data_8S7Q
# 
_entry.id   8S7Q 
# 
_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   8S7Q         pdb_00008s7q 10.2210/pdb8s7q/pdb 
WWPDB D_1292137017 ?            ?                   
# 
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                        8S7Q 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Mattevi 
_pdbx_contact_author.name_last          Andrea 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guerriere, T.B.' 1 0009-0003-3232-6822 
'Mattevi, A.'     2 0000-0002-9523-7128 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1046 
_citation.page_last                 1060 
_citation.title                     
'Dehydrogenase versus oxidase function: the interplay between substrate binding and flavin microenvironment.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c05944 
_citation.pdbx_database_id_PubMed   39781101 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guerriere, T.B.' 1  ? 
primary 'Vancheri, A.'    2  ? 
primary 'Ricotti, I.'     3  ? 
primary 'Serapian, S.A.'  4  ? 
primary 'Eggerichs, D.'   5  ? 
primary 'Tischler, D.'    6  ? 
primary 'Colombo, G.'     7  ? 
primary 'Mascotti, M.L.'  8  ? 
primary 'Fraaije, M.W.'   9  ? 
primary 'Mattevi, A.'     10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Oxidoreductase                58261.840 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   2   ? ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'       106.120   3   ? ? ? ? 
4 non-polymer syn GLYCEROL                      92.094    1   ? ? ? ? 
5 water       nat water                         18.015    358 ? ? ? ? 
# 
_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
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDIGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAAPLPEGVSAEAMSSALDRFARIVGADWVFTEDKITPYEDPYTISNDETEHRPYAAVAPASTEEVQEIVRVANEFGVPL
WPVSRGKNFAYGGAAPVMSGTVVLDMNRMNRILEVNEEFGYALVEPGVSYFELYDYIQEKGLKLWIDVPDIGWGSVVGNA
LDHGIGYTPYGDHFAMQCGMEVVLPNGEVVRTGMGAMPGNNTWQLFKYGYGPYVDGIFSQSNFGVVTKMGIWLMPEPAGY
RPYLITFENEDDIETVTERLRPLKVAGVIQNGATVRSLVLDAAITRTKSQYYDGDGPIPPSVAKTMMADLDLGMWNFCGA
LYGPPPVMDTLWTAIRDSFADIPGVKFYFPEDRRHKVDLLLHRAETMKGVPKLTEFNFLNWDGGGGHVGFSPVSPITGKD
AIKQYNMVSSRVREYGFDYMGLLAIGWRDLHHVTVIVYDKTDPDERKKLDELFNILVDEAAAEGYGEYRTHIRYMDRIAK
TYSWNDNALWKMHETIKDALDPNGILAPGKSGIWGKNRRKA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'DI(HYDROXYETHYL)ETHER'       PEG 
4 GLYCEROL                      GOL 
5 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ALA n 
1 4   PRO n 
1 5   LEU n 
1 6   PRO n 
1 7   GLU n 
1 8   GLY n 
1 9   VAL n 
1 10  SER n 
1 11  ALA n 
1 12  GLU n 
1 13  ALA n 
1 14  MET n 
1 15  SER n 
1 16  SER n 
1 17  ALA n 
1 18  LEU n 
1 19  ASP n 
1 20  ARG n 
1 21  PHE n 
1 22  ALA n 
1 23  ARG n 
1 24  ILE n 
1 25  VAL n 
1 26  GLY n 
1 27  ALA n 
1 28  ASP n 
1 29  TRP n 
1 30  VAL n 
1 31  PHE n 
1 32  THR n 
1 33  GLU n 
1 34  ASP n 
1 35  LYS n 
1 36  ILE n 
1 37  THR n 
1 38  PRO n 
1 39  TYR n 
1 40  GLU n 
1 41  ASP n 
1 42  PRO n 
1 43  TYR n 
1 44  THR n 
1 45  ILE n 
1 46  SER n 
1 47  ASN n 
1 48  ASP n 
1 49  GLU n 
1 50  THR n 
1 51  GLU n 
1 52  HIS n 
1 53  ARG n 
1 54  PRO n 
1 55  TYR n 
1 56  ALA n 
1 57  ALA n 
1 58  VAL n 
1 59  ALA n 
1 60  PRO n 
1 61  ALA n 
1 62  SER n 
1 63  THR n 
1 64  GLU n 
1 65  GLU n 
1 66  VAL n 
1 67  GLN n 
1 68  GLU n 
1 69  ILE n 
1 70  VAL n 
1 71  ARG n 
1 72  VAL n 
1 73  ALA n 
1 74  ASN n 
1 75  GLU n 
1 76  PHE n 
1 77  GLY n 
1 78  VAL n 
1 79  PRO n 
1 80  LEU n 
1 81  TRP n 
1 82  PRO n 
1 83  VAL n 
1 84  SER n 
1 85  ARG n 
1 86  GLY n 
1 87  LYS n 
1 88  ASN n 
1 89  PHE n 
1 90  ALA n 
1 91  TYR n 
1 92  GLY n 
1 93  GLY n 
1 94  ALA n 
1 95  ALA n 
1 96  PRO n 
1 97  VAL n 
1 98  MET n 
1 99  SER n 
1 100 GLY n 
1 101 THR n 
1 102 VAL n 
1 103 VAL n 
1 104 LEU n 
1 105 ASP n 
1 106 MET n 
1 107 ASN n 
1 108 ARG n 
1 109 MET n 
1 110 ASN n 
1 111 ARG n 
1 112 ILE n 
1 113 LEU n 
1 114 GLU n 
1 115 VAL n 
1 116 ASN n 
1 117 GLU n 
1 118 GLU n 
1 119 PHE n 
1 120 GLY n 
1 121 TYR n 
1 122 ALA n 
1 123 LEU n 
1 124 VAL n 
1 125 GLU n 
1 126 PRO n 
1 127 GLY n 
1 128 VAL n 
1 129 SER n 
1 130 TYR n 
1 131 PHE n 
1 132 GLU n 
1 133 LEU n 
1 134 TYR n 
1 135 ASP n 
1 136 TYR n 
1 137 ILE n 
1 138 GLN n 
1 139 GLU n 
1 140 LYS n 
1 141 GLY n 
1 142 LEU n 
1 143 LYS n 
1 144 LEU n 
1 145 TRP n 
1 146 ILE n 
1 147 ASP n 
1 148 VAL n 
1 149 PRO n 
1 150 ASP n 
1 151 ILE 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  
GOL non-polymer         . GLYCEROL                      'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE                     ?                               'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ?                               'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ?                               'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ?                               'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ?                               'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ?                               'C5 H11 N O2 S'     149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'       ?                               'C4 H10 O3'         106.120 
PHE 'L-peptide linking' y PHENYLALANINE                 ?                               'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ?                               'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ?                               'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ?                               'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ?                               'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ?                               'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ?                               'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  MET 14  14  14  MET MET A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ASN 47  47  47  ASN ASN A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  TRP 81  81  81  TRP TRP A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  MET 98  98  98  MET MET A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 TRP 145 145 145 TRP TRP A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 CYS 178 178 178 CYS CYS A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 MET 180 180 180 MET MET A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 MET 197 197 197 MET MET A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 TYR 210 210 210 TYR TYR A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ASN 222 222 222 ASN ASN A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 MET 229 229 229 MET MET A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 TRP 232 232 232 TRP TRP A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 TYR 243 243 243 TYR TYR A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ARG 261 261 261 ARG ARG A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 GLN 290 290 290 GLN GLN A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 PRO 297 297 297 PRO PRO A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 MET 307 307 307 MET MET A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 TRP 315 315 315 TRP TRP A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 CYS 318 318 318 CYS CYS A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 MET 328 328 328 MET MET A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 THR 330 330 330 THR THR A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 THR 333 333 333 THR THR A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 PRO 343 343 343 PRO PRO A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 TYR 348 348 348 TYR TYR A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 ARG 353 353 353 ARG ARG A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 HIS 355 355 355 HIS HIS A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 VAL 357 357 357 VAL VAL A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 HIS 362 362 362 HIS HIS A . n 
A 1 363 ARG 363 363 363 ARG ARG A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 MET 367 367 367 MET MET A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 LYS 372 372 372 LYS LYS A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 TRP 381 381 381 TRP TRP A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 HIS 387 387 387 HIS HIS A . n 
A 1 388 VAL 388 388 388 VAL VAL A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 PRO 395 395 395 PRO PRO A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 LYS 399 399 399 LYS LYS A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 ALA 401 401 401 ALA ALA A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 TYR 405 405 405 TYR TYR A . n 
A 1 406 ASN 406 406 406 ASN ASN A . n 
A 1 407 MET 407 407 407 MET MET A . n 
A 1 408 VAL 408 408 408 VAL VAL A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 ASP 418 418 418 ASP ASP A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLY 426 426 426 GLY GLY A . n 
A 1 427 TRP 427 427 427 TRP TRP A . n 
A 1 428 ARG 428 428 428 ARG ARG A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 HIS 431 431 431 HIS HIS A . n 
A 1 432 HIS 432 432 432 HIS HIS A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 THR 434 434 434 THR THR A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 ILE 436 436 436 ILE ILE A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 TYR 438 438 438 TYR TYR A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 THR 441 441 441 THR THR A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 PRO 443 443 443 PRO PRO A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 LYS 448 448 448 LYS LYS A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 ASP 450 450 450 ASP ASP A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 ASN 454 454 454 ASN ASN A . n 
A 1 455 ILE 455 455 455 ILE ILE A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 ASP 458 458 458 ASP ASP A . n 
A 1 459 GLU 459 459 459 GLU GLU A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ALA 462 462 462 ALA ALA A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 GLU 467 467 467 GLU GLU A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 THR 470 470 470 THR THR A . n 
A 1 471 HIS 471 471 471 HIS HIS A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 TYR 474 474 474 TYR TYR A . n 
A 1 475 MET 475 475 475 MET MET A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 ARG 477 477 477 ARG ARG A . n 
A 1 478 ILE 478 478 478 ILE ILE A . n 
A 1 479 ALA 479 479 479 ALA ALA A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 TYR 482 482 482 TYR TYR A . n 
A 1 483 SER 483 483 483 SER SER A . n 
A 1 484 TRP 484 484 484 TRP TRP A . n 
A 1 485 ASN 485 485 485 ASN ASN A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 ASN 487 487 487 ASN ASN A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 MET 492 492 492 MET MET A . n 
A 1 493 HIS 493 493 493 HIS HIS A . n 
A 1 494 GLU 494 494 494 GLU GLU A . n 
A 1 495 THR 495 495 495 THR THR A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 LYS 497 497 497 LYS LYS A . n 
A 1 498 ASP 498 498 498 ASP ASP A . n 
A 1 499 ALA 499 499 499 ALA ALA A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 ASP 501 501 501 ASP ASP A . n 
A 1 502 PRO 502 502 502 PRO PRO A . n 
A 1 503 ASN 503 503 503 ASN ASN A . n 
A 1 504 GLY 504 504 504 GLY GLY A . n 
A 1 505 ILE 505 505 505 ILE ILE A . n 
A 1 506 LEU 506 506 506 LEU LEU A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 PRO 508 508 508 PRO PRO A . n 
A 1 509 GLY 509 509 509 GLY GLY A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 SER 511 511 511 SER SER A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 ILE 513 513 513 ILE ILE A . n 
A 1 514 TRP 514 514 514 TRP TRP A . n 
A 1 515 GLY 515 515 515 GLY GLY A . n 
A 1 516 LYS 516 516 516 LYS LYS A . n 
A 1 517 ASN 517 517 517 ASN ASN A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 LYS 520 520 ?   ?   ?   A . n 
A 1 521 ALA 521 521 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   ALA 3   3   3   ALA ALA B . n 
B 1 4   PRO 4   4   4   PRO PRO B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  MET 14  14  14  MET MET B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  ARG 23  23  23  ARG ARG B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  GLU 33  33  33  GLU GLU B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  TYR 43  43  43  TYR TYR B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  ILE 45  45  45  ILE ILE B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ASN 47  47  47  ASN ASN B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  ARG 53  53  53  ARG ARG B . n 
B 1 54  PRO 54  54  54  PRO PRO B . n 
B 1 55  TYR 55  55  55  TYR TYR B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  GLU 68  68  68  GLU GLU B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  PRO 79  79  79  PRO PRO B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  TRP 81  81  81  TRP TRP B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  ARG 85  85  85  ARG ARG B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  MET 98  98  98  MET MET B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 THR 101 101 101 THR THR B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 MET 106 106 106 MET MET B . n 
B 1 107 ASN 107 107 107 ASN ASN B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 MET 109 109 109 MET MET B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 PRO 126 126 126 PRO PRO B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 TYR 130 130 130 TYR TYR B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 TYR 136 136 136 TYR TYR B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 TRP 145 145 145 TRP TRP B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 TRP 153 153 153 TRP TRP B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 VAL 156 156 156 VAL VAL B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ASP 172 172 172 ASP ASP B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 PHE 174 174 174 PHE PHE B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 GLN 177 177 177 GLN GLN B . n 
B 1 178 CYS 178 178 178 CYS CYS B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 MET 180 180 180 MET MET B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 GLU 188 188 188 GLU GLU B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ARG 191 191 191 ARG ARG B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 MET 194 194 194 MET MET B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 MET 197 197 197 MET MET B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 ASN 200 200 200 ASN ASN B . n 
B 1 201 ASN 201 201 201 ASN ASN B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 TRP 203 203 203 TRP TRP B . n 
B 1 204 GLN 204 204 204 GLN GLN B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 PHE 206 206 206 PHE PHE B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 TYR 210 210 210 TYR TYR B . n 
B 1 211 GLY 211 211 211 GLY GLY B . n 
B 1 212 PRO 212 212 212 PRO PRO B . n 
B 1 213 TYR 213 213 213 TYR TYR B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 GLY 216 216 216 GLY GLY B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 PHE 218 218 218 PHE PHE B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 GLN 220 220 220 GLN GLN B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 ASN 222 222 222 ASN ASN B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 MET 229 229 229 MET MET B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 TRP 232 232 232 TRP TRP B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 TYR 243 243 243 TYR TYR B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 THR 246 246 246 THR THR B . n 
B 1 247 PHE 247 247 247 PHE PHE B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 GLU 250 250 250 GLU GLU B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 THR 255 255 255 THR THR B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 ARG 261 261 261 ARG ARG B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 ILE 269 269 269 ILE ILE B . n 
B 1 270 GLN 270 270 270 GLN GLN B . n 
B 1 271 ASN 271 271 271 ASN ASN B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 ARG 276 276 276 ARG ARG B . n 
B 1 277 SER 277 277 277 SER SER B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 VAL 279 279 279 VAL VAL B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 ASP 281 281 281 ASP ASP B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 ALA 283 283 283 ALA ALA B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 THR 287 287 287 THR THR B . n 
B 1 288 LYS 288 288 288 LYS LYS B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 GLN 290 290 290 GLN GLN B . n 
B 1 291 TYR 291 291 291 TYR TYR B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 GLY 294 294 294 GLY GLY B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 PRO 297 297 297 PRO PRO B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 PRO 300 300 300 PRO PRO B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 ALA 303 303 303 ALA ALA B . n 
B 1 304 LYS 304 304 304 LYS LYS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 MET 306 306 306 MET MET B . n 
B 1 307 MET 307 307 307 MET MET B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 ASP 309 309 309 ASP ASP B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 GLY 313 313 313 GLY GLY B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 TRP 315 315 315 TRP TRP B . n 
B 1 316 ASN 316 316 316 ASN ASN B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 CYS 318 318 318 CYS CYS B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 TYR 322 322 322 TYR TYR B . n 
B 1 323 GLY 323 323 323 GLY GLY B . n 
B 1 324 PRO 324 324 324 PRO PRO B . n 
B 1 325 PRO 325 325 325 PRO PRO B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 MET 328 328 328 MET MET B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 THR 330 330 330 THR THR B . n 
B 1 331 LEU 331 331 331 LEU LEU B . n 
B 1 332 TRP 332 332 332 TRP TRP B . n 
B 1 333 THR 333 333 333 THR THR B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 ILE 335 335 335 ILE ILE B . n 
B 1 336 ARG 336 336 336 ARG ARG B . n 
B 1 337 ASP 337 337 337 ASP ASP B . n 
B 1 338 SER 338 338 338 SER SER B . n 
B 1 339 PHE 339 339 339 PHE PHE B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 ASP 341 341 341 ASP ASP B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 PRO 343 343 343 PRO PRO B . n 
B 1 344 GLY 344 344 344 GLY GLY B . n 
B 1 345 VAL 345 345 345 VAL VAL B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 TYR 348 348 348 TYR TYR B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 ARG 353 353 353 ARG ARG B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 HIS 355 355 355 HIS HIS B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 VAL 357 357 357 VAL VAL B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 LEU 359 359 359 LEU LEU B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 HIS 362 362 362 HIS HIS B . n 
B 1 363 ARG 363 363 363 ARG ARG B . n 
B 1 364 ALA 364 364 364 ALA ALA B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 THR 366 366 366 THR THR B . n 
B 1 367 MET 367 367 367 MET MET B . n 
B 1 368 LYS 368 368 368 LYS LYS B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 VAL 370 370 370 VAL VAL B . n 
B 1 371 PRO 371 371 371 PRO PRO B . n 
B 1 372 LYS 372 372 372 LYS LYS B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 GLU 375 375 375 GLU GLU B . n 
B 1 376 PHE 376 376 376 PHE PHE B . n 
B 1 377 ASN 377 377 377 ASN ASN B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 TRP 381 381 381 TRP TRP B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 GLY 383 383 383 GLY GLY B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 GLY 386 386 386 GLY GLY B . n 
B 1 387 HIS 387 387 387 HIS HIS B . n 
B 1 388 VAL 388 388 388 VAL VAL B . n 
B 1 389 GLY 389 389 389 GLY GLY B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 SER 391 391 391 SER SER B . n 
B 1 392 PRO 392 392 392 PRO PRO B . n 
B 1 393 VAL 393 393 393 VAL VAL B . n 
B 1 394 SER 394 394 394 SER SER B . n 
B 1 395 PRO 395 395 395 PRO PRO B . n 
B 1 396 ILE 396 396 396 ILE ILE B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLY 398 398 398 GLY GLY B . n 
B 1 399 LYS 399 399 399 LYS LYS B . n 
B 1 400 ASP 400 400 400 ASP ASP B . n 
B 1 401 ALA 401 401 401 ALA ALA B . n 
B 1 402 ILE 402 402 402 ILE ILE B . n 
B 1 403 LYS 403 403 403 LYS LYS B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 TYR 405 405 405 TYR TYR B . n 
B 1 406 ASN 406 406 406 ASN ASN B . n 
B 1 407 MET 407 407 407 MET MET B . n 
B 1 408 VAL 408 408 408 VAL VAL B . n 
B 1 409 SER 409 409 409 SER SER B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 VAL 412 412 412 VAL VAL B . n 
B 1 413 ARG 413 413 413 ARG ARG B . n 
B 1 414 GLU 414 414 414 GLU GLU B . n 
B 1 415 TYR 415 415 415 TYR TYR B . n 
B 1 416 GLY 416 416 416 GLY GLY B . n 
B 1 417 PHE 417 417 417 PHE PHE B . n 
B 1 418 ASP 418 418 418 ASP ASP B . n 
B 1 419 TYR 419 419 419 TYR TYR B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLY 421 421 421 GLY GLY B . n 
B 1 422 LEU 422 422 422 LEU LEU B . n 
B 1 423 LEU 423 423 423 LEU LEU B . n 
B 1 424 ALA 424 424 424 ALA ALA B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLY 426 426 426 GLY GLY B . n 
B 1 427 TRP 427 427 427 TRP TRP B . n 
B 1 428 ARG 428 428 428 ARG ARG B . n 
B 1 429 ASP 429 429 429 ASP ASP B . n 
B 1 430 LEU 430 430 430 LEU LEU B . n 
B 1 431 HIS 431 431 431 HIS HIS B . n 
B 1 432 HIS 432 432 432 HIS HIS B . n 
B 1 433 VAL 433 433 433 VAL VAL B . n 
B 1 434 THR 434 434 434 THR THR B . n 
B 1 435 VAL 435 435 435 VAL VAL B . n 
B 1 436 ILE 436 436 436 ILE ILE B . n 
B 1 437 VAL 437 437 437 VAL VAL B . n 
B 1 438 TYR 438 438 438 TYR TYR B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 THR 441 441 441 THR THR B . n 
B 1 442 ASP 442 442 442 ASP ASP B . n 
B 1 443 PRO 443 443 443 PRO PRO B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 LYS 447 447 447 LYS LYS B . n 
B 1 448 LYS 448 448 448 LYS LYS B . n 
B 1 449 LEU 449 449 449 LEU LEU B . n 
B 1 450 ASP 450 450 450 ASP ASP B . n 
B 1 451 GLU 451 451 451 GLU GLU B . n 
B 1 452 LEU 452 452 452 LEU LEU B . n 
B 1 453 PHE 453 453 453 PHE PHE B . n 
B 1 454 ASN 454 454 454 ASN ASN B . n 
B 1 455 ILE 455 455 455 ILE ILE B . n 
B 1 456 LEU 456 456 456 LEU LEU B . n 
B 1 457 VAL 457 457 457 VAL VAL B . n 
B 1 458 ASP 458 458 458 ASP ASP B . n 
B 1 459 GLU 459 459 459 GLU GLU B . n 
B 1 460 ALA 460 460 460 ALA ALA B . n 
B 1 461 ALA 461 461 461 ALA ALA B . n 
B 1 462 ALA 462 462 462 ALA ALA B . n 
B 1 463 GLU 463 463 463 GLU GLU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 TYR 465 465 465 TYR TYR B . n 
B 1 466 GLY 466 466 466 GLY GLY B . n 
B 1 467 GLU 467 467 467 GLU GLU B . n 
B 1 468 TYR 468 468 468 TYR TYR B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 THR 470 470 470 THR THR B . n 
B 1 471 HIS 471 471 471 HIS HIS B . n 
B 1 472 ILE 472 472 472 ILE ILE B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 TYR 474 474 474 TYR TYR B . n 
B 1 475 MET 475 475 475 MET MET B . n 
B 1 476 ASP 476 476 476 ASP ASP B . n 
B 1 477 ARG 477 477 477 ARG ARG B . n 
B 1 478 ILE 478 478 478 ILE ILE B . n 
B 1 479 ALA 479 479 479 ALA ALA B . n 
B 1 480 LYS 480 480 480 LYS LYS B . n 
B 1 481 THR 481 481 481 THR THR B . n 
B 1 482 TYR 482 482 482 TYR TYR B . n 
B 1 483 SER 483 483 483 SER SER B . n 
B 1 484 TRP 484 484 484 TRP TRP B . n 
B 1 485 ASN 485 485 485 ASN ASN B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 ASN 487 487 487 ASN ASN B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 LEU 489 489 489 LEU LEU B . n 
B 1 490 TRP 490 490 490 TRP TRP B . n 
B 1 491 LYS 491 491 491 LYS LYS B . n 
B 1 492 MET 492 492 492 MET MET B . n 
B 1 493 HIS 493 493 493 HIS HIS B . n 
B 1 494 GLU 494 494 494 GLU GLU B . n 
B 1 495 THR 495 495 495 THR THR B . n 
B 1 496 ILE 496 496 496 ILE ILE B . n 
B 1 497 LYS 497 497 497 LYS LYS B . n 
B 1 498 ASP 498 498 498 ASP ASP B . n 
B 1 499 ALA 499 499 499 ALA ALA B . n 
B 1 500 LEU 500 500 500 LEU LEU B . n 
B 1 501 ASP 501 501 501 ASP ASP B . n 
B 1 502 PRO 502 502 502 PRO PRO B . n 
B 1 503 ASN 503 503 503 ASN ASN B . n 
B 1 504 GLY 504 504 504 GLY GLY B . n 
B 1 505 ILE 505 505 505 ILE ILE B . n 
B 1 506 LEU 506 506 506 LEU LEU B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 PRO 508 508 508 PRO PRO B . n 
B 1 509 GLY 509 509 509 GLY GLY B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 SER 511 511 511 SER SER B . n 
B 1 512 GLY 512 512 512 GLY GLY B . n 
B 1 513 ILE 513 513 513 ILE ILE B . n 
B 1 514 TRP 514 514 514 TRP TRP B . n 
B 1 515 GLY 515 515 515 GLY GLY B . n 
B 1 516 LYS 516 516 516 LYS LYS B . n 
B 1 517 ASN 517 517 517 ASN ASN B . n 
B 1 518 ARG 518 518 518 ARG ARG B . n 
B 1 519 ARG 519 519 519 ARG ARG B . n 
B 1 520 LYS 520 520 ?   ?   ?   B . n 
B 1 521 ALA 521 521 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FAD 1   601 601 FAD FAD A . 
D 3 PEG 1   602 615 PEG PEG A . 
E 3 PEG 1   603 616 PEG PEG A . 
F 2 FAD 1   601 601 FAD FAD B . 
G 3 PEG 1   602 611 PEG PEG B . 
H 4 GOL 1   603 612 GOL GOL B . 
I 5 HOH 1   701 352 HOH HOH A . 
I 5 HOH 2   702 136 HOH HOH A . 
I 5 HOH 3   703 170 HOH HOH A . 
I 5 HOH 4   704 85  HOH HOH A . 
I 5 HOH 5   705 7   HOH HOH A . 
I 5 HOH 6   706 135 HOH HOH A . 
I 5 HOH 7   707 88  HOH HOH A . 
I 5 HOH 8   708 107 HOH HOH A . 
I 5 HOH 9   709 12  HOH HOH A . 
I 5 HOH 10  710 298 HOH HOH A . 
I 5 HOH 11  711 38  HOH HOH A . 
I 5 HOH 12  712 35  HOH HOH A . 
I 5 HOH 13  713 283 HOH HOH A . 
I 5 HOH 14  714 57  HOH HOH A . 
I 5 HOH 15  715 258 HOH HOH A . 
I 5 HOH 16  716 89  HOH HOH A . 
I 5 HOH 17  717 84  HOH HOH A . 
I 5 HOH 18  718 132 HOH HOH A . 
I 5 HOH 19  719 74  HOH HOH A . 
I 5 HOH 20  720 202 HOH HOH A . 
I 5 HOH 21  721 49  HOH HOH A . 
I 5 HOH 22  722 58  HOH HOH A . 
I 5 HOH 23  723 272 HOH HOH A . 
I 5 HOH 24  724 317 HOH HOH A . 
I 5 HOH 25  725 273 HOH HOH A . 
I 5 HOH 26  726 51  HOH HOH A . 
I 5 HOH 27  727 20  HOH HOH A . 
I 5 HOH 28  728 72  HOH HOH A . 
I 5 HOH 29  729 327 HOH HOH A . 
I 5 HOH 30  730 253 HOH HOH A . 
I 5 HOH 31  731 42  HOH HOH A . 
I 5 HOH 32  732 43  HOH HOH A . 
I 5 HOH 33  733 195 HOH HOH A . 
I 5 HOH 34  734 1   HOH HOH A . 
I 5 HOH 35  735 304 HOH HOH A . 
I 5 HOH 36  736 10  HOH HOH A . 
I 5 HOH 37  737 263 HOH HOH A . 
I 5 HOH 38  738 161 HOH HOH A . 
I 5 HOH 39  739 266 HOH HOH A . 
I 5 HOH 40  740 26  HOH HOH A . 
I 5 HOH 41  741 245 HOH HOH A . 
I 5 HOH 42  742 111 HOH HOH A . 
I 5 HOH 43  743 95  HOH HOH A . 
I 5 HOH 44  744 289 HOH HOH A . 
I 5 HOH 45  745 156 HOH HOH A . 
I 5 HOH 46  746 27  HOH HOH A . 
I 5 HOH 47  747 141 HOH HOH A . 
I 5 HOH 48  748 100 HOH HOH A . 
I 5 HOH 49  749 2   HOH HOH A . 
I 5 HOH 50  750 19  HOH HOH A . 
I 5 HOH 51  751 66  HOH HOH A . 
I 5 HOH 52  752 98  HOH HOH A . 
I 5 HOH 53  753 63  HOH HOH A . 
I 5 HOH 54  754 148 HOH HOH A . 
I 5 HOH 55  755 110 HOH HOH A . 
I 5 HOH 56  756 130 HOH HOH A . 
I 5 HOH 57  757 216 HOH HOH A . 
I 5 HOH 58  758 295 HOH HOH A . 
I 5 HOH 59  759 205 HOH HOH A . 
I 5 HOH 60  760 60  HOH HOH A . 
I 5 HOH 61  761 326 HOH HOH A . 
I 5 HOH 62  762 285 HOH HOH A . 
I 5 HOH 63  763 321 HOH HOH A . 
I 5 HOH 64  764 118 HOH HOH A . 
I 5 HOH 65  765 79  HOH HOH A . 
I 5 HOH 66  766 112 HOH HOH A . 
I 5 HOH 67  767 168 HOH HOH A . 
I 5 HOH 68  768 122 HOH HOH A . 
I 5 HOH 69  769 109 HOH HOH A . 
I 5 HOH 70  770 142 HOH HOH A . 
I 5 HOH 71  771 108 HOH HOH A . 
I 5 HOH 72  772 54  HOH HOH A . 
I 5 HOH 73  773 55  HOH HOH A . 
I 5 HOH 74  774 302 HOH HOH A . 
I 5 HOH 75  775 278 HOH HOH A . 
I 5 HOH 76  776 36  HOH HOH A . 
I 5 HOH 77  777 280 HOH HOH A . 
I 5 HOH 78  778 239 HOH HOH A . 
I 5 HOH 79  779 143 HOH HOH A . 
I 5 HOH 80  780 62  HOH HOH A . 
I 5 HOH 81  781 277 HOH HOH A . 
I 5 HOH 82  782 259 HOH HOH A . 
I 5 HOH 83  783 301 HOH HOH A . 
I 5 HOH 84  784 101 HOH HOH A . 
I 5 HOH 85  785 117 HOH HOH A . 
I 5 HOH 86  786 97  HOH HOH A . 
I 5 HOH 87  787 313 HOH HOH A . 
I 5 HOH 88  788 147 HOH HOH A . 
I 5 HOH 89  789 314 HOH HOH A . 
I 5 HOH 90  790 215 HOH HOH A . 
I 5 HOH 91  791 287 HOH HOH A . 
I 5 HOH 92  792 324 HOH HOH A . 
I 5 HOH 93  793 299 HOH HOH A . 
I 5 HOH 94  794 177 HOH HOH A . 
I 5 HOH 95  795 297 HOH HOH A . 
I 5 HOH 96  796 24  HOH HOH A . 
I 5 HOH 97  797 48  HOH HOH A . 
I 5 HOH 98  798 279 HOH HOH A . 
I 5 HOH 99  799 292 HOH HOH A . 
I 5 HOH 100 800 208 HOH HOH A . 
I 5 HOH 101 801 354 HOH HOH A . 
I 5 HOH 102 802 212 HOH HOH A . 
I 5 HOH 103 803 155 HOH HOH A . 
I 5 HOH 104 804 252 HOH HOH A . 
I 5 HOH 105 805 52  HOH HOH A . 
I 5 HOH 106 806 178 HOH HOH A . 
I 5 HOH 107 807 194 HOH HOH A . 
I 5 HOH 108 808 291 HOH HOH A . 
I 5 HOH 109 809 306 HOH HOH A . 
I 5 HOH 110 810 319 HOH HOH A . 
I 5 HOH 111 811 307 HOH HOH A . 
I 5 HOH 112 812 332 HOH HOH A . 
I 5 HOH 113 813 209 HOH HOH A . 
I 5 HOH 114 814 243 HOH HOH A . 
I 5 HOH 115 815 355 HOH HOH A . 
I 5 HOH 116 816 345 HOH HOH A . 
I 5 HOH 117 817 269 HOH HOH A . 
I 5 HOH 118 818 150 HOH HOH A . 
I 5 HOH 119 819 191 HOH HOH A . 
I 5 HOH 120 820 231 HOH HOH A . 
I 5 HOH 121 821 225 HOH HOH A . 
I 5 HOH 122 822 192 HOH HOH A . 
I 5 HOH 123 823 286 HOH HOH A . 
I 5 HOH 124 824 175 HOH HOH A . 
I 5 HOH 125 825 308 HOH HOH A . 
I 5 HOH 126 826 335 HOH HOH A . 
I 5 HOH 127 827 183 HOH HOH A . 
I 5 HOH 128 828 217 HOH HOH A . 
I 5 HOH 129 829 330 HOH HOH A . 
I 5 HOH 130 830 176 HOH HOH A . 
I 5 HOH 131 831 242 HOH HOH A . 
I 5 HOH 132 832 348 HOH HOH A . 
I 5 HOH 133 833 320 HOH HOH A . 
I 5 HOH 134 834 276 HOH HOH A . 
I 5 HOH 135 835 346 HOH HOH A . 
I 5 HOH 136 836 173 HOH HOH A . 
I 5 HOH 137 837 325 HOH HOH A . 
I 5 HOH 138 838 249 HOH HOH A . 
I 5 HOH 139 839 350 HOH HOH A . 
I 5 HOH 140 840 303 HOH HOH A . 
I 5 HOH 141 841 353 HOH HOH A . 
I 5 HOH 142 842 234 HOH HOH A . 
I 5 HOH 143 843 78  HOH HOH A . 
I 5 HOH 144 844 329 HOH HOH A . 
I 5 HOH 145 845 184 HOH HOH A . 
I 5 HOH 146 846 351 HOH HOH A . 
I 5 HOH 147 847 230 HOH HOH A . 
I 5 HOH 148 848 235 HOH HOH A . 
I 5 HOH 149 849 349 HOH HOH A . 
J 5 HOH 1   701 247 HOH HOH B . 
J 5 HOH 2   702 172 HOH HOH B . 
J 5 HOH 3   703 69  HOH HOH B . 
J 5 HOH 4   704 13  HOH HOH B . 
J 5 HOH 5   705 102 HOH HOH B . 
J 5 HOH 6   706 11  HOH HOH B . 
J 5 HOH 7   707 106 HOH HOH B . 
J 5 HOH 8   708 163 HOH HOH B . 
J 5 HOH 9   709 198 HOH HOH B . 
J 5 HOH 10  710 115 HOH HOH B . 
J 5 HOH 11  711 44  HOH HOH B . 
J 5 HOH 12  712 144 HOH HOH B . 
J 5 HOH 13  713 46  HOH HOH B . 
J 5 HOH 14  714 140 HOH HOH B . 
J 5 HOH 15  715 80  HOH HOH B . 
J 5 HOH 16  716 281 HOH HOH B . 
J 5 HOH 17  717 164 HOH HOH B . 
J 5 HOH 18  718 158 HOH HOH B . 
J 5 HOH 19  719 264 HOH HOH B . 
J 5 HOH 20  720 73  HOH HOH B . 
J 5 HOH 21  721 40  HOH HOH B . 
J 5 HOH 22  722 86  HOH HOH B . 
J 5 HOH 23  723 134 HOH HOH B . 
J 5 HOH 24  724 171 HOH HOH B . 
J 5 HOH 25  725 261 HOH HOH B . 
J 5 HOH 26  726 29  HOH HOH B . 
J 5 HOH 27  727 246 HOH HOH B . 
J 5 HOH 28  728 257 HOH HOH B . 
J 5 HOH 29  729 99  HOH HOH B . 
J 5 HOH 30  730 121 HOH HOH B . 
J 5 HOH 31  731 113 HOH HOH B . 
J 5 HOH 32  732 4   HOH HOH B . 
J 5 HOH 33  733 294 HOH HOH B . 
J 5 HOH 34  734 64  HOH HOH B . 
J 5 HOH 35  735 47  HOH HOH B . 
J 5 HOH 36  736 77  HOH HOH B . 
J 5 HOH 37  737 8   HOH HOH B . 
J 5 HOH 38  738 120 HOH HOH B . 
J 5 HOH 39  739 90  HOH HOH B . 
J 5 HOH 40  740 92  HOH HOH B . 
J 5 HOH 41  741 31  HOH HOH B . 
J 5 HOH 42  742 103 HOH HOH B . 
J 5 HOH 43  743 197 HOH HOH B . 
J 5 HOH 44  744 296 HOH HOH B . 
J 5 HOH 45  745 23  HOH HOH B . 
J 5 HOH 46  746 6   HOH HOH B . 
J 5 HOH 47  747 53  HOH HOH B . 
J 5 HOH 48  748 290 HOH HOH B . 
J 5 HOH 49  749 133 HOH HOH B . 
J 5 HOH 50  750 75  HOH HOH B . 
J 5 HOH 51  751 50  HOH HOH B . 
J 5 HOH 52  752 309 HOH HOH B . 
J 5 HOH 53  753 87  HOH HOH B . 
J 5 HOH 54  754 17  HOH HOH B . 
J 5 HOH 55  755 341 HOH HOH B . 
J 5 HOH 56  756 61  HOH HOH B . 
J 5 HOH 57  757 262 HOH HOH B . 
J 5 HOH 58  758 270 HOH HOH B . 
J 5 HOH 59  759 105 HOH HOH B . 
J 5 HOH 60  760 21  HOH HOH B . 
J 5 HOH 61  761 305 HOH HOH B . 
J 5 HOH 62  762 41  HOH HOH B . 
J 5 HOH 63  763 244 HOH HOH B . 
J 5 HOH 64  764 166 HOH HOH B . 
J 5 HOH 65  765 131 HOH HOH B . 
J 5 HOH 66  766 126 HOH HOH B . 
J 5 HOH 67  767 153 HOH HOH B . 
J 5 HOH 68  768 71  HOH HOH B . 
J 5 HOH 69  769 3   HOH HOH B . 
J 5 HOH 70  770 5   HOH HOH B . 
J 5 HOH 71  771 67  HOH HOH B . 
J 5 HOH 72  772 127 HOH HOH B . 
J 5 HOH 73  773 179 HOH HOH B . 
J 5 HOH 74  774 185 HOH HOH B . 
J 5 HOH 75  775 16  HOH HOH B . 
J 5 HOH 76  776 68  HOH HOH B . 
J 5 HOH 77  777 318 HOH HOH B . 
J 5 HOH 78  778 22  HOH HOH B . 
J 5 HOH 79  779 76  HOH HOH B . 
J 5 HOH 80  780 137 HOH HOH B . 
J 5 HOH 81  781 37  HOH HOH B . 
J 5 HOH 82  782 167 HOH HOH B . 
J 5 HOH 83  783 201 HOH HOH B . 
J 5 HOH 84  784 275 HOH HOH B . 
J 5 HOH 85  785 159 HOH HOH B . 
J 5 HOH 86  786 162 HOH HOH B . 
J 5 HOH 87  787 160 HOH HOH B . 
J 5 HOH 88  788 59  HOH HOH B . 
J 5 HOH 89  789 93  HOH HOH B . 
J 5 HOH 90  790 293 HOH HOH B . 
J 5 HOH 91  791 157 HOH HOH B . 
J 5 HOH 92  792 254 HOH HOH B . 
J 5 HOH 93  793 241 HOH HOH B . 
J 5 HOH 94  794 300 HOH HOH B . 
J 5 HOH 95  795 203 HOH HOH B . 
J 5 HOH 96  796 240 HOH HOH B . 
J 5 HOH 97  797 39  HOH HOH B . 
J 5 HOH 98  798 123 HOH HOH B . 
J 5 HOH 99  799 82  HOH HOH B . 
J 5 HOH 100 800 18  HOH HOH B . 
J 5 HOH 101 801 251 HOH HOH B . 
J 5 HOH 102 802 81  HOH HOH B . 
J 5 HOH 103 803 9   HOH HOH B . 
J 5 HOH 104 804 91  HOH HOH B . 
J 5 HOH 105 805 237 HOH HOH B . 
J 5 HOH 106 806 310 HOH HOH B . 
J 5 HOH 107 807 104 HOH HOH B . 
J 5 HOH 108 808 96  HOH HOH B . 
J 5 HOH 109 809 70  HOH HOH B . 
J 5 HOH 110 810 337 HOH HOH B . 
J 5 HOH 111 811 28  HOH HOH B . 
J 5 HOH 112 812 124 HOH HOH B . 
J 5 HOH 113 813 25  HOH HOH B . 
J 5 HOH 114 814 34  HOH HOH B . 
J 5 HOH 115 815 169 HOH HOH B . 
J 5 HOH 116 816 129 HOH HOH B . 
J 5 HOH 117 817 45  HOH HOH B . 
J 5 HOH 118 818 33  HOH HOH B . 
J 5 HOH 119 819 186 HOH HOH B . 
J 5 HOH 120 820 145 HOH HOH B . 
J 5 HOH 121 821 114 HOH HOH B . 
J 5 HOH 122 822 138 HOH HOH B . 
J 5 HOH 123 823 358 HOH HOH B . 
J 5 HOH 124 824 94  HOH HOH B . 
J 5 HOH 125 825 268 HOH HOH B . 
J 5 HOH 126 826 199 HOH HOH B . 
J 5 HOH 127 827 210 HOH HOH B . 
J 5 HOH 128 828 139 HOH HOH B . 
J 5 HOH 129 829 284 HOH HOH B . 
J 5 HOH 130 830 128 HOH HOH B . 
J 5 HOH 131 831 315 HOH HOH B . 
J 5 HOH 132 832 224 HOH HOH B . 
J 5 HOH 133 833 196 HOH HOH B . 
J 5 HOH 134 834 336 HOH HOH B . 
J 5 HOH 135 835 146 HOH HOH B . 
J 5 HOH 136 836 32  HOH HOH B . 
J 5 HOH 137 837 204 HOH HOH B . 
J 5 HOH 138 838 165 HOH HOH B . 
J 5 HOH 139 839 119 HOH HOH B . 
J 5 HOH 140 840 15  HOH HOH B . 
J 5 HOH 141 841 149 HOH HOH B . 
J 5 HOH 142 842 236 HOH HOH B . 
J 5 HOH 143 843 328 HOH HOH B . 
J 5 HOH 144 844 311 HOH HOH B . 
J 5 HOH 145 845 265 HOH HOH B . 
J 5 HOH 146 846 267 HOH HOH B . 
J 5 HOH 147 847 322 HOH HOH B . 
J 5 HOH 148 848 250 HOH HOH B . 
J 5 HOH 149 849 271 HOH HOH B . 
J 5 HOH 150 850 282 HOH HOH B . 
J 5 HOH 151 851 30  HOH HOH B . 
J 5 HOH 152 852 193 HOH HOH B . 
J 5 HOH 153 853 229 HOH HOH B . 
J 5 HOH 154 854 116 HOH HOH B . 
J 5 HOH 155 855 334 HOH HOH B . 
J 5 HOH 156 856 206 HOH HOH B . 
J 5 HOH 157 857 174 HOH HOH B . 
J 5 HOH 158 858 181 HOH HOH B . 
J 5 HOH 159 859 260 HOH HOH B . 
J 5 HOH 160 860 56  HOH HOH B . 
J 5 HOH 161 861 125 HOH HOH B . 
J 5 HOH 162 862 211 HOH HOH B . 
J 5 HOH 163 863 152 HOH HOH B . 
J 5 HOH 164 864 248 HOH HOH B . 
J 5 HOH 165 865 357 HOH HOH B . 
J 5 HOH 166 866 232 HOH HOH B . 
J 5 HOH 167 867 189 HOH HOH B . 
J 5 HOH 168 868 187 HOH HOH B . 
J 5 HOH 169 869 65  HOH HOH B . 
J 5 HOH 170 870 347 HOH HOH B . 
J 5 HOH 171 871 221 HOH HOH B . 
J 5 HOH 172 872 331 HOH HOH B . 
J 5 HOH 173 873 323 HOH HOH B . 
J 5 HOH 174 874 219 HOH HOH B . 
J 5 HOH 175 875 182 HOH HOH B . 
J 5 HOH 176 876 220 HOH HOH B . 
J 5 HOH 177 877 312 HOH HOH B . 
J 5 HOH 178 878 233 HOH HOH B . 
J 5 HOH 179 879 228 HOH HOH B . 
J 5 HOH 180 880 333 HOH HOH B . 
J 5 HOH 181 881 154 HOH HOH B . 
J 5 HOH 182 882 338 HOH HOH B . 
J 5 HOH 183 883 222 HOH HOH B . 
J 5 HOH 184 884 180 HOH HOH B . 
J 5 HOH 185 885 288 HOH HOH B . 
J 5 HOH 186 886 214 HOH HOH B . 
J 5 HOH 187 887 223 HOH HOH B . 
J 5 HOH 188 888 343 HOH HOH B . 
J 5 HOH 189 889 207 HOH HOH B . 
J 5 HOH 190 890 344 HOH HOH B . 
J 5 HOH 191 891 316 HOH HOH B . 
J 5 HOH 192 892 256 HOH HOH B . 
J 5 HOH 193 893 200 HOH HOH B . 
J 5 HOH 194 894 226 HOH HOH B . 
J 5 HOH 195 895 339 HOH HOH B . 
J 5 HOH 196 896 255 HOH HOH B . 
J 5 HOH 197 897 227 HOH HOH B . 
J 5 HOH 198 898 151 HOH HOH B . 
J 5 HOH 199 899 342 HOH HOH B . 
J 5 HOH 200 900 340 HOH HOH B . 
J 5 HOH 201 901 274 HOH HOH B . 
J 5 HOH 202 902 218 HOH HOH B . 
J 5 HOH 203 903 238 HOH HOH B . 
J 5 HOH 204 904 83  HOH HOH B . 
J 5 HOH 205 905 213 HOH HOH B . 
J 5 HOH 206 906 14  HOH HOH B . 
J 5 HOH 207 907 356 HOH HOH B . 
J 5 HOH 208 908 188 HOH HOH B . 
J 5 HOH 209 909 190 HOH HOH B . 
# 
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                     8S7Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.443 
_cell.length_a_esd                 ? 
_cell.length_b                     113.338 
_cell.length_b_esd                 ? 
_cell.length_c                     130.168 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8S7Q 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8S7Q 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              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 potassium iodide 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 R 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         2023-03-04 
_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   0.967697 
_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        0.967697 
_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                                       8S7Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.40 
_reflns.d_resolution_low                               56.67 
_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                                     58641 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_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                                0.210 
_reflns.pdbx_Rpim_I_all                                0.070 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       517344 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.198 
_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                                    2.40 
_reflns_shell.d_res_low                                     2.47 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           34054 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4368 
_reflns_shell.percent_possible_obs                          96.9 
_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                               7.8 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.1 
_reflns_shell.pdbx_Rrim_I_all                               1.106 
_reflns_shell.pdbx_Rpim_I_all                               0.390 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.664 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.032 
_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]                            0.52 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.25 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.27 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.616 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.919 
_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                                 8S7Q 
_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                            2.40 
_refine.ls_d_res_low                             52.01 
_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                     55531 
_refine.ls_number_reflns_R_free                  3039 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.68 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18082 
_refine.ls_R_factor_R_free                       0.23064 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17813 
_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                       0.281 
_refine.pdbx_overall_ESU_R_Free                  0.223 
_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                             6.926 
_refine.overall_SU_ML                            0.157 
_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                       2.40 
_refine_hist.d_res_low                        52.01 
_refine_hist.number_atoms_solvent             358 
_refine_hist.number_atoms_total               8671 
_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        8180 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         133 
_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' ? 0.007  0.012  8550  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  7827  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.394  1.651  11645 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.488  1.568  18040 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.009  5.000  1036  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.090  5.000  52    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.517 10.000 1324  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  1223  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  9966  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1977  ? 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' ? 2.459  3.189  4150  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.457  3.189  4150  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.584  5.730  5184  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.584  5.730  5185  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.399  3.564  4400  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.398  3.565  4401  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.270  6.364  6462  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.292  31.73  9889  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.292  31.67  9843  ? 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                       2.400 
_refine_ls_shell.d_res_low                        2.462 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             217 
_refine_ls_shell.number_reflns_R_work             3907 
_refine_ls_shell.percent_reflns_obs               96.38 
_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                  0.255 
_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                  0.296 
# 
_struct.entry_id                     8S7Q 
_struct.title                        'Vanillyl-alcohol dehydrogenase from Marinicaulis flavus: P151I mutant' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8S7Q 
_struct_keywords.text            'FAD, flavin, oxidase, alcohol, enzyme mechanism, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    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 8S7Q A 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
2 1 8S7Q B 1 ? 521 ? A0A2S7K3M2 1 ? 521 ? 1 521 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8S7Q ILE A 151 ? UNP A0A2S7K3M2 PRO 151 'engineered mutation' 151 1 
2 8S7Q ILE B 151 ? UNP A0A2S7K3M2 PRO 151 'engineered mutation' 151 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 11230 ? 
1 MORE         -74   ? 
1 'SSA (A^2)'  33610 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 26  ? SER A 10  GLY A 26  1 ? 17 
HELX_P HELX_P2  AA2 THR A 32  ? GLU A 40  ? THR A 32  GLU A 40  5 ? 9  
HELX_P HELX_P3  AA3 SER A 62  ? GLY A 77  ? SER A 62  GLY A 77  1 ? 16 
HELX_P HELX_P4  AA4 SER A 129 ? LYS A 140 ? SER A 129 LYS A 140 1 ? 12 
HELX_P HELX_P5  AA5 SER A 155 ? ASP A 162 ? SER A 155 ASP A 162 1 ? 8  
HELX_P HELX_P6  AA6 HIS A 173 ? ALA A 175 ? HIS A 173 ALA A 175 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 193 ? MET A 197 ? GLY A 193 MET A 197 5 ? 5  
HELX_P HELX_P8  AA8 VAL A 214 ? SER A 219 ? VAL A 214 SER A 219 5 ? 6  
HELX_P HELX_P9  AA9 ASN A 249 ? ASP A 251 ? ASN A 249 ASP A 251 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 252 ? ALA A 266 ? ASP A 252 ALA A 266 1 ? 15 
HELX_P HELX_P11 AB2 LEU A 278 ? ALA A 283 ? LEU A 278 ALA A 283 1 ? 6  
HELX_P HELX_P12 AB3 THR A 287 ? TYR A 291 ? THR A 287 TYR A 291 5 ? 5  
HELX_P HELX_P13 AB4 PRO A 299 ? ASP A 311 ? PRO A 299 ASP A 311 1 ? 13 
HELX_P HELX_P14 AB5 PRO A 324 ? ALA A 340 ? PRO A 324 ALA A 340 1 ? 17 
HELX_P HELX_P15 AB6 PHE A 349 ? ARG A 353 ? PHE A 349 ARG A 353 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 358 ? MET A 367 ? ASP A 358 MET A 367 1 ? 10 
HELX_P HELX_P17 AB8 LEU A 373 ? TRP A 381 ? LEU A 373 TRP A 381 5 ? 9  
HELX_P HELX_P18 AB9 THR A 397 ? TYR A 415 ? THR A 397 TYR A 415 1 ? 19 
HELX_P HELX_P19 AC1 ASP A 442 ? ALA A 462 ? ASP A 442 ALA A 462 1 ? 21 
HELX_P HELX_P20 AC2 HIS A 471 ? ARG A 473 ? HIS A 471 ARG A 473 5 ? 3  
HELX_P HELX_P21 AC3 TYR A 474 ? LYS A 480 ? TYR A 474 LYS A 480 1 ? 7  
HELX_P HELX_P22 AC4 SER A 483 ? ASP A 501 ? SER A 483 ASP A 501 1 ? 19 
HELX_P HELX_P23 AC5 GLY A 509 ? ILE A 513 ? GLY A 509 ILE A 513 5 ? 5  
HELX_P HELX_P24 AC6 SER B 10  ? GLY B 26  ? SER B 10  GLY B 26  1 ? 17 
HELX_P HELX_P25 AC7 THR B 32  ? GLU B 40  ? THR B 32  GLU B 40  5 ? 9  
HELX_P HELX_P26 AC8 SER B 62  ? GLY B 77  ? SER B 62  GLY B 77  1 ? 16 
HELX_P HELX_P27 AC9 SER B 129 ? GLY B 141 ? SER B 129 GLY B 141 1 ? 13 
HELX_P HELX_P28 AD1 SER B 155 ? ASP B 162 ? SER B 155 ASP B 162 1 ? 8  
HELX_P HELX_P29 AD2 GLY B 193 ? MET B 197 ? GLY B 193 MET B 197 5 ? 5  
HELX_P HELX_P30 AD3 VAL B 214 ? SER B 219 ? VAL B 214 SER B 219 5 ? 6  
HELX_P HELX_P31 AD4 ASN B 249 ? ASP B 251 ? ASN B 249 ASP B 251 5 ? 3  
HELX_P HELX_P32 AD5 ASP B 252 ? ALA B 266 ? ASP B 252 ALA B 266 1 ? 15 
HELX_P HELX_P33 AD6 LEU B 278 ? ALA B 283 ? LEU B 278 ALA B 283 1 ? 6  
HELX_P HELX_P34 AD7 THR B 287 ? TYR B 291 ? THR B 287 TYR B 291 5 ? 5  
HELX_P HELX_P35 AD8 PRO B 299 ? ASP B 311 ? PRO B 299 ASP B 311 1 ? 13 
HELX_P HELX_P36 AD9 PRO B 324 ? ALA B 340 ? PRO B 324 ALA B 340 1 ? 17 
HELX_P HELX_P37 AE1 PHE B 349 ? ARG B 353 ? PHE B 349 ARG B 353 5 ? 5  
HELX_P HELX_P38 AE2 ASP B 358 ? MET B 367 ? ASP B 358 MET B 367 1 ? 10 
HELX_P HELX_P39 AE3 LEU B 373 ? TRP B 381 ? LEU B 373 TRP B 381 5 ? 9  
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 ? TYR B 482 ? TYR B 474 TYR B 482 1 ? 9  
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  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 8 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 30  ? PHE A 31  ? VAL A 30  PHE A 31  
AA1 2 ALA A 56  ? VAL A 58  ? ALA A 56  VAL A 58  
AA1 3 VAL A 102 ? ASP A 105 ? VAL A 102 ASP A 105 
AA1 4 LEU A 80  ? VAL A 83  ? LEU A 80  VAL A 83  
AA2 1 ILE A 112 ? ASN A 116 ? ILE A 112 ASN A 116 
AA2 2 TYR A 121 ? VAL A 124 ? TYR A 121 VAL A 124 
AA2 3 VAL A 225 ? TRP A 232 ? VAL A 225 TRP A 232 
AA2 4 GLN A 177 ? VAL A 183 ? GLN A 177 VAL A 183 
AA2 5 VAL A 189 ? ARG A 191 ? VAL A 189 ARG A 191 
AA3 1 LEU A 144 ? TRP A 145 ? LEU A 144 TRP A 145 
AA3 2 MET A 234 ? PRO A 235 ? MET A 234 PRO A 235 
AA4 1 LYS A 346 ? TYR A 348 ? LYS A 346 TYR A 348 
AA4 2 TYR A 240 ? PHE A 247 ? TYR A 240 PHE A 247 
AA4 3 TRP A 315 ? TYR A 322 ? TRP A 315 TYR A 322 
AA4 4 ALA A 273 ? SER A 277 ? ALA A 273 SER A 277 
AA4 5 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 PRO A 392 ? PRO A 395 ? PRO A 392 PRO A 395 
AA5 8 GLY A 466 ? GLU A 467 ? GLY A 466 GLU A 467 
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 LEU B 144 ? TRP B 145 ? LEU B 144 TRP B 145 
AA8 2 MET B 234 ? PRO B 235 ? MET B 234 PRO B 235 
AA9 1 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AA9 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AA9 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AA9 4 ALA B 273 ? SER B 277 ? ALA B 273 SER B 277 
AA9 5 GLY B 421 ? ILE B 425 ? GLY B 421 ILE B 425 
AA9 6 ASP B 429 ? TYR B 438 ? ASP B 429 TYR B 438 
AA9 7 GLY B 386 ? PHE B 390 ? GLY B 386 PHE B 390 
AB1 1 LYS B 346 ? TYR B 348 ? LYS B 346 TYR B 348 
AB1 2 TYR B 240 ? PHE B 247 ? TYR B 240 PHE B 247 
AB1 3 TRP B 315 ? TYR B 322 ? TRP B 315 TYR B 322 
AB1 4 ALA B 273 ? SER B 277 ? ALA B 273 SER B 277 
AB1 5 GLY B 421 ? ILE B 425 ? GLY B 421 ILE B 425 
AB1 6 ASP B 429 ? TYR B 438 ? ASP B 429 TYR B 438 
AB1 7 VAL B 393 ? PRO B 395 ? VAL B 393 PRO B 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 VAL A 103 ? O VAL A 103 
AA1 3 4 O VAL A 102 ? O VAL A 102 N TRP A 81  ? N TRP A 81  
AA2 1 2 N ASN A 116 ? N ASN A 116 O TYR A 121 ? O TYR A 121 
AA2 2 3 N VAL A 124 ? N VAL A 124 O MET A 229 ? O MET A 229 
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 SER A 277 ? N SER A 277 O GLY A 421 ? O GLY A 421 
AA4 5 6 N MET A 420 ? N MET A 420 O VAL A 435 ? O VAL A 435 
AA4 6 7 O THR A 434 ? O THR A 434 N PHE A 390 ? N PHE A 390 
AA5 1 2 O TYR A 348 ? O TYR A 348 N LEU A 244 ? N LEU A 244 
AA5 2 3 N ILE A 245 ? N ILE A 245 O PHE A 317 ? O PHE A 317 
AA5 3 4 O ASN A 316 ? O ASN A 316 N ARG A 276 ? N ARG A 276 
AA5 4 5 N SER A 277 ? N SER A 277 O GLY A 421 ? O GLY A 421 
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 
AA5 7 8 N VAL A 393 ? N VAL A 393 O GLY A 466 ? O GLY A 466 
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 VAL B 102 ? O VAL B 102 N TRP B 81  ? N TRP B 81  
AA7 1 2 N ASN B 116 ? N ASN B 116 O TYR B 121 ? O TYR B 121 
AA7 2 3 N ALA B 122 ? N ALA B 122 O ILE B 231 ? O ILE B 231 
AA7 3 4 O VAL B 225 ? O VAL B 225 N VAL B 183 ? N VAL B 183 
AA7 4 5 N VAL B 182 ? N VAL B 182 O VAL B 190 ? O VAL B 190 
AA8 1 2 N TRP B 145 ? N TRP B 145 O MET B 234 ? O MET B 234 
