.120  98.231  1.00 83.09  ? 293 ASP B N     1 
ATOM   6324  C CA    . ASP B 1 293 ? 29.967  -3.462  98.434  1.00 96.44  ? 293 ASP B CA    1 
ATOM   6325  C C     . ASP B 1 293 ? 28.959  -4.552  98.053  1.00 103.05 ? 293 ASP B C     1 
ATOM   6326  O O     . ASP B 1 293 ? 29.372  -5.631  97.630  1.00 99.98  ? 293 ASP B O     1 
ATOM   6327  C CB    . ASP B 1 293 ? 30.435  -3.663  99.887  1.00 109.37 ? 293 ASP B CB    1 
ATOM   6328  C CG    . ASP B 1 293 ? 31.945  -3.589  100.117 1.00 123.96 ? 293 ASP B CG    1 
ATOM   6329  O OD1   . ASP B 1 293 ? 32.704  -3.584  99.113  1.00 127.28 ? 293 ASP B OD1   1 
ATOM   6330  O OD2   . ASP B 1 293 ? 32.365  -3.548  101.309 1.00 97.94  ? 293 ASP B OD2   1 
ATOM   6331  N N     . GLY B 1 294 ? 27.651  -4.280  98.207  1.00 102.92 ? 294 GLY B N     1 
ATOM   6332  C CA    . GLY B 1 294 ? 26.616  -5.312  98.207  1.00 93.54  ? 294 GLY B CA    1 
ATOM   6333  C C     . GLY B 1 294 ? 26.380  -5.977  96.848  1.00 85.99  ? 294 GLY B C     1 
ATOM   6334  O O     . GLY B 1 294 ? 26.922  -5.548  95.836  1.00 70.43  ? 294 GLY B O     1 
ATOM   6335  N N     . ASP B 1 295 ? 25.528  -7.016  96.841  1.00 106.82 ? 295 ASP B N     1 
ATOM   6336  C CA    . ASP B 1 295 ? 25.272  -7.849  95.668  1.00 115.09 ? 295 ASP B CA    1 
ATOM   6337  C C     . ASP B 1 295 ? 24.350  -7.144  94.653  1.00 121.25 ? 295 ASP B C     1 
ATOM   6338  O O     . ASP B 1 295 ? 24.520  -7.330  93.442  1.00 109.42 ? 295 ASP B O     1 
ATOM   6339  C CB    . ASP B 1 295 ? 24.728  -9.220  96.101  1.00 96.54  ? 295 ASP B CB    1 
ATOM   6340  N N     . GLY B 1 296 ? 23.398  -6.317  95.131  1.00 106.95 ? 296 GLY B N     1 
ATOM   6341  C CA    . GLY B 1 296 ? 22.331  -5.769  94.299  1.00 100.66 ? 296 GLY B CA    1 
ATOM   6342  C C     . GLY B 1 296 ? 22.685  -4.429  93.648  1.00 89.84  ? 296 GLY B C     1 
ATOM   6343  O O     . GLY B 1 296 ? 23.801  -3.960  93.788  1.00 93.58  ? 296 GLY B O     1 
ATOM   6344  N N     . PRO B 1 297 ? 21.767  -3.797  92.871  1.00 92.41  ? 297 PRO B N     1 
ATOM   6345  C CA    . PRO B 1 297 ? 21.985  -2.461  92.285  1.00 92.19  ? 297 PRO B CA    1 
ATOM   6346  C C     . PRO B 1 297 ? 22.228  -1.265  93.217  1.00 79.55  ? 297 PRO B C     1 
ATOM   6347  O O     . PRO B 1 297 ? 21.649  -1.178  94.299  1.00 77.08  ? 297 PRO B O     1 
ATOM   6348  C CB    . PRO B 1 297 ? 20.666  -2.182  91.536  1.00 92.31  ? 297 PRO B CB    1 
ATOM   6349  C CG    . PRO B 1 297 ? 20.106  -3.553  91.224  1.00 94.22  ? 297 PRO B CG    1 
ATOM   6350  C CD    . PRO B 1 297 ? 20.505  -4.404  92.411  1.00 95.08  ? 297 PRO B CD    1 
ATOM   6351  N N     . ILE B 1 298 ? 23.019  -0.290  92.738  1.00 78.58  ? 298 ILE B N     1 
ATOM   6352  C CA    . ILE B 1 298 ? 23.581  0.758   93.586  1.00 83.53  ? 298 ILE B CA    1 
ATOM   6353  C C     . ILE B 1 298 ? 22.460  1.594   94.196  1.00 75.42  ? 298 ILE B C     1 
ATOM   6354  O O     . ILE B 1 298 ? 21.547  2.026   93.509  1.00 86.00  ? 298 ILE B O     1 
ATOM   6355  C CB    . ILE B 1 298 ? 24.625  1.636   92.854  1.00 84.34  ? 298 ILE B CB    1 
ATOM   6356  C CG1   . ILE B 1 298 ? 24.030  2.481   91.719  1.00 101.04 ? 298 ILE B CG1   1 
ATOM   6357  C CG2   . ILE B 1 298 ? 25.798  0.794   92.364  1.00 80.38  ? 298 ILE B CG2   1 
ATOM   6358  C CD1   . ILE B 1 298 ? 23.690  3.913   92.108  1.00 106.65 ? 298 ILE B CD1   1 
ATOM   6359  N N     . PRO B 1 299 ? 22.486  1.841   95.519  1.00 79.23  ? 299 PRO B N     1 
ATOM   6360  C CA    . PRO B 1 299 ? 21.492  2.705   96.150  1.00 83.90  ? 299 PRO B CA    1 
ATOM   6361  C C     . PRO B 1 299 ? 21.675  4.197   95.864  1.00 78.10  ? 299 PRO B C     1 
ATOM   6362  O O     . PRO B 1 299 ? 22.785  4.673   95.649  1.00 74.28  ? 299 PRO B O     1 
ATOM   6363  C CB    . PRO B 1 299 ? 21.673  2.388   97.645  1.00 85.38  ? 299 PRO B CB    1 
ATOM   6364  C CG    . PRO B 1 299 ? 23.113  1.961   97.784  1.00 78.92  ? 299 PRO B CG    1 
ATOM   6365  C CD    . PRO B 1 299 ? 23.434  1.261   96.482  1.00 83.67  ? 299 PRO B CD    1 
ATOM   6366  N N     . PRO B 1 300 ? 20.576  4.984   95.847  1.00 90.03  ? 300 PRO B N     1 
ATOM   6367  C CA    . PRO B 1 300 ? 20.653  6.429   95.663  1.00 82.84  ? 300 PRO B CA    1 
ATOM   6368  C C     . PRO B 1 300 ? 21.748  7.112   96.462  1.00 72.32  ? 300 PRO B C     1 
ATOM   6369  O O     . PRO B 1 300 ? 22.213  8.147   96.015  1.00 67.62  ? 300 PRO B O     1 
ATOM   6370  C CB    . PRO B 1 300 ? 19.287  6.927   96.162  1.00 88.39  ? 300 PRO B CB    1 
ATOM   6371  C CG    . PRO B 1 300 ? 18.352  5.794   95.805  1.00 102.00 ? 300 PRO B CG    1 
ATOM   6372  C CD    . PRO B 1 300 ? 19.180  4.526   95.950  1.00 100.43 ? 300 PRO B CD    1 
ATOM   6373  N N     . SER B 1 301 ? 22.098  6.566   97.643  1.00 85.10  ? 301 SER B N     1 
ATOM   6374  C CA    . SER B 1 301 ? 23.073  7.170   98.556  1.00 88.65  ? 301 SER B CA    1 
ATOM   6375  C C     . SER B 1 301 ? 24.386  7.441   97.822  1.00 83.21  ? 301 SER B C     1 
ATOM   6376  O O     . SER B 1 301 ? 25.000  8.508   97.922  1.00 70.83  ? 301 SER B O     1 
ATOM   6377  C CB    . SER B 1 301 ? 23.360  6.274   99.772  1.00 86.14  ? 301 SER B CB    1 
ATOM   6378  O OG    . SER B 1 301 ? 22.189  5.637   100.261 1.00 95.41  ? 301 SER B OG    1 
ATOM   6379  N N     . VAL B 1 302 ? 24.799  6.414   97.084  1.00 75.25  ? 302 VAL B N     1 
ATOM   6380  C CA    . VAL B 1 302 ? 26.129  6.323   96.532  1.00 74.45  ? 302 VAL B CA    1 
ATOM   6381  C C     . VAL B 1 302 ? 26.288  7.330   95.401  1.00 72.12  ? 302 VAL B C     1 
ATOM   6382  O O     . VAL B 1 302 ? 27.384  7.831   95.181  1.00 83.25  ? 302 VAL B O     1 
ATOM   6383  C CB    . VAL B 1 302 ? 26.367  4.877   96.071  1.00 77.04  ? 302 VAL B CB    1 
ATOM   6384  C CG1   . VAL B 1 302 ? 27.693  4.708   95.359  1.00 82.38  ? 302 VAL B CG1   1 
ATOM   6385  C CG2   . VAL B 1 302 ? 26.273  3.918   97.246  1.00 73.65  ? 302 VAL B CG2   1 
ATOM   6386  N N     . ALA B 1 303 ? 25.178  7.646   94.726  1.00 67.31  ? 303 ALA B N     1 
ATOM   6387  C CA    . ALA B 1 303 ? 25.189  8.467   93.527  1.00 70.35  ? 303 ALA B CA    1 
ATOM   6388  C C     . ALA B 1 303 ? 25.890  9.802   93.767  1.00 69.59  ? 303 ALA B C     1 
ATOM   6389  O O     . ALA B 1 303 ? 26.690  10.224  92.943  1.00 77.92  ? 303 ALA B O     1 
ATOM   6390  C CB    . ALA B 1 303 ? 23.780  8.675   93.041  1.00 67.18  ? 303 ALA B CB    1 
ATOM   6391  N N     . LYS B 1 304 ? 25.587  10.470  94.882  1.00 71.80  ? 304 LYS B N     1 
ATOM   6392  C CA    . LYS B 1 304 ? 26.198  11.756  95.175  1.00 75.79  ? 304 LYS B CA    1 
ATOM   6393  C C     . LYS B 1 304 ? 27.712  11.618  95.320  1.00 72.46  ? 304 LYS B C     1 
ATOM   6394  O O     . LYS B 1 304 ? 28.439  12.561  95.025  1.00 64.40  ? 304 LYS B O     1 
ATOM   6395  C CB    . LYS B 1 304 ? 25.557  12.379  96.418  1.00 91.97  ? 304 LYS B CB    1 
ATOM   6396  C CG    . LYS B 1 304 ? 24.233  13.087  96.150  1.00 114.02 ? 304 LYS B CG    1 
ATOM   6397  C CD    . LYS B 1 304 ? 24.368  14.241  95.154  1.00 125.96 ? 304 LYS B CD    1 
ATOM   6398  C CE    . LYS B 1 304 ? 23.060  14.909  94.785  1.00 125.70 ? 304 LYS B CE    1 
ATOM   6399  N NZ    . LYS B 1 304 ? 22.656  15.897  95.810  1.00 130.47 ? 304 LYS B NZ    1 
ATOM   6400  N N     . THR B 1 305 ? 28.179  10.443  95.761  1.00 70.01  ? 305 THR B N     1 
ATOM   6401  C CA    . THR B 1 305 ? 29.601  10.177  95.929  1.00 71.77  ? 305 THR B CA    1 
ATOM   6402  C C     . THR B 1 305 ? 30.245  9.942   94.558  1.00 68.47  ? 305 THR B C     1 
ATOM   6403  O O     . THR B 1 305 ? 31.300  10.500  94.259  1.00 71.36  ? 305 THR B O     1 
ATOM   6404  C CB    . THR B 1 305 ? 29.789  9.053   96.962  1.00 77.11  ? 305 THR B CB    1 
ATOM   6405  O OG1   . THR B 1 305 ? 29.594  9.713   98.215  1.00 68.62  ? 305 THR B OG1   1 
ATOM   6406  C CG2   . THR B 1 305 ? 31.137  8.360   96.906  1.00 74.84  ? 305 THR B CG2   1 
ATOM   6407  N N     . MET B 1 306 ? 29.574  9.155   93.710  1.00 64.79  ? 306 MET B N     1 
ATOM   6408  C CA    . MET B 1 306 ? 30.032  8.862   92.362  1.00 52.82  ? 306 MET B CA    1 
ATOM   6409  C C     . MET B 1 306 ? 30.205  10.155  91.583  1.00 49.77  ? 306 MET B C     1 
ATOM   6410  O O     . MET B 1 306 ? 31.199  10.341  90.889  1.00 42.61  ? 306 MET B O     1 
ATOM   6411  C CB    . MET B 1 306 ? 29.026  7.951   91.664  1.00 56.42  ? 306 MET B CB    1 
ATOM   6412  C CG    . MET B 1 306 ? 28.995  6.574   92.278  1.00 58.21  ? 306 MET B CG    1 
ATOM   6413  S SD    . MET B 1 306 ? 27.963  5.377   91.400  1.00 64.51  ? 306 MET B SD    1 
ATOM   6414  C CE    . MET B 1 306 ? 29.035  5.002   90.022  1.00 66.16  ? 306 MET B CE    1 
ATOM   6415  N N     . MET B 1 307 ? 29.262  11.074  91.788  1.00 56.44  ? 307 MET B N     1 
ATOM   6416  C CA    . MET B 1 307 ? 29.236  12.370  91.116  1.00 59.70  ? 307 MET B CA    1 
ATOM   6417  C C     . MET B 1 307 ? 30.462  13.227  91.438  1.00 55.97  ? 307 MET B C     1 
ATOM   6418  O O     . MET B 1 307 ? 31.066  13.791  90.534  1.00 54.22  ? 307 MET B O     1 
ATOM   6419  C CB    . MET B 1 307 ? 27.956  13.126  91.483  1.00 55.85  ? 307 MET B CB    1 
ATOM   6420  C CG    . MET B 1 307 ? 26.791  12.701  90.597  1.00 61.94  ? 307 MET B CG    1 
ATOM   6421  S SD    . MET B 1 307 ? 25.192  13.170  91.256  1.00 68.38  ? 307 MET B SD    1 
ATOM   6422  C CE    . MET B 1 307 ? 25.383  14.959  91.290  1.00 52.31  ? 307 MET B CE    1 
ATOM   6423  N N     . ALA B 1 308 ? 30.802  13.356  92.721  1.00 61.39  ? 308 ALA B N     1 
ATOM   6424  C CA    . ALA B 1 308 ? 31.914  14.187  93.146  1.00 63.31  ? 308 ALA B CA    1 
ATOM   6425  C C     . ALA B 1 308 ? 33.247  13.563  92.713  1.00 59.50  ? 308 ALA B C     1 
ATOM   6426  O O     . ALA B 1 308 ? 34.116  14.286  92.243  1.00 58.90  ? 308 ALA B O     1 
ATOM   6427  C CB    . ALA B 1 308 ? 31.839  14.391  94.644  1.00 67.28  ? 308 ALA B CB    1 
ATOM   6428  N N     . ASP B 1 309 ? 33.383  12.234  92.877  1.00 57.50  ? 309 ASP B N     1 
ATOM   6429  C CA    . ASP B 1 309 ? 34.524  11.432  92.432  1.00 59.56  ? 309 ASP B CA    1 
ATOM   6430  C C     . ASP B 1 309 ? 34.839  11.695  90.950  1.00 64.34  ? 309 ASP B C     1 
ATOM   6431  O O     . ASP B 1 309 ? 35.947  12.121  90.609  1.00 67.62  ? 309 ASP B O     1 
ATOM   6432  C CB    . ASP B 1 309 ? 34.244  9.936   92.676  1.00 61.98  ? 309 ASP B CB    1 
ATOM   6433  C CG    . ASP B 1 309 ? 35.451  9.007   92.636  1.00 64.50  ? 309 ASP B CG    1 
ATOM   6434  O OD1   . ASP B 1 309 ? 36.344  9.172   93.481  1.00 74.36  ? 309 ASP B OD1   1 
ATOM   6435  O OD2   . ASP B 1 309 ? 35.487  8.118   91.779  1.00 55.33  ? 309 ASP B OD2   1 
ATOM   6436  N N     . LEU B 1 310 ? 33.842  11.469  90.079  1.00 62.39  ? 310 LEU B N     1 
ATOM   6437  C CA    . LEU B 1 310 ? 33.995  11.542  88.632  1.00 60.88  ? 310 LEU B CA    1 
ATOM   6438  C C     . LEU B 1 310 ? 33.815  12.955  88.038  1.00 62.67  ? 310 LEU B C     1 
ATOM   6439  O O     . LEU B 1 310 ? 34.041  13.128  86.842  1.00 58.01  ? 310 LEU B O     1 
ATOM   6440  C CB    . LEU B 1 310 ? 32.969  10.589  88.026  1.00 57.92  ? 310 LEU B CB    1 
ATOM   6441  C CG    . LEU B 1 310 ? 33.342  9.112   88.045  1.00 62.31  ? 310 LEU B CG    1 
ATOM   6442  C CD1   . LEU B 1 310 ? 32.076  8.273   88.154  1.00 66.30  ? 310 LEU B CD1   1 
ATOM   6443  C CD2   . LEU B 1 310 ? 34.114  8.716   86.784  1.00 62.92  ? 310 LEU B CD2   1 
ATOM   6444  N N     . ASP B 1 311 ? 33.425  13.974  88.821  1.00 59.46  ? 311 ASP B N     1 
ATOM   6445  C CA    . ASP B 1 311 ? 33.098  15.301  88.281  1.00 72.18  ? 311 ASP B CA    1 
ATOM   6446  C C     . ASP B 1 311 ? 32.070  15.233  87.146  1.00 66.62  ? 311 ASP B C     1 
ATOM   6447  O O     . ASP B 1 311 ? 32.116  16.025  86.207  1.00 75.19  ? 311 ASP B O     1 
ATOM   6448  C CB    . ASP B 1 311 ? 34.329  16.072  87.792  1.00 78.06  ? 311 ASP B CB    1 
ATOM   6449  C CG    . ASP B 1 311 ? 35.072  16.788  88.901  1.00 86.67  ? 311 ASP B CG    1 
ATOM   6450  O OD1   . ASP B 1 311 ? 35.625  16.093  89.779  1.00 109.98 ? 311 ASP B OD1   1 
ATOM   6451  O OD2   . ASP B 1 311 ? 35.083  18.030  88.883  1.00 94.28  ? 311 ASP B OD2   1 
ATOM   6452  N N     . LEU B 1 312 ? 31.111  14.315  87.285  1.00 58.31  ? 312 LEU B N     1 
ATOM   6453  C CA    . LEU B 1 312 ? 29.962  14.187  86.407  1.00 54.75  ? 312 LEU B CA    1 
ATOM   6454  C C     . LEU B 1 312 ? 28.675  14.583  87.150  1.00 58.89  ? 312 LEU B C     1 
ATOM   6455  O O     . LEU B 1 312 ? 28.661  15.018  88.318  1.00 58.34  ? 312 LEU B O     1 
ATOM   6456  C CB    . LEU B 1 312 ? 29.897  12.724  85.923  1.00 56.23  ? 312 LEU B CB    1 
ATOM   6457  C CG    . LEU B 1 312 ? 31.023  12.278  84.985  1.00 55.21  ? 312 LEU B CG    1 
ATOM   6458  C CD1   . LEU B 1 312 ? 30.942  10.792  84.665  1.00 58.77  ? 312 LEU B CD1   1 
ATOM   6459  C CD2   . LEU B 1 312 ? 31.015  13.081  83.694  1.00 56.12  ? 312 LEU B CD2   1 
ATOM   6460  N N     . GLY B 1 313 ? 27.560  14.427  86.432  1.00 56.19  ? 313 GLY B N     1 
ATOM   6461  C CA    . GLY B 1 313 ? 26.236  14.591  86.997  1.00 48.67  ? 313 GLY B CA    1 
ATOM   6462  C C     . GLY B 1 313 ? 25.440  13.298  86.895  1.00 49.88  ? 313 GLY B C     1 
ATOM   6463  O O     . GLY B 1 313 ? 25.979  12.223  86.603  1.00 46.00  ? 313 GLY B O     1 
ATOM   6464  N N     . MET B 1 314 ? 24.133  13.449  87.117  1.00 49.13  ? 314 MET B N     1 
ATOM   6465  C CA    . MET B 1 314 ? 23.168  12.380  86.920  1.00 51.46  ? 314 MET B CA    1 
ATOM   6466  C C     . MET B 1 314 ? 22.929  12.182  85.420  1.00 50.19  ? 314 MET B C     1 
ATOM   6467  O O     . MET B 1 314 ? 22.754  11.060  84.951  1.00 47.33  ? 314 MET B O     1 
ATOM   6468  C CB    . MET B 1 314 ? 21.874  12.723  87.675  1.00 52.28  ? 314 MET B CB    1 
ATOM   6469  C CG    . MET B 1 314 ? 22.041  12.679  89.213  1.00 49.96  ? 314 MET B CG    1 
ATOM   6470  S SD    . MET B 1 314 ? 22.496  10.993  89.829  1.00 59.48  ? 314 MET B SD    1 
ATOM   6471  C CE    . MET B 1 314 ? 21.088  10.033  89.277  1.00 63.06  ? 314 MET B CE    1 
ATOM   6472  N N     . TRP B 1 315 ? 22.927  13.285  84.663  1.00 49.28  ? 315 TRP B N     1 
ATOM   6473  C CA    . TRP B 1 315 ? 22.876  13.206  83.213  1.00 54.10  ? 315 TRP B CA    1 
ATOM   6474  C C     . TRP B 1 315 ? 23.982  14.080  82.652  1.00 50.26  ? 315 TRP B C     1 
ATOM   6475  O O     . TRP B 1 315 ? 24.247  15.144  83.218  1.00 48.80  ? 315 TRP B O     1 
ATOM   6476  C CB    . TRP B 1 315 ? 21.505  13.624  82.679  1.00 56.34  ? 315 TRP B CB    1 
ATOM   6477  C CG    . TRP B 1 315 ? 20.396  12.713  83.100  1.00 51.64  ? 315 TRP B CG    1 
ATOM   6478  C CD1   . TRP B 1 315 ? 19.446  12.977  84.036  1.00 51.66  ? 315 TRP B CD1   1 
ATOM   6479  C CD2   . TRP B 1 315 ? 20.078  11.419  82.568  1.00 49.82  ? 315 TRP B CD2   1 
ATOM   6480  N NE1   . TRP B 1 315 ? 18.578  11.922  84.143  1.00 54.49  ? 315 TRP B NE1   1 
ATOM   6481  C CE2   . TRP B 1 315 ? 18.938  10.952  83.260  1.00 49.45  ? 315 TRP B CE2   1 
ATOM   6482  C CE3   . TRP B 1 315 ? 20.653  10.598  81.598  1.00 49.31  ? 315 TRP B CE3   1 
ATOM   6483  C CZ2   . TRP B 1 315 ? 18.353  9.714   83.015  1.00 51.60  ? 315 TRP B CZ2   1 
ATOM   6484  C CZ3   . TRP B 1 315 ? 20.070  9.372   81.347  1.00 62.19  ? 315 TRP B CZ3   1 
ATOM   6485  C CH2   . TRP B 1 315 ? 18.930  8.939   82.040  1.00 56.47  ? 315 TRP B CH2   1 
ATOM   6486  N N     . ASN B 1 316 ? 24.624  13.587  81.578  1.00 47.90  ? 316 ASN B N     1 
ATOM   6487  C CA    . ASN B 1 316 ? 25.851  14.183  81.045  1.00 50.86  ? 316 ASN B CA    1 
ATOM   6488  C C     . ASN B 1 316 ? 25.775  14.268  79.515  1.00 49.01  ? 316 ASN B C     1 
ATOM   6489  O O     . ASN B 1 316 ? 25.849  13.247  78.822  1.00 45.70  ? 316 ASN B O     1 
ATOM   6490  C CB    . ASN B 1 316 ? 27.092  13.420  81.532  1.00 49.66  ? 316 ASN B CB    1 
ATOM   6491  C CG    . ASN B 1 316 ? 27.224  13.435  83.046  1.00 53.94  ? 316 ASN B CG    1 
ATOM   6492  O OD1   . ASN B 1 316 ? 27.365  14.496  83.651  1.00 45.93  ? 316 ASN B OD1   1 
ATOM   6493  N ND2   . ASN B 1 316 ? 27.116  12.279  83.681  1.00 50.69  ? 316 ASN B ND2   1 
ATOM   6494  N N     . PHE B 1 317 ? 25.647  15.511  79.014  1.00 48.38  ? 317 PHE B N     1 
ATOM   6495  C CA    . PHE B 1 317 ? 25.482  15.820  77.597  1.00 45.24  ? 317 PHE B CA    1 
ATOM   6496  C C     . PHE B 1 317 ? 26.794  16.332  77.005  1.00 43.54  ? 317 PHE B C     1 
ATOM   6497  O O     . PHE B 1 317 ? 27.218  17.467  77.278  1.00 44.40  ? 317 PHE B O     1 
ATOM   6498  C CB    . PHE B 1 317 ? 24.376  16.864  77.430  1.00 42.49  ? 317 PHE B CB    1 
ATOM   6499  C CG    . PHE B 1 317 ? 24.343  17.575  76.101  1.00 41.65  ? 317 PHE B CG    1 
ATOM   6500  C CD1   . PHE B 1 317 ? 24.500  16.880  74.913  1.00 39.51  ? 317 PHE B CD1   1 
ATOM   6501  C CD2   . PHE B 1 317 ? 24.147  18.949  76.038  1.00 37.78  ? 317 PHE B CD2   1 
ATOM   6502  C CE1   . PHE B 1 317 ? 24.477  17.546  73.698  1.00 37.51  ? 317 PHE B CE1   1 
ATOM   6503  C CE2   . PHE B 1 317 ? 24.089  19.607  74.821  1.00 35.64  ? 317 PHE B CE2   1 
ATOM   6504  C CZ    . PHE B 1 317 ? 24.292  18.914  73.658  1.00 37.59  ? 317 PHE B CZ    1 
ATOM   6505  N N     . CYS B 1 318 ? 27.446  15.504  76.191  1.00 42.33  ? 318 CYS B N     1 
ATOM   6506  C CA    . CYS B 1 318 ? 28.570  16.023  75.427  1.00 62.16  ? 318 CYS B CA    1 
ATOM   6507  C C     . CYS B 1 318 ? 28.189  16.083  73.949  1.00 55.67  ? 318 CYS B C     1 
ATOM   6508  O O     . CYS B 1 318 ? 27.494  15.211  73.441  1.00 48.73  ? 318 CYS B O     1 
ATOM   6509  C CB    . CYS B 1 318 ? 29.892  15.304  75.702  1.00 67.90  ? 318 CYS B CB    1 
ATOM   6510  S SG    . CYS B 1 318 ? 29.832  13.527  75.419  1.00 94.23  ? 318 CYS B SG    1 
ATOM   6511  N N     . GLY B 1 319 ? 28.563  17.211  73.338  1.00 61.99  ? 319 GLY B N     1 
ATOM   6512  C CA    . GLY B 1 319 ? 28.491  17.437  71.905  1.00 64.90  ? 319 GLY B CA    1 
ATOM   6513  C C     . GLY B 1 319 ? 29.715  18.223  71.427  1.00 56.60  ? 319 GLY B C     1 
ATOM   6514  O O     . GLY B 1 319 ? 30.701  18.396  72.148  1.00 56.09  ? 319 GLY B O     1 
ATOM   6515  N N     . ALA B 1 320 ? 29.634  18.720  70.197  1.00 52.53  ? 320 ALA B N     1 
ATOM   6516  C CA    . ALA B 1 320 ? 30.726  19.478  69.617  1.00 50.88  ? 320 ALA B CA    1 
ATOM   6517  C C     . ALA B 1 320 ? 30.197  20.505  68.623  1.00 47.35  ? 320 ALA B C     1 
ATOM   6518  O O     . ALA B 1 320 ? 29.172  20.302  67.958  1.00 50.67  ? 320 ALA B O     1 
ATOM   6519  C CB    . ALA B 1 320 ? 31.713  18.549  68.969  1.00 55.56  ? 320 ALA B CB    1 
ATOM   6520  N N     . LEU B 1 321 ? 30.918  21.627  68.584  1.00 41.92  ? 321 LEU B N     1 
ATOM   6521  C CA    . LEU B 1 321 ? 30.688  22.670  67.611  1.00 43.47  ? 321 LEU B CA    1 
ATOM   6522  C C     . LEU B 1 321 ? 31.746  22.513  66.530  1.00 43.97  ? 321 LEU B C     1 
ATOM   6523  O O     . LEU B 1 321 ? 32.912  22.238  66.851  1.00 46.57  ? 321 LEU B O     1 
ATOM   6524  C CB    . LEU B 1 321 ? 30.829  24.043  68.265  1.00 45.09  ? 321 LEU B CB    1 
ATOM   6525  C CG    . LEU B 1 321 ? 30.281  24.174  69.677  1.00 49.15  ? 321 LEU B CG    1 
ATOM   6526  C CD1   . LEU B 1 321 ? 30.916  25.369  70.372  1.00 51.31  ? 321 LEU B CD1   1 
ATOM   6527  C CD2   . LEU B 1 321 ? 28.763  24.300  69.652  1.00 55.17  ? 321 LEU B CD2   1 
ATOM   6528  N N     . TYR B 1 322 ? 31.332  22.716  65.271  1.00 38.26  ? 322 TYR B N     1 
ATOM   6529  C CA    . TYR B 1 322 ? 32.256  22.599  64.162  1.00 41.58  ? 322 TYR B CA    1 
ATOM   6530  C C     . TYR B 1 322 ? 32.073  23.813  63.270  1.00 47.46  ? 322 TYR B C     1 
ATOM   6531  O O     . TYR B 1 322 ? 30.940  24.166  62.981  1.00 48.46  ? 322 TYR B O     1 
ATOM   6532  C CB    . TYR B 1 322 ? 32.036  21.320  63.353  1.00 40.45  ? 322 TYR B CB    1 
ATOM   6533  C CG    . TYR B 1 322 ? 31.794  20.033  64.112  1.00 39.60  ? 322 TYR B CG    1 
ATOM   6534  C CD1   . TYR B 1 322 ? 30.617  19.819  64.816  1.00 41.36  ? 322 TYR B CD1   1 
ATOM   6535  C CD2   . TYR B 1 322 ? 32.676  18.973  64.019  1.00 42.98  ? 322 TYR B CD2   1 
ATOM   6536  C CE1   . TYR B 1 322 ? 30.358  18.617  65.457  1.00 42.10  ? 322 TYR B CE1   1 
ATOM   6537  C CE2   . TYR B 1 322 ? 32.439  17.760  64.658  1.00 46.38  ? 322 TYR B CE2   1 
ATOM   6538  C CZ    . TYR B 1 322 ? 31.275  17.585  65.390  1.00 42.87  ? 322 TYR B CZ    1 
ATOM   6539  O OH    . TYR B 1 322 ? 31.009  16.412  66.041  1.00 43.25  ? 322 TYR B OH    1 
ATOM   6540  N N     . GLY B 1 323 ? 33.188  24.432  62.854  1.00 52.15  ? 323 GLY B N     1 
ATOM   6541  C CA    . GLY B 1 323 ? 33.133  25.620  62.020  1.00 54.06  ? 323 GLY B CA    1 
ATOM   6542  C C     . GLY B 1 323 ? 34.286  26.606  62.247  1.00 52.99  ? 323 GLY B C     1 
ATOM   6543  O O     . GLY B 1 323 ? 35.167  26.399  63.073  1.00 46.77  ? 323 GLY B O     1 
ATOM   6544  N N     . PRO B 1 324 ? 34.326  27.728  61.490  1.00 58.56  ? 324 PRO B N     1 
ATOM   6545  C CA    . PRO B 1 324 ? 35.234  28.822  61.829  1.00 62.20  ? 324 PRO B CA    1 
ATOM   6546  C C     . PRO B 1 324 ? 34.823  29.326  63.207  1.00 64.37  ? 324 PRO B C     1 
ATOM   6547  O O     . PRO B 1 324 ? 33.636  29.251  63.540  1.00 65.93  ? 324 PRO B O     1 
ATOM   6548  C CB    . PRO B 1 324 ? 35.007  29.875  60.730  1.00 65.49  ? 324 PRO B CB    1 
ATOM   6549  C CG    . PRO B 1 324 ? 33.667  29.503  60.062  1.00 56.84  ? 324 PRO B CG    1 
ATOM   6550  C CD    . PRO B 1 324 ? 33.472  28.021  60.317  1.00 55.06  ? 324 PRO B CD    1 
ATOM   6551  N N     . PRO B 1 325 ? 35.761  29.845  64.038  1.00 74.14  ? 325 PRO B N     1 
ATOM   6552  C CA    . PRO B 1 325 ? 35.411  30.315  65.390  1.00 77.11  ? 325 PRO B CA    1 
ATOM   6553  C C     . PRO B 1 325 ? 34.211  31.280  65.493  1.00 77.67  ? 325 PRO B C     1 
ATOM   6554  O O     . PRO B 1 325 ? 33.345  31.122  66.360  1.00 64.65  ? 325 PRO B O     1 
ATOM   6555  C CB    . PRO B 1 325 ? 36.741  30.909  65.895  1.00 73.58  ? 325 PRO B CB    1 
ATOM   6556  C CG    . PRO B 1 325 ? 37.815  30.163  65.116  1.00 71.53  ? 325 PRO B CG    1 
ATOM   6557  C CD    . PRO B 1 325 ? 37.207  29.949  63.743  1.00 70.29  ? 325 PRO B CD    1 
ATOM   6558  N N     . PRO B 1 326 ? 34.072  32.312  64.631  1.00 74.30  ? 326 PRO B N     1 
ATOM   6559  C CA    . PRO B 1 326 ? 32.855  33.129  64.631  1.00 75.40  ? 326 PRO B CA    1 
ATOM   6560  C C     . PRO B 1 326 ? 31.524  32.381  64.639  1.00 68.45  ? 326 PRO B C     1 
ATOM   6561  O O     . PRO B 1 326 ? 30.584  32.842  65.277  1.00 75.34  ? 326 PRO B O     1 
ATOM   6562  C CB    . PRO B 1 326 ? 32.998  33.941  63.332  1.00 78.40  ? 326 PRO B CB    1 
ATOM   6563  C CG    . PRO B 1 326 ? 34.498  34.135  63.202  1.00 73.94  ? 326 PRO B CG    1 
ATOM   6564  C CD    . PRO B 1 326 ? 35.095  32.831  63.707  1.00 74.41  ? 326 PRO B CD    1 
ATOM   6565  N N     . VAL B 1 327 ? 31.438  31.251  63.922  1.00 69.71  ? 327 VAL B N     1 
ATOM   6566  C CA    . VAL B 1 327 ? 30.198  30.487  63.811  1.00 65.94  ? 327 VAL B CA    1 
ATOM   6567  C C     . VAL B 1 327 ? 30.001  29.613  65.051  1.00 66.34  ? 327 VAL B C     1 
ATOM   6568  O O     . VAL B 1 327 ? 28.869  29.410  65.491  1.00 58.09  ? 327 VAL B O     1 
ATOM   6569  C CB    . VAL B 1 327 ? 30.170  29.640  62.517  1.00 66.65  ? 327 VAL B CB    1 
ATOM   6570  C CG1   . VAL B 1 327 ? 29.034  28.620  62.489  1.00 60.88  ? 327 VAL B CG1   1 
ATOM   6571  C CG2   . VAL B 1 327 ? 30.091  30.526  61.288  1.00 68.23  ? 327 VAL B CG2   1 
ATOM   6572  N N     . MET B 1 328 ? 31.104  29.056  65.578  1.00 68.25  ? 328 MET B N     1 
ATOM   6573  C CA    . MET B 1 328 ? 31.046  28.223  66.769  1.00 64.55  ? 328 MET B CA    1 
ATOM   6574  C C     . MET B 1 328 ? 30.568  29.087  67.935  1.00 69.47  ? 328 MET B C     1 
ATOM   6575  O O     . MET B 1 328 ? 29.700  28.667  68.697  1.00 70.61  ? 328 MET B O     1 
ATOM   6576  C CB    . MET B 1 328 ? 32.405  27.572  67.074  1.00 60.16  ? 328 MET B CB    1 
ATOM   6577  C CG    . MET B 1 328 ? 32.669  26.322  66.195  1.00 66.15  ? 328 MET B CG    1 
ATOM   6578  S SD    . MET B 1 328 ? 34.148  25.309  66.573  1.00 57.80  ? 328 MET B SD    1 
ATOM   6579  C CE    . MET B 1 328 ? 35.395  26.593  66.606  1.00 57.62  ? 328 MET B CE    1 
ATOM   6580  N N     . ASP B 1 329 ? 31.089  30.320  68.023  1.00 64.75  ? 329 ASP B N     1 
ATOM   6581  C CA    . ASP B 1 329 ? 30.728  31.237  69.093  1.00 63.35  ? 329 ASP B CA    1 
ATOM   6582  C C     . ASP B 1 329 ? 29.219  31.440  69.134  1.00 57.25  ? 329 ASP B C     1 
ATOM   6583  O O     . ASP B 1 329 ? 28.611  31.354  70.202  1.00 56.96  ? 329 ASP B O     1 
ATOM   6584  C CB    . ASP B 1 329 ? 31.441  32.577  68.932  1.00 64.46  ? 329 ASP B CB    1 
ATOM   6585  C CG    . ASP B 1 329 ? 32.911  32.521  69.305  1.00 63.78  ? 329 ASP B CG    1 
ATOM   6586  O OD1   . ASP B 1 329 ? 33.369  31.449  69.726  1.00 64.05  ? 329 ASP B OD1   1 
ATOM   6587  O OD2   . ASP B 1 329 ? 33.581  33.548  69.162  1.00 72.38  ? 329 ASP B OD2   1 
ATOM   6588  N N     . THR B 1 330 ? 28.636  31.684  67.957  1.00 53.35  ? 330 THR B N     1 
ATOM   6589  C CA    . THR B 1 330 ? 27.222  32.005  67.827  1.00 54.46  ? 330 THR B CA    1 
ATOM   6590  C C     . THR B 1 330 ? 26.396  30.822  68.323  1.00 57.29  ? 330 THR B C     1 
ATOM   6591  O O     . THR B 1 330 ? 25.380  30.985  69.009  1.00 60.92  ? 330 THR B O     1 
ATOM   6592  C CB    . THR B 1 330 ? 26.914  32.466  66.391  1.00 56.60  ? 330 THR B CB    1 
ATOM   6593  O OG1   . THR B 1 330 ? 27.581  33.713  66.177  1.00 48.53  ? 330 THR B OG1   1 
ATOM   6594  C CG2   . THR B 1 330 ? 25.438  32.652  66.101  1.00 56.87  ? 330 THR B CG2   1 
ATOM   6595  N N     . LEU B 1 331 ? 26.873  29.619  68.003  1.00 62.30  ? 331 LEU B N     1 
ATOM   6596  C CA    . LEU B 1 331 ? 26.160  28.397  68.344  1.00 62.71  ? 331 LEU B CA    1 
ATOM   6597  C C     . LEU B 1 331 ? 26.247  28.105  69.850  1.00 62.07  ? 331 LEU B C     1 
ATOM   6598  O O     . LEU B 1 331 ? 25.242  27.779  70.501  1.00 51.27  ? 331 LEU B O     1 
ATOM   6599  C CB    . LEU B 1 331 ? 26.764  27.281  67.491  1.00 63.07  ? 331 LEU B CB    1 
ATOM   6600  C CG    . LEU B 1 331 ? 26.628  27.470  65.977  1.00 59.77  ? 331 LEU B CG    1 
ATOM   6601  C CD1   . LEU B 1 331 ? 27.514  26.471  65.252  1.00 65.49  ? 331 LEU B CD1   1 
ATOM   6602  C CD2   . LEU B 1 331 ? 25.186  27.315  65.526  1.00 54.81  ? 331 LEU B CD2   1 
ATOM   6603  N N     . TRP B 1 332 ? 27.461  28.246  70.397  1.00 52.60  ? 332 TRP B N     1 
ATOM   6604  C CA    . TRP B 1 332 ? 27.706  28.010  71.805  1.00 53.69  ? 332 TRP B CA    1 
ATOM   6605  C C     . TRP B 1 332 ? 26.761  28.848  72.664  1.00 51.33  ? 332 TRP B C     1 
ATOM   6606  O O     . TRP B 1 332 ? 26.048  28.308  73.509  1.00 50.65  ? 332 TRP B O     1 
ATOM   6607  C CB    . TRP B 1 332 ? 29.176  28.302  72.140  1.00 54.95  ? 332 TRP B CB    1 
ATOM   6608  C CG    . TRP B 1 332 ? 29.435  28.064  73.586  1.00 53.99  ? 332 TRP B CG    1 
ATOM   6609  C CD1   . TRP B 1 332 ? 29.921  28.943  74.507  1.00 59.94  ? 332 TRP B CD1   1 
ATOM   6610  C CD2   . TRP B 1 332 ? 29.112  26.860  74.299  1.00 52.33  ? 332 TRP B CD2   1 
ATOM   6611  N NE1   . TRP B 1 332 ? 29.982  28.339  75.736  1.00 62.57  ? 332 TRP B NE1   1 
ATOM   6612  C CE2   . TRP B 1 332 ? 29.480  27.066  75.639  1.00 53.62  ? 332 TRP B CE2   1 
ATOM   6613  C CE3   . TRP B 1 332 ? 28.596  25.620  73.924  1.00 54.07  ? 332 TRP B CE3   1 
ATOM   6614  C CZ2   . TRP B 1 332 ? 29.337  26.074  76.600  1.00 56.50  ? 332 TRP B CZ2   1 
ATOM   6615  C CZ3   . TRP B 1 332 ? 28.429  24.647  74.875  1.00 52.91  ? 332 TRP B CZ3   1 
ATOM   6616  C CH2   . TRP B 1 332 ? 28.801  24.873  76.195  1.00 58.27  ? 332 TRP B CH2   1 
ATOM   6617  N N     . THR B 1 333 ? 26.765  30.162  72.389  1.00 52.52  ? 333 THR B N     1 
ATOM   6618  C CA    . THR B 1 333 ? 25.840  31.122  72.953  1.00 48.86  ? 333 THR B CA    1 
ATOM   6619  C C     . THR B 1 333 ? 24.413  30.610  72.886  1.00 50.00  ? 333 THR B C     1 
ATOM   6620  O O     . THR B 1 333 ? 23.726  30.648  73.888  1.00 57.05  ? 333 THR B O     1 
ATOM   6621  C CB    . THR B 1 333 ? 25.919  32.476  72.246  1.00 54.92  ? 333 THR B CB    1 
ATOM   6622  O OG1   . THR B 1 333 ? 27.163  33.060  72.642  1.00 56.48  ? 333 THR B OG1   1 
ATOM   6623  C CG2   . THR B 1 333 ? 24.755  33.385  72.585  1.00 53.47  ? 333 THR B CG2   1 
ATOM   6624  N N     . ALA B 1 334 ? 23.962  30.133  71.731  1.00 55.27  ? 334 ALA B N     1 
ATOM   6625  C CA    . ALA B 1 334 ? 22.590  29.656  71.648  1.00 64.49  ? 334 ALA B CA    1 
ATOM   6626  C C     . ALA B 1 334 ? 22.397  28.386  72.482  1.00 64.32  ? 334 ALA B C     1 
ATOM   6627  O O     . ALA B 1 334 ? 21.289  28.139  72.977  1.00 62.90  ? 334 ALA B O     1 
ATOM   6628  C CB    . ALA B 1 334 ? 22.194  29.427  70.213  1.00 69.47  ? 334 ALA B CB    1 
ATOM   6629  N N     . ILE B 1 335 ? 23.469  27.598  72.662  1.00 53.64  ? 335 ILE B N     1 
ATOM   6630  C CA    . ILE B 1 335 ? 23.346  26.325  73.361  1.00 55.70  ? 335 ILE B CA    1 
ATOM   6631  C C     . ILE B 1 335 ? 23.526  26.523  74.871  1.00 60.46  ? 335 ILE B C     1 
ATOM   6632  O O     . ILE B 1 335 ? 22.763  25.953  75.668  1.00 53.28  ? 335 ILE B O     1 
ATOM   6633  C CB    . ILE B 1 335 ? 24.327  25.293  72.775  1.00 52.01  ? 335 ILE B CB    1 
ATOM   6634  C CG1   . ILE B 1 335 ? 23.937  24.906  71.344  1.00 50.84  ? 335 ILE B CG1   1 
ATOM   6635  C CG2   . ILE B 1 335 ? 24.451  24.068  73.670  1.00 54.07  ? 335 ILE B CG2   1 
ATOM   6636  C CD1   . ILE B 1 335 ? 25.060  24.296  70.528  1.00 46.48  ? 335 ILE B CD1   1 
ATOM   6637  N N     . ARG B 1 336 ? 24.520  27.330  75.270  1.00 58.28  ? 336 ARG B N     1 
ATOM   6638  C CA    . ARG B 1 336 ? 24.695  27.618  76.688  1.00 61.79  ? 336 ARG B CA    1 
ATOM   6639  C C     . ARG B 1 336 ? 23.429  28.299  77.218  1.00 57.66  ? 336 ARG B C     1 
ATOM   6640  O O     . ARG B 1 336 ? 22.907  27.881  78.238  1.00 54.44  ? 336 ARG B O     1 
ATOM   6641  C CB    . ARG B 1 336 ? 25.965  28.427  76.995  1.00 61.72  ? 336 ARG B CB    1 
ATOM   6642  C CG    . ARG B 1 336 ? 26.461  28.248  78.429  1.00 72.85  ? 336 ARG B CG    1 
ATOM   6643  C CD    . ARG B 1 336 ? 27.593  29.154  78.906  1.00 76.43  ? 336 ARG B CD    1 
ATOM   6644  N NE    . ARG B 1 336 ? 27.132  30.351  79.610  1.00 99.77  ? 336 ARG B NE    1 
ATOM   6645  C CZ    . ARG B 1 336 ? 27.096  31.591  79.101  1.00 119.20 ? 336 ARG B CZ    1 
ATOM   6646  N NH1   . ARG B 1 336 ? 27.401  31.812  77.831  1.00 122.17 ? 336 ARG B NH1   1 
ATOM   6647  N NH2   . ARG B 1 336 ? 26.736  32.615  79.862  1.00 106.87 ? 336 ARG B NH2   1 
ATOM   6648  N N     . ASP B 1 337 ? 22.881  29.295  76.505  1.00 62.21  ? 337 ASP B N     1 
ATOM   6649  C CA    . ASP B 1 337 ? 21.714  30.023  77.000  1.00 60.47  ? 337 ASP B CA    1 
ATOM   6650  C C     . ASP B 1 337 ? 20.488  29.113  77.102  1.00 53.96  ? 337 ASP B C     1 
ATOM   6651  O O     . ASP B 1 337 ? 19.633  29.340  77.937  1.00 50.81  ? 337 ASP B O     1 
ATOM   6652  C CB    . ASP B 1 337 ? 21.440  31.302  76.202  1.00 57.53  ? 337 ASP B CB    1 
ATOM   6653  C CG    . ASP B 1 337 ? 22.575  32.316  76.304  1.00 64.69  ? 337 ASP B CG    1 
ATOM   6654  O OD1   . ASP B 1 337 ? 23.584  31.999  76.983  1.00 69.22  ? 337 ASP B OD1   1 
ATOM   6655  O OD2   . ASP B 1 337 ? 22.458  33.416  75.700  1.00 60.60  ? 337 ASP B OD2   1 
ATOM   6656  N N     . SER B 1 338 ? 20.408  28.048  76.311  1.00 59.04  ? 338 SER B N     1 
ATOM   6657  C CA    . SER B 1 338 ? 19.289  27.121  76.421  1.00 58.88  ? 338 SER B CA    1 
ATOM   6658  C C     . SER B 1 338 ? 19.265  26.397  77.762  1.00 52.00  ? 338 SER B C     1 
ATOM   6659  O O     . SER B 1 338 ? 18.214  25.950  78.182  1.00 65.70  ? 338 SER B O     1 
ATOM   6660  C CB    . SER B 1 338 ? 19.283  26.132  75.282  1.00 59.86  ? 338 SER B CB    1 
ATOM   6661  O OG    . SER B 1 338 ? 18.889  26.772  74.069  1.00 63.18  ? 338 SER B OG    1 
ATOM   6662  N N     . PHE B 1 339 ? 20.402  26.261  78.437  1.00 56.89  ? 339 PHE B N     1 
ATOM   6663  C CA    . PHE B 1 339 ? 20.464  25.430  79.632  1.00 59.46  ? 339 PHE B CA    1 
ATOM   6664  C C     . PHE B 1 339 ? 20.896  26.188  80.896  1.00 55.46  ? 339 PHE B C     1 
ATOM   6665  O O     . PHE B 1 339 ? 20.862  25.607  81.983  1.00 45.19  ? 339 PHE B O     1 
ATOM   6666  C CB    . PHE B 1 339 ? 21.440  24.280  79.391  1.00 59.24  ? 339 PHE B CB    1 
ATOM   6667  C CG    . PHE B 1 339 ? 21.008  23.296  78.338  1.00 58.20  ? 339 PHE B CG    1 
ATOM   6668  C CD1   . PHE B 1 339 ? 20.044  22.348  78.625  1.00 50.20  ? 339 PHE B CD1   1 
ATOM   6669  C CD2   . PHE B 1 339 ? 21.573  23.318  77.066  1.00 61.80  ? 339 PHE B CD2   1 
ATOM   6670  C CE1   . PHE B 1 339 ? 19.682  21.414  77.678  1.00 49.88  ? 339 PHE B CE1   1 
ATOM   6671  C CE2   . PHE B 1 339 ? 21.176  22.407  76.105  1.00 53.12  ? 339 PHE B CE2   1 
ATOM   6672  C CZ    . PHE B 1 339 ? 20.226  21.465  76.415  1.00 51.86  ? 339 PHE B CZ    1 
ATOM   6673  N N     . ALA B 1 340 ? 21.273  27.471  80.767  1.00 51.45  ? 340 ALA B N     1 
ATOM   6674  C CA    . ALA B 1 340 ? 21.952  28.209  81.828  1.00 58.38  ? 340 ALA B CA    1 
ATOM   6675  C C     . ALA B 1 340 ? 21.088  28.316  83.089  1.00 59.47  ? 340 ALA B C     1 
ATOM   6676  O O     . ALA B 1 340 ? 21.637  28.392  84.180  1.00 62.70  ? 340 ALA B O     1 
ATOM   6677  C CB    . ALA B 1 340 ? 22.369  29.585  81.337  1.00 54.64  ? 340 ALA B CB    1 
ATOM   6678  N N     . ASP B 1 341 ? 19.756  28.307  82.932  1.00 62.51  ? 341 ASP B N     1 
ATOM   6679  C CA    . ASP B 1 341 ? 18.828  28.614  84.003  1.00 58.92  ? 341 ASP B CA    1 
ATOM   6680  C C     . ASP B 1 341 ? 18.410  27.344  84.743  1.00 60.47  ? 341 ASP B C     1 
ATOM   6681  O O     . ASP B 1 341 ? 17.488  27.381  85.554  1.00 76.76  ? 341 ASP B O     1 
ATOM   6682  C CB    . ASP B 1 341 ? 17.606  29.382  83.477  1.00 61.67  ? 341 ASP B CB    1 
ATOM   6683  C CG    . ASP B 1 341 ? 16.598  28.569  82.670  1.00 66.49  ? 341 ASP B CG    1 
ATOM   6684  O OD1   . ASP B 1 341 ? 16.126  27.538  83.164  1.00 71.87  ? 341 ASP B OD1   1 
ATOM   6685  O OD2   . ASP B 1 341 ? 16.282  28.976  81.544  1.00 74.24  ? 341 ASP B OD2   1 
ATOM   6686  N N     . ILE B 1 342 ? 19.049  26.204  84.488  1.00 59.44  ? 342 ILE B N     1 
ATOM   6687  C CA    . ILE B 1 342 ? 18.672  25.010  85.234  1.00 59.13  ? 342 ILE B CA    1 
ATOM   6688  C C     . ILE B 1 342 ? 19.441  25.027  86.549  1.00 72.48  ? 342 ILE B C     1 
ATOM   6689  O O     . ILE B 1 342 ? 20.625  25.376  86.585  1.00 77.29  ? 342 ILE B O     1 
ATOM   6690  C CB    . ILE B 1 342 ? 18.893  23.702  84.447  1.00 59.76  ? 342 ILE B CB    1 
ATOM   6691  C CG1   . ILE B 1 342 ? 18.005  23.630  83.194  1.00 60.40  ? 342 ILE B CG1   1 
ATOM   6692  C CG2   . ILE B 1 342 ? 18.696  22.491  85.353  1.00 63.48  ? 342 ILE B CG2   1 
ATOM   6693  C CD1   . ILE B 1 342 ? 18.269  22.434  82.281  1.00 55.72  ? 342 ILE B CD1   1 
ATOM   6694  N N     . PRO B 1 343 ? 18.767  24.719  87.678  1.00 67.82  ? 343 PRO B N     1 
ATOM   6695  C CA    . PRO B 1 343 ? 19.472  24.498  88.931  1.00 56.58  ? 343 PRO B CA    1 
ATOM   6696  C C     . PRO B 1 343 ? 20.449  23.334  88.805  1.00 60.63  ? 343 PRO B C     1 
ATOM   6697  O O     . PRO B 1 343 ? 20.041  22.210  88.493  1.00 64.59  ? 343 PRO B O     1 
ATOM   6698  C CB    . PRO B 1 343 ? 18.362  24.182  89.939  1.00 60.70  ? 343 PRO B CB    1 
ATOM   6699  C CG    . PRO B 1 343 ? 17.074  24.665  89.298  1.00 63.26  ? 343 PRO B CG    1 
ATOM   6700  C CD    . PRO B 1 343 ? 17.305  24.624  87.808  1.00 63.69  ? 343 PRO B CD    1 
ATOM   6701  N N     . GLY B 1 344 ? 21.740  23.649  89.025  1.00 66.72  ? 344 GLY B N     1 
ATOM   6702  C CA    . GLY B 1 344 ? 22.807  22.674  89.215  1.00 61.72  ? 344 GLY B CA    1 
ATOM   6703  C C     . GLY B 1 344 ? 23.639  22.433  87.956  1.00 62.49  ? 344 GLY B C     1 
ATOM   6704  O O     . GLY B 1 344 ? 24.490  21.547  87.921  1.00 61.12  ? 344 GLY B O     1 
ATOM   6705  N N     . VAL B 1 345 ? 23.405  23.225  86.912  1.00 65.77  ? 345 VAL B N     1 
ATOM   6706  C CA    . VAL B 1 345 ? 24.039  22.967  85.631  1.00 67.86  ? 345 VAL B CA    1 
ATOM   6707  C C     . VAL B 1 345 ? 25.506  23.374  85.703  1.00 67.56  ? 345 VAL B C     1 
ATOM   6708  O O     . VAL B 1 345 ? 25.834  24.429  86.252  1.00 67.42  ? 345 VAL B O     1 
ATOM   6709  C CB    . VAL B 1 345 ? 23.322  23.718  84.498  1.00 61.59  ? 345 VAL B CB    1 
ATOM   6710  C CG1   . VAL B 1 345 ? 23.542  25.226  84.591  1.00 61.11  ? 345 VAL B CG1   1 
ATOM   6711  C CG2   . VAL B 1 345 ? 23.753  23.177  83.144  1.00 63.48  ? 345 VAL B CG2   1 
ATOM   6712  N N     . LYS B 1 346 ? 26.377  22.556  85.105  1.00 65.19  ? 346 LYS B N     1 
ATOM   6713  C CA    . LYS B 1 346 ? 27.777  22.926  84.982  1.00 71.52  ? 346 LYS B CA    1 
ATOM   6714  C C     . LYS B 1 346 ? 28.184  22.797  83.520  1.00 71.13  ? 346 LYS B C     1 
ATOM   6715  O O     . LYS B 1 346 ? 27.584  22.027  82.785  1.00 64.44  ? 346 LYS B O     1 
ATOM   6716  C CB    . LYS B 1 346 ? 28.648  22.089  85.922  1.00 82.19  ? 346 LYS B CB    1 
ATOM   6717  C CG    . LYS B 1 346 ? 28.540  22.478  87.393  1.00 95.86  ? 346 LYS B CG    1 
ATOM   6718  C CD    . LYS B 1 346 ? 29.558  21.827  88.322  1.00 103.97 ? 346 LYS B CD    1 
ATOM   6719  C CE    . LYS B 1 346 ? 29.398  22.230  89.780  1.00 106.39 ? 346 LYS B CE    1 
ATOM   6720  N NZ    . LYS B 1 346 ? 28.327  21.472  90.479  1.00 98.43  ? 346 LYS B NZ    1 
ATOM   6721  N N     . PHE B 1 347 ? 29.198  23.580  83.127  1.00 72.78  ? 347 PHE B N     1 
ATOM   6722  C CA    . PHE B 1 347 ? 29.638  23.717  81.746  1.00 63.73  ? 347 PHE B CA    1 
ATOM   6723  C C     . PHE B 1 347 ? 31.131  23.402  81.685  1.00 57.83  ? 347 PHE B C     1 
ATOM   6724  O O     . PHE B 1 347 ? 31.907  23.964  82.423  1.00 51.46  ? 347 PHE B O     1 
ATOM   6725  C CB    . PHE B 1 347 ? 29.321  25.130  81.226  1.00 64.88  ? 347 PHE B CB    1 
ATOM   6726  C CG    . PHE B 1 347 ? 27.850  25.372  81.007  1.00 62.97  ? 347 PHE B CG    1 
ATOM   6727  C CD1   . PHE B 1 347 ? 27.185  24.779  79.947  1.00 62.87  ? 347 PHE B CD1   1 
ATOM   6728  C CD2   . PHE B 1 347 ? 27.112  26.116  81.911  1.00 62.32  ? 347 PHE B CD2   1 
ATOM   6729  C CE1   . PHE B 1 347 ? 25.822  24.955  79.775  1.00 58.95  ? 347 PHE B CE1   1 
ATOM   6730  C CE2   . PHE B 1 347 ? 25.749  26.289  81.737  1.00 62.21  ? 347 PHE B CE2   1 
ATOM   6731  C CZ    . PHE B 1 347 ? 25.107  25.706  80.670  1.00 60.52  ? 347 PHE B CZ    1 
ATOM   6732  N N     . TYR B 1 348 ? 31.543  22.503  80.797  1.00 60.05  ? 348 TYR B N     1 
ATOM   6733  C CA    . TYR B 1 348 ? 32.941  22.134  80.718  1.00 61.22  ? 348 TYR B CA    1 
ATOM   6734  C C     . TYR B 1 348 ? 33.432  22.189  79.268  1.00 61.56  ? 348 TYR B C     1 
ATOM   6735  O O     . TYR B 1 348 ? 32.807  21.610  78.383  1.00 59.03  ? 348 TYR B O     1 
ATOM   6736  C CB    . TYR B 1 348 ? 33.135  20.727  81.295  1.00 63.27  ? 348 TYR B CB    1 
ATOM   6737  C CG    . TYR B 1 348 ? 32.775  20.543  82.750  1.00 68.05  ? 348 TYR B CG    1 
ATOM   6738  C CD1   . TYR B 1 348 ? 31.457  20.371  83.138  1.00 69.37  ? 348 TYR B CD1   1 
ATOM   6739  C CD2   . TYR B 1 348 ? 33.750  20.517  83.741  1.00 63.20  ? 348 TYR B CD2   1 
ATOM   6740  C CE1   . TYR B 1 348 ? 31.109  20.159  84.462  1.00 68.18  ? 348 TYR B CE1   1 
ATOM   6741  C CE2   . TYR B 1 348 ? 33.418  20.320  85.073  1.00 68.45  ? 348 TYR B CE2   1 
ATOM   6742  C CZ    . TYR B 1 348 ? 32.091  20.141  85.434  1.00 70.23  ? 348 TYR B CZ    1 
ATOM   6743  O OH    . TYR B 1 348 ? 31.722  19.972  86.737  1.00 56.50  ? 348 TYR B OH    1 
ATOM   6744  N N     . PHE B 1 349 ? 34.558  22.888  79.042  1.00 69.25  ? 349 PHE B N     1 
ATOM   6745  C CA    . PHE B 1 349 ? 35.424  22.641  77.894  1.00 64.97  ? 349 PHE B CA    1 
ATOM   6746  C C     . PHE B 1 349 ? 36.497  21.647  78.332  1.00 56.14  ? 349 PHE B C     1 
ATOM   6747  O O     . PHE B 1 349 ? 36.561  21.361  79.523  1.00 49.04  ? 349 PHE B O     1 
ATOM   6748  C CB    . PHE B 1 349 ? 35.957  23.965  77.349  1.00 64.34  ? 349 PHE B CB    1 
ATOM   6749  C CG    . PHE B 1 349 ? 34.898  24.839  76.722  1.00 67.09  ? 349 PHE B CG    1 
ATOM   6750  C CD1   . PHE B 1 349 ? 34.084  24.352  75.708  1.00 65.07  ? 349 PHE B CD1   1 
ATOM   6751  C CD2   . PHE B 1 349 ? 34.733  26.161  77.119  1.00 71.11  ? 349 PHE B CD2   1 
ATOM   6752  C CE1   . PHE B 1 349 ? 33.114  25.161  75.127  1.00 74.90  ? 349 PHE B CE1   1 
ATOM   6753  C CE2   . PHE B 1 349 ? 33.769  26.969  76.531  1.00 74.20  ? 349 PHE B CE2   1 
ATOM   6754  C CZ    . PHE B 1 349 ? 32.956  26.468  75.538  1.00 73.13  ? 349 PHE B CZ    1 
ATOM   6755  N N     . PRO B 1 350 ? 37.272  21.012  77.407  1.00 60.91  ? 350 PRO B N     1 
ATOM   6756  C CA    . PRO B 1 350 ? 38.243  19.964  77.762  1.00 62.07  ? 350 PRO B CA    1 
ATOM   6757  C C     . PRO B 1 350 ? 39.334  20.286  78.787  1.00 58.61  ? 350 PRO B C     1 
ATOM   6758  O O     . PRO B 1 350 ? 39.718  19.410  79.542  1.00 58.93  ? 350 PRO B O     1 
ATOM   6759  C CB    . PRO B 1 350 ? 38.948  19.631  76.437  1.00 55.31  ? 350 PRO B CB    1 
ATOM   6760  C CG    . PRO B 1 350 ? 37.927  19.993  75.391  1.00 60.08  ? 350 PRO B CG    1 
ATOM   6761  C CD    . PRO B 1 350 ? 37.219  21.212  75.948  1.00 60.23  ? 350 PRO B CD    1 
ATOM   6762  N N     . GLU B 1 351 ? 39.826  21.530  78.828  1.00 71.73  ? 351 GLU B N     1 
ATOM   6763  C CA    . GLU B 1 351 ? 40.911  21.905  79.734  1.00 77.33  ? 351 GLU B CA    1 
ATOM   6764  C C     . GLU B 1 351 ? 40.358  22.229  81.124  1.00 73.58  ? 351 GLU B C     1 
ATOM   6765  O O     . GLU B 1 351 ? 41.151  22.480  82.036  1.00 70.96  ? 351 GLU B O     1 
ATOM   6766  C CB    . GLU B 1 351 ? 41.762  23.060  79.178  1.00 81.69  ? 351 GLU B CB    1 
ATOM   6767  C CG    . GLU B 1 351 ? 41.015  24.382  78.996  1.00 90.13  ? 351 GLU B CG    1 
ATOM   6768  C CD    . GLU B 1 351 ? 39.911  24.405  77.937  1.00 99.06  ? 351 GLU B CD    1 
ATOM   6769  O OE1   . GLU B 1 351 ? 39.785  23.410  77.157  1.00 86.70  ? 351 GLU B OE1   1 
ATOM   6770  O OE2   . GLU B 1 351 ? 39.160  25.419  77.880  1.00 82.84  ? 351 GLU B OE2   1 
ATOM   6771  N N     . ASP B 1 352 ? 39.016  22.227  81.268  1.00 64.23  ? 352 ASP B N     1 
ATOM   6772  C CA    . ASP B 1 352 ? 38.346  22.347  82.557  1.00 61.63  ? 352 ASP B CA    1 
ATOM   6773  C C     . ASP B 1 352 ? 38.245  20.990  83.253  1.00 69.22  ? 352 ASP B C     1 
ATOM   6774  O O     . ASP B 1 352 ? 37.819  20.947  84.400  1.00 71.26  ? 352 ASP B O     1 
ATOM   6775  C CB    . ASP B 1 352 ? 36.921  22.898  82.448  1.00 57.54  ? 352 ASP B CB    1 
ATOM   6776  C CG    . ASP B 1 352 ? 36.866  24.276  81.827  1.00 60.89  ? 352 ASP B CG    1 
ATOM   6777  O OD1   . ASP B 1 352 ? 37.720  25.085  82.197  1.00 65.99  ? 352 ASP B OD1   1 
ATOM   6778  O OD2   . ASP B 1 352 ? 35.995  24.517  80.965  1.00 59.98  ? 352 ASP B OD2   1 
ATOM   6779  N N     . ARG B 1 353 ? 38.626  19.888  82.583  1.00 75.58  ? 353 ARG B N     1 
ATOM   6780  C CA    . ARG B 1 353 ? 38.523  18.562  83.189  1.00 77.01  ? 353 ARG B CA    1 
ATOM   6781  C C     . ARG B 1 353 ? 39.793  18.210  83.976  1.00 88.51  ? 353 ARG B C     1 
ATOM   6782  O O     . ARG B 1 353 ? 40.869  17.978  83.404  1.00 80.42  ? 353 ARG B O     1 
ATOM   6783  C CB    . ARG B 1 353 ? 38.223  17.493  82.133  1.00 68.94  ? 353 ARG B CB    1 
ATOM   6784  C CG    . ARG B 1 353 ? 37.015  17.798  81.260  1.00 66.01  ? 353 ARG B CG    1 
ATOM   6785  C CD    . ARG B 1 353 ? 35.743  17.898  82.061  1.00 58.63  ? 353 ARG B CD    1 
ATOM   6786  N NE    . ARG B 1 353 ? 35.395  16.581  82.569  1.00 54.58  ? 353 ARG B NE    1 
ATOM   6787  C CZ    . ARG B 1 353 ? 34.414  16.333  83.435  1.00 45.99  ? 353 ARG B CZ    1 
ATOM   6788  N NH1   . ARG B 1 353 ? 33.825  17.321  84.086  1.00 46.77  ? 353 ARG B NH1   1 
ATOM   6789  N NH2   . ARG B 1 353 ? 34.055  15.082  83.671  1.00 44.39  ? 353 ARG B NH2   1 
ATOM   6790  N N     . ARG B 1 354 ? 39.621  18.139  85.306  1.00 83.96  ? 354 ARG B N     1 
ATOM   6791  C CA    . ARG B 1 354 ? 40.664  17.743  86.238  1.00 79.87  ? 354 ARG B CA    1 
ATOM   6792  C C     . ARG B 1 354 ? 41.210  16.368  85.844  1.00 73.53  ? 354 ARG B C     1 
ATOM   6793  O O     . ARG B 1 354 ? 42.421  16.204  85.854  1.00 77.70  ? 354 ARG B O     1 
ATOM   6794  C CB    . ARG B 1 354 ? 40.138  17.767  87.683  1.00 83.97  ? 354 ARG B CB    1 
ATOM   6795  C CG    . ARG B 1 354 ? 39.630  19.124  88.172  1.00 89.72  ? 354 ARG B CG    1 
ATOM   6796  C CD    . ARG B 1 354 ? 39.221  19.159  89.647  1.00 92.76  ? 354 ARG B CD    1 
ATOM   6797  N NE    . ARG B 1 354 ? 38.302  18.081  90.035  1.00 99.26  ? 354 ARG B NE    1 
ATOM   6798  C CZ    . ARG B 1 354 ? 38.628  16.980  90.728  1.00 98.86  ? 354 ARG B CZ    1 
ATOM   6799  N NH1   . ARG B 1 354 ? 39.848  16.819  91.216  1.00 98.66  ? 354 ARG B NH1   1 
ATOM   6800  N NH2   . ARG B 1 354 ? 37.729  16.030  90.944  1.00 88.84  ? 354 ARG B NH2   1 
ATOM   6801  N N     . HIS B 1 355 ? 40.332  15.412  85.473  1.00 68.88  ? 355 HIS B N     1 
ATOM   6802  C CA    . HIS B 1 355 ? 40.724  14.058  85.068  1.00 75.09  ? 355 HIS B CA    1 
ATOM   6803  C C     . HIS B 1 355 ? 41.100  13.981  83.573  1.00 71.14  ? 355 HIS B C     1 
ATOM   6804  O O     . HIS B 1 355 ? 40.369  14.468  82.719  1.00 75.40  ? 355 HIS B O     1 
ATOM   6805  C CB    . HIS B 1 355 ? 39.593  13.052  85.366  1.00 70.21  ? 355 HIS B CB    1 
ATOM   6806  C CG    . HIS B 1 355 ? 39.192  12.907  86.807  1.00 71.20  ? 355 HIS B CG    1 
ATOM   6807  N ND1   . HIS B 1 355 ? 38.613  13.908  87.563  1.00 76.36  ? 355 HIS B ND1   1 
ATOM   6808  C CD2   . HIS B 1 355 ? 39.273  11.841  87.626  1.00 72.99  ? 355 HIS B CD2   1 
ATOM   6809  C CE1   . HIS B 1 355 ? 38.374  13.458  88.791  1.00 77.48  ? 355 HIS B CE1   1 
ATOM   6810  N NE2   . HIS B 1 355 ? 38.793  12.212  88.859  1.00 73.41  ? 355 HIS B NE2   1 
ATOM   6811  N N     . LYS B 1 356 ? 42.210  13.308  83.240  1.00 55.29  ? 356 LYS B N     1 
ATOM   6812  C CA    . LYS B 1 356 ? 42.632  13.144  81.855  1.00 59.66  ? 356 LYS B CA    1 
ATOM   6813  C C     . LYS B 1 356 ? 42.213  11.778  81.299  1.00 61.99  ? 356 LYS B C     1 
ATOM   6814  O O     . LYS B 1 356 ? 42.206  11.591  80.084  1.00 60.34  ? 356 LYS B O     1 
ATOM   6815  C CB    . LYS B 1 356 ? 44.145  13.360  81.727  1.00 62.73  ? 356 LYS B CB    1 
ATOM   6816  C CG    . LYS B 1 356 ? 44.648  14.726  82.189  1.00 67.11  ? 356 LYS B CG    1 
ATOM   6817  C CD    . LYS B 1 356 ? 44.150  15.868  81.302  1.00 77.94  ? 356 LYS B CD    1 
ATOM   6818  C CE    . LYS B 1 356 ? 44.485  17.259  81.800  1.00 83.21  ? 356 LYS B CE    1 
ATOM   6819  N NZ    . LYS B 1 356 ? 43.704  17.618  83.005  1.00 84.46  ? 356 LYS B NZ    1 
ATOM   6820  N N     . VAL B 1 357 ? 41.901  10.810  82.175  1.00 60.86  ? 357 VAL B N     1 
ATOM   6821  C CA    . VAL B 1 357 ? 40.975  9.729   81.840  1.00 70.63  ? 357 VAL B CA    1 
ATOM   6822  C C     . VAL B 1 357 ? 39.558  10.170  82.246  1.00 71.99  ? 357 VAL B C     1 
ATOM   6823  O O     . VAL B 1 357 ? 39.218  10.221  83.438  1.00 60.12  ? 357 VAL B O     1 
ATOM   6824  C CB    . VAL B 1 357 ? 41.374  8.376   82.475  1.00 67.80  ? 357 VAL B CB    1 
ATOM   6825  C CG1   . VAL B 1 357 ? 40.306  7.300   82.287  1.00 62.46  ? 357 VAL B CG1   1 
ATOM   6826  C CG2   . VAL B 1 357 ? 42.709  7.890   81.934  1.00 66.45  ? 357 VAL B CG2   1 
ATOM   6827  N N     . ASP B 1 358 ? 38.747  10.465  81.213  1.00 67.17  ? 358 ASP B N     1 
ATOM   6828  C CA    . ASP B 1 358 ? 37.523  11.254  81.323  1.00 69.82  ? 358 ASP B CA    1 
ATOM   6829  C C     . ASP B 1 358 ? 36.650  11.089  80.069  1.00 69.50  ? 358 ASP B C     1 
ATOM   6830  O O     . ASP B 1 358 ? 37.176  10.943  78.955  1.00 56.74  ? 358 ASP B O     1 
ATOM   6831  C CB    . ASP B 1 358 ? 37.875  12.731  81.503  1.00 62.70  ? 358 ASP B CB    1 
ATOM   6832  C CG    . ASP B 1 358 ? 36.703  13.563  81.965  1.00 56.07  ? 358 ASP B CG    1 
ATOM   6833  O OD1   . ASP B 1 358 ? 36.479  13.611  83.175  1.00 59.16  ? 358 ASP B OD1   1 
ATOM   6834  O OD2   . ASP B 1 358 ? 36.028  14.131  81.103  1.00 63.78  ? 358 ASP B OD2   1 
ATOM   6835  N N     . LEU B 1 359 ? 35.319  11.151  80.273  1.00 62.79  ? 359 LEU B N     1 
ATOM   6836  C CA    . LEU B 1 359 ? 34.317  11.091  79.209  1.00 54.70  ? 359 LEU B CA    1 
ATOM   6837  C C     . LEU B 1 359 ? 34.543  12.194  78.160  1.00 50.80  ? 359 LEU B C     1 
ATOM   6838  O O     . LEU B 1 359 ? 34.613  11.906  76.960  1.00 40.63  ? 359 LEU B O     1 
ATOM   6839  C CB    . LEU B 1 359 ? 32.917  11.195  79.842  1.00 60.47  ? 359 LEU B CB    1 
ATOM   6840  C CG    . LEU B 1 359 ? 31.741  11.480  78.896  1.00 61.09  ? 359 LEU B CG    1 
ATOM   6841  C CD1   . LEU B 1 359 ? 31.373  10.252  78.068  1.00 58.84  ? 359 LEU B CD1   1 
ATOM   6842  C CD2   . LEU B 1 359 ? 30.517  11.965  79.662  1.00 63.19  ? 359 LEU B CD2   1 
ATOM   6843  N N     . LEU B 1 360 ? 34.643  13.470  78.563  1.00 51.97  ? 360 LEU B N     1 
ATOM   6844  C CA    . LEU B 1 360 ? 34.756  14.505  77.543  1.00 55.20  ? 360 LEU B CA    1 
ATOM   6845  C C     . LEU B 1 360 ? 36.018  14.258  76.698  1.00 61.09  ? 360 LEU B C     1 
ATOM   6846  O O     . LEU B 1 360 ? 35.949  14.115  75.477  1.00 61.16  ? 360 LEU B O     1 
ATOM   6847  C CB    . LEU B 1 360 ? 34.717  15.898  78.186  1.00 51.91  ? 360 LEU B CB    1 
ATOM   6848  C CG    . LEU B 1 360 ? 34.877  17.079  77.218  1.00 51.64  ? 360 LEU B CG    1 
ATOM   6849  C CD1   . LEU B 1 360 ? 33.844  17.077  76.099  1.00 49.30  ? 360 LEU B CD1   1 
ATOM   6850  C CD2   . LEU B 1 360 ? 34.773  18.393  77.948  1.00 52.32  ? 360 LEU B CD2   1 
ATOM   6851  N N     . LEU B 1 361 ? 37.178  14.127  77.340  1.00 56.68  ? 361 LEU B N     1 
ATOM   6852  C CA    . LEU B 1 361 ? 38.407  13.988  76.578  1.00 52.47  ? 361 LEU B CA    1 
ATOM   6853  C C     . LEU B 1 361 ? 38.305  12.785  75.666  1.00 49.18  ? 361 LEU B C     1 
ATOM   6854  O O     . LEU B 1 361 ? 38.881  12.825  74.586  1.00 51.95  ? 361 LEU B O     1 
ATOM   6855  C CB    . LEU B 1 361 ? 39.614  13.814  77.500  1.00 50.94  ? 361 LEU B CB    1 
ATOM   6856  C CG    . LEU B 1 361 ? 40.301  15.101  77.923  1.00 62.11  ? 361 LEU B CG    1 
ATOM   6857  C CD1   . LEU B 1 361 ? 39.313  16.246  78.043  1.00 70.13  ? 361 LEU B CD1   1 
ATOM   6858  C CD2   . LEU B 1 361 ? 41.010  14.895  79.254  1.00 71.20  ? 361 LEU B CD2   1 
ATOM   6859  N N     . HIS B 1 362 ? 37.642  11.714  76.120  1.00 43.77  ? 362 HIS B N     1 
ATOM   6860  C CA    . HIS B 1 362 ? 37.650  10.499  75.321  1.00 52.70  ? 362 HIS B CA    1 
ATOM   6861  C C     . HIS B 1 362 ? 36.677  10.696  74.161  1.00 62.60  ? 362 HIS B C     1 
ATOM   6862  O O     . HIS B 1 362 ? 36.887  10.185  73.059  1.00 66.60  ? 362 HIS B O     1 
ATOM   6863  C CB    . HIS B 1 362 ? 37.384  9.220   76.130  1.00 51.98  ? 362 HIS B CB    1 
ATOM   6864  C CG    . HIS B 1 362 ? 37.158  8.045   75.231  1.00 64.60  ? 362 HIS B CG    1 
ATOM   6865  N ND1   . HIS B 1 362 ? 36.111  7.159   75.358  1.00 74.19  ? 362 HIS B ND1   1 
ATOM   6866  C CD2   . HIS B 1 362 ? 37.824  7.657   74.132  1.00 76.86  ? 362 HIS B CD2   1 
ATOM   6867  C CE1   . HIS B 1 362 ? 36.163  6.261   74.387  1.00 72.04  ? 362 HIS B CE1   1 
ATOM   6868  N NE2   . HIS B 1 362 ? 37.190  6.553   73.627  1.00 77.70  ? 362 HIS B NE2   1 
ATOM   6869  N N     . ARG B 1 363 ? 35.618  11.457  74.429  1.00 60.80  ? 363 ARG B N     1 
ATOM   6870  C CA    . ARG B 1 363 ? 34.588  11.653  73.438  1.00 70.31  ? 363 ARG B CA    1 
ATOM   6871  C C     . ARG B 1 363 ? 35.047  12.730  72.458  1.00 65.26  ? 363 ARG B C     1 
ATOM   6872  O O     . ARG B 1 363 ? 34.565  12.768  71.336  1.00 60.73  ? 363 ARG B O     1 
ATOM   6873  C CB    . ARG B 1 363 ? 33.257  11.991  74.115  1.00 76.36  ? 363 ARG B CB    1 
ATOM   6874  C CG    . ARG B 1 363 ? 32.058  11.946  73.177  1.00 92.27  ? 363 ARG B CG    1 
ATOM   6875  C CD    . ARG B 1 363 ? 31.896  10.601  72.489  1.00 97.81  ? 363 ARG B CD    1 
ATOM   6876  N NE    . ARG B 1 363 ? 31.892  9.505   73.445  1.00 88.08  ? 363 ARG B NE    1 
ATOM   6877  C CZ    . ARG B 1 363 ? 30.886  8.654   73.610  1.00 82.03  ? 363 ARG B CZ    1 
ATOM   6878  N NH1   . ARG B 1 363 ? 29.941  8.545   72.698  1.00 70.60  ? 363 ARG B NH1   1 
ATOM   6879  N NH2   . ARG B 1 363 ? 30.858  7.869   74.670  1.00 91.07  ? 363 ARG B NH2   1 
ATOM   6880  N N     . ALA B 1 364 ? 35.996  13.587  72.851  1.00 54.78  ? 364 ALA B N     1 
ATOM   6881  C CA    . ALA B 1 364 ? 36.446  14.628  71.939  1.00 62.17  ? 364 ALA B CA    1 
ATOM   6882  C C     . ALA B 1 364 ? 37.095  13.982  70.707  1.00 59.79  ? 364 ALA B C     1 
ATOM   6883  O O     . ALA B 1 364 ? 37.076  14.513  69.598  1.00 66.17  ? 364 ALA B O     1 
ATOM   6884  C CB    . ALA B 1 364 ? 37.376  15.584  72.658  1.00 60.65  ? 364 ALA B CB    1 
ATOM   6885  N N     . GLU B 1 365 ? 37.684  12.814  70.924  1.00 55.35  ? 365 GLU B N     1 
ATOM   6886  C CA    . GLU B 1 365 ? 38.268  12.028  69.857  1.00 57.04  ? 365 GLU B CA    1 
ATOM   6887  C C     . GLU B 1 365 ? 37.175  11.535  68.902  1.00 54.38  ? 365 GLU B C     1 
ATOM   6888  O O     . GLU B 1 365 ? 37.270  11.735  67.692  1.00 47.32  ? 365 GLU B O     1 
ATOM   6889  C CB    . GLU B 1 365 ? 39.079  10.901  70.499  1.00 60.07  ? 365 GLU B CB    1 
ATOM   6890  C CG    . GLU B 1 365 ? 40.309  11.398  71.241  1.00 61.86  ? 365 GLU B CG    1 
ATOM   6891  C CD    . GLU B 1 365 ? 41.505  11.690  70.349  1.00 74.71  ? 365 GLU B CD    1 
ATOM   6892  O OE1   . GLU B 1 365 ? 41.449  12.637  69.536  1.00 87.48  ? 365 GLU B OE1   1 
ATOM   6893  O OE2   . GLU B 1 365 ? 42.496  10.951  70.460  1.00 85.56  ? 365 GLU B OE2   1 
ATOM   6894  N N     . THR B 1 366 ? 36.123  10.928  69.461  1.00 49.65  ? 366 THR B N     1 
ATOM   6895  C CA    . THR B 1 366 ? 35.076  10.291  68.687  1.00 50.51  ? 366 THR B CA    1 
ATOM   6896  C C     . THR B 1 366 ? 34.273  11.296  67.859  1.00 55.95  ? 366 THR B C     1 
ATOM   6897  O O     . THR B 1 366 ? 33.894  11.008  66.714  1.00 59.84  ? 366 THR B O     1 
ATOM   6898  C CB    . THR B 1 366 ? 34.163  9.501   69.625  1.00 58.53  ? 366 THR B CB    1 
ATOM   6899  O OG1   . THR B 1 366 ? 34.940  8.719   70.548  1.00 48.27  ? 366 THR B OG1   1 
ATOM   6900  C CG2   . THR B 1 366 ? 33.222  8.610   68.843  1.00 57.15  ? 366 THR B CG2   1 
ATOM   6901  N N     . MET B 1 367 ? 34.027  12.484  68.440  1.00 56.29  ? 367 MET B N     1 
ATOM   6902  C CA    . MET B 1 367 ? 33.207  13.507  67.814  1.00 46.25  ? 367 MET B CA    1 
ATOM   6903  C C     . MET B 1 367 ? 34.018  14.292  66.778  1.00 47.86  ? 367 MET B C     1 
ATOM   6904  O O     . MET B 1 367 ? 33.495  15.248  66.213  1.00 52.09  ? 367 MET B O     1 
ATOM   6905  C CB    . MET B 1 367 ? 32.642  14.470  68.864  1.00 45.68  ? 367 MET B CB    1 
ATOM   6906  C CG    . MET B 1 367 ? 31.478  13.910  69.691  1.00 44.88  ? 367 MET B CG    1 
ATOM   6907  S SD    . MET B 1 367 ? 30.835  15.022  71.042  1.00 49.17  ? 367 MET B SD    1 
ATOM   6908  C CE    . MET B 1 367 ? 32.364  15.671  71.718  1.00 44.96  ? 367 MET B CE    1 
ATOM   6909  N N     . LYS B 1 368 ? 35.298  13.939  66.568  1.00 53.01  ? 368 LYS B N     1 
ATOM   6910  C CA    . LYS B 1 368 ? 36.077  14.399  65.422  1.00 51.36  ? 368 LYS B CA    1 
ATOM   6911  C C     . LYS B 1 368 ? 36.510  13.204  64.555  1.00 50.36  ? 368 LYS B C     1 
ATOM   6912  O O     . LYS B 1 368 ? 37.320  13.348  63.652  1.00 55.67  ? 368 LYS B O     1 
ATOM   6913  C CB    . LYS B 1 368 ? 37.264  15.259  65.885  1.00 56.82  ? 368 LYS B CB    1 
ATOM   6914  C CG    . LYS B 1 368 ? 38.587  14.540  66.111  1.00 63.61  ? 368 LYS B CG    1 
ATOM   6915  C CD    . LYS B 1 368 ? 39.565  15.286  66.997  1.00 75.82  ? 368 LYS B CD    1 
ATOM   6916  C CE    . LYS B 1 368 ? 40.267  16.441  66.318  1.00 84.17  ? 368 LYS B CE    1 
ATOM   6917  N NZ    . LYS B 1 368 ? 41.189  17.132  67.258  1.00 82.24  ? 368 LYS B NZ    1 
ATOM   6918  N N     . GLY B 1 369 ? 35.957  12.013  64.789  1.00 47.29  ? 369 GLY B N     1 
ATOM   6919  C CA    . GLY B 1 369 ? 36.046  10.946  63.802  1.00 50.86  ? 369 GLY B CA    1 
ATOM   6920  C C     . GLY B 1 369 ? 37.311  10.102  63.960  1.00 49.39  ? 369 GLY B C     1 
ATOM   6921  O O     . GLY B 1 369 ? 37.719  9.390   63.034  1.00 44.87  ? 369 GLY B O     1 
ATOM   6922  N N     . VAL B 1 370 ? 37.932  10.193  65.144  1.00 42.64  ? 370 VAL B N     1 
ATOM   6923  C CA    . VAL B 1 370 ? 39.087  9.376   65.443  1.00 42.78  ? 370 VAL B CA    1 
ATOM   6924  C C     . VAL B 1 370 ? 38.593  8.094   66.108  1.00 44.72  ? 370 VAL B C     1 
ATOM   6925  O O     . VAL B 1 370 ? 37.984  8.143   67.180  1.00 53.64  ? 370 VAL B O     1 
ATOM   6926  C CB    . VAL B 1 370 ? 40.119  10.104  66.331  1.00 50.32  ? 370 VAL B CB    1 
ATOM   6927  C CG1   . VAL B 1 370 ? 41.371  9.261   66.538  1.00 45.81  ? 370 VAL B CG1   1 
ATOM   6928  C CG2   . VAL B 1 370 ? 40.484  11.496  65.810  1.00 53.51  ? 370 VAL B CG2   1 
ATOM   6929  N N     . PRO B 1 371 ? 38.880  6.919   65.508  1.00 40.40  ? 371 PRO B N     1 
ATOM   6930  C CA    . PRO B 1 371 ? 38.561  5.628   66.102  1.00 44.21  ? 371 PRO B CA    1 
ATOM   6931  C C     . PRO B 1 371 ? 39.563  5.246   67.185  1.00 50.82  ? 371 PRO B C     1 
ATOM   6932  O O     . PRO B 1 371 ? 40.774  5.411   67.022  1.00 45.11  ? 371 PRO B O     1 
ATOM   6933  C CB    . PRO B 1 371 ? 38.679  4.656   64.926  1.00 42.10  ? 371 PRO B CB    1 
ATOM   6934  C CG    . PRO B 1 371 ? 39.707  5.287   64.016  1.00 46.59  ? 371 PRO B CG    1 
ATOM   6935  C CD    . PRO B 1 371 ? 39.618  6.779   64.249  1.00 44.91  ? 371 PRO B CD    1 
ATOM   6936  N N     . LYS B 1 372 ? 39.042  4.753   68.307  1.00 59.27  ? 372 LYS B N     1 
ATOM   6937  C CA    . LYS B 1 372 ? 39.921  4.402   69.405  1.00 56.50  ? 372 LYS B CA    1 
ATOM   6938  C C     . LYS B 1 372 ? 39.503  3.065   70.021  1.00 65.99  ? 372 LYS B C     1 
ATOM   6939  O O     . LYS B 1 372 ? 38.306  2.752   70.117  1.00 63.22  ? 372 LYS B O     1 
ATOM   6940  C CB    . LYS B 1 372 ? 39.953  5.568   70.398  1.00 57.10  ? 372 LYS B CB    1 
ATOM   6941  C CG    . LYS B 1 372 ? 40.906  6.719   70.056  1.00 59.99  ? 372 LYS B CG    1 
ATOM   6942  C CD    . LYS B 1 372 ? 42.342  6.313   69.649  1.00 56.65  ? 372 LYS B CD    1 
ATOM   6943  C CE    . LYS B 1 372 ? 43.421  7.203   70.226  1.00 61.12  ? 372 LYS B CE    1 
ATOM   6944  N NZ    . LYS B 1 372 ? 43.324  8.612   69.776  1.00 57.23  ? 372 LYS B NZ    1 
ATOM   6945  N N     . LEU B 1 373 ? 40.530  2.252   70.339  1.00 71.33  ? 373 LEU B N     1 
ATOM   6946  C CA    . LEU B 1 373 ? 40.459  1.238   71.385  1.00 82.43  ? 373 LEU B CA    1 
ATOM   6947  C C     . LEU B 1 373 ? 41.196  1.796   72.595  1.00 81.91  ? 373 LEU B C     1 
ATOM   6948  O O     . LEU B 1 373 ? 42.211  2.459   72.418  1.00 89.07  ? 373 LEU B O     1 
ATOM   6949  C CB    . LEU B 1 373 ? 41.127  -0.073  70.945  1.00 85.17  ? 373 LEU B CB    1 
ATOM   6950  C CG    . LEU B 1 373 ? 40.497  -0.823  69.769  1.00 94.28  ? 373 LEU B CG    1 
ATOM   6951  C CD1   . LEU B 1 373 ? 41.279  -2.107  69.462  1.00 85.75  ? 373 LEU B CD1   1 
ATOM   6952  C CD2   . LEU B 1 373 ? 39.018  -1.116  70.025  1.00 91.09  ? 373 LEU B CD2   1 
ATOM   6953  N N     . THR B 1 374 ? 40.658  1.564   73.800  1.00 91.47  ? 374 THR B N     1 
ATOM   6954  C CA    . THR B 1 374 ? 41.362  1.853   75.047  1.00 89.59  ? 374 THR B CA    1 
ATOM   6955  C C     . THR B 1 374 ? 41.428  0.561   75.874  1.00 95.43  ? 374 THR B C     1 
ATOM   6956  O O     . THR B 1 374 ? 40.919  -0.480  75.446  1.00 83.05  ? 374 THR B O     1 
ATOM   6957  C CB    . THR B 1 374 ? 40.741  3.050   75.802  1.00 85.18  ? 374 THR B CB    1 
ATOM   6958  O OG1   . THR B 1 374 ? 39.412  2.705   76.218  1.00 65.80  ? 374 THR B OG1   1 
ATOM   6959  C CG2   . THR B 1 374 ? 40.750  4.350   75.010  1.00 81.08  ? 374 THR B CG2   1 
ATOM   6960  N N     . GLU B 1 375 ? 42.061  0.636   77.060  1.00 102.26 ? 375 GLU B N     1 
ATOM   6961  C CA    . GLU B 1 375 ? 42.144  -0.487  77.988  1.00 97.45  ? 375 GLU B CA    1 
ATOM   6962  C C     . GLU B 1 375 ? 40.852  -0.625  78.812  1.00 93.40  ? 375 GLU B C     1 
ATOM   6963  O O     . GLU B 1 375 ? 40.832  -1.405  79.758  1.00 94.48  ? 375 GLU B O     1 
ATOM   6964  C CB    . GLU B 1 375 ? 43.374  -0.318  78.895  1.00 84.52  ? 375 GLU B CB    1 
ATOM   6965  N N     . PHE B 1 376 ? 39.765  0.075   78.435  1.00 98.80  ? 376 PHE B N     1 
ATOM   6966  C CA    . PHE B 1 376 ? 38.549  0.163   79.241  1.00 108.32 ? 376 PHE B CA    1 
ATOM   6967  C C     . PHE B 1 376 ? 37.381  -0.517  78.515  1.00 102.21 ? 376 PHE B C     1 
ATOM   6968  O O     . PHE B 1 376 ? 37.443  -0.717  77.305  1.00 104.45 ? 376 PHE B O     1 
ATOM   6969  C CB    . PHE B 1 376 ? 38.232  1.637   79.548  1.00 116.03 ? 376 PHE B CB    1 
ATOM   6970  C CG    . PHE B 1 376 ? 39.215  2.361   80.442  1.00 121.72 ? 376 PHE B CG    1 
ATOM   6971  C CD1   . PHE B 1 376 ? 39.220  2.152   81.819  1.00 118.61 ? 376 PHE B CD1   1 
ATOM   6972  C CD2   . PHE B 1 376 ? 40.134  3.263   79.912  1.00 117.79 ? 376 PHE B CD2   1 
ATOM   6973  C CE1   . PHE B 1 376 ? 40.119  2.819   82.640  1.00 113.26 ? 376 PHE B CE1   1 
ATOM   6974  C CE2   . PHE B 1 376 ? 41.041  3.922   80.732  1.00 112.32 ? 376 PHE B CE2   1 
ATOM   6975  C CZ    . PHE B 1 376 ? 41.029  3.700   82.093  1.00 120.87 ? 376 PHE B CZ    1 
ATOM   6976  N N     . ASN B 1 377 ? 36.354  -0.931  79.278  1.00 110.56 ? 377 ASN B N     1 
ATOM   6977  C CA    . ASN B 1 377 ? 34.986  -1.095  78.784  1.00 125.11 ? 377 ASN B CA    1 
ATOM   6978  C C     . ASN B 1 377 ? 34.106  -1.600  79.936  1.00 131.77 ? 377 ASN B C     1 
ATOM   6979  O O     . ASN B 1 377 ? 34.569  -1.650  81.076  1.00 130.43 ? 377 ASN B O     1 
ATOM   6980  C CB    . ASN B 1 377 ? 34.907  -1.987  77.536  1.00 113.11 ? 377 ASN B CB    1 
ATOM   6981  C CG    . ASN B 1 377 ? 34.168  -1.348  76.371  1.00 102.19 ? 377 ASN B CG    1 
ATOM   6982  O OD1   . ASN B 1 377 ? 33.421  -0.374  76.514  1.00 75.21  ? 377 ASN B OD1   1 
ATOM   6983  N ND2   . ASN B 1 377 ? 34.386  -1.895  75.188  1.00 107.19 ? 377 ASN B ND2   1 
ATOM   6984  N N     . PHE B 1 378 ? 32.845  -1.974  79.647  1.00 133.61 ? 378 PHE B N     1 
ATOM   6985  C CA    . PHE B 1 378 ? 31.890  -2.396  80.671  1.00 115.14 ? 378 PHE B CA    1 
ATOM   6986  C C     . PHE B 1 378 ? 32.279  -3.756  81.249  1.00 119.41 ? 378 PHE B C     1 
ATOM   6987  O O     . PHE B 1 378 ? 31.553  -4.735  81.104  1.00 125.75 ? 378 PHE B O     1 
ATOM   6988  C CB    . PHE B 1 378 ? 30.461  -2.486  80.128  1.00 100.08 ? 378 PHE B CB    1 
ATOM   6989  C CG    . PHE B 1 378 ? 30.072  -1.384  79.181  1.00 100.86 ? 378 PHE B CG    1 
ATOM   6990  C CD1   . PHE B 1 378 ? 30.162  -0.057  79.564  1.00 102.82 ? 378 PHE B CD1   1 
ATOM   6991  C CD2   . PHE B 1 378 ? 29.637  -1.678  77.893  1.00 105.02 ? 378 PHE B CD2   1 
ATOM   6992  C CE1   . PHE B 1 378 ? 29.827  0.950   78.667  1.00 123.03 ? 378 PHE B CE1   1 
ATOM   6993  C CE2   . PHE B 1 378 ? 29.299  -0.669  76.999  1.00 108.62 ? 378 PHE B CE2   1 
ATOM   6994  C CZ    . PHE B 1 378 ? 29.399  0.646   77.385  1.00 115.05 ? 378 PHE B CZ    1 
ATOM   6995  N N     . LEU B 1 379 ? 33.442  -3.788  81.904  1.00 126.15 ? 379 LEU B N     1 
ATOM   6996  C CA    . LEU B 1 379 ? 33.921  -4.916  82.686  1.00 126.66 ? 379 LEU B CA    1 
ATOM   6997  C C     . LEU B 1 379 ? 34.533  -4.276  83.917  1.00 125.88 ? 379 LEU B C     1 
ATOM   6998  O O     . LEU B 1 379 ? 34.543  -3.050  84.013  1.00 133.73 ? 379 LEU B O     1 
ATOM   6999  C CB    . LEU B 1 379 ? 34.979  -5.695  81.892  1.00 132.93 ? 379 LEU B CB    1 
ATOM   7000  C CG    . LEU B 1 379 ? 34.871  -7.224  81.900  1.00 129.56 ? 379 LEU B CG    1 
ATOM   7001  C CD1   . LEU B 1 379 ? 35.750  -7.823  80.807  1.00 127.58 ? 379 LEU B CD1   1 
ATOM   7002  C CD2   . LEU B 1 379 ? 35.233  -7.830  83.251  1.00 112.33 ? 379 LEU B CD2   1 
ATOM   7003  N N     . ASN B 1 380 ? 35.043  -5.083  84.846  1.00 120.76 ? 380 ASN B N     1 
ATOM   7004  C CA    . ASN B 1 380 ? 35.777  -4.522  85.965  1.00 116.65 ? 380 ASN B CA    1 
ATOM   7005  C C     . ASN B 1 380 ? 34.853  -3.525  86.676  1.00 106.50 ? 380 ASN B C     1 
ATOM   7006  O O     . ASN B 1 380 ? 35.302  -2.672  87.436  1.00 104.29 ? 380 ASN B O     1 
ATOM   7007  C CB    . ASN B 1 380 ? 37.110  -3.948  85.460  1.00 116.03 ? 380 ASN B CB    1 
ATOM   7008  C CG    . ASN B 1 380 ? 38.255  -4.070  86.445  1.00 112.27 ? 380 ASN B CG    1 
ATOM   7009  O OD1   . ASN B 1 380 ? 39.109  -3.190  86.517  1.00 111.76 ? 380 ASN B OD1   1 
ATOM   7010  N ND2   . ASN B 1 380 ? 38.323  -5.178  87.166  1.00 106.28 ? 380 ASN B ND2   1 
ATOM   7011  N N     . TRP B 1 381 ? 33.542  -3.647  86.409  1.00 106.32 ? 381 TRP B N     1 
ATOM   7012  C CA    . TRP B 1 381 ? 32.494  -2.952  87.137  1.00 94.52  ? 381 TRP B CA    1 
ATOM   7013  C C     . TRP B 1 381 ? 31.920  -3.943  88.142  1.00 93.46  ? 381 TRP B C     1 
ATOM   7014  O O     . TRP B 1 381 ? 32.051  -3.744  89.355  1.00 78.16  ? 381 TRP B O     1 
ATOM   7015  C CB    . TRP B 1 381 ? 31.423  -2.424  86.170  1.00 84.12  ? 381 TRP B CB    1 
ATOM   7016  C CG    . TRP B 1 381 ? 30.213  -1.843  86.834  1.00 85.55  ? 381 TRP B CG    1 
ATOM   7017  C CD1   . TRP B 1 381 ? 28.950  -2.372  86.856  1.00 75.68  ? 381 TRP B CD1   1 
ATOM   7018  C CD2   . TRP B 1 381 ? 30.143  -0.599  87.557  1.00 79.11  ? 381 TRP B CD2   1 
ATOM   7019  N NE1   . TRP B 1 381 ? 28.105  -1.547  87.552  1.00 76.55  ? 381 TRP B NE1   1 
ATOM   7020  C CE2   . TRP B 1 381 ? 28.806  -0.454  87.989  1.00 65.61  ? 381 TRP B CE2   1 
ATOM   7021  C CE3   . TRP B 1 381 ? 31.072  0.398   87.881  1.00 74.97  ? 381 TRP B CE3   1 
ATOM   7022  C CZ2   . TRP B 1 381 ? 28.384  0.640   88.733  1.00 62.47  ? 381 TRP B CZ2   1 
ATOM   7023  C CZ3   . TRP B 1 381 ? 30.645  1.491   88.603  1.00 68.99  ? 381 TRP B CZ3   1 
ATOM   7024  C CH2   . TRP B 1 381 ? 29.319  1.606   89.015  1.00 64.93  ? 381 TRP B CH2   1 
ATOM   7025  N N     . ASP B 1 382 ? 31.354  -5.034  87.589  1.00 89.73  ? 382 ASP B N     1 
ATOM   7026  C CA    . ASP B 1 382 ? 30.781  -6.120  88.367  1.00 97.07  ? 382 ASP B CA    1 
ATOM   7027  C C     . ASP B 1 382 ? 31.235  -7.477  87.821  1.00 87.43  ? 382 ASP B C     1 
ATOM   7028  O O     . ASP B 1 382 ? 30.530  -8.471  87.977  1.00 99.33  ? 382 ASP B O     1 
ATOM   7029  C CB    . ASP B 1 382 ? 29.250  -6.033  88.352  1.00 105.12 ? 382 ASP B CB    1 
ATOM   7030  C CG    . ASP B 1 382 ? 28.608  -6.727  89.538  1.00 108.16 ? 382 ASP B CG    1 
ATOM   7031  O OD1   . ASP B 1 382 ? 29.275  -6.783  90.605  1.00 87.73  ? 382 ASP B OD1   1 
ATOM   7032  O OD2   . ASP B 1 382 ? 27.473  -7.242  89.371  1.00 111.18 ? 382 ASP B OD2   1 
ATOM   7033  N N     . GLY B 1 383 ? 32.414  -7.532  87.192  1.00 81.31  ? 383 GLY B N     1 
ATOM   7034  C CA    . GLY B 1 383 ? 32.846  -8.730  86.486  1.00 77.49  ? 383 GLY B CA    1 
ATOM   7035  C C     . GLY B 1 383 ? 31.813  -9.156  85.444  1.00 80.52  ? 383 GLY B C     1 
ATOM   7036  O O     . GLY B 1 383 ? 31.446  -10.330 85.388  1.00 78.94  ? 383 GLY B O     1 
ATOM   7037  N N     . GLY B 1 384 ? 31.347  -8.175  84.648  1.00 81.75  ? 384 GLY B N     1 
ATOM   7038  C CA    . GLY B 1 384 ? 30.335  -8.371  83.622  1.00 81.15  ? 384 GLY B CA    1 
ATOM   7039  C C     . GLY B 1 384 ? 30.862  -9.175  82.434  1.00 82.65  ? 384 GLY B C     1 
ATOM   7040  O O     . GLY B 1 384 ? 30.854  -10.407 82.459  1.00 92.81  ? 384 GLY B O     1 
ATOM   7041  N N     . GLY B 1 385 ? 31.313  -8.478  81.387  1.00 74.63  ? 385 GLY B N     1 
ATOM   7042  C CA    . GLY B 1 385 ? 31.778  -9.156  80.186  1.00 77.43  ? 385 GLY B CA    1 
ATOM   7043  C C     . GLY B 1 385 ? 30.835  -8.946  79.003  1.00 74.72  ? 385 GLY B C     1 
ATOM   7044  O O     . GLY B 1 385 ? 31.224  -8.308  78.034  1.00 64.51  ? 385 GLY B O     1 
ATOM   7045  N N     . GLY B 1 386 ? 29.610  -9.496  79.090  1.00 73.28  ? 386 GLY B N     1 
ATOM   7046  C CA    . GLY B 1 386 ? 28.587  -9.333  78.062  1.00 69.52  ? 386 GLY B CA    1 
ATOM   7047  C C     . GLY B 1 386 ? 27.901  -7.961  78.094  1.00 64.54  ? 386 GLY B C     1 
ATOM   7048  O O     . GLY B 1 386 ? 27.799  -7.302  79.125  1.00 54.01  ? 386 GLY B O     1 
ATOM   7049  N N     . HIS B 1 387 ? 27.432  -7.491  76.939  1.00 66.33  ? 387 HIS B N     1 
ATOM   7050  C CA    . HIS B 1 387 ? 26.472  -6.403  76.979  1.00 70.34  ? 387 HIS B CA    1 
ATOM   7051  C C     . HIS B 1 387 ? 25.512  -6.519  75.802  1.00 63.82  ? 387 HIS B C     1 
ATOM   7052  O O     . HIS B 1 387 ? 25.826  -7.191  74.825  1.00 54.74  ? 387 HIS B O     1 
ATOM   7053  C CB    . HIS B 1 387 ? 27.162  -5.045  77.118  1.00 72.05  ? 387 HIS B CB    1 
ATOM   7054  C CG    . HIS B 1 387 ? 27.551  -4.452  75.821  1.00 79.70  ? 387 HIS B CG    1 
ATOM   7055  N ND1   . HIS B 1 387 ? 26.801  -3.476  75.199  1.00 83.74  ? 387 HIS B ND1   1 
ATOM   7056  C CD2   . HIS B 1 387 ? 28.579  -4.713  75.022  1.00 80.53  ? 387 HIS B CD2   1 
ATOM   7057  C CE1   . HIS B 1 387 ? 27.386  -3.145  74.066  1.00 78.58  ? 387 HIS B CE1   1 
ATOM   7058  N NE2   . HIS B 1 387 ? 28.456  -3.892  73.943  1.00 77.02  ? 387 HIS B NE2   1 
ATOM   7059  N N     . VAL B 1 388 ? 24.319  -5.927  75.998  1.00 68.99  ? 388 VAL B N     1 
ATOM   7060  C CA    . VAL B 1 388 ? 23.272  -5.823  74.990  1.00 62.60  ? 388 VAL B CA    1 
ATOM   7061  C C     . VAL B 1 388 ? 22.534  -4.487  75.148  1.00 56.50  ? 388 VAL B C     1 
ATOM   7062  O O     . VAL B 1 388 ? 22.415  -3.948  76.244  1.00 55.87  ? 388 VAL B O     1 
ATOM   7063  C CB    . VAL B 1 388 ? 22.301  -7.014  75.055  1.00 61.97  ? 388 VAL B CB    1 
ATOM   7064  C CG1   . VAL B 1 388 ? 21.256  -6.840  76.144  1.00 67.62  ? 388 VAL B CG1   1 
ATOM   7065  C CG2   . VAL B 1 388 ? 21.625  -7.254  73.713  1.00 66.42  ? 388 VAL B CG2   1 
ATOM   7066  N N     . GLY B 1 389 ? 22.009  -3.978  74.026  1.00 57.23  ? 389 GLY B N     1 
ATOM   7067  C CA    . GLY B 1 389 ? 21.401  -2.657  73.942  1.00 51.15  ? 389 GLY B CA    1 
ATOM   7068  C C     . GLY B 1 389 ? 19.936  -2.733  73.516  1.00 47.17  ? 389 GLY B C     1 
ATOM   7069  O O     . GLY B 1 389 ? 19.556  -3.636  72.794  1.00 44.03  ? 389 GLY B O     1 
ATOM   7070  N N     . PHE B 1 390 ? 19.124  -1.796  74.021  1.00 53.74  ? 390 PHE B N     1 
ATOM   7071  C CA    . PHE B 1 390 ? 17.745  -1.590  73.598  1.00 52.78  ? 390 PHE B CA    1 
ATOM   7072  C C     . PHE B 1 390 ? 17.596  -0.110  73.287  1.00 49.34  ? 390 PHE B C     1 
ATOM   7073  O O     . PHE B 1 390 ? 17.718  0.687   74.218  1.00 49.28  ? 390 PHE B O     1 
ATOM   7074  C CB    . PHE B 1 390 ? 16.756  -2.000  74.694  1.00 58.31  ? 390 PHE B CB    1 
ATOM   7075  C CG    . PHE B 1 390 ? 15.309  -1.934  74.288  1.00 54.73  ? 390 PHE B CG    1 
ATOM   7076  C CD1   . PHE B 1 390 ? 14.864  -2.644  73.193  1.00 59.22  ? 390 PHE B CD1   1 
ATOM   7077  C CD2   . PHE B 1 390 ? 14.398  -1.154  74.981  1.00 60.83  ? 390 PHE B CD2   1 
ATOM   7078  C CE1   . PHE B 1 390 ? 13.545  -2.561  72.784  1.00 58.87  ? 390 PHE B CE1   1 
ATOM   7079  C CE2   . PHE B 1 390 ? 13.073  -1.074  74.577  1.00 51.36  ? 390 PHE B CE2   1 
ATOM   7080  C CZ    . PHE B 1 390 ? 12.650  -1.790  73.493  1.00 56.82  ? 390 PHE B CZ    1 
ATOM   7081  N N     . SER B 1 391 ? 17.384  0.238   71.998  1.00 49.73  ? 391 SER B N     1 