AA9 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AA9 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AA9 3 4 O ASN B 316 ? O ASN B 316 N ARG B 276 ? N ARG B 276 
AA9 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AA9 5 6 N LEU B 422 ? N LEU B 422 O VAL B 433 ? O VAL B 433 
AA9 6 7 O THR B 434 ? O THR B 434 N PHE B 390 ? N PHE B 390 
AB1 1 2 O TYR B 348 ? O TYR B 348 N LEU B 244 ? N LEU B 244 
AB1 2 3 N ILE B 245 ? N ILE B 245 O PHE B 317 ? O PHE B 317 
AB1 3 4 O ASN B 316 ? O ASN B 316 N ARG B 276 ? N ARG B 276 
AB1 4 5 N SER B 277 ? N SER B 277 O GLY B 421 ? O GLY B 421 
AB1 5 6 N LEU B 422 ? N LEU B 422 O VAL B 433 ? O VAL B 433 
AB1 6 7 O LEU B 430 ? O LEU B 430 N SER B 394 ? N SER B 394 
# 
_pdbx_entry_details.entry_id                   8S7Q 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NE2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    387 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   C8M 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   FAD 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.48 
# 
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  ? ? 51.84   -120.11 
2  1 TYR A 43  ? ? -116.67 67.97   
3  1 LYS A 87  ? ? -96.89  35.50   
4  1 ALA A 90  ? ? 88.30   -13.77  
5  1 ASP A 150 ? ? 71.06   -75.35  
6  1 TYR A 170 ? ? -96.46  34.18   
7  1 LEU A 423 ? ? -62.65  97.35   
8  1 TRP A 427 ? ? -124.01 -52.79  
9  1 HIS A 431 ? ? -109.75 52.25   
10 1 HIS A 432 ? ? -35.60  98.02   
11 1 TYR A 482 ? ? -95.67  58.68   
12 1 ALA A 507 ? ? 35.71   61.49   
13 1 GLU B 33  ? ? 52.23   -121.86 
14 1 TYR B 43  ? ? -109.78 63.84   
15 1 ALA B 90  ? ? 100.79  -22.37  
16 1 PRO B 149 ? ? -66.04  -179.99 
17 1 TYR B 170 ? ? -96.85  35.59   
18 1 GLN B 220 ? ? 35.93   54.68   
19 1 TYR B 240 ? ? -163.74 118.05  
20 1 TRP B 427 ? ? -131.48 -61.00  
21 1 ALA B 507 ? ? 38.98   64.15   
# 
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 20  ? ? 0.133 'SIDE CHAIN' 
2 1 ARG A 108 ? ? 0.074 'SIDE CHAIN' 
3 1 ARG A 191 ? ? 0.079 'SIDE CHAIN' 
4 1 ARG A 413 ? ? 0.078 'SIDE CHAIN' 
5 1 ARG A 519 ? ? 0.081 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A LYS 520 ? A LYS 520 
2 1 Y 1 A ALA 521 ? A ALA 521 
3 1 Y 1 B LYS 520 ? B LYS 520 
4 1 Y 1 B ALA 521 ? B ALA 521 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
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 
GOL C1     C N N 223 
GOL O1     O N N 224 
GOL C2     C N N 225 
GOL O2     O N N 226 
GOL C3     C N N 227 
GOL O3     O N N 228 
GOL H11    H N N 229 
GOL H12    H N N 230 
GOL HO1    H N N 231 
GOL H2     H N N 232 
GOL HO2    H N N 233 
GOL H31    H N N 234 
GOL H32    H N N 235 
GOL HO3    H N N 236 
HIS N      N N N 237 
HIS CA     C N S 238 
HIS C      C N N 239 
HIS O      O N N 240 
HIS CB     C N N 241 
HIS CG     C Y N 242 
HIS ND1    N Y N 243 
HIS CD2    C Y N 244 
HIS CE1    C Y N 245 
HIS NE2    N Y N 246 
HIS OXT    O N N 247 
HIS H      H N N 248 
HIS H2     H N N 249 
HIS HA     H N N 250 
HIS HB2    H N N 251 
HIS HB3    H N N 252 
HIS HD1    H N N 253 
HIS HD2    H N N 254 
HIS HE1    H N N 255 
HIS HE2    H N N 256 
HIS HXT    H N N 257 
HOH O      O N N 258 
HOH H1     H N N 259 
HOH H2     H N N 260 
ILE N      N N N 261 
ILE CA     C N S 262 
ILE C      C N N 263 
ILE O      O N N 264 
ILE CB     C N S 265 
ILE CG1    C N N 266 
ILE CG2    C N N 267 
ILE CD1    C N N 268 
ILE OXT    O N N 269 
ILE H      H N N 270 
ILE H2     H N N 271 
ILE HA     H N N 272 
ILE HB     H N N 273 
ILE HG12   H N N 274 
ILE HG13   H N N 275 
ILE HG21   H N N 276 
ILE HG22   H N N 277 
ILE HG23   H N N 278 
ILE HD11   H N N 279 
ILE HD12   H N N 280 
ILE HD13   H N N 281 
ILE HXT    H N N 282 
LEU N      N N N 283 
LEU CA     C N S 284 
LEU C      C N N 285 
LEU O      O N N 286 
LEU CB     C N N 287 
LEU CG     C N N 288 
LEU CD1    C N N 289 
LEU CD2    C N N 290 
LEU OXT    O N N 291 
LEU H      H N N 292 
LEU H2     H N N 293 
LEU HA     H N N 294 
LEU HB2    H N N 295 
LEU HB3    H N N 296 
LEU HG     H N N 297 
LEU HD11   H N N 298 
LEU HD12   H N N 299 
LEU HD13   H N N 300 
LEU HD21   H N N 301 
LEU HD22   H N N 302 
LEU HD23   H N N 303 
LEU HXT    H N N 304 
LYS N      N N N 305 
LYS CA     C N S 306 
LYS C      C N N 307 
LYS O      O N N 308 
LYS CB     C N N 309 
LYS CG     C N N 310 
LYS CD     C N N 311 
LYS CE     C N N 312 
LYS NZ     N N N 313 
LYS OXT    O N N 314 
LYS H      H N N 315 
LYS H2     H N N 316 
LYS HA     H N N 317 
LYS HB2    H N N 318 
LYS HB3    H N N 319 
LYS HG2    H N N 320 
LYS HG3    H N N 321 
LYS HD2    H N N 322 
LYS HD3    H N N 323 
LYS HE2    H N N 324 
LYS HE3    H N N 325 
LYS HZ1    H N N 326 
LYS HZ2    H N N 327 
LYS HZ3    H N N 328 
LYS HXT    H N N 329 
MET N      N N N 330 
MET CA     C N S 331 
MET C      C N N 332 
MET O      O N N 333 
MET CB     C N N 334 
MET CG     C N N 335 
MET SD     S N N 336 
MET CE     C N N 337 
MET OXT    O N N 338 
MET H      H N N 339 
MET H2     H N N 340 
MET HA     H N N 341 
MET HB2    H N N 342 
MET HB3    H N N 343 
MET HG2    H N N 344 
MET HG3    H N N 345 
MET HE1    H N N 346 
MET HE2    H N N 347 
MET HE3    H N N 348 
MET HXT    H N N 349 
PEG C1     C N N 350 
PEG O1     O N N 351 
PEG C2     C N N 352 
PEG O2     O N N 353 
PEG C3     C N N 354 
PEG C4     C N N 355 
PEG O4     O N N 356 
PEG H11    H N N 357 
PEG H12    H N N 358 
PEG HO1    H N N 359 
PEG H21    H N N 360 
PEG H22    H N N 361 
PEG H31    H N N 362 
PEG H32    H N N 363 
PEG H41    H N N 364 
PEG H42    H N N 365 
PEG HO4    H N N 366 
PHE N      N N N 367 
PHE CA     C N S 368 
PHE C      C N N 369 
PHE O      O N N 370 
PHE CB     C N N 371 
PHE CG     C Y N 372 
PHE CD1    C Y N 373 
PHE CD2    C Y N 374 
PHE CE1    C Y N 375 
PHE CE2    C Y N 376 
PHE CZ     C Y N 377 
PHE OXT    O N N 378 
PHE H      H N N 379 
PHE H2     H N N 380 
PHE HA     H N N 381 
PHE HB2    H N N 382 
PHE HB3    H N N 383 
PHE HD1    H N N 384 
PHE HD2    H N N 385 
PHE HE1    H N N 386 
PHE HE2    H N N 387 
PHE HZ     H N N 388 
PHE HXT    H N N 389 
PRO N      N N N 390 
PRO CA     C N S 391 
PRO C      C N N 392 
PRO O      O N N 393 
PRO CB     C N N 394 
PRO CG     C N N 395 
PRO CD     C N N 396 
PRO OXT    O N N 397 
PRO H      H N N 398 
PRO HA     H N N 399 
PRO HB2    H N N 400 
PRO HB3    H N N 401 
PRO HG2    H N N 402 
PRO HG3    H N N 403 
PRO HD2    H N N 404 
PRO HD3    H N N 405 
PRO HXT    H N N 406 
SER N      N N N 407 
SER CA     C N S 408 
SER C      C N N 409 
SER O      O N N 410 
SER CB     C N N 411 
SER OG     O N N 412 
SER OXT    O N N 413 
SER H      H N N 414 
SER H2     H N N 415 
SER HA     H N N 416 
SER HB2    H N N 417 
SER HB3    H N N 418 
SER HG     H N N 419 
SER HXT    H N N 420 
THR N      N N N 421 
THR CA     C N S 422 
THR C      C N N 423 
THR O      O N N 424 
THR CB     C N R 425 
THR OG1    O N N 426 
THR CG2    C N N 427 
THR OXT    O N N 428 
THR H      H N N 429 
THR H2     H N N 430 
THR HA     H N N 431 
THR HB     H N N 432 
THR HG1    H N N 433 
THR HG21   H N N 434 
THR HG22   H N N 435 
THR HG23   H N N 436 
THR HXT    H N N 437 
TRP N      N N N 438 
TRP CA     C N S 439 
TRP C      C N N 440 
TRP O      O N N 441 
TRP CB     C N N 442 
TRP CG     C Y N 443 
TRP CD1    C Y N 444 
TRP CD2    C Y N 445 
TRP NE1    N Y N 446 
TRP CE2    C Y N 447 
TRP CE3    C Y N 448 
TRP CZ2    C Y N 449 
TRP CZ3    C Y N 450 
TRP CH2    C Y N 451 
TRP OXT    O N N 452 
TRP H      H N N 453 
TRP H2     H N N 454 
TRP HA     H N N 455 
TRP HB2    H N N 456 
TRP HB3    H N N 457 
TRP HD1    H N N 458 
TRP HE1    H N N 459 
TRP HE3    H N N 460 
TRP HZ2    H N N 461 
TRP HZ3    H N N 462 
TRP HH2    H N N 463 
TRP HXT    H N N 464 
TYR N      N N N 465 
TYR CA     C N S 466 
TYR C      C N N 467 
TYR O      O N N 468 
TYR CB     C N N 469 
TYR CG     C Y N 470 
TYR CD1    C Y N 471 
TYR CD2    C Y N 472 
TYR CE1    C Y N 473 
TYR CE2    C Y N 474 
TYR CZ     C Y N 475 
TYR OH     O N N 476 
TYR OXT    O N N 477 
TYR H      H N N 478 
TYR H2     H N N 479 
TYR HA     H N N 480 
TYR HB2    H N N 481 
TYR HB3    H N N 482 
TYR HD1    H N N 483 
TYR HD2    H N N 484 
TYR HE1    H N N 485 
TYR HE2    H N N 486 
TYR HH     H N N 487 
TYR HXT    H N N 488 
VAL N      N N N 489 
VAL CA     C N S 490 
VAL C      C N N 491 
VAL O      O N N 492 
VAL CB     C N N 493 
VAL CG1    C N N 494 
VAL CG2    C N N 495 
VAL OXT    O N N 496 
VAL H      H N N 497 
VAL H2     H N N 498 
VAL HA     H N N 499 
VAL HB     H N N 500 
VAL HG11   H N N 501 
VAL HG12   H N N 502 
VAL HG13   H N N 503 
VAL HG21   H N N 504 
VAL HG22   H N N 505 
VAL HG23   H N N 506 
VAL HXT    H N N 507 
# 
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 
GOL C1    O1     sing N N 220 
GOL C1    C2     sing N N 221 
GOL C1    H11    sing N N 222 
GOL C1    H12    sing N N 223 
GOL O1    HO1    sing N N 224 
GOL C2    O2     sing N N 225 
GOL C2    C3     sing N N 226 
GOL C2    H2     sing N N 227 
GOL O2    HO2    sing N N 228 
GOL C3    O3     sing N N 229 
GOL C3    H31    sing N N 230 
GOL C3    H32    sing N N 231 
GOL O3    HO3    sing N N 232 
HIS N     CA     sing N N 233 
HIS N     H      sing N N 234 
HIS N     H2     sing N N 235 
HIS CA    C      sing N N 236 
HIS CA    CB     sing N N 237 
HIS CA    HA     sing N N 238 
HIS C     O      doub N N 239 
HIS C     OXT    sing N N 240 
HIS CB    CG     sing N N 241 
HIS CB    HB2    sing N N 242 
HIS CB    HB3    sing N N 243 
HIS CG    ND1    sing Y N 244 
HIS CG    CD2    doub Y N 245 
HIS ND1   CE1    doub Y N 246 
HIS ND1   HD1    sing N N 247 
HIS CD2   NE2    sing Y N 248 
HIS CD2   HD2    sing N N 249 
HIS CE1   NE2    sing Y N 250 
HIS CE1   HE1    sing N N 251 
HIS NE2   HE2    sing N N 252 
HIS OXT   HXT    sing N N 253 
HOH O     H1     sing N N 254 
HOH O     H2     sing N N 255 
ILE N     CA     sing N N 256 
ILE N     H      sing N N 257 
ILE N     H2     sing N N 258 
ILE CA    C      sing N N 259 
ILE CA    CB     sing N N 260 
ILE CA    HA     sing N N 261 
ILE C     O      doub N N 262 
ILE C     OXT    sing N N 263 
ILE CB    CG1    sing N N 264 
ILE CB    CG2    sing N N 265 
ILE CB    HB     sing N N 266 
ILE CG1   CD1    sing N N 267 
ILE CG1   HG12   sing N N 268 
ILE CG1   HG13   sing N N 269 
ILE CG2   HG21   sing N N 270 
ILE CG2   HG22   sing N N 271 
ILE CG2   HG23   sing N N 272 
ILE CD1   HD11   sing N N 273 
ILE CD1   HD12   sing N N 274 
ILE CD1   HD13   sing N N 275 
ILE OXT   HXT    sing N N 276 
LEU N     CA     sing N N 277 
LEU N     H      sing N N 278 
LEU N     H2     sing N N 279 
LEU CA    C      sing N N 280 
LEU CA    CB     sing N N 281 
LEU CA    HA     sing N N 282 
LEU C     O      doub N N 283 
LEU C     OXT    sing N N 284 
LEU CB    CG     sing N N 285 
LEU CB    HB2    sing N N 286 
LEU CB    HB3    sing N N 287 
LEU CG    CD1    sing N N 288 
LEU CG    CD2    sing N N 289 
LEU CG    HG     sing N N 290 
LEU CD1   HD11   sing N N 291 
LEU CD1   HD12   sing N N 292 
LEU CD1   HD13   sing N N 293 
LEU CD2   HD21   sing N N 294 
LEU CD2   HD22   sing N N 295 
LEU CD2   HD23   sing N N 296 
LEU OXT   HXT    sing N N 297 
LYS N     CA     sing N N 298 
LYS N     H      sing N N 299 
LYS N     H2     sing N N 300 
LYS CA    C      sing N N 301 
LYS CA    CB     sing N N 302 
LYS CA    HA     sing N N 303 
LYS C     O      doub N N 304 
LYS C     OXT    sing N N 305 
LYS CB    CG     sing N N 306 
LYS CB    HB2    sing N N 307 
LYS CB    HB3    sing N N 308 
LYS CG    CD     sing N N 309 
LYS CG    HG2    sing N N 310 
LYS CG    HG3    sing N N 311 
LYS CD    CE     sing N N 312 
LYS CD    HD2    sing N N 313 
LYS CD    HD3    sing N N 314 
LYS CE    NZ     sing N N 315 
LYS CE    HE2    sing N N 316 
LYS CE    HE3    sing N N 317 
LYS NZ    HZ1    sing N N 318 
LYS NZ    HZ2    sing N N 319 
LYS NZ    HZ3    sing N N 320 
LYS OXT   HXT    sing N N 321 
MET N     CA     sing N N 322 
MET N     H      sing N N 323 
MET N     H2     sing N N 324 
MET CA    C      sing N N 325 
MET CA    CB     sing N N 326 
MET CA    HA     sing N N 327 
MET C     O      doub N N 328 
MET C     OXT    sing N N 329 
MET CB    CG     sing N N 330 
MET CB    HB2    sing N N 331 
MET CB    HB3    sing N N 332 
MET CG    SD     sing N N 333 
MET CG    HG2    sing N N 334 
MET CG    HG3    sing N N 335 
MET SD    CE     sing N N 336 
MET CE    HE1    sing N N 337 
MET CE    HE2    sing N N 338 
MET CE    HE3    sing N N 339 
MET OXT   HXT    sing N N 340 
PEG C1    O1     sing N N 341 
PEG C1    C2     sing N N 342 
PEG C1    H11    sing N N 343 
PEG C1    H12    sing N N 344 
PEG O1    HO1    sing N N 345 
PEG C2    O2     sing N N 346 
PEG C2    H21    sing N N 347 
PEG C2    H22    sing N N 348 
PEG O2    C3     sing N N 349 
PEG C3    C4     sing N N 350 
PEG C3    H31    sing N N 351 
PEG C3    H32    sing N N 352 
PEG C4    O4     sing N N 353 
PEG C4    H41    sing N N 354 
PEG C4    H42    sing N N 355 
PEG O4    HO4    sing N N 356 
PHE N     CA     sing N N 357 
PHE N     H      sing N N 358 
PHE N     H2     sing N N 359 
PHE CA    C      sing N N 360 
PHE CA    CB     sing N N 361 
PHE CA    HA     sing N N 362 
PHE C     O      doub N N 363 
PHE C     OXT    sing N N 364 
PHE CB    CG     sing N N 365 
PHE CB    HB2    sing N N 366 
PHE CB    HB3    sing N N 367 
PHE CG    CD1    doub Y N 368 
PHE CG    CD2    sing Y N 369 
PHE CD1   CE1    sing Y N 370 
PHE CD1   HD1    sing N N 371 
PHE CD2   CE2    doub Y N 372 
PHE CD2   HD2    sing N N 373 
PHE CE1   CZ     doub Y N 374 
PHE CE1   HE1    sing N N 375 
PHE CE2   CZ     sing Y N 376 
PHE CE2   HE2    sing N N 377 
PHE CZ    HZ     sing N N 378 
PHE OXT   HXT    sing N N 379 
PRO N     CA     sing N N 380 
PRO N     CD     sing N N 381 
PRO N     H      sing N N 382 
PRO CA    C      sing N N 383 
PRO CA    CB     sing N N 384 
PRO CA    HA     sing N N 385 
PRO C     O      doub N N 386 
PRO C     OXT    sing N N 387 
PRO CB    CG     sing N N 388 
PRO CB    HB2    sing N N 389 
PRO CB    HB3    sing N N 390 
PRO CG    CD     sing N N 391 
PRO CG    HG2    sing N N 392 
PRO CG    HG3    sing N N 393 
PRO CD    HD2    sing N N 394 
PRO CD    HD3    sing N N 395 
PRO OXT   HXT    sing N N 396 
SER N     CA     sing N N 397 
SER N     H      sing N N 398 
SER N     H2     sing N N 399 
SER CA    C      sing N N 400 
SER CA    CB     sing N N 401 
SER CA    HA     sing N N 402 
SER C     O      doub N N 403 
SER C     OXT    sing N N 404 
SER CB    OG     sing N N 405 
SER CB    HB2    sing N N 406 
SER CB    HB3    sing N N 407 
SER OG    HG     sing N N 408 
SER OXT   HXT    sing N N 409 
THR N     CA     sing N N 410 
THR N     H      sing N N 411 
THR N     H2     sing N N 412 
THR CA    C      sing N N 413 
THR CA    CB     sing N N 414 
THR CA    HA     sing N N 415 
THR C     O      doub N N 416 
THR C     OXT    sing N N 417 
THR CB    OG1    sing N N 418 
THR CB    CG2    sing N N 419 
THR CB    HB     sing N N 420 
THR OG1   HG1    sing N N 421 
THR CG2   HG21   sing N N 422 
THR CG2   HG22   sing N N 423 
THR CG2   HG23   sing N N 424 
THR OXT   HXT    sing N N 425 
TRP N     CA     sing N N 426 
TRP N     H      sing N N 427 
TRP N     H2     sing N N 428 
TRP CA    C      sing N N 429 
TRP CA    CB     sing N N 430 
TRP CA    HA     sing N N 431 
TRP C     O      doub N N 432 
TRP C     OXT    sing N N 433 
TRP CB    CG     sing N N 434 
TRP CB    HB2    sing N N 435 
TRP CB    HB3    sing N N 436 
TRP CG    CD1    doub Y N 437 
TRP CG    CD2    sing Y N 438 
TRP CD1   NE1    sing Y N 439 
TRP CD1   HD1    sing N N 440 
TRP CD2   CE2    doub Y N 441 
TRP CD2   CE3    sing Y N 442 
TRP NE1   CE2    sing Y N 443 
TRP NE1   HE1    sing N N 444 
TRP CE2   CZ2    sing Y N 445 
TRP CE3   CZ3    doub Y N 446 
TRP CE3   HE3    sing N N 447 
TRP CZ2   CH2    doub Y N 448 
TRP CZ2   HZ2    sing N N 449 
TRP CZ3   CH2    sing Y N 450 
TRP CZ3   HZ3    sing N N 451 
TRP CH2   HH2    sing N N 452 
TRP OXT   HXT    sing N N 453 
TYR N     CA     sing N N 454 
TYR N     H      sing N N 455 
TYR N     H2     sing N N 456 
TYR CA    C      sing N N 457 
TYR CA    CB     sing N N 458 
TYR CA    HA     sing N N 459 
TYR C     O      doub N N 460 
TYR C     OXT    sing N N 461 
TYR CB    CG     sing N N 462 
TYR CB    HB2    sing N N 463 
TYR CB    HB3    sing N N 464 
TYR CG    CD1    doub Y N 465 
TYR CG    CD2    sing Y N 466 
TYR CD1   CE1    sing Y N 467 
TYR CD1   HD1    sing N N 468 
TYR CD2   CE2    doub Y N 469 
TYR CD2   HD2    sing N N 470 
TYR CE1   CZ     doub Y N 471 
TYR CE1   HE1    sing N N 472 
TYR CE2   CZ     sing Y N 473 
TYR CE2   HE2    sing N N 474 
TYR CZ    OH     sing N N 475 
TYR OH    HH     sing N N 476 
TYR OXT   HXT    sing N N 477 
VAL N     CA     sing N N 478 
VAL N     H      sing N N 479 
VAL N     H2     sing N N 480 
VAL CA    C      sing N N 481 
VAL CA    CB     sing N N 482 
VAL CA    HA     sing N N 483 
VAL C     O      doub N N 484 
VAL C     OXT    sing N N 485 
VAL CB    CG1    sing N N 486 
VAL CB    CG2    sing N N 487 
VAL CB    HB     sing N N 488 
VAL CG1   HG11   sing N N 489 
VAL CG1   HG12   sing N N 490 
VAL CG1   HG13   sing N N 491 
VAL CG2   HG21   sing N N 492 
VAL CG2   HG22   sing N N 493 
VAL CG2   HG23   sing N N 494 
VAL OXT   HXT    sing N N 495 
# 
_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                    8S7Q 
_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]   0.009956 
_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]   0.008823 
_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]   0.007682 
_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     . MET A 1 1   ? 7.688  -39.831 -10.293 1.00 75.06  ? 1   MET A N     1 
ATOM   2    C CA    . MET A 1 1   ? 8.211  -40.049 -8.912  1.00 84.27  ? 1   MET A CA    1 
ATOM   3    C C     . MET A 1 1   ? 9.738  -40.191 -8.936  1.00 79.93  ? 1   MET A C     1 
ATOM   4    O O     . MET A 1 1   ? 10.463 -39.274 -8.556  1.00 75.25  ? 1   MET A O     1 
ATOM   5    C CB    . MET A 1 1   ? 7.565  -41.291 -8.281  1.00 99.40  ? 1   MET A CB    1 
ATOM   6    C CG    . MET A 1 1   ? 6.613  -40.969 -7.142  1.00 106.71 ? 1   MET A CG    1 
ATOM   7    S SD    . MET A 1 1   ? 5.429  -42.306 -6.819  1.00 105.65 ? 1   MET A SD    1 
ATOM   8    C CE    . MET A 1 1   ? 4.012  -41.349 -6.275  1.00 101.35 ? 1   MET A CE    1 
ATOM   9    N N     . ALA A 1 2   ? 10.221 -41.369 -9.343  1.00 73.50  ? 2   ALA A N     1 
ATOM   10   C CA    . ALA A 1 2   ? 11.591 -41.542 -9.789  1.00 65.21  ? 2   ALA A CA    1 
ATOM   11   C C     . ALA A 1 2   ? 11.570 -41.495 -11.314 1.00 63.01  ? 2   ALA A C     1 
ATOM   12   O O     . ALA A 1 2   ? 10.520 -41.721 -11.922 1.00 52.00  ? 2   ALA A O     1 
ATOM   13   C CB    . ALA A 1 2   ? 12.150 -42.847 -9.272  1.00 61.50  ? 2   ALA A CB    1 
ATOM   14   N N     . ALA A 1 3   ? 12.726 -41.204 -11.925 1.00 59.77  ? 3   ALA A N     1 
ATOM   15   C CA    . ALA A 1 3   ? 12.775 -40.945 -13.355 1.00 53.69  ? 3   ALA A CA    1 
ATOM   16   C C     . ALA A 1 3   ? 12.387 -42.207 -14.122 1.00 49.75  ? 3   ALA A C     1 
ATOM   17   O O     . ALA A 1 3   ? 12.807 -43.313 -13.789 1.00 47.71  ? 3   ALA A O     1 
ATOM   18   C CB    . ALA A 1 3   ? 14.140 -40.439 -13.758 1.00 57.94  ? 3   ALA A CB    1 
ATOM   19   N N     . PRO A 1 4   ? 11.534 -42.075 -15.156 1.00 49.94  ? 4   PRO A N     1 
ATOM   20   C CA    . PRO A 1 4   ? 11.200 -43.195 -16.036 1.00 53.47  ? 4   PRO A CA    1 
ATOM   21   C C     . PRO A 1 4   ? 12.271 -43.497 -17.087 1.00 56.13  ? 4   PRO A C     1 
ATOM   22   O O     . PRO A 1 4   ? 13.057 -42.617 -17.431 1.00 60.73  ? 4   PRO A O     1 
ATOM   23   C CB    . PRO A 1 4   ? 9.923  -42.683 -16.729 1.00 55.81  ? 4   PRO A CB    1 
ATOM   24   C CG    . PRO A 1 4   ? 10.119 -41.180 -16.808 1.00 52.52  ? 4   PRO A CG    1 
ATOM   25   C CD    . PRO A 1 4   ? 10.832 -40.831 -15.518 1.00 52.08  ? 4   PRO A CD    1 
ATOM   26   N N     . LEU A 1 5   ? 12.257 -44.723 -17.629 1.00 48.65  ? 5   LEU A N     1 
ATOM   27   C CA    . LEU A 1 5   ? 13.135 -45.104 -18.729 1.00 51.35  ? 5   LEU A CA    1 
ATOM   28   C C     . LEU A 1 5   ? 12.786 -44.301 -19.981 1.00 50.82  ? 5   LEU A C     1 
ATOM   29   O O     . LEU A 1 5   ? 11.619 -44.008 -20.223 1.00 52.25  ? 5   LEU A O     1 
ATOM   30   C CB    . LEU A 1 5   ? 12.990 -46.604 -19.015 1.00 49.09  ? 5   LEU A CB    1 
ATOM   31   C CG    . LEU A 1 5   ? 13.685 -47.537 -18.023 1.00 52.13  ? 5   LEU A CG    1 
ATOM   32   C CD1   . LEU A 1 5   ? 13.115 -48.946 -18.107 1.00 50.10  ? 5   LEU A CD1   1 
ATOM   33   C CD2   . LEU A 1 5   ? 15.188 -47.563 -18.267 1.00 53.49  ? 5   LEU A CD2   1 
ATOM   34   N N     . PRO A 1 6   ? 13.772 -43.949 -20.839 1.00 46.57  ? 6   PRO A N     1 
ATOM   35   C CA    . PRO A 1 6   ? 13.471 -43.301 -22.112 1.00 44.73  ? 6   PRO A CA    1 
ATOM   36   C C     . PRO A 1 6   ? 12.700 -44.287 -22.983 1.00 44.05  ? 6   PRO A C     1 
ATOM   37   O O     . PRO A 1 6   ? 13.008 -45.466 -23.002 1.00 41.77  ? 6   PRO A O     1 
ATOM   38   C CB    . PRO A 1 6   ? 14.841 -42.938 -22.714 1.00 43.45  ? 6   PRO A CB    1 
ATOM   39   C CG    . PRO A 1 6   ? 15.853 -43.815 -21.981 1.00 45.52  ? 6   PRO A CG    1 
ATOM   40   C CD    . PRO A 1 6   ? 15.213 -44.195 -20.658 1.00 48.50  ? 6   PRO A CD    1 
ATOM   41   N N     . GLU A 1 7   ? 11.688 -43.798 -23.689 1.00 48.41  ? 7   GLU A N     1 
ATOM   42   C CA    . GLU A 1 7   ? 10.857 -44.662 -24.499 1.00 53.75  ? 7   GLU A CA    1 
ATOM   43   C C     . GLU A 1 7   ? 11.770 -45.425 -25.450 1.00 53.47  ? 7   GLU A C     1 
ATOM   44   O O     . GLU A 1 7   ? 12.733 -44.851 -25.959 1.00 48.57  ? 7   GLU A O     1 
ATOM   45   C CB    . GLU A 1 7   ? 9.819  -43.835 -25.259 1.00 65.38  ? 7   GLU A CB    1 
ATOM   46   C CG    . GLU A 1 7   ? 8.724  -44.671 -25.895 1.00 74.46  ? 7   GLU A CG    1 
ATOM   47   C CD    . GLU A 1 7   ? 7.778  -43.889 -26.788 1.00 83.23  ? 7   GLU A CD    1 
ATOM   48   O OE1   . GLU A 1 7   ? 7.913  -42.646 -26.862 1.00 81.31  ? 7   GLU A OE1   1 
ATOM   49   O OE2   . GLU A 1 7   ? 6.920  -44.528 -27.425 1.00 88.07  ? 7   GLU A OE2   1 
ATOM   50   N N     . GLY A 1 8   ? 11.474 -46.720 -25.633 1.00 47.97  ? 8   GLY A N     1 
ATOM   51   C CA    . GLY A 1 8   ? 12.173 -47.558 -26.594 1.00 42.33  ? 8   GLY A CA    1 
ATOM   52   C C     . GLY A 1 8   ? 13.359 -48.283 -25.971 1.00 44.08  ? 8   GLY A C     1 
ATOM   53   O O     . GLY A 1 8   ? 14.025 -49.064 -26.643 1.00 43.52  ? 8   GLY A O     1 
ATOM   54   N N     . VAL A 1 9   ? 13.620 -48.029 -24.687 1.00 41.03  ? 9   VAL A N     1 
ATOM   55   C CA    . VAL A 1 9   ? 14.859 -48.471 -24.078 1.00 44.41  ? 9   VAL A CA    1 
ATOM   56   C C     . VAL A 1 9   ? 14.518 -49.422 -22.937 1.00 45.92  ? 9   VAL A C     1 
ATOM   57   O O     . VAL A 1 9   ? 14.008 -48.995 -21.901 1.00 48.11  ? 9   VAL A O     1 
ATOM   58   C CB    . VAL A 1 9   ? 15.708 -47.280 -23.579 1.00 47.17  ? 9   VAL A CB    1 
ATOM   59   C CG1   . VAL A 1 9   ? 16.946 -47.747 -22.825 1.00 46.47  ? 9   VAL A CG1   1 
ATOM   60   C CG2   . VAL A 1 9   ? 16.098 -46.330 -24.710 1.00 48.63  ? 9   VAL A CG2   1 
ATOM   61   N N     . SER A 1 10  ? 14.845 -50.698 -23.150 1.00 44.05  ? 10  SER A N     1 
ATOM   62   C CA    . SER A 1 10  ? 14.688 -51.756 -22.163 1.00 45.48  ? 10  SER A CA    1 
ATOM   63   C C     . SER A 1 10  ? 15.421 -51.428 -20.859 1.00 44.90  ? 10  SER A C     1 
ATOM   64   O O     . SER A 1 10  ? 16.395 -50.690 -20.846 1.00 49.29  ? 10  SER A O     1 
ATOM   65   C CB    . SER A 1 10  ? 15.174 -53.056 -22.758 1.00 45.18  ? 10  SER A CB    1 
ATOM   66   O OG    . SER A 1 10  ? 15.764 -53.874 -21.767 1.00 50.68  ? 10  SER A OG    1 
ATOM   67   N N     . ALA A 1 11  ? 14.951 -51.998 -19.747 1.00 44.67  ? 11  ALA A N     1 
ATOM   68   C CA    . ALA A 1 11  ? 15.598 -51.816 -18.457 1.00 43.35  ? 11  ALA A CA    1 
ATOM   69   C C     . ALA A 1 11  ? 16.950 -52.535 -18.428 1.00 44.77  ? 11  ALA A C     1 
ATOM   70   O O     . ALA A 1 11  ? 17.849 -52.162 -17.676 1.00 47.46  ? 11  ALA A O     1 
ATOM   71   C CB    . ALA A 1 11  ? 14.667 -52.319 -17.374 1.00 44.06  ? 11  ALA A CB    1 
ATOM   72   N N     . GLU A 1 12  ? 17.076 -53.598 -19.225 1.00 46.28  ? 12  GLU A N     1 
ATOM   73   C CA    . GLU A 1 12  ? 18.303 -54.365 -19.303 1.00 51.66  ? 12  GLU A CA    1 
ATOM   74   C C     . GLU A 1 12  ? 19.329 -53.536 -20.051 1.00 49.23  ? 12  GLU A C     1 
ATOM   75   O O     . GLU A 1 12  ? 20.501 -53.493 -19.665 1.00 51.94  ? 12  GLU A O     1 
ATOM   76   C CB    . GLU A 1 12  ? 18.116 -55.701 -20.029 1.00 61.01  ? 12  GLU A CB    1 
ATOM   77   C CG    . GLU A 1 12  ? 17.963 -56.887 -19.097 1.00 70.62  ? 12  GLU A CG    1 
ATOM   78   C CD    . GLU A 1 12  ? 16.587 -57.049 -18.480 1.00 85.26  ? 12  GLU A CD    1 
ATOM   79   O OE1   . GLU A 1 12  ? 15.668 -56.292 -18.870 1.00 93.81  ? 12  GLU A OE1   1 
ATOM   80   O OE2   . GLU A 1 12  ? 16.440 -57.937 -17.615 1.00 90.12  ? 12  GLU A OE2   1 
ATOM   81   N N     . ALA A 1 13  ? 18.856 -52.898 -21.126 1.00 43.44  ? 13  ALA A N     1 
ATOM   82   C CA    . ALA A 1 13  ? 19.708 -52.037 -21.927 1.00 43.96  ? 13  ALA A CA    1 
ATOM   83   C C     . ALA A 1 13  ? 20.310 -50.949 -21.034 1.00 43.07  ? 13  ALA A C     1 
ATOM   84   O O     . ALA A 1 13  ? 21.499 -50.655 -21.135 1.00 45.22  ? 13  ALA A O     1 
ATOM   85   C CB    . ALA A 1 13  ? 18.931 -51.474 -23.098 1.00 43.55  ? 13  ALA A CB    1 
ATOM   86   N N     . MET A 1 14  ? 19.504 -50.412 -20.111 1.00 39.89  ? 14  MET A N     1 
ATOM   87   C CA    . MET A 1 14  ? 19.931 -49.290 -19.297 1.00 43.38  ? 14  MET A CA    1 
ATOM   88   C C     . MET A 1 14  ? 20.945 -49.786 -18.271 1.00 44.01  ? 14  MET A C     1 
ATOM   89   O O     . MET A 1 14  ? 21.990 -49.166 -18.089 1.00 49.36  ? 14  MET A O     1 
ATOM   90   C CB    . MET A 1 14  ? 18.727 -48.620 -18.619 1.00 44.61  ? 14  MET A CB    1 
ATOM   91   C CG    . MET A 1 14  ? 19.071 -47.447 -17.699 1.00 45.40  ? 14  MET A CG    1 
ATOM   92   S SD    . MET A 1 14  ? 19.942 -46.038 -18.490 1.00 44.98  ? 14  MET A SD    1 
ATOM   93   C CE    . MET A 1 14  ? 18.625 -45.388 -19.519 1.00 46.06  ? 14  MET A CE    1 
ATOM   94   N N     . SER A 1 15  ? 20.664 -50.936 -17.651 1.00 45.63  ? 15  SER A N     1 
ATOM   95   C CA    . SER A 1 15  ? 21.563 -51.505 -16.656 1.00 44.56  ? 15  SER A CA    1 
ATOM   96   C C     . SER A 1 15  ? 22.923 -51.834 -17.263 1.00 44.26  ? 15  SER A C     1 
ATOM   97   O O     . SER A 1 15  ? 23.948 -51.589 -16.634 1.00 40.90  ? 15  SER A O     1 
ATOM   98   C CB    . SER A 1 15  ? 20.963 -52.722 -16.013 1.00 47.73  ? 15  SER A CB    1 
ATOM   99   O OG    . SER A 1 15  ? 20.041 -52.328 -15.014 1.00 53.39  ? 15  SER A OG    1 
ATOM   100  N N     . SER A 1 16  ? 22.909 -52.405 -18.476 1.00 44.96  ? 16  SER A N     1 
ATOM   101  C CA    . SER A 1 16  ? 24.120 -52.762 -19.195 1.00 44.33  ? 16  SER A CA    1 
ATOM   102  C C     . SER A 1 16  ? 24.950 -51.521 -19.498 1.00 44.62  ? 16  SER A C     1 
ATOM   103  O O     . SER A 1 16  ? 26.142 -51.490 -19.199 1.00 43.31  ? 16  SER A O     1 
ATOM   104  C CB    . SER A 1 16  ? 23.783 -53.487 -20.453 1.00 45.26  ? 16  SER A CB    1 
ATOM   105  O OG    . SER A 1 16  ? 23.068 -54.668 -20.152 1.00 48.64  ? 16  SER A OG    1 
ATOM   106  N N     . ALA A 1 17  ? 24.305 -50.505 -20.085 1.00 40.10  ? 17  ALA A N     1 
ATOM   107  C CA    . ALA A 1 17  ? 24.954 -49.228 -20.324 1.00 38.11  ? 17  ALA A CA    1 
ATOM   108  C C     . ALA A 1 17  ? 25.552 -48.699 -19.031 1.00 36.41  ? 17  ALA A C     1 
ATOM   109  O O     . ALA A 1 17  ? 26.731 -48.369 -18.993 1.00 34.27  ? 17  ALA A O     1 
ATOM   110  C CB    . ALA A 1 17  ? 23.968 -48.231 -20.872 1.00 40.03  ? 17  ALA A CB    1 
ATOM   111  N N     . LEU A 1 18  ? 24.730 -48.603 -17.980 1.00 37.29  ? 18  LEU A N     1 
ATOM   112  C CA    . LEU A 1 18  ? 25.193 -47.998 -16.738 1.00 41.67  ? 18  LEU A CA    1 
ATOM   113  C C     . LEU A 1 18  ? 26.394 -48.764 -16.173 1.00 44.53  ? 18  LEU A C     1 
ATOM   114  O O     . LEU A 1 18  ? 27.330 -48.143 -15.666 1.00 40.36  ? 18  LEU A O     1 
ATOM   115  C CB    . LEU A 1 18  ? 24.036 -47.898 -15.735 1.00 42.34  ? 18  LEU A CB    1 
ATOM   116  C CG    . LEU A 1 18  ? 22.932 -46.898 -16.100 1.00 47.45  ? 18  LEU A CG    1 
ATOM   117  C CD1   . LEU A 1 18  ? 21.910 -46.777 -14.983 1.00 48.89  ? 18  LEU A CD1   1 
ATOM   118  C CD2   . LEU A 1 18  ? 23.496 -45.518 -16.422 1.00 48.55  ? 18  LEU A CD2   1 
ATOM   119  N N     . ASP A 1 19  ? 26.373 -50.103 -16.289 1.00 48.65  ? 19  ASP A N     1 
ATOM   120  C CA    . ASP A 1 19  ? 27.491 -50.952 -15.890 1.00 51.38  ? 19  ASP A CA    1 
ATOM   121  C C     . ASP A 1 19  ? 28.748 -50.591 -16.670 1.00 46.67  ? 19  ASP A C     1 
ATOM   122  O O     . ASP A 1 19  ? 29.843 -50.484 -16.118 1.00 41.59  ? 19  ASP A O     1 
ATOM   123  C CB    . ASP A 1 19  ? 27.220 -52.439 -16.143 1.00 56.54  ? 19  ASP A CB    1 
ATOM   124  C CG    . ASP A 1 19  ? 26.821 -53.204 -14.896 1.00 66.99  ? 19  ASP A CG    1 
ATOM   125  O OD1   . ASP A 1 19  ? 26.381 -52.547 -13.908 1.00 61.09  ? 19  ASP A OD1   1 
ATOM   126  O OD2   . ASP A 1 19  ? 27.006 -54.444 -14.906 1.00 75.12  ? 19  ASP A OD2   1 
ATOM   127  N N     . ARG A 1 20  ? 28.572 -50.434 -17.976 1.00 46.22  ? 20  ARG A N     1 
ATOM   128  C CA    . ARG A 1 20  ? 29.692 -50.200 -18.860 1.00 47.22  ? 20  ARG A CA    1 
ATOM   129  C C     . ARG A 1 20  ? 30.208 -48.765 -18.688 1.00 48.81  ? 20  ARG A C     1 
ATOM   130  O O     . ARG A 1 20  ? 31.410 -48.543 -18.816 1.00 53.17  ? 20  ARG A O     1 
ATOM   131  C CB    . ARG A 1 20  ? 29.257 -50.572 -20.275 1.00 50.63  ? 20  ARG A CB    1 
ATOM   132  C CG    . ARG A 1 20  ? 30.412 -50.953 -21.185 1.00 60.57  ? 20  ARG A CG    1 
ATOM   133  C CD    . ARG A 1 20  ? 30.371 -52.399 -21.625 1.00 56.28  ? 20  ARG A CD    1 
ATOM   134  N NE    . ARG A 1 20  ? 30.619 -52.393 -23.046 1.00 51.24  ? 20  ARG A NE    1 
ATOM   135  C CZ    . ARG A 1 20  ? 29.873 -53.047 -23.920 1.00 56.83  ? 20  ARG A CZ    1 
ATOM   136  N NH1   . ARG A 1 20  ? 29.266 -54.173 -23.578 1.00 57.18  ? 20  ARG A NH1   1 
ATOM   137  N NH2   . ARG A 1 20  ? 29.804 -52.602 -25.158 1.00 59.21  ? 20  ARG A NH2   1 
ATOM   138  N N     . PHE A 1 21  ? 29.328 -47.806 -18.340 1.00 42.55  ? 21  PHE A N     1 
ATOM   139  C CA    . PHE A 1 21  ? 29.762 -46.452 -18.023 1.00 39.01  ? 21  PHE A CA    1 
ATOM   140  C C     . PHE A 1 21  ? 30.690 -46.475 -16.817 1.00 36.68  ? 21  PHE A C     1 
ATOM   141  O O     . PHE A 1 21  ? 31.712 -45.800 -16.813 1.00 39.54  ? 21  PHE A O     1 
ATOM   142  C CB    . PHE A 1 21  ? 28.580 -45.505 -17.764 1.00 38.43  ? 21  PHE A CB    1 
ATOM   143  C CG    . PHE A 1 21  ? 27.710 -45.185 -18.956 1.00 34.36  ? 21  PHE A CG    1 
ATOM   144  C CD1   . PHE A 1 21  ? 28.161 -45.360 -20.257 1.00 36.03  ? 21  PHE A CD1   1 
ATOM   145  C CD2   . PHE A 1 21  ? 26.418 -44.746 -18.776 1.00 31.79  ? 21  PHE A CD2   1 
ATOM   146  C CE1   . PHE A 1 21  ? 27.344 -45.092 -21.345 1.00 33.85  ? 21  PHE A CE1   1 
ATOM   147  C CE2   . PHE A 1 21  ? 25.603 -44.474 -19.864 1.00 34.55  ? 21  PHE A CE2   1 
ATOM   148  C CZ    . PHE A 1 21  ? 26.067 -44.644 -21.147 1.00 33.55  ? 21  PHE A CZ    1 
ATOM   149  N N     . ALA A 1 22  ? 30.334 -47.287 -15.821 1.00 43.53  ? 22  ALA A N     1 
ATOM   150  C CA    . ALA A 1 22  ? 31.022 -47.354 -14.538 1.00 45.41  ? 22  ALA A CA    1 
ATOM   151  C C     . ALA A 1 22  ? 32.455 -47.859 -14.686 1.00 43.50  ? 22  ALA A C     1 
ATOM   152  O O     . ALA A 1 22  ? 33.307 -47.518 -13.864 1.00 45.78  ? 22  ALA A O     1 
ATOM   153  C CB    . ALA A 1 22  ? 30.248 -48.229 -13.578 1.00 42.59  ? 22  ALA A CB    1 
ATOM   154  N N     . ARG A 1 23  ? 32.697 -48.690 -15.704 1.00 44.47  ? 23  ARG A N     1 
ATOM   155  C CA    . ARG A 1 23  ? 34.028 -49.221 -15.960 1.00 50.61  ? 23  ARG A CA    1 
ATOM   156  C C     . ARG A 1 23  ? 34.809 -48.268 -16.860 1.00 47.29  ? 23  ARG A C     1 
ATOM   157  O O     . ARG A 1 23  ? 36.041 -48.314 -16.865 1.00 53.76  ? 23  ARG A O     1 
ATOM   158  C CB    . ARG A 1 23  ? 33.966 -50.628 -16.574 1.00 52.36  ? 23  ARG A CB    1 
ATOM   159  C CG    . ARG A 1 23  ? 33.581 -51.723 -15.584 1.00 54.38  ? 23  ARG A CG    1 
ATOM   160  C CD    . ARG A 1 23  ? 33.217 -53.013 -16.298 1.00 59.86  ? 23  ARG A CD    1 
ATOM   161  N NE    . ARG A 1 23  ? 32.038 -53.655 -15.728 1.00 61.51  ? 23  ARG A NE    1 
ATOM   162  C CZ    . ARG A 1 23  ? 31.013 -54.139 -16.425 1.00 59.28  ? 23  ARG A CZ    1 
ATOM   163  N NH1   . ARG A 1 23  ? 31.022 -54.123 -17.751 1.00 51.10  ? 23  ARG A NH1   1 
ATOM   164  N NH2   . ARG A 1 23  ? 29.977 -54.649 -15.778 1.00 67.96  ? 23  ARG A NH2   1 
ATOM   165  N N     . ILE A 1 24  ? 34.092 -47.445 -17.644 1.00 41.56  ? 24  ILE A N     1 
ATOM   166  C CA    . ILE A 1 24  ? 34.727 -46.368 -18.381 1.00 38.14  ? 24  ILE A CA    1 
ATOM   167  C C     . ILE A 1 24  ? 35.234 -45.297 -17.412 1.00 38.17  ? 24  ILE A C     1 
ATOM   168  O O     . ILE A 1 24  ? 36.385 -44.891 -17.559 1.00 41.14  ? 24  ILE A O     1 
ATOM   169  C CB    . ILE A 1 24  ? 33.808 -45.786 -19.468 1.00 37.83  ? 24  ILE A CB    1 
ATOM   170  C CG1   . ILE A 1 24  ? 33.529 -46.821 -20.559 1.00 40.97  ? 24  ILE A CG1   1 
ATOM   171  C CG2   . ILE A 1 24  ? 34.412 -44.516 -20.061 1.00 37.95  ? 24  ILE A CG2   1 
ATOM   172  C CD1   . ILE A 1 24  ? 32.322 -46.492 -21.430 1.00 43.13  ? 24  ILE A CD1   1 
ATOM   173  N N     . VAL A 1 25  ? 34.420 -44.860 -16.425 1.00 34.19  ? 25  VAL A N     1 
ATOM   174  C CA    . VAL A 1 25  ? 34.773 -43.670 -15.656 1.00 37.32  ? 25  VAL A CA    1 
ATOM   175  C C     . VAL A 1 25  ? 35.040 -43.973 -14.185 1.00 42.45  ? 25  VAL A C     1 
ATOM   176  O O     . VAL A 1 25  ? 35.489 -43.075 -13.466 1.00 38.92  ? 25  VAL A O     1 
ATOM   177  C CB    . VAL A 1 25  ? 33.686 -42.589 -15.754 1.00 38.95  ? 25  VAL A CB    1 
ATOM   178  C CG1   . VAL A 1 25  ? 33.472 -42.132 -17.191 1.00 37.92  ? 25  VAL A CG1   1 
ATOM   179  C CG2   . VAL A 1 25  ? 32.379 -43.054 -15.121 1.00 39.62  ? 25  VAL A CG2   1 
ATOM   180  N N     . GLY A 1 26  ? 34.740 -45.211 -13.751 1.00 46.85  ? 26  GLY A N     1 
ATOM   181  C CA    . GLY A 1 26  ? 34.799 -45.599 -12.351 1.00 47.55  ? 26  GLY A CA    1 
ATOM   182  C C     . GLY A 1 26  ? 33.443 -45.455 -11.655 1.00 51.31  ? 26  GLY A C     1 
ATOM   183  O O     . GLY A 1 26  ? 32.669 -44.553 -11.960 1.00 50.55  ? 26  GLY A O     1 
ATOM   184  N N     . ALA A 1 27  ? 33.195 -46.322 -10.669 1.00 53.85  ? 27  ALA A N     1 
ATOM   185  C CA    . ALA A 1 27  ? 31.885 -46.473 -10.052 1.00 47.95  ? 27  ALA A CA    1 
ATOM   186  C C     . ALA A 1 27  ? 31.479 -45.189 -9.342  1.00 44.79  ? 27  ALA A C     1 
ATOM   187  O O     . ALA A 1 27  ? 30.289 -44.928 -9.156  1.00 45.23  ? 27  ALA A O     1 
ATOM   188  C CB    . ALA A 1 27  ? 31.913 -47.638 -9.079  1.00 48.93  ? 27  ALA A CB    1 
ATOM   189  N N     . ASP A 1 28  ? 32.473 -44.408 -8.910  1.00 45.40  ? 28  ASP A N     1 
ATOM   190  C CA    . ASP A 1 28  ? 32.201 -43.244 -8.087  1.00 49.14  ? 28  ASP A CA    1 
ATOM   191  C C     . ASP A 1 28  ? 31.626 -42.102 -8.923  1.00 48.20  ? 28  ASP A C     1 
ATOM   192  O O     . ASP A 1 28  ? 31.182 -41.107 -8.354  1.00 49.25  ? 28  ASP A O     1 
ATOM   193  C CB    . ASP A 1 28  ? 33.462 -42.798 -7.339  1.00 62.36  ? 28  ASP A CB    1 
ATOM   194  C CG    . ASP A 1 28  ? 33.652 -43.443 -5.974  1.00 65.84  ? 28  ASP A CG    1 
ATOM   195  O OD1   . ASP A 1 28  ? 32.710 -44.107 -5.497  1.00 71.10  ? 28  ASP A OD1   1 
ATOM   196  O OD2   . ASP A 1 28  ? 34.735 -43.263 -5.393  1.00 61.58  ? 28  ASP A OD2   1 
ATOM   197  N N     . TRP A 1 29  ? 31.645 -42.245 -10.259 1.00 44.09  ? 29  TRP A N     1 
ATOM   198  C CA    . TRP A 1 29  ? 31.279 -41.164 -11.163 1.00 45.63  ? 29  TRP A CA    1 
ATOM   199  C C     . TRP A 1 29  ? 30.098 -41.573 -12.047 1.00 46.94  ? 29  TRP A C     1 
ATOM   200  O O     . TRP A 1 29  ? 29.866 -40.989 -13.103 1.00 45.25  ? 29  TRP A O     1 
ATOM   201  C CB    . TRP A 1 29  ? 32.514 -40.727 -11.964 1.00 41.95  ? 29  TRP A CB    1 
ATOM   202  C CG    . TRP A 1 29  ? 33.686 -40.384 -11.087 1.00 42.29  ? 29  TRP A CG    1 
ATOM   203  C CD1   . TRP A 1 29  ? 34.859 -41.082 -10.956 1.00 40.11  ? 29  TRP A CD1   1 
ATOM   204  C CD2   . TRP A 1 29  ? 33.794 -39.252 -10.199 1.00 37.63  ? 29  TRP A CD2   1 
ATOM   205  N NE1   . TRP A 1 29  ? 35.681 -40.466 -10.048 1.00 39.53  ? 29  TRP A NE1   1 
ATOM   206  C CE2   . TRP A 1 29  ? 35.058 -39.337 -9.573  1.00 40.51  ? 29  TRP A CE2   1 
ATOM   207  C CE3   . TRP A 1 29  ? 32.951 -38.184 -9.873  1.00 38.90  ? 29  TRP A CE3   1 
ATOM   208  C CZ2   . TRP A 1 29  ? 35.494 -38.389 -8.646  1.00 43.62  ? 29  TRP A CZ2   1 
ATOM   209  C CZ3   . TRP A 1 29  ? 33.380 -37.252 -8.949  1.00 41.99  ? 29  TRP A CZ3   1 
ATOM   210  C CH2   . TRP A 1 29  ? 34.632 -37.358 -8.338  1.00 43.45  ? 29  TRP A CH2   1 
ATOM   211  N N     . VAL A 1 30  ? 29.345 -42.585 -11.597 1.00 46.38  ? 30  VAL A N     1 
ATOM   212  C CA    . VAL A 1 30  ? 28.018 -42.846 -12.120 1.00 40.43  ? 30  VAL A CA    1 
ATOM   213  C C     . VAL A 1 30  ? 27.045 -42.618 -10.982 1.00 41.41  ? 30  VAL A C     1 
ATOM   214  O O     . VAL A 1 30  ? 27.222 -43.198 -9.919  1.00 43.71  ? 30  VAL A O     1 
ATOM   215  C CB    . VAL A 1 30  ? 27.881 -44.259 -12.704 1.00 38.85  ? 30  VAL A CB    1 
ATOM   216  C CG1   . VAL A 1 30  ? 26.479 -44.517 -13.258 1.00 36.90  ? 30  VAL A CG1   1 
ATOM   217  C CG2   . VAL A 1 30  ? 28.933 -44.511 -13.768 1.00 39.05  ? 30  VAL A CG2   1 
ATOM   218  N N     . PHE A 1 31  ? 26.058 -41.748 -11.234 1.00 43.41  ? 31  PHE A N     1 
ATOM   219  C CA    . PHE A 1 31  ? 25.170 -41.227 -10.220 1.00 43.38  ? 31  PHE A CA    1 
ATOM   220  C C     . PHE A 1 31  ? 23.739 -41.599 -10.564 1.00 45.22  ? 31  PHE A C     1 
ATOM   221  O O     . PHE A 1 31  ? 23.217 -41.176 -11.591 1.00 47.01  ? 31  PHE A O     1 
ATOM   222  C CB    . PHE A 1 31  ? 25.282 -39.706 -10.134 1.00 47.69  ? 31  PHE A CB    1 
ATOM   223  C CG    . PHE A 1 31  ? 26.644 -39.185 -9.761  1.00 49.30  ? 31  PHE A CG    1 
ATOM   224  C CD1   . PHE A 1 31  ? 27.137 -39.330 -8.475  1.00 52.06  ? 31  PHE A CD1   1 
ATOM   225  C CD2   . PHE A 1 31  ? 27.433 -38.529 -10.692 1.00 53.03  ? 31  PHE A CD2   1 
ATOM   226  C CE1   . PHE A 1 31  ? 28.391 -38.836 -8.136  1.00 55.32  ? 31  PHE A CE1   1 
ATOM   227  C CE2   . PHE A 1 31  ? 28.687 -38.034 -10.350 1.00 56.05  ? 31  PHE A CE2   1 
ATOM   228  C CZ    . PHE A 1 31  ? 29.174 -38.202 -9.077  1.00 53.81  ? 31  PHE A CZ    1 
ATOM   229  N N     . THR A 1 32  ? 23.121 -42.369 -9.665  1.00 50.39  ? 32  THR A N     1 
ATOM   230  C CA    . THR A 1 32  ? 21.713 -42.714 -9.748  1.00 52.53  ? 32  THR A CA    1 
ATOM   231  C C     . THR A 1 32  ? 21.044 -42.345 -8.424  1.00 57.76  ? 32  THR A C     1 
ATOM   232  O O     . THR A 1 32  ? 21.707 -41.834 -7.517  1.00 50.54  ? 32  THR A O     1 
ATOM   233  C CB    . THR A 1 32  ? 21.539 -44.201 -10.079 1.00 51.64  ? 32  THR A CB    1 
ATOM   234  O OG1   . THR A 1 32  ? 22.103 -44.948 -9.004  1.00 49.94  ? 32  THR A OG1   1 
ATOM   235  C CG2   . THR A 1 32  ? 22.216 -44.617 -11.365 1.00 48.49  ? 32  THR A CG2   1 
ATOM   236  N N     . GLU A 1 33  ? 19.720 -42.565 -8.362  1.00 64.85  ? 33  GLU A N     1 
ATOM   237  C CA    . GLU A 1 33  ? 18.928 -42.452 -7.143  1.00 69.53  ? 33  GLU A CA    1 
ATOM   238  C C     . GLU A 1 33  ? 19.178 -41.099 -6.472  1.00 68.95  ? 33  GLU A C     1 
ATOM   239  O O     . GLU A 1 33  ? 18.938 -40.067 -7.091  1.00 67.98  ? 33  GLU A O     1 
ATOM   240  C CB    . GLU A 1 33  ? 19.191 -43.691 -6.287  1.00 71.91  ? 33  GLU A CB    1 
ATOM   241  C CG    . GLU A 1 33  ? 18.739 -44.970 -6.982  1.00 76.91  ? 33  GLU A CG    1 
ATOM   242  C CD    . GLU A 1 33  ? 19.549 -46.220 -6.673  1.00 78.55  ? 33  GLU A CD    1 
ATOM   243  O OE1   . GLU A 1 33  ? 20.458 -46.136 -5.826  1.00 83.36  ? 33  GLU A OE1   1 
ATOM   244  O OE2   . GLU A 1 33  ? 19.281 -47.273 -7.297  1.00 72.25  ? 33  GLU A OE2   1 
ATOM   245  N N     . ASP A 1 34  ? 19.671 -41.097 -5.224  1.00 73.45  ? 34  ASP A N     1 
ATOM   246  C CA    . ASP A 1 34  ? 19.737 -39.887 -4.411  1.00 79.94  ? 34  ASP A CA    1 
ATOM   247  C C     . ASP A 1 34  ? 20.713 -38.859 -4.994  1.00 73.02  ? 34  ASP A C     1 
ATOM   248  O O     . ASP A 1 34  ? 20.590 -37.663 -4.731  1.00 64.34  ? 34  ASP A O     1 
ATOM   249  C CB    . ASP A 1 34  ? 20.128 -40.206 -2.960  1.00 87.65  ? 34  ASP A CB    1 
ATOM   250  C CG    . ASP A 1 34  ? 19.047 -40.924 -2.167  1.00 92.91  ? 34  ASP A CG    1 
ATOM   251  O OD1   . ASP A 1 34  ? 17.911 -40.413 -2.141  1.00 96.94  ? 34  ASP A OD1   1 
ATOM   252  O OD2   . ASP A 1 34  ? 19.353 -41.977 -1.567  1.00 85.50  ? 34  ASP A OD2   1 
ATOM   253  N N     . LYS A 1 35  ? 21.696 -39.314 -5.777  1.00 67.36  ? 35  LYS A N     1 
ATOM   254  C CA    . LYS A 1 35  ? 22.748 -38.422 -6.230  1.00 65.27  ? 35  LYS A CA    1 
ATOM   255  C C     . LYS A 1 35  ? 22.378 -37.792 -7.572  1.00 60.55  ? 35  LYS A C     1 
ATOM   256  O O     . LYS A 1 35  ? 23.174 -37.017 -8.097  1.00 59.34  ? 35  LYS A O     1 
ATOM   257  C CB    . LYS A 1 35  ? 24.080 -39.178 -6.269  1.00 72.33  ? 35  LYS A CB    1 
ATOM   258  C CG    . LYS A 1 35  ? 24.615 -39.588 -4.901  1.00 77.53  ? 35  LYS A CG    1 
ATOM   259  C CD    . LYS A 1 35  ? 25.969 -40.273 -4.916  1.00 80.24  ? 35  LYS A CD    1 
ATOM   260  C CE    . LYS A 1 35  ? 26.520 -40.471 -3.519  1.00 87.41  ? 35  LYS A CE    1 
ATOM   261  N NZ    . LYS A 1 35  ? 27.932 -40.918 -3.537  1.00 90.55  ? 35  LYS A NZ    1 
ATOM   262  N N     . ILE A 1 36  ? 21.171 -38.093 -8.094  1.00 57.82  ? 36  ILE A N     1 
ATOM   263  C CA    . ILE A 1 36  ? 20.648 -37.480 -9.314  1.00 54.62  ? 36  ILE A CA    1 
ATOM   264  C C     . ILE A 1 36  ? 20.105 -36.067 -9.048  1.00 52.59  ? 36  ILE A C     1 
ATOM   265  O O     . ILE A 1 36  ? 20.039 -35.278 -9.990  1.00 47.86  ? 36  ILE A O     1 
ATOM   266  C CB    . ILE A 1 36  ? 19.567 -38.366 -9.990  1.00 57.95  ? 36  ILE A CB    1 
ATOM   267  C CG1   . ILE A 1 36  ? 19.485 -38.153 -11.505 1.00 59.41  ? 36  ILE A CG1   1 
ATOM   268  C CG2   . ILE A 1 36  ? 18.192 -38.160 -9.366  1.00 58.53  ? 36  ILE A CG2   1 
ATOM   269  C CD1   . ILE A 1 36  ? 20.815 -38.242 -12.217 1.00 64.03  ? 36  ILE A CD1   1 
ATOM   270  N N     . THR A 1 37  ? 19.715 -35.731 -7.797  1.00 52.73  ? 37  THR A N     1 
ATOM   271  C CA    . THR A 1 37  ? 18.891 -34.546 -7.551  1.00 56.67  ? 37  THR A CA    1 
ATOM   272  C C     . THR A 1 37  ? 19.572 -33.277 -8.076  1.00 49.25  ? 37  THR A C     1 
ATOM   273  O O     . THR A 1 37  ? 18.897 -32.433 -8.658  1.00 46.45  ? 37  THR A O     1 
ATOM   274  C CB    . THR A 1 37  ? 18.421 -34.386 -6.091  1.00 58.33  ? 37  THR A CB    1 
ATOM   275  O OG1   . THR A 1 37  ? 19.431 -34.796 -5.173  1.00 69.58  ? 37  THR A OG1   1 
ATOM   276  C CG2   . THR A 1 37  ? 17.172 -35.184 -5.785  1.00 60.65  ? 37  THR A CG2   1 
ATOM   277  N N     . PRO A 1 38  ? 20.907 -33.103 -7.955  1.00 42.69  ? 38  PRO A N     1 
ATOM   278  C CA    . PRO A 1 38  ? 21.570 -31.913 -8.500  1.00 42.89  ? 38  PRO A CA    1 
ATOM   279  C C     . PRO A 1 38  ? 21.364 -31.702 -10.004 1.00 44.24  ? 38  PRO A C     1 
ATOM   280  O O     . PRO A 1 38  ? 21.521 -30.589 -10.488 1.00 41.82  ? 38  PRO A O     1 
ATOM   281  C CB    . PRO A 1 38  ? 23.058 -32.165 -8.200  1.00 42.06  ? 38  PRO A CB    1 
ATOM   282  C CG    . PRO A 1 38  ? 23.033 -33.107 -7.017  1.00 42.11  ? 38  PRO A CG    1 
ATOM   283  C CD    . PRO A 1 38  ? 21.849 -34.014 -7.289  1.00 41.60  ? 38  PRO A CD    1 
ATOM   284  N N     . TYR A 1 39  ? 20.957 -32.766 -10.719 1.00 45.94  ? 39  TYR A N     1 
ATOM   285  C CA    . TYR A 1 39  ? 20.783 -32.753 -12.167 1.00 44.20  ? 39  TYR A CA    1 
ATOM   286  C C     . TYR A 1 39  ? 19.327 -32.440 -12.557 1.00 44.13  ? 39  TYR A C     1 
ATOM   287  O O     . TYR A 1 39  ? 19.019 -32.328 -13.754 1.00 40.78  ? 39  TYR A O     1 
ATOM   288  C CB    . TYR A 1 39  ? 21.316 -34.068 -12.760 1.00 40.55  ? 39  TYR A CB    1 
ATOM   289  C CG    . TYR A 1 39  ? 22.799 -34.293 -12.560 1.00 41.30  ? 39  TYR A CG    1 
ATOM   290  C CD1   . TYR A 1 39  ? 23.730 -33.607 -13.327 1.00 41.53  ? 39  TYR A CD1   1 
ATOM   291  C CD2   . TYR A 1 39  ? 23.286 -35.133 -11.556 1.00 43.60  ? 39  TYR A CD2   1 
ATOM   292  C CE1   . TYR A 1 39  ? 25.094 -33.769 -13.132 1.00 41.71  ? 39  TYR A CE1   1 
ATOM   293  C CE2   . TYR A 1 39  ? 24.650 -35.307 -11.342 1.00 41.46  ? 39  TYR A CE2   1 
ATOM   294  C CZ    . TYR A 1 39  ? 25.555 -34.626 -12.143 1.00 43.23  ? 39  TYR A CZ    1 
ATOM   295  O OH    . TYR A 1 39  ? 26.901 -34.780 -11.991 1.00 41.05  ? 39  TYR A OH    1 
ATOM   296  N N     . GLU A 1 40  ? 18.444 -32.241 -11.560 1.00 39.03  ? 40  GLU A N     1 
ATOM   297  C CA    . GLU A 1 40  ? 17.070 -31.820 -11.815 1.00 39.63  ? 40  GLU A CA    1 
ATOM   298  C C     . GLU A 1 40  ? 17.054 -30.331 -12.169 1.00 38.35  ? 40  GLU A C     1 
ATOM   299  O O     . GLU A 1 40  ? 17.984 -29.600 -11.816 1.00 33.90  ? 40  GLU A O     1 
ATOM   300  C CB    . GLU A 1 40  ? 16.183 -32.065 -10.590 1.00 42.38  ? 40  GLU A CB    1 
ATOM   301  C CG    . GLU A 1 40  ? 16.246 -33.484 -10.039 1.00 44.32  ? 40  GLU A CG    1 
ATOM   302  C CD    . GLU A 1 40  ? 15.441 -34.549 -10.765 1.00 46.62  ? 40  GLU A CD    1 
ATOM   303  O OE1   . GLU A 1 40  ? 14.798 -34.246 -11.796 1.00 43.86  ? 40  GLU A OE1   1 
ATOM   304  O OE2   . GLU A 1 40  ? 15.461 -35.698 -10.285 1.00 56.53  ? 40  GLU A OE2   1 
ATOM   305  N N     . ASP A 1 41  ? 16.009 -29.875 -12.881 1.00 36.38  ? 41  ASP A N     1 
ATOM   306  C CA    . ASP A 1 41  ? 15.833 -28.439 -13.054 1.00 37.23  ? 41  ASP A CA    1 
ATOM   307  C C     . ASP A 1 41  ? 15.693 -27.844 -11.652 1.00 39.27  ? 41  ASP A C     1 
ATOM   308  O O     . ASP A 1 41  ? 14.832 -28.257 -10.877 1.00 40.76  ? 41  ASP A O     1 
ATOM   309  C CB    . ASP A 1 41  ? 14.652 -28.096 -13.968 1.00 37.69  ? 41  ASP A CB    1 
ATOM   310  C CG    . ASP A 1 41  ? 14.536 -26.618 -14.339 1.00 38.21  ? 41  ASP A CG    1 
ATOM   311  O OD1   . ASP A 1 41  ? 15.328 -25.806 -13.825 1.00 37.85  ? 41  ASP A OD1   1 
ATOM   312  O OD2   . ASP A 1 41  ? 13.647 -26.281 -15.157 1.00 35.89  ? 41  ASP A OD2   1 
ATOM   313  N N     . PRO A 1 42  ? 16.574 -26.909 -11.242 1.00 40.04  ? 42  PRO A N     1 
ATOM   314  C CA    . PRO A 1 42  ? 16.434 -26.268 -9.933  1.00 39.38  ? 42  PRO A CA    1 
ATOM   315  C C     . PRO A 1 42  ? 15.227 -25.324 -9.856  1.00 41.48  ? 42  PRO A C     1 
ATOM   316  O O     . PRO A 1 42  ? 14.740 -25.051 -8.759  1.00 36.47  ? 42  PRO A O     1 
ATOM   317  C CB    . PRO A 1 42  ? 17.757 -25.509 -9.735  1.00 40.41  ? 42  PRO A CB    1 
ATOM   318  C CG    . PRO A 1 42  ? 18.313 -25.314 -11.139 1.00 43.16  ? 42  PRO A CG    1 
ATOM   319  C CD    . PRO A 1 42  ? 17.737 -26.424 -12.005 1.00 41.34  ? 42  PRO A CD    1 
ATOM   320  N N     . TYR A 1 43  ? 14.758 -24.846 -11.026 1.00 40.35  ? 43  TYR A N     1 
ATOM   321  C CA    . TYR A 1 43  ? 13.619 -23.945 -11.136 1.00 37.37  ? 43  TYR A CA    1 
ATOM   322  C C     . TYR A 1 43  ? 12.485 -24.623 -11.915 1.00 36.93  ? 43  TYR A C     1 
ATOM   323  O O     . TYR A 1 43  ? 12.172 -24.202 -13.028 1.00 40.87  ? 43  TYR A O     1 
ATOM   324  C CB    . TYR A 1 43  ? 14.020 -22.637 -11.834 1.00 34.37  ? 43  TYR A CB    1 
ATOM   325  C CG    . TYR A 1 43  ? 15.208 -21.888 -11.283 1.00 34.99  ? 43  TYR A CG    1 
ATOM   326  C CD1   . TYR A 1 43  ? 15.635 -22.021 -9.963  1.00 35.36  ? 43  TYR A CD1   1 
ATOM   327  C CD2   . TYR A 1 43  ? 15.933 -21.038 -12.104 1.00 37.87  ? 43  TYR A CD2   1 
ATOM   328  C CE1   . TYR A 1 43  ? 16.744 -21.336 -9.478  1.00 30.02  ? 43  TYR A CE1   1 
ATOM   329  C CE2   . TYR A 1 43  ? 17.035 -20.333 -11.634 1.00 37.77  ? 43  TYR A CE2   1 
ATOM   330  C CZ    . TYR A 1 43  ? 17.436 -20.482 -10.318 1.00 33.79  ? 43  TYR A CZ    1 
ATOM   331  O OH    . TYR A 1 43  ? 18.531 -19.795 -9.884  1.00 36.10  ? 43  TYR A OH    1 
ATOM   332  N N     . THR A 1 44  ? 11.877 -25.666 -11.319 1.00 38.41  ? 44  THR A N     1 
ATOM   333  C CA    . THR A 1 44  ? 10.779 -26.441 -11.901 1.00 38.69  ? 44  THR A CA    1 
ATOM   334  C C     . THR A 1 44  ? 9.720  -25.542 -12.543 1.00 38.58  ? 44  THR A C     1 
ATOM   335  O O     . THR A 1 44  ? 9.421  -24.476 -12.019 1.00 42.94  ? 44  THR A O     1 
ATOM   336  C CB    . THR A 1 44  ? 10.066 -27.274 -10.827 1.00 40.05  ? 44  THR A CB    1 
ATOM   337  O OG1   . THR A 1 44  ? 11.068 -27.863 -10.000 1.00 44.16  ? 44  THR A OG1   1 
ATOM   338  C CG2   . THR A 1 44  ? 9.168  -28.357 -11.395 1.00 41.35  ? 44  THR A CG2   1 
ATOM   339  N N     . ILE A 1 45  ? 9.146  -25.987 -13.664 1.00 36.36  ? 45  ILE A N     1 
ATOM   340  C CA    . ILE A 1 45  ? 8.031  -25.301 -14.309 1.00 41.03  ? 45  ILE A CA    1 
ATOM   341  C C     . ILE A 1 45  ? 6.872  -26.275 -14.533 1.00 45.92  ? 45  ILE A C     1 
ATOM   342  O O     . ILE A 1 45  ? 5.722  -25.948 -14.238 1.00 57.02  ? 45  ILE A O     1 
ATOM   343  C CB    . ILE A 1 45  ? 8.454  -24.648 -15.639 1.00 39.47  ? 45  ILE A CB    1 
ATOM   344  C CG1   . ILE A 1 45  ? 9.531  -23.580 -15.433 1.00 37.87  ? 45  ILE A CG1   1 
ATOM   345  C CG2   . ILE A 1 45  ? 7.232  -24.094 -16.369 1.00 39.67  ? 45  ILE A CG2   1 
ATOM   346  C CD1   . ILE A 1 45  ? 10.142 -23.067 -16.724 1.00 37.54  ? 45  ILE A CD1   1 
ATOM   347  N N     . SER A 1 46  ? 7.168  -27.444 -15.110 1.00 46.15  ? 46  SER A N     1 
ATOM   348  C CA    . SER A 1 46  ? 6.181  -28.500 -15.267 1.00 45.82  ? 46  SER A CA    1 
ATOM   349  C C     . SER A 1 46  ? 5.641  -28.920 -13.903 1.00 46.31  ? 46  SER A C     1 
ATOM   350  O O     . SER A 1 46  ? 6.398  -29.043 -12.944 1.00 51.52  ? 46  SER A O     1 
ATOM   351  C CB    . SER A 1 46  ? 6.778  -29.682 -15.969 1.00 47.07  ? 46  SER A CB    1 
ATOM   352  O OG    . SER A 1 46  ? 5.818  -30.704 -16.158 1.00 45.92  ? 46  SER A OG    1 
ATOM   353  N N     . ASN A 1 47  ? 4.323  -29.118 -13.850 1.00 45.41  ? 47  ASN A N     1 
ATOM   354  C CA    . ASN A 1 47  ? 3.636  -29.695 -12.709 1.00 48.21  ? 47  ASN A CA    1 
ATOM   355  C C     . ASN A 1 47  ? 3.483  -31.200 -12.886 1.00 47.34  ? 47  ASN A C     1 
ATOM   356  O O     . ASN A 1 47  ? 2.988  -31.867 -11.989 1.00 45.54  ? 47  ASN A O     1 
ATOM   357  C CB    . ASN A 1 47  ? 2.236  -29.101 -12.523 1.00 49.01  ? 47  ASN A CB    1 
ATOM   358  C CG    . ASN A 1 47  ? 2.274  -27.791 -11.775 1.00 47.09  ? 47  ASN A CG    1 
ATOM   359  O OD1   . ASN A 1 47  ? 3.089  -27.626 -10.871 1.00 49.25  ? 47  ASN A OD1   1 
ATOM   360  N ND2   . ASN A 1 47  ? 1.432  -26.851 -12.170 1.00 49.19  ? 47  ASN A ND2   1 
ATOM   361  N N     . ASP A 1 48  ? 3.850  -31.698 -14.069 1.00 48.91  ? 48  ASP A N     1 
ATOM   362  C CA    . ASP A 1 48  ? 3.948  -33.121 -14.331 1.00 50.56  ? 48  ASP A CA    1 
ATOM   363  C C     . ASP A 1 48  ? 5.364  -33.583 -13.968 1.00 51.03  ? 48  ASP A C     1 
ATOM   364  O O     . ASP A 1 48  ? 6.322  -33.247 -14.665 1.00 49.40  ? 48  ASP A O     1 
ATOM   365  C CB    . ASP A 1 48  ? 3.555  -33.389 -15.788 1.00 51.78  ? 48  ASP A CB    1 
ATOM   366  C CG    . ASP A 1 48  ? 3.644  -34.840 -16.235 1.00 52.64  ? 48  ASP A CG    1 
ATOM   367  O OD1   . ASP A 1 48  ? 4.188  -35.660 -15.474 1.00 51.88  ? 48  ASP A OD1   1 
ATOM   368  O OD2   . ASP A 1 48  ? 3.179  -35.136 -17.351 1.00 54.44  ? 48  ASP A OD2   1 
ATOM   369  N N     . GLU A 1 49  ? 5.473  -34.392 -12.900 1.00 55.18  ? 49  GLU A N     1 
ATOM   370  C CA    . GLU A 1 49  ? 6.738  -34.912 -12.385 1.00 54.53  ? 49  GLU A CA    1 
ATOM   371  C C     . GLU A 1 49  ? 7.357  -35.966 -13.303 1.00 52.77  ? 49  GLU A C     1 
ATOM   372  O O     . GLU A 1 49  ? 8.469  -36.416 -13.050 1.00 53.93  ? 49  GLU A O     1 
ATOM   373  C CB    . GLU A 1 49  ? 6.559  -35.542 -11.001 1.00 56.16  ? 49  GLU A CB    1 
ATOM   374  C CG    . GLU A 1 49  ? 6.844  -34.585 -9.858  1.00 65.30  ? 49  GLU A CG    1 
ATOM   375  C CD    . GLU A 1 49  ? 7.043  -35.269 -8.518  1.00 68.98  ? 49  GLU A CD    1 
ATOM   376  O OE1   . GLU A 1 49  ? 6.022  -35.670 -7.916  1.00 65.29  ? 49  GLU A OE1   1 
ATOM   377  O OE2   . GLU A 1 49  ? 8.222  -35.433 -8.104  1.00 64.39  ? 49  GLU A OE2   1 
ATOM   378  N N     . THR A 1 50  ? 6.667  -36.347 -14.379 1.00 53.33  ? 50  THR A N     1 
ATOM   379  C CA    . THR A 1 50  ? 7.200  -37.325 -15.318 1.00 53.74  ? 50  THR A CA    1 
ATOM   380  C C     . THR A 1 50  ? 8.179  -36.679 -16.321 1.00 52.45  ? 50  THR A C     1 
ATOM   381  O O     . THR A 1 50  ? 8.803  -37.403 -17.092 1.00 53.95  ? 50  THR A O     1 
ATOM   382  C CB    . THR A 1 50  ? 6.020  -38.081 -15.959 1.00 54.38  ? 50  THR A CB    1 
ATOM   383  O OG1   . THR A 1 50  ? 6.410  -39.446 -16.062 1.00 72.07  ? 50  THR A OG1   1 
ATOM   384  C CG2   . THR A 1 50  ? 5.577  -37.582 -17.320 1.00 51.21  ? 50  THR A CG2   1 
ATOM   385  N N     . GLU A 1 51  ? 8.344  -35.338 -16.322 1.00 46.96  ? 51  GLU A N     1 
ATOM   386  C CA    . GLU A 1 51  ? 8.999  -34.629 -17.423 1.00 48.35  ? 51  GLU A CA    1 
ATOM   387  C C     . GLU A 1 51  ? 10.370 -34.059 -17.028 1.00 43.41  ? 51  GLU A C     1 
ATOM   388  O O     . GLU A 1 51  ? 10.581 -33.620 -15.898 1.00 38.72  ? 51  GLU A O     1 
ATOM   389  C CB    . GLU A 1 51  ? 8.136  -33.468 -17.934 1.00 53.01  ? 51  GLU A CB    1 
ATOM   390  C CG    . GLU A 1 51  ? 6.867  -33.870 -18.680 1.00 55.73  ? 51  GLU A CG    1 
ATOM   391  C CD    . GLU A 1 51  ? 6.067  -32.678 -19.189 1.00 54.97  ? 51  GLU A CD    1 
ATOM   392  O OE1   . GLU A 1 51  ? 5.619  -31.875 -18.365 1.00 53.81  ? 51  GLU A OE1   1 
ATOM   393  O OE2   . GLU A 1 51  ? 5.926  -32.530 -20.408 1.00 58.75  ? 51  GLU A OE2   1 
ATOM   394  N N     . HIS A 1 52  ? 11.286 -34.017 -18.012 1.00 43.51  ? 52  HIS A N     1 
ATOM   395  C CA    . HIS A 1 52  ? 12.634 -33.487 -17.850 1.00 41.69  ? 52  HIS A CA    1 
ATOM   396  C C     . HIS A 1 52  ? 13.387 -34.199 -16.725 1.00 41.29  ? 52  HIS A C     1 
ATOM   397  O O     . HIS A 1 52  ? 14.162 -33.571 -16.001 1.00 38.15  ? 52  HIS A O     1 
ATOM   398  C CB    . HIS A 1 52  ? 12.587 -31.984 -17.565 1.00 42.43  ? 52  HIS A CB    1 
ATOM   399  C CG    . HIS A 1 52  ? 11.649 -31.268 -18.454 1.00 46.72  ? 52  HIS A CG    1 
ATOM   400  N ND1   . HIS A 1 52  ? 11.749 -31.331 -19.824 1.00 52.36  ? 52  HIS A ND1   1 
ATOM   401  C CD2   . HIS A 1 52  ? 10.594 -30.496 -18.182 1.00 51.78  ? 52  HIS A CD2   1 
ATOM   402  C CE1   . HIS A 1 52  ? 10.775 -30.607 -20.357 1.00 56.93  ? 52  HIS A CE1   1 
ATOM   403  N NE2   . HIS A 1 52  ? 10.063 -30.087 -19.377 1.00 56.81  ? 52  HIS A NE2   1 
ATOM   404  N N     . ARG A 1 53  ? 13.139 -35.508 -16.568 1.00 43.01  ? 53  ARG A N     1 
ATOM   405  C CA    . ARG A 1 53  ? 13.679 -36.259 -15.443 1.00 41.04  ? 53  ARG A CA    1 
ATOM   406  C C     . ARG A 1 53  ? 14.865 -37.076 -15.935 1.00 36.23  ? 53  ARG A C     1 
ATOM   407  O O     . ARG A 1 53  ? 14.681 -38.031 -16.687 1.00 39.54  ? 53  ARG A O     1 
ATOM   408  C CB    . ARG A 1 53  ? 12.601 -37.151 -14.824 1.00 42.63  ? 53  ARG A CB    1 
ATOM   409  C CG    . ARG A 1 53  ? 11.305 -36.435 -14.470 1.00 48.03  ? 53  ARG A CG    1 
ATOM   410  C CD    . ARG A 1 53  ? 11.487 -35.296 -13.479 1.00 52.44  ? 53  ARG A CD    1 
ATOM   411  N NE    . ARG A 1 53  ? 12.229 -35.742 -12.310 1.00 57.33  ? 53  ARG A NE    1 
ATOM   412  C CZ    . ARG A 1 53  ? 11.752 -36.573 -11.389 1.00 55.50  ? 53  ARG A CZ    1 
ATOM   413  N NH1   . ARG A 1 53  ? 10.461 -36.844 -11.345 1.00 57.70  ? 53  ARG A NH1   1 
ATOM   414  N NH2   . ARG A 1 53  ? 12.564 -37.091 -10.485 1.00 51.17  ? 53  ARG A NH2   1 
ATOM   415  N N     . PRO A 1 54  ? 16.112 -36.702 -15.576 1.00 31.64  ? 54  PRO A N     1 
ATOM   416  C CA    . PRO A 1 54  ? 17.294 -37.452 -15.992 1.00 34.18  ? 54  PRO A CA    1 
ATOM   417  C C     . PRO A 1 54  ? 17.336 -38.779 -15.246 1.00 38.74  ? 54  PRO A C     1 
ATOM   418  O O     . PRO A 1 54  ? 17.019 -38.806 -14.060 1.00 38.76  ? 54  PRO A O     1 
ATOM   419  C CB    . PRO A 1 54  ? 18.476 -36.578 -15.579 1.00 31.30  ? 54  PRO A CB    1 
ATOM   420  C CG    . PRO A 1 54  ? 17.948 -35.732 -14.459 1.00 32.19  ? 54  PRO A CG    1 
ATOM   421  C CD    . PRO A 1 54  ? 16.462 -35.561 -14.725 1.00 33.47  ? 54  PRO A CD    1 
ATOM   422  N N     . TYR A 1 55  ? 17.693 -39.856 -15.957 1.00 40.06  ? 55  TYR A N     1 
ATOM   423  C CA    . TYR A 1 55  ? 17.703 -41.186 -15.374 1.00 45.11  ? 55  TYR A CA    1 
ATOM   424  C C     . TYR A 1 55  ? 18.982 -41.417 -14.564 1.00 42.15  ? 55  TYR A C     1 
ATOM   425  O O     . TYR A 1 55  ? 18.958 -42.193 -13.620 1.00 47.60  ? 55  TYR A O     1 
ATOM   426  C CB    . TYR A 1 55  ? 17.480 -42.251 -16.452 1.00 45.39  ? 55  TYR A CB    1 
ATOM   427  C CG    . TYR A 1 55  ? 17.157 -43.616 -15.897 1.00 50.06  ? 55  TYR A CG    1 
ATOM   428  C CD1   . TYR A 1 55  ? 18.153 -44.439 -15.398 1.00 55.46  ? 55  TYR A CD1   1 
ATOM   429  C CD2   . TYR A 1 55  ? 15.847 -44.067 -15.816 1.00 53.53  ? 55  TYR A CD2   1 
ATOM   430  C CE1   . TYR A 1 55  ? 17.857 -45.683 -14.862 1.00 59.22  ? 55  TYR A CE1   1 
ATOM   431  C CE2   . TYR A 1 55  ? 15.532 -45.301 -15.273 1.00 53.39  ? 55  TYR A CE2   1 
ATOM   432  C CZ    . TYR A 1 55  ? 16.544 -46.115 -14.794 1.00 55.76  ? 55  TYR A CZ    1 
ATOM   433  O OH    . TYR A 1 55  ? 16.266 -47.347 -14.256 1.00 51.27  ? 55  TYR A OH    1 
ATOM   434  N N     . ALA A 1 56  ? 20.078 -40.734 -14.916 1.00 41.83  ? 56  ALA A N     1 
ATOM   435  C CA    . ALA A 1 56  ? 21.390 -40.960 -14.318 1.00 40.94  ? 56  ALA A CA    1 
ATOM   436  C C     . ALA A 1 56  ? 22.367 -39.903 -14.840 1.00 41.96  ? 56  ALA A C     1 
ATOM   437  O O     . ALA A 1 56  ? 22.071 -39.227 -15.823 1.00 40.03  ? 56  ALA A O     1 
ATOM   438  C CB    . ALA A 1 56  ? 21.895 -42.353 -14.655 1.00 36.55  ? 56  ALA A CB    1 
ATOM   439  N N     . ALA A 1 57  ? 23.536 -39.795 -14.199 1.00 36.97  ? 57  ALA A N     1 
ATOM   440  C CA    . ALA A 1 57  ? 24.603 -38.945 -14.692 1.00 38.46  ? 57  ALA A CA    1 
ATOM   441  C C     . ALA A 1 57  ? 25.921 -39.716 -14.734 1.00 40.85  ? 57  ALA A C     1 
ATOM   442  O O     . ALA A 1 57  ? 26.161 -40.593 -13.912 1.00 39.95  ? 57  ALA A O     1 
ATOM   443  C CB    . ALA A 1 57  ? 24.725 -37.730 -13.815 1.00 40.41  ? 57  ALA A CB    1 
ATOM   444  N N     . VAL A 1 58  ? 26.782 -39.383 -15.701 1.00 41.20  ? 58  VAL A N     1 
ATOM   445  C CA    . VAL A 1 58  ? 28.122 -39.949 -15.752 1.00 38.09  ? 58  VAL A CA    1 
ATOM   446  C C     . VAL A 1 58  ? 29.099 -38.790 -15.912 1.00 36.86  ? 58  VAL A C     1 
ATOM   447  O O     . VAL A 1 58  ? 28.822 -37.826 -16.619 1.00 37.12  ? 58  VAL A O     1 
ATOM   448  C CB    . VAL A 1 58  ? 28.242 -41.027 -16.845 1.00 38.94  ? 58  VAL A CB    1 
ATOM   449  C CG1   . VAL A 1 58  ? 27.501 -40.650 -18.105 1.00 44.49  ? 58  VAL A CG1   1 
ATOM   450  C CG2   . VAL A 1 58  ? 29.682 -41.360 -17.183 1.00 41.21  ? 58  VAL A CG2   1 
ATOM   451  N N     . ALA A 1 59  ? 30.217 -38.862 -15.190 1.00 36.43  ? 59  ALA A N     1 
ATOM   452  C CA    . ALA A 1 59  ? 31.126 -37.733 -15.096 1.00 36.09  ? 59  ALA A CA    1 
ATOM   453  C C     . ALA A 1 59  ? 32.530 -38.154 -15.513 1.00 36.29  ? 59  ALA A C     1 
ATOM   454  O O     . ALA A 1 59  ? 33.317 -38.593 -14.679 1.00 38.34  ? 59  ALA A O     1 
ATOM   455  C CB    . ALA A 1 59  ? 31.109 -37.206 -13.694 1.00 36.48  ? 59  ALA A CB    1 
ATOM   456  N N     . PRO A 1 60  ? 32.889 -38.054 -16.812 1.00 34.10  ? 60  PRO A N     1 
ATOM   457  C CA    . PRO A 1 60  ? 34.210 -38.465 -17.271 1.00 32.40  ? 60  PRO A CA    1 
ATOM   458  C C     . PRO A 1 60  ? 35.306 -37.463 -16.946 1.00 33.40  ? 60  PRO A C     1 
ATOM   459  O O     . PRO A 1 60  ? 35.028 -36.301 -16.623 1.00 30.91  ? 60  PRO A O     1 
ATOM   460  C CB    . PRO A 1 60  ? 34.069 -38.560 -18.786 1.00 31.66  ? 60  PRO A CB    1 
ATOM   461  C CG    . PRO A 1 60  ? 33.006 -37.548 -19.090 1.00 34.26  ? 60  PRO A CG    1 
ATOM   462  C CD    . PRO A 1 60  ? 32.032 -37.618 -17.924 1.00 33.90  ? 60  PRO A CD    1 
ATOM   463  N N     . ALA A 1 61  ? 36.548 -37.965 -17.039 1.00 33.99  ? 61  ALA A N     1 
ATOM   464  C CA    . ALA A 1 61  ? 37.720 -37.203 -16.659 1.00 34.63  ? 61  ALA A CA    1 
ATOM   465  C C     . ALA A 1 61  ? 38.579 -36.915 -17.879 1.00 31.81  ? 61  ALA A C     1 
ATOM   466  O O     . ALA A 1 61  ? 39.523 -36.153 -17.755 1.00 31.76  ? 61  ALA A O     1 
ATOM   467  C CB    . ALA A 1 61  ? 38.501 -37.919 -15.582 1.00 36.01  ? 61  ALA A CB    1 
ATOM   468  N N     . SER A 1 62  ? 38.216 -37.446 -19.053 1.00 31.09  ? 62  SER A N     1 
ATOM   469  C CA    . SER A 1 62  ? 38.992 -37.179 -20.256 1.00 32.51  ? 62  SER A CA    1 
ATOM   470  C C     . SER A 1 62  ? 38.142 -37.359 -21.515 1.00 28.38  ? 62  SER A C     1 
ATOM   471  O O     . SER A 1 62  ? 37.063 -37.930 -21.452 1.00 26.08  ? 62  SER A O     1 
ATOM   472  C CB    . SER A 1 62  ? 40.213 -38.081 -20.298 1.00 31.85  ? 62  SER A CB    1 
ATOM   473  O OG    . SER A 1 62  ? 39.818 -39.402 -20.610 1.00 34.36  ? 62  SER A OG    1 
ATOM   474  N N     . THR A 1 63  ? 38.682 -36.896 -22.651 1.00 29.31  ? 63  THR A N     1 
ATOM   475  C CA    . THR A 1 63  ? 38.088 -37.044 -23.977 1.00 33.84  ? 63  THR A CA    1 
ATOM   476  C C     . THR A 1 63  ? 37.911 -38.528 -24.328 1.00 35.61  ? 63  THR A C     1 
ATOM   477  O O     . THR A 1 63  ? 36.875 -38.946 -24.854 1.00 36.22  ? 63  THR A O     1 
ATOM   478  C CB    . THR A 1 63  ? 38.946 -36.307 -25.024 1.00 33.66  ? 63  THR A CB    1 
ATOM   479  O OG1   . THR A 1 63  ? 38.983 -34.918 -24.682 1.00 35.23  ? 63  THR A OG1   1 
ATOM   480  C CG2   . THR A 1 63  ? 38.443 -36.440 -26.444 1.00 32.13  ? 63  THR A CG2   1 
ATOM   481  N N     . GLU A 1 64  ? 38.944 -39.327 -24.053 1.00 37.42  ? 64  GLU A N     1 
ATOM   482  C CA    . GLU A 1 64  ? 38.913 -40.749 -24.339 1.00 35.68  ? 64  GLU A CA    1 
ATOM   483  C C     . GLU A 1 64  ? 37.705 -41.350 -23.619 1.00 30.92  ? 64  GLU A C     1 
ATOM   484  O O     . GLU A 1 64  ? 36.978 -42.166 -24.169 1.00 28.86  ? 64  GLU A O     1 
ATOM   485  C CB    . GLU A 1 64  ? 40.238 -41.404 -23.930 1.00 40.28  ? 64  GLU A CB    1 
ATOM   486  C CG    . GLU A 1 64  ? 41.474 -40.885 -24.673 1.00 48.67  ? 64  GLU A CG    1 
ATOM   487  C CD    . GLU A 1 64  ? 41.931 -39.440 -24.453 1.00 52.83  ? 64  GLU A CD    1 
ATOM   488  O OE1   . GLU A 1 64  ? 41.897 -38.960 -23.301 1.00 52.30  ? 64  GLU A OE1   1 
ATOM   489  O OE2   . GLU A 1 64  ? 42.348 -38.786 -25.448 1.00 62.58  ? 64  GLU A OE2   1 
ATOM   490  N N     . GLU A 1 65  ? 37.442 -40.907 -22.394 1.00 29.42  ? 65  GLU A N     1 
ATOM   491  C CA    . GLU A 1 65  ? 36.289 -41.437 -21.681 1.00 31.43  ? 65  GLU A CA    1 
ATOM   492  C C     . GLU A 1 65  ? 34.981 -41.000 -22.335 1.00 30.65  ? 65  GLU A C     1 
ATOM   493  O O     . GLU A 1 65  ? 34.028 -41.793 -22.397 1.00 32.11  ? 65  GLU A O     1 
ATOM   494  C CB    . GLU A 1 65  ? 36.366 -41.083 -20.196 1.00 31.23  ? 65  GLU A CB    1 
ATOM   495  C CG    . GLU A 1 65  ? 37.412 -41.915 -19.493 1.00 30.13  ? 65  GLU A CG    1 
ATOM   496  C CD    . GLU A 1 65  ? 37.690 -41.595 -18.041 1.00 34.20  ? 65  GLU A CD    1 
ATOM   497  O OE1   . GLU A 1 65  ? 36.917 -40.807 -17.418 1.00 35.53  ? 65  GLU A OE1   1 
ATOM   498  O OE2   . GLU A 1 65  ? 38.694 -42.144 -17.540 1.00 36.94  ? 65  GLU A OE2   1 
ATOM   499  N N     . VAL A 1 66  ? 34.937 -39.753 -22.831 1.00 27.71  ? 66  VAL A N     1 
ATOM   500  C CA    . VAL A 1 66  ? 33.750 -39.279 -23.517 1.00 26.77  ? 66  VAL A CA    1 
ATOM   501  C C     . VAL A 1 66  ? 33.508 -40.159 -24.741 1.00 26.53  ? 66  VAL A C     1 
ATOM   502  O O     . VAL A 1 66  ? 32.377 -40.555 -25.000 1.00 26.54  ? 66  VAL A O     1 
ATOM   503  C CB    . VAL A 1 66  ? 33.854 -37.790 -23.882 1.00 27.23  ? 66  VAL A CB    1 
ATOM   504  C CG1   . VAL A 1 66  ? 32.692 -37.353 -24.752 1.00 27.89  ? 66  VAL A CG1   1 
ATOM   505  C CG2   . VAL A 1 66  ? 33.968 -36.917 -22.641 1.00 27.96  ? 66  VAL A CG2   1 
ATOM   506  N N     . GLN A 1 67  ? 34.581 -40.516 -25.456 1.00 26.55  ? 67  GLN A N     1 
ATOM   507  C CA    . GLN A 1 67  ? 34.442 -41.293 -26.676 1.00 27.78  ? 67  GLN A CA    1 
ATOM   508  C C     . GLN A 1 67  ? 33.820 -42.653 -26.372 1.00 31.14  ? 67  GLN A C     1 
ATOM   509  O O     . GLN A 1 67  ? 32.883 -43.081 -27.051 1.00 34.76  ? 67  GLN A O     1 
ATOM   510  C CB    . GLN A 1 67  ? 35.789 -41.467 -27.373 1.00 28.48  ? 67  GLN A CB    1 
ATOM   511  C CG    . GLN A 1 67  ? 36.347 -40.207 -28.014 1.00 27.47  ? 67  GLN A CG    1 
ATOM   512  C CD    . GLN A 1 67  ? 37.722 -40.455 -28.587 1.00 27.79  ? 67  GLN A CD    1 
ATOM   513  O OE1   . GLN A 1 67  ? 38.733 -40.226 -27.927 1.00 29.56  ? 67  GLN A OE1   1 
ATOM   514  N NE2   . GLN A 1 67  ? 37.775 -40.956 -29.813 1.00 26.27  ? 67  GLN A NE2   1 
ATOM   515  N N     . GLU A 1 68  ? 34.318 -43.299 -25.318 1.00 33.35  ? 68  GLU A N     1 
ATOM   516  C CA    . GLU A 1 68  ? 33.862 -44.617 -24.904 1.00 35.84  ? 68  GLU A CA    1 
ATOM   517  C C     . GLU A 1 68  ? 32.399 -44.577 -24.452 1.00 35.69  ? 68  GLU A C     1 
ATOM   518  O O     . GLU A 1 68  ? 31.613 -45.447 -24.824 1.00 34.92  ? 68  GLU A O     1 
ATOM   519  C CB    . GLU A 1 68  ? 34.821 -45.159 -23.836 1.00 37.20  ? 68  GLU A CB    1 
ATOM   520  C CG    . GLU A 1 68  ? 36.157 -45.601 -24.417 1.00 40.88  ? 68  GLU A CG    1 
ATOM   521  C CD    . GLU A 1 68  ? 37.347 -45.612 -23.464 1.00 51.66  ? 68  GLU A CD    1 
ATOM   522  O OE1   . GLU A 1 68  ? 37.136 -45.410 -22.232 1.00 51.07  ? 68  GLU A OE1   1 
ATOM   523  O OE2   . GLU A 1 68  ? 38.500 -45.791 -23.960 1.00 51.52  ? 68  GLU A OE2   1 
ATOM   524  N N     . ILE A 1 69  ? 32.032 -43.562 -23.661 1.00 36.78  ? 69  ILE A N     1 
ATOM   525  C CA    . ILE A 1 69  ? 30.651 -43.385 -23.227 1.00 34.00  ? 69  ILE A CA    1 
ATOM   526  C C     . ILE A 1 69  ? 29.731 -43.234 -24.436 1.00 33.52  ? 69  ILE A C     1 
ATOM   527  O O     . ILE A 1 69  ? 28.647 -43.809 -24.466 1.00 30.54  ? 69  ILE A O     1 
ATOM   528  C CB    . ILE A 1 69  ? 30.538 -42.165 -22.301 1.00 32.80  ? 69  ILE A CB    1 
ATOM   529  C CG1   . ILE A 1 69  ? 31.257 -42.410 -20.974 1.00 30.90  ? 69  ILE A CG1   1 
ATOM   530  C CG2   . ILE A 1 69  ? 29.087 -41.782 -22.103 1.00 31.80  ? 69  ILE A CG2   1 
ATOM   531  C CD1   . ILE A 1 69  ? 31.702 -41.144 -20.301 1.00 31.63  ? 69  ILE A CD1   1 
ATOM   532  N N     . VAL A 1 70  ? 30.160 -42.458 -25.438 1.00 34.21  ? 70  VAL A N     1 
ATOM   533  C CA    . VAL A 1 70  ? 29.341 -42.266 -26.626 1.00 35.63  ? 70  VAL A CA    1 
ATOM   534  C C     . VAL A 1 70  ? 29.168 -43.595 -27.363 1.00 33.85  ? 70  VAL A C     1 
ATOM   535  O O     . VAL A 1 70  ? 28.063 -43.913 -27.802 1.00 31.95  ? 70  VAL A O     1 
ATOM   536  C CB    . VAL A 1 70  ? 29.917 -41.165 -27.538 1.00 36.59  ? 70  VAL A CB    1 
ATOM   537  C CG1   . VAL A 1 70  ? 29.296 -41.171 -28.931 1.00 37.58  ? 70  VAL A CG1   1 
ATOM   538  C CG2   . VAL A 1 70  ? 29.762 -39.799 -26.898 1.00 36.62  ? 70  VAL A CG2   1 
ATOM   539  N N     . ARG A 1 71  ? 30.259 -44.359 -27.522 1.00 35.58  ? 71  ARG A N     1 
ATOM   540  C CA    . ARG A 1 71  ? 30.190 -45.639 -28.224 1.00 35.79  ? 71  ARG A CA    1 
ATOM   541  C C     . ARG A 1 71  ? 29.252 -46.599 -27.499 1.00 33.14  ? 71  ARG A C     1 
ATOM   542  O O     . ARG A 1 71  ? 28.487 -47.303 -28.141 1.00 32.86  ? 71  ARG A O     1 
ATOM   543  C CB    . ARG A 1 71  ? 31.559 -46.302 -28.370 1.00 35.51  ? 71  ARG A CB    1 
ATOM   544  C CG    . ARG A 1 71  ? 32.499 -45.584 -29.325 1.00 36.30  ? 71  ARG A CG    1 
ATOM   545  C CD    . ARG A 1 71  ? 33.862 -46.221 -29.272 1.00 38.43  ? 71  ARG A CD    1 
ATOM   546  N NE    . ARG A 1 71  ? 34.836 -45.385 -29.939 1.00 46.32  ? 71  ARG A NE    1 
ATOM   547  C CZ    . ARG A 1 71  ? 36.026 -45.046 -29.447 1.00 52.12  ? 71  ARG A CZ    1 
ATOM   548  N NH1   . ARG A 1 71  ? 36.405 -45.443 -28.241 1.00 49.57  ? 71  ARG A NH1   1 
ATOM   549  N NH2   . ARG A 1 71  ? 36.836 -44.298 -30.178 1.00 55.19  ? 71  ARG A NH2   1 
ATOM   550  N N     . VAL A 1 72  ? 29.294 -46.598 -26.167 1.00 33.04  ? 72  VAL A N     1 
ATOM   551  C CA    . VAL A 1 72  ? 28.428 -47.464 -25.385 1.00 33.74  ? 72  VAL A CA    1 
ATOM   552  C C     . VAL A 1 72  ? 26.975 -47.041 -25.571 1.00 34.71  ? 72  VAL A C     1 
ATOM   553  O O     . VAL A 1 72  ? 26.092 -47.882 -25.731 1.00 31.48  ? 72  VAL A O     1 
ATOM   554  C CB    . VAL A 1 72  ? 28.840 -47.458 -23.901 1.00 35.40  ? 72  VAL A CB    1 
ATOM   555  C CG1   . VAL A 1 72  ? 27.739 -47.990 -23.005 1.00 36.58  ? 72  VAL A CG1   1 
ATOM   556  C CG2   . VAL A 1 72  ? 30.132 -48.242 -23.680 1.00 36.75  ? 72  VAL A CG2   1 
ATOM   557  N N     . ALA A 1 73  ? 26.741 -45.724 -25.513 1.00 37.45  ? 73  ALA A N     1 
ATOM   558  C CA    . ALA A 1 73  ? 25.412 -45.156 -25.677 1.00 33.56  ? 73  ALA A CA    1 
ATOM   559  C C     . ALA A 1 73  ? 24.817 -45.599 -27.007 1.00 30.79  ? 73  ALA A C     1 
ATOM   560  O O     . ALA A 1 73  ? 23.627 -45.864 -27.074 1.00 35.23  ? 73  ALA A O     1 
ATOM   561  C CB    . ALA A 1 73  ? 25.462 -43.649 -25.576 1.00 33.13  ? 73  ALA A CB    1 
ATOM   562  N N     . ASN A 1 74  ? 25.635 -45.666 -28.060 1.00 32.64  ? 74  ASN A N     1 
ATOM   563  C CA    . ASN A 1 74  ? 25.188 -46.178 -29.353 1.00 32.90  ? 74  ASN A CA    1 
ATOM   564  C C     . ASN A 1 74  ? 24.827 -47.660 -29.265 1.00 34.47  ? 74  ASN A C     1 
ATOM   565  O O     . ASN A 1 74  ? 23.822 -48.083 -29.828 1.00 35.36  ? 74  ASN A O     1 
ATOM   566  C CB    . ASN A 1 74  ? 26.228 -45.987 -30.456 1.00 30.74  ? 74  ASN A CB    1 
ATOM   567  C CG    . ASN A 1 74  ? 26.166 -44.605 -31.062 1.00 31.97  ? 74  ASN A CG    1 
ATOM   568  O OD1   . ASN A 1 74  ? 25.351 -44.339 -31.946 1.00 28.09  ? 74  ASN A OD1   1 
ATOM   569  N ND2   . ASN A 1 74  ? 27.051 -43.731 -30.608 1.00 34.11  ? 74  ASN A ND2   1 
ATOM   570  N N     . GLU A 1 75  ? 25.643 -48.444 -28.558 1.00 36.32  ? 75  GLU A N     1 
ATOM   571  C CA    . GLU A 1 75  ? 25.423 -49.880 -28.475 1.00 41.19  ? 75  GLU A CA    1 
ATOM   572  C C     . GLU A 1 75  ? 24.060 -50.191 -27.852 1.00 36.72  ? 75  GLU A C     1 
ATOM   573  O O     . GLU A 1 75  ? 23.379 -51.090 -28.322 1.00 32.28  ? 75  GLU A O     1 
ATOM   574  C CB    . GLU A 1 75  ? 26.563 -50.559 -27.716 1.00 44.81  ? 75  GLU A CB    1 
ATOM   575  C CG    . GLU A 1 75  ? 26.516 -52.073 -27.765 1.00 52.10  ? 75  GLU A CG    1 
ATOM   576  C CD    . GLU A 1 75  ? 27.783 -52.724 -27.234 1.00 62.44  ? 75  GLU A CD    1 
ATOM   577  O OE1   . GLU A 1 75  ? 27.811 -53.987 -27.076 1.00 63.34  ? 75  GLU A OE1   1 
ATOM   578  O OE2   . GLU A 1 75  ? 28.758 -51.959 -26.989 1.00 65.57  ? 75  GLU A OE2   1 
ATOM   579  N N     . PHE A 1 76  ? 23.647 -49.437 -26.825 1.00 35.35  ? 76  PHE A N     1 
ATOM   580  C CA    . PHE A 1 76  ? 22.465 -49.802 -26.068 1.00 35.34  ? 76  PHE A CA    1 
ATOM   581  C C     . PHE A 1 76  ? 21.269 -48.905 -26.382 1.00 37.77  ? 76  PHE A C     1 
ATOM   582  O O     . PHE A 1 76  ? 20.198 -49.114 -25.802 1.00 38.32  ? 76  PHE A O     1 
ATOM   583  C CB    . PHE A 1 76  ? 22.831 -49.855 -24.586 1.00 37.35  ? 76  PHE A CB    1 
ATOM   584  C CG    . PHE A 1 76  ? 23.731 -51.027 -24.269 1.00 39.66  ? 76  PHE A CG    1 
ATOM   585  C CD1   . PHE A 1 76  ? 23.243 -52.326 -24.313 1.00 39.65  ? 76  PHE A CD1   1 
ATOM   586  C CD2   . PHE A 1 76  ? 25.080 -50.840 -24.002 1.00 39.50  ? 76  PHE A CD2   1 
ATOM   587  C CE1   . PHE A 1 76  ? 24.066 -53.405 -24.042 1.00 39.23  ? 76  PHE A CE1   1 
ATOM   588  C CE2   . PHE A 1 76  ? 25.907 -51.922 -23.743 1.00 42.49  ? 76  PHE A CE2   1 
ATOM   589  C CZ    . PHE A 1 76  ? 25.397 -53.201 -23.760 1.00 42.10  ? 76  PHE A CZ    1 
ATOM   590  N N     . GLY A 1 77  ? 21.430 -47.954 -27.321 1.00 37.92  ? 77  GLY A N     1 
ATOM   591  C CA    . GLY A 1 77  ? 20.397 -46.969 -27.625 1.00 34.86  ? 77  GLY A CA    1 
ATOM   592  C C     . GLY A 1 77  ? 20.068 -46.033 -26.452 1.00 34.23  ? 77  GLY A C     1 
ATOM   593  O O     . GLY A 1 77  ? 18.945 -45.545 -26.357 1.00 33.98  ? 77  GLY A O     1 
ATOM   594  N N     . VAL A 1 78  ? 21.051 -45.749 -25.581 1.00 33.96  ? 78  VAL A N     1 
ATOM   595  C CA    . VAL A 1 78  ? 20.838 -44.920 -24.400 1.00 36.00  ? 78  VAL A CA    1 
ATOM   596  C C     . VAL A 1 78  ? 21.218 -43.472 -24.699 1.00 37.35  ? 78  VAL A C     1 
ATOM   597  O O     . VAL A 1 78  ? 22.355 -43.161 -25.053 1.00 33.52  ? 78  VAL A O     1 
ATOM   598  C CB    . VAL A 1 78  ? 21.614 -45.427 -23.172 1.00 39.66  ? 78  VAL A CB    1 
ATOM   599  C CG1   . VAL A 1 78  ? 21.477 -44.460 -21.999 1.00 40.68  ? 78  VAL A CG1   1 
ATOM   600  C CG2   . VAL A 1 78  ? 21.156 -46.823 -22.775 1.00 43.01  ? 78  VAL A CG2   1 
ATOM   601  N N     . PRO A 1 79  ? 20.248 -42.538 -24.616 1.00 38.53  ? 79  PRO A N     1 
ATOM   602  C CA    . PRO A 1 79  ? 20.524 -41.137 -24.913 1.00 34.25  ? 79  PRO A CA    1 
ATOM   603  C C     . PRO A 1 79  ? 21.253 -40.384 -23.803 1.00 31.50  ? 79  PRO A C     1 
ATOM   604  O O     . PRO A 1 79  ? 21.043 -40.621 -22.617 1.00 33.19  ? 79  PRO A O     1 
ATOM   605  C CB    . PRO A 1 79  ? 19.131 -40.563 -25.196 1.00 39.05  ? 79  PRO A CB    1 
ATOM   606  C CG    . PRO A 1 79  ? 18.179 -41.446 -24.443 1.00 38.67  ? 79  PRO A CG    1 
ATOM   607  C CD    . PRO A 1 79  ? 18.821 -42.816 -24.392 1.00 38.37  ? 79  PRO A CD    1 
ATOM   608  N N     . LEU A 1 80  ? 22.123 -39.470 -24.235 1.00 28.60  ? 80  LEU A N     1 
ATOM   609  C CA    . LEU A 1 80  ? 22.937 -38.646 -23.368 1.00 28.56  ? 80  LEU A CA    1 
ATOM   610  C C     . LEU A 1 80  ? 22.498 -37.189 -23.501 1.00 31.02  ? 80  LEU A C     1 
ATOM   611  O O     . LEU A 1 80  ? 22.081 -36.750 -24.574 1.00 30.40  ? 80  LEU A O     1 
ATOM   612  C CB    . LEU A 1 80  ? 24.392 -38.762 -23.830 1.00 30.73  ? 80  LEU A CB    1 
ATOM   613  C CG    . LEU A 1 80  ? 24.987 -40.166 -23.888 1.00 31.28  ? 80  LEU A CG    1 
ATOM   614  C CD1   . LEU A 1 80  ? 26.343 -40.157 -24.562 1.00 28.91  ? 80  LEU A CD1   1 
ATOM   615  C CD2   . LEU A 1 80  ? 25.119 -40.744 -22.486 1.00 34.50  ? 80  LEU A CD2   1 
ATOM   616  N N     . TRP A 1 81  ? 22.693 -36.432 -22.422 1.00 32.74  ? 81  TRP A N     1 
ATOM   617  C CA    . TRP A 1 81  ? 22.499 -34.997 -22.416 1.00 33.19  ? 81  TRP A CA    1 
ATOM   618  C C     . TRP A 1 81  ? 23.812 -34.344 -21.994 1.00 32.44  ? 81  TRP A C     1 
ATOM   619  O O     . TRP A 1 81  ? 24.094 -34.259 -20.802 1.00 31.05  ? 81  TRP A O     1 
ATOM   620  C CB    . TRP A 1 81  ? 21.347 -34.611 -21.472 1.00 37.81  ? 81  TRP A CB    1 
ATOM   621  C CG    . TRP A 1 81  ? 20.980 -33.162 -21.577 1.00 36.28  ? 81  TRP A CG    1 
ATOM   622  C CD1   . TRP A 1 81  ? 21.464 -32.142 -20.814 1.00 34.06  ? 81  TRP A CD1   1 
ATOM   623  C CD2   . TRP A 1 81  ? 20.077 -32.571 -22.527 1.00 33.26  ? 81  TRP A CD2   1 
ATOM   624  N NE1   . TRP A 1 81  ? 20.953 -30.958 -21.246 1.00 35.40  ? 81  TRP A NE1   1 
ATOM   625  C CE2   . TRP A 1 81  ? 20.079 -31.186 -22.276 1.00 33.59  ? 81  TRP A CE2   1 
ATOM   626  C CE3   . TRP A 1 81  ? 19.269 -33.075 -23.553 1.00 32.35  ? 81  TRP A CE3   1 
ATOM   627  C CZ2   . TRP A 1 81  ? 19.304 -30.292 -23.018 1.00 32.00  ? 81  TRP A CZ2   1 
ATOM   628  C CZ3   . TRP A 1 81  ? 18.503 -32.196 -24.286 1.00 31.48  ? 81  TRP A CZ3   1 
ATOM   629  C CH2   . TRP A 1 81  ? 18.535 -30.823 -24.031 1.00 32.13  ? 81  TRP A CH2   1 
ATOM   630  N N     . PRO A 1 82  ? 24.673 -33.895 -22.941 1.00 34.11  ? 82  PRO A N     1 
ATOM   631  C CA    . PRO A 1 82  ? 25.945 -33.272 -22.586 1.00 34.30  ? 82  PRO A CA    1 
ATOM   632  C C     . PRO A 1 82  ? 25.776 -31.886 -21.971 1.00 35.18  ? 82  PRO A C     1 
ATOM   633  O O     . PRO A 1 82  ? 25.026 -31.068 -22.497 1.00 35.75  ? 82  PRO A O     1 
ATOM   634  C CB    . PRO A 1 82  ? 26.699 -33.141 -23.909 1.00 34.70  ? 82  PRO A CB    1 
ATOM   635  C CG    . PRO A 1 82  ? 25.937 -34.035 -24.870 1.00 36.35  ? 82  PRO A CG    1 
ATOM   636  C CD    . PRO A 1 82  ? 24.505 -33.993 -24.396 1.00 34.08  ? 82  PRO A CD    1 
ATOM   637  N N     . VAL A 1 83  ? 26.511 -31.659 -20.870 1.00 35.29  ? 83  VAL A N     1 
ATOM   638  C CA    . VAL A 1 83  ? 26.686 -30.363 -20.234 1.00 33.18  ? 83  VAL A CA    1 
ATOM   639  C C     . VAL A 1 83  ? 28.167 -30.177 -19.904 1.00 33.57  ? 83  VAL A C     1 
ATOM   640  O O     . VAL A 1 83  ? 28.845 -31.143 -19.555 1.00 33.61  ? 83  VAL A O     1 
ATOM   641  C CB    . VAL A 1 83  ? 25.824 -30.266 -18.962 1.00 32.62  ? 83  VAL A CB    1 
ATOM   642  C CG1   . VAL A 1 83  ? 24.398 -30.720 -19.216 1.00 33.96  ? 83  VAL A CG1   1 
ATOM   643  C CG2   . VAL A 1 83  ? 26.418 -31.057 -17.820 1.00 31.55  ? 83  VAL A CG2   1 
ATOM   644  N N     . SER A 1 84  ? 28.649 -28.925 -19.983 1.00 32.92  ? 84  SER A N     1 
ATOM   645  C CA    . SER A 1 84  ? 30.009 -28.575 -19.610 1.00 31.24  ? 84  SER A CA    1 
ATOM   646  C C     . SER A 1 84  ? 30.135 -28.441 -18.088 1.00 31.95  ? 84  SER A C     1 
ATOM   647  O O     . SER A 1 84  ? 31.012 -29.038 -17.473 1.00 32.66  ? 84  SER A O     1 
ATOM   648  C CB    . SER A 1 84  ? 30.443 -27.323 -20.325 1.00 33.04  ? 84  SER A CB    1 
ATOM   649  O OG    . SER A 1 84  ? 30.524 -27.536 -21.719 1.00 31.41  ? 84  SER A OG    1 
ATOM   650  N N     . ARG A 1 85  ? 29.257 -27.651 -17.463 1.00 33.49  ? 85  ARG A N     1 
ATOM   651  C CA    . ARG A 1 85  ? 29.190 -27.602 -16.006 1.00 32.63  ? 85  ARG A CA    1 
ATOM   652  C C     . ARG A 1 85  ? 27.760 -27.726 -15.504 1.00 33.87  ? 85  ARG A C     1 
ATOM   653  O O     . ARG A 1 85  ? 27.544 -27.981 -14.321 1.00 37.75  ? 85  ARG A O     1 
ATOM   654  C CB    . ARG A 1 85  ? 29.809 -26.316 -15.471 1.00 30.25  ? 85  ARG A CB    1 
ATOM   655  C CG    . ARG A 1 85  ? 31.323 -26.344 -15.529 1.00 32.14  ? 85  ARG A CG    1 
ATOM   656  C CD    . ARG A 1 85  ? 31.929 -25.079 -14.945 1.00 37.68  ? 85  ARG A CD    1 
ATOM   657  N NE    . ARG A 1 85  ? 31.435 -24.771 -13.608 1.00 40.85  ? 85  ARG A NE    1 
ATOM   658  C CZ    . ARG A 1 85  ? 31.986 -25.188 -12.465 1.00 41.33  ? 85  ARG A CZ    1 
ATOM   659  N NH1   . ARG A 1 85  ? 33.030 -25.991 -12.481 1.00 39.54  ? 85  ARG A NH1   1 
ATOM   660  N NH2   . ARG A 1 85  ? 31.457 -24.836 -11.305 1.00 43.27  ? 85  ARG A NH2   1 
ATOM   661  N N     . GLY A 1 86  ? 26.798 -27.488 -16.395 1.00 34.19  ? 86  GLY A N     1 
ATOM   662  C CA    . GLY A 1 86  ? 25.410 -27.762 -16.088 1.00 38.68  ? 86  GLY A CA    1 
ATOM   663  C C     . GLY A 1 86  ? 24.747 -26.686 -15.228 1.00 37.79  ? 86  GLY A C     1 
ATOM   664  O O     . GLY A 1 86  ? 23.743 -26.974 -14.593 1.00 37.58  ? 86  GLY A O     1 
ATOM   665  N N     . LYS A 1 87  ? 25.259 -25.448 -15.277 1.00 36.56  ? 87  LYS A N     1 
ATOM   666  C CA    . LYS A 1 87  ? 24.711 -24.343 -14.508 1.00 36.26  ? 87  LYS A CA    1 
ATOM   667  C C     . LYS A 1 87  ? 23.746 -23.485 -15.340 1.00 34.64  ? 87  LYS A C     1 
ATOM   668  O O     . LYS A 1 87  ? 23.671 -22.277 -15.137 1.00 34.23  ? 87  LYS A O     1 
ATOM   669  C CB    . LYS A 1 87  ? 25.877 -23.502 -13.983 1.00 38.62  ? 87  LYS A CB    1 
ATOM   670  C CG    . LYS A 1 87  ? 26.976 -24.284 -13.270 1.00 42.21  ? 87  LYS A CG    1 
ATOM   671  C CD    . LYS A 1 87  ? 26.522 -25.040 -12.030 1.00 43.16  ? 87  LYS A CD    1 
ATOM   672  C CE    . LYS A 1 87  ? 27.649 -25.830 -11.389 1.00 42.69  ? 87  LYS A CE    1 
ATOM   673  N NZ    . LYS A 1 87  ? 27.144 -26.868 -10.462 1.00 39.58  ? 87  LYS A NZ    1 
ATOM   674  N N     . ASN A 1 88  ? 22.971 -24.103 -16.246 1.00 32.80  ? 88  ASN A N     1 
ATOM   675  C CA    . ASN A 1 88  ? 22.090 -23.373 -17.147 1.00 33.33  ? 88  ASN A CA    1 
ATOM   676  C C     . ASN A 1 88  ? 20.762 -23.018 -16.454 1.00 33.06  ? 88  ASN A C     1 
ATOM   677  O O     . ASN A 1 88  ? 19.660 -23.224 -16.985 1.00 30.21  ? 88  ASN A O     1 
ATOM   678  C CB    . ASN A 1 88  ? 21.884 -24.152 -18.458 1.00 32.64  ? 88  ASN A CB    1 
ATOM   679  C CG    . ASN A 1 88  ? 21.735 -23.250 -19.671 1.00 33.26  ? 88  ASN A CG    1 
ATOM   680  O OD1   . ASN A 1 88  ? 22.098 -22.072 -19.630 1.00 33.10  ? 88  ASN A OD1   1 
ATOM   681  N ND2   . ASN A 1 88  ? 21.204 -23.786 -20.761 1.00 31.04  ? 88  ASN A ND2   1 
ATOM   682  N N     . PHE A 1 89  ? 20.870 -22.431 -15.266 1.00 33.93  ? 89  PHE A N     1 
ATOM   683  C CA    . PHE A 1 89  ? 19.719 -21.953 -14.515 1.00 38.91  ? 89  PHE A CA    1 
ATOM   684  C C     . PHE A 1 89  ? 18.907 -20.961 -15.350 1.00 36.36  ? 89  PHE A C     1 
ATOM   685  O O     . PHE A 1 89  ? 19.463 -20.099 -16.028 1.00 38.37  ? 89  PHE A O     1 
ATOM   686  C CB    . PHE A 1 89  ? 20.178 -21.219 -13.251 1.00 44.21  ? 89  PHE A CB    1 
ATOM   687  C CG    . PHE A 1 89  ? 21.075 -21.985 -12.306 1.00 49.48  ? 89  PHE A CG    1 
ATOM   688  C CD1   . PHE A 1 89  ? 20.546 -22.825 -11.340 1.00 57.44  ? 89  PHE A CD1   1 
ATOM   689  C CD2   . PHE A 1 89  ? 22.453 -21.826 -12.352 1.00 55.14  ? 89  PHE A CD2   1 
ATOM   690  C CE1   . PHE A 1 89  ? 21.375 -23.498 -10.453 1.00 65.53  ? 89  PHE A CE1   1 
ATOM   691  C CE2   . PHE A 1 89  ? 23.282 -22.512 -11.475 1.00 60.90  ? 89  PHE A CE2   1 
ATOM   692  C CZ    . PHE A 1 89  ? 22.743 -23.352 -10.529 1.00 61.80  ? 89  PHE A CZ    1 
ATOM   693  N N     . ALA A 1 90  ? 17.584 -21.071 -15.259 1.00 34.94  ? 90  ALA A N     1 
ATOM   694  C CA    . ALA A 1 90  ? 16.650 -20.270 -16.038 1.00 38.34  ? 90  ALA A CA    1 
ATOM   695  C C     . ALA A 1 90  ? 16.353 -20.949 -17.374 1.00 34.36  ? 90  ALA A C     1 
ATOM   696  O O     . ALA A 1 90  ? 15.391 -20.569 -18.046 1.00 31.52  ? 90  ALA A O     1 
ATOM   697  C CB    . ALA A 1 90  ? 17.138 -18.843 -16.224 1.00 37.57  ? 90  ALA A CB    1 
ATOM   698  N N     . TYR A 1 91  ? 17.168 -21.953 -17.733 1.00 31.25  ? 91  TYR A N     1 
ATOM   699  C CA    . TYR A 1 91  ? 17.013 -22.654 -19.000 1.00 34.32  ? 91  TYR A CA    1 
ATOM   700  C C     . TYR A 1 91  ? 16.899 -24.163 -18.792 1.00 33.61  ? 91  TYR A C     1 
ATOM   701  O O     . TYR A 1 91  ? 16.804 -24.896 -19.762 1.00 32.59  ? 91  TYR A O     1 
ATOM   702  C CB    . TYR A 1 91  ? 18.173 -22.323 -19.948 1.00 33.90  ? 91  TYR A CB    1 
ATOM   703  C CG    . TYR A 1 91  ? 18.281 -20.875 -20.356 1.00 36.77  ? 91  TYR A CG    1 
ATOM   704  C CD1   . TYR A 1 91  ? 17.328 -20.288 -21.164 1.00 42.57  ? 91  TYR A CD1   1 
ATOM   705  C CD2   . TYR A 1 91  ? 19.319 -20.077 -19.911 1.00 39.00  ? 91  TYR A CD2   1 
ATOM   706  C CE1   . TYR A 1 91  ? 17.400 -18.955 -21.531 1.00 43.00  ? 91  TYR A CE1   1 
ATOM   707  C CE2   . TYR A 1 91  ? 19.416 -18.747 -20.278 1.00 40.99  ? 91  TYR A CE2   1 
ATOM   708  C CZ    . TYR A 1 91  ? 18.457 -18.183 -21.098 1.00 40.66  ? 91  TYR A CZ    1 
ATOM   709  O OH    . TYR A 1 91  ? 18.554 -16.869 -21.481 1.00 39.76  ? 91  TYR A OH    1 
ATOM   710  N N     . GLY A 1 92  ? 16.892 -24.624 -17.535 1.00 37.82  ? 92  GLY A N     1 
ATOM   711  C CA    . GLY A 1 92  ? 16.658 -26.028 -17.227 1.00 37.02  ? 92  GLY A CA    1 
ATOM   712  C C     . GLY A 1 92  ? 17.742 -26.637 -16.337 1.00 33.17  ? 92  GLY A C     1 
ATOM   713  O O     . GLY A 1 92  ? 17.669 -27.807 -15.973 1.00 31.51  ? 92  GLY A O     1 
ATOM   714  N N     . GLY A 1 93  ? 18.739 -25.840 -15.971 1.00 31.74  ? 93  GLY A N     1 
ATOM   715  C CA    . GLY A 1 93  ? 19.892 -26.386 -15.283 1.00 33.40  ? 93  GLY A CA    1 
ATOM   716  C C     . GLY A 1 93  ? 20.584 -27.423 -16.162 1.00 34.57  ? 93  GLY A C     1 
ATOM   717  O O     . GLY A 1 93  ? 20.827 -27.183 -17.341 1.00 33.51  ? 93  GLY A O     1 
ATOM   718  N N     . ALA A 1 94  ? 20.854 -28.586 -15.578 1.00 33.98  ? 94  ALA A N     1 
ATOM   719  C CA    . ALA A 1 94  ? 21.532 -29.667 -16.268 1.00 37.23  ? 94  ALA A CA    1 
ATOM   720  C C     . ALA A 1 94  ? 20.522 -30.725 -16.716 1.00 35.59  ? 94  ALA A C     1 
ATOM   721  O O     . ALA A 1 94  ? 20.922 -31.819 -17.098 1.00 35.79  ? 94  ALA A O     1 
ATOM   722  C CB    . ALA A 1 94  ? 22.589 -30.269 -15.351 1.00 35.52  ? 94  ALA A CB    1 
ATOM   723  N N     . ALA A 1 95  ? 19.223 -30.410 -16.684 1.00 35.66  ? 95  ALA A N     1 
ATOM   724  C CA    . ALA A 1 95  ? 18.198 -31.414 -16.951 1.00 36.95  ? 95  ALA A CA    1 
ATOM   725  C C     . ALA A 1 95  ? 17.935 -31.539 -18.448 1.00 35.26  ? 95  ALA A C     1 
ATOM   726  O O     . ALA A 1 95  ? 18.059 -30.583 -19.202 1.00 35.78  ? 95  ALA A O     1 
ATOM   727  C CB    . ALA A 1 95  ? 16.923 -31.081 -16.218 1.00 37.56  ? 95  ALA A CB    1 
ATOM   728  N N     . PRO A 1 96  ? 17.555 -32.736 -18.928 1.00 38.79  ? 96  PRO A N     1 
ATOM   729  C CA    . PRO A 1 96  ? 17.281 -32.940 -20.347 1.00 39.11  ? 96  PRO A CA    1 
ATOM   730  C C     . PRO A 1 96  ? 15.863 -32.577 -20.754 1.00 39.28  ? 96  PRO A C     1 
ATOM   731  O O     . PRO A 1 96  ? 14.989 -32.520 -19.910 1.00 46.18  ? 96  PRO A O     1 
ATOM   732  C CB    . PRO A 1 96  ? 17.468 -34.451 -20.501 1.00 40.50  ? 96  PRO A CB    1 
ATOM   733  C CG    . PRO A 1 96  ? 16.989 -34.999 -19.180 1.00 43.02  ? 96  PRO A CG    1 
ATOM   734  C CD    . PRO A 1 96  ? 17.446 -33.977 -18.148 1.00 41.20  ? 96  PRO A CD    1 
ATOM   735  N N     . VAL A 1 97  ? 15.653 -32.355 -22.055 1.00 38.10  ? 97  VAL A N     1 
ATOM   736  C CA    . VAL A 1 97  ? 14.321 -32.267 -22.626 1.00 37.91  ? 97  VAL A CA    1 
ATOM   737  C C     . VAL A 1 97  ? 13.570 -33.574 -22.375 1.00 36.96  ? 97  VAL A C     1 
ATOM   738  O O     . VAL A 1 97  ? 12.412 -33.538 -21.973 1.00 33.21  ? 97  VAL A O     1 
ATOM   739  C CB    . VAL A 1 97  ? 14.365 -31.944 -24.132 1.00 37.98  ? 97  VAL A CB    1 
ATOM   740  C CG1   . VAL A 1 97  ? 13.008 -32.161 -24.776 1.00 40.38  ? 97  VAL A CG1   1 
ATOM   741  C CG2   . VAL A 1 97  ? 14.885 -30.535 -24.408 1.00 36.63  ? 97  VAL A CG2   1 
ATOM   742  N N     . MET A 1 98  ? 14.219 -34.720 -22.617 1.00 38.39  ? 98  MET A N     1 
ATOM   743  C CA    . MET A 1 98  ? 13.502 -35.987 -22.568 1.00 43.49  ? 98  MET A CA    1 
ATOM   744  C C     . MET A 1 98  ? 13.881 -36.798 -21.328 1.00 40.12  ? 98  MET A C     1 
ATOM   745  O O     . MET A 1 98  ? 15.045 -37.143 -21.131 1.00 42.24  ? 98  MET A O     1 
ATOM   746  C CB    . MET A 1 98  ? 13.770 -36.819 -23.820 1.00 45.78  ? 98  MET A CB    1 
ATOM   747  C CG    . MET A 1 98  ? 12.872 -38.036 -23.922 1.00 43.69  ? 98  MET A CG    1 
ATOM   748  S SD    . MET A 1 98  ? 13.290 -39.004 -25.387 1.00 44.83  ? 98  MET A SD    1 
ATOM   749  C CE    . MET A 1 98  ? 14.829 -39.742 -24.845 1.00 42.81  ? 98  MET A CE    1 
ATOM   750  N N     . SER A 1 99  ? 12.866 -37.119 -20.512 1.00 38.99  ? 99  SER A N     1 
ATOM   751  C CA    . SER A 1 99  ? 13.017 -38.005 -19.361 1.00 34.89  ? 99  SER A CA    1 
ATOM   752  C C     . SER A 1 99  ? 13.592 -39.344 -19.806 1.00 31.65  ? 99  SER A C     1 
ATOM   753  O O     . SER A 1 99  ? 13.242 -39.864 -20.874 1.00 35.01  ? 99  SER A O     1 
ATOM   754  C CB    . SER A 1 99  ? 11.705 -38.210 -18.645 1.00 33.32  ? 99  SER A CB    1 
ATOM   755  O OG    . SER A 1 99  ? 11.288 -37.009 -17.999 1.00 31.47  ? 99  SER A OG    1 
ATOM   756  N N     . GLY A 1 100 ? 14.483 -39.889 -18.984 1.00 31.14  ? 100 GLY A N     1 
ATOM   757  C CA    . GLY A 1 100 ? 15.174 -41.118 -19.333 1.00 35.04  ? 100 GLY A CA    1 
ATOM   758  C C     . GLY A 1 100 ? 16.597 -40.882 -19.832 1.00 36.60  ? 100 GLY A C     1 
ATOM   759  O O     . GLY A 1 100 ? 17.425 -41.785 -19.761 1.00 43.16  ? 100 GLY A O     1 
ATOM   760  N N     . THR A 1 101 ? 16.869 -39.666 -20.324 1.00 36.87  ? 101 THR A N     1 
ATOM   761  C CA    . THR A 1 101 ? 18.181 -39.297 -20.822 1.00 36.51  ? 101 THR A CA    1 
ATOM   762  C C     . THR A 1 101 ? 19.178 -39.294 -19.671 1.00 34.96  ? 101 THR A C     1 
ATOM   763  O O     . THR A 1 101 ? 18.830 -38.930 -18.561 1.00 36.78  ? 101 THR A O     1 
ATOM   764  C CB    . THR A 1 101 ? 18.144 -37.925 -21.508 1.00 39.28  ? 101 THR A CB    1 
ATOM   765  O OG1   . THR A 1 101 ? 17.163 -37.937 -22.542 1.00 38.31  ? 101 THR A OG1   1 
ATOM   766  C CG2   . THR A 1 101 ? 19.471 -37.525 -22.112 1.00 43.35  ? 101 THR A CG2   1 
ATOM   767  N N     . VAL A 1 102 ? 20.418 -39.700 -19.961 1.00 35.12  ? 102 VAL A N     1 
ATOM   768  C CA    . VAL A 1 102 ? 21.493 -39.745 -18.985 1.00 32.33  ? 102 VAL A CA    1 
ATOM   769  C C     . VAL A 1 102 ? 22.340 -38.505 -19.206 1.00 32.25  ? 102 VAL A C     1 
ATOM   770  O O     . VAL A 1 102 ? 22.740 -38.265 -20.342 1.00 32.52  ? 102 VAL A O     1 
ATOM   771  C CB    . VAL A 1 102 ? 22.340 -41.016 -19.189 1.00 33.55  ? 102 VAL A CB    1 
ATOM   772  C CG1   . VAL A 1 102 ? 23.589 -41.070 -18.329 1.00 30.18  ? 102 VAL A CG1   1 
ATOM   773  C CG2   . VAL A 1 102 ? 21.505 -42.268 -19.008 1.00 35.17  ? 102 VAL A CG2   1 
ATOM   774  N N     . VAL A 1 103 ? 22.634 -37.761 -18.127 1.00 31.68  ? 103 VAL A N     1 
ATOM   775  C CA    . VAL A 1 103 ? 23.465 -36.570 -18.217 1.00 30.48  ? 103 VAL A CA    1 
ATOM   776  C C     . VAL A 1 103 ? 24.932 -36.964 -18.340 1.00 30.57  ? 103 VAL A C     1 
ATOM   777  O O     . VAL A 1 103 ? 25.452 -37.768 -17.578 1.00 30.77  ? 103 VAL A O     1 
ATOM   778  C CB    . VAL A 1 103 ? 23.249 -35.583 -17.056 1.00 29.34  ? 103 VAL A CB    1 
ATOM   779  C CG1   . VAL A 1 103 ? 24.156 -34.368 -17.193 1.00 28.10  ? 103 VAL A CG1   1 
ATOM   780  C CG2   . VAL A 1 103 ? 21.796 -35.149 -16.961 1.00 28.19  ? 103 VAL A CG2   1 
ATOM   781  N N     . LEU A 1 104 ? 25.584 -36.375 -19.345 1.00 31.78  ? 104 LEU A N     1 
ATOM   782  C CA    . LEU A 1 104 ? 27.004 -36.555 -19.551 1.00 31.06  ? 104 LEU A CA    1 
ATOM   783  C C     . LEU A 1 104 ? 27.657 -35.292 -19.033 1.00 30.75  ? 104 LEU A C     1 
ATOM   784  O O     . LEU A 1 104 ? 27.713 -34.288 -19.735 1.00 35.39  ? 104 LEU A O     1 
ATOM   785  C CB    . LEU A 1 104 ? 27.300 -36.805 -21.037 1.00 29.38  ? 104 LEU A CB    1 
ATOM   786  C CG    . LEU A 1 104 ? 28.778 -36.741 -21.442 1.00 29.78  ? 104 LEU A CG    1 
ATOM   787  C CD1   . LEU A 1 104 ? 29.645 -37.593 -20.546 1.00 29.36  ? 104 LEU A CD1   1 
ATOM   788  C CD2   . LEU A 1 104 ? 28.980 -37.164 -22.889 1.00 30.67  ? 104 LEU A CD2   1 
ATOM   789  N N     . ASP A 1 105 ? 28.109 -35.353 -17.788 1.00 31.68  ? 105 ASP A N     1 
ATOM   790  C CA    . ASP A 1 105 ? 28.563 -34.166 -17.084 1.00 33.68  ? 105 ASP A CA    1 
ATOM   791  C C     . ASP A 1 105 ? 30.087 -34.074 -17.145 1.00 31.10  ? 105 ASP A C     1 
ATOM   792  O O     . ASP A 1 105 ? 30.787 -34.919 -16.602 1.00 35.54  ? 105 ASP A O     1 
ATOM   793  C CB    . ASP A 1 105 ? 28.035 -34.213 -15.651 1.00 36.20  ? 105 ASP A CB    1 
ATOM   794  C CG    . ASP A 1 105 ? 28.544 -33.107 -14.750 1.00 38.01  ? 105 ASP A CG    1 
ATOM   795  O OD1   . ASP A 1 105 ? 29.253 -32.210 -15.248 1.00 40.85  ? 105 ASP A OD1   1 
ATOM   796  O OD2   . ASP A 1 105 ? 28.257 -33.186 -13.548 1.00 41.91  ? 105 ASP A OD2   1 
ATOM   797  N N     . MET A 1 106 ? 30.613 -33.014 -17.750 1.00 30.23  ? 106 MET A N     1 
ATOM   798  C CA    . MET A 1 106 ? 32.051 -32.927 -17.957 1.00 28.93  ? 106 MET A CA    1 
ATOM   799  C C     . MET A 1 106 ? 32.714 -31.932 -16.998 1.00 27.10  ? 106 MET A C     1 
ATOM   800  O O     . MET A 1 106 ? 33.784 -31.414 -17.291 1.00 28.38  ? 106 MET A O     1 
ATOM   801  C CB    . MET A 1 106 ? 32.305 -32.557 -19.416 1.00 30.51  ? 106 MET A CB    1 
ATOM   802  C CG    . MET A 1 106 ? 32.003 -33.722 -20.347 1.00 32.60  ? 106 MET A CG    1 
ATOM   803  S SD    . MET A 1 106 ? 32.218 -33.330 -22.105 1.00 35.50  ? 106 MET A SD    1 
ATOM   804  C CE    . MET A 1 106 ? 30.844 -32.205 -22.336 1.00 36.53  ? 106 MET A CE    1 
ATOM   805  N N     . ASN A 1 107 ? 32.113 -31.717 -15.821 1.00 28.86  ? 107 ASN A N     1 
ATOM   806  C CA    . ASN A 1 107 ? 32.666 -30.857 -14.777 1.00 32.43  ? 107 ASN A CA    1 
ATOM   807  C C     . ASN A 1 107 ? 34.138 -31.146 -14.484 1.00 31.27  ? 107 ASN A C     1 
ATOM   808  O O     . ASN A 1 107 ? 34.929 -30.226 -14.289 1.00 30.32  ? 107 ASN A O     1 
ATOM   809  C CB    . ASN A 1 107 ? 31.913 -31.014 -13.452 1.00 39.24  ? 107 ASN A CB    1 
ATOM   810  C CG    . ASN A 1 107 ? 30.885 -29.925 -13.282 1.00 50.05  ? 107 ASN A CG    1 
ATOM   811  O OD1   . ASN A 1 107 ? 29.732 -30.071 -13.687 1.00 63.15  ? 107 ASN A OD1   1 
ATOM   812  N ND2   . ASN A 1 107 ? 31.314 -28.799 -12.741 1.00 60.64  ? 107 ASN A ND2   1 
ATOM   813  N N     . ARG A 1 108 ? 34.495 -32.429 -14.396 1.00 30.69  ? 108 ARG A N     1 
ATOM   814  C CA    . ARG A 1 108 ? 35.814 -32.818 -13.919 1.00 31.06  ? 108 ARG A CA    1 
ATOM   815  C C     . ARG A 1 108 ? 36.877 -32.629 -14.996 1.00 30.20  ? 108 ARG A C     1 
ATOM   816  O O     . ARG A 1 108 ? 38.056 -32.595 -14.674 1.00 28.05  ? 108 ARG A O     1 
ATOM   817  C CB    . ARG A 1 108 ? 35.808 -34.276 -13.475 1.00 33.42  ? 108 ARG A CB    1 
ATOM   818  C CG    . ARG A 1 108 ? 34.762 -34.585 -12.414 1.00 35.10  ? 108 ARG A CG    1 
ATOM   819  C CD    . ARG A 1 108 ? 34.570 -36.091 -12.350 1.00 37.47  ? 108 ARG A CD    1 
ATOM   820  N NE    . ARG A 1 108 ? 35.801 -36.703 -11.862 1.00 37.99  ? 108 ARG A NE    1 
ATOM   821  C CZ    . ARG A 1 108 ? 36.437 -37.715 -12.434 1.00 34.79  ? 108 ARG A CZ    1 
ATOM   822  N NH1   . ARG A 1 108 ? 35.828 -38.502 -13.304 1.00 32.79  ? 108 ARG A NH1   1 
ATOM   823  N NH2   . ARG A 1 108 ? 37.671 -37.978 -12.056 1.00 37.19  ? 108 ARG A NH2   1 
ATOM   824  N N     . MET A 1 109 ? 36.469 -32.502 -16.267 1.00 30.34  ? 109 MET A N     1 
ATOM   825  C CA    . MET A 1 109 ? 37.384 -32.077 -17.316 1.00 30.63  ? 109 MET A CA    1 
ATOM   826  C C     . MET A 1 109 ? 37.548 -30.558 -17.224 1.00 29.65  ? 109 MET A C     1 
ATOM   827  O O     . MET A 1 109 ? 36.884 -29.798 -17.911 1.00 31.33  ? 109 MET A O     1 
ATOM   828  C CB    . MET A 1 109 ? 36.864 -32.505 -18.688 1.00 30.44  ? 109 MET A CB    1 
ATOM   829  C CG    . MET A 1 109 ? 36.839 -34.016 -18.823 1.00 30.06  ? 109 MET A CG    1 
ATOM   830  S SD    . MET A 1 109 ? 35.872 -34.588 -20.229 1.00 32.52  ? 109 MET A SD    1 
ATOM   831  C CE    . MET A 1 109 ? 37.007 -34.201 -21.559 1.00 34.53  ? 109 MET A CE    1 
ATOM   832  N N     . ASN A 1 110 ? 38.427 -30.119 -16.328 1.00 30.61  ? 110 ASN A N     1 
ATOM   833  C CA    . ASN A 1 110 ? 38.517 -28.713 -15.970 1.00 33.81  ? 110 ASN A CA    1 
ATOM   834  C C     . ASN A 1 110 ? 39.938 -28.200 -16.121 1.00 31.22  ? 110 ASN A C     1 
ATOM   835  O O     . ASN A 1 110 ? 40.316 -27.320 -15.363 1.00 31.69  ? 110 ASN A O     1 
ATOM   836  C CB    . ASN A 1 110 ? 38.094 -28.469 -14.519 1.00 35.72  ? 110 ASN A CB    1 
ATOM   837  C CG    . ASN A 1 110 ? 38.937 -29.236 -13.515 1.00 36.47  ? 110 ASN A CG    1 
ATOM   838  O OD1   . ASN A 1 110 ? 39.739 -30.101 -13.866 1.00 37.65  ? 110 ASN A OD1   1 
ATOM   839  N ND2   . ASN A 1 110 ? 38.753 -28.932 -12.251 1.00 34.12  ? 110 ASN A ND2   1 
ATOM   840  N N     . ARG A 1 111 ? 40.706 -28.758 -17.068 1.00 34.43  ? 111 ARG A N     1 
ATOM   841  C CA    . ARG A 1 111 ? 42.063 -28.299 -17.331 1.00 37.59  ? 111 ARG A CA    1 
ATOM   842  C C     . ARG A 1 111 ? 42.016 -26.997 -18.128 1.00 34.47  ? 111 ARG A C     1 
ATOM   843  O O     . ARG A 1 111 ? 41.363 -26.907 -19.159 1.00 31.20  ? 111 ARG A O     1 
ATOM   844  C CB    . ARG A 1 111 ? 42.883 -29.314 -18.144 1.00 46.05  ? 111 ARG A CB    1 
ATOM   845  C CG    . ARG A 1 111 ? 43.665 -30.331 -17.329 1.00 57.21  ? 111 ARG A CG    1 
ATOM   846  C CD    . ARG A 1 111 ? 42.856 -31.563 -16.971 1.00 68.84  ? 111 ARG A CD    1 
ATOM   847  N NE    . ARG A 1 111 ? 42.888 -32.595 -18.003 1.00 72.89  ? 111 ARG A NE    1 
ATOM   848  C CZ    . ARG A 1 111 ? 42.051 -33.629 -18.060 1.00 75.60  ? 111 ARG A CZ    1 
ATOM   849  N NH1   . ARG A 1 111 ? 41.051 -33.721 -17.199 1.00 66.15  ? 111 ARG A NH1   1 
ATOM   850  N NH2   . ARG A 1 111 ? 42.195 -34.549 -19.002 1.00 79.25  ? 111 ARG A NH2   1 
ATOM   851  N N     . ILE A 1 112 ? 42.744 -25.994 -17.653 1.00 31.99  ? 112 ILE A N     1 
ATOM   852  C CA    . ILE A 1 112 ? 43.106 -24.877 -18.498 1.00 32.10  ? 112 ILE A CA    1 
ATOM   853  C C     . ILE A 1 112 ? 44.335 -25.288 -19.305 1.00 30.52  ? 112 ILE A C     1 
ATOM   854  O O     . ILE A 1 112 ? 45.419 -25.341 -18.765 1.00 30.14  ? 112 ILE A O     1 
ATOM   855  C CB    . ILE A 1 112 ? 43.338 -23.632 -17.623 1.00 30.46  ? 112 ILE A CB    1 
ATOM   856  C CG1   . ILE A 1 112 ? 42.076 -23.320 -16.805 1.00 32.00  ? 112 ILE A CG1   1 
ATOM   857  C CG2   . ILE A 1 112 ? 43.780 -22.458 -18.480 1.00 29.21  ? 112 ILE A CG2   1 
ATOM   858  C CD1   . ILE A 1 112 ? 42.247 -22.283 -15.708 1.00 34.51  ? 112 ILE A CD1   1 
ATOM   859  N N     . LEU A 1 113 ? 44.154 -25.615 -20.587 1.00 29.49  ? 113 LEU A N     1 
ATOM   860  C CA    . LEU A 1 113 ? 45.217 -26.176 -21.406 1.00 28.15  ? 113 LEU A CA    1 
ATOM   861  C C     . LEU A 1 113 ? 46.232 -25.116 -21.827 1.00 28.36  ? 113 LEU A C     1 
ATOM   862  O O     . LEU A 1 113 ? 47.403 -25.441 -21.963 1.00 27.29  ? 113 LEU A O     1 
ATOM   863  C CB    . LEU A 1 113 ? 44.578 -26.843 -22.626 1.00 30.02  ? 113 LEU A CB    1 
ATOM   864  C CG    . LEU A 1 113 ? 43.677 -28.033 -22.287 1.00 33.63  ? 113 LEU A CG    1 
ATOM   865  C CD1   . LEU A 1 113 ? 42.880 -28.477 -23.492 1.00 35.25  ? 113 LEU A CD1   1 
ATOM   866  C CD2   . LEU A 1 113 ? 44.502 -29.197 -21.751 1.00 33.93  ? 113 LEU A CD2   1 
ATOM   867  N N     . GLU A 1 114 ? 45.791 -23.875 -22.086 1.00 28.02  ? 114 GLU A N     1 
ATOM   868  C CA    . GLU A 1 114 ? 46.706 -22.789 -22.409 1.00 27.80  ? 114 GLU A CA    1 
ATOM   869  C C     . GLU A 1 114 ? 46.028 -21.442 -22.183 1.00 26.71  ? 114 GLU A C     1 
ATOM   870  O O     . GLU A 1 114 ? 44.900 -21.225 -22.595 1.00 26.49  ? 114 GLU A O     1 
ATOM   871  C CB    . GLU A 1 114 ? 47.194 -22.888 -23.864 1.00 31.92  ? 114 GLU A CB    1 
ATOM   872  C CG    . GLU A 1 114 ? 48.321 -21.916 -24.148 1.00 35.85  ? 114 GLU A CG    1 
ATOM   873  C CD    . GLU A 1 114 ? 48.894 -21.851 -25.555 1.00 39.40  ? 114 GLU A CD    1 
ATOM   874  O OE1   . GLU A 1 114 ? 48.290 -22.424 -26.503 1.00 37.52  ? 114 GLU A OE1   1 
ATOM   875  O OE2   . GLU A 1 114 ? 49.955 -21.191 -25.698 1.00 40.22  ? 114 GLU A OE2   1 
ATOM   876  N N     . VAL A 1 115 ? 46.719 -20.529 -21.505 1.00 28.77  ? 115 VAL A N     1 
ATOM   877  C CA    . VAL A 1 115 ? 46.388 -19.122 -21.596 1.00 28.88  ? 115 VAL A CA    1 
ATOM   878  C C     . VAL A 1 115 ? 47.586 -18.413 -22.203 1.00 28.68  ? 115 VAL A C     1 
ATOM   879  O O     . VAL A 1 115 ? 48.689 -18.488 -21.702 1.00 34.65  ? 115 VAL A O     1 
ATOM   880  C CB    . VAL A 1 115 ? 45.992 -18.505 -20.251 1.00 31.24  ? 115 VAL A CB    1 
ATOM   881  C CG1   . VAL A 1 115 ? 45.588 -17.046 -20.418 1.00 33.46  ? 115 VAL A CG1   1 
ATOM   882  C CG2   . VAL A 1 115 ? 44.885 -19.291 -19.576 1.00 32.39  ? 115 VAL A CG2   1 
ATOM   883  N N     . ASN A 1 116 ? 47.351 -17.700 -23.294 1.00 28.26  ? 116 ASN A N     1 
ATOM   884  C CA    . ASN A 1 116 ? 48.416 -17.072 -24.041 1.00 25.62  ? 116 ASN A CA    1 
ATOM   885  C C     . ASN A 1 116 ? 48.198 -15.572 -24.009 1.00 25.22  ? 116 ASN A C     1 
ATOM   886  O O     . ASN A 1 116 ? 47.219 -15.083 -24.562 1.00 28.30  ? 116 ASN A O     1 