ATOM   7082  C CA    . SER B 1 391 ? 17.420  1.634   71.550  1.00 65.16  ? 391 SER B CA    1 
ATOM   7083  C C     . SER B 1 391 ? 16.207  2.020   70.686  1.00 68.13  ? 391 SER B C     1 
ATOM   7084  O O     . SER B 1 391 ? 16.351  2.391   69.520  1.00 68.69  ? 391 SER B O     1 
ATOM   7085  C CB    . SER B 1 391 ? 18.719  1.930   70.818  1.00 65.54  ? 391 SER B CB    1 
ATOM   7086  O OG    . SER B 1 391 ? 18.892  1.032   69.734  1.00 68.83  ? 391 SER B OG    1 
ATOM   7087  N N     . PRO B 1 392 ? 14.969  1.998   71.227  1.00 60.90  ? 392 PRO B N     1 
ATOM   7088  C CA    . PRO B 1 392 ? 13.794  2.444   70.475  1.00 55.33  ? 392 PRO B CA    1 
ATOM   7089  C C     . PRO B 1 392 ? 13.659  3.938   70.192  1.00 51.63  ? 392 PRO B C     1 
ATOM   7090  O O     . PRO B 1 392 ? 14.375  4.779   70.740  1.00 57.01  ? 392 PRO B O     1 
ATOM   7091  C CB    . PRO B 1 392 ? 12.625  2.026   71.382  1.00 62.90  ? 392 PRO B CB    1 
ATOM   7092  C CG    . PRO B 1 392 ? 13.221  2.017   72.781  1.00 61.27  ? 392 PRO B CG    1 
ATOM   7093  C CD    . PRO B 1 392 ? 14.624  1.493   72.570  1.00 61.58  ? 392 PRO B CD    1 
ATOM   7094  N N     . VAL B 1 393 ? 12.709  4.243   69.307  1.00 42.31  ? 393 VAL B N     1 
ATOM   7095  C CA    . VAL B 1 393 ? 12.501  5.592   68.827  1.00 43.53  ? 393 VAL B CA    1 
ATOM   7096  C C     . VAL B 1 393 ? 11.292  6.176   69.549  1.00 39.26  ? 393 VAL B C     1 
ATOM   7097  O O     . VAL B 1 393 ? 10.297  5.475   69.759  1.00 32.52  ? 393 VAL B O     1 
ATOM   7098  C CB    . VAL B 1 393 ? 12.241  5.644   67.303  1.00 46.98  ? 393 VAL B CB    1 
ATOM   7099  C CG1   . VAL B 1 393 ? 12.285  7.072   66.788  1.00 44.03  ? 393 VAL B CG1   1 
ATOM   7100  C CG2   . VAL B 1 393 ? 13.206  4.786   66.504  1.00 58.35  ? 393 VAL B CG2   1 
ATOM   7101  N N     . SER B 1 394 ? 11.351  7.498   69.714  1.00 34.41  ? 394 SER B N     1 
ATOM   7102  C CA    . SER B 1 394 ? 10.363  8.248   70.444  1.00 44.44  ? 394 SER B CA    1 
ATOM   7103  C C     . SER B 1 394 ? 10.479  9.715   70.044  1.00 40.60  ? 394 SER B C     1 
ATOM   7104  O O     . SER B 1 394 ? 11.521  10.200  69.599  1.00 47.37  ? 394 SER B O     1 
ATOM   7105  C CB    . SER B 1 394 ? 10.605  8.088   71.934  1.00 55.66  ? 394 SER B CB    1 
ATOM   7106  O OG    . SER B 1 394 ? 11.827  8.720   72.323  1.00 53.93  ? 394 SER B OG    1 
ATOM   7107  N N     . PRO B 1 395 ? 9.412   10.490  70.215  1.00 34.89  ? 395 PRO B N     1 
ATOM   7108  C CA    . PRO B 1 395 ? 9.511   11.938  70.048  1.00 41.01  ? 395 PRO B CA    1 
ATOM   7109  C C     . PRO B 1 395 ? 10.523  12.571  70.989  1.00 38.86  ? 395 PRO B C     1 
ATOM   7110  O O     . PRO B 1 395 ? 10.745  12.078  72.090  1.00 44.73  ? 395 PRO B O     1 
ATOM   7111  C CB    . PRO B 1 395 ? 8.089   12.440  70.377  1.00 41.54  ? 395 PRO B CB    1 
ATOM   7112  C CG    . PRO B 1 395 ? 7.202   11.216  70.134  1.00 39.97  ? 395 PRO B CG    1 
ATOM   7113  C CD    . PRO B 1 395 ? 8.055   10.011  70.480  1.00 37.54  ? 395 PRO B CD    1 
ATOM   7114  N N     . ILE B 1 396 ? 11.064  13.710  70.586  1.00 38.53  ? 396 ILE B N     1 
ATOM   7115  C CA    . ILE B 1 396 ? 11.940  14.450  71.467  1.00 42.20  ? 396 ILE B CA    1 
ATOM   7116  C C     . ILE B 1 396 ? 11.024  15.251  72.381  1.00 45.84  ? 396 ILE B C     1 
ATOM   7117  O O     . ILE B 1 396 ? 10.759  16.425  72.093  1.00 47.11  ? 396 ILE B O     1 
ATOM   7118  C CB    . ILE B 1 396 ? 12.893  15.387  70.700  1.00 42.67  ? 396 ILE B CB    1 
ATOM   7119  C CG1   . ILE B 1 396 ? 13.565  14.706  69.517  1.00 43.20  ? 396 ILE B CG1   1 
ATOM   7120  C CG2   . ILE B 1 396 ? 13.921  16.003  71.628  1.00 45.56  ? 396 ILE B CG2   1 
ATOM   7121  C CD1   . ILE B 1 396 ? 14.046  15.703  68.489  1.00 50.95  ? 396 ILE B CD1   1 
ATOM   7122  N N     . THR B 1 397 ? 10.564  14.628  73.484  1.00 42.46  ? 397 THR B N     1 
ATOM   7123  C CA    . THR B 1 397 ? 9.912   15.412  74.529  1.00 45.46  ? 397 THR B CA    1 
ATOM   7124  C C     . THR B 1 397 ? 10.450  15.053  75.916  1.00 43.03  ? 397 THR B C     1 
ATOM   7125  O O     . THR B 1 397 ? 10.744  13.901  76.230  1.00 39.68  ? 397 THR B O     1 
ATOM   7126  C CB    . THR B 1 397 ? 8.380   15.312  74.413  1.00 39.99  ? 397 THR B CB    1 
ATOM   7127  O OG1   . THR B 1 397 ? 7.974   14.037  74.898  1.00 37.06  ? 397 THR B OG1   1 
ATOM   7128  C CG2   . THR B 1 397 ? 7.884   15.501  72.991  1.00 36.70  ? 397 THR B CG2   1 
ATOM   7129  N N     . GLY B 1 398 ? 10.545  16.074  76.769  1.00 48.63  ? 398 GLY B N     1 
ATOM   7130  C CA    . GLY B 1 398 ? 10.668  15.853  78.201  1.00 53.74  ? 398 GLY B CA    1 
ATOM   7131  C C     . GLY B 1 398 ? 9.802   14.683  78.674  1.00 55.15  ? 398 GLY B C     1 
ATOM   7132  O O     . GLY B 1 398 ? 10.272  13.765  79.335  1.00 57.54  ? 398 GLY B O     1 
ATOM   7133  N N     . LYS B 1 399 ? 8.523   14.713  78.312  1.00 58.00  ? 399 LYS B N     1 
ATOM   7134  C CA    . LYS B 1 399 ? 7.592   13.741  78.836  1.00 63.79  ? 399 LYS B CA    1 
ATOM   7135  C C     . LYS B 1 399 ? 8.010   12.351  78.354  1.00 57.47  ? 399 LYS B C     1 
ATOM   7136  O O     . LYS B 1 399 ? 7.953   11.389  79.116  1.00 51.90  ? 399 LYS B O     1 
ATOM   7137  C CB    . LYS B 1 399 ? 6.172   14.181  78.461  1.00 78.01  ? 399 LYS B CB    1 
ATOM   7138  C CG    . LYS B 1 399 ? 5.052   13.208  78.817  1.00 95.49  ? 399 LYS B CG    1 
ATOM   7139  C CD    . LYS B 1 399 ? 4.008   13.074  77.707  1.00 107.63 ? 399 LYS B CD    1 
ATOM   7140  C CE    . LYS B 1 399 ? 3.038   11.925  77.900  1.00 104.40 ? 399 LYS B CE    1 
ATOM   7141  N NZ    . LYS B 1 399 ? 2.125   12.173  79.038  1.00 100.13 ? 399 LYS B NZ    1 
ATOM   7142  N N     . ASP B 1 400 ? 8.454   12.228  77.096  1.00 61.96  ? 400 ASP B N     1 
ATOM   7143  C CA    . ASP B 1 400 ? 8.814   10.921  76.554  1.00 58.67  ? 400 ASP B CA    1 
ATOM   7144  C C     . ASP B 1 400 ? 10.127  10.408  77.176  1.00 56.36  ? 400 ASP B C     1 
ATOM   7145  O O     . ASP B 1 400 ? 10.298  9.191   77.434  1.00 42.15  ? 400 ASP B O     1 
ATOM   7146  C CB    . ASP B 1 400 ? 8.881   10.990  75.030  1.00 62.96  ? 400 ASP B CB    1 
ATOM   7147  C CG    . ASP B 1 400 ? 7.531   10.955  74.331  1.00 55.42  ? 400 ASP B CG    1 
ATOM   7148  O OD1   . ASP B 1 400 ? 6.953   9.867   74.265  1.00 44.41  ? 400 ASP B OD1   1 
ATOM   7149  O OD2   . ASP B 1 400 ? 7.111   12.002  73.797  1.00 50.02  ? 400 ASP B OD2   1 
ATOM   7150  N N     . ALA B 1 401 ? 11.056  11.346  77.430  1.00 48.60  ? 401 ALA B N     1 
ATOM   7151  C CA    . ALA B 1 401 ? 12.376  10.984  77.935  1.00 54.01  ? 401 ALA B CA    1 
ATOM   7152  C C     . ALA B 1 401 ? 12.229  10.400  79.333  1.00 58.41  ? 401 ALA B C     1 
ATOM   7153  O O     . ALA B 1 401 ? 12.569  9.234   79.551  1.00 56.20  ? 401 ALA B O     1 
ATOM   7154  C CB    . ALA B 1 401 ? 13.307  12.172  77.936  1.00 56.39  ? 401 ALA B CB    1 
ATOM   7155  N N     . ILE B 1 402 ? 11.661  11.210  80.245  1.00 62.28  ? 402 ILE B N     1 
ATOM   7156  C CA    . ILE B 1 402 ? 11.575  10.848  81.653  1.00 57.77  ? 402 ILE B CA    1 
ATOM   7157  C C     . ILE B 1 402 ? 10.694  9.622   81.805  1.00 53.43  ? 402 ILE B C     1 
ATOM   7158  O O     . ILE B 1 402 ? 10.827  8.896   82.775  1.00 51.83  ? 402 ILE B O     1 
ATOM   7159  C CB    . ILE B 1 402 ? 11.078  12.004  82.539  1.00 53.04  ? 402 ILE B CB    1 
ATOM   7160  C CG1   . ILE B 1 402 ? 11.454  11.787  84.008  1.00 54.15  ? 402 ILE B CG1   1 
ATOM   7161  C CG2   . ILE B 1 402 ? 9.586   12.223  82.359  1.00 57.11  ? 402 ILE B CG2   1 
ATOM   7162  C CD1   . ILE B 1 402 ? 11.440  13.069  84.846  1.00 61.27  ? 402 ILE B CD1   1 
ATOM   7163  N N     . LYS B 1 403 ? 9.817   9.390   80.829  1.00 57.18  ? 403 LYS B N     1 
ATOM   7164  C CA    . LYS B 1 403 ? 8.836   8.327   80.931  1.00 55.84  ? 403 LYS B CA    1 
ATOM   7165  C C     . LYS B 1 403 ? 9.545   7.002   80.686  1.00 54.93  ? 403 LYS B C     1 
ATOM   7166  O O     . LYS B 1 403 ? 9.318   6.016   81.383  1.00 63.30  ? 403 LYS B O     1 
ATOM   7167  C CB    . LYS B 1 403 ? 7.698   8.596   79.944  1.00 53.49  ? 403 LYS B CB    1 
ATOM   7168  C CG    . LYS B 1 403 ? 6.592   7.560   80.004  1.00 63.69  ? 403 LYS B CG    1 
ATOM   7169  C CD    . LYS B 1 403 ? 5.829   7.430   78.704  1.00 67.71  ? 403 LYS B CD    1 
ATOM   7170  C CE    . LYS B 1 403 ? 4.878   6.257   78.704  1.00 65.01  ? 403 LYS B CE    1 
ATOM   7171  N NZ    . LYS B 1 403 ? 4.096   6.202   77.453  1.00 64.20  ? 403 LYS B NZ    1 
ATOM   7172  N N     . GLN B 1 404 ? 10.421  7.010   79.682  1.00 59.90  ? 404 GLN B N     1 
ATOM   7173  C CA    . GLN B 1 404 ? 11.258  5.863   79.372  1.00 58.48  ? 404 GLN B CA    1 
ATOM   7174  C C     . GLN B 1 404 ? 12.379  5.672   80.386  1.00 48.53  ? 404 GLN B C     1 
ATOM   7175  O O     . GLN B 1 404 ? 12.678  4.531   80.725  1.00 45.57  ? 404 GLN B O     1 
ATOM   7176  C CB    . GLN B 1 404 ? 11.836  6.032   77.978  1.00 57.51  ? 404 GLN B CB    1 
ATOM   7177  C CG    . GLN B 1 404 ? 10.776  5.740   76.939  1.00 55.29  ? 404 GLN B CG    1 
ATOM   7178  C CD    . GLN B 1 404 ? 11.304  5.996   75.560  1.00 47.73  ? 404 GLN B CD    1 
ATOM   7179  O OE1   . GLN B 1 404 ? 11.844  5.082   74.949  1.00 41.88  ? 404 GLN B OE1   1 
ATOM   7180  N NE2   . GLN B 1 404 ? 11.238  7.257   75.141  1.00 46.67  ? 404 GLN B NE2   1 
ATOM   7181  N N     . TYR B 1 405 ? 12.982  6.760   80.876  1.00 49.68  ? 405 TYR B N     1 
ATOM   7182  C CA    . TYR B 1 405 ? 13.874  6.649   82.028  1.00 59.38  ? 405 TYR B CA    1 
ATOM   7183  C C     . TYR B 1 405 ? 13.222  5.787   83.112  1.00 60.31  ? 405 TYR B C     1 
ATOM   7184  O O     . TYR B 1 405 ? 13.826  4.803   83.542  1.00 58.59  ? 405 TYR B O     1 
ATOM   7185  C CB    . TYR B 1 405 ? 14.286  8.009   82.605  1.00 59.17  ? 405 TYR B CB    1 
ATOM   7186  C CG    . TYR B 1 405 ? 14.970  7.910   83.950  1.00 64.90  ? 405 TYR B CG    1 
ATOM   7187  C CD1   . TYR B 1 405 ? 15.934  6.947   84.203  1.00 65.65  ? 405 TYR B CD1   1 
ATOM   7188  C CD2   . TYR B 1 405 ? 14.654  8.780   84.976  1.00 69.43  ? 405 TYR B CD2   1 
ATOM   7189  C CE1   . TYR B 1 405 ? 16.536  6.831   85.444  1.00 61.37  ? 405 TYR B CE1   1 
ATOM   7190  C CE2   . TYR B 1 405 ? 15.271  8.698   86.212  1.00 76.45  ? 405 TYR B CE2   1 
ATOM   7191  C CZ    . TYR B 1 405 ? 16.215  7.718   86.448  1.00 68.66  ? 405 TYR B CZ    1 
ATOM   7192  O OH    . TYR B 1 405 ? 16.805  7.619   87.683  1.00 77.65  ? 405 TYR B OH    1 
ATOM   7193  N N     . ASN B 1 406 ? 11.990  6.152   83.520  1.00 61.17  ? 406 ASN B N     1 
ATOM   7194  C CA    . ASN B 1 406 ? 11.317  5.542   84.665  1.00 56.81  ? 406 ASN B CA    1 
ATOM   7195  C C     . ASN B 1 406 ? 10.967  4.094   84.314  1.00 56.02  ? 406 ASN B C     1 
ATOM   7196  O O     . ASN B 1 406 ? 11.156  3.180   85.111  1.00 54.40  ? 406 ASN B O     1 
ATOM   7197  C CB    . ASN B 1 406 ? 10.091  6.359   85.131  1.00 51.91  ? 406 ASN B CB    1 
ATOM   7198  C CG    . ASN B 1 406 ? 10.451  7.522   86.040  1.00 53.32  ? 406 ASN B CG    1 
ATOM   7199  O OD1   . ASN B 1 406 ? 11.104  7.330   87.060  1.00 85.25  ? 406 ASN B OD1   1 
ATOM   7200  N ND2   . ASN B 1 406 ? 10.060  8.739   85.713  1.00 43.56  ? 406 ASN B ND2   1 
ATOM   7201  N N     . MET B 1 407 ? 10.444  3.893   83.107  1.00 52.26  ? 407 MET B N     1 
ATOM   7202  C CA    . MET B 1 407 ? 9.960   2.590   82.688  1.00 52.31  ? 407 MET B CA    1 
ATOM   7203  C C     . MET B 1 407 ? 11.096  1.581   82.760  1.00 51.30  ? 407 MET B C     1 
ATOM   7204  O O     . MET B 1 407 ? 10.885  0.459   83.206  1.00 48.98  ? 407 MET B O     1 
ATOM   7205  C CB    . MET B 1 407 ? 9.453   2.628   81.243  1.00 55.45  ? 407 MET B CB    1 
ATOM   7206  C CG    . MET B 1 407 ? 7.994   2.987   81.103  1.00 63.47  ? 407 MET B CG    1 
ATOM   7207  S SD    . MET B 1 407 ? 7.526   2.968   79.334  1.00 58.99  ? 407 MET B SD    1 
ATOM   7208  C CE    . MET B 1 407 ? 7.323   1.204   79.089  1.00 49.43  ? 407 MET B CE    1 
ATOM   7209  N N     . VAL B 1 408 ? 12.282  1.992   82.281  1.00 52.43  ? 408 VAL B N     1 
ATOM   7210  C CA    . VAL B 1 408 ? 13.407  1.089   82.105  1.00 50.74  ? 408 VAL B CA    1 
ATOM   7211  C C     . VAL B 1 408 ? 14.161  0.905   83.418  1.00 44.47  ? 408 VAL B C     1 
ATOM   7212  O O     . VAL B 1 408 ? 14.323  -0.214  83.888  1.00 48.76  ? 408 VAL B O     1 
ATOM   7213  C CB    . VAL B 1 408 ? 14.328  1.592   80.979  1.00 63.14  ? 408 VAL B CB    1 
ATOM   7214  C CG1   . VAL B 1 408 ? 15.711  0.953   81.048  1.00 61.82  ? 408 VAL B CG1   1 
ATOM   7215  C CG2   . VAL B 1 408 ? 13.676  1.394   79.598  1.00 60.71  ? 408 VAL B CG2   1 
ATOM   7216  N N     . SER B 1 409 ? 14.598  1.995   84.033  1.00 47.70  ? 409 SER B N     1 
ATOM   7217  C CA    . SER B 1 409 ? 15.415  1.878   85.229  1.00 55.23  ? 409 SER B CA    1 
ATOM   7218  C C     . SER B 1 409 ? 14.760  0.914   86.206  1.00 59.18  ? 409 SER B C     1 
ATOM   7219  O O     . SER B 1 409 ? 15.403  -0.039  86.615  1.00 76.13  ? 409 SER B O     1 
ATOM   7220  C CB    . SER B 1 409 ? 15.688  3.203   85.871  1.00 52.72  ? 409 SER B CB    1 
ATOM   7221  O OG    . SER B 1 409 ? 14.468  3.783   86.274  1.00 59.64  ? 409 SER B OG    1 
ATOM   7222  N N     . SER B 1 410 ? 13.477  1.126   86.523  1.00 69.72  ? 410 SER B N     1 
ATOM   7223  C CA    . SER B 1 410 ? 12.757  0.314   87.504  1.00 69.37  ? 410 SER B CA    1 
ATOM   7224  C C     . SER B 1 410 ? 12.848  -1.175  87.183  1.00 60.27  ? 410 SER B C     1 
ATOM   7225  O O     . SER B 1 410 ? 13.102  -1.994  88.063  1.00 64.14  ? 410 SER B O     1 
ATOM   7226  C CB    . SER B 1 410 ? 11.296  0.729   87.630  1.00 80.64  ? 410 SER B CB    1 
ATOM   7227  O OG    . SER B 1 410 ? 10.532  0.357   86.487  1.00 74.17  ? 410 SER B OG    1 
ATOM   7228  N N     . ARG B 1 411 ? 12.602  -1.501  85.917  1.00 52.10  ? 411 ARG B N     1 
ATOM   7229  C CA    . ARG B 1 411 ? 12.658  -2.861  85.427  1.00 55.35  ? 411 ARG B CA    1 
ATOM   7230  C C     . ARG B 1 411 ? 14.071  -3.445  85.430  1.00 56.72  ? 411 ARG B C     1 
ATOM   7231  O O     . ARG B 1 411 ? 14.221  -4.643  85.673  1.00 51.75  ? 411 ARG B O     1 
ATOM   7232  C CB    . ARG B 1 411 ? 12.136  -2.864  83.993  1.00 60.61  ? 411 ARG B CB    1 
ATOM   7233  C CG    . ARG B 1 411 ? 10.635  -2.691  83.909  1.00 59.90  ? 411 ARG B CG    1 
ATOM   7234  C CD    . ARG B 1 411 ? 10.021  -4.066  84.021  1.00 64.47  ? 411 ARG B CD    1 
ATOM   7235  N NE    . ARG B 1 411 ? 8.575   -3.987  83.912  1.00 61.57  ? 411 ARG B NE    1 
ATOM   7236  C CZ    . ARG B 1 411 ? 7.746   -4.215  84.918  1.00 64.71  ? 411 ARG B CZ    1 
ATOM   7237  N NH1   . ARG B 1 411 ? 8.228   -4.615  86.080  1.00 65.82  ? 411 ARG B NH1   1 
ATOM   7238  N NH2   . ARG B 1 411 ? 6.442   -4.075  84.749  1.00 63.97  ? 411 ARG B NH2   1 
ATOM   7239  N N     . VAL B 1 412 ? 15.085  -2.649  85.051  1.00 52.80  ? 412 VAL B N     1 
ATOM   7240  C CA    . VAL B 1 412 ? 16.463  -3.142  84.983  1.00 56.53  ? 412 VAL B CA    1 
ATOM   7241  C C     . VAL B 1 412 ? 16.970  -3.459  86.393  1.00 57.17  ? 412 VAL B C     1 
ATOM   7242  O O     . VAL B 1 412 ? 17.500  -4.547  86.613  1.00 57.68  ? 412 VAL B O     1 
ATOM   7243  C CB    . VAL B 1 412 ? 17.388  -2.151  84.242  1.00 57.04  ? 412 VAL B CB    1 
ATOM   7244  C CG1   . VAL B 1 412 ? 18.821  -2.157  84.745  1.00 70.25  ? 412 VAL B CG1   1 
ATOM   7245  C CG2   . VAL B 1 412 ? 17.374  -2.383  82.751  1.00 52.98  ? 412 VAL B CG2   1 
ATOM   7246  N N     . ARG B 1 413 ? 16.772  -2.509  87.329  1.00 60.14  ? 413 ARG B N     1 
ATOM   7247  C CA    . ARG B 1 413 ? 17.095  -2.664  88.745  1.00 65.21  ? 413 ARG B CA    1 
ATOM   7248  C C     . ARG B 1 413 ? 16.305  -3.830  89.340  1.00 62.32  ? 413 ARG B C     1 
ATOM   7249  O O     . ARG B 1 413 ? 16.839  -4.620  90.105  1.00 71.99  ? 413 ARG B O     1 
ATOM   7250  C CB    . ARG B 1 413 ? 16.867  -1.344  89.498  1.00 58.83  ? 413 ARG B CB    1 
ATOM   7251  C CG    . ARG B 1 413 ? 17.866  -0.247  89.126  1.00 63.73  ? 413 ARG B CG    1 
ATOM   7252  C CD    . ARG B 1 413 ? 17.454  1.172   89.506  1.00 68.16  ? 413 ARG B CD    1 
ATOM   7253  N NE    . ARG B 1 413 ? 17.165  1.349   90.926  1.00 66.91  ? 413 ARG B NE    1 
ATOM   7254  C CZ    . ARG B 1 413 ? 18.067  1.359   91.904  1.00 62.26  ? 413 ARG B CZ    1 
ATOM   7255  N NH1   . ARG B 1 413 ? 19.357  1.265   91.633  1.00 64.50  ? 413 ARG B NH1   1 
ATOM   7256  N NH2   . ARG B 1 413 ? 17.670  1.474   93.158  1.00 60.12  ? 413 ARG B NH2   1 
ATOM   7257  N N     . GLU B 1 414 ? 15.048  -3.977  88.940  1.00 61.71  ? 414 GLU B N     1 
ATOM   7258  C CA    . GLU B 1 414 ? 14.226  -5.070  89.427  1.00 58.37  ? 414 GLU B CA    1 
ATOM   7259  C C     . GLU B 1 414 ? 14.871  -6.391  89.028  1.00 54.60  ? 414 GLU B C     1 
ATOM   7260  O O     . GLU B 1 414 ? 14.751  -7.359  89.755  1.00 55.88  ? 414 GLU B O     1 
ATOM   7261  C CB    . GLU B 1 414 ? 12.785  -4.890  88.930  1.00 57.84  ? 414 GLU B CB    1 
ATOM   7262  C CG    . GLU B 1 414 ? 11.865  -6.106  89.060  1.00 59.19  ? 414 GLU B CG    1 
ATOM   7263  C CD    . GLU B 1 414 ? 10.533  -6.007  88.309  1.00 60.30  ? 414 GLU B CD    1 
ATOM   7264  O OE1   . GLU B 1 414 ? 10.085  -4.871  87.955  1.00 50.69  ? 414 GLU B OE1   1 
ATOM   7265  O OE2   . GLU B 1 414 ? 9.960   -7.067  88.020  1.00 57.87  ? 414 GLU B OE2   1 
ATOM   7266  N N     . TYR B 1 415 ? 15.566  -6.454  87.889  1.00 64.52  ? 415 TYR B N     1 
ATOM   7267  C CA    . TYR B 1 415 ? 16.093  -7.738  87.418  1.00 65.86  ? 415 TYR B CA    1 
ATOM   7268  C C     . TYR B 1 415 ? 17.537  -7.933  87.892  1.00 68.10  ? 415 TYR B C     1 
ATOM   7269  O O     . TYR B 1 415 ? 18.133  -8.970  87.590  1.00 59.19  ? 415 TYR B O     1 
ATOM   7270  C CB    . TYR B 1 415 ? 15.898  -7.916  85.901  1.00 55.20  ? 415 TYR B CB    1 
ATOM   7271  C CG    . TYR B 1 415 ? 14.554  -8.514  85.592  1.00 54.13  ? 415 TYR B CG    1 
ATOM   7272  C CD1   . TYR B 1 415 ? 13.391  -7.753  85.682  1.00 59.44  ? 415 TYR B CD1   1 
ATOM   7273  C CD2   . TYR B 1 415 ? 14.418  -9.873  85.363  1.00 50.79  ? 415 TYR B CD2   1 
ATOM   7274  C CE1   . TYR B 1 415 ? 12.136  -8.316  85.495  1.00 56.22  ? 415 TYR B CE1   1 
ATOM   7275  C CE2   . TYR B 1 415 ? 13.172  -10.451 85.168  1.00 55.83  ? 415 TYR B CE2   1 
ATOM   7276  C CZ    . TYR B 1 415 ? 12.026  -9.674  85.240  1.00 57.81  ? 415 TYR B CZ    1 
ATOM   7277  O OH    . TYR B 1 415 ? 10.792  -10.260 85.059  1.00 56.30  ? 415 TYR B OH    1 
ATOM   7278  N N     . GLY B 1 416 ? 18.061  -6.959  88.666  1.00 65.33  ? 416 GLY B N     1 
ATOM   7279  C CA    . GLY B 1 416 ? 19.361  -7.072  89.317  1.00 66.41  ? 416 GLY B CA    1 
ATOM   7280  C C     . GLY B 1 416 ? 20.479  -6.277  88.635  1.00 68.89  ? 416 GLY B C     1 
ATOM   7281  O O     . GLY B 1 416 ? 21.571  -6.178  89.182  1.00 82.58  ? 416 GLY B O     1 
ATOM   7282  N N     . PHE B 1 417 ? 20.218  -5.723  87.443  1.00 58.03  ? 417 PHE B N     1 
ATOM   7283  C CA    . PHE B 1 417 ? 21.216  -4.973  86.704  1.00 56.76  ? 417 PHE B CA    1 
ATOM   7284  C C     . PHE B 1 417 ? 21.148  -3.517  87.128  1.00 55.04  ? 417 PHE B C     1 
ATOM   7285  O O     . PHE B 1 417 ? 20.104  -3.079  87.608  1.00 52.68  ? 417 PHE B O     1 
ATOM   7286  C CB    . PHE B 1 417 ? 20.986  -5.158  85.206  1.00 55.67  ? 417 PHE B CB    1 
ATOM   7287  C CG    . PHE B 1 417 ? 20.978  -6.609  84.816  1.00 52.66  ? 417 PHE B CG    1 
ATOM   7288  C CD1   . PHE B 1 417 ? 22.154  -7.341  84.796  1.00 50.92  ? 417 PHE B CD1   1 
ATOM   7289  C CD2   . PHE B 1 417 ? 19.783  -7.273  84.578  1.00 53.31  ? 417 PHE B CD2   1 
ATOM   7290  C CE1   . PHE B 1 417 ? 22.138  -8.703  84.505  1.00 48.93  ? 417 PHE B CE1   1 
ATOM   7291  C CE2   . PHE B 1 417 ? 19.768  -8.630  84.284  1.00 49.14  ? 417 PHE B CE2   1 
ATOM   7292  C CZ    . PHE B 1 417 ? 20.946  -9.334  84.212  1.00 49.78  ? 417 PHE B CZ    1 
ATOM   7293  N N     . ASP B 1 418 ? 22.280  -2.809  87.009  1.00 49.11  ? 418 ASP B N     1 
ATOM   7294  C CA    . ASP B 1 418 ? 22.294  -1.374  87.230  1.00 50.53  ? 418 ASP B CA    1 
ATOM   7295  C C     . ASP B 1 418 ? 21.642  -0.690  86.030  1.00 54.13  ? 418 ASP B C     1 
ATOM   7296  O O     . ASP B 1 418 ? 21.718  -1.171  84.885  1.00 46.48  ? 418 ASP B O     1 
ATOM   7297  C CB    . ASP B 1 418 ? 23.709  -0.851  87.511  1.00 57.29  ? 418 ASP B CB    1 
ATOM   7298  C CG    . ASP B 1 418 ? 24.244  -1.246  88.882  1.00 68.41  ? 418 ASP B CG    1 
ATOM   7299  O OD1   . ASP B 1 418 ? 23.512  -1.016  89.878  1.00 62.31  ? 418 ASP B OD1   1 
ATOM   7300  O OD2   . ASP B 1 418 ? 25.384  -1.798  88.944  1.00 70.80  ? 418 ASP B OD2   1 
ATOM   7301  N N     . TYR B 1 419 ? 20.991  0.444   86.313  1.00 56.85  ? 419 TYR B N     1 
ATOM   7302  C CA    . TYR B 1 419 ? 20.462  1.241   85.228  1.00 57.63  ? 419 TYR B CA    1 
ATOM   7303  C C     . TYR B 1 419 ? 21.622  1.995   84.594  1.00 56.96  ? 419 TYR B C     1 
ATOM   7304  O O     . TYR B 1 419 ? 22.291  2.776   85.267  1.00 63.44  ? 419 TYR B O     1 
ATOM   7305  C CB    . TYR B 1 419 ? 19.364  2.211   85.665  1.00 56.53  ? 419 TYR B CB    1 
ATOM   7306  C CG    . TYR B 1 419 ? 19.025  3.185   84.563  1.00 52.59  ? 419 TYR B CG    1 
ATOM   7307  C CD1   . TYR B 1 419 ? 18.491  2.744   83.365  1.00 46.37  ? 419 TYR B CD1   1 
ATOM   7308  C CD2   . TYR B 1 419 ? 19.322  4.536   84.686  1.00 51.75  ? 419 TYR B CD2   1 
ATOM   7309  C CE1   . TYR B 1 419 ? 18.240  3.630   82.330  1.00 51.28  ? 419 TYR B CE1   1 
ATOM   7310  C CE2   . TYR B 1 419 ? 19.062  5.435   83.666  1.00 53.68  ? 419 TYR B CE2   1 
ATOM   7311  C CZ    . TYR B 1 419 ? 18.507  4.979   82.486  1.00 52.62  ? 419 TYR B CZ    1 
ATOM   7312  O OH    . TYR B 1 419 ? 18.279  5.870   81.470  1.00 51.15  ? 419 TYR B OH    1 
ATOM   7313  N N     . MET B 1 420 ? 21.838  1.722   83.304  1.00 63.50  ? 420 MET B N     1 
ATOM   7314  C CA    . MET B 1 420 ? 22.840  2.392   82.490  1.00 61.76  ? 420 MET B CA    1 
ATOM   7315  C C     . MET B 1 420 ? 22.149  2.904   81.235  1.00 58.74  ? 420 MET B C     1 
ATOM   7316  O O     . MET B 1 420 ? 21.695  2.129   80.397  1.00 47.22  ? 420 MET B O     1 
ATOM   7317  C CB    . MET B 1 420 ? 23.953  1.421   82.094  1.00 58.21  ? 420 MET B CB    1 
ATOM   7318  C CG    . MET B 1 420 ? 24.799  1.013   83.275  1.00 58.81  ? 420 MET B CG    1 
ATOM   7319  S SD    . MET B 1 420 ? 26.185  -0.007  82.789  1.00 63.01  ? 420 MET B SD    1 
ATOM   7320  C CE    . MET B 1 420 ? 26.341  -1.021  84.256  1.00 69.92  ? 420 MET B CE    1 
ATOM   7321  N N     . GLY B 1 421 ? 22.029  4.220   81.125  1.00 57.37  ? 421 GLY B N     1 
ATOM   7322  C CA    . GLY B 1 421 ? 21.179  4.749   80.084  1.00 50.81  ? 421 GLY B CA    1 
ATOM   7323  C C     . GLY B 1 421 ? 21.752  5.986   79.425  1.00 49.11  ? 421 GLY B C     1 
ATOM   7324  O O     . GLY B 1 421 ? 22.671  6.625   79.925  1.00 56.58  ? 421 GLY B O     1 
ATOM   7325  N N     . LEU B 1 422 ? 21.104  6.316   78.315  1.00 48.28  ? 422 LEU B N     1 
ATOM   7326  C CA    . LEU B 1 422 ? 21.552  7.327   77.388  1.00 52.93  ? 422 LEU B CA    1 
ATOM   7327  C C     . LEU B 1 422 ? 20.307  7.854   76.655  1.00 54.53  ? 422 LEU B C     1 
ATOM   7328  O O     . LEU B 1 422 ? 19.386  7.097   76.346  1.00 45.05  ? 422 LEU B O     1 
ATOM   7329  C CB    . LEU B 1 422 ? 22.569  6.580   76.516  1.00 57.16  ? 422 LEU B CB    1 
ATOM   7330  C CG    . LEU B 1 422 ? 23.161  7.294   75.312  1.00 60.03  ? 422 LEU B CG    1 
ATOM   7331  C CD1   . LEU B 1 422 ? 24.413  6.569   74.847  1.00 68.56  ? 422 LEU B CD1   1 
ATOM   7332  C CD2   . LEU B 1 422 ? 22.162  7.348   74.188  1.00 59.57  ? 422 LEU B CD2   1 
ATOM   7333  N N     . LEU B 1 423 ? 20.233  9.176   76.463  1.00 51.95  ? 423 LEU B N     1 
ATOM   7334  C CA    . LEU B 1 423 ? 19.272  9.771   75.557  1.00 47.32  ? 423 LEU B CA    1 
ATOM   7335  C C     . LEU B 1 423 ? 20.009  10.392  74.377  1.00 50.12  ? 423 LEU B C     1 
ATOM   7336  O O     . LEU B 1 423 ? 20.839  11.285  74.567  1.00 51.64  ? 423 LEU B O     1 
ATOM   7337  C CB    . LEU B 1 423 ? 18.466  10.807  76.329  1.00 54.59  ? 423 LEU B CB    1 
ATOM   7338  C CG    . LEU B 1 423 ? 17.421  10.197  77.258  1.00 69.33  ? 423 LEU B CG    1 
ATOM   7339  C CD1   . LEU B 1 423 ? 16.894  11.247  78.181  1.00 82.20  ? 423 LEU B CD1   1 
ATOM   7340  C CD2   . LEU B 1 423 ? 16.259  9.567   76.503  1.00 67.54  ? 423 LEU B CD2   1 
ATOM   7341  N N     . ALA B 1 424 ? 19.697  9.894   73.171  1.00 55.97  ? 424 ALA B N     1 
ATOM   7342  C CA    . ALA B 1 424 ? 20.351  10.306  71.930  1.00 56.85  ? 424 ALA B CA    1 
ATOM   7343  C C     . ALA B 1 424 ? 19.315  10.800  70.920  1.00 57.80  ? 424 ALA B C     1 
ATOM   7344  O O     . ALA B 1 424 ? 18.248  10.214  70.744  1.00 51.68  ? 424 ALA B O     1 
ATOM   7345  C CB    . ALA B 1 424 ? 21.147  9.182   71.317  1.00 55.78  ? 424 ALA B CB    1 
ATOM   7346  N N     . ILE B 1 425 ? 19.694  11.886  70.252  1.00 55.06  ? 425 ILE B N     1 
ATOM   7347  C CA    . ILE B 1 425 ? 18.896  12.534  69.244  1.00 55.25  ? 425 ILE B CA    1 
ATOM   7348  C C     . ILE B 1 425 ? 19.732  12.617  67.975  1.00 54.30  ? 425 ILE B C     1 
ATOM   7349  O O     . ILE B 1 425 ? 20.790  13.244  67.995  1.00 56.51  ? 425 ILE B O     1 
ATOM   7350  C CB    . ILE B 1 425 ? 18.490  13.924  69.764  1.00 59.06  ? 425 ILE B CB    1 
ATOM   7351  C CG1   . ILE B 1 425 ? 18.037  13.830  71.226  1.00 59.74  ? 425 ILE B CG1   1 
ATOM   7352  C CG2   . ILE B 1 425 ? 17.435  14.537  68.856  1.00 61.64  ? 425 ILE B CG2   1 
ATOM   7353  C CD1   . ILE B 1 425 ? 17.642  15.138  71.868  1.00 57.40  ? 425 ILE B CD1   1 
ATOM   7354  N N     . GLY B 1 426 ? 19.256  11.974  66.899  1.00 55.74  ? 426 GLY B N     1 
ATOM   7355  C CA    . GLY B 1 426 ? 19.725  12.222  65.540  1.00 56.71  ? 426 GLY B CA    1 
ATOM   7356  C C     . GLY B 1 426 ? 19.321  13.613  65.045  1.00 65.02  ? 426 GLY B C     1 
ATOM   7357  O O     . GLY B 1 426 ? 20.086  14.568  65.234  1.00 83.94  ? 426 GLY B O     1 
ATOM   7358  N N     . TRP B 1 427 ? 18.136  13.743  64.419  1.00 53.49  ? 427 TRP B N     1 
ATOM   7359  C CA    . TRP B 1 427 ? 17.714  15.040  63.891  1.00 50.85  ? 427 TRP B CA    1 
ATOM   7360  C C     . TRP B 1 427 ? 16.368  15.404  64.525  1.00 52.40  ? 427 TRP B C     1 
ATOM   7361  O O     . TRP B 1 427 ? 16.283  16.383  65.279  1.00 50.98  ? 427 TRP B O     1 
ATOM   7362  C CB    . TRP B 1 427 ? 17.704  15.048  62.341  1.00 36.81  ? 427 TRP B CB    1 
ATOM   7363  C CG    . TRP B 1 427 ? 17.577  16.392  61.698  1.00 34.46  ? 427 TRP B CG    1 
ATOM   7364  C CD1   . TRP B 1 427 ? 17.430  17.587  62.327  1.00 40.07  ? 427 TRP B CD1   1 
ATOM   7365  C CD2   . TRP B 1 427 ? 17.574  16.698  60.284  1.00 43.77  ? 427 TRP B CD2   1 
ATOM   7366  N NE1   . TRP B 1 427 ? 17.316  18.610  61.418  1.00 43.67  ? 427 TRP B NE1   1 
ATOM   7367  C CE2   . TRP B 1 427 ? 17.412  18.103  60.158  1.00 38.38  ? 427 TRP B CE2   1 
ATOM   7368  C CE3   . TRP B 1 427 ? 17.706  15.936  59.112  1.00 42.50  ? 427 TRP B CE3   1 
ATOM   7369  C CZ2   . TRP B 1 427 ? 17.404  18.755  58.937  1.00 39.60  ? 427 TRP B CZ2   1 
ATOM   7370  C CZ3   . TRP B 1 427 ? 17.662  16.581  57.895  1.00 44.63  ? 427 TRP B CZ3   1 
ATOM   7371  C CH2   . TRP B 1 427 ? 17.521  17.970  57.813  1.00 43.44  ? 427 TRP B CH2   1 
ATOM   7372  N N     . ARG B 1 428 ? 15.361  14.559  64.238  1.00 49.91  ? 428 ARG B N     1 
ATOM   7373  C CA    . ARG B 1 428 ? 14.008  14.651  64.775  1.00 52.88  ? 428 ARG B CA    1 
ATOM   7374  C C     . ARG B 1 428 ? 13.667  13.450  65.671  1.00 46.30  ? 428 ARG B C     1 
ATOM   7375  O O     . ARG B 1 428 ? 12.519  13.310  66.072  1.00 50.63  ? 428 ARG B O     1 
ATOM   7376  C CB    . ARG B 1 428 ? 13.006  14.769  63.613  1.00 42.53  ? 428 ARG B CB    1 
ATOM   7377  C CG    . ARG B 1 428 ? 12.873  16.199  63.080  1.00 44.57  ? 428 ARG B CG    1 
ATOM   7378  C CD    . ARG B 1 428 ? 12.419  16.311  61.625  1.00 41.31  ? 428 ARG B CD    1 
ATOM   7379  N NE    . ARG B 1 428 ? 12.188  17.670  61.166  1.00 38.13  ? 428 ARG B NE    1 
ATOM   7380  C CZ    . ARG B 1 428 ? 13.050  18.431  60.505  1.00 46.50  ? 428 ARG B CZ    1 
ATOM   7381  N NH1   . ARG B 1 428 ? 14.289  18.019  60.270  1.00 47.25  ? 428 ARG B NH1   1 
ATOM   7382  N NH2   . ARG B 1 428 ? 12.666  19.636  60.115  1.00 52.98  ? 428 ARG B NH2   1 
ATOM   7383  N N     . ASP B 1 429 ? 14.646  12.593  65.988  1.00 41.00  ? 429 ASP B N     1 
ATOM   7384  C CA    . ASP B 1 429 ? 14.405  11.300  66.642  1.00 46.05  ? 429 ASP B CA    1 
ATOM   7385  C C     . ASP B 1 429 ? 15.170  11.170  67.974  1.00 58.03  ? 429 ASP B C     1 
ATOM   7386  O O     . ASP B 1 429 ? 16.407  11.305  68.050  1.00 50.59  ? 429 ASP B O     1 
ATOM   7387  C CB    . ASP B 1 429 ? 14.781  10.130  65.725  1.00 42.50  ? 429 ASP B CB    1 
ATOM   7388  C CG    . ASP B 1 429 ? 16.225  10.122  65.223  1.00 44.31  ? 429 ASP B CG    1 
ATOM   7389  O OD1   . ASP B 1 429 ? 16.844  11.246  65.014  1.00 36.65  ? 429 ASP B OD1   1 
ATOM   7390  O OD2   . ASP B 1 429 ? 16.721  9.000   65.021  1.00 45.72  ? 429 ASP B OD2   1 
ATOM   7391  N N     . LEU B 1 430 ? 14.411  10.891  69.047  1.00 57.40  ? 430 LEU B N     1 
ATOM   7392  C CA    . LEU B 1 430 ? 14.995  10.620  70.344  1.00 48.05  ? 430 LEU B CA    1 
ATOM   7393  C C     . LEU B 1 430 ? 15.014  9.115   70.502  1.00 49.20  ? 430 LEU B C     1 
ATOM   7394  O O     . LEU B 1 430 ? 14.005  8.480   70.203  1.00 44.96  ? 430 LEU B O     1 
ATOM   7395  C CB    . LEU B 1 430 ? 14.143  11.275  71.433  1.00 59.14  ? 430 LEU B CB    1 
ATOM   7396  C CG    . LEU B 1 430 ? 14.648  11.101  72.870  1.00 52.15  ? 430 LEU B CG    1 
ATOM   7397  C CD1   . LEU B 1 430 ? 15.702  12.132  73.190  1.00 46.64  ? 430 LEU B CD1   1 
ATOM   7398  C CD2   . LEU B 1 430 ? 13.506  11.177  73.867  1.00 51.19  ? 430 LEU B CD2   1 
ATOM   7399  N N     . HIS B 1 431 ? 16.165  8.574   70.947  1.00 56.50  ? 431 HIS B N     1 
ATOM   7400  C CA    . HIS B 1 431 ? 16.215  7.243   71.541  1.00 56.82  ? 431 HIS B CA    1 
ATOM   7401  C C     . HIS B 1 431 ? 16.727  7.307   72.972  1.00 56.81  ? 431 HIS B C     1 
ATOM   7402  O O     . HIS B 1 431 ? 17.755  7.919   73.242  1.00 65.15  ? 431 HIS B O     1 
ATOM   7403  C CB    . HIS B 1 431 ? 17.203  6.297   70.865  1.00 53.86  ? 431 HIS B CB    1 
ATOM   7404  C CG    . HIS B 1 431 ? 17.101  6.344   69.407  1.00 53.80  ? 431 HIS B CG    1 
ATOM   7405  N ND1   . HIS B 1 431 ? 17.239  7.535   68.731  1.00 49.75  ? 431 HIS B ND1   1 
ATOM   7406  C CD2   . HIS B 1 431 ? 16.843  5.408   68.508  1.00 52.44  ? 431 HIS B CD2   1 
ATOM   7407  C CE1   . HIS B 1 431 ? 17.124  7.298   67.443  1.00 53.48  ? 431 HIS B CE1   1 
ATOM   7408  N NE2   . HIS B 1 431 ? 16.868  6.018   67.287  1.00 55.67  ? 431 HIS B NE2   1 
ATOM   7409  N N     . HIS B 1 432 ? 15.967  6.672   73.861  1.00 52.27  ? 432 HIS B N     1 
ATOM   7410  C CA    . HIS B 1 432 ? 16.446  6.249   75.154  1.00 49.66  ? 432 HIS B CA    1 
ATOM   7411  C C     . HIS B 1 432 ? 17.072  4.879   74.993  1.00 52.32  ? 432 HIS B C     1 
ATOM   7412  O O     . HIS B 1 432 ? 16.389  3.933   74.601  1.00 48.77  ? 432 HIS B O     1 
ATOM   7413  C CB    . HIS B 1 432 ? 15.292  6.099   76.138  1.00 53.68  ? 432 HIS B CB    1 
ATOM   7414  C CG    . HIS B 1 432 ? 15.703  5.418   77.387  1.00 53.58  ? 432 HIS B CG    1 
ATOM   7415  N ND1   . HIS B 1 432 ? 16.131  6.116   78.499  1.00 56.89  ? 432 HIS B ND1   1 
ATOM   7416  C CD2   . HIS B 1 432 ? 15.783  4.128   77.689  1.00 50.56  ? 432 HIS B CD2   1 
ATOM   7417  C CE1   . HIS B 1 432 ? 16.396  5.258   79.461  1.00 50.58  ? 432 HIS B CE1   1 
ATOM   7418  N NE2   . HIS B 1 432 ? 16.196  4.050   78.992  1.00 55.30  ? 432 HIS B NE2   1 
ATOM   7419  N N     . VAL B 1 433 ? 18.374  4.806   75.306  1.00 59.38  ? 433 VAL B N     1 
ATOM   7420  C CA    . VAL B 1 433 ? 19.163  3.620   75.043  1.00 53.13  ? 433 VAL B CA    1 
ATOM   7421  C C     . VAL B 1 433 ? 19.530  3.024   76.391  1.00 62.88  ? 433 VAL B C     1 
ATOM   7422  O O     . VAL B 1 433 ? 20.101  3.696   77.248  1.00 66.63  ? 433 VAL B O     1 
ATOM   7423  C CB    . VAL B 1 433 ? 20.417  3.928   74.207  1.00 51.07  ? 433 VAL B CB    1 
ATOM   7424  C CG1   . VAL B 1 433 ? 21.238  2.681   73.946  1.00 50.53  ? 433 VAL B CG1   1 
ATOM   7425  C CG2   . VAL B 1 433 ? 20.087  4.618   72.891  1.00 56.25  ? 433 VAL B CG2   1 
ATOM   7426  N N     . THR B 1 434 ? 19.164  1.757   76.555  1.00 61.46  ? 434 THR B N     1 
ATOM   7427  C CA    . THR B 1 434 ? 19.543  0.981   77.710  1.00 55.85  ? 434 THR B CA    1 
ATOM   7428  C C     . THR B 1 434 ? 20.753  0.116   77.369  1.00 59.63  ? 434 THR B C     1 
ATOM   7429  O O     . THR B 1 434 ? 20.678  -0.751  76.502  1.00 60.29  ? 434 THR B O     1 
ATOM   7430  C CB    . THR B 1 434 ? 18.365  0.107   78.125  1.00 57.31  ? 434 THR B CB    1 
ATOM   7431  O OG1   . THR B 1 434 ? 17.211  0.948   78.041  1.00 62.98  ? 434 THR B OG1   1 
ATOM   7432  C CG2   . THR B 1 434 ? 18.563  -0.509  79.493  1.00 52.86  ? 434 THR B CG2   1 
ATOM   7433  N N     . VAL B 1 435 ? 21.867  0.357   78.063  1.00 57.95  ? 435 VAL B N     1 
ATOM   7434  C CA    . VAL B 1 435 ? 22.961  -0.589  78.083  1.00 52.54  ? 435 VAL B CA    1 
ATOM   7435  C C     . VAL B 1 435 ? 22.764  -1.504  79.283  1.00 49.93  ? 435 VAL B C     1 
ATOM   7436  O O     . VAL B 1 435 ? 22.740  -1.029  80.410  1.00 56.67  ? 435 VAL B O     1 
ATOM   7437  C CB    . VAL B 1 435 ? 24.317  0.133   78.124  1.00 53.20  ? 435 VAL B CB    1 
ATOM   7438  C CG1   . VAL B 1 435 ? 25.484  -0.830  78.278  1.00 47.31  ? 435 VAL B CG1   1 
ATOM   7439  C CG2   . VAL B 1 435 ? 24.496  0.999   76.892  1.00 54.62  ? 435 VAL B CG2   1 
ATOM   7440  N N     . ILE B 1 436 ? 22.651  -2.809  79.016  1.00 50.09  ? 436 ILE B N     1 
ATOM   7441  C CA    . ILE B 1 436 ? 22.549  -3.823  80.054  1.00 58.52  ? 436 ILE B CA    1 
ATOM   7442  C C     . ILE B 1 436 ? 23.785  -4.727  80.047  1.00 57.16  ? 436 ILE B C     1 
ATOM   7443  O O     . ILE B 1 436 ? 23.870  -5.621  79.199  1.00 48.13  ? 436 ILE B O     1 
ATOM   7444  C CB    . ILE B 1 436 ? 21.280  -4.674  79.857  1.00 58.35  ? 436 ILE B CB    1 
ATOM   7445  C CG1   . ILE B 1 436 ? 20.022  -3.809  79.722  1.00 61.39  ? 436 ILE B CG1   1 
ATOM   7446  C CG2   . ILE B 1 436 ? 21.155  -5.692  80.978  1.00 53.86  ? 436 ILE B CG2   1 
ATOM   7447  C CD1   . ILE B 1 436 ? 18.776  -4.606  79.398  1.00 54.73  ? 436 ILE B CD1   1 
ATOM   7448  N N     . VAL B 1 437 ? 24.650  -4.545  81.068  1.00 55.00  ? 437 VAL B N     1 
ATOM   7449  C CA    . VAL B 1 437 ? 25.901  -5.274  81.252  1.00 56.91  ? 437 VAL B CA    1 
ATOM   7450  C C     . VAL B 1 437 ? 25.626  -6.505  82.118  1.00 62.72  ? 437 VAL B C     1 
ATOM   7451  O O     . VAL B 1 437 ? 24.799  -6.470  83.022  1.00 60.66  ? 437 VAL B O     1 
ATOM   7452  C CB    . VAL B 1 437 ? 26.975  -4.370  81.898  1.00 56.27  ? 437 VAL B CB    1 
ATOM   7453  C CG1   . VAL B 1 437 ? 28.300  -5.088  82.069  1.00 59.34  ? 437 VAL B CG1   1 
ATOM   7454  C CG2   . VAL B 1 437 ? 27.196  -3.060  81.143  1.00 52.91  ? 437 VAL B CG2   1 
ATOM   7455  N N     . TYR B 1 438 ? 26.328  -7.607  81.852  1.00 68.81  ? 438 TYR B N     1 
ATOM   7456  C CA    . TYR B 1 438 ? 25.995  -8.865  82.502  1.00 69.64  ? 438 TYR B CA    1 
ATOM   7457  C C     . TYR B 1 438 ? 27.048  -9.929  82.210  1.00 65.83  ? 438 TYR B C     1 
ATOM   7458  O O     . TYR B 1 438 ? 27.814  -9.798  81.262  1.00 68.70  ? 438 TYR B O     1 
ATOM   7459  C CB    . TYR B 1 438 ? 24.655  -9.406  82.002  1.00 62.90  ? 438 TYR B CB    1 
ATOM   7460  C CG    . TYR B 1 438 ? 24.684  -9.837  80.556  1.00 67.18  ? 438 TYR B CG    1 
ATOM   7461  C CD1   . TYR B 1 438 ? 24.739  -8.887  79.552  1.00 66.74  ? 438 TYR B CD1   1 
ATOM   7462  C CD2   . TYR B 1 438 ? 24.720  -11.178 80.187  1.00 62.53  ? 438 TYR B CD2   1 
ATOM   7463  C CE1   . TYR B 1 438 ? 24.789  -9.251  78.219  1.00 66.20  ? 438 TYR B CE1   1 
ATOM   7464  C CE2   . TYR B 1 438 ? 24.788  -11.558 78.856  1.00 65.33  ? 438 TYR B CE2   1 
ATOM   7465  C CZ    . TYR B 1 438 ? 24.814  -10.584 77.869  1.00 66.39  ? 438 TYR B CZ    1 
ATOM   7466  O OH    . TYR B 1 438 ? 24.847  -10.853 76.532  1.00 68.74  ? 438 TYR B OH    1 
ATOM   7467  N N     . ASP B 1 439 ? 26.990  -11.022 82.980  1.00 69.05  ? 439 ASP B N     1 
ATOM   7468  C CA    . ASP B 1 439 ? 27.957  -12.105 82.911  1.00 75.32  ? 439 ASP B CA    1 
ATOM   7469  C C     . ASP B 1 439 ? 27.531  -13.062 81.811  1.00 73.14  ? 439 ASP B C     1 
ATOM   7470  O O     . ASP B 1 439 ? 26.477  -13.670 81.927  1.00 65.37  ? 439 ASP B O     1 
ATOM   7471  C CB    . ASP B 1 439 ? 28.054  -12.835 84.256  1.00 81.63  ? 439 ASP B CB    1 
ATOM   7472  C CG    . ASP B 1 439 ? 29.219  -13.796 84.457  1.00 74.41  ? 439 ASP B CG    1 
ATOM   7473  O OD1   . ASP B 1 439 ? 30.011  -14.027 83.514  1.00 66.82  ? 439 ASP B OD1   1 
ATOM   7474  O OD2   . ASP B 1 439 ? 29.329  -14.296 85.581  1.00 69.40  ? 439 ASP B OD2   1 
ATOM   7475  N N     . LYS B 1 440 ? 28.360  -13.171 80.762  1.00 85.54  ? 440 LYS B N     1 
ATOM   7476  C CA    . LYS B 1 440 ? 28.153  -14.137 79.697  1.00 101.61 ? 440 LYS B CA    1 
ATOM   7477  C C     . LYS B 1 440 ? 28.126  -15.550 80.275  1.00 101.17 ? 440 LYS B C     1 
ATOM   7478  O O     . LYS B 1 440 ? 27.263  -16.345 79.905  1.00 97.19  ? 440 LYS B O     1 
ATOM   7479  C CB    . LYS B 1 440 ? 29.273  -14.055 78.653  1.00 117.24 ? 440 LYS B CB    1 
ATOM   7480  C CG    . LYS B 1 440 ? 29.333  -15.243 77.697  1.00 125.44 ? 440 LYS B CG    1 
ATOM   7481  C CD    . LYS B 1 440 ? 30.444  -15.158 76.686  1.00 124.03 ? 440 LYS B CD    1 
ATOM   7482  C CE    . LYS B 1 440 ? 31.820  -15.444 77.248  1.00 109.73 ? 440 LYS B CE    1 
ATOM   7483  N NZ    . LYS B 1 440 ? 32.835  -15.376 76.173  1.00 105.73 ? 440 LYS B NZ    1 
ATOM   7484  N N     . THR B 1 441 ? 29.099  -15.840 81.157  1.00 99.18  ? 441 THR B N     1 
ATOM   7485  C CA    . THR B 1 441 ? 29.353  -17.184 81.656  1.00 88.05  ? 441 THR B CA    1 
ATOM   7486  C C     . THR B 1 441 ? 28.170  -17.694 82.467  1.00 73.68  ? 441 THR B C     1 
ATOM   7487  O O     . THR B 1 441 ? 27.917  -18.889 82.472  1.00 67.15  ? 441 THR B O     1 
ATOM   7488  C CB    . THR B 1 441 ? 30.617  -17.268 82.527  1.00 85.71  ? 441 THR B CB    1 
ATOM   7489  O OG1   . THR B 1 441 ? 30.457  -16.462 83.697  1.00 78.26  ? 441 THR B OG1   1 
ATOM   7490  C CG2   . THR B 1 441 ? 31.862  -16.851 81.778  1.00 86.19  ? 441 THR B CG2   1 
ATOM   7491  N N     . ASP B 1 442 ? 27.458  -16.793 83.152  1.00 68.94  ? 442 ASP B N     1 
ATOM   7492  C CA    . ASP B 1 442 ? 26.500  -17.233 84.154  1.00 67.44  ? 442 ASP B CA    1 
ATOM   7493  C C     . ASP B 1 442 ? 25.165  -17.570 83.498  1.00 66.73  ? 442 ASP B C     1 
ATOM   7494  O O     . ASP B 1 442 ? 24.532  -16.689 82.933  1.00 74.39  ? 442 ASP B O     1 
ATOM   7495  C CB    . ASP B 1 442 ? 26.313  -16.172 85.230  1.00 64.22  ? 442 ASP B CB    1 
ATOM   7496  C CG    . ASP B 1 442 ? 25.567  -16.693 86.438  1.00 67.25  ? 442 ASP B CG    1 
ATOM   7497  O OD1   . ASP B 1 442 ? 25.247  -17.894 86.444  1.00 65.57  ? 442 ASP B OD1   1 
ATOM   7498  O OD2   . ASP B 1 442 ? 25.320  -15.889 87.360  1.00 73.07  ? 442 ASP B OD2   1 
ATOM   7499  N N     . PRO B 1 443 ? 24.671  -18.831 83.556  1.00 74.88  ? 443 PRO B N     1 
ATOM   7500  C CA    . PRO B 1 443 ? 23.363  -19.170 82.986  1.00 69.69  ? 443 PRO B CA    1 
ATOM   7501  C C     . PRO B 1 443 ? 22.188  -18.609 83.786  1.00 69.91  ? 443 PRO B C     1 
ATOM   7502  O O     . PRO B 1 443 ? 21.055  -18.550 83.294  1.00 59.61  ? 443 PRO B O     1 
ATOM   7503  C CB    . PRO B 1 443 ? 23.331  -20.711 82.983  1.00 71.55  ? 443 PRO B CB    1 
ATOM   7504  C CG    . PRO B 1 443 ? 24.772  -21.127 83.240  1.00 80.22  ? 443 PRO B CG    1 
ATOM   7505  C CD    . PRO B 1 443 ? 25.335  -20.020 84.114  1.00 80.59  ? 443 PRO B CD    1 
ATOM   7506  N N     . ASP B 1 444 ? 22.465  -18.186 85.024  1.00 66.47  ? 444 ASP B N     1 
ATOM   7507  C CA    . ASP B 1 444 ? 21.418  -17.662 85.876  1.00 76.16  ? 444 ASP B CA    1 
ATOM   7508  C C     . ASP B 1 444 ? 21.209  -16.189 85.538  1.00 73.12  ? 444 ASP B C     1 
ATOM   7509  O O     . ASP B 1 444 ? 20.069  -15.741 85.569  1.00 76.36  ? 444 ASP B O     1 
ATOM   7510  C CB    . ASP B 1 444 ? 21.696  -17.967 87.353  1.00 83.87  ? 444 ASP B CB    1 
ATOM   7511  C CG    . ASP B 1 444 ? 21.806  -19.458 87.677  1.00 84.83  ? 444 ASP B CG    1 
ATOM   7512  O OD1   . ASP B 1 444 ? 21.619  -20.295 86.770  1.00 73.48  ? 444 ASP B OD1   1 
ATOM   7513  O OD2   . ASP B 1 444 ? 22.101  -19.779 88.836  1.00 84.09  ? 444 ASP B OD2   1 
ATOM   7514  N N     . GLU B 1 445 ? 22.276  -15.451 85.191  1.00 71.15  ? 445 GLU B N     1 
ATOM   7515  C CA    . GLU B 1 445 ? 22.095  -14.070 84.764  1.00 73.01  ? 445 GLU B CA    1 
ATOM   7516  C C     . GLU B 1 445 ? 21.620  -14.040 83.314  1.00 67.92  ? 445 GLU B C     1 
ATOM   7517  O O     . GLU B 1 445 ? 20.960  -13.084 82.940  1.00 62.54  ? 445 GLU B O     1 
ATOM   7518  C CB    . GLU B 1 445 ? 23.325  -13.177 84.956  1.00 66.52  ? 445 GLU B CB    1 
ATOM   7519  C CG    . GLU B 1 445 ? 23.415  -12.544 86.340  1.00 80.27  ? 445 GLU B CG    1 
ATOM   7520  C CD    . GLU B 1 445 ? 24.071  -11.164 86.436  1.00 93.64  ? 445 GLU B CD    1 
ATOM   7521  O OE1   . GLU B 1 445 ? 25.130  -10.923 85.762  1.00 72.20  ? 445 GLU B OE1   1 
ATOM   7522  O OE2   . GLU B 1 445 ? 23.539  -10.316 87.215  1.00 87.09  ? 445 GLU B OE2   1 
ATOM   7523  N N     . ARG B 1 446 ? 21.933  -15.067 82.508  1.00 66.55  ? 446 ARG B N     1 
ATOM   7524  C CA    . ARG B 1 446 ? 21.563  -15.045 81.096  1.00 66.89  ? 446 ARG B CA    1 
ATOM   7525  C C     . ARG B 1 446 ? 20.052  -15.158 80.978  1.00 71.20  ? 446 ARG B C     1 
ATOM   7526  O O     . ARG B 1 446 ? 19.441  -14.460 80.183  1.00 86.07  ? 446 ARG B O     1 
ATOM   7527  C CB    . ARG B 1 446 ? 22.172  -16.192 80.278  1.00 60.55  ? 446 ARG B CB    1 
ATOM   7528  C CG    . ARG B 1 446 ? 23.662  -16.068 80.003  1.00 62.16  ? 446 ARG B CG    1 
ATOM   7529  C CD    . ARG B 1 446 ? 24.134  -16.946 78.855  1.00 70.13  ? 446 ARG B CD    1 
ATOM   7530  N NE    . ARG B 1 446 ? 24.057  -18.394 79.083  1.00 74.41  ? 446 ARG B NE    1 
ATOM   7531  C CZ    . ARG B 1 446 ? 25.101  -19.222 79.075  1.00 75.83  ? 446 ARG B CZ    1 
ATOM   7532  N NH1   . ARG B 1 446 ? 26.333  -18.749 78.976  1.00 78.85  ? 446 ARG B NH1   1 
ATOM   7533  N NH2   . ARG B 1 446 ? 24.916  -20.522 79.212  1.00 77.47  ? 446 ARG B NH2   1 
ATOM   7534  N N     . LYS B 1 447 ? 19.495  -16.095 81.748  1.00 77.09  ? 447 LYS B N     1 
ATOM   7535  C CA    . LYS B 1 447 ? 18.064  -16.314 81.883  1.00 71.86  ? 447 LYS B CA    1 
ATOM   7536  C C     . LYS B 1 447 ? 17.375  -14.988 82.199  1.00 65.31  ? 447 LYS B C     1 
ATOM   7537  O O     . LYS B 1 447 ? 16.479  -14.574 81.468  1.00 60.09  ? 447 LYS B O     1 
ATOM   7538  C CB    . LYS B 1 447 ? 17.843  -17.350 82.991  1.00 77.83  ? 447 LYS B CB    1 
ATOM   7539  C CG    . LYS B 1 447 ? 16.401  -17.689 83.357  1.00 95.28  ? 447 LYS B CG    1 
ATOM   7540  C CD    . LYS B 1 447 ? 16.195  -17.846 84.877  1.00 110.97 ? 447 LYS B CD    1 
ATOM   7541  C CE    . LYS B 1 447 ? 15.200  -18.918 85.282  1.00 109.08 ? 447 LYS B CE    1 
ATOM   7542  N NZ    . LYS B 1 447 ? 13.801  -18.555 84.959  1.00 101.13 ? 447 LYS B NZ    1 
ATOM   7543  N N     . LYS B 1 448 ? 17.811  -14.331 83.283  1.00 61.53  ? 448 LYS B N     1 
ATOM   7544  C CA    . LYS B 1 448 ? 17.169  -13.122 83.769  1.00 67.87  ? 448 LYS B CA    1 
ATOM   7545  C C     . LYS B 1 448 ? 17.257  -12.004 82.720  1.00 64.77  ? 448 LYS B C     1 
ATOM   7546  O O     . LYS B 1 448 ? 16.323  -11.211 82.581  1.00 60.10  ? 448 LYS B O     1 
ATOM   7547  C CB    . LYS B 1 448 ? 17.803  -12.641 85.083  1.00 82.41  ? 448 LYS B CB    1 
ATOM   7548  C CG    . LYS B 1 448 ? 17.736  -13.595 86.270  1.00 91.29  ? 448 LYS B CG    1 
ATOM   7549  C CD    . LYS B 1 448 ? 17.857  -12.896 87.624  1.00 95.65  ? 448 LYS B CD    1 
ATOM   7550  C CE    . LYS B 1 448 ? 16.514  -12.421 88.148  1.00 100.84 ? 448 LYS B CE    1 
ATOM   7551  N NZ    . LYS B 1 448 ? 16.629  -11.653 89.410  1.00 99.51  ? 448 LYS B NZ    1 
ATOM   7552  N N     . LEU B 1 449 ? 18.399  -11.919 82.014  1.00 64.90  ? 449 LEU B N     1 
ATOM   7553  C CA    . LEU B 1 449 ? 18.620  -10.910 80.984  1.00 60.66  ? 449 LEU B CA    1 
ATOM   7554  C C     . LEU B 1 449 ? 17.545  -11.025 79.908  1.00 49.31  ? 449 LEU B C     1 
ATOM   7555  O O     . LEU B 1 449 ? 17.056  -10.018 79.406  1.00 41.63  ? 449 LEU B O     1 
ATOM   7556  C CB    . LEU B 1 449 ? 20.004  -11.090 80.348  1.00 61.16  ? 449 LEU B CB    1 
ATOM   7557  C CG    . LEU B 1 449 ? 20.271  -10.150 79.172  1.00 62.44  ? 449 LEU B CG    1 
ATOM   7558  C CD1   . LEU B 1 449 ? 20.528  -8.732  79.667  1.00 60.21  ? 449 LEU B CD1   1 
ATOM   7559  C CD2   . LEU B 1 449 ? 21.435  -10.646 78.343  1.00 71.94  ? 449 LEU B CD2   1 
ATOM   7560  N N     . ASP B 1 450 ? 17.203  -12.272 79.605  1.00 44.65  ? 450 ASP B N     1 
ATOM   7561  C CA    . ASP B 1 450 ? 16.322  -12.621 78.517  1.00 58.00  ? 450 ASP B CA    1 
ATOM   7562  C C     . ASP B 1 450 ? 14.876  -12.302 78.897  1.00 62.61  ? 450 ASP B C     1 
ATOM   7563  O O     . ASP B 1 450 ? 14.128  -11.804 78.072  1.00 61.70  ? 450 ASP B O     1 
ATOM   7564  C CB    . ASP B 1 450 ? 16.547  -14.083 78.138  1.00 59.41  ? 450 ASP B CB    1 
ATOM   7565  C CG    . ASP B 1 450 ? 15.608  -14.561 77.050  1.00 67.91  ? 450 ASP B CG    1 
ATOM   7566  O OD1   . ASP B 1 450 ? 15.240  -13.740 76.202  1.00 67.02  ? 450 ASP B OD1   1 
ATOM   7567  O OD2   . ASP B 1 450 ? 15.301  -15.765 77.033  1.00 68.70  ? 450 ASP B OD2   1 
ATOM   7568  N N     . GLU B 1 451 ? 14.488  -12.578 80.144  1.00 66.29  ? 451 GLU B N     1 
ATOM   7569  C CA    . GLU B 1 451 ? 13.168  -12.217 80.632  1.00 63.34  ? 451 GLU B CA    1 
ATOM   7570  C C     . GLU B 1 451 ? 13.054  -10.692 80.713  1.00 62.18  ? 451 GLU B C     1 
ATOM   7571  O O     . GLU B 1 451 ? 11.988  -10.129 80.459  1.00 64.14  ? 451 GLU B O     1 
ATOM   7572  C CB    . GLU B 1 451 ? 12.907  -12.843 82.009  1.00 74.60  ? 451 GLU B CB    1 
ATOM   7573  C CG    . GLU B 1 451 ? 12.967  -14.374 82.050  1.00 85.06  ? 451 GLU B CG    1 
ATOM   7574  C CD    . GLU B 1 451 ? 12.831  -15.032 83.426  1.00 92.15  ? 451 GLU B CD    1 
ATOM   7575  O OE1   . GLU B 1 451 ? 12.870  -16.280 83.490  1.00 85.90  ? 451 GLU B OE1   1 
ATOM   7576  O OE2   . GLU B 1 451 ? 12.694  -14.313 84.444  1.00 96.43  ? 451 GLU B OE2   1 
ATOM   7577  N N     . LEU B 1 452 ? 14.147  -10.021 81.099  1.00 52.99  ? 452 LEU B N     1 
ATOM   7578  C CA    . LEU B 1 452 ? 14.144  -8.571  81.219  1.00 54.33  ? 452 LEU B CA    1 
ATOM   7579  C C     . LEU B 1 452 ? 13.998  -7.916  79.844  1.00 62.47  ? 452 LEU B C     1 
ATOM   7580  O O     . LEU B 1 452 ? 13.388  -6.849  79.729  1.00 57.80  ? 452 LEU B O     1 
ATOM   7581  C CB    . LEU B 1 452 ? 15.434  -8.113  81.908  1.00 48.12  ? 452 LEU B CB    1 
ATOM   7582  C CG    . LEU B 1 452 ? 15.837  -6.655  81.674  1.00 48.69  ? 452 LEU B CG    1 
ATOM   7583  C CD1   . LEU B 1 452 ? 14.805  -5.700  82.234  1.00 48.45  ? 452 LEU B CD1   1 
ATOM   7584  C CD2   . LEU B 1 452 ? 17.199  -6.362  82.302  1.00 49.73  ? 452 LEU B CD2   1 
ATOM   7585  N N     . PHE B 1 453 ? 14.597  -8.533  78.815  1.00 64.43  ? 453 PHE B N     1 
ATOM   7586  C CA    . PHE B 1 453 ? 14.714  -7.877  77.523  1.00 63.97  ? 453 PHE B CA    1 
ATOM   7587  C C     . PHE B 1 453 ? 13.337  -7.870  76.859  1.00 55.67  ? 453 PHE B C     1 
ATOM   7588  O O     . PHE B 1 453 ? 12.868  -6.841  76.378  1.00 54.43  ? 453 PHE B O     1 
ATOM   7589  C CB    . PHE B 1 453 ? 15.802  -8.535  76.661  1.00 60.28  ? 453 PHE B CB    1 
ATOM   7590  C CG    . PHE B 1 453 ? 16.283  -7.658  75.531  1.00 58.82  ? 453 PHE B CG    1 
ATOM   7591  C CD1   . PHE B 1 453 ? 17.164  -6.614  75.768  1.00 55.41  ? 453 PHE B CD1   1 
ATOM   7592  C CD2   . PHE B 1 453 ? 15.784  -7.820  74.245  1.00 57.09  ? 453 PHE B CD2   1 
ATOM   7593  C CE1   . PHE B 1 453 ? 17.565  -5.781  74.735  1.00 63.25  ? 453 PHE B CE1   1 
ATOM   7594  C CE2   . PHE B 1 453 ? 16.198  -6.992  73.217  1.00 57.58  ? 453 PHE B CE2   1 
ATOM   7595  C CZ    . PHE B 1 453 ? 17.079  -5.970  73.464  1.00 57.14  ? 453 PHE B CZ    1 
ATOM   7596  N N     . ASN B 1 454 ? 12.689  -9.029  76.915  1.00 48.37  ? 454 ASN B N     1 
ATOM   7597  C CA    . ASN B 1 454 ? 11.350  -9.229  76.390  1.00 57.48  ? 454 ASN B CA    1 
ATOM   7598  C C     . ASN B 1 454 ? 10.338  -8.257  76.997  1.00 59.27  ? 454 ASN B C     1 
ATOM   7599  O O     . ASN B 1 454 ? 9.437   -7.788  76.311  1.00 69.87  ? 454 ASN B O     1 
ATOM   7600  C CB    . ASN B 1 454 ? 10.881  -10.668 76.606  1.00 50.55  ? 454 ASN B CB    1 
ATOM   7601  C CG    . ASN B 1 454 ? 11.626  -11.635 75.714  1.00 50.06  ? 454 ASN B CG    1 
ATOM   7602  O OD1   . ASN B 1 454 ? 11.910  -11.337 74.556  1.00 66.16  ? 454 ASN B OD1   1 
ATOM   7603  N ND2   . ASN B 1 454 ? 11.932  -12.809 76.223  1.00 49.71  ? 454 ASN B ND2   1 
ATOM   7604  N N     . ILE B 1 455 ? 10.459  -7.988  78.288  1.00 51.04  ? 455 ILE B N     1 
ATOM   7605  C CA    . ILE B 1 455 ? 9.573   -7.056  78.949  1.00 46.47  ? 455 ILE B CA    1 
ATOM   7606  C C     . ILE B 1 455 ? 9.803   -5.666  78.365  1.00 51.10  ? 455 ILE B C     1 
ATOM   7607  O O     . ILE B 1 455 ? 8.838   -4.969  78.060  1.00 60.80  ? 455 ILE B O     1 
ATOM   7608  C CB    . ILE B 1 455 ? 9.827   -7.114  80.471  1.00 49.18  ? 455 ILE B CB    1 
ATOM   7609  C CG1   . ILE B 1 455 ? 9.351   -8.454  81.034  1.00 59.37  ? 455 ILE B CG1   1 
ATOM   7610  C CG2   . ILE B 1 455 ? 9.226   -5.919  81.201  1.00 48.09  ? 455 ILE B CG2   1 
ATOM   7611  C CD1   . ILE B 1 455 ? 9.838   -8.764  82.450  1.00 67.87  ? 455 ILE B CD1   1 
ATOM   7612  N N     . LEU B 1 456 ? 11.073  -5.255  78.253  1.00 51.79  ? 456 LEU B N     1 
ATOM   7613  C CA    . LEU B 1 456 ? 11.413  -3.909  77.806  1.00 55.90  ? 456 LEU B CA    1 
ATOM   7614  C C     . LEU B 1 456 ? 10.833  -3.657  76.415  1.00 51.95  ? 456 LEU B C     1 
ATOM   7615  O O     . LEU B 1 456 ? 10.366  -2.566  76.103  1.00 51.59  ? 456 LEU B O     1 
ATOM   7616  C CB    . LEU B 1 456 ? 12.940  -3.763  77.770  1.00 55.92  ? 456 LEU B CB    1 
ATOM   7617  C CG    . LEU B 1 456 ? 13.645  -3.820  79.118  1.00 50.30  ? 456 LEU B CG    1 
ATOM   7618  C CD1   . LEU B 1 456 ? 15.147  -3.660  78.937  1.00 44.20  ? 456 LEU B CD1   1 
ATOM   7619  C CD2   . LEU B 1 456 ? 13.094  -2.743  80.037  1.00 55.38  ? 456 LEU B CD2   1 
ATOM   7620  N N     . VAL B 1 457 ? 10.895  -4.687  75.577  1.00 51.21  ? 457 VAL B N     1 
ATOM   7621  C CA    . VAL B 1 457 ? 10.415  -4.588  74.214  1.00 61.93  ? 457 VAL B CA    1 
ATOM   7622  C C     . VAL B 1 457 ? 8.905   -4.361  74.245  1.00 58.74  ? 457 VAL B C     1 
ATOM   7623  O O     . VAL B 1 457 ? 8.429   -3.310  73.818  1.00 63.32  ? 457 VAL B O     1 
ATOM   7624  C CB    . VAL B 1 457 ? 10.792  -5.846  73.404  1.00 65.62  ? 457 VAL B CB    1 
ATOM   7625  C CG1   . VAL B 1 457 ? 10.079  -5.872  72.051  1.00 66.28  ? 457 VAL B CG1   1 
ATOM   7626  C CG2   . VAL B 1 457 ? 12.305  -6.003  73.245  1.00 53.82  ? 457 VAL B CG2   1 
ATOM   7627  N N     . ASP B 1 458 ? 8.182   -5.336  74.815  1.00 57.74  ? 458 ASP B N     1 
ATOM   7628  C CA    . ASP B 1 458 ? 6.729   -5.305  74.949  1.00 56.81  ? 458 ASP B CA    1 
ATOM   7629  C C     . ASP B 1 458 ? 6.236   -3.961  75.480  1.00 56.44  ? 458 ASP B C     1 
ATOM   7630  O O     . ASP B 1 458 ? 5.359   -3.338  74.873  1.00 68.35  ? 458 ASP B O     1 
ATOM   7631  C CB    . ASP B 1 458 ? 6.237   -6.481  75.791  1.00 59.96  ? 458 ASP B CB    1 
ATOM   7632  C CG    . ASP B 1 458 ? 6.506   -7.854  75.161  1.00 75.49  ? 458 ASP B CG    1 
ATOM   7633  O OD1   . ASP B 1 458 ? 7.276   -7.932  74.159  1.00 76.80  ? 458 ASP B OD1   1 
ATOM   7634  O OD2   . ASP B 1 458 ? 5.959   -8.860  75.667  1.00 73.94  ? 458 ASP B OD2   1 
ATOM   7635  N N     . GLU B 1 459 ? 6.842   -3.489  76.572  1.00 52.16  ? 459 GLU B N     1 
ATOM   7636  C CA    . GLU B 1 459 ? 6.377   -2.288  77.252  1.00 51.98  ? 459 GLU B CA    1 
ATOM   7637  C C     . GLU B 1 459 ? 6.694   -1.033  76.451  1.00 48.45  ? 459 GLU B C     1 
ATOM   7638  O O     . GLU B 1 459 ? 5.874   -0.125  76.435  1.00 54.90  ? 459 GLU B O     1 
ATOM   7639  C CB    . GLU B 1 459 ? 6.974   -2.142  78.660  1.00 49.04  ? 459 GLU B CB    1 
ATOM   7640  C CG    . GLU B 1 459 ? 6.688   -3.348  79.552  1.00 53.22  ? 459 GLU B CG    1 
ATOM   7641  C CD    . GLU B 1 459 ? 6.946   -3.149  81.039  1.00 54.56  ? 459 GLU B CD    1 
ATOM   7642  O OE1   . GLU B 1 459 ? 7.385   -2.048  81.429  1.00 49.92  ? 459 GLU B OE1   1 
ATOM   7643  O OE2   . GLU B 1 459 ? 6.737   -4.108  81.793  1.00 56.46  ? 459 GLU B OE2   1 
ATOM   7644  N N     . ALA B 1 460 ? 7.886   -0.941  75.848  1.00 45.88  ? 460 ALA B N     1 
ATOM   7645  C CA    . ALA B 1 460 ? 8.172   0.187   74.971  1.00 47.48  ? 460 ALA B CA    1 
ATOM   7646  C C     . ALA B 1 460 ? 7.219   0.159   73.753  1.00 41.62  ? 460 ALA B C     1 
ATOM   7647  O O     . ALA B 1 460 ? 6.673   1.200   73.372  1.00 34.79  ? 460 ALA B O     1 
ATOM   7648  C CB    . ALA B 1 460 ? 9.639   0.191   74.581  1.00 44.89  ? 460 ALA B CB    1 
ATOM   7649  N N     . ALA B 1 461 ? 6.954   -1.038  73.206  1.00 37.41  ? 461 ALA B N     1 
ATOM   7650  C CA    . ALA B 1 461 ? 6.147   -1.180  71.995  1.00 55.70  ? 461 ALA B CA    1 
ATOM   7651  C C     . ALA B 1 461 ? 4.688   -0.775  72.273  1.00 58.70  ? 461 ALA B C     1 
ATOM   7652  O O     . ALA B 1 461 ? 4.024   -0.096  71.457  1.00 44.16  ? 461 ALA B O     1 
ATOM   7653  C CB    . ALA B 1 461 ? 6.250   -2.595  71.440  1.00 47.11  ? 461 ALA B CB    1 
ATOM   7654  N N     . ALA B 1 462 ? 4.222   -1.149  73.471  1.00 49.99  ? 462 ALA B N     1 
ATOM   7655  C CA    . ALA B 1 462 ? 2.850   -0.886  73.841  1.00 46.97  ? 462 ALA B CA    1 
ATOM   7656  C C     . ALA B 1 462 ? 2.621   0.622   73.981  1.00 46.57  ? 462 ALA B C     1 
ATOM   7657  O O     . ALA B 1 462 ? 1.489   1.062   73.811  1.00 44.05  ? 462 ALA B O     1 
ATOM   7658  C CB    . ALA B 1 462 ? 2.530   -1.680  75.072  1.00 52.79  ? 462 ALA B CB    1 
ATOM   7659  N N     . GLU B 1 463 ? 3.695   1.426   74.156  1.00 48.58  ? 463 GLU B N     1 
ATOM   7660  C CA    . GLU B 1 463 ? 3.591   2.892   74.159  1.00 47.35  ? 463 GLU B CA    1 
ATOM   7661  C C     . GLU B 1 463 ? 3.998   3.495   72.811  1.00 38.53  ? 463 GLU B C     1 
ATOM   7662  O O     . GLU B 1 463 ? 4.080   4.714   72.658  1.00 33.64  ? 463 GLU B O     1 
ATOM   7663  C CB    . GLU B 1 463 ? 4.512   3.515   75.204  1.00 47.64  ? 463 GLU B CB    1 
ATOM   7664  C CG    . GLU B 1 463 ? 4.384   2.887   76.579  1.00 53.05  ? 463 GLU B CG    1 
ATOM   7665  C CD    . GLU B 1 463 ? 3.021   3.061   77.229  1.00 46.71  ? 463 GLU B CD    1 
ATOM   7666  O OE1   . GLU B 1 463 ? 2.492   4.189   77.157  1.00 36.50  ? 463 GLU B OE1   1 
ATOM   7667  O OE2   . GLU B 1 463 ? 2.536   2.086   77.841  1.00 44.48  ? 463 GLU B OE2   1 
ATOM   7668  N N     . GLY B 1 464 ? 4.277   2.641   71.827  1.00 39.24  ? 464 GLY B N     1 
ATOM   7669  C CA    . GLY B 1 464 ? 4.499   3.132   70.468  1.00 49.71  ? 464 GLY B CA    1 
ATOM   7670  C C     . GLY B 1 464 ? 5.950   3.531   70.188  1.00 51.47  ? 464 GLY B C     1 
ATOM   7671  O O     . GLY B 1 464 ? 6.213   4.359   69.295  1.00 50.55  ? 464 GLY B O     1 
ATOM   7672  N N     . TYR B 1 465 ? 6.872   2.937   70.975  1.00 50.16  ? 465 TYR B N     1 
ATOM   7673  C CA    . TYR B 1 465 ? 8.308   3.093   70.775  1.00 50.72  ? 465 TYR B CA    1 
ATOM   7674  C C     . TYR B 1 465 ? 8.873   1.768   70.281  1.00 43.68  ? 465 TYR B C     1 
ATOM   7675  O O     . TYR B 1 465 ? 8.797   0.769   71.010  1.00 41.93  ? 465 TYR B O     1 
ATOM   7676  C CB    . TYR B 1 465 ? 9.034   3.465   72.062  1.00 51.55  ? 465 TYR B CB    1 
ATOM   7677  C CG    . TYR B 1 465 ? 8.395   4.535   72.902  1.00 55.47  ? 465 TYR B CG    1 
ATOM   7678  C CD1   . TYR B 1 465 ? 7.900   5.703   72.342  1.00 48.50  ? 465 TYR B CD1   1 
ATOM   7679  C CD2   . TYR B 1 465 ? 8.349   4.385   74.286  1.00 57.89  ? 465 TYR B CD2   1 
ATOM   7680  C CE1   . TYR B 1 465 ? 7.359   6.695   73.150  1.00 52.60  ? 465 TYR B CE1   1 
ATOM   7681  C CE2   . TYR B 1 465 ? 7.802   5.357   75.103  1.00 49.83  ? 465 TYR B CE2   1 
ATOM   7682  C CZ    . TYR B 1 465 ? 7.316   6.517   74.527  1.00 51.63  ? 465 TYR B CZ    1 
ATOM   7683  O OH    . TYR B 1 465 ? 6.815   7.462   75.364  1.00 60.55  ? 465 TYR B OH    1 
ATOM   7684  N N     . GLY B 1 466 ? 9.375   1.774   69.031  1.00 36.60  ? 466 GLY B N     1 
ATOM   7685  C CA    . GLY B 1 466 ? 9.848   0.548   68.397  1.00 38.70  ? 466 GLY B CA    1 
ATOM   7686  C C     . GLY B 1 466 ? 11.352  0.609   68.167  1.00 39.61  ? 466 GLY B C     1 
ATOM   7687  O O     . GLY B 1 466 ? 11.914  1.704   68.009  1.00 38.83  ? 466 GLY B O     1 
ATOM   7688  N N     . GLU B 1 467 ? 11.988  -0.564  68.160  1.00 40.82  ? 467 GLU B N     1 
ATOM   7689  C CA    . GLU B 1 467 ? 13.442  -0.659  68.012  1.00 45.91  ? 467 GLU B CA    1 
ATOM   7690  C C     . GLU B 1 467 ? 13.841  -0.498  66.535  1.00 49.52  ? 467 GLU B C     1 
ATOM   7691  O O     . GLU B 1 467 ? 13.111  -0.896  65.630  1.00 47.47  ? 467 GLU B O     1 
ATOM   7692  C CB    . GLU B 1 467 ? 13.878  -1.992  68.632  1.00 51.40  ? 467 GLU B CB    1 
ATOM   7693  C CG    . GLU B 1 467 ? 15.365  -2.328  68.548  1.00 54.43  ? 467 GLU B CG    1 
ATOM   7694  C CD    . GLU B 1 467 ? 16.316  -1.459  69.344  1.00 57.71  ? 467 GLU B CD    1 
ATOM   7695  O OE1   . GLU B 1 467 ? 16.803  -1.941  70.416  1.00 56.01  ? 467 GLU B OE1   1 
ATOM   7696  O OE2   . GLU B 1 467 ? 16.595  -0.322  68.880  1.00 59.70  ? 467 GLU B OE2   1 
ATOM   7697  N N     . TYR B 1 468 ? 15.032  0.068   66.297  1.00 54.37  ? 468 TYR B N     1 
ATOM   7698  C CA    . TYR B 1 468 ? 15.571  0.247   64.955  1.00 51.92  ? 468 TYR B CA    1 
ATOM   7699  C C     . TYR B 1 468 ? 16.741  -0.683  64.646  1.00 52.33  ? 468 TYR B C     1 
ATOM   7700  O O     . TYR B 1 468 ? 17.113  -0.777  63.478  1.00 68.06  ? 468 TYR B O     1 
ATOM   7701  C CB    . TYR B 1 468 ? 16.032  1.690   64.727  1.00 49.65  ? 468 TYR B CB    1 
ATOM   7702  C CG    . TYR B 1 468 ? 17.418  2.048   65.199  1.00 54.63  ? 468 TYR B CG    1 
ATOM   7703  C CD1   . TYR B 1 468 ? 17.688  2.354   66.521  1.00 60.60  ? 468 TYR B CD1   1 
ATOM   7704  C CD2   . TYR B 1 468 ? 18.466  2.148   64.302  1.00 64.94  ? 468 TYR B CD2   1 
ATOM   7705  C CE1   . TYR B 1 468 ? 18.955  2.729   66.940  1.00 61.04  ? 468 TYR B CE1   1 
ATOM   7706  C CE2   . TYR B 1 468 ? 19.742  2.498   64.708  1.00 68.42  ? 468 TYR B CE2   1 
ATOM   7707  C CZ    . TYR B 1 468 ? 19.992  2.790   66.034  1.00 64.57  ? 468 TYR B CZ    1 
ATOM   7708  O OH    . TYR B 1 468 ? 21.264  3.141   66.399  1.00 73.85  ? 468 TYR B OH    1 
ATOM   7709  N N     . ARG B 1 469 ? 17.323  -1.334  65.668  1.00 62.87  ? 469 ARG B N     1 
ATOM   7710  C CA    . ARG B 1 469 ? 18.486  -2.208  65.526  1.00 59.71  ? 469 ARG B CA    1 
ATOM   7711  C C     . ARG B 1 469 ? 18.561  -3.187  66.697  1.00 64.42  ? 469 ARG B C     1 
ATOM   7712  O O     . ARG B 1 469 ? 18.405  -2.782  67.849  1.00 70.52  ? 469 ARG B O     1 
ATOM   7713  C CB    . ARG B 1 469 ? 19.758  -1.360  65.513  1.00 55.17  ? 469 ARG B CB    1 
ATOM   7714  C CG    . ARG B 1 469 ? 20.980  -2.124  65.036  1.00 57.67  ? 469 ARG B CG    1 
ATOM   7715  C CD    . ARG B 1 469 ? 22.218  -1.253  64.979  1.00 56.78  ? 469 ARG B CD    1 
ATOM   7716  N NE    . ARG B 1 469 ? 23.386  -2.068  64.698  1.00 51.49  ? 469 ARG B NE    1 
ATOM   7717  C CZ    . ARG B 1 469 ? 24.629  -1.621  64.787  1.00 55.75  ? 469 ARG B CZ    1 
ATOM   7718  N NH1   . ARG B 1 469 ? 24.846  -0.367  65.167  1.00 51.92  ? 469 ARG B NH1   1 
ATOM   7719  N NH2   . ARG B 1 469 ? 25.638  -2.432  64.497  1.00 52.70  ? 469 ARG B NH2   1 
ATOM   7720  N N     . THR B 1 470 ? 18.830  -4.473  66.432  1.00 62.80  ? 470 THR B N     1 
ATOM   7721  C CA    . THR B 1 470 ? 18.715  -5.456  67.509  1.00 63.25  ? 470 THR B CA    1 
ATOM   7722  C C     . THR B 1 470 ? 19.569  -6.710  67.302  1.00 54.15  ? 470 THR B C     1 
ATOM   7723  O O     . THR B 1 470 ? 20.055  -7.004  66.223  1.00 55.68  ? 470 THR B O     1 
ATOM   7724  C CB    . THR B 1 470 ? 17.262  -5.906  67.720  1.00 63.06  ? 470 THR B CB    1 
ATOM   7725  O OG1   . THR B 1 470 ? 17.180  -6.550  68.993  1.00 54.55  ? 470 THR B OG1   1 
ATOM   7726  C CG2   . THR B 1 470 ? 16.776  -6.835  66.626  1.00 59.87  ? 470 THR B CG2   1 
ATOM   7727  N N     . HIS B 1 471 ? 19.727  -7.443  68.402  1.00 56.50  ? 471 HIS B N     1 
ATOM   7728  C CA    . HIS B 1 471 ? 20.538  -8.646  68.488  1.00 55.27  ? 471 HIS B CA    1 
ATOM   7729  C C     . HIS B 1 471 ? 19.922  -9.719  67.600  1.00 47.08  ? 471 HIS B C     1 
ATOM   7730  O O     . HIS B 1 471 ? 18.711  -9.779  67.442  1.00 52.87  ? 471 HIS B O     1 
ATOM   7731  C CB    . HIS B 1 471 ? 20.666  -9.047  69.973  1.00 51.19  ? 471 HIS B CB    1 
ATOM   7732  C CG    . HIS B 1 471 ? 21.589  -10.186 70.243  1.00 51.72  ? 471 HIS B CG    1 
ATOM   7733  N ND1   . HIS B 1 471 ? 21.318  -11.489 69.876  1.00 50.89  ? 471 HIS B ND1   1 
ATOM   7734  C CD2   . HIS B 1 471 ? 22.787  -10.219 70.856  1.00 56.27  ? 471 HIS B CD2   1 
ATOM   7735  C CE1   . HIS B 1 471 ? 22.313  -12.278 70.257  1.00 53.83  ? 471 HIS B CE1   1 
ATOM   7736  N NE2   . HIS B 1 471 ? 23.224  -11.527 70.853  1.00 58.78  ? 471 HIS B NE2   1 
ATOM   7737  N N     . ILE B 1 472 ? 20.756  -10.596 67.042  1.00 49.97  ? 472 ILE B N     1 
ATOM   7738  C CA    . ILE B 1 472 ? 20.235  -11.665 66.200  1.00 55.46  ? 472 ILE B CA    1 
ATOM   7739  C C     . ILE B 1 472 ? 19.111  -12.409 66.906  1.00 52.65  ? 472 ILE B C     1 
ATOM   7740  O O     . ILE B 1 472 ? 18.224  -12.932 66.239  1.00 65.75  ? 472 ILE B O     1 
ATOM   7741  C CB    . ILE B 1 472 ? 21.309  -12.671 65.748  1.00 54.54  ? 472 ILE B CB    1 
ATOM   7742  C CG1   . ILE B 1 472 ? 22.152  -13.167 66.929  1.00 56.11  ? 472 ILE B CG1   1 
ATOM   7743  C CG2   . ILE B 1 472 ? 22.151  -12.084 64.635  1.00 53.53  ? 472 ILE B CG2   1 
ATOM   7744  C CD1   . ILE B 1 472 ? 23.186  -14.206 66.556  1.00 55.10  ? 472 ILE B CD1   1 
ATOM   7745  N N     . ARG B 1 473 ? 19.183  -12.496 68.238  1.00 54.62  ? 473 ARG B N     1 
ATOM   7746  C CA    . ARG B 1 473 ? 18.295  -13.362 68.996  1.00 53.73  ? 473 ARG B CA    1 
ATOM   7747  C C     . ARG B 1 473 ? 16.869  -12.820 68.963  1.00 51.22  ? 473 ARG B C     1 
ATOM   7748  O O     . ARG B 1 473 ? 15.932  -13.606 69.010  1.00 41.13  ? 473 ARG B O     1 
ATOM   7749  C CB    . ARG B 1 473 ? 18.783  -13.515 70.439  1.00 61.81  ? 473 ARG B CB    1 
ATOM   7750  C CG    . ARG B 1 473 ? 17.832  -14.283 71.352  1.00 73.47  ? 473 ARG B CG    1 
ATOM   7751  C CD    . ARG B 1 473 ? 18.321  -14.403 72.792  1.00 86.08  ? 473 ARG B CD    1 
ATOM   7752  N NE    . ARG B 1 473 ? 17.307  -14.933 73.703  1.00 95.63  ? 473 ARG B NE    1 
ATOM   7753  C CZ    . ARG B 1 473 ? 16.839  -16.183 73.698  1.00 97.36  ? 473 ARG B CZ    1 
ATOM   7754  N NH1   . ARG B 1 473 ? 17.391  -17.121 72.948  1.00 101.61 ? 473 ARG B NH1   1 
ATOM   7755  N NH2   . ARG B 1 473 ? 15.819  -16.498 74.474  1.00 87.57  ? 473 ARG B NH2   1 
ATOM   7756  N N     . TYR B 1 474 ? 16.704  -11.488 68.875  1.00 51.94  ? 474 TYR B N     1 
ATOM   7757  C CA    . TYR B 1 474 ? 15.399  -10.884 69.078  1.00 52.85  ? 474 TYR B CA    1 
ATOM   7758  C C     . TYR B 1 474 ? 14.810  -10.370 67.771  1.00 53.67  ? 474 TYR B C     1 
ATOM   7759  O O     . TYR B 1 474 ? 13.814  -9.661  67.792  1.00 52.69  ? 474 TYR B O     1 
ATOM   7760  C CB    . TYR B 1 474 ? 15.505  -9.761  70.113  1.00 61.11  ? 474 TYR B CB    1 
ATOM   7761  C CG    . TYR B 1 474 ? 15.956  -10.236 71.469  1.00 61.20  ? 474 TYR B CG    1 
ATOM   7762  C CD1   . TYR B 1 474 ? 15.126  -11.025 72.245  1.00 63.73  ? 474 TYR B CD1   1 
ATOM   7763  C CD2   . TYR B 1 474 ? 17.231  -9.961  71.940  1.00 60.59  ? 474 TYR B CD2   1 
ATOM   7764  C CE1   . TYR B 1 474 ? 15.539  -11.495 73.480  1.00 70.21  ? 474 TYR B CE1   1 
ATOM   7765  C CE2   . TYR B 1 474 ? 17.663  -10.428 73.169  1.00 62.68  ? 474 TYR B CE2   1 
ATOM   7766  C CZ    . TYR B 1 474 ? 16.812  -11.199 73.942  1.00 70.75  ? 474 TYR B CZ    1 
ATOM   7767  O OH    . TYR B 1 474 ? 17.218  -11.682 75.165  1.00 78.09  ? 474 TYR B OH    1 
ATOM   7768  N N     . MET B 1 475 ? 15.415  -10.711 66.631  1.00 56.12  ? 475 MET B N     1 
ATOM   7769  C CA    . MET B 1 475 ? 15.025  -10.077 65.377  1.00 54.66  ? 475 MET B CA    1 
ATOM   7770  C C     . MET B 1 475 ? 13.551  -10.319 65.081  1.00 53.61  ? 475 MET B C     1 
ATOM   7771  O O     . MET B 1 475 ? 12.871  -9.395  64.642  1.00 65.04  ? 475 MET B O     1 
ATOM   7772  C CB    . MET B 1 475 ? 15.879  -10.548 64.197  1.00 49.56  ? 475 MET B CB    1 
ATOM   7773  C CG    . MET B 1 475 ? 17.221  -9.861  64.230  1.00 51.62  ? 475 MET B CG    1 
ATOM   7774  S SD    . MET B 1 475 ? 18.443  -10.406 63.037  1.00 44.75  ? 475 MET B SD    1 
ATOM   7775  C CE    . MET B 1 475 ? 19.712  -9.199  63.436  1.00 50.21  ? 475 MET B CE    1 
ATOM   7776  N N     . ASP B 1 476 ? 13.067  -11.539 65.336  1.00 52.46  ? 476 ASP B N     1 
ATOM   7777  C CA    . ASP B 1 476 ? 11.690  -11.902 65.028  1.00 56.74  ? 476 ASP B CA    1 
ATOM   7778  C C     . ASP B 1 476 ? 10.736  -11.076 65.882  1.00 61.50  ? 476 ASP B C     1 
ATOM   7779  O O     . ASP B 1 476 ? 9.695   -10.638 65.389  1.00 67.02  ? 476 ASP B O     1 
ATOM   7780  C CB    . ASP B 1 476 ? 11.422  -13.395 65.237  1.00 57.68  ? 476 ASP B CB    1 
ATOM   7781  C CG    . ASP B 1 476 ? 11.663  -14.294 64.029  1.00 66.68  ? 476 ASP B CG    1 
ATOM   7782  O OD1   . ASP B 1 476 ? 11.630  -13.805 62.883  1.00 64.57  ? 476 ASP B OD1   1 
ATOM   7783  O OD2   . ASP B 1 476 ? 11.892  -15.493 64.236  1.00 78.94  ? 476 ASP B OD2   1 
ATOM   7784  N N     . ARG B 1 477 ? 11.126  -10.857 67.147  1.00 63.40  ? 477 ARG B N     1 
ATOM   7785  C CA    . ARG B 1 477 ? 10.276  -10.223 68.142  1.00 63.91  ? 477 ARG B CA    1 
ATOM   7786  C C     . ARG B 1 477 ? 10.117  -8.731  67.830  1.00 60.38  ? 477 ARG B C     1 
ATOM   7787  O O     . ARG B 1 477 ? 9.014   -8.183  67.906  1.00 62.14  ? 477 ARG B O     1 
ATOM   7788  C CB    . ARG B 1 477 ? 10.843  -10.477 69.546  1.00 66.57  ? 477 ARG B CB    1 
ATOM   7789  C CG    . ARG B 1 477 ? 9.803   -10.388 70.655  1.00 72.15  ? 477 ARG B CG    1 
ATOM   7790  C CD    . ARG B 1 477 ? 10.388  -9.841  71.943  1.00 82.20  ? 477 ARG B CD    1 
ATOM   7791  N NE    . ARG B 1 477 ? 9.420   -9.752  73.029  1.00 83.95  ? 477 ARG B NE    1 
ATOM   7792  C CZ    . ARG B 1 477 ? 8.914   -10.795 73.685  1.00 85.44  ? 477 ARG B CZ    1 
ATOM   7793  N NH1   . ARG B 1 477 ? 9.275   -12.030 73.366  1.00 71.51  ? 477 ARG B NH1   1 
ATOM   7794  N NH2   . ARG B 1 477 ? 8.051   -10.589 74.669  1.00 81.83  ? 477 ARG B NH2   1 
ATOM   7795  N N     . ILE B 1 478 ? 11.218  -8.080  67.434  1.00 57.61  ? 478 ILE B N     1 
ATOM   7796  C CA    . ILE B 1 478 ? 11.197  -6.674  67.056  1.00 50.50  ? 478 ILE B CA    1 
ATOM   7797  C C     . ILE B 1 478 ? 10.351  -6.522  65.786  1.00 53.22  ? 478 ILE B C     1 
ATOM   7798  O O     . ILE B 1 478 ? 9.618   -5.549  65.619  1.00 54.40  ? 478 ILE B O     1 
ATOM   7799  C CB    . ILE B 1 478 ? 12.635  -6.171  66.848  1.00 45.73  ? 478 ILE B CB    1 
ATOM   7800  C CG1   . ILE B 1 478 ? 13.520  -6.395  68.079  1.00 52.36  ? 478 ILE B CG1   1 
ATOM   7801  C CG2   . ILE B 1 478 ? 12.630  -4.718  66.425  1.00 48.89  ? 478 ILE B CG2   1 
ATOM   7802  C CD1   . ILE B 1 478 ? 13.104  -5.615  69.308  1.00 58.26  ? 478 ILE B CD1   1 
ATOM   7803  N N     . ALA B 1 479 ? 10.437  -7.519  64.904  1.00 44.38  ? 479 ALA B N     1 
ATOM   7804  C CA    . ALA B 1 479 ? 9.733   -7.460  63.639  1.00 60.12  ? 479 ALA B CA    1 
ATOM   7805  C C     . ALA B 1 479 ? 8.243   -7.543  63.915  1.00 57.86  ? 479 ALA B C     1 
ATOM   7806  O O     . ALA B 1 479 ? 7.454   -6.834  63.300  1.00 61.75  ? 479 ALA B O     1 
ATOM   7807  C CB    . ALA B 1 479 ? 10.177  -8.557  62.696  1.00 58.67  ? 479 ALA B CB    1 
ATOM   7808  N N     . LYS B 1 480 ? 7.879   -8.388  64.870  1.00 61.29  ? 480 LYS B N     1 
ATOM   7809  C CA    . LYS B 1 480 ? 6.472   -8.588  65.166  1.00 62.84  ? 480 LYS B CA    1 
ATOM   7810  C C     . LYS B 1 480 ? 5.847   -7.387  65.871  1.00 57.20  ? 480 LYS B C     1 
ATOM   7811  O O     . LYS B 1 480 ? 4.633   -7.358  65.980  1.00 59.86  ? 480 LYS B O     1 
ATOM   7812  C CB    . LYS B 1 480 ? 6.279   -9.897  65.934  1.00 64.18  ? 480 LYS B CB    1 
ATOM   7813  C CG    . LYS B 1 480 ? 6.177   -11.108 65.016  1.00 64.10  ? 480 LYS B CG    1 
ATOM   7814  C CD    . LYS B 1 480 ? 6.588   -12.386 65.677  1.00 77.37  ? 480 LYS B CD    1 
ATOM   7815  C CE    . LYS B 1 480 ? 6.597   -13.556 64.719  1.00 84.86  ? 480 LYS B CE    1 
ATOM   7816  N NZ    . LYS B 1 480 ? 7.267   -14.728 65.326  1.00 86.84  ? 480 LYS B NZ    1 
ATOM   7817  N N     . THR B 1 481 ? 6.626   -6.379  66.298  1.00 62.73  ? 481 THR B N     1 
ATOM   7818  C CA    . THR B 1 481 ? 6.031   -5.186  66.890  1.00 54.57  ? 481 THR B CA    1 
ATOM   7819  C C     . THR B 1 481 ? 5.556   -4.233  65.798  1.00 54.95  ? 481 THR B C     1 
ATOM   7820  O O     . THR B 1 481 ? 4.860   -3.261  66.099  1.00 67.55  ? 481 THR B O     1 
ATOM   7821  C CB    . THR B 1 481 ? 7.009   -4.477  67.846  1.00 55.30  ? 481 THR B CB    1 
ATOM   7822  O OG1   . THR B 1 481 ? 8.147   -3.938  67.161  1.00 51.64  ? 481 THR B OG1   1 
ATOM   7823  C CG2   . THR B 1 481 ? 7.487   -5.400  68.942  1.00 51.74  ? 481 THR B CG2   1 
ATOM   7824  N N     . TYR B 1 482 ? 6.017   -4.466  64.560  1.00 53.55  ? 482 TYR B N     1 
ATOM   7825  C CA    . TYR B 1 482 ? 5.788   -3.570  63.427  1.00 54.33  ? 482 TYR B CA    1 
ATOM   7826  C C     . TYR B 1 482 ? 4.639   -4.154  62.596  1.00 56.10  ? 482 TYR B C     1 
ATOM   7827  O O     . TYR B 1 482 ? 4.820   -4.629  61.479  1.00 70.80  ? 482 TYR B O     1 
ATOM   7828  C CB    . TYR B 1 482 ? 7.086   -3.347  62.637  1.00 43.77  ? 482 TYR B CB    1 
ATOM   7829  C CG    . TYR B 1 482 ? 8.083   -2.422  63.289  1.00 38.99  ? 482 TYR B CG    1 
ATOM   7830  C CD1   . TYR B 1 482 ? 7.915   -1.042  63.271  1.00 37.93  ? 482 TYR B CD1   1 
ATOM   7831  C CD2   . TYR B 1 482 ? 9.220   -2.928  63.909  1.00 36.05  ? 482 TYR B CD2   1 
ATOM   7832  C CE1   . TYR B 1 482 ? 8.852   -0.200  63.856  1.00 41.33  ? 482 TYR B CE1   1 
ATOM   7833  C CE2   . TYR B 1 482 ? 10.124  -2.102  64.556  1.00 36.17  ? 482 TYR B CE2   1 
ATOM   7834  C CZ    . TYR B 1 482 ? 9.957   -0.728  64.512  1.00 43.06  ? 482 TYR B CZ    1 
ATOM   7835  O OH    . TYR B 1 482 ? 10.885  0.072   65.158  1.00 42.06  ? 482 TYR B OH    1 
ATOM   7836  N N     . SER B 1 483 ? 3.438   -4.094  63.180  1.00 58.31  ? 483 SER B N     1 
ATOM   7837  C CA    . SER B 1 483 ? 2.379   -5.056  62.925  1.00 57.24  ? 483 SER B CA    1 
ATOM   7838  C C     . SER B 1 483 ? 1.121   -4.407  62.350  1.00 49.66  ? 483 SER B C     1 
ATOM   7839  O O     . SER B 1 483 ? 0.219   -5.146  62.018  1.00 49.11  ? 483 SER B O     1 