ATOM   887  C CB    . ASN A 1 116 ? 48.388 -17.559 -25.483 1.00 25.83  ? 116 ASN A CB    1 
ATOM   888  C CG    . ASN A 1 116 ? 49.592 -17.111 -26.260 1.00 25.82  ? 116 ASN A CG    1 
ATOM   889  O OD1   . ASN A 1 116 ? 49.873 -15.921 -26.368 1.00 24.50  ? 116 ASN A OD1   1 
ATOM   890  N ND2   . ASN A 1 116 ? 50.311 -18.079 -26.793 1.00 29.04  ? 116 ASN A ND2   1 
ATOM   891  N N     . GLU A 1 117 ? 49.152 -14.854 -23.435 1.00 25.49  ? 117 GLU A N     1 
ATOM   892  C CA    . GLU A 1 117 ? 49.005 -13.432 -23.202 1.00 26.64  ? 117 GLU A CA    1 
ATOM   893  C C     . GLU A 1 117 ? 49.317 -12.648 -24.475 1.00 25.63  ? 117 GLU A C     1 
ATOM   894  O O     . GLU A 1 117 ? 48.579 -11.732 -24.809 1.00 25.85  ? 117 GLU A O     1 
ATOM   895  C CB    . GLU A 1 117 ? 49.902 -12.996 -22.036 1.00 28.39  ? 117 GLU A CB    1 
ATOM   896  C CG    . GLU A 1 117 ? 49.821 -11.515 -21.708 1.00 29.56  ? 117 GLU A CG    1 
ATOM   897  C CD    . GLU A 1 117 ? 50.691 -11.113 -20.533 1.00 31.98  ? 117 GLU A CD    1 
ATOM   898  O OE1   . GLU A 1 117 ? 51.913 -11.184 -20.664 1.00 32.91  ? 117 GLU A OE1   1 
ATOM   899  O OE2   . GLU A 1 117 ? 50.133 -10.736 -19.499 1.00 35.39  ? 117 GLU A OE2   1 
ATOM   900  N N     . GLU A 1 118 ? 50.425 -12.958 -25.149 1.00 26.94  ? 118 GLU A N     1 
ATOM   901  C CA    . GLU A 1 118 ? 50.824 -12.169 -26.305 1.00 29.04  ? 118 GLU A CA    1 
ATOM   902  C C     . GLU A 1 118 ? 49.767 -12.261 -27.418 1.00 29.93  ? 118 GLU A C     1 
ATOM   903  O O     . GLU A 1 118 ? 49.590 -11.280 -28.138 1.00 31.11  ? 118 GLU A O     1 
ATOM   904  C CB    . GLU A 1 118 ? 52.250 -12.503 -26.755 1.00 33.03  ? 118 GLU A CB    1 
ATOM   905  C CG    . GLU A 1 118 ? 52.510 -13.986 -27.016 1.00 43.27  ? 118 GLU A CG    1 
ATOM   906  C CD    . GLU A 1 118 ? 53.869 -14.327 -27.624 1.00 48.76  ? 118 GLU A CD    1 
ATOM   907  O OE1   . GLU A 1 118 ? 54.135 -15.523 -27.862 1.00 52.15  ? 118 GLU A OE1   1 
ATOM   908  O OE2   . GLU A 1 118 ? 54.663 -13.406 -27.853 1.00 51.59  ? 118 GLU A OE2   1 
ATOM   909  N N     . PHE A 1 119 ? 49.004 -13.369 -27.528 1.00 28.13  ? 119 PHE A N     1 
ATOM   910  C CA    . PHE A 1 119 ? 47.996 -13.487 -28.582 1.00 27.79  ? 119 PHE A CA    1 
ATOM   911  C C     . PHE A 1 119 ? 46.579 -13.381 -28.030 1.00 25.97  ? 119 PHE A C     1 
ATOM   912  O O     . PHE A 1 119 ? 45.612 -13.481 -28.771 1.00 26.63  ? 119 PHE A O     1 
ATOM   913  C CB    . PHE A 1 119 ? 48.142 -14.811 -29.335 1.00 28.16  ? 119 PHE A CB    1 
ATOM   914  C CG    . PHE A 1 119 ? 49.458 -14.959 -30.041 1.00 31.03  ? 119 PHE A CG    1 
ATOM   915  C CD1   . PHE A 1 119 ? 49.824 -14.063 -31.028 1.00 34.71  ? 119 PHE A CD1   1 
ATOM   916  C CD2   . PHE A 1 119 ? 50.312 -16.010 -29.754 1.00 36.19  ? 119 PHE A CD2   1 
ATOM   917  C CE1   . PHE A 1 119 ? 51.027 -14.204 -31.696 1.00 32.83  ? 119 PHE A CE1   1 
ATOM   918  C CE2   . PHE A 1 119 ? 51.518 -16.153 -30.427 1.00 34.36  ? 119 PHE A CE2   1 
ATOM   919  C CZ    . PHE A 1 119 ? 51.884 -15.228 -31.368 1.00 33.67  ? 119 PHE A CZ    1 
ATOM   920  N N     . GLY A 1 120 ? 46.450 -13.239 -26.716 1.00 25.36  ? 120 GLY A N     1 
ATOM   921  C CA    . GLY A 1 120 ? 45.156 -13.035 -26.088 1.00 23.25  ? 120 GLY A CA    1 
ATOM   922  C C     . GLY A 1 120 ? 44.186 -14.186 -26.313 1.00 21.63  ? 120 GLY A C     1 
ATOM   923  O O     . GLY A 1 120 ? 43.146 -13.997 -26.932 1.00 20.38  ? 120 GLY A O     1 
ATOM   924  N N     . TYR A 1 121 ? 44.500 -15.371 -25.783 1.00 22.71  ? 121 TYR A N     1 
ATOM   925  C CA    . TYR A 1 121 ? 43.551 -16.463 -25.902 1.00 23.75  ? 121 TYR A CA    1 
ATOM   926  C C     . TYR A 1 121 ? 43.712 -17.471 -24.774 1.00 24.50  ? 121 TYR A C     1 
ATOM   927  O O     . TYR A 1 121 ? 44.701 -17.469 -24.053 1.00 25.99  ? 121 TYR A O     1 
ATOM   928  C CB    . TYR A 1 121 ? 43.650 -17.124 -27.279 1.00 24.06  ? 121 TYR A CB    1 
ATOM   929  C CG    . TYR A 1 121 ? 44.858 -17.990 -27.540 1.00 23.06  ? 121 TYR A CG    1 
ATOM   930  C CD1   . TYR A 1 121 ? 44.961 -19.255 -27.003 1.00 21.38  ? 121 TYR A CD1   1 
ATOM   931  C CD2   . TYR A 1 121 ? 45.891 -17.557 -28.347 1.00 24.56  ? 121 TYR A CD2   1 
ATOM   932  C CE1   . TYR A 1 121 ? 46.041 -20.072 -27.269 1.00 21.19  ? 121 TYR A CE1   1 
ATOM   933  C CE2   . TYR A 1 121 ? 46.982 -18.364 -28.624 1.00 24.30  ? 121 TYR A CE2   1 
ATOM   934  C CZ    . TYR A 1 121 ? 47.054 -19.633 -28.088 1.00 22.56  ? 121 TYR A CZ    1 
ATOM   935  O OH    . TYR A 1 121 ? 48.137 -20.454 -28.325 1.00 23.72  ? 121 TYR A OH    1 
ATOM   936  N N     . ALA A 1 122 ? 42.684 -18.306 -24.638 1.00 25.60  ? 122 ALA A N     1 
ATOM   937  C CA    . ALA A 1 122 ? 42.709 -19.463 -23.766 1.00 28.70  ? 122 ALA A CA    1 
ATOM   938  C C     . ALA A 1 122 ? 42.191 -20.680 -24.526 1.00 27.13  ? 122 ALA A C     1 
ATOM   939  O O     . ALA A 1 122 ? 41.317 -20.570 -25.379 1.00 24.07  ? 122 ALA A O     1 
ATOM   940  C CB    . ALA A 1 122 ? 41.871 -19.232 -22.533 1.00 28.84  ? 122 ALA A CB    1 
ATOM   941  N N     . LEU A 1 123 ? 42.725 -21.842 -24.152 1.00 26.69  ? 123 LEU A N     1 
ATOM   942  C CA    . LEU A 1 123 ? 42.201 -23.116 -24.590 1.00 26.07  ? 123 LEU A CA    1 
ATOM   943  C C     . LEU A 1 123 ? 41.770 -23.911 -23.354 1.00 26.39  ? 123 LEU A C     1 
ATOM   944  O O     . LEU A 1 123 ? 42.587 -24.208 -22.488 1.00 29.43  ? 123 LEU A O     1 
ATOM   945  C CB    . LEU A 1 123 ? 43.289 -23.815 -25.408 1.00 24.87  ? 123 LEU A CB    1 
ATOM   946  C CG    . LEU A 1 123 ? 42.950 -25.252 -25.789 1.00 25.28  ? 123 LEU A CG    1 
ATOM   947  C CD1   . LEU A 1 123 ? 41.800 -25.266 -26.786 1.00 23.97  ? 123 LEU A CD1   1 
ATOM   948  C CD2   . LEU A 1 123 ? 44.182 -25.981 -26.330 1.00 25.91  ? 123 LEU A CD2   1 
ATOM   949  N N     . VAL A 1 124 ? 40.483 -24.257 -23.287 1.00 25.10  ? 124 VAL A N     1 
ATOM   950  C CA    . VAL A 1 124 ? 39.891 -24.746 -22.055 1.00 27.67  ? 124 VAL A CA    1 
ATOM   951  C C     . VAL A 1 124 ? 39.071 -26.002 -22.343 1.00 29.14  ? 124 VAL A C     1 
ATOM   952  O O     . VAL A 1 124 ? 38.595 -26.206 -23.459 1.00 28.71  ? 124 VAL A O     1 
ATOM   953  C CB    . VAL A 1 124 ? 39.006 -23.673 -21.388 1.00 26.25  ? 124 VAL A CB    1 
ATOM   954  C CG1   . VAL A 1 124 ? 39.805 -22.465 -20.930 1.00 25.87  ? 124 VAL A CG1   1 
ATOM   955  C CG2   . VAL A 1 124 ? 37.888 -23.240 -22.312 1.00 27.17  ? 124 VAL A CG2   1 
ATOM   956  N N     . GLU A 1 125 ? 38.959 -26.837 -21.304 1.00 29.55  ? 125 GLU A N     1 
ATOM   957  C CA    . GLU A 1 125 ? 38.032 -27.949 -21.256 1.00 28.38  ? 125 GLU A CA    1 
ATOM   958  C C     . GLU A 1 125 ? 36.696 -27.432 -20.745 1.00 25.60  ? 125 GLU A C     1 
ATOM   959  O O     . GLU A 1 125 ? 36.591 -26.328 -20.208 1.00 23.97  ? 125 GLU A O     1 
ATOM   960  C CB    . GLU A 1 125 ? 38.567 -29.063 -20.351 1.00 30.20  ? 125 GLU A CB    1 
ATOM   961  C CG    . GLU A 1 125 ? 39.901 -29.637 -20.806 1.00 32.94  ? 125 GLU A CG    1 
ATOM   962  C CD    . GLU A 1 125 ? 40.322 -30.934 -20.135 1.00 33.91  ? 125 GLU A CD    1 
ATOM   963  O OE1   . GLU A 1 125 ? 40.166 -31.043 -18.897 1.00 33.83  ? 125 GLU A OE1   1 
ATOM   964  O OE2   . GLU A 1 125 ? 40.815 -31.832 -20.852 1.00 38.44  ? 125 GLU A OE2   1 
ATOM   965  N N     . PRO A 1 126 ? 35.623 -28.228 -20.903 1.00 26.06  ? 126 PRO A N     1 
ATOM   966  C CA    . PRO A 1 126 ? 34.279 -27.787 -20.543 1.00 27.71  ? 126 PRO A CA    1 
ATOM   967  C C     . PRO A 1 126 ? 34.041 -27.423 -19.077 1.00 27.79  ? 126 PRO A C     1 
ATOM   968  O O     . PRO A 1 126 ? 33.213 -26.565 -18.799 1.00 33.61  ? 126 PRO A O     1 
ATOM   969  C CB    . PRO A 1 126 ? 33.441 -28.999 -20.936 1.00 26.32  ? 126 PRO A CB    1 
ATOM   970  C CG    . PRO A 1 126 ? 34.242 -29.619 -22.027 1.00 27.09  ? 126 PRO A CG    1 
ATOM   971  C CD    . PRO A 1 126 ? 35.638 -29.574 -21.480 1.00 25.98  ? 126 PRO A CD    1 
ATOM   972  N N     . GLY A 1 127 ? 34.773 -28.055 -18.161 1.00 27.56  ? 127 GLY A N     1 
ATOM   973  C CA    . GLY A 1 127 ? 34.578 -27.874 -16.729 1.00 27.15  ? 127 GLY A CA    1 
ATOM   974  C C     . GLY A 1 127 ? 35.243 -26.619 -16.168 1.00 26.10  ? 127 GLY A C     1 
ATOM   975  O O     . GLY A 1 127 ? 35.045 -26.280 -15.007 1.00 28.28  ? 127 GLY A O     1 
ATOM   976  N N     . VAL A 1 128 ? 36.045 -25.928 -16.979 1.00 26.44  ? 128 VAL A N     1 
ATOM   977  C CA    . VAL A 1 128 ? 36.656 -24.691 -16.533 1.00 25.68  ? 128 VAL A CA    1 
ATOM   978  C C     . VAL A 1 128 ? 35.574 -23.638 -16.353 1.00 28.18  ? 128 VAL A C     1 
ATOM   979  O O     . VAL A 1 128 ? 34.809 -23.354 -17.267 1.00 27.98  ? 128 VAL A O     1 
ATOM   980  C CB    . VAL A 1 128 ? 37.725 -24.196 -17.513 1.00 28.47  ? 128 VAL A CB    1 
ATOM   981  C CG1   . VAL A 1 128 ? 38.243 -22.828 -17.083 1.00 27.87  ? 128 VAL A CG1   1 
ATOM   982  C CG2   . VAL A 1 128 ? 38.866 -25.212 -17.672 1.00 27.91  ? 128 VAL A CG2   1 
ATOM   983  N N     . SER A 1 129 ? 35.497 -23.083 -15.142 1.00 30.86  ? 129 SER A N     1 
ATOM   984  C CA    . SER A 1 129 ? 34.499 -22.079 -14.828 1.00 28.09  ? 129 SER A CA    1 
ATOM   985  C C     . SER A 1 129 ? 35.108 -20.701 -15.056 1.00 26.73  ? 129 SER A C     1 
ATOM   986  O O     . SER A 1 129 ? 36.338 -20.566 -15.125 1.00 24.87  ? 129 SER A O     1 
ATOM   987  C CB    . SER A 1 129 ? 34.031 -22.229 -13.408 1.00 27.96  ? 129 SER A CB    1 
ATOM   988  O OG    . SER A 1 129 ? 35.007 -21.689 -12.528 1.00 27.53  ? 129 SER A OG    1 
ATOM   989  N N     . TYR A 1 130 ? 34.239 -19.683 -15.105 1.00 25.67  ? 130 TYR A N     1 
ATOM   990  C CA    . TYR A 1 130 ? 34.703 -18.300 -15.130 1.00 26.51  ? 130 TYR A CA    1 
ATOM   991  C C     . TYR A 1 130 ? 35.548 -17.973 -13.887 1.00 27.23  ? 130 TYR A C     1 
ATOM   992  O O     . TYR A 1 130 ? 36.601 -17.353 -14.006 1.00 27.89  ? 130 TYR A O     1 
ATOM   993  C CB    . TYR A 1 130 ? 33.512 -17.350 -15.303 1.00 26.34  ? 130 TYR A CB    1 
ATOM   994  C CG    . TYR A 1 130 ? 32.805 -17.488 -16.624 1.00 25.39  ? 130 TYR A CG    1 
ATOM   995  C CD1   . TYR A 1 130 ? 33.349 -16.974 -17.798 1.00 26.38  ? 130 TYR A CD1   1 
ATOM   996  C CD2   . TYR A 1 130 ? 31.613 -18.181 -16.710 1.00 26.02  ? 130 TYR A CD2   1 
ATOM   997  C CE1   . TYR A 1 130 ? 32.710 -17.128 -19.022 1.00 25.37  ? 130 TYR A CE1   1 
ATOM   998  C CE2   . TYR A 1 130 ? 30.964 -18.350 -17.926 1.00 27.76  ? 130 TYR A CE2   1 
ATOM   999  C CZ    . TYR A 1 130 ? 31.518 -17.829 -19.085 1.00 25.60  ? 130 TYR A CZ    1 
ATOM   1000 O OH    . TYR A 1 130 ? 30.827 -17.991 -20.246 1.00 26.79  ? 130 TYR A OH    1 
ATOM   1001 N N     . PHE A 1 131 ? 35.107 -18.372 -12.687 1.00 27.30  ? 131 PHE A N     1 
ATOM   1002 C CA    . PHE A 1 131 ? 35.933 -18.204 -11.495 1.00 28.17  ? 131 PHE A CA    1 
ATOM   1003 C C     . PHE A 1 131 ? 37.326 -18.801 -11.718 1.00 27.86  ? 131 PHE A C     1 
ATOM   1004 O O     . PHE A 1 131 ? 38.329 -18.105 -11.526 1.00 24.06  ? 131 PHE A O     1 
ATOM   1005 C CB    . PHE A 1 131 ? 35.276 -18.821 -10.253 1.00 29.85  ? 131 PHE A CB    1 
ATOM   1006 C CG    . PHE A 1 131 ? 34.140 -18.024 -9.655  1.00 30.92  ? 131 PHE A CG    1 
ATOM   1007 C CD1   . PHE A 1 131 ? 34.316 -16.699 -9.274  1.00 33.17  ? 131 PHE A CD1   1 
ATOM   1008 C CD2   . PHE A 1 131 ? 32.887 -18.593 -9.485  1.00 33.29  ? 131 PHE A CD2   1 
ATOM   1009 C CE1   . PHE A 1 131 ? 33.265 -15.959 -8.747  1.00 31.31  ? 131 PHE A CE1   1 
ATOM   1010 C CE2   . PHE A 1 131 ? 31.836 -17.854 -8.964  1.00 33.25  ? 131 PHE A CE2   1 
ATOM   1011 C CZ    . PHE A 1 131 ? 32.032 -16.544 -8.586  1.00 32.59  ? 131 PHE A CZ    1 
ATOM   1012 N N     . GLU A 1 132 ? 37.400 -20.058 -12.188 1.00 28.41  ? 132 GLU A N     1 
ATOM   1013 C CA    . GLU A 1 132 ? 38.693 -20.722 -12.331 1.00 29.46  ? 132 GLU A CA    1 
ATOM   1014 C C     . GLU A 1 132 ? 39.592 -19.984 -13.321 1.00 28.06  ? 132 GLU A C     1 
ATOM   1015 O O     . GLU A 1 132 ? 40.767 -19.770 -13.038 1.00 29.25  ? 132 GLU A O     1 
ATOM   1016 C CB    . GLU A 1 132 ? 38.568 -22.175 -12.781 1.00 33.63  ? 132 GLU A CB    1 
ATOM   1017 C CG    . GLU A 1 132 ? 37.891 -23.107 -11.783 1.00 39.82  ? 132 GLU A CG    1 
ATOM   1018 C CD    . GLU A 1 132 ? 37.556 -24.476 -12.373 1.00 48.05  ? 132 GLU A CD    1 
ATOM   1019 O OE1   . GLU A 1 132 ? 38.241 -24.867 -13.396 1.00 44.76  ? 132 GLU A OE1   1 
ATOM   1020 O OE2   . GLU A 1 132 ? 36.596 -25.137 -11.855 1.00 44.47  ? 132 GLU A OE2   1 
ATOM   1021 N N     . LEU A 1 133 ? 39.053 -19.594 -14.482 1.00 29.19  ? 133 LEU A N     1 
ATOM   1022 C CA    . LEU A 1 133 ? 39.862 -18.941 -15.500 1.00 26.77  ? 133 LEU A CA    1 
ATOM   1023 C C     . LEU A 1 133 ? 40.352 -17.590 -14.988 1.00 26.70  ? 133 LEU A C     1 
ATOM   1024 O O     . LEU A 1 133 ? 41.510 -17.230 -15.185 1.00 25.61  ? 133 LEU A O     1 
ATOM   1025 C CB    . LEU A 1 133 ? 39.065 -18.782 -16.802 1.00 26.68  ? 133 LEU A CB    1 
ATOM   1026 C CG    . LEU A 1 133 ? 39.811 -18.145 -17.984 1.00 25.53  ? 133 LEU A CG    1 
ATOM   1027 C CD1   . LEU A 1 133 ? 41.158 -18.820 -18.233 1.00 28.43  ? 133 LEU A CD1   1 
ATOM   1028 C CD2   . LEU A 1 133 ? 38.989 -18.224 -19.257 1.00 25.74  ? 133 LEU A CD2   1 
ATOM   1029 N N     . TYR A 1 134 ? 39.454 -16.833 -14.354 1.00 27.35  ? 134 TYR A N     1 
ATOM   1030 C CA    . TYR A 1 134 ? 39.817 -15.537 -13.809 1.00 27.82  ? 134 TYR A CA    1 
ATOM   1031 C C     . TYR A 1 134 ? 40.942 -15.705 -12.796 1.00 27.65  ? 134 TYR A C     1 
ATOM   1032 O O     . TYR A 1 134 ? 41.944 -14.988 -12.853 1.00 29.83  ? 134 TYR A O     1 
ATOM   1033 C CB    . TYR A 1 134 ? 38.601 -14.869 -13.160 1.00 29.85  ? 134 TYR A CB    1 
ATOM   1034 C CG    . TYR A 1 134 ? 38.868 -13.531 -12.515 1.00 32.44  ? 134 TYR A CG    1 
ATOM   1035 C CD1   . TYR A 1 134 ? 38.964 -12.374 -13.281 1.00 35.17  ? 134 TYR A CD1   1 
ATOM   1036 C CD2   . TYR A 1 134 ? 39.009 -13.410 -11.140 1.00 33.14  ? 134 TYR A CD2   1 
ATOM   1037 C CE1   . TYR A 1 134 ? 39.198 -11.137 -12.705 1.00 33.53  ? 134 TYR A CE1   1 
ATOM   1038 C CE2   . TYR A 1 134 ? 39.232 -12.177 -10.544 1.00 33.33  ? 134 TYR A CE2   1 
ATOM   1039 C CZ    . TYR A 1 134 ? 39.332 -11.043 -11.329 1.00 35.35  ? 134 TYR A CZ    1 
ATOM   1040 O OH    . TYR A 1 134 ? 39.542 -9.827  -10.759 1.00 34.42  ? 134 TYR A OH    1 
ATOM   1041 N N     . ASP A 1 135 ? 40.752 -16.644 -11.865 1.00 27.57  ? 135 ASP A N     1 
ATOM   1042 C CA    . ASP A 1 135 ? 41.691 -16.829 -10.768 1.00 32.05  ? 135 ASP A CA    1 
ATOM   1043 C C     . ASP A 1 135 ? 43.053 -17.178 -11.351 1.00 32.02  ? 135 ASP A C     1 
ATOM   1044 O O     . ASP A 1 135 ? 44.044 -16.552 -10.976 1.00 31.94  ? 135 ASP A O     1 
ATOM   1045 C CB    . ASP A 1 135 ? 41.216 -17.875 -9.744  1.00 33.88  ? 135 ASP A CB    1 
ATOM   1046 C CG    . ASP A 1 135 ? 40.113 -17.399 -8.807  1.00 36.76  ? 135 ASP A CG    1 
ATOM   1047 O OD1   . ASP A 1 135 ? 39.770 -16.188 -8.832  1.00 45.08  ? 135 ASP A OD1   1 
ATOM   1048 O OD2   . ASP A 1 135 ? 39.583 -18.237 -8.064  1.00 41.58  ? 135 ASP A OD2   1 
ATOM   1049 N N     . TYR A 1 136 ? 43.072 -18.123 -12.307 1.00 31.54  ? 136 TYR A N     1 
ATOM   1050 C CA    . TYR A 1 136 ? 44.291 -18.518 -12.998 1.00 30.46  ? 136 TYR A CA    1 
ATOM   1051 C C     . TYR A 1 136 ? 45.061 -17.297 -13.506 1.00 31.22  ? 136 TYR A C     1 
ATOM   1052 O O     . TYR A 1 136 ? 46.238 -17.112 -13.162 1.00 28.85  ? 136 TYR A O     1 
ATOM   1053 C CB    . TYR A 1 136 ? 43.966 -19.489 -14.130 1.00 33.67  ? 136 TYR A CB    1 
ATOM   1054 C CG    . TYR A 1 136 ? 45.183 -20.012 -14.851 1.00 39.80  ? 136 TYR A CG    1 
ATOM   1055 C CD1   . TYR A 1 136 ? 45.805 -19.269 -15.844 1.00 37.49  ? 136 TYR A CD1   1 
ATOM   1056 C CD2   . TYR A 1 136 ? 45.749 -21.231 -14.498 1.00 45.67  ? 136 TYR A CD2   1 
ATOM   1057 C CE1   . TYR A 1 136 ? 46.928 -19.745 -16.499 1.00 42.35  ? 136 TYR A CE1   1 
ATOM   1058 C CE2   . TYR A 1 136 ? 46.879 -21.718 -15.137 1.00 45.85  ? 136 TYR A CE2   1 
ATOM   1059 C CZ    . TYR A 1 136 ? 47.471 -20.969 -16.139 1.00 45.94  ? 136 TYR A CZ    1 
ATOM   1060 O OH    . TYR A 1 136 ? 48.591 -21.437 -16.780 1.00 51.21  ? 136 TYR A OH    1 
ATOM   1061 N N     . ILE A 1 137 ? 44.371 -16.464 -14.304 1.00 29.20  ? 137 ILE A N     1 
ATOM   1062 C CA    . ILE A 1 137 ? 44.956 -15.278 -14.911 1.00 28.09  ? 137 ILE A CA    1 
ATOM   1063 C C     . ILE A 1 137 ? 45.521 -14.333 -13.851 1.00 31.24  ? 137 ILE A C     1 
ATOM   1064 O O     . ILE A 1 137 ? 46.600 -13.764 -14.072 1.00 32.69  ? 137 ILE A O     1 
ATOM   1065 C CB    . ILE A 1 137 ? 43.912 -14.574 -15.801 1.00 29.66  ? 137 ILE A CB    1 
ATOM   1066 C CG1   . ILE A 1 137 ? 43.738 -15.315 -17.129 1.00 30.16  ? 137 ILE A CG1   1 
ATOM   1067 C CG2   . ILE A 1 137 ? 44.241 -13.096 -16.029 1.00 31.29  ? 137 ILE A CG2   1 
ATOM   1068 C CD1   . ILE A 1 137 ? 42.485 -14.939 -17.866 1.00 31.60  ? 137 ILE A CD1   1 
ATOM   1069 N N     . GLN A 1 138 ? 44.762 -14.114 -12.757 1.00 33.73  ? 138 GLN A N     1 
ATOM   1070 C CA    . GLN A 1 138 ? 45.173 -13.217 -11.675 1.00 38.29  ? 138 GLN A CA    1 
ATOM   1071 C C     . GLN A 1 138 ? 46.412 -13.760 -10.957 1.00 34.56  ? 138 GLN A C     1 
ATOM   1072 O O     . GLN A 1 138 ? 47.339 -13.003 -10.737 1.00 33.40  ? 138 GLN A O     1 
ATOM   1073 C CB    . GLN A 1 138 ? 44.071 -12.966 -10.635 1.00 39.11  ? 138 GLN A CB    1 
ATOM   1074 C CG    . GLN A 1 138 ? 42.804 -12.314 -11.185 1.00 47.18  ? 138 GLN A CG    1 
ATOM   1075 C CD    . GLN A 1 138 ? 43.019 -11.024 -11.946 1.00 49.27  ? 138 GLN A CD    1 
ATOM   1076 O OE1   . GLN A 1 138 ? 43.516 -10.039 -11.411 1.00 51.28  ? 138 GLN A OE1   1 
ATOM   1077 N NE2   . GLN A 1 138 ? 42.620 -11.008 -13.210 1.00 53.49  ? 138 GLN A NE2   1 
ATOM   1078 N N     . GLU A 1 139 ? 46.419 -15.057 -10.624 1.00 35.50  ? 139 GLU A N     1 
ATOM   1079 C CA    . GLU A 1 139 ? 47.538 -15.734 -9.975  1.00 41.46  ? 139 GLU A CA    1 
ATOM   1080 C C     . GLU A 1 139 ? 48.828 -15.535 -10.765 1.00 39.84  ? 139 GLU A C     1 
ATOM   1081 O O     . GLU A 1 139 ? 49.878 -15.363 -10.161 1.00 40.27  ? 139 GLU A O     1 
ATOM   1082 C CB    . GLU A 1 139 ? 47.278 -17.240 -9.800  1.00 46.96  ? 139 GLU A CB    1 
ATOM   1083 C CG    . GLU A 1 139 ? 46.599 -17.587 -8.481  1.00 57.22  ? 139 GLU A CG    1 
ATOM   1084 C CD    . GLU A 1 139 ? 45.589 -18.730 -8.480  1.00 70.23  ? 139 GLU A CD    1 
ATOM   1085 O OE1   . GLU A 1 139 ? 45.842 -19.784 -9.123  1.00 72.49  ? 139 GLU A OE1   1 
ATOM   1086 O OE2   . GLU A 1 139 ? 44.545 -18.567 -7.808  1.00 72.18  ? 139 GLU A OE2   1 
ATOM   1087 N N     . LYS A 1 140 ? 48.747 -15.542 -12.102 1.00 39.26  ? 140 LYS A N     1 
ATOM   1088 C CA    . LYS A 1 140 ? 49.936 -15.450 -12.941 1.00 39.36  ? 140 LYS A CA    1 
ATOM   1089 C C     . LYS A 1 140 ? 50.176 -14.021 -13.443 1.00 35.83  ? 140 LYS A C     1 
ATOM   1090 O O     . LYS A 1 140 ? 51.146 -13.760 -14.150 1.00 31.90  ? 140 LYS A O     1 
ATOM   1091 C CB    . LYS A 1 140 ? 49.814 -16.476 -14.072 1.00 43.62  ? 140 LYS A CB    1 
ATOM   1092 C CG    . LYS A 1 140 ? 49.595 -17.897 -13.573 1.00 47.93  ? 140 LYS A CG    1 
ATOM   1093 C CD    . LYS A 1 140 ? 50.105 -18.970 -14.504 1.00 56.12  ? 140 LYS A CD    1 
ATOM   1094 C CE    . LYS A 1 140 ? 50.055 -20.354 -13.889 1.00 60.93  ? 140 LYS A CE    1 
ATOM   1095 N NZ    . LYS A 1 140 ? 50.931 -20.448 -12.696 1.00 65.48  ? 140 LYS A NZ    1 
ATOM   1096 N N     . GLY A 1 141 ? 49.289 -13.084 -13.099 1.00 36.21  ? 141 GLY A N     1 
ATOM   1097 C CA    . GLY A 1 141 ? 49.485 -11.696 -13.480 1.00 36.48  ? 141 GLY A CA    1 
ATOM   1098 C C     . GLY A 1 141 ? 49.487 -11.471 -14.994 1.00 34.29  ? 141 GLY A C     1 
ATOM   1099 O O     . GLY A 1 141 ? 50.153 -10.565 -15.476 1.00 34.93  ? 141 GLY A O     1 
ATOM   1100 N N     . LEU A 1 142 ? 48.718 -12.273 -15.740 1.00 34.10  ? 142 LEU A N     1 
ATOM   1101 C CA    . LEU A 1 142 ? 48.569 -12.072 -17.174 1.00 32.20  ? 142 LEU A CA    1 
ATOM   1102 C C     . LEU A 1 142 ? 47.651 -10.867 -17.397 1.00 29.79  ? 142 LEU A C     1 
ATOM   1103 O O     . LEU A 1 142 ? 46.660 -10.699 -16.708 1.00 23.40  ? 142 LEU A O     1 
ATOM   1104 C CB    . LEU A 1 142 ? 48.002 -13.357 -17.800 1.00 32.97  ? 142 LEU A CB    1 
ATOM   1105 C CG    . LEU A 1 142 ? 48.812 -14.637 -17.565 1.00 33.13  ? 142 LEU A CG    1 
ATOM   1106 C CD1   . LEU A 1 142 ? 48.301 -15.783 -18.422 1.00 32.83  ? 142 LEU A CD1   1 
ATOM   1107 C CD2   . LEU A 1 142 ? 50.289 -14.403 -17.827 1.00 33.69  ? 142 LEU A CD2   1 
ATOM   1108 N N     . LYS A 1 143 ? 47.986 -10.018 -18.367 1.00 31.76  ? 143 LYS A N     1 
ATOM   1109 C CA    . LYS A 1 143 ? 47.266 -8.774  -18.581 1.00 31.50  ? 143 LYS A CA    1 
ATOM   1110 C C     . LYS A 1 143 ? 46.110 -9.026  -19.549 1.00 26.10  ? 143 LYS A C     1 
ATOM   1111 O O     . LYS A 1 143 ? 46.078 -8.499  -20.639 1.00 27.86  ? 143 LYS A O     1 
ATOM   1112 C CB    . LYS A 1 143 ? 48.271 -7.717  -19.046 1.00 33.96  ? 143 LYS A CB    1 
ATOM   1113 C CG    . LYS A 1 143 ? 49.328 -7.375  -18.007 1.00 42.09  ? 143 LYS A CG    1 
ATOM   1114 C CD    . LYS A 1 143 ? 50.458 -6.518  -18.569 1.00 55.79  ? 143 LYS A CD    1 
ATOM   1115 C CE    . LYS A 1 143 ? 51.535 -6.205  -17.547 1.00 68.44  ? 143 LYS A CE    1 
ATOM   1116 N NZ    . LYS A 1 143 ? 52.656 -5.420  -18.127 1.00 70.88  ? 143 LYS A NZ    1 
ATOM   1117 N N     . LEU A 1 144 ? 45.143 -9.821  -19.110 1.00 25.54  ? 144 LEU A N     1 
ATOM   1118 C CA    . LEU A 1 144 ? 44.036 -10.275 -19.924 1.00 23.99  ? 144 LEU A CA    1 
ATOM   1119 C C     . LEU A 1 144 ? 42.764 -10.172 -19.112 1.00 24.05  ? 144 LEU A C     1 
ATOM   1120 O O     . LEU A 1 144 ? 42.754 -10.530 -17.937 1.00 25.52  ? 144 LEU A O     1 
ATOM   1121 C CB    . LEU A 1 144 ? 44.241 -11.746 -20.299 1.00 26.61  ? 144 LEU A CB    1 
ATOM   1122 C CG    . LEU A 1 144 ? 45.406 -12.059 -21.240 1.00 27.32  ? 144 LEU A CG    1 
ATOM   1123 C CD1   . LEU A 1 144 ? 45.478 -13.553 -21.514 1.00 27.45  ? 144 LEU A CD1   1 
ATOM   1124 C CD2   . LEU A 1 144 ? 45.317 -11.277 -22.543 1.00 25.19  ? 144 LEU A CD2   1 
ATOM   1125 N N     . TRP A 1 145 ? 41.695 -9.720  -19.770 1.00 26.13  ? 145 TRP A N     1 
ATOM   1126 C CA    . TRP A 1 145 ? 40.364 -9.747  -19.211 1.00 26.21  ? 145 TRP A CA    1 
ATOM   1127 C C     . TRP A 1 145 ? 39.568 -10.897 -19.821 1.00 28.36  ? 145 TRP A C     1 
ATOM   1128 O O     . TRP A 1 145 ? 39.726 -11.250 -20.984 1.00 31.75  ? 145 TRP A O     1 
ATOM   1129 C CB    . TRP A 1 145 ? 39.681 -8.403  -19.450 1.00 29.76  ? 145 TRP A CB    1 
ATOM   1130 C CG    . TRP A 1 145 ? 40.194 -7.291  -18.594 1.00 31.59  ? 145 TRP A CG    1 
ATOM   1131 C CD1   . TRP A 1 145 ? 41.252 -7.333  -17.736 1.00 33.00  ? 145 TRP A CD1   1 
ATOM   1132 C CD2   . TRP A 1 145 ? 39.648 -5.965  -18.491 1.00 31.88  ? 145 TRP A CD2   1 
ATOM   1133 N NE1   . TRP A 1 145 ? 41.418 -6.120  -17.126 1.00 34.40  ? 145 TRP A NE1   1 
ATOM   1134 C CE2   . TRP A 1 145 ? 40.443 -5.262  -17.558 1.00 34.78  ? 145 TRP A CE2   1 
ATOM   1135 C CE3   . TRP A 1 145 ? 38.575 -5.305  -19.092 1.00 31.98  ? 145 TRP A CE3   1 
ATOM   1136 C CZ2   . TRP A 1 145 ? 40.199 -3.929  -17.214 1.00 34.12  ? 145 TRP A CZ2   1 
ATOM   1137 C CZ3   . TRP A 1 145 ? 38.338 -3.992  -18.765 1.00 33.56  ? 145 TRP A CZ3   1 
ATOM   1138 C CH2   . TRP A 1 145 ? 39.136 -3.318  -17.831 1.00 35.47  ? 145 TRP A CH2   1 
ATOM   1139 N N     . ILE A 1 146 ? 38.711 -11.494 -19.001 1.00 26.52  ? 146 ILE A N     1 
ATOM   1140 C CA    . ILE A 1 146 ? 37.707 -12.407 -19.492 1.00 25.79  ? 146 ILE A CA    1 
ATOM   1141 C C     . ILE A 1 146 ? 36.389 -11.643 -19.626 1.00 26.31  ? 146 ILE A C     1 
ATOM   1142 O O     . ILE A 1 146 ? 36.283 -10.482 -19.241 1.00 24.61  ? 146 ILE A O     1 
ATOM   1143 C CB    . ILE A 1 146 ? 37.582 -13.635 -18.571 1.00 25.64  ? 146 ILE A CB    1 
ATOM   1144 C CG1   . ILE A 1 146 ? 37.123 -13.262 -17.159 1.00 26.05  ? 146 ILE A CG1   1 
ATOM   1145 C CG2   . ILE A 1 146 ? 38.887 -14.419 -18.555 1.00 26.45  ? 146 ILE A CG2   1 
ATOM   1146 C CD1   . ILE A 1 146 ? 36.733 -14.458 -16.294 1.00 25.89  ? 146 ILE A CD1   1 
ATOM   1147 N N     . ASP A 1 147 ? 35.391 -12.325 -20.188 1.00 25.59  ? 147 ASP A N     1 
ATOM   1148 C CA    . ASP A 1 147 ? 34.061 -11.779 -20.314 1.00 25.57  ? 147 ASP A CA    1 
ATOM   1149 C C     . ASP A 1 147 ? 33.112 -12.760 -19.644 1.00 27.03  ? 147 ASP A C     1 
ATOM   1150 O O     . ASP A 1 147 ? 33.018 -13.921 -20.030 1.00 29.52  ? 147 ASP A O     1 
ATOM   1151 C CB    . ASP A 1 147 ? 33.750 -11.517 -21.782 1.00 24.41  ? 147 ASP A CB    1 
ATOM   1152 C CG    . ASP A 1 147 ? 32.444 -10.784 -22.001 1.00 23.63  ? 147 ASP A CG    1 
ATOM   1153 O OD1   . ASP A 1 147 ? 31.410 -11.419 -21.752 1.00 24.96  ? 147 ASP A OD1   1 
ATOM   1154 O OD2   . ASP A 1 147 ? 32.478 -9.580  -22.400 1.00 21.43  ? 147 ASP A OD2   1 
ATOM   1155 N N     . VAL A 1 148 ? 32.430 -12.281 -18.612 1.00 28.23  ? 148 VAL A N     1 
ATOM   1156 C CA    . VAL A 1 148 ? 31.627 -13.147 -17.768 1.00 28.90  ? 148 VAL A CA    1 
ATOM   1157 C C     . VAL A 1 148 ? 30.159 -12.831 -17.999 1.00 28.47  ? 148 VAL A C     1 
ATOM   1158 O O     . VAL A 1 148 ? 29.770 -11.668 -18.117 1.00 25.73  ? 148 VAL A O     1 
ATOM   1159 C CB    . VAL A 1 148 ? 31.985 -12.993 -16.277 1.00 30.50  ? 148 VAL A CB    1 
ATOM   1160 C CG1   . VAL A 1 148 ? 33.438 -13.316 -16.034 1.00 30.20  ? 148 VAL A CG1   1 
ATOM   1161 C CG2   . VAL A 1 148 ? 31.668 -11.600 -15.741 1.00 32.60  ? 148 VAL A CG2   1 
ATOM   1162 N N     . PRO A 1 149 ? 29.320 -13.885 -18.027 1.00 30.14  ? 149 PRO A N     1 
ATOM   1163 C CA    . PRO A 1 149 ? 27.877 -13.756 -18.160 1.00 34.83  ? 149 PRO A CA    1 
ATOM   1164 C C     . PRO A 1 149 ? 27.217 -13.578 -16.804 1.00 41.97  ? 149 PRO A C     1 
ATOM   1165 O O     . PRO A 1 149 ? 26.288 -14.318 -16.479 1.00 45.82  ? 149 PRO A O     1 
ATOM   1166 C CB    . PRO A 1 149 ? 27.477 -15.127 -18.711 1.00 33.10  ? 149 PRO A CB    1 
ATOM   1167 C CG    . PRO A 1 149 ? 28.428 -16.056 -17.997 1.00 31.76  ? 149 PRO A CG    1 
ATOM   1168 C CD    . PRO A 1 149 ? 29.736 -15.291 -17.936 1.00 29.68  ? 149 PRO A CD    1 
ATOM   1169 N N     . ASP A 1 150 ? 27.722 -12.602 -16.045 1.00 43.61  ? 150 ASP A N     1 
ATOM   1170 C CA    . ASP A 1 150 ? 27.229 -12.270 -14.715 1.00 53.90  ? 150 ASP A CA    1 
ATOM   1171 C C     . ASP A 1 150 ? 27.599 -13.351 -13.706 1.00 54.97  ? 150 ASP A C     1 
ATOM   1172 O O     . ASP A 1 150 ? 28.528 -13.120 -12.919 1.00 59.60  ? 150 ASP A O     1 
ATOM   1173 C CB    . ASP A 1 150 ? 25.746 -11.897 -14.688 1.00 53.00  ? 150 ASP A CB    1 
ATOM   1174 C CG    . ASP A 1 150 ? 25.556 -10.416 -14.405 1.00 57.41  ? 150 ASP A CG    1 
ATOM   1175 O OD1   . ASP A 1 150 ? 26.089 -9.933  -13.346 1.00 66.46  ? 150 ASP A OD1   1 
ATOM   1176 O OD2   . ASP A 1 150 ? 24.881 -9.761  -15.221 1.00 48.73  ? 150 ASP A OD2   1 
ATOM   1177 N N     . ILE A 1 151 ? 26.899 -14.498 -13.743 1.00 48.48  ? 151 ILE A N     1 
ATOM   1178 C CA    . ILE A 1 151 ? 27.211 -15.582 -12.821 1.00 52.46  ? 151 ILE A CA    1 
ATOM   1179 C C     . ILE A 1 151 ? 28.544 -16.209 -13.224 1.00 45.55  ? 151 ILE A C     1 
ATOM   1180 O O     . ILE A 1 151 ? 28.781 -16.484 -14.388 1.00 49.95  ? 151 ILE A O     1 
ATOM   1181 C CB    . ILE A 1 151 ? 26.078 -16.621 -12.711 1.00 61.96  ? 151 ILE A CB    1 
ATOM   1182 C CG1   . ILE A 1 151 ? 26.200 -17.770 -13.717 1.00 66.21  ? 151 ILE A CG1   1 
ATOM   1183 C CG2   . ILE A 1 151 ? 24.726 -15.925 -12.780 1.00 70.54  ? 151 ILE A CG2   1 
ATOM   1184 C CD1   . ILE A 1 151 ? 25.242 -18.912 -13.447 1.00 70.02  ? 151 ILE A CD1   1 
ATOM   1185 N N     . GLY A 1 152 ? 29.404 -16.436 -12.233 1.00 41.68  ? 152 GLY A N     1 
ATOM   1186 C CA    . GLY A 1 152 ? 30.782 -16.826 -12.460 1.00 40.06  ? 152 GLY A CA    1 
ATOM   1187 C C     . GLY A 1 152 ? 31.003 -18.332 -12.396 1.00 40.53  ? 152 GLY A C     1 
ATOM   1188 O O     . GLY A 1 152 ? 32.036 -18.822 -12.860 1.00 43.50  ? 152 GLY A O     1 
ATOM   1189 N N     . TRP A 1 153 ? 30.050 -19.085 -11.844 1.00 40.44  ? 153 TRP A N     1 
ATOM   1190 C CA    . TRP A 1 153 ? 30.316 -20.503 -11.675 1.00 43.78  ? 153 TRP A CA    1 
ATOM   1191 C C     . TRP A 1 153 ? 29.853 -21.297 -12.895 1.00 38.50  ? 153 TRP A C     1 
ATOM   1192 O O     . TRP A 1 153 ? 29.955 -22.520 -12.901 1.00 36.10  ? 153 TRP A O     1 
ATOM   1193 C CB    . TRP A 1 153 ? 29.793 -21.033 -10.328 1.00 54.85  ? 153 TRP A CB    1 
ATOM   1194 C CG    . TRP A 1 153 ? 28.323 -20.928 -10.081 1.00 64.52  ? 153 TRP A CG    1 
ATOM   1195 C CD1   . TRP A 1 153 ? 27.325 -20.759 -11.000 1.00 72.88  ? 153 TRP A CD1   1 
ATOM   1196 C CD2   . TRP A 1 153 ? 27.681 -21.002 -8.792  1.00 72.02  ? 153 TRP A CD2   1 
ATOM   1197 N NE1   . TRP A 1 153 ? 26.103 -20.745 -10.374 1.00 77.85  ? 153 TRP A NE1   1 
ATOM   1198 C CE2   . TRP A 1 153 ? 26.287 -20.884 -9.020  1.00 75.93  ? 153 TRP A CE2   1 
ATOM   1199 C CE3   . TRP A 1 153 ? 28.143 -21.155 -7.477  1.00 71.76  ? 153 TRP A CE3   1 
ATOM   1200 C CZ2   . TRP A 1 153 ? 25.356 -20.907 -7.978  1.00 73.54  ? 153 TRP A CZ2   1 
ATOM   1201 C CZ3   . TRP A 1 153 ? 27.219 -21.187 -6.450  1.00 72.86  ? 153 TRP A CZ3   1 
ATOM   1202 C CH2   . TRP A 1 153 ? 25.846 -21.067 -6.699  1.00 74.99  ? 153 TRP A CH2   1 
ATOM   1203 N N     . GLY A 1 154 ? 29.450 -20.595 -13.967 1.00 33.28  ? 154 GLY A N     1 
ATOM   1204 C CA    . GLY A 1 154 ? 29.195 -21.237 -15.243 1.00 31.76  ? 154 GLY A CA    1 
ATOM   1205 C C     . GLY A 1 154 ? 30.470 -21.584 -16.025 1.00 28.95  ? 154 GLY A C     1 
ATOM   1206 O O     . GLY A 1 154 ? 31.583 -21.249 -15.618 1.00 29.87  ? 154 GLY A O     1 
ATOM   1207 N N     . SER A 1 155 ? 30.259 -22.209 -17.189 1.00 26.31  ? 155 SER A N     1 
ATOM   1208 C CA    . SER A 1 155 ? 31.306 -22.752 -18.056 1.00 26.96  ? 155 SER A CA    1 
ATOM   1209 C C     . SER A 1 155 ? 31.633 -21.822 -19.219 1.00 24.94  ? 155 SER A C     1 
ATOM   1210 O O     . SER A 1 155 ? 30.738 -21.450 -19.978 1.00 27.26  ? 155 SER A O     1 
ATOM   1211 C CB    . SER A 1 155 ? 30.889 -24.101 -18.615 1.00 26.84  ? 155 SER A CB    1 
ATOM   1212 O OG    . SER A 1 155 ? 31.731 -24.489 -19.692 1.00 27.91  ? 155 SER A OG    1 
ATOM   1213 N N     . VAL A 1 156 ? 32.927 -21.540 -19.414 1.00 26.18  ? 156 VAL A N     1 
ATOM   1214 C CA    . VAL A 1 156 ? 33.415 -20.775 -20.556 1.00 24.22  ? 156 VAL A CA    1 
ATOM   1215 C C     . VAL A 1 156 ? 32.965 -21.415 -21.869 1.00 25.21  ? 156 VAL A C     1 
ATOM   1216 O O     . VAL A 1 156 ? 32.568 -20.725 -22.803 1.00 24.61  ? 156 VAL A O     1 
ATOM   1217 C CB    . VAL A 1 156 ? 34.941 -20.651 -20.497 1.00 25.57  ? 156 VAL A CB    1 
ATOM   1218 C CG1   . VAL A 1 156 ? 35.508 -19.899 -21.703 1.00 26.60  ? 156 VAL A CG1   1 
ATOM   1219 C CG2   . VAL A 1 156 ? 35.358 -19.990 -19.195 1.00 26.74  ? 156 VAL A CG2   1 
ATOM   1220 N N     . VAL A 1 157 ? 32.963 -22.749 -21.900 1.00 26.36  ? 157 VAL A N     1 
ATOM   1221 C CA    . VAL A 1 157 ? 32.584 -23.493 -23.081 1.00 25.45  ? 157 VAL A CA    1 
ATOM   1222 C C     . VAL A 1 157 ? 31.070 -23.521 -23.205 1.00 26.14  ? 157 VAL A C     1 
ATOM   1223 O O     . VAL A 1 157 ? 30.524 -23.191 -24.258 1.00 28.83  ? 157 VAL A O     1 
ATOM   1224 C CB    . VAL A 1 157 ? 33.173 -24.910 -23.070 1.00 24.12  ? 157 VAL A CB    1 
ATOM   1225 C CG1   . VAL A 1 157 ? 32.606 -25.772 -24.188 1.00 24.40  ? 157 VAL A CG1   1 
ATOM   1226 C CG2   . VAL A 1 157 ? 34.686 -24.855 -23.144 1.00 22.83  ? 157 VAL A CG2   1 
ATOM   1227 N N     . GLY A 1 158 ? 30.399 -23.955 -22.146 1.00 25.01  ? 158 GLY A N     1 
ATOM   1228 C CA    . GLY A 1 158 ? 28.994 -24.298 -22.255 1.00 24.21  ? 158 GLY A CA    1 
ATOM   1229 C C     . GLY A 1 158 ? 28.156 -23.068 -22.543 1.00 25.16  ? 158 GLY A C     1 
ATOM   1230 O O     . GLY A 1 158 ? 27.191 -23.096 -23.324 1.00 25.69  ? 158 GLY A O     1 
ATOM   1231 N N     . ASN A 1 159 ? 28.563 -21.975 -21.904 1.00 25.56  ? 159 ASN A N     1 
ATOM   1232 C CA    . ASN A 1 159 ? 27.869 -20.715 -22.100 1.00 24.87  ? 159 ASN A CA    1 
ATOM   1233 C C     . ASN A 1 159 ? 28.007 -20.277 -23.566 1.00 23.48  ? 159 ASN A C     1 
ATOM   1234 O O     . ASN A 1 159 ? 27.033 -19.911 -24.222 1.00 23.09  ? 159 ASN A O     1 
ATOM   1235 C CB    . ASN A 1 159 ? 28.348 -19.681 -21.078 1.00 24.38  ? 159 ASN A CB    1 
ATOM   1236 C CG    . ASN A 1 159 ? 27.808 -18.313 -21.414 1.00 25.15  ? 159 ASN A CG    1 
ATOM   1237 O OD1   . ASN A 1 159 ? 28.311 -17.636 -22.321 1.00 22.46  ? 159 ASN A OD1   1 
ATOM   1238 N ND2   . ASN A 1 159 ? 26.740 -17.950 -20.731 1.00 24.58  ? 159 ASN A ND2   1 
ATOM   1239 N N     . ALA A 1 160 ? 29.224 -20.310 -24.096 1.00 21.98  ? 160 ALA A N     1 
ATOM   1240 C CA    . ALA A 1 160 ? 29.423 -19.906 -25.476 1.00 22.35  ? 160 ALA A CA    1 
ATOM   1241 C C     . ALA A 1 160 ? 28.571 -20.784 -26.381 1.00 22.88  ? 160 ALA A C     1 
ATOM   1242 O O     . ALA A 1 160 ? 27.990 -20.296 -27.352 1.00 23.31  ? 160 ALA A O     1 
ATOM   1243 C CB    . ALA A 1 160 ? 30.888 -19.979 -25.870 1.00 22.08  ? 160 ALA A CB    1 
ATOM   1244 N N     . LEU A 1 161 ? 28.509 -22.082 -26.070 1.00 23.03  ? 161 LEU A N     1 
ATOM   1245 C CA    . LEU A 1 161 ? 27.866 -23.013 -26.983 1.00 23.22  ? 161 LEU A CA    1 
ATOM   1246 C C     . LEU A 1 161 ? 26.372 -22.735 -27.039 1.00 23.26  ? 161 LEU A C     1 
ATOM   1247 O O     . LEU A 1 161 ? 25.748 -22.973 -28.053 1.00 27.50  ? 161 LEU A O     1 
ATOM   1248 C CB    . LEU A 1 161 ? 28.131 -24.451 -26.541 1.00 24.24  ? 161 LEU A CB    1 
ATOM   1249 C CG    . LEU A 1 161 ? 29.583 -24.926 -26.663 1.00 24.71  ? 161 LEU A CG    1 
ATOM   1250 C CD1   . LEU A 1 161 ? 29.705 -26.348 -26.165 1.00 26.21  ? 161 LEU A CD1   1 
ATOM   1251 C CD2   . LEU A 1 161 ? 30.119 -24.816 -28.081 1.00 23.59  ? 161 LEU A CD2   1 
ATOM   1252 N N     . ASP A 1 162 ? 25.817 -22.164 -25.975 1.00 24.71  ? 162 ASP A N     1 
ATOM   1253 C CA    . ASP A 1 162 ? 24.407 -21.828 -25.938 1.00 25.17  ? 162 ASP A CA    1 
ATOM   1254 C C     . ASP A 1 162 ? 24.216 -20.351 -26.303 1.00 24.21  ? 162 ASP A C     1 
ATOM   1255 O O     . ASP A 1 162 ? 23.196 -19.777 -25.999 1.00 25.70  ? 162 ASP A O     1 
ATOM   1256 C CB    . ASP A 1 162 ? 23.839 -22.221 -24.569 1.00 27.78  ? 162 ASP A CB    1 
ATOM   1257 C CG    . ASP A 1 162 ? 22.389 -22.683 -24.591 1.00 33.15  ? 162 ASP A CG    1 
ATOM   1258 O OD1   . ASP A 1 162 ? 22.018 -23.456 -25.517 1.00 34.50  ? 162 ASP A OD1   1 
ATOM   1259 O OD2   . ASP A 1 162 ? 21.633 -22.270 -23.685 1.00 36.83  ? 162 ASP A OD2   1 
ATOM   1260 N N     . HIS A 1 163 ? 25.206 -19.727 -26.942 1.00 24.50  ? 163 HIS A N     1 
ATOM   1261 C CA    . HIS A 1 163 ? 25.098 -18.373 -27.460 1.00 24.72  ? 163 HIS A CA    1 
ATOM   1262 C C     . HIS A 1 163 ? 24.896 -17.377 -26.320 1.00 26.78  ? 163 HIS A C     1 
ATOM   1263 O O     . HIS A 1 163 ? 24.144 -16.402 -26.459 1.00 28.45  ? 163 HIS A O     1 
ATOM   1264 C CB    . HIS A 1 163 ? 23.989 -18.272 -28.510 1.00 24.22  ? 163 HIS A CB    1 
ATOM   1265 C CG    . HIS A 1 163 ? 24.206 -19.165 -29.685 1.00 25.74  ? 163 HIS A CG    1 
ATOM   1266 N ND1   . HIS A 1 163 ? 23.217 -19.447 -30.603 1.00 23.54  ? 163 HIS A ND1   1 
ATOM   1267 C CD2   . HIS A 1 163 ? 25.291 -19.873 -30.069 1.00 24.49  ? 163 HIS A CD2   1 
ATOM   1268 C CE1   . HIS A 1 163 ? 23.722 -20.273 -31.516 1.00 25.40  ? 163 HIS A CE1   1 
ATOM   1269 N NE2   . HIS A 1 163 ? 24.979 -20.535 -31.221 1.00 22.98  ? 163 HIS A NE2   1 
ATOM   1270 N N     . GLY A 1 164 ? 25.591 -17.639 -25.210 1.00 24.80  ? 164 GLY A N     1 
ATOM   1271 C CA    . GLY A 1 164 ? 25.542 -16.794 -24.036 1.00 24.15  ? 164 GLY A CA    1 
ATOM   1272 C C     . GLY A 1 164 ? 26.230 -15.461 -24.282 1.00 24.37  ? 164 GLY A C     1 
ATOM   1273 O O     . GLY A 1 164 ? 26.922 -15.315 -25.284 1.00 25.63  ? 164 GLY A O     1 
ATOM   1274 N N     . ILE A 1 165 ? 26.008 -14.502 -23.366 1.00 25.85  ? 165 ILE A N     1 
ATOM   1275 C CA    . ILE A 1 165 ? 26.445 -13.119 -23.531 1.00 25.41  ? 165 ILE A CA    1 
ATOM   1276 C C     . ILE A 1 165 ? 27.040 -12.613 -22.227 1.00 22.70  ? 165 ILE A C     1 
ATOM   1277 O O     . ILE A 1 165 ? 26.647 -13.026 -21.147 1.00 26.85  ? 165 ILE A O     1 
ATOM   1278 C CB    . ILE A 1 165 ? 25.293 -12.197 -23.968 1.00 28.58  ? 165 ILE A CB    1 
ATOM   1279 C CG1   . ILE A 1 165 ? 24.110 -12.283 -22.989 1.00 33.28  ? 165 ILE A CG1   1 
ATOM   1280 C CG2   . ILE A 1 165 ? 24.877 -12.481 -25.395 1.00 26.81  ? 165 ILE A CG2   1 
ATOM   1281 C CD1   . ILE A 1 165 ? 22.948 -11.369 -23.323 1.00 35.66  ? 165 ILE A CD1   1 
ATOM   1282 N N     . GLY A 1 166 ? 27.972 -11.681 -22.349 1.00 21.77  ? 166 GLY A N     1 
ATOM   1283 C CA    . GLY A 1 166 ? 28.507 -10.942 -21.220 1.00 21.26  ? 166 GLY A CA    1 
ATOM   1284 C C     . GLY A 1 166 ? 28.513 -9.460  -21.558 1.00 21.56  ? 166 GLY A C     1 
ATOM   1285 O O     . GLY A 1 166 ? 27.816 -9.050  -22.478 1.00 22.48  ? 166 GLY A O     1 
ATOM   1286 N N     . TYR A 1 167 ? 29.345 -8.684  -20.869 1.00 21.57  ? 167 TYR A N     1 
ATOM   1287 C CA    . TYR A 1 167 ? 29.129 -7.257  -20.788 1.00 22.22  ? 167 TYR A CA    1 
ATOM   1288 C C     . TYR A 1 167 ? 30.402 -6.453  -21.026 1.00 23.84  ? 167 TYR A C     1 
ATOM   1289 O O     . TYR A 1 167 ? 30.400 -5.293  -20.654 1.00 25.34  ? 167 TYR A O     1 
ATOM   1290 C CB    . TYR A 1 167 ? 28.446 -6.966  -19.452 1.00 23.49  ? 167 TYR A CB    1 
ATOM   1291 C CG    . TYR A 1 167 ? 27.171 -7.761  -19.334 1.00 25.56  ? 167 TYR A CG    1 
ATOM   1292 C CD1   . TYR A 1 167 ? 26.056 -7.426  -20.091 1.00 29.39  ? 167 TYR A CD1   1 
ATOM   1293 C CD2   . TYR A 1 167 ? 27.133 -8.955  -18.631 1.00 26.76  ? 167 TYR A CD2   1 
ATOM   1294 C CE1   . TYR A 1 167 ? 24.906 -8.206  -20.077 1.00 30.13  ? 167 TYR A CE1   1 
ATOM   1295 C CE2   . TYR A 1 167 ? 25.983 -9.728  -18.584 1.00 29.35  ? 167 TYR A CE2   1 
ATOM   1296 C CZ    . TYR A 1 167 ? 24.858 -9.352  -19.301 1.00 31.09  ? 167 TYR A CZ    1 
ATOM   1297 O OH    . TYR A 1 167 ? 23.721 -10.143 -19.295 1.00 34.02  ? 167 TYR A OH    1 
ATOM   1298 N N     . THR A 1 168 ? 31.425 -7.018  -21.709 1.00 24.15  ? 168 THR A N     1 
ATOM   1299 C CA    . THR A 1 168 ? 32.583 -6.260  -22.182 1.00 22.77  ? 168 THR A CA    1 
ATOM   1300 C C     . THR A 1 168 ? 32.501 -6.219  -23.705 1.00 22.43  ? 168 THR A C     1 
ATOM   1301 O O     . THR A 1 168 ? 31.561 -6.756  -24.291 1.00 23.50  ? 168 THR A O     1 
ATOM   1302 C CB    . THR A 1 168 ? 33.933 -6.854  -21.708 1.00 23.47  ? 168 THR A CB    1 
ATOM   1303 O OG1   . THR A 1 168 ? 34.385 -7.930  -22.540 1.00 24.52  ? 168 THR A OG1   1 
ATOM   1304 C CG2   . THR A 1 168 ? 33.905 -7.403  -20.298 1.00 23.25  ? 168 THR A CG2   1 
ATOM   1305 N N     . PRO A 1 169 ? 33.477 -5.629  -24.422 1.00 20.87  ? 169 PRO A N     1 
ATOM   1306 C CA    . PRO A 1 169 ? 33.478 -5.723  -25.878 1.00 22.28  ? 169 PRO A CA    1 
ATOM   1307 C C     . PRO A 1 169 ? 33.542 -7.174  -26.369 1.00 22.57  ? 169 PRO A C     1 
ATOM   1308 O O     . PRO A 1 169 ? 33.137 -7.448  -27.482 1.00 22.97  ? 169 PRO A O     1 
ATOM   1309 C CB    . PRO A 1 169 ? 34.717 -4.911  -26.300 1.00 23.27  ? 169 PRO A CB    1 
ATOM   1310 C CG    . PRO A 1 169 ? 34.994 -3.992  -25.108 1.00 22.59  ? 169 PRO A CG    1 
ATOM   1311 C CD    . PRO A 1 169 ? 34.584 -4.813  -23.903 1.00 22.47  ? 169 PRO A CD    1 
ATOM   1312 N N     . TYR A 1 170 ? 33.965 -8.125  -25.529 1.00 21.53  ? 170 TYR A N     1 
ATOM   1313 C CA    . TYR A 1 170 ? 34.032 -9.520  -25.946 1.00 22.53  ? 170 TYR A CA    1 
ATOM   1314 C C     . TYR A 1 170 ? 32.768 -10.264 -25.499 1.00 22.71  ? 170 TYR A C     1 
ATOM   1315 O O     . TYR A 1 170 ? 32.815 -11.472 -25.247 1.00 22.23  ? 170 TYR A O     1 
ATOM   1316 C CB    . TYR A 1 170 ? 35.315 -10.191 -25.417 1.00 23.10  ? 170 TYR A CB    1 
ATOM   1317 C CG    . TYR A 1 170 ? 36.604 -9.903  -26.169 1.00 23.92  ? 170 TYR A CG    1 
ATOM   1318 C CD1   . TYR A 1 170 ? 36.994 -8.620  -26.531 1.00 25.95  ? 170 TYR A CD1   1 
ATOM   1319 C CD2   . TYR A 1 170 ? 37.454 -10.936 -26.524 1.00 23.80  ? 170 TYR A CD2   1 
ATOM   1320 C CE1   . TYR A 1 170 ? 38.190 -8.378  -27.204 1.00 26.19  ? 170 TYR A CE1   1 
ATOM   1321 C CE2   . TYR A 1 170 ? 38.643 -10.717 -27.200 1.00 22.80  ? 170 TYR A CE2   1 
ATOM   1322 C CZ    . TYR A 1 170 ? 39.025 -9.435  -27.539 1.00 24.34  ? 170 TYR A CZ    1 
ATOM   1323 O OH    . TYR A 1 170 ? 40.230 -9.249  -28.188 1.00 19.88  ? 170 TYR A OH    1 
ATOM   1324 N N     . GLY A 1 171 ? 31.630 -9.550  -25.502 1.00 22.67  ? 171 GLY A N     1 
ATOM   1325 C CA    . GLY A 1 171 ? 30.383 -10.003 -24.906 1.00 22.57  ? 171 GLY A CA    1 
ATOM   1326 C C     . GLY A 1 171 ? 29.624 -11.044 -25.734 1.00 23.69  ? 171 GLY A C     1 
ATOM   1327 O O     . GLY A 1 171 ? 28.811 -11.766 -25.176 1.00 24.54  ? 171 GLY A O     1 
ATOM   1328 N N     . ASP A 1 172 ? 29.860 -11.144 -27.049 1.00 22.33  ? 172 ASP A N     1 
ATOM   1329 C CA    . ASP A 1 172 ? 29.254 -12.220 -27.819 1.00 21.49  ? 172 ASP A CA    1 
ATOM   1330 C C     . ASP A 1 172 ? 30.184 -13.439 -27.731 1.00 21.93  ? 172 ASP A C     1 
ATOM   1331 O O     . ASP A 1 172 ? 31.159 -13.572 -28.461 1.00 21.37  ? 172 ASP A O     1 
ATOM   1332 C CB    . ASP A 1 172 ? 28.949 -11.762 -29.250 1.00 22.22  ? 172 ASP A CB    1 
ATOM   1333 C CG    . ASP A 1 172 ? 28.334 -12.848 -30.130 1.00 24.28  ? 172 ASP A CG    1 
ATOM   1334 O OD1   . ASP A 1 172 ? 28.255 -13.999 -29.677 1.00 26.68  ? 172 ASP A OD1   1 
ATOM   1335 O OD2   . ASP A 1 172 ? 27.930 -12.541 -31.258 1.00 27.63  ? 172 ASP A OD2   1 
ATOM   1336 N N     . HIS A 1 173 ? 29.907 -14.331 -26.790 1.00 22.53  ? 173 HIS A N     1 
ATOM   1337 C CA    . HIS A 1 173 ? 30.887 -15.341 -26.401 1.00 25.39  ? 173 HIS A CA    1 
ATOM   1338 C C     . HIS A 1 173 ? 31.192 -16.328 -27.534 1.00 23.47  ? 173 HIS A C     1 
ATOM   1339 O O     . HIS A 1 173 ? 32.351 -16.626 -27.801 1.00 23.24  ? 173 HIS A O     1 
ATOM   1340 C CB    . HIS A 1 173 ? 30.435 -16.074 -25.135 1.00 24.42  ? 173 HIS A CB    1 
ATOM   1341 C CG    . HIS A 1 173 ? 30.416 -15.223 -23.932 1.00 24.91  ? 173 HIS A CG    1 
ATOM   1342 N ND1   . HIS A 1 173 ? 29.705 -15.622 -22.826 1.00 27.39  ? 173 HIS A ND1   1 
ATOM   1343 C CD2   . HIS A 1 173 ? 30.941 -14.034 -23.627 1.00 28.54  ? 173 HIS A CD2   1 
ATOM   1344 C CE1   . HIS A 1 173 ? 29.817 -14.698 -21.872 1.00 27.57  ? 173 HIS A CE1   1 
ATOM   1345 N NE2   . HIS A 1 173 ? 30.564 -13.725 -22.334 1.00 29.41  ? 173 HIS A NE2   1 
ATOM   1346 N N     . PHE A 1 174 ? 30.165 -16.817 -28.224 1.00 23.19  ? 174 PHE A N     1 
ATOM   1347 C CA    . PHE A 1 174 ? 30.425 -17.706 -29.335 1.00 24.21  ? 174 PHE A CA    1 
ATOM   1348 C C     . PHE A 1 174 ? 31.160 -16.993 -30.485 1.00 23.83  ? 174 PHE A C     1 
ATOM   1349 O O     . PHE A 1 174 ? 31.948 -17.623 -31.198 1.00 20.25  ? 174 PHE A O     1 
ATOM   1350 C CB    . PHE A 1 174 ? 29.152 -18.402 -29.808 1.00 23.55  ? 174 PHE A CB    1 
ATOM   1351 C CG    . PHE A 1 174 ? 29.504 -19.554 -30.713 1.00 24.18  ? 174 PHE A CG    1 
ATOM   1352 C CD1   . PHE A 1 174 ? 30.042 -20.716 -30.179 1.00 24.33  ? 174 PHE A CD1   1 
ATOM   1353 C CD2   . PHE A 1 174 ? 29.443 -19.417 -32.093 1.00 23.36  ? 174 PHE A CD2   1 
ATOM   1354 C CE1   . PHE A 1 174 ? 30.421 -21.756 -31.018 1.00 26.15  ? 174 PHE A CE1   1 
ATOM   1355 C CE2   . PHE A 1 174 ? 29.834 -20.454 -32.924 1.00 23.72  ? 174 PHE A CE2   1 
ATOM   1356 C CZ    . PHE A 1 174 ? 30.327 -21.616 -32.390 1.00 23.86  ? 174 PHE A CZ    1 
ATOM   1357 N N     . ALA A 1 175 ? 30.950 -15.682 -30.664 1.00 22.07  ? 175 ALA A N     1 
ATOM   1358 C CA    . ALA A 1 175 ? 31.698 -14.963 -31.690 1.00 23.56  ? 175 ALA A CA    1 
ATOM   1359 C C     . ALA A 1 175 ? 33.201 -14.979 -31.391 1.00 24.67  ? 175 ALA A C     1 
ATOM   1360 O O     . ALA A 1 175 ? 34.012 -14.860 -32.297 1.00 24.29  ? 175 ALA A O     1 
ATOM   1361 C CB    . ALA A 1 175 ? 31.202 -13.540 -31.853 1.00 21.88  ? 175 ALA A CB    1 
ATOM   1362 N N     . MET A 1 176 ? 33.570 -15.122 -30.121 1.00 24.67  ? 176 MET A N     1 
ATOM   1363 C CA    . MET A 1 176 ? 34.956 -15.034 -29.720 1.00 24.95  ? 176 MET A CA    1 
ATOM   1364 C C     . MET A 1 176 ? 35.594 -16.415 -29.691 1.00 24.35  ? 176 MET A C     1 
ATOM   1365 O O     . MET A 1 176 ? 36.781 -16.524 -29.437 1.00 24.19  ? 176 MET A O     1 
ATOM   1366 C CB    . MET A 1 176 ? 35.045 -14.371 -28.340 1.00 27.07  ? 176 MET A CB    1 
ATOM   1367 C CG    . MET A 1 176 ? 34.515 -12.933 -28.344 1.00 27.98  ? 176 MET A CG    1 
ATOM   1368 S SD    . MET A 1 176 ? 35.474 -11.766 -29.357 1.00 30.45  ? 176 MET A SD    1 
ATOM   1369 C CE    . MET A 1 176 ? 34.455 -11.548 -30.813 1.00 30.52  ? 176 MET A CE    1 
ATOM   1370 N N     . GLN A 1 177 ? 34.806 -17.463 -29.952 1.00 24.45  ? 177 GLN A N     1 
ATOM   1371 C CA    . GLN A 1 177 ? 35.316 -18.818 -30.033 1.00 23.40  ? 177 GLN A CA    1 
ATOM   1372 C C     . GLN A 1 177 ? 36.254 -18.989 -31.232 1.00 22.32  ? 177 GLN A C     1 
ATOM   1373 O O     . GLN A 1 177 ? 36.102 -18.344 -32.255 1.00 20.22  ? 177 GLN A O     1 
ATOM   1374 C CB    . GLN A 1 177 ? 34.158 -19.808 -30.074 1.00 23.90  ? 177 GLN A CB    1 
ATOM   1375 C CG    . GLN A 1 177 ? 34.600 -21.262 -30.164 1.00 24.55  ? 177 GLN A CG    1 
ATOM   1376 C CD    . GLN A 1 177 ? 34.646 -21.761 -31.583 1.00 26.90  ? 177 GLN A CD    1 
ATOM   1377 O OE1   . GLN A 1 177 ? 34.012 -21.216 -32.486 1.00 26.78  ? 177 GLN A OE1   1 
ATOM   1378 N NE2   . GLN A 1 177 ? 35.338 -22.869 -31.773 1.00 28.92  ? 177 GLN A NE2   1 
ATOM   1379 N N     . CYS A 1 178 ? 37.270 -19.843 -31.063 1.00 23.09  ? 178 CYS A N     1 
ATOM   1380 C CA    . CYS A 1 178 ? 38.240 -20.091 -32.114 1.00 23.88  ? 178 CYS A CA    1 
ATOM   1381 C C     . CYS A 1 178 ? 38.871 -21.463 -31.894 1.00 23.34  ? 178 CYS A C     1 
ATOM   1382 O O     . CYS A 1 178 ? 39.620 -21.640 -30.948 1.00 23.10  ? 178 CYS A O     1 
ATOM   1383 C CB    . CYS A 1 178 ? 39.309 -19.011 -32.111 1.00 23.57  ? 178 CYS A CB    1 
ATOM   1384 S SG    . CYS A 1 178 ? 40.343 -18.988 -33.599 1.00 23.92  ? 178 CYS A SG    1 
ATOM   1385 N N     . GLY A 1 179 ? 38.528 -22.420 -32.760 1.00 22.39  ? 179 GLY A N     1 
ATOM   1386 C CA    . GLY A 1 179 ? 38.955 -23.801 -32.635 1.00 22.62  ? 179 GLY A CA    1 
ATOM   1387 C C     . GLY A 1 179 ? 38.132 -24.546 -31.588 1.00 24.03  ? 179 GLY A C     1 
ATOM   1388 O O     . GLY A 1 179 ? 37.844 -23.996 -30.530 1.00 26.26  ? 179 GLY A O     1 
ATOM   1389 N N     . MET A 1 180 ? 37.765 -25.796 -31.886 1.00 25.04  ? 180 MET A N     1 
ATOM   1390 C CA    . MET A 1 180 ? 37.236 -26.709 -30.883 1.00 25.29  ? 180 MET A CA    1 
ATOM   1391 C C     . MET A 1 180 ? 37.588 -28.153 -31.242 1.00 23.90  ? 180 MET A C     1 
ATOM   1392 O O     . MET A 1 180 ? 37.866 -28.499 -32.385 1.00 21.46  ? 180 MET A O     1 
ATOM   1393 C CB    . MET A 1 180 ? 35.706 -26.628 -30.754 1.00 26.26  ? 180 MET A CB    1 
ATOM   1394 C CG    . MET A 1 180 ? 34.966 -26.692 -32.073 1.00 28.20  ? 180 MET A CG    1 
ATOM   1395 S SD    . MET A 1 180 ? 33.174 -26.867 -31.893 1.00 29.55  ? 180 MET A SD    1 
ATOM   1396 C CE    . MET A 1 180 ? 32.748 -25.271 -31.194 1.00 29.74  ? 180 MET A CE    1 
ATOM   1397 N N     . GLU A 1 181 ? 37.503 -29.019 -30.237 1.00 24.88  ? 181 GLU A N     1 
ATOM   1398 C CA    . GLU A 1 181 ? 37.579 -30.445 -30.458 1.00 24.66  ? 181 GLU A CA    1 
ATOM   1399 C C     . GLU A 1 181 ? 36.217 -31.017 -30.110 1.00 24.03  ? 181 GLU A C     1 
ATOM   1400 O O     . GLU A 1 181 ? 35.643 -30.680 -29.068 1.00 23.21  ? 181 GLU A O     1 
ATOM   1401 C CB    . GLU A 1 181 ? 38.665 -31.054 -29.579 1.00 26.18  ? 181 GLU A CB    1 
ATOM   1402 C CG    . GLU A 1 181 ? 38.888 -32.549 -29.780 1.00 27.02  ? 181 GLU A CG    1 
ATOM   1403 C CD    . GLU A 1 181 ? 39.910 -33.083 -28.788 1.00 28.05  ? 181 GLU A CD    1 
ATOM   1404 O OE1   . GLU A 1 181 ? 41.114 -33.140 -29.157 1.00 30.44  ? 181 GLU A OE1   1 
ATOM   1405 O OE2   . GLU A 1 181 ? 39.514 -33.396 -27.646 1.00 23.44  ? 181 GLU A OE2   1 
ATOM   1406 N N     . VAL A 1 182 ? 35.741 -31.915 -30.971 1.00 21.85  ? 182 VAL A N     1 
ATOM   1407 C CA    . VAL A 1 182 ? 34.398 -32.440 -30.814 1.00 22.54  ? 182 VAL A CA    1 
ATOM   1408 C C     . VAL A 1 182 ? 34.483 -33.951 -30.944 1.00 21.37  ? 182 VAL A C     1 
ATOM   1409 O O     . VAL A 1 182 ? 35.087 -34.451 -31.909 1.00 19.66  ? 182 VAL A O     1 
ATOM   1410 C CB    . VAL A 1 182 ? 33.435 -31.870 -31.881 1.00 23.14  ? 182 VAL A CB    1 
ATOM   1411 C CG1   . VAL A 1 182 ? 31.999 -32.221 -31.561 1.00 24.97  ? 182 VAL A CG1   1 
ATOM   1412 C CG2   . VAL A 1 182 ? 33.596 -30.371 -32.077 1.00 22.91  ? 182 VAL A CG2   1 
ATOM   1413 N N     . VAL A 1 183 ? 33.830 -34.631 -29.996 1.00 19.55  ? 183 VAL A N     1 
ATOM   1414 C CA    . VAL A 1 183 ? 33.478 -36.024 -30.157 1.00 20.70  ? 183 VAL A CA    1 
ATOM   1415 C C     . VAL A 1 183 ? 32.141 -36.097 -30.898 1.00 20.93  ? 183 VAL A C     1 
ATOM   1416 O O     . VAL A 1 183 ? 31.113 -35.640 -30.407 1.00 20.44  ? 183 VAL A O     1 
ATOM   1417 C CB    . VAL A 1 183 ? 33.418 -36.765 -28.809 1.00 21.92  ? 183 VAL A CB    1 
ATOM   1418 C CG1   . VAL A 1 183 ? 32.973 -38.211 -28.981 1.00 22.09  ? 183 VAL A CG1   1 
ATOM   1419 C CG2   . VAL A 1 183 ? 34.738 -36.716 -28.072 1.00 22.40  ? 183 VAL A CG2   1 
ATOM   1420 N N     . LEU A 1 184 ? 32.160 -36.710 -32.082 1.00 22.57  ? 184 LEU A N     1 
ATOM   1421 C CA    . LEU A 1 184 ? 30.960 -36.863 -32.881 1.00 23.83  ? 184 LEU A CA    1 
ATOM   1422 C C     . LEU A 1 184 ? 30.112 -37.987 -32.327 1.00 25.09  ? 184 LEU A C     1 
ATOM   1423 O O     . LEU A 1 184 ? 30.543 -38.760 -31.456 1.00 25.75  ? 184 LEU A O     1 
ATOM   1424 C CB    . LEU A 1 184 ? 31.344 -37.112 -34.342 1.00 24.78  ? 184 LEU A CB    1 
ATOM   1425 C CG    . LEU A 1 184 ? 32.195 -36.001 -34.952 1.00 25.32  ? 184 LEU A CG    1 
ATOM   1426 C CD1   . LEU A 1 184 ? 32.695 -36.391 -36.337 1.00 25.02  ? 184 LEU A CD1   1 
ATOM   1427 C CD2   . LEU A 1 184 ? 31.416 -34.701 -35.002 1.00 26.01  ? 184 LEU A CD2   1 
ATOM   1428 N N     . PRO A 1 185 ? 28.851 -38.071 -32.796 1.00 27.25  ? 185 PRO A N     1 
ATOM   1429 C CA    . PRO A 1 185 ? 27.899 -39.045 -32.262 1.00 27.63  ? 185 PRO A CA    1 
ATOM   1430 C C     . PRO A 1 185 ? 28.291 -40.512 -32.410 1.00 29.15  ? 185 PRO A C     1 
ATOM   1431 O O     . PRO A 1 185 ? 27.699 -41.359 -31.749 1.00 30.82  ? 185 PRO A O     1 
ATOM   1432 C CB    . PRO A 1 185 ? 26.632 -38.737 -33.051 1.00 27.54  ? 185 PRO A CB    1 
ATOM   1433 C CG    . PRO A 1 185 ? 26.769 -37.273 -33.334 1.00 29.44  ? 185 PRO A CG    1 
ATOM   1434 C CD    . PRO A 1 185 ? 28.221 -37.134 -33.735 1.00 29.47  ? 185 PRO A CD    1 
ATOM   1435 N N     . ASN A 1 186 ? 29.295 -40.808 -33.247 1.00 29.24  ? 186 ASN A N     1 
ATOM   1436 C CA    . ASN A 1 186 ? 29.749 -42.178 -33.431 1.00 31.18  ? 186 ASN A CA    1 
ATOM   1437 C C     . ASN A 1 186 ? 30.979 -42.466 -32.575 1.00 32.08  ? 186 ASN A C     1 
ATOM   1438 O O     . ASN A 1 186 ? 31.572 -43.531 -32.717 1.00 34.65  ? 186 ASN A O     1 
ATOM   1439 C CB    . ASN A 1 186 ? 30.129 -42.474 -34.882 1.00 31.63  ? 186 ASN A CB    1 
ATOM   1440 C CG    . ASN A 1 186 ? 31.284 -41.612 -35.340 1.00 33.36  ? 186 ASN A CG    1 
ATOM   1441 O OD1   . ASN A 1 186 ? 31.692 -40.692 -34.635 1.00 32.82  ? 186 ASN A OD1   1 
ATOM   1442 N ND2   . ASN A 1 186 ? 31.796 -41.877 -36.525 1.00 35.12  ? 186 ASN A ND2   1 
ATOM   1443 N N     . GLY A 1 187 ? 31.431 -41.488 -31.781 1.00 31.27  ? 187 GLY A N     1 
ATOM   1444 C CA    . GLY A 1 187 ? 32.573 -41.695 -30.901 1.00 30.82  ? 187 GLY A CA    1 
ATOM   1445 C C     . GLY A 1 187 ? 33.912 -41.207 -31.465 1.00 31.06  ? 187 GLY A C     1 
ATOM   1446 O O     . GLY A 1 187 ? 34.892 -41.156 -30.737 1.00 35.20  ? 187 GLY A O     1 
ATOM   1447 N N     . GLU A 1 188 ? 33.985 -40.848 -32.749 1.00 31.60  ? 188 GLU A N     1 
ATOM   1448 C CA    . GLU A 1 188 ? 35.223 -40.327 -33.309 1.00 32.72  ? 188 GLU A CA    1 
ATOM   1449 C C     . GLU A 1 188 ? 35.411 -38.857 -32.928 1.00 31.57  ? 188 GLU A C     1 
ATOM   1450 O O     . GLU A 1 188 ? 34.447 -38.128 -32.691 1.00 27.12  ? 188 GLU A O     1 
ATOM   1451 C CB    . GLU A 1 188 ? 35.203 -40.464 -34.830 1.00 36.41  ? 188 GLU A CB    1 
ATOM   1452 C CG    . GLU A 1 188 ? 35.092 -41.906 -35.295 1.00 41.07  ? 188 GLU A CG    1 
ATOM   1453 C CD    . GLU A 1 188 ? 36.198 -42.785 -34.740 1.00 42.55  ? 188 GLU A CD    1 
ATOM   1454 O OE1   . GLU A 1 188 ? 37.353 -42.607 -35.169 1.00 44.79  ? 188 GLU A OE1   1 
ATOM   1455 O OE2   . GLU A 1 188 ? 35.908 -43.595 -33.841 1.00 41.45  ? 188 GLU A OE2   1 
ATOM   1456 N N     . VAL A 1 189 ? 36.669 -38.406 -32.959 1.00 28.13  ? 189 VAL A N     1 
ATOM   1457 C CA    . VAL A 1 189 ? 36.999 -37.071 -32.516 1.00 27.21  ? 189 VAL A CA    1 
ATOM   1458 C C     . VAL A 1 189 ? 37.581 -36.280 -33.684 1.00 26.56  ? 189 VAL A C     1 
ATOM   1459 O O     . VAL A 1 189 ? 38.293 -36.830 -34.520 1.00 23.75  ? 189 VAL A O     1 
ATOM   1460 C CB    . VAL A 1 189 ? 37.930 -37.114 -31.292 1.00 28.27  ? 189 VAL A CB    1 
ATOM   1461 C CG1   . VAL A 1 189 ? 39.321 -37.617 -31.643 1.00 29.36  ? 189 VAL A CG1   1 
ATOM   1462 C CG2   . VAL A 1 189 ? 38.001 -35.761 -30.622 1.00 29.19  ? 189 VAL A CG2   1 
ATOM   1463 N N     . VAL A 1 190 ? 37.200 -34.992 -33.737 1.00 27.18  ? 190 VAL A N     1 
ATOM   1464 C CA    . VAL A 1 190 ? 37.644 -34.071 -34.763 1.00 27.35  ? 190 VAL A CA    1 
ATOM   1465 C C     . VAL A 1 190 ? 38.099 -32.766 -34.129 1.00 26.72  ? 190 VAL A C     1 
ATOM   1466 O O     . VAL A 1 190 ? 37.574 -32.337 -33.100 1.00 28.05  ? 190 VAL A O     1 
ATOM   1467 C CB    . VAL A 1 190 ? 36.535 -33.759 -35.772 1.00 28.85  ? 190 VAL A CB    1 
ATOM   1468 C CG1   . VAL A 1 190 ? 36.088 -35.003 -36.488 1.00 34.67  ? 190 VAL A CG1   1 
ATOM   1469 C CG2   . VAL A 1 190 ? 35.360 -33.090 -35.094 1.00 30.31  ? 190 VAL A CG2   1 
ATOM   1470 N N     . ARG A 1 191 ? 39.003 -32.096 -34.841 1.00 24.51  ? 191 ARG A N     1 
ATOM   1471 C CA    . ARG A 1 191 ? 39.374 -30.737 -34.515 1.00 26.82  ? 191 ARG A CA    1 
ATOM   1472 C C     . ARG A 1 191 ? 39.054 -29.852 -35.716 1.00 25.81  ? 191 ARG A C     1 
ATOM   1473 O O     . ARG A 1 191 ? 39.345 -30.211 -36.863 1.00 26.19  ? 191 ARG A O     1 
ATOM   1474 C CB    . ARG A 1 191 ? 40.854 -30.673 -34.125 1.00 26.49  ? 191 ARG A CB    1 
ATOM   1475 C CG    . ARG A 1 191 ? 41.172 -31.309 -32.786 1.00 24.61  ? 191 ARG A CG    1 
ATOM   1476 C CD    . ARG A 1 191 ? 42.618 -31.095 -32.389 1.00 25.89  ? 191 ARG A CD    1 
ATOM   1477 N NE    . ARG A 1 191 ? 42.854 -31.752 -31.109 1.00 30.35  ? 191 ARG A NE    1 
ATOM   1478 C CZ    . ARG A 1 191 ? 43.890 -31.529 -30.314 1.00 28.04  ? 191 ARG A CZ    1 
ATOM   1479 N NH1   . ARG A 1 191 ? 44.962 -30.927 -30.768 1.00 29.05  ? 191 ARG A NH1   1 
ATOM   1480 N NH2   . ARG A 1 191 ? 43.848 -31.923 -29.064 1.00 26.72  ? 191 ARG A NH2   1 
ATOM   1481 N N     . THR A 1 192 ? 38.424 -28.715 -35.414 1.00 23.72  ? 192 THR A N     1 
ATOM   1482 C CA    . THR A 1 192 ? 38.064 -27.715 -36.400 1.00 22.46  ? 192 THR A CA    1 
ATOM   1483 C C     . THR A 1 192 ? 39.186 -26.700 -36.593 1.00 21.71  ? 192 THR A C     1 
ATOM   1484 O O     . THR A 1 192 ? 40.132 -26.584 -35.793 1.00 21.30  ? 192 THR A O     1 
ATOM   1485 C CB    . THR A 1 192 ? 36.827 -26.942 -35.956 1.00 23.74  ? 192 THR A CB    1 
ATOM   1486 O OG1   . THR A 1 192 ? 37.175 -26.128 -34.830 1.00 23.16  ? 192 THR A OG1   1 
ATOM   1487 C CG2   . THR A 1 192 ? 35.690 -27.865 -35.599 1.00 24.85  ? 192 THR A CG2   1 
ATOM   1488 N N     . GLY A 1 193 ? 39.018 -25.920 -37.657 1.00 20.18  ? 193 GLY A N     1 
ATOM   1489 C CA    . GLY A 1 193 ? 39.935 -24.841 -37.971 1.00 20.31  ? 193 GLY A CA    1 
ATOM   1490 C C     . GLY A 1 193 ? 41.334 -25.368 -38.222 1.00 21.79  ? 193 GLY A C     1 
ATOM   1491 O O     . GLY A 1 193 ? 41.504 -26.402 -38.859 1.00 24.01  ? 193 GLY A O     1 
ATOM   1492 N N     . MET A 1 194 ? 42.321 -24.644 -37.699 1.00 23.32  ? 194 MET A N     1 
ATOM   1493 C CA    . MET A 1 194 ? 43.718 -24.971 -37.905 1.00 24.94  ? 194 MET A CA    1 
ATOM   1494 C C     . MET A 1 194 ? 44.097 -26.178 -37.035 1.00 23.94  ? 194 MET A C     1 
ATOM   1495 O O     . MET A 1 194 ? 45.112 -26.830 -37.254 1.00 23.18  ? 194 MET A O     1 
ATOM   1496 C CB    . MET A 1 194 ? 44.567 -23.751 -37.533 1.00 27.23  ? 194 MET A CB    1 
ATOM   1497 C CG    . MET A 1 194 ? 44.210 -22.518 -38.348 1.00 29.05  ? 194 MET A CG    1 
ATOM   1498 S SD    . MET A 1 194 ? 44.422 -22.727 -40.146 1.00 27.89  ? 194 MET A SD    1 
ATOM   1499 C CE    . MET A 1 194 ? 46.033 -23.491 -40.268 1.00 30.67  ? 194 MET A CE    1 
ATOM   1500 N N     . GLY A 1 195 ? 43.255 -26.503 -36.056 1.00 23.29  ? 195 GLY A N     1 
ATOM   1501 C CA    . GLY A 1 195 ? 43.463 -27.679 -35.233 1.00 24.30  ? 195 GLY A CA    1 
ATOM   1502 C C     . GLY A 1 195 ? 43.527 -28.959 -36.069 1.00 24.51  ? 195 GLY A C     1 
ATOM   1503 O O     . GLY A 1 195 ? 44.036 -29.983 -35.606 1.00 25.12  ? 195 GLY A O     1 
ATOM   1504 N N     . ALA A 1 196 ? 42.986 -28.909 -37.292 1.00 22.63  ? 196 ALA A N     1 
ATOM   1505 C CA    . ALA A 1 196 ? 42.951 -30.087 -38.141 1.00 23.29  ? 196 ALA A CA    1 
ATOM   1506 C C     . ALA A 1 196 ? 44.298 -30.310 -38.816 1.00 24.10  ? 196 ALA A C     1 
ATOM   1507 O O     . ALA A 1 196 ? 44.487 -31.335 -39.451 1.00 25.09  ? 196 ALA A O     1 
ATOM   1508 C CB    . ALA A 1 196 ? 41.853 -29.966 -39.166 1.00 23.54  ? 196 ALA A CB    1 
ATOM   1509 N N     . MET A 1 197 ? 45.207 -29.337 -38.705 1.00 26.75  ? 197 MET A N     1 
ATOM   1510 C CA    . MET A 1 197 ? 46.552 -29.454 -39.257 1.00 28.78  ? 197 MET A CA    1 
ATOM   1511 C C     . MET A 1 197 ? 47.551 -29.883 -38.171 1.00 26.50  ? 197 MET A C     1 
ATOM   1512 O O     . MET A 1 197 ? 47.813 -29.109 -37.259 1.00 25.58  ? 197 MET A O     1 
ATOM   1513 C CB    . MET A 1 197 ? 47.029 -28.122 -39.846 1.00 26.83  ? 197 MET A CB    1 
ATOM   1514 C CG    . MET A 1 197 ? 48.526 -28.055 -39.938 1.00 29.17  ? 197 MET A CG    1 
ATOM   1515 S SD    . MET A 1 197 ? 49.158 -27.042 -41.271 1.00 35.75  ? 197 MET A SD    1 
ATOM   1516 C CE    . MET A 1 197 ? 48.549 -27.947 -42.701 1.00 33.30  ? 197 MET A CE    1 
ATOM   1517 N N     . PRO A 1 198 ? 48.207 -31.064 -38.284 1.00 24.93  ? 198 PRO A N     1 
ATOM   1518 C CA    . PRO A 1 198 ? 49.244 -31.483 -37.330 1.00 28.52  ? 198 PRO A CA    1 
ATOM   1519 C C     . PRO A 1 198 ? 50.408 -30.499 -37.219 1.00 26.36  ? 198 PRO A C     1 
ATOM   1520 O O     . PRO A 1 198 ? 50.886 -29.982 -38.227 1.00 24.71  ? 198 PRO A O     1 
ATOM   1521 C CB    . PRO A 1 198 ? 49.775 -32.820 -37.883 1.00 29.48  ? 198 PRO A CB    1 
ATOM   1522 C CG    . PRO A 1 198 ? 48.704 -33.301 -38.832 1.00 28.04  ? 198 PRO A CG    1 
ATOM   1523 C CD    . PRO A 1 198 ? 48.013 -32.052 -39.347 1.00 26.15  ? 198 PRO A CD    1 
ATOM   1524 N N     . GLY A 1 199 ? 50.794 -30.196 -35.975 1.00 26.29  ? 199 GLY A N     1 
ATOM   1525 C CA    . GLY A 1 199 ? 51.902 -29.296 -35.684 1.00 25.37  ? 199 GLY A CA    1 
ATOM   1526 C C     . GLY A 1 199 ? 51.550 -27.816 -35.853 1.00 27.13  ? 199 GLY A C     1 
ATOM   1527 O O     . GLY A 1 199 ? 52.441 -26.982 -35.899 1.00 28.31  ? 199 GLY A O     1 
ATOM   1528 N N     . ASN A 1 200 ? 50.269 -27.467 -35.989 1.00 26.22  ? 200 ASN A N     1 
ATOM   1529 C CA    . ASN A 1 200 ? 49.913 -26.057 -36.089 1.00 29.21  ? 200 ASN A CA    1 
ATOM   1530 C C     . ASN A 1 200 ? 50.155 -25.389 -34.736 1.00 28.41  ? 200 ASN A C     1 
ATOM   1531 O O     . ASN A 1 200 ? 50.016 -26.044 -33.700 1.00 28.20  ? 200 ASN A O     1 
ATOM   1532 C CB    . ASN A 1 200 ? 48.438 -25.834 -36.438 1.00 27.24  ? 200 ASN A CB    1 
ATOM   1533 C CG    . ASN A 1 200 ? 47.557 -26.136 -35.244 1.00 26.18  ? 200 ASN A CG    1 
ATOM   1534 O OD1   . ASN A 1 200 ? 47.339 -25.264 -34.408 1.00 27.05  ? 200 ASN A OD1   1 
ATOM   1535 N ND2   . ASN A 1 200 ? 47.146 -27.385 -35.089 1.00 24.98  ? 200 ASN A ND2   1 
ATOM   1536 N N     . ASN A 1 201 ? 50.456 -24.084 -34.761 1.00 27.39  ? 201 ASN A N     1 
ATOM   1537 C CA    . ASN A 1 201 ? 50.378 -23.265 -33.561 1.00 29.93  ? 201 ASN A CA    1 
ATOM   1538 C C     . ASN A 1 201 ? 49.363 -22.135 -33.759 1.00 30.81  ? 201 ASN A C     1 
ATOM   1539 O O     . ASN A 1 201 ? 49.578 -21.028 -33.235 1.00 30.29  ? 201 ASN A O     1 
ATOM   1540 C CB    . ASN A 1 201 ? 51.760 -22.761 -33.139 1.00 33.59  ? 201 ASN A CB    1 
ATOM   1541 C CG    . ASN A 1 201 ? 52.654 -23.897 -32.684 1.00 36.13  ? 201 ASN A CG    1 
ATOM   1542 O OD1   . ASN A 1 201 ? 53.505 -24.368 -33.437 1.00 39.28  ? 201 ASN A OD1   1 
ATOM   1543 N ND2   . ASN A 1 201 ? 52.395 -24.418 -31.500 1.00 34.16  ? 201 ASN A ND2   1 
ATOM   1544 N N     . THR A 1 202 ? 48.254 -22.443 -34.478 1.00 26.89  ? 202 THR A N     1 
ATOM   1545 C CA    . THR A 1 202 ? 47.328 -21.422 -34.955 1.00 23.77  ? 202 THR A CA    1 
ATOM   1546 C C     . THR A 1 202 ? 45.855 -21.717 -34.673 1.00 20.25  ? 202 THR A C     1 
ATOM   1547 O O     . THR A 1 202 ? 44.989 -21.026 -35.183 1.00 19.60  ? 202 THR A O     1 
ATOM   1548 C CB    . THR A 1 202 ? 47.519 -21.195 -36.458 1.00 23.80  ? 202 THR A CB    1 
ATOM   1549 O OG1   . THR A 1 202 ? 47.434 -22.449 -37.117 1.00 23.36  ? 202 THR A OG1   1 
ATOM   1550 C CG2   . THR A 1 202 ? 48.839 -20.561 -36.795 1.00 24.67  ? 202 THR A CG2   1 
ATOM   1551 N N     . TRP A 1 203 ? 45.570 -22.736 -33.870 1.00 21.69  ? 203 TRP A N     1 
ATOM   1552 C CA    . TRP A 1 203 ? 44.220 -23.197 -33.596 1.00 21.94  ? 203 TRP A CA    1 
ATOM   1553 C C     . TRP A 1 203 ? 43.349 -22.073 -33.027 1.00 24.08  ? 203 TRP A C     1 
ATOM   1554 O O     . TRP A 1 203 ? 42.162 -21.979 -33.353 1.00 26.15  ? 203 TRP A O     1 
ATOM   1555 C CB    . TRP A 1 203 ? 44.286 -24.362 -32.608 1.00 21.30  ? 203 TRP A CB    1 
ATOM   1556 C CG    . TRP A 1 203 ? 43.083 -25.247 -32.595 1.00 22.45  ? 203 TRP A CG    1 
ATOM   1557 C CD1   . TRP A 1 203 ? 42.010 -25.253 -33.447 1.00 22.19  ? 203 TRP A CD1   1 
ATOM   1558 C CD2   . TRP A 1 203 ? 42.852 -26.309 -31.652 1.00 24.28  ? 203 TRP A CD2   1 
ATOM   1559 N NE1   . TRP A 1 203 ? 41.128 -26.253 -33.102 1.00 23.06  ? 203 TRP A NE1   1 
ATOM   1560 C CE2   . TRP A 1 203 ? 41.628 -26.925 -32.010 1.00 22.93  ? 203 TRP A CE2   1 
ATOM   1561 C CE3   . TRP A 1 203 ? 43.545 -26.769 -30.527 1.00 23.47  ? 203 TRP A CE3   1 
ATOM   1562 C CZ2   . TRP A 1 203 ? 41.102 -27.978 -31.271 1.00 21.89  ? 203 TRP A CZ2   1 
ATOM   1563 C CZ3   . TRP A 1 203 ? 43.020 -27.813 -29.801 1.00 23.01  ? 203 TRP A CZ3   1 
ATOM   1564 C CH2   . TRP A 1 203 ? 41.814 -28.406 -30.176 1.00 23.25  ? 203 TRP A CH2   1 
ATOM   1565 N N     . GLN A 1 204 ? 43.935 -21.273 -32.125 1.00 21.90  ? 204 GLN A N     1 
ATOM   1566 C CA    . GLN A 1 204 ? 43.224 -20.188 -31.473 1.00 22.28  ? 204 GLN A CA    1 
ATOM   1567 C C     . GLN A 1 204 ? 43.549 -18.837 -32.120 1.00 20.45  ? 204 GLN A C     1 
ATOM   1568 O O     . GLN A 1 204 ? 43.223 -17.824 -31.531 1.00 17.91  ? 204 GLN A O     1 
ATOM   1569 C CB    . GLN A 1 204 ? 43.599 -20.128 -29.986 1.00 22.88  ? 204 GLN A CB    1 
ATOM   1570 C CG    . GLN A 1 204 ? 42.862 -21.130 -29.114 1.00 24.06  ? 204 GLN A CG    1 
ATOM   1571 C CD    . GLN A 1 204 ? 43.070 -22.576 -29.509 1.00 26.59  ? 204 GLN A CD    1 
ATOM   1572 O OE1   . GLN A 1 204 ? 44.105 -23.182 -29.242 1.00 32.46  ? 204 GLN A OE1   1 
ATOM   1573 N NE2   . GLN A 1 204 ? 42.057 -23.166 -30.121 1.00 25.92  ? 204 GLN A NE2   1 
ATOM   1574 N N     . LEU A 1 205 ? 44.234 -18.813 -33.272 1.00 19.97  ? 205 LEU A N     1 
ATOM   1575 C CA    . LEU A 1 205 ? 44.600 -17.568 -33.937 1.00 21.35  ? 205 LEU A CA    1 
ATOM   1576 C C     . LEU A 1 205 ? 43.756 -17.275 -35.184 1.00 24.70  ? 205 LEU A C     1 
ATOM   1577 O O     . LEU A 1 205 ? 43.727 -16.120 -35.619 1.00 26.33  ? 205 LEU A O     1 
ATOM   1578 C CB    . LEU A 1 205 ? 46.068 -17.645 -34.351 1.00 22.16  ? 205 LEU A CB    1 
ATOM   1579 C CG    . LEU A 1 205 ? 47.070 -17.902 -33.225 1.00 21.87  ? 205 LEU A CG    1 
ATOM   1580 C CD1   . LEU A 1 205 ? 48.490 -17.740 -33.740 1.00 20.99  ? 205 LEU A CD1   1 
ATOM   1581 C CD2   . LEU A 1 205 ? 46.824 -16.977 -32.049 1.00 21.00  ? 205 LEU A CD2   1 
ATOM   1582 N N     . PHE A 1 206 ? 43.148 -18.313 -35.800 1.00 24.66  ? 206 PHE A N     1 
ATOM   1583 C CA    . PHE A 1 206 ? 42.447 -18.182 -37.078 1.00 24.84  ? 206 PHE A CA    1 
ATOM   1584 C C     . PHE A 1 206 ? 41.259 -19.140 -37.097 1.00 22.86  ? 206 PHE A C     1 
ATOM   1585 O O     . PHE A 1 206 ? 41.432 -20.354 -37.030 1.00 23.75  ? 206 PHE A O     1 
ATOM   1586 C CB    . PHE A 1 206 ? 43.394 -18.428 -38.266 1.00 23.88  ? 206 PHE A CB    1 
ATOM   1587 C CG    . PHE A 1 206 ? 42.754 -18.326 -39.629 1.00 22.11  ? 206 PHE A CG    1 
ATOM   1588 C CD1   . PHE A 1 206 ? 42.322 -17.103 -40.132 1.00 23.86  ? 206 PHE A CD1   1 
ATOM   1589 C CD2   . PHE A 1 206 ? 42.547 -19.453 -40.402 1.00 21.52  ? 206 PHE A CD2   1 
ATOM   1590 C CE1   . PHE A 1 206 ? 41.700 -17.014 -41.376 1.00 21.20  ? 206 PHE A CE1   1 
ATOM   1591 C CE2   . PHE A 1 206 ? 41.927 -19.360 -41.642 1.00 21.64  ? 206 PHE A CE2   1 
ATOM   1592 C CZ    . PHE A 1 206 ? 41.506 -18.141 -42.129 1.00 19.98  ? 206 PHE A CZ    1 
ATOM   1593 N N     . LYS A 1 207 ? 40.049 -18.585 -37.154 1.00 22.37  ? 207 LYS A N     1 
ATOM   1594 C CA    . LYS A 1 207 ? 38.846 -19.367 -36.937 1.00 24.62  ? 207 LYS A CA    1 
ATOM   1595 C C     . LYS A 1 207 ? 38.586 -20.378 -38.054 1.00 24.15  ? 207 LYS A C     1 
ATOM   1596 O O     . LYS A 1 207 ? 38.146 -21.492 -37.772 1.00 25.67  ? 207 LYS A O     1 
ATOM   1597 C CB    . LYS A 1 207 ? 37.598 -18.487 -36.902 1.00 27.13  ? 207 LYS A CB    1 
ATOM   1598 C CG    . LYS A 1 207 ? 37.337 -17.671 -35.651 1.00 28.55  ? 207 LYS A CG    1 
ATOM   1599 C CD    . LYS A 1 207 ? 36.228 -16.674 -35.947 1.00 31.07  ? 207 LYS A CD    1 
ATOM   1600 C CE    . LYS A 1 207 ? 35.485 -16.181 -34.730 1.00 32.30  ? 207 LYS A CE    1 
ATOM   1601 N NZ    . LYS A 1 207 ? 34.425 -17.129 -34.328 1.00 34.58  ? 207 LYS A NZ    1 
ATOM   1602 N N     . TYR A 1 208 ? 38.747 -19.972 -39.319 1.00 23.61  ? 208 TYR A N     1 
ATOM   1603 C CA    . TYR A 1 208 ? 38.132 -20.727 -40.409 1.00 25.64  ? 208 TYR A CA    1 
ATOM   1604 C C     . TYR A 1 208 ? 38.834 -22.062 -40.640 1.00 24.61  ? 208 TYR A C     1 
ATOM   1605 O O     . TYR A 1 208 ? 38.188 -23.060 -40.916 1.00 24.76  ? 208 TYR A O     1 
ATOM   1606 C CB    . TYR A 1 208 ? 38.143 -19.949 -41.732 1.00 25.59  ? 208 TYR A CB    1 
ATOM   1607 C CG    . TYR A 1 208 ? 37.329 -18.680 -41.727 1.00 26.92  ? 208 TYR A CG    1 
ATOM   1608 C CD1   . TYR A 1 208 ? 36.024 -18.671 -41.284 1.00 27.48  ? 208 TYR A CD1   1 
ATOM   1609 C CD2   . TYR A 1 208 ? 37.873 -17.476 -42.136 1.00 27.65  ? 208 TYR A CD2   1 
ATOM   1610 C CE1   . TYR A 1 208 ? 35.296 -17.494 -41.223 1.00 28.74  ? 208 TYR A CE1   1 
ATOM   1611 C CE2   . TYR A 1 208 ? 37.149 -16.299 -42.107 1.00 27.10  ? 208 TYR A CE2   1 
ATOM   1612 C CZ    . TYR A 1 208 ? 35.845 -16.311 -41.664 1.00 26.18  ? 208 TYR A CZ    1 
ATOM   1613 O OH    . TYR A 1 208 ? 35.120 -15.161 -41.612 1.00 25.68  ? 208 TYR A OH    1 
ATOM   1614 N N     . GLY A 1 209 ? 40.165 -22.065 -40.570 1.00 24.51  ? 209 GLY A N     1 
ATOM   1615 C CA    . GLY A 1 209 ? 40.925 -23.099 -41.244 1.00 23.78  ? 209 GLY A CA    1 
ATOM   1616 C C     . GLY A 1 209 ? 40.614 -23.108 -42.735 1.00 22.15  ? 209 GLY A C     1 
ATOM   1617 O O     . GLY A 1 209 ? 40.665 -22.070 -43.384 1.00 21.11  ? 209 GLY A O     1 
ATOM   1618 N N     . TYR A 1 210 ? 40.257 -24.286 -43.258 1.00 21.04  ? 210 TYR A N     1 
ATOM   1619 C CA    . TYR A 1 210 ? 40.027 -24.442 -44.680 1.00 21.11  ? 210 TYR A CA    1 
ATOM   1620 C C     . TYR A 1 210 ? 38.746 -25.233 -44.873 1.00 21.05  ? 210 TYR A C     1 
ATOM   1621 O O     . TYR A 1 210 ? 38.431 -26.143 -44.102 1.00 20.55  ? 210 TYR A O     1 
ATOM   1622 C CB    . TYR A 1 210 ? 41.262 -25.052 -45.355 1.00 23.02  ? 210 TYR A CB    1 
ATOM   1623 C CG    . TYR A 1 210 ? 41.115 -25.504 -46.792 1.00 23.56  ? 210 TYR A CG    1 
ATOM   1624 C CD1   . TYR A 1 210 ? 40.983 -24.598 -47.836 1.00 24.40  ? 210 TYR A CD1   1 
ATOM   1625 C CD2   . TYR A 1 210 ? 41.127 -26.851 -47.121 1.00 25.18  ? 210 TYR A CD2   1 
ATOM   1626 C CE1   . TYR A 1 210 ? 40.855 -25.015 -49.154 1.00 23.28  ? 210 TYR A CE1   1 
ATOM   1627 C CE2   . TYR A 1 210 ? 41.027 -27.283 -48.439 1.00 24.02  ? 210 TYR A CE2   1 
ATOM   1628 C CZ    . TYR A 1 210 ? 40.900 -26.363 -49.459 1.00 23.67  ? 210 TYR A CZ    1 
ATOM   1629 O OH    . TYR A 1 210 ? 40.788 -26.802 -50.759 1.00 23.72  ? 210 TYR A OH    1 
ATOM   1630 N N     . GLY A 1 211 ? 37.997 -24.838 -45.908 1.00 20.90  ? 211 GLY A N     1 
ATOM   1631 C CA    . GLY A 1 211 ? 36.790 -25.556 -46.266 1.00 21.05  ? 211 GLY A CA    1 
ATOM   1632 C C     . GLY A 1 211 ? 35.608 -24.998 -45.493 1.00 21.07  ? 211 GLY A C     1 
ATOM   1633 O O     . GLY A 1 211 ? 35.655 -23.864 -45.025 1.00 22.73  ? 211 GLY A O     1 
ATOM   1634 N N     . PRO A 1 212 ? 34.508 -25.759 -45.395 1.00 20.03  ? 212 PRO A N     1 
ATOM   1635 C CA    . PRO A 1 212 ? 33.327 -25.315 -44.671 1.00 21.40  ? 212 PRO A CA    1 
ATOM   1636 C C     . PRO A 1 212 ? 33.587 -24.944 -43.215 1.00 21.08  ? 212 PRO A C     1 
ATOM   1637 O O     . PRO A 1 212 ? 34.242 -25.684 -42.469 1.00 19.24  ? 212 PRO A O     1 
ATOM   1638 C CB    . PRO A 1 212 ? 32.369 -26.509 -44.746 1.00 20.95  ? 212 PRO A CB    1 
ATOM   1639 C CG    . PRO A 1 212 ? 32.802 -27.237 -45.990 1.00 21.85  ? 212 PRO A CG    1 
ATOM   1640 C CD    . PRO A 1 212 ? 34.302 -27.050 -46.048 1.00 21.92  ? 212 PRO A CD    1 
ATOM   1641 N N     . TYR A 1 213 ? 32.974 -23.822 -42.817 1.00 20.87  ? 213 TYR A N     1 
ATOM   1642 C CA    . TYR A 1 213 ? 33.017 -23.358 -41.439 1.00 23.30  ? 213 TYR A CA    1 
ATOM   1643 C C     . TYR A 1 213 ? 31.945 -24.070 -40.600 1.00 23.29  ? 213 TYR A C     1 
ATOM   1644 O O     . TYR A 1 213 ? 30.757 -23.843 -40.780 1.00 24.70  ? 213 TYR A O     1 
ATOM   1645 C CB    . TYR A 1 213 ? 32.882 -21.839 -41.451 1.00 24.16  ? 213 TYR A CB    1 
ATOM   1646 C CG    . TYR A 1 213 ? 33.147 -21.193 -40.131 1.00 30.73  ? 213 TYR A CG    1 
ATOM   1647 C CD1   . TYR A 1 213 ? 34.234 -21.582 -39.361 1.00 31.23  ? 213 TYR A CD1   1 
ATOM   1648 C CD2   . TYR A 1 213 ? 32.300 -20.219 -39.631 1.00 39.77  ? 213 TYR A CD2   1 
ATOM   1649 C CE1   . TYR A 1 213 ? 34.467 -21.019 -38.123 1.00 34.58  ? 213 TYR A CE1   1 
ATOM   1650 C CE2   . TYR A 1 213 ? 32.534 -19.631 -38.398 1.00 43.72  ? 213 TYR A CE2   1 
ATOM   1651 C CZ    . TYR A 1 213 ? 33.622 -20.034 -37.647 1.00 37.18  ? 213 TYR A CZ    1 
ATOM   1652 O OH    . TYR A 1 213 ? 33.889 -19.478 -36.443 1.00 41.51  ? 213 TYR A OH    1 
ATOM   1653 N N     . VAL A 1 214 ? 32.362 -24.951 -39.679 1.00 22.64  ? 214 VAL A N     1 
ATOM   1654 C CA    . VAL A 1 214 ? 31.431 -25.863 -39.032 1.00 22.24  ? 214 VAL A CA    1 
ATOM   1655 C C     . VAL A 1 214 ? 31.361 -25.663 -37.517 1.00 21.67  ? 214 VAL A C     1 
ATOM   1656 O O     . VAL A 1 214 ? 30.510 -26.287 -36.892 1.00 20.66  ? 214 VAL A O     1 
ATOM   1657 C CB    . VAL A 1 214 ? 31.780 -27.333 -39.345 1.00 24.08  ? 214 VAL A CB    1 
ATOM   1658 C CG1   . VAL A 1 214 ? 31.674 -27.636 -40.823 1.00 24.43  ? 214 VAL A CG1   1 
ATOM   1659 C CG2   . VAL A 1 214 ? 33.166 -27.706 -38.843 1.00 27.62  ? 214 VAL A CG2   1 
ATOM   1660 N N     . ASP A 1 215 ? 32.228 -24.836 -36.908 1.00 21.69  ? 215 ASP A N     1 
ATOM   1661 C CA    . ASP A 1 215 ? 32.206 -24.694 -35.458 1.00 23.04  ? 215 ASP A CA    1 
ATOM   1662 C C     . ASP A 1 215 ? 30.781 -24.395 -34.996 1.00 22.39  ? 215 ASP A C     1 
ATOM   1663 O O     . ASP A 1 215 ? 30.310 -25.017 -34.059 1.00 23.42  ? 215 ASP A O     1 
ATOM   1664 C CB    . ASP A 1 215 ? 33.194 -23.636 -34.950 1.00 25.23  ? 215 ASP A CB    1 
ATOM   1665 C CG    . ASP A 1 215 ? 34.647 -23.969 -35.277 1.00 25.95  ? 215 ASP A CG    1 
ATOM   1666 O OD1   . ASP A 1 215 ? 34.937 -24.082 -36.471 1.00 26.95  ? 215 ASP A OD1   1 
ATOM   1667 O OD2   . ASP A 1 215 ? 35.468 -24.135 -34.336 1.00 23.12  ? 215 ASP A OD2   1 
ATOM   1668 N N     . GLY A 1 216 ? 30.102 -23.481 -35.707 1.00 21.19  ? 216 GLY A N     1 
ATOM   1669 C CA    . GLY A 1 216 ? 28.750 -23.052 -35.419 1.00 19.67  ? 216 GLY A CA    1 
ATOM   1670 C C     . GLY A 1 216 ? 27.734 -24.183 -35.327 1.00 20.08  ? 216 GLY A C     1 
ATOM   1671 O O     . GLY A 1 216 ? 26.766 -24.065 -34.599 1.00 22.43  ? 216 GLY A O     1 
ATOM   1672 N N     . ILE A 1 217 ? 27.924 -25.292 -36.040 1.00 20.90  ? 217 ILE A N     1 
ATOM   1673 C CA    . ILE A 1 217 ? 26.910 -26.330 -35.998 1.00 22.84  ? 217 ILE A CA    1 
ATOM   1674 C C     . ILE A 1 217 ? 26.950 -27.064 -34.658 1.00 24.56  ? 217 ILE A C     1 
ATOM   1675 O O     . ILE A 1 217 ? 26.047 -27.854 -34.399 1.00 25.50  ? 217 ILE A O     1 
ATOM   1676 C CB    . ILE A 1 217 ? 26.992 -27.329 -37.172 1.00 23.23  ? 217 ILE A CB    1 
ATOM   1677 C CG1   . ILE A 1 217 ? 28.020 -28.443 -36.929 1.00 23.84  ? 217 ILE A CG1   1 
ATOM   1678 C CG2   . ILE A 1 217 ? 27.207 -26.598 -38.492 1.00 22.25  ? 217 ILE A CG2   1 
ATOM   1679 C CD1   . ILE A 1 217 ? 28.061 -29.505 -38.040 1.00 24.81  ? 217 ILE A CD1   1 
ATOM   1680 N N     . PHE A 1 218 ? 28.001 -26.864 -33.845 1.00 23.50  ? 218 PHE A N     1 
ATOM   1681 C CA    . PHE A 1 218 ? 28.062 -27.513 -32.550 1.00 23.77  ? 218 PHE A CA    1 
ATOM   1682 C C     . PHE A 1 218 ? 27.554 -26.588 -31.442 1.00 25.22  ? 218 PHE A C     1 
ATOM   1683 O O     . PHE A 1 218 ? 27.654 -26.929 -30.258 1.00 27.21  ? 218 PHE A O     1 
ATOM   1684 C CB    . PHE A 1 218 ? 29.467 -28.054 -32.310 1.00 22.66  ? 218 PHE A CB    1 
ATOM   1685 C CG    . PHE A 1 218 ? 29.857 -29.085 -33.329 1.00 22.95  ? 218 PHE A CG    1 
ATOM   1686 C CD1   . PHE A 1 218 ? 29.215 -30.322 -33.365 1.00 24.16  ? 218 PHE A CD1   1 
ATOM   1687 C CD2   . PHE A 1 218 ? 30.836 -28.814 -34.272 1.00 21.95  ? 218 PHE A CD2   1 
ATOM   1688 C CE1   . PHE A 1 218 ? 29.562 -31.270 -34.318 1.00 23.56  ? 218 PHE A CE1   1 
ATOM   1689 C CE2   . PHE A 1 218 ? 31.138 -29.740 -35.261 1.00 22.40  ? 218 PHE A CE2   1 
ATOM   1690 C CZ    . PHE A 1 218 ? 30.509 -30.967 -35.276 1.00 23.64  ? 218 PHE A CZ    1 
ATOM   1691 N N     . SER A 1 219 ? 26.993 -25.428 -31.812 1.00 25.73  ? 219 SER A N     1 
ATOM   1692 C CA    . SER A 1 219 ? 26.400 -24.526 -30.826 1.00 23.64  ? 219 SER A CA    1 
ATOM   1693 C C     . SER A 1 219 ? 24.886 -24.685 -30.871 1.00 24.03  ? 219 SER A C     1 
ATOM   1694 O O     . SER A 1 219 ? 24.327 -24.911 -31.952 1.00 26.62  ? 219 SER A O     1 
ATOM   1695 C CB    . SER A 1 219 ? 26.838 -23.102 -31.018 1.00 22.07  ? 219 SER A CB    1 
ATOM   1696 O OG    . SER A 1 219 ? 26.363 -22.537 -32.235 1.00 21.07  ? 219 SER A OG    1 
ATOM   1697 N N     . GLN A 1 220 ? 24.253 -24.600 -29.691 1.00 22.15  ? 220 GLN A N     1 
ATOM   1698 C CA    . GLN A 1 220 ? 22.825 -24.827 -29.530 1.00 21.72  ? 220 GLN A CA    1 
ATOM   1699 C C     . GLN A 1 220 ? 22.438 -26.068 -30.331 1.00 23.52  ? 220 GLN A C     1 
ATOM   1700 O O     . GLN A 1 220 ? 21.447 -26.037 -31.088 1.00 20.19  ? 220 GLN A O     1 
ATOM   1701 C CB    . GLN A 1 220 ? 22.010 -23.594 -29.936 1.00 22.30  ? 220 GLN A CB    1 
ATOM   1702 C CG    . GLN A 1 220 ? 21.980 -22.495 -28.892 1.00 23.19  ? 220 GLN A CG    1 
ATOM   1703 C CD    . GLN A 1 220 ? 20.904 -21.442 -29.080 1.00 25.60  ? 220 GLN A CD    1 
ATOM   1704 O OE1   . GLN A 1 220 ? 20.162 -21.427 -30.065 1.00 26.73  ? 220 GLN A OE1   1 
ATOM   1705 N NE2   . GLN A 1 220 ? 20.788 -20.556 -28.097 1.00 24.80  ? 220 GLN A NE2   1 
ATOM   1706 N N     . SER A 1 221 ? 23.222 -27.154 -30.103 1.00 24.62  ? 221 SER A N     1 
ATOM   1707 C CA    . SER A 1 221 ? 23.226 -28.320 -30.975 1.00 26.46  ? 221 SER A CA    1 
ATOM   1708 C C     . SER A 1 221 ? 23.253 -29.639 -30.211 1.00 26.06  ? 221 SER A C     1 
ATOM   1709 O O     . SER A 1 221 ? 23.767 -29.708 -29.099 1.00 28.10  ? 221 SER A O     1 
ATOM   1710 C CB    . SER A 1 221 ? 24.417 -28.303 -31.897 1.00 27.68  ? 221 SER A CB    1 
ATOM   1711 O OG    . SER A 1 221 ? 24.268 -29.334 -32.861 1.00 30.86  ? 221 SER A OG    1 
ATOM   1712 N N     . ASN A 1 222 ? 22.803 -30.698 -30.898 1.00 24.75  ? 222 ASN A N     1 
ATOM   1713 C CA    . ASN A 1 222 ? 23.027 -32.061 -30.460 1.00 25.11  ? 222 ASN A CA    1 
ATOM   1714 C C     . ASN A 1 222 ? 23.778 -32.843 -31.543 1.00 26.03  ? 222 ASN A C     1 
ATOM   1715 O O     . ASN A 1 222 ? 23.532 -34.031 -31.722 1.00 28.44  ? 222 ASN A O     1 
ATOM   1716 C CB    . ASN A 1 222 ? 21.708 -32.722 -30.050 1.00 25.51  ? 222 ASN A CB    1 
ATOM   1717 C CG    . ASN A 1 222 ? 20.627 -32.665 -31.107 1.00 27.04  ? 222 ASN A CG    1 
ATOM   1718 O OD1   . ASN A 1 222 ? 20.870 -32.286 -32.253 1.00 26.30  ? 222 ASN A OD1   1 
ATOM   1719 N ND2   . ASN A 1 222 ? 19.434 -33.107 -30.737 1.00 29.24  ? 222 ASN A ND2   1 
ATOM   1720 N N     . PHE A 1 223 ? 24.719 -32.180 -32.229 1.00 24.37  ? 223 PHE A N     1 
ATOM   1721 C CA    . PHE A 1 223 ? 25.491 -32.780 -33.308 1.00 25.16  ? 223 PHE A CA    1 
ATOM   1722 C C     . PHE A 1 223 ? 26.844 -33.302 -32.810 1.00 26.35  ? 223 PHE A C     1 
ATOM   1723 O O     . PHE A 1 223 ? 27.562 -33.971 -33.552 1.00 23.05  ? 223 PHE A O     1 
ATOM   1724 C CB    . PHE A 1 223 ? 25.720 -31.765 -34.434 1.00 23.07  ? 223 PHE A CB    1 
ATOM   1725 C CG    . PHE A 1 223 ? 24.488 -31.344 -35.190 1.00 21.63  ? 223 PHE A CG    1 
ATOM   1726 C CD1   . PHE A 1 223 ? 23.302 -32.030 -35.083 1.00 21.12  ? 223 PHE A CD1   1 
ATOM   1727 C CD2   . PHE A 1 223 ? 24.518 -30.234 -36.012 1.00 23.47  ? 223 PHE A CD2   1 
ATOM   1728 C CE1   . PHE A 1 223 ? 22.177 -31.623 -35.781 1.00 22.00  ? 223 PHE A CE1   1 
ATOM   1729 C CE2   . PHE A 1 223 ? 23.391 -29.816 -36.699 1.00 22.68  ? 223 PHE A CE2   1 
ATOM   1730 C CZ    . PHE A 1 223 ? 22.216 -30.505 -36.576 1.00 22.20  ? 223 PHE A CZ    1 
ATOM   1731 N N     . GLY A 1 224 ? 27.195 -33.010 -31.554 1.00 24.88  ? 224 GLY A N     1 
ATOM   1732 C CA    . GLY A 1 224 ? 28.463 -33.489 -31.037 1.00 25.74  ? 224 GLY A CA    1 
ATOM   1733 C C     . GLY A 1 224 ? 28.712 -33.075 -29.595 1.00 24.51  ? 224 GLY A C     1 
ATOM   1734 O O     . GLY A 1 224 ? 27.993 -32.260 -29.043 1.00 29.14  ? 224 GLY A O     1 
ATOM   1735 N N     . VAL A 1 225 ? 29.755 -33.646 -29.007 1.00 25.39  ? 225 VAL A N     1 
ATOM   1736 C CA    . VAL A 1 225 ? 30.192 -33.287 -27.671 1.00 25.52  ? 225 VAL A CA    1 
ATOM   1737 C C     . VAL A 1 225 ? 31.510 -32.516 -27.792 1.00 25.70  ? 225 VAL A C     1 
ATOM   1738 O O     . VAL A 1 225 ? 32.512 -33.068 -28.238 1.00 26.58  ? 225 VAL A O     1 
ATOM   1739 C CB    . VAL A 1 225 ? 30.329 -34.548 -26.791 1.00 26.34  ? 225 VAL A CB    1 
ATOM   1740 C CG1   . VAL A 1 225 ? 30.700 -34.212 -25.356 1.00 26.45  ? 225 VAL A CG1   1 
ATOM   1741 C CG2   . VAL A 1 225 ? 29.068 -35.396 -26.819 1.00 28.07  ? 225 VAL A CG2   1 
ATOM   1742 N N     . VAL A 1 226 ? 31.499 -31.242 -27.378 1.00 24.79  ? 226 VAL A N     1 
ATOM   1743 C CA    . VAL A 1 226 ? 32.684 -30.403 -27.410 1.00 24.99  ? 226 VAL A CA    1 
ATOM   1744 C C     . VAL A 1 226 ? 33.540 -30.725 -26.185 1.00 24.00  ? 226 VAL A C     1 
ATOM   1745 O O     . VAL A 1 226 ? 33.042 -30.688 -25.065 1.00 19.87  ? 226 VAL A O     1 
ATOM   1746 C CB    . VAL A 1 226 ? 32.315 -28.902 -27.496 1.00 25.30  ? 226 VAL A CB    1 
ATOM   1747 C CG1   . VAL A 1 226 ? 33.550 -28.024 -27.482 1.00 25.20  ? 226 VAL A CG1   1 
ATOM   1748 C CG2   . VAL A 1 226 ? 31.460 -28.578 -28.729 1.00 26.19  ? 226 VAL A CG2   1 
ATOM   1749 N N     . THR A 1 227 ? 34.846 -30.974 -26.404 1.00 24.30  ? 227 THR A N     1 
ATOM   1750 C CA    . THR A 1 227 ? 35.732 -31.406 -25.327 1.00 25.04  ? 227 THR A CA    1 
ATOM   1751 C C     . THR A 1 227 ? 36.903 -30.442 -25.089 1.00 26.45  ? 227 THR A C     1 
ATOM   1752 O O     . THR A 1 227 ? 37.528 -30.465 -24.019 1.00 27.89  ? 227 THR A O     1 
ATOM   1753 C CB    . THR A 1 227 ? 36.213 -32.838 -25.595 1.00 24.63  ? 227 THR A CB    1 
ATOM   1754 O OG1   . THR A 1 227 ? 36.939 -32.884 -26.827 1.00 24.33  ? 227 THR A OG1   1 
ATOM   1755 C CG2   . THR A 1 227 ? 35.067 -33.822 -25.652 1.00 23.86  ? 227 THR A CG2   1 
ATOM   1756 N N     . LYS A 1 228 ? 37.240 -29.640 -26.102 1.00 25.07  ? 228 LYS A N     1 
ATOM   1757 C CA    . LYS A 1 228 ? 38.111 -28.492 -25.932 1.00 25.51  ? 228 LYS A CA    1 
ATOM   1758 C C     . LYS A 1 228 ? 37.576 -27.330 -26.758 1.00 25.31  ? 228 LYS A C     1 
ATOM   1759 O O     . LYS A 1 228 ? 36.931 -27.550 -27.782 1.00 27.72  ? 228 LYS A O     1 
ATOM   1760 C CB    . LYS A 1 228 ? 39.521 -28.801 -26.431 1.00 26.55  ? 228 LYS A CB    1 
ATOM   1761 C CG    . LYS A 1 228 ? 40.186 -30.022 -25.817 1.00 26.35  ? 228 LYS A CG    1 
ATOM   1762 C CD    . LYS A 1 228 ? 41.473 -30.396 -26.517 1.00 26.36  ? 228 LYS A CD    1 
ATOM   1763 C CE    . LYS A 1 228 ? 42.261 -31.448 -25.766 1.00 25.58  ? 228 LYS A CE    1 
ATOM   1764 N NZ    . LYS A 1 228 ? 41.463 -32.688 -25.665 1.00 27.49  ? 228 LYS A NZ    1 
ATOM   1765 N N     . MET A 1 229 ? 37.880 -26.103 -26.342 1.00 23.07  ? 229 MET A N     1 
ATOM   1766 C CA    . MET A 1 229 ? 37.454 -24.944 -27.094 1.00 24.48  ? 229 MET A CA    1 
ATOM   1767 C C     . MET A 1 229 ? 38.403 -23.787 -26.815 1.00 24.09  ? 229 MET A C     1 
ATOM   1768 O O     . MET A 1 229 ? 38.746 -23.498 -25.676 1.00 25.10  ? 229 MET A O     1 
ATOM   1769 C CB    . MET A 1 229 ? 36.025 -24.540 -26.711 1.00 27.10  ? 229 MET A CB    1 
ATOM   1770 C CG    . MET A 1 229 ? 35.453 -23.411 -27.559 1.00 27.14  ? 229 MET A CG    1 
ATOM   1771 S SD    . MET A 1 229 ? 33.886 -22.787 -26.891 1.00 28.10  ? 229 MET A SD    1 
ATOM   1772 C CE    . MET A 1 229 ? 34.561 -21.608 -25.721 1.00 25.07  ? 229 MET A CE    1 
ATOM   1773 N N     . GLY A 1 230 ? 38.823 -23.123 -27.879 1.00 22.40  ? 230 GLY A N     1 
ATOM   1774 C CA    . GLY A 1 230 ? 39.565 -21.899 -27.700 1.00 22.53  ? 230 GLY A CA    1 
ATOM   1775 C C     . GLY A 1 230 ? 38.624 -20.705 -27.609 1.00 21.14  ? 230 GLY A C     1 
ATOM   1776 O O     . GLY A 1 230 ? 37.506 -20.728 -28.126 1.00 18.96  ? 230 GLY A O     1 
ATOM   1777 N N     . ILE A 1 231 ? 39.127 -19.643 -26.980 1.00 21.62  ? 231 ILE A N     1 
ATOM   1778 C CA    . ILE A 1 231 ? 38.394 -18.405 -26.913 1.00 21.09  ? 231 ILE A CA    1 
ATOM   1779 C C     . ILE A 1 231 ? 39.363 -17.240 -26.850 1.00 22.20  ? 231 ILE A C     1 
ATOM   1780 O O     . ILE A 1 231 ? 40.371 -17.270 -26.137 1.00 23.30  ? 231 ILE A O     1 
ATOM   1781 C CB    . ILE A 1 231 ? 37.399 -18.403 -25.743 1.00 21.06  ? 231 ILE A CB    1 
ATOM   1782 C CG1   . ILE A 1 231 ? 36.476 -17.188 -25.841 1.00 21.20  ? 231 ILE A CG1   1 
ATOM   1783 C CG2   . ILE A 1 231 ? 38.111 -18.458 -24.409 1.00 21.64  ? 231 ILE A CG2   1 
ATOM   1784 C CD1   . ILE A 1 231 ? 35.307 -17.265 -24.926 1.00 23.08  ? 231 ILE A CD1   1 
ATOM   1785 N N     . TRP A 1 232 ? 39.009 -16.197 -27.606 1.00 22.52  ? 232 TRP A N     1 
ATOM   1786 C CA    . TRP A 1 232 ? 39.770 -14.966 -27.595 1.00 25.45  ? 232 TRP A CA    1 
ATOM   1787 C C     . TRP A 1 232 ? 39.509 -14.222 -26.283 1.00 25.50  ? 232 TRP A C     1 
ATOM   1788 O O     . TRP A 1 232 ? 38.373 -14.183 -25.800 1.00 23.07  ? 232 TRP A O     1 
ATOM   1789 C CB    . TRP A 1 232 ? 39.437 -14.142 -28.847 1.00 27.01  ? 232 TRP A CB    1 
ATOM   1790 C CG    . TRP A 1 232 ? 39.881 -14.786 -30.131 1.00 27.49  ? 232 TRP A CG    1 
ATOM   1791 C CD1   . TRP A 1 232 ? 40.872 -15.711 -30.295 1.00 28.38  ? 232 TRP A CD1   1 
ATOM   1792 C CD2   . TRP A 1 232 ? 39.362 -14.536 -31.451 1.00 29.99  ? 232 TRP A CD2   1 
ATOM   1793 N NE1   . TRP A 1 232 ? 41.005 -16.051 -31.615 1.00 28.15  ? 232 TRP A NE1   1 
ATOM   1794 C CE2   . TRP A 1 232 ? 40.090 -15.356 -32.348 1.00 28.96  ? 232 TRP A CE2   1 
ATOM   1795 C CE3   . TRP A 1 232 ? 38.353 -13.707 -31.965 1.00 29.39  ? 232 TRP A CE3   1 
ATOM   1796 C CZ2   . TRP A 1 232 ? 39.850 -15.359 -33.721 1.00 29.95  ? 232 TRP A CZ2   1 
ATOM   1797 C CZ3   . TRP A 1 232 ? 38.100 -13.727 -33.321 1.00 28.55  ? 232 TRP A CZ3   1 
ATOM   1798 C CH2   . TRP A 1 232 ? 38.841 -14.543 -34.185 1.00 30.47  ? 232 TRP A CH2   1 
ATOM   1799 N N     . LEU A 1 233 ? 40.594 -13.670 -25.718 1.00 26.04  ? 233 LEU A N     1 
ATOM   1800 C CA    . LEU A 1 233 ? 40.559 -12.874 -24.498 1.00 26.17  ? 233 LEU A CA    1 
ATOM   1801 C C     . LEU A 1 233 ? 41.047 -11.451 -24.791 1.00 25.70  ? 233 LEU A C     1 
ATOM   1802 O O     . LEU A 1 233 ? 42.070 -11.240 -25.441 1.00 26.63  ? 233 LEU A O     1 
ATOM   1803 C CB    . LEU A 1 233 ? 41.479 -13.530 -23.462 1.00 27.29  ? 233 LEU A CB    1 
ATOM   1804 C CG    . LEU A 1 233 ? 41.111 -14.931 -22.979 1.00 28.79  ? 233 LEU A CG    1 
ATOM   1805 C CD1   . LEU A 1 233 ? 42.075 -15.400 -21.884 1.00 28.35  ? 233 LEU A CD1   1 
ATOM   1806 C CD2   . LEU A 1 233 ? 39.681 -14.975 -22.475 1.00 29.42  ? 233 LEU A CD2   1 
ATOM   1807 N N     . MET A 1 234 ? 40.366 -10.458 -24.235 1.00 24.70  ? 234 MET A N     1 
ATOM   1808 C CA    . MET A 1 234 ? 40.756 -9.083  -24.463 1.00 25.74  ? 234 MET A CA    1 
ATOM   1809 C C     . MET A 1 234 ? 42.026 -8.737  -23.671 1.00 24.52  ? 234 MET A C     1 
ATOM   1810 O O     . MET A 1 234 ? 42.127 -8.974  -22.475 1.00 20.10  ? 234 MET A O     1 
ATOM   1811 C CB    . MET A 1 234 ? 39.620 -8.155  -24.038 1.00 28.90  ? 234 MET A CB    1 
ATOM   1812 C CG    . MET A 1 234 ? 39.937 -6.695  -24.206 1.00 29.97  ? 234 MET A CG    1 
ATOM   1813 S SD    . MET A 1 234 ? 38.443 -5.696  -24.149 1.00 32.98  ? 234 MET A SD    1 
ATOM   1814 C CE    . MET A 1 234 ? 38.134 -5.687  -22.389 1.00 37.12  ? 234 MET A CE    1 
ATOM   1815 N N     . PRO A 1 235 ? 43.042 -8.133  -24.314 1.00 23.31  ? 235 PRO A N     1 
ATOM   1816 C CA    . PRO A 1 235 ? 44.150 -7.519  -23.601 1.00 24.78  ? 235 PRO A CA    1 
ATOM   1817 C C     . PRO A 1 235 ? 43.621 -6.429  -22.681 1.00 26.44  ? 235 PRO A C     1 
ATOM   1818 O O     . PRO A 1 235 ? 42.677 -5.711  -23.011 1.00 27.32  ? 235 PRO A O     1 
ATOM   1819 C CB    . PRO A 1 235 ? 45.018 -6.865  -24.685 1.00 23.85  ? 235 PRO A CB    1 
ATOM   1820 C CG    . PRO A 1 235 ? 44.627 -7.587  -25.940 1.00 25.29  ? 235 PRO A CG    1 
ATOM   1821 C CD    . PRO A 1 235 ? 43.170 -7.964  -25.762 1.00 24.84  ? 235 PRO A CD    1 
ATOM   1822 N N     . GLU A 1 236 ? 44.261 -6.307  -21.530 1.00 28.22  ? 236 GLU A N     1 
ATOM   1823 C CA    . GLU A 1 236 ? 43.883 -5.292  -20.568 1.00 30.64  ? 236 GLU A CA    1 
ATOM   1824 C C     . GLU A 1 236 ? 43.981 -3.936  -21.256 1.00 27.23  ? 236 GLU A C     1 
ATOM   1825 O O     . GLU A 1 236 ? 44.995 -3.630  -21.867 1.00 26.16  ? 236 GLU A O     1 
ATOM   1826 C CB    . GLU A 1 236 ? 44.805 -5.448  -19.363 1.00 35.45  ? 236 GLU A CB    1 
ATOM   1827 C CG    . GLU A 1 236 ? 44.646 -4.389  -18.294 1.00 42.78  ? 236 GLU A CG    1 
ATOM   1828 C CD    . GLU A 1 236 ? 45.486 -4.742  -17.083 1.00 45.37  ? 236 GLU A CD    1 
ATOM   1829 O OE1   . GLU A 1 236 ? 46.705 -4.615  -17.184 1.00 46.26  ? 236 GLU A OE1   1 
ATOM   1830 O OE2   . GLU A 1 236 ? 44.922 -5.248  -16.100 1.00 51.45  ? 236 GLU A OE2   1 
ATOM   1831 N N     . PRO A 1 237 ? 42.929 -3.095  -21.224 1.00 27.30  ? 237 PRO A N     1 
ATOM   1832 C CA    . PRO A 1 237 ? 42.997 -1.786  -21.859 1.00 26.88  ? 237 PRO A CA    1 
ATOM   1833 C C     . PRO A 1 237 ? 43.734 -0.775  -20.988 1.00 30.38  ? 237 PRO A C     1 
ATOM   1834 O O     . PRO A 1 237 ? 43.920 -0.967  -19.789 1.00 28.85  ? 237 PRO A O     1 
ATOM   1835 C CB    . PRO A 1 237 ? 41.519 -1.449  -22.048 1.00 28.55  ? 237 PRO A CB    1 
ATOM   1836 C CG    . PRO A 1 237 ? 40.836 -2.098  -20.867 1.00 28.97  ? 237 PRO A CG    1 
ATOM   1837 C CD    . PRO A 1 237 ? 41.617 -3.366  -20.612 1.00 29.18  ? 237 PRO A CD    1 
ATOM   1838 N N     . ALA A 1 238 ? 44.137 0.326   -21.620 1.00 33.90  ? 238 ALA A N     1 
ATOM   1839 C CA    . ALA A 1 238 ? 44.911 1.361   -20.959 1.00 36.17  ? 238 ALA A CA    1 
ATOM   1840 C C     . ALA A 1 238 ? 44.049 2.188   -20.005 1.00 35.48  ? 238 ALA A C     1 
ATOM   1841 O O     . ALA A 1 238 ? 44.579 2.994   -19.263 1.00 39.81  ? 238 ALA A O     1 
ATOM   1842 C CB    . ALA A 1 238 ? 45.536 2.238   -22.014 1.00 36.45  ? 238 ALA A CB    1 
ATOM   1843 N N     . GLY A 1 239 ? 42.725 2.024   -20.066 1.00 36.23  ? 239 GLY A N     1 
ATOM   1844 C CA    . GLY A 1 239 ? 41.794 2.732   -19.200 1.00 33.41  ? 239 GLY A CA    1 
ATOM   1845 C C     . GLY A 1 239 ? 40.401 2.107   -19.257 1.00 33.13  ? 239 GLY A C     1 
ATOM   1846 O O     . GLY A 1 239 ? 40.064 1.408   -20.219 1.00 33.65  ? 239 GLY A O     1 
ATOM   1847 N N     . TYR A 1 240 ? 39.616 2.370   -18.204 1.00 31.82  ? 240 TYR A N     1 
ATOM   1848 C CA    . TYR A 1 240 ? 38.308 1.766   -17.984 1.00 29.90  ? 240 TYR A CA    1 
ATOM   1849 C C     . TYR A 1 240 ? 37.436 2.725   -17.171 1.00 31.52  ? 240 TYR A C     1 
ATOM   1850 O O     . TYR A 1 240 ? 37.835 3.141   -16.085 1.00 31.17  ? 240 TYR A O     1 
ATOM   1851 C CB    . TYR A 1 240 ? 38.445 0.452   -17.221 1.00 26.32  ? 240 TYR A CB    1 
ATOM   1852 C CG    . TYR A 1 240 ? 37.137 -0.201  -16.855 1.00 28.18  ? 240 TYR A CG    1 
ATOM   1853 C CD1   . TYR A 1 240 ? 36.278 -0.682  -17.836 1.00 28.25  ? 240 TYR A CD1   1 
ATOM   1854 C CD2   . TYR A 1 240 ? 36.755 -0.361  -15.530 1.00 27.38  ? 240 TYR A CD2   1 
ATOM   1855 C CE1   . TYR A 1 240 ? 35.053 -1.243  -17.515 1.00 28.23  ? 240 TYR A CE1   1 
ATOM   1856 C CE2   . TYR A 1 240 ? 35.549 -0.957  -15.189 1.00 26.99  ? 240 TYR A CE2   1 
ATOM   1857 C CZ    . TYR A 1 240 ? 34.701 -1.416  -16.184 1.00 27.53  ? 240 TYR A CZ    1 
ATOM   1858 O OH    . TYR A 1 240 ? 33.505 -2.019  -15.870 1.00 27.05  ? 240 TYR A OH    1 
ATOM   1859 N N     . ARG A 1 241 ? 36.271 3.092   -17.717 1.00 29.39  ? 241 ARG A N     1 
ATOM   1860 C CA    . ARG A 1 241 ? 35.383 4.036   -17.066 1.00 30.95  ? 241 ARG A CA    1 
ATOM   1861 C C     . ARG A 1 241 ? 33.936 3.590   -17.261 1.00 27.16  ? 241 ARG A C     1 
ATOM   1862 O O     . ARG A 1 241 ? 33.304 3.944   -18.246 1.00 23.79  ? 241 ARG A O     1 
ATOM   1863 C CB    . ARG A 1 241 ? 35.606 5.443   -17.633 1.00 39.00  ? 241 ARG A CB    1 
ATOM   1864 C CG    . ARG A 1 241 ? 36.903 6.130   -17.205 1.00 44.81  ? 241 ARG A CG    1 
ATOM   1865 C CD    . ARG A 1 241 ? 36.916 6.604   -15.754 1.00 48.27  ? 241 ARG A CD    1 
ATOM   1866 N NE    . ARG A 1 241 ? 36.205 7.871   -15.549 1.00 51.80  ? 241 ARG A NE    1 
ATOM   1867 C CZ    . ARG A 1 241 ? 35.410 8.151   -14.517 1.00 48.66  ? 241 ARG A CZ    1 
ATOM   1868 N NH1   . ARG A 1 241 ? 35.222 7.264   -13.559 1.00 49.34  ? 241 ARG A NH1   1 
ATOM   1869 N NH2   . ARG A 1 241 ? 34.815 9.330   -14.434 1.00 47.31  ? 241 ARG A NH2   1 
ATOM   1870 N N     . PRO A 1 242 ? 33.338 2.845   -16.301 1.00 25.96  ? 242 PRO A N     1 
ATOM   1871 C CA    . PRO A 1 242 ? 31.939 2.431   -16.403 1.00 24.25  ? 242 PRO A CA    1 
ATOM   1872 C C     . PRO A 1 242 ? 30.988 3.543   -15.972 1.00 26.33  ? 242 PRO A C     1 
ATOM   1873 O O     . PRO A 1 242 ? 31.389 4.423   -15.216 1.00 27.94  ? 242 PRO A O     1 
ATOM   1874 C CB    . PRO A 1 242 ? 31.902 1.214   -15.484 1.00 24.22  ? 242 PRO A CB    1 
ATOM   1875 C CG    . PRO A 1 242 ? 32.900 1.541   -14.399 1.00 23.75  ? 242 PRO A CG    1 
ATOM   1876 C CD    . PRO A 1 242 ? 33.985 2.345   -15.083 1.00 24.05  ? 242 PRO A CD    1 
ATOM   1877 N N     . TYR A 1 243 ? 29.743 3.502   -16.480 1.00 24.75  ? 243 TYR A N     1 
ATOM   1878 C CA    . TYR A 1 243 ? 28.819 4.604   -16.327 1.00 25.36  ? 243 TYR A CA    1 
ATOM   1879 C C     . TYR A 1 243 ? 27.395 4.079   -16.201 1.00 25.13  ? 243 TYR A C     1 
ATOM   1880 O O     . TYR A 1 243 ? 27.098 2.969   -16.602 1.00 25.32  ? 243 TYR A O     1 
ATOM   1881 C CB    . TYR A 1 243 ? 29.002 5.609   -17.470 1.00 28.01  ? 243 TYR A CB    1 
ATOM   1882 C CG    . TYR A 1 243 ? 28.672 5.104   -18.850 1.00 29.44  ? 243 TYR A CG    1 
ATOM   1883 C CD1   . TYR A 1 243 ? 27.355 4.963   -19.264 1.00 29.88  ? 243 TYR A CD1   1 
ATOM   1884 C CD2   . TYR A 1 243 ? 29.676 4.754   -19.741 1.00 29.77  ? 243 TYR A CD2   1 
ATOM   1885 C CE1   . TYR A 1 243 ? 27.039 4.483   -20.523 1.00 30.26  ? 243 TYR A CE1   1 
ATOM   1886 C CE2   . TYR A 1 243 ? 29.376 4.258   -21.004 1.00 28.79  ? 243 TYR A CE2   1 
ATOM   1887 C CZ    . TYR A 1 243 ? 28.056 4.121   -21.393 1.00 30.47  ? 243 TYR A CZ    1 
ATOM   1888 O OH    . TYR A 1 243 ? 27.732 3.647   -22.633 1.00 31.02  ? 243 TYR A OH    1 
ATOM   1889 N N     . LEU A 1 244 ? 26.532 4.872   -15.565 1.00 27.52  ? 244 LEU A N     1 
ATOM   1890 C CA    . LEU A 1 244 ? 25.097 4.601   -15.519 1.00 28.32  ? 244 LEU A CA    1 
ATOM   1891 C C     . LEU A 1 244 ? 24.335 5.865   -15.918 1.00 28.17  ? 244 LEU A C     1 
ATOM   1892 O O     . LEU A 1 244 ? 24.619 6.954   -15.429 1.00 31.38  ? 244 LEU A O     1 
ATOM   1893 C CB    . LEU A 1 244 ? 24.719 4.174   -14.103 1.00 29.54  ? 244 LEU A CB    1 
ATOM   1894 C CG    . LEU A 1 244 ? 23.223 4.113   -13.804 1.00 31.99  ? 244 LEU A CG    1 
ATOM   1895 C CD1   . LEU A 1 244 ? 22.557 2.985   -14.582 1.00 33.24  ? 244 LEU A CD1   1 
ATOM   1896 C CD2   . LEU A 1 244 ? 22.985 3.935   -12.311 1.00 31.40  ? 244 LEU A CD2   1 
ATOM   1897 N N     . ILE A 1 245 ? 23.384 5.722   -16.836 1.00 26.29  ? 245 ILE A N     1 
ATOM   1898 C CA    . ILE A 1 245 ? 22.532 6.823   -17.223 1.00 26.09  ? 245 ILE A CA    1 
ATOM   1899 C C     . ILE A 1 245 ? 21.117 6.376   -16.901 1.00 27.09  ? 245 ILE A C     1 
ATOM   1900 O O     . ILE A 1 245 ? 20.679 5.336   -17.388 1.00 28.78  ? 245 ILE A O     1 
ATOM   1901 C CB    . ILE A 1 245 ? 22.730 7.178   -18.711 1.00 28.88  ? 245 ILE A CB    1 
ATOM   1902 C CG1   . ILE A 1 245 ? 24.201 7.427   -19.063 1.00 29.87  ? 245 ILE A CG1   1 
ATOM   1903 C CG2   . ILE A 1 245 ? 21.887 8.370   -19.121 1.00 31.12  ? 245 ILE A CG2   1 
ATOM   1904 C CD1   . ILE A 1 245 ? 24.432 7.667   -20.542 1.00 28.38  ? 245 ILE A CD1   1 
ATOM   1905 N N     . THR A 1 246 ? 20.434 7.130   -16.041 1.00 26.81  ? 246 THR A N     1 
ATOM   1906 C CA    . THR A 1 246 ? 19.062 6.796   -15.691 1.00 29.29  ? 246 THR A CA    1 
ATOM   1907 C C     . THR A 1 246 ? 18.071 7.735   -16.375 1.00 29.09  ? 246 THR A C     1 
ATOM   1908 O O     . THR A 1 246 ? 18.395 8.883   -16.719 1.00 27.48  ? 246 THR A O     1 
ATOM   1909 C CB    . THR A 1 246 ? 18.812 6.817   -14.178 1.00 30.78  ? 246 THR A CB    1 
ATOM   1910 O OG1   . THR A 1 246 ? 18.731 8.189   -13.781 1.00 28.86  ? 246 THR A OG1   1 
ATOM   1911 C CG2   . THR A 1 246 ? 19.870 6.050   -13.409 1.00 30.94  ? 246 THR A CG2   1 
ATOM   1912 N N     . PHE A 1 247 ? 16.853 7.196   -16.516 1.00 28.33  ? 247 PHE A N     1 
ATOM   1913 C CA    . PHE A 1 247 ? 15.717 7.844   -17.157 1.00 30.91  ? 247 PHE A CA    1 
ATOM   1914 C C     . PHE A 1 247 ? 14.491 7.635   -16.275 1.00 31.78  ? 247 PHE A C     1 
ATOM   1915 O O     . PHE A 1 247 ? 14.259 6.513   -15.833 1.00 29.68  ? 247 PHE A O     1 
ATOM   1916 C CB    . PHE A 1 247 ? 15.471 7.208   -18.535 1.00 29.45  ? 247 PHE A CB    1 
ATOM   1917 C CG    . PHE A 1 247 ? 16.671 7.216   -19.443 1.00 29.43  ? 247 PHE A CG    1 
ATOM   1918 C CD1   . PHE A 1 247 ? 17.065 8.375   -20.089 1.00 28.42  ? 247 PHE A CD1   1 
ATOM   1919 C CD2   . PHE A 1 247 ? 17.439 6.073   -19.612 1.00 31.17  ? 247 PHE A CD2   1 
ATOM   1920 C CE1   . PHE A 1 247 ? 18.174 8.375   -20.918 1.00 30.15  ? 247 PHE A CE1   1 
ATOM   1921 C CE2   . PHE A 1 247 ? 18.555 6.077   -20.430 1.00 29.33  ? 247 PHE A CE2   1 
ATOM   1922 C CZ    . PHE A 1 247 ? 18.924 7.228   -21.082 1.00 30.68  ? 247 PHE A CZ    1 
ATOM   1923 N N     . GLU A 1 248 ? 13.680 8.675   -16.054 1.00 35.88  ? 248 GLU A N     1 
ATOM   1924 C CA    . GLU A 1 248 ? 12.670 8.574   -15.005 1.00 37.85  ? 248 GLU A CA    1 
ATOM   1925 C C     . GLU A 1 248 ? 11.306 8.117   -15.530 1.00 35.72  ? 248 GLU A C     1 
ATOM   1926 O O     . GLU A 1 248 ? 10.500 7.649   -14.737 1.00 34.04  ? 248 GLU A O     1 
ATOM   1927 C CB    . GLU A 1 248 ? 12.616 9.847   -14.158 1.00 44.58  ? 248 GLU A CB    1 
ATOM   1928 C CG    . GLU A 1 248 ? 12.078 11.080  -14.839 1.00 54.55  ? 248 GLU A CG    1 
ATOM   1929 C CD    . GLU A 1 248 ? 11.980 12.281  -13.904 1.00 65.42  ? 248 GLU A CD    1 
ATOM   1930 O OE1   . GLU A 1 248 ? 12.519 12.204  -12.772 1.00 69.01  ? 248 GLU A OE1   1 
ATOM   1931 O OE2   . GLU A 1 248 ? 11.372 13.299  -14.309 1.00 73.24  ? 248 GLU A OE2   1 
ATOM   1932 N N     . ASN A 1 249 ? 11.057 8.169   -16.843 1.00 36.34  ? 249 ASN A N     1 
ATOM   1933 C CA    . ASN A 1 249 ? 9.757  7.793   -17.391 1.00 36.29  ? 249 ASN A CA    1 
ATOM   1934 C C     . ASN A 1 249 ? 9.842  6.501   -18.193 1.00 33.95  ? 249 ASN A C     1 
ATOM   1935 O O     . ASN A 1 249 ? 10.715 6.346   -19.037 1.00 38.43  ? 249 ASN A O     1 
ATOM   1936 C CB    . ASN A 1 249 ? 9.203  8.865   -18.329 1.00 37.62  ? 249 ASN A CB    1 
ATOM   1937 C CG    . ASN A 1 249 ? 9.050  10.191  -17.629 1.00 38.83  ? 249 ASN A CG    1 
ATOM   1938 O OD1   . ASN A 1 249 ? 8.250  10.313  -16.712 1.00 45.48  ? 249 ASN A OD1   1 
ATOM   1939 N ND2   . ASN A 1 249 ? 9.839  11.171  -18.017 1.00 43.54  ? 249 ASN A ND2   1 
ATOM   1940 N N     . GLU A 1 250 ? 8.873  5.613   -17.987 1.00 36.06  ? 250 GLU A N     1 
ATOM   1941 C CA    . GLU A 1 250 ? 8.810  4.356   -18.714 1.00 39.20  ? 250 GLU A CA    1 
ATOM   1942 C C     . GLU A 1 250 ? 8.714  4.578   -20.228 1.00 38.58  ? 250 GLU A C     1 
ATOM   1943 O O     . GLU A 1 250 ? 9.180  3.739   -20.987 1.00 37.24  ? 250 GLU A O     1 
ATOM   1944 C CB    . GLU A 1 250 ? 7.659  3.485   -18.195 1.00 47.33  ? 250 GLU A CB    1 
ATOM   1945 C CG    . GLU A 1 250 ? 6.282  4.152   -18.203 1.00 55.95  ? 250 GLU A CG    1 
ATOM   1946 C CD    . GLU A 1 250 ? 5.124  3.236   -17.820 1.00 61.38  ? 250 GLU A CD    1 
ATOM   1947 O OE1   . GLU A 1 250 ? 5.387  2.093   -17.352 1.00 60.77  ? 250 GLU A OE1   1 
ATOM   1948 O OE2   . GLU A 1 250 ? 3.957  3.652   -18.025 1.00 58.51  ? 250 GLU A OE2   1 
ATOM   1949 N N     . ASP A 1 251 ? 8.101  5.684   -20.674 1.00 39.36  ? 251 ASP A N     1 
ATOM   1950 C CA    . ASP A 1 251 ? 7.976  5.957   -22.098 1.00 41.05  ? 251 ASP A CA    1 
ATOM   1951 C C     . ASP A 1 251 ? 9.294  6.450   -22.705 1.00 37.41  ? 251 ASP A C     1 
ATOM   1952 O O     . ASP A 1 251 ? 9.395  6.504   -23.930 1.00 35.78  ? 251 ASP A O     1 
ATOM   1953 C CB    . ASP A 1 251 ? 6.858  6.960   -22.393 1.00 43.68  ? 251 ASP A CB    1 
ATOM   1954 C CG    . ASP A 1 251 ? 5.461  6.364   -22.388 1.00 49.45  ? 251 ASP A CG    1 
ATOM   1955 O OD1   . ASP A 1 251 ? 5.338  5.114   -22.391 1.00 42.95  ? 251 ASP A OD1   1 
ATOM   1956 O OD2   . ASP A 1 251 ? 4.493  7.169   -22.371 1.00 58.99  ? 251 ASP A OD2   1 
ATOM   1957 N N     . ASP A 1 252 ? 10.271 6.827   -21.869 1.00 31.42  ? 252 ASP A N     1 
ATOM   1958 C CA    . ASP A 1 252 ? 11.576 7.264   -22.338 1.00 33.63  ? 252 ASP A CA    1 
ATOM   1959 C C     . ASP A 1 252 ? 12.287 6.178   -23.153 1.00 32.96  ? 252 ASP A C     1 
ATOM   1960 O O     . ASP A 1 252 ? 13.170 6.479   -23.943 1.00 32.29  ? 252 ASP A O     1 
ATOM   1961 C CB    . ASP A 1 252 ? 12.498 7.652   -21.176 1.00 36.18  ? 252 ASP A CB    1 
ATOM   1962 C CG    . ASP A 1 252 ? 12.148 8.953   -20.479 1.00 38.55  ? 252 ASP A CG    1 