ATOM   7840  C CB    . SER B 1 483 ? 2.039   -5.794  64.200  1.00 55.09  ? 483 SER B CB    1 
ATOM   7841  O OG    . SER B 1 483 ? 1.699   -4.860  65.220  1.00 52.11  ? 483 SER B OG    1 
ATOM   7842  N N     . TRP B 1 484 ? 1.082   -3.075  62.179  1.00 43.57  ? 484 TRP B N     1 
ATOM   7843  C CA    . TRP B 1 484 ? -0.039  -2.393  61.554  1.00 47.32  ? 484 TRP B CA    1 
ATOM   7844  C C     . TRP B 1 484 ? -0.567  -3.140  60.327  1.00 53.68  ? 484 TRP B C     1 
ATOM   7845  O O     . TRP B 1 484 ? 0.185   -3.433  59.391  1.00 49.95  ? 484 TRP B O     1 
ATOM   7846  C CB    . TRP B 1 484 ? 0.352   -0.962  61.194  1.00 53.32  ? 484 TRP B CB    1 
ATOM   7847  C CG    . TRP B 1 484 ? -0.789  -0.128  60.712  1.00 61.11  ? 484 TRP B CG    1 
ATOM   7848  C CD1   . TRP B 1 484 ? -1.678  0.578   61.467  1.00 65.82  ? 484 TRP B CD1   1 
ATOM   7849  C CD2   . TRP B 1 484 ? -1.160  0.087   59.343  1.00 62.45  ? 484 TRP B CD2   1 
ATOM   7850  N NE1   . TRP B 1 484 ? -2.555  1.245   60.655  1.00 68.87  ? 484 TRP B NE1   1 
ATOM   7851  C CE2   . TRP B 1 484 ? -2.279  0.941   59.348  1.00 65.35  ? 484 TRP B CE2   1 
ATOM   7852  C CE3   . TRP B 1 484 ? -0.645  -0.346  58.119  1.00 61.84  ? 484 TRP B CE3   1 
ATOM   7853  C CZ2   . TRP B 1 484 ? -2.905  1.347   58.170  1.00 63.23  ? 484 TRP B CZ2   1 
ATOM   7854  C CZ3   . TRP B 1 484 ? -1.257  0.059   56.955  1.00 56.96  ? 484 TRP B CZ3   1 
ATOM   7855  C CH2   . TRP B 1 484 ? -2.371  0.893   56.986  1.00 61.95  ? 484 TRP B CH2   1 
ATOM   7856  N N     . ASN B 1 485 ? -1.884  -3.437  60.359  1.00 50.94  ? 485 ASN B N     1 
ATOM   7857  C CA    . ASN B 1 485 ? -2.629  -4.030  59.255  1.00 44.83  ? 485 ASN B CA    1 
ATOM   7858  C C     . ASN B 1 485 ? -2.186  -5.472  59.079  1.00 48.68  ? 485 ASN B C     1 
ATOM   7859  O O     . ASN B 1 485 ? -1.929  -5.945  57.977  1.00 58.07  ? 485 ASN B O     1 
ATOM   7860  C CB    . ASN B 1 485 ? -2.522  -3.215  57.967  1.00 48.23  ? 485 ASN B CB    1 
ATOM   7861  C CG    . ASN B 1 485 ? -3.435  -3.689  56.859  1.00 51.06  ? 485 ASN B CG    1 
ATOM   7862  O OD1   . ASN B 1 485 ? -4.561  -4.101  57.092  1.00 55.54  ? 485 ASN B OD1   1 
ATOM   7863  N ND2   . ASN B 1 485 ? -2.945  -3.671  55.640  1.00 55.64  ? 485 ASN B ND2   1 
ATOM   7864  N N     . ASP B 1 486 ? -2.139  -6.168  60.207  1.00 53.43  ? 486 ASP B N     1 
ATOM   7865  C CA    . ASP B 1 486 ? -1.801  -7.576  60.243  1.00 55.63  ? 486 ASP B CA    1 
ATOM   7866  C C     . ASP B 1 486 ? -0.451  -7.807  59.565  1.00 61.59  ? 486 ASP B C     1 
ATOM   7867  O O     . ASP B 1 486 ? -0.295  -8.749  58.790  1.00 67.32  ? 486 ASP B O     1 
ATOM   7868  C CB    . ASP B 1 486 ? -2.902  -8.435  59.619  1.00 52.38  ? 486 ASP B CB    1 
ATOM   7869  C CG    . ASP B 1 486 ? -2.821  -9.858  60.131  1.00 58.86  ? 486 ASP B CG    1 
ATOM   7870  O OD1   . ASP B 1 486 ? -2.545  -10.003 61.330  1.00 67.61  ? 486 ASP B OD1   1 
ATOM   7871  O OD2   . ASP B 1 486 ? -3.024  -10.800 59.349  1.00 57.91  ? 486 ASP B OD2   1 
ATOM   7872  N N     . ASN B 1 487 ? 0.539   -6.981  59.912  1.00 59.27  ? 487 ASN B N     1 
ATOM   7873  C CA    . ASN B 1 487 ? 1.919   -7.234  59.513  1.00 72.12  ? 487 ASN B CA    1 
ATOM   7874  C C     . ASN B 1 487 ? 2.038   -7.094  58.003  1.00 63.79  ? 487 ASN B C     1 
ATOM   7875  O O     . ASN B 1 487 ? 2.680   -7.927  57.360  1.00 50.70  ? 487 ASN B O     1 
ATOM   7876  C CB    . ASN B 1 487 ? 2.449   -8.634  59.865  1.00 62.35  ? 487 ASN B CB    1 
ATOM   7877  C CG    . ASN B 1 487 ? 2.423   -8.950  61.342  1.00 58.23  ? 487 ASN B CG    1 
ATOM   7878  O OD1   . ASN B 1 487 ? 2.927   -8.198  62.178  1.00 63.09  ? 487 ASN B OD1   1 
ATOM   7879  N ND2   . ASN B 1 487 ? 1.865   -10.094 61.664  1.00 59.98  ? 487 ASN B ND2   1 
ATOM   7880  N N     . ALA B 1 488 ? 1.346   -6.082  57.468  1.00 59.28  ? 488 ALA B N     1 
ATOM   7881  C CA    . ALA B 1 488 ? 1.377   -5.790  56.049  1.00 57.41  ? 488 ALA B CA    1 
ATOM   7882  C C     . ALA B 1 488 ? 2.834   -5.573  55.602  1.00 63.98  ? 488 ALA B C     1 
ATOM   7883  O O     . ALA B 1 488 ? 3.276   -6.117  54.580  1.00 55.93  ? 488 ALA B O     1 
ATOM   7884  C CB    . ALA B 1 488 ? 0.500   -4.595  55.790  1.00 54.34  ? 488 ALA B CB    1 
ATOM   7885  N N     . LEU B 1 489 ? 3.607   -4.819  56.394  1.00 52.22  ? 489 LEU B N     1 
ATOM   7886  C CA    . LEU B 1 489 ? 4.913   -4.440  55.912  1.00 51.68  ? 489 LEU B CA    1 
ATOM   7887  C C     . LEU B 1 489 ? 5.779   -5.691  55.798  1.00 45.81  ? 489 LEU B C     1 
ATOM   7888  O O     . LEU B 1 489 ? 6.468   -5.880  54.787  1.00 48.79  ? 489 LEU B O     1 
ATOM   7889  C CB    . LEU B 1 489 ? 5.530   -3.354  56.791  1.00 51.85  ? 489 LEU B CB    1 
ATOM   7890  C CG    . LEU B 1 489 ? 6.888   -2.860  56.302  1.00 51.52  ? 489 LEU B CG    1 
ATOM   7891  C CD1   . LEU B 1 489 ? 6.756   -2.242  54.927  1.00 50.76  ? 489 LEU B CD1   1 
ATOM   7892  C CD2   . LEU B 1 489 ? 7.494   -1.863  57.264  1.00 49.83  ? 489 LEU B CD2   1 
ATOM   7893  N N     . TRP B 1 490 ? 5.724   -6.575  56.792  1.00 47.52  ? 490 TRP B N     1 
ATOM   7894  C CA    . TRP B 1 490 ? 6.520   -7.800  56.693  1.00 49.31  ? 490 TRP B CA    1 
ATOM   7895  C C     . TRP B 1 490 ? 5.964   -8.731  55.616  1.00 46.33  ? 490 TRP B C     1 
ATOM   7896  O O     . TRP B 1 490 ? 6.727   -9.487  55.015  1.00 53.16  ? 490 TRP B O     1 
ATOM   7897  C CB    . TRP B 1 490 ? 6.790   -8.520  58.038  1.00 43.28  ? 490 TRP B CB    1 
ATOM   7898  C CG    . TRP B 1 490 ? 8.175   -8.266  58.588  1.00 35.07  ? 490 TRP B CG    1 
ATOM   7899  C CD1   . TRP B 1 490 ? 9.192   -9.167  58.779  1.00 38.65  ? 490 TRP B CD1   1 
ATOM   7900  C CD2   . TRP B 1 490 ? 8.709   -6.988  58.977  1.00 35.76  ? 490 TRP B CD2   1 
ATOM   7901  N NE1   . TRP B 1 490 ? 10.330  -8.537  59.241  1.00 41.22  ? 490 TRP B NE1   1 
ATOM   7902  C CE2   . TRP B 1 490 ? 10.044  -7.199  59.395  1.00 43.41  ? 490 TRP B CE2   1 
ATOM   7903  C CE3   . TRP B 1 490 ? 8.188   -5.692  59.015  1.00 36.81  ? 490 TRP B CE3   1 
ATOM   7904  C CZ2   . TRP B 1 490 ? 10.842  -6.146  59.845  1.00 45.36  ? 490 TRP B CZ2   1 
ATOM   7905  C CZ3   . TRP B 1 490 ? 8.962   -4.667  59.512  1.00 39.94  ? 490 TRP B CZ3   1 
ATOM   7906  C CH2   . TRP B 1 490 ? 10.291  -4.884  59.875  1.00 42.65  ? 490 TRP B CH2   1 
ATOM   7907  N N     . LYS B 1 491 ? 4.669   -8.623  55.304  1.00 46.32  ? 491 LYS B N     1 
ATOM   7908  C CA    . LYS B 1 491 ? 4.088   -9.364  54.189  1.00 45.17  ? 491 LYS B CA    1 
ATOM   7909  C C     . LYS B 1 491 ? 4.636   -8.898  52.827  1.00 48.19  ? 491 LYS B C     1 
ATOM   7910  O O     . LYS B 1 491 ? 4.887   -9.738  51.955  1.00 46.39  ? 491 LYS B O     1 
ATOM   7911  C CB    . LYS B 1 491 ? 2.559   -9.267  54.259  1.00 52.84  ? 491 LYS B CB    1 
ATOM   7912  C CG    . LYS B 1 491 ? 1.930   -10.314 55.168  1.00 57.16  ? 491 LYS B CG    1 
ATOM   7913  C CD    . LYS B 1 491 ? 0.470   -10.115 55.460  1.00 57.93  ? 491 LYS B CD    1 
ATOM   7914  C CE    . LYS B 1 491 ? 0.028   -11.021 56.593  1.00 62.73  ? 491 LYS B CE    1 
ATOM   7915  N NZ    . LYS B 1 491 ? -1.443  -11.176 56.629  1.00 63.60  ? 491 LYS B NZ    1 
ATOM   7916  N N     . MET B 1 492 ? 4.826   -7.576  52.639  1.00 40.55  ? 492 MET B N     1 
ATOM   7917  C CA    . MET B 1 492 ? 5.515   -7.061  51.479  1.00 42.82  ? 492 MET B CA    1 
ATOM   7918  C C     . MET B 1 492 ? 6.983   -7.508  51.456  1.00 53.85  ? 492 MET B C     1 
ATOM   7919  O O     . MET B 1 492 ? 7.438   -7.995  50.412  1.00 55.28  ? 492 MET B O     1 
ATOM   7920  C CB    . MET B 1 492 ? 5.460   -5.540  51.441  1.00 45.07  ? 492 MET B CB    1 
ATOM   7921  C CG    . MET B 1 492 ? 6.209   -4.968  50.272  1.00 40.73  ? 492 MET B CG    1 
ATOM   7922  S SD    . MET B 1 492 ? 6.116   -3.168  50.307  1.00 48.87  ? 492 MET B SD    1 
ATOM   7923  C CE    . MET B 1 492 ? 7.759   -2.847  50.948  1.00 50.97  ? 492 MET B CE    1 
ATOM   7924  N N     . HIS B 1 493 ? 7.735   -7.350  52.571  1.00 49.78  ? 493 HIS B N     1 
ATOM   7925  C CA    . HIS B 1 493 ? 9.140   -7.752  52.545  1.00 46.79  ? 493 HIS B CA    1 
ATOM   7926  C C     . HIS B 1 493 ? 9.230   -9.235  52.188  1.00 47.83  ? 493 HIS B C     1 
ATOM   7927  O O     . HIS B 1 493 ? 10.210  -9.651  51.561  1.00 54.41  ? 493 HIS B O     1 
ATOM   7928  C CB    . HIS B 1 493 ? 9.944   -7.555  53.849  1.00 46.99  ? 493 HIS B CB    1 
ATOM   7929  C CG    . HIS B 1 493 ? 10.099  -6.169  54.393  1.00 49.36  ? 493 HIS B CG    1 
ATOM   7930  N ND1   . HIS B 1 493 ? 10.328  -5.036  53.644  1.00 46.16  ? 493 HIS B ND1   1 
ATOM   7931  C CD2   . HIS B 1 493 ? 10.041  -5.766  55.674  1.00 50.28  ? 493 HIS B CD2   1 
ATOM   7932  C CE1   . HIS B 1 493 ? 10.432  -3.994  54.455  1.00 58.27  ? 493 HIS B CE1   1 
ATOM   7933  N NE2   . HIS B 1 493 ? 10.259  -4.416  55.696  1.00 60.12  ? 493 HIS B NE2   1 
ATOM   7934  N N     . GLU B 1 494 ? 8.240   -10.045 52.617  1.00 47.75  ? 494 GLU B N     1 
ATOM   7935  C CA    . GLU B 1 494 ? 8.319   -11.481 52.357  1.00 52.58  ? 494 GLU B CA    1 
ATOM   7936  C C     . GLU B 1 494 ? 8.072   -11.695 50.866  1.00 50.85  ? 494 GLU B C     1 
ATOM   7937  O O     . GLU B 1 494 ? 8.637   -12.605 50.288  1.00 51.20  ? 494 GLU B O     1 
ATOM   7938  C CB    . GLU B 1 494 ? 7.351   -12.336 53.195  1.00 59.10  ? 494 GLU B CB    1 
ATOM   7939  C CG    . GLU B 1 494 ? 7.547   -12.342 54.725  1.00 65.23  ? 494 GLU B CG    1 
ATOM   7940  C CD    . GLU B 1 494 ? 8.584   -13.250 55.391  1.00 81.56  ? 494 GLU B CD    1 
ATOM   7941  O OE1   . GLU B 1 494 ? 9.413   -13.897 54.674  1.00 79.65  ? 494 GLU B OE1   1 
ATOM   7942  O OE2   . GLU B 1 494 ? 8.588   -13.296 56.666  1.00 76.81  ? 494 GLU B OE2   1 
ATOM   7943  N N     . THR B 1 495 ? 7.214   -10.867 50.250  1.00 54.89  ? 495 THR B N     1 
ATOM   7944  C CA    . THR B 1 495 ? 6.978   -10.939 48.811  1.00 61.59  ? 495 THR B CA    1 
ATOM   7945  C C     . THR B 1 495 ? 8.306   -10.726 48.080  1.00 60.03  ? 495 THR B C     1 
ATOM   7946  O O     . THR B 1 495 ? 8.691   -11.502 47.200  1.00 57.94  ? 495 THR B O     1 
ATOM   7947  C CB    . THR B 1 495 ? 5.942   -9.907  48.328  1.00 59.79  ? 495 THR B CB    1 
ATOM   7948  O OG1   . THR B 1 495 ? 4.659   -10.176 48.892  1.00 53.65  ? 495 THR B OG1   1 
ATOM   7949  C CG2   . THR B 1 495 ? 5.804   -9.896  46.822  1.00 58.03  ? 495 THR B CG2   1 
ATOM   7950  N N     . ILE B 1 496 ? 9.012   -9.664  48.475  1.00 57.95  ? 496 ILE B N     1 
ATOM   7951  C CA    . ILE B 1 496 ? 10.215  -9.268  47.771  1.00 55.80  ? 496 ILE B CA    1 
ATOM   7952  C C     . ILE B 1 496 ? 11.278  -10.346 47.940  1.00 51.15  ? 496 ILE B C     1 
ATOM   7953  O O     . ILE B 1 496 ? 12.030  -10.591 47.000  1.00 51.92  ? 496 ILE B O     1 
ATOM   7954  C CB    . ILE B 1 496 ? 10.690  -7.884  48.229  1.00 50.69  ? 496 ILE B CB    1 
ATOM   7955  C CG1   . ILE B 1 496 ? 9.694   -6.788  47.837  1.00 44.79  ? 496 ILE B CG1   1 
ATOM   7956  C CG2   . ILE B 1 496 ? 12.091  -7.609  47.698  1.00 55.42  ? 496 ILE B CG2   1 
ATOM   7957  C CD1   . ILE B 1 496 ? 9.974   -5.431  48.476  1.00 43.09  ? 496 ILE B CD1   1 
ATOM   7958  N N     . LYS B 1 497 ? 11.273  -11.010 49.103  1.00 49.13  ? 497 LYS B N     1 
ATOM   7959  C CA    . LYS B 1 497 ? 12.285  -11.994 49.470  1.00 52.37  ? 497 LYS B CA    1 
ATOM   7960  C C     . LYS B 1 497 ? 12.167  -13.219 48.570  1.00 50.97  ? 497 LYS B C     1 
ATOM   7961  O O     . LYS B 1 497 ? 13.181  -13.837 48.197  1.00 45.76  ? 497 LYS B O     1 
ATOM   7962  C CB    . LYS B 1 497 ? 12.142  -12.411 50.941  1.00 54.38  ? 497 LYS B CB    1 
ATOM   7963  C CG    . LYS B 1 497 ? 13.024  -13.577 51.408  1.00 51.53  ? 497 LYS B CG    1 
ATOM   7964  C CD    . LYS B 1 497 ? 14.511  -13.342 51.329  1.00 45.64  ? 497 LYS B CD    1 
ATOM   7965  C CE    . LYS B 1 497 ? 15.354  -14.362 52.069  1.00 44.39  ? 497 LYS B CE    1 
ATOM   7966  N NZ    . LYS B 1 497 ? 16.787  -13.940 52.164  1.00 48.29  ? 497 LYS B NZ    1 
ATOM   7967  N N     . ASP B 1 498 ? 10.915  -13.544 48.224  1.00 50.94  ? 498 ASP B N     1 
ATOM   7968  C CA    . ASP B 1 498 ? 10.610  -14.700 47.399  1.00 54.54  ? 498 ASP B CA    1 
ATOM   7969  C C     . ASP B 1 498 ? 10.967  -14.455 45.935  1.00 59.05  ? 498 ASP B C     1 
ATOM   7970  O O     . ASP B 1 498 ? 11.321  -15.401 45.219  1.00 51.02  ? 498 ASP B O     1 
ATOM   7971  C CB    . ASP B 1 498 ? 9.137   -15.078 47.510  1.00 61.26  ? 498 ASP B CB    1 
ATOM   7972  C CG    . ASP B 1 498 ? 8.761   -15.577 48.892  1.00 68.28  ? 498 ASP B CG    1 
ATOM   7973  O OD1   . ASP B 1 498 ? 9.556   -16.341 49.489  1.00 68.78  ? 498 ASP B OD1   1 
ATOM   7974  O OD2   . ASP B 1 498 ? 7.677   -15.204 49.348  1.00 69.95  ? 498 ASP B OD2   1 
ATOM   7975  N N     . ALA B 1 499 ? 10.848  -13.196 45.489  1.00 54.80  ? 499 ALA B N     1 
ATOM   7976  C CA    . ALA B 1 499 ? 11.130  -12.894 44.098  1.00 52.55  ? 499 ALA B CA    1 
ATOM   7977  C C     . ALA B 1 499 ? 12.637  -12.929 43.868  1.00 54.67  ? 499 ALA B C     1 
ATOM   7978  O O     . ALA B 1 499 ? 13.083  -13.458 42.847  1.00 67.28  ? 499 ALA B O     1 
ATOM   7979  C CB    . ALA B 1 499 ? 10.515  -11.578 43.735  1.00 53.92  ? 499 ALA B CB    1 
ATOM   7980  N N     . LEU B 1 500 ? 13.400  -12.432 44.859  1.00 55.74  ? 500 LEU B N     1 
ATOM   7981  C CA    . LEU B 1 500 ? 14.850  -12.254 44.771  1.00 54.24  ? 500 LEU B CA    1 
ATOM   7982  C C     . LEU B 1 500 ? 15.593  -13.503 45.234  1.00 53.44  ? 500 LEU B C     1 
ATOM   7983  O O     . LEU B 1 500 ? 16.691  -13.800 44.763  1.00 43.02  ? 500 LEU B O     1 
ATOM   7984  C CB    . LEU B 1 500 ? 15.262  -11.077 45.671  1.00 51.76  ? 500 LEU B CB    1 
ATOM   7985  C CG    . LEU B 1 500 ? 14.950  -9.669  45.159  1.00 49.63  ? 500 LEU B CG    1 
ATOM   7986  C CD1   . LEU B 1 500 ? 15.484  -8.614  46.131  1.00 45.40  ? 500 LEU B CD1   1 
ATOM   7987  C CD2   . LEU B 1 500 ? 15.532  -9.467  43.765  1.00 49.83  ? 500 LEU B CD2   1 
ATOM   7988  N N     . ASP B 1 501 ? 15.025  -14.157 46.252  1.00 62.24  ? 501 ASP B N     1 
ATOM   7989  C CA    . ASP B 1 501 ? 15.679  -15.266 46.919  1.00 63.14  ? 501 ASP B CA    1 
ATOM   7990  C C     . ASP B 1 501 ? 14.659  -16.395 47.022  1.00 65.52  ? 501 ASP B C     1 
ATOM   7991  O O     . ASP B 1 501 ? 14.131  -16.702 48.090  1.00 61.71  ? 501 ASP B O     1 
ATOM   7992  C CB    . ASP B 1 501 ? 16.265  -14.828 48.265  1.00 57.50  ? 501 ASP B CB    1 
ATOM   7993  C CG    . ASP B 1 501 ? 17.191  -15.870 48.864  1.00 60.03  ? 501 ASP B CG    1 
ATOM   7994  O OD1   . ASP B 1 501 ? 17.467  -16.871 48.143  1.00 63.43  ? 501 ASP B OD1   1 
ATOM   7995  O OD2   . ASP B 1 501 ? 17.623  -15.692 50.049  1.00 57.27  ? 501 ASP B OD2   1 
ATOM   7996  N N     . PRO B 1 502 ? 14.328  -17.031 45.885  1.00 65.81  ? 502 PRO B N     1 
ATOM   7997  C CA    . PRO B 1 502 ? 13.296  -18.062 45.869  1.00 68.57  ? 502 PRO B CA    1 
ATOM   7998  C C     . PRO B 1 502 ? 13.726  -19.347 46.580  1.00 60.14  ? 502 PRO B C     1 
ATOM   7999  O O     . PRO B 1 502 ? 12.885  -20.035 47.141  1.00 48.93  ? 502 PRO B O     1 
ATOM   8000  C CB    . PRO B 1 502 ? 13.030  -18.264 44.366  1.00 69.26  ? 502 PRO B CB    1 
ATOM   8001  C CG    . PRO B 1 502 ? 14.324  -17.873 43.681  1.00 62.45  ? 502 PRO B CG    1 
ATOM   8002  C CD    . PRO B 1 502 ? 14.919  -16.795 44.561  1.00 71.38  ? 502 PRO B CD    1 
ATOM   8003  N N     . ASN B 1 503 ? 15.030  -19.658 46.581  1.00 59.91  ? 503 ASN B N     1 
ATOM   8004  C CA    . ASN B 1 503 ? 15.535  -20.815 47.309  1.00 56.07  ? 503 ASN B CA    1 
ATOM   8005  C C     . ASN B 1 503 ? 15.873  -20.492 48.771  1.00 58.60  ? 503 ASN B C     1 
ATOM   8006  O O     . ASN B 1 503 ? 16.207  -21.408 49.520  1.00 53.35  ? 503 ASN B O     1 
ATOM   8007  C CB    . ASN B 1 503 ? 16.754  -21.437 46.625  1.00 55.93  ? 503 ASN B CB    1 
ATOM   8008  C CG    . ASN B 1 503 ? 16.450  -21.887 45.210  1.00 55.38  ? 503 ASN B CG    1 
ATOM   8009  O OD1   . ASN B 1 503 ? 15.435  -22.516 44.971  1.00 49.73  ? 503 ASN B OD1   1 
ATOM   8010  N ND2   . ASN B 1 503 ? 17.289  -21.532 44.253  1.00 54.60  ? 503 ASN B ND2   1 
ATOM   8011  N N     . GLY B 1 504 ? 15.789  -19.216 49.182  1.00 59.60  ? 504 GLY B N     1 
ATOM   8012  C CA    . GLY B 1 504 ? 15.996  -18.830 50.571  1.00 58.47  ? 504 GLY B CA    1 
ATOM   8013  C C     . GLY B 1 504 ? 17.376  -19.240 51.083  1.00 59.76  ? 504 GLY B C     1 
ATOM   8014  O O     . GLY B 1 504 ? 17.482  -20.095 51.956  1.00 69.16  ? 504 GLY B O     1 
ATOM   8015  N N     . ILE B 1 505 ? 18.429  -18.618 50.545  1.00 56.46  ? 505 ILE B N     1 
ATOM   8016  C CA    . ILE B 1 505 ? 19.789  -19.020 50.858  1.00 53.65  ? 505 ILE B CA    1 
ATOM   8017  C C     . ILE B 1 505 ? 20.599  -17.862 51.447  1.00 54.51  ? 505 ILE B C     1 
ATOM   8018  O O     . ILE B 1 505 ? 21.738  -18.080 51.876  1.00 59.95  ? 505 ILE B O     1 
ATOM   8019  C CB    . ILE B 1 505 ? 20.439  -19.651 49.610  1.00 61.84  ? 505 ILE B CB    1 
ATOM   8020  C CG1   . ILE B 1 505 ? 20.397  -18.745 48.377  1.00 62.44  ? 505 ILE B CG1   1 
ATOM   8021  C CG2   . ILE B 1 505 ? 19.804  -21.004 49.311  1.00 65.78  ? 505 ILE B CG2   1 
ATOM   8022  C CD1   . ILE B 1 505 ? 21.569  -17.810 48.277  1.00 70.16  ? 505 ILE B CD1   1 
ATOM   8023  N N     . LEU B 1 506 ? 20.040  -16.640 51.443  1.00 47.77  ? 506 LEU B N     1 
ATOM   8024  C CA    . LEU B 1 506 ? 20.682  -15.522 52.109  1.00 52.71  ? 506 LEU B CA    1 
ATOM   8025  C C     . LEU B 1 506 ? 20.036  -15.321 53.481  1.00 52.48  ? 506 LEU B C     1 
ATOM   8026  O O     . LEU B 1 506 ? 18.852  -15.022 53.581  1.00 55.91  ? 506 LEU B O     1 
ATOM   8027  C CB    . LEU B 1 506 ? 20.563  -14.248 51.265  1.00 53.76  ? 506 LEU B CB    1 
ATOM   8028  C CG    . LEU B 1 506 ? 21.599  -14.003 50.165  1.00 53.88  ? 506 LEU B CG    1 
ATOM   8029  C CD1   . LEU B 1 506 ? 21.773  -12.508 49.917  1.00 57.67  ? 506 LEU B CD1   1 
ATOM   8030  C CD2   . LEU B 1 506 ? 22.943  -14.597 50.499  1.00 57.96  ? 506 LEU B CD2   1 
ATOM   8031  N N     . ALA B 1 507 ? 20.841  -15.534 54.525  1.00 52.96  ? 507 ALA B N     1 
ATOM   8032  C CA    . ALA B 1 507 ? 20.650  -14.977 55.859  1.00 50.92  ? 507 ALA B CA    1 
ATOM   8033  C C     . ALA B 1 507 ? 19.204  -15.110 56.331  1.00 49.27  ? 507 ALA B C     1 
ATOM   8034  O O     . ALA B 1 507 ? 18.577  -14.125 56.722  1.00 54.98  ? 507 ALA B O     1 
ATOM   8035  C CB    . ALA B 1 507 ? 21.117  -13.537 55.873  1.00 47.76  ? 507 ALA B CB    1 
ATOM   8036  N N     . PRO B 1 508 ? 18.646  -16.335 56.334  1.00 42.01  ? 508 PRO B N     1 
ATOM   8037  C CA    . PRO B 1 508 ? 17.266  -16.549 56.767  1.00 47.74  ? 508 PRO B CA    1 
ATOM   8038  C C     . PRO B 1 508 ? 17.054  -16.143 58.227  1.00 49.25  ? 508 PRO B C     1 
ATOM   8039  O O     . PRO B 1 508 ? 17.815  -16.533 59.102  1.00 54.90  ? 508 PRO B O     1 
ATOM   8040  C CB    . PRO B 1 508 ? 17.031  -18.052 56.515  1.00 50.31  ? 508 PRO B CB    1 
ATOM   8041  C CG    . PRO B 1 508 ? 18.420  -18.677 56.364  1.00 48.34  ? 508 PRO B CG    1 
ATOM   8042  C CD    . PRO B 1 508 ? 19.327  -17.566 55.916  1.00 48.03  ? 508 PRO B CD    1 
ATOM   8043  N N     . GLY B 1 509 ? 16.058  -15.288 58.462  1.00 50.44  ? 509 GLY B N     1 
ATOM   8044  C CA    . GLY B 1 509 ? 15.843  -14.696 59.769  1.00 49.99  ? 509 GLY B CA    1 
ATOM   8045  C C     . GLY B 1 509 ? 16.221  -13.217 59.836  1.00 51.95  ? 509 GLY B C     1 
ATOM   8046  O O     . GLY B 1 509 ? 15.594  -12.473 60.581  1.00 62.70  ? 509 GLY B O     1 
ATOM   8047  N N     . LYS B 1 510 ? 17.261  -12.783 59.112  1.00 50.57  ? 510 LYS B N     1 
ATOM   8048  C CA    . LYS B 1 510 ? 17.687  -11.386 59.188  1.00 49.52  ? 510 LYS B CA    1 
ATOM   8049  C C     . LYS B 1 510 ? 16.448  -10.486 59.232  1.00 39.52  ? 510 LYS B C     1 
ATOM   8050  O O     . LYS B 1 510 ? 15.510  -10.666 58.464  1.00 40.01  ? 510 LYS B O     1 
ATOM   8051  C CB    . LYS B 1 510 ? 18.643  -11.037 58.040  1.00 44.26  ? 510 LYS B CB    1 
ATOM   8052  C CG    . LYS B 1 510 ? 19.215  -9.629  58.081  1.00 49.78  ? 510 LYS B CG    1 
ATOM   8053  C CD    . LYS B 1 510 ? 19.951  -9.243  59.367  1.00 55.79  ? 510 LYS B CD    1 
ATOM   8054  C CE    . LYS B 1 510 ? 20.395  -7.787  59.332  1.00 60.21  ? 510 LYS B CE    1 
ATOM   8055  N NZ    . LYS B 1 510 ? 20.633  -7.198  60.671  1.00 48.84  ? 510 LYS B NZ    1 
ATOM   8056  N N     . SER B 1 511 ? 16.397  -9.594  60.213  1.00 37.95  ? 511 SER B N     1 
ATOM   8057  C CA    . SER B 1 511 ? 15.268  -8.699  60.396  1.00 43.95  ? 511 SER B CA    1 
ATOM   8058  C C     . SER B 1 511 ? 13.916  -9.421  60.334  1.00 47.62  ? 511 SER B C     1 
ATOM   8059  O O     . SER B 1 511 ? 12.881  -8.828  60.004  1.00 51.62  ? 511 SER B O     1 
ATOM   8060  C CB    . SER B 1 511 ? 15.364  -7.582  59.403  1.00 45.51  ? 511 SER B CB    1 
ATOM   8061  O OG    . SER B 1 511 ? 16.641  -6.980  59.518  1.00 48.21  ? 511 SER B OG    1 
ATOM   8062  N N     . GLY B 1 512 ? 13.917  -10.704 60.698  1.00 41.75  ? 512 GLY B N     1 
ATOM   8063  C CA    . GLY B 1 512 ? 12.696  -11.467 60.807  1.00 42.34  ? 512 GLY B CA    1 
ATOM   8064  C C     . GLY B 1 512 ? 12.069  -11.779 59.454  1.00 45.66  ? 512 GLY B C     1 
ATOM   8065  O O     . GLY B 1 512 ? 10.838  -11.901 59.330  1.00 41.90  ? 512 GLY B O     1 
ATOM   8066  N N     . ILE B 1 513 ? 12.935  -11.914 58.446  1.00 52.97  ? 513 ILE B N     1 
ATOM   8067  C CA    . ILE B 1 513 ? 12.486  -12.153 57.079  1.00 52.03  ? 513 ILE B CA    1 
ATOM   8068  C C     . ILE B 1 513 ? 12.883  -13.573 56.686  1.00 49.59  ? 513 ILE B C     1 
ATOM   8069  O O     . ILE B 1 513 ? 14.068  -13.891 56.602  1.00 55.52  ? 513 ILE B O     1 
ATOM   8070  C CB    . ILE B 1 513 ? 13.067  -11.102 56.114  1.00 52.00  ? 513 ILE B CB    1 
ATOM   8071  C CG1   . ILE B 1 513 ? 12.585  -9.681  56.439  1.00 56.14  ? 513 ILE B CG1   1 
ATOM   8072  C CG2   . ILE B 1 513 ? 12.753  -11.489 54.677  1.00 58.01  ? 513 ILE B CG2   1 
ATOM   8073  C CD1   . ILE B 1 513 ? 13.346  -8.563  55.723  1.00 50.11  ? 513 ILE B CD1   1 
ATOM   8074  N N     . TRP B 1 514 ? 11.890  -14.428 56.426  1.00 52.27  ? 514 TRP B N     1 
ATOM   8075  C CA    . TRP B 1 514 ? 12.154  -15.855 56.365  1.00 54.42  ? 514 TRP B CA    1 
ATOM   8076  C C     . TRP B 1 514 ? 12.055  -16.398 54.943  1.00 63.38  ? 514 TRP B C     1 
ATOM   8077  O O     . TRP B 1 514 ? 12.915  -17.184 54.537  1.00 77.03  ? 514 TRP B O     1 
ATOM   8078  C CB    . TRP B 1 514 ? 11.256  -16.598 57.369  1.00 55.34  ? 514 TRP B CB    1 
ATOM   8079  C CG    . TRP B 1 514 ? 11.743  -16.405 58.777  1.00 54.57  ? 514 TRP B CG    1 
ATOM   8080  C CD1   . TRP B 1 514 ? 11.358  -15.445 59.672  1.00 50.93  ? 514 TRP B CD1   1 
ATOM   8081  C CD2   . TRP B 1 514 ? 12.772  -17.172 59.431  1.00 50.32  ? 514 TRP B CD2   1 
ATOM   8082  N NE1   . TRP B 1 514 ? 12.075  -15.573 60.835  1.00 56.53  ? 514 TRP B NE1   1 
ATOM   8083  C CE2   . TRP B 1 514 ? 12.945  -16.627 60.717  1.00 50.09  ? 514 TRP B CE2   1 
ATOM   8084  C CE3   . TRP B 1 514 ? 13.544  -18.282 59.057  1.00 55.60  ? 514 TRP B CE3   1 
ATOM   8085  C CZ2   . TRP B 1 514 ? 13.859  -17.154 61.629  1.00 50.52  ? 514 TRP B CZ2   1 
ATOM   8086  C CZ3   . TRP B 1 514 ? 14.464  -18.786 59.951  1.00 58.32  ? 514 TRP B CZ3   1 
ATOM   8087  C CH2   . TRP B 1 514 ? 14.616  -18.229 61.224  1.00 47.55  ? 514 TRP B CH2   1 
ATOM   8088  N N     . GLY B 1 515 ? 10.993  -16.052 54.207  1.00 64.49  ? 515 GLY B N     1 
ATOM   8089  C CA    . GLY B 1 515 ? 10.846  -16.557 52.839  1.00 75.05  ? 515 GLY B CA    1 
ATOM   8090  C C     . GLY B 1 515 ? 10.346  -18.007 52.743  1.00 64.27  ? 515 GLY B C     1 
ATOM   8091  O O     . GLY B 1 515 ? 10.622  -18.805 53.627  1.00 71.16  ? 515 GLY B O     1 
ATOM   8092  N N     . LYS B 1 516 ? 9.746   -18.357 51.588  1.00 59.71  ? 516 LYS B N     1 
ATOM   8093  C CA    . LYS B 1 516 ? 8.681   -19.350 51.442  1.00 63.34  ? 516 LYS B CA    1 
ATOM   8094  C C     . LYS B 1 516 ? 9.015   -20.689 52.100  1.00 60.27  ? 516 LYS B C     1 
ATOM   8095  O O     . LYS B 1 516 ? 8.224   -21.192 52.883  1.00 57.51  ? 516 LYS B O     1 
ATOM   8096  C CB    . LYS B 1 516 ? 8.324   -19.599 49.964  1.00 61.42  ? 516 LYS B CB    1 
ATOM   8097  N N     . ASN B 1 517 ? 10.173  -21.277 51.796  1.00 64.62  ? 517 ASN B N     1 
ATOM   8098  C CA    . ASN B 1 517 ? 10.509  -22.603 52.312  1.00 73.11  ? 517 ASN B CA    1 
ATOM   8099  C C     . ASN B 1 517 ? 10.436  -22.721 53.841  1.00 78.79  ? 517 ASN B C     1 
ATOM   8100  O O     . ASN B 1 517 ? 10.184  -23.817 54.342  1.00 78.92  ? 517 ASN B O     1 
ATOM   8101  C CB    . ASN B 1 517 ? 11.919  -23.052 51.928  1.00 71.05  ? 517 ASN B CB    1 
ATOM   8102  C CG    . ASN B 1 517 ? 12.213  -22.779 50.477  1.00 79.99  ? 517 ASN B CG    1 
ATOM   8103  O OD1   . ASN B 1 517 ? 11.951  -23.630 49.634  1.00 66.66  ? 517 ASN B OD1   1 
ATOM   8104  N ND2   . ASN B 1 517 ? 12.674  -21.571 50.186  1.00 92.22  ? 517 ASN B ND2   1 
ATOM   8105  N N     . ARG B 1 518 ? 10.726  -21.640 54.587  1.00 76.20  ? 518 ARG B N     1 
ATOM   8106  C CA    . ARG B 1 518 ? 10.950  -21.739 56.022  1.00 71.46  ? 518 ARG B CA    1 
ATOM   8107  C C     . ARG B 1 518 ? 9.877   -20.964 56.784  1.00 71.21  ? 518 ARG B C     1 
ATOM   8108  O O     . ARG B 1 518 ? 10.160  -20.404 57.832  1.00 85.46  ? 518 ARG B O     1 
ATOM   8109  C CB    . ARG B 1 518 ? 12.357  -21.226 56.372  1.00 70.21  ? 518 ARG B CB    1 
ATOM   8110  C CG    . ARG B 1 518 ? 13.504  -22.174 56.038  1.00 62.50  ? 518 ARG B CG    1 
ATOM   8111  C CD    . ARG B 1 518 ? 14.827  -21.427 55.984  1.00 75.44  ? 518 ARG B CD    1 
ATOM   8112  N NE    . ARG B 1 518 ? 15.976  -22.287 55.731  1.00 82.34  ? 518 ARG B NE    1 
ATOM   8113  C CZ    . ARG B 1 518 ? 16.472  -22.572 54.524  1.00 96.61  ? 518 ARG B CZ    1 
ATOM   8114  N NH1   . ARG B 1 518 ? 15.919  -22.064 53.429  1.00 99.43  ? 518 ARG B NH1   1 
ATOM   8115  N NH2   . ARG B 1 518 ? 17.510  -23.390 54.415  1.00 89.65  ? 518 ARG B NH2   1 
ATOM   8116  N N     . ARG B 1 519 ? 8.638   -20.950 56.282  1.00 74.61  ? 519 ARG B N     1 
ATOM   8117  C CA    . ARG B 1 519 ? 7.584   -20.125 56.859  1.00 78.98  ? 519 ARG B CA    1 
ATOM   8118  C C     . ARG B 1 519 ? 6.314   -20.983 57.009  1.00 82.52  ? 519 ARG B C     1 
ATOM   8119  O O     . ARG B 1 519 ? 5.694   -20.940 58.101  1.00 76.56  ? 519 ARG B O     1 
ATOM   8120  C CB    . ARG B 1 519 ? 7.366   -18.908 55.949  1.00 77.48  ? 519 ARG B CB    1 
ATOM   8121  C CG    . ARG B 1 519 ? 7.149   -17.574 56.650  1.00 83.57  ? 519 ARG B CG    1 
ATOM   8122  C CD    . ARG B 1 519 ? 6.571   -16.507 55.722  1.00 85.91  ? 519 ARG B CD    1 
ATOM   8123  N NE    . ARG B 1 519 ? 7.158   -16.564 54.386  1.00 101.66 ? 519 ARG B NE    1 
ATOM   8124  C CZ    . ARG B 1 519 ? 6.593   -16.119 53.265  1.00 96.28  ? 519 ARG B CZ    1 
ATOM   8125  N NH1   . ARG B 1 519 ? 5.470   -15.425 53.295  1.00 101.19 ? 519 ARG B NH1   1 
ATOM   8126  N NH2   . ARG B 1 519 ? 7.176   -16.358 52.105  1.00 88.22  ? 519 ARG B NH2   1 
ATOM   8127  N N     . ALA C 1 3   ? 14.359  29.038  -17.904 1.00 118.36 ? 3   ALA C N     1 
ATOM   8128  C CA    . ALA C 1 3   ? 14.410  27.677  -17.314 1.00 112.88 ? 3   ALA C CA    1 
ATOM   8129  C C     . ALA C 1 3   ? 13.025  27.274  -16.802 1.00 104.15 ? 3   ALA C C     1 
ATOM   8130  O O     . ALA C 1 3   ? 12.341  28.061  -16.126 1.00 76.51  ? 3   ALA C O     1 
ATOM   8131  C CB    . ALA C 1 3   ? 15.449  27.608  -16.219 1.00 112.84 ? 3   ALA C CB    1 
ATOM   8132  N N     . PRO C 1 4   ? 12.583  26.030  -17.120 1.00 92.64  ? 4   PRO C N     1 
ATOM   8133  C CA    . PRO C 1 4   ? 11.227  25.581  -16.816 1.00 92.88  ? 4   PRO C CA    1 
ATOM   8134  C C     . PRO C 1 4   ? 11.101  24.975  -15.423 1.00 89.03  ? 4   PRO C C     1 
ATOM   8135  O O     . PRO C 1 4   ? 12.090  24.566  -14.821 1.00 88.82  ? 4   PRO C O     1 
ATOM   8136  C CB    . PRO C 1 4   ? 10.972  24.509  -17.890 1.00 92.40  ? 4   PRO C CB    1 
ATOM   8137  C CG    . PRO C 1 4   ? 12.343  23.922  -18.186 1.00 93.27  ? 4   PRO C CG    1 
ATOM   8138  C CD    . PRO C 1 4   ? 13.360  24.989  -17.815 1.00 95.52  ? 4   PRO C CD    1 
ATOM   8139  N N     . LEU C 1 5   ? 9.865   24.933  -14.923 1.00 77.54  ? 5   LEU C N     1 
ATOM   8140  C CA    . LEU C 1 5   ? 9.527   24.090  -13.793 1.00 84.44  ? 5   LEU C CA    1 
ATOM   8141  C C     . LEU C 1 5   ? 9.843   22.643  -14.171 1.00 91.81  ? 5   LEU C C     1 
ATOM   8142  O O     . LEU C 1 5   ? 9.922   22.326  -15.359 1.00 77.64  ? 5   LEU C O     1 
ATOM   8143  C CB    . LEU C 1 5   ? 8.041   24.280  -13.478 1.00 89.38  ? 5   LEU C CB    1 
ATOM   8144  C CG    . LEU C 1 5   ? 7.631   25.693  -13.072 1.00 88.07  ? 5   LEU C CG    1 
ATOM   8145  C CD1   . LEU C 1 5   ? 6.135   25.767  -12.812 1.00 88.51  ? 5   LEU C CD1   1 
ATOM   8146  C CD2   . LEU C 1 5   ? 8.414   26.146  -11.845 1.00 91.25  ? 5   LEU C CD2   1 
ATOM   8147  N N     . PRO C 1 6   ? 10.114  21.744  -13.192 1.00 104.14 ? 6   PRO C N     1 
ATOM   8148  C CA    . PRO C 1 6   ? 10.384  20.332  -13.486 1.00 98.57  ? 6   PRO C CA    1 
ATOM   8149  C C     . PRO C 1 6   ? 9.103   19.504  -13.563 1.00 94.81  ? 6   PRO C C     1 
ATOM   8150  O O     . PRO C 1 6   ? 8.140   19.803  -12.861 1.00 91.98  ? 6   PRO C O     1 
ATOM   8151  C CB    . PRO C 1 6   ? 11.283  19.915  -12.310 1.00 97.23  ? 6   PRO C CB    1 
ATOM   8152  C CG    . PRO C 1 6   ? 10.825  20.787  -11.150 1.00 100.48 ? 6   PRO C CG    1 
ATOM   8153  C CD    . PRO C 1 6   ? 10.261  22.057  -11.760 1.00 103.01 ? 6   PRO C CD    1 
ATOM   8154  N N     . GLU C 1 7   ? 9.107   18.469  -14.418 1.00 93.94  ? 7   GLU C N     1 
ATOM   8155  C CA    . GLU C 1 7   ? 7.923   17.664  -14.696 1.00 92.08  ? 7   GLU C CA    1 
ATOM   8156  C C     . GLU C 1 7   ? 7.134   17.458  -13.400 1.00 77.61  ? 7   GLU C C     1 
ATOM   8157  O O     . GLU C 1 7   ? 7.666   16.938  -12.426 1.00 79.98  ? 7   GLU C O     1 
ATOM   8158  C CB    . GLU C 1 7   ? 8.339   16.339  -15.351 1.00 104.46 ? 7   GLU C CB    1 
ATOM   8159  C CG    . GLU C 1 7   ? 7.186   15.510  -15.924 1.00 118.11 ? 7   GLU C CG    1 
ATOM   8160  C CD    . GLU C 1 7   ? 7.576   14.321  -16.805 1.00 124.14 ? 7   GLU C CD    1 
ATOM   8161  O OE1   . GLU C 1 7   ? 7.883   14.530  -18.001 1.00 110.83 ? 7   GLU C OE1   1 
ATOM   8162  O OE2   . GLU C 1 7   ? 7.585   13.176  -16.298 1.00 113.43 ? 7   GLU C OE2   1 
ATOM   8163  N N     . GLY C 1 8   ? 5.882   17.931  -13.376 1.00 68.28  ? 8   GLY C N     1 
ATOM   8164  C CA    . GLY C 1 8   ? 4.939   17.592  -12.319 1.00 73.47  ? 8   GLY C CA    1 
ATOM   8165  C C     . GLY C 1 8   ? 5.087   18.408  -11.030 1.00 71.43  ? 8   GLY C C     1 
ATOM   8166  O O     . GLY C 1 8   ? 4.610   17.972  -9.985  1.00 66.29  ? 8   GLY C O     1 
ATOM   8167  N N     . VAL C 1 9   ? 5.701   19.599  -11.105 1.00 64.36  ? 9   VAL C N     1 
ATOM   8168  C CA    . VAL C 1 9   ? 5.796   20.486  -9.958  1.00 71.02  ? 9   VAL C CA    1 
ATOM   8169  C C     . VAL C 1 9   ? 5.033   21.765  -10.278 1.00 75.18  ? 9   VAL C C     1 
ATOM   8170  O O     . VAL C 1 9   ? 5.490   22.559  -11.093 1.00 75.27  ? 9   VAL C O     1 
ATOM   8171  C CB    . VAL C 1 9   ? 7.264   20.808  -9.591  1.00 75.67  ? 9   VAL C CB    1 
ATOM   8172  C CG1   . VAL C 1 9   ? 7.367   21.783  -8.421  1.00 73.68  ? 9   VAL C CG1   1 
ATOM   8173  C CG2   . VAL C 1 9   ? 8.067   19.552  -9.289  1.00 74.66  ? 9   VAL C CG2   1 
ATOM   8174  N N     . SER C 1 10  ? 3.904   21.994  -9.598  1.00 77.40  ? 10  SER C N     1 
ATOM   8175  C CA    . SER C 1 10  ? 3.116   23.191  -9.851  1.00 76.31  ? 10  SER C CA    1 
ATOM   8176  C C     . SER C 1 10  ? 3.898   24.433  -9.428  1.00 74.36  ? 10  SER C C     1 
ATOM   8177  O O     . SER C 1 10  ? 4.810   24.346  -8.617  1.00 79.64  ? 10  SER C O     1 
ATOM   8178  C CB    . SER C 1 10  ? 1.747   23.112  -9.195  1.00 80.75  ? 10  SER C CB    1 
ATOM   8179  O OG    . SER C 1 10  ? 1.830   22.769  -7.821  1.00 79.80  ? 10  SER C OG    1 
ATOM   8180  N N     . ALA C 1 11  ? 3.532   25.585  -9.998  1.00 86.98  ? 11  ALA C N     1 
ATOM   8181  C CA    . ALA C 1 11  ? 4.202   26.851  -9.730  1.00 90.01  ? 11  ALA C CA    1 
ATOM   8182  C C     . ALA C 1 11  ? 3.914   27.366  -8.314  1.00 87.11  ? 11  ALA C C     1 
ATOM   8183  O O     . ALA C 1 11  ? 4.733   28.109  -7.771  1.00 76.10  ? 11  ALA C O     1 
ATOM   8184  C CB    . ALA C 1 11  ? 3.792   27.864  -10.769 1.00 89.48  ? 11  ALA C CB    1 
ATOM   8185  N N     . GLU C 1 12  ? 2.759   26.991  -7.728  1.00 93.07  ? 12  GLU C N     1 
ATOM   8186  C CA    . GLU C 1 12  ? 2.451   27.311  -6.336  1.00 103.55 ? 12  GLU C CA    1 
ATOM   8187  C C     . GLU C 1 12  ? 3.317   26.469  -5.406  1.00 104.39 ? 12  GLU C C     1 
ATOM   8188  O O     . GLU C 1 12  ? 3.687   26.937  -4.333  1.00 108.75 ? 12  GLU C O     1 
ATOM   8189  C CB    . GLU C 1 12  ? 1.010   27.002  -5.910  1.00 111.80 ? 12  GLU C CB    1 
ATOM   8190  C CG    . GLU C 1 12  ? -0.046  27.886  -6.541  1.00 122.28 ? 12  GLU C CG    1 
ATOM   8191  C CD    . GLU C 1 12  ? -0.417  27.478  -7.957  1.00 124.28 ? 12  GLU C CD    1 
ATOM   8192  O OE1   . GLU C 1 12  ? -0.319  28.340  -8.852  1.00 119.35 ? 12  GLU C OE1   1 
ATOM   8193  O OE2   . GLU C 1 12  ? -0.779  26.292  -8.165  1.00 111.20 ? 12  GLU C OE2   1 
ATOM   8194  N N     . ALA C 1 13  ? 3.586   25.217  -5.809  1.00 103.13 ? 13  ALA C N     1 
ATOM   8195  C CA    . ALA C 1 13  ? 4.413   24.307  -5.029  1.00 96.64  ? 13  ALA C CA    1 
ATOM   8196  C C     . ALA C 1 13  ? 5.878   24.753  -5.055  1.00 85.67  ? 13  ALA C C     1 
ATOM   8197  O O     . ALA C 1 13  ? 6.510   24.838  -4.002  1.00 76.61  ? 13  ALA C O     1 
ATOM   8198  C CB    . ALA C 1 13  ? 4.245   22.892  -5.528  1.00 99.03  ? 13  ALA C CB    1 
ATOM   8199  N N     . MET C 1 14  ? 6.413   25.073  -6.245  1.00 79.03  ? 14  MET C N     1 
ATOM   8200  C CA    . MET C 1 14  ? 7.804   25.498  -6.370  1.00 74.46  ? 14  MET C CA    1 
ATOM   8201  C C     . MET C 1 14  ? 8.017   26.849  -5.685  1.00 83.21  ? 14  MET C C     1 
ATOM   8202  O O     . MET C 1 14  ? 9.157   27.225  -5.385  1.00 83.57  ? 14  MET C O     1 
ATOM   8203  C CB    . MET C 1 14  ? 8.232   25.585  -7.837  1.00 68.72  ? 14  MET C CB    1 
ATOM   8204  C CG    . MET C 1 14  ? 9.578   26.261  -8.062  1.00 72.91  ? 14  MET C CG    1 
ATOM   8205  S SD    . MET C 1 14  ? 10.978  25.437  -7.228  1.00 78.31  ? 14  MET C SD    1 
ATOM   8206  C CE    . MET C 1 14  ? 11.569  24.373  -8.542  1.00 68.89  ? 14  MET C CE    1 
ATOM   8207  N N     . SER C 1 15  ? 6.914   27.569  -5.439  1.00 84.17  ? 15  SER C N     1 
ATOM   8208  C CA    . SER C 1 15  ? 6.965   28.888  -4.827  1.00 92.91  ? 15  SER C CA    1 
ATOM   8209  C C     . SER C 1 15  ? 7.009   28.757  -3.301  1.00 83.98  ? 15  SER C C     1 
ATOM   8210  O O     . SER C 1 15  ? 7.906   29.312  -2.672  1.00 79.54  ? 15  SER C O     1 
ATOM   8211  C CB    . SER C 1 15  ? 5.810   29.744  -5.313  1.00 89.26  ? 15  SER C CB    1 
ATOM   8212  O OG    . SER C 1 15  ? 5.948   31.083  -4.870  1.00 73.66  ? 15  SER C OG    1 
ATOM   8213  N N     . SER C 1 16  ? 6.038   28.026  -2.725  1.00 72.80  ? 16  SER C N     1 
ATOM   8214  C CA    . SER C 1 16  ? 6.042   27.611  -1.324  1.00 79.50  ? 16  SER C CA    1 
ATOM   8215  C C     . SER C 1 16  ? 7.410   27.097  -0.856  1.00 86.68  ? 16  SER C C     1 
ATOM   8216  O O     . SER C 1 16  ? 7.803   27.342  0.287   1.00 86.89  ? 16  SER C O     1 
ATOM   8217  C CB    . SER C 1 16  ? 5.018   26.530  -1.077  1.00 75.96  ? 16  SER C CB    1 
ATOM   8218  O OG    . SER C 1 16  ? 3.693   27.031  -1.096  1.00 73.06  ? 16  SER C OG    1 
ATOM   8219  N N     . ALA C 1 17  ? 8.097   26.341  -1.727  1.00 78.27  ? 17  ALA C N     1 
ATOM   8220  C CA    . ALA C 1 17  ? 9.336   25.664  -1.380  1.00 79.87  ? 17  ALA C CA    1 
ATOM   8221  C C     . ALA C 1 17  ? 10.496  26.648  -1.278  1.00 74.31  ? 17  ALA C C     1 
ATOM   8222  O O     . ALA C 1 17  ? 11.301  26.547  -0.353  1.00 80.88  ? 17  ALA C O     1 
ATOM   8223  C CB    . ALA C 1 17  ? 9.645   24.583  -2.387  1.00 85.59  ? 17  ALA C CB    1 
ATOM   8224  N N     . LEU C 1 18  ? 10.600  27.568  -2.242  1.00 65.67  ? 18  LEU C N     1 
ATOM   8225  C CA    . LEU C 1 18  ? 11.646  28.579  -2.210  1.00 65.66  ? 18  LEU C CA    1 
ATOM   8226  C C     . LEU C 1 18  ? 11.385  29.534  -1.043  1.00 74.17  ? 18  LEU C C     1 
ATOM   8227  O O     . LEU C 1 18  ? 12.309  30.108  -0.478  1.00 75.96  ? 18  LEU C O     1 
ATOM   8228  C CB    . LEU C 1 18  ? 11.679  29.323  -3.546  1.00 72.09  ? 18  LEU C CB    1 
ATOM   8229  C CG    . LEU C 1 18  ? 12.027  28.470  -4.764  1.00 82.60  ? 18  LEU C CG    1 
ATOM   8230  C CD1   . LEU C 1 18  ? 11.498  29.103  -6.036  1.00 94.00  ? 18  LEU C CD1   1 
ATOM   8231  C CD2   . LEU C 1 18  ? 13.526  28.270  -4.879  1.00 85.71  ? 18  LEU C CD2   1 
ATOM   8232  N N     . ASP C 1 19  ? 10.115  29.705  -0.677  1.00 79.96  ? 19  ASP C N     1 
ATOM   8233  C CA    . ASP C 1 19  ? 9.770   30.530  0.460   1.00 82.96  ? 19  ASP C CA    1 
ATOM   8234  C C     . ASP C 1 19  ? 10.445  29.927  1.687   1.00 80.27  ? 19  ASP C C     1 
ATOM   8235  O O     . ASP C 1 19  ? 11.302  30.545  2.319   1.00 78.14  ? 19  ASP C O     1 
ATOM   8236  C CB    . ASP C 1 19  ? 8.250   30.618  0.628   1.00 91.08  ? 19  ASP C CB    1 
ATOM   8237  C CG    . ASP C 1 19  ? 7.833   31.788  1.492   1.00 98.93  ? 19  ASP C CG    1 
ATOM   8238  O OD1   . ASP C 1 19  ? 8.162   32.912  1.095   1.00 97.04  ? 19  ASP C OD1   1 
ATOM   8239  O OD2   . ASP C 1 19  ? 7.218   31.562  2.562   1.00 100.46 ? 19  ASP C OD2   1 
ATOM   8240  N N     . ARG C 1 20  ? 10.072  28.679  1.977   1.00 74.45  ? 20  ARG C N     1 
ATOM   8241  C CA    . ARG C 1 20  ? 10.498  27.997  3.185   1.00 66.81  ? 20  ARG C CA    1 
ATOM   8242  C C     . ARG C 1 20  ? 12.022  27.851  3.236   1.00 63.05  ? 20  ARG C C     1 
ATOM   8243  O O     . ARG C 1 20  ? 12.612  28.081  4.288   1.00 70.48  ? 20  ARG C O     1 
ATOM   8244  C CB    . ARG C 1 20  ? 9.780   26.658  3.239   1.00 66.33  ? 20  ARG C CB    1 
ATOM   8245  C CG    . ARG C 1 20  ? 8.302   26.759  3.585   1.00 73.12  ? 20  ARG C CG    1 
ATOM   8246  C CD    . ARG C 1 20  ? 8.072   26.610  5.075   1.00 80.31  ? 20  ARG C CD    1 
ATOM   8247  N NE    . ARG C 1 20  ? 7.194   25.471  5.306   1.00 89.16  ? 20  ARG C NE    1 
ATOM   8248  C CZ    . ARG C 1 20  ? 7.553   24.340  5.915   1.00 87.88  ? 20  ARG C CZ    1 
ATOM   8249  N NH1   . ARG C 1 20  ? 8.747   24.226  6.480   1.00 83.41  ? 20  ARG C NH1   1 
ATOM   8250  N NH2   . ARG C 1 20  ? 6.700   23.330  5.967   1.00 82.93  ? 20  ARG C NH2   1 
ATOM   8251  N N     . PHE C 1 21  ? 12.659  27.509  2.106   1.00 53.29  ? 21  PHE C N     1 
ATOM   8252  C CA    . PHE C 1 21  ? 14.113  27.449  2.025   1.00 59.43  ? 21  PHE C CA    1 
ATOM   8253  C C     . PHE C 1 21  ? 14.745  28.736  2.552   1.00 67.41  ? 21  PHE C C     1 
ATOM   8254  O O     . PHE C 1 21  ? 15.714  28.694  3.312   1.00 62.64  ? 21  PHE C O     1 
ATOM   8255  C CB    . PHE C 1 21  ? 14.614  27.230  0.591   1.00 55.44  ? 21  PHE C CB    1 
ATOM   8256  C CG    . PHE C 1 21  ? 14.285  25.900  -0.048  1.00 52.13  ? 21  PHE C CG    1 
ATOM   8257  C CD1   . PHE C 1 21  ? 13.840  24.819  0.694   1.00 52.72  ? 21  PHE C CD1   1 
ATOM   8258  C CD2   . PHE C 1 21  ? 14.417  25.733  -1.416  1.00 53.98  ? 21  PHE C CD2   1 
ATOM   8259  C CE1   . PHE C 1 21  ? 13.541  23.606  0.089   1.00 51.03  ? 21  PHE C CE1   1 
ATOM   8260  C CE2   . PHE C 1 21  ? 14.092  24.529  -2.026  1.00 51.66  ? 21  PHE C CE2   1 
ATOM   8261  C CZ    . PHE C 1 21  ? 13.661  23.468  -1.270  1.00 53.97  ? 21  PHE C CZ    1 
ATOM   8262  N N     . ALA C 1 22  ? 14.195  29.876  2.125   1.00 76.54  ? 22  ALA C N     1 
ATOM   8263  C CA    . ALA C 1 22  ? 14.732  31.182  2.472   1.00 72.41  ? 22  ALA C CA    1 
ATOM   8264  C C     . ALA C 1 22  ? 14.513  31.498  3.951   1.00 66.36  ? 22  ALA C C     1 
ATOM   8265  O O     . ALA C 1 22  ? 15.319  32.229  4.518   1.00 69.87  ? 22  ALA C O     1 
ATOM   8266  C CB    . ALA C 1 22  ? 14.099  32.238  1.607   1.00 83.13  ? 22  ALA C CB    1 
ATOM   8267  N N     . ARG C 1 23  ? 13.433  30.966  4.554   1.00 69.60  ? 23  ARG C N     1 
ATOM   8268  C CA    . ARG C 1 23  ? 13.204  31.078  5.993   1.00 81.34  ? 23  ARG C CA    1 
ATOM   8269  C C     . ARG C 1 23  ? 14.146  30.170  6.784   1.00 76.59  ? 23  ARG C C     1 
ATOM   8270  O O     . ARG C 1 23  ? 14.229  30.310  8.008   1.00 71.14  ? 23  ARG C O     1 
ATOM   8271  C CB    . ARG C 1 23  ? 11.781  30.680  6.411   1.00 90.08  ? 23  ARG C CB    1 
ATOM   8272  C CG    . ARG C 1 23  ? 10.716  31.725  6.116   1.00 112.35 ? 23  ARG C CG    1 
ATOM   8273  C CD    . ARG C 1 23  ? 9.569   31.688  7.115   1.00 123.45 ? 23  ARG C CD    1 
ATOM   8274  N NE    . ARG C 1 23  ? 9.837   32.453  8.334   1.00 125.62 ? 23  ARG C NE    1 
ATOM   8275  C CZ    . ARG C 1 23  ? 9.392   32.143  9.552   1.00 117.92 ? 23  ARG C CZ    1 
ATOM   8276  N NH1   . ARG C 1 23  ? 8.700   31.036  9.759   1.00 118.97 ? 23  ARG C NH1   1 
ATOM   8277  N NH2   . ARG C 1 23  ? 9.637   32.948  10.570  1.00 105.51 ? 23  ARG C NH2   1 
ATOM   8278  N N     . ILE C 1 24  ? 14.782  29.211  6.085   1.00 68.22  ? 24  ILE C N     1 
ATOM   8279  C CA    . ILE C 1 24  ? 15.665  28.233  6.697   1.00 58.08  ? 24  ILE C CA    1 
ATOM   8280  C C     . ILE C 1 24  ? 17.100  28.741  6.699   1.00 52.33  ? 24  ILE C C     1 
ATOM   8281  O O     . ILE C 1 24  ? 17.755  28.613  7.735   1.00 59.95  ? 24  ILE C O     1 
ATOM   8282  C CB    . ILE C 1 24  ? 15.566  26.857  6.013   1.00 56.00  ? 24  ILE C CB    1 
ATOM   8283  C CG1   . ILE C 1 24  ? 14.336  26.086  6.493   1.00 49.87  ? 24  ILE C CG1   1 
ATOM   8284  C CG2   . ILE C 1 24  ? 16.848  26.062  6.240   1.00 54.52  ? 24  ILE C CG2   1 
ATOM   8285  C CD1   . ILE C 1 24  ? 13.936  24.951  5.564   1.00 52.44  ? 24  ILE C CD1   1 
ATOM   8286  N N     . VAL C 1 25  ? 17.560  29.299  5.563   1.00 51.09  ? 25  VAL C N     1 
ATOM   8287  C CA    . VAL C 1 25  ? 18.956  29.686  5.368   1.00 54.13  ? 25  VAL C CA    1 
ATOM   8288  C C     . VAL C 1 25  ? 19.119  31.202  5.331   1.00 61.14  ? 25  VAL C C     1 
ATOM   8289  O O     . VAL C 1 25  ? 20.250  31.677  5.203   1.00 65.16  ? 25  VAL C O     1 
ATOM   8290  C CB    . VAL C 1 25  ? 19.540  29.090  4.070   1.00 60.25  ? 25  VAL C CB    1 
ATOM   8291  C CG1   . VAL C 1 25  ? 19.506  27.567  4.072   1.00 62.78  ? 25  VAL C CG1   1 
ATOM   8292  C CG2   . VAL C 1 25  ? 18.845  29.629  2.824   1.00 59.23  ? 25  VAL C CG2   1 
ATOM   8293  N N     . GLY C 1 26  ? 18.000  31.947  5.374   1.00 73.23  ? 26  GLY C N     1 
ATOM   8294  C CA    . GLY C 1 26  ? 17.999  33.385  5.130   1.00 79.99  ? 26  GLY C CA    1 
ATOM   8295  C C     . GLY C 1 26  ? 17.793  33.716  3.649   1.00 86.50  ? 26  GLY C C     1 
ATOM   8296  O O     . GLY C 1 26  ? 18.268  33.001  2.763   1.00 73.85  ? 26  GLY C O     1 
ATOM   8297  N N     . ALA C 1 27  ? 17.094  34.825  3.383   1.00 86.28  ? 27  ALA C N     1 
ATOM   8298  C CA    . ALA C 1 27  ? 16.719  35.172  2.019   1.00 80.55  ? 27  ALA C CA    1 
ATOM   8299  C C     . ALA C 1 27  ? 17.949  35.478  1.165   1.00 66.42  ? 27  ALA C C     1 
ATOM   8300  O O     . ALA C 1 27  ? 17.869  35.391  -0.054  1.00 66.94  ? 27  ALA C O     1 
ATOM   8301  C CB    . ALA C 1 27  ? 15.737  36.324  2.018   1.00 83.76  ? 27  ALA C CB    1 
ATOM   8302  N N     . ASP C 1 28  ? 19.093  35.782  1.791   1.00 62.72  ? 28  ASP C N     1 
ATOM   8303  C CA    . ASP C 1 28  ? 20.320  36.100  1.062   1.00 76.98  ? 28  ASP C CA    1 
ATOM   8304  C C     . ASP C 1 28  ? 20.883  34.925  0.241   1.00 77.67  ? 28  ASP C C     1 
ATOM   8305  O O     . ASP C 1 28  ? 21.758  35.124  -0.608  1.00 85.32  ? 28  ASP C O     1 
ATOM   8306  C CB    . ASP C 1 28  ? 21.424  36.572  2.019   1.00 84.61  ? 28  ASP C CB    1 
ATOM   8307  C CG    . ASP C 1 28  ? 21.559  38.080  2.134   1.00 87.57  ? 28  ASP C CG    1 
ATOM   8308  O OD1   . ASP C 1 28  ? 21.848  38.719  1.105   1.00 83.89  ? 28  ASP C OD1   1 
ATOM   8309  O OD2   . ASP C 1 28  ? 21.399  38.594  3.255   1.00 89.97  ? 28  ASP C OD2   1 
ATOM   8310  N N     . TRP C 1 29  ? 20.421  33.698  0.510   1.00 73.64  ? 29  TRP C N     1 
ATOM   8311  C CA    . TRP C 1 29  ? 21.111  32.493  0.074   1.00 71.73  ? 29  TRP C CA    1 
ATOM   8312  C C     . TRP C 1 29  ? 20.173  31.606  -0.743  1.00 73.81  ? 29  TRP C C     1 
ATOM   8313  O O     . TRP C 1 29  ? 20.376  30.397  -0.811  1.00 64.97  ? 29  TRP C O     1 
ATOM   8314  C CB    . TRP C 1 29  ? 21.682  31.751  1.298   1.00 66.36  ? 29  TRP C CB    1 
ATOM   8315  C CG    . TRP C 1 29  ? 22.668  32.540  2.111   1.00 53.19  ? 29  TRP C CG    1 
ATOM   8316  C CD1   . TRP C 1 29  ? 22.490  33.033  3.375   1.00 53.98  ? 29  TRP C CD1   1 
ATOM   8317  C CD2   . TRP C 1 29  ? 23.988  32.940  1.703   1.00 49.11  ? 29  TRP C CD2   1 
ATOM   8318  N NE1   . TRP C 1 29  ? 23.605  33.718  3.779   1.00 53.81  ? 29  TRP C NE1   1 
ATOM   8319  C CE2   . TRP C 1 29  ? 24.537  33.680  2.773   1.00 48.91  ? 29  TRP C CE2   1 
ATOM   8320  C CE3   . TRP C 1 29  ? 24.742  32.772  0.530   1.00 52.77  ? 29  TRP C CE3   1 
ATOM   8321  C CZ2   . TRP C 1 29  ? 25.816  34.228  2.710   1.00 52.10  ? 29  TRP C CZ2   1 
ATOM   8322  C CZ3   . TRP C 1 29  ? 26.012  33.306  0.475   1.00 55.25  ? 29  TRP C CZ3   1 
ATOM   8323  C CH2   . TRP C 1 29  ? 26.538  34.024  1.554   1.00 53.50  ? 29  TRP C CH2   1 
ATOM   8324  N N     . VAL C 1 30  ? 19.142  32.230  -1.328  1.00 76.87  ? 30  VAL C N     1 
ATOM   8325  C CA    . VAL C 1 30  ? 18.258  31.598  -2.293  1.00 73.64  ? 30  VAL C CA    1 
ATOM   8326  C C     . VAL C 1 30  ? 18.395  32.342  -3.619  1.00 77.58  ? 30  VAL C C     1 
ATOM   8327  O O     . VAL C 1 30  ? 17.784  33.387  -3.796  1.00 90.66  ? 30  VAL C O     1 
ATOM   8328  C CB    . VAL C 1 30  ? 16.805  31.614  -1.789  1.00 62.60  ? 30  VAL C CB    1 
ATOM   8329  C CG1   . VAL C 1 30  ? 15.852  31.010  -2.811  1.00 62.99  ? 30  VAL C CG1   1 
ATOM   8330  C CG2   . VAL C 1 30  ? 16.676  30.914  -0.444  1.00 61.49  ? 30  VAL C CG2   1 
ATOM   8331  N N     . PHE C 1 31  ? 19.206  31.810  -4.540  1.00 78.39  ? 31  PHE C N     1 
ATOM   8332  C CA    . PHE C 1 31  ? 19.514  32.499  -5.779  1.00 77.83  ? 31  PHE C CA    1 
ATOM   8333  C C     . PHE C 1 31  ? 18.562  32.049  -6.885  1.00 92.35  ? 31  PHE C C     1 
ATOM   8334  O O     . PHE C 1 31  ? 18.610  30.890  -7.292  1.00 99.36  ? 31  PHE C O     1 
ATOM   8335  C CB    . PHE C 1 31  ? 20.961  32.237  -6.196  1.00 78.28  ? 31  PHE C CB    1 
ATOM   8336  C CG    . PHE C 1 31  ? 21.978  32.390  -5.098  1.00 90.09  ? 31  PHE C CG    1 
ATOM   8337  C CD1   . PHE C 1 31  ? 22.016  33.529  -4.312  1.00 90.30  ? 31  PHE C CD1   1 
ATOM   8338  C CD2   . PHE C 1 31  ? 22.901  31.385  -4.852  1.00 104.45 ? 31  PHE C CD2   1 
ATOM   8339  C CE1   . PHE C 1 31  ? 22.963  33.664  -3.310  1.00 93.10  ? 31  PHE C CE1   1 
ATOM   8340  C CE2   . PHE C 1 31  ? 23.844  31.521  -3.848  1.00 106.61 ? 31  PHE C CE2   1 
ATOM   8341  C CZ    . PHE C 1 31  ? 23.874  32.662  -3.080  1.00 103.49 ? 31  PHE C CZ    1 
ATOM   8342  N N     . THR C 1 32  ? 17.721  32.984  -7.369  1.00 106.49 ? 32  THR C N     1 
ATOM   8343  C CA    . THR C 1 32  ? 16.847  32.775  -8.521  1.00 103.69 ? 32  THR C CA    1 
ATOM   8344  C C     . THR C 1 32  ? 17.258  33.704  -9.664  1.00 106.56 ? 32  THR C C     1 
ATOM   8345  O O     . THR C 1 32  ? 18.445  34.001  -9.824  1.00 100.31 ? 32  THR C O     1 
ATOM   8346  C CB    . THR C 1 32  ? 15.370  33.018  -8.174  1.00 97.87  ? 32  THR C CB    1 
ATOM   8347  O OG1   . THR C 1 32  ? 15.261  34.374  -7.741  1.00 94.25  ? 32  THR C OG1   1 
ATOM   8348  C CG2   . THR C 1 32  ? 14.818  32.080  -7.124  1.00 95.68  ? 32  THR C CG2   1 
ATOM   8349  N N     . GLU C 1 33  ? 16.256  34.119  -10.463 1.00 116.46 ? 33  GLU C N     1 
ATOM   8350  C CA    . GLU C 1 33  ? 16.387  35.137  -11.496 1.00 123.82 ? 33  GLU C CA    1 
ATOM   8351  C C     . GLU C 1 33  ? 17.581  34.781  -12.386 1.00 128.29 ? 33  GLU C C     1 
ATOM   8352  O O     . GLU C 1 33  ? 17.530  33.757  -13.064 1.00 109.83 ? 33  GLU C O     1 
ATOM   8353  C CB    . GLU C 1 33  ? 16.438  36.533  -10.862 1.00 124.34 ? 33  GLU C CB    1 
ATOM   8354  C CG    . GLU C 1 33  ? 16.097  37.653  -11.837 1.00 127.41 ? 33  GLU C CG    1 
ATOM   8355  C CD    . GLU C 1 33  ? 16.791  38.985  -11.586 1.00 123.43 ? 33  GLU C CD    1 
ATOM   8356  O OE1   . GLU C 1 33  ? 18.036  38.979  -11.464 1.00 109.96 ? 33  GLU C OE1   1 
ATOM   8357  O OE2   . GLU C 1 33  ? 16.092  40.031  -11.549 1.00 101.11 ? 33  GLU C OE2   1 
ATOM   8358  N N     . ASP C 1 34  ? 18.646  35.605  -12.359 1.00 134.60 ? 34  ASP C N     1 
ATOM   8359  C CA    . ASP C 1 34  ? 19.811  35.440  -13.219 1.00 134.14 ? 34  ASP C CA    1 
ATOM   8360  C C     . ASP C 1 34  ? 21.094  35.509  -12.384 1.00 128.07 ? 34  ASP C C     1 
ATOM   8361  O O     . ASP C 1 34  ? 22.121  35.990  -12.864 1.00 119.97 ? 34  ASP C O     1 
ATOM   8362  C CB    . ASP C 1 34  ? 19.817  36.483  -14.346 1.00 128.49 ? 34  ASP C CB    1 
ATOM   8363  N N     . LYS C 1 35  ? 21.028  35.015  -11.136 1.00 118.95 ? 35  LYS C N     1 
ATOM   8364  C CA    . LYS C 1 35  ? 22.216  34.733  -10.344 1.00 110.88 ? 35  LYS C CA    1 
ATOM   8365  C C     . LYS C 1 35  ? 22.536  33.232  -10.439 1.00 117.68 ? 35  LYS C C     1 
ATOM   8366  O O     . LYS C 1 35  ? 23.458  32.751  -9.781  1.00 99.78  ? 35  LYS C O     1 
ATOM   8367  C CB    . LYS C 1 35  ? 22.003  35.252  -8.916  1.00 95.51  ? 35  LYS C CB    1 
ATOM   8368  N N     . ILE C 1 36  ? 21.812  32.523  -11.330 1.00 122.65 ? 36  ILE C N     1 
ATOM   8369  C CA    . ILE C 1 36  ? 21.898  31.079  -11.524 1.00 109.68 ? 36  ILE C CA    1 
ATOM   8370  C C     . ILE C 1 36  ? 22.819  30.753  -12.710 1.00 103.98 ? 36  ILE C C     1 
ATOM   8371  O O     . ILE C 1 36  ? 22.730  29.666  -13.278 1.00 102.65 ? 36  ILE C O     1 
ATOM   8372  C CB    . ILE C 1 36  ? 20.472  30.504  -11.719 1.00 105.77 ? 36  ILE C CB    1 
ATOM   8373  C CG1   . ILE C 1 36  ? 20.379  28.996  -11.459 1.00 109.55 ? 36  ILE C CG1   1 
ATOM   8374  C CG2   . ILE C 1 36  ? 19.912  30.855  -13.093 1.00 100.52 ? 36  ILE C CG2   1 
ATOM   8375  C CD1   . ILE C 1 36  ? 20.628  28.588  -10.025 1.00 112.08 ? 36  ILE C CD1   1 
ATOM   8376  N N     . THR C 1 37  ? 23.708  31.683  -13.091 1.00 104.41 ? 37  THR C N     1 
ATOM   8377  C CA    . THR C 1 37  ? 24.588  31.473  -14.237 1.00 114.04 ? 37  THR C CA    1 
ATOM   8378  C C     . THR C 1 37  ? 25.910  30.798  -13.834 1.00 112.60 ? 37  THR C C     1 
ATOM   8379  O O     . THR C 1 37  ? 26.450  30.038  -14.644 1.00 83.99  ? 37  THR C O     1 
ATOM   8380  C CB    . THR C 1 37  ? 24.777  32.756  -15.067 1.00 110.54 ? 37  THR C CB    1 
ATOM   8381  O OG1   . THR C 1 37  ? 24.781  33.890  -14.200 1.00 115.39 ? 37  THR C OG1   1 
ATOM   8382  C CG2   . THR C 1 37  ? 23.694  32.944  -16.110 1.00 106.57 ? 37  THR C CG2   1 
ATOM   8383  N N     . PRO C 1 38  ? 26.483  31.000  -12.611 1.00 110.65 ? 38  PRO C N     1 
ATOM   8384  C CA    . PRO C 1 38  ? 27.666  30.237  -12.183 1.00 100.43 ? 38  PRO C CA    1 
ATOM   8385  C C     . PRO C 1 38  ? 27.425  28.739  -11.950 1.00 97.27  ? 38  PRO C C     1 
ATOM   8386  O O     . PRO C 1 38  ? 28.386  27.991  -11.767 1.00 79.82  ? 38  PRO C O     1 
ATOM   8387  C CB    . PRO C 1 38  ? 28.103  30.875  -10.849 1.00 101.74 ? 38  PRO C CB    1 
ATOM   8388  C CG    . PRO C 1 38  ? 27.309  32.170  -10.737 1.00 104.96 ? 38  PRO C CG    1 
ATOM   8389  C CD    . PRO C 1 38  ? 26.070  31.983  -11.592 1.00 103.79 ? 38  PRO C CD    1 
ATOM   8390  N N     . TYR C 1 39  ? 26.146  28.314  -11.932 1.00 101.35 ? 39  TYR C N     1 
ATOM   8391  C CA    . TYR C 1 39  ? 25.776  26.913  -11.753 1.00 106.92 ? 39  TYR C CA    1 
ATOM   8392  C C     . TYR C 1 39  ? 25.443  26.255  -13.094 1.00 98.13  ? 39  TYR C C     1 
ATOM   8393  O O     . TYR C 1 39  ? 25.062  25.086  -13.115 1.00 75.22  ? 39  TYR C O     1 
ATOM   8394  C CB    . TYR C 1 39  ? 24.601  26.775  -10.778 1.00 102.53 ? 39  TYR C CB    1 
ATOM   8395  C CG    . TYR C 1 39  ? 24.861  27.393  -9.428  1.00 101.43 ? 39  TYR C CG    1 
ATOM   8396  C CD1   . TYR C 1 39  ? 25.731  26.811  -8.520  1.00 99.92  ? 39  TYR C CD1   1 
ATOM   8397  C CD2   . TYR C 1 39  ? 24.294  28.608  -9.086  1.00 97.56  ? 39  TYR C CD2   1 
ATOM   8398  C CE1   . TYR C 1 39  ? 25.991  27.399  -7.289  1.00 101.18 ? 39  TYR C CE1   1 
ATOM   8399  C CE2   . TYR C 1 39  ? 24.545  29.209  -7.864  1.00 103.49 ? 39  TYR C CE2   1 
ATOM   8400  C CZ    . TYR C 1 39  ? 25.395  28.602  -6.960  1.00 98.37  ? 39  TYR C CZ    1 
ATOM   8401  O OH    . TYR C 1 39  ? 25.621  29.220  -5.760  1.00 97.98  ? 39  TYR C OH    1 
ATOM   8402  N N     . GLU C 1 40  ? 25.621  26.998  -14.200 1.00 102.55 ? 40  GLU C N     1 
ATOM   8403  C CA    . GLU C 1 40  ? 25.454  26.457  -15.542 1.00 102.54 ? 40  GLU C CA    1 
ATOM   8404  C C     . GLU C 1 40  ? 26.580  25.474  -15.862 1.00 104.21 ? 40  GLU C C     1 
ATOM   8405  O O     . GLU C 1 40  ? 27.621  25.440  -15.196 1.00 94.91  ? 40  GLU C O     1 
ATOM   8406  C CB    . GLU C 1 40  ? 25.465  27.552  -16.618 1.00 96.33  ? 40  GLU C CB    1 
ATOM   8407  C CG    . GLU C 1 40  ? 24.391  28.613  -16.452 1.00 103.57 ? 40  GLU C CG    1 
ATOM   8408  C CD    . GLU C 1 40  ? 22.937  28.179  -16.577 1.00 97.22  ? 40  GLU C CD    1 
ATOM   8409  O OE1   . GLU C 1 40  ? 22.669  27.011  -16.966 1.00 78.42  ? 40  GLU C OE1   1 
ATOM   8410  O OE2   . GLU C 1 40  ? 22.066  29.023  -16.268 1.00 89.08  ? 40  GLU C OE2   1 
ATOM   8411  N N     . ASP C 1 41  ? 26.328  24.678  -16.905 1.00 104.76 ? 41  ASP C N     1 
ATOM   8412  C CA    . ASP C 1 41  ? 27.333  23.864  -17.566 1.00 114.28 ? 41  ASP C CA    1 
ATOM   8413  C C     . ASP C 1 41  ? 28.289  24.795  -18.329 1.00 119.04 ? 41  ASP C C     1 
ATOM   8414  O O     . ASP C 1 41  ? 27.906  25.321  -19.377 1.00 119.22 ? 41  ASP C O     1 
ATOM   8415  C CB    . ASP C 1 41  ? 26.587  22.856  -18.452 1.00 109.45 ? 41  ASP C CB    1 
ATOM   8416  C CG    . ASP C 1 41  ? 27.401  21.686  -18.972 1.00 98.22  ? 41  ASP C CG    1 
ATOM   8417  O OD1   . ASP C 1 41  ? 28.627  21.643  -18.700 1.00 82.31  ? 41  ASP C OD1   1 
ATOM   8418  O OD2   . ASP C 1 41  ? 26.789  20.825  -19.650 1.00 90.76  ? 41  ASP C OD2   1 
ATOM   8419  N N     . PRO C 1 42  ? 29.538  25.066  -17.846 1.00 117.87 ? 42  PRO C N     1 
ATOM   8420  C CA    . PRO C 1 42  ? 30.463  25.967  -18.552 1.00 112.81 ? 42  PRO C CA    1 
ATOM   8421  C C     . PRO C 1 42  ? 31.014  25.407  -19.872 1.00 120.69 ? 42  PRO C C     1 
ATOM   8422  O O     . PRO C 1 42  ? 31.328  26.184  -20.777 1.00 102.54 ? 42  PRO C O     1 
ATOM   8423  C CB    . PRO C 1 42  ? 31.603  26.193  -17.543 1.00 104.78 ? 42  PRO C CB    1 
ATOM   8424  C CG    . PRO C 1 42  ? 31.598  24.938  -16.688 1.00 112.19 ? 42  PRO C CG    1 
ATOM   8425  C CD    . PRO C 1 42  ? 30.143  24.515  -16.617 1.00 115.19 ? 42  PRO C CD    1 
ATOM   8426  N N     . TYR C 1 43  ? 31.117  24.062  -19.959 1.00 131.33 ? 43  TYR C N     1 
ATOM   8427  C CA    . TYR C 1 43  ? 31.556  23.330  -21.147 1.00 119.97 ? 43  TYR C CA    1 
ATOM   8428  C C     . TYR C 1 43  ? 30.344  22.684  -21.837 1.00 108.65 ? 43  TYR C C     1 
ATOM   8429  O O     . TYR C 1 43  ? 30.134  21.475  -21.719 1.00 115.15 ? 43  TYR C O     1 
ATOM   8430  C CB    . TYR C 1 43  ? 32.627  22.287  -20.771 1.00 115.66 ? 43  TYR C CB    1 
ATOM   8431  C CG    . TYR C 1 43  ? 33.899  22.812  -20.133 1.00 103.44 ? 43  TYR C CG    1 
ATOM   8432  C CD1   . TYR C 1 43  ? 34.244  24.159  -20.195 1.00 104.46 ? 43  TYR C CD1   1 
ATOM   8433  C CD2   . TYR C 1 43  ? 34.768  21.966  -19.453 1.00 85.87  ? 43  TYR C CD2   1 
ATOM   8434  C CE1   . TYR C 1 43  ? 35.406  24.646  -19.615 1.00 93.90  ? 43  TYR C CE1   1 
ATOM   8435  C CE2   . TYR C 1 43  ? 35.927  22.441  -18.854 1.00 84.38  ? 43  TYR C CE2   1 
ATOM   8436  C CZ    . TYR C 1 43  ? 36.246  23.789  -18.931 1.00 87.37  ? 43  TYR C CZ    1 
ATOM   8437  O OH    . TYR C 1 43  ? 37.381  24.330  -18.376 1.00 72.62  ? 43  TYR C OH    1 
ATOM   8438  N N     . THR C 1 44  ? 29.574  23.503  -22.581 1.00 103.64 ? 44  THR C N     1 
ATOM   8439  C CA    . THR C 1 44  ? 28.311  23.107  -23.204 1.00 107.94 ? 44  THR C CA    1 
ATOM   8440  C C     . THR C 1 44  ? 28.554  22.104  -24.339 1.00 93.08  ? 44  THR C C     1 
ATOM   8441  O O     . THR C 1 44  ? 29.445  22.299  -25.160 1.00 100.58 ? 44  THR C O     1 
ATOM   8442  C CB    . THR C 1 44  ? 27.501  24.322  -23.715 1.00 112.52 ? 44  THR C CB    1 
ATOM   8443  O OG1   . THR C 1 44  ? 28.377  25.322  -24.242 1.00 96.89  ? 44  THR C OG1   1 
ATOM   8444  C CG2   . THR C 1 44  ? 26.632  24.973  -22.656 1.00 109.51 ? 44  THR C CG2   1 
ATOM   8445  N N     . ILE C 1 45  ? 27.744  21.031  -24.367 1.00 85.20  ? 45  ILE C N     1 
ATOM   8446  C CA    . ILE C 1 45  ? 27.784  20.006  -25.406 1.00 92.03  ? 45  ILE C CA    1 
ATOM   8447  C C     . ILE C 1 45  ? 26.446  19.986  -26.151 1.00 87.15  ? 45  ILE C C     1 
ATOM   8448  O O     . ILE C 1 45  ? 26.419  19.752  -27.360 1.00 85.24  ? 45  ILE C O     1 
ATOM   8449  C CB    . ILE C 1 45  ? 28.121  18.607  -24.834 1.00 93.59  ? 45  ILE C CB    1 
ATOM   8450  C CG1   . ILE C 1 45  ? 29.372  18.608  -23.948 1.00 83.45  ? 45  ILE C CG1   1 
ATOM   8451  C CG2   . ILE C 1 45  ? 28.235  17.581  -25.958 1.00 89.44  ? 45  ILE C CG2   1 
ATOM   8452  C CD1   . ILE C 1 45  ? 29.638  17.296  -23.262 1.00 77.15  ? 45  ILE C CD1   1 
ATOM   8453  N N     . SER C 1 46  ? 25.340  20.206  -25.422 1.00 87.56  ? 46  SER C N     1 
ATOM   8454  C CA    . SER C 1 46  ? 24.004  20.210  -26.005 1.00 98.52  ? 46  SER C CA    1 
ATOM   8455  C C     . SER C 1 46  ? 23.760  21.511  -26.778 1.00 102.01 ? 46  SER C C     1 
ATOM   8456  O O     . SER C 1 46  ? 24.280  22.560  -26.394 1.00 98.04  ? 46  SER C O     1 
ATOM   8457  C CB    . SER C 1 46  ? 22.968  19.995  -24.925 1.00 101.50 ? 46  SER C CB    1 
ATOM   8458  O OG    . SER C 1 46  ? 21.784  19.422  -25.459 1.00 99.06  ? 46  SER C OG    1 
ATOM   8459  N N     . ASN C 1 47  ? 22.975  21.429  -27.871 1.00 101.66 ? 47  ASN C N     1 
ATOM   8460  C CA    . ASN C 1 47  ? 22.613  22.586  -28.687 1.00 108.56 ? 47  ASN C CA    1 
ATOM   8461  C C     . ASN C 1 47  ? 21.220  23.107  -28.312 1.00 117.81 ? 47  ASN C C     1 
ATOM   8462  O O     . ASN C 1 47  ? 20.891  24.261  -28.605 1.00 103.63 ? 47  ASN C O     1 
ATOM   8463  C CB    . ASN C 1 47  ? 22.666  22.287  -30.191 1.00 103.58 ? 47  ASN C CB    1 
ATOM   8464  C CG    . ASN C 1 47  ? 24.048  21.921  -30.696 1.00 96.68  ? 47  ASN C CG    1 
ATOM   8465  O OD1   . ASN C 1 47  ? 24.953  21.638  -29.915 1.00 100.93 ? 47  ASN C OD1   1 
ATOM   8466  N ND2   . ASN C 1 47  ? 24.222  21.900  -32.007 1.00 85.72  ? 47  ASN C ND2   1 
ATOM   8467  N N     . ASP C 1 48  ? 20.409  22.246  -27.677 1.00 117.07 ? 48  ASP C N     1 
ATOM   8468  C CA    . ASP C 1 48  ? 19.087  22.597  -27.173 1.00 124.69 ? 48  ASP C CA    1 
ATOM   8469  C C     . ASP C 1 48  ? 19.241  23.150  -25.755 1.00 121.23 ? 48  ASP C C     1 
ATOM   8470  O O     . ASP C 1 48  ? 19.456  22.377  -24.826 1.00 120.71 ? 48  ASP C O     1 
ATOM   8471  C CB    . ASP C 1 48  ? 18.179  21.360  -27.246 1.00 122.14 ? 48  ASP C CB    1 
ATOM   8472  C CG    . ASP C 1 48  ? 16.740  21.551  -26.794 1.00 116.26 ? 48  ASP C CG    1 
ATOM   8473  O OD1   . ASP C 1 48  ? 16.489  21.465  -25.575 1.00 97.75  ? 48  ASP C OD1   1 
ATOM   8474  O OD2   . ASP C 1 48  ? 15.876  21.768  -27.672 1.00 118.52 ? 48  ASP C OD2   1 
ATOM   8475  N N     . GLU C 1 49  ? 19.132  24.480  -25.589 1.00 117.05 ? 49  GLU C N     1 
ATOM   8476  C CA    . GLU C 1 49  ? 19.464  25.138  -24.329 1.00 117.51 ? 49  GLU C CA    1 
ATOM   8477  C C     . GLU C 1 49  ? 18.245  25.152  -23.402 1.00 123.59 ? 49  GLU C C     1 
ATOM   8478  O O     . GLU C 1 49  ? 17.924  26.188  -22.818 1.00 127.93 ? 49  GLU C O     1 
ATOM   8479  C CB    . GLU C 1 49  ? 20.021  26.542  -24.589 1.00 108.44 ? 49  GLU C CB    1 
ATOM   8480  N N     . THR C 1 50  ? 17.580  23.987  -23.276 1.00 126.79 ? 50  THR C N     1 
ATOM   8481  C CA    . THR C 1 50  ? 16.571  23.722  -22.253 1.00 118.94 ? 50  THR C CA    1 
ATOM   8482  C C     . THR C 1 50  ? 16.950  22.483  -21.422 1.00 114.71 ? 50  THR C C     1 
ATOM   8483  O O     . THR C 1 50  ? 16.160  22.042  -20.584 1.00 95.98  ? 50  THR C O     1 
ATOM   8484  C CB    . THR C 1 50  ? 15.168  23.592  -22.879 1.00 110.75 ? 50  THR C CB    1 
ATOM   8485  O OG1   . THR C 1 50  ? 15.102  22.435  -23.720 1.00 90.04  ? 50  THR C OG1   1 
ATOM   8486  C CG2   . THR C 1 50  ? 14.763  24.810  -23.686 1.00 103.35 ? 50  THR C CG2   1 
ATOM   8487  N N     . GLU C 1 51  ? 18.165  21.936  -21.646 1.00 119.17 ? 51  GLU C N     1 
ATOM   8488  C CA    . GLU C 1 51  ? 18.711  20.804  -20.899 1.00 118.40 ? 51  GLU C CA    1 
ATOM   8489  C C     . GLU C 1 51  ? 19.840  21.305  -19.991 1.00 114.69 ? 51  GLU C C     1 
ATOM   8490  O O     . GLU C 1 51  ? 20.549  22.240  -20.372 1.00 100.08 ? 51  GLU C O     1 
ATOM   8491  C CB    . GLU C 1 51  ? 19.267  19.715  -21.833 1.00 109.75 ? 51  GLU C CB    1 
ATOM   8492  C CG    . GLU C 1 51  ? 18.445  19.463  -23.092 1.00 97.47  ? 51  GLU C CG    1 
ATOM   8493  C CD    . GLU C 1 51  ? 18.903  18.310  -23.978 1.00 91.42  ? 51  GLU C CD    1 
ATOM   8494  O OE1   . GLU C 1 51  ? 20.118  18.207  -24.273 1.00 85.81  ? 51  GLU C OE1   1 
ATOM   8495  O OE2   . GLU C 1 51  ? 18.036  17.513  -24.387 1.00 80.85  ? 51  GLU C OE2   1 
ATOM   8496  N N     . HIS C 1 52  ? 19.995  20.677  -18.806 1.00 109.40 ? 52  HIS C N     1 
ATOM   8497  C CA    . HIS C 1 52  ? 21.006  21.030  -17.801 1.00 108.52 ? 52  HIS C CA    1 
ATOM   8498  C C     . HIS C 1 52  ? 20.958  22.523  -17.428 1.00 112.43 ? 52  HIS C C     1 
ATOM   8499  O O     . HIS C 1 52  ? 22.019  23.148  -17.298 1.00 103.55 ? 52  HIS C O     1 
ATOM   8500  C CB    . HIS C 1 52  ? 22.397  20.501  -18.203 1.00 91.02  ? 52  HIS C CB    1 
ATOM   8501  C CG    . HIS C 1 52  ? 22.257  19.261  -18.995 1.00 87.56  ? 52  HIS C CG    1 
ATOM   8502  N ND1   . HIS C 1 52  ? 22.872  19.022  -20.203 1.00 104.58 ? 52  HIS C ND1   1 
ATOM   8503  C CD2   . HIS C 1 52  ? 21.442  18.231  -18.778 1.00 90.75  ? 52  HIS C CD2   1 
ATOM   8504  C CE1   . HIS C 1 52  ? 22.454  17.853  -20.673 1.00 104.06 ? 52  HIS C CE1   1 
ATOM   8505  N NE2   . HIS C 1 52  ? 21.585  17.355  -19.818 1.00 93.86  ? 52  HIS C NE2   1 
ATOM   8506  N N     . ARG C 1 53  ? 19.721  23.042  -17.209 1.00 112.27 ? 53  ARG C N     1 
ATOM   8507  C CA    . ARG C 1 53  ? 19.413  24.431  -16.856 1.00 103.79 ? 53  ARG C CA    1 
ATOM   8508  C C     . ARG C 1 53  ? 18.699  24.483  -15.499 1.00 95.63  ? 53  ARG C C     1 
ATOM   8509  O O     . ARG C 1 53  ? 17.481  24.320  -15.433 1.00 103.44 ? 53  ARG C O     1 
ATOM   8510  C CB    . ARG C 1 53  ? 18.480  25.099  -17.881 1.00 96.34  ? 53  ARG C CB    1 
ATOM   8511  C CG    . ARG C 1 53  ? 18.821  24.873  -19.350 1.00 101.57 ? 53  ARG C CG    1 
ATOM   8512  C CD    . ARG C 1 53  ? 20.173  25.400  -19.816 1.00 100.99 ? 53  ARG C CD    1 
ATOM   8513  N NE    . ARG C 1 53  ? 20.376  26.797  -19.451 1.00 113.60 ? 53  ARG C NE    1 
ATOM   8514  C CZ    . ARG C 1 53  ? 19.916  27.839  -20.139 1.00 106.29 ? 53  ARG C CZ    1 
ATOM   8515  N NH1   . ARG C 1 53  ? 19.411  27.669  -21.348 1.00 111.11 ? 53  ARG C NH1   1 
ATOM   8516  N NH2   . ARG C 1 53  ? 19.995  29.053  -19.622 1.00 96.42  ? 53  ARG C NH2   1 
ATOM   8517  N N     . PRO C 1 54  ? 19.407  24.712  -14.367 1.00 72.41  ? 54  PRO C N     1 
ATOM   8518  C CA    . PRO C 1 54  ? 18.766  24.680  -13.047 1.00 59.76  ? 54  PRO C CA    1 
ATOM   8519  C C     . PRO C 1 54  ? 17.843  25.851  -12.717 1.00 62.04  ? 54  PRO C C     1 
ATOM   8520  O O     . PRO C 1 54  ? 18.094  26.971  -13.154 1.00 68.17  ? 54  PRO C O     1 
ATOM   8521  C CB    . PRO C 1 54  ? 19.964  24.640  -12.096 1.00 65.79  ? 54  PRO C CB    1 
ATOM   8522  C CG    . PRO C 1 54  ? 21.101  25.313  -12.862 1.00 70.42  ? 54  PRO C CG    1 
ATOM   8523  C CD    . PRO C 1 54  ? 20.861  24.932  -14.304 1.00 69.25  ? 54  PRO C CD    1 
ATOM   8524  N N     . TYR C 1 55  ? 16.801  25.581  -11.905 1.00 56.68  ? 55  TYR C N     1 
ATOM   8525  C CA    . TYR C 1 55  ? 15.731  26.538  -11.644 1.00 64.31  ? 55  TYR C CA    1 
ATOM   8526  C C     . TYR C 1 55  ? 16.069  27.532  -10.521 1.00 71.92  ? 55  TYR C C     1 
ATOM   8527  O O     . TYR C 1 55  ? 15.683  28.695  -10.600 1.00 69.32  ? 55  TYR C O     1 
ATOM   8528  C CB    . TYR C 1 55  ? 14.421  25.818  -11.315 1.00 66.03  ? 55  TYR C CB    1 
ATOM   8529  C CG    . TYR C 1 55  ? 13.246  26.756  -11.196 1.00 83.59  ? 55  TYR C CG    1 
ATOM   8530  C CD1   . TYR C 1 55  ? 13.040  27.504  -10.044 1.00 86.51  ? 55  TYR C CD1   1 
ATOM   8531  C CD2   . TYR C 1 55  ? 12.377  26.954  -12.260 1.00 91.77  ? 55  TYR C CD2   1 
ATOM   8532  C CE1   . TYR C 1 55  ? 11.985  28.394  -9.937  1.00 93.03  ? 55  TYR C CE1   1 
ATOM   8533  C CE2   . TYR C 1 55  ? 11.315  27.842  -12.169 1.00 90.64  ? 55  TYR C CE2   1 
ATOM   8534  C CZ    . TYR C 1 55  ? 11.120  28.564  -11.004 1.00 93.74  ? 55  TYR C CZ    1 
ATOM   8535  O OH    . TYR C 1 55  ? 10.078  29.451  -10.890 1.00 94.47  ? 55  TYR C OH    1 
ATOM   8536  N N     . ALA C 1 56  ? 16.707  27.064  -9.437  1.00 76.63  ? 56  ALA C N     1 
ATOM   8537  C CA    . ALA C 1 56  ? 17.148  27.923  -8.340  1.00 69.13  ? 56  ALA C CA    1 
ATOM   8538  C C     . ALA C 1 56  ? 18.407  27.330  -7.691  1.00 66.87  ? 56  ALA C C     1 
ATOM   8539  O O     . ALA C 1 56  ? 18.946  26.327  -8.149  1.00 57.91  ? 56  ALA C O     1 
ATOM   8540  C CB    . ALA C 1 56  ? 16.025  28.123  -7.345  1.00 57.96  ? 56  ALA C CB    1 
ATOM   8541  N N     . ALA C 1 57  ? 18.923  27.990  -6.655  1.00 60.94  ? 57  ALA C N     1 
ATOM   8542  C CA    . ALA C 1 57  ? 19.977  27.406  -5.844  1.00 57.91  ? 57  ALA C CA    1 
ATOM   8543  C C     . ALA C 1 57  ? 19.714  27.774  -4.394  1.00 60.67  ? 57  ALA C C     1 
ATOM   8544  O O     . ALA C 1 57  ? 19.129  28.821  -4.143  1.00 71.65  ? 57  ALA C O     1 
ATOM   8545  C CB    . ALA C 1 57  ? 21.331  27.875  -6.313  1.00 56.79  ? 57  ALA C CB    1 
ATOM   8546  N N     . VAL C 1 58  ? 20.103  26.893  -3.459  1.00 61.06  ? 58  VAL C N     1 
ATOM   8547  C CA    . VAL C 1 58  ? 19.991  27.157  -2.028  1.00 50.49  ? 58  VAL C CA    1 
ATOM   8548  C C     . VAL C 1 58  ? 21.334  26.827  -1.406  1.00 51.74  ? 58  VAL C C     1 
ATOM   8549  O O     . VAL C 1 58  ? 21.909  25.775  -1.692  1.00 60.97  ? 58  VAL C O     1 
ATOM   8550  C CB    . VAL C 1 58  ? 18.868  26.352  -1.360  1.00 51.44  ? 58  VAL C CB    1 
ATOM   8551  C CG1   . VAL C 1 58  ? 18.708  26.724  0.100   1.00 55.38  ? 58  VAL C CG1   1 
ATOM   8552  C CG2   . VAL C 1 58  ? 17.542  26.526  -2.075  1.00 56.46  ? 58  VAL C CG2   1 
ATOM   8553  N N     . ALA C 1 59  ? 21.846  27.735  -0.575  1.00 46.64  ? 59  ALA C N     1 
ATOM   8554  C CA    . ALA C 1 59  ? 23.176  27.542  -0.020  1.00 45.46  ? 59  ALA C CA    1 
ATOM   8555  C C     . ALA C 1 59  ? 23.113  27.493  1.502   1.00 43.02  ? 59  ALA C C     1 
ATOM   8556  O O     . ALA C 1 59  ? 23.287  28.521  2.137   1.00 49.65  ? 59  ALA C O     1 
ATOM   8557  C CB    . ALA C 1 59  ? 24.096  28.634  -0.495  1.00 44.97  ? 59  ALA C CB    1 
ATOM   8558  N N     . PRO C 1 60  ? 22.945  26.311  2.140   1.00 42.49  ? 60  PRO C N     1 
ATOM   8559  C CA    . PRO C 1 60  ? 22.831  26.227  3.600   1.00 43.01  ? 60  PRO C CA    1 
ATOM   8560  C C     . PRO C 1 60  ? 24.148  26.422  4.339   1.00 42.96  ? 60  PRO C C     1 
ATOM   8561  O O     . PRO C 1 60  ? 25.236  26.265  3.777   1.00 42.41  ? 60  PRO C O     1 
ATOM   8562  C CB    . PRO C 1 60  ? 22.297  24.807  3.830   1.00 47.83  ? 60  PRO C CB    1 
ATOM   8563  C CG    . PRO C 1 60  ? 22.875  24.020  2.671   1.00 50.71  ? 60  PRO C CG    1 
ATOM   8564  C CD    . PRO C 1 60  ? 22.895  24.988  1.503   1.00 47.45  ? 60  PRO C CD    1 
ATOM   8565  N N     . ALA C 1 61  ? 24.027  26.744  5.628   1.00 50.38  ? 61  ALA C N     1 
ATOM   8566  C CA    . ALA C 1 61  ? 25.184  27.029  6.471   1.00 46.37  ? 61  ALA C CA    1 
ATOM   8567  C C     . ALA C 1 61  ? 25.677  25.767  7.158   1.00 46.13  ? 61  ALA C C     1 
ATOM   8568  O O     . ALA C 1 61  ? 26.824  25.715  7.617   1.00 48.01  ? 61  ALA C O     1 
ATOM   8569  C CB    . ALA C 1 61  ? 24.815  28.036  7.515   1.00 48.93  ? 61  ALA C CB    1 
ATOM   8570  N N     . SER C 1 62  ? 24.809  24.755  7.236   1.00 42.86  ? 62  SER C N     1 
ATOM   8571  C CA    . SER C 1 62  ? 25.006  23.732  8.244   1.00 48.11  ? 62  SER C CA    1 
ATOM   8572  C C     . SER C 1 62  ? 24.300  22.441  7.867   1.00 45.37  ? 62  SER C C     1 
ATOM   8573  O O     . SER C 1 62  ? 23.363  22.439  7.082   1.00 54.73  ? 62  SER C O     1 
ATOM   8574  C CB    . SER C 1 62  ? 24.482  24.197  9.571   1.00 41.46  ? 62  SER C CB    1 
ATOM   8575  O OG    . SER C 1 62  ? 23.104  23.861  9.658   1.00 42.75  ? 62  SER C OG    1 
ATOM   8576  N N     . THR C 1 63  ? 24.717  21.365  8.528   1.00 43.79  ? 63  THR C N     1 
ATOM   8577  C CA    . THR C 1 63  ? 24.100  20.072  8.347   1.00 43.27  ? 63  THR C CA    1 
ATOM   8578  C C     . THR C 1 63  ? 22.608  20.185  8.633   1.00 51.04  ? 63  THR C C     1 
ATOM   8579  O O     . THR C 1 63  ? 21.792  19.685  7.859   1.00 43.27  ? 63  THR C O     1 
ATOM   8580  C CB    . THR C 1 63  ? 24.825  19.022  9.193   1.00 42.86  ? 63  THR C CB    1 
ATOM   8581  O OG1   . THR C 1 63  ? 26.146  18.883  8.659   1.00 46.17  ? 63  THR C OG1   1 
ATOM   8582  C CG2   . THR C 1 63  ? 24.131  17.680  9.205   1.00 39.82  ? 63  THR C CG2   1 
ATOM   8583  N N     . GLU C 1 64  ? 22.254  20.860  9.733   1.00 49.87  ? 64  GLU C N     1 
ATOM   8584  C CA    . GLU C 1 64  ? 20.866  20.856  10.168  1.00 46.37  ? 64  GLU C CA    1 
ATOM   8585  C C     . GLU C 1 64  ? 19.983  21.618  9.171   1.00 45.40  ? 64  GLU C C     1 
ATOM   8586  O O     . GLU C 1 64  ? 18.848  21.227  8.918   1.00 46.41  ? 64  GLU C O     1 
ATOM   8587  C CB    . GLU C 1 64  ? 20.748  21.434  11.582  1.00 45.34  ? 64  GLU C CB    1 
ATOM   8588  C CG    . GLU C 1 64  ? 19.518  20.933  12.321  1.00 47.21  ? 64  GLU C CG    1 
ATOM   8589  C CD    . GLU C 1 64  ? 18.138  21.447  11.902  1.00 43.47  ? 64  GLU C CD    1 
ATOM   8590  O OE1   . GLU C 1 64  ? 18.012  22.656  11.726  1.00 39.65  ? 64  GLU C OE1   1 
ATOM   8591  O OE2   . GLU C 1 64  ? 17.169  20.636  11.851  1.00 44.29  ? 64  GLU C OE2   1 
ATOM   8592  N N     . GLU C 1 65  ? 20.508  22.712  8.625   1.00 46.88  ? 65  GLU C N     1 
ATOM   8593  C CA    . GLU C 1 65  ? 19.871  23.456  7.550   1.00 49.62  ? 65  GLU C CA    1 
ATOM   8594  C C     . GLU C 1 65  ? 19.584  22.514  6.372   1.00 48.34  ? 65  GLU C C     1 
ATOM   8595  O O     . GLU C 1 65  ? 18.447  22.412  5.902   1.00 49.76  ? 65  GLU C O     1 
ATOM   8596  C CB    . GLU C 1 65  ? 20.740  24.682  7.206   1.00 50.08  ? 65  GLU C CB    1 
ATOM   8597  C CG    . GLU C 1 65  ? 20.356  25.943  7.979   1.00 47.23  ? 65  GLU C CG    1 