ATOM   1963 O OD1   . ASP A 1 252 ? 11.410 9.751   -21.084 1.00 46.79  ? 252 ASP A OD1   1 
ATOM   1964 O OD2   . ASP A 1 252 ? 12.637 9.171   -19.344 1.00 34.44  ? 252 ASP A OD2   1 
ATOM   1965 N N     . ILE A 1 253 ? 11.941 4.905   -22.970 1.00 32.33  ? 253 ILE A N     1 
ATOM   1966 C CA    . ILE A 1 253 ? 12.682 3.843   -23.631 1.00 30.37  ? 253 ILE A CA    1 
ATOM   1967 C C     . ILE A 1 253 ? 12.622 3.934   -25.158 1.00 32.36  ? 253 ILE A C     1 
ATOM   1968 O O     . ILE A 1 253 ? 13.530 3.433   -25.829 1.00 33.11  ? 253 ILE A O     1 
ATOM   1969 C CB    . ILE A 1 253 ? 12.207 2.469   -23.148 1.00 28.33  ? 253 ILE A CB    1 
ATOM   1970 C CG1   . ILE A 1 253 ? 13.188 1.376   -23.584 1.00 30.35  ? 253 ILE A CG1   1 
ATOM   1971 C CG2   . ILE A 1 253 ? 10.799 2.201   -23.620 1.00 28.28  ? 253 ILE A CG2   1 
ATOM   1972 C CD1   . ILE A 1 253 ? 14.640 1.663   -23.208 1.00 30.99  ? 253 ILE A CD1   1 
ATOM   1973 N N     . GLU A 1 254 ? 11.559 4.547   -25.697 1.00 30.72  ? 254 GLU A N     1 
ATOM   1974 C CA    . GLU A 1 254 ? 11.424 4.785   -27.128 1.00 32.44  ? 254 GLU A CA    1 
ATOM   1975 C C     . GLU A 1 254 ? 12.586 5.642   -27.635 1.00 31.10  ? 254 GLU A C     1 
ATOM   1976 O O     . GLU A 1 254 ? 13.378 5.192   -28.460 1.00 32.10  ? 254 GLU A O     1 
ATOM   1977 C CB    . GLU A 1 254 ? 10.056 5.404   -27.435 1.00 34.33  ? 254 GLU A CB    1 
ATOM   1978 C CG    . GLU A 1 254 ? 9.924  5.918   -28.864 1.00 39.53  ? 254 GLU A CG    1 
ATOM   1979 C CD    . GLU A 1 254 ? 8.538  5.905   -29.503 1.00 41.36  ? 254 GLU A CD    1 
ATOM   1980 O OE1   . GLU A 1 254 ? 7.491  5.851   -28.785 1.00 34.38  ? 254 GLU A OE1   1 
ATOM   1981 O OE2   . GLU A 1 254 ? 8.512  5.904   -30.742 1.00 43.97  ? 254 GLU A OE2   1 
ATOM   1982 N N     . THR A 1 255 ? 12.719 6.862   -27.104 1.00 30.57  ? 255 THR A N     1 
ATOM   1983 C CA    . THR A 1 255 ? 13.704 7.793   -27.623 1.00 28.21  ? 255 THR A CA    1 
ATOM   1984 C C     . THR A 1 255 ? 15.099 7.267   -27.290 1.00 27.52  ? 255 THR A C     1 
ATOM   1985 O O     . THR A 1 255 ? 16.047 7.500   -28.046 1.00 23.88  ? 255 THR A O     1 
ATOM   1986 C CB    . THR A 1 255 ? 13.421 9.249   -27.200 1.00 27.54  ? 255 THR A CB    1 
ATOM   1987 O OG1   . THR A 1 255 ? 14.411 10.091  -27.812 1.00 28.07  ? 255 THR A OG1   1 
ATOM   1988 C CG2   . THR A 1 255 ? 13.470 9.495   -25.709 1.00 29.64  ? 255 THR A CG2   1 
ATOM   1989 N N     . VAL A 1 256 ? 15.206 6.541   -26.173 1.00 28.91  ? 256 VAL A N     1 
ATOM   1990 C CA    . VAL A 1 256 ? 16.491 6.072   -25.677 1.00 31.03  ? 256 VAL A CA    1 
ATOM   1991 C C     . VAL A 1 256 ? 17.063 5.094   -26.700 1.00 29.59  ? 256 VAL A C     1 
ATOM   1992 O O     . VAL A 1 256 ? 18.253 5.164   -27.035 1.00 27.33  ? 256 VAL A O     1 
ATOM   1993 C CB    . VAL A 1 256 ? 16.378 5.427   -24.274 1.00 35.45  ? 256 VAL A CB    1 
ATOM   1994 C CG1   . VAL A 1 256 ? 17.532 4.468   -23.970 1.00 34.63  ? 256 VAL A CG1   1 
ATOM   1995 C CG2   . VAL A 1 256 ? 16.272 6.477   -23.167 1.00 34.53  ? 256 VAL A CG2   1 
ATOM   1996 N N     . THR A 1 257 ? 16.191 4.203   -27.184 1.00 26.39  ? 257 THR A N     1 
ATOM   1997 C CA    . THR A 1 257 ? 16.587 3.173   -28.123 1.00 28.23  ? 257 THR A CA    1 
ATOM   1998 C C     . THR A 1 257 ? 16.995 3.817   -29.451 1.00 30.86  ? 257 THR A C     1 
ATOM   1999 O O     . THR A 1 257 ? 18.038 3.457   -30.004 1.00 31.27  ? 257 THR A O     1 
ATOM   2000 C CB    . THR A 1 257 ? 15.488 2.107   -28.276 1.00 28.96  ? 257 THR A CB    1 
ATOM   2001 O OG1   . THR A 1 257 ? 15.158 1.568   -26.994 1.00 29.32  ? 257 THR A OG1   1 
ATOM   2002 C CG2   . THR A 1 257 ? 15.890 0.959   -29.172 1.00 27.90  ? 257 THR A CG2   1 
ATOM   2003 N N     . GLU A 1 258 ? 16.188 4.766   -29.956 1.00 29.98  ? 258 GLU A N     1 
ATOM   2004 C CA    . GLU A 1 258 ? 16.535 5.505   -31.171 1.00 31.97  ? 258 GLU A CA    1 
ATOM   2005 C C     . GLU A 1 258 ? 17.943 6.106   -31.082 1.00 30.94  ? 258 GLU A C     1 
ATOM   2006 O O     . GLU A 1 258 ? 18.632 6.245   -32.088 1.00 36.06  ? 258 GLU A O     1 
ATOM   2007 C CB    . GLU A 1 258 ? 15.571 6.670   -31.447 1.00 31.09  ? 258 GLU A CB    1 
ATOM   2008 C CG    . GLU A 1 258 ? 14.206 6.240   -31.963 1.00 32.37  ? 258 GLU A CG    1 
ATOM   2009 C CD    . GLU A 1 258 ? 14.280 5.483   -33.277 1.00 35.62  ? 258 GLU A CD    1 
ATOM   2010 O OE1   . GLU A 1 258 ? 14.576 6.125   -34.309 1.00 36.97  ? 258 GLU A OE1   1 
ATOM   2011 O OE2   . GLU A 1 258 ? 14.066 4.256   -33.259 1.00 34.63  ? 258 GLU A OE2   1 
ATOM   2012 N N     . ARG A 1 259 ? 18.352 6.543   -29.895 1.00 30.76  ? 259 ARG A N     1 
ATOM   2013 C CA    . ARG A 1 259 ? 19.621 7.239   -29.759 1.00 31.41  ? 259 ARG A CA    1 
ATOM   2014 C C     . ARG A 1 259 ? 20.740 6.215   -29.628 1.00 27.95  ? 259 ARG A C     1 
ATOM   2015 O O     . ARG A 1 259 ? 21.847 6.483   -30.063 1.00 27.75  ? 259 ARG A O     1 
ATOM   2016 C CB    . ARG A 1 259 ? 19.572 8.212   -28.575 1.00 33.14  ? 259 ARG A CB    1 
ATOM   2017 C CG    . ARG A 1 259 ? 18.594 9.363   -28.776 1.00 34.65  ? 259 ARG A CG    1 
ATOM   2018 C CD    . ARG A 1 259 ? 18.004 9.806   -27.456 1.00 39.35  ? 259 ARG A CD    1 
ATOM   2019 N NE    . ARG A 1 259 ? 16.934 10.788  -27.592 1.00 39.67  ? 259 ARG A NE    1 
ATOM   2020 C CZ    . ARG A 1 259 ? 17.069 12.069  -27.273 1.00 36.24  ? 259 ARG A CZ    1 
ATOM   2021 N NH1   . ARG A 1 259 ? 18.249 12.550  -26.938 1.00 33.39  ? 259 ARG A NH1   1 
ATOM   2022 N NH2   . ARG A 1 259 ? 16.025 12.870  -27.302 1.00 37.71  ? 259 ARG A NH2   1 
ATOM   2023 N N     . LEU A 1 260 ? 20.422 5.039   -29.077 1.00 26.72  ? 260 LEU A N     1 
ATOM   2024 C CA    . LEU A 1 260 ? 21.403 3.975   -28.917 1.00 28.09  ? 260 LEU A CA    1 
ATOM   2025 C C     . LEU A 1 260 ? 21.821 3.420   -30.279 1.00 25.63  ? 260 LEU A C     1 
ATOM   2026 O O     . LEU A 1 260 ? 22.975 3.053   -30.423 1.00 24.72  ? 260 LEU A O     1 
ATOM   2027 C CB    . LEU A 1 260 ? 20.857 2.857   -28.010 1.00 26.67  ? 260 LEU A CB    1 
ATOM   2028 C CG    . LEU A 1 260 ? 20.778 3.164   -26.512 1.00 27.42  ? 260 LEU A CG    1 
ATOM   2029 C CD1   . LEU A 1 260 ? 20.041 2.064   -25.772 1.00 30.24  ? 260 LEU A CD1   1 
ATOM   2030 C CD2   . LEU A 1 260 ? 22.152 3.355   -25.901 1.00 26.63  ? 260 LEU A CD2   1 
ATOM   2031 N N     . ARG A 1 261 ? 20.906 3.375   -31.262 1.00 26.05  ? 261 ARG A N     1 
ATOM   2032 C CA    . ARG A 1 261 ? 21.142 2.659   -32.513 1.00 27.12  ? 261 ARG A CA    1 
ATOM   2033 C C     . ARG A 1 261 ? 22.407 3.169   -33.204 1.00 26.98  ? 261 ARG A C     1 
ATOM   2034 O O     . ARG A 1 261 ? 23.366 2.429   -33.392 1.00 28.25  ? 261 ARG A O     1 
ATOM   2035 C CB    . ARG A 1 261 ? 19.935 2.756   -33.453 1.00 28.10  ? 261 ARG A CB    1 
ATOM   2036 C CG    . ARG A 1 261 ? 20.193 2.196   -34.852 1.00 28.10  ? 261 ARG A CG    1 
ATOM   2037 C CD    . ARG A 1 261 ? 18.969 2.258   -35.743 1.00 26.09  ? 261 ARG A CD    1 
ATOM   2038 N NE    . ARG A 1 261 ? 18.497 3.635   -35.869 1.00 29.03  ? 261 ARG A NE    1 
ATOM   2039 C CZ    . ARG A 1 261 ? 17.353 4.101   -35.378 1.00 28.68  ? 261 ARG A CZ    1 
ATOM   2040 N NH1   . ARG A 1 261 ? 16.522 3.314   -34.724 1.00 28.90  ? 261 ARG A NH1   1 
ATOM   2041 N NH2   . ARG A 1 261 ? 17.061 5.376   -35.505 1.00 29.69  ? 261 ARG A NH2   1 
ATOM   2042 N N     . PRO A 1 262 ? 22.505 4.463   -33.558 1.00 28.51  ? 262 PRO A N     1 
ATOM   2043 C CA    . PRO A 1 262 ? 23.694 4.946   -34.250 1.00 27.83  ? 262 PRO A CA    1 
ATOM   2044 C C     . PRO A 1 262 ? 24.953 4.722   -33.429 1.00 28.19  ? 262 PRO A C     1 
ATOM   2045 O O     . PRO A 1 262 ? 26.013 4.436   -33.983 1.00 28.50  ? 262 PRO A O     1 
ATOM   2046 C CB    . PRO A 1 262 ? 23.420 6.446   -34.489 1.00 27.42  ? 262 PRO A CB    1 
ATOM   2047 C CG    . PRO A 1 262 ? 22.298 6.800   -33.519 1.00 29.46  ? 262 PRO A CG    1 
ATOM   2048 C CD    . PRO A 1 262 ? 21.504 5.523   -33.333 1.00 29.30  ? 262 PRO A CD    1 
ATOM   2049 N N     . LEU A 1 263 ? 24.850 4.914   -32.109 1.00 29.07  ? 263 LEU A N     1 
ATOM   2050 C CA    . LEU A 1 263 ? 26.021 4.796   -31.246 1.00 28.01  ? 263 LEU A CA    1 
ATOM   2051 C C     . LEU A 1 263 ? 26.550 3.359   -31.282 1.00 26.52  ? 263 LEU A C     1 
ATOM   2052 O O     . LEU A 1 263 ? 27.756 3.132   -31.210 1.00 24.92  ? 263 LEU A O     1 
ATOM   2053 C CB    . LEU A 1 263 ? 25.643 5.193   -29.814 1.00 30.06  ? 263 LEU A CB    1 
ATOM   2054 C CG    . LEU A 1 263 ? 25.282 6.661   -29.579 1.00 29.07  ? 263 LEU A CG    1 
ATOM   2055 C CD1   . LEU A 1 263 ? 24.694 6.850   -28.197 1.00 26.89  ? 263 LEU A CD1   1 
ATOM   2056 C CD2   . LEU A 1 263 ? 26.500 7.561   -29.741 1.00 30.45  ? 263 LEU A CD2   1 
ATOM   2057 N N     . LYS A 1 264 ? 25.643 2.386   -31.390 1.00 26.27  ? 264 LYS A N     1 
ATOM   2058 C CA    . LYS A 1 264 ? 26.042 1.001   -31.288 1.00 30.55  ? 264 LYS A CA    1 
ATOM   2059 C C     . LYS A 1 264 ? 26.482 0.513   -32.664 1.00 28.05  ? 264 LYS A C     1 
ATOM   2060 O O     . LYS A 1 264 ? 27.543 -0.068  -32.795 1.00 29.22  ? 264 LYS A O     1 
ATOM   2061 C CB    . LYS A 1 264 ? 24.936 0.175   -30.622 1.00 37.12  ? 264 LYS A CB    1 
ATOM   2062 C CG    . LYS A 1 264 ? 25.374 -1.215  -30.156 1.00 51.06  ? 264 LYS A CG    1 
ATOM   2063 C CD    . LYS A 1 264 ? 26.509 -1.248  -29.130 1.00 52.51  ? 264 LYS A CD    1 
ATOM   2064 C CE    . LYS A 1 264 ? 27.698 -2.085  -29.566 1.00 55.33  ? 264 LYS A CE    1 
ATOM   2065 N NZ    . LYS A 1 264 ? 27.819 -3.330  -28.774 1.00 61.39  ? 264 LYS A NZ    1 
ATOM   2066 N N     . VAL A 1 265 ? 25.702 0.803   -33.702 1.00 29.81  ? 265 VAL A N     1 
ATOM   2067 C CA    . VAL A 1 265 ? 26.043 0.377   -35.050 1.00 28.70  ? 265 VAL A CA    1 
ATOM   2068 C C     . VAL A 1 265 ? 27.433 0.884   -35.414 1.00 28.76  ? 265 VAL A C     1 
ATOM   2069 O O     . VAL A 1 265 ? 28.202 0.185   -36.082 1.00 27.34  ? 265 VAL A O     1 
ATOM   2070 C CB    . VAL A 1 265 ? 24.992 0.866   -36.054 1.00 30.22  ? 265 VAL A CB    1 
ATOM   2071 C CG1   . VAL A 1 265 ? 25.412 0.616   -37.492 1.00 31.00  ? 265 VAL A CG1   1 
ATOM   2072 C CG2   . VAL A 1 265 ? 23.654 0.212   -35.769 1.00 30.41  ? 265 VAL A CG2   1 
ATOM   2073 N N     . ALA A 1 266 ? 27.766 2.084   -34.928 1.00 25.93  ? 266 ALA A N     1 
ATOM   2074 C CA    . ALA A 1 266 ? 29.059 2.660   -35.241 1.00 26.30  ? 266 ALA A CA    1 
ATOM   2075 C C     . ALA A 1 266 ? 30.120 2.197   -34.246 1.00 26.68  ? 266 ALA A C     1 
ATOM   2076 O O     . ALA A 1 266 ? 31.287 2.481   -34.435 1.00 27.04  ? 266 ALA A O     1 
ATOM   2077 C CB    . ALA A 1 266 ? 28.951 4.163   -35.288 1.00 25.28  ? 266 ALA A CB    1 
ATOM   2078 N N     . GLY A 1 267 ? 29.736 1.538   -33.156 1.00 28.63  ? 267 GLY A N     1 
ATOM   2079 C CA    . GLY A 1 267 ? 30.716 1.068   -32.174 1.00 31.82  ? 267 GLY A CA    1 
ATOM   2080 C C     . GLY A 1 267 ? 31.265 2.152   -31.235 1.00 32.18  ? 267 GLY A C     1 
ATOM   2081 O O     . GLY A 1 267 ? 32.334 1.984   -30.649 1.00 33.01  ? 267 GLY A O     1 
ATOM   2082 N N     . VAL A 1 268 ? 30.520 3.255   -31.076 1.00 33.29  ? 268 VAL A N     1 
ATOM   2083 C CA    . VAL A 1 268 ? 30.858 4.299   -30.114 1.00 32.59  ? 268 VAL A CA    1 
ATOM   2084 C C     . VAL A 1 268 ? 30.672 3.753   -28.690 1.00 29.23  ? 268 VAL A C     1 
ATOM   2085 O O     . VAL A 1 268 ? 31.491 4.008   -27.810 1.00 29.42  ? 268 VAL A O     1 
ATOM   2086 C CB    . VAL A 1 268 ? 30.012 5.566   -30.369 1.00 30.13  ? 268 VAL A CB    1 
ATOM   2087 C CG1   . VAL A 1 268 ? 30.243 6.638   -29.313 1.00 29.15  ? 268 VAL A CG1   1 
ATOM   2088 C CG2   . VAL A 1 268 ? 30.260 6.120   -31.756 1.00 29.45  ? 268 VAL A CG2   1 
ATOM   2089 N N     . ILE A 1 269 ? 29.570 3.023   -28.482 1.00 26.10  ? 269 ILE A N     1 
ATOM   2090 C CA    . ILE A 1 269 ? 29.404 2.149   -27.335 1.00 25.40  ? 269 ILE A CA    1 
ATOM   2091 C C     . ILE A 1 269 ? 30.127 0.834   -27.600 1.00 27.07  ? 269 ILE A C     1 
ATOM   2092 O O     . ILE A 1 269 ? 29.747 0.092   -28.493 1.00 29.78  ? 269 ILE A O     1 
ATOM   2093 C CB    . ILE A 1 269 ? 27.916 1.920   -27.048 1.00 26.11  ? 269 ILE A CB    1 
ATOM   2094 C CG1   . ILE A 1 269 ? 27.225 3.219   -26.630 1.00 26.33  ? 269 ILE A CG1   1 
ATOM   2095 C CG2   . ILE A 1 269 ? 27.725 0.823   -25.999 1.00 26.78  ? 269 ILE A CG2   1 
ATOM   2096 C CD1   . ILE A 1 269 ? 25.728 3.160   -26.803 1.00 28.03  ? 269 ILE A CD1   1 
ATOM   2097 N N     . GLN A 1 270 ? 31.179 0.561   -26.820 1.00 27.61  ? 270 GLN A N     1 
ATOM   2098 C CA    . GLN A 1 270 ? 32.143 -0.472  -27.140 1.00 26.52  ? 270 GLN A CA    1 
ATOM   2099 C C     . GLN A 1 270 ? 31.730 -1.852  -26.632 1.00 26.80  ? 270 GLN A C     1 
ATOM   2100 O O     . GLN A 1 270 ? 32.313 -2.829  -27.092 1.00 30.18  ? 270 GLN A O     1 
ATOM   2101 C CB    . GLN A 1 270 ? 33.494 -0.108  -26.524 1.00 26.35  ? 270 GLN A CB    1 
ATOM   2102 C CG    . GLN A 1 270 ? 34.153 1.080   -27.193 1.00 25.88  ? 270 GLN A CG    1 
ATOM   2103 C CD    . GLN A 1 270 ? 35.145 1.765   -26.283 1.00 25.99  ? 270 GLN A CD    1 
ATOM   2104 O OE1   . GLN A 1 270 ? 34.782 2.371   -25.275 1.00 26.11  ? 270 GLN A OE1   1 
ATOM   2105 N NE2   . GLN A 1 270 ? 36.410 1.686   -26.648 1.00 25.33  ? 270 GLN A NE2   1 
ATOM   2106 N N     . ASN A 1 271 ? 30.806 -1.932  -25.658 1.00 26.41  ? 271 ASN A N     1 
ATOM   2107 C CA    . ASN A 1 271 ? 30.425 -3.194  -25.014 1.00 27.20  ? 271 ASN A CA    1 
ATOM   2108 C C     . ASN A 1 271 ? 28.934 -3.422  -25.193 1.00 27.39  ? 271 ASN A C     1 
ATOM   2109 O O     . ASN A 1 271 ? 28.272 -2.618  -25.814 1.00 25.93  ? 271 ASN A O     1 
ATOM   2110 C CB    . ASN A 1 271 ? 30.777 -3.269  -23.521 1.00 25.59  ? 271 ASN A CB    1 
ATOM   2111 C CG    . ASN A 1 271 ? 30.120 -2.202  -22.664 1.00 27.77  ? 271 ASN A CG    1 
ATOM   2112 O OD1   . ASN A 1 271 ? 29.906 -1.076  -23.118 1.00 27.84  ? 271 ASN A OD1   1 
ATOM   2113 N ND2   . ASN A 1 271 ? 29.806 -2.534  -21.416 1.00 27.07  ? 271 ASN A ND2   1 
ATOM   2114 N N     . GLY A 1 272 ? 28.420 -4.529  -24.665 1.00 38.49  ? 272 GLY A N     1 
ATOM   2115 C CA    . GLY A 1 272 ? 26.983 -4.688  -24.507 1.00 45.30  ? 272 GLY A CA    1 
ATOM   2116 C C     . GLY A 1 272 ? 26.343 -3.507  -23.772 1.00 48.94  ? 272 GLY A C     1 
ATOM   2117 O O     . GLY A 1 272 ? 26.685 -3.214  -22.631 1.00 60.63  ? 272 GLY A O     1 
ATOM   2118 N N     . ALA A 1 273 ? 25.430 -2.821  -24.466 1.00 51.09  ? 273 ALA A N     1 
ATOM   2119 C CA    . ALA A 1 273 ? 24.535 -1.847  -23.868 1.00 58.61  ? 273 ALA A CA    1 
ATOM   2120 C C     . ALA A 1 273 ? 23.375 -2.589  -23.212 1.00 55.99  ? 273 ALA A C     1 
ATOM   2121 O O     . ALA A 1 273 ? 22.541 -3.140  -23.928 1.00 57.82  ? 273 ALA A O     1 
ATOM   2122 C CB    . ALA A 1 273 ? 24.002 -0.887  -24.923 1.00 55.94  ? 273 ALA A CB    1 
ATOM   2123 N N     . THR A 1 274 ? 23.322 -2.582  -21.871 1.00 50.14  ? 274 THR A N     1 
ATOM   2124 C CA    . THR A 1 274 ? 22.133 -3.035  -21.159 1.00 49.52  ? 274 THR A CA    1 
ATOM   2125 C C     . THR A 1 274 ? 21.356 -1.814  -20.680 1.00 39.94  ? 274 THR A C     1 
ATOM   2126 O O     . THR A 1 274 ? 21.958 -0.885  -20.158 1.00 44.52  ? 274 THR A O     1 
ATOM   2127 C CB    . THR A 1 274 ? 22.485 -4.005  -20.021 1.00 47.96  ? 274 THR A CB    1 
ATOM   2128 O OG1   . THR A 1 274 ? 23.252 -3.369  -18.997 1.00 61.95  ? 274 THR A OG1   1 
ATOM   2129 C CG2   . THR A 1 274 ? 23.283 -5.185  -20.518 1.00 49.31  ? 274 THR A CG2   1 
ATOM   2130 N N     . VAL A 1 275 ? 20.040 -1.815  -20.912 1.00 34.99  ? 275 VAL A N     1 
ATOM   2131 C CA    . VAL A 1 275 ? 19.120 -0.859  -20.311 1.00 36.20  ? 275 VAL A CA    1 
ATOM   2132 C C     . VAL A 1 275 ? 18.143 -1.659  -19.451 1.00 37.01  ? 275 VAL A C     1 
ATOM   2133 O O     . VAL A 1 275 ? 17.353 -2.446  -19.980 1.00 40.48  ? 275 VAL A O     1 
ATOM   2134 C CB    . VAL A 1 275 ? 18.378 0.003   -21.362 1.00 34.52  ? 275 VAL A CB    1 
ATOM   2135 C CG1   . VAL A 1 275 ? 17.770 1.247   -20.743 1.00 34.95  ? 275 VAL A CG1   1 
ATOM   2136 C CG2   . VAL A 1 275 ? 19.285 0.430   -22.497 1.00 34.71  ? 275 VAL A CG2   1 
ATOM   2137 N N     . ARG A 1 276 ? 18.239 -1.498  -18.125 1.00 32.60  ? 276 ARG A N     1 
ATOM   2138 C CA    . ARG A 1 276 ? 17.523 -2.366  -17.202 1.00 32.02  ? 276 ARG A CA    1 
ATOM   2139 C C     . ARG A 1 276 ? 16.326 -1.628  -16.599 1.00 29.15  ? 276 ARG A C     1 
ATOM   2140 O O     . ARG A 1 276 ? 16.420 -0.448  -16.291 1.00 28.85  ? 276 ARG A O     1 
ATOM   2141 C CB    . ARG A 1 276 ? 18.500 -2.895  -16.152 1.00 34.00  ? 276 ARG A CB    1 
ATOM   2142 C CG    . ARG A 1 276 ? 19.312 -4.093  -16.629 1.00 38.52  ? 276 ARG A CG    1 
ATOM   2143 C CD    . ARG A 1 276 ? 20.671 -4.209  -15.968 1.00 46.61  ? 276 ARG A CD    1 
ATOM   2144 N NE    . ARG A 1 276 ? 21.193 -5.557  -16.056 1.00 54.00  ? 276 ARG A NE    1 
ATOM   2145 C CZ    . ARG A 1 276 ? 21.057 -6.471  -15.095 1.00 72.90  ? 276 ARG A CZ    1 
ATOM   2146 N NH1   . ARG A 1 276 ? 20.678 -6.104  -13.881 1.00 76.50  ? 276 ARG A NH1   1 
ATOM   2147 N NH2   . ARG A 1 276 ? 21.318 -7.747  -15.344 1.00 74.65  ? 276 ARG A NH2   1 
ATOM   2148 N N     . SER A 1 277 ? 15.199 -2.338  -16.436 1.00 28.82  ? 277 SER A N     1 
ATOM   2149 C CA    . SER A 1 277 ? 14.034 -1.800  -15.742 1.00 28.90  ? 277 SER A CA    1 
ATOM   2150 C C     . SER A 1 277 ? 14.304 -1.639  -14.240 1.00 29.63  ? 277 SER A C     1 
ATOM   2151 O O     . SER A 1 277 ? 15.181 -2.289  -13.671 1.00 28.04  ? 277 SER A O     1 
ATOM   2152 C CB    . SER A 1 277 ? 12.834 -2.656  -15.995 1.00 29.02  ? 277 SER A CB    1 
ATOM   2153 O OG    . SER A 1 277 ? 12.918 -3.865  -15.250 1.00 30.54  ? 277 SER A OG    1 
ATOM   2154 N N     . LEU A 1 278 ? 13.525 -0.757  -13.597 1.00 30.34  ? 278 LEU A N     1 
ATOM   2155 C CA    . LEU A 1 278 ? 13.700 -0.402  -12.196 1.00 27.72  ? 278 LEU A CA    1 
ATOM   2156 C C     . LEU A 1 278 ? 13.723 -1.629  -11.300 1.00 25.94  ? 278 LEU A C     1 
ATOM   2157 O O     . LEU A 1 278 ? 14.570 -1.727  -10.424 1.00 28.64  ? 278 LEU A O     1 
ATOM   2158 C CB    . LEU A 1 278 ? 12.556 0.511   -11.754 1.00 28.35  ? 278 LEU A CB    1 
ATOM   2159 C CG    . LEU A 1 278 ? 12.444 0.748   -10.247 1.00 28.55  ? 278 LEU A CG    1 
ATOM   2160 C CD1   . LEU A 1 278 ? 13.618 1.568   -9.713  1.00 27.98  ? 278 LEU A CD1   1 
ATOM   2161 C CD2   . LEU A 1 278 ? 11.136 1.445   -9.917  1.00 30.47  ? 278 LEU A CD2   1 
ATOM   2162 N N     . VAL A 1 279 ? 12.746 -2.516  -11.446 1.00 26.47  ? 279 VAL A N     1 
ATOM   2163 C CA    . VAL A 1 279 ? 12.606 -3.587  -10.478 1.00 28.43  ? 279 VAL A CA    1 
ATOM   2164 C C     . VAL A 1 279 ? 13.797 -4.534  -10.606 1.00 31.92  ? 279 VAL A C     1 
ATOM   2165 O O     . VAL A 1 279 ? 14.302 -5.009  -9.589  1.00 34.79  ? 279 VAL A O     1 
ATOM   2166 C CB    . VAL A 1 279 ? 11.257 -4.324  -10.586 1.00 28.17  ? 279 VAL A CB    1 
ATOM   2167 C CG1   . VAL A 1 279 ? 11.190 -5.494  -9.627  1.00 28.62  ? 279 VAL A CG1   1 
ATOM   2168 C CG2   . VAL A 1 279 ? 10.088 -3.396  -10.318 1.00 28.42  ? 279 VAL A CG2   1 
ATOM   2169 N N     . LEU A 1 280 ? 14.273 -4.775  -11.839 1.00 30.80  ? 280 LEU A N     1 
ATOM   2170 C CA    . LEU A 1 280 ? 15.380 -5.694  -12.028 1.00 30.18  ? 280 LEU A CA    1 
ATOM   2171 C C     . LEU A 1 280 ? 16.620 -5.195  -11.293 1.00 31.52  ? 280 LEU A C     1 
ATOM   2172 O O     . LEU A 1 280 ? 17.324 -5.995  -10.680 1.00 30.93  ? 280 LEU A O     1 
ATOM   2173 C CB    . LEU A 1 280 ? 15.650 -5.893  -13.518 1.00 29.87  ? 280 LEU A CB    1 
ATOM   2174 C CG    . LEU A 1 280 ? 16.818 -6.821  -13.831 1.00 30.72  ? 280 LEU A CG    1 
ATOM   2175 C CD1   . LEU A 1 280 ? 16.635 -8.178  -13.176 1.00 31.94  ? 280 LEU A CD1   1 
ATOM   2176 C CD2   . LEU A 1 280 ? 16.980 -6.977  -15.328 1.00 33.62  ? 280 LEU A CD2   1 
ATOM   2177 N N     . ASP A 1 281 ? 16.879 -3.883  -11.364 1.00 32.86  ? 281 ASP A N     1 
ATOM   2178 C CA    . ASP A 1 281 ? 18.062 -3.273  -10.770 1.00 34.38  ? 281 ASP A CA    1 
ATOM   2179 C C     . ASP A 1 281 ? 17.915 -3.116  -9.257  1.00 32.54  ? 281 ASP A C     1 
ATOM   2180 O O     . ASP A 1 281 ? 18.862 -3.308  -8.493  1.00 29.16  ? 281 ASP A O     1 
ATOM   2181 C CB    . ASP A 1 281 ? 18.341 -1.920  -11.427 1.00 39.27  ? 281 ASP A CB    1 
ATOM   2182 C CG    . ASP A 1 281 ? 19.112 -2.009  -12.735 1.00 46.70  ? 281 ASP A CG    1 
ATOM   2183 O OD1   . ASP A 1 281 ? 19.800 -3.028  -12.968 1.00 46.11  ? 281 ASP A OD1   1 
ATOM   2184 O OD2   . ASP A 1 281 ? 19.021 -1.051  -13.519 1.00 59.72  ? 281 ASP A OD2   1 
ATOM   2185 N N     . ALA A 1 282 ? 16.718 -2.742  -8.819  1.00 33.73  ? 282 ALA A N     1 
ATOM   2186 C CA    . ALA A 1 282 ? 16.485 -2.532  -7.403  1.00 33.69  ? 282 ALA A CA    1 
ATOM   2187 C C     . ALA A 1 282 ? 16.614 -3.854  -6.651  1.00 29.77  ? 282 ALA A C     1 
ATOM   2188 O O     . ALA A 1 282 ? 17.117 -3.874  -5.530  1.00 26.13  ? 282 ALA A O     1 
ATOM   2189 C CB    . ALA A 1 282 ? 15.124 -1.926  -7.200  1.00 35.50  ? 282 ALA A CB    1 
ATOM   2190 N N     . ALA A 1 283 ? 16.187 -4.948  -7.300  1.00 28.36  ? 283 ALA A N     1 
ATOM   2191 C CA    . ALA A 1 283 ? 16.141 -6.263  -6.683  1.00 27.63  ? 283 ALA A CA    1 
ATOM   2192 C C     . ALA A 1 283 ? 17.539 -6.804  -6.389  1.00 29.51  ? 283 ALA A C     1 
ATOM   2193 O O     . ALA A 1 283 ? 17.673 -7.830  -5.732  1.00 33.21  ? 283 ALA A O     1 
ATOM   2194 C CB    . ALA A 1 283 ? 15.397 -7.213  -7.569  1.00 28.01  ? 283 ALA A CB    1 
ATOM   2195 N N     . ILE A 1 284 ? 18.574 -6.105  -6.863  1.00 31.38  ? 284 ILE A N     1 
ATOM   2196 C CA    . ILE A 1 284 ? 19.944 -6.465  -6.569  1.00 34.82  ? 284 ILE A CA    1 
ATOM   2197 C C     . ILE A 1 284 ? 20.319 -6.045  -5.143  1.00 36.18  ? 284 ILE A C     1 
ATOM   2198 O O     . ILE A 1 284 ? 21.205 -6.668  -4.552  1.00 38.88  ? 284 ILE A O     1 
ATOM   2199 C CB    . ILE A 1 284 ? 20.896 -5.883  -7.644  1.00 39.74  ? 284 ILE A CB    1 
ATOM   2200 C CG1   . ILE A 1 284 ? 20.563 -6.407  -9.046  1.00 42.36  ? 284 ILE A CG1   1 
ATOM   2201 C CG2   . ILE A 1 284 ? 22.364 -6.133  -7.300  1.00 39.34  ? 284 ILE A CG2   1 
ATOM   2202 C CD1   . ILE A 1 284 ? 20.974 -7.850  -9.302  1.00 42.55  ? 284 ILE A CD1   1 
ATOM   2203 N N     . THR A 1 285 ? 19.688 -4.993  -4.598  1.00 34.77  ? 285 THR A N     1 
ATOM   2204 C CA    . THR A 1 285 ? 20.090 -4.463  -3.300  1.00 36.56  ? 285 THR A CA    1 
ATOM   2205 C C     . THR A 1 285 ? 18.919 -4.377  -2.309  1.00 32.48  ? 285 THR A C     1 
ATOM   2206 O O     . THR A 1 285 ? 19.140 -4.105  -1.146  1.00 30.69  ? 285 THR A O     1 
ATOM   2207 C CB    . THR A 1 285 ? 20.823 -3.120  -3.475  1.00 40.55  ? 285 THR A CB    1 
ATOM   2208 O OG1   . THR A 1 285 ? 19.925 -2.060  -3.823  1.00 37.57  ? 285 THR A OG1   1 
ATOM   2209 C CG2   . THR A 1 285 ? 21.920 -3.208  -4.518  1.00 40.03  ? 285 THR A CG2   1 
ATOM   2210 N N     . ARG A 1 286 ? 17.682 -4.631  -2.740  1.00 31.31  ? 286 ARG A N     1 
ATOM   2211 C CA    . ARG A 1 286 ? 16.517 -4.516  -1.879  1.00 28.98  ? 286 ARG A CA    1 
ATOM   2212 C C     . ARG A 1 286 ? 15.482 -5.576  -2.258  1.00 29.70  ? 286 ARG A C     1 
ATOM   2213 O O     . ARG A 1 286 ? 15.513 -6.116  -3.374  1.00 33.87  ? 286 ARG A O     1 
ATOM   2214 C CB    . ARG A 1 286 ? 15.874 -3.134  -2.049  1.00 34.71  ? 286 ARG A CB    1 
ATOM   2215 C CG    . ARG A 1 286 ? 16.719 -1.926  -1.644  1.00 39.64  ? 286 ARG A CG    1 
ATOM   2216 C CD    . ARG A 1 286 ? 17.091 -1.860  -0.169  1.00 45.02  ? 286 ARG A CD    1 
ATOM   2217 N NE    . ARG A 1 286 ? 17.098 -0.498  0.353   1.00 58.09  ? 286 ARG A NE    1 
ATOM   2218 C CZ    . ARG A 1 286 ? 18.191 0.244   0.533   1.00 67.01  ? 286 ARG A CZ    1 
ATOM   2219 N NH1   . ARG A 1 286 ? 19.371 -0.250  0.200   1.00 62.10  ? 286 ARG A NH1   1 
ATOM   2220 N NH2   . ARG A 1 286 ? 18.098 1.479   1.012   1.00 73.82  ? 286 ARG A NH2   1 
ATOM   2221 N N     . THR A 1 287 ? 14.540 -5.845  -1.338  1.00 28.10  ? 287 THR A N     1 
ATOM   2222 C CA    . THR A 1 287 ? 13.388 -6.687  -1.619  1.00 29.33  ? 287 THR A CA    1 
ATOM   2223 C C     . THR A 1 287 ? 12.095 -5.872  -1.678  1.00 30.31  ? 287 THR A C     1 
ATOM   2224 O O     . THR A 1 287 ? 12.016 -4.750  -1.170  1.00 29.29  ? 287 THR A O     1 
ATOM   2225 C CB    . THR A 1 287 ? 13.200 -7.788  -0.573  1.00 30.06  ? 287 THR A CB    1 
ATOM   2226 O OG1   . THR A 1 287 ? 12.644 -7.176  0.603   1.00 31.46  ? 287 THR A OG1   1 
ATOM   2227 C CG2   . THR A 1 287 ? 14.494 -8.517  -0.290  1.00 29.07  ? 287 THR A CG2   1 
ATOM   2228 N N     . LYS A 1 288 ? 11.061 -6.499  -2.257  1.00 28.84  ? 288 LYS A N     1 
ATOM   2229 C CA    . LYS A 1 288 ? 9.759  -5.875  -2.407  1.00 29.80  ? 288 LYS A CA    1 
ATOM   2230 C C     . LYS A 1 288 ? 9.252  -5.363  -1.058  1.00 28.58  ? 288 LYS A C     1 
ATOM   2231 O O     . LYS A 1 288 ? 8.723  -4.259  -0.967  1.00 27.55  ? 288 LYS A O     1 
ATOM   2232 C CB    . LYS A 1 288 ? 8.748  -6.862  -3.004  1.00 31.25  ? 288 LYS A CB    1 
ATOM   2233 C CG    . LYS A 1 288 ? 7.418  -6.203  -3.337  1.00 35.81  ? 288 LYS A CG    1 
ATOM   2234 C CD    . LYS A 1 288 ? 6.530  -6.954  -4.273  1.00 37.60  ? 288 LYS A CD    1 
ATOM   2235 C CE    . LYS A 1 288 ? 5.758  -8.067  -3.614  1.00 41.99  ? 288 LYS A CE    1 
ATOM   2236 N NZ    . LYS A 1 288 ? 4.627  -8.501  -4.468  1.00 45.44  ? 288 LYS A NZ    1 
ATOM   2237 N N     . SER A 1 289 ? 9.439  -6.179  -0.026  1.00 29.23  ? 289 SER A N     1 
ATOM   2238 C CA    . SER A 1 289 ? 8.862  -5.962  1.288   1.00 33.03  ? 289 SER A CA    1 
ATOM   2239 C C     . SER A 1 289 ? 9.407  -4.690  1.940   1.00 30.58  ? 289 SER A C     1 
ATOM   2240 O O     . SER A 1 289 ? 8.814  -4.182  2.870   1.00 30.28  ? 289 SER A O     1 
ATOM   2241 C CB    . SER A 1 289 ? 9.121  -7.174  2.175   1.00 32.65  ? 289 SER A CB    1 
ATOM   2242 O OG    . SER A 1 289 ? 10.519 -7.325  2.432   1.00 30.60  ? 289 SER A OG    1 
ATOM   2243 N N     . GLN A 1 290 ? 10.537 -4.176  1.469   1.00 34.30  ? 290 GLN A N     1 
ATOM   2244 C CA    . GLN A 1 290 ? 11.033 -2.895  1.955   1.00 38.89  ? 290 GLN A CA    1 
ATOM   2245 C C     . GLN A 1 290 ? 10.133 -1.723  1.550   1.00 33.56  ? 290 GLN A C     1 
ATOM   2246 O O     . GLN A 1 290 ? 10.198 -0.652  2.160   1.00 28.85  ? 290 GLN A O     1 
ATOM   2247 C CB    . GLN A 1 290 ? 12.427 -2.623  1.402   1.00 48.95  ? 290 GLN A CB    1 
ATOM   2248 C CG    . GLN A 1 290 ? 13.285 -1.769  2.329   1.00 66.24  ? 290 GLN A CG    1 
ATOM   2249 C CD    . GLN A 1 290 ? 14.549 -2.511  2.697   1.00 90.48  ? 290 GLN A CD    1 
ATOM   2250 O OE1   . GLN A 1 290 ? 14.616 -3.742  2.618   1.00 92.45  ? 290 GLN A OE1   1 
ATOM   2251 N NE2   . GLN A 1 290 ? 15.563 -1.763  3.105   1.00 101.21 ? 290 GLN A NE2   1 
ATOM   2252 N N     . TYR A 1 291 ? 9.318  -1.911  0.502   1.00 32.84  ? 291 TYR A N     1 
ATOM   2253 C CA    . TYR A 1 291 ? 8.539  -0.832  -0.090  1.00 29.71  ? 291 TYR A CA    1 
ATOM   2254 C C     . TYR A 1 291 ? 7.047  -1.148  -0.048  1.00 28.17  ? 291 TYR A C     1 
ATOM   2255 O O     . TYR A 1 291 ? 6.230  -0.237  0.004   1.00 32.42  ? 291 TYR A O     1 
ATOM   2256 C CB    . TYR A 1 291 ? 8.975  -0.603  -1.544  1.00 28.37  ? 291 TYR A CB    1 
ATOM   2257 C CG    . TYR A 1 291 ? 10.432 -0.279  -1.722  1.00 27.14  ? 291 TYR A CG    1 
ATOM   2258 C CD1   . TYR A 1 291 ? 10.916 0.984   -1.433  1.00 26.73  ? 291 TYR A CD1   1 
ATOM   2259 C CD2   . TYR A 1 291 ? 11.335 -1.231  -2.170  1.00 29.64  ? 291 TYR A CD2   1 
ATOM   2260 C CE1   . TYR A 1 291 ? 12.255 1.303   -1.590  1.00 28.07  ? 291 TYR A CE1   1 
ATOM   2261 C CE2   . TYR A 1 291 ? 12.684 -0.933  -2.321  1.00 29.82  ? 291 TYR A CE2   1 
ATOM   2262 C CZ    . TYR A 1 291 ? 13.146 0.340   -2.030  1.00 29.93  ? 291 TYR A CZ    1 
ATOM   2263 O OH    . TYR A 1 291 ? 14.472 0.678   -2.166  1.00 30.06  ? 291 TYR A OH    1 
ATOM   2264 N N     . TYR A 1 292 ? 6.670  -2.422  -0.122  1.00 30.21  ? 292 TYR A N     1 
ATOM   2265 C CA    . TYR A 1 292 ? 5.276  -2.747  -0.374  1.00 36.11  ? 292 TYR A CA    1 
ATOM   2266 C C     . TYR A 1 292 ? 4.939  -4.162  0.096   1.00 36.85  ? 292 TYR A C     1 
ATOM   2267 O O     . TYR A 1 292 ? 5.562  -5.123  -0.340  1.00 40.61  ? 292 TYR A O     1 
ATOM   2268 C CB    . TYR A 1 292 ? 5.017  -2.555  -1.867  1.00 38.08  ? 292 TYR A CB    1 
ATOM   2269 C CG    . TYR A 1 292 ? 3.640  -2.899  -2.372  1.00 45.47  ? 292 TYR A CG    1 
ATOM   2270 C CD1   . TYR A 1 292 ? 2.546  -2.096  -2.082  1.00 52.71  ? 292 TYR A CD1   1 
ATOM   2271 C CD2   . TYR A 1 292 ? 3.443  -3.998  -3.196  1.00 49.78  ? 292 TYR A CD2   1 
ATOM   2272 C CE1   . TYR A 1 292 ? 1.289  -2.379  -2.596  1.00 52.77  ? 292 TYR A CE1   1 
ATOM   2273 C CE2   . TYR A 1 292 ? 2.198  -4.295  -3.722  1.00 51.94  ? 292 TYR A CE2   1 
ATOM   2274 C CZ    . TYR A 1 292 ? 1.120  -3.480  -3.420  1.00 55.88  ? 292 TYR A CZ    1 
ATOM   2275 O OH    . TYR A 1 292 ? -0.111 -3.775  -3.934  1.00 59.20  ? 292 TYR A OH    1 
ATOM   2276 N N     . ASP A 1 293 ? 3.881  -4.280  0.907   1.00 42.89  ? 293 ASP A N     1 
ATOM   2277 C CA    . ASP A 1 293 ? 3.509  -5.530  1.556   1.00 45.50  ? 293 ASP A CA    1 
ATOM   2278 C C     . ASP A 1 293 ? 2.410  -6.275  0.792   1.00 45.98  ? 293 ASP A C     1 
ATOM   2279 O O     . ASP A 1 293 ? 2.074  -7.391  1.152   1.00 48.71  ? 293 ASP A O     1 
ATOM   2280 C CB    . ASP A 1 293 ? 3.084  -5.272  3.006   1.00 50.75  ? 293 ASP A CB    1 
ATOM   2281 C CG    . ASP A 1 293 ? 4.209  -4.754  3.898   1.00 56.28  ? 293 ASP A CG    1 
ATOM   2282 O OD1   . ASP A 1 293 ? 5.368  -5.279  3.755   1.00 48.37  ? 293 ASP A OD1   1 
ATOM   2283 O OD2   . ASP A 1 293 ? 3.924  -3.856  4.765   1.00 52.28  ? 293 ASP A OD2   1 
ATOM   2284 N N     . GLY A 1 294 ? 1.870  -5.710  -0.286  1.00 47.88  ? 294 GLY A N     1 
ATOM   2285 C CA    . GLY A 1 294 ? 0.851  -6.399  -1.071  1.00 53.27  ? 294 GLY A CA    1 
ATOM   2286 C C     . GLY A 1 294 ? 1.363  -7.623  -1.841  1.00 54.20  ? 294 GLY A C     1 
ATOM   2287 O O     . GLY A 1 294 ? 2.538  -7.716  -2.209  1.00 47.00  ? 294 GLY A O     1 
ATOM   2288 N N     . ASP A 1 295 ? 0.440  -8.556  -2.111  1.00 57.15  ? 295 ASP A N     1 
ATOM   2289 C CA    . ASP A 1 295 ? 0.766  -9.826  -2.747  1.00 57.51  ? 295 ASP A CA    1 
ATOM   2290 C C     . ASP A 1 295 ? 1.213  -9.627  -4.198  1.00 51.48  ? 295 ASP A C     1 
ATOM   2291 O O     . ASP A 1 295 ? 2.115  -10.311 -4.671  1.00 48.08  ? 295 ASP A O     1 
ATOM   2292 C CB    . ASP A 1 295 ? -0.413 -10.803 -2.648  1.00 58.47  ? 295 ASP A CB    1 
ATOM   2293 C CG    . ASP A 1 295 ? -0.185 -11.977 -1.706  1.00 61.54  ? 295 ASP A CG    1 
ATOM   2294 O OD1   . ASP A 1 295 ? 0.988  -12.347 -1.486  1.00 65.41  ? 295 ASP A OD1   1 
ATOM   2295 O OD2   . ASP A 1 295 ? -1.178 -12.525 -1.210  1.00 57.20  ? 295 ASP A OD2   1 
ATOM   2296 N N     . GLY A 1 296 ? 0.574  -8.701  -4.913  1.00 50.21  ? 296 GLY A N     1 
ATOM   2297 C CA    . GLY A 1 296 ? 0.782  -8.580  -6.347  1.00 54.28  ? 296 GLY A CA    1 
ATOM   2298 C C     . GLY A 1 296 ? 1.949  -7.668  -6.736  1.00 56.41  ? 296 GLY A C     1 
ATOM   2299 O O     . GLY A 1 296 ? 2.817  -7.328  -5.930  1.00 54.83  ? 296 GLY A O     1 
ATOM   2300 N N     . PRO A 1 297 ? 2.002  -7.244  -8.016  1.00 51.08  ? 297 PRO A N     1 
ATOM   2301 C CA    . PRO A 1 297 ? 3.084  -6.389  -8.502  1.00 52.29  ? 297 PRO A CA    1 
ATOM   2302 C C     . PRO A 1 297 ? 2.971  -4.963  -7.960  1.00 47.44  ? 297 PRO A C     1 
ATOM   2303 O O     . PRO A 1 297 ? 1.903  -4.552  -7.532  1.00 43.82  ? 297 PRO A O     1 
ATOM   2304 C CB    . PRO A 1 297 ? 2.904  -6.458  -10.029 1.00 53.42  ? 297 PRO A CB    1 
ATOM   2305 C CG    . PRO A 1 297 ? 1.417  -6.712  -10.231 1.00 49.60  ? 297 PRO A CG    1 
ATOM   2306 C CD    . PRO A 1 297 ? 1.018  -7.577  -9.057  1.00 48.93  ? 297 PRO A CD    1 
ATOM   2307 N N     . ILE A 1 298 ? 4.083  -4.218  -7.963  1.00 48.74  ? 298 ILE A N     1 
ATOM   2308 C CA    . ILE A 1 298 ? 4.129  -2.911  -7.314  1.00 46.51  ? 298 ILE A CA    1 
ATOM   2309 C C     . ILE A 1 298 ? 3.300  -1.903  -8.105  1.00 44.80  ? 298 ILE A C     1 
ATOM   2310 O O     . ILE A 1 298 ? 3.253  -1.949  -9.332  1.00 43.83  ? 298 ILE A O     1 
ATOM   2311 C CB    . ILE A 1 298 ? 5.576  -2.401  -7.139  1.00 41.07  ? 298 ILE A CB    1 
ATOM   2312 C CG1   . ILE A 1 298 ? 6.250  -2.141  -8.491  1.00 42.14  ? 298 ILE A CG1   1 
ATOM   2313 C CG2   . ILE A 1 298 ? 6.370  -3.354  -6.269  1.00 38.40  ? 298 ILE A CG2   1 
ATOM   2314 C CD1   . ILE A 1 298 ? 7.566  -1.409  -8.414  1.00 41.59  ? 298 ILE A CD1   1 
ATOM   2315 N N     . PRO A 1 299 ? 2.654  -0.934  -7.423  1.00 41.89  ? 299 PRO A N     1 
ATOM   2316 C CA    . PRO A 1 299 ? 2.007  0.186   -8.096  1.00 39.04  ? 299 PRO A CA    1 
ATOM   2317 C C     . PRO A 1 299 ? 2.960  1.335   -8.397  1.00 40.39  ? 299 PRO A C     1 
ATOM   2318 O O     . PRO A 1 299 ? 4.059  1.393   -7.852  1.00 39.88  ? 299 PRO A O     1 
ATOM   2319 C CB    . PRO A 1 299 ? 1.001  0.642   -7.042  1.00 36.84  ? 299 PRO A CB    1 
ATOM   2320 C CG    . PRO A 1 299 ? 1.743  0.438   -5.765  1.00 38.21  ? 299 PRO A CG    1 
ATOM   2321 C CD    . PRO A 1 299 ? 2.487  -0.869  -5.966  1.00 39.51  ? 299 PRO A CD    1 
ATOM   2322 N N     . PRO A 1 300 ? 2.562  2.266   -9.290  1.00 39.95  ? 300 PRO A N     1 
ATOM   2323 C CA    . PRO A 1 300 ? 3.361  3.445   -9.617  1.00 38.62  ? 300 PRO A CA    1 
ATOM   2324 C C     . PRO A 1 300 ? 3.927  4.239   -8.445  1.00 38.81  ? 300 PRO A C     1 
ATOM   2325 O O     . PRO A 1 300 ? 5.075  4.686   -8.511  1.00 42.85  ? 300 PRO A O     1 
ATOM   2326 C CB    . PRO A 1 300 ? 2.355  4.300   -10.402 1.00 41.04  ? 300 PRO A CB    1 
ATOM   2327 C CG    . PRO A 1 300 ? 1.562  3.257   -11.155 1.00 41.22  ? 300 PRO A CG    1 
ATOM   2328 C CD    . PRO A 1 300 ? 1.356  2.164   -10.125 1.00 40.56  ? 300 PRO A CD    1 
ATOM   2329 N N     . SER A 1 301 ? 3.147  4.422   -7.374  1.00 36.52  ? 301 SER A N     1 
ATOM   2330 C CA    . SER A 1 301 ? 3.623  5.264   -6.279  1.00 35.67  ? 301 SER A CA    1 
ATOM   2331 C C     . SER A 1 301 ? 4.858  4.633   -5.621  1.00 33.70  ? 301 SER A C     1 
ATOM   2332 O O     . SER A 1 301 ? 5.785  5.336   -5.215  1.00 35.30  ? 301 SER A O     1 
ATOM   2333 C CB    . SER A 1 301 ? 2.516  5.584   -5.288  1.00 35.24  ? 301 SER A CB    1 
ATOM   2334 O OG    . SER A 1 301 ? 1.932  4.404   -4.764  1.00 35.32  ? 301 SER A OG    1 
ATOM   2335 N N     . VAL A 1 302 ? 4.891  3.296   -5.556  1.00 30.49  ? 302 VAL A N     1 
ATOM   2336 C CA    . VAL A 1 302 ? 6.037  2.579   -5.017  1.00 31.04  ? 302 VAL A CA    1 
ATOM   2337 C C     . VAL A 1 302 ? 7.247  2.731   -5.941  1.00 31.29  ? 302 VAL A C     1 
ATOM   2338 O O     . VAL A 1 302 ? 8.371  2.911   -5.479  1.00 33.31  ? 302 VAL A O     1 
ATOM   2339 C CB    . VAL A 1 302 ? 5.697  1.095   -4.772  1.00 31.31  ? 302 VAL A CB    1 
ATOM   2340 C CG1   . VAL A 1 302 ? 6.942  0.214   -4.628  1.00 31.08  ? 302 VAL A CG1   1 
ATOM   2341 C CG2   . VAL A 1 302 ? 4.776  0.932   -3.570  1.00 29.04  ? 302 VAL A CG2   1 
ATOM   2342 N N     . ALA A 1 303 ? 7.043  2.645   -7.257  1.00 31.56  ? 303 ALA A N     1 
ATOM   2343 C CA    . ALA A 1 303 ? 8.165  2.821   -8.166  1.00 31.36  ? 303 ALA A CA    1 
ATOM   2344 C C     . ALA A 1 303 ? 8.873  4.154   -7.893  1.00 29.43  ? 303 ALA A C     1 
ATOM   2345 O O     . ALA A 1 303 ? 10.103 4.203   -7.887  1.00 28.17  ? 303 ALA A O     1 
ATOM   2346 C CB    . ALA A 1 303 ? 7.717  2.691   -9.603  1.00 31.55  ? 303 ALA A CB    1 
ATOM   2347 N N     . LYS A 1 304 ? 8.111  5.226   -7.633  1.00 29.74  ? 304 LYS A N     1 
ATOM   2348 C CA    . LYS A 1 304 ? 8.720  6.534   -7.462  1.00 33.81  ? 304 LYS A CA    1 
ATOM   2349 C C     . LYS A 1 304 ? 9.554  6.544   -6.182  1.00 31.32  ? 304 LYS A C     1 
ATOM   2350 O O     . LYS A 1 304 ? 10.624 7.160   -6.154  1.00 31.41  ? 304 LYS A O     1 
ATOM   2351 C CB    . LYS A 1 304 ? 7.671  7.655   -7.472  1.00 41.02  ? 304 LYS A CB    1 
ATOM   2352 C CG    . LYS A 1 304 ? 7.043  7.951   -8.832  1.00 52.42  ? 304 LYS A CG    1 
ATOM   2353 C CD    . LYS A 1 304 ? 5.792  8.826   -8.746  1.00 64.42  ? 304 LYS A CD    1 
ATOM   2354 C CE    . LYS A 1 304 ? 4.685  8.432   -9.707  1.00 71.51  ? 304 LYS A CE    1 
ATOM   2355 N NZ    . LYS A 1 304 ? 3.344  8.615   -9.090  1.00 74.53  ? 304 LYS A NZ    1 
ATOM   2356 N N     . THR A 1 305 ? 9.046  5.884   -5.129  1.00 27.32  ? 305 THR A N     1 
ATOM   2357 C CA    . THR A 1 305 ? 9.749  5.821   -3.862  1.00 27.11  ? 305 THR A CA    1 
ATOM   2358 C C     . THR A 1 305 ? 11.070 5.077   -4.071  1.00 26.25  ? 305 THR A C     1 
ATOM   2359 O O     . THR A 1 305 ? 12.149 5.532   -3.667  1.00 25.74  ? 305 THR A O     1 
ATOM   2360 C CB    . THR A 1 305 ? 8.863  5.160   -2.798  1.00 28.71  ? 305 THR A CB    1 
ATOM   2361 O OG1   . THR A 1 305 ? 7.760  6.031   -2.529  1.00 32.37  ? 305 THR A OG1   1 
ATOM   2362 C CG2   . THR A 1 305 ? 9.595  4.870   -1.510  1.00 27.00  ? 305 THR A CG2   1 
ATOM   2363 N N     . MET A 1 306 ? 10.981 3.960   -4.782  1.00 24.37  ? 306 MET A N     1 
ATOM   2364 C CA    . MET A 1 306 ? 12.152 3.158   -5.072  1.00 28.81  ? 306 MET A CA    1 
ATOM   2365 C C     . MET A 1 306 ? 13.199 3.965   -5.836  1.00 24.16  ? 306 MET A C     1 
ATOM   2366 O O     . MET A 1 306 ? 14.375 3.852   -5.552  1.00 21.63  ? 306 MET A O     1 
ATOM   2367 C CB    . MET A 1 306 ? 11.756 1.922   -5.888  1.00 32.31  ? 306 MET A CB    1 
ATOM   2368 C CG    . MET A 1 306 ? 11.012 0.890   -5.056  1.00 31.86  ? 306 MET A CG    1 
ATOM   2369 S SD    . MET A 1 306 ? 10.293 -0.371  -6.119  1.00 33.85  ? 306 MET A SD    1 
ATOM   2370 C CE    . MET A 1 306 ? 11.816 -1.087  -6.738  1.00 34.59  ? 306 MET A CE    1 
ATOM   2371 N N     . MET A 1 307 ? 12.772 4.748   -6.825  1.00 25.86  ? 307 MET A N     1 
ATOM   2372 C CA    . MET A 1 307 ? 13.691 5.516   -7.655  1.00 26.37  ? 307 MET A CA    1 
ATOM   2373 C C     . MET A 1 307 ? 14.430 6.533   -6.791  1.00 24.72  ? 307 MET A C     1 
ATOM   2374 O O     . MET A 1 307 ? 15.627 6.719   -6.944  1.00 20.95  ? 307 MET A O     1 
ATOM   2375 C CB    . MET A 1 307 ? 12.937 6.274   -8.750  1.00 28.28  ? 307 MET A CB    1 
ATOM   2376 C CG    . MET A 1 307 ? 12.585 5.443   -9.960  1.00 32.79  ? 307 MET A CG    1 
ATOM   2377 S SD    . MET A 1 307 ? 11.264 6.234   -10.927 1.00 38.05  ? 307 MET A SD    1 
ATOM   2378 C CE    . MET A 1 307 ? 12.118 7.716   -11.446 1.00 33.11  ? 307 MET A CE    1 
ATOM   2379 N N     . ALA A 1 308 ? 13.687 7.221   -5.911  1.00 26.15  ? 308 ALA A N     1 
ATOM   2380 C CA    . ALA A 1 308 ? 14.278 8.222   -5.029  1.00 28.33  ? 308 ALA A CA    1 
ATOM   2381 C C     . ALA A 1 308 ? 15.216 7.554   -4.024  1.00 29.76  ? 308 ALA A C     1 
ATOM   2382 O O     . ALA A 1 308 ? 16.288 8.074   -3.721  1.00 34.76  ? 308 ALA A O     1 
ATOM   2383 C CB    . ALA A 1 308 ? 13.187 8.982   -4.327  1.00 29.17  ? 308 ALA A CB    1 
ATOM   2384 N N     . ASP A 1 309 ? 14.807 6.391   -3.508  1.00 27.91  ? 309 ASP A N     1 
ATOM   2385 C CA    . ASP A 1 309 ? 15.593 5.714   -2.499  1.00 28.41  ? 309 ASP A CA    1 
ATOM   2386 C C     . ASP A 1 309 ? 16.911 5.222   -3.093  1.00 29.68  ? 309 ASP A C     1 
ATOM   2387 O O     . ASP A 1 309 ? 17.932 5.332   -2.429  1.00 29.05  ? 309 ASP A O     1 
ATOM   2388 C CB    . ASP A 1 309 ? 14.781 4.600   -1.848  1.00 29.43  ? 309 ASP A CB    1 
ATOM   2389 C CG    . ASP A 1 309 ? 15.557 3.786   -0.829  1.00 29.99  ? 309 ASP A CG    1 
ATOM   2390 O OD1   . ASP A 1 309 ? 16.175 4.412   0.059   1.00 32.63  ? 309 ASP A OD1   1 
ATOM   2391 O OD2   . ASP A 1 309 ? 15.529 2.528   -0.939  1.00 27.86  ? 309 ASP A OD2   1 
ATOM   2392 N N     . LEU A 1 310 ? 16.911 4.723   -4.346  1.00 33.24  ? 310 LEU A N     1 
ATOM   2393 C CA    . LEU A 1 310 ? 18.076 4.017   -4.882  1.00 31.61  ? 310 LEU A CA    1 
ATOM   2394 C C     . LEU A 1 310 ? 18.871 4.856   -5.875  1.00 27.89  ? 310 LEU A C     1 
ATOM   2395 O O     . LEU A 1 310 ? 19.953 4.450   -6.252  1.00 29.72  ? 310 LEU A O     1 
ATOM   2396 C CB    . LEU A 1 310 ? 17.633 2.692   -5.515  1.00 32.60  ? 310 LEU A CB    1 
ATOM   2397 C CG    . LEU A 1 310 ? 16.980 1.713   -4.535  1.00 37.15  ? 310 LEU A CG    1 
ATOM   2398 C CD1   . LEU A 1 310 ? 16.474 0.468   -5.241  1.00 39.34  ? 310 LEU A CD1   1 
ATOM   2399 C CD2   . LEU A 1 310 ? 17.927 1.315   -3.402  1.00 39.00  ? 310 LEU A CD2   1 
ATOM   2400 N N     . ASP A 1 311 ? 18.366 6.020   -6.282  1.00 31.49  ? 311 ASP A N     1 
ATOM   2401 C CA    . ASP A 1 311 ? 18.962 6.785   -7.371  1.00 32.09  ? 311 ASP A CA    1 
ATOM   2402 C C     . ASP A 1 311 ? 18.950 5.942   -8.641  1.00 30.87  ? 311 ASP A C     1 
ATOM   2403 O O     . ASP A 1 311 ? 19.977 5.740   -9.286  1.00 31.14  ? 311 ASP A O     1 
ATOM   2404 C CB    . ASP A 1 311 ? 20.375 7.255   -7.017  1.00 36.16  ? 311 ASP A CB    1 
ATOM   2405 C CG    . ASP A 1 311 ? 20.410 8.190   -5.819  1.00 41.90  ? 311 ASP A CG    1 
ATOM   2406 O OD1   . ASP A 1 311 ? 19.631 9.163   -5.826  1.00 45.31  ? 311 ASP A OD1   1 
ATOM   2407 O OD2   . ASP A 1 311 ? 21.200 7.927   -4.883  1.00 46.59  ? 311 ASP A OD2   1 
ATOM   2408 N N     . LEU A 1 312 ? 17.783 5.386   -8.948  1.00 29.40  ? 312 LEU A N     1 
ATOM   2409 C CA    . LEU A 1 312 ? 17.602 4.606   -10.158 1.00 29.85  ? 312 LEU A CA    1 
ATOM   2410 C C     . LEU A 1 312 ? 16.450 5.222   -10.930 1.00 28.40  ? 312 LEU A C     1 
ATOM   2411 O O     . LEU A 1 312 ? 15.615 5.887   -10.316 1.00 27.36  ? 312 LEU A O     1 
ATOM   2412 C CB    . LEU A 1 312 ? 17.274 3.154   -9.818  1.00 28.10  ? 312 LEU A CB    1 
ATOM   2413 C CG    . LEU A 1 312 ? 18.435 2.346   -9.249  1.00 30.25  ? 312 LEU A CG    1 
ATOM   2414 C CD1   . LEU A 1 312 ? 17.966 0.934   -8.917  1.00 31.28  ? 312 LEU A CD1   1 
ATOM   2415 C CD2   . LEU A 1 312 ? 19.613 2.323   -10.217 1.00 29.36  ? 312 LEU A CD2   1 
ATOM   2416 N N     . GLY A 1 313 ? 16.445 4.983   -12.248 1.00 24.65  ? 313 GLY A N     1 
ATOM   2417 C CA    . GLY A 1 313 ? 15.368 5.421   -13.109 1.00 26.40  ? 313 GLY A CA    1 
ATOM   2418 C C     . GLY A 1 313 ? 14.377 4.288   -13.324 1.00 27.42  ? 313 GLY A C     1 
ATOM   2419 O O     . GLY A 1 313 ? 14.526 3.216   -12.742 1.00 30.01  ? 313 GLY A O     1 
ATOM   2420 N N     . MET A 1 314 ? 13.360 4.545   -14.153 1.00 29.98  ? 314 MET A N     1 
ATOM   2421 C CA    . MET A 1 314 ? 12.522 3.479   -14.686 1.00 31.21  ? 314 MET A CA    1 
ATOM   2422 C C     . MET A 1 314 ? 13.316 2.658   -15.704 1.00 26.96  ? 314 MET A C     1 
ATOM   2423 O O     . MET A 1 314 ? 13.076 1.475   -15.886 1.00 25.99  ? 314 MET A O     1 
ATOM   2424 C CB    . MET A 1 314 ? 11.269 4.074   -15.333 1.00 32.55  ? 314 MET A CB    1 
ATOM   2425 C CG    . MET A 1 314 ? 10.303 4.646   -14.297 1.00 35.07  ? 314 MET A CG    1 
ATOM   2426 S SD    . MET A 1 314 ? 9.716  3.410   -13.083 1.00 42.03  ? 314 MET A SD    1 
ATOM   2427 C CE    . MET A 1 314 ? 8.655  2.369   -14.083 1.00 40.38  ? 314 MET A CE    1 
ATOM   2428 N N     . TRP A 1 315 ? 14.303 3.298   -16.326 1.00 26.90  ? 315 TRP A N     1 
ATOM   2429 C CA    . TRP A 1 315 ? 15.246 2.644   -17.212 1.00 27.17  ? 315 TRP A CA    1 
ATOM   2430 C C     . TRP A 1 315 ? 16.648 3.076   -16.817 1.00 27.22  ? 315 TRP A C     1 
ATOM   2431 O O     . TRP A 1 315 ? 16.882 4.244   -16.480 1.00 25.92  ? 315 TRP A O     1 
ATOM   2432 C CB    . TRP A 1 315 ? 14.929 2.968   -18.672 1.00 28.56  ? 315 TRP A CB    1 
ATOM   2433 C CG    . TRP A 1 315 ? 13.607 2.419   -19.127 1.00 27.51  ? 315 TRP A CG    1 
ATOM   2434 C CD1   . TRP A 1 315 ? 12.463 3.112   -19.404 1.00 27.69  ? 315 TRP A CD1   1 
ATOM   2435 C CD2   . TRP A 1 315 ? 13.300 1.040   -19.365 1.00 26.48  ? 315 TRP A CD2   1 
ATOM   2436 N NE1   . TRP A 1 315 ? 11.471 2.257   -19.810 1.00 26.81  ? 315 TRP A NE1   1 
ATOM   2437 C CE2   . TRP A 1 315 ? 11.957 0.979   -19.781 1.00 27.12  ? 315 TRP A CE2   1 
ATOM   2438 C CE3   . TRP A 1 315 ? 14.038 -0.138  -19.280 1.00 29.83  ? 315 TRP A CE3   1 
ATOM   2439 C CZ2   . TRP A 1 315 ? 11.337 -0.219  -20.096 1.00 27.23  ? 315 TRP A CZ2   1 
ATOM   2440 C CZ3   . TRP A 1 315 ? 13.425 -1.333  -19.580 1.00 29.25  ? 315 TRP A CZ3   1 
ATOM   2441 C CH2   . TRP A 1 315 ? 12.092 -1.361  -19.976 1.00 31.93  ? 315 TRP A CH2   1 
ATOM   2442 N N     . ASN A 1 316 ? 17.547 2.088   -16.815 1.00 26.84  ? 316 ASN A N     1 
ATOM   2443 C CA    . ASN A 1 316 ? 18.889 2.250   -16.296 1.00 27.34  ? 316 ASN A CA    1 
ATOM   2444 C C     . ASN A 1 316 ? 19.876 1.692   -17.312 1.00 26.46  ? 316 ASN A C     1 
ATOM   2445 O O     . ASN A 1 316 ? 20.032 0.490   -17.421 1.00 24.16  ? 316 ASN A O     1 
ATOM   2446 C CB    . ASN A 1 316 ? 19.037 1.557   -14.948 1.00 30.24  ? 316 ASN A CB    1 
ATOM   2447 C CG    . ASN A 1 316 ? 18.056 2.085   -13.930 1.00 30.65  ? 316 ASN A CG    1 
ATOM   2448 O OD1   . ASN A 1 316 ? 18.186 3.204   -13.467 1.00 32.43  ? 316 ASN A OD1   1 
ATOM   2449 N ND2   . ASN A 1 316 ? 17.037 1.313   -13.618 1.00 34.46  ? 316 ASN A ND2   1 
ATOM   2450 N N     . PHE A 1 317 ? 20.536 2.602   -18.028 1.00 27.93  ? 317 PHE A N     1 
ATOM   2451 C CA    . PHE A 1 317 ? 21.465 2.263   -19.076 1.00 27.58  ? 317 PHE A CA    1 
ATOM   2452 C C     . PHE A 1 317 ? 22.867 2.191   -18.486 1.00 30.22  ? 317 PHE A C     1 
ATOM   2453 O O     . PHE A 1 317 ? 23.488 3.222   -18.241 1.00 34.91  ? 317 PHE A O     1 
ATOM   2454 C CB    . PHE A 1 317 ? 21.334 3.265   -20.234 1.00 27.75  ? 317 PHE A CB    1 
ATOM   2455 C CG    . PHE A 1 317 ? 22.474 3.203   -21.219 1.00 27.50  ? 317 PHE A CG    1 
ATOM   2456 C CD1   . PHE A 1 317 ? 23.036 1.985   -21.578 1.00 27.16  ? 317 PHE A CD1   1 
ATOM   2457 C CD2   . PHE A 1 317 ? 23.013 4.360   -21.752 1.00 27.49  ? 317 PHE A CD2   1 
ATOM   2458 C CE1   . PHE A 1 317 ? 24.098 1.924   -22.465 1.00 27.40  ? 317 PHE A CE1   1 
ATOM   2459 C CE2   . PHE A 1 317 ? 24.065 4.300   -22.652 1.00 28.64  ? 317 PHE A CE2   1 
ATOM   2460 C CZ    . PHE A 1 317 ? 24.603 3.081   -23.008 1.00 29.32  ? 317 PHE A CZ    1 
ATOM   2461 N N     . CYS A 1 318 ? 23.370 0.960   -18.311 1.00 30.93  ? 318 CYS A N     1 
ATOM   2462 C CA    . CYS A 1 318 ? 24.749 0.736   -17.913 1.00 32.56  ? 318 CYS A CA    1 
ATOM   2463 C C     . CYS A 1 318 ? 25.628 0.400   -19.117 1.00 29.97  ? 318 CYS A C     1 
ATOM   2464 O O     . CYS A 1 318 ? 25.281 -0.465  -19.916 1.00 29.03  ? 318 CYS A O     1 
ATOM   2465 C CB    . CYS A 1 318 ? 24.844 -0.413  -16.923 1.00 36.96  ? 318 CYS A CB    1 
ATOM   2466 S SG    . CYS A 1 318 ? 24.503 0.081   -15.223 1.00 49.48  ? 318 CYS A SG    1 
ATOM   2467 N N     . GLY A 1 319 ? 26.790 1.053   -19.196 1.00 26.89  ? 319 GLY A N     1 
ATOM   2468 C CA    . GLY A 1 319 ? 27.764 0.803   -20.250 1.00 28.26  ? 319 GLY A CA    1 
ATOM   2469 C C     . GLY A 1 319 ? 29.162 1.148   -19.753 1.00 27.31  ? 319 GLY A C     1 
ATOM   2470 O O     . GLY A 1 319 ? 29.309 1.601   -18.623 1.00 25.95  ? 319 GLY A O     1 
ATOM   2471 N N     . ALA A 1 320 ? 30.184 0.933   -20.582 1.00 25.54  ? 320 ALA A N     1 
ATOM   2472 C CA    . ALA A 1 320 ? 31.526 1.291   -20.161 1.00 25.96  ? 320 ALA A CA    1 
ATOM   2473 C C     . ALA A 1 320 ? 32.373 1.790   -21.330 1.00 27.64  ? 320 ALA A C     1 
ATOM   2474 O O     . ALA A 1 320 ? 32.223 1.333   -22.468 1.00 31.36  ? 320 ALA A O     1 
ATOM   2475 C CB    . ALA A 1 320 ? 32.178 0.105   -19.490 1.00 25.94  ? 320 ALA A CB    1 
ATOM   2476 N N     . LEU A 1 321 ? 33.327 2.670   -20.987 1.00 29.42  ? 321 LEU A N     1 
ATOM   2477 C CA    . LEU A 1 321 ? 34.332 3.180   -21.906 1.00 28.97  ? 321 LEU A CA    1 
ATOM   2478 C C     . LEU A 1 321 ? 35.627 2.400   -21.687 1.00 26.35  ? 321 LEU A C     1 
ATOM   2479 O O     . LEU A 1 321 ? 35.952 2.064   -20.557 1.00 25.71  ? 321 LEU A O     1 
ATOM   2480 C CB    . LEU A 1 321 ? 34.558 4.672   -21.646 1.00 27.74  ? 321 LEU A CB    1 
ATOM   2481 C CG    . LEU A 1 321 ? 33.298 5.513   -21.481 1.00 29.43  ? 321 LEU A CG    1 
ATOM   2482 C CD1   . LEU A 1 321 ? 33.649 6.888   -20.921 1.00 28.66  ? 321 LEU A CD1   1 
ATOM   2483 C CD2   . LEU A 1 321 ? 32.552 5.636   -22.802 1.00 28.84  ? 321 LEU A CD2   1 
ATOM   2484 N N     . TYR A 1 322 ? 36.363 2.142   -22.775 1.00 24.31  ? 322 TYR A N     1 
ATOM   2485 C CA    . TYR A 1 322 ? 37.586 1.367   -22.700 1.00 24.50  ? 322 TYR A CA    1 
ATOM   2486 C C     . TYR A 1 322 ? 38.680 2.035   -23.513 1.00 24.66  ? 322 TYR A C     1 
ATOM   2487 O O     . TYR A 1 322 ? 38.408 2.574   -24.560 1.00 24.80  ? 322 TYR A O     1 
ATOM   2488 C CB    . TYR A 1 322 ? 37.384 -0.056  -23.213 1.00 21.05  ? 322 TYR A CB    1 
ATOM   2489 C CG    . TYR A 1 322 ? 36.304 -0.850  -22.535 1.00 20.23  ? 322 TYR A CG    1 
ATOM   2490 C CD1   . TYR A 1 322 ? 34.968 -0.655  -22.859 1.00 21.53  ? 322 TYR A CD1   1 
ATOM   2491 C CD2   . TYR A 1 322 ? 36.591 -1.778  -21.552 1.00 20.00  ? 322 TYR A CD2   1 
ATOM   2492 C CE1   . TYR A 1 322 ? 33.953 -1.412  -22.297 1.00 20.32  ? 322 TYR A CE1   1 
ATOM   2493 C CE2   . TYR A 1 322 ? 35.575 -2.517  -20.944 1.00 20.59  ? 322 TYR A CE2   1 
ATOM   2494 C CZ    . TYR A 1 322 ? 34.262 -2.343  -21.327 1.00 19.96  ? 322 TYR A CZ    1 
ATOM   2495 O OH    . TYR A 1 322 ? 33.244 -3.083  -20.798 1.00 23.81  ? 322 TYR A OH    1 
ATOM   2496 N N     . GLY A 1 323 ? 39.898 2.020   -22.974 1.00 29.09  ? 323 GLY A N     1 
ATOM   2497 C CA    . GLY A 1 323 ? 41.080 2.433   -23.699 1.00 30.37  ? 323 GLY A CA    1 
ATOM   2498 C C     . GLY A 1 323 ? 41.684 3.701   -23.111 1.00 33.35  ? 323 GLY A C     1 
ATOM   2499 O O     . GLY A 1 323 ? 41.333 4.102   -22.005 1.00 30.62  ? 323 GLY A O     1 
ATOM   2500 N N     . PRO A 1 324 ? 42.570 4.386   -23.874 1.00 37.76  ? 324 PRO A N     1 
ATOM   2501 C CA    . PRO A 1 324 ? 43.246 5.597   -23.394 1.00 34.10  ? 324 PRO A CA    1 