ATOM   8598  C CD    . GLU C 1 65  ? 21.223  27.193  7.867   1.00 51.30  ? 65  GLU C CD    1 
ATOM   8599  O OE1   . GLU C 1 65  ? 21.738  27.523  6.747   1.00 45.33  ? 65  GLU C OE1   1 
ATOM   8600  O OE2   . GLU C 1 65  ? 21.366  27.872  8.918   1.00 52.80  ? 65  GLU C OE2   1 
ATOM   8601  N N     . VAL C 1 66  ? 20.608  21.779  5.930   1.00 46.30  ? 66  VAL C N     1 
ATOM   8602  C CA    . VAL C 1 66  ? 20.458  20.788  4.866   1.00 43.43  ? 66  VAL C CA    1 
ATOM   8603  C C     . VAL C 1 66  ? 19.253  19.900  5.139   1.00 43.59  ? 66  VAL C C     1 
ATOM   8604  O O     . VAL C 1 66  ? 18.499  19.572  4.226   1.00 49.98  ? 66  VAL C O     1 
ATOM   8605  C CB    . VAL C 1 66  ? 21.735  19.936  4.688   1.00 40.98  ? 66  VAL C CB    1 
ATOM   8606  C CG1   . VAL C 1 66  ? 21.481  18.634  3.967   1.00 40.78  ? 66  VAL C CG1   1 
ATOM   8607  C CG2   . VAL C 1 66  ? 22.844  20.702  3.989   1.00 44.28  ? 66  VAL C CG2   1 
ATOM   8608  N N     . GLN C 1 67  ? 19.104  19.461  6.387   1.00 48.05  ? 67  GLN C N     1 
ATOM   8609  C CA    . GLN C 1 67  ? 18.057  18.511  6.720   1.00 51.68  ? 67  GLN C CA    1 
ATOM   8610  C C     . GLN C 1 67  ? 16.701  19.160  6.488   1.00 49.38  ? 67  GLN C C     1 
ATOM   8611  O O     . GLN C 1 67  ? 15.783  18.465  6.070   1.00 48.74  ? 67  GLN C O     1 
ATOM   8612  C CB    . GLN C 1 67  ? 18.126  18.031  8.177   1.00 47.54  ? 67  GLN C CB    1 
ATOM   8613  C CG    . GLN C 1 67  ? 19.245  17.043  8.431   1.00 49.99  ? 67  GLN C CG    1 
ATOM   8614  C CD    . GLN C 1 67  ? 19.513  16.847  9.902   1.00 43.96  ? 67  GLN C CD    1 
ATOM   8615  O OE1   . GLN C 1 67  ? 20.425  17.450  10.453  1.00 44.35  ? 67  GLN C OE1   1 
ATOM   8616  N NE2   . GLN C 1 67  ? 18.738  15.988  10.538  1.00 43.38  ? 67  GLN C NE2   1 
ATOM   8617  N N     . GLU C 1 68  ? 16.590  20.451  6.855   1.00 49.13  ? 68  GLU C N     1 
ATOM   8618  C CA    . GLU C 1 68  ? 15.318  21.163  6.843   1.00 49.94  ? 68  GLU C CA    1 
ATOM   8619  C C     . GLU C 1 68  ? 14.878  21.317  5.388   1.00 46.53  ? 68  GLU C C     1 
ATOM   8620  O O     . GLU C 1 68  ? 13.714  21.102  5.047   1.00 40.31  ? 68  GLU C O     1 
ATOM   8621  C CB    . GLU C 1 68  ? 15.436  22.495  7.593   1.00 49.00  ? 68  GLU C CB    1 
ATOM   8622  C CG    . GLU C 1 68  ? 15.366  22.348  9.119   1.00 57.05  ? 68  GLU C CG    1 
ATOM   8623  C CD    . GLU C 1 68  ? 15.242  23.647  9.913   1.00 53.36  ? 68  GLU C CD    1 
ATOM   8624  O OE1   . GLU C 1 68  ? 16.222  24.033  10.535  1.00 41.59  ? 68  GLU C OE1   1 
ATOM   8625  O OE2   . GLU C 1 68  ? 14.160  24.274  9.906   1.00 56.64  ? 68  GLU C OE2   1 
ATOM   8626  N N     . ILE C 1 69  ? 15.853  21.624  4.526   1.00 42.56  ? 69  ILE C N     1 
ATOM   8627  C CA    . ILE C 1 69  ? 15.618  21.739  3.098   1.00 42.44  ? 69  ILE C CA    1 
ATOM   8628  C C     . ILE C 1 69  ? 15.087  20.400  2.585   1.00 44.04  ? 69  ILE C C     1 
ATOM   8629  O O     . ILE C 1 69  ? 14.033  20.322  1.949   1.00 42.15  ? 69  ILE C O     1 
ATOM   8630  C CB    . ILE C 1 69  ? 16.919  22.200  2.410   1.00 43.45  ? 69  ILE C CB    1 
ATOM   8631  C CG1   . ILE C 1 69  ? 17.288  23.614  2.847   1.00 41.33  ? 69  ILE C CG1   1 
ATOM   8632  C CG2   . ILE C 1 69  ? 16.828  22.097  0.896   1.00 46.00  ? 69  ILE C CG2   1 
ATOM   8633  C CD1   . ILE C 1 69  ? 18.739  23.924  2.661   1.00 47.63  ? 69  ILE C CD1   1 
ATOM   8634  N N     . VAL C 1 70  ? 15.785  19.315  2.923   1.00 41.58  ? 70  VAL C N     1 
ATOM   8635  C CA    . VAL C 1 70  ? 15.395  18.043  2.367   1.00 37.86  ? 70  VAL C CA    1 
ATOM   8636  C C     . VAL C 1 70  ? 13.971  17.761  2.801   1.00 40.33  ? 70  VAL C C     1 
ATOM   8637  O O     . VAL C 1 70  ? 13.209  17.182  2.029   1.00 46.04  ? 70  VAL C O     1 
ATOM   8638  C CB    . VAL C 1 70  ? 16.362  16.920  2.753   1.00 40.59  ? 70  VAL C CB    1 
ATOM   8639  C CG1   . VAL C 1 70  ? 15.818  15.544  2.404   1.00 45.06  ? 70  VAL C CG1   1 
ATOM   8640  C CG2   . VAL C 1 70  ? 17.716  17.140  2.104   1.00 41.19  ? 70  VAL C CG2   1 
ATOM   8641  N N     . ARG C 1 71  ? 13.617  18.173  4.025   1.00 42.41  ? 71  ARG C N     1 
ATOM   8642  C CA    . ARG C 1 71  ? 12.282  17.910  4.551   1.00 44.33  ? 71  ARG C CA    1 
ATOM   8643  C C     . ARG C 1 71  ? 11.243  18.716  3.774   1.00 46.25  ? 71  ARG C C     1 
ATOM   8644  O O     . ARG C 1 71  ? 10.165  18.209  3.457   1.00 44.08  ? 71  ARG C O     1 
ATOM   8645  C CB    . ARG C 1 71  ? 12.215  18.198  6.051   1.00 47.02  ? 71  ARG C CB    1 
ATOM   8646  C CG    . ARG C 1 71  ? 12.826  17.100  6.920   1.00 52.97  ? 71  ARG C CG    1 
ATOM   8647  C CD    . ARG C 1 71  ? 12.998  17.476  8.388   1.00 52.12  ? 71  ARG C CD    1 
ATOM   8648  N NE    . ARG C 1 71  ? 13.641  16.429  9.158   1.00 45.60  ? 71  ARG C NE    1 
ATOM   8649  C CZ    . ARG C 1 71  ? 14.545  16.629  10.106  1.00 48.48  ? 71  ARG C CZ    1 
ATOM   8650  N NH1   . ARG C 1 71  ? 14.835  17.856  10.498  1.00 46.89  ? 71  ARG C NH1   1 
ATOM   8651  N NH2   . ARG C 1 71  ? 15.126  15.585  10.683  1.00 49.69  ? 71  ARG C NH2   1 
ATOM   8652  N N     . VAL C 1 72  ? 11.582  19.978  3.496   1.00 47.20  ? 72  VAL C N     1 
ATOM   8653  C CA    . VAL C 1 72  ? 10.732  20.847  2.700   1.00 53.14  ? 72  VAL C CA    1 
ATOM   8654  C C     . VAL C 1 72  ? 10.585  20.244  1.302   1.00 53.97  ? 72  VAL C C     1 
ATOM   8655  O O     . VAL C 1 72  ? 9.478   19.953  0.827   1.00 55.32  ? 72  VAL C O     1 
ATOM   8656  C CB    . VAL C 1 72  ? 11.323  22.270  2.634   1.00 52.38  ? 72  VAL C CB    1 
ATOM   8657  C CG1   . VAL C 1 72  ? 10.768  23.044  1.445   1.00 54.49  ? 72  VAL C CG1   1 
ATOM   8658  C CG2   . VAL C 1 72  ? 11.138  23.043  3.934   1.00 47.94  ? 72  VAL C CG2   1 
ATOM   8659  N N     . ALA C 1 73  ? 11.738  20.060  0.658   1.00 52.50  ? 73  ALA C N     1 
ATOM   8660  C CA    . ALA C 1 73  ? 11.799  19.424  -0.641  1.00 55.32  ? 73  ALA C CA    1 
ATOM   8661  C C     . ALA C 1 73  ? 10.818  18.254  -0.683  1.00 56.14  ? 73  ALA C C     1 
ATOM   8662  O O     . ALA C 1 73  ? 10.116  18.093  -1.680  1.00 59.95  ? 73  ALA C O     1 
ATOM   8663  C CB    . ALA C 1 73  ? 13.216  18.997  -0.935  1.00 53.29  ? 73  ALA C CB    1 
ATOM   8664  N N     . ASN C 1 74  ? 10.752  17.467  0.406   1.00 52.86  ? 74  ASN C N     1 
ATOM   8665  C CA    . ASN C 1 74  ? 9.888   16.294  0.446   1.00 56.80  ? 74  ASN C CA    1 
ATOM   8666  C C     . ASN C 1 74  ? 8.421   16.734  0.463   1.00 62.98  ? 74  ASN C C     1 
ATOM   8667  O O     . ASN C 1 74  ? 7.576   16.121  -0.182  1.00 61.93  ? 74  ASN C O     1 
ATOM   8668  C CB    . ASN C 1 74  ? 10.226  15.341  1.607   1.00 51.99  ? 74  ASN C CB    1 
ATOM   8669  C CG    . ASN C 1 74  ? 11.137  14.191  1.222   1.00 47.34  ? 74  ASN C CG    1 
ATOM   8670  O OD1   . ASN C 1 74  ? 10.700  13.195  0.655   1.00 49.04  ? 74  ASN C OD1   1 
ATOM   8671  N ND2   . ASN C 1 74  ? 12.410  14.297  1.558   1.00 45.59  ? 74  ASN C ND2   1 
ATOM   8672  N N     . GLU C 1 75  ? 8.120   17.796  1.211   1.00 70.89  ? 75  GLU C N     1 
ATOM   8673  C CA    . GLU C 1 75  ? 6.744   18.186  1.454   1.00 79.87  ? 75  GLU C CA    1 
ATOM   8674  C C     . GLU C 1 75  ? 6.101   18.606  0.135   1.00 74.49  ? 75  GLU C C     1 
ATOM   8675  O O     . GLU C 1 75  ? 4.960   18.230  -0.125  1.00 63.31  ? 75  GLU C O     1 
ATOM   8676  C CB    . GLU C 1 75  ? 6.715   19.305  2.498   1.00 93.96  ? 75  GLU C CB    1 
ATOM   8677  C CG    . GLU C 1 75  ? 5.314   19.685  2.950   1.00 100.08 ? 75  GLU C CG    1 
ATOM   8678  C CD    . GLU C 1 75  ? 5.252   20.559  4.194   1.00 106.89 ? 75  GLU C CD    1 
ATOM   8679  O OE1   . GLU C 1 75  ? 4.132   20.759  4.695   1.00 97.31  ? 75  GLU C OE1   1 
ATOM   8680  O OE2   . GLU C 1 75  ? 6.320   21.034  4.663   1.00 105.50 ? 75  GLU C OE2   1 
ATOM   8681  N N     . PHE C 1 76  ? 6.867   19.353  -0.683  1.00 72.14  ? 76  PHE C N     1 
ATOM   8682  C CA    . PHE C 1 76  ? 6.374   19.999  -1.898  1.00 77.68  ? 76  PHE C CA    1 
ATOM   8683  C C     . PHE C 1 76  ? 6.858   19.325  -3.193  1.00 65.95  ? 76  PHE C C     1 
ATOM   8684  O O     . PHE C 1 76  ? 6.766   19.924  -4.256  1.00 62.25  ? 76  PHE C O     1 
ATOM   8685  C CB    . PHE C 1 76  ? 6.807   21.471  -1.907  1.00 76.16  ? 76  PHE C CB    1 
ATOM   8686  C CG    . PHE C 1 76  ? 6.130   22.305  -0.857  1.00 91.23  ? 76  PHE C CG    1 
ATOM   8687  C CD1   . PHE C 1 76  ? 4.748   22.277  -0.715  1.00 103.27 ? 76  PHE C CD1   1 
ATOM   8688  C CD2   . PHE C 1 76  ? 6.869   23.102  0.000   1.00 99.07  ? 76  PHE C CD2   1 
ATOM   8689  C CE1   . PHE C 1 76  ? 4.117   23.021  0.270   1.00 106.06 ? 76  PHE C CE1   1 
ATOM   8690  C CE2   . PHE C 1 76  ? 6.235   23.850  0.982   1.00 105.84 ? 76  PHE C CE2   1 
ATOM   8691  C CZ    . PHE C 1 76  ? 4.863   23.803  1.120   1.00 105.28 ? 76  PHE C CZ    1 
ATOM   8692  N N     . GLY C 1 77  ? 7.410   18.108  -3.106  1.00 55.50  ? 77  GLY C N     1 
ATOM   8693  C CA    . GLY C 1 77  ? 7.828   17.338  -4.268  1.00 54.87  ? 77  GLY C CA    1 
ATOM   8694  C C     . GLY C 1 77  ? 8.894   17.988  -5.153  1.00 48.26  ? 77  GLY C C     1 
ATOM   8695  O O     . GLY C 1 77  ? 8.977   17.613  -6.312  1.00 51.45  ? 77  GLY C O     1 
ATOM   8696  N N     . VAL C 1 78  ? 9.719   18.904  -4.617  1.00 45.73  ? 78  VAL C N     1 
ATOM   8697  C CA    . VAL C 1 78  ? 10.730  19.610  -5.401  1.00 49.49  ? 78  VAL C CA    1 
ATOM   8698  C C     . VAL C 1 78  ? 12.105  18.937  -5.323  1.00 51.67  ? 78  VAL C C     1 
ATOM   8699  O O     . VAL C 1 78  ? 12.634  18.662  -4.251  1.00 51.35  ? 78  VAL C O     1 
ATOM   8700  C CB    . VAL C 1 78  ? 10.884  21.063  -4.928  1.00 52.08  ? 78  VAL C CB    1 
ATOM   8701  C CG1   . VAL C 1 78  ? 11.933  21.813  -5.738  1.00 49.06  ? 78  VAL C CG1   1 
ATOM   8702  C CG2   . VAL C 1 78  ? 9.554   21.783  -4.962  1.00 59.18  ? 78  VAL C CG2   1 
ATOM   8703  N N     . PRO C 1 79  ? 12.794  18.745  -6.459  1.00 50.40  ? 79  PRO C N     1 
ATOM   8704  C CA    . PRO C 1 79  ? 14.085  18.060  -6.483  1.00 50.92  ? 79  PRO C CA    1 
ATOM   8705  C C     . PRO C 1 79  ? 15.282  18.934  -6.172  1.00 47.40  ? 79  PRO C C     1 
ATOM   8706  O O     . PRO C 1 79  ? 15.230  20.134  -6.406  1.00 49.27  ? 79  PRO C O     1 
ATOM   8707  C CB    . PRO C 1 79  ? 14.238  17.636  -7.952  1.00 62.60  ? 79  PRO C CB    1 
ATOM   8708  C CG    . PRO C 1 79  ? 12.874  17.934  -8.586  1.00 59.59  ? 79  PRO C CG    1 
ATOM   8709  C CD    . PRO C 1 79  ? 12.339  19.106  -7.804  1.00 58.56  ? 79  PRO C CD    1 
ATOM   8710  N N     . LEU C 1 80  ? 16.371  18.308  -5.695  1.00 53.33  ? 80  LEU C N     1 
ATOM   8711  C CA    . LEU C 1 80  ? 17.576  19.018  -5.283  1.00 44.40  ? 80  LEU C CA    1 
ATOM   8712  C C     . LEU C 1 80  ? 18.762  18.378  -5.976  1.00 44.78  ? 80  LEU C C     1 
ATOM   8713  O O     . LEU C 1 80  ? 18.794  17.161  -6.168  1.00 45.92  ? 80  LEU C O     1 
ATOM   8714  C CB    . LEU C 1 80  ? 17.742  18.930  -3.764  1.00 47.78  ? 80  LEU C CB    1 
ATOM   8715  C CG    . LEU C 1 80  ? 16.550  19.390  -2.916  1.00 48.68  ? 80  LEU C CG    1 
ATOM   8716  C CD1   . LEU C 1 80  ? 16.767  19.089  -1.436  1.00 51.61  ? 80  LEU C CD1   1 
ATOM   8717  C CD2   . LEU C 1 80  ? 16.323  20.878  -3.089  1.00 47.57  ? 80  LEU C CD2   1 
ATOM   8718  N N     . TRP C 1 81  ? 19.735  19.214  -6.346  1.00 46.41  ? 81  TRP C N     1 
ATOM   8719  C CA    . TRP C 1 81  ? 20.951  18.726  -6.954  1.00 44.33  ? 81  TRP C CA    1 
ATOM   8720  C C     . TRP C 1 81  ? 22.135  19.216  -6.135  1.00 41.45  ? 81  TRP C C     1 
ATOM   8721  O O     . TRP C 1 81  ? 22.581  20.339  -6.310  1.00 49.95  ? 81  TRP C O     1 
ATOM   8722  C CB    . TRP C 1 81  ? 21.061  19.129  -8.440  1.00 43.10  ? 81  TRP C CB    1 
ATOM   8723  C CG    . TRP C 1 81  ? 22.104  18.317  -9.150  1.00 43.22  ? 81  TRP C CG    1 
ATOM   8724  C CD1   . TRP C 1 81  ? 23.449  18.483  -9.089  1.00 49.70  ? 81  TRP C CD1   1 
ATOM   8725  C CD2   . TRP C 1 81  ? 21.896  17.123  -9.921  1.00 43.57  ? 81  TRP C CD2   1 
ATOM   8726  N NE1   . TRP C 1 81  ? 24.089  17.521  -9.822  1.00 51.27  ? 81  TRP C NE1   1 
ATOM   8727  C CE2   . TRP C 1 81  ? 23.169  16.652  -10.308 1.00 41.28  ? 81  TRP C CE2   1 
ATOM   8728  C CE3   . TRP C 1 81  ? 20.752  16.450  -10.378 1.00 46.65  ? 81  TRP C CE3   1 
ATOM   8729  C CZ2   . TRP C 1 81  ? 23.347  15.539  -11.115 1.00 42.68  ? 81  TRP C CZ2   1 
ATOM   8730  C CZ3   . TRP C 1 81  ? 20.925  15.320  -11.148 1.00 46.51  ? 81  TRP C CZ3   1 
ATOM   8731  C CH2   . TRP C 1 81  ? 22.204  14.884  -11.515 1.00 46.97  ? 81  TRP C CH2   1 
ATOM   8732  N N     . PRO C 1 82  ? 22.744  18.387  -5.269  1.00 43.35  ? 82  PRO C N     1 
ATOM   8733  C CA    . PRO C 1 82  ? 23.806  18.875  -4.389  1.00 49.91  ? 82  PRO C CA    1 
ATOM   8734  C C     . PRO C 1 82  ? 25.133  19.039  -5.115  1.00 48.33  ? 82  PRO C C     1 
ATOM   8735  O O     . PRO C 1 82  ? 25.447  18.284  -6.027  1.00 55.08  ? 82  PRO C O     1 
ATOM   8736  C CB    . PRO C 1 82  ? 23.924  17.812  -3.283  1.00 48.11  ? 82  PRO C CB    1 
ATOM   8737  C CG    . PRO C 1 82  ? 22.825  16.792  -3.589  1.00 44.09  ? 82  PRO C CG    1 
ATOM   8738  C CD    . PRO C 1 82  ? 22.457  16.966  -5.048  1.00 40.31  ? 82  PRO C CD    1 
ATOM   8739  N N     . VAL C 1 83  ? 25.918  20.005  -4.653  1.00 51.65  ? 83  VAL C N     1 
ATOM   8740  C CA    . VAL C 1 83  ? 27.228  20.282  -5.213  1.00 62.11  ? 83  VAL C CA    1 
ATOM   8741  C C     . VAL C 1 83  ? 28.152  20.764  -4.102  1.00 58.47  ? 83  VAL C C     1 
ATOM   8742  O O     . VAL C 1 83  ? 27.871  21.778  -3.471  1.00 69.64  ? 83  VAL C O     1 
ATOM   8743  C CB    . VAL C 1 83  ? 27.112  21.330  -6.327  1.00 72.01  ? 83  VAL C CB    1 
ATOM   8744  C CG1   . VAL C 1 83  ? 26.694  20.709  -7.651  1.00 78.82  ? 83  VAL C CG1   1 
ATOM   8745  C CG2   . VAL C 1 83  ? 26.149  22.434  -5.928  1.00 78.41  ? 83  VAL C CG2   1 
ATOM   8746  N N     . SER C 1 84  ? 29.254  20.035  -3.878  1.00 57.17  ? 84  SER C N     1 
ATOM   8747  C CA    . SER C 1 84  ? 30.212  20.392  -2.841  1.00 57.77  ? 84  SER C CA    1 
ATOM   8748  C C     . SER C 1 84  ? 30.755  21.795  -3.095  1.00 62.87  ? 84  SER C C     1 
ATOM   8749  O O     . SER C 1 84  ? 30.558  22.692  -2.286  1.00 78.03  ? 84  SER C O     1 
ATOM   8750  C CB    . SER C 1 84  ? 31.316  19.376  -2.711  1.00 56.55  ? 84  SER C CB    1 
ATOM   8751  O OG    . SER C 1 84  ? 30.885  18.218  -1.993  1.00 49.92  ? 84  SER C OG    1 
ATOM   8752  N N     . ARG C 1 85  ? 31.443  21.970  -4.219  1.00 69.16  ? 85  ARG C N     1 
ATOM   8753  C CA    . ARG C 1 85  ? 31.841  23.288  -4.671  1.00 72.28  ? 85  ARG C CA    1 
ATOM   8754  C C     . ARG C 1 85  ? 31.294  23.506  -6.073  1.00 72.25  ? 85  ARG C C     1 
ATOM   8755  O O     . ARG C 1 85  ? 31.169  24.647  -6.513  1.00 74.64  ? 85  ARG C O     1 
ATOM   8756  C CB    . ARG C 1 85  ? 33.363  23.460  -4.600  1.00 70.73  ? 85  ARG C CB    1 
ATOM   8757  C CG    . ARG C 1 85  ? 33.870  23.725  -3.188  1.00 66.72  ? 85  ARG C CG    1 
ATOM   8758  C CD    . ARG C 1 85  ? 35.389  23.726  -3.094  1.00 66.52  ? 85  ARG C CD    1 
ATOM   8759  N NE    . ARG C 1 85  ? 36.024  24.829  -3.806  1.00 73.27  ? 85  ARG C NE    1 
ATOM   8760  C CZ    . ARG C 1 85  ? 36.031  26.098  -3.396  1.00 73.21  ? 85  ARG C CZ    1 
ATOM   8761  N NH1   . ARG C 1 85  ? 35.393  26.458  -2.292  1.00 68.00  ? 85  ARG C NH1   1 
ATOM   8762  N NH2   . ARG C 1 85  ? 36.679  27.009  -4.102  1.00 69.00  ? 85  ARG C NH2   1 
ATOM   8763  N N     . GLY C 1 86  ? 30.948  22.409  -6.748  1.00 64.52  ? 86  GLY C N     1 
ATOM   8764  C CA    . GLY C 1 86  ? 30.370  22.503  -8.074  1.00 76.60  ? 86  GLY C CA    1 
ATOM   8765  C C     . GLY C 1 86  ? 31.416  22.803  -9.148  1.00 75.77  ? 86  GLY C C     1 
ATOM   8766  O O     . GLY C 1 86  ? 31.045  23.287  -10.214 1.00 71.70  ? 86  GLY C O     1 
ATOM   8767  N N     . LYS C 1 87  ? 32.692  22.469  -8.864  1.00 95.46  ? 87  LYS C N     1 
ATOM   8768  C CA    . LYS C 1 87  ? 33.821  22.673  -9.775  1.00 98.57  ? 87  LYS C CA    1 
ATOM   8769  C C     . LYS C 1 87  ? 34.211  21.359  -10.473 1.00 77.01  ? 87  LYS C C     1 
ATOM   8770  O O     . LYS C 1 87  ? 35.389  21.064  -10.666 1.00 73.15  ? 87  LYS C O     1 
ATOM   8771  C CB    . LYS C 1 87  ? 34.994  23.304  -9.010  1.00 111.77 ? 87  LYS C CB    1 
ATOM   8772  C CG    . LYS C 1 87  ? 34.589  24.420  -8.051  1.00 121.40 ? 87  LYS C CG    1 
ATOM   8773  C CD    . LYS C 1 87  ? 35.470  25.651  -8.076  1.00 127.69 ? 87  LYS C CD    1 
ATOM   8774  C CE    . LYS C 1 87  ? 34.704  26.900  -7.686  1.00 119.96 ? 87  LYS C CE    1 
ATOM   8775  N NZ    . LYS C 1 87  ? 35.491  28.129  -7.938  1.00 117.14 ? 87  LYS C NZ    1 
ATOM   8776  N N     . ASN C 1 88  ? 33.189  20.609  -10.910 1.00 72.37  ? 88  ASN C N     1 
ATOM   8777  C CA    . ASN C 1 88  ? 33.343  19.353  -11.614 1.00 72.87  ? 88  ASN C CA    1 
ATOM   8778  C C     . ASN C 1 88  ? 33.432  19.683  -13.109 1.00 75.16  ? 88  ASN C C     1 
ATOM   8779  O O     . ASN C 1 88  ? 32.548  19.362  -13.902 1.00 49.24  ? 88  ASN C O     1 
ATOM   8780  C CB    . ASN C 1 88  ? 32.195  18.397  -11.240 1.00 68.77  ? 88  ASN C CB    1 
ATOM   8781  C CG    . ASN C 1 88  ? 32.547  16.914  -11.291 1.00 67.27  ? 88  ASN C CG    1 
ATOM   8782  O OD1   . ASN C 1 88  ? 33.718  16.526  -11.302 1.00 71.41  ? 88  ASN C OD1   1 
ATOM   8783  N ND2   . ASN C 1 88  ? 31.528  16.066  -11.305 1.00 56.54  ? 88  ASN C ND2   1 
ATOM   8784  N N     . PHE C 1 89  ? 34.521  20.334  -13.515 1.00 82.72  ? 89  PHE C N     1 
ATOM   8785  C CA    . PHE C 1 89  ? 34.619  20.785  -14.893 1.00 85.78  ? 89  PHE C CA    1 
ATOM   8786  C C     . PHE C 1 89  ? 34.822  19.543  -15.776 1.00 86.88  ? 89  PHE C C     1 
ATOM   8787  O O     . PHE C 1 89  ? 35.636  18.683  -15.413 1.00 70.97  ? 89  PHE C O     1 
ATOM   8788  C CB    . PHE C 1 89  ? 35.675  21.898  -14.980 1.00 85.93  ? 89  PHE C CB    1 
ATOM   8789  C CG    . PHE C 1 89  ? 35.450  23.118  -14.102 1.00 89.87  ? 89  PHE C CG    1 
ATOM   8790  C CD1   . PHE C 1 89  ? 34.203  23.733  -14.012 1.00 98.22  ? 89  PHE C CD1   1 
ATOM   8791  C CD2   . PHE C 1 89  ? 36.504  23.686  -13.390 1.00 86.74  ? 89  PHE C CD2   1 
ATOM   8792  C CE1   . PHE C 1 89  ? 34.014  24.863  -13.224 1.00 98.05  ? 89  PHE C CE1   1 
ATOM   8793  C CE2   . PHE C 1 89  ? 36.320  24.813  -12.601 1.00 90.83  ? 89  PHE C CE2   1 
ATOM   8794  C CZ    . PHE C 1 89  ? 35.073  25.400  -12.518 1.00 103.22 ? 89  PHE C CZ    1 
ATOM   8795  N N     . ALA C 1 90  ? 34.009  19.432  -16.864 1.00 92.21  ? 90  ALA C N     1 
ATOM   8796  C CA    . ALA C 1 90  ? 34.061  18.383  -17.900 1.00 90.49  ? 90  ALA C CA    1 
ATOM   8797  C C     . ALA C 1 90  ? 33.077  17.234  -17.625 1.00 83.46  ? 90  ALA C C     1 
ATOM   8798  O O     . ALA C 1 90  ? 33.017  16.216  -18.340 1.00 62.68  ? 90  ALA C O     1 
ATOM   8799  C CB    . ALA C 1 90  ? 35.465  17.854  -18.084 1.00 85.25  ? 90  ALA C CB    1 
ATOM   8800  N N     . TYR C 1 91  ? 32.288  17.435  -16.571 1.00 82.55  ? 91  TYR C N     1 
ATOM   8801  C CA    . TYR C 1 91  ? 31.305  16.474  -16.119 1.00 79.57  ? 91  TYR C CA    1 
ATOM   8802  C C     . TYR C 1 91  ? 29.948  17.177  -15.977 1.00 70.30  ? 91  TYR C C     1 
ATOM   8803  O O     . TYR C 1 91  ? 28.939  16.525  -15.738 1.00 75.03  ? 91  TYR C O     1 
ATOM   8804  C CB    . TYR C 1 91  ? 31.840  15.798  -14.844 1.00 77.07  ? 91  TYR C CB    1 
ATOM   8805  C CG    . TYR C 1 91  ? 33.089  14.964  -15.036 1.00 72.21  ? 91  TYR C CG    1 
ATOM   8806  C CD1   . TYR C 1 91  ? 33.023  13.726  -15.645 1.00 79.60  ? 91  TYR C CD1   1 
ATOM   8807  C CD2   . TYR C 1 91  ? 34.347  15.407  -14.646 1.00 77.03  ? 91  TYR C CD2   1 
ATOM   8808  C CE1   . TYR C 1 91  ? 34.156  12.957  -15.866 1.00 78.02  ? 91  TYR C CE1   1 
ATOM   8809  C CE2   . TYR C 1 91  ? 35.494  14.645  -14.843 1.00 60.66  ? 91  TYR C CE2   1 
ATOM   8810  C CZ    . TYR C 1 91  ? 35.395  13.407  -15.452 1.00 62.51  ? 91  TYR C CZ    1 
ATOM   8811  O OH    . TYR C 1 91  ? 36.458  12.567  -15.657 1.00 56.26  ? 91  TYR C OH    1 
ATOM   8812  N N     . GLY C 1 92  ? 29.911  18.502  -16.175 1.00 71.20  ? 92  GLY C N     1 
ATOM   8813  C CA    . GLY C 1 92  ? 28.694  19.273  -15.976 1.00 78.45  ? 92  GLY C CA    1 
ATOM   8814  C C     . GLY C 1 92  ? 28.896  20.581  -15.208 1.00 81.91  ? 92  GLY C C     1 
ATOM   8815  O O     . GLY C 1 92  ? 27.970  21.391  -15.097 1.00 72.86  ? 92  GLY C O     1 
ATOM   8816  N N     . GLY C 1 93  ? 30.106  20.785  -14.680 1.00 95.04  ? 93  GLY C N     1 
ATOM   8817  C CA    . GLY C 1 93  ? 30.323  21.790  -13.655 1.00 92.96  ? 93  GLY C CA    1 
ATOM   8818  C C     . GLY C 1 93  ? 29.370  21.565  -12.486 1.00 86.04  ? 93  GLY C C     1 
ATOM   8819  O O     . GLY C 1 93  ? 29.421  20.537  -11.807 1.00 91.68  ? 93  GLY C O     1 
ATOM   8820  N N     . ALA C 1 94  ? 28.464  22.523  -12.309 1.00 86.86  ? 94  ALA C N     1 
ATOM   8821  C CA    . ALA C 1 94  ? 27.592  22.551  -11.152 1.00 89.79  ? 94  ALA C CA    1 
ATOM   8822  C C     . ALA C 1 94  ? 26.157  22.175  -11.544 1.00 79.48  ? 94  ALA C C     1 
ATOM   8823  O O     . ALA C 1 94  ? 25.235  22.357  -10.756 1.00 99.99  ? 94  ALA C O     1 
ATOM   8824  C CB    . ALA C 1 94  ? 27.687  23.933  -10.529 1.00 86.98  ? 94  ALA C CB    1 
ATOM   8825  N N     . ALA C 1 95  ? 25.948  21.620  -12.742 1.00 73.67  ? 95  ALA C N     1 
ATOM   8826  C CA    . ALA C 1 95  ? 24.615  21.639  -13.334 1.00 78.95  ? 95  ALA C CA    1 
ATOM   8827  C C     . ALA C 1 95  ? 23.902  20.302  -13.146 1.00 67.05  ? 95  ALA C C     1 
ATOM   8828  O O     . ALA C 1 95  ? 24.539  19.260  -13.203 1.00 78.31  ? 95  ALA C O     1 
ATOM   8829  C CB    . ALA C 1 95  ? 24.704  22.007  -14.799 1.00 87.06  ? 95  ALA C CB    1 
ATOM   8830  N N     . PRO C 1 96  ? 22.568  20.285  -12.917 1.00 64.83  ? 96  PRO C N     1 
ATOM   8831  C CA    . PRO C 1 96  ? 21.778  19.054  -12.976 1.00 72.94  ? 96  PRO C CA    1 
ATOM   8832  C C     . PRO C 1 96  ? 21.471  18.452  -14.361 1.00 91.39  ? 96  PRO C C     1 
ATOM   8833  O O     . PRO C 1 96  ? 21.289  19.189  -15.328 1.00 95.81  ? 96  PRO C O     1 
ATOM   8834  C CB    . PRO C 1 96  ? 20.472  19.525  -12.318 1.00 71.79  ? 96  PRO C CB    1 
ATOM   8835  C CG    . PRO C 1 96  ? 20.344  20.934  -12.774 1.00 74.40  ? 96  PRO C CG    1 
ATOM   8836  C CD    . PRO C 1 96  ? 21.748  21.444  -12.540 1.00 71.44  ? 96  PRO C CD    1 
ATOM   8837  N N     . VAL C 1 97  ? 21.403  17.098  -14.419 1.00 88.40  ? 97  VAL C N     1 
ATOM   8838  C CA    . VAL C 1 97  ? 20.995  16.277  -15.560 1.00 78.48  ? 97  VAL C CA    1 
ATOM   8839  C C     . VAL C 1 97  ? 19.554  16.588  -15.966 1.00 73.74  ? 97  VAL C C     1 
ATOM   8840  O O     . VAL C 1 97  ? 19.228  16.771  -17.149 1.00 54.87  ? 97  VAL C O     1 
ATOM   8841  C CB    . VAL C 1 97  ? 21.111  14.773  -15.217 1.00 89.33  ? 97  VAL C CB    1 
ATOM   8842  C CG1   . VAL C 1 97  ? 20.362  13.895  -16.211 1.00 94.76  ? 97  VAL C CG1   1 
ATOM   8843  C CG2   . VAL C 1 97  ? 22.558  14.303  -15.074 1.00 90.15  ? 97  VAL C CG2   1 
ATOM   8844  N N     . MET C 1 98  ? 18.668  16.579  -14.971 1.00 73.04  ? 98  MET C N     1 
ATOM   8845  C CA    . MET C 1 98  ? 17.326  17.045  -15.227 1.00 84.54  ? 98  MET C CA    1 
ATOM   8846  C C     . MET C 1 98  ? 17.294  18.535  -14.897 1.00 92.52  ? 98  MET C C     1 
ATOM   8847  O O     . MET C 1 98  ? 17.870  18.979  -13.903 1.00 87.38  ? 98  MET C O     1 
ATOM   8848  C CB    . MET C 1 98  ? 16.294  16.268  -14.413 1.00 86.79  ? 98  MET C CB    1 
ATOM   8849  C CG    . MET C 1 98  ? 14.913  16.248  -15.060 1.00 81.75  ? 98  MET C CG    1 
ATOM   8850  S SD    . MET C 1 98  ? 13.645  15.651  -13.903 1.00 85.56  ? 98  MET C SD    1 
ATOM   8851  C CE    . MET C 1 98  ? 13.185  17.198  -13.118 1.00 94.59  ? 98  MET C CE    1 
ATOM   8852  N N     . SER C 1 99  ? 16.684  19.304  -15.806 1.00 87.67  ? 99  SER C N     1 
ATOM   8853  C CA    . SER C 1 99  ? 16.534  20.732  -15.622 1.00 77.03  ? 99  SER C CA    1 
ATOM   8854  C C     . SER C 1 99  ? 15.334  20.944  -14.725 1.00 68.52  ? 99  SER C C     1 
ATOM   8855  O O     . SER C 1 99  ? 14.500  20.053  -14.582 1.00 64.19  ? 99  SER C O     1 
ATOM   8856  C CB    . SER C 1 99  ? 16.392  21.475  -16.943 1.00 87.62  ? 99  SER C CB    1 
ATOM   8857  O OG    . SER C 1 99  ? 15.229  21.087  -17.663 1.00 81.51  ? 99  SER C OG    1 
ATOM   8858  N N     . GLY C 1 100 ? 15.258  22.138  -14.146 1.00 70.91  ? 100 GLY C N     1 
ATOM   8859  C CA    . GLY C 1 100 ? 14.198  22.449  -13.209 1.00 69.14  ? 100 GLY C CA    1 
ATOM   8860  C C     . GLY C 1 100 ? 14.609  22.063  -11.797 1.00 59.75  ? 100 GLY C C     1 
ATOM   8861  O O     . GLY C 1 100 ? 13.839  22.174  -10.860 1.00 62.24  ? 100 GLY C O     1 
ATOM   8862  N N     . THR C 1 101 ? 15.857  21.646  -11.650 1.00 62.88  ? 101 THR C N     1 
ATOM   8863  C CA    . THR C 1 101 ? 16.329  21.175  -10.366 1.00 67.86  ? 101 THR C CA    1 
ATOM   8864  C C     . THR C 1 101 ? 16.832  22.360  -9.540  1.00 66.79  ? 101 THR C C     1 
ATOM   8865  O O     . THR C 1 101 ? 17.537  23.221  -10.054 1.00 65.21  ? 101 THR C O     1 
ATOM   8866  C CB    . THR C 1 101 ? 17.387  20.099  -10.608 1.00 62.33  ? 101 THR C CB    1 
ATOM   8867  O OG1   . THR C 1 101 ? 16.752  19.013  -11.288 1.00 65.93  ? 101 THR C OG1   1 
ATOM   8868  C CG2   . THR C 1 101 ? 17.989  19.599  -9.325  1.00 66.03  ? 101 THR C CG2   1 
ATOM   8869  N N     . VAL C 1 102 ? 16.482  22.392  -8.248  1.00 70.02  ? 102 VAL C N     1 
ATOM   8870  C CA    . VAL C 1 102 ? 17.081  23.350  -7.328  1.00 62.45  ? 102 VAL C CA    1 
ATOM   8871  C C     . VAL C 1 102 ? 18.463  22.842  -6.923  1.00 54.73  ? 102 VAL C C     1 
ATOM   8872  O O     . VAL C 1 102 ? 18.578  21.784  -6.314  1.00 54.91  ? 102 VAL C O     1 
ATOM   8873  C CB    . VAL C 1 102 ? 16.231  23.580  -6.070  1.00 58.27  ? 102 VAL C CB    1 
ATOM   8874  C CG1   . VAL C 1 102 ? 16.589  24.912  -5.438  1.00 60.81  ? 102 VAL C CG1   1 
ATOM   8875  C CG2   . VAL C 1 102 ? 14.741  23.500  -6.344  1.00 63.50  ? 102 VAL C CG2   1 
ATOM   8876  N N     . VAL C 1 103 ? 19.504  23.612  -7.243  1.00 53.23  ? 103 VAL C N     1 
ATOM   8877  C CA    . VAL C 1 103 ? 20.854  23.287  -6.822  1.00 54.23  ? 103 VAL C CA    1 
ATOM   8878  C C     . VAL C 1 103 ? 21.036  23.495  -5.316  1.00 53.17  ? 103 VAL C C     1 
ATOM   8879  O O     . VAL C 1 103 ? 20.866  24.590  -4.805  1.00 51.42  ? 103 VAL C O     1 
ATOM   8880  C CB    . VAL C 1 103 ? 21.858  24.136  -7.598  1.00 53.22  ? 103 VAL C CB    1 
ATOM   8881  C CG1   . VAL C 1 103 ? 23.258  23.990  -7.030  1.00 58.28  ? 103 VAL C CG1   1 
ATOM   8882  C CG2   . VAL C 1 103 ? 21.824  23.783  -9.067  1.00 54.41  ? 103 VAL C CG2   1 
ATOM   8883  N N     . LEU C 1 104 ? 21.403  22.424  -4.608  1.00 52.40  ? 104 LEU C N     1 
ATOM   8884  C CA    . LEU C 1 104 ? 21.745  22.511  -3.201  1.00 52.38  ? 104 LEU C CA    1 
ATOM   8885  C C     . LEU C 1 104 ? 23.243  22.760  -3.124  1.00 49.69  ? 104 LEU C C     1 
ATOM   8886  O O     . LEU C 1 104 ? 24.025  21.832  -3.249  1.00 45.70  ? 104 LEU C O     1 
ATOM   8887  C CB    . LEU C 1 104 ? 21.332  21.222  -2.487  1.00 53.10  ? 104 LEU C CB    1 
ATOM   8888  C CG    . LEU C 1 104 ? 21.557  21.180  -0.971  1.00 56.84  ? 104 LEU C CG    1 
ATOM   8889  C CD1   . LEU C 1 104 ? 20.613  22.123  -0.236  1.00 55.05  ? 104 LEU C CD1   1 
ATOM   8890  C CD2   . LEU C 1 104 ? 21.395  19.749  -0.432  1.00 53.16  ? 104 LEU C CD2   1 
ATOM   8891  N N     . ASP C 1 105 ? 23.609  24.031  -2.966  1.00 46.90  ? 105 ASP C N     1 
ATOM   8892  C CA    . ASP C 1 105 ? 24.995  24.446  -2.977  1.00 49.84  ? 105 ASP C CA    1 
ATOM   8893  C C     . ASP C 1 105 ? 25.530  24.403  -1.552  1.00 51.00  ? 105 ASP C C     1 
ATOM   8894  O O     . ASP C 1 105 ? 24.895  24.878  -0.621  1.00 53.47  ? 105 ASP C O     1 
ATOM   8895  C CB    . ASP C 1 105 ? 25.105  25.850  -3.574  1.00 53.48  ? 105 ASP C CB    1 
ATOM   8896  C CG    . ASP C 1 105 ? 26.522  26.337  -3.789  1.00 53.81  ? 105 ASP C CG    1 
ATOM   8897  O OD1   . ASP C 1 105 ? 27.420  25.504  -3.795  1.00 54.23  ? 105 ASP C OD1   1 
ATOM   8898  O OD2   . ASP C 1 105 ? 26.709  27.557  -3.923  1.00 66.57  ? 105 ASP C OD2   1 
ATOM   8899  N N     . MET C 1 106 ? 26.727  23.855  -1.395  1.00 53.62  ? 106 MET C N     1 
ATOM   8900  C CA    . MET C 1 106 ? 27.250  23.572  -0.079  1.00 51.57  ? 106 MET C CA    1 
ATOM   8901  C C     . MET C 1 106 ? 28.616  24.222  0.079   1.00 53.48  ? 106 MET C C     1 
ATOM   8902  O O     . MET C 1 106 ? 29.341  23.925  1.017   1.00 46.06  ? 106 MET C O     1 
ATOM   8903  C CB    . MET C 1 106 ? 27.284  22.054  0.103   1.00 55.52  ? 106 MET C CB    1 
ATOM   8904  C CG    . MET C 1 106 ? 25.868  21.480  0.051   1.00 56.08  ? 106 MET C CG    1 
ATOM   8905  S SD    . MET C 1 106 ? 25.623  20.172  1.245   1.00 59.13  ? 106 MET C SD    1 
ATOM   8906  C CE    . MET C 1 106 ? 26.785  18.999  0.560   1.00 81.24  ? 106 MET C CE    1 
ATOM   8907  N N     . ASN C 1 107 ? 28.891  25.207  -0.787  1.00 59.43  ? 107 ASN C N     1 
ATOM   8908  C CA    . ASN C 1 107 ? 30.097  26.016  -0.736  1.00 61.43  ? 107 ASN C CA    1 
ATOM   8909  C C     . ASN C 1 107 ? 30.369  26.540  0.674   1.00 52.50  ? 107 ASN C C     1 
ATOM   8910  O O     . ASN C 1 107 ? 31.525  26.643  1.063   1.00 46.94  ? 107 ASN C O     1 
ATOM   8911  C CB    . ASN C 1 107 ? 30.030  27.188  -1.724  1.00 68.16  ? 107 ASN C CB    1 
ATOM   8912  C CG    . ASN C 1 107 ? 30.551  26.799  -3.093  1.00 93.84  ? 107 ASN C CG    1 
ATOM   8913  O OD1   . ASN C 1 107 ? 29.886  26.076  -3.837  1.00 92.10  ? 107 ASN C OD1   1 
ATOM   8914  N ND2   . ASN C 1 107 ? 31.751  27.257  -3.430  1.00 105.71 ? 107 ASN C ND2   1 
ATOM   8915  N N     . ARG C 1 108 ? 29.311  26.918  1.396   1.00 52.86  ? 108 ARG C N     1 
ATOM   8916  C CA    . ARG C 1 108 ? 29.444  27.694  2.622   1.00 57.21  ? 108 ARG C CA    1 
ATOM   8917  C C     . ARG C 1 108 ? 29.884  26.789  3.772   1.00 50.91  ? 108 ARG C C     1 
ATOM   8918  O O     . ARG C 1 108 ? 30.467  27.254  4.745   1.00 48.67  ? 108 ARG C O     1 
ATOM   8919  C CB    . ARG C 1 108 ? 28.116  28.382  2.967   1.00 64.44  ? 108 ARG C CB    1 
ATOM   8920  C CG    . ARG C 1 108 ? 27.671  29.479  2.004   1.00 59.29  ? 108 ARG C CG    1 
ATOM   8921  C CD    . ARG C 1 108 ? 26.322  30.057  2.418   1.00 60.41  ? 108 ARG C CD    1 
ATOM   8922  N NE    . ARG C 1 108 ? 26.383  30.740  3.713   1.00 66.34  ? 108 ARG C NE    1 
ATOM   8923  C CZ    . ARG C 1 108 ? 25.419  30.726  4.641   1.00 61.79  ? 108 ARG C CZ    1 
ATOM   8924  N NH1   . ARG C 1 108 ? 24.290  30.081  4.428   1.00 56.38  ? 108 ARG C NH1   1 
ATOM   8925  N NH2   . ARG C 1 108 ? 25.567  31.377  5.783   1.00 57.33  ? 108 ARG C NH2   1 
ATOM   8926  N N     . MET C 1 109 ? 29.587  25.496  3.637   1.00 47.99  ? 109 MET C N     1 
ATOM   8927  C CA    . MET C 1 109 ? 29.982  24.471  4.588   1.00 47.73  ? 109 MET C CA    1 
ATOM   8928  C C     . MET C 1 109 ? 31.417  24.071  4.280   1.00 49.28  ? 109 MET C C     1 
ATOM   8929  O O     . MET C 1 109 ? 31.667  22.992  3.732   1.00 52.59  ? 109 MET C O     1 
ATOM   8930  C CB    . MET C 1 109 ? 29.053  23.248  4.468   1.00 50.23  ? 109 MET C CB    1 
ATOM   8931  C CG    . MET C 1 109 ? 27.723  23.457  5.185   1.00 51.07  ? 109 MET C CG    1 
ATOM   8932  S SD    . MET C 1 109 ? 26.397  22.334  4.731   1.00 48.01  ? 109 MET C SD    1 
ATOM   8933  C CE    . MET C 1 109 ? 26.744  20.955  5.822   1.00 55.18  ? 109 MET C CE    1 
ATOM   8934  N N     . ASN C 1 110 ? 32.349  24.951  4.647   1.00 48.59  ? 110 ASN C N     1 
ATOM   8935  C CA    . ASN C 1 110 ? 33.701  24.924  4.114   1.00 50.98  ? 110 ASN C CA    1 
ATOM   8936  C C     . ASN C 1 110 ? 34.743  24.867  5.230   1.00 49.56  ? 110 ASN C C     1 
ATOM   8937  O O     . ASN C 1 110 ? 35.896  25.276  5.031   1.00 47.88  ? 110 ASN C O     1 
ATOM   8938  C CB    . ASN C 1 110 ? 33.938  26.163  3.254   1.00 59.14  ? 110 ASN C CB    1 
ATOM   8939  C CG    . ASN C 1 110 ? 34.030  27.411  4.103   1.00 57.33  ? 110 ASN C CG    1 
ATOM   8940  O OD1   . ASN C 1 110 ? 33.241  27.591  5.031   1.00 50.36  ? 110 ASN C OD1   1 
ATOM   8941  N ND2   . ASN C 1 110 ? 35.040  28.222  3.840   1.00 59.72  ? 110 ASN C ND2   1 
ATOM   8942  N N     . ARG C 1 111 ? 34.336  24.333  6.390   1.00 54.23  ? 111 ARG C N     1 
ATOM   8943  C CA    . ARG C 1 111 ? 35.232  24.199  7.530   1.00 55.19  ? 111 ARG C CA    1 
ATOM   8944  C C     . ARG C 1 111 ? 36.054  22.912  7.451   1.00 55.80  ? 111 ARG C C     1 
ATOM   8945  O O     . ARG C 1 111 ? 35.586  21.847  7.041   1.00 53.42  ? 111 ARG C O     1 
ATOM   8946  C CB    . ARG C 1 111 ? 34.451  24.231  8.840   1.00 59.93  ? 111 ARG C CB    1 
ATOM   8947  C CG    . ARG C 1 111 ? 33.626  25.493  9.025   1.00 68.50  ? 111 ARG C CG    1 
ATOM   8948  C CD    . ARG C 1 111 ? 32.438  25.209  9.918   1.00 75.53  ? 111 ARG C CD    1 
ATOM   8949  N NE    . ARG C 1 111 ? 32.851  24.779  11.246  1.00 72.62  ? 111 ARG C NE    1 
ATOM   8950  C CZ    . ARG C 1 111 ? 32.044  24.188  12.123  1.00 79.82  ? 111 ARG C CZ    1 
ATOM   8951  N NH1   . ARG C 1 111 ? 30.853  23.761  11.732  1.00 74.35  ? 111 ARG C NH1   1 
ATOM   8952  N NH2   . ARG C 1 111 ? 32.442  23.993  13.374  1.00 76.23  ? 111 ARG C NH2   1 
ATOM   8953  N N     . ILE C 1 112 ? 37.316  23.073  7.845   1.00 53.65  ? 112 ILE C N     1 
ATOM   8954  C CA    . ILE C 1 112 ? 38.229  21.992  8.131   1.00 46.63  ? 112 ILE C CA    1 
ATOM   8955  C C     . ILE C 1 112 ? 38.094  21.641  9.608   1.00 44.00  ? 112 ILE C C     1 
ATOM   8956  O O     . ILE C 1 112 ? 38.668  22.328  10.446  1.00 43.49  ? 112 ILE C O     1 
ATOM   8957  C CB    . ILE C 1 112 ? 39.650  22.447  7.764   1.00 44.51  ? 112 ILE C CB    1 
ATOM   8958  C CG1   . ILE C 1 112 ? 39.757  22.763  6.264   1.00 44.94  ? 112 ILE C CG1   1 
ATOM   8959  C CG2   . ILE C 1 112 ? 40.669  21.420  8.227   1.00 42.98  ? 112 ILE C CG2   1 
ATOM   8960  C CD1   . ILE C 1 112 ? 41.042  23.469  5.856   1.00 41.33  ? 112 ILE C CD1   1 
ATOM   8961  N N     . LEU C 1 113 ? 37.320  20.589  9.917   1.00 44.25  ? 113 LEU C N     1 
ATOM   8962  C CA    . LEU C 1 113 ? 36.902  20.314  11.289  1.00 43.40  ? 113 LEU C CA    1 
ATOM   8963  C C     . LEU C 1 113 ? 38.067  19.752  12.103  1.00 43.93  ? 113 LEU C C     1 
ATOM   8964  O O     . LEU C 1 113 ? 38.118  19.932  13.310  1.00 49.64  ? 113 LEU C O     1 
ATOM   8965  C CB    . LEU C 1 113 ? 35.722  19.344  11.244  1.00 44.61  ? 113 LEU C CB    1 
ATOM   8966  C CG    . LEU C 1 113 ? 34.419  19.943  10.699  1.00 46.78  ? 113 LEU C CG    1 
ATOM   8967  C CD1   . LEU C 1 113 ? 33.360  18.871  10.446  1.00 45.01  ? 113 LEU C CD1   1 
ATOM   8968  C CD2   . LEU C 1 113 ? 33.868  20.987  11.666  1.00 45.51  ? 113 LEU C CD2   1 
ATOM   8969  N N     . GLU C 1 114 ? 38.990  19.060  11.431  1.00 42.53  ? 114 GLU C N     1 
ATOM   8970  C CA    . GLU C 1 114 ? 40.181  18.528  12.052  1.00 42.00  ? 114 GLU C CA    1 
ATOM   8971  C C     . GLU C 1 114 ? 41.190  18.089  10.998  1.00 39.40  ? 114 GLU C C     1 
ATOM   8972  O O     . GLU C 1 114 ? 40.820  17.553  9.970   1.00 42.43  ? 114 GLU C O     1 
ATOM   8973  C CB    . GLU C 1 114 ? 39.875  17.319  12.928  1.00 47.79  ? 114 GLU C CB    1 
ATOM   8974  C CG    . GLU C 1 114 ? 41.089  16.873  13.742  1.00 52.94  ? 114 GLU C CG    1 
ATOM   8975  C CD    . GLU C 1 114 ? 40.903  15.659  14.647  1.00 55.36  ? 114 GLU C CD    1 
ATOM   8976  O OE1   . GLU C 1 114 ? 39.784  15.037  14.628  1.00 49.64  ? 114 GLU C OE1   1 
ATOM   8977  O OE2   . GLU C 1 114 ? 41.890  15.344  15.387  1.00 55.21  ? 114 GLU C OE2   1 
ATOM   8978  N N     . VAL C 1 115 ? 42.472  18.303  11.299  1.00 40.23  ? 115 VAL C N     1 
ATOM   8979  C CA    . VAL C 1 115 ? 43.562  17.658  10.598  1.00 41.09  ? 115 VAL C CA    1 
ATOM   8980  C C     . VAL C 1 115 ? 44.458  17.061  11.659  1.00 41.49  ? 115 VAL C C     1 
ATOM   8981  O O     . VAL C 1 115 ? 45.050  17.803  12.418  1.00 40.11  ? 115 VAL C O     1 
ATOM   8982  C CB    . VAL C 1 115 ? 44.384  18.599  9.705   1.00 43.92  ? 115 VAL C CB    1 
ATOM   8983  C CG1   . VAL C 1 115 ? 45.669  17.932  9.267   1.00 41.52  ? 115 VAL C CG1   1 
ATOM   8984  C CG2   . VAL C 1 115 ? 43.593  19.078  8.490   1.00 48.74  ? 115 VAL C CG2   1 
ATOM   8985  N N     . ASN C 1 116 ? 44.606  15.727  11.631  1.00 44.56  ? 116 ASN C N     1 
ATOM   8986  C CA    . ASN C 1 116 ? 45.390  15.030  12.625  1.00 43.88  ? 116 ASN C CA    1 
ATOM   8987  C C     . ASN C 1 116 ? 46.743  14.597  12.061  1.00 44.51  ? 116 ASN C C     1 
ATOM   8988  O O     . ASN C 1 116 ? 46.793  13.744  11.195  1.00 48.80  ? 116 ASN C O     1 
ATOM   8989  C CB    . ASN C 1 116 ? 44.618  13.822  13.114  1.00 45.05  ? 116 ASN C CB    1 
ATOM   8990  C CG    . ASN C 1 116 ? 45.274  13.232  14.331  1.00 40.45  ? 116 ASN C CG    1 
ATOM   8991  O OD1   . ASN C 1 116 ? 46.487  13.024  14.366  1.00 38.34  ? 116 ASN C OD1   1 
ATOM   8992  N ND2   . ASN C 1 116 ? 44.458  13.004  15.332  1.00 41.25  ? 116 ASN C ND2   1 
ATOM   8993  N N     . GLU C 1 117 ? 47.846  15.125  12.599  1.00 42.43  ? 117 GLU C N     1 
ATOM   8994  C CA    . GLU C 1 117 ? 49.168  14.833  12.068  1.00 38.13  ? 117 GLU C CA    1 
ATOM   8995  C C     . GLU C 1 117 ? 49.626  13.440  12.507  1.00 37.61  ? 117 GLU C C     1 
ATOM   8996  O O     . GLU C 1 117 ? 50.245  12.726  11.729  1.00 40.44  ? 117 GLU C O     1 
ATOM   8997  C CB    . GLU C 1 117 ? 50.157  15.905  12.523  1.00 38.29  ? 117 GLU C CB    1 
ATOM   8998  C CG    . GLU C 1 117 ? 51.576  15.597  12.087  1.00 46.63  ? 117 GLU C CG    1 
ATOM   8999  C CD    . GLU C 1 117 ? 52.624  16.648  12.407  1.00 48.07  ? 117 GLU C CD    1 
ATOM   9000  O OE1   . GLU C 1 117 ? 52.896  16.817  13.600  1.00 52.49  ? 117 GLU C OE1   1 
ATOM   9001  O OE2   . GLU C 1 117 ? 53.163  17.296  11.454  1.00 50.06  ? 117 GLU C OE2   1 
ATOM   9002  N N     . GLU C 1 118 ? 49.365  13.077  13.763  1.00 38.54  ? 118 GLU C N     1 
ATOM   9003  C CA    . GLU C 1 118 ? 49.934  11.870  14.336  1.00 42.08  ? 118 GLU C CA    1 
ATOM   9004  C C     . GLU C 1 118 ? 49.305  10.653  13.661  1.00 39.06  ? 118 GLU C C     1 
ATOM   9005  O O     . GLU C 1 118 ? 49.974  9.657   13.515  1.00 41.91  ? 118 GLU C O     1 
ATOM   9006  C CB    . GLU C 1 118 ? 49.820  11.816  15.875  1.00 49.81  ? 118 GLU C CB    1 
ATOM   9007  C CG    . GLU C 1 118 ? 48.483  12.226  16.486  1.00 59.99  ? 118 GLU C CG    1 
ATOM   9008  C CD    . GLU C 1 118 ? 48.256  12.112  18.003  1.00 69.49  ? 118 GLU C CD    1 
ATOM   9009  O OE1   . GLU C 1 118 ? 48.927  11.329  18.710  1.00 58.26  ? 118 GLU C OE1   1 
ATOM   9010  O OE2   . GLU C 1 118 ? 47.368  12.833  18.500  1.00 88.30  ? 118 GLU C OE2   1 
ATOM   9011  N N     . PHE C 1 119 ? 48.025  10.743  13.282  1.00 41.56  ? 119 PHE C N     1 
ATOM   9012  C CA    . PHE C 1 119 ? 47.260  9.657   12.690  1.00 38.06  ? 119 PHE C CA    1 
ATOM   9013  C C     . PHE C 1 119 ? 47.000  9.861   11.182  1.00 40.30  ? 119 PHE C C     1 
ATOM   9014  O O     . PHE C 1 119 ? 46.288  9.092   10.548  1.00 43.69  ? 119 PHE C O     1 
ATOM   9015  C CB    . PHE C 1 119 ? 45.916  9.572   13.414  1.00 41.38  ? 119 PHE C CB    1 
ATOM   9016  C CG    . PHE C 1 119 ? 45.931  9.238   14.888  1.00 45.31  ? 119 PHE C CG    1 
ATOM   9017  C CD1   . PHE C 1 119 ? 46.586  8.117   15.365  1.00 43.39  ? 119 PHE C CD1   1 
ATOM   9018  C CD2   . PHE C 1 119 ? 45.167  9.975   15.788  1.00 50.37  ? 119 PHE C CD2   1 
ATOM   9019  C CE1   . PHE C 1 119 ? 46.539  7.795   16.712  1.00 49.03  ? 119 PHE C CE1   1 
ATOM   9020  C CE2   . PHE C 1 119 ? 45.122  9.660   17.140  1.00 46.25  ? 119 PHE C CE2   1 
ATOM   9021  C CZ    . PHE C 1 119 ? 45.808  8.564   17.599  1.00 48.31  ? 119 PHE C CZ    1 
ATOM   9022  N N     . GLY C 1 120 ? 47.521  10.939  10.590  1.00 40.91  ? 120 GLY C N     1 
ATOM   9023  C CA    . GLY C 1 120 ? 47.436  11.186  9.159   1.00 34.94  ? 120 GLY C CA    1 
ATOM   9024  C C     . GLY C 1 120 ? 46.004  11.241  8.634   1.00 37.89  ? 120 GLY C C     1 
ATOM   9025  O O     . GLY C 1 120 ? 45.652  10.500  7.731   1.00 46.84  ? 120 GLY C O     1 
ATOM   9026  N N     . TYR C 1 121 ? 45.170  12.154  9.121   1.00 39.28  ? 121 TYR C N     1 
ATOM   9027  C CA    . TYR C 1 121 ? 43.841  12.271  8.552   1.00 37.87  ? 121 TYR C CA    1 
ATOM   9028  C C     . TYR C 1 121 ? 43.388  13.716  8.562   1.00 38.11  ? 121 TYR C C     1 
ATOM   9029  O O     . TYR C 1 121 ? 44.072  14.556  9.111   1.00 36.83  ? 121 TYR C O     1 
ATOM   9030  C CB    . TYR C 1 121 ? 42.854  11.312  9.221   1.00 37.86  ? 121 TYR C CB    1 
ATOM   9031  C CG    . TYR C 1 121 ? 42.376  11.628  10.610  1.00 37.12  ? 121 TYR C CG    1 
ATOM   9032  C CD1   . TYR C 1 121 ? 41.421  12.599  10.829  1.00 40.15  ? 121 TYR C CD1   1 
ATOM   9033  C CD2   . TYR C 1 121 ? 42.769  10.861  11.697  1.00 37.83  ? 121 TYR C CD2   1 
ATOM   9034  C CE1   . TYR C 1 121 ? 40.940  12.856  12.109  1.00 41.73  ? 121 TYR C CE1   1 
ATOM   9035  C CE2   . TYR C 1 121 ? 42.283  11.091  12.977  1.00 35.94  ? 121 TYR C CE2   1 
ATOM   9036  C CZ    . TYR C 1 121 ? 41.396  12.128  13.194  1.00 36.49  ? 121 TYR C CZ    1 
ATOM   9037  O OH    . TYR C 1 121 ? 40.862  12.406  14.434  1.00 34.07  ? 121 TYR C OH    1 
ATOM   9038  N N     . ALA C 1 122 ? 42.286  13.973  7.842   1.00 45.23  ? 122 ALA C N     1 
ATOM   9039  C CA    . ALA C 1 122 ? 41.509  15.203  7.947   1.00 45.12  ? 122 ALA C CA    1 
ATOM   9040  C C     . ALA C 1 122 ? 40.022  14.861  7.992   1.00 39.09  ? 122 ALA C C     1 
ATOM   9041  O O     . ALA C 1 122 ? 39.609  13.845  7.427   1.00 38.25  ? 122 ALA C O     1 
ATOM   9042  C CB    . ALA C 1 122 ? 41.821  16.104  6.785   1.00 46.18  ? 122 ALA C CB    1 
ATOM   9043  N N     . LEU C 1 123 ? 39.247  15.678  8.719   1.00 35.50  ? 123 LEU C N     1 
ATOM   9044  C CA    . LEU C 1 123 ? 37.793  15.641  8.645   1.00 34.60  ? 123 LEU C CA    1 
ATOM   9045  C C     . LEU C 1 123 ? 37.354  16.984  8.090   1.00 42.33  ? 123 LEU C C     1 
ATOM   9046  O O     . LEU C 1 123 ? 37.667  18.023  8.693   1.00 47.12  ? 123 LEU C O     1 
ATOM   9047  C CB    . LEU C 1 123 ? 37.178  15.391  10.020  1.00 38.78  ? 123 LEU C CB    1 
ATOM   9048  C CG    . LEU C 1 123 ? 35.651  15.470  10.114  1.00 36.02  ? 123 LEU C CG    1 
ATOM   9049  C CD1   . LEU C 1 123 ? 34.984  14.370  9.325   1.00 34.34  ? 123 LEU C CD1   1 
ATOM   9050  C CD2   . LEU C 1 123 ? 35.240  15.363  11.560  1.00 34.60  ? 123 LEU C CD2   1 
ATOM   9051  N N     . VAL C 1 124 ? 36.670  16.932  6.928   1.00 37.36  ? 124 VAL C N     1 
ATOM   9052  C CA    . VAL C 1 124 ? 36.376  18.114  6.143   1.00 38.82  ? 124 VAL C CA    1 
ATOM   9053  C C     . VAL C 1 124 ? 34.897  18.148  5.742   1.00 38.34  ? 124 VAL C C     1 
ATOM   9054  O O     . VAL C 1 124 ? 34.240  17.097  5.671   1.00 35.78  ? 124 VAL C O     1 
ATOM   9055  C CB    . VAL C 1 124 ? 37.274  18.176  4.899   1.00 38.67  ? 124 VAL C CB    1 
ATOM   9056  C CG1   . VAL C 1 124 ? 38.725  18.289  5.296   1.00 42.76  ? 124 VAL C CG1   1 
ATOM   9057  C CG2   . VAL C 1 124 ? 37.054  16.989  3.967   1.00 40.96  ? 124 VAL C CG2   1 
ATOM   9058  N N     . GLU C 1 125 ? 34.438  19.382  5.456   1.00 29.42  ? 125 GLU C N     1 
ATOM   9059  C CA    . GLU C 1 125 ? 33.102  19.653  4.980   1.00 35.12  ? 125 GLU C CA    1 
ATOM   9060  C C     . GLU C 1 125 ? 33.155  19.781  3.458   1.00 32.14  ? 125 GLU C C     1 
ATOM   9061  O O     . GLU C 1 125 ? 34.225  19.866  2.861   1.00 35.64  ? 125 GLU C O     1 
ATOM   9062  C CB    . GLU C 1 125 ? 32.544  20.920  5.620   1.00 41.54  ? 125 GLU C CB    1 
ATOM   9063  C CG    . GLU C 1 125 ? 32.422  20.869  7.128   1.00 46.23  ? 125 GLU C CG    1 
ATOM   9064  C CD    . GLU C 1 125 ? 31.496  21.939  7.693   1.00 51.24  ? 125 GLU C CD    1 
ATOM   9065  O OE1   . GLU C 1 125 ? 31.796  23.173  7.532   1.00 52.69  ? 125 GLU C OE1   1 
ATOM   9066  O OE2   . GLU C 1 125 ? 30.453  21.539  8.255   1.00 50.98  ? 125 GLU C OE2   1 
ATOM   9067  N N     . PRO C 1 126 ? 32.006  19.719  2.770   1.00 29.98  ? 126 PRO C N     1 
ATOM   9068  C CA    . PRO C 1 126 ? 31.963  19.745  1.303   1.00 35.54  ? 126 PRO C CA    1 
ATOM   9069  C C     . PRO C 1 126 ? 32.665  20.901  0.584   1.00 40.80  ? 126 PRO C C     1 
ATOM   9070  O O     . PRO C 1 126 ? 33.346  20.678  -0.407  1.00 57.05  ? 126 PRO C O     1 
ATOM   9071  C CB    . PRO C 1 126 ? 30.444  19.771  1.064   1.00 32.50  ? 126 PRO C CB    1 
ATOM   9072  C CG    . PRO C 1 126 ? 29.938  18.947  2.151   1.00 30.16  ? 126 PRO C CG    1 
ATOM   9073  C CD    . PRO C 1 126 ? 30.689  19.478  3.349   1.00 30.24  ? 126 PRO C CD    1 
ATOM   9074  N N     . GLY C 1 127 ? 32.562  22.130  1.095   1.00 45.64  ? 127 GLY C N     1 
ATOM   9075  C CA    . GLY C 1 127 ? 33.145  23.276  0.412   1.00 42.27  ? 127 GLY C CA    1 
ATOM   9076  C C     . GLY C 1 127 ? 34.659  23.447  0.605   1.00 46.41  ? 127 GLY C C     1 
ATOM   9077  O O     . GLY C 1 127 ? 35.216  24.463  0.175   1.00 54.67  ? 127 GLY C O     1 
ATOM   9078  N N     . VAL C 1 128 ? 35.346  22.535  1.307   1.00 44.82  ? 128 VAL C N     1 
ATOM   9079  C CA    . VAL C 1 128 ? 36.796  22.663  1.395   1.00 41.06  ? 128 VAL C CA    1 
ATOM   9080  C C     . VAL C 1 128 ? 37.370  22.195  0.072   1.00 42.34  ? 128 VAL C C     1 
ATOM   9081  O O     . VAL C 1 128 ? 37.000  21.135  -0.420  1.00 48.54  ? 128 VAL C O     1 
ATOM   9082  C CB    . VAL C 1 128 ? 37.431  21.850  2.525   1.00 41.52  ? 128 VAL C CB    1 
ATOM   9083  C CG1   . VAL C 1 128 ? 38.964  21.914  2.474   1.00 41.34  ? 128 VAL C CG1   1 
ATOM   9084  C CG2   . VAL C 1 128 ? 36.884  22.245  3.887   1.00 39.97  ? 128 VAL C CG2   1 
ATOM   9085  N N     . SER C 1 129 ? 38.250  23.020  -0.484  1.00 45.34  ? 129 SER C N     1 
ATOM   9086  C CA    . SER C 1 129 ? 38.968  22.705  -1.708  1.00 45.18  ? 129 SER C CA    1 
ATOM   9087  C C     . SER C 1 129 ? 40.362  22.190  -1.354  1.00 39.63  ? 129 SER C C     1 
ATOM   9088  O O     . SER C 1 129 ? 40.830  22.323  -0.218  1.00 36.54  ? 129 SER C O     1 
ATOM   9089  C CB    . SER C 1 129 ? 39.069  23.924  -2.613  1.00 42.29  ? 129 SER C CB    1 
ATOM   9090  O OG    . SER C 1 129 ? 40.046  24.843  -2.115  1.00 46.78  ? 129 SER C OG    1 
ATOM   9091  N N     . TYR C 1 130 ? 41.022  21.661  -2.377  1.00 37.62  ? 130 TYR C N     1 
ATOM   9092  C CA    . TYR C 1 130 ? 42.407  21.243  -2.302  1.00 40.77  ? 130 TYR C CA    1 
ATOM   9093  C C     . TYR C 1 130 ? 43.293  22.409  -1.907  1.00 42.98  ? 130 TYR C C     1 
ATOM   9094  O O     . TYR C 1 130 ? 44.105  22.248  -0.995  1.00 43.82  ? 130 TYR C O     1 
ATOM   9095  C CB    . TYR C 1 130 ? 42.817  20.623  -3.629  1.00 38.03  ? 130 TYR C CB    1 
ATOM   9096  C CG    . TYR C 1 130 ? 42.102  19.332  -3.932  1.00 36.67  ? 130 TYR C CG    1 
ATOM   9097  C CD1   . TYR C 1 130 ? 42.415  18.147  -3.283  1.00 41.86  ? 130 TYR C CD1   1 
ATOM   9098  C CD2   . TYR C 1 130 ? 41.069  19.313  -4.844  1.00 40.56  ? 130 TYR C CD2   1 
ATOM   9099  C CE1   . TYR C 1 130 ? 41.737  16.968  -3.563  1.00 45.34  ? 130 TYR C CE1   1 
ATOM   9100  C CE2   . TYR C 1 130 ? 40.403  18.148  -5.162  1.00 43.38  ? 130 TYR C CE2   1 
ATOM   9101  C CZ    . TYR C 1 130 ? 40.731  16.971  -4.515  1.00 41.69  ? 130 TYR C CZ    1 
ATOM   9102  O OH    . TYR C 1 130 ? 40.057  15.868  -4.919  1.00 33.72  ? 130 TYR C OH    1 
ATOM   9103  N N     . PHE C 1 131 ? 43.082  23.577  -2.554  1.00 45.49  ? 131 PHE C N     1 
ATOM   9104  C CA    . PHE C 1 131 ? 43.831  24.800  -2.234  1.00 42.62  ? 131 PHE C CA    1 
ATOM   9105  C C     . PHE C 1 131 ? 43.691  25.125  -0.741  1.00 38.93  ? 131 PHE C C     1 
ATOM   9106  O O     . PHE C 1 131 ? 44.688  25.210  -0.038  1.00 38.38  ? 131 PHE C O     1 
ATOM   9107  C CB    . PHE C 1 131 ? 43.447  25.964  -3.167  1.00 37.37  ? 131 PHE C CB    1 
ATOM   9108  C CG    . PHE C 1 131 ? 44.044  25.858  -4.546  1.00 33.49  ? 131 PHE C CG    1 
ATOM   9109  C CD1   . PHE C 1 131 ? 45.408  26.013  -4.734  1.00 39.99  ? 131 PHE C CD1   1 
ATOM   9110  C CD2   . PHE C 1 131 ? 43.261  25.528  -5.634  1.00 34.43  ? 131 PHE C CD2   1 
ATOM   9111  C CE1   . PHE C 1 131 ? 45.979  25.851  -5.987  1.00 43.36  ? 131 PHE C CE1   1 
ATOM   9112  C CE2   . PHE C 1 131 ? 43.825  25.347  -6.884  1.00 37.44  ? 131 PHE C CE2   1 
ATOM   9113  C CZ    . PHE C 1 131 ? 45.185  25.500  -7.059  1.00 45.99  ? 131 PHE C CZ    1 
ATOM   9114  N N     . GLU C 1 132 ? 42.451  25.234  -0.247  1.00 40.76  ? 132 GLU C N     1 
ATOM   9115  C CA    . GLU C 1 132 ? 42.197  25.537  1.154   1.00 41.47  ? 132 GLU C CA    1 
ATOM   9116  C C     . GLU C 1 132 ? 42.890  24.537  2.068   1.00 42.58  ? 132 GLU C C     1 
ATOM   9117  O O     . GLU C 1 132 ? 43.446  24.941  3.084   1.00 55.88  ? 132 GLU C O     1 
ATOM   9118  C CB    . GLU C 1 132 ? 40.690  25.567  1.427   1.00 48.65  ? 132 GLU C CB    1 
ATOM   9119  C CG    . GLU C 1 132 ? 39.980  26.789  0.866   1.00 51.44  ? 132 GLU C CG    1 
ATOM   9120  C CD    . GLU C 1 132 ? 38.475  26.665  0.751   1.00 52.68  ? 132 GLU C CD    1 
ATOM   9121  O OE1   . GLU C 1 132 ? 37.947  25.607  1.100   1.00 58.75  ? 132 GLU C OE1   1 
ATOM   9122  O OE2   . GLU C 1 132 ? 37.834  27.628  0.308   1.00 63.64  ? 132 GLU C OE2   1 
ATOM   9123  N N     . LEU C 1 133 ? 42.851  23.231  1.726   1.00 47.12  ? 133 LEU C N     1 
ATOM   9124  C CA    . LEU C 1 133 ? 43.415  22.205  2.599   1.00 36.76  ? 133 LEU C CA    1 
ATOM   9125  C C     . LEU C 1 133 ? 44.931  22.240  2.509   1.00 36.48  ? 133 LEU C C     1 
ATOM   9126  O O     . LEU C 1 133 ? 45.592  22.205  3.542   1.00 38.23  ? 133 LEU C O     1 
ATOM   9127  C CB    . LEU C 1 133 ? 42.869  20.824  2.240   1.00 37.79  ? 133 LEU C CB    1 
ATOM   9128  C CG    . LEU C 1 133 ? 43.221  19.673  3.183   1.00 39.24  ? 133 LEU C CG    1 
ATOM   9129  C CD1   . LEU C 1 133 ? 42.829  19.961  4.617   1.00 37.68  ? 133 LEU C CD1   1 
ATOM   9130  C CD2   . LEU C 1 133 ? 42.539  18.402  2.710   1.00 41.04  ? 133 LEU C CD2   1 
ATOM   9131  N N     . TYR C 1 134 ? 45.486  22.401  1.298   1.00 35.86  ? 134 TYR C N     1 
ATOM   9132  C CA    . TYR C 1 134 ? 46.934  22.441  1.175   1.00 39.38  ? 134 TYR C CA    1 
ATOM   9133  C C     . TYR C 1 134 ? 47.462  23.568  2.046   1.00 48.62  ? 134 TYR C C     1 
ATOM   9134  O O     . TYR C 1 134 ? 48.360  23.344  2.849   1.00 51.25  ? 134 TYR C O     1 
ATOM   9135  C CB    . TYR C 1 134 ? 47.386  22.563  -0.278  1.00 41.95  ? 134 TYR C CB    1 
ATOM   9136  C CG    . TYR C 1 134 ? 48.881  22.658  -0.441  1.00 43.45  ? 134 TYR C CG    1 
ATOM   9137  C CD1   . TYR C 1 134 ? 49.684  21.535  -0.392  1.00 47.88  ? 134 TYR C CD1   1 
ATOM   9138  C CD2   . TYR C 1 134 ? 49.503  23.877  -0.670  1.00 48.63  ? 134 TYR C CD2   1 
ATOM   9139  C CE1   . TYR C 1 134 ? 51.062  21.616  -0.563  1.00 52.21  ? 134 TYR C CE1   1 
ATOM   9140  C CE2   . TYR C 1 134 ? 50.880  23.981  -0.841  1.00 48.07  ? 134 TYR C CE2   1 
ATOM   9141  C CZ    . TYR C 1 134 ? 51.665  22.845  -0.788  1.00 54.84  ? 134 TYR C CZ    1 
ATOM   9142  O OH    . TYR C 1 134 ? 53.024  22.944  -0.932  1.00 54.30  ? 134 TYR C OH    1 
ATOM   9143  N N     . ASP C 1 135 ? 46.830  24.752  1.938   1.00 59.81  ? 135 ASP C N     1 
ATOM   9144  C CA    . ASP C 1 135 ? 47.292  25.970  2.607   1.00 56.42  ? 135 ASP C CA    1 
ATOM   9145  C C     . ASP C 1 135 ? 47.222  25.814  4.136   1.00 53.13  ? 135 ASP C C     1 
ATOM   9146  O O     . ASP C 1 135 ? 48.186  26.126  4.844   1.00 55.00  ? 135 ASP C O     1 
ATOM   9147  C CB    . ASP C 1 135 ? 46.548  27.213  2.076   1.00 53.23  ? 135 ASP C CB    1 
ATOM   9148  C CG    . ASP C 1 135 ? 46.808  27.578  0.611   1.00 53.51  ? 135 ASP C CG    1 
ATOM   9149  O OD1   . ASP C 1 135 ? 47.960  27.433  0.149   1.00 48.08  ? 135 ASP C OD1   1 
ATOM   9150  O OD2   . ASP C 1 135 ? 45.854  28.039  -0.062  1.00 57.31  ? 135 ASP C OD2   1 
ATOM   9151  N N     . TYR C 1 136 ? 46.089  25.309  4.648   1.00 51.68  ? 136 TYR C N     1 
ATOM   9152  C CA    . TYR C 1 136 ? 45.912  25.063  6.080   1.00 50.43  ? 136 TYR C CA    1 
ATOM   9153  C C     . TYR C 1 136 ? 47.062  24.228  6.633   1.00 50.58  ? 136 TYR C C     1 
ATOM   9154  O O     . TYR C 1 136 ? 47.555  24.527  7.724   1.00 61.40  ? 136 TYR C O     1 
ATOM   9155  C CB    . TYR C 1 136 ? 44.554  24.396  6.341   1.00 53.21  ? 136 TYR C CB    1 
ATOM   9156  C CG    . TYR C 1 136 ? 44.228  24.100  7.783   1.00 51.31  ? 136 TYR C CG    1 
ATOM   9157  C CD1   . TYR C 1 136 ? 44.731  22.966  8.396   1.00 56.50  ? 136 TYR C CD1   1 
ATOM   9158  C CD2   . TYR C 1 136 ? 43.415  24.934  8.531   1.00 50.85  ? 136 TYR C CD2   1 
ATOM   9159  C CE1   . TYR C 1 136 ? 44.481  22.681  9.723   1.00 49.37  ? 136 TYR C CE1   1 
ATOM   9160  C CE2   . TYR C 1 136 ? 43.125  24.651  9.853   1.00 55.63  ? 136 TYR C CE2   1 
ATOM   9161  C CZ    . TYR C 1 136 ? 43.667  23.522  10.456  1.00 60.36  ? 136 TYR C CZ    1 
ATOM   9162  O OH    . TYR C 1 136 ? 43.426  23.180  11.773  1.00 59.73  ? 136 TYR C OH    1 
ATOM   9163  N N     . ILE C 1 137 ? 47.488  23.214  5.862   1.00 47.37  ? 137 ILE C N     1 
ATOM   9164  C CA    . ILE C 1 137 ? 48.526  22.286  6.277   1.00 49.53  ? 137 ILE C CA    1 
ATOM   9165  C C     . ILE C 1 137 ? 49.884  22.974  6.260   1.00 50.70  ? 137 ILE C C     1 
ATOM   9166  O O     . ILE C 1 137 ? 50.640  22.853  7.226   1.00 51.93  ? 137 ILE C O     1 
ATOM   9167  C CB    . ILE C 1 137 ? 48.511  20.997  5.418   1.00 45.65  ? 137 ILE C CB    1 
ATOM   9168  C CG1   . ILE C 1 137 ? 47.294  20.128  5.747   1.00 44.37  ? 137 ILE C CG1   1 
ATOM   9169  C CG2   . ILE C 1 137 ? 49.800  20.213  5.581   1.00 42.61  ? 137 ILE C CG2   1 
ATOM   9170  C CD1   . ILE C 1 137 ? 47.015  19.039  4.749   1.00 42.38  ? 137 ILE C CD1   1 
ATOM   9171  N N     . GLN C 1 138 ? 50.210  23.661  5.156   1.00 58.17  ? 138 GLN C N     1 
ATOM   9172  C CA    . GLN C 1 138 ? 51.486  24.362  5.065   1.00 56.32  ? 138 GLN C CA    1 
ATOM   9173  C C     . GLN C 1 138 ? 51.577  25.383  6.190   1.00 55.73  ? 138 GLN C C     1 
ATOM   9174  O O     . GLN C 1 138 ? 52.641  25.499  6.790   1.00 55.08  ? 138 GLN C O     1 
ATOM   9175  C CB    . GLN C 1 138 ? 51.716  25.052  3.715   1.00 56.25  ? 138 GLN C CB    1 
ATOM   9176  C CG    . GLN C 1 138 ? 51.952  24.094  2.544   1.00 63.63  ? 138 GLN C CG    1 
ATOM   9177  C CD    . GLN C 1 138 ? 52.917  22.942  2.777   1.00 64.01  ? 138 GLN C CD    1 
ATOM   9178  O OE1   . GLN C 1 138 ? 54.140  23.071  2.702   1.00 59.82  ? 138 GLN C OE1   1 
ATOM   9179  N NE2   . GLN C 1 138 ? 52.366  21.761  3.002   1.00 59.27  ? 138 GLN C NE2   1 
ATOM   9180  N N     . GLU C 1 139 ? 50.454  26.057  6.497   1.00 56.93  ? 139 GLU C N     1 
ATOM   9181  C CA    . GLU C 1 139 ? 50.449  27.178  7.431   1.00 70.17  ? 139 GLU C CA    1 
ATOM   9182  C C     . GLU C 1 139 ? 50.654  26.743  8.879   1.00 63.34  ? 139 GLU C C     1 
ATOM   9183  O O     . GLU C 1 139 ? 51.113  27.551  9.677   1.00 60.40  ? 139 GLU C O     1 
ATOM   9184  C CB    . GLU C 1 139 ? 49.147  27.977  7.377   1.00 76.47  ? 139 GLU C CB    1 
ATOM   9185  C CG    . GLU C 1 139 ? 49.123  29.000  6.262   1.00 89.70  ? 139 GLU C CG    1 
ATOM   9186  C CD    . GLU C 1 139 ? 47.743  29.579  5.994   1.00 99.01  ? 139 GLU C CD    1 
ATOM   9187  O OE1   . GLU C 1 139 ? 47.506  30.064  4.870   1.00 106.68 ? 139 GLU C OE1   1 
ATOM   9188  O OE2   . GLU C 1 139 ? 46.911  29.555  6.917   1.00 101.65 ? 139 GLU C OE2   1 
ATOM   9189  N N     . LYS C 1 140 ? 50.264  25.513  9.232   1.00 62.54  ? 140 LYS C N     1 
ATOM   9190  C CA    . LYS C 1 140 ? 50.384  25.050  10.611  1.00 56.79  ? 140 LYS C CA    1 
ATOM   9191  C C     . LYS C 1 140 ? 51.651  24.214  10.728  1.00 49.31  ? 140 LYS C C     1 
ATOM   9192  O O     . LYS C 1 140 ? 51.985  23.743  11.811  1.00 52.14  ? 140 LYS C O     1 
ATOM   9193  C CB    . LYS C 1 140 ? 49.181  24.204  11.050  1.00 61.47  ? 140 LYS C CB    1 
ATOM   9194  C CG    . LYS C 1 140 ? 47.794  24.781  10.775  1.00 72.65  ? 140 LYS C CG    1 
ATOM   9195  C CD    . LYS C 1 140 ? 47.357  25.827  11.768  1.00 82.35  ? 140 LYS C CD    1 
ATOM   9196  C CE    . LYS C 1 140 ? 46.160  26.625  11.298  1.00 85.32  ? 140 LYS C CE    1 
ATOM   9197  N NZ    . LYS C 1 140 ? 46.143  27.960  11.940  1.00 86.83  ? 140 LYS C NZ    1 
ATOM   9198  N N     . GLY C 1 141 ? 52.327  24.013  9.593   1.00 50.49  ? 141 GLY C N     1 
ATOM   9199  C CA    . GLY C 1 141 ? 53.581  23.274  9.541   1.00 55.87  ? 141 GLY C CA    1 
ATOM   9200  C C     . GLY C 1 141 ? 53.419  21.758  9.736   1.00 57.84  ? 141 GLY C C     1 
ATOM   9201  O O     . GLY C 1 141 ? 54.363  21.106  10.168  1.00 58.86  ? 141 GLY C O     1 
ATOM   9202  N N     . LEU C 1 142 ? 52.245  21.194  9.394   1.00 54.73  ? 142 LEU C N     1 
ATOM   9203  C CA    . LEU C 1 142 ? 51.960  19.774  9.590   1.00 50.81  ? 142 LEU C CA    1 
ATOM   9204  C C     . LEU C 1 142 ? 52.630  18.950  8.491   1.00 49.12  ? 142 LEU C C     1 
ATOM   9205  O O     . LEU C 1 142 ? 52.497  19.263  7.305   1.00 44.50  ? 142 LEU C O     1 
ATOM   9206  C CB    . LEU C 1 142 ? 50.440  19.557  9.602   1.00 47.25  ? 142 LEU C CB    1 
ATOM   9207  C CG    . LEU C 1 142 ? 49.635  20.329  10.660  1.00 46.45  ? 142 LEU C CG    1 
ATOM   9208  C CD1   . LEU C 1 142 ? 48.145  20.008  10.579  1.00 45.37  ? 142 LEU C CD1   1 
ATOM   9209  C CD2   . LEU C 1 142 ? 50.137  20.040  12.067  1.00 45.03  ? 142 LEU C CD2   1 
ATOM   9210  N N     . LYS C 1 143 ? 53.323  17.875  8.891   1.00 47.97  ? 143 LYS C N     1 
ATOM   9211  C CA    . LYS C 1 143 ? 54.128  17.088  7.969   1.00 48.39  ? 143 LYS C CA    1 
ATOM   9212  C C     . LYS C 1 143 ? 53.220  16.100  7.226   1.00 44.89  ? 143 LYS C C     1 
ATOM   9213  O O     . LYS C 1 143 ? 53.394  14.879  7.279   1.00 50.04  ? 143 LYS C O     1 
ATOM   9214  C CB    . LYS C 1 143 ? 55.272  16.374  8.711   1.00 58.62  ? 143 LYS C CB    1 
ATOM   9215  C CG    . LYS C 1 143 ? 56.139  17.207  9.643   1.00 58.85  ? 143 LYS C CG    1 
ATOM   9216  C CD    . LYS C 1 143 ? 57.128  18.061  8.897   1.00 77.27  ? 143 LYS C CD    1 
ATOM   9217  C CE    . LYS C 1 143 ? 57.983  18.972  9.764   1.00 86.61  ? 143 LYS C CE    1 
ATOM   9218  N NZ    . LYS C 1 143 ? 57.534  20.384  9.696   1.00 76.75  ? 143 LYS C NZ    1 
ATOM   9219  N N     . LEU C 1 144 ? 52.249  16.635  6.486   1.00 45.37  ? 144 LEU C N     1 
ATOM   9220  C CA    . LEU C 1 144 ? 51.323  15.811  5.729   1.00 43.09  ? 144 LEU C CA    1 
ATOM   9221  C C     . LEU C 1 144 ? 51.271  16.287  4.283   1.00 42.54  ? 144 LEU C C     1 
ATOM   9222  O O     . LEU C 1 144 ? 51.366  17.481  4.021   1.00 39.80  ? 144 LEU C O     1 
ATOM   9223  C CB    . LEU C 1 144 ? 49.931  15.942  6.337   1.00 39.57  ? 144 LEU C CB    1 
ATOM   9224  C CG    . LEU C 1 144 ? 49.756  15.464  7.774   1.00 42.49  ? 144 LEU C CG    1 
ATOM   9225  C CD1   . LEU C 1 144 ? 48.325  15.764  8.236   1.00 45.77  ? 144 LEU C CD1   1 
ATOM   9226  C CD2   . LEU C 1 144 ? 50.043  13.960  7.903   1.00 39.99  ? 144 LEU C CD2   1 
ATOM   9227  N N     . TRP C 1 145 ? 51.044  15.335  3.369   1.00 43.79  ? 145 TRP C N     1 
ATOM   9228  C CA    . TRP C 1 145 ? 50.668  15.619  1.994   1.00 38.18  ? 145 TRP C CA    1 
ATOM   9229  C C     . TRP C 1 145 ? 49.196  15.331  1.777   1.00 37.11  ? 145 TRP C C     1 
ATOM   9230  O O     . TRP C 1 145 ? 48.616  14.420  2.371   1.00 48.78  ? 145 TRP C O     1 
ATOM   9231  C CB    . TRP C 1 145 ? 51.503  14.815  1.001   1.00 38.91  ? 145 TRP C CB    1 
ATOM   9232  C CG    . TRP C 1 145 ? 52.942  15.229  0.997   1.00 41.91  ? 145 TRP C CG    1 
ATOM   9233  C CD1   . TRP C 1 145 ? 53.512  16.167  1.807   1.00 40.49  ? 145 TRP C CD1   1 
ATOM   9234  C CD2   . TRP C 1 145 ? 53.999  14.737  0.152   1.00 40.34  ? 145 TRP C CD2   1 
ATOM   9235  N NE1   . TRP C 1 145 ? 54.846  16.271  1.537   1.00 45.85  ? 145 TRP C NE1   1 
ATOM   9236  C CE2   . TRP C 1 145 ? 55.171  15.431  0.510   1.00 42.57  ? 145 TRP C CE2   1 
ATOM   9237  C CE3   . TRP C 1 145 ? 54.083  13.778  -0.855  1.00 43.99  ? 145 TRP C CE3   1 
ATOM   9238  C CZ2   . TRP C 1 145 ? 56.398  15.215  -0.108  1.00 45.37  ? 145 TRP C CZ2   1 
ATOM   9239  C CZ3   . TRP C 1 145 ? 55.300  13.552  -1.464  1.00 47.33  ? 145 TRP C CZ3   1 
ATOM   9240  C CH2   . TRP C 1 145 ? 56.439  14.271  -1.106  1.00 43.52  ? 145 TRP C CH2   1 
ATOM   9241  N N     . ILE C 1 146 ? 48.624  16.070  0.828   1.00 40.03  ? 146 ILE C N     1 
ATOM   9242  C CA    . ILE C 1 146 ? 47.312  15.747  0.316   1.00 35.91  ? 146 ILE C CA    1 
ATOM   9243  C C     . ILE C 1 146 ? 47.532  15.119  -1.047  1.00 37.39  ? 146 ILE C C     1 
ATOM   9244  O O     . ILE C 1 146 ? 48.699  14.955  -1.425  1.00 39.17  ? 146 ILE C O     1 
ATOM   9245  C CB    . ILE C 1 146 ? 46.422  16.999  0.301   1.00 43.02  ? 146 ILE C CB    1 
ATOM   9246  C CG1   . ILE C 1 146 ? 46.982  18.109  -0.590  1.00 39.43  ? 146 ILE C CG1   1 
ATOM   9247  C CG2   . ILE C 1 146 ? 46.172  17.484  1.726   1.00 44.73  ? 146 ILE C CG2   1 
ATOM   9248  C CD1   . ILE C 1 146 ? 45.968  19.166  -0.912  1.00 40.70  ? 146 ILE C CD1   1 
ATOM   9249  N N     . ASP C 1 147 ? 46.426  14.723  -1.712  1.00 35.92  ? 147 ASP C N     1 
ATOM   9250  C CA    . ASP C 1 147 ? 46.465  14.185  -3.058  1.00 38.22  ? 147 ASP C CA    1 
ATOM   9251  C C     . ASP C 1 147 ? 45.386  14.858  -3.903  1.00 42.49  ? 147 ASP C C     1 
ATOM   9252  O O     . ASP C 1 147 ? 44.198  14.878  -3.562  1.00 50.14  ? 147 ASP C O     1 
ATOM   9253  C CB    . ASP C 1 147 ? 46.340  12.652  -3.040  1.00 38.80  ? 147 ASP C CB    1 
ATOM   9254  C CG    . ASP C 1 147 ? 46.537  12.006  -4.402  1.00 36.07  ? 147 ASP C CG    1 
ATOM   9255  O OD1   . ASP C 1 147 ? 45.668  12.184  -5.246  1.00 41.19  ? 147 ASP C OD1   1 
ATOM   9256  O OD2   . ASP C 1 147 ? 47.556  11.341  -4.612  1.00 36.45  ? 147 ASP C OD2   1 
ATOM   9257  N N     . VAL C 1 148 ? 45.797  15.265  -5.099  1.00 43.98  ? 148 VAL C N     1 
ATOM   9258  C CA    . VAL C 1 148 ? 45.234  16.432  -5.754  1.00 47.83  ? 148 VAL C CA    1 
ATOM   9259  C C     . VAL C 1 148 ? 45.004  16.129  -7.231  1.00 42.70  ? 148 VAL C C     1 
ATOM   9260  O O     . VAL C 1 148 ? 45.820  15.479  -7.876  1.00 46.77  ? 148 VAL C O     1 
ATOM   9261  C CB    . VAL C 1 148 ? 46.214  17.607  -5.562  1.00 49.43  ? 148 VAL C CB    1 
ATOM   9262  C CG1   . VAL C 1 148 ? 45.848  18.785  -6.405  1.00 65.27  ? 148 VAL C CG1   1 
ATOM   9263  C CG2   . VAL C 1 148 ? 46.290  18.067  -4.122  1.00 56.68  ? 148 VAL C CG2   1 
ATOM   9264  N N     . PRO C 1 149 ? 43.922  16.615  -7.858  1.00 47.76  ? 149 PRO C N     1 
ATOM   9265  C CA    . PRO C 1 149 ? 43.780  16.495  -9.321  1.00 48.29  ? 149 PRO C CA    1 
ATOM   9266  C C     . PRO C 1 149 ? 44.636  17.500  -10.097 1.00 52.23  ? 149 PRO C C     1 
ATOM   9267  O O     . PRO C 1 149 ? 45.112  18.487  -9.539  1.00 53.41  ? 149 PRO C O     1 
ATOM   9268  C CB    . PRO C 1 149 ? 42.274  16.731  -9.520  1.00 42.00  ? 149 PRO C CB    1 
ATOM   9269  C CG    . PRO C 1 149 ? 41.898  17.651  -8.388  1.00 49.23  ? 149 PRO C CG    1 
ATOM   9270  C CD    . PRO C 1 149 ? 42.768  17.252  -7.207  1.00 45.85  ? 149 PRO C CD    1 
ATOM   9271  N N     . ASP C 1 150 ? 44.827  17.261  -11.399 1.00 61.91  ? 150 ASP C N     1 
ATOM   9272  C CA    . ASP C 1 150 ? 45.634  18.140  -12.243 1.00 64.67  ? 150 ASP C CA    1 
ATOM   9273  C C     . ASP C 1 150 ? 44.761  18.788  -13.306 1.00 55.01  ? 150 ASP C C     1 
ATOM   9274  O O     . ASP C 1 150 ? 44.449  18.116  -14.281 1.00 43.66  ? 150 ASP C O     1 
ATOM   9275  C CB    . ASP C 1 150 ? 46.724  17.385  -13.010 1.00 66.64  ? 150 ASP C CB    1 
ATOM   9276  C CG    . ASP C 1 150 ? 47.851  18.240  -13.583 1.00 69.50  ? 150 ASP C CG    1 
ATOM   9277  O OD1   . ASP C 1 150 ? 47.753  19.531  -13.590 1.00 56.04  ? 150 ASP C OD1   1 
ATOM   9278  O OD2   . ASP C 1 150 ? 48.867  17.603  -13.972 1.00 70.08  ? 150 ASP C OD2   1 
ATOM   9279  N N     . PRO C 1 151 ? 44.396  20.086  -13.179 1.00 58.40  ? 151 PRO C N     1 
ATOM   9280  C CA    . PRO C 1 151 ? 44.833  20.938  -12.076 1.00 63.15  ? 151 PRO C CA    1 
ATOM   9281  C C     . PRO C 1 151 ? 43.917  20.847  -10.858 1.00 65.31  ? 151 PRO C C     1 
ATOM   9282  O O     . PRO C 1 151 ? 42.879  20.185  -10.881 1.00 67.01  ? 151 PRO C O     1 
ATOM   9283  C CB    . PRO C 1 151 ? 44.802  22.356  -12.671 1.00 63.52  ? 151 PRO C CB    1 
ATOM   9284  C CG    . PRO C 1 151 ? 44.035  22.261  -13.983 1.00 56.66  ? 151 PRO C CG    1 
ATOM   9285  C CD    . PRO C 1 151 ? 43.536  20.836  -14.103 1.00 60.62  ? 151 PRO C CD    1 
ATOM   9286  N N     . GLY C 1 152 ? 44.313  21.567  -9.806  1.00 72.57  ? 152 GLY C N     1 
ATOM   9287  C CA    . GLY C 1 152 ? 43.884  21.263  -8.454  1.00 77.98  ? 152 GLY C CA    1 
ATOM   9288  C C     . GLY C 1 152 ? 42.650  22.033  -7.999  1.00 74.17  ? 152 GLY C C     1 
ATOM   9289  O O     . GLY C 1 152 ? 42.528  22.375  -6.820  1.00 78.91  ? 152 GLY C O     1 
ATOM   9290  N N     . TRP C 1 153 ? 41.710  22.295  -8.906  1.00 78.28  ? 153 TRP C N     1 
ATOM   9291  C CA    . TRP C 1 153 ? 40.459  22.867  -8.433  1.00 87.84  ? 153 TRP C CA    1 
ATOM   9292  C C     . TRP C 1 153 ? 39.585  21.722  -7.944  1.00 69.52  ? 153 TRP C C     1 
ATOM   9293  O O     . TRP C 1 153 ? 39.763  20.558  -8.320  1.00 51.15  ? 153 TRP C O     1 
ATOM   9294  C CB    . TRP C 1 153 ? 39.720  23.753  -9.458  1.00 98.73  ? 153 TRP C CB    1 
ATOM   9295  C CG    . TRP C 1 153 ? 39.646  23.163  -10.831 1.00 108.51 ? 153 TRP C CG    1 
ATOM   9296  C CD1   . TRP C 1 153 ? 39.208  21.915  -11.168 1.00 103.47 ? 153 TRP C CD1   1 
ATOM   9297  C CD2   . TRP C 1 153 ? 40.075  23.787  -12.055 1.00 113.91 ? 153 TRP C CD2   1 
ATOM   9298  N NE1   . TRP C 1 153 ? 39.333  21.720  -12.516 1.00 109.48 ? 153 TRP C NE1   1 
ATOM   9299  C CE2   . TRP C 1 153 ? 39.867  22.846  -13.087 1.00 106.70 ? 153 TRP C CE2   1 
ATOM   9300  C CE3   . TRP C 1 153 ? 40.616  25.038  -12.377 1.00 119.99 ? 153 TRP C CE3   1 
ATOM   9301  C CZ2   . TRP C 1 153 ? 40.169  23.125  -14.420 1.00 107.21 ? 153 TRP C CZ2   1 
ATOM   9302  C CZ3   . TRP C 1 153 ? 40.928  25.305  -13.693 1.00 125.57 ? 153 TRP C CZ3   1 
ATOM   9303  C CH2   . TRP C 1 153 ? 40.706  24.360  -14.699 1.00 120.13 ? 153 TRP C CH2   1 
ATOM   9304  N N     . GLY C 1 154 ? 38.650  22.103  -7.083  1.00 65.62  ? 154 GLY C N     1 
ATOM   9305  C CA    . GLY C 1 154 ? 37.525  21.254  -6.768  1.00 59.95  ? 154 GLY C CA    1 
ATOM   9306  C C     . GLY C 1 154 ? 37.533  20.938  -5.291  1.00 54.76  ? 154 GLY C C     1 
ATOM   9307  O O     . GLY C 1 154 ? 38.335  21.522  -4.560  1.00 62.06  ? 154 GLY C O     1 
ATOM   9308  N N     . SER C 1 155 ? 36.676  19.979  -4.926  1.00 48.33  ? 155 SER C N     1 
ATOM   9309  C CA    . SER C 1 155 ? 36.385  19.646  -3.544  1.00 45.33  ? 155 SER C CA    1 
ATOM   9310  C C     . SER C 1 155 ? 37.003  18.297  -3.182  1.00 44.63  ? 155 SER C C     1 
ATOM   9311  O O     . SER C 1 155 ? 36.817  17.283  -3.878  1.00 41.98  ? 155 SER C O     1 
ATOM   9312  C CB    . SER C 1 155 ? 34.896  19.615  -3.300  1.00 46.66  ? 155 SER C CB    1 
ATOM   9313  O OG    . SER C 1 155 ? 34.627  18.954  -2.070  1.00 61.36  ? 155 SER C OG    1 
ATOM   9314  N N     . VAL C 1 156 ? 37.670  18.290  -2.027  1.00 36.28  ? 156 VAL C N     1 
ATOM   9315  C CA    . VAL C 1 156 ? 38.216  17.074  -1.476  1.00 35.75  ? 156 VAL C CA    1 
ATOM   9316  C C     . VAL C 1 156 ? 37.113  16.019  -1.408  1.00 37.62  ? 156 VAL C C     1 
ATOM   9317  O O     . VAL C 1 156 ? 37.362  14.861  -1.742  1.00 45.39  ? 156 VAL C O     1 
ATOM   9318  C CB    . VAL C 1 156 ? 38.848  17.330  -0.096  1.00 36.39  ? 156 VAL C CB    1 
ATOM   9319  C CG1   . VAL C 1 156 ? 39.490  16.063  0.434   1.00 38.11  ? 156 VAL C CG1   1 
ATOM   9320  C CG2   . VAL C 1 156 ? 39.888  18.452  -0.134  1.00 37.11  ? 156 VAL C CG2   1 
ATOM   9321  N N     . VAL C 1 157 ? 35.888  16.444  -1.046  1.00 40.13  ? 157 VAL C N     1 
ATOM   9322  C CA    . VAL C 1 157 ? 34.734  15.564  -0.913  1.00 36.21  ? 157 VAL C CA    1 
ATOM   9323  C C     . VAL C 1 157 ? 34.115  15.253  -2.273  1.00 39.85  ? 157 VAL C C     1 
ATOM   9324  O O     . VAL C 1 157 ? 33.954  14.080  -2.648  1.00 43.68  ? 157 VAL C O     1 
ATOM   9325  C CB    . VAL C 1 157 ? 33.708  16.175  0.050   1.00 37.50  ? 157 VAL C CB    1 
ATOM   9326  C CG1   . VAL C 1 157 ? 32.389  15.410  0.087   1.00 40.29  ? 157 VAL C CG1   1 
ATOM   9327  C CG2   . VAL C 1 157 ? 34.284  16.286  1.455   1.00 39.30  ? 157 VAL C CG2   1 
ATOM   9328  N N     . GLY C 1 158 ? 33.786  16.300  -3.033  1.00 38.89  ? 158 GLY C N     1 
ATOM   9329  C CA    . GLY C 1 158 ? 33.128  16.111  -4.323  1.00 38.85  ? 158 GLY C CA    1 
ATOM   9330  C C     . GLY C 1 158 ? 33.894  15.161  -5.241  1.00 37.72  ? 158 GLY C C     1 
ATOM   9331  O O     . GLY C 1 158 ? 33.351  14.221  -5.818  1.00 35.40  ? 158 GLY C O     1 
ATOM   9332  N N     . ASN C 1 159 ? 35.197  15.397  -5.343  1.00 37.71  ? 159 ASN C N     1 
ATOM   9333  C CA    . ASN C 1 159 ? 36.029  14.612  -6.225  1.00 33.79  ? 159 ASN C CA    1 
ATOM   9334  C C     . ASN C 1 159 ? 36.038  13.186  -5.688  1.00 35.55  ? 159 ASN C C     1 
ATOM   9335  O O     . ASN C 1 159 ? 35.855  12.236  -6.436  1.00 40.22  ? 159 ASN C O     1 
ATOM   9336  C CB    . ASN C 1 159 ? 37.395  15.285  -6.313  1.00 38.91  ? 159 ASN C CB    1 
ATOM   9337  C CG    . ASN C 1 159 ? 38.425  14.399  -6.948  1.00 41.90  ? 159 ASN C CG    1 
ATOM   9338  O OD1   . ASN C 1 159 ? 38.697  13.319  -6.435  1.00 56.95  ? 159 ASN C OD1   1 
ATOM   9339  N ND2   . ASN C 1 159 ? 39.006  14.842  -8.039  1.00 43.43  ? 159 ASN C ND2   1 
ATOM   9340  N N     . ALA C 1 160 ? 36.182  13.027  -4.373  1.00 30.19  ? 160 ALA C N     1 
ATOM   9341  C CA    . ALA C 1 160 ? 36.231  11.689  -3.827  1.00 29.91  ? 160 ALA C CA    1 
ATOM   9342  C C     . ALA C 1 160 ? 34.873  11.001  -4.009  1.00 32.98  ? 160 ALA C C     1 
ATOM   9343  O O     . ALA C 1 160 ? 34.822  9.791   -4.301  1.00 30.13  ? 160 ALA C O     1 
ATOM   9344  C CB    . ALA C 1 160 ? 36.670  11.734  -2.376  1.00 31.89  ? 160 ALA C CB    1 
ATOM   9345  N N     . LEU C 1 161 ? 33.754  11.737  -3.875  1.00 32.29  ? 161 LEU C N     1 
ATOM   9346  C CA    . LEU C 1 161 ? 32.463  11.072  -4.067  1.00 34.15  ? 161 LEU C CA    1 
ATOM   9347  C C     . LEU C 1 161 ? 32.319  10.610  -5.516  1.00 31.01  ? 161 LEU C C     1 
ATOM   9348  O O     . LEU C 1 161 ? 31.663  9.606   -5.775  1.00 38.43  ? 161 LEU C O     1 
ATOM   9349  C CB    . LEU C 1 161 ? 31.281  11.949  -3.601  1.00 35.63  ? 161 LEU C CB    1 
ATOM   9350  C CG    . LEU C 1 161 ? 31.218  12.253  -2.098  1.00 37.43  ? 161 LEU C CG    1 
ATOM   9351  C CD1   . LEU C 1 161 ? 29.968  13.008  -1.779  1.00 42.06  ? 161 LEU C CD1   1 
ATOM   9352  C CD2   . LEU C 1 161 ? 31.289  11.003  -1.222  1.00 38.35  ? 161 LEU C CD2   1 
ATOM   9353  N N     . ASP C 1 162 ? 33.032  11.239  -6.448  1.00 35.07  ? 162 ASP C N     1 
ATOM   9354  C CA    . ASP C 1 162 ? 32.921  10.861  -7.852  1.00 43.13  ? 162 ASP C CA    1 
ATOM   9355  C C     . ASP C 1 162 ? 34.015  9.893   -8.291  1.00 42.95  ? 162 ASP C C     1 
ATOM   9356  O O     . ASP C 1 162 ? 34.195  9.711   -9.487  1.00 36.67  ? 162 ASP C O     1 
ATOM   9357  C CB    . ASP C 1 162 ? 33.062  12.068  -8.778  1.00 52.28  ? 162 ASP C CB    1 
ATOM   9358  C CG    . ASP C 1 162 ? 32.200  12.010  -10.027 1.00 58.09  ? 162 ASP C CG    1 
ATOM   9359  O OD1   . ASP C 1 162 ? 30.973  11.750  -9.882  1.00 61.68  ? 162 ASP C OD1   1 
ATOM   9360  O OD2   . ASP C 1 162 ? 32.738  12.326  -11.107 1.00 58.98  ? 162 ASP C OD2   1 
ATOM   9361  N N     . HIS C 1 163 ? 34.746  9.300   -7.343  1.00 37.61  ? 163 HIS C N     1 
ATOM   9362  C CA    . HIS C 1 163 ? 35.788  8.326   -7.642  1.00 38.73  ? 163 HIS C CA    1 
ATOM   9363  C C     . HIS C 1 163 ? 36.962  8.935   -8.409  1.00 42.05  ? 163 HIS C C     1 
ATOM   9364  O O     . HIS C 1 163 ? 37.696  8.226   -9.105  1.00 36.65  ? 163 HIS C O     1 
ATOM   9365  C CB    . HIS C 1 163 ? 35.249  7.104   -8.384  1.00 38.66  ? 163 HIS C CB    1 
ATOM   9366  C CG    . HIS C 1 163 ? 34.168  6.399   -7.665  1.00 35.64  ? 163 HIS C CG    1 
ATOM   9367  N ND1   . HIS C 1 163 ? 33.307  5.585   -8.346  1.00 35.23  ? 163 HIS C ND1   1 
ATOM   9368  C CD2   . HIS C 1 163 ? 33.737  6.420   -6.399  1.00 39.84  ? 163 HIS C CD2   1 
ATOM   9369  C CE1   . HIS C 1 163 ? 32.387  5.141   -7.499  1.00 35.13  ? 163 HIS C CE1   1 
ATOM   9370  N NE2   . HIS C 1 163 ? 32.646  5.599   -6.317  1.00 32.63  ? 163 HIS C NE2   1 
ATOM   9371  N N     . GLY C 1 164 ? 37.218  10.222  -8.178  1.00 40.62  ? 164 GLY C N     1 
ATOM   9372  C CA    . GLY C 1 164 ? 38.335  10.878  -8.812  1.00 42.34  ? 164 GLY C CA    1 
ATOM   9373  C C     . GLY C 1 164 ? 39.685  10.325  -8.369  1.00 47.51  ? 164 GLY C C     1 
ATOM   9374  O O     . GLY C 1 164 ? 39.805  9.725   -7.305  1.00 54.72  ? 164 GLY C O     1 
ATOM   9375  N N     . ILE C 1 165 ? 40.706  10.595  -9.188  1.00 47.79  ? 165 ILE C N     1 
ATOM   9376  C CA    . ILE C 1 165 ? 42.047  10.132  -8.916  1.00 50.34  ? 165 ILE C CA    1 
ATOM   9377  C C     . ILE C 1 165 ? 43.010  11.318  -8.896  1.00 49.98  ? 165 ILE C C     1 
ATOM   9378  O O     . ILE C 1 165 ? 42.690  12.444  -9.270  1.00 55.27  ? 165 ILE C O     1 
ATOM   9379  C CB    . ILE C 1 165 ? 42.465  9.043   -9.920  1.00 64.76  ? 165 ILE C CB    1 
ATOM   9380  C CG1   . ILE C 1 165 ? 42.694  9.629   -11.320 1.00 78.24  ? 165 ILE C CG1   1 
ATOM   9381  C CG2   . ILE C 1 165 ? 41.468  7.877   -9.916  1.00 57.51  ? 165 ILE C CG2   1 
ATOM   9382  C CD1   . ILE C 1 165 ? 43.426  8.685   -12.271 1.00 90.25  ? 165 ILE C CD1   1 
ATOM   9383  N N     . GLY C 1 166 ? 44.190  11.048  -8.350  1.00 44.31  ? 166 GLY C N     1 
ATOM   9384  C CA    . GLY C 1 166 ? 45.320  11.951  -8.377  1.00 36.63  ? 166 GLY C CA    1 
ATOM   9385  C C     . GLY C 1 166 ? 46.554  11.100  -8.629  1.00 38.94  ? 166 GLY C C     1 
ATOM   9386  O O     . GLY C 1 166 ? 46.388  10.019  -9.208  1.00 36.85  ? 166 GLY C O     1 
ATOM   9387  N N     . TYR C 1 167 ? 47.713  11.541  -8.093  1.00 35.41  ? 167 TYR C N     1 
ATOM   9388  C CA    . TYR C 1 167 ? 49.022  11.281  -8.671  1.00 34.60  ? 167 TYR C CA    1 
ATOM   9389  C C     . TYR C 1 167 ? 50.069  10.972  -7.594  1.00 33.63  ? 167 TYR C C     1 
ATOM   9390  O O     . TYR C 1 167 ? 51.227  10.742  -7.928  1.00 31.11  ? 167 TYR C O     1 
ATOM   9391  C CB    . TYR C 1 167 ? 49.396  12.486  -9.558  1.00 42.95  ? 167 TYR C CB    1 
ATOM   9392  C CG    . TYR C 1 167 ? 48.440  12.700  -10.700 1.00 46.67  ? 167 TYR C CG    1 
ATOM   9393  C CD1   . TYR C 1 167 ? 48.542  11.951  -11.870 1.00 51.25  ? 167 TYR C CD1   1 
ATOM   9394  C CD2   . TYR C 1 167 ? 47.326  13.514  -10.560 1.00 50.40  ? 167 TYR C CD2   1 
ATOM   9395  C CE1   . TYR C 1 167 ? 47.601  12.049  -12.885 1.00 48.38  ? 167 TYR C CE1   1 
ATOM   9396  C CE2   . TYR C 1 167 ? 46.371  13.621  -11.569 1.00 49.93  ? 167 TYR C CE2   1 
ATOM   9397  C CZ    . TYR C 1 167 ? 46.506  12.889  -12.741 1.00 53.40  ? 167 TYR C CZ    1 
ATOM   9398  O OH    . TYR C 1 167 ? 45.557  12.978  -13.753 1.00 47.25  ? 167 TYR C OH    1 
ATOM   9399  N N     . THR C 1 168 ? 49.687  10.930  -6.303  1.00 31.27  ? 168 THR C N     1 
ATOM   9400  C CA    . THR C 1 168 ? 50.565  10.407  -5.269  1.00 32.09  ? 168 THR C CA    1 
ATOM   9401  C C     . THR C 1 168 ? 50.180  8.957   -4.944  1.00 37.50  ? 168 THR C C     1 
ATOM   9402  O O     . THR C 1 168 ? 49.267  8.411   -5.540  1.00 36.54  ? 168 THR C O     1 
ATOM   9403  C CB    . THR C 1 168 ? 50.502  11.302  -4.039  1.00 33.79  ? 168 THR C CB    1 
ATOM   9404  O OG1   . THR C 1 168 ? 49.385  10.925  -3.237  1.00 31.25  ? 168 THR C OG1   1 
ATOM   9405  C CG2   . THR C 1 168 ? 50.383  12.763  -4.406  1.00 36.96  ? 168 THR C CG2   1 
ATOM   9406  N N     . PRO C 1 169 ? 50.831  8.246   -3.991  1.00 40.59  ? 169 PRO C N     1 
ATOM   9407  C CA    . PRO C 1 169 ? 50.346  6.916   -3.600  1.00 41.53  ? 169 PRO C CA    1 
ATOM   9408  C C     . PRO C 1 169 ? 48.937  6.912   -3.000  1.00 34.26  ? 169 PRO C C     1 
ATOM   9409  O O     . PRO C 1 169 ? 48.309  5.847   -2.927  1.00 28.14  ? 169 PRO C O     1 
ATOM   9410  C CB    . PRO C 1 169 ? 51.402  6.412   -2.615  1.00 37.14  ? 169 PRO C CB    1 
ATOM   9411  C CG    . PRO C 1 169 ? 52.634  7.229   -2.956  1.00 40.14  ? 169 PRO C CG    1 
ATOM   9412  C CD    . PRO C 1 169 ? 52.087  8.597   -3.311  1.00 41.01  ? 169 PRO C CD    1 
ATOM   9413  N N     . TYR C 1 170 ? 48.405  8.103   -2.678  1.00 29.67  ? 170 TYR C N     1 
ATOM   9414  C CA    . TYR C 1 170 ? 47.006  8.214   -2.233  1.00 31.10  ? 170 TYR C CA    1 
ATOM   9415  C C     . TYR C 1 170 ? 46.121  8.646   -3.400  1.00 33.81  ? 170 TYR C C     1 
ATOM   9416  O O     . TYR C 1 170 ? 45.054  9.195   -3.190  1.00 35.46  ? 170 TYR C O     1 
ATOM   9417  C CB    . TYR C 1 170 ? 46.843  9.169   -1.044  1.00 31.00  ? 170 TYR C CB    1 
ATOM   9418  C CG    . TYR C 1 170 ? 47.315  8.660   0.305   1.00 30.08  ? 170 TYR C CG    1 
ATOM   9419  C CD1   . TYR C 1 170 ? 48.515  7.985   0.459   1.00 33.93  ? 170 TYR C CD1   1 
ATOM   9420  C CD2   . TYR C 1 170 ? 46.506  8.775   1.412   1.00 33.83  ? 170 TYR C CD2   1 
ATOM   9421  C CE1   . TYR C 1 170 ? 48.930  7.505   1.686   1.00 38.19  ? 170 TYR C CE1   1 
ATOM   9422  C CE2   . TYR C 1 170 ? 46.902  8.316   2.661   1.00 38.83  ? 170 TYR C CE2   1 
ATOM   9423  C CZ    . TYR C 1 170 ? 48.122  7.693   2.798   1.00 38.16  ? 170 TYR C CZ    1 
ATOM   9424  O OH    . TYR C 1 170 ? 48.476  7.260   4.018   1.00 28.47  ? 170 TYR C OH    1 
ATOM   9425  N N     . GLY C 1 171 ? 46.588  8.392   -4.634  1.00 31.07  ? 171 GLY C N     1 
ATOM   9426  C CA    . GLY C 1 171 ? 45.790  8.515   -5.835  1.00 31.16  ? 171 GLY C CA    1 
ATOM   9427  C C     . GLY C 1 171 ? 44.299  8.219   -5.723  1.00 34.67  ? 171 GLY C C     1 
ATOM   9428  O O     . GLY C 1 171 ? 43.532  8.903   -6.361  1.00 43.36  ? 171 GLY C O     1 
ATOM   9429  N N     . ASP C 1 172 ? 43.884  7.119   -5.092  1.00 43.68  ? 172 ASP C N     1 
ATOM   9430  C CA    . ASP C 1 172 ? 42.510  6.639   -5.226  1.00 39.25  ? 172 ASP C CA    1 
ATOM   9431  C C     . ASP C 1 172 ? 41.724  7.327   -4.109  1.00 41.49  ? 172 ASP C C     1 
ATOM   9432  O O     . ASP C 1 172 ? 41.717  6.908   -2.942  1.00 45.64  ? 172 ASP C O     1 
ATOM   9433  C CB    . ASP C 1 172 ? 42.489  5.100   -5.267  1.00 36.15  ? 172 ASP C CB    1 
ATOM   9434  C CG    . ASP C 1 172 ? 41.128  4.413   -5.464  1.00 45.68  ? 172 ASP C CG    1 
ATOM   9435  O OD1   . ASP C 1 172 ? 40.092  5.128   -5.438  1.00 41.59  ? 172 ASP C OD1   1 
ATOM   9436  O OD2   . ASP C 1 172 ? 41.097  3.124   -5.643  1.00 41.62  ? 172 ASP C OD2   1 
ATOM   9437  N N     . HIS C 1 173 ? 41.102  8.442   -4.459  1.00 38.08  ? 173 HIS C N     1 
ATOM   9438  C CA    . HIS C 1 173 ? 40.641  9.390   -3.451  1.00 39.21  ? 173 HIS C CA    1 
ATOM   9439  C C     . HIS C 1 173 ? 39.569  8.763   -2.581  1.00 34.82  ? 173 HIS C C     1 
ATOM   9440  O O     . HIS C 1 173 ? 39.552  8.967   -1.385  1.00 41.24  ? 173 HIS C O     1 
ATOM   9441  C CB    . HIS C 1 173 ? 40.100  10.680  -4.078  1.00 34.31  ? 173 HIS C CB    1 
ATOM   9442  C CG    . HIS C 1 173 ? 41.144  11.494  -4.733  1.00 33.32  ? 173 HIS C CG    1 
ATOM   9443  N ND1   . HIS C 1 173 ? 40.883  12.731  -5.266  1.00 37.28  ? 173 HIS C ND1   1 
ATOM   9444  C CD2   . HIS C 1 173 ? 42.470  11.319  -4.847  1.00 38.90  ? 173 HIS C CD2   1 
ATOM   9445  C CE1   . HIS C 1 173 ? 42.019  13.257  -5.712  1.00 38.61  ? 173 HIS C CE1   1 
ATOM   9446  N NE2   . HIS C 1 173 ? 42.996  12.417  -5.459  1.00 35.42  ? 173 HIS C NE2   1 
ATOM   9447  N N     . PHE C 1 174 ? 38.656  8.021   -3.177  1.00 36.19  ? 174 PHE C N     1 
ATOM   9448  C CA    . PHE C 1 174 ? 37.580  7.455   -2.389  1.00 40.44  ? 174 PHE C CA    1 
ATOM   9449  C C     . PHE C 1 174 ? 38.057  6.250   -1.577  1.00 41.36  ? 174 PHE C C     1 
ATOM   9450  O O     . PHE C 1 174 ? 37.452  5.942   -0.556  1.00 39.67  ? 174 PHE C O     1 
ATOM   9451  C CB    . PHE C 1 174 ? 36.384  7.055   -3.251  1.00 37.49  ? 174 PHE C CB    1 
ATOM   9452  C CG    . PHE C 1 174 ? 35.188  6.716   -2.401  1.00 36.80  ? 174 PHE C CG    1 
ATOM   9453  C CD1   . PHE C 1 174 ? 34.553  7.705   -1.673  1.00 29.45  ? 174 PHE C CD1   1 
ATOM   9454  C CD2   . PHE C 1 174 ? 34.757  5.400   -2.274  1.00 31.94  ? 174 PHE C CD2   1 
ATOM   9455  C CE1   . PHE C 1 174 ? 33.477  7.392   -0.875  1.00 31.38  ? 174 PHE C CE1   1 
ATOM   9456  C CE2   . PHE C 1 174 ? 33.678  5.093   -1.477  1.00 28.99  ? 174 PHE C CE2   1 
ATOM   9457  C CZ    . PHE C 1 174 ? 33.052  6.090   -0.773  1.00 32.12  ? 174 PHE C CZ    1 
ATOM   9458  N N     . ALA C 1 175 ? 39.152  5.597   -2.000  1.00 42.90  ? 175 ALA C N     1 
ATOM   9459  C CA    . ALA C 1 175 ? 39.712  4.479   -1.240  1.00 38.87  ? 175 ALA C CA    1 
ATOM   9460  C C     . ALA C 1 175 ? 40.345  5.000   0.049   1.00 38.76  ? 175 ALA C C     1 
ATOM   9461  O O     . ALA C 1 175 ? 40.586  4.217   0.954   1.00 37.46  ? 175 ALA C O     1 
ATOM   9462  C CB    . ALA C 1 175 ? 40.717  3.682   -2.063  1.00 31.43  ? 175 ALA C CB    1 
ATOM   9463  N N     . MET C 1 176 ? 40.612  6.317   0.135   1.00 36.29  ? 176 MET C N     1 
ATOM   9464  C CA    . MET C 1 176 ? 41.263  6.891   1.303   1.00 30.39  ? 176 MET C CA    1 
ATOM   9465  C C     . MET C 1 176 ? 40.231  7.563   2.192   1.00 31.68  ? 176 MET C C     1 
ATOM   9466  O O     . MET C 1 176 ? 40.572  7.994   3.305   1.00 29.30  ? 176 MET C O     1 
ATOM   9467  C CB    . MET C 1 176 ? 42.325  7.906   0.900   1.00 34.47  ? 176 MET C CB    1 
ATOM   9468  C CG    . MET C 1 176 ? 43.515  7.309   0.122   1.00 32.51  ? 176 MET C CG    1 
ATOM   9469  S SD    . MET C 1 176 ? 44.457  6.035   1.021   1.00 38.09  ? 176 MET C SD    1 
ATOM   9470  C CE    . MET C 1 176 ? 43.709  4.517   0.432   1.00 34.93  ? 176 MET C CE    1 
ATOM   9471  N N     . GLN C 1 177 ? 38.963  7.551   1.730   1.00 33.24  ? 177 GLN C N     1 
ATOM   9472  C CA    . GLN C 1 177 ? 37.838  8.054   2.500   1.00 32.06  ? 177 GLN C CA    1 
ATOM   9473  C C     . GLN C 1 177 ? 37.685  7.208   3.749   1.00 36.55  ? 177 GLN C C     1 
ATOM   9474  O O     . GLN C 1 177 ? 37.944  6.015   3.737   1.00 37.24  ? 177 GLN C O     1 
ATOM   9475  C CB    . GLN C 1 177 ? 36.557  8.044   1.662   1.00 37.80  ? 177 GLN C CB    1 
ATOM   9476  C CG    . GLN C 1 177 ? 35.280  8.556   2.349   1.00 36.13  ? 177 GLN C CG    1 
ATOM   9477  C CD    . GLN C 1 177 ? 34.546  7.467   3.075   1.00 38.19  ? 177 GLN C CD    1 
ATOM   9478  O OE1   . GLN C 1 177 ? 34.694  6.287   2.778   1.00 56.94  ? 177 GLN C OE1   1 
ATOM   9479  N NE2   . GLN C 1 177 ? 33.774  7.841   4.076   1.00 41.35  ? 177 GLN C NE2   1 
ATOM   9480  N N     . CYS C 1 178 ? 37.238  7.830   4.838   1.00 42.14  ? 178 CYS C N     1 
ATOM   9481  C CA    . CYS C 1 178 ? 37.019  7.093   6.072   1.00 43.48  ? 178 CYS C CA    1 
ATOM   9482  C C     . CYS C 1 178 ? 36.044  7.854   6.966   1.00 40.75  ? 178 CYS C C     1 
ATOM   9483  O O     . CYS C 1 178 ? 36.415  8.843   7.580   1.00 36.85  ? 178 CYS C O     1 
ATOM   9484  C CB    . CYS C 1 178 ? 38.331  6.866   6.824   1.00 46.17  ? 178 CYS C CB    1 
ATOM   9485  S SG    . CYS C 1 178 ? 38.162  5.647   8.149   1.00 38.43  ? 178 CYS C SG    1 
ATOM   9486  N N     . GLY C 1 179 ? 34.789  7.410   7.009   1.00 38.68  ? 179 GLY C N     1 
ATOM   9487  C CA    . GLY C 1 179 ? 33.816  8.082   7.847   1.00 39.45  ? 179 GLY C CA    1 
ATOM   9488  C C     . GLY C 1 179 ? 33.141  9.216   7.083   1.00 39.40  ? 179 GLY C C     1 
ATOM   9489  O O     . GLY C 1 179 ? 33.819  9.982   6.403   1.00 30.64  ? 179 GLY C O     1 
ATOM   9490  N N     . MET C 1 180 ? 31.800  9.283   7.182   1.00 35.17  ? 180 MET C N     1 
ATOM   9491  C CA    . MET C 1 180 ? 31.093  10.441  6.697   1.00 34.51  ? 180 MET C CA    1 
ATOM   9492  C C     . MET C 1 180 ? 29.832  10.627  7.534   1.00 36.65  ? 180 MET C C     1 
ATOM   9493  O O     . MET C 1 180 ? 29.273  9.678   8.104   1.00 34.28  ? 180 MET C O     1 
ATOM   9494  C CB    . MET C 1 180 ? 30.735  10.309  5.206   1.00 33.45  ? 180 MET C CB    1 
ATOM   9495  C CG    . MET C 1 180 ? 30.097  8.992   4.870   1.00 36.61  ? 180 MET C CG    1 
ATOM   9496  S SD    . MET C 1 180 ? 29.269  8.842   3.250   1.00 41.38  ? 180 MET C SD    1 
ATOM   9497  C CE    . MET C 1 180 ? 30.712  8.606   2.215   1.00 34.58  ? 180 MET C CE    1 
ATOM   9498  N N     . GLU C 1 181 ? 29.379  11.884  7.556   1.00 33.61  ? 181 GLU C N     1 
ATOM   9499  C CA    . GLU C 1 181 ? 28.009  12.186  7.903   1.00 35.20  ? 181 GLU C CA    1 
ATOM   9500  C C     . GLU C 1 181 ? 27.210  12.340  6.612   1.00 37.51  ? 181 GLU C C     1 
ATOM   9501  O O     . GLU C 1 181 ? 27.679  12.977  5.667   1.00 39.03  ? 181 GLU C O     1 
ATOM   9502  C CB    . GLU C 1 181 ? 27.979  13.465  8.733   1.00 34.08  ? 181 GLU C CB    1 
ATOM   9503  C CG    . GLU C 1 181 ? 26.639  13.812  9.349   1.00 33.71  ? 181 GLU C CG    1 
ATOM   9504  C CD    . GLU C 1 181 ? 26.789  15.016  10.275  1.00 39.81  ? 181 GLU C CD    1 
ATOM   9505  O OE1   . GLU C 1 181 ? 26.693  14.823  11.518  1.00 38.09  ? 181 GLU C OE1   1 
ATOM   9506  O OE2   . GLU C 1 181 ? 27.051  16.163  9.756   1.00 37.49  ? 181 GLU C OE2   1 
ATOM   9507  N N     . VAL C 1 182 ? 25.973  11.834  6.648   1.00 36.30  ? 182 VAL C N     1 
ATOM   9508  C CA    . VAL C 1 182 ? 25.095  11.811  5.499   1.00 37.85  ? 182 VAL C CA    1 
ATOM   9509  C C     . VAL C 1 182 ? 23.708  12.276  5.919   1.00 36.47  ? 182 VAL C C     1 
ATOM   9510  O O     . VAL C 1 182 ? 23.147  11.788  6.883   1.00 42.19  ? 182 VAL C O     1 
ATOM   9511  C CB    . VAL C 1 182 ? 25.035  10.386  4.915   1.00 38.71  ? 182 VAL C CB    1 
ATOM   9512  C CG1   . VAL C 1 182 ? 23.972  10.242  3.844   1.00 41.28  ? 182 VAL C CG1   1 
ATOM   9513  C CG2   . VAL C 1 182 ? 26.377  9.971   4.376   1.00 41.69  ? 182 VAL C CG2   1 
ATOM   9514  N N     . VAL C 1 183 ? 23.137  13.197  5.164   1.00 42.05  ? 183 VAL C N     1 
ATOM   9515  C CA    . VAL C 1 183 ? 21.732  13.524  5.312   1.00 42.17  ? 183 VAL C CA    1 
ATOM   9516  C C     . VAL C 1 183 ? 20.991  12.682  4.304   1.00 37.05  ? 183 VAL C C     1 
ATOM   9517  O O     . VAL C 1 183 ? 21.205  12.866  3.110   1.00 43.58  ? 183 VAL C O     1 
ATOM   9518  C CB    . VAL C 1 183 ? 21.438  15.021  5.111   1.00 44.03  ? 183 VAL C CB    1 
ATOM   9519  C CG1   . VAL C 1 183 ? 19.944  15.283  5.121   1.00 48.16  ? 183 VAL C CG1   1 
ATOM   9520  C CG2   . VAL C 1 183 ? 22.129  15.863  6.177   1.00 42.64  ? 183 VAL C CG2   1 
ATOM   9521  N N     . LEU C 1 184 ? 20.200  11.742  4.814   1.00 36.42  ? 184 LEU C N     1 
ATOM   9522  C CA    . LEU C 1 184 ? 19.412  10.851  3.989   1.00 46.58  ? 184 LEU C CA    1 
ATOM   9523  C C     . LEU C 1 184 ? 18.302  11.637  3.302   1.00 41.36  ? 184 LEU C C     1 
ATOM   9524  O O     . LEU C 1 184 ? 17.865  12.650  3.810   1.00 45.44  ? 184 LEU C O     1 
ATOM   9525  C CB    . LEU C 1 184 ? 18.808  9.732   4.842   1.00 51.65  ? 184 LEU C CB    1 
ATOM   9526  C CG    . LEU C 1 184 ? 19.800  8.765   5.497   1.00 51.85  ? 184 LEU C CG    1 
ATOM   9527  C CD1   . LEU C 1 184 ? 19.067  7.630   6.216   1.00 41.81  ? 184 LEU C CD1   1 
ATOM   9528  C CD2   . LEU C 1 184 ? 20.797  8.207   4.474   1.00 50.91  ? 184 LEU C CD2   1 
ATOM   9529  N N     . PRO C 1 185 ? 17.817  11.167  2.136   1.00 39.82  ? 185 PRO C N     1 
ATOM   9530  C CA    . PRO C 1 185 ? 16.714  11.822  1.437   1.00 47.08  ? 185 PRO C CA    1 
ATOM   9531  C C     . PRO C 1 185 ? 15.415  12.063  2.225   1.00 44.99  ? 185 PRO C C     1 
ATOM   9532  O O     . PRO C 1 185 ? 14.594  12.848  1.770   1.00 51.11  ? 185 PRO C O     1 
ATOM   9533  C CB    . PRO C 1 185 ? 16.374  10.855  0.285   1.00 46.10  ? 185 PRO C CB    1 
ATOM   9534  C CG    . PRO C 1 185 ? 17.577  9.962   0.133   1.00 42.54  ? 185 PRO C CG    1 
ATOM   9535  C CD    . PRO C 1 185 ? 18.237  9.911   1.488   1.00 38.98  ? 185 PRO C CD    1 
ATOM   9536  N N     . ASN C 1 186 ? 15.214  11.401  3.381   1.00 46.80  ? 186 ASN C N     1 
ATOM   9537  C CA    . ASN C 1 186 ? 14.041  11.637  4.224   1.00 45.40  ? 186 ASN C CA    1 
ATOM   9538  C C     . ASN C 1 186 ? 14.322  12.774  5.195   1.00 40.51  ? 186 ASN C C     1 
ATOM   9539  O O     . ASN C 1 186 ? 13.445  13.151  5.954   1.00 50.65  ? 186 ASN C O     1 
ATOM   9540  C CB    . ASN C 1 186 ? 13.577  10.425  5.040   1.00 42.33  ? 186 ASN C CB    1 
ATOM   9541  C CG    . ASN C 1 186 ? 14.682  9.839   5.901   1.00 47.22  ? 186 ASN C CG    1 
ATOM   9542  O OD1   . ASN C 1 186 ? 15.732  10.449  6.071   1.00 38.07  ? 186 ASN C OD1   1 
ATOM   9543  N ND2   . ASN C 1 186 ? 14.483  8.633   6.411   1.00 46.83  ? 186 ASN C ND2   1 
ATOM   9544  N N     . GLY C 1 187 ? 15.544  13.298  5.179   1.00 38.50  ? 187 GLY C N     1 
ATOM   9545  C CA    . GLY C 1 187 ? 15.920  14.352  6.104   1.00 37.79  ? 187 GLY C CA    1 
ATOM   9546  C C     . GLY C 1 187 ? 16.621  13.848  7.372   1.00 37.16  ? 187 GLY C C     1 
ATOM   9547  O O     . GLY C 1 187 ? 17.004  14.671  8.187   1.00 38.33  ? 187 GLY C O     1 
ATOM   9548  N N     . GLU C 1 188 ? 16.809  12.528  7.551   1.00 33.95  ? 188 GLU C N     1 
ATOM   9549  C CA    . GLU C 1 188 ? 17.438  11.984  8.741   1.00 33.26  ? 188 GLU C CA    1 
ATOM   9550  C C     . GLU C 1 188 ? 18.953  12.094  8.601   1.00 39.23  ? 188 GLU C C     1 
ATOM   9551  O O     . GLU C 1 188 ? 19.456  12.009  7.489   1.00 37.60  ? 188 GLU C O     1 
ATOM   9552  C CB    . GLU C 1 188 ? 17.052  10.514  8.933   1.00 37.50  ? 188 GLU C CB    1 
ATOM   9553  C CG    . GLU C 1 188 ? 15.594  10.296  9.360   1.00 38.96  ? 188 GLU C CG    1 
ATOM   9554  C CD    . GLU C 1 188 ? 15.207  10.875  10.714  1.00 47.69  ? 188 GLU C CD    1 
ATOM   9555  O OE1   . GLU C 1 188 ? 15.439  10.208  11.747  1.00 56.64  ? 188 GLU C OE1   1 
ATOM   9556  O OE2   . GLU C 1 188 ? 14.737  12.009  10.740  1.00 48.66  ? 188 GLU C OE2   1 
ATOM   9557  N N     . VAL C 1 189 ? 19.692  12.260  9.715   1.00 39.09  ? 189 VAL C N     1 
ATOM   9558  C CA    . VAL C 1 189 ? 21.151  12.346  9.646   1.00 35.29  ? 189 VAL C CA    1 
ATOM   9559  C C     . VAL C 1 189 ? 21.738  11.056  10.212  1.00 38.75  ? 189 VAL C C     1 
ATOM   9560  O O     . VAL C 1 189 ? 21.235  10.553  11.201  1.00 38.16  ? 189 VAL C O     1 
ATOM   9561  C CB    . VAL C 1 189 ? 21.698  13.581  10.377  1.00 30.48  ? 189 VAL C CB    1 
ATOM   9562  C CG1   . VAL C 1 189 ? 21.495  13.483  11.862  1.00 33.34  ? 189 VAL C CG1   1 
ATOM   9563  C CG2   . VAL C 1 189 ? 23.166  13.830  10.084  1.00 33.85  ? 189 VAL C CG2   1 
ATOM   9564  N N     . VAL C 1 190 ? 22.746  10.492  9.531   1.00 38.34  ? 190 VAL C N     1 
ATOM   9565  C CA    . VAL C 1 190 ? 23.487  9.326   10.001  1.00 36.76  ? 190 VAL C CA    1 
ATOM   9566  C C     . VAL C 1 190 ? 24.989  9.620   9.926   1.00 38.75  ? 190 VAL C C     1 
ATOM   9567  O O     . VAL C 1 190 ? 25.449  10.586  9.291   1.00 40.06  ? 190 VAL C O     1 
ATOM   9568  C CB    . VAL C 1 190 ? 23.155  8.048   9.211   1.00 34.85  ? 190 VAL C CB    1 
ATOM   9569  C CG1   . VAL C 1 190 ? 21.690  7.705   9.230   1.00 39.72  ? 190 VAL C CG1   1 
ATOM   9570  C CG2   . VAL C 1 190 ? 23.575  8.153   7.763   1.00 42.46  ? 190 VAL C CG2   1 
ATOM   9571  N N     . ARG C 1 191 ? 25.750  8.748   10.586  1.00 40.53  ? 191 ARG C N     1 
ATOM   9572  C CA    . ARG C 1 191 ? 27.202  8.740   10.484  1.00 38.28  ? 191 ARG C CA    1 
ATOM   9573  C C     . ARG C 1 191 ? 27.647  7.299   10.290  1.00 33.06  ? 191 ARG C C     1 
ATOM   9574  O O     . ARG C 1 191 ? 27.221  6.425   11.022  1.00 30.20  ? 191 ARG C O     1 
ATOM   9575  C CB    . ARG C 1 191 ? 27.815  9.370   11.726  1.00 33.85  ? 191 ARG C CB    1 
ATOM   9576  C CG    . ARG C 1 191 ? 27.468  10.840  11.826  1.00 39.23  ? 191 ARG C CG    1 
ATOM   9577  C CD    . ARG C 1 191 ? 28.059  11.464  13.065  1.00 41.49  ? 191 ARG C CD    1 
ATOM   9578  N NE    . ARG C 1 191 ? 27.781  12.887  13.177  1.00 40.35  ? 191 ARG C NE    1 
ATOM   9579  C CZ    . ARG C 1 191 ? 28.373  13.670  14.055  1.00 40.83  ? 191 ARG C CZ    1 
ATOM   9580  N NH1   . ARG C 1 191 ? 29.086  13.137  15.040  1.00 38.21  ? 191 ARG C NH1   1 
ATOM   9581  N NH2   . ARG C 1 191 ? 28.277  14.978  13.918  1.00 39.74  ? 191 ARG C NH2   1 
ATOM   9582  N N     . THR C 1 192 ? 28.468  7.060   9.273   1.00 30.04  ? 192 THR C N     1 
ATOM   9583  C CA    . THR C 1 192 ? 28.879  5.706   8.955   1.00 30.05  ? 192 THR C CA    1 
ATOM   9584  C C     . THR C 1 192 ? 29.986  5.239   9.884   1.00 31.11  ? 192 THR C C     1 
ATOM   9585  O O     . THR C 1 192 ? 30.676  6.062   10.493  1.00 28.88  ? 192 THR C O     1 
ATOM   9586  C CB    . THR C 1 192 ? 29.433  5.607   7.539   1.00 33.01  ? 192 THR C CB    1 
ATOM   9587  O OG1   . THR C 1 192 ? 30.696  6.296   7.526   1.00 29.02  ? 192 THR C OG1   1 
ATOM   9588  C CG2   . THR C 1 192 ? 28.417  6.129   6.548   1.00 35.16  ? 192 THR C CG2   1 
ATOM   9589  N N     . GLY C 1 193 ? 30.187  3.911   9.921   1.00 28.98  ? 193 GLY C N     1 
ATOM   9590  C CA    . GLY C 1 193 ? 31.438  3.423   10.473  1.00 32.49  ? 193 GLY C CA    1 
ATOM   9591  C C     . GLY C 1 193 ? 31.467  3.766   11.963  1.00 29.08  ? 193 GLY C C     1 
ATOM   9592  O O     . GLY C 1 193 ? 30.414  3.810   12.578  1.00 28.03  ? 193 GLY C O     1 
ATOM   9593  N N     . MET C 1 194 ? 32.639  4.105   12.490  1.00 27.78  ? 194 MET C N     1 
ATOM   9594  C CA    . MET C 1 194 ? 32.812  4.288   13.913  1.00 28.27  ? 194 MET C CA    1 
ATOM   9595  C C     . MET C 1 194 ? 32.055  5.502   14.409  1.00 31.32  ? 194 MET C C     1 
ATOM   9596  O O     . MET C 1 194 ? 31.834  5.601   15.610  1.00 32.97  ? 194 MET C O     1 
ATOM   9597  C CB    . MET C 1 194 ? 34.286  4.476   14.268  1.00 28.15  ? 194 MET C CB    1 
ATOM   9598  C CG    . MET C 1 194 ? 35.134  3.265   14.025  1.00 30.64  ? 194 MET C CG    1 
ATOM   9599  S SD    . MET C 1 194 ? 34.481  1.655   14.514  1.00 31.92  ? 194 MET C SD    1 
ATOM   9600  C CE    . MET C 1 194 ? 34.169  1.866   16.260  1.00 31.71  ? 194 MET C CE    1 
ATOM   9601  N N     . GLY C 1 195 ? 31.685  6.420   13.503  1.00 34.65  ? 195 GLY C N     1 
ATOM   9602  C CA    . GLY C 1 195 ? 31.017  7.654   13.903  1.00 34.58  ? 195 GLY C CA    1 
ATOM   9603  C C     . GLY C 1 195 ? 29.631  7.429   14.508  1.00 35.07  ? 195 GLY C C     1 
ATOM   9604  O O     . GLY C 1 195 ? 29.085  8.295   15.210  1.00 33.34  ? 195 GLY C O     1 
ATOM   9605  N N     . ALA C 1 196 ? 29.075  6.246   14.225  1.00 32.97  ? 196 ALA C N     1 
ATOM   9606  C CA    . ALA C 1 196 ? 27.808  5.827   14.782  1.00 28.71  ? 196 ALA C CA    1 
ATOM   9607  C C     . ALA C 1 196 ? 27.977  5.502   16.256  1.00 31.20  ? 196 ALA C C     1 
ATOM   9608  O O     . ALA C 1 196 ? 26.988  5.255   16.950  1.00 31.82  ? 196 ALA C O     1 
ATOM   9609  C CB    . ALA C 1 196 ? 27.286  4.612   14.061  1.00 28.13  ? 196 ALA C CB    1 
ATOM   9610  N N     . MET C 1 197 ? 29.226  5.428   16.716  1.00 33.04  ? 197 MET C N     1 
ATOM   9611  C CA    . MET C 1 197 ? 29.426  5.051   18.104  1.00 36.54  ? 197 MET C CA    1 
ATOM   9612  C C     . MET C 1 197 ? 29.745  6.317   18.862  1.00 35.32  ? 197 MET C C     1 
ATOM   9613  O O     . MET C 1 197 ? 30.833  6.893   18.707  1.00 34.35  ? 197 MET C O     1 
ATOM   9614  C CB    . MET C 1 197 ? 30.518  4.006   18.352  1.00 36.55  ? 197 MET C CB    1 
ATOM   9615  C CG    . MET C 1 197 ? 31.024  4.072   19.792  1.00 47.99  ? 197 MET C CG    1 
ATOM   9616  S SD    . MET C 1 197 ? 32.143  2.762   20.292  1.00 42.31  ? 197 MET C SD    1 
ATOM   9617  C CE    . MET C 1 197 ? 30.859  1.628   20.811  1.00 49.17  ? 197 MET C CE    1 
ATOM   9618  N N     . PRO C 1 198 ? 28.818  6.758   19.732  1.00 34.24  ? 198 PRO C N     1 
ATOM   9619  C CA    . PRO C 1 198 ? 28.982  8.051   20.391  1.00 36.67  ? 198 PRO C CA    1 
ATOM   9620  C C     . PRO C 1 198 ? 30.214  7.821   21.252  1.00 37.60  ? 198 PRO C C     1 
ATOM   9621  O O     . PRO C 1 198 ? 30.421  6.708   21.732  1.00 40.47  ? 198 PRO C O     1 
ATOM   9622  C CB    . PRO C 1 198 ? 27.635  8.233   21.086  1.00 36.43  ? 198 PRO C CB    1 
ATOM   9623  C CG    . PRO C 1 198 ? 27.249  6.823   21.414  1.00 39.01  ? 198 PRO C CG    1 
ATOM   9624  C CD    . PRO C 1 198 ? 27.625  6.038   20.179  1.00 35.22  ? 198 PRO C CD    1 
ATOM   9625  N N     . GLY C 1 199 ? 31.081  8.826   21.306  1.00 39.53  ? 199 GLY C N     1 
ATOM   9626  C CA    . GLY C 1 199 ? 32.267  8.781   22.141  1.00 40.01  ? 199 GLY C CA    1 
ATOM   9627  C C     . GLY C 1 199 ? 33.496  8.307   21.385  1.00 43.18  ? 199 GLY C C     1 
ATOM   9628  O O     . GLY C 1 199 ? 34.603  8.393   21.911  1.00 39.79  ? 199 GLY C O     1 
ATOM   9629  N N     . ASN C 1 200 ? 33.322  7.856   20.136  1.00 40.53  ? 200 ASN C N     1 
ATOM   9630  C CA    . ASN C 1 200 ? 34.466  7.313   19.428  1.00 35.49  ? 200 ASN C CA    1 
ATOM   9631  C C     . ASN C 1 200 ? 35.522  8.383   19.223  1.00 35.59  ? 200 ASN C C     1 
ATOM   9632  O O     . ASN C 1 200 ? 35.250  9.577   19.151  1.00 41.63  ? 200 ASN C O     1 
ATOM   9633  C CB    . ASN C 1 200 ? 34.137  6.798   18.022  1.00 38.22  ? 200 ASN C CB    1 
ATOM   9634  C CG    . ASN C 1 200 ? 33.889  7.915   17.039  1.00 30.54  ? 200 ASN C CG    1 
ATOM   9635  O OD1   . ASN C 1 200 ? 34.824  8.503   16.529  1.00 33.62  ? 200 ASN C OD1   1 
ATOM   9636  N ND2   . ASN C 1 200 ? 32.637  8.217   16.763  1.00 32.54  ? 200 ASN C ND2   1 
ATOM   9637  N N     . ASN C 1 201 ? 36.746  7.919   19.054  1.00 36.57  ? 201 ASN C N     1 
ATOM   9638  C CA    . ASN C 1 201 ? 37.812  8.771   18.589  1.00 33.34  ? 201 ASN C CA    1 
ATOM   9639  C C     . ASN C 1 201 ? 38.451  8.053   17.419  1.00 33.33  ? 201 ASN C C     1 
ATOM   9640  O O     . ASN C 1 201 ? 39.682  8.065   17.299  1.00 28.49  ? 201 ASN C O     1 
ATOM   9641  C CB    . ASN C 1 201 ? 38.825  9.047   19.685  1.00 34.17  ? 201 ASN C CB    1 
ATOM   9642  C CG    . ASN C 1 201 ? 38.316  10.103  20.632  1.00 37.01  ? 201 ASN C CG    1 
ATOM   9643  O OD1   . ASN C 1 201 ? 37.957  9.774   21.755  1.00 47.18  ? 201 ASN C OD1   1 
ATOM   9644  N ND2   . ASN C 1 201 ? 38.255  11.353  20.199  1.00 34.67  ? 201 ASN C ND2   1 
ATOM   9645  N N     . THR C 1 202 ? 37.588  7.368   16.651  1.00 28.98  ? 202 THR C N     1 
ATOM   9646  C CA    . THR C 1 202 ? 38.057  6.405   15.666  1.00 38.67  ? 202 THR C CA    1 
ATOM   9647  C C     . THR C 1 202 ? 37.331  6.527   14.318  1.00 37.23  ? 202 THR C C     1 
ATOM   9648  O O     . THR C 1 202 ? 37.539  5.697   13.441  1.00 37.36  ? 202 THR C O     1 
ATOM   9649  C CB    . THR C 1 202 ? 37.992  4.970   16.231  1.00 32.28  ? 202 THR C CB    1 
ATOM   9650  O OG1   . THR C 1 202 ? 36.668  4.683   16.683  1.00 29.67  ? 202 THR C OG1   1 
ATOM   9651  C CG2   . THR C 1 202 ? 39.028  4.765   17.312  1.00 28.68  ? 202 THR C CG2   1 
ATOM   9652  N N     . TRP C 1 203 ? 36.519  7.571   14.142  1.00 37.20  ? 203 TRP C N     1 
ATOM   9653  C CA    . TRP C 1 203 ? 35.784  7.812   12.914  1.00 37.82  ? 203 TRP C CA    1 
ATOM   9654  C C     . TRP C 1 203 ? 36.701  7.741   11.699  1.00 33.93  ? 203 TRP C C     1 
ATOM   9655  O O     . TRP C 1 203 ? 36.313  7.216   10.666  1.00 39.16  ? 203 TRP C O     1 
ATOM   9656  C CB    . TRP C 1 203 ? 35.079  9.177   12.938  1.00 37.91  ? 203 TRP C CB    1 
ATOM   9657  C CG    . TRP C 1 203 ? 33.836  9.233   12.099  1.00 30.27  ? 203 TRP C CG    1 
ATOM   9658  C CD1   . TRP C 1 203 ? 33.236  8.208   11.437  1.00 32.50  ? 203 TRP C CD1   1 
ATOM   9659  C CD2   . TRP C 1 203 ? 33.037  10.390  11.836  1.00 29.86  ? 203 TRP C CD2   1 
ATOM   9660  N NE1   . TRP C 1 203 ? 32.088  8.641   10.815  1.00 34.81  ? 203 TRP C NE1   1 
ATOM   9661  C CE2   . TRP C 1 203 ? 31.938  9.975   11.056  1.00 33.63  ? 203 TRP C CE2   1 
ATOM   9662  C CE3   . TRP C 1 203 ? 33.107  11.726  12.234  1.00 32.76  ? 203 TRP C CE3   1 
ATOM   9663  C CZ2   . TRP C 1 203 ? 30.938  10.852  10.660  1.00 32.04  ? 203 TRP C CZ2   1 
ATOM   9664  C CZ3   . TRP C 1 203 ? 32.115  12.594  11.850  1.00 29.49  ? 203 TRP C CZ3   1 
ATOM   9665  C CH2   . TRP C 1 203 ? 31.060  12.163  11.060  1.00 32.19  ? 203 TRP C CH2   1 
ATOM   9666  N N     . GLN C 1 204 ? 37.900  8.292   11.853  1.00 35.32  ? 204 GLN C N     1 
ATOM   9667  C CA    . GLN C 1 204 ? 38.833  8.485   10.763  1.00 33.95  ? 204 GLN C CA    1 
ATOM   9668  C C     . GLN C 1 204 ? 39.947  7.454   10.800  1.00 33.28  ? 204 GLN C C     1 
ATOM   9669  O O     . GLN C 1 204 ? 40.909  7.574   10.040  1.00 40.30  ? 204 GLN C O     1 
ATOM   9670  C CB    . GLN C 1 204 ? 39.403  9.907   10.819  1.00 37.43  ? 204 GLN C CB    1 
ATOM   9671  C CG    . GLN C 1 204 ? 38.544  10.917  10.095  1.00 36.20  ? 204 GLN C CG    1 
ATOM   9672  C CD    . GLN C 1 204 ? 37.179  11.097  10.705  1.00 34.04  ? 204 GLN C CD    1 
ATOM   9673  O OE1   . GLN C 1 204 ? 36.980  11.813  11.681  1.00 43.33  ? 204 GLN C OE1   1 
ATOM   9674  N NE2   . GLN C 1 204 ? 36.184  10.578  10.032  1.00 33.48  ? 204 GLN C NE2   1 
ATOM   9675  N N     . LEU C 1 205 ? 39.776  6.372   11.568  1.00 36.85  ? 205 LEU C N     1 
ATOM   9676  C CA    . LEU C 1 205 ? 40.880  5.447   11.750  1.00 37.62  ? 205 LEU C CA    1 
ATOM   9677  C C     . LEU C 1 205 ? 40.534  4.046   11.262  1.00 38.23  ? 205 LEU C C     1 
ATOM   9678  O O     . LEU C 1 205 ? 41.434  3.229   11.035  1.00 49.35  ? 205 LEU C O     1 
ATOM   9679  C CB    . LEU C 1 205 ? 41.273  5.428   13.232  1.00 38.40  ? 205 LEU C CB    1 
ATOM   9680  C CG    . LEU C 1 205 ? 41.726  6.755   13.829  1.00 33.23  ? 205 LEU C CG    1 
ATOM   9681  C CD1   . LEU C 1 205 ? 42.221  6.558   15.255  1.00 37.22  ? 205 LEU C CD1   1 
ATOM   9682  C CD2   . LEU C 1 205 ? 42.806  7.390   13.015  1.00 34.39  ? 205 LEU C CD2   1 
ATOM   9683  N N     . PHE C 1 206 ? 39.242  3.754   11.120  1.00 32.58  ? 206 PHE C N     1 
ATOM   9684  C CA    . PHE C 1 206 ? 38.814  2.417   10.745  1.00 30.43  ? 206 PHE C CA    1 
ATOM   9685  C C     . PHE C 1 206 ? 37.514  2.540   9.956   1.00 31.38  ? 206 PHE C C     1 
ATOM   9686  O O     . PHE C 1 206 ? 36.547  3.163   10.394  1.00 38.19  ? 206 PHE C O     1 
ATOM   9687  C CB    . PHE C 1 206 ? 38.669  1.559   12.000  1.00 35.14  ? 206 PHE C CB    1 
ATOM   9688  C CG    . PHE C 1 206 ? 38.212  0.141   11.750  1.00 36.58  ? 206 PHE C CG    1 
ATOM   9689  C CD1   . PHE C 1 206 ? 39.094  -0.813  11.292  1.00 36.27  ? 206 PHE C CD1   1 
ATOM   9690  C CD2   . PHE C 1 206 ? 36.907  -0.245  12.012  1.00 37.83  ? 206 PHE C CD2   1 
ATOM   9691  C CE1   . PHE C 1 206 ? 38.690  -2.131  11.112  1.00 37.17  ? 206 PHE C CE1   1 
ATOM   9692  C CE2   . PHE C 1 206 ? 36.499  -1.557  11.815  1.00 38.46  ? 206 PHE C CE2   1 
ATOM   9693  C CZ    . PHE C 1 206 ? 37.380  -2.497  11.342  1.00 34.13  ? 206 PHE C CZ    1 
ATOM   9694  N N     . LYS C 1 207 ? 37.489  1.961   8.768   1.00 30.38  ? 207 LYS C N     1 
ATOM   9695  C CA    . LYS C 1 207 ? 36.477  2.331   7.802   1.00 33.33  ? 207 LYS C CA    1 
ATOM   9696  C C     . LYS C 1 207 ? 35.136  1.723   8.172   1.00 30.02  ? 207 LYS C C     1 
ATOM   9697  O O     . LYS C 1 207 ? 34.138  2.399   8.168   1.00 40.01  ? 207 LYS C O     1 
ATOM   9698  C CB    . LYS C 1 207 ? 36.834  1.831   6.402   1.00 36.06  ? 207 LYS C CB    1 
ATOM   9699  C CG    . LYS C 1 207 ? 37.882  2.617   5.646   1.00 41.69  ? 207 LYS C CG    1 
ATOM   9700  C CD    . LYS C 1 207 ? 38.091  1.962   4.270   1.00 46.46  ? 207 LYS C CD    1 
ATOM   9701  C CE    . LYS C 1 207 ? 39.062  2.686   3.372   1.00 38.82  ? 207 LYS C CE    1 
ATOM   9702  N NZ    . LYS C 1 207 ? 38.363  3.722   2.585   1.00 41.23  ? 207 LYS C NZ    1 
ATOM   9703  N N     . TYR C 1 208 ? 35.132  0.437   8.490   1.00 32.12  ? 208 TYR C N     1 
ATOM   9704  C CA    . TYR C 1 208 ? 33.943  -0.375  8.412   1.00 33.33  ? 208 TYR C CA    1 
ATOM   9705  C C     . TYR C 1 208 ? 32.967  -0.089  9.550   1.00 35.49  ? 208 TYR C C     1 
ATOM   9706  O O     . TYR C 1 208 ? 31.758  -0.102  9.357   1.00 35.71  ? 208 TYR C O     1 
ATOM   9707  C CB    . TYR C 1 208 ? 34.343  -1.854  8.487   1.00 37.19  ? 208 TYR C CB    1 
ATOM   9708  C CG    . TYR C 1 208 ? 35.312  -2.367  7.448   1.00 41.33  ? 208 TYR C CG    1 
ATOM   9709  C CD1   . TYR C 1 208 ? 35.126  -2.159  6.087   1.00 39.60  ? 208 TYR C CD1   1 
ATOM   9710  C CD2   . TYR C 1 208 ? 36.404  -3.133  7.834   1.00 44.67  ? 208 TYR C CD2   1 
ATOM   9711  C CE1   . TYR C 1 208 ? 36.012  -2.670  5.150   1.00 41.60  ? 208 TYR C CE1   1 
ATOM   9712  C CE2   . TYR C 1 208 ? 37.273  -3.684  6.910   1.00 43.23  ? 208 TYR C CE2   1 
ATOM   9713  C CZ    . TYR C 1 208 ? 37.081  -3.452  5.560   1.00 46.40  ? 208 TYR C CZ    1 
ATOM   9714  O OH    . TYR C 1 208 ? 38.007  -3.988  4.691   1.00 47.02  ? 208 TYR C OH    1 
ATOM   9715  N N     . GLY C 1 209 ? 33.502  0.077   10.761  1.00 35.95  ? 209 GLY C N     1 
ATOM   9716  C CA    . GLY C 1 209 ? 32.691  -0.033  11.958  1.00 34.56  ? 209 GLY C CA    1 
ATOM   9717  C C     . GLY C 1 209 ? 32.214  -1.479  12.108  1.00 33.71  ? 209 GLY C C     1 
ATOM   9718  O O     . GLY C 1 209 ? 32.996  -2.421  12.041  1.00 35.22  ? 209 GLY C O     1 
ATOM   9719  N N     . TYR C 1 210 ? 30.909  -1.636  12.284  1.00 32.41  ? 210 TYR C N     1 
ATOM   9720  C CA    . TYR C 1 210 ? 30.297  -2.930  12.359  1.00 31.64  ? 210 TYR C CA    1 
ATOM   9721  C C     . TYR C 1 210 ? 29.109  -2.972  11.411  1.00 31.61  ? 210 TYR C C     1 
ATOM   9722  O O     . TYR C 1 210 ? 28.422  -1.972  11.207  1.00 27.49  ? 210 TYR C O     1 
ATOM   9723  C CB    . TYR C 1 210 ? 29.836  -3.160  13.796  1.00 35.21  ? 210 TYR C CB    1 
ATOM   9724  C CG    . TYR C 1 210 ? 29.111  -4.452  14.030  1.00 32.64  ? 210 TYR C CG    1 
ATOM   9725  C CD1   . TYR C 1 210 ? 29.686  -5.673  13.707  1.00 38.07  ? 210 TYR C CD1   1 
ATOM   9726  C CD2   . TYR C 1 210 ? 27.830  -4.441  14.550  1.00 41.45  ? 210 TYR C CD2   1 
ATOM   9727  C CE1   . TYR C 1 210 ? 28.999  -6.865  13.914  1.00 39.59  ? 210 TYR C CE1   1 
ATOM   9728  C CE2   . TYR C 1 210 ? 27.135  -5.619  14.774  1.00 42.59  ? 210 TYR C CE2   1 
ATOM   9729  C CZ    . TYR C 1 210 ? 27.725  -6.820  14.450  1.00 37.85  ? 210 TYR C CZ    1 
ATOM   9730  O OH    . TYR C 1 210 ? 27.005  -7.903  14.746  1.00 54.04  ? 210 TYR C OH    1 
ATOM   9731  N N     . GLY C 1 211 ? 28.841  -4.150  10.853  1.00 27.83  ? 211 GLY C N     1 
ATOM   9732  C CA    . GLY C 1 211 ? 27.658  -4.270  10.026  1.00 28.55  ? 211 GLY C CA    1 
ATOM   9733  C C     . GLY C 1 211 ? 27.979  -3.995  8.569   1.00 26.92  ? 211 GLY C C     1 
ATOM   9734  O O     . GLY C 1 211 ? 29.149  -4.042  8.180   1.00 32.88  ? 211 GLY C O     1 
ATOM   9735  N N     . PRO C 1 212 ? 26.954  -3.792  7.726   1.00 29.23  ? 212 PRO C N     1 
ATOM   9736  C CA    . PRO C 1 212 ? 27.166  -3.581  6.294   1.00 32.34  ? 212 PRO C CA    1 
ATOM   9737  C C     . PRO C 1 212 ? 27.975  -2.303  6.060   1.00 33.71  ? 212 PRO C C     1 
ATOM   9738  O O     . PRO C 1 212 ? 27.758  -1.298  6.728   1.00 32.73  ? 212 PRO C O     1 
ATOM   9739  C CB    . PRO C 1 212 ? 25.741  -3.431  5.696   1.00 32.36  ? 212 PRO C CB    1 
ATOM   9740  C CG    . PRO C 1 212 ? 24.761  -3.736  6.784   1.00 30.02  ? 212 PRO C CG    1 
ATOM   9741  C CD    . PRO C 1 212 ? 25.530  -3.805  8.092   1.00 31.24  ? 212 PRO C CD    1 
ATOM   9742  N N     . TYR C 1 213 ? 28.897  -2.354  5.101   1.00 32.53  ? 213 TYR C N     1 
ATOM   9743  C CA    . TYR C 1 213 ? 29.759  -1.241  4.779   1.00 34.03  ? 213 TYR C CA    1 
ATOM   9744  C C     . TYR C 1 213 ? 29.071  -0.447  3.694   1.00 33.25  ? 213 TYR C C     1 
ATOM   9745  O O     . TYR C 1 213 ? 28.861  -0.993  2.623   1.00 36.82  ? 213 TYR C O     1 
ATOM   9746  C CB    . TYR C 1 213 ? 31.127  -1.739  4.309   1.00 35.50  ? 213 TYR C CB    1 
ATOM   9747  C CG    . TYR C 1 213 ? 32.107  -0.654  3.983   1.00 33.04  ? 213 TYR C CG    1 
ATOM   9748  C CD1   . TYR C 1 213 ? 32.106  0.517   4.712   1.00 35.06  ? 213 TYR C CD1   1 
ATOM   9749  C CD2   . TYR C 1 213 ? 33.089  -0.804  3.021   1.00 42.41  ? 213 TYR C CD2   1 
ATOM   9750  C CE1   . TYR C 1 213 ? 33.006  1.533   4.461   1.00 34.83  ? 213 TYR C CE1   1 
ATOM   9751  C CE2   . TYR C 1 213 ? 34.006  0.217   2.752   1.00 42.99  ? 213 TYR C CE2   1 
ATOM   9752  C CZ    . TYR C 1 213 ? 33.944  1.413   3.451   1.00 38.19  ? 213 TYR C CZ    1 
ATOM   9753  O OH    . TYR C 1 213 ? 34.805  2.510   3.322   1.00 45.16  ? 213 TYR C OH    1 
ATOM   9754  N N     . VAL C 1 214 ? 28.694  0.796   3.995   1.00 33.29  ? 214 VAL C N     1 
ATOM   9755  C CA    . VAL C 1 214 ? 27.710  1.515   3.205   1.00 31.56  ? 214 VAL C CA    1 
ATOM   9756  C C     . VAL C 1 214 ? 28.242  2.840   2.696   1.00 34.22  ? 214 VAL C C     1 
ATOM   9757  O O     . VAL C 1 214 ? 27.608  3.412   1.785   1.00 39.34  ? 214 VAL C O     1 
ATOM   9758  C CB    . VAL C 1 214 ? 26.406  1.783   3.979   1.00 33.11  ? 214 VAL C CB    1 
ATOM   9759  C CG1   . VAL C 1 214 ? 25.725  0.513   4.372   1.00 33.61  ? 214 VAL C CG1   1 
ATOM   9760  C CG2   . VAL C 1 214 ? 26.609  2.652   5.183   1.00 32.69  ? 214 VAL C CG2   1 
ATOM   9761  N N     . ASP C 1 215 ? 29.380  3.316   3.239   1.00 28.90  ? 215 ASP C N     1 
ATOM   9762  C CA    . ASP C 1 215 ? 29.959  4.543   2.707   1.00 31.53  ? 215 ASP C CA    1 
ATOM   9763  C C     . ASP C 1 215 ? 29.915  4.591   1.176   1.00 32.20  ? 215 ASP C C     1 
ATOM   9764  O O     . ASP C 1 215 ? 29.671  5.623   0.558   1.00 34.33  ? 215 ASP C O     1 
ATOM   9765  C CB    . ASP C 1 215 ? 31.404  4.709   3.132   1.00 32.36  ? 215 ASP C CB    1 
ATOM   9766  C CG    . ASP C 1 215 ? 31.507  4.875   4.643   1.00 34.22  ? 215 ASP C CG    1 
ATOM   9767  O OD1   . ASP C 1 215 ? 31.301  3.859   5.310   1.00 25.69  ? 215 ASP C OD1   1 
ATOM   9768  O OD2   . ASP C 1 215 ? 31.756  6.041   5.120   1.00 29.20  ? 215 ASP C OD2   1 
ATOM   9769  N N     . GLY C 1 216 ? 30.206  3.463   0.548   1.00 29.11  ? 216 GLY C N     1 
ATOM   9770  C CA    . GLY C 1 216 ? 30.341  3.447   -0.884  1.00 28.36  ? 216 GLY C CA    1 
ATOM   9771  C C     . GLY C 1 216 ? 29.009  3.745   -1.554  1.00 31.26  ? 216 GLY C C     1 
ATOM   9772  O O     . GLY C 1 216 ? 29.064  4.200   -2.670  1.00 29.39  ? 216 GLY C O     1 
ATOM   9773  N N     . ILE C 1 217 ? 27.839  3.499   -0.907  1.00 29.42  ? 217 ILE C N     1 
ATOM   9774  C CA    . ILE C 1 217 ? 26.593  3.716   -1.618  1.00 29.13  ? 217 ILE C CA    1 
ATOM   9775  C C     . ILE C 1 217 ? 26.325  5.213   -1.823  1.00 36.46  ? 217 ILE C C     1 
ATOM   9776  O O     . ILE C 1 217 ? 25.472  5.567   -2.657  1.00 33.41  ? 217 ILE C O     1 
ATOM   9777  C CB    . ILE C 1 217 ? 25.398  2.983   -0.982  1.00 32.69  ? 217 ILE C CB    1 
ATOM   9778  C CG1   . ILE C 1 217 ? 24.788  3.709   0.217   1.00 35.45  ? 217 ILE C CG1   1 
ATOM   9779  C CG2   . ILE C 1 217 ? 25.733  1.547   -0.649  1.00 33.44  ? 217 ILE C CG2   1 
ATOM   9780  C CD1   . ILE C 1 217 ? 23.492  3.109   0.658   1.00 34.35  ? 217 ILE C CD1   1 
ATOM   9781  N N     . PHE C 1 218 ? 27.067  6.089   -1.107  1.00 36.77  ? 218 PHE C N     1 
ATOM   9782  C CA    . PHE C 1 218 ? 26.902  7.537   -1.230  1.00 37.97  ? 218 PHE C CA    1 
ATOM   9783  C C     . PHE C 1 218 ? 27.958  8.165   -2.144  1.00 36.14  ? 218 PHE C C     1 
ATOM   9784  O O     . PHE C 1 218 ? 28.104  9.396   -2.143  1.00 33.42  ? 218 PHE C O     1 
ATOM   9785  C CB    . PHE C 1 218 ? 26.957  8.206   0.153   1.00 39.94  ? 218 PHE C CB    1 
ATOM   9786  C CG    . PHE C 1 218 ? 25.945  7.641   1.111   1.00 37.84  ? 218 PHE C CG    1 
ATOM   9787  C CD1   . PHE C 1 218 ? 24.594  7.692   0.812   1.00 35.67  ? 218 PHE C CD1   1 
ATOM   9788  C CD2   . PHE C 1 218 ? 26.344  6.958   2.237   1.00 36.00  ? 218 PHE C CD2   1 
ATOM   9789  C CE1   . PHE C 1 218 ? 23.660  7.121   1.653   1.00 34.91  ? 218 PHE C CE1   1 
ATOM   9790  C CE2   . PHE C 1 218 ? 25.406  6.368   3.064   1.00 39.47  ? 218 PHE C CE2   1 
ATOM   9791  C CZ    . PHE C 1 218 ? 24.064  6.460   2.779   1.00 35.95  ? 218 PHE C CZ    1 
ATOM   9792  N N     . SER C 1 219 ? 28.728  7.333   -2.870  1.00 30.31  ? 219 SER C N     1 
ATOM   9793  C CA    . SER C 1 219 ? 29.591  7.822   -3.937  1.00 35.23  ? 219 SER C CA    1 
ATOM   9794  C C     . SER C 1 219 ? 28.893  7.579   -5.277  1.00 34.64  ? 219 SER C C     1 
ATOM   9795  O O     . SER C 1 219 ? 28.115  6.654   -5.382  1.00 37.62  ? 219 SER C O     1 
ATOM   9796  C CB    . SER C 1 219 ? 30.983  7.234   -3.888  1.00 31.66  ? 219 SER C CB    1 
ATOM   9797  O OG    . SER C 1 219 ? 30.970  5.833   -4.157  1.00 40.99  ? 219 SER C OG    1 
ATOM   9798  N N     . GLN C 1 220 ? 29.168  8.427   -6.283  1.00 33.43  ? 220 GLN C N     1 
ATOM   9799  C CA    . GLN C 1 220 ? 28.457  8.463   -7.559  1.00 33.59  ? 220 GLN C CA    1 
ATOM   9800  C C     . GLN C 1 220 ? 26.976  8.055   -7.463  1.00 34.38  ? 220 GLN C C     1 
ATOM   9801  O O     . GLN C 1 220 ? 26.529  7.137   -8.156  1.00 35.48  ? 220 GLN C O     1 
ATOM   9802  C CB    . GLN C 1 220 ? 29.179  7.561   -8.548  1.00 35.03  ? 220 GLN C CB    1 
ATOM   9803  C CG    . GLN C 1 220 ? 30.566  8.071   -8.919  1.00 36.21  ? 220 GLN C CG    1 
ATOM   9804  C CD    . GLN C 1 220 ? 31.100  7.468   -10.202 1.00 34.29  ? 220 GLN C CD    1 
ATOM   9805  O OE1   . GLN C 1 220 ? 30.638  6.443   -10.689 1.00 36.90  ? 220 GLN C OE1   1 
ATOM   9806  N NE2   . GLN C 1 220 ? 32.098  8.119   -10.768 1.00 39.32  ? 220 GLN C NE2   1 
ATOM   9807  N N     . SER C 1 221 ? 26.208  8.737   -6.612  1.00 31.83  ? 221 SER C N     1 
ATOM   9808  C CA    . SER C 1 221 ? 24.851  8.315   -6.328  1.00 39.47  ? 221 SER C CA    1 
ATOM   9809  C C     . SER C 1 221 ? 24.015  9.511   -5.926  1.00 35.27  ? 221 SER C C     1 
ATOM   9810  O O     . SER C 1 221 ? 24.525  10.594  -5.683  1.00 36.83  ? 221 SER C O     1 
ATOM   9811  C CB    . SER C 1 221 ? 24.788  7.233   -5.244  1.00 52.41  ? 221 SER C CB    1 
ATOM   9812  O OG    . SER C 1 221 ? 24.998  7.749   -3.929  1.00 54.13  ? 221 SER C OG    1 
ATOM   9813  N N     . ASN C 1 222 ? 22.724  9.249   -5.842  1.00 34.02  ? 222 ASN C N     1 
ATOM   9814  C CA    . ASN C 1 222 ? 21.742  10.192  -5.350  1.00 34.29  ? 222 ASN C CA    1 
ATOM   9815  C C     . ASN C 1 222 ? 21.021  9.543   -4.161  1.00 35.11  ? 222 ASN C C     1 
ATOM   9816  O O     . ASN C 1 222 ? 19.788  9.581   -4.084  1.00 32.47  ? 222 ASN C O     1 
ATOM   9817  C CB    . ASN C 1 222 ? 20.758  10.570  -6.464  1.00 34.01  ? 222 ASN C CB    1 
ATOM   9818  C CG    . ASN C 1 222 ? 20.124  9.365   -7.142  1.00 38.10  ? 222 ASN C CG    1 
ATOM   9819  O OD1   . ASN C 1 222 ? 20.263  8.219   -6.720  1.00 39.54  ? 222 ASN C OD1   1 
ATOM   9820  N ND2   . ASN C 1 222 ? 19.462  9.593   -8.255  1.00 47.31  ? 222 ASN C ND2   1 
ATOM   9821  N N     . PHE C 1 223 ? 21.800  8.919   -3.263  1.00 35.98  ? 223 PHE C N     1 
ATOM   9822  C CA    . PHE C 1 223 ? 21.268  8.206   -2.107  1.00 39.92  ? 223 PHE C CA    1 
ATOM   9823  C C     . PHE C 1 223 ? 21.403  9.025   -0.827  1.00 39.20  ? 223 PHE C C     1 
ATOM   9824  O O     . PHE C 1 223 ? 20.904  8.627   0.228   1.00 36.83  ? 223 PHE C O     1 
ATOM   9825  C CB    . PHE C 1 223 ? 21.970  6.863   -1.917  1.00 38.18  ? 223 PHE C CB    1 
ATOM   9826  C CG    . PHE C 1 223 ? 21.653  5.830   -2.961  1.00 40.25  ? 223 PHE C CG    1 
ATOM   9827  C CD1   . PHE C 1 223 ? 20.715  6.065   -3.960  1.00 41.78  ? 223 PHE C CD1   1 
ATOM   9828  C CD2   . PHE C 1 223 ? 22.261  4.588   -2.910  1.00 41.15  ? 223 PHE C CD2   1 
ATOM   9829  C CE1   . PHE C 1 223 ? 20.439  5.087   -4.909  1.00 42.47  ? 223 PHE C CE1   1 
ATOM   9830  C CE2   . PHE C 1 223 ? 21.995  3.623   -3.874  1.00 40.92  ? 223 PHE C CE2   1 
ATOM   9831  C CZ    . PHE C 1 223 ? 21.079  3.873   -4.867  1.00 36.19  ? 223 PHE C CZ    1 
ATOM   9832  N N     . GLY C 1 224 ? 22.089  10.168  -0.909  1.00 39.90  ? 224 GLY C N     1 
ATOM   9833  C CA    . GLY C 1 224 ? 22.120  11.069  0.231   1.00 40.71  ? 224 GLY C CA    1 
ATOM   9834  C C     . GLY C 1 224 ? 23.070  12.244  0.044   1.00 39.39  ? 224 GLY C C     1 
ATOM   9835  O O     . GLY C 1 224 ? 23.893  12.232  -0.863  1.00 41.89  ? 224 GLY C O     1 
ATOM   9836  N N     . VAL C 1 225 ? 22.974  13.233  0.944   1.00 40.88  ? 225 VAL C N     1 
ATOM   9837  C CA    . VAL C 1 225 ? 23.852  14.389  0.886   1.00 37.25  ? 225 VAL C CA    1 
ATOM   9838  C C     . VAL C 1 225 ? 24.921  14.254  1.972   1.00 38.42  ? 225 VAL C C     1 
ATOM   9839  O O     . VAL C 1 225 ? 24.608  14.264  3.160   1.00 44.95  ? 225 VAL C O     1 
ATOM   9840  C CB    . VAL C 1 225 ? 23.058  15.705  1.014   1.00 37.18  ? 225 VAL C CB    1 
ATOM   9841  C CG1   . VAL C 1 225 ? 23.946  16.914  1.003   1.00 34.40  ? 225 VAL C CG1   1 
ATOM   9842  C CG2   . VAL C 1 225 ? 21.997  15.841  -0.052  1.00 43.32  ? 225 VAL C CG2   1 
ATOM   9843  N N     . VAL C 1 226 ? 26.186  14.147  1.546   1.00 34.24  ? 226 VAL C N     1 
ATOM   9844  C CA    . VAL C 1 226 ? 27.351  14.064  2.402   1.00 27.81  ? 226 VAL C CA    1 
ATOM   9845  C C     . VAL C 1 226 ? 27.663  15.461  2.946   1.00 36.36  ? 226 VAL C C     1 
ATOM   9846  O O     . VAL C 1 226 ? 27.859  16.406  2.170   1.00 33.02  ? 226 VAL C O     1 
ATOM   9847  C CB    . VAL C 1 226 ? 28.496  13.482  1.564   1.00 29.85  ? 226 VAL C CB    1 
ATOM   9848  C CG1   . VAL C 1 226 ? 29.851  13.572  2.275   1.00 34.27  ? 226 VAL C CG1   1 
ATOM   9849  C CG2   . VAL C 1 226 ? 28.206  12.037  1.130   1.00 32.66  ? 226 VAL C CG2   1 
ATOM   9850  N N     . THR C 1 227 ? 27.747  15.576  4.281   1.00 35.55  ? 227 THR C N     1 
ATOM   9851  C CA    . THR C 1 227 ? 27.898  16.866  4.944   1.00 35.89  ? 227 THR C CA    1 
ATOM   9852  C C     . THR C 1 227 ? 29.231  16.957  5.698   1.00 33.26  ? 227 THR C C     1 
ATOM   9853  O O     . THR C 1 227 ? 29.716  18.041  5.966   1.00 29.72  ? 227 THR C O     1 
ATOM   9854  C CB    . THR C 1 227 ? 26.737  17.075  5.918   1.00 42.24  ? 227 THR C CB    1 
ATOM   9855  O OG1   . THR C 1 227 ? 26.763  16.018  6.887   1.00 45.60  ? 227 THR C OG1   1 
ATOM   9856  C CG2   . THR C 1 227 ? 25.396  17.077  5.223   1.00 43.69  ? 227 THR C CG2   1 
ATOM   9857  N N     . LYS C 1 228 ? 29.800  15.809  6.067   1.00 33.42  ? 228 LYS C N     1 
ATOM   9858  C CA    . LYS C 1 228 ? 31.168  15.719  6.551   1.00 36.35  ? 228 LYS C CA    1 
ATOM   9859  C C     . LYS C 1 228 ? 31.757  14.418  6.025   1.00 38.90  ? 228 LYS C C     1 
ATOM   9860  O O     . LYS C 1 228 ? 31.037  13.393  5.926   1.00 33.22  ? 228 LYS C O     1 
ATOM   9861  C CB    . LYS C 1 228 ? 31.230  15.659  8.088   1.00 35.55  ? 228 LYS C CB    1 
ATOM   9862  C CG    . LYS C 1 228 ? 30.452  16.744  8.825   1.00 37.93  ? 228 LYS C CG    1 
ATOM   9863  C CD    . LYS C 1 228 ? 30.397  16.566  10.358  1.00 45.02  ? 228 LYS C CD    1 
ATOM   9864  C CE    . LYS C 1 228 ? 29.922  17.786  11.123  1.00 36.48  ? 228 LYS C CE    1 
ATOM   9865  N NZ    . LYS C 1 228 ? 28.517  18.073  10.790  1.00 38.66  ? 228 LYS C NZ    1 
ATOM   9866  N N     . MET C 1 229 ? 33.075  14.451  5.784   1.00 32.65  ? 229 MET C N     1 
ATOM   9867  C CA    . MET C 1 229 ? 33.761  13.274  5.294   1.00 30.41  ? 229 MET C CA    1 
ATOM   9868  C C     . MET C 1 229 ? 35.170  13.251  5.856   1.00 33.57  ? 229 MET C C     1 
ATOM   9869  O O     . MET C 1 229 ? 35.811  14.294  5.959   1.00 34.35  ? 229 MET C O     1 
ATOM   9870  C CB    . MET C 1 229 ? 33.852  13.345  3.770   1.00 31.84  ? 229 MET C CB    1 
ATOM   9871  C CG    . MET C 1 229 ? 34.210  12.015  3.127   1.00 36.91  ? 229 MET C CG    1 
ATOM   9872  S SD    . MET C 1 229 ? 34.511  12.182  1.342   1.00 35.47  ? 229 MET C SD    1 
ATOM   9873  C CE    . MET C 1 229 ? 36.276  12.485  1.346   1.00 28.46  ? 229 MET C CE    1 
ATOM   9874  N N     . GLY C 1 230 ? 35.661  12.059  6.195   1.00 34.02  ? 230 GLY C N     1 
ATOM   9875  C CA    . GLY C 1 230 ? 37.057  11.907  6.575   1.00 33.07  ? 230 GLY C CA    1 
ATOM   9876  C C     . GLY C 1 230 ? 37.861  11.413  5.380   1.00 35.56  ? 230 GLY C C     1 
ATOM   9877  O O     . GLY C 1 230 ? 37.254  10.796  4.486   1.00 31.90  ? 230 GLY C O     1 
ATOM   9878  N N     . ILE C 1 231 ? 39.189  11.656  5.392   1.00 30.08  ? 231 ILE C N     1 
ATOM   9879  C CA    . ILE C 1 231 ? 40.068  11.189  4.320   1.00 32.49  ? 231 ILE C CA    1 
ATOM   9880  C C     . ILE C 1 231 ? 41.470  11.023  4.877   1.00 35.24  ? 231 ILE C C     1 
ATOM   9881  O O     . ILE C 1 231 ? 41.954  11.931  5.536   1.00 39.51  ? 231 ILE C O     1 
ATOM   9882  C CB    . ILE C 1 231 ? 40.128  12.155  3.127   1.00 34.31  ? 231 ILE C CB    1 
ATOM   9883  C CG1   . ILE C 1 231 ? 41.131  11.697  2.059   1.00 36.78  ? 231 ILE C CG1   1 
ATOM   9884  C CG2   . ILE C 1 231 ? 40.506  13.551  3.589   1.00 38.07  ? 231 ILE C CG2   1 
ATOM   9885  C CD1   . ILE C 1 231 ? 40.863  12.280  0.671   1.00 33.64  ? 231 ILE C CD1   1 
ATOM   9886  N N     . TRP C 1 232 ? 42.099  9.872   4.607   1.00 36.94  ? 232 TRP C N     1 
ATOM   9887  C CA    . TRP C 1 232 ? 43.459  9.619   5.050   1.00 38.46  ? 232 TRP C CA    1 
ATOM   9888  C C     . TRP C 1 232 ? 44.412  10.512  4.262   1.00 37.34  ? 232 TRP C C     1 
ATOM   9889  O O     . TRP C 1 232 ? 44.188  10.752  3.077   1.00 32.57  ? 232 TRP C O     1 
ATOM   9890  C CB    . TRP C 1 232 ? 43.819  8.126   4.923   1.00 36.31  ? 232 TRP C CB    1 
ATOM   9891  C CG    . TRP C 1 232 ? 43.014  7.242   5.832   1.00 41.22  ? 232 TRP C CG    1 
ATOM   9892  C CD1   . TRP C 1 232 ? 42.422  7.602   7.015   1.00 36.54  ? 232 TRP C CD1   1 
ATOM   9893  C CD2   . TRP C 1 232 ? 42.641  5.868   5.608   1.00 38.17  ? 232 TRP C CD2   1 
ATOM   9894  N NE1   . TRP C 1 232 ? 41.711  6.562   7.536   1.00 37.66  ? 232 TRP C NE1   1 
ATOM   9895  C CE2   . TRP C 1 232 ? 41.827  5.482   6.694   1.00 39.04  ? 232 TRP C CE2   1 
ATOM   9896  C CE3   . TRP C 1 232 ? 42.936  4.919   4.624   1.00 40.47  ? 232 TRP C CE3   1 
ATOM   9897  C CZ2   . TRP C 1 232 ? 41.318  4.190   6.817   1.00 35.53  ? 232 TRP C CZ2   1 
ATOM   9898  C CZ3   . TRP C 1 232 ? 42.440  3.635   4.753   1.00 40.28  ? 232 TRP C CZ3   1 
ATOM   9899  C CH2   . TRP C 1 232 ? 41.642  3.275   5.842   1.00 34.62  ? 232 TRP C CH2   1 
ATOM   9900  N N     . LEU C 1 233 ? 45.449  10.996  4.964   1.00 39.05  ? 233 LEU C N     1 
ATOM   9901  C CA    . LEU C 1 233 ? 46.527  11.802  4.407   1.00 44.33  ? 233 LEU C CA    1 
ATOM   9902  C C     . LEU C 1 233 ? 47.877  11.119  4.606   1.00 39.97  ? 233 LEU C C     1 
ATOM   9903  O O     . LEU C 1 233 ? 48.174  10.607  5.686   1.00 41.17  ? 233 LEU C O     1 
ATOM   9904  C CB    . LEU C 1 233 ? 46.546  13.162  5.114   1.00 44.86  ? 233 LEU C CB    1 
ATOM   9905  C CG    . LEU C 1 233 ? 45.276  13.990  4.960   1.00 42.36  ? 233 LEU C CG    1 
ATOM   9906  C CD1   . LEU C 1 233 ? 45.446  15.315  5.677   1.00 44.63  ? 233 LEU C CD1   1 
ATOM   9907  C CD2   . LEU C 1 233 ? 44.926  14.214  3.480   1.00 37.66  ? 233 LEU C CD2   1 
ATOM   9908  N N     . MET C 1 234 ? 48.694  11.188  3.560   1.00 36.11  ? 234 MET C N     1 
ATOM   9909  C CA    . MET C 1 234 ? 49.959  10.505  3.511   1.00 39.64  ? 234 MET C CA    1 
ATOM   9910  C C     . MET C 1 234 ? 50.914  11.302  4.370   1.00 41.78  ? 234 MET C C     1 
ATOM   9911  O O     . MET C 1 234 ? 51.029  12.501  4.149   1.00 44.56  ? 234 MET C O     1 
ATOM   9912  C CB    . MET C 1 234 ? 50.509  10.455  2.079   1.00 44.79  ? 234 MET C CB    1 
ATOM   9913  C CG    . MET C 1 234 ? 51.853  9.717   1.952   1.00 43.53  ? 234 MET C CG    1 
ATOM   9914  S SD    . MET C 1 234 ? 52.393  9.367   0.251   1.00 46.04  ? 234 MET C SD    1 
ATOM   9915  C CE    . MET C 1 234 ? 52.807  11.023  -0.267  1.00 53.02  ? 234 MET C CE    1 
ATOM   9916  N N     . PRO C 1 235 ? 51.606  10.681  5.355   1.00 43.68  ? 235 PRO C N     1 
ATOM   9917  C CA    . PRO C 1 235 ? 52.739  11.318  6.035   1.00 42.83  ? 235 PRO C CA    1 
ATOM   9918  C C     . PRO C 1 235 ? 53.802  11.759  5.048   1.00 39.98  ? 235 PRO C C     1 
ATOM   9919  O O     . PRO C 1 235 ? 54.118  11.021  4.128   1.00 46.02  ? 235 PRO C O     1 
ATOM   9920  C CB    . PRO C 1 235 ? 53.333  10.204  6.916   1.00 39.50  ? 235 PRO C CB    1 
ATOM   9921  C CG    . PRO C 1 235 ? 52.164  9.283   7.153   1.00 43.21  ? 235 PRO C CG    1 
ATOM   9922  C CD    . PRO C 1 235 ? 51.369  9.324   5.858   1.00 41.61  ? 235 PRO C CD    1 
ATOM   9923  N N     . GLU C 1 236 ? 54.351  12.948  5.256   1.00 46.51  ? 236 GLU C N     1 
ATOM   9924  C CA    . GLU C 1 236 ? 55.501  13.404  4.487   1.00 48.13  ? 236 GLU C CA    1 
ATOM   9925  C C     . GLU C 1 236 ? 56.570  12.316  4.470   1.00 37.34  ? 236 GLU C C     1 
ATOM   9926  O O     . GLU C 1 236 ? 57.024  11.873  5.513   1.00 46.42  ? 236 GLU C O     1 
ATOM   9927  C CB    . GLU C 1 236 ? 56.070  14.694  5.079   1.00 55.55  ? 236 GLU C CB    1 
ATOM   9928  C CG    . GLU C 1 236 ? 57.420  15.101  4.504   1.00 65.39  ? 236 GLU C CG    1 
ATOM   9929  C CD    . GLU C 1 236 ? 57.667  16.608  4.491   1.00 73.29  ? 236 GLU C CD    1 
ATOM   9930  O OE1   . GLU C 1 236 ? 57.381  17.278  5.513   1.00 63.12  ? 236 GLU C OE1   1 
ATOM   9931  O OE2   . GLU C 1 236 ? 58.135  17.117  3.449   1.00 74.79  ? 236 GLU C OE2   1 
ATOM   9932  N N     . PRO C 1 237 ? 56.977  11.814  3.294   1.00 32.86  ? 237 PRO C N     1 
ATOM   9933  C CA    . PRO C 1 237 ? 58.026  10.814  3.225   1.00 37.95  ? 237 PRO C CA    1 
ATOM   9934  C C     . PRO C 1 237 ? 59.435  11.390  3.348   1.00 40.26  ? 237 PRO C C     1 
ATOM   9935  O O     . PRO C 1 237 ? 59.647  12.597  3.288   1.00 41.46  ? 237 PRO C O     1 
ATOM   9936  C CB    . PRO C 1 237 ? 57.760  10.229  1.835   1.00 39.55  ? 237 PRO C CB    1 
ATOM   9937  C CG    . PRO C 1 237 ? 57.396  11.445  1.035   1.00 41.45  ? 237 PRO C CG    1 
ATOM   9938  C CD    . PRO C 1 237 ? 56.454  12.173  1.967   1.00 37.55  ? 237 PRO C CD    1 
ATOM   9939  N N     . ALA C 1 238 ? 60.401  10.499  3.544   1.00 40.86  ? 238 ALA C N     1 
ATOM   9940  C CA    . ALA C 1 238 ? 61.779  10.907  3.740   1.00 44.57  ? 238 ALA C CA    1 
ATOM   9941  C C     . ALA C 1 238 ? 62.458  11.303  2.426   1.00 45.20  ? 238 ALA C C     1 
ATOM   9942  O O     . ALA C 1 238 ? 63.516  11.910  2.454   1.00 49.23  ? 238 ALA C O     1 
ATOM   9943  C CB    . ALA C 1 238 ? 62.503  9.787   4.420   1.00 46.16  ? 238 ALA C CB    1 
ATOM   9944  N N     . GLY C 1 239 ? 61.862  10.996  1.273   1.00 49.95  ? 239 GLY C N     1 
ATOM   9945  C CA    . GLY C 1 239 ? 62.448  11.390  -0.005  1.00 47.98  ? 239 GLY C CA    1 
ATOM   9946  C C     . GLY C 1 239 ? 61.410  11.459  -1.134  1.00 48.69  ? 239 GLY C C     1 
ATOM   9947  O O     . GLY C 1 239 ? 60.309  10.914  -1.015  1.00 44.72  ? 239 GLY C O     1 
ATOM   9948  N N     . TYR C 1 240 ? 61.780  12.135  -2.228  1.00 43.34  ? 240 TYR C N     1 
ATOM   9949  C CA    . TYR C 1 240 ? 60.917  12.296  -3.380  1.00 44.52  ? 240 TYR C CA    1 
ATOM   9950  C C     . TYR C 1 240 ? 61.784  12.572  -4.603  1.00 45.93  ? 240 TYR C C     1 
ATOM   9951  O O     . TYR C 1 240 ? 62.508  13.553  -4.648  1.00 57.37  ? 240 TYR C O     1 
ATOM   9952  C CB    . TYR C 1 240 ? 59.898  13.406  -3.123  1.00 43.05  ? 240 TYR C CB    1 
ATOM   9953  C CG    . TYR C 1 240 ? 58.973  13.716  -4.274  1.00 45.09  ? 240 TYR C CG    1 
ATOM   9954  C CD1   . TYR C 1 240 ? 58.069  12.777  -4.744  1.00 45.63  ? 240 TYR C CD1   1 
ATOM   9955  C CD2   . TYR C 1 240 ? 58.994  14.953  -4.905  1.00 44.12  ? 240 TYR C CD2   1 
ATOM   9956  C CE1   . TYR C 1 240 ? 57.197  13.057  -5.795  1.00 42.81  ? 240 TYR C CE1   1 
ATOM   9957  C CE2   . TYR C 1 240 ? 58.138  15.240  -5.961  1.00 48.44  ? 240 TYR C CE2   1 
ATOM   9958  C CZ    . TYR C 1 240 ? 57.232  14.294  -6.416  1.00 43.01  ? 240 TYR C CZ    1 
ATOM   9959  O OH    . TYR C 1 240 ? 56.393  14.575  -7.478  1.00 39.58  ? 240 TYR C OH    1 
ATOM   9960  N N     . ARG C 1 241 ? 61.700  11.685  -5.589  1.00 50.05  ? 241 ARG C N     1 
ATOM   9961  C CA    . ARG C 1 241 ? 62.438  11.795  -6.832  1.00 50.96  ? 241 ARG C CA    1 
ATOM   9962  C C     . ARG C 1 241 ? 61.418  11.620  -7.959  1.00 50.87  ? 241 ARG C C     1 
ATOM   9963  O O     . ARG C 1 241 ? 60.985  10.503  -8.219  1.00 54.77  ? 241 ARG C O     1 
ATOM   9964  C CB    . ARG C 1 241 ? 63.560  10.743  -6.834  1.00 54.59  ? 241 ARG C CB    1 
ATOM   9965  C CG    . ARG C 1 241 ? 64.858  11.153  -6.135  1.00 62.07  ? 241 ARG C CG    1 
ATOM   9966  C CD    . ARG C 1 241 ? 65.924  10.051  -6.033  1.00 72.95  ? 241 ARG C CD    1 
ATOM   9967  N NE    . ARG C 1 241 ? 66.604  9.706   -7.296  1.00 83.22  ? 241 ARG C NE    1 
ATOM   9968  C CZ    . ARG C 1 241 ? 67.238  8.551   -7.533  1.00 76.90  ? 241 ARG C CZ    1 
ATOM   9969  N NH1   . ARG C 1 241 ? 67.288  7.613   -6.605  1.00 81.58  ? 241 ARG C NH1   1 
ATOM   9970  N NH2   . ARG C 1 241 ? 67.820  8.324   -8.699  1.00 70.43  ? 241 ARG C NH2   1 
ATOM   9971  N N     . PRO C 1 242 ? 60.917  12.700  -8.610  1.00 48.62  ? 242 PRO C N     1 
ATOM   9972  C CA    . PRO C 1 242 ? 60.009  12.561  -9.757  1.00 42.46  ? 242 PRO C CA    1 
ATOM   9973  C C     . PRO C 1 242 ? 60.847  12.186  -10.961 1.00 40.15  ? 242 PRO C C     1 
ATOM   9974  O O     . PRO C 1 242 ? 62.017  12.525  -10.994 1.00 45.26  ? 242 PRO C O     1 
ATOM   9975  C CB    . PRO C 1 242 ? 59.338  13.927  -9.922  1.00 40.90  ? 242 PRO C CB    1 
ATOM   9976  C CG    . PRO C 1 242 ? 60.269  14.896  -9.192  1.00 46.44  ? 242 PRO C CG    1 
ATOM   9977  C CD    . PRO C 1 242 ? 61.141  14.103  -8.238  1.00 48.74  ? 242 PRO C CD    1 
ATOM   9978  N N     . TYR C 1 243 ? 60.280  11.445  -11.916 1.00 43.56  ? 243 TYR C N     1 
ATOM   9979  C CA    . TYR C 1 243 ? 61.063  11.050  -13.078 1.00 40.91  ? 243 TYR C CA    1 
ATOM   9980  C C     . TYR C 1 243 ? 60.215  11.136  -14.345 1.00 36.47  ? 243 TYR C C     1 
ATOM   9981  O O     . TYR C 1 243 ? 58.993  11.246  -14.282 1.00 36.10  ? 243 TYR C O     1 
ATOM   9982  C CB    . TYR C 1 243 ? 61.684  9.672   -12.834 1.00 45.50  ? 243 TYR C CB    1 
ATOM   9983  C CG    . TYR C 1 243 ? 60.717  8.518   -12.702 1.00 44.11  ? 243 TYR C CG    1 
ATOM   9984  C CD1   . TYR C 1 243 ? 60.013  8.017   -13.786 1.00 40.21  ? 243 TYR C CD1   1 
ATOM   9985  C CD2   . TYR C 1 243 ? 60.511  7.911   -11.477 1.00 47.84  ? 243 TYR C CD2   1 
ATOM   9986  C CE1   . TYR C 1 243 ? 59.117  6.967   -13.639 1.00 46.83  ? 243 TYR C CE1   1 
ATOM   9987  C CE2   . TYR C 1 243 ? 59.622  6.863   -11.313 1.00 46.69  ? 243 TYR C CE2   1 
ATOM   9988  C CZ    . TYR C 1 243 ? 58.927  6.377   -12.402 1.00 46.70  ? 243 TYR C CZ    1 
ATOM   9989  O OH    . TYR C 1 243 ? 58.068  5.319   -12.220 1.00 50.67  ? 243 TYR C OH    1 
ATOM   9990  N N     . LEU C 1 244 ? 60.888  11.107  -15.502 1.00 37.82  ? 244 LEU C N     1 
ATOM   9991  C CA    . LEU C 1 244 ? 60.216  11.077  -16.798 1.00 41.42  ? 244 LEU C CA    1 
ATOM   9992  C C     . LEU C 1 244 ? 60.960  10.116  -17.713 1.00 40.61  ? 244 LEU C C     1 
ATOM   9993  O O     . LEU C 1 244 ? 62.174  10.216  -17.861 1.00 44.01  ? 244 LEU C O     1 
ATOM   9994  C CB    . LEU C 1 244 ? 60.192  12.467  -17.442 1.00 40.16  ? 244 LEU C CB    1 
ATOM   9995  C CG    . LEU C 1 244 ? 59.820  12.519  -18.932 1.00 42.93  ? 244 LEU C CG    1 
ATOM   9996  C CD1   . LEU C 1 244 ? 58.432  11.942  -19.201 1.00 46.67  ? 244 LEU C CD1   1 
ATOM   9997  C CD2   . LEU C 1 244 ? 59.861  13.959  -19.436 1.00 42.00  ? 244 LEU C CD2   1 
ATOM   9998  N N     . ILE C 1 245 ? 60.212  9.209   -18.336 1.00 37.94  ? 245 ILE C N     1 
ATOM   9999  C CA    . ILE C 1 245 ? 60.778  8.317   -19.321 1.00 36.70  ? 245 ILE C CA    1 
ATOM   10000 C C     . ILE C 1 245 ? 59.976  8.548   -20.584 1.00 40.65  ? 245 ILE C C     1 
ATOM   10001 O O     . ILE C 1 245 ? 58.740  8.628   -20.495 1.00 40.46  ? 245 ILE C O     1 
ATOM   10002 C CB    . ILE C 1 245 ? 60.655  6.852   -18.873 1.00 38.55  ? 245 ILE C CB    1 
ATOM   10003 C CG1   . ILE C 1 245 ? 61.169  6.666   -17.445 1.00 40.82  ? 245 ILE C CG1   1 
ATOM   10004 C CG2   . ILE C 1 245 ? 61.345  5.936   -19.888 1.00 41.56  ? 245 ILE C CG2   1 
ATOM   10005 C CD1   . ILE C 1 245 ? 60.985  5.268   -16.873 1.00 42.63  ? 245 ILE C CD1   1 
ATOM   10006 N N     . THR C 1 246 ? 60.690  8.659   -21.711 1.00 37.34  ? 246 THR C N     1 
ATOM   10007 C CA    . THR C 1 246 ? 60.062  8.956   -22.988 1.00 42.79  ? 246 THR C CA    1 
ATOM   10008 C C     . THR C 1 246 ? 60.339  7.826   -23.978 1.00 42.28  ? 246 THR C C     1 
ATOM   10009 O O     . THR C 1 246 ? 61.346  7.134   -23.852 1.00 37.36  ? 246 THR C O     1 
ATOM   10010 C CB    . THR C 1 246 ? 60.538  10.302  -23.561 1.00 40.59  ? 246 THR C CB    1 
ATOM   10011 O OG1   . THR C 1 246 ? 61.898  10.243  -23.995 1.00 40.05  ? 246 THR C OG1   1 
ATOM   10012 C CG2   . THR C 1 246 ? 60.404  11.429  -22.568 1.00 40.82  ? 246 THR C CG2   1 
ATOM   10013 N N     . PHE C 1 247 ? 59.466  7.716   -24.990 1.00 43.15  ? 247 PHE C N     1 
ATOM   10014 C CA    . PHE C 1 247 ? 59.557  6.681   -26.010 1.00 46.77  ? 247 PHE C CA    1 
ATOM   10015 C C     . PHE C 1 247 ? 59.383  7.337   -27.380 1.00 45.39  ? 247 PHE C C     1 
ATOM   10016 O O     . PHE C 1 247 ? 58.537  8.221   -27.513 1.00 47.78  ? 247 PHE C O     1 
ATOM   10017 C CB    . PHE C 1 247 ? 58.523  5.590   -25.709 1.00 44.97  ? 247 PHE C CB    1 
ATOM   10018 C CG    . PHE C 1 247 ? 58.613  5.054   -24.303 1.00 44.76  ? 247 PHE C CG    1 
ATOM   10019 C CD1   . PHE C 1 247 ? 59.726  4.351   -23.877 1.00 45.27  ? 247 PHE C CD1   1 
ATOM   10020 C CD2   . PHE C 1 247 ? 57.609  5.302   -23.377 1.00 44.21  ? 247 PHE C CD2   1 
ATOM   10021 C CE1   . PHE C 1 247 ? 59.808  3.875   -22.571 1.00 45.36  ? 247 PHE C CE1   1 
ATOM   10022 C CE2   . PHE C 1 247 ? 57.712  4.844   -22.067 1.00 42.82  ? 247 PHE C CE2   1 
ATOM   10023 C CZ    . PHE C 1 247 ? 58.812  4.147   -21.662 1.00 40.35  ? 247 PHE C CZ    1 
ATOM   10024 N N     . GLU C 1 248 ? 60.224  6.938   -28.351 1.00 47.29  ? 248 GLU C N     1 
ATOM   10025 C CA    . GLU C 1 248 ? 60.378  7.598   -29.647 1.00 46.56  ? 248 GLU C CA    1 
ATOM   10026 C C     . GLU C 1 248 ? 59.190  7.300   -30.572 1.00 48.87  ? 248 GLU C C     1 
ATOM   10027 O O     . GLU C 1 248 ? 58.724  8.180   -31.299 1.00 43.42  ? 248 GLU C O     1 
ATOM   10028 C CB    . GLU C 1 248 ? 61.645  7.090   -30.348 1.00 57.76  ? 248 GLU C CB    1 
ATOM   10029 C CG    . GLU C 1 248 ? 62.429  8.148   -31.102 1.00 70.64  ? 248 GLU C CG    1 
ATOM   10030 C CD    . GLU C 1 248 ? 63.357  8.938   -30.187 1.00 90.47  ? 248 GLU C CD    1 
ATOM   10031 O OE1   . GLU C 1 248 ? 64.428  8.404   -29.833 1.00 101.61 ? 248 GLU C OE1   1 
ATOM   10032 O OE2   . GLU C 1 248 ? 62.989  10.063  -29.775 1.00 98.40  ? 248 GLU C OE2   1 
ATOM   10033 N N     . ASN C 1 249 ? 58.697  6.052   -30.561 1.00 43.57  ? 249 ASN C N     1 
ATOM   10034 C CA    . ASN C 1 249 ? 57.751  5.606   -31.573 1.00 44.83  ? 249 ASN C CA    1 
ATOM   10035 C C     . ASN C 1 249 ? 56.372  5.347   -30.980 1.00 45.34  ? 249 ASN C C     1 
ATOM   10036 O O     . ASN C 1 249 ? 56.237  4.917   -29.835 1.00 52.97  ? 249 ASN C O     1 
ATOM   10037 C CB    . ASN C 1 249 ? 58.281  4.359   -32.256 1.00 47.05  ? 249 ASN C CB    1 
ATOM   10038 C CG    . ASN C 1 249 ? 59.495  4.695   -33.096 1.00 59.70  ? 249 ASN C CG    1 
ATOM   10039 O OD1   . ASN C 1 249 ? 59.372  5.307   -34.157 1.00 68.77  ? 249 ASN C OD1   1 
ATOM   10040 N ND2   . ASN C 1 249 ? 60.669  4.316   -32.622 1.00 59.04  ? 249 ASN C ND2   1 
ATOM   10041 N N     . GLU C 1 250 ? 55.342  5.539   -31.798 1.00 45.16  ? 250 GLU C N     1 
ATOM   10042 C CA    . GLU C 1 250 ? 53.989  5.446   -31.283 1.00 51.74  ? 250 GLU C CA    1 
ATOM   10043 C C     . GLU C 1 250 ? 53.632  4.003   -30.925 1.00 50.57  ? 250 GLU C C     1 
ATOM   10044 O O     . GLU C 1 250 ? 52.892  3.792   -29.965 1.00 45.99  ? 250 GLU C O     1 
ATOM   10045 C CB    . GLU C 1 250 ? 52.986  6.135   -32.202 1.00 61.14  ? 250 GLU C CB    1 
ATOM   10046 C CG    . GLU C 1 250 ? 53.192  5.915   -33.675 1.00 80.48  ? 250 GLU C CG    1 
ATOM   10047 C CD    . GLU C 1 250 ? 52.069  6.570   -34.457 1.00 93.49  ? 250 GLU C CD    1 
ATOM   10048 O OE1   . GLU C 1 250 ? 51.815  7.773   -34.189 1.00 97.35  ? 250 GLU C OE1   1 
ATOM   10049 O OE2   . GLU C 1 250 ? 51.438  5.874   -35.296 1.00 77.04  ? 250 GLU C OE2   1 
ATOM   10050 N N     . ASP C 1 251 ? 54.243  3.019   -31.601 1.00 55.63  ? 251 ASP C N     1 
ATOM   10051 C CA    . ASP C 1 251 ? 53.988  1.601   -31.344 1.00 54.80  ? 251 ASP C CA    1 
ATOM   10052 C C     . ASP C 1 251 ? 54.654  1.117   -30.051 1.00 53.86  ? 251 ASP C C     1 
ATOM   10053 O O     . ASP C 1 251 ? 54.497  -0.050  -29.674 1.00 52.77  ? 251 ASP C O     1 
ATOM   10054 C CB    . ASP C 1 251 ? 54.485  0.724   -32.504 1.00 55.02  ? 251 ASP C CB    1 
ATOM   10055 C CG    . ASP C 1 251 ? 53.592  0.705   -33.743 1.00 67.02  ? 251 ASP C CG    1 
ATOM   10056 O OD1   . ASP C 1 251 ? 52.382  1.139   -33.685 1.00 55.87  ? 251 ASP C OD1   1 
ATOM   10057 O OD2   . ASP C 1 251 ? 54.103  0.238   -34.767 1.00 75.09  ? 251 ASP C OD2   1 
ATOM   10058 N N     . ASP C 1 252 ? 55.432  1.981   -29.379 1.00 47.35  ? 252 ASP C N     1 
ATOM   10059 C CA    . ASP C 1 252 ? 56.110  1.557   -28.168 1.00 45.05  ? 252 ASP C CA    1 
ATOM   10060 C C     . ASP C 1 252 ? 55.121  1.364   -27.014 1.00 39.37  ? 252 ASP C C     1 
ATOM   10061 O O     . ASP C 1 252 ? 55.419  0.705   -26.025 1.00 41.14  ? 252 ASP C O     1 
ATOM   10062 C CB    . ASP C 1 252 ? 57.210  2.545   -27.787 1.00 54.69  ? 252 ASP C CB    1 
ATOM   10063 C CG    . ASP C 1 252 ? 58.410  2.541   -28.716 1.00 53.29  ? 252 ASP C CG    1 
ATOM   10064 O OD1   . ASP C 1 252 ? 58.816  1.457   -29.177 1.00 45.76  ? 252 ASP C OD1   1 
ATOM   10065 O OD2   . ASP C 1 252 ? 58.953  3.627   -28.925 1.00 57.95  ? 252 ASP C OD2   1 
ATOM   10066 N N     . ILE C 1 253 ? 53.909  1.893   -27.131 1.00 41.29  ? 253 ILE C N     1 
ATOM   10067 C CA    . ILE C 1 253 ? 53.008  1.866   -26.000 1.00 41.39  ? 253 ILE C CA    1 
ATOM   10068 C C     . ILE C 1 253 ? 52.603  0.428   -25.709 1.00 41.18  ? 253 ILE C C     1 
ATOM   10069 O O     . ILE C 1 253 ? 52.318  0.091   -24.558 1.00 49.09  ? 253 ILE C O     1 
ATOM   10070 C CB    . ILE C 1 253 ? 51.828  2.833   -26.181 1.00 44.84  ? 253 ILE C CB    1 
ATOM   10071 C CG1   . ILE C 1 253 ? 50.993  2.944   -24.911 1.00 43.42  ? 253 ILE C CG1   1 
ATOM   10072 C CG2   . ILE C 1 253 ? 50.951  2.477   -27.365 1.00 47.88  ? 253 ILE C CG2   1 
ATOM   10073 C CD1   . ILE C 1 253 ? 51.755  3.409   -23.714 1.00 44.42  ? 253 ILE C CD1   1 
ATOM   10074 N N     . GLU C 1 254 ? 52.722  -0.454  -26.701 1.00 40.21  ? 254 GLU C N     1 
ATOM   10075 C CA    . GLU C 1 254 ? 52.416  -1.868  -26.486 1.00 37.51  ? 254 GLU C CA    1 
ATOM   10076 C C     . GLU C 1 254 ? 53.422  -2.536  -25.558 1.00 38.24  ? 254 GLU C C     1 
ATOM   10077 O O     . GLU C 1 254 ? 53.067  -3.006  -24.474 1.00 41.77  ? 254 GLU C O     1 
ATOM   10078 C CB    . GLU C 1 254 ? 52.323  -2.595  -27.814 1.00 41.90  ? 254 GLU C CB    1 
ATOM   10079 C CG    . GLU C 1 254 ? 52.140  -4.078  -27.635 1.00 50.24  ? 254 GLU C CG    1 
ATOM   10080 C CD    . GLU C 1 254 ? 51.855  -4.888  -28.880 1.00 44.63  ? 254 GLU C CD    1 
ATOM   10081 O OE1   . GLU C 1 254 ? 51.934  -4.322  -29.978 1.00 35.94  ? 254 GLU C OE1   1 
ATOM   10082 O OE2   . GLU C 1 254 ? 51.570  -6.094  -28.706 1.00 52.45  ? 254 GLU C OE2   1 
ATOM   10083 N N     . THR C 1 255 ? 54.704  -2.554  -25.932 1.00 38.87  ? 255 THR C N     1 
ATOM   10084 C CA    . THR C 1 255 ? 55.701  -3.134  -25.047 1.00 36.10  ? 255 THR C CA    1 
ATOM   10085 C C     . THR C 1 255 ? 55.735  -2.405  -23.686 1.00 37.00  ? 255 THR C C     1 
ATOM   10086 O O     . THR C 1 255 ? 56.018  -3.012  -22.648 1.00 41.38  ? 255 THR C O     1 
ATOM   10087 C CB    . THR C 1 255 ? 57.067  -3.180  -25.756 1.00 42.00  ? 255 THR C CB    1 
ATOM   10088 O OG1   . THR C 1 255 ? 57.984  -3.919  -24.944 1.00 40.36  ? 255 THR C OG1   1 
ATOM   10089 C CG2   . THR C 1 255 ? 57.663  -1.810  -26.017 1.00 44.31  ? 255 THR C CG2   1 
ATOM   10090 N N     . VAL C 1 256 ? 55.520  -1.084  -23.683 1.00 32.97  ? 256 VAL C N     1 
ATOM   10091 C CA    . VAL C 1 256 ? 55.628  -0.284  -22.471 1.00 35.46  ? 256 VAL C CA    1 
ATOM   10092 C C     . VAL C 1 256 ? 54.589  -0.729  -21.449 1.00 33.25  ? 256 VAL C C     1 
ATOM   10093 O O     . VAL C 1 256 ? 54.904  -0.890  -20.282 1.00 30.58  ? 256 VAL C O     1 
ATOM   10094 C CB    . VAL C 1 256 ? 55.449  1.227   -22.754 1.00 42.26  ? 256 VAL C CB    1 
ATOM   10095 C CG1   . VAL C 1 256 ? 55.082  1.995   -21.477 1.00 41.01  ? 256 VAL C CG1   1 
ATOM   10096 C CG2   . VAL C 1 256 ? 56.660  1.853   -23.441 1.00 37.65  ? 256 VAL C CG2   1 
ATOM   10097 N N     . THR C 1 257 ? 53.330  -0.863  -21.882 1.00 36.34  ? 257 THR C N     1 
ATOM   10098 C CA    . THR C 1 257 ? 52.277  -1.377  -21.028 1.00 34.72  ? 257 THR C CA    1 
ATOM   10099 C C     . THR C 1 257 ? 52.579  -2.785  -20.511 1.00 37.05  ? 257 THR C C     1 
ATOM   10100 O O     . THR C 1 257 ? 52.273  -3.058  -19.354 1.00 41.55  ? 257 THR C O     1 
ATOM   10101 C CB    . THR C 1 257 ? 50.931  -1.381  -21.747 1.00 38.45  ? 257 THR C CB    1 
ATOM   10102 O OG1   . THR C 1 257 ? 50.698  -0.041  -22.174 1.00 35.33  ? 257 THR C OG1   1 
ATOM   10103 C CG2   . THR C 1 257 ? 49.821  -1.875  -20.846 1.00 44.71  ? 257 THR C CG2   1 
ATOM   10104 N N     . GLU C 1 258 ? 53.141  -3.690  -21.333 1.00 35.93  ? 258 GLU C N     1 
ATOM   10105 C CA    . GLU C 1 258 ? 53.519  -5.018  -20.832 1.00 41.66  ? 258 GLU C CA    1 
ATOM   10106 C C     . GLU C 1 258 ? 54.550  -4.912  -19.707 1.00 40.22  ? 258 GLU C C     1 
ATOM   10107 O O     . GLU C 1 258 ? 54.500  -5.680  -18.762 1.00 42.17  ? 258 GLU C O     1 
ATOM   10108 C CB    . GLU C 1 258 ? 54.058  -5.959  -21.922 1.00 41.82  ? 258 GLU C CB    1 
ATOM   10109 C CG    . GLU C 1 258 ? 53.003  -6.389  -22.954 1.00 42.22  ? 258 GLU C CG    1 
ATOM   10110 C CD    . GLU C 1 258 ? 52.013  -7.435  -22.472 1.00 43.12  ? 258 GLU C CD    1 
ATOM   10111 O OE1   . GLU C 1 258 ? 52.493  -8.482  -22.022 1.00 39.17  ? 258 GLU C OE1   1 
ATOM   10112 O OE2   . GLU C 1 258 ? 50.760  -7.205  -22.553 1.00 40.32  ? 258 GLU C OE2   1 
ATOM   10113 N N     . ARG C 1 259 ? 55.488  -3.971  -19.791 1.00 38.44  ? 259 ARG C N     1 