ATOM   2502 C C     . PRO A 1 324 ? 42.253 6.711   -23.066 1.00 37.18  ? 324 PRO A C     1 
ATOM   2503 O O     . PRO A 1 324 ? 41.206 6.809   -23.706 1.00 33.33  ? 324 PRO A O     1 
ATOM   2504 C CB    . PRO A 1 324 ? 44.113 6.018   -24.588 1.00 35.98  ? 324 PRO A CB    1 
ATOM   2505 C CG    . PRO A 1 324 ? 44.239 4.765   -25.458 1.00 34.57  ? 324 PRO A CG    1 
ATOM   2506 C CD    . PRO A 1 324 ? 42.932 4.032   -25.264 1.00 35.78  ? 324 PRO A CD    1 
ATOM   2507 N N     . PRO A 1 325 ? 42.536 7.587   -22.070 1.00 38.27  ? 325 PRO A N     1 
ATOM   2508 C CA    . PRO A 1 325 ? 41.645 8.703   -21.737 1.00 35.93  ? 325 PRO A CA    1 
ATOM   2509 C C     . PRO A 1 325 ? 41.167 9.529   -22.926 1.00 34.21  ? 325 PRO A C     1 
ATOM   2510 O O     . PRO A 1 325 ? 39.976 9.831   -23.016 1.00 35.56  ? 325 PRO A O     1 
ATOM   2511 C CB    . PRO A 1 325 ? 42.484 9.525   -20.740 1.00 37.29  ? 325 PRO A CB    1 
ATOM   2512 C CG    . PRO A 1 325 ? 43.281 8.459   -20.023 1.00 38.35  ? 325 PRO A CG    1 
ATOM   2513 C CD    . PRO A 1 325 ? 43.664 7.489   -21.128 1.00 40.11  ? 325 PRO A CD    1 
ATOM   2514 N N     . PRO A 1 326 ? 42.049 9.949   -23.862 1.00 32.57  ? 326 PRO A N     1 
ATOM   2515 C CA    . PRO A 1 326 ? 41.603 10.724  -25.018 1.00 32.20  ? 326 PRO A CA    1 
ATOM   2516 C C     . PRO A 1 326 ? 40.466 10.038  -25.759 1.00 28.79  ? 326 PRO A C     1 
ATOM   2517 O O     . PRO A 1 326 ? 39.544 10.703  -26.162 1.00 30.17  ? 326 PRO A O     1 
ATOM   2518 C CB    . PRO A 1 326 ? 42.875 10.876  -25.879 1.00 31.71  ? 326 PRO A CB    1 
ATOM   2519 C CG    . PRO A 1 326 ? 43.985 10.842  -24.858 1.00 31.67  ? 326 PRO A CG    1 
ATOM   2520 C CD    . PRO A 1 326 ? 43.518 9.823   -23.830 1.00 33.48  ? 326 PRO A CD    1 
ATOM   2521 N N     . VAL A 1 327 ? 40.527 8.713   -25.901 1.00 30.33  ? 327 VAL A N     1 
ATOM   2522 C CA    . VAL A 1 327 ? 39.500 7.946   -26.586 1.00 28.49  ? 327 VAL A CA    1 
ATOM   2523 C C     . VAL A 1 327 ? 38.243 7.969   -25.725 1.00 26.26  ? 327 VAL A C     1 
ATOM   2524 O O     . VAL A 1 327 ? 37.177 8.357   -26.198 1.00 26.23  ? 327 VAL A O     1 
ATOM   2525 C CB    . VAL A 1 327 ? 39.972 6.504   -26.865 1.00 28.81  ? 327 VAL A CB    1 
ATOM   2526 C CG1   . VAL A 1 327 ? 38.891 5.630   -27.481 1.00 28.02  ? 327 VAL A CG1   1 
ATOM   2527 C CG2   . VAL A 1 327 ? 41.217 6.502   -27.732 1.00 30.62  ? 327 VAL A CG2   1 
ATOM   2528 N N     . MET A 1 328 ? 38.374 7.576   -24.455 1.00 24.99  ? 328 MET A N     1 
ATOM   2529 C CA    . MET A 1 328 ? 37.205 7.501   -23.582 1.00 27.22  ? 328 MET A CA    1 
ATOM   2530 C C     . MET A 1 328 ? 36.479 8.850   -23.531 1.00 27.45  ? 328 MET A C     1 
ATOM   2531 O O     . MET A 1 328 ? 35.259 8.864   -23.562 1.00 28.07  ? 328 MET A O     1 
ATOM   2532 C CB    . MET A 1 328 ? 37.564 7.033   -22.168 1.00 27.61  ? 328 MET A CB    1 
ATOM   2533 C CG    . MET A 1 328 ? 38.015 5.594   -22.146 1.00 29.94  ? 328 MET A CG    1 
ATOM   2534 S SD    . MET A 1 328 ? 38.259 4.882   -20.510 1.00 32.99  ? 328 MET A SD    1 
ATOM   2535 C CE    . MET A 1 328 ? 39.606 5.898   -19.909 1.00 32.17  ? 328 MET A CE    1 
ATOM   2536 N N     . ASP A 1 329 ? 37.210 9.976   -23.511 1.00 27.93  ? 329 ASP A N     1 
ATOM   2537 C CA    . ASP A 1 329 ? 36.589 11.295  -23.483 1.00 30.65  ? 329 ASP A CA    1 
ATOM   2538 C C     . ASP A 1 329 ? 35.791 11.565  -24.758 1.00 31.43  ? 329 ASP A C     1 
ATOM   2539 O O     . ASP A 1 329 ? 34.697 12.134  -24.702 1.00 31.63  ? 329 ASP A O     1 
ATOM   2540 C CB    . ASP A 1 329 ? 37.612 12.427  -23.378 1.00 33.38  ? 329 ASP A CB    1 
ATOM   2541 C CG    . ASP A 1 329 ? 38.288 12.545  -22.024 1.00 36.52  ? 329 ASP A CG    1 
ATOM   2542 O OD1   . ASP A 1 329 ? 37.714 12.055  -21.045 1.00 39.67  ? 329 ASP A OD1   1 
ATOM   2543 O OD2   . ASP A 1 329 ? 39.412 13.076  -21.979 1.00 39.32  ? 329 ASP A OD2   1 
ATOM   2544 N N     . THR A 1 330 ? 36.366 11.202  -25.908 1.00 29.66  ? 330 THR A N     1 
ATOM   2545 C CA    . THR A 1 330 ? 35.731 11.474  -27.181 1.00 28.50  ? 330 THR A CA    1 
ATOM   2546 C C     . THR A 1 330 ? 34.431 10.691  -27.282 1.00 26.74  ? 330 THR A C     1 
ATOM   2547 O O     . THR A 1 330 ? 33.400 11.236  -27.677 1.00 27.72  ? 330 THR A O     1 
ATOM   2548 C CB    . THR A 1 330 ? 36.634 11.068  -28.341 1.00 29.98  ? 330 THR A CB    1 
ATOM   2549 O OG1   . THR A 1 330 ? 37.881 11.709  -28.107 1.00 27.52  ? 330 THR A OG1   1 
ATOM   2550 C CG2   . THR A 1 330 ? 36.070 11.471  -29.687 1.00 30.77  ? 330 THR A CG2   1 
ATOM   2551 N N     . LEU A 1 331 ? 34.507 9.414   -26.905 1.00 26.65  ? 331 LEU A N     1 
ATOM   2552 C CA    . LEU A 1 331 ? 33.355 8.533   -26.944 1.00 28.62  ? 331 LEU A CA    1 
ATOM   2553 C C     . LEU A 1 331 ? 32.319 9.035   -25.937 1.00 26.35  ? 331 LEU A C     1 
ATOM   2554 O O     . LEU A 1 331 ? 31.136 9.110   -26.232 1.00 26.65  ? 331 LEU A O     1 
ATOM   2555 C CB    . LEU A 1 331 ? 33.786 7.081   -26.657 1.00 29.44  ? 331 LEU A CB    1 
ATOM   2556 C CG    . LEU A 1 331 ? 34.810 6.455   -27.615 1.00 31.02  ? 331 LEU A CG    1 
ATOM   2557 C CD1   . LEU A 1 331 ? 35.001 4.977   -27.325 1.00 31.16  ? 331 LEU A CD1   1 
ATOM   2558 C CD2   . LEU A 1 331 ? 34.418 6.618   -29.080 1.00 31.68  ? 331 LEU A CD2   1 
ATOM   2559 N N     . TRP A 1 332 ? 32.753 9.400   -24.738 1.00 27.90  ? 332 TRP A N     1 
ATOM   2560 C CA    . TRP A 1 332 ? 31.807 9.871   -23.732 1.00 29.72  ? 332 TRP A CA    1 
ATOM   2561 C C     . TRP A 1 332 ? 31.053 11.109  -24.240 1.00 28.59  ? 332 TRP A C     1 
ATOM   2562 O O     . TRP A 1 332 ? 29.828 11.182  -24.108 1.00 29.51  ? 332 TRP A O     1 
ATOM   2563 C CB    . TRP A 1 332 ? 32.513 10.116  -22.389 1.00 29.64  ? 332 TRP A CB    1 
ATOM   2564 C CG    . TRP A 1 332 ? 31.552 10.579  -21.347 1.00 29.94  ? 332 TRP A CG    1 
ATOM   2565 C CD1   . TRP A 1 332 ? 31.525 11.791  -20.725 1.00 28.69  ? 332 TRP A CD1   1 
ATOM   2566 C CD2   . TRP A 1 332 ? 30.403 9.856   -20.884 1.00 30.59  ? 332 TRP A CD2   1 
ATOM   2567 N NE1   . TRP A 1 332 ? 30.451 11.859  -19.887 1.00 31.21  ? 332 TRP A NE1   1 
ATOM   2568 C CE2   . TRP A 1 332 ? 29.726 10.701  -19.984 1.00 29.27  ? 332 TRP A CE2   1 
ATOM   2569 C CE3   . TRP A 1 332 ? 29.888 8.583   -21.144 1.00 30.84  ? 332 TRP A CE3   1 
ATOM   2570 C CZ2   . TRP A 1 332 ? 28.573 10.303  -19.317 1.00 27.97  ? 332 TRP A CZ2   1 
ATOM   2571 C CZ3   . TRP A 1 332 ? 28.746 8.188   -20.485 1.00 33.09  ? 332 TRP A CZ3   1 
ATOM   2572 C CH2   . TRP A 1 332 ? 28.099 9.041   -19.586 1.00 31.75  ? 332 TRP A CH2   1 
ATOM   2573 N N     . THR A 1 333 ? 31.762 12.056  -24.869 1.00 27.05  ? 333 THR A N     1 
ATOM   2574 C CA    . THR A 1 333 ? 31.129 13.267  -25.376 1.00 28.88  ? 333 THR A CA    1 
ATOM   2575 C C     . THR A 1 333 ? 29.945 12.904  -26.270 1.00 29.38  ? 333 THR A C     1 
ATOM   2576 O O     . THR A 1 333 ? 28.860 13.442  -26.109 1.00 28.75  ? 333 THR A O     1 
ATOM   2577 C CB    . THR A 1 333 ? 32.130 14.137  -26.140 1.00 33.41  ? 333 THR A CB    1 
ATOM   2578 O OG1   . THR A 1 333 ? 33.187 14.468  -25.249 1.00 33.46  ? 333 THR A OG1   1 
ATOM   2579 C CG2   . THR A 1 333 ? 31.549 15.421  -26.691 1.00 34.76  ? 333 THR A CG2   1 
ATOM   2580 N N     . ALA A 1 334 ? 30.146 11.946  -27.180 1.00 29.95  ? 334 ALA A N     1 
ATOM   2581 C CA    . ALA A 1 334 ? 29.103 11.542  -28.112 1.00 29.61  ? 334 ALA A CA    1 
ATOM   2582 C C     . ALA A 1 334 ? 27.948 10.847  -27.393 1.00 29.05  ? 334 ALA A C     1 
ATOM   2583 O O     . ALA A 1 334 ? 26.791 11.009  -27.793 1.00 27.61  ? 334 ALA A O     1 
ATOM   2584 C CB    . ALA A 1 334 ? 29.669 10.633  -29.175 1.00 31.02  ? 334 ALA A CB    1 
ATOM   2585 N N     . ILE A 1 335 ? 28.269 10.038  -26.374 1.00 26.10  ? 335 ILE A N     1 
ATOM   2586 C CA    . ILE A 1 335 ? 27.247 9.306   -25.643 1.00 27.52  ? 335 ILE A CA    1 
ATOM   2587 C C     . ILE A 1 335 ? 26.418 10.260  -24.772 1.00 27.43  ? 335 ILE A C     1 
ATOM   2588 O O     . ILE A 1 335 ? 25.201 10.278  -24.875 1.00 28.15  ? 335 ILE A O     1 
ATOM   2589 C CB    . ILE A 1 335 ? 27.855 8.154   -24.820 1.00 27.04  ? 335 ILE A CB    1 
ATOM   2590 C CG1   . ILE A 1 335 ? 28.556 7.131   -25.709 1.00 25.67  ? 335 ILE A CG1   1 
ATOM   2591 C CG2   . ILE A 1 335 ? 26.779 7.491   -23.961 1.00 28.23  ? 335 ILE A CG2   1 
ATOM   2592 C CD1   . ILE A 1 335 ? 29.492 6.214   -24.962 1.00 26.48  ? 335 ILE A CD1   1 
ATOM   2593 N N     . ARG A 1 336 ? 27.075 11.059  -23.932 1.00 31.48  ? 336 ARG A N     1 
ATOM   2594 C CA    . ARG A 1 336 ? 26.398 12.045  -23.101 1.00 33.80  ? 336 ARG A CA    1 
ATOM   2595 C C     . ARG A 1 336 ? 25.498 12.938  -23.960 1.00 31.94  ? 336 ARG A C     1 
ATOM   2596 O O     . ARG A 1 336 ? 24.295 13.021  -23.706 1.00 33.75  ? 336 ARG A O     1 
ATOM   2597 C CB    . ARG A 1 336 ? 27.441 12.844  -22.308 1.00 39.05  ? 336 ARG A CB    1 
ATOM   2598 C CG    . ARG A 1 336 ? 26.890 13.806  -21.257 1.00 41.57  ? 336 ARG A CG    1 
ATOM   2599 C CD    . ARG A 1 336 ? 27.905 14.908  -20.947 1.00 49.66  ? 336 ARG A CD    1 
ATOM   2600 N NE    . ARG A 1 336 ? 28.214 15.747  -22.130 1.00 55.77  ? 336 ARG A NE    1 
ATOM   2601 C CZ    . ARG A 1 336 ? 29.434 16.150  -22.526 1.00 55.00  ? 336 ARG A CZ    1 
ATOM   2602 N NH1   . ARG A 1 336 ? 30.521 15.873  -21.819 1.00 55.40  ? 336 ARG A NH1   1 
ATOM   2603 N NH2   . ARG A 1 336 ? 29.569 16.855  -23.638 1.00 52.49  ? 336 ARG A NH2   1 
ATOM   2604 N N     . ASP A 1 337 ? 26.055 13.568  -25.002 1.00 30.01  ? 337 ASP A N     1 
ATOM   2605 C CA    . ASP A 1 337 ? 25.286 14.484  -25.836 1.00 30.17  ? 337 ASP A CA    1 
ATOM   2606 C C     . ASP A 1 337 ? 24.114 13.778  -26.513 1.00 30.96  ? 337 ASP A C     1 
ATOM   2607 O O     . ASP A 1 337 ? 23.150 14.447  -26.861 1.00 33.46  ? 337 ASP A O     1 
ATOM   2608 C CB    . ASP A 1 337 ? 26.134 15.162  -26.914 1.00 32.57  ? 337 ASP A CB    1 
ATOM   2609 C CG    . ASP A 1 337 ? 27.271 15.991  -26.346 1.00 36.45  ? 337 ASP A CG    1 
ATOM   2610 O OD1   . ASP A 1 337 ? 27.252 16.253  -25.128 1.00 39.92  ? 337 ASP A OD1   1 
ATOM   2611 O OD2   . ASP A 1 337 ? 28.190 16.324  -27.114 1.00 44.90  ? 337 ASP A OD2   1 
ATOM   2612 N N     . SER A 1 338 ? 24.154 12.447  -26.679 1.00 28.20  ? 338 SER A N     1 
ATOM   2613 C CA    . SER A 1 338 ? 22.990 11.753  -27.225 1.00 29.12  ? 338 SER A CA    1 
ATOM   2614 C C     . SER A 1 338 ? 21.817 11.749  -26.241 1.00 30.41  ? 338 SER A C     1 
ATOM   2615 O O     . SER A 1 338 ? 20.683 11.571  -26.676 1.00 29.20  ? 338 SER A O     1 
ATOM   2616 C CB    . SER A 1 338 ? 23.294 10.333  -27.644 1.00 27.48  ? 338 SER A CB    1 
ATOM   2617 O OG    . SER A 1 338 ? 24.331 10.274  -28.606 1.00 25.71  ? 338 SER A OG    1 
ATOM   2618 N N     . PHE A 1 339 ? 22.071 11.869  -24.929 1.00 30.01  ? 339 PHE A N     1 
ATOM   2619 C CA    . PHE A 1 339 ? 21.003 11.657  -23.958 1.00 33.28  ? 339 PHE A CA    1 
ATOM   2620 C C     . PHE A 1 339 ? 20.701 12.900  -23.113 1.00 34.82  ? 339 PHE A C     1 
ATOM   2621 O O     . PHE A 1 339 ? 19.682 12.916  -22.426 1.00 34.78  ? 339 PHE A O     1 
ATOM   2622 C CB    . PHE A 1 339 ? 21.340 10.464  -23.061 1.00 33.13  ? 339 PHE A CB    1 
ATOM   2623 C CG    . PHE A 1 339 ? 21.390 9.151   -23.795 1.00 31.00  ? 339 PHE A CG    1 
ATOM   2624 C CD1   . PHE A 1 339 ? 20.220 8.512   -24.168 1.00 29.41  ? 339 PHE A CD1   1 
ATOM   2625 C CD2   . PHE A 1 339 ? 22.602 8.586   -24.152 1.00 28.48  ? 339 PHE A CD2   1 
ATOM   2626 C CE1   . PHE A 1 339 ? 20.256 7.313   -24.857 1.00 30.80  ? 339 PHE A CE1   1 
ATOM   2627 C CE2   . PHE A 1 339 ? 22.635 7.394   -24.853 1.00 29.21  ? 339 PHE A CE2   1 
ATOM   2628 C CZ    . PHE A 1 339 ? 21.464 6.770   -25.221 1.00 28.75  ? 339 PHE A CZ    1 
ATOM   2629 N N     . ALA A 1 340 ? 21.533 13.949  -23.223 1.00 34.37  ? 340 ALA A N     1 
ATOM   2630 C CA    . ALA A 1 340 ? 21.517 15.079  -22.304 1.00 37.01  ? 340 ALA A CA    1 
ATOM   2631 C C     . ALA A 1 340 ? 20.222 15.897  -22.341 1.00 37.36  ? 340 ALA A C     1 
ATOM   2632 O O     . ALA A 1 340 ? 19.901 16.537  -21.355 1.00 43.87  ? 340 ALA A O     1 
ATOM   2633 C CB    . ALA A 1 340 ? 22.709 15.963  -22.551 1.00 34.17  ? 340 ALA A CB    1 
ATOM   2634 N N     . ASP A 1 341 ? 19.467 15.884  -23.436 1.00 40.92  ? 341 ASP A N     1 
ATOM   2635 C CA    . ASP A 1 341 ? 18.316 16.765  -23.572 1.00 41.44  ? 341 ASP A CA    1 
ATOM   2636 C C     . ASP A 1 341 ? 17.028 16.040  -23.151 1.00 40.25  ? 341 ASP A C     1 
ATOM   2637 O O     . ASP A 1 341 ? 15.937 16.562  -23.346 1.00 37.83  ? 341 ASP A O     1 
ATOM   2638 C CB    . ASP A 1 341 ? 18.266 17.349  -25.001 1.00 44.03  ? 341 ASP A CB    1 
ATOM   2639 C CG    . ASP A 1 341 ? 17.890 16.404  -26.147 1.00 48.86  ? 341 ASP A CG    1 
ATOM   2640 O OD1   . ASP A 1 341 ? 17.547 15.244  -25.882 1.00 51.36  ? 341 ASP A OD1   1 
ATOM   2641 O OD2   . ASP A 1 341 ? 17.910 16.846  -27.325 1.00 49.30  ? 341 ASP A OD2   1 
ATOM   2642 N N     . ILE A 1 342 ? 17.118 14.811  -22.625 1.00 39.21  ? 342 ILE A N     1 
ATOM   2643 C CA    . ILE A 1 342 ? 15.920 14.081  -22.234 1.00 36.83  ? 342 ILE A CA    1 
ATOM   2644 C C     . ILE A 1 342 ? 15.522 14.556  -20.841 1.00 36.67  ? 342 ILE A C     1 
ATOM   2645 O O     . ILE A 1 342 ? 16.337 14.525  -19.920 1.00 34.31  ? 342 ILE A O     1 
ATOM   2646 C CB    . ILE A 1 342 ? 16.133 12.559  -22.282 1.00 35.88  ? 342 ILE A CB    1 
ATOM   2647 C CG1   . ILE A 1 342 ? 16.377 12.071  -23.709 1.00 34.28  ? 342 ILE A CG1   1 
ATOM   2648 C CG2   . ILE A 1 342 ? 14.980 11.805  -21.632 1.00 35.19  ? 342 ILE A CG2   1 
ATOM   2649 C CD1   . ILE A 1 342 ? 16.952 10.662  -23.774 1.00 34.48  ? 342 ILE A CD1   1 
ATOM   2650 N N     . PRO A 1 343 ? 14.286 15.071  -20.657 1.00 39.16  ? 343 PRO A N     1 
ATOM   2651 C CA    . PRO A 1 343 ? 13.863 15.564  -19.345 1.00 37.00  ? 343 PRO A CA    1 
ATOM   2652 C C     . PRO A 1 343 ? 13.964 14.433  -18.320 1.00 33.24  ? 343 PRO A C     1 
ATOM   2653 O O     . PRO A 1 343 ? 13.452 13.336  -18.567 1.00 34.62  ? 343 PRO A O     1 
ATOM   2654 C CB    . PRO A 1 343 ? 12.405 16.030  -19.545 1.00 35.37  ? 343 PRO A CB    1 
ATOM   2655 C CG    . PRO A 1 343 ? 12.230 16.149  -21.055 1.00 37.10  ? 343 PRO A CG    1 
ATOM   2656 C CD    . PRO A 1 343 ? 13.224 15.182  -21.676 1.00 38.61  ? 343 PRO A CD    1 
ATOM   2657 N N     . GLY A 1 344 ? 14.666 14.701  -17.213 1.00 29.70  ? 344 GLY A N     1 
ATOM   2658 C CA    . GLY A 1 344 ? 14.729 13.795  -16.075 1.00 32.54  ? 344 GLY A CA    1 
ATOM   2659 C C     . GLY A 1 344 ? 15.941 12.858  -16.116 1.00 35.51  ? 344 GLY A C     1 
ATOM   2660 O O     . GLY A 1 344 ? 16.074 11.976  -15.262 1.00 35.14  ? 344 GLY A O     1 
ATOM   2661 N N     . VAL A 1 345 ? 16.839 13.068  -17.089 1.00 33.64  ? 345 VAL A N     1 
ATOM   2662 C CA    . VAL A 1 345 ? 17.989 12.193  -17.276 1.00 34.72  ? 345 VAL A CA    1 
ATOM   2663 C C     . VAL A 1 345 ? 19.046 12.483  -16.203 1.00 31.00  ? 345 VAL A C     1 
ATOM   2664 O O     . VAL A 1 345 ? 19.323 13.631  -15.902 1.00 29.10  ? 345 VAL A O     1 
ATOM   2665 C CB    . VAL A 1 345 ? 18.559 12.322  -18.712 1.00 35.61  ? 345 VAL A CB    1 
ATOM   2666 C CG1   . VAL A 1 345 ? 19.254 13.650  -18.983 1.00 33.68  ? 345 VAL A CG1   1 
ATOM   2667 C CG2   . VAL A 1 345 ? 19.498 11.176  -19.070 1.00 36.59  ? 345 VAL A CG2   1 
ATOM   2668 N N     . LYS A 1 346 ? 19.697 11.437  -15.688 1.00 32.68  ? 346 LYS A N     1 
ATOM   2669 C CA    . LYS A 1 346 ? 20.849 11.616  -14.814 1.00 33.63  ? 346 LYS A CA    1 
ATOM   2670 C C     . LYS A 1 346 ? 22.006 10.692  -15.223 1.00 34.60  ? 346 LYS A C     1 
ATOM   2671 O O     . LYS A 1 346 ? 21.811 9.528   -15.622 1.00 30.31  ? 346 LYS A O     1 
ATOM   2672 C CB    . LYS A 1 346 ? 20.446 11.396  -13.350 1.00 37.03  ? 346 LYS A CB    1 
ATOM   2673 C CG    . LYS A 1 346 ? 19.477 12.420  -12.769 1.00 41.39  ? 346 LYS A CG    1 
ATOM   2674 C CD    . LYS A 1 346 ? 18.769 11.938  -11.514 1.00 49.78  ? 346 LYS A CD    1 
ATOM   2675 C CE    . LYS A 1 346 ? 17.672 12.866  -11.021 1.00 55.30  ? 346 LYS A CE    1 
ATOM   2676 N NZ    . LYS A 1 346 ? 16.500 12.880  -11.935 1.00 59.14  ? 346 LYS A NZ    1 
ATOM   2677 N N     . PHE A 1 347 ? 23.226 11.243  -15.083 1.00 32.93  ? 347 PHE A N     1 
ATOM   2678 C CA    . PHE A 1 347 ? 24.469 10.578  -15.436 1.00 34.17  ? 347 PHE A CA    1 
ATOM   2679 C C     . PHE A 1 347 ? 25.276 10.296  -14.166 1.00 36.54  ? 347 PHE A C     1 
ATOM   2680 O O     . PHE A 1 347 ? 25.429 11.169  -13.319 1.00 43.19  ? 347 PHE A O     1 
ATOM   2681 C CB    . PHE A 1 347 ? 25.297 11.443  -16.396 1.00 34.94  ? 347 PHE A CB    1 
ATOM   2682 C CG    . PHE A 1 347 ? 24.591 11.867  -17.662 1.00 36.73  ? 347 PHE A CG    1 
ATOM   2683 C CD1   . PHE A 1 347 ? 23.849 13.039  -17.711 1.00 34.56  ? 347 PHE A CD1   1 
ATOM   2684 C CD2   . PHE A 1 347 ? 24.633 11.073  -18.798 1.00 39.06  ? 347 PHE A CD2   1 
ATOM   2685 C CE1   . PHE A 1 347 ? 23.202 13.417  -18.877 1.00 37.31  ? 347 PHE A CE1   1 
ATOM   2686 C CE2   . PHE A 1 347 ? 23.957 11.435  -19.958 1.00 37.82  ? 347 PHE A CE2   1 
ATOM   2687 C CZ    . PHE A 1 347 ? 23.240 12.606  -19.998 1.00 37.90  ? 347 PHE A CZ    1 
ATOM   2688 N N     . TYR A 1 348 ? 25.810 9.076   -14.046 1.00 33.21  ? 348 TYR A N     1 
ATOM   2689 C CA    . TYR A 1 348 ? 26.674 8.716   -12.938 1.00 31.49  ? 348 TYR A CA    1 
ATOM   2690 C C     . TYR A 1 348 ? 27.880 7.936   -13.442 1.00 34.00  ? 348 TYR A C     1 
ATOM   2691 O O     . TYR A 1 348 ? 27.739 7.067   -14.301 1.00 34.53  ? 348 TYR A O     1 
ATOM   2692 C CB    . TYR A 1 348 ? 25.975 7.769   -11.967 1.00 32.86  ? 348 TYR A CB    1 
ATOM   2693 C CG    . TYR A 1 348 ? 24.655 8.243   -11.420 1.00 33.96  ? 348 TYR A CG    1 
ATOM   2694 C CD1   . TYR A 1 348 ? 24.588 8.995   -10.252 1.00 31.97  ? 348 TYR A CD1   1 
ATOM   2695 C CD2   . TYR A 1 348 ? 23.472 7.941   -12.077 1.00 32.80  ? 348 TYR A CD2   1 
ATOM   2696 C CE1   . TYR A 1 348 ? 23.371 9.419   -9.739  1.00 32.63  ? 348 TYR A CE1   1 
ATOM   2697 C CE2   . TYR A 1 348 ? 22.252 8.382   -11.592 1.00 34.99  ? 348 TYR A CE2   1 
ATOM   2698 C CZ    . TYR A 1 348 ? 22.203 9.110   -10.413 1.00 33.41  ? 348 TYR A CZ    1 
ATOM   2699 O OH    . TYR A 1 348 ? 20.995 9.507   -9.925  1.00 33.78  ? 348 TYR A OH    1 
ATOM   2700 N N     . PHE A 1 349 ? 29.047 8.260   -12.876 1.00 35.35  ? 349 PHE A N     1 
ATOM   2701 C CA    . PHE A 1 349 ? 30.199 7.379   -12.817 1.00 35.47  ? 349 PHE A CA    1 
ATOM   2702 C C     . PHE A 1 349 ? 30.266 6.833   -11.398 1.00 37.91  ? 349 PHE A C     1 
ATOM   2703 O O     . PHE A 1 349 ? 29.547 7.320   -10.526 1.00 37.66  ? 349 PHE A O     1 
ATOM   2704 C CB    . PHE A 1 349 ? 31.454 8.152   -13.240 1.00 38.74  ? 349 PHE A CB    1 
ATOM   2705 C CG    . PHE A 1 349 ? 31.449 8.474   -14.709 1.00 41.57  ? 349 PHE A CG    1 
ATOM   2706 C CD1   . PHE A 1 349 ? 31.900 7.541   -15.626 1.00 47.23  ? 349 PHE A CD1   1 
ATOM   2707 C CD2   . PHE A 1 349 ? 30.852 9.630   -15.182 1.00 44.18  ? 349 PHE A CD2   1 
ATOM   2708 C CE1   . PHE A 1 349 ? 31.849 7.805   -16.984 1.00 47.58  ? 349 PHE A CE1   1 
ATOM   2709 C CE2   . PHE A 1 349 ? 30.786 9.883   -16.543 1.00 45.07  ? 349 PHE A CE2   1 
ATOM   2710 C CZ    . PHE A 1 349 ? 31.286 8.971   -17.440 1.00 44.25  ? 349 PHE A CZ    1 
ATOM   2711 N N     . PRO A 1 350 ? 31.098 5.802   -11.111 1.00 35.12  ? 350 PRO A N     1 
ATOM   2712 C CA    . PRO A 1 350 ? 31.160 5.222   -9.767  1.00 35.66  ? 350 PRO A CA    1 
ATOM   2713 C C     . PRO A 1 350 ? 31.310 6.249   -8.643  1.00 34.28  ? 350 PRO A C     1 
ATOM   2714 O O     . PRO A 1 350 ? 30.639 6.140   -7.625  1.00 37.30  ? 350 PRO A O     1 
ATOM   2715 C CB    . PRO A 1 350 ? 32.408 4.322   -9.840  1.00 35.49  ? 350 PRO A CB    1 
ATOM   2716 C CG    . PRO A 1 350 ? 32.459 3.907   -11.295 1.00 33.33  ? 350 PRO A CG    1 
ATOM   2717 C CD    . PRO A 1 350 ? 32.005 5.136   -12.049 1.00 31.68  ? 350 PRO A CD    1 
ATOM   2718 N N     . GLU A 1 351 ? 32.178 7.250   -8.831  1.00 34.07  ? 351 GLU A N     1 
ATOM   2719 C CA    . GLU A 1 351 ? 32.462 8.218   -7.776  1.00 35.43  ? 351 GLU A CA    1 
ATOM   2720 C C     . GLU A 1 351 ? 31.212 9.040   -7.442  1.00 36.12  ? 351 GLU A C     1 
ATOM   2721 O O     . GLU A 1 351 ? 31.181 9.663   -6.389  1.00 41.81  ? 351 GLU A O     1 
ATOM   2722 C CB    . GLU A 1 351 ? 33.705 9.074   -8.088  1.00 33.71  ? 351 GLU A CB    1 
ATOM   2723 C CG    . GLU A 1 351 ? 33.613 9.984   -9.301  1.00 38.02  ? 351 GLU A CG    1 
ATOM   2724 C CD    . GLU A 1 351 ? 33.996 9.395   -10.656 1.00 45.64  ? 351 GLU A CD    1 
ATOM   2725 O OE1   . GLU A 1 351 ? 34.197 8.138   -10.748 1.00 42.39  ? 351 GLU A OE1   1 
ATOM   2726 O OE2   . GLU A 1 351 ? 34.092 10.200  -11.634 1.00 42.47  ? 351 GLU A OE2   1 
ATOM   2727 N N     . ASP A 1 352 ? 30.165 8.984   -8.286  1.00 37.57  ? 352 ASP A N     1 
ATOM   2728 C CA    . ASP A 1 352 ? 28.937 9.750   -8.099  1.00 38.18  ? 352 ASP A CA    1 
ATOM   2729 C C     . ASP A 1 352 ? 27.881 8.965   -7.306  1.00 37.44  ? 352 ASP A C     1 
ATOM   2730 O O     . ASP A 1 352 ? 26.844 9.519   -6.965  1.00 42.86  ? 352 ASP A O     1 
ATOM   2731 C CB    . ASP A 1 352 ? 28.363 10.200  -9.456  1.00 36.70  ? 352 ASP A CB    1 
ATOM   2732 C CG    . ASP A 1 352 ? 29.336 11.012  -10.303 1.00 37.46  ? 352 ASP A CG    1 
ATOM   2733 O OD1   . ASP A 1 352 ? 29.895 11.994  -9.765  1.00 40.36  ? 352 ASP A OD1   1 
ATOM   2734 O OD2   . ASP A 1 352 ? 29.533 10.667  -11.494 1.00 33.77  ? 352 ASP A OD2   1 
ATOM   2735 N N     . ARG A 1 353 ? 28.110 7.678   -7.024  1.00 37.52  ? 353 ARG A N     1 
ATOM   2736 C CA    . ARG A 1 353 ? 27.075 6.826   -6.458  1.00 41.50  ? 353 ARG A CA    1 
ATOM   2737 C C     . ARG A 1 353 ? 27.187 6.791   -4.935  1.00 49.94  ? 353 ARG A C     1 
ATOM   2738 O O     . ARG A 1 353 ? 28.204 6.326   -4.422  1.00 39.15  ? 353 ARG A O     1 
ATOM   2739 C CB    . ARG A 1 353 ? 27.197 5.396   -6.987  1.00 37.43  ? 353 ARG A CB    1 
ATOM   2740 C CG    . ARG A 1 353 ? 27.042 5.287   -8.496  1.00 38.01  ? 353 ARG A CG    1 
ATOM   2741 C CD    . ARG A 1 353 ? 25.674 5.731   -8.985  1.00 35.92  ? 353 ARG A CD    1 
ATOM   2742 N NE    . ARG A 1 353 ? 24.636 4.800   -8.570  1.00 31.89  ? 353 ARG A NE    1 
ATOM   2743 C CZ    . ARG A 1 353 ? 23.336 5.000   -8.710  1.00 30.27  ? 353 ARG A CZ    1 
ATOM   2744 N NH1   . ARG A 1 353 ? 22.901 6.084   -9.325  1.00 30.19  ? 353 ARG A NH1   1 
ATOM   2745 N NH2   . ARG A 1 353 ? 22.474 4.111   -8.238  1.00 28.29  ? 353 ARG A NH2   1 
ATOM   2746 N N     . ARG A 1 354 ? 26.120 7.236   -4.236  1.00 57.55  ? 354 ARG A N     1 
ATOM   2747 C CA    . ARG A 1 354 ? 26.187 7.442   -2.793  1.00 65.33  ? 354 ARG A CA    1 
ATOM   2748 C C     . ARG A 1 354 ? 26.096 6.091   -2.076  1.00 60.26  ? 354 ARG A C     1 
ATOM   2749 O O     . ARG A 1 354 ? 26.862 5.868   -1.142  1.00 52.71  ? 354 ARG A O     1 
ATOM   2750 C CB    . ARG A 1 354 ? 25.216 8.533   -2.287  1.00 72.01  ? 354 ARG A CB    1 
ATOM   2751 C CG    . ARG A 1 354 ? 23.721 8.330   -2.530  1.00 87.81  ? 354 ARG A CG    1 
ATOM   2752 C CD    . ARG A 1 354 ? 22.845 9.350   -1.784  1.00 93.81  ? 354 ARG A CD    1 
ATOM   2753 N NE    . ARG A 1 354 ? 21.436 9.474   -2.196  1.00 86.74  ? 354 ARG A NE    1 
ATOM   2754 C CZ    . ARG A 1 354 ? 20.395 8.903   -1.583  1.00 94.16  ? 354 ARG A CZ    1 
ATOM   2755 N NH1   . ARG A 1 354 ? 20.586 7.981   -0.655  1.00 103.41 ? 354 ARG A NH1   1 
ATOM   2756 N NH2   . ARG A 1 354 ? 19.156 9.209   -1.938  1.00 87.34  ? 354 ARG A NH2   1 
ATOM   2757 N N     . HIS A 1 355 ? 25.238 5.175   -2.558  1.00 60.57  ? 355 HIS A N     1 
ATOM   2758 C CA    . HIS A 1 355 ? 25.085 3.847   -1.963  1.00 66.20  ? 355 HIS A CA    1 
ATOM   2759 C C     . HIS A 1 355 ? 26.413 3.067   -2.008  1.00 73.56  ? 355 HIS A C     1 
ATOM   2760 O O     . HIS A 1 355 ? 27.207 3.216   -2.943  1.00 68.19  ? 355 HIS A O     1 
ATOM   2761 C CB    . HIS A 1 355 ? 23.898 3.100   -2.602  1.00 62.12  ? 355 HIS A CB    1 
ATOM   2762 C CG    . HIS A 1 355 ? 22.584 3.798   -2.436  1.00 63.72  ? 355 HIS A CG    1 
ATOM   2763 N ND1   . HIS A 1 355 ? 21.709 3.513   -1.408  1.00 63.28  ? 355 HIS A ND1   1 
ATOM   2764 C CD2   . HIS A 1 355 ? 22.015 4.800   -3.130  1.00 71.51  ? 355 HIS A CD2   1 
ATOM   2765 C CE1   . HIS A 1 355 ? 20.650 4.305   -1.489  1.00 67.24  ? 355 HIS A CE1   1 
ATOM   2766 N NE2   . HIS A 1 355 ? 20.810 5.094   -2.536  1.00 69.36  ? 355 HIS A NE2   1 
ATOM   2767 N N     . LYS A 1 356 ? 26.662 2.239   -0.977  1.00 72.13  ? 356 LYS A N     1 
ATOM   2768 C CA    . LYS A 1 356 ? 27.924 1.515   -0.845  1.00 75.85  ? 356 LYS A CA    1 
ATOM   2769 C C     . LYS A 1 356 ? 27.801 0.119   -1.461  1.00 69.97  ? 356 LYS A C     1 
ATOM   2770 O O     . LYS A 1 356 ? 28.777 -0.398  -2.009  1.00 58.62  ? 356 LYS A O     1 
ATOM   2771 C CB    . LYS A 1 356 ? 28.361 1.467   0.624   1.00 82.15  ? 356 LYS A CB    1 
ATOM   2772 C CG    . LYS A 1 356 ? 28.970 2.766   1.146   1.00 89.19  ? 356 LYS A CG    1 
ATOM   2773 C CD    . LYS A 1 356 ? 29.363 2.718   2.607   1.00 91.01  ? 356 LYS A CD    1 
ATOM   2774 C CE    . LYS A 1 356 ? 30.039 3.987   3.087   1.00 94.20  ? 356 LYS A CE    1 
ATOM   2775 N NZ    . LYS A 1 356 ? 30.395 3.917   4.527   1.00 93.83  ? 356 LYS A NZ    1 
ATOM   2776 N N     . VAL A 1 357 ? 26.612 -0.490  -1.307  1.00 66.34  ? 357 VAL A N     1 
ATOM   2777 C CA    . VAL A 1 357 ? 26.162 -1.595  -2.141  1.00 62.40  ? 357 VAL A CA    1 
ATOM   2778 C C     . VAL A 1 357 ? 25.249 -0.987  -3.196  1.00 60.93  ? 357 VAL A C     1 
ATOM   2779 O O     . VAL A 1 357 ? 24.159 -0.501  -2.884  1.00 52.70  ? 357 VAL A O     1 
ATOM   2780 C CB    . VAL A 1 357 ? 25.425 -2.699  -1.353  1.00 66.15  ? 357 VAL A CB    1 
ATOM   2781 C CG1   . VAL A 1 357 ? 25.322 -3.987  -2.167  1.00 65.95  ? 357 VAL A CG1   1 
ATOM   2782 C CG2   . VAL A 1 357 ? 26.074 -2.966  -0.002  1.00 68.89  ? 357 VAL A CG2   1 
ATOM   2783 N N     . ASP A 1 358 ? 25.723 -0.990  -4.445  1.00 57.71  ? 358 ASP A N     1 
ATOM   2784 C CA    . ASP A 1 358 ? 25.090 -0.183  -5.468  1.00 48.85  ? 358 ASP A CA    1 
ATOM   2785 C C     . ASP A 1 358 ? 25.165 -0.882  -6.821  1.00 48.00  ? 358 ASP A C     1 
ATOM   2786 O O     . ASP A 1 358 ? 26.158 -1.527  -7.164  1.00 42.92  ? 358 ASP A O     1 
ATOM   2787 C CB    . ASP A 1 358 ? 25.749 1.192   -5.515  1.00 47.89  ? 358 ASP A CB    1 
ATOM   2788 C CG    . ASP A 1 358 ? 25.161 2.086   -6.588  1.00 43.29  ? 358 ASP A CG    1 
ATOM   2789 O OD1   . ASP A 1 358 ? 24.041 2.622   -6.375  1.00 38.34  ? 358 ASP A OD1   1 
ATOM   2790 O OD2   . ASP A 1 358 ? 25.824 2.214   -7.635  1.00 41.35  ? 358 ASP A OD2   1 
ATOM   2791 N N     . LEU A 1 359 ? 24.103 -0.694  -7.603  1.00 46.36  ? 359 LEU A N     1 
ATOM   2792 C CA    . LEU A 1 359 ? 23.994 -1.321  -8.906  1.00 45.82  ? 359 LEU A CA    1 
ATOM   2793 C C     . LEU A 1 359 ? 25.256 -1.061  -9.728  1.00 43.20  ? 359 LEU A C     1 
ATOM   2794 O O     . LEU A 1 359 ? 25.838 -1.993  -10.278 1.00 39.27  ? 359 LEU A O     1 
ATOM   2795 C CB    . LEU A 1 359 ? 22.760 -0.779  -9.628  1.00 43.97  ? 359 LEU A CB    1 
ATOM   2796 C CG    . LEU A 1 359 ? 22.589 -1.334  -11.034 1.00 50.37  ? 359 LEU A CG    1 
ATOM   2797 C CD1   . LEU A 1 359 ? 21.920 -2.698  -10.981 1.00 55.08  ? 359 LEU A CD1   1 
ATOM   2798 C CD2   . LEU A 1 359 ? 21.832 -0.361  -11.922 1.00 51.51  ? 359 LEU A CD2   1 
ATOM   2799 N N     . LEU A 1 360 ? 25.665 0.209   -9.827  1.00 42.75  ? 360 LEU A N     1 
ATOM   2800 C CA    . LEU A 1 360 ? 26.698 0.579   -10.780 1.00 39.81  ? 360 LEU A CA    1 
ATOM   2801 C C     . LEU A 1 360 ? 28.039 0.003   -10.341 1.00 40.33  ? 360 LEU A C     1 
ATOM   2802 O O     . LEU A 1 360 ? 28.869 -0.333  -11.175 1.00 39.94  ? 360 LEU A O     1 
ATOM   2803 C CB    . LEU A 1 360 ? 26.787 2.098   -10.931 1.00 36.61  ? 360 LEU A CB    1 
ATOM   2804 C CG    . LEU A 1 360 ? 27.980 2.565   -11.770 1.00 37.94  ? 360 LEU A CG    1 
ATOM   2805 C CD1   . LEU A 1 360 ? 27.958 1.919   -13.164 1.00 37.17  ? 360 LEU A CD1   1 
ATOM   2806 C CD2   . LEU A 1 360 ? 28.022 4.080   -11.882 1.00 35.46  ? 360 LEU A CD2   1 
ATOM   2807 N N     . LEU A 1 361 ? 28.240 -0.129  -9.029  1.00 39.78  ? 361 LEU A N     1 
ATOM   2808 C CA    . LEU A 1 361 ? 29.475 -0.693  -8.531  1.00 37.60  ? 361 LEU A CA    1 
ATOM   2809 C C     . LEU A 1 361 ? 29.505 -2.200  -8.821  1.00 35.11  ? 361 LEU A C     1 
ATOM   2810 O O     . LEU A 1 361 ? 30.571 -2.732  -9.139  1.00 33.46  ? 361 LEU A O     1 
ATOM   2811 C CB    . LEU A 1 361 ? 29.607 -0.316  -7.051  1.00 39.79  ? 361 LEU A CB    1 
ATOM   2812 C CG    . LEU A 1 361 ? 29.492 1.189   -6.765  1.00 45.82  ? 361 LEU A CG    1 
ATOM   2813 C CD1   . LEU A 1 361 ? 29.713 1.491   -5.283  1.00 46.52  ? 361 LEU A CD1   1 
ATOM   2814 C CD2   . LEU A 1 361 ? 30.454 2.006   -7.625  1.00 40.75  ? 361 LEU A CD2   1 
ATOM   2815 N N     . HIS A 1 362 ? 28.348 -2.879  -8.782  1.00 32.89  ? 362 HIS A N     1 
ATOM   2816 C CA    . HIS A 1 362 ? 28.289 -4.281  -9.184  1.00 37.94  ? 362 HIS A CA    1 
ATOM   2817 C C     . HIS A 1 362 ? 28.530 -4.390  -10.689 1.00 36.92  ? 362 HIS A C     1 
ATOM   2818 O O     . HIS A 1 362 ? 29.423 -5.104  -11.129 1.00 34.95  ? 362 HIS A O     1 
ATOM   2819 C CB    . HIS A 1 362 ? 26.979 -4.979  -8.786  1.00 40.78  ? 362 HIS A CB    1 
ATOM   2820 C CG    . HIS A 1 362 ? 26.659 -6.217  -9.593  1.00 54.11  ? 362 HIS A CG    1 
ATOM   2821 N ND1   . HIS A 1 362 ? 27.557 -7.241  -9.854  1.00 58.35  ? 362 HIS A ND1   1 
ATOM   2822 C CD2   . HIS A 1 362 ? 25.507 -6.565  -10.228 1.00 56.93  ? 362 HIS A CD2   1 
ATOM   2823 C CE1   . HIS A 1 362 ? 26.958 -8.167  -10.600 1.00 63.43  ? 362 HIS A CE1   1 
ATOM   2824 N NE2   . HIS A 1 362 ? 25.709 -7.784  -10.833 1.00 58.69  ? 362 HIS A NE2   1 
ATOM   2825 N N     . ARG A 1 363 ? 27.734 -3.661  -11.469 1.00 35.45  ? 363 ARG A N     1 
ATOM   2826 C CA    . ARG A 1 363 ? 27.807 -3.745  -12.914 1.00 38.33  ? 363 ARG A CA    1 
ATOM   2827 C C     . ARG A 1 363 ? 29.184 -3.293  -13.409 1.00 34.66  ? 363 ARG A C     1 
ATOM   2828 O O     . ARG A 1 363 ? 29.626 -3.805  -14.431 1.00 33.72  ? 363 ARG A O     1 
ATOM   2829 C CB    . ARG A 1 363 ? 26.608 -3.020  -13.542 1.00 41.76  ? 363 ARG A CB    1 
ATOM   2830 C CG    . ARG A 1 363 ? 25.280 -3.676  -13.186 1.00 43.97  ? 363 ARG A CG    1 
ATOM   2831 C CD    . ARG A 1 363 ? 24.353 -3.946  -14.354 1.00 53.69  ? 363 ARG A CD    1 
ATOM   2832 N NE    . ARG A 1 363 ? 24.946 -4.658  -15.499 1.00 65.75  ? 363 ARG A NE    1 
ATOM   2833 C CZ    . ARG A 1 363 ? 25.110 -5.984  -15.607 1.00 68.67  ? 363 ARG A CZ    1 
ATOM   2834 N NH1   . ARG A 1 363 ? 24.924 -6.781  -14.565 1.00 66.68  ? 363 ARG A NH1   1 
ATOM   2835 N NH2   . ARG A 1 363 ? 25.486 -6.510  -16.764 1.00 65.67  ? 363 ARG A NH2   1 
ATOM   2836 N N     . ALA A 1 364 ? 29.893 -2.433  -12.658 1.00 30.83  ? 364 ALA A N     1 
ATOM   2837 C CA    . ALA A 1 364 ? 31.251 -2.036  -13.018 1.00 32.92  ? 364 ALA A CA    1 
ATOM   2838 C C     . ALA A 1 364 ? 32.202 -3.230  -12.969 1.00 34.95  ? 364 ALA A C     1 
ATOM   2839 O O     . ALA A 1 364 ? 33.193 -3.281  -13.695 1.00 32.83  ? 364 ALA A O     1 
ATOM   2840 C CB    . ALA A 1 364 ? 31.779 -0.940  -12.119 1.00 30.00  ? 364 ALA A CB    1 
ATOM   2841 N N     . GLU A 1 365 ? 31.937 -4.159  -12.058 1.00 35.27  ? 365 GLU A N     1 
ATOM   2842 C CA    . GLU A 1 365 ? 32.780 -5.331  -11.944 1.00 34.74  ? 365 GLU A CA    1 
ATOM   2843 C C     . GLU A 1 365 ? 32.533 -6.220  -13.154 1.00 32.45  ? 365 GLU A C     1 
ATOM   2844 O O     . GLU A 1 365 ? 33.475 -6.735  -13.755 1.00 31.38  ? 365 GLU A O     1 
ATOM   2845 C CB    . GLU A 1 365 ? 32.504 -6.017  -10.614 1.00 37.06  ? 365 GLU A CB    1 
ATOM   2846 C CG    . GLU A 1 365 ? 32.868 -5.107  -9.466  1.00 45.49  ? 365 GLU A CG    1 
ATOM   2847 C CD    . GLU A 1 365 ? 33.526 -5.787  -8.284  1.00 59.21  ? 365 GLU A CD    1 
ATOM   2848 O OE1   . GLU A 1 365 ? 32.820 -6.556  -7.572  1.00 62.62  ? 365 GLU A OE1   1 
ATOM   2849 O OE2   . GLU A 1 365 ? 34.754 -5.570  -8.109  1.00 64.50  ? 365 GLU A OE2   1 
ATOM   2850 N N     . THR A 1 366 ? 31.256 -6.367  -13.508 1.00 29.70  ? 366 THR A N     1 
ATOM   2851 C CA    . THR A 1 366 ? 30.847 -7.262  -14.577 1.00 27.96  ? 366 THR A CA    1 
ATOM   2852 C C     . THR A 1 366 ? 31.396 -6.794  -15.920 1.00 28.62  ? 366 THR A C     1 
ATOM   2853 O O     . THR A 1 366 ? 31.813 -7.619  -16.726 1.00 31.80  ? 366 THR A O     1 
ATOM   2854 C CB    . THR A 1 366 ? 29.328 -7.335  -14.617 1.00 27.36  ? 366 THR A CB    1 
ATOM   2855 O OG1   . THR A 1 366 ? 28.995 -7.622  -13.264 1.00 30.12  ? 366 THR A OG1   1 
ATOM   2856 C CG2   . THR A 1 366 ? 28.806 -8.377  -15.570 1.00 29.72  ? 366 THR A CG2   1 
ATOM   2857 N N     . MET A 1 367 ? 31.443 -5.470  -16.114 1.00 27.91  ? 367 MET A N     1 
ATOM   2858 C CA    . MET A 1 367 ? 31.787 -4.896  -17.397 1.00 30.97  ? 367 MET A CA    1 
ATOM   2859 C C     . MET A 1 367 ? 33.303 -4.826  -17.562 1.00 30.96  ? 367 MET A C     1 
ATOM   2860 O O     . MET A 1 367 ? 33.760 -4.356  -18.596 1.00 29.52  ? 367 MET A O     1 
ATOM   2861 C CB    . MET A 1 367 ? 31.149 -3.510  -17.571 1.00 31.09  ? 367 MET A CB    1 
ATOM   2862 C CG    . MET A 1 367 ? 29.652 -3.599  -17.846 1.00 29.34  ? 367 MET A CG    1 
ATOM   2863 S SD    . MET A 1 367 ? 28.795 -2.005  -18.084 1.00 30.43  ? 367 MET A SD    1 
ATOM   2864 C CE    . MET A 1 367 ? 29.439 -1.061  -16.698 1.00 30.99  ? 367 MET A CE    1 
ATOM   2865 N N     . LYS A 1 368 ? 34.077 -5.288  -16.566 1.00 31.47  ? 368 LYS A N     1 
ATOM   2866 C CA    . LYS A 1 368 ? 35.505 -5.501  -16.786 1.00 34.37  ? 368 LYS A CA    1 
ATOM   2867 C C     . LYS A 1 368 ? 35.864 -6.965  -16.541 1.00 30.85  ? 368 LYS A C     1 
ATOM   2868 O O     . LYS A 1 368 ? 37.036 -7.294  -16.395 1.00 27.45  ? 368 LYS A O     1 
ATOM   2869 C CB    . LYS A 1 368 ? 36.398 -4.550  -15.973 1.00 36.65  ? 368 LYS A CB    1 
ATOM   2870 C CG    . LYS A 1 368 ? 36.509 -4.751  -14.465 1.00 39.58  ? 368 LYS A CG    1 
ATOM   2871 C CD    . LYS A 1 368 ? 37.731 -4.047  -13.907 1.00 41.79  ? 368 LYS A CD    1 
ATOM   2872 C CE    . LYS A 1 368 ? 37.728 -3.979  -12.397 1.00 53.68  ? 368 LYS A CE    1 
ATOM   2873 N NZ    . LYS A 1 368 ? 39.042 -3.530  -11.877 1.00 59.11  ? 368 LYS A NZ    1 
ATOM   2874 N N     . GLY A 1 369 ? 34.847 -7.829  -16.538 1.00 28.29  ? 369 GLY A N     1 
ATOM   2875 C CA    . GLY A 1 369 ? 35.068 -9.254  -16.642 1.00 29.84  ? 369 GLY A CA    1 
ATOM   2876 C C     . GLY A 1 369 ? 35.426 -9.898  -15.307 1.00 30.70  ? 369 GLY A C     1 
ATOM   2877 O O     . GLY A 1 369 ? 36.209 -10.845 -15.286 1.00 29.82  ? 369 GLY A O     1 
ATOM   2878 N N     . VAL A 1 370 ? 34.807 -9.414  -14.222 1.00 31.99  ? 370 VAL A N     1 
ATOM   2879 C CA    . VAL A 1 370 ? 35.033 -9.952  -12.892 1.00 31.08  ? 370 VAL A CA    1 
ATOM   2880 C C     . VAL A 1 370 ? 33.863 -10.877 -12.541 1.00 29.75  ? 370 VAL A C     1 
ATOM   2881 O O     . VAL A 1 370 ? 32.733 -10.435 -12.396 1.00 27.82  ? 370 VAL A O     1 
ATOM   2882 C CB    . VAL A 1 370 ? 35.227 -8.830  -11.850 1.00 31.37  ? 370 VAL A CB    1 
ATOM   2883 C CG1   . VAL A 1 370 ? 35.541 -9.389  -10.466 1.00 29.48  ? 370 VAL A CG1   1 
ATOM   2884 C CG2   . VAL A 1 370 ? 36.312 -7.841  -12.269 1.00 31.87  ? 370 VAL A CG2   1 
ATOM   2885 N N     . PRO A 1 371 ? 34.096 -12.198 -12.383 1.00 29.82  ? 371 PRO A N     1 
ATOM   2886 C CA    . PRO A 1 371 ? 33.012 -13.138 -12.085 1.00 29.72  ? 371 PRO A CA    1 
ATOM   2887 C C     . PRO A 1 371 ? 32.477 -12.946 -10.667 1.00 29.47  ? 371 PRO A C     1 
ATOM   2888 O O     . PRO A 1 371 ? 33.265 -12.813 -9.737  1.00 30.15  ? 371 PRO A O     1 
ATOM   2889 C CB    . PRO A 1 371 ? 33.684 -14.521 -12.217 1.00 27.49  ? 371 PRO A CB    1 
ATOM   2890 C CG    . PRO A 1 371 ? 35.141 -14.251 -11.881 1.00 27.04  ? 371 PRO A CG    1 
ATOM   2891 C CD    . PRO A 1 371 ? 35.423 -12.852 -12.401 1.00 26.92  ? 371 PRO A CD    1 
ATOM   2892 N N     . LYS A 1 372 ? 31.144 -12.958 -10.533 1.00 31.87  ? 372 LYS A N     1 
ATOM   2893 C CA    . LYS A 1 372 ? 30.437 -12.730 -9.283  1.00 34.85  ? 372 LYS A CA    1 
ATOM   2894 C C     . LYS A 1 372 ? 29.174 -13.596 -9.245  1.00 34.91  ? 372 LYS A C     1 
ATOM   2895 O O     . LYS A 1 372 ? 28.826 -14.229 -10.245 1.00 32.47  ? 372 LYS A O     1 
ATOM   2896 C CB    . LYS A 1 372 ? 30.109 -11.240 -9.147  1.00 42.96  ? 372 LYS A CB    1 
ATOM   2897 C CG    . LYS A 1 372 ? 31.267 -10.325 -8.753  1.00 47.84  ? 372 LYS A CG    1 
ATOM   2898 C CD    . LYS A 1 372 ? 31.756 -10.538 -7.326  1.00 54.83  ? 372 LYS A CD    1 
ATOM   2899 C CE    . LYS A 1 372 ? 32.719 -9.469  -6.840  1.00 62.48  ? 372 LYS A CE    1 
ATOM   2900 N NZ    . LYS A 1 372 ? 33.507 -9.920  -5.665  1.00 61.79  ? 372 LYS A NZ    1 
ATOM   2901 N N     . LEU A 1 373 ? 28.518 -13.658 -8.069  1.00 34.98  ? 373 LEU A N     1 
ATOM   2902 C CA    . LEU A 1 373 ? 27.260 -14.382 -7.910  1.00 37.48  ? 373 LEU A CA    1 
ATOM   2903 C C     . LEU A 1 373 ? 26.142 -13.438 -7.473  1.00 36.53  ? 373 LEU A C     1 
ATOM   2904 O O     . LEU A 1 373 ? 25.064 -13.904 -7.114  1.00 38.90  ? 373 LEU A O     1 
ATOM   2905 C CB    . LEU A 1 373 ? 27.432 -15.525 -6.898  1.00 36.82  ? 373 LEU A CB    1 
ATOM   2906 C CG    . LEU A 1 373 ? 28.403 -16.628 -7.322  1.00 39.89  ? 373 LEU A CG    1 
ATOM   2907 C CD1   . LEU A 1 373 ? 28.641 -17.639 -6.216  1.00 39.58  ? 373 LEU A CD1   1 
ATOM   2908 C CD2   . LEU A 1 373 ? 27.900 -17.338 -8.564  1.00 40.05  ? 373 LEU A CD2   1 
ATOM   2909 N N     . THR A 1 374 ? 26.419 -12.132 -7.525  1.00 34.92  ? 374 THR A N     1 
ATOM   2910 C CA    . THR A 1 374 ? 25.555 -11.069 -7.053  1.00 33.91  ? 374 THR A CA    1 
ATOM   2911 C C     . THR A 1 374 ? 24.193 -11.127 -7.749  1.00 40.09  ? 374 THR A C     1 
ATOM   2912 O O     . THR A 1 374 ? 23.136 -10.960 -7.129  1.00 40.52  ? 374 THR A O     1 
ATOM   2913 C CB    . THR A 1 374 ? 26.201 -9.706  -7.346  1.00 37.29  ? 374 THR A CB    1 
ATOM   2914 O OG1   . THR A 1 374 ? 27.599 -9.773  -7.074  1.00 38.55  ? 374 THR A OG1   1 
ATOM   2915 C CG2   . THR A 1 374 ? 25.609 -8.562  -6.552  1.00 41.78  ? 374 THR A CG2   1 
ATOM   2916 N N     . GLU A 1 375 ? 24.215 -11.360 -9.062  1.00 38.75  ? 375 GLU A N     1 
ATOM   2917 C CA    . GLU A 1 375 ? 23.009 -11.228 -9.857  1.00 36.78  ? 375 GLU A CA    1 
ATOM   2918 C C     . GLU A 1 375 ? 21.904 -12.120 -9.287  1.00 36.14  ? 375 GLU A C     1 
ATOM   2919 O O     . GLU A 1 375 ? 20.730 -11.769 -9.375  1.00 35.06  ? 375 GLU A O     1 
ATOM   2920 C CB    . GLU A 1 375 ? 23.322 -11.510 -11.330 1.00 38.37  ? 375 GLU A CB    1 
ATOM   2921 C CG    . GLU A 1 375 ? 22.234 -11.058 -12.281 1.00 39.41  ? 375 GLU A CG    1 
ATOM   2922 C CD    . GLU A 1 375 ? 22.093 -9.558  -12.495 1.00 39.71  ? 375 GLU A CD    1 
ATOM   2923 O OE1   . GLU A 1 375 ? 23.026 -8.793  -12.141 1.00 38.58  ? 375 GLU A OE1   1 
ATOM   2924 O OE2   . GLU A 1 375 ? 21.031 -9.163  -13.043 1.00 51.32  ? 375 GLU A OE2   1 
ATOM   2925 N N     . PHE A 1 376 ? 22.258 -13.243 -8.653  1.00 36.25  ? 376 PHE A N     1 
ATOM   2926 C CA    . PHE A 1 376 ? 21.251 -14.092 -8.024  1.00 38.07  ? 376 PHE A CA    1 
ATOM   2927 C C     . PHE A 1 376 ? 20.378 -13.355 -6.998  1.00 37.84  ? 376 PHE A C     1 
ATOM   2928 O O     . PHE A 1 376 ? 19.287 -13.826 -6.696  1.00 43.41  ? 376 PHE A O     1 
ATOM   2929 C CB    . PHE A 1 376 ? 21.907 -15.324 -7.402  1.00 38.83  ? 376 PHE A CB    1 
ATOM   2930 C CG    . PHE A 1 376 ? 22.087 -16.435 -8.400  1.00 45.35  ? 376 PHE A CG    1 
ATOM   2931 C CD1   . PHE A 1 376 ? 20.988 -17.113 -8.904  1.00 45.96  ? 376 PHE A CD1   1 
ATOM   2932 C CD2   . PHE A 1 376 ? 23.343 -16.766 -8.883  1.00 53.58  ? 376 PHE A CD2   1 
ATOM   2933 C CE1   . PHE A 1 376 ? 21.138 -18.114 -9.854  1.00 47.94  ? 376 PHE A CE1   1 
ATOM   2934 C CE2   . PHE A 1 376 ? 23.490 -17.776 -9.825  1.00 57.94  ? 376 PHE A CE2   1 
ATOM   2935 C CZ    . PHE A 1 376 ? 22.388 -18.452 -10.307 1.00 50.71  ? 376 PHE A CZ    1 
ATOM   2936 N N     . ASN A 1 377 ? 20.833 -12.207 -6.477  1.00 37.35  ? 377 ASN A N     1 
ATOM   2937 C CA    . ASN A 1 377 ? 20.083 -11.409 -5.517  1.00 35.31  ? 377 ASN A CA    1 
ATOM   2938 C C     . ASN A 1 377 ? 18.657 -11.111 -5.984  1.00 35.56  ? 377 ASN A C     1 
ATOM   2939 O O     . ASN A 1 377 ? 17.743 -11.086 -5.154  1.00 35.76  ? 377 ASN A O     1 
ATOM   2940 C CB    . ASN A 1 377 ? 20.785 -10.085 -5.216  1.00 36.40  ? 377 ASN A CB    1 
ATOM   2941 C CG    . ASN A 1 377 ? 22.060 -10.255 -4.410  1.00 39.21  ? 377 ASN A CG    1 
ATOM   2942 O OD1   . ASN A 1 377 ? 22.328 -11.336 -3.896  1.00 38.59  ? 377 ASN A OD1   1 
ATOM   2943 N ND2   . ASN A 1 377 ? 22.856 -9.202  -4.298  1.00 39.53  ? 377 ASN A ND2   1 
ATOM   2944 N N     . PHE A 1 378 ? 18.436 -10.885 -7.288  1.00 30.39  ? 378 PHE A N     1 
ATOM   2945 C CA    . PHE A 1 378 ? 17.098 -10.515 -7.722  1.00 33.13  ? 378 PHE A CA    1 
ATOM   2946 C C     . PHE A 1 378 ? 16.078 -11.639 -7.493  1.00 33.58  ? 378 PHE A C     1 
ATOM   2947 O O     . PHE A 1 378 ? 14.882 -11.371 -7.490  1.00 33.74  ? 378 PHE A O     1 
ATOM   2948 C CB    . PHE A 1 378 ? 17.094 -9.970  -9.152  1.00 36.10  ? 378 PHE A CB    1 
ATOM   2949 C CG    . PHE A 1 378 ? 17.285 -10.954 -10.279 1.00 37.14  ? 378 PHE A CG    1 
ATOM   2950 C CD1   . PHE A 1 378 ? 16.362 -11.962 -10.515 1.00 40.63  ? 378 PHE A CD1   1 
ATOM   2951 C CD2   . PHE A 1 378 ? 18.338 -10.800 -11.174 1.00 38.13  ? 378 PHE A CD2   1 
ATOM   2952 C CE1   . PHE A 1 378 ? 16.535 -12.847 -11.567 1.00 39.21  ? 378 PHE A CE1   1 
ATOM   2953 C CE2   . PHE A 1 378 ? 18.498 -11.680 -12.237 1.00 38.04  ? 378 PHE A CE2   1 
ATOM   2954 C CZ    . PHE A 1 378 ? 17.605 -12.706 -12.421 1.00 36.23  ? 378 PHE A CZ    1 
ATOM   2955 N N     . LEU A 1 379 ? 16.515 -12.876 -7.229  1.00 33.16  ? 379 LEU A N     1 
ATOM   2956 C CA    . LEU A 1 379 ? 15.606 -13.965 -6.887  1.00 33.70  ? 379 LEU A CA    1 
ATOM   2957 C C     . LEU A 1 379 ? 14.964 -13.790 -5.509  1.00 35.55  ? 379 LEU A C     1 
ATOM   2958 O O     . LEU A 1 379 ? 13.966 -14.451 -5.211  1.00 43.20  ? 379 LEU A O     1 
ATOM   2959 C CB    . LEU A 1 379 ? 16.386 -15.284 -6.937  1.00 35.90  ? 379 LEU A CB    1 
ATOM   2960 C CG    . LEU A 1 379 ? 16.849 -15.712 -8.329  1.00 37.83  ? 379 LEU A CG    1 
ATOM   2961 C CD1   . LEU A 1 379 ? 17.433 -17.122 -8.308  1.00 39.23  ? 379 LEU A CD1   1 
ATOM   2962 C CD2   . LEU A 1 379 ? 15.701 -15.634 -9.322  1.00 37.68  ? 379 LEU A CD2   1 
ATOM   2963 N N     . ASN A 1 380 ? 15.519 -12.907 -4.665  1.00 35.23  ? 380 ASN A N     1 
ATOM   2964 C CA    . ASN A 1 380 ? 14.953 -12.627 -3.355  1.00 34.83  ? 380 ASN A CA    1 
ATOM   2965 C C     . ASN A 1 380 ? 13.918 -11.499 -3.393  1.00 33.47  ? 380 ASN A C     1 
ATOM   2966 O O     . ASN A 1 380 ? 13.500 -11.030 -2.339  1.00 34.71  ? 380 ASN A O     1 
ATOM   2967 C CB    . ASN A 1 380 ? 16.049 -12.280 -2.346  1.00 40.94  ? 380 ASN A CB    1 
ATOM   2968 C CG    . ASN A 1 380 ? 16.975 -13.446 -2.074  1.00 49.46  ? 380 ASN A CG    1 
ATOM   2969 O OD1   . ASN A 1 380 ? 16.535 -14.593 -1.976  1.00 63.01  ? 380 ASN A OD1   1 
ATOM   2970 N ND2   . ASN A 1 380 ? 18.261 -13.165 -1.963  1.00 51.16  ? 380 ASN A ND2   1 
ATOM   2971 N N     . TRP A 1 381 ? 13.474 -11.075 -4.583  1.00 32.76  ? 381 TRP A N     1 
ATOM   2972 C CA    . TRP A 1 381 ? 12.605 -9.913  -4.688  1.00 32.17  ? 381 TRP A CA    1 
ATOM   2973 C C     . TRP A 1 381 ? 11.339 -10.104 -3.852  1.00 34.47  ? 381 TRP A C     1 
ATOM   2974 O O     . TRP A 1 381 ? 10.961 -9.205  -3.092  1.00 34.25  ? 381 TRP A O     1 
ATOM   2975 C CB    . TRP A 1 381 ? 12.253 -9.630  -6.146  1.00 29.46  ? 381 TRP A CB    1 
ATOM   2976 C CG    . TRP A 1 381 ? 11.285 -8.507  -6.338  1.00 27.71  ? 381 TRP A CG    1 
ATOM   2977 C CD1   . TRP A 1 381 ? 10.038 -8.578  -6.885  1.00 29.95  ? 381 TRP A CD1   1 
ATOM   2978 C CD2   . TRP A 1 381 ? 11.474 -7.138  -5.961  1.00 25.72  ? 381 TRP A CD2   1 
ATOM   2979 N NE1   . TRP A 1 381 ? 9.439  -7.349  -6.876  1.00 29.93  ? 381 TRP A NE1   1 
ATOM   2980 C CE2   . TRP A 1 381 ? 10.307 -6.445  -6.320  1.00 28.66  ? 381 TRP A CE2   1 
ATOM   2981 C CE3   . TRP A 1 381 ? 12.508 -6.441  -5.343  1.00 27.04  ? 381 TRP A CE3   1 
ATOM   2982 C CZ2   . TRP A 1 381 ? 10.154 -5.084  -6.088  1.00 29.21  ? 381 TRP A CZ2   1 
ATOM   2983 C CZ3   . TRP A 1 381 ? 12.363 -5.096  -5.126  1.00 27.54  ? 381 TRP A CZ3   1 
ATOM   2984 C CH2   . TRP A 1 381 ? 11.202 -4.429  -5.493  1.00 28.88  ? 381 TRP A CH2   1 
ATOM   2985 N N     . ASP A 1 382 ? 10.721 -11.283 -4.004  1.00 34.34  ? 382 ASP A N     1 
ATOM   2986 C CA    . ASP A 1 382 ? 9.449  -11.614 -3.393  1.00 38.04  ? 382 ASP A CA    1 
ATOM   2987 C C     . ASP A 1 382 ? 9.599  -12.785 -2.415  1.00 36.42  ? 382 ASP A C     1 
ATOM   2988 O O     . ASP A 1 382 ? 8.743  -13.661 -2.369  1.00 39.15  ? 382 ASP A O     1 
ATOM   2989 C CB    . ASP A 1 382 ? 8.422  -11.936 -4.484  1.00 44.29  ? 382 ASP A CB    1 
ATOM   2990 C CG    . ASP A 1 382 ? 6.968  -11.812 -4.043  1.00 53.85  ? 382 ASP A CG    1 
ATOM   2991 O OD1   . ASP A 1 382 ? 6.696  -11.251 -2.930  1.00 49.53  ? 382 ASP A OD1   1 
ATOM   2992 O OD2   . ASP A 1 382 ? 6.107  -12.284 -4.807  1.00 57.64  ? 382 ASP A OD2   1 
ATOM   2993 N N     . GLY A 1 383 ? 10.685 -12.810 -1.638  1.00 36.37  ? 383 GLY A N     1 
ATOM   2994 C CA    . GLY A 1 383 ? 10.830 -13.770 -0.548  1.00 43.95  ? 383 GLY A CA    1 
ATOM   2995 C C     . GLY A 1 383 ? 11.760 -14.939 -0.883  1.00 48.42  ? 383 GLY A C     1 
ATOM   2996 O O     . GLY A 1 383 ? 12.463 -15.449 -0.006  1.00 46.13  ? 383 GLY A O     1 
ATOM   2997 N N     . GLY A 1 384 ? 11.746 -15.344 -2.163  1.00 50.28  ? 384 GLY A N     1 
ATOM   2998 C CA    . GLY A 1 384 ? 12.706 -16.281 -2.723  1.00 46.18  ? 384 GLY A CA    1 
ATOM   2999 C C     . GLY A 1 384 ? 12.047 -17.057 -3.855  1.00 44.76  ? 384 GLY A C     1 
ATOM   3000 O O     . GLY A 1 384 ? 10.870 -17.388 -3.765  1.00 42.65  ? 384 GLY A O     1 
ATOM   3001 N N     . GLY A 1 385 ? 12.793 -17.305 -4.931  1.00 40.38  ? 385 GLY A N     1 
ATOM   3002 C CA    . GLY A 1 385 ? 12.247 -18.036 -6.053  1.00 40.00  ? 385 GLY A CA    1 
ATOM   3003 C C     . GLY A 1 385 ? 13.304 -18.379 -7.094  1.00 42.50  ? 385 GLY A C     1 
ATOM   3004 O O     . GLY A 1 385 ? 14.459 -17.988 -6.970  1.00 42.66  ? 385 GLY A O     1 
ATOM   3005 N N     . GLY A 1 386 ? 12.872 -19.119 -8.122  1.00 45.69  ? 386 GLY A N     1 
ATOM   3006 C CA    . GLY A 1 386 ? 13.640 -19.292 -9.344  1.00 43.71  ? 386 GLY A CA    1 
ATOM   3007 C C     . GLY A 1 386 ? 13.213 -18.290 -10.420 1.00 40.96  ? 386 GLY A C     1 
ATOM   3008 O O     . GLY A 1 386 ? 12.339 -17.465 -10.198 1.00 37.30  ? 386 GLY A O     1 
ATOM   3009 N N     . HIS A 1 387 ? 13.826 -18.374 -11.602 1.00 41.13  ? 387 HIS A N     1 
ATOM   3010 C CA    . HIS A 1 387 ? 13.409 -17.539 -12.711 1.00 41.47  ? 387 HIS A CA    1 
ATOM   3011 C C     . HIS A 1 387 ? 13.523 -18.292 -14.023 1.00 38.97  ? 387 HIS A C     1 
ATOM   3012 O O     . HIS A 1 387 ? 14.165 -19.336 -14.099 1.00 43.16  ? 387 HIS A O     1 
ATOM   3013 C CB    . HIS A 1 387 ? 14.224 -16.241 -12.805 1.00 39.98  ? 387 HIS A CB    1 
ATOM   3014 C CG    . HIS A 1 387 ? 15.647 -16.373 -13.236 1.00 34.88  ? 387 HIS A CG    1 
ATOM   3015 N ND1   . HIS A 1 387 ? 16.144 -15.678 -14.326 1.00 33.13  ? 387 HIS A ND1   1 
ATOM   3016 C CD2   . HIS A 1 387 ? 16.682 -17.056 -12.726 1.00 35.27  ? 387 HIS A CD2   1 
ATOM   3017 C CE1   . HIS A 1 387 ? 17.439 -15.934 -14.461 1.00 33.38  ? 387 HIS A CE1   1 
ATOM   3018 N NE2   . HIS A 1 387 ? 17.780 -16.787 -13.515 1.00 35.20  ? 387 HIS A NE2   1 
ATOM   3019 N N     . VAL A 1 388 ? 12.862 -17.714 -15.024 1.00 35.55  ? 388 VAL A N     1 
ATOM   3020 C CA    . VAL A 1 388 ? 12.916 -18.154 -16.401 1.00 34.62  ? 388 VAL A CA    1 
ATOM   3021 C C     . VAL A 1 388 ? 12.975 -16.883 -17.237 1.00 33.08  ? 388 VAL A C     1 
ATOM   3022 O O     . VAL A 1 388 ? 12.530 -15.838 -16.777 1.00 32.96  ? 388 VAL A O     1 
ATOM   3023 C CB    . VAL A 1 388 ? 11.704 -19.037 -16.745 1.00 34.10  ? 388 VAL A CB    1 
ATOM   3024 C CG1   . VAL A 1 388 ? 10.418 -18.232 -16.768 1.00 39.58  ? 388 VAL A CG1   1 
ATOM   3025 C CG2   . VAL A 1 388 ? 11.881 -19.769 -18.060 1.00 34.35  ? 388 VAL A CG2   1 
ATOM   3026 N N     . GLY A 1 389 ? 13.541 -16.968 -18.444 1.00 35.48  ? 389 GLY A N     1 
ATOM   3027 C CA    . GLY A 1 389 ? 13.698 -15.795 -19.285 1.00 32.78  ? 389 GLY A CA    1 
ATOM   3028 C C     . GLY A 1 389 ? 13.060 -15.962 -20.657 1.00 32.98  ? 389 GLY A C     1 
ATOM   3029 O O     . GLY A 1 389 ? 13.049 -17.054 -21.219 1.00 38.93  ? 389 GLY A O     1 
ATOM   3030 N N     . PHE A 1 390 ? 12.581 -14.832 -21.186 1.00 33.23  ? 390 PHE A N     1 
ATOM   3031 C CA    . PHE A 1 390 ? 12.046 -14.739 -22.521 1.00 35.29  ? 390 PHE A CA    1 
ATOM   3032 C C     . PHE A 1 390 ? 12.846 -13.646 -23.219 1.00 36.68  ? 390 PHE A C     1 
ATOM   3033 O O     . PHE A 1 390 ? 12.792 -12.494 -22.805 1.00 37.78  ? 390 PHE A O     1 
ATOM   3034 C CB    . PHE A 1 390 ? 10.526 -14.518 -22.473 1.00 38.88  ? 390 PHE A CB    1 
ATOM   3035 C CG    . PHE A 1 390 ? 9.887  -14.355 -23.832 1.00 41.41  ? 390 PHE A CG    1 
ATOM   3036 C CD1   . PHE A 1 390 ? 9.977  -15.363 -24.780 1.00 42.52  ? 390 PHE A CD1   1 
ATOM   3037 C CD2   . PHE A 1 390 ? 9.250  -13.175 -24.186 1.00 40.55  ? 390 PHE A CD2   1 
ATOM   3038 C CE1   . PHE A 1 390 ? 9.437  -15.197 -26.049 1.00 51.29  ? 390 PHE A CE1   1 
ATOM   3039 C CE2   . PHE A 1 390 ? 8.703  -13.012 -25.452 1.00 42.41  ? 390 PHE A CE2   1 