ATOM   10114 C CA    . ARG C 1 259 ? 56.528  -3.852  -18.782 1.00 41.94  ? 259 ARG C CA    1 
ATOM   10115 C C     . ARG C 1 259 ? 55.996  -3.174  -17.519 1.00 45.00  ? 259 ARG C C     1 
ATOM   10116 O O     . ARG C 1 259 ? 56.539  -3.356  -16.429 1.00 49.23  ? 259 ARG C O     1 
ATOM   10117 C CB    . ARG C 1 259 ? 57.693  -3.068  -19.387 1.00 47.01  ? 259 ARG C CB    1 
ATOM   10118 C CG    . ARG C 1 259 ? 58.305  -3.772  -20.588 1.00 48.32  ? 259 ARG C CG    1 
ATOM   10119 C CD    . ARG C 1 259 ? 58.836  -2.835  -21.649 1.00 49.36  ? 259 ARG C CD    1 
ATOM   10120 N NE    . ARG C 1 259 ? 59.416  -3.545  -22.801 1.00 49.57  ? 259 ARG C NE    1 
ATOM   10121 C CZ    . ARG C 1 259 ? 60.730  -3.684  -23.021 1.00 46.05  ? 259 ARG C CZ    1 
ATOM   10122 N NH1   . ARG C 1 259 ? 61.601  -3.431  -22.065 1.00 39.10  ? 259 ARG C NH1   1 
ATOM   10123 N NH2   . ARG C 1 259 ? 61.191  -4.092  -24.190 1.00 46.07  ? 259 ARG C NH2   1 
ATOM   10124 N N     . LEU C 1 260 ? 54.948  -2.368  -17.668 1.00 38.40  ? 260 LEU C N     1 
ATOM   10125 C CA    . LEU C 1 260 ? 54.412  -1.648  -16.534 1.00 39.62  ? 260 LEU C CA    1 
ATOM   10126 C C     . LEU C 1 260 ? 53.614  -2.601  -15.652 1.00 41.46  ? 260 LEU C C     1 
ATOM   10127 O O     . LEU C 1 260 ? 53.562  -2.422  -14.432 1.00 39.21  ? 260 LEU C O     1 
ATOM   10128 C CB    . LEU C 1 260 ? 53.536  -0.494  -17.031 1.00 39.49  ? 260 LEU C CB    1 
ATOM   10129 C CG    . LEU C 1 260 ? 54.243  0.822   -17.368 1.00 39.80  ? 260 LEU C CG    1 
ATOM   10130 C CD1   . LEU C 1 260 ? 53.264  1.792   -18.017 1.00 39.29  ? 260 LEU C CD1   1 
ATOM   10131 C CD2   . LEU C 1 260 ? 54.888  1.462   -16.149 1.00 37.69  ? 260 LEU C CD2   1 
ATOM   10132 N N     . ARG C 1 261 ? 52.944  -3.565  -16.280 1.00 38.95  ? 261 ARG C N     1 
ATOM   10133 C CA    . ARG C 1 261 ? 52.049  -4.474  -15.573 1.00 41.36  ? 261 ARG C CA    1 
ATOM   10134 C C     . ARG C 1 261 ? 52.695  -5.046  -14.311 1.00 37.17  ? 261 ARG C C     1 
ATOM   10135 O O     . ARG C 1 261 ? 52.233  -4.787  -13.216 1.00 33.06  ? 261 ARG C O     1 
ATOM   10136 C CB    . ARG C 1 261 ? 51.602  -5.632  -16.470 1.00 42.44  ? 261 ARG C CB    1 
ATOM   10137 C CG    . ARG C 1 261 ? 50.703  -6.624  -15.751 1.00 41.06  ? 261 ARG C CG    1 
ATOM   10138 C CD    . ARG C 1 261 ? 50.157  -7.676  -16.679 1.00 36.04  ? 261 ARG C CD    1 
ATOM   10139 N NE    . ARG C 1 261 ? 51.262  -8.259  -17.407 1.00 38.55  ? 261 ARG C NE    1 
ATOM   10140 C CZ    . ARG C 1 261 ? 51.312  -8.341  -18.734 1.00 40.66  ? 261 ARG C CZ    1 
ATOM   10141 N NH1   . ARG C 1 261 ? 50.453  -7.664  -19.479 1.00 45.99  ? 261 ARG C NH1   1 
ATOM   10142 N NH2   . ARG C 1 261 ? 52.231  -9.083  -19.309 1.00 30.60  ? 261 ARG C NH2   1 
ATOM   10143 N N     . PRO C 1 262 ? 53.764  -5.866  -14.373 1.00 43.38  ? 262 PRO C N     1 
ATOM   10144 C CA    . PRO C 1 262 ? 54.377  -6.384  -13.144 1.00 39.68  ? 262 PRO C CA    1 
ATOM   10145 C C     . PRO C 1 262 ? 54.724  -5.295  -12.131 1.00 37.04  ? 262 PRO C C     1 
ATOM   10146 O O     . PRO C 1 262 ? 54.430  -5.413  -10.936 1.00 36.49  ? 262 PRO C O     1 
ATOM   10147 C CB    . PRO C 1 262 ? 55.641  -7.108  -13.605 1.00 39.30  ? 262 PRO C CB    1 
ATOM   10148 C CG    . PRO C 1 262 ? 55.812  -6.744  -15.070 1.00 37.72  ? 262 PRO C CG    1 
ATOM   10149 C CD    . PRO C 1 262 ? 54.437  -6.348  -15.587 1.00 37.77  ? 262 PRO C CD    1 
ATOM   10150 N N     . LEU C 1 263 ? 55.293  -4.192  -12.620 1.00 42.46  ? 263 LEU C N     1 
ATOM   10151 C CA    . LEU C 1 263 ? 55.755  -3.130  -11.730 1.00 40.65  ? 263 LEU C CA    1 
ATOM   10152 C C     . LEU C 1 263 ? 54.589  -2.590  -10.911 1.00 34.24  ? 263 LEU C C     1 
ATOM   10153 O O     . LEU C 1 263 ? 54.729  -2.321  -9.724  1.00 39.50  ? 263 LEU C O     1 
ATOM   10154 C CB    . LEU C 1 263 ? 56.430  -2.027  -12.548 1.00 44.08  ? 263 LEU C CB    1 
ATOM   10155 C CG    . LEU C 1 263 ? 57.720  -2.415  -13.286 1.00 48.82  ? 263 LEU C CG    1 
ATOM   10156 C CD1   . LEU C 1 263 ? 58.191  -1.244  -14.156 1.00 45.39  ? 263 LEU C CD1   1 
ATOM   10157 C CD2   . LEU C 1 263 ? 58.830  -2.841  -12.311 1.00 49.27  ? 263 LEU C CD2   1 
ATOM   10158 N N     . LYS C 1 264 ? 53.421  -2.473  -11.538 1.00 36.25  ? 264 LYS C N     1 
ATOM   10159 C CA    . LYS C 1 264 ? 52.247  -1.908  -10.899 1.00 33.64  ? 264 LYS C CA    1 
ATOM   10160 C C     . LYS C 1 264 ? 51.478  -2.917  -10.050 1.00 39.61  ? 264 LYS C C     1 
ATOM   10161 O O     . LYS C 1 264 ? 51.046  -2.547  -8.962  1.00 44.89  ? 264 LYS C O     1 
ATOM   10162 C CB    . LYS C 1 264 ? 51.355  -1.303  -11.967 1.00 40.87  ? 264 LYS C CB    1 
ATOM   10163 C CG    . LYS C 1 264 ? 51.771  0.110   -12.372 1.00 45.12  ? 264 LYS C CG    1 
ATOM   10164 C CD    . LYS C 1 264 ? 51.834  1.076   -11.227 1.00 47.67  ? 264 LYS C CD    1 
ATOM   10165 C CE    . LYS C 1 264 ? 50.546  1.164   -10.434 1.00 45.63  ? 264 LYS C CE    1 
ATOM   10166 N NZ    . LYS C 1 264 ? 50.724  1.984   -9.217  1.00 46.40  ? 264 LYS C NZ    1 
ATOM   10167 N N     . VAL C 1 265 ? 51.329  -4.179  -10.506 1.00 40.11  ? 265 VAL C N     1 
ATOM   10168 C CA    . VAL C 1 265 ? 50.632  -5.197  -9.728  1.00 35.22  ? 265 VAL C CA    1 
ATOM   10169 C C     . VAL C 1 265 ? 51.370  -5.372  -8.396  1.00 33.69  ? 265 VAL C C     1 
ATOM   10170 O O     . VAL C 1 265 ? 50.744  -5.459  -7.331  1.00 38.76  ? 265 VAL C O     1 
ATOM   10171 C CB    . VAL C 1 265 ? 50.458  -6.526  -10.506 1.00 38.89  ? 265 VAL C CB    1 
ATOM   10172 C CG1   . VAL C 1 265 ? 49.740  -7.600  -9.719  1.00 39.60  ? 265 VAL C CG1   1 
ATOM   10173 C CG2   . VAL C 1 265 ? 49.709  -6.347  -11.803 1.00 40.06  ? 265 VAL C CG2   1 
ATOM   10174 N N     . ALA C 1 266 ? 52.700  -5.371  -8.435  1.00 32.38  ? 266 ALA C N     1 
ATOM   10175 C CA    . ALA C 1 266 ? 53.494  -5.592  -7.233  1.00 33.71  ? 266 ALA C CA    1 
ATOM   10176 C C     . ALA C 1 266 ? 53.821  -4.302  -6.490  1.00 39.46  ? 266 ALA C C     1 
ATOM   10177 O O     . ALA C 1 266 ? 54.436  -4.373  -5.438  1.00 43.27  ? 266 ALA C O     1 
ATOM   10178 C CB    . ALA C 1 266 ? 54.770  -6.311  -7.565  1.00 34.89  ? 266 ALA C CB    1 
ATOM   10179 N N     . GLY C 1 267 ? 53.484  -3.128  -7.037  1.00 47.51  ? 267 GLY C N     1 
ATOM   10180 C CA    . GLY C 1 267 ? 53.632  -1.883  -6.293  1.00 41.50  ? 267 GLY C CA    1 
ATOM   10181 C C     . GLY C 1 267 ? 55.068  -1.372  -6.202  1.00 39.19  ? 267 GLY C C     1 
ATOM   10182 O O     . GLY C 1 267 ? 55.396  -0.620  -5.297  1.00 38.15  ? 267 GLY C O     1 
ATOM   10183 N N     . VAL C 1 268 ? 55.907  -1.732  -7.176  1.00 42.21  ? 268 VAL C N     1 
ATOM   10184 C CA    . VAL C 1 268 ? 57.261  -1.205  -7.298  1.00 41.56  ? 268 VAL C CA    1 
ATOM   10185 C C     . VAL C 1 268 ? 57.192  0.282   -7.670  1.00 45.78  ? 268 VAL C C     1 
ATOM   10186 O O     . VAL C 1 268 ? 58.028  1.088   -7.257  1.00 55.09  ? 268 VAL C O     1 
ATOM   10187 C CB    . VAL C 1 268 ? 58.029  -1.999  -8.371  1.00 38.42  ? 268 VAL C CB    1 
ATOM   10188 C CG1   . VAL C 1 268 ? 59.402  -1.401  -8.635  1.00 35.44  ? 268 VAL C CG1   1 
ATOM   10189 C CG2   . VAL C 1 268 ? 58.129  -3.485  -8.029  1.00 36.55  ? 268 VAL C CG2   1 
ATOM   10190 N N     . ILE C 1 269 ? 56.232  0.605   -8.549  1.00 47.53  ? 269 ILE C N     1 
ATOM   10191 C CA    . ILE C 1 269 ? 55.864  1.962   -8.905  1.00 41.50  ? 269 ILE C CA    1 
ATOM   10192 C C     . ILE C 1 269 ? 54.774  2.380   -7.936  1.00 41.15  ? 269 ILE C C     1 
ATOM   10193 O O     . ILE C 1 269 ? 53.683  1.833   -8.022  1.00 44.03  ? 269 ILE C O     1 
ATOM   10194 C CB    . ILE C 1 269 ? 55.351  2.027   -10.354 1.00 44.85  ? 269 ILE C CB    1 
ATOM   10195 C CG1   . ILE C 1 269 ? 56.449  1.738   -11.388 1.00 47.31  ? 269 ILE C CG1   1 
ATOM   10196 C CG2   . ILE C 1 269 ? 54.671  3.369   -10.581 1.00 48.24  ? 269 ILE C CG2   1 
ATOM   10197 C CD1   . ILE C 1 269 ? 55.952  1.520   -12.836 1.00 43.34  ? 269 ILE C CD1   1 
ATOM   10198 N N     . GLN C 1 270 ? 55.053  3.372   -7.081  1.00 47.53  ? 270 GLN C N     1 
ATOM   10199 C CA    . GLN C 1 270 ? 54.253  3.621   -5.887  1.00 50.11  ? 270 GLN C CA    1 
ATOM   10200 C C     . GLN C 1 270 ? 53.007  4.456   -6.180  1.00 48.17  ? 270 GLN C C     1 
ATOM   10201 O O     . GLN C 1 270 ? 52.085  4.459   -5.375  1.00 54.23  ? 270 GLN C O     1 
ATOM   10202 C CB    . GLN C 1 270 ? 55.103  4.314   -4.819  1.00 46.01  ? 270 GLN C CB    1 
ATOM   10203 C CG    . GLN C 1 270 ? 56.169  3.395   -4.258  1.00 50.64  ? 270 GLN C CG    1 
ATOM   10204 C CD    . GLN C 1 270 ? 57.463  4.102   -3.942  1.00 50.25  ? 270 GLN C CD    1 
ATOM   10205 O OE1   . GLN C 1 270 ? 58.202  4.512   -4.831  1.00 50.24  ? 270 GLN C OE1   1 
ATOM   10206 N NE2   . GLN C 1 270 ? 57.752  4.220   -2.661  1.00 49.47  ? 270 GLN C NE2   1 
ATOM   10207 N N     . ASN C 1 271 ? 53.003  5.215   -7.279  1.00 44.60  ? 271 ASN C N     1 
ATOM   10208 C CA    . ASN C 1 271 ? 51.854  6.029   -7.623  1.00 39.55  ? 271 ASN C CA    1 
ATOM   10209 C C     . ASN C 1 271 ? 51.237  5.494   -8.903  1.00 36.19  ? 271 ASN C C     1 
ATOM   10210 O O     . ASN C 1 271 ? 51.678  4.465   -9.402  1.00 38.58  ? 271 ASN C O     1 
ATOM   10211 C CB    . ASN C 1 271 ? 52.187  7.527   -7.711  1.00 43.53  ? 271 ASN C CB    1 
ATOM   10212 C CG    . ASN C 1 271 ? 53.339  7.892   -8.627  1.00 45.81  ? 271 ASN C CG    1 
ATOM   10213 O OD1   . ASN C 1 271 ? 54.130  7.031   -9.028  1.00 42.18  ? 271 ASN C OD1   1 
ATOM   10214 N ND2   . ASN C 1 271 ? 53.473  9.189   -8.901  1.00 44.50  ? 271 ASN C ND2   1 
ATOM   10215 N N     . GLY C 1 272 ? 50.158  6.159   -9.352  1.00 38.61  ? 272 GLY C N     1 
ATOM   10216 C CA    . GLY C 1 272 ? 49.556  5.931   -10.655 1.00 39.12  ? 272 GLY C CA    1 
ATOM   10217 C C     . GLY C 1 272 ? 50.644  6.049   -11.719 1.00 41.05  ? 272 GLY C C     1 
ATOM   10218 O O     . GLY C 1 272 ? 51.556  6.842   -11.545 1.00 44.96  ? 272 GLY C O     1 
ATOM   10219 N N     . ALA C 1 273 ? 50.610  5.180   -12.725 1.00 41.11  ? 273 ALA C N     1 
ATOM   10220 C CA    . ALA C 1 273 ? 51.529  5.260   -13.841 1.00 45.24  ? 273 ALA C CA    1 
ATOM   10221 C C     . ALA C 1 273 ? 50.776  5.976   -14.932 1.00 43.83  ? 273 ALA C C     1 
ATOM   10222 O O     . ALA C 1 273 ? 49.736  5.483   -15.340 1.00 51.10  ? 273 ALA C O     1 
ATOM   10223 C CB    . ALA C 1 273 ? 51.978  3.897   -14.323 1.00 45.21  ? 273 ALA C CB    1 
ATOM   10224 N N     . THR C 1 274 ? 51.303  7.118   -15.378 1.00 46.13  ? 274 THR C N     1 
ATOM   10225 C CA    . THR C 1 274 ? 50.642  7.926   -16.385 1.00 42.59  ? 274 THR C CA    1 
ATOM   10226 C C     . THR C 1 274 ? 51.566  8.018   -17.600 1.00 40.56  ? 274 THR C C     1 
ATOM   10227 O O     . THR C 1 274 ? 52.701  8.456   -17.480 1.00 43.84  ? 274 THR C O     1 
ATOM   10228 C CB    . THR C 1 274 ? 50.265  9.266   -15.742 1.00 50.84  ? 274 THR C CB    1 
ATOM   10229 O OG1   . THR C 1 274 ? 51.231  9.569   -14.726 1.00 65.45  ? 274 THR C OG1   1 
ATOM   10230 C CG2   . THR C 1 274 ? 48.916  9.246   -15.073 1.00 50.43  ? 274 THR C CG2   1 
ATOM   10231 N N     . VAL C 1 275 ? 51.073  7.634   -18.775 1.00 39.85  ? 275 VAL C N     1 
ATOM   10232 C CA    . VAL C 1 275 ? 51.877  7.615   -19.993 1.00 42.25  ? 275 VAL C CA    1 
ATOM   10233 C C     . VAL C 1 275 ? 51.163  8.445   -21.058 1.00 39.65  ? 275 VAL C C     1 
ATOM   10234 O O     . VAL C 1 275 ? 50.242  7.972   -21.712 1.00 42.29  ? 275 VAL C O     1 
ATOM   10235 C CB    . VAL C 1 275 ? 52.092  6.171   -20.481 1.00 41.31  ? 275 VAL C CB    1 
ATOM   10236 C CG1   . VAL C 1 275 ? 53.059  6.098   -21.643 1.00 43.30  ? 275 VAL C CG1   1 
ATOM   10237 C CG2   . VAL C 1 275 ? 52.550  5.274   -19.346 1.00 43.81  ? 275 VAL C CG2   1 
ATOM   10238 N N     . ARG C 1 276 ? 51.601  9.686   -21.251 1.00 35.24  ? 276 ARG C N     1 
ATOM   10239 C CA    . ARG C 1 276 ? 50.821  10.632  -22.029 1.00 35.66  ? 276 ARG C CA    1 
ATOM   10240 C C     . ARG C 1 276 ? 51.333  10.720  -23.470 1.00 39.86  ? 276 ARG C C     1 
ATOM   10241 O O     . ARG C 1 276 ? 52.537  10.671  -23.742 1.00 45.02  ? 276 ARG C O     1 
ATOM   10242 C CB    . ARG C 1 276 ? 50.872  11.990  -21.333 1.00 39.38  ? 276 ARG C CB    1 
ATOM   10243 C CG    . ARG C 1 276 ? 50.242  11.998  -19.947 1.00 41.77  ? 276 ARG C CG    1 
ATOM   10244 C CD    . ARG C 1 276 ? 50.223  13.404  -19.404 1.00 43.00  ? 276 ARG C CD    1 
ATOM   10245 N NE    . ARG C 1 276 ? 49.583  13.450  -18.111 1.00 43.47  ? 276 ARG C NE    1 
ATOM   10246 C CZ    . ARG C 1 276 ? 50.146  13.123  -16.951 1.00 50.77  ? 276 ARG C CZ    1 
ATOM   10247 N NH1   . ARG C 1 276 ? 51.431  12.807  -16.866 1.00 54.25  ? 276 ARG C NH1   1 
ATOM   10248 N NH2   . ARG C 1 276 ? 49.402  13.136  -15.854 1.00 56.62  ? 276 ARG C NH2   1 
ATOM   10249 N N     . SER C 1 277 ? 50.396  10.828  -24.406 1.00 37.64  ? 277 SER C N     1 
ATOM   10250 C CA    . SER C 1 277 ? 50.755  11.111  -25.777 1.00 40.15  ? 277 SER C CA    1 
ATOM   10251 C C     . SER C 1 277 ? 51.400  12.502  -25.869 1.00 44.57  ? 277 SER C C     1 
ATOM   10252 O O     . SER C 1 277 ? 51.280  13.317  -24.951 1.00 37.90  ? 277 SER C O     1 
ATOM   10253 C CB    . SER C 1 277 ? 49.548  10.987  -26.661 1.00 37.39  ? 277 SER C CB    1 
ATOM   10254 O OG    . SER C 1 277 ? 48.733  12.133  -26.560 1.00 35.21  ? 277 SER C OG    1 
ATOM   10255 N N     . LEU C 1 278 ? 52.066  12.736  -27.010 1.00 43.97  ? 278 LEU C N     1 
ATOM   10256 C CA    . LEU C 1 278 ? 52.863  13.919  -27.299 1.00 44.92  ? 278 LEU C CA    1 
ATOM   10257 C C     . LEU C 1 278 ? 52.081  15.205  -27.098 1.00 40.80  ? 278 LEU C C     1 
ATOM   10258 O O     . LEU C 1 278 ? 52.543  16.130  -26.462 1.00 44.83  ? 278 LEU C O     1 
ATOM   10259 C CB    . LEU C 1 278 ? 53.339  13.851  -28.759 1.00 45.00  ? 278 LEU C CB    1 
ATOM   10260 C CG    . LEU C 1 278 ? 54.188  15.026  -29.245 1.00 45.36  ? 278 LEU C CG    1 
ATOM   10261 C CD1   . LEU C 1 278 ? 55.381  15.257  -28.313 1.00 46.72  ? 278 LEU C CD1   1 
ATOM   10262 C CD2   . LEU C 1 278 ? 54.672  14.789  -30.667 1.00 43.90  ? 278 LEU C CD2   1 
ATOM   10263 N N     . VAL C 1 279 ? 50.929  15.310  -27.739 1.00 46.23  ? 279 VAL C N     1 
ATOM   10264 C CA    . VAL C 1 279 ? 50.234  16.573  -27.714 1.00 39.61  ? 279 VAL C CA    1 
ATOM   10265 C C     . VAL C 1 279 ? 49.821  16.870  -26.285 1.00 40.05  ? 279 VAL C C     1 
ATOM   10266 O O     . VAL C 1 279 ? 49.713  18.017  -25.888 1.00 48.50  ? 279 VAL C O     1 
ATOM   10267 C CB    . VAL C 1 279 ? 49.043  16.575  -28.677 1.00 42.46  ? 279 VAL C CB    1 
ATOM   10268 C CG1   . VAL C 1 279 ? 48.258  17.883  -28.605 1.00 45.41  ? 279 VAL C CG1   1 
ATOM   10269 C CG2   . VAL C 1 279 ? 49.526  16.317  -30.101 1.00 47.75  ? 279 VAL C CG2   1 
ATOM   10270 N N     . LEU C 1 280 ? 49.552  15.844  -25.502 1.00 45.20  ? 280 LEU C N     1 
ATOM   10271 C CA    . LEU C 1 280 ? 48.961  16.087  -24.200 1.00 44.15  ? 280 LEU C CA    1 
ATOM   10272 C C     . LEU C 1 280 ? 50.003  16.732  -23.299 1.00 37.74  ? 280 LEU C C     1 
ATOM   10273 O O     . LEU C 1 280 ? 49.668  17.640  -22.549 1.00 42.75  ? 280 LEU C O     1 
ATOM   10274 C CB    . LEU C 1 280 ? 48.435  14.771  -23.630 1.00 46.17  ? 280 LEU C CB    1 
ATOM   10275 C CG    . LEU C 1 280 ? 47.600  14.908  -22.366 1.00 47.28  ? 280 LEU C CG    1 
ATOM   10276 C CD1   . LEU C 1 280 ? 46.395  15.798  -22.601 1.00 43.60  ? 280 LEU C CD1   1 
ATOM   10277 C CD2   . LEU C 1 280 ? 47.175  13.534  -21.889 1.00 51.48  ? 280 LEU C CD2   1 
ATOM   10278 N N     . ASP C 1 281 ? 51.271  16.338  -23.481 1.00 41.21  ? 281 ASP C N     1 
ATOM   10279 C CA    . ASP C 1 281 ? 52.388  16.847  -22.686 1.00 46.34  ? 281 ASP C CA    1 
ATOM   10280 C C     . ASP C 1 281 ? 52.947  18.151  -23.294 1.00 53.87  ? 281 ASP C C     1 
ATOM   10281 O O     . ASP C 1 281 ? 53.345  19.073  -22.566 1.00 50.36  ? 281 ASP C O     1 
ATOM   10282 C CB    . ASP C 1 281 ? 53.410  15.718  -22.458 1.00 39.62  ? 281 ASP C CB    1 
ATOM   10283 C CG    . ASP C 1 281 ? 53.199  14.934  -21.162 1.00 46.09  ? 281 ASP C CG    1 
ATOM   10284 O OD1   . ASP C 1 281 ? 52.447  15.404  -20.281 1.00 56.99  ? 281 ASP C OD1   1 
ATOM   10285 O OD2   . ASP C 1 281 ? 53.764  13.842  -21.018 1.00 54.30  ? 281 ASP C OD2   1 
ATOM   10286 N N     . ALA C 1 282 ? 52.963  18.236  -24.637 1.00 50.79  ? 282 ALA C N     1 
ATOM   10287 C CA    . ALA C 1 282 ? 53.338  19.451  -25.345 1.00 47.91  ? 282 ALA C CA    1 
ATOM   10288 C C     . ALA C 1 282 ? 52.465  20.621  -24.901 1.00 44.12  ? 282 ALA C C     1 
ATOM   10289 O O     . ALA C 1 282 ? 52.984  21.667  -24.573 1.00 46.48  ? 282 ALA C O     1 
ATOM   10290 C CB    . ALA C 1 282 ? 53.272  19.247  -26.845 1.00 46.59  ? 282 ALA C CB    1 
ATOM   10291 N N     . ALA C 1 283 ? 51.147  20.422  -24.840 1.00 46.28  ? 283 ALA C N     1 
ATOM   10292 C CA    . ALA C 1 283 ? 50.195  21.472  -24.516 1.00 45.69  ? 283 ALA C CA    1 
ATOM   10293 C C     . ALA C 1 283 ? 50.391  22.098  -23.141 1.00 45.90  ? 283 ALA C C     1 
ATOM   10294 O O     . ALA C 1 283 ? 49.753  23.116  -22.870 1.00 51.19  ? 283 ALA C O     1 
ATOM   10295 C CB    . ALA C 1 283 ? 48.791  20.940  -24.584 1.00 49.09  ? 283 ALA C CB    1 
ATOM   10296 N N     . ILE C 1 284 ? 51.209  21.491  -22.270 1.00 49.55  ? 284 ILE C N     1 
ATOM   10297 C CA    . ILE C 1 284 ? 51.547  22.104  -20.990 1.00 48.87  ? 284 ILE C CA    1 
ATOM   10298 C C     . ILE C 1 284 ? 52.427  23.339  -21.220 1.00 49.36  ? 284 ILE C C     1 
ATOM   10299 O O     . ILE C 1 284 ? 52.398  24.263  -20.421 1.00 48.55  ? 284 ILE C O     1 
ATOM   10300 C CB    . ILE C 1 284 ? 52.202  21.082  -20.025 1.00 53.35  ? 284 ILE C CB    1 
ATOM   10301 C CG1   . ILE C 1 284 ? 51.224  19.985  -19.577 1.00 55.81  ? 284 ILE C CG1   1 
ATOM   10302 C CG2   . ILE C 1 284 ? 52.845  21.764  -18.822 1.00 47.99  ? 284 ILE C CG2   1 
ATOM   10303 C CD1   . ILE C 1 284 ? 50.072  20.464  -18.695 1.00 56.58  ? 284 ILE C CD1   1 
ATOM   10304 N N     . THR C 1 285 ? 53.245  23.350  -22.281 1.00 52.86  ? 285 THR C N     1 
ATOM   10305 C CA    . THR C 1 285 ? 54.169  24.449  -22.499 1.00 46.91  ? 285 THR C CA    1 
ATOM   10306 C C     . THR C 1 285 ? 54.018  25.078  -23.881 1.00 51.90  ? 285 THR C C     1 
ATOM   10307 O O     . THR C 1 285 ? 54.718  26.054  -24.146 1.00 58.59  ? 285 THR C O     1 
ATOM   10308 C CB    . THR C 1 285 ? 55.643  24.057  -22.296 1.00 43.93  ? 285 THR C CB    1 
ATOM   10309 O OG1   . THR C 1 285 ? 56.172  23.149  -23.273 1.00 35.59  ? 285 THR C OG1   1 
ATOM   10310 C CG2   . THR C 1 285 ? 55.866  23.514  -20.910 1.00 43.09  ? 285 THR C CG2   1 
ATOM   10311 N N     . ARG C 1 286 ? 53.156  24.544  -24.764 1.00 45.17  ? 286 ARG C N     1 
ATOM   10312 C CA    . ARG C 1 286 ? 53.049  25.096  -26.111 1.00 44.91  ? 286 ARG C CA    1 
ATOM   10313 C C     . ARG C 1 286 ? 51.599  25.018  -26.539 1.00 42.24  ? 286 ARG C C     1 
ATOM   10314 O O     . ARG C 1 286 ? 50.835  24.412  -25.830 1.00 50.24  ? 286 ARG C O     1 
ATOM   10315 C CB    . ARG C 1 286 ? 53.913  24.356  -27.137 1.00 40.80  ? 286 ARG C CB    1 
ATOM   10316 C CG    . ARG C 1 286 ? 55.400  24.295  -26.811 1.00 42.57  ? 286 ARG C CG    1 
ATOM   10317 C CD    . ARG C 1 286 ? 56.103  25.652  -26.892 1.00 41.27  ? 286 ARG C CD    1 
ATOM   10318 N NE    . ARG C 1 286 ? 57.558  25.547  -26.791 1.00 36.48  ? 286 ARG C NE    1 
ATOM   10319 C CZ    . ARG C 1 286 ? 58.258  25.702  -25.670 1.00 37.87  ? 286 ARG C CZ    1 
ATOM   10320 N NH1   . ARG C 1 286 ? 57.643  25.961  -24.526 1.00 33.29  ? 286 ARG C NH1   1 
ATOM   10321 N NH2   . ARG C 1 286 ? 59.572  25.530  -25.686 1.00 38.54  ? 286 ARG C NH2   1 
ATOM   10322 N N     . THR C 1 287 ? 51.262  25.619  -27.687 1.00 47.88  ? 287 THR C N     1 
ATOM   10323 C CA    . THR C 1 287 ? 49.935  25.575  -28.293 1.00 44.36  ? 287 THR C CA    1 
ATOM   10324 C C     . THR C 1 287 ? 50.100  25.207  -29.763 1.00 46.62  ? 287 THR C C     1 
ATOM   10325 O O     . THR C 1 287 ? 51.194  25.305  -30.323 1.00 44.18  ? 287 THR C O     1 
ATOM   10326 C CB    . THR C 1 287 ? 49.183  26.909  -28.157 1.00 51.50  ? 287 THR C CB    1 
ATOM   10327 O OG1   . THR C 1 287 ? 49.693  27.806  -29.137 1.00 58.28  ? 287 THR C OG1   1 
ATOM   10328 C CG2   . THR C 1 287 ? 49.301  27.566  -26.797 1.00 48.49  ? 287 THR C CG2   1 
ATOM   10329 N N     . LYS C 1 288 ? 49.003  24.761  -30.393 1.00 57.94  ? 288 LYS C N     1 
ATOM   10330 C CA    . LYS C 1 288 ? 49.056  24.165  -31.728 1.00 44.73  ? 288 LYS C CA    1 
ATOM   10331 C C     . LYS C 1 288 ? 49.611  25.154  -32.749 1.00 45.05  ? 288 LYS C C     1 
ATOM   10332 O O     . LYS C 1 288 ? 50.381  24.769  -33.620 1.00 49.44  ? 288 LYS C O     1 
ATOM   10333 C CB    . LYS C 1 288 ? 47.667  23.719  -32.193 1.00 45.30  ? 288 LYS C CB    1 
ATOM   10334 C CG    . LYS C 1 288 ? 47.620  23.248  -33.636 1.00 44.87  ? 288 LYS C CG    1 
ATOM   10335 C CD    . LYS C 1 288 ? 46.564  22.255  -33.945 1.00 49.30  ? 288 LYS C CD    1 
ATOM   10336 C CE    . LYS C 1 288 ? 45.341  22.831  -34.613 1.00 59.50  ? 288 LYS C CE    1 
ATOM   10337 N NZ    . LYS C 1 288 ? 44.843  21.928  -35.683 1.00 54.12  ? 288 LYS C NZ    1 
ATOM   10338 N N     . SER C 1 289 ? 49.220  26.431  -32.647 1.00 45.25  ? 289 SER C N     1 
ATOM   10339 C CA    . SER C 1 289 ? 49.506  27.367  -33.722 1.00 47.92  ? 289 SER C CA    1 
ATOM   10340 C C     . SER C 1 289 ? 50.993  27.761  -33.777 1.00 49.16  ? 289 SER C C     1 
ATOM   10341 O O     . SER C 1 289 ? 51.412  28.421  -34.732 1.00 53.62  ? 289 SER C O     1 
ATOM   10342 C CB    . SER C 1 289 ? 48.549  28.554  -33.688 1.00 45.15  ? 289 SER C CB    1 
ATOM   10343 O OG    . SER C 1 289 ? 48.567  29.253  -32.446 1.00 40.73  ? 289 SER C OG    1 
ATOM   10344 N N     . GLN C 1 290 ? 51.804  27.293  -32.812 1.00 45.16  ? 290 GLN C N     1 
ATOM   10345 C CA    . GLN C 1 290 ? 53.242  27.541  -32.791 1.00 46.35  ? 290 GLN C CA    1 
ATOM   10346 C C     . GLN C 1 290 ? 54.011  26.420  -33.477 1.00 46.82  ? 290 GLN C C     1 
ATOM   10347 O O     . GLN C 1 290 ? 55.233  26.449  -33.516 1.00 48.23  ? 290 GLN C O     1 
ATOM   10348 C CB    . GLN C 1 290 ? 53.720  27.635  -31.344 1.00 50.33  ? 290 GLN C CB    1 
ATOM   10349 C CG    . GLN C 1 290 ? 53.034  28.761  -30.582 1.00 52.47  ? 290 GLN C CG    1 
ATOM   10350 C CD    . GLN C 1 290 ? 53.235  28.724  -29.093 1.00 53.85  ? 290 GLN C CD    1 
ATOM   10351 O OE1   . GLN C 1 290 ? 52.876  29.662  -28.393 1.00 60.14  ? 290 GLN C OE1   1 
ATOM   10352 N NE2   . GLN C 1 290 ? 53.814  27.651  -28.587 1.00 61.50  ? 290 GLN C NE2   1 
ATOM   10353 N N     . TYR C 1 291 ? 53.297  25.391  -33.941 1.00 49.53  ? 291 TYR C N     1 
ATOM   10354 C CA    . TYR C 1 291 ? 53.915  24.307  -34.677 1.00 45.73  ? 291 TYR C CA    1 
ATOM   10355 C C     . TYR C 1 291 ? 53.162  24.034  -35.981 1.00 47.38  ? 291 TYR C C     1 
ATOM   10356 O O     . TYR C 1 291 ? 53.783  23.554  -36.930 1.00 51.76  ? 291 TYR C O     1 
ATOM   10357 C CB    . TYR C 1 291 ? 54.046  23.085  -33.776 1.00 44.98  ? 291 TYR C CB    1 
ATOM   10358 C CG    . TYR C 1 291 ? 55.144  23.168  -32.746 1.00 42.40  ? 291 TYR C CG    1 
ATOM   10359 C CD1   . TYR C 1 291 ? 56.449  22.849  -33.072 1.00 40.15  ? 291 TYR C CD1   1 
ATOM   10360 C CD2   . TYR C 1 291 ? 54.872  23.518  -31.430 1.00 43.70  ? 291 TYR C CD2   1 
ATOM   10361 C CE1   . TYR C 1 291 ? 57.465  22.909  -32.129 1.00 42.57  ? 291 TYR C CE1   1 
ATOM   10362 C CE2   . TYR C 1 291 ? 55.878  23.590  -30.477 1.00 40.04  ? 291 TYR C CE2   1 
ATOM   10363 C CZ    . TYR C 1 291 ? 57.184  23.291  -30.827 1.00 42.22  ? 291 TYR C CZ    1 
ATOM   10364 O OH    . TYR C 1 291 ? 58.207  23.375  -29.885 1.00 57.89  ? 291 TYR C OH    1 
ATOM   10365 N N     . TYR C 1 292 ? 51.870  24.395  -36.077 1.00 45.33  ? 292 TYR C N     1 
ATOM   10366 C CA    . TYR C 1 292 ? 51.121  24.041  -37.273 1.00 52.91  ? 292 TYR C CA    1 
ATOM   10367 C C     . TYR C 1 292 ? 49.985  25.018  -37.586 1.00 51.19  ? 292 TYR C C     1 
ATOM   10368 O O     . TYR C 1 292 ? 49.125  25.295  -36.758 1.00 48.97  ? 292 TYR C O     1 
ATOM   10369 C CB    . TYR C 1 292 ? 50.603  22.613  -37.130 1.00 55.29  ? 292 TYR C CB    1 
ATOM   10370 C CG    . TYR C 1 292 ? 49.886  22.083  -38.338 1.00 57.57  ? 292 TYR C CG    1 
ATOM   10371 C CD1   . TYR C 1 292 ? 50.571  21.897  -39.529 1.00 57.74  ? 292 TYR C CD1   1 
ATOM   10372 C CD2   . TYR C 1 292 ? 48.532  21.755  -38.293 1.00 61.33  ? 292 TYR C CD2   1 
ATOM   10373 C CE1   . TYR C 1 292 ? 49.934  21.402  -40.656 1.00 58.98  ? 292 TYR C CE1   1 
ATOM   10374 C CE2   . TYR C 1 292 ? 47.878  21.258  -39.414 1.00 62.20  ? 292 TYR C CE2   1 
ATOM   10375 C CZ    . TYR C 1 292 ? 48.588  21.076  -40.595 1.00 64.50  ? 292 TYR C CZ    1 
ATOM   10376 O OH    . TYR C 1 292 ? 48.022  20.582  -41.733 1.00 73.95  ? 292 TYR C OH    1 
ATOM   10377 N N     . ASP C 1 293 ? 49.955  25.449  -38.850 1.00 56.65  ? 293 ASP C N     1 
ATOM   10378 C CA    . ASP C 1 293 ? 49.063  26.491  -39.317 1.00 70.97  ? 293 ASP C CA    1 
ATOM   10379 C C     . ASP C 1 293 ? 47.661  25.941  -39.543 1.00 65.86  ? 293 ASP C C     1 
ATOM   10380 O O     . ASP C 1 293 ? 46.689  26.679  -39.430 1.00 66.21  ? 293 ASP C O     1 
ATOM   10381 C CB    . ASP C 1 293 ? 49.568  27.100  -40.634 1.00 89.72  ? 293 ASP C CB    1 
ATOM   10382 C CG    . ASP C 1 293 ? 50.146  28.507  -40.529 1.00 102.64 ? 293 ASP C CG    1 
ATOM   10383 O OD1   . ASP C 1 293 ? 50.155  29.075  -39.413 1.00 109.30 ? 293 ASP C OD1   1 
ATOM   10384 O OD2   . ASP C 1 293 ? 50.569  29.039  -41.576 1.00 107.96 ? 293 ASP C OD2   1 
ATOM   10385 N N     . GLY C 1 294 ? 47.576  24.671  -39.941 1.00 69.56  ? 294 GLY C N     1 
ATOM   10386 C CA    . GLY C 1 294 ? 46.345  24.097  -40.462 1.00 72.01  ? 294 GLY C CA    1 
ATOM   10387 C C     . GLY C 1 294 ? 45.257  23.920  -39.405 1.00 75.76  ? 294 GLY C C     1 
ATOM   10388 O O     . GLY C 1 294 ? 45.525  24.011  -38.201 1.00 67.29  ? 294 GLY C O     1 
ATOM   10389 N N     . ASP C 1 295 ? 44.040  23.642  -39.910 1.00 86.67  ? 295 ASP C N     1 
ATOM   10390 C CA    . ASP C 1 295 ? 42.806  23.533  -39.135 1.00 88.23  ? 295 ASP C CA    1 
ATOM   10391 C C     . ASP C 1 295 ? 42.667  22.170  -38.447 1.00 82.22  ? 295 ASP C C     1 
ATOM   10392 O O     . ASP C 1 295 ? 42.006  22.065  -37.409 1.00 76.75  ? 295 ASP C O     1 
ATOM   10393 C CB    . ASP C 1 295 ? 41.574  23.748  -40.029 1.00 98.49  ? 295 ASP C CB    1 
ATOM   10394 C CG    . ASP C 1 295 ? 41.011  25.160  -40.036 1.00 103.95 ? 295 ASP C CG    1 
ATOM   10395 O OD1   . ASP C 1 295 ? 41.660  26.047  -39.437 1.00 96.23  ? 295 ASP C OD1   1 
ATOM   10396 O OD2   . ASP C 1 295 ? 39.906  25.354  -40.618 1.00 93.24  ? 295 ASP C OD2   1 
ATOM   10397 N N     . GLY C 1 296 ? 43.261  21.120  -39.033 1.00 77.78  ? 296 GLY C N     1 
ATOM   10398 C CA    . GLY C 1 296 ? 43.099  19.771  -38.511 1.00 80.04  ? 296 GLY C CA    1 
ATOM   10399 C C     . GLY C 1 296 ? 44.347  19.202  -37.829 1.00 78.56  ? 296 GLY C C     1 
ATOM   10400 O O     . GLY C 1 296 ? 45.290  19.912  -37.493 1.00 86.57  ? 296 GLY C O     1 
ATOM   10401 N N     . PRO C 1 297 ? 44.385  17.871  -37.619 1.00 67.03  ? 297 PRO C N     1 
ATOM   10402 C CA    . PRO C 1 297 ? 45.451  17.224  -36.859 1.00 69.04  ? 297 PRO C CA    1 
ATOM   10403 C C     . PRO C 1 297 ? 46.858  17.634  -37.273 1.00 61.76  ? 297 PRO C C     1 
ATOM   10404 O O     . PRO C 1 297 ? 47.105  17.829  -38.457 1.00 58.00  ? 297 PRO C O     1 
ATOM   10405 C CB    . PRO C 1 297 ? 45.303  15.741  -37.240 1.00 76.52  ? 297 PRO C CB    1 
ATOM   10406 C CG    . PRO C 1 297 ? 43.866  15.566  -37.677 1.00 66.32  ? 297 PRO C CG    1 
ATOM   10407 C CD    . PRO C 1 297 ? 43.399  16.921  -38.145 1.00 65.99  ? 297 PRO C CD    1 
ATOM   10408 N N     . ILE C 1 298 ? 47.788  17.664  -36.310 1.00 59.84  ? 298 ILE C N     1 
ATOM   10409 C CA    . ILE C 1 298 ? 49.184  17.949  -36.619 1.00 53.72  ? 298 ILE C CA    1 
ATOM   10410 C C     . ILE C 1 298 ? 49.716  16.809  -37.474 1.00 51.08  ? 298 ILE C C     1 
ATOM   10411 O O     . ILE C 1 298 ? 49.488  15.644  -37.185 1.00 55.84  ? 298 ILE C O     1 
ATOM   10412 C CB    . ILE C 1 298 ? 50.096  18.181  -35.381 1.00 52.83  ? 298 ILE C CB    1 
ATOM   10413 C CG1   . ILE C 1 298 ? 50.212  16.966  -34.460 1.00 49.76  ? 298 ILE C CG1   1 
ATOM   10414 C CG2   . ILE C 1 298 ? 49.705  19.422  -34.581 1.00 48.20  ? 298 ILE C CG2   1 
ATOM   10415 C CD1   . ILE C 1 298 ? 51.482  16.986  -33.620 1.00 51.98  ? 298 ILE C CD1   1 
ATOM   10416 N N     . PRO C 1 299 ? 50.478  17.094  -38.541 1.00 54.00  ? 299 PRO C N     1 
ATOM   10417 C CA    . PRO C 1 299 ? 51.079  16.025  -39.322 1.00 56.49  ? 299 PRO C CA    1 
ATOM   10418 C C     . PRO C 1 299 ? 52.303  15.458  -38.617 1.00 53.20  ? 299 PRO C C     1 
ATOM   10419 O O     . PRO C 1 299 ? 52.842  16.072  -37.707 1.00 49.38  ? 299 PRO C O     1 
ATOM   10420 C CB    . PRO C 1 299 ? 51.413  16.663  -40.681 1.00 53.88  ? 299 PRO C CB    1 
ATOM   10421 C CG    . PRO C 1 299 ? 51.384  18.168  -40.446 1.00 54.68  ? 299 PRO C CG    1 
ATOM   10422 C CD    . PRO C 1 299 ? 50.766  18.424  -39.083 1.00 56.06  ? 299 PRO C CD    1 
ATOM   10423 N N     . PRO C 1 300 ? 52.732  14.243  -39.020 1.00 61.68  ? 300 PRO C N     1 
ATOM   10424 C CA    . PRO C 1 300 ? 53.926  13.605  -38.480 1.00 61.81  ? 300 PRO C CA    1 
ATOM   10425 C C     . PRO C 1 300 ? 55.173  14.470  -38.407 1.00 59.12  ? 300 PRO C C     1 
ATOM   10426 O O     . PRO C 1 300 ? 55.972  14.299  -37.493 1.00 64.89  ? 300 PRO C O     1 
ATOM   10427 C CB    . PRO C 1 300 ? 54.206  12.477  -39.489 1.00 60.43  ? 300 PRO C CB    1 
ATOM   10428 C CG    . PRO C 1 300 ? 52.812  12.077  -39.941 1.00 68.10  ? 300 PRO C CG    1 
ATOM   10429 C CD    . PRO C 1 300 ? 52.030  13.374  -39.981 1.00 62.59  ? 300 PRO C CD    1 
ATOM   10430 N N     . SER C 1 301 ? 55.397  15.318  -39.413 1.00 52.74  ? 301 SER C N     1 
ATOM   10431 C CA    . SER C 1 301 ? 56.663  16.042  -39.486 1.00 54.08  ? 301 SER C CA    1 
ATOM   10432 C C     . SER C 1 301 ? 56.696  17.117  -38.398 1.00 52.08  ? 301 SER C C     1 
ATOM   10433 O O     . SER C 1 301 ? 57.780  17.485  -37.924 1.00 42.37  ? 301 SER C O     1 
ATOM   10434 C CB    . SER C 1 301 ? 56.901  16.638  -40.850 1.00 47.93  ? 301 SER C CB    1 
ATOM   10435 O OG    . SER C 1 301 ? 55.796  17.466  -41.200 1.00 51.72  ? 301 SER C OG    1 
ATOM   10436 N N     . VAL C 1 302 ? 55.494  17.603  -38.024 1.00 44.70  ? 302 VAL C N     1 
ATOM   10437 C CA    . VAL C 1 302 ? 55.349  18.554  -36.940 1.00 52.84  ? 302 VAL C CA    1 
ATOM   10438 C C     . VAL C 1 302 ? 55.630  17.859  -35.607 1.00 56.36  ? 302 VAL C C     1 
ATOM   10439 O O     . VAL C 1 302 ? 56.316  18.419  -34.745 1.00 55.39  ? 302 VAL C O     1 
ATOM   10440 C CB    . VAL C 1 302 ? 53.972  19.235  -36.982 1.00 60.34  ? 302 VAL C CB    1 
ATOM   10441 C CG1   . VAL C 1 302 ? 53.667  19.996  -35.700 1.00 58.27  ? 302 VAL C CG1   1 
ATOM   10442 C CG2   . VAL C 1 302 ? 53.878  20.158  -38.188 1.00 54.19  ? 302 VAL C CG2   1 
ATOM   10443 N N     . ALA C 1 303 ? 55.159  16.615  -35.469 1.00 56.90  ? 303 ALA C N     1 
ATOM   10444 C CA    . ALA C 1 303 ? 55.438  15.820  -34.283 1.00 55.74  ? 303 ALA C CA    1 
ATOM   10445 C C     . ALA C 1 303 ? 56.941  15.709  -34.009 1.00 46.12  ? 303 ALA C C     1 
ATOM   10446 O O     . ALA C 1 303 ? 57.358  15.960  -32.872 1.00 41.66  ? 303 ALA C O     1 
ATOM   10447 C CB    . ALA C 1 303 ? 54.774  14.466  -34.400 1.00 64.18  ? 303 ALA C CB    1 
ATOM   10448 N N     . LYS C 1 304 ? 57.747  15.369  -35.031 1.00 48.56  ? 304 LYS C N     1 
ATOM   10449 C CA    . LYS C 1 304 ? 59.184  15.139  -34.851 1.00 55.07  ? 304 LYS C CA    1 
ATOM   10450 C C     . LYS C 1 304 ? 59.840  16.391  -34.274 1.00 57.50  ? 304 LYS C C     1 
ATOM   10451 O O     . LYS C 1 304 ? 60.727  16.308  -33.427 1.00 63.13  ? 304 LYS C O     1 
ATOM   10452 C CB    . LYS C 1 304 ? 59.983  14.846  -36.132 1.00 65.67  ? 304 LYS C CB    1 
ATOM   10453 C CG    . LYS C 1 304 ? 59.354  13.964  -37.205 1.00 92.19  ? 304 LYS C CG    1 
ATOM   10454 C CD    . LYS C 1 304 ? 58.867  12.586  -36.753 1.00 106.71 ? 304 LYS C CD    1 
ATOM   10455 C CE    . LYS C 1 304 ? 58.138  11.837  -37.855 1.00 106.42 ? 304 LYS C CE    1 
ATOM   10456 N NZ    . LYS C 1 304 ? 57.236  10.800  -37.304 1.00 109.12 ? 304 LYS C NZ    1 
ATOM   10457 N N     . THR C 1 305 ? 59.408  17.550  -34.782 1.00 57.59  ? 305 THR C N     1 
ATOM   10458 C CA    . THR C 1 305 ? 59.944  18.851  -34.407 1.00 51.29  ? 305 THR C CA    1 
ATOM   10459 C C     . THR C 1 305 ? 59.599  19.141  -32.942 1.00 46.33  ? 305 THR C C     1 
ATOM   10460 O O     . THR C 1 305 ? 60.475  19.433  -32.125 1.00 40.80  ? 305 THR C O     1 
ATOM   10461 C CB    . THR C 1 305 ? 59.470  19.847  -35.477 1.00 55.75  ? 305 THR C CB    1 
ATOM   10462 O OG1   . THR C 1 305 ? 60.381  19.722  -36.580 1.00 63.03  ? 305 THR C OG1   1 
ATOM   10463 C CG2   . THR C 1 305 ? 59.395  21.279  -34.996 1.00 57.51  ? 305 THR C CG2   1 
ATOM   10464 N N     . MET C 1 306 ? 58.303  19.009  -32.618 1.00 47.05  ? 306 MET C N     1 
ATOM   10465 C CA    . MET C 1 306 ? 57.795  19.125  -31.268 1.00 42.69  ? 306 MET C CA    1 
ATOM   10466 C C     . MET C 1 306 ? 58.626  18.254  -30.329 1.00 42.21  ? 306 MET C C     1 
ATOM   10467 O O     . MET C 1 306 ? 58.980  18.682  -29.241 1.00 42.22  ? 306 MET C O     1 
ATOM   10468 C CB    . MET C 1 306 ? 56.341  18.655  -31.221 1.00 47.13  ? 306 MET C CB    1 
ATOM   10469 C CG    . MET C 1 306 ? 55.355  19.683  -31.678 1.00 48.80  ? 306 MET C CG    1 
ATOM   10470 S SD    . MET C 1 306 ? 53.685  19.055  -31.571 1.00 52.95  ? 306 MET C SD    1 
ATOM   10471 C CE    . MET C 1 306 ? 53.361  19.376  -29.843 1.00 65.26  ? 306 MET C CE    1 
ATOM   10472 N N     . MET C 1 307 ? 58.943  17.035  -30.770 1.00 42.90  ? 307 MET C N     1 
ATOM   10473 C CA    . MET C 1 307 ? 59.671  16.073  -29.967 1.00 43.76  ? 307 MET C CA    1 
ATOM   10474 C C     . MET C 1 307 ? 61.112  16.515  -29.709 1.00 48.82  ? 307 MET C C     1 
ATOM   10475 O O     . MET C 1 307 ? 61.602  16.356  -28.586 1.00 50.38  ? 307 MET C O     1 
ATOM   10476 C CB    . MET C 1 307 ? 59.693  14.714  -30.671 1.00 47.66  ? 307 MET C CB    1 
ATOM   10477 C CG    . MET C 1 307 ? 58.421  13.886  -30.505 1.00 49.00  ? 307 MET C CG    1 
ATOM   10478 S SD    . MET C 1 307 ? 58.440  12.382  -31.546 1.00 52.15  ? 307 MET C SD    1 
ATOM   10479 C CE    . MET C 1 307 ? 60.025  11.663  -31.127 1.00 54.19  ? 307 MET C CE    1 
ATOM   10480 N N     . ALA C 1 308 ? 61.794  17.033  -30.748 1.00 53.34  ? 308 ALA C N     1 
ATOM   10481 C CA    . ALA C 1 308 ? 63.190  17.464  -30.651 1.00 53.44  ? 308 ALA C CA    1 
ATOM   10482 C C     . ALA C 1 308 ? 63.304  18.765  -29.864 1.00 44.75  ? 308 ALA C C     1 
ATOM   10483 O O     . ALA C 1 308 ? 64.223  18.923  -29.066 1.00 41.80  ? 308 ALA C O     1 
ATOM   10484 C CB    . ALA C 1 308 ? 63.832  17.629  -32.014 1.00 52.61  ? 308 ALA C CB    1 
ATOM   10485 N N     . ASP C 1 309 ? 62.382  19.696  -30.082 1.00 40.30  ? 309 ASP C N     1 
ATOM   10486 C CA    . ASP C 1 309 ? 62.384  20.903  -29.276 1.00 43.86  ? 309 ASP C CA    1 
ATOM   10487 C C     . ASP C 1 309 ? 62.208  20.561  -27.799 1.00 45.44  ? 309 ASP C C     1 
ATOM   10488 O O     . ASP C 1 309 ? 63.003  20.969  -26.957 1.00 48.88  ? 309 ASP C O     1 
ATOM   10489 C CB    . ASP C 1 309 ? 61.235  21.845  -29.632 1.00 47.91  ? 309 ASP C CB    1 
ATOM   10490 C CG    . ASP C 1 309 ? 61.346  22.564  -30.956 1.00 47.97  ? 309 ASP C CG    1 
ATOM   10491 O OD1   . ASP C 1 309 ? 62.317  22.282  -31.741 1.00 49.42  ? 309 ASP C OD1   1 
ATOM   10492 O OD2   . ASP C 1 309 ? 60.490  23.443  -31.153 1.00 49.35  ? 309 ASP C OD2   1 
ATOM   10493 N N     . LEU C 1 310 ? 61.123  19.849  -27.481 1.00 44.10  ? 310 LEU C N     1 
ATOM   10494 C CA    . LEU C 1 310 ? 60.668  19.771  -26.105 1.00 43.41  ? 310 LEU C CA    1 
ATOM   10495 C C     . LEU C 1 310 ? 61.309  18.615  -25.338 1.00 38.20  ? 310 LEU C C     1 
ATOM   10496 O O     . LEU C 1 310 ? 61.029  18.480  -24.154 1.00 44.95  ? 310 LEU C O     1 
ATOM   10497 C CB    . LEU C 1 310 ? 59.147  19.634  -26.089 1.00 40.54  ? 310 LEU C CB    1 
ATOM   10498 C CG    . LEU C 1 310 ? 58.372  20.752  -26.766 1.00 43.16  ? 310 LEU C CG    1 
ATOM   10499 C CD1   . LEU C 1 310 ? 56.867  20.479  -26.691 1.00 41.45  ? 310 LEU C CD1   1 
ATOM   10500 C CD2   . LEU C 1 310 ? 58.716  22.101  -26.137 1.00 45.15  ? 310 LEU C CD2   1 
ATOM   10501 N N     . ASP C 1 311 ? 62.179  17.809  -25.963 1.00 46.16  ? 311 ASP C N     1 
ATOM   10502 C CA    . ASP C 1 311 ? 62.679  16.583  -25.330 1.00 50.51  ? 311 ASP C CA    1 
ATOM   10503 C C     . ASP C 1 311 ? 61.524  15.767  -24.738 1.00 43.77  ? 311 ASP C C     1 
ATOM   10504 O O     . ASP C 1 311 ? 61.484  15.538  -23.540 1.00 44.77  ? 311 ASP C O     1 
ATOM   10505 C CB    . ASP C 1 311 ? 63.727  16.910  -24.257 1.00 49.34  ? 311 ASP C CB    1 
ATOM   10506 C CG    . ASP C 1 311 ? 65.052  17.361  -24.847 1.00 51.44  ? 311 ASP C CG    1 
ATOM   10507 O OD1   . ASP C 1 311 ? 65.081  17.590  -26.073 1.00 45.53  ? 311 ASP C OD1   1 
ATOM   10508 O OD2   . ASP C 1 311 ? 66.057  17.399  -24.096 1.00 50.63  ? 311 ASP C OD2   1 
ATOM   10509 N N     . LEU C 1 312 ? 60.530  15.469  -25.581 1.00 43.30  ? 312 LEU C N     1 
ATOM   10510 C CA    . LEU C 1 312 ? 59.430  14.564  -25.305 1.00 41.36  ? 312 LEU C CA    1 
ATOM   10511 C C     . LEU C 1 312 ? 59.479  13.467  -26.353 1.00 40.96  ? 312 LEU C C     1 
ATOM   10512 O O     . LEU C 1 312 ? 59.960  13.685  -27.453 1.00 40.15  ? 312 LEU C O     1 
ATOM   10513 C CB    . LEU C 1 312 ? 58.085  15.285  -25.409 1.00 44.78  ? 312 LEU C CB    1 
ATOM   10514 C CG    . LEU C 1 312 ? 57.892  16.473  -24.473 1.00 47.74  ? 312 LEU C CG    1 
ATOM   10515 C CD1   . LEU C 1 312 ? 56.571  17.172  -24.758 1.00 47.47  ? 312 LEU C CD1   1 
ATOM   10516 C CD2   . LEU C 1 312 ? 57.976  16.039  -23.014 1.00 47.18  ? 312 LEU C CD2   1 
ATOM   10517 N N     . GLY C 1 313 ? 59.004  12.282  -25.976 1.00 45.40  ? 313 GLY C N     1 
ATOM   10518 C CA    . GLY C 1 313 ? 58.741  11.211  -26.924 1.00 44.22  ? 313 GLY C CA    1 
ATOM   10519 C C     . GLY C 1 313 ? 57.287  11.241  -27.387 1.00 40.80  ? 313 GLY C C     1 
ATOM   10520 O O     . GLY C 1 313 ? 56.538  12.168  -27.046 1.00 43.50  ? 313 GLY C O     1 
ATOM   10521 N N     . MET C 1 314 ? 56.909  10.213  -28.154 1.00 37.89  ? 314 MET C N     1 
ATOM   10522 C CA    . MET C 1 314 ? 55.557  10.089  -28.677 1.00 41.09  ? 314 MET C CA    1 
ATOM   10523 C C     . MET C 1 314 ? 54.641  9.632   -27.546 1.00 42.59  ? 314 MET C C     1 
ATOM   10524 O O     . MET C 1 314 ? 53.429  9.832   -27.595 1.00 42.26  ? 314 MET C O     1 
ATOM   10525 C CB    . MET C 1 314 ? 55.487  9.065   -29.803 1.00 42.09  ? 314 MET C CB    1 
ATOM   10526 C CG    . MET C 1 314 ? 56.027  9.557   -31.119 1.00 49.19  ? 314 MET C CG    1 
ATOM   10527 S SD    . MET C 1 314 ? 55.082  10.889  -31.869 1.00 55.78  ? 314 MET C SD    1 
ATOM   10528 C CE    . MET C 1 314 ? 53.441  10.183  -32.029 1.00 58.86  ? 314 MET C CE    1 
ATOM   10529 N N     . TRP C 1 315 ? 55.265  8.992   -26.557 1.00 37.58  ? 315 TRP C N     1 
ATOM   10530 C CA    . TRP C 1 315 ? 54.646  8.646   -25.303 1.00 44.06  ? 315 TRP C CA    1 
ATOM   10531 C C     . TRP C 1 315 ? 55.576  9.090   -24.180 1.00 43.22  ? 315 TRP C C     1 
ATOM   10532 O O     . TRP C 1 315 ? 56.785  8.896   -24.290 1.00 38.14  ? 315 TRP C O     1 
ATOM   10533 C CB    . TRP C 1 315 ? 54.405  7.121   -25.227 1.00 48.86  ? 315 TRP C CB    1 
ATOM   10534 C CG    . TRP C 1 315 ? 53.404  6.628   -26.214 1.00 39.02  ? 315 TRP C CG    1 
ATOM   10535 C CD1   . TRP C 1 315 ? 53.667  5.971   -27.368 1.00 36.45  ? 315 TRP C CD1   1 
ATOM   10536 C CD2   . TRP C 1 315 ? 51.981  6.796   -26.152 1.00 32.05  ? 315 TRP C CD2   1 
ATOM   10537 N NE1   . TRP C 1 315 ? 52.502  5.732   -28.033 1.00 36.41  ? 315 TRP C NE1   1 
ATOM   10538 C CE2   . TRP C 1 315 ? 51.450  6.205   -27.302 1.00 31.31  ? 315 TRP C CE2   1 
ATOM   10539 C CE3   . TRP C 1 315 ? 51.108  7.386   -25.240 1.00 31.64  ? 315 TRP C CE3   1 
ATOM   10540 C CZ2   . TRP C 1 315 ? 50.085  6.171   -27.570 1.00 30.84  ? 315 TRP C CZ2   1 
ATOM   10541 C CZ3   . TRP C 1 315 ? 49.758  7.344   -25.495 1.00 33.69  ? 315 TRP C CZ3   1 
ATOM   10542 C CH2   . TRP C 1 315 ? 49.250  6.734   -26.641 1.00 30.99  ? 315 TRP C CH2   1 
ATOM   10543 N N     . ASN C 1 316 ? 54.982  9.551   -23.066 1.00 42.81  ? 316 ASN C N     1 
ATOM   10544 C CA    . ASN C 1 316 ? 55.728  10.153  -21.978 1.00 40.45  ? 316 ASN C CA    1 
ATOM   10545 C C     . ASN C 1 316 ? 55.211  9.627   -20.640 1.00 39.04  ? 316 ASN C C     1 
ATOM   10546 O O     . ASN C 1 316 ? 54.100  9.939   -20.227 1.00 45.18  ? 316 ASN C O     1 
ATOM   10547 C CB    . ASN C 1 316 ? 55.648  11.674  -22.138 1.00 41.03  ? 316 ASN C CB    1 
ATOM   10548 C CG    . ASN C 1 316 ? 56.148  12.086  -23.503 1.00 39.78  ? 316 ASN C CG    1 
ATOM   10549 O OD1   . ASN C 1 316 ? 57.352  12.200  -23.729 1.00 39.16  ? 316 ASN C OD1   1 
ATOM   10550 N ND2   . ASN C 1 316 ? 55.232  12.227  -24.440 1.00 42.82  ? 316 ASN C ND2   1 
ATOM   10551 N N     . PHE C 1 317 ? 56.051  8.848   -19.960 1.00 40.89  ? 317 PHE C N     1 
ATOM   10552 C CA    . PHE C 1 317 ? 55.707  8.211   -18.697 1.00 42.55  ? 317 PHE C CA    1 
ATOM   10553 C C     . PHE C 1 317 ? 56.307  9.036   -17.569 1.00 41.51  ? 317 PHE C C     1 
ATOM   10554 O O     . PHE C 1 317 ? 57.553  9.135   -17.473 1.00 36.95  ? 317 PHE C O     1 
ATOM   10555 C CB    . PHE C 1 317 ? 56.181  6.743   -18.686 1.00 44.20  ? 317 PHE C CB    1 
ATOM   10556 C CG    . PHE C 1 317 ? 56.232  6.049   -17.347 1.00 40.85  ? 317 PHE C CG    1 
ATOM   10557 C CD1   . PHE C 1 317 ? 55.252  6.240   -16.384 1.00 41.81  ? 317 PHE C CD1   1 
ATOM   10558 C CD2   . PHE C 1 317 ? 57.268  5.170   -17.046 1.00 46.01  ? 317 PHE C CD2   1 
ATOM   10559 C CE1   . PHE C 1 317 ? 55.333  5.611   -15.145 1.00 38.75  ? 317 PHE C CE1   1 
ATOM   10560 C CE2   . PHE C 1 317 ? 57.338  4.535   -15.808 1.00 43.77  ? 317 PHE C CE2   1 
ATOM   10561 C CZ    . PHE C 1 317 ? 56.372  4.759   -14.857 1.00 35.28  ? 317 PHE C CZ    1 
ATOM   10562 N N     . CYS C 1 318 ? 55.383  9.655   -16.797 1.00 36.37  ? 318 CYS C N     1 
ATOM   10563 C CA    . CYS C 1 318 ? 55.679  10.265  -15.506 1.00 43.96  ? 318 CYS C CA    1 
ATOM   10564 C C     . CYS C 1 318 ? 55.274  9.391   -14.320 1.00 44.17  ? 318 CYS C C     1 
ATOM   10565 O O     . CYS C 1 318 ? 54.122  8.962   -14.170 1.00 41.19  ? 318 CYS C O     1 
ATOM   10566 C CB    . CYS C 1 318 ? 54.964  11.592  -15.301 1.00 46.86  ? 318 CYS C CB    1 
ATOM   10567 S SG    . CYS C 1 318 ? 55.705  12.907  -16.286 1.00 47.97  ? 318 CYS C SG    1 
ATOM   10568 N N     . GLY C 1 319 ? 56.247  9.221   -13.425 1.00 50.29  ? 319 GLY C N     1 
ATOM   10569 C CA    . GLY C 1 319 ? 55.989  8.706   -12.095 1.00 45.90  ? 319 GLY C CA    1 
ATOM   10570 C C     . GLY C 1 319 ? 56.974  9.297   -11.107 1.00 47.26  ? 319 GLY C C     1 
ATOM   10571 O O     . GLY C 1 319 ? 57.626  10.291  -11.411 1.00 52.45  ? 319 GLY C O     1 
ATOM   10572 N N     . ALA C 1 320 ? 57.032  8.693   -9.915  1.00 47.29  ? 320 ALA C N     1 
ATOM   10573 C CA    . ALA C 1 320 ? 57.772  9.267   -8.809  1.00 43.13  ? 320 ALA C CA    1 
ATOM   10574 C C     . ALA C 1 320 ? 58.035  8.196   -7.771  1.00 41.86  ? 320 ALA C C     1 
ATOM   10575 O O     . ALA C 1 320 ? 57.175  7.367   -7.513  1.00 41.52  ? 320 ALA C O     1 
ATOM   10576 C CB    . ALA C 1 320 ? 57.029  10.408  -8.199  1.00 41.29  ? 320 ALA C CB    1 
ATOM   10577 N N     . LEU C 1 321 ? 59.260  8.252   -7.248  1.00 39.35  ? 321 LEU C N     1 
ATOM   10578 C CA    . LEU C 1 321 ? 59.762  7.391   -6.205  1.00 41.24  ? 321 LEU C CA    1 
ATOM   10579 C C     . LEU C 1 321 ? 59.575  8.123   -4.892  1.00 38.93  ? 321 LEU C C     1 
ATOM   10580 O O     . LEU C 1 321 ? 59.675  9.345   -4.840  1.00 40.61  ? 321 LEU C O     1 
ATOM   10581 C CB    . LEU C 1 321 ? 61.239  7.125   -6.468  1.00 44.65  ? 321 LEU C CB    1 
ATOM   10582 C CG    . LEU C 1 321 ? 61.568  6.671   -7.885  1.00 44.56  ? 321 LEU C CG    1 
ATOM   10583 C CD1   . LEU C 1 321 ? 63.049  6.860   -8.157  1.00 47.90  ? 321 LEU C CD1   1 
ATOM   10584 C CD2   . LEU C 1 321 ? 61.189  5.212   -8.069  1.00 47.44  ? 321 LEU C CD2   1 
ATOM   10585 N N     . TYR C 1 322 ? 59.221  7.362   -3.864  1.00 38.07  ? 322 TYR C N     1 
ATOM   10586 C CA    . TYR C 1 322 ? 58.945  7.931   -2.553  1.00 37.64  ? 322 TYR C CA    1 
ATOM   10587 C C     . TYR C 1 322 ? 59.643  7.096   -1.481  1.00 36.79  ? 322 TYR C C     1 
ATOM   10588 O O     . TYR C 1 322 ? 59.711  5.885   -1.581  1.00 43.23  ? 322 TYR C O     1 
ATOM   10589 C CB    . TYR C 1 322 ? 57.433  7.970   -2.302  1.00 34.11  ? 322 TYR C CB    1 
ATOM   10590 C CG    . TYR C 1 322 ? 56.586  8.684   -3.331  1.00 37.09  ? 322 TYR C CG    1 
ATOM   10591 C CD1   . TYR C 1 322 ? 56.166  8.049   -4.489  1.00 39.13  ? 322 TYR C CD1   1 
ATOM   10592 C CD2   . TYR C 1 322 ? 56.146  9.982   -3.128  1.00 37.34  ? 322 TYR C CD2   1 
ATOM   10593 C CE1   . TYR C 1 322 ? 55.297  8.660   -5.386  1.00 37.45  ? 322 TYR C CE1   1 
ATOM   10594 C CE2   . TYR C 1 322 ? 55.308  10.619  -4.031  1.00 36.07  ? 322 TYR C CE2   1 
ATOM   10595 C CZ    . TYR C 1 322 ? 54.888  9.962   -5.175  1.00 36.41  ? 322 TYR C CZ    1 
ATOM   10596 O OH    . TYR C 1 322 ? 54.034  10.580  -6.070  1.00 31.47  ? 322 TYR C OH    1 
ATOM   10597 N N     . GLY C 1 323 ? 60.168  7.740   -0.443  1.00 43.68  ? 323 GLY C N     1 
ATOM   10598 C CA    . GLY C 1 323 ? 60.775  7.032   0.672   1.00 45.53  ? 323 GLY C CA    1 
ATOM   10599 C C     . GLY C 1 323 ? 62.258  7.358   0.788   1.00 45.80  ? 323 GLY C C     1 
ATOM   10600 O O     . GLY C 1 323 ? 62.780  8.156   0.010   1.00 43.11  ? 323 GLY C O     1 
ATOM   10601 N N     . PRO C 1 324 ? 62.973  6.730   1.748   1.00 49.52  ? 324 PRO C N     1 
ATOM   10602 C CA    . PRO C 1 324 ? 64.378  7.043   1.981   1.00 54.14  ? 324 PRO C CA    1 
ATOM   10603 C C     . PRO C 1 324 ? 65.206  6.660   0.765   1.00 50.63  ? 324 PRO C C     1 
ATOM   10604 O O     . PRO C 1 324 ? 64.829  5.775   -0.001  1.00 47.42  ? 324 PRO C O     1 
ATOM   10605 C CB    . PRO C 1 324 ? 64.796  6.230   3.211   1.00 59.10  ? 324 PRO C CB    1 
ATOM   10606 C CG    . PRO C 1 324 ? 63.629  5.273   3.515   1.00 57.57  ? 324 PRO C CG    1 
ATOM   10607 C CD    . PRO C 1 324 ? 62.460  5.688   2.648   1.00 51.42  ? 324 PRO C CD    1 
ATOM   10608 N N     . PRO C 1 325 ? 66.345  7.344   0.550   1.00 56.04  ? 325 PRO C N     1 
ATOM   10609 C CA    . PRO C 1 325 ? 67.199  7.096   -0.621  1.00 52.77  ? 325 PRO C CA    1 
ATOM   10610 C C     . PRO C 1 325 ? 67.466  5.641   -1.013  1.00 47.70  ? 325 PRO C C     1 
ATOM   10611 O O     . PRO C 1 325 ? 67.331  5.291   -2.186  1.00 44.44  ? 325 PRO C O     1 
ATOM   10612 C CB    . PRO C 1 325 ? 68.468  7.866   -0.222  1.00 54.90  ? 325 PRO C CB    1 
ATOM   10613 C CG    . PRO C 1 325 ? 67.905  9.092   0.488   1.00 53.57  ? 325 PRO C CG    1 
ATOM   10614 C CD    . PRO C 1 325 ? 66.796  8.503   1.343   1.00 53.83  ? 325 PRO C CD    1 
ATOM   10615 N N     . PRO C 1 326 ? 67.916  4.744   -0.105  1.00 46.04  ? 326 PRO C N     1 
ATOM   10616 C CA    . PRO C 1 326 ? 68.148  3.346   -0.495  1.00 42.48  ? 326 PRO C CA    1 
ATOM   10617 C C     . PRO C 1 326 ? 66.925  2.686   -1.126  1.00 43.42  ? 326 PRO C C     1 
ATOM   10618 O O     . PRO C 1 326 ? 67.030  2.027   -2.166  1.00 41.57  ? 326 PRO C O     1 
ATOM   10619 C CB    . PRO C 1 326 ? 68.588  2.636   0.788   1.00 40.48  ? 326 PRO C CB    1 
ATOM   10620 C CG    . PRO C 1 326 ? 69.079  3.768   1.687   1.00 43.95  ? 326 PRO C CG    1 
ATOM   10621 C CD    . PRO C 1 326 ? 68.366  5.040   1.262   1.00 42.87  ? 326 PRO C CD    1 
ATOM   10622 N N     . VAL C 1 327 ? 65.740  2.932   -0.544  1.00 48.29  ? 327 VAL C N     1 
ATOM   10623 C CA    . VAL C 1 327 ? 64.502  2.372   -1.083  1.00 41.72  ? 327 VAL C CA    1 
ATOM   10624 C C     . VAL C 1 327 ? 64.289  2.845   -2.520  1.00 39.35  ? 327 VAL C C     1 
ATOM   10625 O O     . VAL C 1 327 ? 64.137  2.022   -3.419  1.00 40.04  ? 327 VAL C O     1 
ATOM   10626 C CB    . VAL C 1 327 ? 63.316  2.719   -0.169  1.00 45.93  ? 327 VAL C CB    1 
ATOM   10627 C CG1   . VAL C 1 327 ? 61.987  2.238   -0.738  1.00 45.27  ? 327 VAL C CG1   1 
ATOM   10628 C CG2   . VAL C 1 327 ? 63.537  2.150   1.227   1.00 46.48  ? 327 VAL C CG2   1 
ATOM   10629 N N     . MET C 1 328 ? 64.339  4.176   -2.714  1.00 38.42  ? 328 MET C N     1 
ATOM   10630 C CA    . MET C 1 328 ? 64.225  4.834   -4.004  1.00 41.24  ? 328 MET C CA    1 
ATOM   10631 C C     . MET C 1 328 ? 65.251  4.320   -5.015  1.00 48.01  ? 328 MET C C     1 
ATOM   10632 O O     . MET C 1 328 ? 64.866  3.925   -6.119  1.00 47.70  ? 328 MET C O     1 
ATOM   10633 C CB    . MET C 1 328 ? 64.356  6.355   -3.855  1.00 44.38  ? 328 MET C CB    1 
ATOM   10634 C CG    . MET C 1 328 ? 63.117  6.979   -3.208  1.00 41.86  ? 328 MET C CG    1 
ATOM   10635 S SD    . MET C 1 328 ? 62.960  8.771   -3.371  1.00 51.63  ? 328 MET C SD    1 
ATOM   10636 C CE    . MET C 1 328 ? 64.594  9.350   -2.909  1.00 50.06  ? 328 MET C CE    1 
ATOM   10637 N N     . ASP C 1 329 ? 66.537  4.312   -4.638  1.00 50.15  ? 329 ASP C N     1 
ATOM   10638 C CA    . ASP C 1 329 ? 67.583  3.784   -5.501  1.00 50.12  ? 329 ASP C CA    1 
ATOM   10639 C C     . ASP C 1 329 ? 67.225  2.376   -5.972  1.00 49.35  ? 329 ASP C C     1 
ATOM   10640 O O     . ASP C 1 329 ? 67.375  2.051   -7.140  1.00 59.63  ? 329 ASP C O     1 
ATOM   10641 C CB    . ASP C 1 329 ? 68.935  3.709   -4.782  1.00 52.85  ? 329 ASP C CB    1 
ATOM   10642 C CG    . ASP C 1 329 ? 69.673  5.020   -4.567  1.00 58.78  ? 329 ASP C CG    1 
ATOM   10643 O OD1   . ASP C 1 329 ? 69.138  6.079   -4.946  1.00 59.96  ? 329 ASP C OD1   1 
ATOM   10644 O OD2   . ASP C 1 329 ? 70.809  4.962   -4.033  1.00 67.48  ? 329 ASP C OD2   1 
ATOM   10645 N N     . THR C 1 330 ? 66.809  1.511   -5.041  1.00 47.72  ? 330 THR C N     1 
ATOM   10646 C CA    . THR C 1 330 ? 66.507  0.126   -5.370  1.00 45.48  ? 330 THR C CA    1 
ATOM   10647 C C     . THR C 1 330 ? 65.329  0.063   -6.353  1.00 52.29  ? 330 THR C C     1 
ATOM   10648 O O     . THR C 1 330 ? 65.397  -0.669  -7.347  1.00 47.74  ? 330 THR C O     1 
ATOM   10649 C CB    . THR C 1 330 ? 66.190  -0.660  -4.091  1.00 48.11  ? 330 THR C CB    1 
ATOM   10650 O OG1   . THR C 1 330 ? 67.158  -0.396  -3.066  1.00 45.68  ? 330 THR C OG1   1 
ATOM   10651 C CG2   . THR C 1 330 ? 66.084  -2.150  -4.317  1.00 50.59  ? 330 THR C CG2   1 
ATOM   10652 N N     . LEU C 1 331 ? 64.248  0.828   -6.077  1.00 45.46  ? 331 LEU C N     1 
ATOM   10653 C CA    . LEU C 1 331 ? 63.066  0.808   -6.928  1.00 43.51  ? 331 LEU C CA    1 
ATOM   10654 C C     . LEU C 1 331 ? 63.404  1.326   -8.325  1.00 48.59  ? 331 LEU C C     1 
ATOM   10655 O O     . LEU C 1 331 ? 62.883  0.820   -9.316  1.00 46.60  ? 331 LEU C O     1 
ATOM   10656 C CB    . LEU C 1 331 ? 61.963  1.678   -6.332  1.00 42.63  ? 331 LEU C CB    1 
ATOM   10657 C CG    . LEU C 1 331 ? 61.298  1.214   -5.039  1.00 41.30  ? 331 LEU C CG    1 
ATOM   10658 C CD1   . LEU C 1 331 ? 60.136  2.124   -4.730  1.00 38.48  ? 331 LEU C CD1   1 
ATOM   10659 C CD2   . LEU C 1 331 ? 60.820  -0.240  -5.116  1.00 41.51  ? 331 LEU C CD2   1 
ATOM   10660 N N     . TRP C 1 332 ? 64.272  2.342   -8.395  1.00 51.87  ? 332 TRP C N     1 
ATOM   10661 C CA    . TRP C 1 332 ? 64.612  2.970   -9.659  1.00 49.49  ? 332 TRP C CA    1 
ATOM   10662 C C     . TRP C 1 332 ? 65.361  1.965   -10.535 1.00 52.37  ? 332 TRP C C     1 
ATOM   10663 O O     . TRP C 1 332 ? 65.079  1.866   -11.733 1.00 53.98  ? 332 TRP C O     1 
ATOM   10664 C CB    . TRP C 1 332 ? 65.381  4.292   -9.457  1.00 47.08  ? 332 TRP C CB    1 
ATOM   10665 C CG    . TRP C 1 332 ? 65.817  4.909   -10.753 1.00 47.15  ? 332 TRP C CG    1 
ATOM   10666 C CD1   . TRP C 1 332 ? 67.101  5.115   -11.172 1.00 41.00  ? 332 TRP C CD1   1 
ATOM   10667 C CD2   . TRP C 1 332 ? 64.964  5.328   -11.842 1.00 43.20  ? 332 TRP C CD2   1 
ATOM   10668 N NE1   . TRP C 1 332 ? 67.099  5.653   -12.430 1.00 44.84  ? 332 TRP C NE1   1 
ATOM   10669 C CE2   . TRP C 1 332 ? 65.808  5.798   -12.867 1.00 41.41  ? 332 TRP C CE2   1 
ATOM   10670 C CE3   . TRP C 1 332 ? 63.579  5.391   -12.036 1.00 37.53  ? 332 TRP C CE3   1 
ATOM   10671 C CZ2   . TRP C 1 332 ? 65.307  6.303   -14.064 1.00 40.16  ? 332 TRP C CZ2   1 
ATOM   10672 C CZ3   . TRP C 1 332 ? 63.087  5.883   -13.219 1.00 38.29  ? 332 TRP C CZ3   1 
ATOM   10673 C CH2   . TRP C 1 332 ? 63.942  6.322   -14.225 1.00 39.42  ? 332 TRP C CH2   1 
ATOM   10674 N N     . THR C 1 333 ? 66.264  1.182   -9.925  1.00 48.67  ? 333 THR C N     1 
ATOM   10675 C CA    . THR C 1 333 ? 66.973  0.131   -10.645 1.00 47.73  ? 333 THR C CA    1 
ATOM   10676 C C     . THR C 1 333 ? 65.978  -0.764  -11.391 1.00 41.74  ? 333 THR C C     1 
ATOM   10677 O O     . THR C 1 333 ? 66.131  -1.017  -12.576 1.00 47.04  ? 333 THR C O     1 
ATOM   10678 C CB    . THR C 1 333 ? 67.896  -0.666  -9.709  1.00 49.43  ? 333 THR C CB    1 
ATOM   10679 O OG1   . THR C 1 333 ? 68.868  0.229   -9.178  1.00 52.41  ? 333 THR C OG1   1 
ATOM   10680 C CG2   . THR C 1 333 ? 68.623  -1.802  -10.392 1.00 44.15  ? 333 THR C CG2   1 
ATOM   10681 N N     . ALA C 1 334 ? 64.958  -1.251  -10.695 1.00 42.58  ? 334 ALA C N     1 
ATOM   10682 C CA    . ALA C 1 334 ? 63.956  -2.143  -11.270 1.00 39.54  ? 334 ALA C CA    1 
ATOM   10683 C C     . ALA C 1 334 ? 63.172  -1.466  -12.390 1.00 38.52  ? 334 ALA C C     1 
ATOM   10684 O O     . ALA C 1 334 ? 62.906  -2.074  -13.422 1.00 40.73  ? 334 ALA C O     1 
ATOM   10685 C CB    . ALA C 1 334 ? 63.010  -2.575  -10.188 1.00 37.25  ? 334 ALA C CB    1 
ATOM   10686 N N     . ILE C 1 335 ? 62.797  -0.200  -12.171 1.00 41.51  ? 335 ILE C N     1 
ATOM   10687 C CA    . ILE C 1 335 ? 61.979  0.520   -13.125 1.00 37.97  ? 335 ILE C CA    1 
ATOM   10688 C C     . ILE C 1 335 ? 62.804  0.786   -14.377 1.00 40.50  ? 335 ILE C C     1 
ATOM   10689 O O     . ILE C 1 335 ? 62.349  0.471   -15.468 1.00 41.71  ? 335 ILE C O     1 
ATOM   10690 C CB    . ILE C 1 335 ? 61.377  1.789   -12.500 1.00 38.32  ? 335 ILE C CB    1 
ATOM   10691 C CG1   . ILE C 1 335 ? 60.425  1.419   -11.365 1.00 39.62  ? 335 ILE C CG1   1 
ATOM   10692 C CG2   . ILE C 1 335 ? 60.650  2.601   -13.560 1.00 39.53  ? 335 ILE C CG2   1 
ATOM   10693 C CD1   . ILE C 1 335 ? 59.986  2.573   -10.503 1.00 39.10  ? 335 ILE C CD1   1 
ATOM   10694 N N     . ARG C 1 336 ? 64.007  1.352   -14.225 1.00 42.93  ? 336 ARG C N     1 
ATOM   10695 C CA    . ARG C 1 336 ? 64.820  1.712   -15.381 1.00 46.86  ? 336 ARG C CA    1 
ATOM   10696 C C     . ARG C 1 336 ? 65.179  0.457   -16.161 1.00 44.51  ? 336 ARG C C     1 
ATOM   10697 O O     . ARG C 1 336 ? 65.009  0.406   -17.374 1.00 47.75  ? 336 ARG C O     1 
ATOM   10698 C CB    . ARG C 1 336 ? 66.086  2.467   -14.979 1.00 52.96  ? 336 ARG C CB    1 
ATOM   10699 C CG    . ARG C 1 336 ? 67.005  2.803   -16.135 1.00 51.61  ? 336 ARG C CG    1 
ATOM   10700 C CD    . ARG C 1 336 ? 68.308  3.443   -15.707 1.00 51.80  ? 336 ARG C CD    1 
ATOM   10701 N NE    . ARG C 1 336 ? 69.163  3.491   -16.890 1.00 61.14  ? 336 ARG C NE    1 
ATOM   10702 C CZ    . ARG C 1 336 ? 69.591  4.603   -17.484 1.00 66.96  ? 336 ARG C CZ    1 
ATOM   10703 N NH1   . ARG C 1 336 ? 69.308  5.796   -16.988 1.00 68.82  ? 336 ARG C NH1   1 
ATOM   10704 N NH2   . ARG C 1 336 ? 70.318  4.524   -18.582 1.00 66.15  ? 336 ARG C NH2   1 
ATOM   10705 N N     . ASP C 1 337 ? 65.600  -0.598  -15.471 1.00 49.93  ? 337 ASP C N     1 
ATOM   10706 C CA    . ASP C 1 337 ? 65.974  -1.817  -16.182 1.00 54.61  ? 337 ASP C CA    1 
ATOM   10707 C C     . ASP C 1 337 ? 64.782  -2.406  -16.933 1.00 44.48  ? 337 ASP C C     1 
ATOM   10708 O O     . ASP C 1 337 ? 64.986  -2.912  -18.013 1.00 44.96  ? 337 ASP C O     1 
ATOM   10709 C CB    . ASP C 1 337 ? 66.704  -2.824  -15.287 1.00 61.17  ? 337 ASP C CB    1 
ATOM   10710 C CG    . ASP C 1 337 ? 68.103  -2.372  -14.869 1.00 65.50  ? 337 ASP C CG    1 
ATOM   10711 O OD1   . ASP C 1 337 ? 68.410  -1.143  -14.933 1.00 63.14  ? 337 ASP C OD1   1 
ATOM   10712 O OD2   . ASP C 1 337 ? 68.888  -3.248  -14.500 1.00 69.04  ? 337 ASP C OD2   1 
ATOM   10713 N N     . SER C 1 338 ? 63.548  -2.279  -16.423 1.00 42.94  ? 338 SER C N     1 
ATOM   10714 C CA    . SER C 1 338 ? 62.349  -2.731  -17.129 1.00 41.75  ? 338 SER C CA    1 
ATOM   10715 C C     . SER C 1 338 ? 62.208  -2.178  -18.560 1.00 42.04  ? 338 SER C C     1 
ATOM   10716 O O     . SER C 1 338 ? 61.546  -2.808  -19.389 1.00 43.69  ? 338 SER C O     1 
ATOM   10717 C CB    . SER C 1 338 ? 61.111  -2.397  -16.342 1.00 42.48  ? 338 SER C CB    1 
ATOM   10718 O OG    . SER C 1 338 ? 61.050  -3.123  -15.114 1.00 47.44  ? 338 SER C OG    1 
ATOM   10719 N N     . PHE C 1 339 ? 62.795  -1.003  -18.834 1.00 42.17  ? 339 PHE C N     1 
ATOM   10720 C CA    . PHE C 1 339 ? 62.586  -0.229  -20.053 1.00 40.42  ? 339 PHE C CA    1 
ATOM   10721 C C     . PHE C 1 339 ? 63.854  0.046   -20.883 1.00 38.95  ? 339 PHE C C     1 
ATOM   10722 O O     . PHE C 1 339 ? 63.758  0.630   -21.951 1.00 43.54  ? 339 PHE C O     1 
ATOM   10723 C CB    . PHE C 1 339 ? 61.984  1.124   -19.672 1.00 43.42  ? 339 PHE C CB    1 
ATOM   10724 C CG    . PHE C 1 339 ? 60.558  1.044   -19.186 1.00 41.24  ? 339 PHE C CG    1 
ATOM   10725 C CD1   . PHE C 1 339 ? 59.528  0.802   -20.074 1.00 38.49  ? 339 PHE C CD1   1 
ATOM   10726 C CD2   . PHE C 1 339 ? 60.263  1.199   -17.834 1.00 38.71  ? 339 PHE C CD2   1 
ATOM   10727 C CE1   . PHE C 1 339 ? 58.226  0.699   -19.599 1.00 45.43  ? 339 PHE C CE1   1 
ATOM   10728 C CE2   . PHE C 1 339 ? 58.969  1.098   -17.361 1.00 40.36  ? 339 PHE C CE2   1 
ATOM   10729 C CZ    . PHE C 1 339 ? 57.949  0.836   -18.241 1.00 44.87  ? 339 PHE C CZ    1 
ATOM   10730 N N     . ALA C 1 340 ? 65.043  -0.388  -20.450 1.00 42.80  ? 340 ALA C N     1 
ATOM   10731 C CA    . ALA C 1 340 ? 66.289  0.114   -21.018 1.00 41.98  ? 340 ALA C CA    1 
ATOM   10732 C C     . ALA C 1 340 ? 66.462  -0.302  -22.471 1.00 40.87  ? 340 ALA C C     1 
ATOM   10733 O O     . ALA C 1 340 ? 66.983  0.476   -23.255 1.00 51.80  ? 340 ALA C O     1 
ATOM   10734 C CB    . ALA C 1 340 ? 67.460  -0.333  -20.198 1.00 35.51  ? 340 ALA C CB    1 
ATOM   10735 N N     . ASP C 1 341 ? 66.001  -1.502  -22.818 1.00 46.11  ? 341 ASP C N     1 
ATOM   10736 C CA    . ASP C 1 341 ? 66.339  -2.147  -24.075 1.00 48.81  ? 341 ASP C CA    1 
ATOM   10737 C C     . ASP C 1 341 ? 65.403  -1.688  -25.188 1.00 49.67  ? 341 ASP C C     1 
ATOM   10738 O O     . ASP C 1 341 ? 65.542  -2.135  -26.314 1.00 61.34  ? 341 ASP C O     1 
ATOM   10739 C CB    . ASP C 1 341 ? 66.299  -3.681  -23.975 1.00 47.76  ? 341 ASP C CB    1 
ATOM   10740 C CG    . ASP C 1 341 ? 64.929  -4.232  -23.618 1.00 57.39  ? 341 ASP C CG    1 
ATOM   10741 O OD1   . ASP C 1 341 ? 64.534  -4.096  -22.452 1.00 71.19  ? 341 ASP C OD1   1 
ATOM   10742 O OD2   . ASP C 1 341 ? 64.257  -4.766  -24.497 1.00 60.52  ? 341 ASP C OD2   1 
ATOM   10743 N N     . ILE C 1 342 ? 64.461  -0.793  -24.905 1.00 49.56  ? 342 ILE C N     1 
ATOM   10744 C CA    . ILE C 1 342 ? 63.564  -0.292  -25.943 1.00 49.14  ? 342 ILE C CA    1 
ATOM   10745 C C     . ILE C 1 342 ? 64.292  0.739   -26.812 1.00 53.73  ? 342 ILE C C     1 
ATOM   10746 O O     . ILE C 1 342 ? 64.665  1.792   -26.285 1.00 56.06  ? 342 ILE C O     1 
ATOM   10747 C CB    . ILE C 1 342 ? 62.329  0.359   -25.284 1.00 46.26  ? 342 ILE C CB    1 
ATOM   10748 C CG1   . ILE C 1 342 ? 61.561  -0.623  -24.398 1.00 47.60  ? 342 ILE C CG1   1 
ATOM   10749 C CG2   . ILE C 1 342 ? 61.436  1.034   -26.312 1.00 38.58  ? 342 ILE C CG2   1 
ATOM   10750 C CD1   . ILE C 1 342 ? 60.718  0.039   -23.301 1.00 48.34  ? 342 ILE C CD1   1 
ATOM   10751 N N     . PRO C 1 343 ? 64.491  0.536   -28.148 1.00 46.59  ? 343 PRO C N     1 
ATOM   10752 C CA    . PRO C 1 343 ? 65.144  1.545   -28.981 1.00 45.07  ? 343 PRO C CA    1 
ATOM   10753 C C     . PRO C 1 343 ? 64.523  2.919   -28.766 1.00 48.39  ? 343 PRO C C     1 
ATOM   10754 O O     . PRO C 1 343 ? 63.308  3.081   -28.942 1.00 62.80  ? 343 PRO C O     1 
ATOM   10755 C CB    . PRO C 1 343 ? 64.928  1.067   -30.431 1.00 42.81  ? 343 PRO C CB    1 
ATOM   10756 C CG    . PRO C 1 343 ? 64.771  -0.432  -30.309 1.00 43.95  ? 343 PRO C CG    1 
ATOM   10757 C CD    . PRO C 1 343 ? 64.178  -0.668  -28.929 1.00 49.92  ? 343 PRO C CD    1 
ATOM   10758 N N     . GLY C 1 344 ? 65.366  3.881   -28.362 1.00 47.47  ? 344 GLY C N     1 
ATOM   10759 C CA    . GLY C 1 344 ? 65.038  5.301   -28.458 1.00 43.28  ? 344 GLY C CA    1 
ATOM   10760 C C     . GLY C 1 344 ? 64.640  5.890   -27.114 1.00 45.18  ? 344 GLY C C     1 
ATOM   10761 O O     . GLY C 1 344 ? 64.445  7.089   -26.989 1.00 50.59  ? 344 GLY C O     1 
ATOM   10762 N N     . VAL C 1 345 ? 64.566  5.027   -26.104 1.00 44.95  ? 345 VAL C N     1 
ATOM   10763 C CA    . VAL C 1 345 ? 64.080  5.409   -24.793 1.00 45.91  ? 345 VAL C CA    1 
ATOM   10764 C C     . VAL C 1 345 ? 65.048  6.419   -24.190 1.00 47.81  ? 345 VAL C C     1 
ATOM   10765 O O     . VAL C 1 345 ? 66.265  6.357   -24.420 1.00 50.49  ? 345 VAL C O     1 
ATOM   10766 C CB    . VAL C 1 345 ? 63.930  4.150   -23.915 1.00 49.32  ? 345 VAL C CB    1 
ATOM   10767 C CG1   . VAL C 1 345 ? 65.286  3.593   -23.497 1.00 48.49  ? 345 VAL C CG1   1 
ATOM   10768 C CG2   . VAL C 1 345 ? 63.049  4.371   -22.702 1.00 48.22  ? 345 VAL C CG2   1 
ATOM   10769 N N     . LYS C 1 346 ? 64.486  7.366   -23.433 1.00 51.06  ? 346 LYS C N     1 
ATOM   10770 C CA    . LYS C 1 346 ? 65.313  8.293   -22.686 1.00 52.57  ? 346 LYS C CA    1 
ATOM   10771 C C     . LYS C 1 346 ? 64.782  8.456   -21.268 1.00 47.56  ? 346 LYS C C     1 
ATOM   10772 O O     . LYS C 1 346 ? 63.574  8.459   -21.023 1.00 46.87  ? 346 LYS C O     1 
ATOM   10773 C CB    . LYS C 1 346 ? 65.437  9.607   -23.457 1.00 58.05  ? 346 LYS C CB    1 
ATOM   10774 C CG    . LYS C 1 346 ? 66.387  9.538   -24.644 1.00 63.08  ? 346 LYS C CG    1 
ATOM   10775 C CD    . LYS C 1 346 ? 66.184  10.678  -25.623 1.00 78.54  ? 346 LYS C CD    1 
ATOM   10776 C CE    . LYS C 1 346 ? 66.381  10.260  -27.065 1.00 84.74  ? 346 LYS C CE    1 
ATOM   10777 N NZ    . LYS C 1 346 ? 67.689  9.581   -27.218 1.00 88.77  ? 346 LYS C NZ    1 
ATOM   10778 N N     . PHE C 1 347 ? 65.741  8.639   -20.352 1.00 51.81  ? 347 PHE C N     1 
ATOM   10779 C CA    . PHE C 1 347 ? 65.479  8.735   -18.928 1.00 46.19  ? 347 PHE C CA    1 
ATOM   10780 C C     . PHE C 1 347 ? 65.895  10.109  -18.412 1.00 48.57  ? 347 PHE C C     1 
ATOM   10781 O O     . PHE C 1 347 ? 67.015  10.537  -18.685 1.00 49.34  ? 347 PHE C O     1 
ATOM   10782 C CB    . PHE C 1 347 ? 66.263  7.639   -18.220 1.00 42.19  ? 347 PHE C CB    1 
ATOM   10783 C CG    . PHE C 1 347 ? 65.851  6.226   -18.535 1.00 42.24  ? 347 PHE C CG    1 
ATOM   10784 C CD1   . PHE C 1 347 ? 64.694  5.683   -17.997 1.00 47.19  ? 347 PHE C CD1   1 
ATOM   10785 C CD2   . PHE C 1 347 ? 66.623  5.426   -19.352 1.00 44.64  ? 347 PHE C CD2   1 
ATOM   10786 C CE1   . PHE C 1 347 ? 64.342  4.367   -18.251 1.00 40.61  ? 347 PHE C CE1   1 
ATOM   10787 C CE2   . PHE C 1 347 ? 66.255  4.117   -19.626 1.00 45.95  ? 347 PHE C CE2   1 
ATOM   10788 C CZ    . PHE C 1 347 ? 65.121  3.593   -19.072 1.00 43.76  ? 347 PHE C CZ    1 
ATOM   10789 N N     . TYR C 1 348 ? 65.005  10.742  -17.625 1.00 45.87  ? 348 TYR C N     1 
ATOM   10790 C CA    . TYR C 1 348 ? 65.203  12.086  -17.095 1.00 46.05  ? 348 TYR C CA    1 
ATOM   10791 C C     . TYR C 1 348 ? 64.721  12.208  -15.645 1.00 46.07  ? 348 TYR C C     1 
ATOM   10792 O O     . TYR C 1 348 ? 63.576  11.851  -15.337 1.00 39.86  ? 348 TYR C O     1 
ATOM   10793 C CB    . TYR C 1 348 ? 64.364  13.118  -17.853 1.00 51.08  ? 348 TYR C CB    1 
ATOM   10794 C CG    . TYR C 1 348 ? 64.568  13.197  -19.347 1.00 55.41  ? 348 TYR C CG    1 
ATOM   10795 C CD1   . TYR C 1 348 ? 65.578  13.975  -19.913 1.00 50.66  ? 348 TYR C CD1   1 
ATOM   10796 C CD2   . TYR C 1 348 ? 63.717  12.512  -20.196 1.00 50.47  ? 348 TYR C CD2   1 
ATOM   10797 C CE1   . TYR C 1 348 ? 65.737  14.068  -21.288 1.00 47.55  ? 348 TYR C CE1   1 
ATOM   10798 C CE2   . TYR C 1 348 ? 63.872  12.584  -21.567 1.00 54.67  ? 348 TYR C CE2   1 
ATOM   10799 C CZ    . TYR C 1 348 ? 64.882  13.359  -22.116 1.00 52.27  ? 348 TYR C CZ    1 
ATOM   10800 O OH    . TYR C 1 348 ? 64.972  13.370  -23.482 1.00 47.77  ? 348 TYR C OH    1 
ATOM   10801 N N     . PHE C 1 349 ? 65.601  12.736  -14.770 1.00 44.04  ? 349 PHE C N     1 
ATOM   10802 C CA    . PHE C 1 349 ? 65.198  13.366  -13.515 1.00 47.04  ? 349 PHE C CA    1 
ATOM   10803 C C     . PHE C 1 349 ? 65.126  14.885  -13.707 1.00 44.84  ? 349 PHE C C     1 
ATOM   10804 O O     . PHE C 1 349 ? 65.480  15.392  -14.773 1.00 44.93  ? 349 PHE C O     1 
ATOM   10805 C CB    . PHE C 1 349 ? 66.167  12.936  -12.417 1.00 48.43  ? 349 PHE C CB    1 
ATOM   10806 C CG    . PHE C 1 349 ? 66.011  11.489  -12.054 1.00 55.00  ? 349 PHE C CG    1 
ATOM   10807 C CD1   . PHE C 1 349 ? 64.931  11.077  -11.294 1.00 63.97  ? 349 PHE C CD1   1 
ATOM   10808 C CD2   . PHE C 1 349 ? 66.896  10.541  -12.534 1.00 63.72  ? 349 PHE C CD2   1 
ATOM   10809 C CE1   . PHE C 1 349 ? 64.753  9.738   -11.000 1.00 66.02  ? 349 PHE C CE1   1 
ATOM   10810 C CE2   . PHE C 1 349 ? 66.725  9.203   -12.231 1.00 65.20  ? 349 PHE C CE2   1 
ATOM   10811 C CZ    . PHE C 1 349 ? 65.651  8.807   -11.468 1.00 75.02  ? 349 PHE C CZ    1 
ATOM   10812 N N     . PRO C 1 350 ? 64.639  15.681  -12.728 1.00 42.83  ? 350 PRO C N     1 
ATOM   10813 C CA    . PRO C 1 350 ? 64.547  17.128  -12.924 1.00 48.66  ? 350 PRO C CA    1 
ATOM   10814 C C     . PRO C 1 350 ? 65.832  17.729  -13.478 1.00 49.46  ? 350 PRO C C     1 
ATOM   10815 O O     . PRO C 1 350 ? 65.807  18.400  -14.499 1.00 55.52  ? 350 PRO C O     1 
ATOM   10816 C CB    . PRO C 1 350 ? 64.180  17.670  -11.536 1.00 46.53  ? 350 PRO C CB    1 
ATOM   10817 C CG    . PRO C 1 350 ? 63.413  16.512  -10.891 1.00 47.49  ? 350 PRO C CG    1 
ATOM   10818 C CD    . PRO C 1 350 ? 64.056  15.256  -11.448 1.00 45.55  ? 350 PRO C CD    1 
ATOM   10819 N N     . GLU C 1 351 ? 66.962  17.420  -12.847 1.00 58.07  ? 351 GLU C N     1 
ATOM   10820 C CA    . GLU C 1 351 ? 68.228  18.045  -13.191 1.00 55.80  ? 351 GLU C CA    1 
ATOM   10821 C C     . GLU C 1 351 ? 68.582  17.820  -14.663 1.00 53.40  ? 351 GLU C C     1 
ATOM   10822 O O     . GLU C 1 351 ? 69.243  18.659  -15.255 1.00 59.85  ? 351 GLU C O     1 
ATOM   10823 C CB    . GLU C 1 351 ? 69.329  17.602  -12.221 1.00 62.46  ? 351 GLU C CB    1 
ATOM   10824 C CG    . GLU C 1 351 ? 69.730  16.128  -12.299 1.00 74.15  ? 351 GLU C CG    1 
ATOM   10825 C CD    . GLU C 1 351 ? 69.101  15.171  -11.290 1.00 76.99  ? 351 GLU C CD    1 
ATOM   10826 O OE1   . GLU C 1 351 ? 68.041  15.515  -10.687 1.00 63.63  ? 351 GLU C OE1   1 
ATOM   10827 O OE2   . GLU C 1 351 ? 69.681  14.070  -11.101 1.00 81.60  ? 351 GLU C OE2   1 
ATOM   10828 N N     . ASP C 1 352 ? 68.127  16.728  -15.280 1.00 58.79  ? 352 ASP C N     1 
ATOM   10829 C CA    . ASP C 1 352 ? 68.480  16.430  -16.665 1.00 56.25  ? 352 ASP C CA    1 
ATOM   10830 C C     . ASP C 1 352 ? 67.493  17.078  -17.643 1.00 52.90  ? 352 ASP C C     1 
ATOM   10831 O O     . ASP C 1 352 ? 67.475  16.720  -18.809 1.00 57.52  ? 352 ASP C O     1 
ATOM   10832 C CB    . ASP C 1 352 ? 68.505  14.918  -16.951 1.00 57.38  ? 352 ASP C CB    1 
ATOM   10833 C CG    . ASP C 1 352 ? 69.168  14.060  -15.889 1.00 58.63  ? 352 ASP C CG    1 
ATOM   10834 O OD1   . ASP C 1 352 ? 70.371  14.232  -15.690 1.00 73.17  ? 352 ASP C OD1   1 
ATOM   10835 O OD2   . ASP C 1 352 ? 68.462  13.251  -15.246 1.00 60.08  ? 352 ASP C OD2   1 
ATOM   10836 N N     . ARG C 1 353 ? 66.653  18.011  -17.196 1.00 52.14  ? 353 ARG C N     1 
ATOM   10837 C CA    . ARG C 1 353 ? 65.697  18.649  -18.088 1.00 51.94  ? 353 ARG C CA    1 
ATOM   10838 C C     . ARG C 1 353 ? 66.210  20.052  -18.375 1.00 53.97  ? 353 ARG C C     1 
ATOM   10839 O O     . ARG C 1 353 ? 66.236  20.907  -17.489 1.00 53.47  ? 353 ARG C O     1 
ATOM   10840 C CB    . ARG C 1 353 ? 64.280  18.733  -17.490 1.00 46.74  ? 353 ARG C CB    1 
ATOM   10841 C CG    . ARG C 1 353 ? 63.633  17.390  -17.168 1.00 40.80  ? 353 ARG C CG    1 
ATOM   10842 C CD    . ARG C 1 353 ? 63.315  16.572  -18.395 1.00 39.04  ? 353 ARG C CD    1 
ATOM   10843 N NE    . ARG C 1 353 ? 62.321  17.202  -19.250 1.00 38.28  ? 353 ARG C NE    1 
ATOM   10844 C CZ    . ARG C 1 353 ? 62.041  16.781  -20.476 1.00 39.48  ? 353 ARG C CZ    1 
ATOM   10845 N NH1   . ARG C 1 353 ? 62.770  15.831  -21.024 1.00 43.43  ? 353 ARG C NH1   1 
ATOM   10846 N NH2   . ARG C 1 353 ? 61.030  17.279  -21.167 1.00 40.30  ? 353 ARG C NH2   1 
ATOM   10847 N N     . ARG C 1 354 ? 66.564  20.298  -19.633 1.00 54.02  ? 354 ARG C N     1 
ATOM   10848 C CA    . ARG C 1 354 ? 67.303  21.501  -19.975 1.00 51.03  ? 354 ARG C CA    1 
ATOM   10849 C C     . ARG C 1 354 ? 66.385  22.712  -20.103 1.00 51.62  ? 354 ARG C C     1 
ATOM   10850 O O     . ARG C 1 354 ? 66.880  23.830  -20.085 1.00 52.62  ? 354 ARG C O     1 
ATOM   10851 C CB    . ARG C 1 354 ? 68.117  21.267  -21.241 1.00 47.23  ? 354 ARG C CB    1 
ATOM   10852 C CG    . ARG C 1 354 ? 67.282  21.098  -22.497 1.00 47.73  ? 354 ARG C CG    1 
ATOM   10853 C CD    . ARG C 1 354 ? 68.166  20.597  -23.620 1.00 47.47  ? 354 ARG C CD    1 
ATOM   10854 N NE    . ARG C 1 354 ? 67.331  20.204  -24.738 1.00 54.18  ? 354 ARG C NE    1 
ATOM   10855 C CZ    . ARG C 1 354 ? 66.765  21.037  -25.594 1.00 51.91  ? 354 ARG C CZ    1 
ATOM   10856 N NH1   . ARG C 1 354 ? 67.174  22.288  -25.679 1.00 57.72  ? 354 ARG C NH1   1 
ATOM   10857 N NH2   . ARG C 1 354 ? 65.799  20.602  -26.381 1.00 50.00  ? 354 ARG C NH2   1 
ATOM   10858 N N     . HIS C 1 355 ? 65.070  22.493  -20.217 1.00 55.95  ? 355 HIS C N     1 
ATOM   10859 C CA    . HIS C 1 355 ? 64.087  23.568  -20.158 1.00 51.03  ? 355 HIS C CA    1 
ATOM   10860 C C     . HIS C 1 355 ? 63.634  23.833  -18.728 1.00 53.84  ? 355 HIS C C     1 
ATOM   10861 O O     . HIS C 1 355 ? 63.465  22.903  -17.942 1.00 66.65  ? 355 HIS C O     1 
ATOM   10862 C CB    . HIS C 1 355 ? 62.809  23.205  -20.914 1.00 47.77  ? 355 HIS C CB    1 
ATOM   10863 C CG    . HIS C 1 355 ? 63.042  22.961  -22.357 1.00 51.11  ? 355 HIS C CG    1 
ATOM   10864 N ND1   . HIS C 1 355 ? 62.676  23.866  -23.329 1.00 56.69  ? 355 HIS C ND1   1 
ATOM   10865 C CD2   . HIS C 1 355 ? 63.600  21.933  -22.986 1.00 49.51  ? 355 HIS C CD2   1 
ATOM   10866 C CE1   . HIS C 1 355 ? 63.022  23.379  -24.506 1.00 56.45  ? 355 HIS C CE1   1 
ATOM   10867 N NE2   . HIS C 1 355 ? 63.569  22.201  -24.320 1.00 52.44  ? 355 HIS C NE2   1 
ATOM   10868 N N     . LYS C 1 356 ? 63.362  25.101  -18.419 1.00 53.95  ? 356 LYS C N     1 
ATOM   10869 C CA    . LYS C 1 356 ? 63.093  25.490  -17.045 1.00 60.09  ? 356 LYS C CA    1 
ATOM   10870 C C     . LYS C 1 356 ? 61.589  25.666  -16.871 1.00 56.75  ? 356 LYS C C     1 
ATOM   10871 O O     . LYS C 1 356 ? 61.097  25.765  -15.751 1.00 60.41  ? 356 LYS C O     1 
ATOM   10872 C CB    . LYS C 1 356 ? 63.959  26.708  -16.697 1.00 72.17  ? 356 LYS C CB    1 
ATOM   10873 C CG    . LYS C 1 356 ? 65.464  26.416  -16.683 1.00 79.78  ? 356 LYS C CG    1 
ATOM   10874 C CD    . LYS C 1 356 ? 66.348  27.599  -16.344 1.00 93.07  ? 356 LYS C CD    1 
ATOM   10875 C CE    . LYS C 1 356 ? 65.922  28.324  -15.078 1.00 93.90  ? 356 LYS C CE    1 
ATOM   10876 N NZ    . LYS C 1 356 ? 66.937  29.304  -14.621 1.00 84.57  ? 356 LYS C NZ    1 
ATOM   10877 N N     . VAL C 1 357 ? 60.876  25.723  -17.998 1.00 52.69  ? 357 VAL C N     1 
ATOM   10878 C CA    . VAL C 1 357 ? 59.438  25.545  -18.033 1.00 52.46  ? 357 VAL C CA    1 
ATOM   10879 C C     . VAL C 1 357 ? 59.217  24.269  -18.827 1.00 50.55  ? 357 VAL C C     1 
ATOM   10880 O O     . VAL C 1 357 ? 59.689  24.207  -19.962 1.00 61.44  ? 357 VAL C O     1 
ATOM   10881 C CB    . VAL C 1 357 ? 58.746  26.771  -18.658 1.00 57.91  ? 357 VAL C CB    1 
ATOM   10882 C CG1   . VAL C 1 357 ? 57.307  26.491  -19.045 1.00 56.50  ? 357 VAL C CG1   1 
ATOM   10883 C CG2   . VAL C 1 357 ? 58.805  27.962  -17.722 1.00 56.68  ? 357 VAL C CG2   1 
ATOM   10884 N N     . ASP C 1 358 ? 58.608  23.248  -18.192 1.00 46.22  ? 358 ASP C N     1 
ATOM   10885 C CA    . ASP C 1 358 ? 58.805  21.858  -18.602 1.00 45.14  ? 358 ASP C CA    1 
ATOM   10886 C C     . ASP C 1 358 ? 57.774  20.910  -17.983 1.00 51.10  ? 358 ASP C C     1 
ATOM   10887 O O     . ASP C 1 358 ? 57.246  21.100  -16.866 1.00 42.46  ? 358 ASP C O     1 
ATOM   10888 C CB    . ASP C 1 358 ? 60.193  21.326  -18.217 1.00 40.22  ? 358 ASP C CB    1 
ATOM   10889 C CG    . ASP C 1 358 ? 60.579  19.988  -18.839 1.00 43.04  ? 358 ASP C CG    1 
ATOM   10890 O OD1   . ASP C 1 358 ? 61.061  19.985  -19.979 1.00 41.28  ? 358 ASP C OD1   1 
ATOM   10891 O OD2   . ASP C 1 358 ? 60.426  18.943  -18.175 1.00 50.11  ? 358 ASP C OD2   1 
ATOM   10892 N N     . LEU C 1 359 ? 57.561  19.814  -18.714 1.00 48.52  ? 359 LEU C N     1 
ATOM   10893 C CA    . LEU C 1 359 ? 56.565  18.843  -18.319 1.00 47.50  ? 359 LEU C CA    1 
ATOM   10894 C C     . LEU C 1 359 ? 56.922  18.268  -16.948 1.00 44.90  ? 359 LEU C C     1 
ATOM   10895 O O     . LEU C 1 359 ? 56.083  18.223  -16.046 1.00 39.44  ? 359 LEU C O     1 
ATOM   10896 C CB    . LEU C 1 359 ? 56.511  17.745  -19.374 1.00 49.57  ? 359 LEU C CB    1 
ATOM   10897 C CG    . LEU C 1 359 ? 55.744  16.524  -18.899 1.00 60.88  ? 359 LEU C CG    1 
ATOM   10898 C CD1   . LEU C 1 359 ? 54.263  16.836  -18.847 1.00 61.75  ? 359 LEU C CD1   1 
ATOM   10899 C CD2   . LEU C 1 359 ? 56.046  15.339  -19.777 1.00 65.46  ? 359 LEU C CD2   1 
ATOM   10900 N N     . LEU C 1 360 ? 58.171  17.810  -16.805 1.00 43.75  ? 360 LEU C N     1 
ATOM   10901 C CA    . LEU C 1 360 ? 58.562  17.099  -15.606 1.00 44.65  ? 360 LEU C CA    1 
ATOM   10902 C C     . LEU C 1 360 ? 58.428  18.026  -14.411 1.00 47.36  ? 360 LEU C C     1 
ATOM   10903 O O     . LEU C 1 360 ? 57.917  17.587  -13.396 1.00 51.73  ? 360 LEU C O     1 
ATOM   10904 C CB    . LEU C 1 360 ? 59.973  16.533  -15.712 1.00 47.94  ? 360 LEU C CB    1 
ATOM   10905 C CG    . LEU C 1 360 ? 60.400  15.760  -14.459 1.00 58.92  ? 360 LEU C CG    1 
ATOM   10906 C CD1   . LEU C 1 360 ? 59.350  14.718  -14.076 1.00 53.68  ? 360 LEU C CD1   1 
ATOM   10907 C CD2   . LEU C 1 360 ? 61.769  15.095  -14.626 1.00 53.05  ? 360 LEU C CD2   1 
ATOM   10908 N N     . LEU C 1 361 ? 58.814  19.305  -14.556 1.00 56.33  ? 361 LEU C N     1 
ATOM   10909 C CA    . LEU C 1 361 ? 58.802  20.240  -13.437 1.00 52.92  ? 361 LEU C CA    1 
ATOM   10910 C C     . LEU C 1 361 ? 57.373  20.592  -13.056 1.00 49.84  ? 361 LEU C C     1 
ATOM   10911 O O     . LEU C 1 361 ? 57.125  20.887  -11.891 1.00 48.01  ? 361 LEU C O     1 
ATOM   10912 C CB    . LEU C 1 361 ? 59.616  21.499  -13.754 1.00 64.05  ? 361 LEU C CB    1 
ATOM   10913 C CG    . LEU C 1 361 ? 61.065  21.292  -14.225 1.00 77.04  ? 361 LEU C CG    1 
ATOM   10914 C CD1   . LEU C 1 361 ? 61.852  22.589  -14.133 1.00 86.85  ? 361 LEU C CD1   1 
ATOM   10915 C CD2   . LEU C 1 361 ? 61.792  20.205  -13.448 1.00 75.20  ? 361 LEU C CD2   1 
ATOM   10916 N N     . HIS C 1 362 ? 56.434  20.540  -14.020 1.00 52.39  ? 362 HIS C N     1 
ATOM   10917 C CA    . HIS C 1 362 ? 55.028  20.748  -13.697 1.00 45.66  ? 362 HIS C CA    1 
ATOM   10918 C C     . HIS C 1 362 ? 54.492  19.511  -12.969 1.00 53.70  ? 362 HIS C C     1 
ATOM   10919 O O     . HIS C 1 362 ? 54.010  19.637  -11.845 1.00 74.72  ? 362 HIS C O     1 
ATOM   10920 C CB    . HIS C 1 362 ? 54.203  21.182  -14.918 1.00 49.71  ? 362 HIS C CB    1 
ATOM   10921 C CG    . HIS C 1 362 ? 52.729  21.113  -14.650 1.00 56.10  ? 362 HIS C CG    1 
ATOM   10922 N ND1   . HIS C 1 362 ? 52.045  22.116  -14.010 1.00 69.43  ? 362 HIS C ND1   1 
ATOM   10923 C CD2   . HIS C 1 362 ? 51.840  20.119  -14.795 1.00 62.07  ? 362 HIS C CD2   1 
ATOM   10924 C CE1   . HIS C 1 362 ? 50.794  21.734  -13.793 1.00 73.51  ? 362 HIS C CE1   1 
ATOM   10925 N NE2   . HIS C 1 362 ? 50.637  20.536  -14.284 1.00 65.38  ? 362 HIS C NE2   1 
ATOM   10926 N N     . ARG C 1 363 ? 54.604  18.318  -13.584 1.00 49.96  ? 363 ARG C N     1 
ATOM   10927 C CA    . ARG C 1 363 ? 54.021  17.091  -13.049 1.00 49.06  ? 363 ARG C CA    1 
ATOM   10928 C C     . ARG C 1 363 ? 54.680  16.654  -11.727 1.00 51.06  ? 363 ARG C C     1 
ATOM   10929 O O     . ARG C 1 363 ? 54.024  15.989  -10.924 1.00 56.46  ? 363 ARG C O     1 
ATOM   10930 C CB    . ARG C 1 363 ? 54.158  15.912  -14.020 1.00 49.11  ? 363 ARG C CB    1 
ATOM   10931 C CG    . ARG C 1 363 ? 53.584  16.131  -15.411 1.00 52.77  ? 363 ARG C CG    1 
ATOM   10932 C CD    . ARG C 1 363 ? 52.143  15.692  -15.602 1.00 55.30  ? 363 ARG C CD    1 
ATOM   10933 N NE    . ARG C 1 363 ? 51.754  15.855  -17.001 1.00 53.02  ? 363 ARG C NE    1 
ATOM   10934 C CZ    . ARG C 1 363 ? 50.693  16.524  -17.449 1.00 56.78  ? 363 ARG C CZ    1 
ATOM   10935 N NH1   . ARG C 1 363 ? 49.745  16.917  -16.618 1.00 57.60  ? 363 ARG C NH1   1 
ATOM   10936 N NH2   . ARG C 1 363 ? 50.533  16.719  -18.752 1.00 62.72  ? 363 ARG C NH2   1 
ATOM   10937 N N     . ALA C 1 364 ? 55.959  16.993  -11.491 1.00 43.82  ? 364 ALA C N     1 
ATOM   10938 C CA    . ALA C 1 364 ? 56.600  16.770  -10.196 1.00 43.12  ? 364 ALA C CA    1 
ATOM   10939 C C     . ALA C 1 364 ? 55.801  17.424  -9.081  1.00 41.49  ? 364 ALA C C     1 
ATOM   10940 O O     . ALA C 1 364 ? 55.724  16.886  -7.994  1.00 43.28  ? 364 ALA C O     1 
ATOM   10941 C CB    . ALA C 1 364 ? 58.015  17.307  -10.153 1.00 39.57  ? 364 ALA C CB    1 
ATOM   10942 N N     . GLU C 1 365 ? 55.247  18.603  -9.341  1.00 43.33  ? 365 GLU C N     1 
ATOM   10943 C CA    . GLU C 1 365 ? 54.471  19.280  -8.326  1.00 50.12  ? 365 GLU C CA    1 
ATOM   10944 C C     . GLU C 1 365 ? 53.277  18.412  -7.958  1.00 46.64  ? 365 GLU C C     1 
ATOM   10945 O O     . GLU C 1 365 ? 52.995  18.254  -6.773  1.00 50.47  ? 365 GLU C O     1 
ATOM   10946 C CB    . GLU C 1 365 ? 54.017  20.661  -8.811  1.00 55.87  ? 365 GLU C CB    1 
ATOM   10947 C CG    . GLU C 1 365 ? 55.163  21.663  -8.949  1.00 63.11  ? 365 GLU C CG    1 
ATOM   10948 C CD    . GLU C 1 365 ? 55.611  22.387  -7.686  1.00 69.61  ? 365 GLU C CD    1 
ATOM   10949 O OE1   . GLU C 1 365 ? 55.598  23.635  -7.708  1.00 75.85  ? 365 GLU C OE1   1 
ATOM   10950 O OE2   . GLU C 1 365 ? 55.988  21.720  -6.690  1.00 59.87  ? 365 GLU C OE2   1 
ATOM   10951 N N     . THR C 1 366 ? 52.583  17.863  -8.967  1.00 38.24  ? 366 THR C N     1 
ATOM   10952 C CA    . THR C 1 366 ? 51.328  17.167  -8.718  1.00 45.26  ? 366 THR C CA    1 
ATOM   10953 C C     . THR C 1 366 ? 51.597  15.770  -8.147  1.00 43.67  ? 366 THR C C     1 
ATOM   10954 O O     . THR C 1 366 ? 50.817  15.244  -7.359  1.00 35.85  ? 366 THR C O     1 
ATOM   10955 C CB    . THR C 1 366 ? 50.448  17.180  -9.970  1.00 48.53  ? 366 THR C CB    1 
ATOM   10956 O OG1   . THR C 1 366 ? 51.192  16.473  -10.945 1.00 66.32  ? 366 THR C OG1   1 
ATOM   10957 C CG2   . THR C 1 366 ? 50.185  18.580  -10.485 1.00 56.80  ? 366 THR C CG2   1 
ATOM   10958 N N     . MET C 1 367 ? 52.766  15.196  -8.429  1.00 37.59  ? 367 MET C N     1 
ATOM   10959 C CA    . MET C 1 367 ? 53.036  13.886  -7.869  1.00 37.82  ? 367 MET C CA    1 
ATOM   10960 C C     . MET C 1 367 ? 53.496  14.068  -6.423  1.00 36.90  ? 367 MET C C     1 
ATOM   10961 O O     . MET C 1 367 ? 53.865  13.093  -5.755  1.00 30.46  ? 367 MET C O     1 
ATOM   10962 C CB    . MET C 1 367 ? 54.054  13.121  -8.727  1.00 35.66  ? 367 MET C CB    1 
ATOM   10963 C CG    . MET C 1 367 ? 53.431  12.642  -10.057 1.00 34.51  ? 367 MET C CG    1 
ATOM   10964 S SD    . MET C 1 367 ? 54.627  11.805  -11.120 1.00 41.09  ? 367 MET C SD    1 
ATOM   10965 C CE    . MET C 1 367 ? 55.743  13.143  -11.519 1.00 47.87  ? 367 MET C CE    1 
ATOM   10966 N N     . LYS C 1 368 ? 53.462  15.325  -5.961  1.00 34.32  ? 368 LYS C N     1 
ATOM   10967 C CA    . LYS C 1 368 ? 53.859  15.674  -4.602  1.00 40.99  ? 368 LYS C CA    1 
ATOM   10968 C C     . LYS C 1 368 ? 52.656  16.210  -3.824  1.00 39.21  ? 368 LYS C C     1 
ATOM   10969 O O     . LYS C 1 368 ? 52.783  16.575  -2.675  1.00 36.54  ? 368 LYS C O     1 
ATOM   10970 C CB    . LYS C 1 368 ? 54.936  16.757  -4.667  1.00 50.29  ? 368 LYS C CB    1 
ATOM   10971 C CG    . LYS C 1 368 ? 55.897  16.771  -3.501  1.00 61.39  ? 368 LYS C CG    1 
ATOM   10972 C CD    . LYS C 1 368 ? 56.466  18.128  -3.211  1.00 66.56  ? 368 LYS C CD    1 
ATOM   10973 C CE    . LYS C 1 368 ? 57.514  18.577  -4.196  1.00 79.09  ? 368 LYS C CE    1 
ATOM   10974 N NZ    . LYS C 1 368 ? 58.320  19.679  -3.617  1.00 90.58  ? 368 LYS C NZ    1 
ATOM   10975 N N     . GLY C 1 369 ? 51.492  16.321  -4.477  1.00 39.59  ? 369 GLY C N     1 
ATOM   10976 C CA    . GLY C 1 369 ? 50.278  16.716  -3.794  1.00 38.92  ? 369 GLY C CA    1 
ATOM   10977 C C     . GLY C 1 369 ? 50.088  18.227  -3.757  1.00 45.23  ? 369 GLY C C     1 
ATOM   10978 O O     . GLY C 1 369 ? 49.237  18.703  -3.020  1.00 49.56  ? 369 GLY C O     1 
ATOM   10979 N N     . VAL C 1 370 ? 50.844  18.966  -4.579  1.00 46.15  ? 370 VAL C N     1 
ATOM   10980 C CA    . VAL C 1 370 ? 50.738  20.419  -4.621  1.00 47.33  ? 370 VAL C CA    1 
ATOM   10981 C C     . VAL C 1 370 ? 49.685  20.826  -5.657  1.00 46.66  ? 370 VAL C C     1 
ATOM   10982 O O     . VAL C 1 370 ? 49.907  20.765  -6.862  1.00 49.02  ? 370 VAL C O     1 
ATOM   10983 C CB    . VAL C 1 370 ? 52.103  21.078  -4.921  1.00 48.51  ? 370 VAL C CB    1 
ATOM   10984 C CG1   . VAL C 1 370 ? 52.064  22.592  -4.791  1.00 47.16  ? 370 VAL C CG1   1 
ATOM   10985 C CG2   . VAL C 1 370 ? 53.209  20.526  -4.038  1.00 49.64  ? 370 VAL C CG2   1 
ATOM   10986 N N     . PRO C 1 371 ? 48.533  21.371  -5.232  1.00 44.89  ? 371 PRO C N     1 
ATOM   10987 C CA    . PRO C 1 371 ? 47.550  21.878  -6.175  1.00 46.66  ? 371 PRO C CA    1 
ATOM   10988 C C     . PRO C 1 371 ? 48.104  23.139  -6.844  1.00 49.02  ? 371 PRO C C     1 
ATOM   10989 O O     . PRO C 1 371 ? 48.646  24.013  -6.172  1.00 46.00  ? 371 PRO C O     1 
ATOM   10990 C CB    . PRO C 1 371 ? 46.325  22.145  -5.268  1.00 46.43  ? 371 PRO C CB    1 
ATOM   10991 C CG    . PRO C 1 371 ? 46.927  22.546  -3.940  1.00 46.34  ? 371 PRO C CG    1 
ATOM   10992 C CD    . PRO C 1 371 ? 48.195  21.716  -3.839  1.00 48.79  ? 371 PRO C CD    1 
ATOM   10993 N N     . LYS C 1 372 ? 47.965  23.188  -8.174  1.00 56.75  ? 372 LYS C N     1 
ATOM   10994 C CA    . LYS C 1 372 ? 48.433  24.269  -9.027  1.00 58.64  ? 372 LYS C CA    1 
ATOM   10995 C C     . LYS C 1 372 ? 47.394  24.468  -10.127 1.00 66.35  ? 372 LYS C C     1 
ATOM   10996 O O     . LYS C 1 372 ? 46.830  23.490  -10.622 1.00 62.51  ? 372 LYS C O     1 
ATOM   10997 C CB    . LYS C 1 372 ? 49.821  23.956  -9.603  1.00 54.61  ? 372 LYS C CB    1 
ATOM   10998 C CG    . LYS C 1 372 ? 51.002  24.423  -8.757  1.00 59.74  ? 372 LYS C CG    1 
ATOM   10999 C CD    . LYS C 1 372 ? 51.282  25.927  -8.891  1.00 71.03  ? 372 LYS C CD    1 
ATOM   11000 C CE    . LYS C 1 372 ? 52.033  26.527  -7.719  1.00 75.08  ? 372 LYS C CE    1 
ATOM   11001 N NZ    . LYS C 1 372 ? 53.383  25.934  -7.584  1.00 81.80  ? 372 LYS C NZ    1 
ATOM   11002 N N     . LEU C 1 373 ? 47.106  25.746  -10.424 1.00 80.27  ? 373 LEU C N     1 
ATOM   11003 C CA    . LEU C 1 373 ? 46.360  26.176  -11.603 1.00 83.97  ? 373 LEU C CA    1 
ATOM   11004 C C     . LEU C 1 373 ? 47.381  26.575  -12.674 1.00 88.25  ? 373 LEU C C     1 
ATOM   11005 O O     . LEU C 1 373 ? 48.405  27.177  -12.351 1.00 95.57  ? 373 LEU C O     1 
ATOM   11006 C CB    . LEU C 1 373 ? 45.424  27.330  -11.211 1.00 84.43  ? 373 LEU C CB    1 
ATOM   11007 C CG    . LEU C 1 373 ? 46.084  28.511  -10.481 1.00 107.47 ? 373 LEU C CG    1 
ATOM   11008 C CD1   . LEU C 1 373 ? 46.527  29.604  -11.460 1.00 115.77 ? 373 LEU C CD1   1 
ATOM   11009 C CD2   . LEU C 1 373 ? 45.173  29.091  -9.394  1.00 100.11 ? 373 LEU C CD2   1 
ATOM   11010 N N     . THR C 1 374 ? 47.118  26.206  -13.937 1.00 92.98  ? 374 THR C N     1 
ATOM   11011 C CA    . THR C 1 374 ? 48.121  26.235  -15.000 1.00 98.17  ? 374 THR C CA    1 
ATOM   11012 C C     . THR C 1 374 ? 47.821  27.352  -16.005 1.00 94.60  ? 374 THR C C     1 
ATOM   11013 O O     . THR C 1 374 ? 46.659  27.639  -16.274 1.00 87.12  ? 374 THR C O     1 
ATOM   11014 C CB    . THR C 1 374 ? 48.204  24.862  -15.691 1.00 104.75 ? 374 THR C CB    1 
ATOM   11015 O OG1   . THR C 1 374 ? 46.933  24.204  -15.678 1.00 102.21 ? 374 THR C OG1   1 
ATOM   11016 C CG2   . THR C 1 374 ? 49.178  23.924  -15.020 1.00 105.77 ? 374 THR C CG2   1 
ATOM   11017 N N     . GLU C 1 375 ? 48.871  27.963  -16.581 1.00 98.16  ? 375 GLU C N     1 
ATOM   11018 C CA    . GLU C 1 375 ? 48.714  29.058  -17.536 1.00 99.28  ? 375 GLU C CA    1 
ATOM   11019 C C     . GLU C 1 375 ? 48.345  28.498  -18.909 1.00 94.01  ? 375 GLU C C     1 
ATOM   11020 O O     . GLU C 1 375 ? 47.308  28.863  -19.466 1.00 87.54  ? 375 GLU C O     1 
ATOM   11021 C CB    . GLU C 1 375 ? 49.988  29.907  -17.648 1.00 98.45  ? 375 GLU C CB    1 
ATOM   11022 N N     . PHE C 1 376 ? 49.237  27.649  -19.445 1.00 91.30  ? 376 PHE C N     1 
ATOM   11023 C CA    . PHE C 1 376 ? 48.990  26.855  -20.642 1.00 91.03  ? 376 PHE C CA    1 
ATOM   11024 C C     . PHE C 1 376 ? 48.678  25.412  -20.216 1.00 85.43  ? 376 PHE C C     1 
ATOM   11025 O O     . PHE C 1 376 ? 49.168  24.925  -19.199 1.00 73.62  ? 376 PHE C O     1 
ATOM   11026 C CB    . PHE C 1 376 ? 50.167  26.968  -21.626 1.00 76.97  ? 376 PHE C CB    1 
ATOM   11027 N N     . ASN C 1 377 ? 47.789  24.749  -20.965 1.00 84.85  ? 377 ASN C N     1 
ATOM   11028 C CA    . ASN C 1 377 ? 47.506  23.327  -20.809 1.00 76.40  ? 377 ASN C CA    1 
ATOM   11029 C C     . ASN C 1 377 ? 46.596  22.928  -21.969 1.00 64.57  ? 377 ASN C C     1 
ATOM   11030 O O     . ASN C 1 377 ? 46.260  23.759  -22.800 1.00 63.05  ? 377 ASN C O     1 
ATOM   11031 C CB    . ASN C 1 377 ? 46.939  22.973  -19.425 1.00 82.86  ? 377 ASN C CB    1 
ATOM   11032 C CG    . ASN C 1 377 ? 45.453  23.220  -19.256 1.00 84.08  ? 377 ASN C CG    1 
ATOM   11033 O OD1   . ASN C 1 377 ? 44.739  22.318  -18.844 1.00 87.38  ? 377 ASN C OD1   1 
ATOM   11034 N ND2   . ASN C 1 377 ? 44.980  24.430  -19.510 1.00 93.90  ? 377 ASN C ND2   1 
ATOM   11035 N N     . PHE C 1 378 ? 46.169  21.670  -22.009 1.00 61.39  ? 378 PHE C N     1 
ATOM   11036 C CA    . PHE C 1 378 ? 45.455  21.134  -23.155 1.00 56.49  ? 378 PHE C CA    1 
ATOM   11037 C C     . PHE C 1 378 ? 44.190  21.929  -23.486 1.00 59.58  ? 378 PHE C C     1 
ATOM   11038 O O     . PHE C 1 378 ? 43.701  21.862  -24.609 1.00 63.62  ? 378 PHE C O     1 
ATOM   11039 C CB    . PHE C 1 378 ? 45.093  19.672  -22.906 1.00 54.38  ? 378 PHE C CB    1 
ATOM   11040 C CG    . PHE C 1 378 ? 44.078  19.472  -21.821 1.00 50.91  ? 378 PHE C CG    1 
ATOM   11041 C CD1   . PHE C 1 378 ? 42.749  19.712  -22.060 1.00 52.07  ? 378 PHE C CD1   1 
ATOM   11042 C CD2   . PHE C 1 378 ? 44.464  19.077  -20.551 1.00 63.22  ? 378 PHE C CD2   1 
ATOM   11043 C CE1   . PHE C 1 378 ? 41.815  19.543  -21.055 1.00 57.16  ? 378 PHE C CE1   1 
ATOM   11044 C CE2   . PHE C 1 378 ? 43.529  18.898  -19.549 1.00 64.35  ? 378 PHE C CE2   1 
ATOM   11045 C CZ    . PHE C 1 378 ? 42.207  19.144  -19.802 1.00 56.83  ? 378 PHE C CZ    1 
ATOM   11046 N N     . LEU C 1 379 ? 43.640  22.680  -22.532 1.00 58.43  ? 379 LEU C N     1 
ATOM   11047 C CA    . LEU C 1 379 ? 42.565  23.609  -22.847 1.00 57.30  ? 379 LEU C CA    1 
ATOM   11048 C C     . LEU C 1 379 ? 43.010  24.688  -23.846 1.00 55.38  ? 379 LEU C C     1 
ATOM   11049 O O     . LEU C 1 379 ? 42.200  25.126  -24.654 1.00 62.36  ? 379 LEU C O     1 
ATOM   11050 C CB    . LEU C 1 379 ? 42.047  24.220  -21.544 1.00 52.45  ? 379 LEU C CB    1 
ATOM   11051 C CG    . LEU C 1 379 ? 40.989  23.393  -20.825 1.00 54.04  ? 379 LEU C CG    1 
ATOM   11052 C CD1   . LEU C 1 379 ? 40.741  23.913  -19.423 1.00 55.56  ? 379 LEU C CD1   1 
ATOM   11053 C CD2   . LEU C 1 379 ? 39.698  23.407  -21.612 1.00 60.31  ? 379 LEU C CD2   1 
ATOM   11054 N N     . ASN C 1 380 ? 44.297  25.076  -23.826 1.00 65.95  ? 380 ASN C N     1 
ATOM   11055 C CA    . ASN C 1 380 ? 44.830  26.183  -24.623 1.00 70.08  ? 380 ASN C CA    1 
ATOM   11056 C C     . ASN C 1 380 ? 45.440  25.727  -25.947 1.00 65.93  ? 380 ASN C C     1 
ATOM   11057 O O     . ASN C 1 380 ? 45.894  26.556  -26.727 1.00 65.72  ? 380 ASN C O     1 
ATOM   11058 C CB    . ASN C 1 380 ? 45.928  26.946  -23.877 1.00 78.41  ? 380 ASN C CB    1 
ATOM   11059 C CG    . ASN C 1 380 ? 45.358  27.965  -22.917 1.00 102.42 ? 380 ASN C CG    1 
ATOM   11060 O OD1   . ASN C 1 380 ? 44.799  28.972  -23.349 1.00 115.06 ? 380 ASN C OD1   1 
ATOM   11061 N ND2   . ASN C 1 380 ? 45.485  27.710  -21.623 1.00 110.36 ? 380 ASN C ND2   1 
ATOM   11062 N N     . TRP C 1 381 ? 45.454  24.416  -26.213 1.00 56.07  ? 381 TRP C N     1 
ATOM   11063 C CA    . TRP C 1 381 ? 46.199  23.895  -27.337 1.00 51.94  ? 381 TRP C CA    1 
ATOM   11064 C C     . TRP C 1 381 ? 45.685  24.503  -28.648 1.00 56.57  ? 381 TRP C C     1 
ATOM   11065 O O     . TRP C 1 381 ? 46.473  24.708  -29.580 1.00 48.77  ? 381 TRP C O     1 
ATOM   11066 C CB    . TRP C 1 381 ? 46.164  22.350  -27.326 1.00 46.25  ? 381 TRP C CB    1 
ATOM   11067 C CG    . TRP C 1 381 ? 46.806  21.710  -28.522 1.00 42.79  ? 381 TRP C CG    1 
ATOM   11068 C CD1   . TRP C 1 381 ? 46.160  21.168  -29.594 1.00 45.41  ? 381 TRP C CD1   1 
ATOM   11069 C CD2   . TRP C 1 381 ? 48.210  21.612  -28.821 1.00 44.44  ? 381 TRP C CD2   1 
ATOM   11070 N NE1   . TRP C 1 381 ? 47.054  20.705  -30.518 1.00 46.52  ? 381 TRP C NE1   1 
ATOM   11071 C CE2   . TRP C 1 381 ? 48.320  20.975  -30.076 1.00 44.24  ? 381 TRP C CE2   1 
ATOM   11072 C CE3   . TRP C 1 381 ? 49.378  22.044  -28.182 1.00 42.29  ? 381 TRP C CE3   1 
ATOM   11073 C CZ2   . TRP C 1 381 ? 49.545  20.724  -30.683 1.00 42.85  ? 381 TRP C CZ2   1 
ATOM   11074 C CZ3   . TRP C 1 381 ? 50.591  21.787  -28.779 1.00 43.08  ? 381 TRP C CZ3   1 
ATOM   11075 C CH2   . TRP C 1 381 ? 50.673  21.139  -30.013 1.00 43.79  ? 381 TRP C CH2   1 
ATOM   11076 N N     . ASP C 1 382 ? 44.373  24.795  -28.688 1.00 60.64  ? 382 ASP C N     1 
ATOM   11077 C CA    . ASP C 1 382 ? 43.614  24.951  -29.919 1.00 66.67  ? 382 ASP C CA    1 
ATOM   11078 C C     . ASP C 1 382 ? 42.798  26.246  -29.856 1.00 78.14  ? 382 ASP C C     1 
ATOM   11079 O O     . ASP C 1 382 ? 41.708  26.332  -30.423 1.00 74.47  ? 382 ASP C O     1 
ATOM   11080 C CB    . ASP C 1 382 ? 42.713  23.723  -30.097 1.00 75.41  ? 382 ASP C CB    1 
ATOM   11081 C CG    . ASP C 1 382 ? 42.298  23.408  -31.523 1.00 83.33  ? 382 ASP C CG    1 
ATOM   11082 O OD1   . ASP C 1 382 ? 43.052  23.769  -32.461 1.00 70.25  ? 382 ASP C OD1   1 
ATOM   11083 O OD2   . ASP C 1 382 ? 41.212  22.801  -31.680 1.00 101.51 ? 382 ASP C OD2   1 
ATOM   11084 N N     . GLY C 1 383 ? 43.332  27.254  -29.148 1.00 83.66  ? 383 GLY C N     1 
ATOM   11085 C CA    . GLY C 1 383 ? 42.639  28.518  -28.940 1.00 92.33  ? 383 GLY C CA    1 
ATOM   11086 C C     . GLY C 1 383 ? 41.665  28.491  -27.754 1.00 106.37 ? 383 GLY C C     1 
ATOM   11087 O O     . GLY C 1 383 ? 41.195  29.547  -27.326 1.00 92.20  ? 383 GLY C O     1 
ATOM   11088 N N     . GLY C 1 384 ? 41.343  27.290  -27.239 1.00 107.88 ? 384 GLY C N     1 
ATOM   11089 C CA    . GLY C 1 384 ? 40.470  27.164  -26.081 1.00 98.91  ? 384 GLY C CA    1 
ATOM   11090 C C     . GLY C 1 384 ? 39.096  26.566  -26.396 1.00 82.12  ? 384 GLY C C     1 
ATOM   11091 O O     . GLY C 1 384 ? 38.730  26.327  -27.548 1.00 72.94  ? 384 GLY C O     1 
ATOM   11092 N N     . GLY C 1 385 ? 38.349  26.329  -25.318 1.00 66.99  ? 385 GLY C N     1 
ATOM   11093 C CA    . GLY C 1 385 ? 36.952  25.949  -25.393 1.00 74.38  ? 385 GLY C CA    1 
ATOM   11094 C C     . GLY C 1 385 ? 36.559  25.027  -24.233 1.00 76.23  ? 385 GLY C C     1 
ATOM   11095 O O     . GLY C 1 385 ? 36.846  25.319  -23.071 1.00 81.21  ? 385 GLY C O     1 
ATOM   11096 N N     . GLY C 1 386 ? 35.891  23.913  -24.570 1.00 65.75  ? 386 GLY C N     1 
ATOM   11097 C CA    . GLY C 1 386 ? 35.498  22.906  -23.603 1.00 63.58  ? 386 GLY C CA    1 
ATOM   11098 C C     . GLY C 1 386 ? 36.332  21.633  -23.715 1.00 59.13  ? 386 GLY C C     1 
ATOM   11099 O O     . GLY C 1 386 ? 37.151  21.483  -24.616 1.00 49.41  ? 386 GLY C O     1 
ATOM   11100 N N     . HIS C 1 387 ? 36.139  20.721  -22.755 1.00 65.11  ? 387 HIS C N     1 
ATOM   11101 C CA    . HIS C 1 387 ? 36.750  19.410  -22.862 1.00 60.62  ? 387 HIS C CA    1 
ATOM   11102 C C     . HIS C 1 387 ? 35.758  18.347  -22.390 1.00 60.14  ? 387 HIS C C     1 
ATOM   11103 O O     . HIS C 1 387 ? 34.773  18.647  -21.718 1.00 62.97  ? 387 HIS C O     1 
ATOM   11104 C CB    . HIS C 1 387 ? 38.148  19.423  -22.241 1.00 60.00  ? 387 HIS C CB    1 
ATOM   11105 C CG    . HIS C 1 387 ? 38.193  19.234  -20.765 1.00 72.62  ? 387 HIS C CG    1 
ATOM   11106 N ND1   . HIS C 1 387 ? 38.605  18.047  -20.183 1.00 82.90  ? 387 HIS C ND1   1 
ATOM   11107 C CD2   . HIS C 1 387 ? 37.892  20.057  -19.769 1.00 72.21  ? 387 HIS C CD2   1 
ATOM   11108 C CE1   . HIS C 1 387 ? 38.565  18.161  -18.867 1.00 78.14  ? 387 HIS C CE1   1 
ATOM   11109 N NE2   . HIS C 1 387 ? 38.133  19.376  -18.597 1.00 83.52  ? 387 HIS C NE2   1 
ATOM   11110 N N     . VAL C 1 388 ? 35.957  17.135  -22.911 1.00 52.18  ? 388 VAL C N     1 
ATOM   11111 C CA    . VAL C 1 388 ? 35.344  15.931  -22.396 1.00 54.16  ? 388 VAL C CA    1 
ATOM   11112 C C     . VAL C 1 388 ? 36.434  14.888  -22.390 1.00 50.72  ? 388 VAL C C     1 
ATOM   11113 O O     . VAL C 1 388 ? 37.306  14.894  -23.270 1.00 46.40  ? 388 VAL C O     1 
ATOM   11114 C CB    . VAL C 1 388 ? 34.168  15.364  -23.219 1.00 54.56  ? 388 VAL C CB    1 
ATOM   11115 C CG1   . VAL C 1 388 ? 32.886  16.118  -22.971 1.00 57.51  ? 388 VAL C CG1   1 
ATOM   11116 C CG2   . VAL C 1 388 ? 34.487  15.299  -24.700 1.00 57.74  ? 388 VAL C CG2   1 
ATOM   11117 N N     . GLY C 1 389 ? 36.282  14.001  -21.404 1.00 44.94  ? 389 GLY C N     1 
ATOM   11118 C CA    . GLY C 1 389 ? 37.161  12.881  -21.164 1.00 45.79  ? 389 GLY C CA    1 
ATOM   11119 C C     . GLY C 1 389 ? 36.382  11.582  -21.330 1.00 44.32  ? 389 GLY C C     1 
ATOM   11120 O O     . GLY C 1 389 ? 35.166  11.533  -21.145 1.00 41.04  ? 389 GLY C O     1 
ATOM   11121 N N     . PHE C 1 390 ? 37.102  10.555  -21.764 1.00 42.27  ? 390 PHE C N     1 
ATOM   11122 C CA    . PHE C 1 390 ? 36.560  9.218   -21.863 1.00 40.95  ? 390 PHE C CA    1 
ATOM   11123 C C     . PHE C 1 390 ? 37.673  8.322   -21.332 1.00 37.77  ? 390 PHE C C     1 
ATOM   11124 O O     . PHE C 1 390 ? 38.783  8.299   -21.872 1.00 39.29  ? 390 PHE C O     1 
ATOM   11125 C CB    . PHE C 1 390 ? 36.080  8.919   -23.293 1.00 43.45  ? 390 PHE C CB    1 
ATOM   11126 C CG    . PHE C 1 390 ? 35.604  7.497   -23.469 1.00 43.96  ? 390 PHE C CG    1 
ATOM   11127 C CD1   . PHE C 1 390 ? 34.581  7.013   -22.669 1.00 44.83  ? 390 PHE C CD1   1 
ATOM   11128 C CD2   . PHE C 1 390 ? 36.187  6.640   -24.388 1.00 42.25  ? 390 PHE C CD2   1 
ATOM   11129 C CE1   . PHE C 1 390 ? 34.150  5.706   -22.790 1.00 45.49  ? 390 PHE C CE1   1 
ATOM   11130 C CE2   . PHE C 1 390 ? 35.751  5.333   -24.512 1.00 41.43  ? 390 PHE C CE2   1 
ATOM   11131 C CZ    . PHE C 1 390 ? 34.741  4.869   -23.711 1.00 43.86  ? 390 PHE C CZ    1 
ATOM   11132 N N     . SER C 1 391 ? 37.390  7.679   -20.202 1.00 35.55  ? 391 SER C N     1 
ATOM   11133 C CA    . SER C 1 391 ? 38.420  7.052   -19.403 1.00 37.60  ? 391 SER C CA    1 
ATOM   11134 C C     . SER C 1 391 ? 38.045  5.610   -19.050 1.00 36.35  ? 391 SER C C     1 
ATOM   11135 O O     . SER C 1 391 ? 38.181  5.221   -17.910 1.00 39.91  ? 391 SER C O     1 
ATOM   11136 C CB    . SER C 1 391 ? 38.627  7.894   -18.174 1.00 36.27  ? 391 SER C CB    1 
ATOM   11137 O OG    . SER C 1 391 ? 37.375  8.339   -17.671 1.00 39.55  ? 391 SER C OG    1 
ATOM   11138 N N     . PRO C 1 392 ? 37.595  4.742   -19.982 1.00 36.00  ? 392 PRO C N     1 
ATOM   11139 C CA    . PRO C 1 392 ? 37.242  3.357   -19.637 1.00 37.14  ? 392 PRO C CA    1 
ATOM   11140 C C     . PRO C 1 392 ? 38.301  2.462   -19.013 1.00 31.28  ? 392 PRO C C     1 
ATOM   11141 O O     . PRO C 1 392 ? 39.494  2.676   -19.160 1.00 39.11  ? 392 PRO C O     1 
ATOM   11142 C CB    . PRO C 1 392 ? 36.969  2.707   -20.995 1.00 35.05  ? 392 PRO C CB    1 
ATOM   11143 C CG    . PRO C 1 392 ? 37.747  3.561   -21.950 1.00 33.61  ? 392 PRO C CG    1 
ATOM   11144 C CD    . PRO C 1 392 ? 37.502  4.969   -21.426 1.00 35.89  ? 392 PRO C CD    1 
ATOM   11145 N N     . VAL C 1 393 ? 37.840  1.362   -18.443 1.00 34.83  ? 393 VAL C N     1 
ATOM   11146 C CA    . VAL C 1 393 ? 38.738  0.410   -17.822 1.00 32.57  ? 393 VAL C CA    1 
ATOM   11147 C C     . VAL C 1 393 ? 39.045  -0.699  -18.795 1.00 30.88  ? 393 VAL C C     1 
ATOM   11148 O O     . VAL C 1 393 ? 38.177  -1.101  -19.557 1.00 38.77  ? 393 VAL C O     1 
ATOM   11149 C CB    . VAL C 1 393 ? 38.153  -0.187  -16.535 1.00 32.74  ? 393 VAL C CB    1 
ATOM   11150 C CG1   . VAL C 1 393 ? 39.217  -0.905  -15.741 1.00 35.19  ? 393 VAL C CG1   1 
ATOM   11151 C CG2   . VAL C 1 393 ? 37.472  0.874   -15.688 1.00 37.73  ? 393 VAL C CG2   1 
ATOM   11152 N N     . SER C 1 394 ? 40.264  -1.233  -18.641 1.00 35.73  ? 394 SER C N     1 
ATOM   11153 C CA    . SER C 1 394 ? 40.830  -2.295  -19.445 1.00 34.99  ? 394 SER C CA    1 
ATOM   11154 C C     . SER C 1 394 ? 41.927  -2.997  -18.656 1.00 38.52  ? 394 SER C C     1 
ATOM   11155 O O     . SER C 1 394 ? 42.449  -2.484  -17.667 1.00 37.08  ? 394 SER C O     1 
ATOM   11156 C CB    . SER C 1 394 ? 41.416  -1.751  -20.689 1.00 34.34  ? 394 SER C CB    1 
ATOM   11157 O OG    . SER C 1 394 ? 42.354  -0.738  -20.377 1.00 41.85  ? 394 SER C OG    1 
ATOM   11158 N N     . PRO C 1 395 ? 42.276  -4.228  -19.042 1.00 32.10  ? 395 PRO C N     1 
ATOM   11159 C CA    . PRO C 1 395 ? 43.403  -4.901  -18.427 1.00 35.96  ? 395 PRO C CA    1 
ATOM   11160 C C     . PRO C 1 395 ? 44.735  -4.285  -18.862 1.00 34.86  ? 395 PRO C C     1 
ATOM   11161 O O     . PRO C 1 395 ? 44.893  -3.817  -19.979 1.00 32.12  ? 395 PRO C O     1 
ATOM   11162 C CB    . PRO C 1 395 ? 43.300  -6.380  -18.885 1.00 37.55  ? 395 PRO C CB    1 
ATOM   11163 C CG    . PRO C 1 395 ? 41.996  -6.495  -19.691 1.00 35.69  ? 395 PRO C CG    1 
ATOM   11164 C CD    . PRO C 1 395 ? 41.521  -5.072  -19.970 1.00 34.36  ? 395 PRO C CD    1 
ATOM   11165 N N     . ILE C 1 396 ? 45.739  -4.414  -17.995 1.00 38.10  ? 396 ILE C N     1 
ATOM   11166 C CA    . ILE C 1 396 ? 47.052  -3.883  -18.283 1.00 37.32  ? 396 ILE C CA    1 
ATOM   11167 C C     . ILE C 1 396 ? 47.736  -4.861  -19.216 1.00 35.60  ? 396 ILE C C     1 
ATOM   11168 O O     . ILE C 1 396 ? 48.423  -5.777  -18.784 1.00 39.96  ? 396 ILE C O     1 
ATOM   11169 C CB    . ILE C 1 396 ? 47.884  -3.601  -17.015 1.00 35.48  ? 396 ILE C CB    1 
ATOM   11170 C CG1   . ILE C 1 396 ? 47.085  -2.848  -15.948 1.00 31.94  ? 396 ILE C CG1   1 
ATOM   11171 C CG2   . ILE C 1 396 ? 49.145  -2.839  -17.389 1.00 36.59  ? 396 ILE C CG2   1 
ATOM   11172 C CD1   . ILE C 1 396 ? 47.640  -2.971  -14.512 1.00 32.64  ? 396 ILE C CD1   1 
ATOM   11173 N N     . THR C 1 397 ? 47.559  -4.583  -20.508 1.00 41.38  ? 397 THR C N     1 
ATOM   11174 C CA    . THR C 1 397 ? 48.052  -5.419  -21.598 1.00 38.28  ? 397 THR C CA    1 
ATOM   11175 C C     . THR C 1 397 ? 48.450  -4.546  -22.786 1.00 37.03  ? 397 THR C C     1 
ATOM   11176 O O     . THR C 1 397 ? 47.710  -3.678  -23.230 1.00 33.75  ? 397 THR C O     1 
ATOM   11177 C CB    . THR C 1 397 ? 46.982  -6.477  -21.865 1.00 38.68  ? 397 THR C CB    1 
ATOM   11178 O OG1   . THR C 1 397 ? 47.351  -7.654  -21.145 1.00 36.97  ? 397 THR C OG1   1 
ATOM   11179 C CG2   . THR C 1 397 ? 46.749  -6.789  -23.311 1.00 37.43  ? 397 THR C CG2   1 
ATOM   11180 N N     . GLY C 1 398 ? 49.664  -4.763  -23.288 1.00 44.14  ? 398 GLY C N     1 
ATOM   11181 C CA    . GLY C 1 398 ? 50.087  -4.140  -24.534 1.00 42.36  ? 398 GLY C CA    1 
ATOM   11182 C C     . GLY C 1 398 ? 48.986  -4.167  -25.588 1.00 40.82  ? 398 GLY C C     1 
ATOM   11183 O O     . GLY C 1 398 ? 48.571  -3.128  -26.101 1.00 48.06  ? 398 GLY C O     1 
ATOM   11184 N N     . LYS C 1 399 ? 48.508  -5.378  -25.851 1.00 41.55  ? 399 LYS C N     1 
ATOM   11185 C CA    . LYS C 1 399 ? 47.408  -5.647  -26.770 1.00 47.27  ? 399 LYS C CA    1 
ATOM   11186 C C     . LYS C 1 399 ? 46.225  -4.705  -26.514 1.00 40.79  ? 399 LYS C C     1 
ATOM   11187 O O     . LYS C 1 399 ? 45.724  -4.116  -27.454 1.00 42.28  ? 399 LYS C O     1 
ATOM   11188 C CB    . LYS C 1 399 ? 47.125  -7.159  -26.716 1.00 49.71  ? 399 LYS C CB    1 
ATOM   11189 C CG    . LYS C 1 399 ? 45.746  -7.657  -27.121 1.00 67.41  ? 399 LYS C CG    1 
ATOM   11190 C CD    . LYS C 1 399 ? 45.536  -7.761  -28.624 1.00 86.13  ? 399 LYS C CD    1 
ATOM   11191 C CE    . LYS C 1 399 ? 44.192  -8.365  -28.980 1.00 88.42  ? 399 LYS C CE    1 
ATOM   11192 N NZ    . LYS C 1 399 ? 43.624  -7.717  -30.184 1.00 87.53  ? 399 LYS C NZ    1 
ATOM   11193 N N     . ASP C 1 400 ? 45.770  -4.525  -25.269 1.00 38.39  ? 400 ASP C N     1 
ATOM   11194 C CA    . ASP C 1 400 ? 44.597  -3.703  -25.027 1.00 40.14  ? 400 ASP C CA    1 
ATOM   11195 C C     . ASP C 1 400 ? 45.000  -2.233  -25.120 1.00 38.97  ? 400 ASP C C     1 
ATOM   11196 O O     . ASP C 1 400 ? 44.219  -1.402  -25.579 1.00 37.53  ? 400 ASP C O     1 
ATOM   11197 C CB    . ASP C 1 400 ? 43.961  -3.978  -23.657 1.00 46.19  ? 400 ASP C CB    1 
ATOM   11198 C CG    . ASP C 1 400 ? 43.295  -5.342  -23.499 1.00 45.35  ? 400 ASP C CG    1 
ATOM   11199 O OD1   . ASP C 1 400 ? 42.143  -5.494  -23.953 1.00 44.04  ? 400 ASP C OD1   1 
ATOM   11200 O OD2   . ASP C 1 400 ? 43.936  -6.245  -22.906 1.00 39.20  ? 400 ASP C OD2   1 
ATOM   11201 N N     . ALA C 1 401 ? 46.224  -1.920  -24.684 1.00 41.26  ? 401 ALA C N     1 
ATOM   11202 C CA    . ALA C 1 401 ? 46.752  -0.566  -24.766 1.00 41.80  ? 401 ALA C CA    1 
ATOM   11203 C C     . ALA C 1 401 ? 46.804  -0.071  -26.209 1.00 42.62  ? 401 ALA C C     1 
ATOM   11204 O O     . ALA C 1 401 ? 46.392  1.048   -26.472 1.00 46.35  ? 401 ALA C O     1 
ATOM   11205 C CB    . ALA C 1 401 ? 48.103  -0.495  -24.128 1.00 42.78  ? 401 ALA C CB    1 
ATOM   11206 N N     . ILE C 1 402 ? 47.268  -0.888  -27.157 1.00 43.34  ? 402 ILE C N     1 
ATOM   11207 C CA    . ILE C 1 402 ? 47.450  -0.433  -28.541 1.00 43.66  ? 402 ILE C CA    1 
ATOM   11208 C C     . ILE C 1 402 ? 46.112  -0.440  -29.295 1.00 44.46  ? 402 ILE C C     1 
ATOM   11209 O O     . ILE C 1 402 ? 45.809  0.450   -30.079 1.00 44.56  ? 402 ILE C O     1 
ATOM   11210 C CB    . ILE C 1 402 ? 48.538  -1.282  -29.239 1.00 47.14  ? 402 ILE C CB    1 
ATOM   11211 C CG1   . ILE C 1 402 ? 49.022  -0.677  -30.560 1.00 53.54  ? 402 ILE C CG1   1 
ATOM   11212 C CG2   . ILE C 1 402 ? 48.082  -2.720  -29.445 1.00 48.05  ? 402 ILE C CG2   1 
ATOM   11213 C CD1   . ILE C 1 402 ? 50.081  0.367   -30.419 1.00 50.84  ? 402 ILE C CD1   1 
ATOM   11214 N N     . LYS C 1 403 ? 45.258  -1.427  -29.043 1.00 44.67  ? 403 LYS C N     1 
ATOM   11215 C CA    . LYS C 1 403 ? 43.969  -1.439  -29.696 1.00 43.10  ? 403 LYS C CA    1 
ATOM   11216 C C     . LYS C 1 403 ? 43.229  -0.142  -29.412 1.00 40.88  ? 403 LYS C C     1 
ATOM   11217 O O     . LYS C 1 403 ? 42.540  0.391   -30.269 1.00 48.01  ? 403 LYS C O     1 
ATOM   11218 C CB    . LYS C 1 403 ? 43.080  -2.602  -29.254 1.00 45.77  ? 403 LYS C CB    1 
ATOM   11219 C CG    . LYS C 1 403 ? 41.830  -2.772  -30.119 1.00 49.27  ? 403 LYS C CG    1 
ATOM   11220 C CD    . LYS C 1 403 ? 40.765  -3.567  -29.441 1.00 61.63  ? 403 LYS C CD    1 
ATOM   11221 C CE    . LYS C 1 403 ? 41.214  -4.970  -29.066 1.00 70.39  ? 403 LYS C CE    1 
ATOM   11222 N NZ    . LYS C 1 403 ? 40.389  -5.553  -27.975 1.00 63.90  ? 403 LYS C NZ    1 
ATOM   11223 N N     . GLN C 1 404 ? 43.313  0.352   -28.188 1.00 42.02  ? 404 GLN C N     1 
ATOM   11224 C CA    . GLN C 1 404 ? 42.513  1.511   -27.837 1.00 40.93  ? 404 GLN C CA    1 
ATOM   11225 C C     . GLN C 1 404 ? 43.126  2.756   -28.487 1.00 36.36  ? 404 GLN C C     1 
ATOM   11226 O O     . GLN C 1 404 ? 42.433  3.532   -29.087 1.00 41.51  ? 404 GLN C O     1 
ATOM   11227 C CB    . GLN C 1 404 ? 42.362  1.588   -26.315 1.00 38.36  ? 404 GLN C CB    1 
ATOM   11228 C CG    . GLN C 1 404 ? 41.588  0.433   -25.714 1.00 38.33  ? 404 GLN C CG    1 
ATOM   11229 C CD    . GLN C 1 404 ? 41.342  0.620   -24.235 1.00 42.34  ? 404 GLN C CD    1 
ATOM   11230 O OE1   . GLN C 1 404 ? 42.075  0.117   -23.392 1.00 44.36  ? 404 GLN C OE1   1 
ATOM   11231 N NE2   . GLN C 1 404 ? 40.331  1.396   -23.902 1.00 46.85  ? 404 GLN C NE2   1 
ATOM   11232 N N     . TYR C 1 405 ? 44.441  2.926   -28.409 1.00 39.02  ? 405 TYR C N     1 
ATOM   11233 C CA    . TYR C 1 405 ? 45.152  3.940   -29.169 1.00 40.05  ? 405 TYR C CA    1 
ATOM   11234 C C     . TYR C 1 405 ? 44.690  4.004   -30.628 1.00 34.62  ? 405 TYR C C     1 
ATOM   11235 O O     . TYR C 1 405 ? 44.406  5.100   -31.125 1.00 35.18  ? 405 TYR C O     1 
ATOM   11236 C CB    . TYR C 1 405 ? 46.668  3.694   -29.146 1.00 39.56  ? 405 TYR C CB    1 
ATOM   11237 C CG    . TYR C 1 405 ? 47.417  4.619   -30.057 1.00 41.02  ? 405 TYR C CG    1 
ATOM   11238 C CD1   . TYR C 1 405 ? 47.456  5.976   -29.802 1.00 49.72  ? 405 TYR C CD1   1 
ATOM   11239 C CD2   . TYR C 1 405 ? 47.953  4.170   -31.251 1.00 51.61  ? 405 TYR C CD2   1 
ATOM   11240 C CE1   . TYR C 1 405 ? 48.077  6.858   -30.678 1.00 56.62  ? 405 TYR C CE1   1 
ATOM   11241 C CE2   . TYR C 1 405 ? 48.586  5.039   -32.131 1.00 60.09  ? 405 TYR C CE2   1 
ATOM   11242 C CZ    . TYR C 1 405 ? 48.645  6.393   -31.849 1.00 57.32  ? 405 TYR C CZ    1 
ATOM   11243 O OH    . TYR C 1 405 ? 49.295  7.265   -32.686 1.00 62.05  ? 405 TYR C OH    1 
ATOM   11244 N N     . ASN C 1 406 ? 44.671  2.866   -31.327 1.00 33.91  ? 406 ASN C N     1 
ATOM   11245 C CA    . ASN C 1 406 ? 44.364  2.856   -32.762 1.00 40.53  ? 406 ASN C CA    1 
ATOM   11246 C C     . ASN C 1 406 ? 42.890  3.170   -32.988 1.00 42.84  ? 406 ASN C C     1 
ATOM   11247 O O     . ASN C 1 406 ? 42.558  4.015   -33.824 1.00 47.96  ? 406 ASN C O     1 
ATOM   11248 C CB    . ASN C 1 406 ? 44.733  1.541   -33.462 1.00 41.62  ? 406 ASN C CB    1 
ATOM   11249 C CG    . ASN C 1 406 ? 46.234  1.319   -33.545 1.00 44.82  ? 406 ASN C CG    1 
ATOM   11250 O OD1   . ASN C 1 406 ? 47.005  2.250   -33.787 1.00 48.34  ? 406 ASN C OD1   1 
ATOM   11251 N ND2   . ASN C 1 406 ? 46.677  0.103   -33.284 1.00 46.58  ? 406 ASN C ND2   1 
ATOM   11252 N N     . MET C 1 407 ? 42.020  2.544   -32.188 1.00 41.51  ? 407 MET C N     1 
ATOM   11253 C CA    . MET C 1 407 ? 40.581  2.775   -32.286 1.00 45.81  ? 407 MET C CA    1 
ATOM   11254 C C     . MET C 1 407 ? 40.222  4.257   -32.153 1.00 41.97  ? 407 MET C C     1 
ATOM   11255 O O     . MET C 1 407 ? 39.278  4.723   -32.784 1.00 44.53  ? 407 MET C O     1 
ATOM   11256 C CB    . MET C 1 407 ? 39.829  2.101   -31.144 1.00 46.86  ? 407 MET C CB    1 
ATOM   11257 C CG    . MET C 1 407 ? 39.469  0.711   -31.390 1.00 52.67  ? 407 MET C CG    1 
ATOM   11258 S SD    . MET C 1 407 ? 38.846  0.135   -29.817 1.00 44.62  ? 407 MET C SD    1 
ATOM   11259 C CE    . MET C 1 407 ? 37.088  0.397   -30.020 1.00 37.79  ? 407 MET C CE    1 
ATOM   11260 N N     . VAL C 1 408 ? 40.871  4.927   -31.202 1.00 40.19  ? 408 VAL C N     1 
ATOM   11261 C CA    . VAL C 1 408 ? 40.427  6.223   -30.706 1.00 47.20  ? 408 VAL C CA    1 
ATOM   11262 C C     . VAL C 1 408 ? 41.049  7.320   -31.556 1.00 42.62  ? 408 VAL C C     1 
ATOM   11263 O O     . VAL C 1 408 ? 40.329  8.106   -32.159 1.00 45.07  ? 408 VAL C O     1 
ATOM   11264 C CB    . VAL C 1 408 ? 40.782  6.417   -29.222 1.00 42.33  ? 408 VAL C CB    1 
ATOM   11265 C CG1   . VAL C 1 408 ? 40.457  7.819   -28.755 1.00 41.13  ? 408 VAL C CG1   1 
ATOM   11266 C CG2   . VAL C 1 408 ? 40.064  5.397   -28.352 1.00 45.85  ? 408 VAL C CG2   1 
ATOM   11267 N N     . SER C 1 409 ? 42.382  7.284   -31.643 1.00 42.01  ? 409 SER C N     1 
ATOM   11268 C CA    . SER C 1 409 ? 43.111  8.222   -32.464 1.00 45.04  ? 409 SER C CA    1 
ATOM   11269 C C     . SER C 1 409 ? 42.579  8.226   -33.900 1.00 45.97  ? 409 SER C C     1 
ATOM   11270 O O     . SER C 1 409 ? 42.526  9.298   -34.487 1.00 46.76  ? 409 SER C O     1 
ATOM   11271 C CB    . SER C 1 409 ? 44.604  8.010   -32.400 1.00 45.16  ? 409 SER C CB    1 
ATOM   11272 O OG    . SER C 1 409 ? 44.987  6.837   -33.075 1.00 44.68  ? 409 SER C OG    1 
ATOM   11273 N N     . SER C 1 410 ? 42.190  7.080   -34.476 1.00 47.20  ? 410 SER C N     1 
ATOM   11274 C CA    . SER C 1 410 ? 41.636  7.072   -35.836 1.00 45.88  ? 410 SER C CA    1 
ATOM   11275 C C     . SER C 1 410 ? 40.384  7.929   -35.897 1.00 43.94  ? 410 SER C C     1 
ATOM   11276 O O     . SER C 1 410 ? 40.258  8.799   -36.754 1.00 48.81  ? 410 SER C O     1 
ATOM   11277 C CB    . SER C 1 410 ? 41.292  5.705   -36.308 1.00 47.88  ? 410 SER C CB    1 
ATOM   11278 O OG    . SER C 1 410 ? 42.461  4.914   -36.267 1.00 67.52  ? 410 SER C OG    1 
ATOM   11279 N N     . ARG C 1 411 ? 39.463  7.680   -34.975 1.00 41.85  ? 411 ARG C N     1 
ATOM   11280 C CA    . ARG C 1 411 ? 38.200  8.385   -35.008 1.00 43.85  ? 411 ARG C CA    1 
ATOM   11281 C C     . ARG C 1 411 ? 38.454  9.838   -34.662 1.00 41.58  ? 411 ARG C C     1 
ATOM   11282 O O     . ARG C 1 411 ? 37.881  10.707  -35.281 1.00 45.89  ? 411 ARG C O     1 
ATOM   11283 C CB    . ARG C 1 411 ? 37.210  7.836   -33.980 1.00 48.91  ? 411 ARG C CB    1 
ATOM   11284 C CG    . ARG C 1 411 ? 36.732  6.425   -34.266 1.00 52.43  ? 411 ARG C CG    1 
ATOM   11285 C CD    . ARG C 1 411 ? 35.622  6.472   -35.270 1.00 53.17  ? 411 ARG C CD    1 
ATOM   11286 N NE    . ARG C 1 411 ? 34.912  5.224   -35.452 1.00 47.78  ? 411 ARG C NE    1 
ATOM   11287 C CZ    . ARG C 1 411 ? 34.146  5.007   -36.509 1.00 50.14  ? 411 ARG C CZ    1 
ATOM   11288 N NH1   . ARG C 1 411 ? 34.011  5.972   -37.401 1.00 44.83  ? 411 ARG C NH1   1 
ATOM   11289 N NH2   . ARG C 1 411 ? 33.499  3.863   -36.656 1.00 53.34  ? 411 ARG C NH2   1 
ATOM   11290 N N     . VAL C 1 412 ? 39.218  10.091  -33.599 1.00 40.24  ? 412 VAL C N     1 
ATOM   11291 C CA    . VAL C 1 412 ? 39.303  11.452  -33.109 1.00 44.97  ? 412 VAL C CA    1 
ATOM   11292 C C     . VAL C 1 412 ? 39.910  12.311  -34.220 1.00 42.25  ? 412 VAL C C     1 
ATOM   11293 O O     . VAL C 1 412 ? 39.463  13.416  -34.445 1.00 37.46  ? 412 VAL C O     1 
ATOM   11294 C CB    . VAL C 1 412 ? 40.085  11.571  -31.784 1.00 44.17  ? 412 VAL C CB    1 
ATOM   11295 C CG1   . VAL C 1 412 ? 40.341  13.016  -31.430 1.00 50.67  ? 412 VAL C CG1   1 
ATOM   11296 C CG2   . VAL C 1 412 ? 39.366  10.932  -30.621 1.00 45.47  ? 412 VAL C CG2   1 
ATOM   11297 N N     . ARG C 1 413 ? 40.906  11.771  -34.921 1.00 44.19  ? 413 ARG C N     1 
ATOM   11298 C CA    . ARG C 1 413 ? 41.585  12.477  -35.995 1.00 49.37  ? 413 ARG C CA    1 
ATOM   11299 C C     . ARG C 1 413 ? 40.643  12.632  -37.184 1.00 50.72  ? 413 ARG C C     1 
ATOM   11300 O O     . ARG C 1 413 ? 40.541  13.718  -37.747 1.00 55.85  ? 413 ARG C O     1 
ATOM   11301 C CB    . ARG C 1 413 ? 42.946  11.834  -36.313 1.00 45.70  ? 413 ARG C CB    1 
ATOM   11302 C CG    . ARG C 1 413 ? 44.020  12.231  -35.299 1.00 52.85  ? 413 ARG C CG    1 
ATOM   11303 C CD    . ARG C 1 413 ? 45.341  11.477  -35.282 1.00 56.04  ? 413 ARG C CD    1 
ATOM   11304 N NE    . ARG C 1 413 ? 46.069  11.555  -36.544 1.00 65.93  ? 413 ARG C NE    1 
ATOM   11305 C CZ    . ARG C 1 413 ? 46.837  12.560  -36.967 1.00 66.87  ? 413 ARG C CZ    1 
ATOM   11306 N NH1   . ARG C 1 413 ? 47.082  13.615  -36.210 1.00 68.61  ? 413 ARG C NH1   1 
ATOM   11307 N NH2   . ARG C 1 413 ? 47.394  12.481  -38.162 1.00 69.29  ? 413 ARG C NH2   1 
ATOM   11308 N N     . GLU C 1 414 ? 39.882  11.598  -37.513 1.00 56.03  ? 414 GLU C N     1 
ATOM   11309 C CA    . GLU C 1 414 ? 39.007  11.691  -38.673 1.00 60.84  ? 414 GLU C CA    1 
ATOM   11310 C C     . GLU C 1 414 ? 37.987  12.800  -38.442 1.00 50.97  ? 414 GLU C C     1 
ATOM   11311 O O     . GLU C 1 414 ? 37.459  13.362  -39.391 1.00 52.78  ? 414 GLU C O     1 
ATOM   11312 C CB    . GLU C 1 414 ? 38.302  10.367  -39.004 1.00 64.62  ? 414 GLU C CB    1 
ATOM   11313 C CG    . GLU C 1 414 ? 37.838  10.306  -40.459 1.00 71.94  ? 414 GLU C CG    1 
ATOM   11314 C CD    . GLU C 1 414 ? 36.774  9.277   -40.813 1.00 77.76  ? 414 GLU C CD    1 
ATOM   11315 O OE1   . GLU C 1 414 ? 37.113  8.076   -40.925 1.00 83.46  ? 414 GLU C OE1   1 
ATOM   11316 O OE2   . GLU C 1 414 ? 35.604  9.680   -40.976 1.00 62.71  ? 414 GLU C OE2   1 
ATOM   11317 N N     . TYR C 1 415 ? 37.719  13.116  -37.178 1.00 44.13  ? 415 TYR C N     1 
ATOM   11318 C CA    . TYR C 1 415 ? 36.695  14.090  -36.851 1.00 44.08  ? 415 TYR C CA    1 
ATOM   11319 C C     . TYR C 1 415 ? 37.248  15.515  -36.862 1.00 44.91  ? 415 TYR C C     1 
ATOM   11320 O O     . TYR C 1 415 ? 36.478  16.446  -36.687 1.00 49.28  ? 415 TYR C O     1 
ATOM   11321 C CB    . TYR C 1 415 ? 36.057  13.752  -35.493 1.00 39.67  ? 415 TYR C CB    1 
ATOM   11322 C CG    . TYR C 1 415 ? 34.826  12.902  -35.647 1.00 36.40  ? 415 TYR C CG    1 
ATOM   11323 C CD1   . TYR C 1 415 ? 34.939  11.572  -36.014 1.00 38.61  ? 415 TYR C CD1   1 
ATOM   11324 C CD2   . TYR C 1 415 ? 33.560  13.420  -35.469 1.00 31.85  ? 415 TYR C CD2   1 
ATOM   11325 C CE1   . TYR C 1 415 ? 33.822  10.775  -36.202 1.00 37.87  ? 415 TYR C CE1   1 
ATOM   11326 C CE2   . TYR C 1 415 ? 32.434  12.632  -35.650 1.00 36.28  ? 415 TYR C CE2   1 
ATOM   11327 C CZ    . TYR C 1 415 ? 32.557  11.306  -36.032 1.00 35.58  ? 415 TYR C CZ    1 
ATOM   11328 O OH    . TYR C 1 415 ? 31.459  10.489  -36.272 1.00 34.07  ? 415 TYR C OH    1 
ATOM   11329 N N     . GLY C 1 416 ? 38.573  15.688  -36.999 1.00 48.94  ? 416 GLY C N     1 
ATOM   11330 C CA    . GLY C 1 416 ? 39.190  17.008  -37.069 1.00 48.23  ? 416 GLY C CA    1 
ATOM   11331 C C     . GLY C 1 416 ? 39.917  17.453  -35.796 1.00 48.00  ? 416 GLY C C     1 
ATOM   11332 O O     . GLY C 1 416 ? 40.473  18.540  -35.761 1.00 51.09  ? 416 GLY C O     1 
ATOM   11333 N N     . PHE C 1 417 ? 39.919  16.628  -34.751 1.00 47.01  ? 417 PHE C N     1 
ATOM   11334 C CA    . PHE C 1 417 ? 40.482  17.010  -33.470 1.00 44.47  ? 417 PHE C CA    1 
ATOM   11335 C C     . PHE C 1 417 ? 41.904  16.480  -33.340 1.00 49.25  ? 417 PHE C C     1 
ATOM   11336 O O     . PHE C 1 417 ? 42.307  15.527  -33.999 1.00 54.81  ? 417 PHE C O     1 
ATOM   11337 C CB    . PHE C 1 417 ? 39.615  16.420  -32.368 1.00 43.64  ? 417 PHE C CB    1 
ATOM   11338 C CG    . PHE C 1 417 ? 38.191  16.916  -32.368 1.00 41.90  ? 417 PHE C CG    1 
ATOM   11339 C CD1   . PHE C 1 417 ? 37.888  18.214  -32.000 1.00 41.00  ? 417 PHE C CD1   1 
ATOM   11340 C CD2   . PHE C 1 417 ? 37.146  16.074  -32.673 1.00 39.95  ? 417 PHE C CD2   1 
ATOM   11341 C CE1   . PHE C 1 417 ? 36.577  18.651  -31.948 1.00 41.97  ? 417 PHE C CE1   1 
ATOM   11342 C CE2   . PHE C 1 417 ? 35.831  16.514  -32.642 1.00 43.48  ? 417 PHE C CE2   1 
ATOM   11343 C CZ    . PHE C 1 417 ? 35.546  17.802  -32.274 1.00 46.56  ? 417 PHE C CZ    1 
ATOM   11344 N N     . ASP C 1 418 ? 42.686  17.075  -32.447 1.00 59.11  ? 418 ASP C N     1 
ATOM   11345 C CA    . ASP C 1 418 ? 43.969  16.471  -32.118 1.00 56.99  ? 418 ASP C CA    1 
ATOM   11346 C C     . ASP C 1 418 ? 43.720  15.319  -31.132 1.00 51.33  ? 418 ASP C C     1 
ATOM   11347 O O     . ASP C 1 418 ? 42.916  15.439  -30.192 1.00 46.30  ? 418 ASP C O     1 
ATOM   11348 C CB    . ASP C 1 418 ? 44.976  17.520  -31.623 1.00 57.14  ? 418 ASP C CB    1 
ATOM   11349 C CG    . ASP C 1 418 ? 45.812  18.168  -32.715 1.00 58.81  ? 418 ASP C CG    1 
ATOM   11350 O OD1   . ASP C 1 418 ? 46.524  17.412  -33.437 1.00 51.58  ? 418 ASP C OD1   1 
ATOM   11351 O OD2   . ASP C 1 418 ? 45.770  19.431  -32.818 1.00 53.34  ? 418 ASP C OD2   1 
ATOM   11352 N N     . TYR C 1 419 ? 44.412  14.202  -31.379 1.00 42.27  ? 419 TYR C N     1 
ATOM   11353 C CA    . TYR C 1 419 ? 44.444  13.089  -30.450 1.00 42.02  ? 419 TYR C CA    1 
ATOM   11354 C C     . TYR C 1 419 ? 45.313  13.446  -29.257 1.00 36.86  ? 419 TYR C C     1 
ATOM   11355 O O     . TYR C 1 419 ? 46.530  13.680  -29.378 1.00 39.30  ? 419 TYR C O     1 
ATOM   11356 C CB    . TYR C 1 419 ? 45.008  11.790  -31.050 1.00 43.69  ? 419 TYR C CB    1 
ATOM   11357 C CG    . TYR C 1 419 ? 45.234  10.698  -30.028 1.00 42.43  ? 419 TYR C CG    1 
ATOM   11358 C CD1   . TYR C 1 419 ? 44.164  10.052  -29.383 1.00 42.30  ? 419 TYR C CD1   1 
ATOM   11359 C CD2   . TYR C 1 419 ? 46.523  10.349  -29.658 1.00 39.41  ? 419 TYR C CD2   1 
ATOM   11360 C CE1   . TYR C 1 419 ? 44.376  9.065   -28.430 1.00 43.44  ? 419 TYR C CE1   1 
ATOM   11361 C CE2   . TYR C 1 419 ? 46.758  9.363   -28.711 1.00 40.70  ? 419 TYR C CE2   1 
ATOM   11362 C CZ    . TYR C 1 419 ? 45.688  8.727   -28.099 1.00 45.27  ? 419 TYR C CZ    1 
ATOM   11363 O OH    . TYR C 1 419 ? 46.010  7.784   -27.177 1.00 43.25  ? 419 TYR C OH    1 
ATOM   11364 N N     . MET C 1 420 ? 44.657  13.394  -28.103 1.00 38.15  ? 420 MET C N     1 
ATOM   11365 C CA    . MET C 1 420 ? 45.276  13.646  -26.803 1.00 42.09  ? 420 MET C CA    1 
ATOM   11366 C C     . MET C 1 420 ? 44.927  12.456  -25.923 1.00 41.87  ? 420 MET C C     1 
ATOM   11367 O O     . MET C 1 420 ? 43.772  12.206  -25.598 1.00 39.33  ? 420 MET C O     1 
ATOM   11368 C CB    . MET C 1 420 ? 44.703  14.914  -26.167 1.00 38.82  ? 420 MET C CB    1 
ATOM   11369 C CG    . MET C 1 420 ? 45.283  16.164  -26.756 1.00 45.06  ? 420 MET C CG    1 
ATOM   11370 S SD    . MET C 1 420 ? 44.362  17.602  -26.230 1.00 48.76  ? 420 MET C SD    1 
ATOM   11371 C CE    . MET C 1 420 ? 45.014  18.858  -27.326 1.00 52.61  ? 420 MET C CE    1 
ATOM   11372 N N     . GLY C 1 421 ? 45.912  11.638  -25.637 1.00 48.54  ? 421 GLY C N     1 
ATOM   11373 C CA    . GLY C 1 421 ? 45.598  10.339  -25.085 1.00 49.84  ? 421 GLY C CA    1 
ATOM   11374 C C     . GLY C 1 421 ? 46.579  10.027  -23.979 1.00 48.13  ? 421 GLY C C     1 
ATOM   11375 O O     . GLY C 1 421 ? 47.746  10.424  -24.052 1.00 51.36  ? 421 GLY C O     1 
ATOM   11376 N N     . LEU C 1 422 ? 46.068  9.305   -22.994 1.00 49.23  ? 422 LEU C N     1 
ATOM   11377 C CA    . LEU C 1 422 ? 46.821  8.966   -21.801 1.00 54.19  ? 422 LEU C CA    1 
ATOM   11378 C C     . LEU C 1 422 ? 46.550  7.485   -21.487 1.00 50.51  ? 422 LEU C C     1 
ATOM   11379 O O     . LEU C 1 422 ? 45.405  7.039   -21.587 1.00 45.90  ? 422 LEU C O     1 
ATOM   11380 C CB    . LEU C 1 422 ? 46.268  9.955   -20.774 1.00 53.70  ? 422 LEU C CB    1 
ATOM   11381 C CG    . LEU C 1 422 ? 46.877  9.977   -19.389 1.00 62.31  ? 422 LEU C CG    1 
ATOM   11382 C CD1   . LEU C 1 422 ? 46.591  11.314  -18.726 1.00 65.32  ? 422 LEU C CD1   1 
ATOM   11383 C CD2   . LEU C 1 422 ? 46.307  8.865   -18.549 1.00 63.29  ? 422 LEU C CD2   1 
ATOM   11384 N N     . LEU C 1 423 ? 47.600  6.700   -21.205 1.00 42.72  ? 423 LEU C N     1 
ATOM   11385 C CA    . LEU C 1 423 ? 47.418  5.387   -20.603 1.00 43.25  ? 423 LEU C CA    1 
ATOM   11386 C C     . LEU C 1 423 ? 47.780  5.413   -19.125 1.00 41.82  ? 423 LEU C C     1 
ATOM   11387 O O     . LEU C 1 423 ? 48.964  5.496   -18.796 1.00 44.94  ? 423 LEU C O     1 
ATOM   11388 C CB    . LEU C 1 423 ? 48.207  4.340   -21.388 1.00 45.83  ? 423 LEU C CB    1 
ATOM   11389 C CG    . LEU C 1 423 ? 47.524  4.049   -22.726 1.00 54.33  ? 423 LEU C CG    1 
ATOM   11390 C CD1   . LEU C 1 423 ? 48.343  4.598   -23.868 1.00 54.75  ? 423 LEU C CD1   1 
ATOM   11391 C CD2   . LEU C 1 423 ? 47.201  2.579   -22.914 1.00 52.67  ? 423 LEU C CD2   1 
ATOM   11392 N N     . ALA C 1 424 ? 46.731  5.327   -18.278 1.00 38.76  ? 424 ALA C N     1 
ATOM   11393 C CA    . ALA C 1 424 ? 46.810  5.426   -16.822 1.00 43.14  ? 424 ALA C CA    1 
ATOM   11394 C C     . ALA C 1 424 ? 46.583  4.068   -16.139 1.00 44.52  ? 424 ALA C C     1 
ATOM   11395 O O     . ALA C 1 424 ? 45.555  3.430   -16.343 1.00 48.12  ? 424 ALA C O     1 
ATOM   11396 C CB    . ALA C 1 424 ? 45.811  6.443   -16.309 1.00 39.44  ? 424 ALA C CB    1 
ATOM   11397 N N     . ILE C 1 425 ? 47.518  3.669   -15.268 1.00 41.18  ? 425 ILE C N     1 
ATOM   11398 C CA    . ILE C 1 425 ? 47.358  2.494   -14.431 1.00 42.74  ? 425 ILE C CA    1 
ATOM   11399 C C     . ILE C 1 425 ? 47.307  2.920   -12.970 1.00 39.37  ? 425 ILE C C     1 
ATOM   11400 O O     . ILE C 1 425 ? 48.298  3.454   -12.495 1.00 43.96  ? 425 ILE C O     1 
ATOM   11401 C CB    . ILE C 1 425 ? 48.535  1.518   -14.619 1.00 43.27  ? 425 ILE C CB    1 
ATOM   11402 C CG1   . ILE C 1 425 ? 48.812  1.152   -16.070 1.00 40.28  ? 425 ILE C CG1   1 
ATOM   11403 C CG2   . ILE C 1 425 ? 48.335  0.275   -13.760 1.00 46.46  ? 425 ILE C CG2   1 
ATOM   11404 C CD1   . ILE C 1 425 ? 50.145  0.470   -16.252 1.00 37.98  ? 425 ILE C CD1   1 
ATOM   11405 N N     . GLY C 1 426 ? 46.222  2.623   -12.236 1.00 46.38  ? 426 GLY C N     1 
ATOM   11406 C CA    . GLY C 1 426 ? 46.226  2.734   -10.777 1.00 50.11  ? 426 GLY C CA    1 
ATOM   11407 C C     . GLY C 1 426 ? 46.948  1.561   -10.089 1.00 57.64  ? 426 GLY C C     1 
ATOM   11408 O O     . GLY C 1 426 ? 48.171  1.584   -9.875  1.00 71.26  ? 426 GLY C O     1 
ATOM   11409 N N     . TRP C 1 427 ? 46.160  0.545   -9.715  1.00 56.09  ? 427 TRP C N     1 
ATOM   11410 C CA    . TRP C 1 427 ? 46.633  -0.738  -9.216  1.00 57.90  ? 427 TRP C CA    1 
ATOM   11411 C C     . TRP C 1 427 ? 45.912  -1.835  -10.003 1.00 63.75  ? 427 TRP C C     1 
ATOM   11412 O O     . TRP C 1 427 ? 44.697  -2.032  -9.837  1.00 90.88  ? 427 TRP C O     1 
ATOM   11413 C CB    . TRP C 1 427 ? 46.292  -0.830  -7.709  1.00 51.09  ? 427 TRP C CB    1 
ATOM   11414 C CG    . TRP C 1 427 ? 47.055  -1.853  -6.932  1.00 51.51  ? 427 TRP C CG    1 
ATOM   11415 C CD1   . TRP C 1 427 ? 48.200  -2.487  -7.316  1.00 48.01  ? 427 TRP C CD1   1 
ATOM   11416 C CD2   . TRP C 1 427 ? 46.747  -2.332  -5.608  1.00 54.30  ? 427 TRP C CD2   1 
ATOM   11417 N NE1   . TRP C 1 427 ? 48.631  -3.317  -6.321  1.00 49.44  ? 427 TRP C NE1   1 
ATOM   11418 C CE2   . TRP C 1 427 ? 47.768  -3.241  -5.261  1.00 50.94  ? 427 TRP C CE2   1 
ATOM   11419 C CE3   . TRP C 1 427 ? 45.736  -2.063  -4.671  1.00 49.25  ? 427 TRP C CE3   1 
ATOM   11420 C CZ2   . TRP C 1 427 ? 47.790  -3.897  -4.030  1.00 54.54  ? 427 TRP C CZ2   1 
ATOM   11421 C CZ3   . TRP C 1 427 ? 45.771  -2.695  -3.448  1.00 46.53  ? 427 TRP C CZ3   1 
ATOM   11422 C CH2   . TRP C 1 427 ? 46.785  -3.602  -3.138  1.00 51.99  ? 427 TRP C CH2   1 
ATOM   11423 N N     . ARG C 1 428 ? 46.599  -2.521  -10.905 1.00 46.41  ? 428 ARG C N     1 
ATOM   11424 C CA    . ARG C 1 428 ? 45.922  -3.574  -11.683 1.00 47.62  ? 428 ARG C CA    1 
ATOM   11425 C C     . ARG C 1 428 ? 44.977  -3.095  -12.795 1.00 38.54  ? 428 ARG C C     1 
ATOM   11426 O O     . ARG C 1 428 ? 44.554  -3.933  -13.600 1.00 32.82  ? 428 ARG C O     1 
ATOM   11427 C CB    . ARG C 1 428 ? 45.082  -4.543  -10.830 1.00 44.25  ? 428 ARG C CB    1 
ATOM   11428 C CG    . ARG C 1 428 ? 45.892  -5.464  -9.927  1.00 42.62  ? 428 ARG C CG    1 
ATOM   11429 C CD    . ARG C 1 428 ? 45.061  -6.315  -8.992  1.00 44.94  ? 428 ARG C CD    1 
ATOM   11430 N NE    . ARG C 1 428 ? 45.663  -6.227  -7.673  1.00 53.64  ? 428 ARG C NE    1 
ATOM   11431 C CZ    . ARG C 1 428 ? 46.446  -7.155  -7.200  1.00 43.44  ? 428 ARG C CZ    1 
ATOM   11432 N NH1   . ARG C 1 428 ? 47.166  -6.965  -6.129  1.00 50.65  ? 428 ARG C NH1   1 
ATOM   11433 N NH2   . ARG C 1 428 ? 46.540  -8.270  -7.865  1.00 50.26  ? 428 ARG C NH2   1 
ATOM   11434 N N     . ASP C 1 429 ? 44.688  -1.788  -12.894 1.00 35.54  ? 429 ASP C N     1 
ATOM   11435 C CA    . ASP C 1 429 ? 43.669  -1.302  -13.813 1.00 41.28  ? 429 ASP C CA    1 
ATOM   11436 C C     . ASP C 1 429 ? 44.245  -0.261  -14.786 1.00 39.35  ? 429 ASP C C     1 
ATOM   11437 O O     . ASP C 1 429 ? 44.616  0.834   -14.391 1.00 40.32  ? 429 ASP C O     1 
ATOM   11438 C CB    . ASP C 1 429 ? 42.468  -0.730  -13.036 1.00 40.02  ? 429 ASP C CB    1 
ATOM   11439 C CG    . ASP C 1 429 ? 42.801  0.466   -12.158 1.00 43.10  ? 429 ASP C CG    1 
ATOM   11440 O OD1   . ASP C 1 429 ? 43.780  0.382   -11.364 1.00 41.93  ? 429 ASP C OD1   1 
ATOM   11441 O OD2   . ASP C 1 429 ? 42.104  1.490   -12.289 1.00 44.88  ? 429 ASP C OD2   1 
ATOM   11442 N N     . LEU C 1 430 ? 44.203  -0.584  -16.083 1.00 40.07  ? 430 LEU C N     1 
ATOM   11443 C CA    . LEU C 1 430 ? 44.548  0.306   -17.181 1.00 36.59  ? 430 LEU C CA    1 
ATOM   11444 C C     . LEU C 1 430 ? 43.358  1.155   -17.614 1.00 38.75  ? 430 LEU C C     1 
ATOM   11445 O O     . LEU C 1 430 ? 42.244  0.658   -17.735 1.00 37.74  ? 430 LEU C O     1 
ATOM   11446 C CB    . LEU C 1 430 ? 45.017  -0.538  -18.371 1.00 39.36  ? 430 LEU C CB    1 
ATOM   11447 C CG    . LEU C 1 430 ? 45.492  0.274   -19.572 1.00 41.72  ? 430 LEU C CG    1 
ATOM   11448 C CD1   . LEU C 1 430 ? 46.835  0.920   -19.264 1.00 39.87  ? 430 LEU C CD1   1 
ATOM   11449 C CD2   . LEU C 1 430 ? 45.577  -0.585  -20.825 1.00 37.14  ? 430 LEU C CD2   1 
ATOM   11450 N N     . HIS C 1 431 ? 43.606  2.452   -17.838 1.00 40.58  ? 431 HIS C N     1 
ATOM   11451 C CA    . HIS C 1 431 ? 42.658  3.307   -18.521 1.00 37.62  ? 431 HIS C CA    1 
ATOM   11452 C C     . HIS C 1 431 ? 43.341  3.960   -19.721 1.00 39.11  ? 431 HIS C C     1 
ATOM   11453 O O     . HIS C 1 431 ? 44.357  4.620   -19.552 1.00 32.80  ? 431 HIS C O     1 
ATOM   11454 C CB    . HIS C 1 431 ? 42.138  4.403   -17.604 1.00 39.23  ? 431 HIS C CB    1 
ATOM   11455 C CG    . HIS C 1 431 ? 41.460  3.920   -16.371 1.00 37.46  ? 431 HIS C CG    1 
ATOM   11456 N ND1   . HIS C 1 431 ? 42.136  3.339   -15.325 1.00 36.74  ? 431 HIS C ND1   1 
ATOM   11457 C CD2   . HIS C 1 431 ? 40.180  3.989   -15.988 1.00 36.08  ? 431 HIS C CD2   1 
ATOM   11458 C CE1   . HIS C 1 431 ? 41.269  3.047   -14.366 1.00 35.72  ? 431 HIS C CE1   1 
ATOM   11459 N NE2   . HIS C 1 431 ? 40.081  3.400   -14.760 1.00 34.83  ? 431 HIS C NE2   1 
ATOM   11460 N N     . HIS C 1 432 ? 42.763  3.750   -20.925 1.00 41.22  ? 432 HIS C N     1 
ATOM   11461 C CA    . HIS C 1 432 ? 42.949  4.627   -22.069 1.00 35.51  ? 432 HIS C CA    1 
ATOM   11462 C C     . HIS C 1 432 ? 42.073  5.872   -21.917 1.00 38.37  ? 432 HIS C C     1 
ATOM   11463 O O     . HIS C 1 432 ? 40.866  5.820   -22.164 1.00 46.20  ? 432 HIS C O     1 
ATOM   11464 C CB    . HIS C 1 432 ? 42.643  3.951   -23.409 1.00 38.23  ? 432 HIS C CB    1 
ATOM   11465 C CG    . HIS C 1 432 ? 43.058  4.857   -24.538 1.00 38.47  ? 432 HIS C CG    1 
ATOM   11466 N ND1   . HIS C 1 432 ? 42.202  5.718   -25.184 1.00 32.18  ? 432 HIS C ND1   1 
ATOM   11467 C CD2   . HIS C 1 432 ? 44.297  5.125   -24.991 1.00 38.36  ? 432 HIS C CD2   1 
ATOM   11468 C CE1   . HIS C 1 432 ? 42.914  6.469   -26.002 1.00 42.22  ? 432 HIS C CE1   1 
ATOM   11469 N NE2   . HIS C 1 432 ? 44.186  6.117   -25.907 1.00 38.81  ? 432 HIS C NE2   1 
ATOM   11470 N N     . VAL C 1 433 ? 42.702  6.982   -21.491 1.00 36.56  ? 433 VAL C N     1 
ATOM   11471 C CA    . VAL C 1 433 ? 42.025  8.246   -21.257 1.00 39.43  ? 433 VAL C CA    1 
ATOM   11472 C C     . VAL C 1 433 ? 42.225  9.138   -22.480 1.00 44.28  ? 433 VAL C C     1 
ATOM   11473 O O     . VAL C 1 433 ? 43.357  9.535   -22.772 1.00 47.93  ? 433 VAL C O     1 
ATOM   11474 C CB    . VAL C 1 433 ? 42.528  8.973   -19.990 1.00 37.87  ? 433 VAL C CB    1 
ATOM   11475 C CG1   . VAL C 1 433 ? 41.817  10.283  -19.759 1.00 34.05  ? 433 VAL C CG1   1 
ATOM   11476 C CG2   . VAL C 1 433 ? 42.408  8.124   -18.747 1.00 38.96  ? 433 VAL C CG2   1 
ATOM   11477 N N     . THR C 1 434 ? 41.088  9.446   -23.122 1.00 41.96  ? 434 THR C N     1 
ATOM   11478 C CA    . THR C 1 434 ? 40.954  10.341  -24.248 1.00 45.96  ? 434 THR C CA    1 
ATOM   11479 C C     . THR C 1 434 ? 40.518  11.721  -23.737 1.00 47.20  ? 434 THR C C     1 
ATOM   11480 O O     . THR C 1 434 ? 39.496  11.851  -23.057 1.00 48.64  ? 434 THR C O     1 
ATOM   11481 C CB    . THR C 1 434 ? 39.944  9.731   -25.237 1.00 51.11  ? 434 THR C CB    1 
ATOM   11482 O OG1   . THR C 1 434 ? 40.331  8.396   -25.572 1.00 57.33  ? 434 THR C OG1   1 
ATOM   11483 C CG2   . THR C 1 434 ? 39.797  10.536  -26.511 1.00 54.58  ? 434 THR C CG2   1 
ATOM   11484 N N     . VAL C 1 435 ? 41.287  12.765  -24.081 1.00 51.85  ? 435 VAL C N     1 
ATOM   11485 C CA    . VAL C 1 435 ? 40.828  14.144  -23.954 1.00 49.67  ? 435 VAL C CA    1 
ATOM   11486 C C     . VAL C 1 435 ? 40.530  14.709  -25.339 1.00 48.39  ? 435 VAL C C     1 
ATOM   11487 O O     . VAL C 1 435 ? 41.322  14.577  -26.282 1.00 51.61  ? 435 VAL C O     1 
ATOM   11488 C CB    . VAL C 1 435 ? 41.845  15.029  -23.229 1.00 51.61  ? 435 VAL C CB    1 
ATOM   11489 C CG1   . VAL C 1 435 ? 41.157  16.265  -22.692 1.00 57.65  ? 435 VAL C CG1   1 
ATOM   11490 C CG2   . VAL C 1 435 ? 42.536  14.273  -22.110 1.00 55.11  ? 435 VAL C CG2   1 
ATOM   11491 N N     . ILE C 1 436 ? 39.336  15.283  -25.454 1.00 49.27  ? 436 ILE C N     1 
ATOM   11492 C CA    . ILE C 1 436 ? 38.943  16.002  -26.652 1.00 57.13  ? 436 ILE C CA    1 
ATOM   11493 C C     . ILE C 1 436 ? 38.621  17.462  -26.302 1.00 54.01  ? 436 ILE C C     1 
ATOM   11494 O O     . ILE C 1 436 ? 37.764  17.768  -25.473 1.00 50.74  ? 436 ILE C O     1 
ATOM   11495 C CB    . ILE C 1 436 ? 37.757  15.305  -27.339 1.00 54.91  ? 436 ILE C CB    1 
ATOM   11496 C CG1   . ILE C 1 436 ? 37.909  13.783  -27.352 1.00 53.71  ? 436 ILE C CG1   1 
ATOM   11497 C CG2   . ILE C 1 436 ? 37.564  15.869  -28.739 1.00 57.25  ? 436 ILE C CG2   1 
ATOM   11498 C CD1   . ILE C 1 436 ? 36.637  13.074  -27.748 1.00 48.34  ? 436 ILE C CD1   1 
ATOM   11499 N N     . VAL C 1 437 ? 39.315  18.379  -26.964 1.00 53.29  ? 437 VAL C N     1 
ATOM   11500 C CA    . VAL C 1 437 ? 39.122  19.796  -26.730 1.00 48.04  ? 437 VAL C CA    1 
ATOM   11501 C C     . VAL C 1 437 ? 38.392  20.334  -27.939 1.00 42.84  ? 437 VAL C C     1 
ATOM   11502 O O     . VAL C 1 437 ? 38.770  20.047  -29.058 1.00 44.95  ? 437 VAL C O     1 
ATOM   11503 C CB    . VAL C 1 437 ? 40.477  20.477  -26.535 1.00 51.04  ? 437 VAL C CB    1 
ATOM   11504 C CG1   . VAL C 1 437 ? 40.320  21.975  -26.364 1.00 68.72  ? 437 VAL C CG1   1 
ATOM   11505 C CG2   . VAL C 1 437 ? 41.223  19.857  -25.356 1.00 45.84  ? 437 VAL C CG2   1 
ATOM   11506 N N     . TYR C 1 438 ? 37.326  21.078  -27.702 1.00 49.59  ? 438 TYR C N     1 
ATOM   11507 C CA    . TYR C 1 438 ? 36.480  21.561  -28.775 1.00 49.44  ? 438 TYR C CA    1 
ATOM   11508 C C     . TYR C 1 438 ? 36.150  23.021  -28.503 1.00 56.24  ? 438 TYR C C     1 
ATOM   11509 O O     . TYR C 1 438 ? 36.232  23.457  -27.365 1.00 55.71  ? 438 TYR C O     1 
ATOM   11510 C CB    . TYR C 1 438 ? 35.217  20.709  -28.854 1.00 49.62  ? 438 TYR C CB    1 
ATOM   11511 C CG    . TYR C 1 438 ? 34.388  20.629  -27.597 1.00 50.54  ? 438 TYR C CG    1 
ATOM   11512 C CD1   . TYR C 1 438 ? 34.887  20.090  -26.428 1.00 49.56  ? 438 TYR C CD1   1 
ATOM   11513 C CD2   . TYR C 1 438 ? 33.070  21.049  -27.594 1.00 52.24  ? 438 TYR C CD2   1 
ATOM   11514 C CE1   . TYR C 1 438 ? 34.101  20.000  -25.289 1.00 64.29  ? 438 TYR C CE1   1 
ATOM   11515 C CE2   . TYR C 1 438 ? 32.268  20.961  -26.465 1.00 55.32  ? 438 TYR C CE2   1 
ATOM   11516 C CZ    . TYR C 1 438 ? 32.782  20.435  -25.298 1.00 62.07  ? 438 TYR C CZ    1 
ATOM   11517 O OH    . TYR C 1 438 ? 32.007  20.359  -24.152 1.00 59.89  ? 438 TYR C OH    1 
ATOM   11518 N N     . ASP C 1 439 ? 35.775  23.766  -29.542 1.00 63.10  ? 439 ASP C N     1 
ATOM   11519 C CA    . ASP C 1 439 ? 35.194  25.081  -29.342 1.00 64.18  ? 439 ASP C CA    1 
ATOM   11520 C C     . ASP C 1 439 ? 33.729  24.919  -28.947 1.00 57.61  ? 439 ASP C C     1 
ATOM   11521 O O     . ASP C 1 439 ? 32.906  24.550  -29.767 1.00 56.23  ? 439 ASP C O     1 
ATOM   11522 C CB    . ASP C 1 439 ? 35.324  25.955  -30.591 1.00 66.63  ? 439 ASP C CB    1 
ATOM   11523 C CG    . ASP C 1 439 ? 34.709  27.338  -30.441 1.00 74.58  ? 439 ASP C CG    1 
ATOM   11524 O OD1   . ASP C 1 439 ? 34.004  27.593  -29.421 1.00 70.35  ? 439 ASP C OD1   1 
ATOM   11525 O OD2   . ASP C 1 439 ? 34.937  28.148  -31.343 1.00 79.52  ? 439 ASP C OD2   1 
ATOM   11526 N N     . LYS C 1 440 ? 33.396  25.287  -27.714 1.00 60.60  ? 440 LYS C N     1 
ATOM   11527 C CA    . LYS C 1 440 ? 32.056  25.070  -27.197 1.00 68.38  ? 440 LYS C CA    1 
ATOM   11528 C C     . LYS C 1 440 ? 31.086  26.101  -27.767 1.00 71.18  ? 440 LYS C C     1 
ATOM   11529 O O     . LYS C 1 440 ? 29.883  25.900  -27.642 1.00 71.55  ? 440 LYS C O     1 
ATOM   11530 C CB    . LYS C 1 440 ? 32.063  25.106  -25.662 1.00 74.46  ? 440 LYS C CB    1 
ATOM   11531 C CG    . LYS C 1 440 ? 32.644  26.380  -25.061 1.00 85.34  ? 440 LYS C CG    1 
ATOM   11532 C CD    . LYS C 1 440 ? 32.815  26.377  -23.560 1.00 90.21  ? 440 LYS C CD    1 
ATOM   11533 C CE    . LYS C 1 440 ? 33.797  27.432  -23.086 1.00 88.92  ? 440 LYS C CE    1 
ATOM   11534 N NZ    . LYS C 1 440 ? 33.505  28.762  -23.672 1.00 83.79  ? 440 LYS C NZ    1 
ATOM   11535 N N     . THR C 1 441 ? 31.597  27.181  -28.394 1.00 79.32  ? 441 THR C N     1 
ATOM   11536 C CA    . THR C 1 441 ? 30.767  28.318  -28.799 1.00 81.23  ? 441 THR C CA    1 
ATOM   11537 C C     . THR C 1 441 ? 30.261  28.141  -30.232 1.00 85.92  ? 441 THR C C     1 
ATOM   11538 O O     . THR C 1 441 ? 29.759  29.092  -30.826 1.00 98.68  ? 441 THR C O     1 
ATOM   11539 C CB    . THR C 1 441 ? 31.507  29.668  -28.728 1.00 74.60  ? 441 THR C CB    1 
ATOM   11540 O OG1   . THR C 1 441 ? 32.303  29.877  -29.900 1.00 72.37  ? 441 THR C OG1   1 
ATOM   11541 C CG2   . THR C 1 441 ? 32.404  29.817  -27.517 1.00 72.83  ? 441 THR C CG2   1 
ATOM   11542 N N     . ASP C 1 442 ? 30.388  26.919  -30.767 1.00 79.48  ? 442 ASP C N     1 
ATOM   11543 C CA    . ASP C 1 442 ? 30.172  26.620  -32.172 1.00 67.56  ? 442 ASP C CA    1 
ATOM   11544 C C     . ASP C 1 442 ? 29.256  25.407  -32.248 1.00 69.15  ? 442 ASP C C     1 
ATOM   11545 O O     . ASP C 1 442 ? 29.711  24.298  -32.001 1.00 64.31  ? 442 ASP C O     1 
ATOM   11546 C CB    . ASP C 1 442 ? 31.514  26.342  -32.859 1.00 62.72  ? 442 ASP C CB    1 
ATOM   11547 C CG    . ASP C 1 442 ? 31.461  26.024  -34.353 1.00 68.18  ? 442 ASP C CG    1 
ATOM   11548 O OD1   . ASP C 1 442 ? 30.353  25.727  -34.865 1.00 71.40  ? 442 ASP C OD1   1 
ATOM   11549 O OD2   . ASP C 1 442 ? 32.545  26.071  -35.008 1.00 62.97  ? 442 ASP C OD2   1 
ATOM   11550 N N     . PRO C 1 443 ? 27.953  25.557  -32.572 1.00 70.98  ? 443 PRO C N     1 
ATOM   11551 C CA    . PRO C 1 443 ? 27.043  24.411  -32.629 1.00 70.82  ? 443 PRO C CA    1 
ATOM   11552 C C     . PRO C 1 443 ? 27.522  23.283  -33.542 1.00 72.23  ? 443 PRO C C     1 
ATOM   11553 O O     . PRO C 1 443 ? 27.196  22.113  -33.316 1.00 62.41  ? 443 PRO C O     1 
ATOM   11554 C CB    . PRO C 1 443 ? 25.740  25.015  -33.161 1.00 64.24  ? 443 PRO C CB    1 
ATOM   11555 C CG    . PRO C 1 443 ? 25.812  26.441  -32.693 1.00 71.92  ? 443 PRO C CG    1 
ATOM   11556 C CD    . PRO C 1 443 ? 27.270  26.824  -32.855 1.00 71.76  ? 443 PRO C CD    1 
ATOM   11557 N N     . ASP C 1 444 ? 28.303  23.646  -34.568 1.00 62.18  ? 444 ASP C N     1 
ATOM   11558 C CA    . ASP C 1 444 ? 28.771  22.655  -35.514 1.00 59.85  ? 444 ASP C CA    1 
ATOM   11559 C C     . ASP C 1 444 ? 29.799  21.773  -34.817 1.00 52.63  ? 444 ASP C C     1 
ATOM   11560 O O     . ASP C 1 444 ? 29.718  20.550  -34.908 1.00 49.17  ? 444 ASP C O     1 
ATOM   11561 C CB    . ASP C 1 444 ? 29.227  23.307  -36.821 1.00 66.77  ? 444 ASP C CB    1 
ATOM   11562 C CG    . ASP C 1 444 ? 28.046  23.740  -37.681 1.00 73.55  ? 444 ASP C CG    1 
ATOM   11563 O OD1   . ASP C 1 444 ? 27.195  22.863  -37.995 1.00 69.59  ? 444 ASP C OD1   1 
ATOM   11564 O OD2   . ASP C 1 444 ? 27.969  24.946  -38.012 1.00 70.40  ? 444 ASP C OD2   1 
ATOM   11565 N N     . GLU C 1 445 ? 30.717  22.385  -34.061 1.00 50.03  ? 445 GLU C N     1 
ATOM   11566 C CA    . GLU C 1 445 ? 31.730  21.615  -33.357 1.00 51.78  ? 445 GLU C CA    1 
ATOM   11567 C C     . GLU C 1 445 ? 31.126  20.800  -32.205 1.00 48.79  ? 445 GLU C C     1 
ATOM   11568 O O     . GLU C 1 445 ? 31.640  19.734  -31.897 1.00 47.90  ? 445 GLU C O     1 
ATOM   11569 C CB    . GLU C 1 445 ? 32.850  22.554  -32.955 1.00 58.05  ? 445 GLU C CB    1 
ATOM   11570 C CG    . GLU C 1 445 ? 33.829  22.776  -34.088 1.00 61.44  ? 445 GLU C CG    1 
ATOM   11571 C CD    . GLU C 1 445 ? 35.110  22.000  -33.867 1.00 73.14  ? 445 GLU C CD    1 
ATOM   11572 O OE1   . GLU C 1 445 ? 35.729  22.180  -32.762 1.00 70.18  ? 445 GLU C OE1   1 
ATOM   11573 O OE2   . GLU C 1 445 ? 35.484  21.224  -34.776 1.00 76.97  ? 445 GLU C OE2   1 
ATOM   11574 N N     . ARG C 1 446 ? 29.977  21.226  -31.663 1.00 47.55  ? 446 ARG C N     1 
ATOM   11575 C CA    . ARG C 1 446 ? 29.277  20.509  -30.601 1.00 50.38  ? 446 ARG C CA    1 
ATOM   11576 C C     . ARG C 1 446 ? 28.653  19.201  -31.100 1.00 52.71  ? 446 ARG C C     1 
ATOM   11577 O O     . ARG C 1 446 ? 28.663  18.202  -30.382 1.00 51.10  ? 446 ARG C O     1 
ATOM   11578 C CB    . ARG C 1 446 ? 28.186  21.382  -29.952 1.00 53.33  ? 446 ARG C CB    1 
ATOM   11579 C CG    . ARG C 1 446 ? 28.701  22.502  -29.043 1.00 58.42  ? 446 ARG C CG    1 
ATOM   11580 C CD    . ARG C 1 446 ? 27.674  23.129  -28.102 1.00 59.09  ? 446 ARG C CD    1 
ATOM   11581 N NE    . ARG C 1 446 ? 26.511  23.707  -28.775 1.00 69.49  ? 446 ARG C NE    1 
ATOM   11582 C CZ    . ARG C 1 446 ? 26.181  25.001  -28.798 1.00 68.63  ? 446 ARG C CZ    1 
ATOM   11583 N NH1   . ARG C 1 446 ? 26.978  25.910  -28.270 1.00 59.68  ? 446 ARG C NH1   1 
ATOM   11584 N NH2   . ARG C 1 446 ? 25.058  25.390  -29.382 1.00 79.20  ? 446 ARG C NH2   1 
ATOM   11585 N N     . LYS C 1 447 ? 28.041  19.214  -32.291 1.00 56.41  ? 447 LYS C N     1 
ATOM   11586 C CA    . LYS C 1 447 ? 27.321  18.046  -32.758 1.00 53.30  ? 447 LYS C CA    1 
ATOM   11587 C C     . LYS C 1 447 ? 28.366  16.993  -33.087 1.00 48.82  ? 447 LYS C C     1 
ATOM   11588 O O     . LYS C 1 447 ? 28.223  15.828  -32.737 1.00 50.03  ? 447 LYS C O     1 
ATOM   11589 C CB    . LYS C 1 447 ? 26.429  18.349  -33.969 1.00 59.98  ? 447 LYS C CB    1 
ATOM   11590 C CG    . LYS C 1 447 ? 25.515  17.189  -34.351 1.00 64.51  ? 447 LYS C CG    1 
ATOM   11591 C CD    . LYS C 1 447 ? 24.307  17.581  -35.174 1.00 78.65  ? 447 LYS C CD    1 
ATOM   11592 C CE    . LYS C 1 447 ? 22.985  17.082  -34.609 1.00 86.42  ? 447 LYS C CE    1 
ATOM   11593 N NZ    . LYS C 1 447 ? 22.979  15.624  -34.327 1.00 82.52  ? 447 LYS C NZ    1 
ATOM   11594 N N     . LYS C 1 448 ? 29.424  17.451  -33.751 1.00 46.49  ? 448 LYS C N     1 
ATOM   11595 C CA    . LYS C 1 448 ? 30.598  16.643  -34.023 1.00 49.79  ? 448 LYS C CA    1 
ATOM   11596 C C     . LYS C 1 448 ? 31.114  15.961  -32.756 1.00 45.27  ? 448 LYS C C     1 
ATOM   11597 O O     . LYS C 1 448 ? 31.323  14.747  -32.753 1.00 43.35  ? 448 LYS C O     1 
ATOM   11598 C CB    . LYS C 1 448 ? 31.696  17.518  -34.636 1.00 49.53  ? 448 LYS C CB    1 
ATOM   11599 C CG    . LYS C 1 448 ? 31.489  17.802  -36.116 1.00 58.18  ? 448 LYS C CG    1 
ATOM   11600 C CD    . LYS C 1 448 ? 32.545  18.698  -36.733 1.00 58.03  ? 448 LYS C CD    1 
ATOM   11601 C CE    . LYS C 1 448 ? 33.941  18.175  -36.513 1.00 52.28  ? 448 LYS C CE    1 
ATOM   11602 N NZ    . LYS C 1 448 ? 34.910  18.904  -37.349 1.00 51.53  ? 448 LYS C NZ    1 
ATOM   11603 N N     . LEU C 1 449 ? 31.389  16.755  -31.714 1.00 40.85  ? 449 LEU C N     1 
ATOM   11604 C CA    . LEU C 1 449 ? 31.860  16.205  -30.446 1.00 46.90  ? 449 LEU C CA    1 
ATOM   11605 C C     . LEU C 1 449 ? 30.916  15.125  -29.930 1.00 40.06  ? 449 LEU C C     1 
ATOM   11606 O O     . LEU C 1 449 ? 31.327  14.008  -29.657 1.00 38.78  ? 449 LEU C O     1 
ATOM   11607 C CB    . LEU C 1 449 ? 31.970  17.281  -29.370 1.00 45.16  ? 449 LEU C CB    1 
ATOM   11608 C CG    . LEU C 1 449 ? 32.600  16.733  -28.101 1.00 48.93  ? 449 LEU C CG    1 
ATOM   11609 C CD1   . LEU C 1 449 ? 34.099  16.865  -28.196 1.00 48.07  ? 449 LEU C CD1   1 
ATOM   11610 C CD2   . LEU C 1 449 ? 32.048  17.400  -26.858 1.00 51.81  ? 449 LEU C CD2   1 
ATOM   11611 N N     . ASP C 1 450 ? 29.634  15.463  -29.837 1.00 41.90  ? 450 ASP C N     1 
ATOM   11612 C CA    . ASP C 1 450 ? 28.669  14.581  -29.216 1.00 43.13  ? 450 ASP C CA    1 
ATOM   11613 C C     . ASP C 1 450 ? 28.661  13.236  -29.950 1.00 42.04  ? 450 ASP C C     1 
ATOM   11614 O O     . ASP C 1 450 ? 28.725  12.173  -29.336 1.00 45.95  ? 450 ASP C O     1 
ATOM   11615 C CB    . ASP C 1 450 ? 27.348  15.339  -29.117 1.00 48.98  ? 450 ASP C CB    1 
ATOM   11616 C CG    . ASP C 1 450 ? 26.225  14.539  -28.503 1.00 54.41  ? 450 ASP C CG    1 
ATOM   11617 O OD1   . ASP C 1 450 ? 26.353  14.122  -27.320 1.00 59.18  ? 450 ASP C OD1   1 
ATOM   11618 O OD2   . ASP C 1 450 ? 25.226  14.380  -29.202 1.00 52.85  ? 450 ASP C OD2   1 
ATOM   11619 N N     . GLU C 1 451 ? 28.675  13.293  -31.280 1.00 38.23  ? 451 GLU C N     1 
ATOM   11620 C CA    . GLU C 1 451 ? 28.624  12.114  -32.109 1.00 37.04  ? 451 GLU C CA    1 
ATOM   11621 C C     . GLU C 1 451 ? 29.935  11.351  -31.979 1.00 42.17  ? 451 GLU C C     1 
ATOM   11622 O O     . GLU C 1 451 ? 29.916  10.140  -31.786 1.00 52.06  ? 451 GLU C O     1 
ATOM   11623 C CB    . GLU C 1 451 ? 28.309  12.530  -33.551 1.00 40.98  ? 451 GLU C CB    1 
ATOM   11624 C CG    . GLU C 1 451 ? 28.585  11.451  -34.577 1.00 40.13  ? 451 GLU C CG    1 
ATOM   11625 C CD    . GLU C 1 451 ? 28.414  11.937  -35.995 1.00 42.28  ? 451 GLU C CD    1 
ATOM   11626 O OE1   . GLU C 1 451 ? 27.310  12.426  -36.295 1.00 45.94  ? 451 GLU C OE1   1 
ATOM   11627 O OE2   . GLU C 1 451 ? 29.389  11.831  -36.767 1.00 42.31  ? 451 GLU C OE2   1 
ATOM   11628 N N     . LEU C 1 452 ? 31.079  12.038  -32.058 1.00 40.75  ? 452 LEU C N     1 
ATOM   11629 C CA    . LEU C 1 452 ? 32.328  11.345  -31.788 1.00 41.75  ? 452 LEU C CA    1 
ATOM   11630 C C     . LEU C 1 452 ? 32.221  10.626  -30.449 1.00 38.56  ? 452 LEU C C     1 
ATOM   11631 O O     . LEU C 1 452 ? 32.524  9.440   -30.354 1.00 41.60  ? 452 LEU C O     1 
ATOM   11632 C CB    . LEU C 1 452 ? 33.508  12.315  -31.797 1.00 41.71  ? 452 LEU C CB    1 
ATOM   11633 C CG    . LEU C 1 452 ? 34.853  11.711  -31.391 1.00 40.54  ? 452 LEU C CG    1 
ATOM   11634 C CD1   . LEU C 1 452 ? 35.206  10.463  -32.185 1.00 39.40  ? 452 LEU C CD1   1 
ATOM   11635 C CD2   . LEU C 1 452 ? 35.940  12.739  -31.570 1.00 34.76  ? 452 LEU C CD2   1 
ATOM   11636 N N     . PHE C 1 453 ? 31.747  11.311  -29.411 1.00 36.81  ? 453 PHE C N     1 
ATOM   11637 C CA    . PHE C 1 453 ? 31.862  10.718  -28.083 1.00 38.21  ? 453 PHE C CA    1 
ATOM   11638 C C     . PHE C 1 453 ? 31.044  9.428   -28.008 1.00 42.60  ? 453 PHE C C     1 
ATOM   11639 O O     . PHE C 1 453 ? 31.549  8.400   -27.540 1.00 41.22  ? 453 PHE C O     1 
ATOM   11640 C CB    . PHE C 1 453 ? 31.436  11.695  -27.000 1.00 38.25  ? 453 PHE C CB    1 
ATOM   11641 C CG    . PHE C 1 453 ? 31.445  11.160  -25.590 1.00 39.31  ? 453 PHE C CG    1 
ATOM   11642 C CD1   . PHE C 1 453 ? 32.621  11.151  -24.847 1.00 37.63  ? 453 PHE C CD1   1 
ATOM   11643 C CD2   . PHE C 1 453 ? 30.269  10.718  -24.994 1.00 36.76  ? 453 PHE C CD2   1 
ATOM   11644 C CE1   . PHE C 1 453 ? 32.632  10.688  -23.538 1.00 37.89  ? 453 PHE C CE1   1 
ATOM   11645 C CE2   . PHE C 1 453 ? 30.277  10.260  -23.684 1.00 40.99  ? 453 PHE C CE2   1 
ATOM   11646 C CZ    . PHE C 1 453 ? 31.459  10.255  -22.951 1.00 40.78  ? 453 PHE C CZ    1 
ATOM   11647 N N     . ASN C 1 454 ? 29.794  9.511   -28.489 1.00 40.21  ? 454 ASN C N     1 
ATOM   11648 C CA    . ASN C 1 454 ? 28.870  8.397   -28.510 1.00 41.51  ? 454 ASN C CA    1 
ATOM   11649 C C     . ASN C 1 454 ? 29.474  7.177   -29.207 1.00 41.56  ? 454 ASN C C     1 
ATOM   11650 O O     . ASN C 1 454 ? 29.414  6.095   -28.644 1.00 45.28  ? 454 ASN C O     1 
ATOM   11651 C CB    . ASN C 1 454 ? 27.538  8.802   -29.144 1.00 46.89  ? 454 ASN C CB    1 
ATOM   11652 C CG    . ASN C 1 454 ? 26.562  9.320   -28.117 1.00 49.91  ? 454 ASN C CG    1 
ATOM   11653 O OD1   . ASN C 1 454 ? 26.230  8.598   -27.172 1.00 60.05  ? 454 ASN C OD1   1 
ATOM   11654 N ND2   . ASN C 1 454 ? 26.123  10.558  -28.288 1.00 47.72  ? 454 ASN C ND2   1 
ATOM   11655 N N     . ILE C 1 455 ? 30.015  7.350   -30.423 1.00 41.37  ? 455 ILE C N     1 
ATOM   11656 C CA    . ILE C 1 455 ? 30.682  6.287   -31.164 1.00 44.79  ? 455 ILE C CA    1 
ATOM   11657 C C     . ILE C 1 455 ? 31.871  5.727   -30.368 1.00 41.91  ? 455 ILE C C     1 
ATOM   11658 O O     . ILE C 1 455 ? 32.065  4.497   -30.306 1.00 45.50  ? 455 ILE C O     1 
ATOM   11659 C CB    . ILE C 1 455 ? 31.085  6.771   -32.587 1.00 45.24  ? 455 ILE C CB    1 
ATOM   11660 C CG1   . ILE C 1 455 ? 29.850  6.949   -33.462 1.00 40.64  ? 455 ILE C CG1   1 
ATOM   11661 C CG2   . ILE C 1 455 ? 32.109  5.855   -33.269 1.00 41.16  ? 455 ILE C CG2   1 
ATOM   11662 C CD1   . ILE C 1 455 ? 30.138  7.593   -34.794 1.00 43.67  ? 455 ILE C CD1   1 
ATOM   11663 N N     . LEU C 1 456 ? 32.698  6.590   -29.767 1.00 39.60  ? 456 LEU C N     1 
ATOM   11664 C CA    . LEU C 1 456 ? 33.840  6.082   -28.995 1.00 37.62  ? 456 LEU C CA    1 
ATOM   11665 C C     . LEU C 1 456 ? 33.341  5.129   -27.907 1.00 39.97  ? 456 LEU C C     1 
ATOM   11666 O O     . LEU C 1 456 ? 33.908  4.043   -27.705 1.00 42.86  ? 456 LEU C O     1 
ATOM   11667 C CB    . LEU C 1 456 ? 34.613  7.232   -28.358 1.00 37.59  ? 456 LEU C CB    1 
ATOM   11668 C CG    . LEU C 1 456 ? 35.529  8.033   -29.280 1.00 42.89  ? 456 LEU C CG    1 
ATOM   11669 C CD1   . LEU C 1 456 ? 36.183  9.166   -28.511 1.00 45.15  ? 456 LEU C CD1   1 
ATOM   11670 C CD2   . LEU C 1 456 ? 36.606  7.160   -29.908 1.00 40.25  ? 456 LEU C CD2   1 
ATOM   11671 N N     . VAL C 1 457 ? 32.267  5.546   -27.215 1.00 33.12  ? 457 VAL C N     1 
ATOM   11672 C CA    . VAL C 1 457 ? 31.717  4.760   -26.123 1.00 38.16  ? 457 VAL C CA    1 
ATOM   11673 C C     . VAL C 1 457 ? 31.219  3.412   -26.662 1.00 44.03  ? 457 VAL C C     1 
ATOM   11674 O O     . VAL C 1 457 ? 31.527  2.350   -26.114 1.00 42.70  ? 457 VAL C O     1 
ATOM   11675 C CB    . VAL C 1 457 ? 30.602  5.536   -25.387 1.00 44.72  ? 457 VAL C CB    1 
ATOM   11676 C CG1   . VAL C 1 457 ? 29.736  4.633   -24.518 1.00 47.12  ? 457 VAL C CG1   1 
ATOM   11677 C CG2   . VAL C 1 457 ? 31.172  6.675   -24.548 1.00 45.23  ? 457 VAL C CG2   1 
ATOM   11678 N N     . ASP C 1 458 ? 30.454  3.469   -27.760 1.00 43.17  ? 458 ASP C N     1 
ATOM   11679 C CA    . ASP C 1 458 ? 29.827  2.304   -28.334 1.00 39.64  ? 458 ASP C CA    1 
ATOM   11680 C C     . ASP C 1 458 ? 30.897  1.275   -28.690 1.00 37.70  ? 458 ASP C C     1 
ATOM   11681 O O     . ASP C 1 458 ? 30.745  0.102   -28.367 1.00 46.63  ? 458 ASP C O     1 
ATOM   11682 C CB    . ASP C 1 458 ? 28.961  2.743   -29.512 1.00 44.18  ? 458 ASP C CB    1 
ATOM   11683 C CG    . ASP C 1 458 ? 27.638  3.414   -29.164 1.00 43.15  ? 458 ASP C CG    1 
ATOM   11684 O OD1   . ASP C 1 458 ? 27.234  3.361   -27.993 1.00 42.34  ? 458 ASP C OD1   1 
ATOM   11685 O OD2   . ASP C 1 458 ? 26.993  3.953   -30.096 1.00 42.26  ? 458 ASP C OD2   1 
ATOM   11686 N N     . GLU C 1 459 ? 32.006  1.729   -29.292 1.00 37.61  ? 459 GLU C N     1 
ATOM   11687 C CA    . GLU C 1 459 ? 33.077  0.843   -29.737 1.00 36.60  ? 459 GLU C CA    1 
ATOM   11688 C C     . GLU C 1 459 ? 33.976  0.403   -28.584 1.00 35.16  ? 459 GLU C C     1 
ATOM   11689 O O     . GLU C 1 459 ? 34.524  -0.691  -28.611 1.00 41.58  ? 459 GLU C O     1 
ATOM   11690 C CB    . GLU C 1 459 ? 33.858  1.479   -30.893 1.00 37.78  ? 459 GLU C CB    1 
ATOM   11691 C CG    . GLU C 1 459 ? 32.934  1.756   -32.084 1.00 41.39  ? 459 GLU C CG    1 
ATOM   11692 C CD    . GLU C 1 459 ? 33.463  2.361   -33.370 1.00 43.74  ? 459 GLU C CD    1 
ATOM   11693 O OE1   . GLU C 1 459 ? 34.603  2.905   -33.369 1.00 41.59  ? 459 GLU C OE1   1 
ATOM   11694 O OE2   . GLU C 1 459 ? 32.708  2.279   -34.388 1.00 40.70  ? 459 GLU C OE2   1 
ATOM   11695 N N     . ALA C 1 460 ? 34.117  1.211   -27.541 1.00 37.98  ? 460 ALA C N     1 
ATOM   11696 C CA    . ALA C 1 460 ? 34.796  0.735   -26.345 1.00 35.89  ? 460 ALA C CA    1 
ATOM   11697 C C     . ALA C 1 460 ? 34.046  -0.441  -25.706 1.00 35.56  ? 460 ALA C C     1 
ATOM   11698 O O     . ALA C 1 460 ? 34.666  -1.446  -25.333 1.00 36.21  ? 460 ALA C O     1 
ATOM   11699 C CB    . ALA C 1 460 ? 34.965  1.877   -25.389 1.00 35.51  ? 460 ALA C CB    1 
ATOM   11700 N N     . ALA C 1 461 ? 32.708  -0.323  -25.588 1.00 32.40  ? 461 ALA C N     1 
ATOM   11701 C CA    . ALA C 1 461 ? 31.930  -1.265  -24.806 1.00 32.55  ? 461 ALA C CA    1 
ATOM   11702 C C     . ALA C 1 461 ? 31.922  -2.625  -25.508 1.00 37.61  ? 461 ALA C C     1 
ATOM   11703 O O     . ALA C 1 461 ? 32.005  -3.683  -24.880 1.00 40.07  ? 461 ALA C O     1 
ATOM   11704 C CB    . ALA C 1 461 ? 30.526  -0.723  -24.576 1.00 35.03  ? 461 ALA C CB    1 
ATOM   11705 N N     . ALA C 1 462 ? 31.869  -2.603  -26.839 1.00 37.00  ? 462 ALA C N     1 
ATOM   11706 C CA    . ALA C 1 462 ? 31.858  -3.840  -27.592 1.00 41.40  ? 462 ALA C CA    1 
ATOM   11707 C C     . ALA C 1 462 ? 33.154  -4.632  -27.411 1.00 40.08  ? 462 ALA C C     1 
ATOM   11708 O O     . ALA C 1 462 ? 33.147  -5.847  -27.616 1.00 45.49  ? 462 ALA C O     1 
ATOM   11709 C CB    . ALA C 1 462 ? 31.573  -3.531  -29.036 1.00 40.92  ? 462 ALA C CB    1 
ATOM   11710 N N     . GLU C 1 463 ? 34.232  -3.964  -26.971 1.00 44.60  ? 463 GLU C N     1 
ATOM   11711 C CA    . GLU C 1 463 ? 35.494  -4.623  -26.667 1.00 39.13  ? 463 GLU C CA    1 
ATOM   11712 C C     . GLU C 1 463 ? 35.577  -5.029  -25.197 1.00 36.84  ? 463 GLU C C     1 
ATOM   11713 O O     . GLU C 1 463 ? 36.552  -5.675  -24.797 1.00 37.08  ? 463 GLU C O     1 
ATOM   11714 C CB    . GLU C 1 463 ? 36.666  -3.695  -26.954 1.00 38.01  ? 463 GLU C CB    1 
ATOM   11715 C CG    . GLU C 1 463 ? 36.731  -3.250  -28.375 1.00 43.30  ? 463 GLU C CG    1 
ATOM   11716 C CD    . GLU C 1 463 ? 36.937  -4.372  -29.365 1.00 45.51  ? 463 GLU C CD    1 
ATOM   11717 O OE1   . GLU C 1 463 ? 37.901  -5.103  -29.153 1.00 45.78  ? 463 GLU C OE1   1 
ATOM   11718 O OE2   . GLU C 1 463 ? 36.137  -4.492  -30.347 1.00 47.64  ? 463 GLU C OE2   1 
ATOM   11719 N N     . GLY C 1 464 ? 34.581  -4.640  -24.396 1.00 39.92  ? 464 GLY C N     1 
ATOM   11720 C CA    . GLY C 1 464 ? 34.556  -4.956  -22.961 1.00 42.53  ? 464 GLY C CA    1 
ATOM   11721 C C     . GLY C 1 464 ? 35.183  -3.870  -22.061 1.00 41.13  ? 464 GLY C C     1 
ATOM   11722 O O     . GLY C 1 464 ? 35.620  -4.152  -20.947 1.00 46.80  ? 464 GLY C O     1 
ATOM   11723 N N     . TYR C 1 465 ? 35.181  -2.614  -22.532 1.00 37.37  ? 465 TYR C N     1 
ATOM   11724 C CA    . TYR C 1 465 ? 35.842  -1.534  -21.847 1.00 36.38  ? 465 TYR C CA    1 
ATOM   11725 C C     . TYR C 1 465 ? 34.792  -0.520  -21.483 1.00 34.12  ? 465 TYR C C     1 
ATOM   11726 O O     . TYR C 1 465 ? 34.232  0.078   -22.394 1.00 34.20  ? 465 TYR C O     1 
ATOM   11727 C CB    . TYR C 1 465 ? 36.853  -0.815  -22.740 1.00 41.52  ? 465 TYR C CB    1 
ATOM   11728 C CG    . TYR C 1 465 ? 37.902  -1.650  -23.422 1.00 40.37  ? 465 TYR C CG    1 
ATOM   11729 C CD1   . TYR C 1 465 ? 38.497  -2.732  -22.800 1.00 40.12  ? 465 TYR C CD1   1 
ATOM   11730 C CD2   . TYR C 1 465 ? 38.361  -1.298  -24.683 1.00 40.98  ? 465 TYR C CD2   1 
ATOM   11731 C CE1   . TYR C 1 465 ? 39.499  -3.476  -23.423 1.00 37.20  ? 465 TYR C CE1   1 
ATOM   11732 C CE2   . TYR C 1 465 ? 39.326  -2.050  -25.329 1.00 41.33  ? 465 TYR C CE2   1 
ATOM   11733 C CZ    . TYR C 1 465 ? 39.898  -3.142  -24.704 1.00 36.30  ? 465 TYR C CZ    1 
ATOM   11734 O OH    . TYR C 1 465 ? 40.899  -3.838  -25.332 1.00 36.07  ? 465 TYR C OH    1 
ATOM   11735 N N     . GLY C 1 466 ? 34.528  -0.370  -20.177 1.00 33.26  ? 466 GLY C N     1 
ATOM   11736 C CA    . GLY C 1 466 ? 33.465  0.487   -19.685 1.00 29.99  ? 466 GLY C CA    1 
ATOM   11737 C C     . GLY C 1 466 ? 33.997  1.701   -18.910 1.00 34.58  ? 466 GLY C C     1 
ATOM   11738 O O     . GLY C 1 466 ? 35.077  1.655   -18.319 1.00 40.68  ? 466 GLY C O     1 
ATOM   11739 N N     . GLU C 1 467 ? 33.206  2.784   -18.919 1.00 33.56  ? 467 GLU C N     1 
ATOM   11740 C CA    . GLU C 1 467 ? 33.544  4.049   -18.301 1.00 36.97  ? 467 GLU C CA    1 
ATOM   11741 C C     . GLU C 1 467 ? 33.181  4.009   -16.816 1.00 42.91  ? 467 GLU C C     1 
ATOM   11742 O O     . GLU C 1 467 ? 32.226  3.353   -16.454 1.00 46.86  ? 467 GLU C O     1 
ATOM   11743 C CB    . GLU C 1 467 ? 32.766  5.157   -19.000 1.00 37.33  ? 467 GLU C CB    1 
ATOM   11744 C CG    . GLU C 1 467 ? 32.974  6.547   -18.419 1.00 41.03  ? 467 GLU C CG    1 
ATOM   11745 C CD    . GLU C 1 467 ? 34.375  7.122   -18.542 1.00 45.45  ? 467 GLU C CD    1 
ATOM   11746 O OE1   . GLU C 1 467 ? 34.573  8.008   -19.435 1.00 43.22  ? 467 GLU C OE1   1 
ATOM   11747 O OE2   . GLU C 1 467 ? 35.262  6.704   -17.749 1.00 46.27  ? 467 GLU C OE2   1 
ATOM   11748 N N     . TYR C 1 468 ? 33.942  4.728   -15.977 1.00 40.77  ? 468 TYR C N     1 
ATOM   11749 C CA    . TYR C 1 468 ? 33.741  4.746   -14.550 1.00 37.60  ? 468 TYR C CA    1 
ATOM   11750 C C     . TYR C 1 468 ? 33.344  6.118   -14.024 1.00 39.40  ? 468 TYR C C     1 
ATOM   11751 O O     . TYR C 1 468 ? 32.935  6.247   -12.864 1.00 45.54  ? 468 TYR C O     1 
ATOM   11752 C CB    . TYR C 1 468 ? 35.020  4.352   -13.827 1.00 43.04  ? 468 TYR C CB    1 
ATOM   11753 C CG    . TYR C 1 468 ? 36.137  5.369   -13.746 1.00 45.37  ? 468 TYR C CG    1 
ATOM   11754 C CD1   . TYR C 1 468 ? 37.079  5.499   -14.762 1.00 45.69  ? 468 TYR C CD1   1 
ATOM   11755 C CD2   . TYR C 1 468 ? 36.374  6.058   -12.572 1.00 44.23  ? 468 TYR C CD2   1 
ATOM   11756 C CE1   . TYR C 1 468 ? 38.153  6.370   -14.659 1.00 43.17  ? 468 TYR C CE1   1 
ATOM   11757 C CE2   . TYR C 1 468 ? 37.444  6.929   -12.451 1.00 46.74  ? 468 TYR C CE2   1 
ATOM   11758 C CZ    . TYR C 1 468 ? 38.344  7.077   -13.489 1.00 46.20  ? 468 TYR C CZ    1 
ATOM   11759 O OH    . TYR C 1 468 ? 39.390  7.938   -13.361 1.00 44.91  ? 468 TYR C OH    1 
ATOM   11760 N N     . ARG C 1 469 ? 33.501  7.135   -14.860 1.00 43.29  ? 469 ARG C N     1 
ATOM   11761 C CA    . ARG C 1 469 ? 33.233  8.510   -14.462 1.00 40.48  ? 469 ARG C CA    1 
ATOM   11762 C C     . ARG C 1 469 ? 32.901  9.322   -15.711 1.00 42.97  ? 469 ARG C C     1 
ATOM   11763 O O     . ARG C 1 469 ? 33.703  9.363   -16.636 1.00 48.05  ? 469 ARG C O     1 
ATOM   11764 C CB    . ARG C 1 469 ? 34.471  9.004   -13.726 1.00 38.93  ? 469 ARG C CB    1 
ATOM   11765 C CG    . ARG C 1 469 ? 34.276  10.331  -13.027 1.00 46.14  ? 469 ARG C CG    1 
ATOM   11766 C CD    . ARG C 1 469 ? 35.469  10.703  -12.170 1.00 50.10  ? 469 ARG C CD    1 
ATOM   11767 N NE    . ARG C 1 469 ? 35.154  12.008  -11.626 1.00 51.92  ? 469 ARG C NE    1 
ATOM   11768 C CZ    . ARG C 1 469 ? 36.027  12.977  -11.480 1.00 49.39  ? 469 ARG C CZ    1 
ATOM   11769 N NH1   . ARG C 1 469 ? 37.312  12.715  -11.625 1.00 40.11  ? 469 ARG C NH1   1 
ATOM   11770 N NH2   . ARG C 1 469 ? 35.594  14.188  -11.179 1.00 55.30  ? 469 ARG C NH2   1 
ATOM   11771 N N     . THR C 1 470 ? 31.713  9.945   -15.761 1.00 52.04  ? 470 THR C N     1 
ATOM   11772 C CA    . THR C 1 470 ? 31.273  10.599  -16.987 1.00 51.53  ? 470 THR C CA    1 
ATOM   11773 C C     . THR C 1 470 ? 30.569  11.938  -16.742 1.00 55.06  ? 470 THR C C     1 
ATOM   11774 O O     . THR C 1 470 ? 30.385  12.362  -15.609 1.00 52.07  ? 470 THR C O     1 
ATOM   11775 C CB    . THR C 1 470 ? 30.353  9.686   -17.793 1.00 44.49  ? 470 THR C CB    1 
ATOM   11776 O OG1   . THR C 1 470 ? 30.455  10.142  -19.146 1.00 44.33  ? 470 THR C OG1   1 
ATOM   11777 C CG2   . THR C 1 470 ? 28.929  9.698   -17.289 1.00 42.91  ? 470 THR C CG2   1 
ATOM   11778 N N     . HIS C 1 471 ? 30.242  12.615  -17.857 1.00 53.03  ? 471 HIS C N     1 
ATOM   11779 C CA    . HIS C 1 471 ? 29.619  13.929  -17.868 1.00 50.11  ? 471 HIS C CA    1 
ATOM   11780 C C     . HIS C 1 471 ? 28.134  13.732  -17.569 1.00 44.79  ? 471 HIS C C     1 
ATOM   11781 O O     . HIS C 1 471 ? 27.596  12.681  -17.874 1.00 44.35  ? 471 HIS C O     1 
ATOM   11782 C CB    . HIS C 1 471 ? 29.963  14.622  -19.204 1.00 55.88  ? 471 HIS C CB    1 
ATOM   11783 C CG    . HIS C 1 471 ? 29.407  16.001  -19.409 1.00 60.07  ? 471 HIS C CG    1 
ATOM   11784 N ND1   . HIS C 1 471 ? 28.079  16.230  -19.705 1.00 61.20  ? 471 HIS C ND1   1 
ATOM   11785 C CD2   . HIS C 1 471 ? 29.985  17.229  -19.359 1.00 62.52  ? 471 HIS C CD2   1 
ATOM   11786 C CE1   . HIS C 1 471 ? 27.864  17.549  -19.794 1.00 62.03  ? 471 HIS C CE1   1 
ATOM   11787 N NE2   . HIS C 1 471 ? 29.005  18.174  -19.593 1.00 59.34  ? 471 HIS C NE2   1 
ATOM   11788 N N     . ILE C 1 472 ? 27.484  14.710  -16.922 1.00 44.33  ? 472 ILE C N     1 
ATOM   11789 C CA    . ILE C 1 472 ? 26.070  14.606  -16.577 1.00 45.15  ? 472 ILE C CA    1 
ATOM   11790 C C     . ILE C 1 472 ? 25.286  14.212  -17.817 1.00 47.30  ? 472 ILE C C     1 
ATOM   11791 O O     . ILE C 1 472 ? 24.261  13.528  -17.750 1.00 52.10  ? 472 ILE C O     1 
ATOM   11792 C CB    . ILE C 1 472 ? 25.526  15.921  -15.990 1.00 51.72  ? 472 ILE C CB    1 
ATOM   11793 C CG1   . ILE C 1 472 ? 25.991  17.126  -16.813 1.00 68.77  ? 472 ILE C CG1   1 
ATOM   11794 C CG2   . ILE C 1 472 ? 25.873  16.066  -14.515 1.00 48.35  ? 472 ILE C CG2   1 
ATOM   11795 C CD1   . ILE C 1 472 ? 25.254  18.422  -16.524 1.00 82.41  ? 472 ILE C CD1   1 
ATOM   11796 N N     . ARG C 1 473 ? 25.772  14.689  -18.960 1.00 45.07  ? 473 ARG C N     1 
ATOM   11797 C CA    . ARG C 1 473 ? 24.980  14.611  -20.168 1.00 48.08  ? 473 ARG C CA    1 
ATOM   11798 C C     . ARG C 1 473 ? 24.884  13.134  -20.543 1.00 43.91  ? 473 ARG C C     1 
ATOM   11799 O O     . ARG C 1 473 ? 23.930  12.731  -21.183 1.00 42.17  ? 473 ARG C O     1 
ATOM   11800 C CB    . ARG C 1 473 ? 25.598  15.540  -21.219 1.00 53.89  ? 473 ARG C CB    1 
ATOM   11801 C CG    . ARG C 1 473 ? 25.091  15.320  -22.633 1.00 71.95  ? 473 ARG C CG    1 
ATOM   11802 C CD    . ARG C 1 473 ? 25.628  16.328  -23.634 1.00 85.75  ? 473 ARG C CD    1 
ATOM   11803 N NE    . ARG C 1 473 ? 25.163  16.010  -24.984 1.00 99.37  ? 473 ARG C NE    1 
ATOM   11804 C CZ    . ARG C 1 473 ? 23.892  16.034  -25.393 1.00 94.50  ? 473 ARG C CZ    1 
ATOM   11805 N NH1   . ARG C 1 473 ? 22.941  16.551  -24.628 1.00 91.10  ? 473 ARG C NH1   1 
ATOM   11806 N NH2   . ARG C 1 473 ? 23.586  15.566  -26.593 1.00 88.52  ? 473 ARG C NH2   1 
ATOM   11807 N N     . TYR C 1 474 ? 25.870  12.329  -20.117 1.00 42.18  ? 474 TYR C N     1 
ATOM   11808 C CA    . TYR C 1 474 ? 26.064  10.986  -20.651 1.00 43.25  ? 474 TYR C CA    1 
ATOM   11809 C C     . TYR C 1 474 ? 25.807  9.934   -19.574 1.00 41.68  ? 474 TYR C C     1 
ATOM   11810 O O     . TYR C 1 474 ? 26.003  8.751   -19.822 1.00 44.54  ? 474 TYR C O     1 
ATOM   11811 C CB    . TYR C 1 474 ? 27.472  10.860  -21.251 1.00 45.05  ? 474 TYR C CB    1 
ATOM   11812 C CG    . TYR C 1 474 ? 27.738  11.781  -22.427 1.00 52.17  ? 474 TYR C CG    1 
ATOM   11813 C CD1   . TYR C 1 474 ? 26.917  11.773  -23.547 1.00 53.96  ? 474 TYR C CD1   1 
ATOM   11814 C CD2   . TYR C 1 474 ? 28.838  12.628  -22.446 1.00 55.43  ? 474 TYR C CD2   1 
ATOM   11815 C CE1   . TYR C 1 474 ? 27.139  12.622  -24.616 1.00 56.40  ? 474 TYR C CE1   1 
ATOM   11816 C CE2   . TYR C 1 474 ? 29.080  13.482  -23.509 1.00 55.17  ? 474 TYR C CE2   1 
ATOM   11817 C CZ    . TYR C 1 474 ? 28.220  13.489  -24.594 1.00 57.62  ? 474 TYR C CZ    1 
ATOM   11818 O OH    . TYR C 1 474 ? 28.458  14.322  -25.667 1.00 57.22  ? 474 TYR C OH    1 
ATOM   11819 N N     . MET C 1 475 ? 25.289  10.364  -18.408 1.00 40.96  ? 475 MET C N     1 
ATOM   11820 C CA    . MET C 1 475 ? 25.122  9.494   -17.265 1.00 37.40  ? 475 MET C CA    1 
ATOM   11821 C C     . MET C 1 475 ? 24.228  8.310   -17.601 1.00 38.90  ? 475 MET C C     1 
ATOM   11822 O O     . MET C 1 475 ? 24.500  7.212   -17.136 1.00 46.51  ? 475 MET C O     1 
ATOM   11823 C CB    . MET C 1 475 ? 24.558  10.255  -16.068 1.00 41.45  ? 475 MET C CB    1 
ATOM   11824 C CG    . MET C 1 475 ? 25.650  10.929  -15.260 1.00 43.49  ? 475 MET C CG    1 
ATOM   11825 S SD    . MET C 1 475 ? 25.144  11.901  -13.818 1.00 47.83  ? 475 MET C SD    1 
ATOM   11826 C CE    . MET C 1 475 ? 26.720  12.714  -13.534 1.00 60.25  ? 475 MET C CE    1 
ATOM   11827 N N     . ASP C 1 476 ? 23.164  8.508   -18.383 1.00 42.45  ? 476 ASP C N     1 
ATOM   11828 C CA    . ASP C 1 476 ? 22.296  7.389   -18.731 1.00 43.30  ? 476 ASP C CA    1 
ATOM   11829 C C     . ASP C 1 476 ? 23.032  6.444   -19.657 1.00 40.67  ? 476 ASP C C     1 
ATOM   11830 O O     . ASP C 1 476 ? 22.977  5.236   -19.479 1.00 47.63  ? 476 ASP C O     1 
ATOM   11831 C CB    . ASP C 1 476 ? 20.972  7.785   -19.390 1.00 42.42  ? 476 ASP C CB    1 
ATOM   11832 C CG    . ASP C 1 476 ? 19.931  8.290   -18.416 1.00 48.77  ? 476 ASP C CG    1 
ATOM   11833 O OD1   . ASP C 1 476 ? 20.107  8.116   -17.197 1.00 46.43  ? 476 ASP C OD1   1 
ATOM   11834 O OD2   . ASP C 1 476 ? 18.982  8.905   -18.881 1.00 66.79  ? 476 ASP C OD2   1 
ATOM   11835 N N     . ARG C 1 477 ? 23.712  7.009   -20.643 1.00 40.62  ? 477 ARG C N     1 
ATOM   11836 C CA    . ARG C 1 477 ? 24.387  6.191   -21.629 1.00 45.95  ? 477 ARG C CA    1 
ATOM   11837 C C     . ARG C 1 477 ? 25.341  5.249   -20.889 1.00 42.79  ? 477 ARG C C     1 
ATOM   11838 O O     . ARG C 1 477 ? 25.360  4.039   -21.116 1.00 39.65  ? 477 ARG C O     1 
ATOM   11839 C CB    . ARG C 1 477 ? 25.041  7.097   -22.684 1.00 52.03  ? 477 ARG C CB    1 
ATOM   11840 C CG    . ARG C 1 477 ? 25.764  6.363   -23.802 1.00 61.53  ? 477 ARG C CG    1 
ATOM   11841 C CD    . ARG C 1 477 ? 24.895  5.861   -24.948 1.00 70.79  ? 477 ARG C CD    1 
ATOM   11842 N NE    . ARG C 1 477 ? 25.560  4.730   -25.588 1.00 80.09  ? 477 ARG C NE    1 
ATOM   11843 C CZ    . ARG C 1 477 ? 25.705  3.520   -25.037 1.00 79.93  ? 477 ARG C CZ    1 
ATOM   11844 N NH1   . ARG C 1 477 ? 25.002  3.170   -23.974 1.00 81.19  ? 477 ARG C NH1   1 
ATOM   11845 N NH2   . ARG C 1 477 ? 26.534  2.637   -25.569 1.00 81.48  ? 477 ARG C NH2   1 
ATOM   11846 N N     . ILE C 1 478 ? 26.087  5.777   -19.923 1.00 41.30  ? 478 ILE C N     1 
ATOM   11847 C CA    . ILE C 1 478 ? 27.117  4.962   -19.304 1.00 41.86  ? 478 ILE C CA    1 
ATOM   11848 C C     . ILE C 1 478 ? 26.498  3.865   -18.432 1.00 42.79  ? 478 ILE C C     1 
ATOM   11849 O O     . ILE C 1 478 ? 27.019  2.743   -18.374 1.00 45.12  ? 478 ILE C O     1 
ATOM   11850 C CB    . ILE C 1 478 ? 28.113  5.881   -18.586 1.00 44.17  ? 478 ILE C CB    1 
ATOM   11851 C CG1   . ILE C 1 478 ? 28.697  6.862   -19.591 1.00 41.92  ? 478 ILE C CG1   1 
ATOM   11852 C CG2   . ILE C 1 478 ? 29.222  5.082   -17.929 1.00 48.10  ? 478 ILE C CG2   1 
ATOM   11853 C CD1   . ILE C 1 478 ? 29.544  6.147   -20.605 1.00 44.22  ? 478 ILE C CD1   1 
ATOM   11854 N N     . ALA C 1 479 ? 25.338  4.144   -17.824 1.00 41.12  ? 479 ALA C N     1 
ATOM   11855 C CA    . ALA C 1 479 ? 24.671  3.141   -17.011 1.00 40.01  ? 479 ALA C CA    1 
ATOM   11856 C C     . ALA C 1 479 ? 24.155  2.031   -17.905 1.00 42.95  ? 479 ALA C C     1 
ATOM   11857 O O     . ALA C 1 479 ? 24.159  0.858   -17.533 1.00 48.00  ? 479 ALA C O     1 
ATOM   11858 C CB    . ALA C 1 479 ? 23.542  3.748   -16.226 1.00 45.06  ? 479 ALA C CB    1 
ATOM   11859 N N     . LYS C 1 480 ? 23.703  2.408   -19.101 1.00 47.71  ? 480 LYS C N     1 
ATOM   11860 C CA    . LYS C 1 480 ? 23.114  1.411   -19.965 1.00 46.37  ? 480 LYS C CA    1 
ATOM   11861 C C     . LYS C 1 480 ? 24.199  0.491   -20.493 1.00 37.72  ? 480 LYS C C     1 
ATOM   11862 O O     . LYS C 1 480 ? 23.859  -0.611  -20.853 1.00 45.70  ? 480 LYS C O     1 
ATOM   11863 C CB    . LYS C 1 480 ? 22.201  2.043   -21.012 1.00 54.15  ? 480 LYS C CB    1 
ATOM   11864 C CG    . LYS C 1 480 ? 20.831  2.417   -20.456 1.00 62.93  ? 480 LYS C CG    1 
ATOM   11865 C CD    . LYS C 1 480 ? 20.123  3.476   -21.283 1.00 79.68  ? 480 LYS C CD    1 
ATOM   11866 C CE    . LYS C 1 480 ? 18.848  3.977   -20.642 1.00 82.63  ? 480 LYS C CE    1 
ATOM   11867 N NZ    . LYS C 1 480 ? 18.299  5.123   -21.398 1.00 80.19  ? 480 LYS C NZ    1 
ATOM   11868 N N     . THR C 1 481 ? 25.484  0.840   -20.373 1.00 40.87  ? 481 THR C N     1 
ATOM   11869 C CA    . THR C 1 481 ? 26.568  -0.075  -20.728 1.00 43.25  ? 481 THR C CA    1 
ATOM   11870 C C     . THR C 1 481 ? 26.801  -1.172  -19.688 1.00 46.27  ? 481 THR C C     1 
ATOM   11871 O O     . THR C 1 481 ? 27.389  -2.196  -20.028 1.00 46.79  ? 481 THR C O     1 
ATOM   11872 C CB    . THR C 1 481 ? 27.902  0.645   -21.018 1.00 50.46  ? 481 THR C CB    1 
ATOM   11873 O OG1   . THR C 1 481 ? 28.532  1.204   -19.877 1.00 44.91  ? 481 THR C OG1   1 
ATOM   11874 C CG2   . THR C 1 481 ? 27.751  1.796   -21.990 1.00 56.45  ? 481 THR C CG2   1 
ATOM   11875 N N     . TYR C 1 482 ? 26.357  -0.985  -18.434 1.00 49.98  ? 482 TYR C N     1 
ATOM   11876 C CA    . TYR C 1 482 ? 26.493  -2.016  -17.402 1.00 46.62  ? 482 TYR C CA    1 
ATOM   11877 C C     . TYR C 1 482 ? 25.218  -2.865  -17.308 1.00 45.17  ? 482 TYR C C     1 
ATOM   11878 O O     . TYR C 1 482 ? 24.624  -2.957  -16.237 1.00 47.46  ? 482 TYR C O     1 
ATOM   11879 C CB    . TYR C 1 482 ? 26.866  -1.355  -16.066 1.00 45.37  ? 482 TYR C CB    1 
ATOM   11880 C CG    . TYR C 1 482 ? 28.254  -0.757  -16.063 1.00 40.58  ? 482 TYR C CG    1 
ATOM   11881 C CD1   . TYR C 1 482 ? 29.369  -1.505  -15.702 1.00 39.64  ? 482 TYR C CD1   1 
ATOM   11882 C CD2   . TYR C 1 482 ? 28.465  0.526   -16.539 1.00 35.49  ? 482 TYR C CD2   1 
ATOM   11883 C CE1   . TYR C 1 482 ? 30.650  -0.968  -15.768 1.00 47.12  ? 482 TYR C CE1   1 
ATOM   11884 C CE2   . TYR C 1 482 ? 29.740  1.059   -16.648 1.00 40.38  ? 482 TYR C CE2   1 
ATOM   11885 C CZ    . TYR C 1 482 ? 30.837  0.332   -16.220 1.00 42.59  ? 482 TYR C CZ    1 
ATOM   11886 O OH    . TYR C 1 482 ? 32.102  0.886   -16.312 1.00 40.99  ? 482 TYR C OH    1 
ATOM   11887 N N     . SER C 1 483 ? 24.928  -3.628  -18.372 1.00 37.59  ? 483 SER C N     1 
ATOM   11888 C CA    . SER C 1 483 ? 23.587  -4.082  -18.713 1.00 36.72  ? 483 SER C CA    1 
ATOM   11889 C C     . SER C 1 483 ? 23.389  -5.581  -18.462 1.00 35.30  ? 483 SER C C     1 
ATOM   11890 O O     . SER C 1 483 ? 22.367  -6.157  -18.823 1.00 40.65  ? 483 SER C O     1 
ATOM   11891 C CB    . SER C 1 483 ? 23.300  -3.763  -20.193 1.00 37.11  ? 483 SER C CB    1 
ATOM   11892 O OG    . SER C 1 483 ? 24.272  -4.366  -21.052 1.00 34.39  ? 483 SER C OG    1 
ATOM   11893 N N     . TRP C 1 484 ? 24.370  -6.243  -17.868 1.00 37.15  ? 484 TRP C N     1 
ATOM   11894 C CA    . TRP C 1 484 ? 24.265  -7.682  -17.657 1.00 40.92  ? 484 TRP C CA    1 
ATOM   11895 C C     . TRP C 1 484 ? 22.949  -8.062  -16.962 1.00 44.21  ? 484 TRP C C     1 
ATOM   11896 O O     . TRP C 1 484 ? 22.520  -7.451  -15.971 1.00 41.14  ? 484 TRP C O     1 
ATOM   11897 C CB    . TRP C 1 484 ? 25.489  -8.200  -16.889 1.00 39.04  ? 484 TRP C CB    1 
ATOM   11898 C CG    . TRP C 1 484 ? 25.548  -9.694  -16.793 1.00 39.98  ? 484 TRP C CG    1 
ATOM   11899 C CD1   . TRP C 1 484 ? 25.992  -10.558 -17.742 1.00 36.32  ? 484 TRP C CD1   1 
ATOM   11900 C CD2   . TRP C 1 484 ? 25.140  -10.504 -15.675 1.00 34.81  ? 484 TRP C CD2   1 
ATOM   11901 N NE1   . TRP C 1 484 ? 25.883  -11.843 -17.293 1.00 34.75  ? 484 TRP C NE1   1 
ATOM   11902 C CE2   . TRP C 1 484 ? 25.333  -11.841 -16.047 1.00 32.82  ? 484 TRP C CE2   1 
ATOM   11903 C CE3   . TRP C 1 484 ? 24.573  -10.230 -14.427 1.00 33.19  ? 484 TRP C CE3   1 
ATOM   11904 C CZ2   . TRP C 1 484 ? 25.021  -12.895 -15.198 1.00 33.76  ? 484 TRP C CZ2   1 
ATOM   11905 C CZ3   . TRP C 1 484 ? 24.241  -11.270 -13.596 1.00 32.24  ? 484 TRP C CZ3   1 
ATOM   11906 C CH2   . TRP C 1 484 ? 24.464  -12.590 -13.978 1.00 30.41  ? 484 TRP C CH2   1 
ATOM   11907 N N     . ASN C 1 485 ? 22.348  -9.132  -17.493 1.00 45.91  ? 485 ASN C N     1 
ATOM   11908 C CA    . ASN C 1 485 ? 21.093  -9.713  -17.028 1.00 45.12  ? 485 ASN C CA    1 
ATOM   11909 C C     . ASN C 1 485 ? 19.971  -8.674  -17.064 1.00 39.44  ? 485 ASN C C     1 
ATOM   11910 O O     . ASN C 1 485 ? 19.377  -8.342  -16.052 1.00 38.61  ? 485 ASN C O     1 
ATOM   11911 C CB    . ASN C 1 485 ? 21.267  -10.407 -15.673 1.00 38.17  ? 485 ASN C CB    1 
ATOM   11912 C CG    . ASN C 1 485 ? 19.967  -11.024 -15.198 1.00 37.92  ? 485 ASN C CG    1 
ATOM   11913 O OD1   . ASN C 1 485 ? 19.072  -11.342 -15.983 1.00 36.01  ? 485 ASN C OD1   1 
ATOM   11914 N ND2   . ASN C 1 485 ? 19.832  -11.159 -13.893 1.00 35.64  ? 485 ASN C ND2   1 
ATOM   11915 N N     . ASP C 1 486 ? 19.706  -8.138  -18.252 1.00 40.06  ? 486 ASP C N     1 
ATOM   11916 C CA    . ASP C 1 486 ? 18.737  -7.058  -18.439 1.00 40.92  ? 486 ASP C CA    1 
ATOM   11917 C C     . ASP C 1 486 ? 18.805  -6.030  -17.303 1.00 39.13  ? 486 ASP C C     1 
ATOM   11918 O O     . ASP C 1 486 ? 17.791  -5.663  -16.684 1.00 37.73  ? 486 ASP C O     1 
ATOM   11919 C CB    . ASP C 1 486 ? 17.349  -7.650  -18.668 1.00 43.62  ? 486 ASP C CB    1 
ATOM   11920 C CG    . ASP C 1 486 ? 16.191  -6.673  -18.756 1.00 46.71  ? 486 ASP C CG    1 
ATOM   11921 O OD1   . ASP C 1 486 ? 16.392  -5.574  -19.297 1.00 49.49  ? 486 ASP C OD1   1 
ATOM   11922 O OD2   . ASP C 1 486 ? 15.081  -7.046  -18.278 1.00 49.15  ? 486 ASP C OD2   1 
ATOM   11923 N N     . ASN C 1 487 ? 20.004  -5.477  -17.106 1.00 35.35  ? 487 ASN C N     1 
ATOM   11924 C CA    . ASN C 1 487 ? 20.177  -4.295  -16.278 1.00 40.41  ? 487 ASN C CA    1 
ATOM   11925 C C     . ASN C 1 487 ? 19.826  -4.595  -14.819 1.00 35.64  ? 487 ASN C C     1 
ATOM   11926 O O     . ASN C 1 487 ? 19.331  -3.730  -14.111 1.00 44.79  ? 487 ASN C O     1 
ATOM   11927 C CB    . ASN C 1 487 ? 19.376  -3.104  -16.819 1.00 40.04  ? 487 ASN C CB    1 
ATOM   11928 C CG    . ASN C 1 487 ? 19.935  -2.592  -18.128 1.00 44.49  ? 487 ASN C CG    1 
ATOM   11929 O OD1   . ASN C 1 487 ? 19.235  -2.580  -19.129 1.00 43.56  ? 487 ASN C OD1   1 
ATOM   11930 N ND2   . ASN C 1 487 ? 21.176  -2.138  -18.132 1.00 47.08  ? 487 ASN C ND2   1 
ATOM   11931 N N     . ALA C 1 488 ? 20.127  -5.808  -14.364 1.00 34.55  ? 488 ALA C N     1 
ATOM   11932 C CA    . ALA C 1 488 ? 19.844  -6.253  -13.005 1.00 37.04  ? 488 ALA C CA    1 
ATOM   11933 C C     . ALA C 1 488 ? 20.395  -5.278  -11.974 1.00 34.05  ? 488 ALA C C     1 
ATOM   11934 O O     . ALA C 1 488 ? 19.653  -4.823  -11.120 1.00 42.83  ? 488 ALA C O     1 
ATOM   11935 C CB    . ALA C 1 488 ? 20.428  -7.635  -12.761 1.00 36.99  ? 488 ALA C CB    1 
ATOM   11936 N N     . LEU C 1 489 ? 21.687  -4.974  -12.083 1.00 30.70  ? 489 LEU C N     1 
ATOM   11937 C CA    . LEU C 1 489 ? 22.365  -4.156  -11.106 1.00 34.26  ? 489 LEU C CA    1 
ATOM   11938 C C     . LEU C 1 489 ? 21.681  -2.806  -10.946 1.00 34.30  ? 489 LEU C C     1 
ATOM   11939 O O     . LEU C 1 489 ? 21.486  -2.359  -9.825  1.00 34.98  ? 489 LEU C O     1 
ATOM   11940 C CB    . LEU C 1 489 ? 23.819  -3.956  -11.526 1.00 35.99  ? 489 LEU C CB    1 
ATOM   11941 C CG    . LEU C 1 489 ? 24.587  -2.966  -10.657 1.00 36.35  ? 489 LEU C CG    1 
ATOM   11942 C CD1   . LEU C 1 489 ? 24.477  -3.352  -9.213  1.00 38.29  ? 489 LEU C CD1   1 
ATOM   11943 C CD2   . LEU C 1 489 ? 26.059  -2.948  -11.038 1.00 38.61  ? 489 LEU C CD2   1 
ATOM   11944 N N     . TRP C 1 490 ? 21.361  -2.135  -12.053 1.00 36.06  ? 490 TRP C N     1 
ATOM   11945 C CA    . TRP C 1 490 ? 20.652  -0.858  -11.953 1.00 40.72  ? 490 TRP C CA    1 
ATOM   11946 C C     . TRP C 1 490 ? 19.246  -1.017  -11.350 1.00 36.99  ? 490 TRP C C     1 
ATOM   11947 O O     . TRP C 1 490 ? 18.729  -0.042  -10.804 1.00 33.45  ? 490 TRP C O     1 
ATOM   11948 C CB    . TRP C 1 490 ? 20.595  -0.073  -13.282 1.00 34.30  ? 490 TRP C CB    1 
ATOM   11949 C CG    . TRP C 1 490 ? 21.509  1.115   -13.273 1.00 31.10  ? 490 TRP C CG    1 
ATOM   11950 C CD1   . TRP C 1 490 ? 21.165  2.435   -13.368 1.00 31.45  ? 490 TRP C CD1   1 
ATOM   11951 C CD2   . TRP C 1 490 ? 22.930  1.094   -13.062 1.00 27.08  ? 490 TRP C CD2   1 
ATOM   11952 N NE1   . TRP C 1 490 ? 22.289  3.228   -13.235 1.00 29.67  ? 490 TRP C NE1   1 
ATOM   11953 C CE2   . TRP C 1 490 ? 23.373  2.426   -13.038 1.00 26.30  ? 490 TRP C CE2   1 
ATOM   11954 C CE3   . TRP C 1 490 ? 23.877  0.077   -12.926 1.00 29.18  ? 490 TRP C CE3   1 
ATOM   11955 C CZ2   . TRP C 1 490 ? 24.716  2.756   -12.876 1.00 32.44  ? 490 TRP C CZ2   1 
ATOM   11956 C CZ3   . TRP C 1 490 ? 25.215  0.401   -12.781 1.00 30.69  ? 490 TRP C CZ3   1 
ATOM   11957 C CH2   . TRP C 1 490 ? 25.630  1.733   -12.750 1.00 29.87  ? 490 TRP C CH2   1 
ATOM   11958 N N     . LYS C 1 491 ? 18.636  -2.203  -11.456 1.00 33.39  ? 491 LYS C N     1 
ATOM   11959 C CA    . LYS C 1 491 ? 17.310  -2.417  -10.896 1.00 44.87  ? 491 LYS C CA    1 
ATOM   11960 C C     . LYS C 1 491 ? 17.429  -2.564  -9.383  1.00 45.78  ? 491 LYS C C     1 
ATOM   11961 O O     . LYS C 1 491 ? 16.478  -2.296  -8.654  1.00 39.91  ? 491 LYS C O     1 
ATOM   11962 C CB    . LYS C 1 491 ? 16.643  -3.704  -11.397 1.00 51.87  ? 491 LYS C CB    1 
ATOM   11963 C CG    . LYS C 1 491 ? 16.139  -3.658  -12.826 1.00 52.24  ? 491 LYS C CG    1 
ATOM   11964 C CD    . LYS C 1 491 ? 15.882  -5.030  -13.432 1.00 52.23  ? 491 LYS C CD    1 
ATOM   11965 C CE    . LYS C 1 491 ? 15.432  -4.861  -14.868 1.00 53.39  ? 491 LYS C CE    1 
ATOM   11966 N NZ    . LYS C 1 491 ? 15.073  -6.136  -15.502 1.00 54.53  ? 491 LYS C NZ    1 
ATOM   11967 N N     . MET C 1 492 ? 18.593  -3.040  -8.925  1.00 40.45  ? 492 MET C N     1 
ATOM   11968 C CA    . MET C 1 492 ? 18.811  -3.066  -7.497  1.00 42.84  ? 492 MET C CA    1 
ATOM   11969 C C     . MET C 1 492 ? 19.118  -1.641  -7.046  1.00 40.05  ? 492 MET C C     1 
ATOM   11970 O O     . MET C 1 492 ? 18.596  -1.206  -6.018  1.00 39.40  ? 492 MET C O     1 
ATOM   11971 C CB    . MET C 1 492 ? 19.883  -4.072  -7.100  1.00 39.76  ? 492 MET C CB    1 
ATOM   11972 C CG    . MET C 1 492 ? 20.182  -4.102  -5.627  1.00 40.72  ? 492 MET C CG    1 
ATOM   11973 S SD    . MET C 1 492 ? 21.894  -4.666  -5.379  1.00 40.59  ? 492 MET C SD    1 
ATOM   11974 C CE    . MET C 1 492 ? 22.740  -3.154  -5.812  1.00 41.45  ? 492 MET C CE    1 
ATOM   11975 N N     . HIS C 1 493 ? 19.830  -0.854  -7.866  1.00 39.48  ? 493 HIS C N     1 
ATOM   11976 C CA    . HIS C 1 493 ? 19.961  0.560   -7.529  1.00 35.90  ? 493 HIS C CA    1 
ATOM   11977 C C     . HIS C 1 493 ? 18.593  1.221   -7.419  1.00 40.59  ? 493 HIS C C     1 
ATOM   11978 O O     . HIS C 1 493 ? 18.345  1.902   -6.427  1.00 42.84  ? 493 HIS C O     1 
ATOM   11979 C CB    . HIS C 1 493 ? 20.827  1.327   -8.503  1.00 32.60  ? 493 HIS C CB    1 
ATOM   11980 C CG    . HIS C 1 493 ? 22.248  0.938   -8.470  1.00 33.39  ? 493 HIS C CG    1 
ATOM   11981 N ND1   . HIS C 1 493 ? 22.908  0.507   -7.354  1.00 34.41  ? 493 HIS C ND1   1 
ATOM   11982 C CD2   . HIS C 1 493 ? 23.149  0.921   -9.466  1.00 36.47  ? 493 HIS C CD2   1 
ATOM   11983 C CE1   . HIS C 1 493 ? 24.164  0.240   -7.684  1.00 35.61  ? 493 HIS C CE1   1 
ATOM   11984 N NE2   . HIS C 1 493 ? 24.334  0.479   -8.966  1.00 31.74  ? 493 HIS C NE2   1 
ATOM   11985 N N     . GLU C 1 494 ? 17.701  0.969   -8.396  1.00 39.43  ? 494 GLU C N     1 
ATOM   11986 C CA    . GLU C 1 494 ? 16.362  1.533   -8.366  1.00 37.54  ? 494 GLU C CA    1 
ATOM   11987 C C     . GLU C 1 494 ? 15.638  1.100   -7.088  1.00 37.77  ? 494 GLU C C     1 
ATOM   11988 O O     . GLU C 1 494 ? 14.954  1.894   -6.458  1.00 36.98  ? 494 GLU C O     1 
ATOM   11989 C CB    . GLU C 1 494 ? 15.500  1.075   -9.554  1.00 45.83  ? 494 GLU C CB    1 
ATOM   11990 C CG    . GLU C 1 494 ? 16.021  1.390   -10.964 1.00 50.86  ? 494 GLU C CG    1 
ATOM   11991 C CD    . GLU C 1 494 ? 16.024  2.844   -11.423 1.00 66.56  ? 494 GLU C CD    1 
ATOM   11992 O OE1   . GLU C 1 494 ? 15.614  3.788   -10.616 1.00 60.59  ? 494 GLU C OE1   1 
ATOM   11993 O OE2   . GLU C 1 494 ? 16.434  3.050   -12.617 1.00 68.03  ? 494 GLU C OE2   1 
ATOM   11994 N N     . THR C 1 495 ? 15.749  -0.182  -6.708  1.00 36.41  ? 495 THR C N     1 
ATOM   11995 C CA    . THR C 1 495 ? 15.115  -0.637  -5.498  1.00 35.30  ? 495 THR C CA    1 
ATOM   11996 C C     . THR C 1 495 ? 15.562  0.139   -4.254  1.00 36.93  ? 495 THR C C     1 
ATOM   11997 O O     . THR C 1 495 ? 14.755  0.361   -3.365  1.00 37.67  ? 495 THR C O     1 
ATOM   11998 C CB    . THR C 1 495 ? 15.455  -2.087  -5.194  1.00 41.58  ? 495 THR C CB    1 
ATOM   11999 O OG1   . THR C 1 495 ? 14.936  -2.926  -6.223  1.00 44.76  ? 495 THR C OG1   1 
ATOM   12000 C CG2   . THR C 1 495 ? 14.903  -2.498  -3.842  1.00 40.77  ? 495 THR C CG2   1 
ATOM   12001 N N     . ILE C 1 496 ? 16.863  0.429   -4.127  1.00 31.71  ? 496 ILE C N     1 
ATOM   12002 C CA    . ILE C 1 496 ? 17.391  1.111   -2.955  1.00 31.91  ? 496 ILE C CA    1 
ATOM   12003 C C     . ILE C 1 496 ? 16.990  2.579   -3.026  1.00 39.36  ? 496 ILE C C     1 
ATOM   12004 O O     . ILE C 1 496 ? 16.661  3.193   -2.005  1.00 46.75  ? 496 ILE C O     1 
ATOM   12005 C CB    . ILE C 1 496 ? 18.918  0.944   -2.921  1.00 31.32  ? 496 ILE C CB    1 
ATOM   12006 C CG1   . ILE C 1 496 ? 19.292  -0.516  -2.690  1.00 29.66  ? 496 ILE C CG1   1 
ATOM   12007 C CG2   . ILE C 1 496 ? 19.594  1.874   -1.931  1.00 32.33  ? 496 ILE C CG2   1 
ATOM   12008 C CD1   . ILE C 1 496 ? 20.736  -0.766  -2.886  1.00 30.72  ? 496 ILE C CD1   1 
ATOM   12009 N N     . LYS C 1 497 ? 17.022  3.132   -4.245  1.00 36.48  ? 497 LYS C N     1 
ATOM   12010 C CA    . LYS C 1 497 ? 16.652  4.517   -4.484  1.00 34.00  ? 497 LYS C CA    1 
ATOM   12011 C C     . LYS C 1 497 ? 15.222  4.792   -4.027  1.00 38.89  ? 497 LYS C C     1 
ATOM   12012 O O     . LYS C 1 497 ? 14.962  5.876   -3.512  1.00 41.20  ? 497 LYS C O     1 
ATOM   12013 C CB    . LYS C 1 497 ? 16.744  4.845   -5.972  1.00 33.96  ? 497 LYS C CB    1 
ATOM   12014 C CG    . LYS C 1 497 ? 16.333  6.252   -6.374  1.00 31.02  ? 497 LYS C CG    1 
ATOM   12015 C CD    . LYS C 1 497 ? 17.148  7.336   -5.694  1.00 28.79  ? 497 LYS C CD    1 
ATOM   12016 C CE    . LYS C 1 497 ? 16.780  8.710   -6.201  1.00 32.15  ? 497 LYS C CE    1 
ATOM   12017 N NZ    . LYS C 1 497 ? 17.594  9.766   -5.554  1.00 36.73  ? 497 LYS C NZ    1 
ATOM   12018 N N     . ASP C 1 498 ? 14.310  3.822   -4.179  1.00 38.19  ? 498 ASP C N     1 
ATOM   12019 C CA    . ASP C 1 498 ? 12.924  4.043   -3.776  1.00 42.54  ? 498 ASP C CA    1 
ATOM   12020 C C     . ASP C 1 498 ? 12.735  3.879   -2.266  1.00 48.15  ? 498 ASP C C     1 
ATOM   12021 O O     . ASP C 1 498 ? 11.949  4.592   -1.655  1.00 56.41  ? 498 ASP C O     1 
ATOM   12022 C CB    . ASP C 1 498 ? 11.964  3.108   -4.507  1.00 37.13  ? 498 ASP C CB    1 
ATOM   12023 C CG    . ASP C 1 498 ? 11.883  3.417   -5.987  1.00 34.55  ? 498 ASP C CG    1 
ATOM   12024 O OD1   . ASP C 1 498 ? 11.875  4.622   -6.345  1.00 33.24  ? 498 ASP C OD1   1 
ATOM   12025 O OD2   . ASP C 1 498 ? 11.847  2.457   -6.762  1.00 37.52  ? 498 ASP C OD2   1 
ATOM   12026 N N     . ALA C 1 499 ? 13.429  2.924   -1.659  1.00 43.19  ? 499 ALA C N     1 
ATOM   12027 C CA    . ALA C 1 499 ? 13.395  2.808   -0.217  1.00 43.55  ? 499 ALA C CA    1 
ATOM   12028 C C     . ALA C 1 499 ? 13.853  4.100   0.452   1.00 41.16  ? 499 ALA C C     1 
ATOM   12029 O O     . ALA C 1 499 ? 13.218  4.590   1.379   1.00 46.47  ? 499 ALA C O     1 
ATOM   12030 C CB    . ALA C 1 499 ? 14.298  1.688   0.168   1.00 50.16  ? 499 ALA C CB    1 
ATOM   12031 N N     . LEU C 1 500 ? 15.001  4.612   0.019   1.00 41.15  ? 500 LEU C N     1 
ATOM   12032 C CA    . LEU C 1 500 ? 15.608  5.753   0.678   1.00 41.66  ? 500 LEU C CA    1 
ATOM   12033 C C     . LEU C 1 500 ? 14.991  7.060   0.220   1.00 41.30  ? 500 LEU C C     1 
ATOM   12034 O O     . LEU C 1 500 ? 15.006  8.008   0.980   1.00 40.77  ? 500 LEU C O     1 
ATOM   12035 C CB    . LEU C 1 500 ? 17.099  5.808   0.351   1.00 43.44  ? 500 LEU C CB    1 
ATOM   12036 C CG    . LEU C 1 500 ? 17.948  4.661   0.865   1.00 38.20  ? 500 LEU C CG    1 
ATOM   12037 C CD1   . LEU C 1 500 ? 19.384  4.874   0.439   1.00 44.48  ? 500 LEU C CD1   1 
ATOM   12038 C CD2   . LEU C 1 500 ? 17.852  4.557   2.371   1.00 42.46  ? 500 LEU C CD2   1 
ATOM   12039 N N     . ASP C 1 501 ? 14.550  7.130   -1.044  1.00 49.92  ? 501 ASP C N     1 
ATOM   12040 C CA    . ASP C 1 501 ? 14.009  8.360   -1.614  1.00 43.71  ? 501 ASP C CA    1 
ATOM   12041 C C     . ASP C 1 501 ? 12.669  8.113   -2.295  1.00 44.50  ? 501 ASP C C     1 
ATOM   12042 O O     . ASP C 1 501 ? 12.537  8.354   -3.500  1.00 49.44  ? 501 ASP C O     1 
ATOM   12043 C CB    . ASP C 1 501 ? 14.947  8.953   -2.659  1.00 43.44  ? 501 ASP C CB    1 
ATOM   12044 C CG    . ASP C 1 501 ? 14.690  10.419  -2.915  1.00 43.80  ? 501 ASP C CG    1 
ATOM   12045 O OD1   . ASP C 1 501 ? 13.694  10.950  -2.332  1.00 42.49  ? 501 ASP C OD1   1 
ATOM   12046 O OD2   . ASP C 1 501 ? 15.492  11.012  -3.681  1.00 39.12  ? 501 ASP C OD2   1 
ATOM   12047 N N     . PRO C 1 502 ? 11.620  7.704   -1.550  1.00 47.32  ? 502 PRO C N     1 
ATOM   12048 C CA    . PRO C 1 502 ? 10.319  7.410   -2.152  1.00 50.98  ? 502 PRO C CA    1 
ATOM   12049 C C     . PRO C 1 502 ? 9.835   8.519   -3.073  1.00 48.31  ? 502 PRO C C     1 
ATOM   12050 O O     . PRO C 1 502 ? 9.213   8.208   -4.070  1.00 46.99  ? 502 PRO C O     1 
ATOM   12051 C CB    . PRO C 1 502 ? 9.333   7.230   -0.976  1.00 47.39  ? 502 PRO C CB    1 
ATOM   12052 C CG    . PRO C 1 502 ? 10.098  7.711   0.237   1.00 52.05  ? 502 PRO C CG    1 
ATOM   12053 C CD    . PRO C 1 502 ? 11.583  7.550   -0.089  1.00 50.12  ? 502 PRO C CD    1 
ATOM   12054 N N     . ASN C 1 503 ? 10.131  9.786   -2.734  1.00 53.97  ? 503 ASN C N     1 
ATOM   12055 C CA    . ASN C 1 503 ? 9.618   10.941  -3.461  1.00 51.59  ? 503 ASN C CA    1 
ATOM   12056 C C     . ASN C 1 503 ? 10.629  11.429  -4.489  1.00 51.40  ? 503 ASN C C     1 
ATOM   12057 O O     . ASN C 1 503 ? 10.462  12.494  -5.073  1.00 57.45  ? 503 ASN C O     1 
ATOM   12058 C CB    . ASN C 1 503 ? 9.248   12.090  -2.513  1.00 56.32  ? 503 ASN C CB    1 
ATOM   12059 C CG    . ASN C 1 503 ? 8.176   11.725  -1.495  1.00 56.98  ? 503 ASN C CG    1 
ATOM   12060 O OD1   . ASN C 1 503 ? 7.132   11.158  -1.830  1.00 51.89  ? 503 ASN C OD1   1 
ATOM   12061 N ND2   . ASN C 1 503 ? 8.439   12.033  -0.234  1.00 49.35  ? 503 ASN C ND2   1 
ATOM   12062 N N     . GLY C 1 504 ? 11.704  10.665  -4.685  1.00 56.79  ? 504 GLY C N     1 
ATOM   12063 C CA    . GLY C 1 504 ? 12.731  11.023  -5.646  1.00 49.06  ? 504 GLY C CA    1 
ATOM   12064 C C     . GLY C 1 504 ? 13.051  12.513  -5.623  1.00 45.46  ? 504 GLY C C     1 
ATOM   12065 O O     . GLY C 1 504 ? 13.056  13.147  -6.657  1.00 48.83  ? 504 GLY C O     1 
ATOM   12066 N N     . ILE C 1 505 ? 13.406  13.077  -4.472  1.00 44.97  ? 505 ILE C N     1 
ATOM   12067 C CA    . ILE C 1 505 ? 13.798  14.480  -4.476  1.00 51.18  ? 505 ILE C CA    1 
ATOM   12068 C C     . ILE C 1 505 ? 15.313  14.673  -4.423  1.00 45.56  ? 505 ILE C C     1 
ATOM   12069 O O     . ILE C 1 505 ? 15.740  15.835  -4.335  1.00 46.38  ? 505 ILE C O     1 
ATOM   12070 C CB    . ILE C 1 505 ? 13.077  15.300  -3.385  1.00 49.84  ? 505 ILE C CB    1 
ATOM   12071 C CG1   . ILE C 1 505 ? 13.204  14.687  -1.992  1.00 50.27  ? 505 ILE C CG1   1 
ATOM   12072 C CG2   . ILE C 1 505 ? 11.622  15.470  -3.773  1.00 56.42  ? 505 ILE C CG2   1 
ATOM   12073 C CD1   . ILE C 1 505 ? 14.631  14.589  -1.511  1.00 59.15  ? 505 ILE C CD1   1 
ATOM   12074 N N     . LEU C 1 506 ? 16.119  13.596  -4.497  1.00 39.93  ? 506 LEU C N     1 
ATOM   12075 C CA    . LEU C 1 506 ? 17.566  13.801  -4.621  1.00 48.62  ? 506 LEU C CA    1 
ATOM   12076 C C     . LEU C 1 506 ? 18.112  13.452  -6.006  1.00 42.79  ? 506 LEU C C     1 
ATOM   12077 O O     . LEU C 1 506 ? 18.064  12.294  -6.423  1.00 38.31  ? 506 LEU C O     1 
ATOM   12078 C CB    . LEU C 1 506 ? 18.336  13.034  -3.553  1.00 50.32  ? 506 LEU C CB    1 
ATOM   12079 C CG    . LEU C 1 506 ? 18.803  13.864  -2.367  1.00 60.06  ? 506 LEU C CG    1 
ATOM   12080 C CD1   . LEU C 1 506 ? 19.726  13.036  -1.479  1.00 68.13  ? 506 LEU C CD1   1 
ATOM   12081 C CD2   . LEU C 1 506 ? 19.504  15.133  -2.830  1.00 63.93  ? 506 LEU C CD2   1 
ATOM   12082 N N     . ALA C 1 507 ? 18.643  14.490  -6.679  1.00 44.22  ? 507 ALA C N     1 
ATOM   12083 C CA    . ALA C 1 507 ? 19.366  14.392  -7.951  1.00 46.60  ? 507 ALA C CA    1 
ATOM   12084 C C     . ALA C 1 507 ? 18.826  13.272  -8.837  1.00 44.81  ? 507 ALA C C     1 
ATOM   12085 O O     . ALA C 1 507 ? 19.540  12.325  -9.143  1.00 48.55  ? 507 ALA C O     1 
ATOM   12086 C CB    . ALA C 1 507 ? 20.845  14.178  -7.689  1.00 48.37  ? 507 ALA C CB    1 
ATOM   12087 N N     . PRO C 1 508 ? 17.559  13.327  -9.290  1.00 49.62  ? 508 PRO C N     1 
ATOM   12088 C CA    . PRO C 1 508 ? 17.007  12.251  -10.108 1.00 55.20  ? 508 PRO C CA    1 
ATOM   12089 C C     . PRO C 1 508 ? 17.736  12.220  -11.453 1.00 48.17  ? 508 PRO C C     1 
ATOM   12090 O O     . PRO C 1 508 ? 17.868  13.272  -12.077 1.00 52.13  ? 508 PRO C O     1 
ATOM   12091 C CB    . PRO C 1 508 ? 15.502  12.596  -10.206 1.00 51.93  ? 508 PRO C CB    1 
ATOM   12092 C CG    . PRO C 1 508 ? 15.442  14.072  -9.983  1.00 44.25  ? 508 PRO C CG    1 
ATOM   12093 C CD    . PRO C 1 508 ? 16.593  14.411  -9.060  1.00 48.52  ? 508 PRO C CD    1 
ATOM   12094 N N     . GLY C 1 509 ? 18.238  11.036  -11.845 1.00 35.82  ? 509 GLY C N     1 
ATOM   12095 C CA    . GLY C 1 509 ? 19.101  10.913  -13.014 1.00 37.27  ? 509 GLY C CA    1 
ATOM   12096 C C     . GLY C 1 509 ? 20.587  10.662  -12.722 1.00 40.19  ? 509 GLY C C     1 
ATOM   12097 O O     . GLY C 1 509 ? 21.304  10.192  -13.605 1.00 44.12  ? 509 GLY C O     1 
ATOM   12098 N N     . LYS C 1 510 ? 21.095  10.992  -11.524 1.00 37.06  ? 510 LYS C N     1 
ATOM   12099 C CA    . LYS C 1 510 ? 22.518  10.840  -11.267 1.00 38.40  ? 510 LYS C CA    1 
ATOM   12100 C C     . LYS C 1 510 ? 22.895  9.373   -11.457 1.00 38.95  ? 510 LYS C C     1 
ATOM   12101 O O     . LYS C 1 510 ? 22.155  8.499   -11.034 1.00 38.04  ? 510 LYS C O     1 
ATOM   12102 C CB    . LYS C 1 510 ? 22.866  11.346  -9.859  1.00 50.88  ? 510 LYS C CB    1 
ATOM   12103 C CG    . LYS C 1 510 ? 24.313  11.193  -9.402  1.00 51.60  ? 510 LYS C CG    1 
ATOM   12104 C CD    . LYS C 1 510 ? 25.293  12.110  -10.076 1.00 60.66  ? 510 LYS C CD    1 
ATOM   12105 C CE    . LYS C 1 510 ? 26.737  11.951  -9.632  1.00 62.69  ? 510 LYS C CE    1 
ATOM   12106 N NZ    . LYS C 1 510 ? 27.566  11.181  -10.596 1.00 60.38  ? 510 LYS C NZ    1 
ATOM   12107 N N     . SER C 1 511 ? 24.005  9.114   -12.168 1.00 37.31  ? 511 SER C N     1 
ATOM   12108 C CA    . SER C 1 511 ? 24.455  7.772   -12.476 1.00 37.40  ? 511 SER C CA    1 
ATOM   12109 C C     . SER C 1 511 ? 23.353  6.950   -13.137 1.00 37.03  ? 511 SER C C     1 
ATOM   12110 O O     . SER C 1 511 ? 23.444  5.723   -13.247 1.00 35.46  ? 511 SER C O     1 
ATOM   12111 C CB    . SER C 1 511 ? 25.001  7.103   -11.248 1.00 43.91  ? 511 SER C CB    1 
ATOM   12112 O OG    . SER C 1 511 ? 26.026  7.884   -10.656 1.00 43.30  ? 511 SER C OG    1 
ATOM   12113 N N     . GLY C 1 512 ? 22.357  7.665   -13.667 1.00 40.62  ? 512 GLY C N     1 
ATOM   12114 C CA    . GLY C 1 512 ? 21.228  7.068   -14.359 1.00 39.71  ? 512 GLY C CA    1 
ATOM   12115 C C     . GLY C 1 512 ? 20.286  6.310   -13.434 1.00 37.98  ? 512 GLY C C     1 
ATOM   12116 O O     . GLY C 1 512 ? 19.744  5.277   -13.806 1.00 36.91  ? 512 GLY C O     1 
ATOM   12117 N N     . ILE C 1 513 ? 20.085  6.839   -12.231 1.00 39.14  ? 513 ILE C N     1 
ATOM   12118 C CA    . ILE C 1 513 ? 19.162  6.236   -11.292 1.00 36.71  ? 513 ILE C CA    1 
ATOM   12119 C C     . ILE C 1 513 ? 18.024  7.221   -11.169 1.00 42.39  ? 513 ILE C C     1 
ATOM   12120 O O     . ILE C 1 513 ? 18.268  8.365   -10.820 1.00 38.71  ? 513 ILE C O     1 
ATOM   12121 C CB    . ILE C 1 513 ? 19.843  5.998   -9.940  1.00 42.94  ? 513 ILE C CB    1 
ATOM   12122 C CG1   . ILE C 1 513 ? 21.133  5.188   -10.102 1.00 41.59  ? 513 ILE C CG1   1 
ATOM   12123 C CG2   . ILE C 1 513 ? 18.855  5.389   -8.961  1.00 45.33  ? 513 ILE C CG2   1 
ATOM   12124 C CD1   . ILE C 1 513 ? 22.036  5.136   -8.882  1.00 41.04  ? 513 ILE C CD1   1 
ATOM   12125 N N     . TRP C 1 514 ? 16.795  6.791   -11.469 1.00 51.49  ? 514 TRP C N     1 
ATOM   12126 C CA    . TRP C 1 514 ? 15.753  7.778   -11.656 1.00 48.10  ? 514 TRP C CA    1 
ATOM   12127 C C     . TRP C 1 514 ? 14.753  7.852   -10.488 1.00 53.87  ? 514 TRP C C     1 
ATOM   12128 O O     . TRP C 1 514 ? 14.410  8.957   -10.031 1.00 65.58  ? 514 TRP C O     1 
ATOM   12129 C CB    . TRP C 1 514 ? 15.130  7.555   -13.031 1.00 50.69  ? 514 TRP C CB    1 
ATOM   12130 C CG    . TRP C 1 514 ? 15.950  8.219   -14.097 1.00 48.68  ? 514 TRP C CG    1 
ATOM   12131 C CD1   . TRP C 1 514 ? 16.830  7.645   -14.974 1.00 44.57  ? 514 TRP C CD1   1 
ATOM   12132 C CD2   . TRP C 1 514 ? 15.952  9.630   -14.394 1.00 44.89  ? 514 TRP C CD2   1 
ATOM   12133 N NE1   . TRP C 1 514 ? 17.396  8.606   -15.780 1.00 37.70  ? 514 TRP C NE1   1 
ATOM   12134 C CE2   . TRP C 1 514 ? 16.878  9.833   -15.441 1.00 40.39  ? 514 TRP C CE2   1 
ATOM   12135 C CE3   . TRP C 1 514 ? 15.279  10.734  -13.861 1.00 40.55  ? 514 TRP C CE3   1 
ATOM   12136 C CZ2   . TRP C 1 514 ? 17.119  11.103  -15.970 1.00 40.07  ? 514 TRP C CZ2   1 
ATOM   12137 C CZ3   . TRP C 1 514 ? 15.548  11.987  -14.364 1.00 41.37  ? 514 TRP C CZ3   1 
ATOM   12138 C CH2   . TRP C 1 514 ? 16.447  12.165  -15.411 1.00 39.26  ? 514 TRP C CH2   1 
ATOM   12139 N N     . GLY C 1 515 ? 14.280  6.718   -9.973  1.00 45.94  ? 515 GLY C N     1 
ATOM   12140 C CA    . GLY C 1 515 ? 13.202  6.776   -8.986  1.00 47.17  ? 515 GLY C CA    1 
ATOM   12141 C C     . GLY C 1 515 ? 11.841  6.466   -9.607  1.00 45.93  ? 515 GLY C C     1 
ATOM   12142 O O     . GLY C 1 515 ? 11.664  6.630   -10.801 1.00 45.06  ? 515 GLY C O     1 
ATOM   12143 N N     . LYS C 1 516 ? 10.891  5.990   -8.799  1.00 57.71  ? 516 LYS C N     1 
ATOM   12144 C CA    . LYS C 1 516 ? 9.618   5.466   -9.294  1.00 58.85  ? 516 LYS C CA    1 
ATOM   12145 C C     . LYS C 1 516 ? 8.881   6.498   -10.137 1.00 51.66  ? 516 LYS C C     1 
ATOM   12146 O O     . LYS C 1 516 ? 8.352   6.148   -11.176 1.00 58.30  ? 516 LYS C O     1 
ATOM   12147 C CB    . LYS C 1 516 ? 8.680   5.043   -8.157  1.00 66.93  ? 516 LYS C CB    1 
ATOM   12148 C CG    . LYS C 1 516 ? 8.642   3.548   -7.897  1.00 86.86  ? 516 LYS C CG    1 
ATOM   12149 C CD    . LYS C 1 516 ? 8.038   3.154   -6.570  1.00 100.45 ? 516 LYS C CD    1 
ATOM   12150 C CE    . LYS C 1 516 ? 8.430   1.741   -6.175  1.00 107.65 ? 516 LYS C CE    1 
ATOM   12151 N NZ    . LYS C 1 516 ? 8.303   1.527   -4.713  1.00 111.50 ? 516 LYS C NZ    1 
ATOM   12152 N N     . ASN C 1 517 ? 8.862   7.757   -9.689  1.00 50.44  ? 517 ASN C N     1 
ATOM   12153 C CA    . ASN C 1 517 ? 7.992   8.769   -10.262 1.00 55.53  ? 517 ASN C CA    1 
ATOM   12154 C C     . ASN C 1 517 ? 8.466   9.185   -11.661 1.00 67.28  ? 517 ASN C C     1 
ATOM   12155 O O     . ASN C 1 517 ? 7.634   9.390   -12.533 1.00 69.14  ? 517 ASN C O     1 
ATOM   12156 C CB    . ASN C 1 517 ? 7.803   9.944   -9.295  1.00 53.54  ? 517 ASN C CB    1 
ATOM   12157 C CG    . ASN C 1 517 ? 7.181   9.489   -7.983  1.00 57.40  ? 517 ASN C CG    1 
ATOM   12158 O OD1   . ASN C 1 517 ? 6.526   8.444   -7.924  1.00 55.63  ? 517 ASN C OD1   1 
ATOM   12159 N ND2   . ASN C 1 517 ? 7.396   10.245  -6.920  1.00 47.41  ? 517 ASN C ND2   1 
ATOM   12160 N N     . ARG C 1 518 ? 9.781   9.279   -11.907 1.00 71.72  ? 518 ARG C N     1 
ATOM   12161 C CA    . ARG C 1 518 ? 10.266  9.719   -13.208 1.00 67.81  ? 518 ARG C CA    1 
ATOM   12162 C C     . ARG C 1 518 ? 10.674  8.550   -14.119 1.00 73.89  ? 518 ARG C C     1 
ATOM   12163 O O     . ARG C 1 518 ? 11.282  8.788   -15.158 1.00 84.27  ? 518 ARG C O     1 
ATOM   12164 C CB    . ARG C 1 518 ? 11.391  10.732  -12.997 1.00 63.41  ? 518 ARG C CB    1 
ATOM   12165 C CG    . ARG C 1 518 ? 10.876  12.073  -12.513 1.00 70.19  ? 518 ARG C CG    1 
ATOM   12166 C CD    . ARG C 1 518 ? 11.919  12.857  -11.754 1.00 86.44  ? 518 ARG C CD    1 
ATOM   12167 N NE    . ARG C 1 518 ? 11.266  13.739  -10.794 1.00 95.31  ? 518 ARG C NE    1 
ATOM   12168 C CZ    . ARG C 1 518 ? 11.685  14.952  -10.469 1.00 113.34 ? 518 ARG C CZ    1 
ATOM   12169 N NH1   . ARG C 1 518 ? 12.872  15.383  -10.864 1.00 141.11 ? 518 ARG C NH1   1 
ATOM   12170 N NH2   . ARG C 1 518 ? 10.914  15.718  -9.717  1.00 113.64 ? 518 ARG C NH2   1 
ATOM   12171 N N     . ARG C 1 519 ? 10.299  7.305   -13.782 1.00 77.80  ? 519 ARG C N     1 
ATOM   12172 C CA    . ARG C 1 519 ? 10.567  6.135   -14.619 1.00 80.71  ? 519 ARG C CA    1 
ATOM   12173 C C     . ARG C 1 519 ? 9.298   5.658   -15.346 1.00 87.77  ? 519 ARG C C     1 
ATOM   12174 O O     . ARG C 1 519 ? 8.200   5.894   -14.795 1.00 85.52  ? 519 ARG C O     1 
ATOM   12175 C CB    . ARG C 1 519 ? 11.072  4.964   -13.771 1.00 71.90  ? 519 ARG C CB    1 
ATOM   12176 C CG    . ARG C 1 519 ? 12.573  4.748   -13.807 1.00 69.30  ? 519 ARG C CG    1 
ATOM   12177 C CD    . ARG C 1 519 ? 13.093  3.846   -12.689 1.00 72.75  ? 519 ARG C CD    1 
ATOM   12178 N NE    . ARG C 1 519 ? 12.180  2.868   -12.069 1.00 70.15  ? 519 ARG C NE    1 
ATOM   12179 C CZ    . ARG C 1 519 ? 12.008  2.698   -10.747 1.00 61.05  ? 519 ARG C CZ    1 
ATOM   12180 N NH1   . ARG C 1 519 ? 12.728  3.375   -9.868  1.00 61.39  ? 519 ARG C NH1   1 
ATOM   12181 N NH2   . ARG C 1 519 ? 11.123  1.829   -10.293 1.00 53.38  ? 519 ARG C NH2   1 
HETATM 12182 P PA    . FAD D 2 .   ? 2.576   14.464  39.384  1.00 73.74  ? 601 FAD A PA    1 
HETATM 12183 O O1A   . FAD D 2 .   ? 2.429   14.518  37.893  1.00 74.38  ? 601 FAD A O1A   1 
HETATM 12184 O O2A   . FAD D 2 .   ? 1.312   14.428  40.173  1.00 79.44  ? 601 FAD A O2A   1 
HETATM 12185 O O5B   . FAD D 2 .   ? 3.457   13.165  39.702  1.00 84.01  ? 601 FAD A O5B   1 
HETATM 12186 C C5B   . FAD D 2 .   ? 4.740   12.933  39.040  1.00 89.04  ? 601 FAD A C5B   1 
HETATM 12187 C C4B   . FAD D 2 .   ? 4.840   11.498  38.565  1.00 84.96  ? 601 FAD A C4B   1 
HETATM 12188 O O4B   . FAD D 2 .   ? 5.273   10.630  39.648  1.00 82.34  ? 601 FAD A O4B   1 
HETATM 12189 C C3B   . FAD D 2 .   ? 3.535   10.862  38.062  1.00 80.77  ? 601 FAD A C3B   1 
HETATM 12190 O O3B   . FAD D 2 .   ? 3.345   11.108  36.681  1.00 68.00  ? 601 FAD A O3B   1 
HETATM 12191 C C2B   . FAD D 2 .   ? 3.703   9.374   38.404  1.00 76.51  ? 601 FAD A C2B   1 
HETATM 12192 O O2B   . FAD D 2 .   ? 4.437   8.549   37.516  1.00 67.52  ? 601 FAD A O2B   1 
HETATM 12193 C C1B   . FAD D 2 .   ? 4.403   9.515   39.749  1.00 69.12  ? 601 FAD A C1B   1 
HETATM 12194 N N9A   . FAD D 2 .   ? 3.483   9.753   40.872  1.00 63.14  ? 601 FAD A N9A   1 
HETATM 12195 C C8A   . FAD D 2 .   ? 3.061   10.971  41.367  1.00 62.72  ? 601 FAD A C8A   1 
HETATM 12196 N N7A   . FAD D 2 .   ? 2.267   10.856  42.403  1.00 56.35  ? 601 FAD A N7A   1 
HETATM 12197 C C5A   . FAD D 2 .   ? 2.165   9.489   42.607  1.00 50.95  ? 601 FAD A C5A   1 
HETATM 12198 C C6A   . FAD D 2 .   ? 1.490   8.743   43.588  1.00 51.01  ? 601 FAD A C6A   1 
HETATM 12199 N N6A   . FAD D 2 .   ? 0.732   9.305   44.535  1.00 49.95  ? 601 FAD A N6A   1 
HETATM 12200 N N1A   . FAD D 2 .   ? 1.634   7.391   43.536  1.00 50.30  ? 601 FAD A N1A   1 
HETATM 12201 C C2A   . FAD D 2 .   ? 2.371   6.860   42.542  1.00 55.55  ? 601 FAD A C2A   1 
HETATM 12202 N N3A   . FAD D 2 .   ? 3.039   7.468   41.558  1.00 50.39  ? 601 FAD A N3A   1 
HETATM 12203 C C4A   . FAD D 2 .   ? 2.909   8.800   41.669  1.00 52.94  ? 601 FAD A C4A   1 
HETATM 12204 N N1    . FAD D 2 .   ? 10.321  20.683  38.940  1.00 55.83  ? 601 FAD A N1    1 
HETATM 12205 C C2    . FAD D 2 .   ? 11.103  20.861  40.019  1.00 52.04  ? 601 FAD A C2    1 
HETATM 12206 O O2    . FAD D 2 .   ? 11.297  19.926  40.790  1.00 55.75  ? 601 FAD A O2    1 
HETATM 12207 N N3    . FAD D 2 .   ? 11.686  22.089  40.322  1.00 56.02  ? 601 FAD A N3    1 
HETATM 12208 C C4    . FAD D 2 .   ? 11.508  23.185  39.511  1.00 57.97  ? 601 FAD A C4    1 
HETATM 12209 O O4    . FAD D 2 .   ? 12.041  24.251  39.772  1.00 57.00  ? 601 FAD A O4    1 
HETATM 12210 C C4X   . FAD D 2 .   ? 10.700  23.022  38.374  1.00 67.80  ? 601 FAD A C4X   1 
HETATM 12211 N N5    . FAD D 2 .   ? 10.537  24.056  37.605  1.00 77.20  ? 601 FAD A N5    1 
HETATM 12212 C C5X   . FAD D 2 .   ? 9.737   23.903  36.508  1.00 79.34  ? 601 FAD A C5X   1 
HETATM 12213 C C6    . FAD D 2 .   ? 9.566   25.012  35.660  1.00 77.46  ? 601 FAD A C6    1 
HETATM 12214 C C7    . FAD D 2 .   ? 8.786   24.947  34.530  1.00 76.03  ? 601 FAD A C7    1 
HETATM 12215 C C7M   . FAD D 2 .   ? 8.615   26.177  33.670  1.00 67.22  ? 601 FAD A C7M   1 
HETATM 12216 C C8    . FAD D 2 .   ? 8.148   23.711  34.206  1.00 78.50  ? 601 FAD A C8    1 
HETATM 12217 C C8M   . FAD D 2 .   ? 7.237   23.593  33.010  1.00 79.93  ? 601 FAD A C8M   1 
HETATM 12218 C C9    . FAD D 2 .   ? 8.319   22.616  35.023  1.00 76.21  ? 601 FAD A C9    1 
HETATM 12219 C C9A   . FAD D 2 .   ? 9.101   22.683  36.190  1.00 76.23  ? 601 FAD A C9A   1 
HETATM 12220 N N10   . FAD D 2 .   ? 9.287   21.592  37.042  1.00 68.97  ? 601 FAD A N10   1 
HETATM 12221 C C10   . FAD D 2 .   ? 10.114  21.718  38.150  1.00 69.88  ? 601 FAD A C10   1 
HETATM 12222 C "C1'" . FAD D 2 .   ? 8.658   20.289  36.720  1.00 74.35  ? 601 FAD A "C1'" 1 
HETATM 12223 C "C2'" . FAD D 2 .   ? 7.188   20.135  37.216  1.00 82.66  ? 601 FAD A "C2'" 1 
HETATM 12224 O "O2'" . FAD D 2 .   ? 6.247   21.061  36.602  1.00 75.03  ? 601 FAD A "O2'" 1 
HETATM 12225 C "C3'" . FAD D 2 .   ? 7.102   20.252  38.747  1.00 80.96  ? 601 FAD A "C3'" 1 
HETATM 12226 O "O3'" . FAD D 2 .   ? 8.032   19.360  39.338  1.00 82.47  ? 601 FAD A "O3'" 1 
HETATM 12227 C "C4'" . FAD D 2 .   ? 5.726   19.955  39.358  1.00 76.30  ? 601 FAD A "C4'" 1 
HETATM 12228 O "O4'" . FAD D 2 .   ? 5.594   20.744  40.539  1.00 83.92  ? 601 FAD A "O4'" 1 
HETATM 12229 C "C5'" . FAD D 2 .   ? 5.506   18.498  39.712  1.00 73.22  ? 601 FAD A "C5'" 1 
HETATM 12230 O "O5'" . FAD D 2 .   ? 4.209   17.988  39.239  1.00 65.47  ? 601 FAD A "O5'" 1 
HETATM 12231 P P     . FAD D 2 .   ? 3.200   17.212  40.238  1.00 68.22  ? 601 FAD A P     1 
HETATM 12232 O O1P   . FAD D 2 .   ? 3.574   17.672  41.608  1.00 67.79  ? 601 FAD A O1P   1 
HETATM 12233 O O2P   . FAD D 2 .   ? 1.780   17.385  39.803  1.00 67.55  ? 601 FAD A O2P   1 
HETATM 12234 O O3P   . FAD D 2 .   ? 3.470   15.643  40.021  1.00 53.42  ? 601 FAD A O3P   1 
HETATM 12235 P PA    . FAD E 2 .   ? 29.037  -6.725  60.676  1.00 59.27  ? 601 FAD B PA    1 
HETATM 12236 O O1A   . FAD E 2 .   ? 28.854  -7.793  61.710  1.00 63.43  ? 601 FAD B O1A   1 
HETATM 12237 O O2A   . FAD E 2 .   ? 30.066  -6.994  59.631  1.00 61.57  ? 601 FAD B O2A   1 
HETATM 12238 O O5B   . FAD E 2 .   ? 27.615  -6.457  59.981  1.00 63.10  ? 601 FAD B O5B   1 
HETATM 12239 C C5B   . FAD E 2 .   ? 26.396  -6.299  60.756  1.00 57.49  ? 601 FAD B C5B   1 
HETATM 12240 C C4B   . FAD E 2 .   ? 25.251  -7.002  60.062  1.00 66.64  ? 601 FAD B C4B   1 
HETATM 12241 O O4B   . FAD E 2 .   ? 24.953  -6.384  58.775  1.00 66.08  ? 601 FAD B O4B   1 
HETATM 12242 C C3B   . FAD E 2 .   ? 25.474  -8.487  59.749  1.00 62.22  ? 601 FAD B C3B   1 
HETATM 12243 O O3B   . FAD E 2 .   ? 24.987  -9.277  60.818  1.00 70.75  ? 601 FAD B O3B   1 
HETATM 12244 C C2B   . FAD E 2 .   ? 24.609  -8.718  58.502  1.00 63.79  ? 601 FAD B C2B   1 
HETATM 12245 O O2B   . FAD E 2 .   ? 23.248  -9.026  58.763  1.00 57.05  ? 601 FAD B O2B   1 
HETATM 12246 C C1B   . FAD E 2 .   ? 24.740  -7.376  57.785  1.00 59.69  ? 601 FAD B C1B   1 
HETATM 12247 N N9A   . FAD E 2 .   ? 25.835  -7.295  56.794  1.00 65.39  ? 601 FAD B N9A   1 
HETATM 12248 C C8A   . FAD E 2 .   ? 27.172  -6.998  56.999  1.00 61.54  ? 601 FAD B C8A   1 
HETATM 12249 N N7A   . FAD E 2 .   ? 27.863  -6.968  55.883  1.00 55.18  ? 601 FAD B N7A   1 
HETATM 12250 C C5A   . FAD E 2 .   ? 26.937  -7.246  54.889  1.00 62.64  ? 601 FAD B C5A   1 
HETATM 12251 C C6A   . FAD E 2 .   ? 27.044  -7.331  53.485  1.00 67.23  ? 601 FAD B C6A   1 
HETATM 12252 N N6A   . FAD E 2 .   ? 28.190  -7.165  52.825  1.00 59.33  ? 601 FAD B N6A   1 
HETATM 12253 N N1A   . FAD E 2 .   ? 25.911  -7.610  52.785  1.00 64.29  ? 601 FAD B N1A   1 
HETATM 12254 C C2A   . FAD E 2 .   ? 24.770  -7.799  53.462  1.00 58.52  ? 601 FAD B C2A   1 
HETATM 12255 N N3A   . FAD E 2 .   ? 24.556  -7.742  54.776  1.00 59.30  ? 601 FAD B N3A   1 
HETATM 12256 C C4A   . FAD E 2 .   ? 25.689  -7.450  55.439  1.00 61.18  ? 601 FAD B C4A   1 
HETATM 12257 N N1    . FAD E 2 .   ? 27.583  0.587   66.953  1.00 68.81  ? 601 FAD B N1    1 
HETATM 12258 C C2    . FAD E 2 .   ? 27.453  1.858   66.484  1.00 77.93  ? 601 FAD B C2    1 
HETATM 12259 O O2    . FAD E 2 .   ? 26.889  2.070   65.407  1.00 67.81  ? 601 FAD B O2    1 
HETATM 12260 N N3    . FAD E 2 .   ? 27.941  2.956   67.181  1.00 83.41  ? 601 FAD B N3    1 
HETATM 12261 C C4    . FAD E 2 .   ? 28.606  2.821   68.385  1.00 80.59  ? 601 FAD B C4    1 
HETATM 12262 O O4    . FAD E 2 .   ? 29.028  3.826   68.964  1.00 63.46  ? 601 FAD B O4    1 
HETATM 12263 C C4X   . FAD E 2 .   ? 28.767  1.469   68.898  1.00 75.43  ? 601 FAD B C4X   1 
HETATM 12264 N N5    . FAD E 2 .   ? 29.380  1.291   70.046  1.00 75.50  ? 601 FAD B N5    1 
HETATM 12265 C C5X   . FAD E 2 .   ? 29.497  0.007   70.509  1.00 72.69  ? 601 FAD B C5X   1 
HETATM 12266 C C6    . FAD E 2 .   ? 30.156  -0.217  71.733  1.00 68.45  ? 601 FAD B C6    1 
HETATM 12267 C C7    . FAD E 2 .   ? 30.308  -1.484  72.252  1.00 72.07  ? 601 FAD B C7    1 
HETATM 12268 C C7M   . FAD E 2 .   ? 31.026  -1.669  73.569  1.00 68.76  ? 601 FAD B C7M   1 
HETATM 12269 C C8    . FAD E 2 .   ? 29.791  -2.604  71.520  1.00 73.99  ? 601 FAD B C8    1 
HETATM 12270 C C8M   . FAD E 2 .   ? 29.974  -4.031  71.981  1.00 70.40  ? 601 FAD B C8M   1 
HETATM 12271 C C9    . FAD E 2 .   ? 29.161  -2.387  70.324  1.00 84.18  ? 601 FAD B C9    1 
HETATM 12272 C C9A   . FAD E 2 .   ? 28.993  -1.097  69.797  1.00 75.38  ? 601 FAD B C9A   1 
HETATM 12273 N N10   . FAD E 2 .   ? 28.371  -0.876  68.574  1.00 65.30  ? 601 FAD B N10   1 
HETATM 12274 C C10   . FAD E 2 .   ? 28.215  0.402   68.093  1.00 66.38  ? 601 FAD B C10   1 
HETATM 12275 C "C1'" . FAD E 2 .   ? 27.844  -2.026  67.812  1.00 66.97  ? 601 FAD B "C1'" 1 
HETATM 12276 C "C2'" . FAD E 2 .   ? 28.894  -2.698  66.912  1.00 66.64  ? 601 FAD B "C2'" 1 
HETATM 12277 O "O2'" . FAD E 2 .   ? 30.110  -3.068  67.563  1.00 69.53  ? 601 FAD B "O2'" 1 
HETATM 12278 C "C3'" . FAD E 2 .   ? 29.254  -1.794  65.732  1.00 63.60  ? 601 FAD B "C3'" 1 
HETATM 12279 O "O3'" . FAD E 2 .   ? 28.083  -1.530  65.003  1.00 61.31  ? 601 FAD B "O3'" 1 
HETATM 12280 C "C4'" . FAD E 2 .   ? 30.237  -2.410  64.744  1.00 69.80  ? 601 FAD B "C4'" 1 
HETATM 12281 O "O4'" . FAD E 2 .   ? 30.856  -1.361  63.998  1.00 70.82  ? 601 FAD B "O4'" 1 
HETATM 12282 C "C5'" . FAD E 2 .   ? 29.556  -3.386  63.809  1.00 66.75  ? 601 FAD B "C5'" 1 
HETATM 12283 O "O5'" . FAD E 2 .   ? 30.492  -4.417  63.390  1.00 65.48  ? 601 FAD B "O5'" 1 
HETATM 12284 P P     . FAD E 2 .   ? 30.754  -4.680  61.822  1.00 70.60  ? 601 FAD B P     1 
HETATM 12285 O O1P   . FAD E 2 .   ? 30.971  -3.332  61.215  1.00 55.52  ? 601 FAD B O1P   1 
HETATM 12286 O O2P   . FAD E 2 .   ? 31.786  -5.766  61.711  1.00 55.40  ? 601 FAD B O2P   1 
HETATM 12287 O O3P   . FAD E 2 .   ? 29.354  -5.280  61.296  1.00 57.15  ? 601 FAD B O3P   1 
HETATM 12288 P PA    . FAD F 2 .   ? 31.372  19.009  -7.445  1.00 75.06  ? 601 FAD C PA    1 
HETATM 12289 O O1A   . FAD F 2 .   ? 30.312  19.647  -8.311  1.00 68.30  ? 601 FAD C O1A   1 
HETATM 12290 O O2A   . FAD F 2 .   ? 31.418  19.186  -5.962  1.00 66.79  ? 601 FAD C O2A   1 
HETATM 12291 O O5B   . FAD F 2 .   ? 31.439  17.468  -7.824  1.00 75.01  ? 601 FAD C O5B   1 
HETATM 12292 C C5B   . FAD F 2 .   ? 30.248  17.032  -8.522  1.00 94.20  ? 601 FAD C C5B   1 
HETATM 12293 C C4B   . FAD F 2 .   ? 29.742  15.947  -7.638  1.00 99.94  ? 601 FAD C C4B   1 
HETATM 12294 O O4B   . FAD F 2 .   ? 28.347  16.052  -7.276  1.00 102.87 ? 601 FAD C O4B   1 
HETATM 12295 C C3B   . FAD F 2 .   ? 29.902  14.500  -8.125  1.00 114.62 ? 601 FAD C C3B   1 
HETATM 12296 O O3B   . FAD F 2 .   ? 31.026  13.976  -7.429  1.00 110.84 ? 601 FAD C O3B   1 
HETATM 12297 C C2B   . FAD F 2 .   ? 28.599  13.863  -7.629  1.00 111.40 ? 601 FAD C C2B   1 
HETATM 12298 O O2B   . FAD F 2 .   ? 28.817  12.510  -7.273  1.00 119.49 ? 601 FAD C O2B   1 
HETATM 12299 C C1B   . FAD F 2 .   ? 28.413  14.885  -6.520  1.00 91.30  ? 601 FAD C C1B   1 
HETATM 12300 N N9A   . FAD F 2 .   ? 27.497  14.780  -5.464  1.00 83.51  ? 601 FAD C N9A   1 
HETATM 12301 C C8A   . FAD F 2 .   ? 26.382  13.967  -5.342  1.00 100.09 ? 601 FAD C C8A   1 
HETATM 12302 N N7A   . FAD F 2 .   ? 25.893  13.970  -4.121  1.00 77.74  ? 601 FAD C N7A   1 
HETATM 12303 C C5A   . FAD F 2 .   ? 26.792  14.747  -3.401  1.00 57.93  ? 601 FAD C C5A   1 
HETATM 12304 C C6A   . FAD F 2 .   ? 26.803  15.143  -2.067  1.00 54.90  ? 601 FAD C C6A   1 
HETATM 12305 N N6A   . FAD F 2 .   ? 25.863  14.724  -1.252  1.00 64.65  ? 601 FAD C N6A   1 
HETATM 12306 N N1A   . FAD F 2 .   ? 27.809  15.941  -1.614  1.00 53.68  ? 601 FAD C N1A   1 
HETATM 12307 C C2A   . FAD F 2 .   ? 28.722  16.322  -2.528  1.00 63.08  ? 601 FAD C C2A   1 
HETATM 12308 N N3A   . FAD F 2 .   ? 28.798  16.051  -3.841  1.00 48.00  ? 601 FAD C N3A   1 
HETATM 12309 C C4A   . FAD F 2 .   ? 27.790  15.240  -4.208  1.00 61.06  ? 601 FAD C C4A   1 
HETATM 12310 N N1    . FAD F 2 .   ? 39.347  15.151  -11.668 1.00 82.53  ? 601 FAD C N1    1 
HETATM 12311 C C2    . FAD F 2 .   ? 40.165  14.271  -11.068 1.00 78.30  ? 601 FAD C C2    1 
HETATM 12312 O O2    . FAD F 2 .   ? 39.723  13.491  -10.221 1.00 65.75  ? 601 FAD C O2    1 
HETATM 12313 N N3    . FAD F 2 .   ? 41.514  14.222  -11.345 1.00 95.03  ? 601 FAD C N3    1 
HETATM 12314 C C4    . FAD F 2 .   ? 42.098  15.068  -12.261 1.00 95.67  ? 601 FAD C C4    1 
HETATM 12315 O O4    . FAD F 2 .   ? 43.307  14.999  -12.478 1.00 90.27  ? 601 FAD C O4    1 
HETATM 12316 C C4X   . FAD F 2 .   ? 41.249  16.010  -12.912 1.00 89.35  ? 601 FAD C C4X   1 
HETATM 12317 N N5    . FAD F 2 .   ? 41.776  16.823  -13.786 1.00 93.08  ? 601 FAD C N5    1 
HETATM 12318 C C5X   . FAD F 2 .   ? 40.940  17.709  -14.406 1.00 104.74 ? 601 FAD C C5X   1 
HETATM 12319 C C6    . FAD F 2 .   ? 41.494  18.584  -15.355 1.00 103.21 ? 601 FAD C C6    1 
HETATM 12320 C C7    . FAD F 2 .   ? 40.726  19.515  -16.010 1.00 105.86 ? 601 FAD C C7    1 
HETATM 12321 C C7M   . FAD F 2 .   ? 41.384  20.454  -16.988 1.00 107.15 ? 601 FAD C C7M   1 
HETATM 12322 C C8    . FAD F 2 .   ? 39.328  19.583  -15.732 1.00 107.33 ? 601 FAD C C8    1 
HETATM 12323 C C8M   . FAD F 2 .   ? 38.437  20.597  -16.403 1.00 113.94 ? 601 FAD C C8M   1 
HETATM 12324 C C9    . FAD F 2 .   ? 38.776  18.721  -14.813 1.00 107.11 ? 601 FAD C C9    1 
HETATM 12325 C C9A   . FAD F 2 .   ? 39.559  17.779  -14.128 1.00 106.81 ? 601 FAD C C9A   1 
HETATM 12326 N N10   . FAD F 2 .   ? 39.031  16.904  -13.184 1.00 103.22 ? 601 FAD C N10   1 
HETATM 12327 C C10   . FAD F 2 .   ? 39.853  15.984  -12.552 1.00 89.99  ? 601 FAD C C10   1 
HETATM 12328 C "C1'" . FAD F 2 .   ? 37.584  16.945  -12.879 1.00 108.81 ? 601 FAD C "C1'" 1 
HETATM 12329 C "C2'" . FAD F 2 .   ? 37.237  17.963  -11.794 1.00 105.12 ? 601 FAD C "C2'" 1 
HETATM 12330 O "O2'" . FAD F 2 .   ? 37.829  19.239  -12.038 1.00 111.50 ? 601 FAD C "O2'" 1 
HETATM 12331 C "C3'" . FAD F 2 .   ? 37.692  17.466  -10.422 1.00 95.10  ? 601 FAD C "C3'" 1 
HETATM 12332 O "O3'" . FAD F 2 .   ? 37.182  16.147  -10.223 1.00 91.10  ? 601 FAD C "O3'" 1 
HETATM 12333 C "C4'" . FAD F 2 .   ? 37.257  18.383  -9.277  1.00 93.63  ? 601 FAD C "C4'" 1 
HETATM 12334 O "O4'" . FAD F 2 .   ? 38.196  18.289  -8.203  1.00 100.23 ? 601 FAD C "O4'" 1 
HETATM 12335 C "C5'" . FAD F 2 .   ? 35.870  18.058  -8.772  1.00 92.22  ? 601 FAD C "C5'" 1 
HETATM 12336 O "O5'" . FAD F 2 .   ? 35.219  19.298  -8.425  1.00 80.40  ? 601 FAD C "O5'" 1 
HETATM 12337 P P     . FAD F 2 .   ? 34.213  19.343  -7.194  1.00 65.50  ? 601 FAD C P     1 
HETATM 12338 O O1P   . FAD F 2 .   ? 34.265  18.044  -6.477  1.00 77.68  ? 601 FAD C O1P   1 
HETATM 12339 O O2P   . FAD F 2 .   ? 34.327  20.638  -6.463  1.00 66.84  ? 601 FAD C O2P   1 
HETATM 12340 O O3P   . FAD F 2 .   ? 32.821  19.401  -7.964  1.00 75.33  ? 601 FAD C O3P   1 
HETATM 12341 O O     . HOH G 3 .   ? 15.024  46.062  23.046  1.00 45.69  ? 701 HOH A O     1 
HETATM 12342 O O     . HOH G 3 .   ? 10.193  24.120  64.118  1.00 39.93  ? 702 HOH A O     1 
HETATM 12343 O O     . HOH G 3 .   ? 13.284  9.163   51.159  1.00 26.32  ? 703 HOH A O     1 
HETATM 12344 O O     . HOH G 3 .   ? 39.604  27.977  38.596  1.00 42.90  ? 704 HOH A O     1 
HETATM 12345 O O     . HOH G 3 .   ? 7.392   52.514  44.019  1.00 50.93  ? 705 HOH A O     1 
HETATM 12346 O O     . HOH G 3 .   ? 30.171  44.604  31.010  1.00 48.94  ? 706 HOH A O     1 
HETATM 12347 O O     . HOH G 3 .   ? -9.688  16.634  51.210  1.00 43.72  ? 707 HOH A O     1 
HETATM 12348 O O     . HOH G 3 .   ? 8.969   6.268   59.458  1.00 35.24  ? 708 HOH A O     1 
HETATM 12349 O O     . HOH G 3 .   ? 37.633  33.253  33.683  1.00 43.49  ? 709 HOH A O     1 
HETATM 12350 O O     . HOH G 3 .   ? 18.860  44.335  20.688  1.00 53.47  ? 710 HOH A O     1 
HETATM 12351 O O     . HOH G 3 .   ? 11.369  23.332  66.789  1.00 48.32  ? 711 HOH A O     1 
HETATM 12352 O O     . HOH G 3 .   ? 14.312  25.591  16.050  1.00 42.77  ? 712 HOH A O     1 
HETATM 12353 O O     . HOH G 3 .   ? 22.580  10.762  28.817  1.00 36.40  ? 713 HOH A O     1 
HETATM 12354 O O     . HOH G 3 .   ? 12.255  30.493  16.505  1.00 44.84  ? 714 HOH A O     1 
HETATM 12355 O O     . HOH G 3 .   ? 20.482  20.896  48.341  1.00 41.43  ? 715 HOH A O     1 
HETATM 12356 O O     . HOH G 3 .   ? -13.487 7.472   26.255  1.00 61.14  ? 716 HOH A O     1 
HETATM 12357 O O     . HOH H 3 .   ? 36.248  5.071   94.914  1.00 56.92  ? 701 HOH B O     1 
HETATM 12358 O O     . HOH H 3 .   ? 29.759  1.106   37.099  1.00 26.11  ? 702 HOH B O     1 
HETATM 12359 O O     . HOH H 3 .   ? 17.173  2.627   39.869  1.00 30.94  ? 703 HOH B O     1 
HETATM 12360 O O     . HOH H 3 .   ? -0.000  2.223   71.937  0.50 50.67  ? 704 HOH B O     1 
HETATM 12361 O O     . HOH H 3 .   ? 34.556  11.226  40.438  1.00 37.34  ? 705 HOH B O     1 
HETATM 12362 O O     . HOH H 3 .   ? 18.598  -24.336 62.463  1.00 50.49  ? 706 HOH B O     1 
HETATM 12363 O O     . HOH H 3 .   ? 10.300  -2.738  68.519  1.00 39.91  ? 707 HOH B O     1 
HETATM 12364 O O     . HOH H 3 .   ? 9.603   -11.831 80.628  1.00 41.78  ? 708 HOH B O     1 
HETATM 12365 O O     . HOH H 3 .   ? 40.380  9.933   78.321  1.00 38.86  ? 709 HOH B O     1 
HETATM 12366 O O     . HOH H 3 .   ? 29.836  33.121  80.077  1.00 49.86  ? 710 HOH B O     1 
HETATM 12367 O O     . HOH H 3 .   ? 7.202   -0.004  86.390  1.00 48.71  ? 711 HOH B O     1 
HETATM 12368 O O     . HOH H 3 .   ? 36.138  -12.862 63.407  1.00 54.32  ? 712 HOH B O     1 
HETATM 12369 O O     . HOH H 3 .   ? 36.803  -6.560  69.899  1.00 52.90  ? 713 HOH B O     1 
HETATM 12370 O O     . HOH I 3 .   ? 27.246  -0.581  8.988   1.00 40.30  ? 701 HOH C O     1 
HETATM 12371 O O     . HOH I 3 .   ? 29.525  10.641  15.904  1.00 30.14  ? 702 HOH C O     1 
HETATM 12372 O O     . HOH I 3 .   ? 49.514  12.281  -1.075  1.00 31.90  ? 703 HOH C O     1 
HETATM 12373 O O     . HOH I 3 .   ? 38.115  25.666  3.713   1.00 43.87  ? 704 HOH C O     1 
HETATM 12374 O O     . HOH I 3 .   ? 12.190  -0.137  -3.441  1.00 35.29  ? 705 HOH C O     1 
HETATM 12375 O O     . HOH I 3 .   ? 21.605  26.337  -30.031 1.00 58.54  ? 706 HOH C O     1 
HETATM 12376 O O     . HOH I 3 .   ? 55.913  20.564  -22.940 1.00 36.06  ? 707 HOH C O     1 
HETATM 12377 O O     . HOH I 3 .   ? 34.680  5.169   10.561  1.00 38.15  ? 708 HOH C O     1 
HETATM 12378 O O     . HOH I 3 .   ? 41.820  17.039  -28.383 1.00 50.40  ? 709 HOH C O     1 
HETATM 12379 O O     . HOH I 3 .   ? 29.356  1.207   9.248   1.00 30.13  ? 710 HOH C O     1 
HETATM 12380 O O     . HOH I 3 .   ? 32.051  6.397   -39.315 1.00 46.52  ? 711 HOH C O     1 
HETATM 12381 O O     . HOH I 3 .   ? 63.745  19.824  -20.805 1.00 36.65  ? 712 HOH C O     1 
HETATM 12382 O O     . HOH I 3 .   ? 39.677  0.416   7.718   1.00 38.26  ? 713 HOH C O     1 
HETATM 12383 O O     . HOH I 3 .   ? 64.677  13.114  -2.039  1.00 41.40  ? 714 HOH C O     1 
HETATM 12384 O O     . HOH I 3 .   ? 27.617  10.913  -4.931  1.00 33.74  ? 715 HOH C O     1 
HETATM 12385 O O     . HOH I 3 .   ? 47.173  17.741  -18.528 1.00 32.72  ? 716 HOH C O     1 
HETATM 12386 O O     . HOH I 3 .   ? 8.502   3.976   -18.009 1.00 50.67  ? 717 HOH C O     1 
HETATM 12387 O O     . HOH I 3 .   ? 16.457  -0.614  -15.701 1.00 43.93  ? 718 HOH C O     1 
HETATM 12388 O O     . HOH I 3 .   ? 42.963  14.500  -17.750 1.00 50.11  ? 719 HOH C O     1 
# 