ATOM   3040 C CZ    . PHE A 1 390 ? 8.790  -14.024 -26.380 1.00 47.62  ? 390 PHE A CZ    1 
ATOM   3041 N N     . SER A 1 391 ? 13.587 -14.012 -24.277 1.00 36.99  ? 391 SER A N     1 
ATOM   3042 C CA    . SER A 1 391 ? 14.710 -13.195 -24.732 1.00 42.07  ? 391 SER A CA    1 
ATOM   3043 C C     . SER A 1 391 ? 14.607 -12.898 -26.235 1.00 42.04  ? 391 SER A C     1 
ATOM   3044 O O     . SER A 1 391 ? 15.611 -12.919 -26.941 1.00 45.33  ? 391 SER A O     1 
ATOM   3045 C CB    . SER A 1 391 ? 16.060 -13.849 -24.391 1.00 40.36  ? 391 SER A CB    1 
ATOM   3046 O OG    . SER A 1 391 ? 15.939 -14.854 -23.378 1.00 46.69  ? 391 SER A OG    1 
ATOM   3047 N N     . PRO A 1 392 ? 13.427 -12.556 -26.801 1.00 36.57  ? 392 PRO A N     1 
ATOM   3048 C CA    . PRO A 1 392 ? 13.319 -12.360 -28.241 1.00 35.05  ? 392 PRO A CA    1 
ATOM   3049 C C     . PRO A 1 392 ? 14.267 -11.275 -28.735 1.00 36.60  ? 392 PRO A C     1 
ATOM   3050 O O     . PRO A 1 392 ? 14.790 -10.501 -27.950 1.00 39.27  ? 392 PRO A O     1 
ATOM   3051 C CB    . PRO A 1 392 ? 11.861 -11.929 -28.432 1.00 34.70  ? 392 PRO A CB    1 
ATOM   3052 C CG    . PRO A 1 392 ? 11.506 -11.324 -27.112 1.00 31.33  ? 392 PRO A CG    1 
ATOM   3053 C CD    . PRO A 1 392 ? 12.163 -12.250 -26.115 1.00 35.38  ? 392 PRO A CD    1 
ATOM   3054 N N     . VAL A 1 393 ? 14.425 -11.233 -30.051 1.00 36.21  ? 393 VAL A N     1 
ATOM   3055 C CA    . VAL A 1 393 ? 15.291 -10.303 -30.736 1.00 38.12  ? 393 VAL A CA    1 
ATOM   3056 C C     . VAL A 1 393 ? 14.435 -9.335  -31.548 1.00 39.03  ? 393 VAL A C     1 
ATOM   3057 O O     . VAL A 1 393 ? 13.553 -9.770  -32.293 1.00 35.51  ? 393 VAL A O     1 
ATOM   3058 C CB    . VAL A 1 393 ? 16.204 -11.092 -31.683 1.00 40.00  ? 393 VAL A CB    1 
ATOM   3059 C CG1   . VAL A 1 393 ? 16.967 -10.163 -32.614 1.00 41.55  ? 393 VAL A CG1   1 
ATOM   3060 C CG2   . VAL A 1 393 ? 17.118 -12.014 -30.900 1.00 42.27  ? 393 VAL A CG2   1 
ATOM   3061 N N     . SER A 1 394 ? 14.756 -8.041  -31.443 1.00 40.03  ? 394 SER A N     1 
ATOM   3062 C CA    . SER A 1 394 ? 14.098 -7.018  -32.242 1.00 39.97  ? 394 SER A CA    1 
ATOM   3063 C C     . SER A 1 394 ? 15.139 -6.108  -32.887 1.00 35.36  ? 394 SER A C     1 
ATOM   3064 O O     . SER A 1 394 ? 16.298 -6.060  -32.463 1.00 33.36  ? 394 SER A O     1 
ATOM   3065 C CB    . SER A 1 394 ? 13.121 -6.208  -31.403 1.00 40.51  ? 394 SER A CB    1 
ATOM   3066 O OG    . SER A 1 394 ? 13.773 -5.561  -30.317 1.00 37.82  ? 394 SER A OG    1 
ATOM   3067 N N     . PRO A 1 395 ? 14.725 -5.331  -33.906 1.00 30.72  ? 395 PRO A N     1 
ATOM   3068 C CA    . PRO A 1 395 ? 15.523 -4.219  -34.399 1.00 32.06  ? 395 PRO A CA    1 
ATOM   3069 C C     . PRO A 1 395 ? 15.718 -3.201  -33.283 1.00 37.95  ? 395 PRO A C     1 
ATOM   3070 O O     . PRO A 1 395 ? 14.881 -3.098  -32.396 1.00 44.14  ? 395 PRO A O     1 
ATOM   3071 C CB    . PRO A 1 395 ? 14.689 -3.580  -35.511 1.00 31.70  ? 395 PRO A CB    1 
ATOM   3072 C CG    . PRO A 1 395 ? 13.577 -4.568  -35.814 1.00 33.00  ? 395 PRO A CG    1 
ATOM   3073 C CD    . PRO A 1 395 ? 13.440 -5.458  -34.595 1.00 32.04  ? 395 PRO A CD    1 
ATOM   3074 N N     . ILE A 1 396 ? 16.808 -2.432  -33.353 1.00 39.70  ? 396 ILE A N     1 
ATOM   3075 C CA    . ILE A 1 396 ? 17.034 -1.350  -32.409 1.00 35.36  ? 396 ILE A CA    1 
ATOM   3076 C C     . ILE A 1 396 ? 16.185 -0.164  -32.856 1.00 35.91  ? 396 ILE A C     1 
ATOM   3077 O O     . ILE A 1 396 ? 16.657 0.735   -33.533 1.00 37.40  ? 396 ILE A O     1 
ATOM   3078 C CB    . ILE A 1 396 ? 18.525 -1.000  -32.322 1.00 32.29  ? 396 ILE A CB    1 
ATOM   3079 C CG1   . ILE A 1 396 ? 19.422 -2.236  -32.205 1.00 33.21  ? 396 ILE A CG1   1 
ATOM   3080 C CG2   . ILE A 1 396 ? 18.762 -0.041  -31.180 1.00 33.61  ? 396 ILE A CG2   1 
ATOM   3081 C CD1   . ILE A 1 396 ? 20.898 -1.943  -32.472 1.00 33.71  ? 396 ILE A CD1   1 
ATOM   3082 N N     . THR A 1 397 ? 14.898 -0.199  -32.521 1.00 38.13  ? 397 THR A N     1 
ATOM   3083 C CA    . THR A 1 397 ? 14.022 0.927   -32.780 1.00 40.70  ? 397 THR A CA    1 
ATOM   3084 C C     . THR A 1 397 ? 13.263 1.267   -31.502 1.00 37.38  ? 397 THR A C     1 
ATOM   3085 O O     . THR A 1 397 ? 12.889 0.385   -30.729 1.00 29.71  ? 397 THR A O     1 
ATOM   3086 C CB    . THR A 1 397 ? 13.061 0.626   -33.937 1.00 46.01  ? 397 THR A CB    1 
ATOM   3087 O OG1   . THR A 1 397 ? 13.891 0.256   -35.033 1.00 49.12  ? 397 THR A OG1   1 
ATOM   3088 C CG2   . THR A 1 397 ? 12.216 1.802   -34.368 1.00 52.09  ? 397 THR A CG2   1 
ATOM   3089 N N     . GLY A 1 398 ? 13.029 2.565   -31.319 1.00 36.43  ? 398 GLY A N     1 
ATOM   3090 C CA    . GLY A 1 398 ? 12.127 3.038   -30.288 1.00 39.04  ? 398 GLY A CA    1 
ATOM   3091 C C     . GLY A 1 398 ? 10.812 2.274   -30.342 1.00 39.24  ? 398 GLY A C     1 
ATOM   3092 O O     . GLY A 1 398 ? 10.366 1.732   -29.336 1.00 41.58  ? 398 GLY A O     1 
ATOM   3093 N N     . LYS A 1 399 ? 10.245 2.223   -31.549 1.00 41.94  ? 399 LYS A N     1 
ATOM   3094 C CA    . LYS A 1 399 ? 8.946  1.634   -31.808 1.00 42.51  ? 399 LYS A CA    1 
ATOM   3095 C C     . LYS A 1 399 ? 8.954  0.167   -31.397 1.00 35.73  ? 399 LYS A C     1 
ATOM   3096 O O     . LYS A 1 399 ? 8.014  -0.289  -30.780 1.00 37.55  ? 399 LYS A O     1 
ATOM   3097 C CB    . LYS A 1 399 ? 8.556  1.836   -33.277 1.00 50.50  ? 399 LYS A CB    1 
ATOM   3098 C CG    . LYS A 1 399 ? 7.201  1.256   -33.657 1.00 63.41  ? 399 LYS A CG    1 
ATOM   3099 C CD    . LYS A 1 399 ? 6.721  1.585   -35.058 1.00 73.34  ? 399 LYS A CD    1 
ATOM   3100 C CE    . LYS A 1 399 ? 5.372  0.958   -35.344 1.00 80.41  ? 399 LYS A CE    1 
ATOM   3101 N NZ    . LYS A 1 399 ? 4.599  1.748   -36.332 1.00 82.56  ? 399 LYS A NZ    1 
ATOM   3102 N N     . ASP A 1 400 ? 10.012 -0.571  -31.714 1.00 37.20  ? 400 ASP A N     1 
ATOM   3103 C CA    . ASP A 1 400 ? 10.098 -1.973  -31.332 1.00 36.15  ? 400 ASP A CA    1 
ATOM   3104 C C     . ASP A 1 400 ? 10.310 -2.111  -29.823 1.00 34.53  ? 400 ASP A C     1 
ATOM   3105 O O     . ASP A 1 400 ? 9.746  -2.981  -29.179 1.00 34.62  ? 400 ASP A O     1 
ATOM   3106 C CB    . ASP A 1 400 ? 11.209 -2.677  -32.109 1.00 37.19  ? 400 ASP A CB    1 
ATOM   3107 C CG    . ASP A 1 400 ? 10.831 -2.878  -33.562 1.00 36.85  ? 400 ASP A CG    1 
ATOM   3108 O OD1   . ASP A 1 400 ? 9.916  -3.664  -33.805 1.00 35.40  ? 400 ASP A OD1   1 
ATOM   3109 O OD2   . ASP A 1 400 ? 11.431 -2.209  -34.421 1.00 38.47  ? 400 ASP A OD2   1 
ATOM   3110 N N     . ALA A 1 401 ? 11.144 -1.260  -29.250 1.00 37.01  ? 401 ALA A N     1 
ATOM   3111 C CA    . ALA A 1 401 ? 11.419 -1.346  -27.827 1.00 37.92  ? 401 ALA A CA    1 
ATOM   3112 C C     . ALA A 1 401 ? 10.126 -1.159  -27.036 1.00 36.18  ? 401 ALA A C     1 
ATOM   3113 O O     . ALA A 1 401 ? 9.762  -2.022  -26.244 1.00 36.44  ? 401 ALA A O     1 
ATOM   3114 C CB    . ALA A 1 401 ? 12.472 -0.333  -27.441 1.00 35.11  ? 401 ALA A CB    1 
ATOM   3115 N N     . ILE A 1 402 ? 9.431  -0.041  -27.269 1.00 38.60  ? 402 ILE A N     1 
ATOM   3116 C CA    . ILE A 1 402 ? 8.303  0.313   -26.429 1.00 40.95  ? 402 ILE A CA    1 
ATOM   3117 C C     . ILE A 1 402 ? 7.136  -0.625  -26.712 1.00 44.01  ? 402 ILE A C     1 
ATOM   3118 O O     . ILE A 1 402 ? 6.386  -0.933  -25.793 1.00 44.09  ? 402 ILE A O     1 
ATOM   3119 C CB    . ILE A 1 402 ? 7.883  1.784   -26.570 1.00 41.38  ? 402 ILE A CB    1 
ATOM   3120 C CG1   . ILE A 1 402 ? 7.003  2.179   -25.380 1.00 46.43  ? 402 ILE A CG1   1 
ATOM   3121 C CG2   . ILE A 1 402 ? 7.212  2.056   -27.910 1.00 38.64  ? 402 ILE A CG2   1 
ATOM   3122 C CD1   . ILE A 1 402 ? 6.618  3.631   -25.349 1.00 51.87  ? 402 ILE A CD1   1 
ATOM   3123 N N     . LYS A 1 403 ? 6.985  -1.079  -27.965 1.00 41.51  ? 403 LYS A N     1 
ATOM   3124 C CA    . LYS A 1 403 ? 5.927  -2.031  -28.270 1.00 41.02  ? 403 LYS A CA    1 
ATOM   3125 C C     . LYS A 1 403 ? 6.118  -3.249  -27.377 1.00 42.78  ? 403 LYS A C     1 
ATOM   3126 O O     . LYS A 1 403 ? 5.185  -3.722  -26.738 1.00 45.02  ? 403 LYS A O     1 
ATOM   3127 C CB    . LYS A 1 403 ? 5.933  -2.530  -29.717 1.00 40.42  ? 403 LYS A CB    1 
ATOM   3128 C CG    . LYS A 1 403 ? 4.661  -3.269  -30.106 1.00 43.59  ? 403 LYS A CG    1 
ATOM   3129 C CD    . LYS A 1 403 ? 4.836  -4.312  -31.167 1.00 46.16  ? 403 LYS A CD    1 
ATOM   3130 C CE    . LYS A 1 403 ? 5.109  -3.740  -32.542 1.00 52.62  ? 403 LYS A CE    1 
ATOM   3131 N NZ    . LYS A 1 403 ? 5.120  -4.824  -33.556 1.00 55.99  ? 403 LYS A NZ    1 
ATOM   3132 N N     . GLN A 1 404 ? 7.355  -3.736  -27.339 1.00 41.89  ? 404 GLN A N     1 
ATOM   3133 C CA    . GLN A 1 404 ? 7.657  -4.955  -26.623 1.00 43.11  ? 404 GLN A CA    1 
ATOM   3134 C C     . GLN A 1 404 ? 7.569  -4.738  -25.114 1.00 43.69  ? 404 GLN A C     1 
ATOM   3135 O O     . GLN A 1 404 ? 7.115  -5.615  -24.401 1.00 42.90  ? 404 GLN A O     1 
ATOM   3136 C CB    . GLN A 1 404 ? 9.034  -5.446  -27.028 1.00 41.11  ? 404 GLN A CB    1 
ATOM   3137 C CG    . GLN A 1 404 ? 8.998  -6.402  -28.193 1.00 42.24  ? 404 GLN A CG    1 
ATOM   3138 C CD    . GLN A 1 404 ? 10.416 -6.676  -28.609 1.00 45.52  ? 404 GLN A CD    1 
ATOM   3139 O OE1   . GLN A 1 404 ? 11.080 -5.779  -29.127 1.00 49.48  ? 404 GLN A OE1   1 
ATOM   3140 N NE2   . GLN A 1 404 ? 10.899 -7.880  -28.333 1.00 42.79  ? 404 GLN A NE2   1 
ATOM   3141 N N     . TYR A 1 405 ? 7.987  -3.573  -24.621 1.00 46.56  ? 405 TYR A N     1 
ATOM   3142 C CA    . TYR A 1 405 ? 7.832  -3.300  -23.203 1.00 48.26  ? 405 TYR A CA    1 
ATOM   3143 C C     . TYR A 1 405 ? 6.359  -3.407  -22.824 1.00 47.42  ? 405 TYR A C     1 
ATOM   3144 O O     . TYR A 1 405 ? 6.031  -4.168  -21.913 1.00 45.41  ? 405 TYR A O     1 
ATOM   3145 C CB    . TYR A 1 405 ? 8.402  -1.934  -22.827 1.00 46.96  ? 405 TYR A CB    1 
ATOM   3146 C CG    . TYR A 1 405 ? 7.950  -1.430  -21.480 1.00 46.14  ? 405 TYR A CG    1 
ATOM   3147 C CD1   . TYR A 1 405 ? 8.325  -2.062  -20.304 1.00 48.88  ? 405 TYR A CD1   1 
ATOM   3148 C CD2   . TYR A 1 405 ? 7.139  -0.318  -21.383 1.00 44.96  ? 405 TYR A CD2   1 
ATOM   3149 C CE1   . TYR A 1 405 ? 7.923  -1.589  -19.064 1.00 45.39  ? 405 TYR A CE1   1 
ATOM   3150 C CE2   . TYR A 1 405 ? 6.724  0.166   -20.155 1.00 52.81  ? 405 TYR A CE2   1 
ATOM   3151 C CZ    . TYR A 1 405 ? 7.118  -0.468  -18.987 1.00 53.45  ? 405 TYR A CZ    1 
ATOM   3152 O OH    . TYR A 1 405 ? 6.684  0.028   -17.773 1.00 55.96  ? 405 TYR A OH    1 
ATOM   3153 N N     . ASN A 1 406 ? 5.506  -2.654  -23.547 1.00 46.20  ? 406 ASN A N     1 
ATOM   3154 C CA    . ASN A 1 406 ? 4.067  -2.586  -23.314 1.00 48.22  ? 406 ASN A CA    1 
ATOM   3155 C C     . ASN A 1 406 ? 3.395  -3.959  -23.410 1.00 47.86  ? 406 ASN A C     1 
ATOM   3156 O O     . ASN A 1 406 ? 2.511  -4.250  -22.608 1.00 50.23  ? 406 ASN A O     1 
ATOM   3157 C CB    . ASN A 1 406 ? 3.378  -1.590  -24.257 1.00 48.77  ? 406 ASN A CB    1 
ATOM   3158 C CG    . ASN A 1 406 ? 3.621  -0.138  -23.879 1.00 46.90  ? 406 ASN A CG    1 
ATOM   3159 O OD1   . ASN A 1 406 ? 3.960  0.178   -22.744 1.00 53.67  ? 406 ASN A OD1   1 
ATOM   3160 N ND2   . ASN A 1 406 ? 3.457  0.770   -24.820 1.00 43.67  ? 406 ASN A ND2   1 
ATOM   3161 N N     . MET A 1 407 ? 3.803  -4.799  -24.372 1.00 46.70  ? 407 MET A N     1 
ATOM   3162 C CA    . MET A 1 407 ? 3.188  -6.107  -24.590 1.00 48.48  ? 407 MET A CA    1 
ATOM   3163 C C     . MET A 1 407 ? 3.483  -7.045  -23.429 1.00 47.89  ? 407 MET A C     1 
ATOM   3164 O O     . MET A 1 407 ? 2.656  -7.880  -23.088 1.00 49.14  ? 407 MET A O     1 
ATOM   3165 C CB    . MET A 1 407 ? 3.769  -6.841  -25.805 1.00 47.82  ? 407 MET A CB    1 
ATOM   3166 C CG    . MET A 1 407 ? 3.197  -6.458  -27.128 1.00 45.71  ? 407 MET A CG    1 
ATOM   3167 S SD    . MET A 1 407 ? 4.283  -7.137  -28.391 1.00 46.85  ? 407 MET A SD    1 
ATOM   3168 C CE    . MET A 1 407 ? 3.487  -8.723  -28.669 1.00 46.77  ? 407 MET A CE    1 
ATOM   3169 N N     . VAL A 1 408 ? 4.731  -7.001  -22.957 1.00 49.19  ? 408 VAL A N     1 
ATOM   3170 C CA    . VAL A 1 408 ? 5.246  -7.992  -22.024 1.00 50.99  ? 408 VAL A CA    1 
ATOM   3171 C C     . VAL A 1 408 ? 4.937  -7.547  -20.596 1.00 50.20  ? 408 VAL A C     1 
ATOM   3172 O O     . VAL A 1 408 ? 4.470  -8.361  -19.802 1.00 51.52  ? 408 VAL A O     1 
ATOM   3173 C CB    . VAL A 1 408 ? 6.750  -8.248  -22.234 1.00 46.31  ? 408 VAL A CB    1 
ATOM   3174 C CG1   . VAL A 1 408 ? 7.306  -9.182  -21.180 1.00 51.53  ? 408 VAL A CG1   1 
ATOM   3175 C CG2   . VAL A 1 408 ? 7.037  -8.810  -23.613 1.00 45.67  ? 408 VAL A CG2   1 
ATOM   3176 N N     . SER A 1 409 ? 5.164  -6.258  -20.299 1.00 48.11  ? 409 SER A N     1 
ATOM   3177 C CA    . SER A 1 409 ? 4.938  -5.737  -18.963 1.00 50.30  ? 409 SER A CA    1 
ATOM   3178 C C     . SER A 1 409 ? 3.469  -5.916  -18.588 1.00 49.53  ? 409 SER A C     1 
ATOM   3179 O O     . SER A 1 409 ? 3.177  -6.368  -17.484 1.00 42.18  ? 409 SER A O     1 
ATOM   3180 C CB    . SER A 1 409 ? 5.411  -4.303  -18.809 1.00 49.48  ? 409 SER A CB    1 
ATOM   3181 O OG    . SER A 1 409 ? 4.506  -3.367  -19.382 1.00 53.84  ? 409 SER A OG    1 
ATOM   3182 N N     . SER A 1 410 ? 2.572  -5.600  -19.535 1.00 50.74  ? 410 SER A N     1 
ATOM   3183 C CA    . SER A 1 410 ? 1.139  -5.806  -19.385 1.00 51.56  ? 410 SER A CA    1 
ATOM   3184 C C     . SER A 1 410 ? 0.835  -7.219  -18.904 1.00 47.24  ? 410 SER A C     1 
ATOM   3185 O O     . SER A 1 410 ? 0.080  -7.420  -17.956 1.00 50.12  ? 410 SER A O     1 
ATOM   3186 C CB    . SER A 1 410 ? 0.417  -5.562  -20.684 1.00 54.87  ? 410 SER A CB    1 
ATOM   3187 O OG    . SER A 1 410 ? 0.368  -4.176  -20.969 1.00 65.20  ? 410 SER A OG    1 
ATOM   3188 N N     . ARG A 1 411 ? 1.413  -8.184  -19.610 1.00 41.59  ? 411 ARG A N     1 
ATOM   3189 C CA    . ARG A 1 411 ? 1.012  -9.568  -19.509 1.00 43.53  ? 411 ARG A CA    1 
ATOM   3190 C C     . ARG A 1 411 ? 1.582  -10.193 -18.249 1.00 40.37  ? 411 ARG A C     1 
ATOM   3191 O O     . ARG A 1 411 ? 0.934  -11.008 -17.616 1.00 42.14  ? 411 ARG A O     1 
ATOM   3192 C CB    . ARG A 1 411 ? 1.539  -10.335 -20.725 1.00 45.04  ? 411 ARG A CB    1 
ATOM   3193 C CG    . ARG A 1 411 ? 0.729  -10.109 -21.988 1.00 42.88  ? 411 ARG A CG    1 
ATOM   3194 C CD    . ARG A 1 411 ? -0.558 -10.879 -21.858 1.00 42.30  ? 411 ARG A CD    1 
ATOM   3195 N NE    . ARG A 1 411 ? -1.368 -10.651 -23.027 1.00 44.43  ? 411 ARG A NE    1 
ATOM   3196 C CZ    . ARG A 1 411 ? -2.628 -11.014 -23.135 1.00 45.42  ? 411 ARG A CZ    1 
ATOM   3197 N NH1   . ARG A 1 411 ? -3.242 -11.573 -22.107 1.00 47.53  ? 411 ARG A NH1   1 
ATOM   3198 N NH2   . ARG A 1 411 ? -3.258 -10.812 -24.274 1.00 49.10  ? 411 ARG A NH2   1 
ATOM   3199 N N     . VAL A 1 412 ? 2.836  -9.858  -17.961 1.00 42.22  ? 412 VAL A N     1 
ATOM   3200 C CA    . VAL A 1 412 ? 3.520  -10.360 -16.785 1.00 44.91  ? 412 VAL A CA    1 
ATOM   3201 C C     . VAL A 1 412 ? 2.777  -9.871  -15.540 1.00 40.61  ? 412 VAL A C     1 
ATOM   3202 O O     . VAL A 1 412 ? 2.494  -10.652 -14.645 1.00 40.32  ? 412 VAL A O     1 
ATOM   3203 C CB    . VAL A 1 412 ? 4.995  -9.921  -16.820 1.00 46.41  ? 412 VAL A CB    1 
ATOM   3204 C CG1   . VAL A 1 412 ? 5.723  -10.178 -15.508 1.00 49.72  ? 412 VAL A CG1   1 
ATOM   3205 C CG2   . VAL A 1 412 ? 5.720  -10.582 -17.982 1.00 46.32  ? 412 VAL A CG2   1 
ATOM   3206 N N     . ARG A 1 413 ? 2.415  -8.585  -15.520 1.00 42.89  ? 413 ARG A N     1 
ATOM   3207 C CA    . ARG A 1 413 ? 1.758  -7.984  -14.368 1.00 45.81  ? 413 ARG A CA    1 
ATOM   3208 C C     . ARG A 1 413 ? 0.386  -8.628  -14.184 1.00 43.00  ? 413 ARG A C     1 
ATOM   3209 O O     . ARG A 1 413 ? 0.050  -9.001  -13.065 1.00 38.17  ? 413 ARG A O     1 
ATOM   3210 C CB    . ARG A 1 413 ? 1.761  -6.452  -14.481 1.00 42.48  ? 413 ARG A CB    1 
ATOM   3211 C CG    . ARG A 1 413 ? 3.131  -5.842  -14.180 1.00 41.75  ? 413 ARG A CG    1 
ATOM   3212 C CD    . ARG A 1 413 ? 3.280  -4.360  -14.508 1.00 41.39  ? 413 ARG A CD    1 
ATOM   3213 N NE    . ARG A 1 413 ? 2.372  -3.524  -13.744 1.00 43.98  ? 413 ARG A NE    1 
ATOM   3214 C CZ    . ARG A 1 413 ? 2.567  -3.132  -12.485 1.00 47.50  ? 413 ARG A CZ    1 
ATOM   3215 N NH1   . ARG A 1 413 ? 3.771  -3.178  -11.939 1.00 54.81  ? 413 ARG A NH1   1 
ATOM   3216 N NH2   . ARG A 1 413 ? 1.562  -2.641  -11.787 1.00 44.82  ? 413 ARG A NH2   1 
ATOM   3217 N N     . GLU A 1 414 ? -0.334 -8.820  -15.301 1.00 43.59  ? 414 GLU A N     1 
ATOM   3218 C CA    . GLU A 1 414 ? -1.650 -9.437  -15.345 1.00 42.56  ? 414 GLU A CA    1 
ATOM   3219 C C     . GLU A 1 414 ? -1.622 -10.813 -14.678 1.00 42.20  ? 414 GLU A C     1 
ATOM   3220 O O     . GLU A 1 414 ? -2.591 -11.202 -14.034 1.00 42.60  ? 414 GLU A O     1 
ATOM   3221 C CB    . GLU A 1 414 ? -2.120 -9.522  -16.804 1.00 49.39  ? 414 GLU A CB    1 
ATOM   3222 C CG    . GLU A 1 414 ? -3.443 -10.267 -17.023 1.00 57.00  ? 414 GLU A CG    1 
ATOM   3223 C CD    . GLU A 1 414 ? -3.756 -10.680 -18.459 1.00 63.36  ? 414 GLU A CD    1 
ATOM   3224 O OE1   . GLU A 1 414 ? -3.011 -10.287 -19.378 1.00 68.57  ? 414 GLU A OE1   1 
ATOM   3225 O OE2   . GLU A 1 414 ? -4.742 -11.405 -18.666 1.00 63.51  ? 414 GLU A OE2   1 
ATOM   3226 N N     . TYR A 1 415 ? -0.524 -11.552 -14.854 1.00 40.33  ? 415 TYR A N     1 
ATOM   3227 C CA    . TYR A 1 415 ? -0.386 -12.891 -14.300 1.00 41.17  ? 415 TYR A CA    1 
ATOM   3228 C C     . TYR A 1 415 ? 0.244  -12.856 -12.900 1.00 44.20  ? 415 TYR A C     1 
ATOM   3229 O O     . TYR A 1 415 ? 0.568  -13.907 -12.341 1.00 44.07  ? 415 TYR A O     1 
ATOM   3230 C CB    . TYR A 1 415 ? 0.387  -13.776 -15.285 1.00 40.72  ? 415 TYR A CB    1 
ATOM   3231 C CG    . TYR A 1 415 ? -0.507 -14.379 -16.333 1.00 40.11  ? 415 TYR A CG    1 
ATOM   3232 C CD1   . TYR A 1 415 ? -1.016 -13.614 -17.368 1.00 38.97  ? 415 TYR A CD1   1 
ATOM   3233 C CD2   . TYR A 1 415 ? -0.905 -15.706 -16.245 1.00 39.89  ? 415 TYR A CD2   1 
ATOM   3234 C CE1   . TYR A 1 415 ? -1.887 -14.159 -18.297 1.00 40.54  ? 415 TYR A CE1   1 
ATOM   3235 C CE2   . TYR A 1 415 ? -1.780 -16.261 -17.162 1.00 37.53  ? 415 TYR A CE2   1 
ATOM   3236 C CZ    . TYR A 1 415 ? -2.283 -15.480 -18.183 1.00 38.30  ? 415 TYR A CZ    1 
ATOM   3237 O OH    . TYR A 1 415 ? -3.148 -16.034 -19.091 1.00 44.51  ? 415 TYR A OH    1 
ATOM   3238 N N     . GLY A 1 416 ? 0.415  -11.654 -12.332 1.00 41.98  ? 416 GLY A N     1 
ATOM   3239 C CA    . GLY A 1 416 ? 0.684  -11.510 -10.913 1.00 43.19  ? 416 GLY A CA    1 
ATOM   3240 C C     . GLY A 1 416 ? 2.168  -11.414 -10.568 1.00 44.51  ? 416 GLY A C     1 
ATOM   3241 O O     . GLY A 1 416 ? 2.509  -11.430 -9.395  1.00 44.71  ? 416 GLY A O     1 
ATOM   3242 N N     . PHE A 1 417 ? 3.046  -11.284 -11.572 1.00 46.12  ? 417 PHE A N     1 
ATOM   3243 C CA    . PHE A 1 417 ? 4.480  -11.150 -11.335 1.00 40.03  ? 417 PHE A CA    1 
ATOM   3244 C C     . PHE A 1 417 ? 4.905  -9.712  -11.598 1.00 39.77  ? 417 PHE A C     1 
ATOM   3245 O O     . PHE A 1 417 ? 4.251  -9.004  -12.357 1.00 42.35  ? 417 PHE A O     1 
ATOM   3246 C CB    . PHE A 1 417 ? 5.271  -12.066 -12.267 1.00 38.88  ? 417 PHE A CB    1 
ATOM   3247 C CG    . PHE A 1 417 ? 4.886  -13.525 -12.235 1.00 35.82  ? 417 PHE A CG    1 
ATOM   3248 C CD1   . PHE A 1 417 ? 5.330  -14.363 -11.228 1.00 35.84  ? 417 PHE A CD1   1 
ATOM   3249 C CD2   . PHE A 1 417 ? 4.058  -14.059 -13.206 1.00 33.10  ? 417 PHE A CD2   1 
ATOM   3250 C CE1   . PHE A 1 417 ? 4.972  -15.704 -11.210 1.00 33.26  ? 417 PHE A CE1   1 
ATOM   3251 C CE2   . PHE A 1 417 ? 3.707  -15.400 -13.189 1.00 31.28  ? 417 PHE A CE2   1 
ATOM   3252 C CZ    . PHE A 1 417 ? 4.180  -16.225 -12.199 1.00 31.10  ? 417 PHE A CZ    1 
ATOM   3253 N N     . ASP A 1 418 ? 5.993  -9.269  -10.964 1.00 38.17  ? 418 ASP A N     1 
ATOM   3254 C CA    . ASP A 1 418 ? 6.543  -7.962  -11.289 1.00 38.59  ? 418 ASP A CA    1 
ATOM   3255 C C     . ASP A 1 418 ? 7.302  -8.042  -12.613 1.00 39.03  ? 418 ASP A C     1 
ATOM   3256 O O     . ASP A 1 418 ? 7.963  -9.042  -12.905 1.00 36.41  ? 418 ASP A O     1 
ATOM   3257 C CB    . ASP A 1 418 ? 7.477  -7.422  -10.202 1.00 36.89  ? 418 ASP A CB    1 
ATOM   3258 C CG    . ASP A 1 418 ? 6.795  -6.540  -9.176  1.00 34.38  ? 418 ASP A CG    1 
ATOM   3259 O OD1   . ASP A 1 418 ? 6.213  -5.510  -9.574  1.00 37.66  ? 418 ASP A OD1   1 
ATOM   3260 O OD2   . ASP A 1 418 ? 6.833  -6.899  -8.000  1.00 36.41  ? 418 ASP A OD2   1 
ATOM   3261 N N     . TYR A 1 419 ? 7.244  -6.943  -13.366 1.00 38.71  ? 419 TYR A N     1 
ATOM   3262 C CA    . TYR A 1 419 ? 7.996  -6.809  -14.601 1.00 40.55  ? 419 TYR A CA    1 
ATOM   3263 C C     . TYR A 1 419 ? 9.458  -6.500  -14.290 1.00 38.63  ? 419 TYR A C     1 
ATOM   3264 O O     . TYR A 1 419 ? 9.762  -5.486  -13.677 1.00 40.15  ? 419 TYR A O     1 
ATOM   3265 C CB    . TYR A 1 419 ? 7.451  -5.676  -15.476 1.00 42.58  ? 419 TYR A CB    1 
ATOM   3266 C CG    . TYR A 1 419 ? 8.321  -5.410  -16.680 1.00 44.17  ? 419 TYR A CG    1 
ATOM   3267 C CD1   . TYR A 1 419 ? 8.390  -6.331  -17.716 1.00 43.87  ? 419 TYR A CD1   1 
ATOM   3268 C CD2   . TYR A 1 419 ? 9.132  -4.290  -16.748 1.00 42.24  ? 419 TYR A CD2   1 
ATOM   3269 C CE1   . TYR A 1 419 ? 9.232  -6.146  -18.797 1.00 44.30  ? 419 TYR A CE1   1 
ATOM   3270 C CE2   . TYR A 1 419 ? 9.961  -4.076  -17.834 1.00 44.83  ? 419 TYR A CE2   1 
ATOM   3271 C CZ    . TYR A 1 419 ? 10.004 -5.004  -18.860 1.00 45.28  ? 419 TYR A CZ    1 
ATOM   3272 O OH    . TYR A 1 419 ? 10.810 -4.821  -19.936 1.00 48.70  ? 419 TYR A OH    1 
ATOM   3273 N N     . MET A 1 420 ? 10.349 -7.366  -14.758 1.00 38.89  ? 420 MET A N     1 
ATOM   3274 C CA    . MET A 1 420 ? 11.774 -7.118  -14.727 1.00 44.14  ? 420 MET A CA    1 
ATOM   3275 C C     . MET A 1 420 ? 12.324 -7.239  -16.151 1.00 49.95  ? 420 MET A C     1 
ATOM   3276 O O     . MET A 1 420 ? 12.318 -8.323  -16.726 1.00 54.49  ? 420 MET A O     1 
ATOM   3277 C CB    . MET A 1 420 ? 12.442 -8.155  -13.826 1.00 45.44  ? 420 MET A CB    1 
ATOM   3278 C CG    . MET A 1 420 ? 12.053 -8.021  -12.363 1.00 48.15  ? 420 MET A CG    1 
ATOM   3279 S SD    . MET A 1 420 ? 12.744 -9.392  -11.427 1.00 44.28  ? 420 MET A SD    1 
ATOM   3280 C CE    . MET A 1 420 ? 12.016 -9.112  -9.816  1.00 45.97  ? 420 MET A CE    1 
ATOM   3281 N N     . GLY A 1 421 ? 12.803 -6.123  -16.713 1.00 52.89  ? 421 GLY A N     1 
ATOM   3282 C CA    . GLY A 1 421 ? 13.226 -6.062  -18.105 1.00 52.27  ? 421 GLY A CA    1 
ATOM   3283 C C     . GLY A 1 421 ? 14.665 -5.586  -18.273 1.00 51.64  ? 421 GLY A C     1 
ATOM   3284 O O     . GLY A 1 421 ? 15.134 -4.749  -17.508 1.00 58.11  ? 421 GLY A O     1 
ATOM   3285 N N     . LEU A 1 422 ? 15.326 -6.128  -19.304 1.00 59.69  ? 422 LEU A N     1 
ATOM   3286 C CA    . LEU A 1 422 ? 16.716 -5.869  -19.668 1.00 59.05  ? 422 LEU A CA    1 
ATOM   3287 C C     . LEU A 1 422 ? 16.795 -5.810  -21.196 1.00 65.00  ? 422 LEU A C     1 
ATOM   3288 O O     . LEU A 1 422 ? 17.103 -6.840  -21.803 1.00 46.56  ? 422 LEU A O     1 
ATOM   3289 C CB    . LEU A 1 422 ? 17.608 -7.004  -19.125 1.00 56.71  ? 422 LEU A CB    1 
ATOM   3290 C CG    . LEU A 1 422 ? 18.907 -7.321  -19.891 1.00 62.59  ? 422 LEU A CG    1 
ATOM   3291 C CD1   . LEU A 1 422 ? 19.937 -6.208  -19.744 1.00 63.02  ? 422 LEU A CD1   1 
ATOM   3292 C CD2   . LEU A 1 422 ? 19.530 -8.655  -19.463 1.00 64.89  ? 422 LEU A CD2   1 
ATOM   3293 N N     . LEU A 1 423 ? 16.452 -4.644  -21.796 1.00 63.78  ? 423 LEU A N     1 
ATOM   3294 C CA    . LEU A 1 423 ? 16.790 -4.334  -23.185 1.00 54.58  ? 423 LEU A CA    1 
ATOM   3295 C C     . LEU A 1 423 ? 18.299 -4.285  -23.370 1.00 50.78  ? 423 LEU A C     1 
ATOM   3296 O O     . LEU A 1 423 ? 18.905 -3.256  -23.104 1.00 55.30  ? 423 LEU A O     1 
ATOM   3297 C CB    . LEU A 1 423 ? 16.225 -2.976  -23.587 1.00 53.22  ? 423 LEU A CB    1 
ATOM   3298 C CG    . LEU A 1 423 ? 14.751 -2.958  -23.957 1.00 57.62  ? 423 LEU A CG    1 
ATOM   3299 C CD1   . LEU A 1 423 ? 14.282 -1.540  -24.119 1.00 55.18  ? 423 LEU A CD1   1 
ATOM   3300 C CD2   . LEU A 1 423 ? 14.505 -3.727  -25.235 1.00 62.85  ? 423 LEU A CD2   1 
ATOM   3301 N N     . ALA A 1 424 ? 18.874 -5.396  -23.849 1.00 53.63  ? 424 ALA A N     1 
ATOM   3302 C CA    . ALA A 1 424 ? 20.287 -5.486  -24.179 1.00 54.30  ? 424 ALA A CA    1 
ATOM   3303 C C     . ALA A 1 424 ? 20.495 -5.192  -25.668 1.00 57.61  ? 424 ALA A C     1 
ATOM   3304 O O     . ALA A 1 424 ? 19.564 -5.304  -26.477 1.00 55.56  ? 424 ALA A O     1 
ATOM   3305 C CB    . ALA A 1 424 ? 20.810 -6.852  -23.822 1.00 55.27  ? 424 ALA A CB    1 
ATOM   3306 N N     . ILE A 1 425 ? 21.724 -4.791  -26.025 1.00 51.35  ? 425 ILE A N     1 
ATOM   3307 C CA    . ILE A 1 425 ? 22.036 -4.526  -27.419 1.00 49.01  ? 425 ILE A CA    1 
ATOM   3308 C C     . ILE A 1 425 ? 23.426 -5.065  -27.729 1.00 41.42  ? 425 ILE A C     1 
ATOM   3309 O O     . ILE A 1 425 ? 24.421 -4.675  -27.106 1.00 30.25  ? 425 ILE A O     1 
ATOM   3310 C CB    . ILE A 1 425 ? 21.884 -3.041  -27.814 1.00 59.34  ? 425 ILE A CB    1 
ATOM   3311 C CG1   . ILE A 1 425 ? 20.416 -2.586  -27.836 1.00 59.42  ? 425 ILE A CG1   1 
ATOM   3312 C CG2   . ILE A 1 425 ? 22.535 -2.783  -29.168 1.00 61.63  ? 425 ILE A CG2   1 
ATOM   3313 C CD1   . ILE A 1 425 ? 20.214 -1.156  -28.317 1.00 53.85  ? 425 ILE A CD1   1 
ATOM   3314 N N     . GLY A 1 426 ? 23.437 -5.952  -28.734 1.00 34.67  ? 426 GLY A N     1 
ATOM   3315 C CA    . GLY A 1 426 ? 24.644 -6.568  -29.236 1.00 35.06  ? 426 GLY A CA    1 
ATOM   3316 C C     . GLY A 1 426 ? 25.398 -5.637  -30.175 1.00 36.88  ? 426 GLY A C     1 
ATOM   3317 O O     . GLY A 1 426 ? 26.257 -4.887  -29.721 1.00 46.07  ? 426 GLY A O     1 
ATOM   3318 N N     . TRP A 1 427 ? 25.151 -5.755  -31.481 1.00 34.54  ? 427 TRP A N     1 
ATOM   3319 C CA    . TRP A 1 427 ? 25.780 -4.864  -32.445 1.00 32.81  ? 427 TRP A CA    1 
ATOM   3320 C C     . TRP A 1 427 ? 24.698 -4.173  -33.276 1.00 31.55  ? 427 TRP A C     1 
ATOM   3321 O O     . TRP A 1 427 ? 24.648 -2.948  -33.322 1.00 33.82  ? 427 TRP A O     1 
ATOM   3322 C CB    . TRP A 1 427 ? 26.837 -5.580  -33.293 1.00 32.30  ? 427 TRP A CB    1 
ATOM   3323 C CG    . TRP A 1 427 ? 27.753 -4.635  -34.028 1.00 38.42  ? 427 TRP A CG    1 
ATOM   3324 C CD1   . TRP A 1 427 ? 27.656 -3.270  -34.084 1.00 38.48  ? 427 TRP A CD1   1 
ATOM   3325 C CD2   . TRP A 1 427 ? 28.885 -4.975  -34.858 1.00 41.96  ? 427 TRP A CD2   1 
ATOM   3326 N NE1   . TRP A 1 427 ? 28.658 -2.740  -34.852 1.00 40.68  ? 427 TRP A NE1   1 
ATOM   3327 C CE2   . TRP A 1 427 ? 29.419 -3.762  -35.355 1.00 44.26  ? 427 TRP A CE2   1 
ATOM   3328 C CE3   . TRP A 1 427 ? 29.517 -6.175  -35.221 1.00 43.84  ? 427 TRP A CE3   1 
ATOM   3329 C CZ2   . TRP A 1 427 ? 30.547 -3.728  -36.180 1.00 43.60  ? 427 TRP A CZ2   1 
ATOM   3330 C CZ3   . TRP A 1 427 ? 30.637 -6.138  -36.024 1.00 39.79  ? 427 TRP A CZ3   1 
ATOM   3331 C CH2   . TRP A 1 427 ? 31.137 -4.932  -36.505 1.00 39.91  ? 427 TRP A CH2   1 
ATOM   3332 N N     . ARG A 1 428 ? 23.789 -4.951  -33.873 1.00 28.15  ? 428 ARG A N     1 
ATOM   3333 C CA    . ARG A 1 428 ? 22.684 -4.386  -34.628 1.00 25.03  ? 428 ARG A CA    1 
ATOM   3334 C C     . ARG A 1 428 ? 21.365 -4.907  -34.079 1.00 23.11  ? 428 ARG A C     1 
ATOM   3335 O O     . ARG A 1 428 ? 20.322 -4.686  -34.694 1.00 20.98  ? 428 ARG A O     1 
ATOM   3336 C CB    . ARG A 1 428 ? 22.860 -4.732  -36.113 1.00 23.94  ? 428 ARG A CB    1 
ATOM   3337 C CG    . ARG A 1 428 ? 23.853 -3.818  -36.814 1.00 25.87  ? 428 ARG A CG    1 
ATOM   3338 C CD    . ARG A 1 428 ? 24.504 -4.436  -38.040 1.00 28.92  ? 428 ARG A CD    1 
ATOM   3339 N NE    . ARG A 1 428 ? 25.237 -3.466  -38.854 1.00 26.90  ? 428 ARG A NE    1 
ATOM   3340 C CZ    . ARG A 1 428 ? 26.529 -3.202  -38.750 1.00 26.84  ? 428 ARG A CZ    1 
ATOM   3341 N NH1   . ARG A 1 428 ? 27.216 -3.761  -37.780 1.00 28.90  ? 428 ARG A NH1   1 
ATOM   3342 N NH2   . ARG A 1 428 ? 27.121 -2.362  -39.591 1.00 26.51  ? 428 ARG A NH2   1 
ATOM   3343 N N     . ASP A 1 429 ? 21.412 -5.588  -32.927 1.00 23.36  ? 429 ASP A N     1 
ATOM   3344 C CA    . ASP A 1 429 ? 20.242 -6.324  -32.482 1.00 27.39  ? 429 ASP A CA    1 
ATOM   3345 C C     . ASP A 1 429 ? 19.803 -5.852  -31.105 1.00 31.54  ? 429 ASP A C     1 
ATOM   3346 O O     . ASP A 1 429 ? 20.602 -5.766  -30.177 1.00 32.47  ? 429 ASP A O     1 
ATOM   3347 C CB    . ASP A 1 429 ? 20.464 -7.844  -32.460 1.00 29.00  ? 429 ASP A CB    1 
ATOM   3348 C CG    . ASP A 1 429 ? 21.557 -8.282  -31.501 1.00 29.06  ? 429 ASP A CG    1 
ATOM   3349 O OD1   . ASP A 1 429 ? 22.667 -7.782  -31.643 1.00 29.76  ? 429 ASP A OD1   1 
ATOM   3350 O OD2   . ASP A 1 429 ? 21.267 -9.058  -30.603 1.00 29.57  ? 429 ASP A OD2   1 
ATOM   3351 N N     . LEU A 1 430 ? 18.495 -5.633  -30.996 1.00 39.91  ? 430 LEU A N     1 
ATOM   3352 C CA    . LEU A 1 430 ? 17.821 -5.441  -29.727 1.00 48.76  ? 430 LEU A CA    1 
ATOM   3353 C C     . LEU A 1 430 ? 17.283 -6.794  -29.246 1.00 57.47  ? 430 LEU A C     1 
ATOM   3354 O O     . LEU A 1 430 ? 16.504 -7.432  -29.972 1.00 45.51  ? 430 LEU A O     1 
ATOM   3355 C CB    . LEU A 1 430 ? 16.697 -4.429  -29.976 1.00 47.14  ? 430 LEU A CB    1 
ATOM   3356 C CG    . LEU A 1 430 ? 16.093 -3.783  -28.734 1.00 48.59  ? 430 LEU A CG    1 
ATOM   3357 C CD1   . LEU A 1 430 ? 17.140 -2.969  -27.968 1.00 44.01  ? 430 LEU A CD1   1 
ATOM   3358 C CD2   . LEU A 1 430 ? 14.907 -2.909  -29.131 1.00 51.74  ? 430 LEU A CD2   1 
ATOM   3359 N N     . HIS A 1 431 ? 17.737 -7.195  -28.039 1.00 57.85  ? 431 HIS A N     1 
ATOM   3360 C CA    . HIS A 1 431 ? 17.318 -8.399  -27.324 1.00 62.18  ? 431 HIS A CA    1 
ATOM   3361 C C     . HIS A 1 431 ? 16.468 -8.117  -26.069 1.00 66.90  ? 431 HIS A C     1 
ATOM   3362 O O     . HIS A 1 431 ? 16.815 -8.626  -25.004 1.00 73.77  ? 431 HIS A O     1 
ATOM   3363 C CB    . HIS A 1 431 ? 18.519 -9.079  -26.652 1.00 61.86  ? 431 HIS A CB    1 
ATOM   3364 C CG    . HIS A 1 431 ? 19.422 -9.892  -27.503 1.00 72.28  ? 431 HIS A CG    1 
ATOM   3365 N ND1   . HIS A 1 431 ? 20.543 -10.481 -26.939 1.00 72.87  ? 431 HIS A ND1   1 
ATOM   3366 C CD2   . HIS A 1 431 ? 19.405 -10.245 -28.792 1.00 67.01  ? 431 HIS A CD2   1 
ATOM   3367 C CE1   . HIS A 1 431 ? 21.189 -11.169 -27.874 1.00 75.66  ? 431 HIS A CE1   1 
ATOM   3368 N NE2   . HIS A 1 431 ? 20.514 -11.040 -29.008 1.00 77.98  ? 431 HIS A NE2   1 
ATOM   3369 N N     . HIS A 1 432 ? 15.378 -7.329  -26.153 1.00 53.04  ? 432 HIS A N     1 
ATOM   3370 C CA    . HIS A 1 432 ? 14.422 -7.201  -25.052 1.00 56.44  ? 432 HIS A CA    1 
ATOM   3371 C C     . HIS A 1 432 ? 14.192 -8.486  -24.247 1.00 57.84  ? 432 HIS A C     1 
ATOM   3372 O O     . HIS A 1 432 ? 13.336 -9.289  -24.606 1.00 54.97  ? 432 HIS A O     1 
ATOM   3373 C CB    . HIS A 1 432 ? 13.000 -6.883  -25.526 1.00 56.68  ? 432 HIS A CB    1 
ATOM   3374 C CG    . HIS A 1 432 ? 12.013 -6.944  -24.403 1.00 61.51  ? 432 HIS A CG    1 
ATOM   3375 N ND1   . HIS A 1 432 ? 12.433 -7.132  -23.104 1.00 68.63  ? 432 HIS A ND1   1 
ATOM   3376 C CD2   . HIS A 1 432 ? 10.683 -6.859  -24.341 1.00 63.64  ? 432 HIS A CD2   1 
ATOM   3377 C CE1   . HIS A 1 432 ? 11.378 -7.136  -22.300 1.00 69.04  ? 432 HIS A CE1   1 
ATOM   3378 N NE2   . HIS A 1 432 ? 10.304 -6.980  -23.028 1.00 55.37  ? 432 HIS A NE2   1 
ATOM   3379 N N     . VAL A 1 433 ? 14.879 -8.606  -23.100 1.00 61.10  ? 433 VAL A N     1 
ATOM   3380 C CA    . VAL A 1 433 ? 14.788 -9.772  -22.238 1.00 64.50  ? 433 VAL A CA    1 
ATOM   3381 C C     . VAL A 1 433 ? 13.798 -9.508  -21.105 1.00 71.23  ? 433 VAL A C     1 
ATOM   3382 O O     . VAL A 1 433 ? 13.953 -8.551  -20.353 1.00 72.50  ? 433 VAL A O     1 
ATOM   3383 C CB    . VAL A 1 433 ? 16.150 -10.134 -21.631 1.00 60.06  ? 433 VAL A CB    1 
ATOM   3384 C CG1   . VAL A 1 433 ? 16.059 -11.420 -20.829 1.00 56.91  ? 433 VAL A CG1   1 
ATOM   3385 C CG2   . VAL A 1 433 ? 17.239 -10.221 -22.687 1.00 65.02  ? 433 VAL A CG2   1 
ATOM   3386 N N     . THR A 1 434 ? 12.819 -10.410 -20.966 1.00 65.50  ? 434 THR A N     1 
ATOM   3387 C CA    . THR A 1 434 ? 11.975 -10.495 -19.789 1.00 54.46  ? 434 THR A CA    1 
ATOM   3388 C C     . THR A 1 434 ? 12.538 -11.534 -18.824 1.00 52.83  ? 434 THR A C     1 
ATOM   3389 O O     . THR A 1 434 ? 12.902 -12.635 -19.236 1.00 43.21  ? 434 THR A O     1 
ATOM   3390 C CB    . THR A 1 434 ? 10.564 -10.931 -20.175 1.00 53.69  ? 434 THR A CB    1 
ATOM   3391 O OG1   . THR A 1 434 ? 10.207 -10.164 -21.321 1.00 56.79  ? 434 THR A OG1   1 
ATOM   3392 C CG2   . THR A 1 434 ? 9.560  -10.752 -19.056 1.00 55.33  ? 434 THR A CG2   1 
ATOM   3393 N N     . VAL A 1 435 ? 12.581 -11.191 -17.531 1.00 50.44  ? 435 VAL A N     1 
ATOM   3394 C CA    . VAL A 1 435 ? 12.967 -12.156 -16.511 1.00 47.86  ? 435 VAL A CA    1 
ATOM   3395 C C     . VAL A 1 435 ? 11.831 -12.266 -15.493 1.00 45.77  ? 435 VAL A C     1 
ATOM   3396 O O     . VAL A 1 435 ? 11.326 -11.263 -14.984 1.00 44.26  ? 435 VAL A O     1 
ATOM   3397 C CB    . VAL A 1 435 ? 14.347 -11.816 -15.913 1.00 49.38  ? 435 VAL A CB    1 
ATOM   3398 C CG1   . VAL A 1 435 ? 14.822 -10.450 -16.361 1.00 52.48  ? 435 VAL A CG1   1 
ATOM   3399 C CG2   . VAL A 1 435 ? 14.419 -11.950 -14.400 1.00 49.30  ? 435 VAL A CG2   1 
ATOM   3400 N N     . ILE A 1 436 ? 11.371 -13.502 -15.286 1.00 36.93  ? 436 ILE A N     1 
ATOM   3401 C CA    . ILE A 1 436 ? 10.185 -13.753 -14.490 1.00 37.73  ? 436 ILE A CA    1 
ATOM   3402 C C     . ILE A 1 436 ? 10.595 -14.569 -13.270 1.00 36.00  ? 436 ILE A C     1 
ATOM   3403 O O     . ILE A 1 436 ? 11.012 -15.719 -13.408 1.00 37.82  ? 436 ILE A O     1 
ATOM   3404 C CB    . ILE A 1 436 ? 9.112  -14.475 -15.323 1.00 38.05  ? 436 ILE A CB    1 
ATOM   3405 C CG1   . ILE A 1 436 ? 9.001  -13.888 -16.731 1.00 39.54  ? 436 ILE A CG1   1 
ATOM   3406 C CG2   . ILE A 1 436 ? 7.770  -14.462 -14.613 1.00 36.00  ? 436 ILE A CG2   1 
ATOM   3407 C CD1   . ILE A 1 436 ? 8.122  -14.716 -17.642 1.00 39.69  ? 436 ILE A CD1   1 
ATOM   3408 N N     . VAL A 1 437 ? 10.493 -13.941 -12.094 1.00 32.32  ? 437 VAL A N     1 
ATOM   3409 C CA    . VAL A 1 437 ? 10.800 -14.594 -10.838 1.00 32.57  ? 437 VAL A CA    1 
ATOM   3410 C C     . VAL A 1 437 ? 9.513  -15.159 -10.254 1.00 32.04  ? 437 VAL A C     1 
ATOM   3411 O O     . VAL A 1 437 ? 8.522  -14.457 -10.147 1.00 34.67  ? 437 VAL A O     1 
ATOM   3412 C CB    . VAL A 1 437 ? 11.453 -13.624 -9.848  1.00 34.23  ? 437 VAL A CB    1 
ATOM   3413 C CG1   . VAL A 1 437 ? 11.748 -14.317 -8.537  1.00 34.20  ? 437 VAL A CG1   1 
ATOM   3414 C CG2   . VAL A 1 437 ? 12.708 -12.987 -10.409 1.00 34.24  ? 437 VAL A CG2   1 
ATOM   3415 N N     . TYR A 1 438 ? 9.545  -16.435 -9.872  1.00 33.21  ? 438 TYR A N     1 
ATOM   3416 C CA    . TYR A 1 438 ? 8.363  -17.128 -9.389  1.00 37.29  ? 438 TYR A CA    1 
ATOM   3417 C C     . TYR A 1 438 ? 8.737  -18.132 -8.294  1.00 45.59  ? 438 TYR A C     1 
ATOM   3418 O O     . TYR A 1 438 ? 9.906  -18.520 -8.168  1.00 47.45  ? 438 TYR A O     1 
ATOM   3419 C CB    . TYR A 1 438 ? 7.692  -17.856 -10.549 1.00 37.27  ? 438 TYR A CB    1 
ATOM   3420 C CG    . TYR A 1 438 ? 8.568  -18.891 -11.214 1.00 37.60  ? 438 TYR A CG    1 
ATOM   3421 C CD1   . TYR A 1 438 ? 9.626  -18.532 -12.047 1.00 35.76  ? 438 TYR A CD1   1 
ATOM   3422 C CD2   . TYR A 1 438 ? 8.342  -20.239 -10.997 1.00 36.10  ? 438 TYR A CD2   1 
ATOM   3423 C CE1   . TYR A 1 438 ? 10.434 -19.491 -12.638 1.00 38.03  ? 438 TYR A CE1   1 
ATOM   3424 C CE2   . TYR A 1 438 ? 9.119  -21.208 -11.607 1.00 38.43  ? 438 TYR A CE2   1 
ATOM   3425 C CZ    . TYR A 1 438 ? 10.177 -20.836 -12.418 1.00 38.49  ? 438 TYR A CZ    1 
ATOM   3426 O OH    . TYR A 1 438 ? 10.901 -21.826 -13.017 1.00 35.76  ? 438 TYR A OH    1 
ATOM   3427 N N     . ASP A 1 439 ? 7.720  -18.561 -7.525  1.00 48.59  ? 439 ASP A N     1 
ATOM   3428 C CA    . ASP A 1 439 ? 7.877  -19.562 -6.483  1.00 45.28  ? 439 ASP A CA    1 
ATOM   3429 C C     . ASP A 1 439 ? 7.810  -20.949 -7.122  1.00 43.41  ? 439 ASP A C     1 
ATOM   3430 O O     . ASP A 1 439 ? 6.728  -21.470 -7.363  1.00 43.58  ? 439 ASP A O     1 
ATOM   3431 C CB    . ASP A 1 439 ? 6.808  -19.363 -5.408  1.00 48.66  ? 439 ASP A CB    1 
ATOM   3432 C CG    . ASP A 1 439 ? 6.854  -20.340 -4.243  1.00 50.23  ? 439 ASP A CG    1 
ATOM   3433 O OD1   . ASP A 1 439 ? 7.605  -21.341 -4.308  1.00 46.48  ? 439 ASP A OD1   1 
ATOM   3434 O OD2   . ASP A 1 439 ? 6.128  -20.089 -3.281  1.00 53.82  ? 439 ASP A OD2   1 
ATOM   3435 N N     . LYS A 1 440 ? 8.983  -21.541 -7.374  1.00 43.38  ? 440 LYS A N     1 
ATOM   3436 C CA    . LYS A 1 440 ? 9.110  -22.798 -8.095  1.00 46.72  ? 440 LYS A CA    1 
ATOM   3437 C C     . LYS A 1 440 ? 8.520  -23.971 -7.307  1.00 44.40  ? 440 LYS A C     1 
ATOM   3438 O O     . LYS A 1 440 ? 8.310  -25.035 -7.875  1.00 44.40  ? 440 LYS A O     1 
ATOM   3439 C CB    . LYS A 1 440 ? 10.594 -23.063 -8.361  1.00 55.06  ? 440 LYS A CB    1 
ATOM   3440 C CG    . LYS A 1 440 ? 11.409 -23.380 -7.112  1.00 66.19  ? 440 LYS A CG    1 
ATOM   3441 C CD    . LYS A 1 440 ? 12.809 -22.801 -7.117  1.00 82.17  ? 440 LYS A CD    1 
ATOM   3442 C CE    . LYS A 1 440 ? 13.403 -22.593 -5.734  1.00 89.16  ? 440 LYS A CE    1 
ATOM   3443 N NZ    . LYS A 1 440 ? 13.422 -23.849 -4.948  1.00 92.05  ? 440 LYS A NZ    1 
ATOM   3444 N N     . THR A 1 441 ? 8.305  -23.803 -5.993  1.00 45.38  ? 441 THR A N     1 
ATOM   3445 C CA    . THR A 1 441 ? 7.782  -24.869 -5.138  1.00 43.77  ? 441 THR A CA    1 
ATOM   3446 C C     . THR A 1 441 ? 6.255  -24.940 -5.232  1.00 44.51  ? 441 THR A C     1 
ATOM   3447 O O     . THR A 1 441 ? 5.662  -25.938 -4.845  1.00 44.30  ? 441 THR A O     1 
ATOM   3448 C CB    . THR A 1 441 ? 8.176  -24.674 -3.665  1.00 39.72  ? 441 THR A CB    1 
ATOM   3449 O OG1   . THR A 1 441 ? 7.414  -23.569 -3.187  1.00 43.03  ? 441 THR A OG1   1 
ATOM   3450 C CG2   . THR A 1 441 ? 9.647  -24.400 -3.429  1.00 36.66  ? 441 THR A CG2   1 
ATOM   3451 N N     . ASP A 1 442 ? 5.631  -23.888 -5.779  1.00 48.34  ? 442 ASP A N     1 
ATOM   3452 C CA    . ASP A 1 442 ? 4.190  -23.686 -5.746  1.00 45.36  ? 442 ASP A CA    1 
ATOM   3453 C C     . ASP A 1 442 ? 3.541  -24.132 -7.062  1.00 44.17  ? 442 ASP A C     1 
ATOM   3454 O O     . ASP A 1 442 ? 3.648  -23.447 -8.077  1.00 43.63  ? 442 ASP A O     1 
ATOM   3455 C CB    . ASP A 1 442 ? 3.925  -22.203 -5.478  1.00 46.96  ? 442 ASP A CB    1 
ATOM   3456 C CG    . ASP A 1 442 ? 2.495  -21.867 -5.098  1.00 49.11  ? 442 ASP A CG    1 
ATOM   3457 O OD1   . ASP A 1 442 ? 1.566  -22.493 -5.664  1.00 46.01  ? 442 ASP A OD1   1 
ATOM   3458 O OD2   . ASP A 1 442 ? 2.333  -20.944 -4.270  1.00 50.61  ? 442 ASP A OD2   1 
ATOM   3459 N N     . PRO A 1 443 ? 2.791  -25.257 -7.100  1.00 45.61  ? 443 PRO A N     1 
ATOM   3460 C CA    . PRO A 1 443 ? 2.135  -25.709 -8.330  1.00 46.64  ? 443 PRO A CA    1 
ATOM   3461 C C     . PRO A 1 443 ? 1.220  -24.711 -9.035  1.00 50.62  ? 443 PRO A C     1 
ATOM   3462 O O     . PRO A 1 443 ? 1.064  -24.786 -10.256 1.00 48.97  ? 443 PRO A O     1 
ATOM   3463 C CB    . PRO A 1 443 ? 1.265  -26.883 -7.861  1.00 44.75  ? 443 PRO A CB    1 
ATOM   3464 C CG    . PRO A 1 443 ? 2.009  -27.416 -6.662  1.00 44.59  ? 443 PRO A CG    1 
ATOM   3465 C CD    . PRO A 1 443 ? 2.538  -26.172 -5.977  1.00 44.91  ? 443 PRO A CD    1 
ATOM   3466 N N     . ASP A 1 444 ? 0.587  -23.803 -8.279  1.00 47.30  ? 444 ASP A N     1 
ATOM   3467 C CA    . ASP A 1 444 ? -0.298 -22.838 -8.915  1.00 50.74  ? 444 ASP A CA    1 
ATOM   3468 C C     . ASP A 1 444 ? 0.533  -21.764 -9.617  1.00 47.89  ? 444 ASP A C     1 
ATOM   3469 O O     . ASP A 1 444 ? 0.195  -21.390 -10.734 1.00 48.83  ? 444 ASP A O     1 
ATOM   3470 C CB    . ASP A 1 444 ? -1.326 -22.237 -7.948  1.00 56.93  ? 444 ASP A CB    1 
ATOM   3471 C CG    . ASP A 1 444 ? -2.201 -23.268 -7.249  1.00 60.29  ? 444 ASP A CG    1 
ATOM   3472 O OD1   . ASP A 1 444 ? -2.675 -24.212 -7.928  1.00 57.60  ? 444 ASP A OD1   1 
ATOM   3473 O OD2   . ASP A 1 444 ? -2.403 -23.118 -6.029  1.00 62.38  ? 444 ASP A OD2   1 
ATOM   3474 N N     . GLU A 1 445 ? 1.599  -21.268 -8.966  1.00 45.36  ? 445 GLU A N     1 
ATOM   3475 C CA    . GLU A 1 445 ? 2.507  -20.315 -9.586  1.00 46.59  ? 445 GLU A CA    1 
ATOM   3476 C C     . GLU A 1 445 ? 3.111  -20.894 -10.873 1.00 45.48  ? 445 GLU A C     1 
ATOM   3477 O O     . GLU A 1 445 ? 3.190  -20.194 -11.887 1.00 36.88  ? 445 GLU A O     1 
ATOM   3478 C CB    . GLU A 1 445 ? 3.602  -19.888 -8.611  1.00 49.00  ? 445 GLU A CB    1 
ATOM   3479 C CG    . GLU A 1 445 ? 3.177  -18.794 -7.645  1.00 56.87  ? 445 GLU A CG    1 
ATOM   3480 C CD    . GLU A 1 445 ? 3.588  -17.388 -8.060  1.00 63.03  ? 445 GLU A CD    1 
ATOM   3481 O OE1   . GLU A 1 445 ? 4.815  -17.022 -7.870  1.00 57.06  ? 445 GLU A OE1   1 
ATOM   3482 O OE2   . GLU A 1 445 ? 2.690  -16.659 -8.582  1.00 57.13  ? 445 GLU A OE2   1 
ATOM   3483 N N     . ARG A 1 446 ? 3.520  -22.172 -10.834 1.00 45.71  ? 446 ARG A N     1 
ATOM   3484 C CA    . ARG A 1 446 ? 4.133  -22.817 -11.986 1.00 44.88  ? 446 ARG A CA    1 
ATOM   3485 C C     . ARG A 1 446 ? 3.149  -22.871 -13.145 1.00 46.08  ? 446 ARG A C     1 
ATOM   3486 O O     . ARG A 1 446 ? 3.519  -22.542 -14.268 1.00 50.35  ? 446 ARG A O     1 
ATOM   3487 C CB    . ARG A 1 446 ? 4.642  -24.213 -11.634 1.00 41.07  ? 446 ARG A CB    1 
ATOM   3488 C CG    . ARG A 1 446 ? 5.839  -24.167 -10.698 1.00 42.50  ? 446 ARG A CG    1 
ATOM   3489 C CD    . ARG A 1 446 ? 6.517  -25.509 -10.582 1.00 43.73  ? 446 ARG A CD    1 
ATOM   3490 N NE    . ARG A 1 446 ? 5.583  -26.508 -10.081 1.00 48.49  ? 446 ARG A NE    1 
ATOM   3491 C CZ    . ARG A 1 446 ? 5.791  -27.284 -9.023  1.00 48.96  ? 446 ARG A CZ    1 
ATOM   3492 N NH1   . ARG A 1 446 ? 6.874  -27.134 -8.276  1.00 48.16  ? 446 ARG A NH1   1 
ATOM   3493 N NH2   . ARG A 1 446 ? 4.902  -28.213 -8.719  1.00 50.05  ? 446 ARG A NH2   1 
ATOM   3494 N N     . LYS A 1 447 ? 1.904  -23.250 -12.842 1.00 47.81  ? 447 LYS A N     1 
ATOM   3495 C CA    . LYS A 1 447 ? 0.864  -23.378 -13.845 1.00 47.76  ? 447 LYS A CA    1 
ATOM   3496 C C     . LYS A 1 447 ? 0.693  -22.050 -14.570 1.00 44.46  ? 447 LYS A C     1 
ATOM   3497 O O     . LYS A 1 447 ? 0.611  -22.035 -15.788 1.00 47.50  ? 447 LYS A O     1 
ATOM   3498 C CB    . LYS A 1 447 ? -0.458 -23.812 -13.211 1.00 54.78  ? 447 LYS A CB    1 
ATOM   3499 C CG    . LYS A 1 447 ? -1.494 -24.364 -14.183 1.00 64.23  ? 447 LYS A CG    1 
ATOM   3500 C CD    . LYS A 1 447 ? -2.943 -24.180 -13.738 1.00 73.58  ? 447 LYS A CD    1 
ATOM   3501 C CE    . LYS A 1 447 ? -3.420 -22.742 -13.849 1.00 81.68  ? 447 LYS A CE    1 
ATOM   3502 N NZ    . LYS A 1 447 ? -4.886 -22.660 -14.061 1.00 80.95  ? 447 LYS A NZ    1 
ATOM   3503 N N     . LYS A 1 448 ? 0.639  -20.937 -13.832 1.00 45.00  ? 448 LYS A N     1 
ATOM   3504 C CA    . LYS A 1 448 ? 0.333  -19.664 -14.469 1.00 50.18  ? 448 LYS A CA    1 
ATOM   3505 C C     . LYS A 1 448 ? 1.587  -19.070 -15.109 1.00 47.72  ? 448 LYS A C     1 
ATOM   3506 O O     . LYS A 1 448 ? 1.464  -18.313 -16.068 1.00 44.11  ? 448 LYS A O     1 
ATOM   3507 C CB    . LYS A 1 448 ? -0.395 -18.663 -13.554 1.00 54.31  ? 448 LYS A CB    1 
ATOM   3508 C CG    . LYS A 1 448 ? 0.182  -18.389 -12.175 1.00 59.21  ? 448 LYS A CG    1 
ATOM   3509 C CD    . LYS A 1 448 ? -0.895 -18.000 -11.165 1.00 60.89  ? 448 LYS A CD    1 
ATOM   3510 C CE    . LYS A 1 448 ? -1.202 -16.521 -11.123 1.00 62.46  ? 448 LYS A CE    1 
ATOM   3511 N NZ    . LYS A 1 448 ? -0.214 -15.802 -10.283 1.00 66.86  ? 448 LYS A NZ    1 
ATOM   3512 N N     . LEU A 1 449 ? 2.776  -19.433 -14.613 1.00 43.32  ? 449 LEU A N     1 
ATOM   3513 C CA    . LEU A 1 449 ? 3.996  -19.149 -15.350 1.00 42.34  ? 449 LEU A CA    1 
ATOM   3514 C C     . LEU A 1 449 ? 3.926  -19.767 -16.748 1.00 41.74  ? 449 LEU A C     1 
ATOM   3515 O O     . LEU A 1 449 ? 4.105  -19.056 -17.733 1.00 42.69  ? 449 LEU A O     1 
ATOM   3516 C CB    . LEU A 1 449 ? 5.222  -19.677 -14.604 1.00 41.72  ? 449 LEU A CB    1 
ATOM   3517 C CG    . LEU A 1 449 ? 6.541  -19.375 -15.312 1.00 40.23  ? 449 LEU A CG    1 
ATOM   3518 C CD1   . LEU A 1 449 ? 6.901  -17.898 -15.182 1.00 40.41  ? 449 LEU A CD1   1 
ATOM   3519 C CD2   . LEU A 1 449 ? 7.643  -20.254 -14.780 1.00 37.78  ? 449 LEU A CD2   1 
ATOM   3520 N N     . ASP A 1 450 ? 3.668  -21.081 -16.826 1.00 41.47  ? 450 ASP A N     1 
ATOM   3521 C CA    . ASP A 1 450 ? 3.636  -21.786 -18.097 1.00 40.43  ? 450 ASP A CA    1 
ATOM   3522 C C     . ASP A 1 450 ? 2.669  -21.093 -19.057 1.00 40.45  ? 450 ASP A C     1 
ATOM   3523 O O     . ASP A 1 450 ? 2.972  -20.850 -20.224 1.00 41.23  ? 450 ASP A O     1 
ATOM   3524 C CB    . ASP A 1 450 ? 3.275  -23.255 -17.902 1.00 44.88  ? 450 ASP A CB    1 
ATOM   3525 C CG    . ASP A 1 450 ? 3.394  -24.070 -19.178 1.00 51.78  ? 450 ASP A CG    1 
ATOM   3526 O OD1   . ASP A 1 450 ? 4.527  -24.318 -19.617 1.00 54.89  ? 450 ASP A OD1   1 
ATOM   3527 O OD2   . ASP A 1 450 ? 2.347  -24.415 -19.745 1.00 67.24  ? 450 ASP A OD2   1 
ATOM   3528 N N     . GLU A 1 451 ? 1.502  -20.739 -18.541 1.00 41.44  ? 451 GLU A N     1 
ATOM   3529 C CA    . GLU A 1 451 ? 0.440  -20.165 -19.341 1.00 41.61  ? 451 GLU A CA    1 
ATOM   3530 C C     . GLU A 1 451 ? 0.881  -18.793 -19.877 1.00 40.52  ? 451 GLU A C     1 
ATOM   3531 O O     . GLU A 1 451 ? 0.596  -18.449 -21.028 1.00 43.04  ? 451 GLU A O     1 
ATOM   3532 C CB    . GLU A 1 451 ? -0.814 -20.174 -18.459 1.00 45.05  ? 451 GLU A CB    1 
ATOM   3533 C CG    . GLU A 1 451 ? -2.119 -19.970 -19.210 1.00 53.74  ? 451 GLU A CG    1 
ATOM   3534 C CD    . GLU A 1 451 ? -3.302 -19.772 -18.276 1.00 58.18  ? 451 GLU A CD    1 
ATOM   3535 O OE1   . GLU A 1 451 ? -3.435 -20.631 -17.352 1.00 53.93  ? 451 GLU A OE1   1 
ATOM   3536 O OE2   . GLU A 1 451 ? -4.046 -18.739 -18.442 1.00 43.30  ? 451 GLU A OE2   1 
ATOM   3537 N N     . LEU A 1 452 ? 1.629  -18.035 -19.056 1.00 39.13  ? 452 LEU A N     1 
ATOM   3538 C CA    . LEU A 1 452 ? 2.135  -16.723 -19.432 1.00 36.79  ? 452 LEU A CA    1 
ATOM   3539 C C     . LEU A 1 452 ? 3.243  -16.864 -20.466 1.00 34.23  ? 452 LEU A C     1 
ATOM   3540 O O     . LEU A 1 452 ? 3.303  -16.097 -21.412 1.00 33.35  ? 452 LEU A O     1 
ATOM   3541 C CB    . LEU A 1 452 ? 2.676  -15.996 -18.196 1.00 37.39  ? 452 LEU A CB    1 
ATOM   3542 C CG    . LEU A 1 452 ? 3.450  -14.708 -18.479 1.00 35.02  ? 452 LEU A CG    1 
ATOM   3543 C CD1   . LEU A 1 452 ? 2.539  -13.642 -19.020 1.00 34.25  ? 452 LEU A CD1   1 
ATOM   3544 C CD2   . LEU A 1 452 ? 4.155  -14.202 -17.234 1.00 36.32  ? 452 LEU A CD2   1 
ATOM   3545 N N     . PHE A 1 453 ? 4.152  -17.809 -20.241 1.00 33.74  ? 453 PHE A N     1 
ATOM   3546 C CA    . PHE A 1 453 ? 5.253  -17.998 -21.162 1.00 36.91  ? 453 PHE A CA    1 
ATOM   3547 C C     . PHE A 1 453 ? 4.700  -18.292 -22.552 1.00 36.09  ? 453 PHE A C     1 
ATOM   3548 O O     . PHE A 1 453 ? 5.067  -17.613 -23.510 1.00 34.54  ? 453 PHE A O     1 
ATOM   3549 C CB    . PHE A 1 453 ? 6.224  -19.071 -20.664 1.00 36.30  ? 453 PHE A CB    1 
ATOM   3550 C CG    . PHE A 1 453 ? 7.585  -18.967 -21.298 1.00 36.72  ? 453 PHE A CG    1 
ATOM   3551 C CD1   . PHE A 1 453 ? 7.836  -19.513 -22.550 1.00 38.48  ? 453 PHE A CD1   1 
ATOM   3552 C CD2   . PHE A 1 453 ? 8.597  -18.265 -20.672 1.00 38.31  ? 453 PHE A CD2   1 
ATOM   3553 C CE1   . PHE A 1 453 ? 9.084  -19.391 -23.143 1.00 34.56  ? 453 PHE A CE1   1 
ATOM   3554 C CE2   . PHE A 1 453 ? 9.849  -18.160 -21.260 1.00 40.05  ? 453 PHE A CE2   1 
ATOM   3555 C CZ    . PHE A 1 453 ? 10.085 -18.711 -22.499 1.00 36.48  ? 453 PHE A CZ    1 
ATOM   3556 N N     . ASN A 1 454 ? 3.779  -19.257 -22.639 1.00 38.83  ? 454 ASN A N     1 
ATOM   3557 C CA    . ASN A 1 454 ? 3.208  -19.644 -23.923 1.00 42.26  ? 454 ASN A CA    1 
ATOM   3558 C C     . ASN A 1 454 ? 2.568  -18.430 -24.602 1.00 40.35  ? 454 ASN A C     1 
ATOM   3559 O O     . ASN A 1 454 ? 2.716  -18.252 -25.802 1.00 45.44  ? 454 ASN A O     1 
ATOM   3560 C CB    . ASN A 1 454 ? 2.261  -20.845 -23.799 1.00 42.53  ? 454 ASN A CB    1 
ATOM   3561 C CG    . ASN A 1 454 ? 2.976  -22.127 -23.422 1.00 44.64  ? 454 ASN A CG    1 
ATOM   3562 O OD1   . ASN A 1 454 ? 3.959  -22.504 -24.053 1.00 54.45  ? 454 ASN A OD1   1 
ATOM   3563 N ND2   . ASN A 1 454 ? 2.507  -22.813 -22.393 1.00 48.54  ? 454 ASN A ND2   1 
ATOM   3564 N N     . ILE A 1 455 ? 1.926  -17.544 -23.838 1.00 40.28  ? 455 ILE A N     1 
ATOM   3565 C CA    . ILE A 1 455 ? 1.321  -16.360 -24.425 1.00 37.67  ? 455 ILE A CA    1 
ATOM   3566 C C     . ILE A 1 455 ? 2.393  -15.398 -24.931 1.00 35.89  ? 455 ILE A C     1 
ATOM   3567 O O     . ILE A 1 455 ? 2.228  -14.823 -26.008 1.00 37.95  ? 455 ILE A O     1 
ATOM   3568 C CB    . ILE A 1 455 ? 0.344  -15.682 -23.438 1.00 39.23  ? 455 ILE A CB    1 
ATOM   3569 C CG1   . ILE A 1 455 ? -0.929 -16.508 -23.265 1.00 39.97  ? 455 ILE A CG1   1 
ATOM   3570 C CG2   . ILE A 1 455 ? 0.006  -14.261 -23.866 1.00 39.56  ? 455 ILE A CG2   1 
ATOM   3571 C CD1   . ILE A 1 455 ? -1.697 -16.171 -22.020 1.00 41.29  ? 455 ILE A CD1   1 
ATOM   3572 N N     . LEU A 1 456 ? 3.441  -15.159 -24.140 1.00 31.58  ? 456 LEU A N     1 
ATOM   3573 C CA    . LEU A 1 456 ? 4.503  -14.241 -24.543 1.00 32.76  ? 456 LEU A CA    1 
ATOM   3574 C C     . LEU A 1 456 ? 5.146  -14.644 -25.880 1.00 32.69  ? 456 LEU A C     1 
ATOM   3575 O O     . LEU A 1 456 ? 5.453  -13.776 -26.704 1.00 30.64  ? 456 LEU A O     1 
ATOM   3576 C CB    . LEU A 1 456 ? 5.575  -14.222 -23.453 1.00 31.38  ? 456 LEU A CB    1 
ATOM   3577 C CG    . LEU A 1 456 ? 5.183  -13.579 -22.128 1.00 32.05  ? 456 LEU A CG    1 
ATOM   3578 C CD1   . LEU A 1 456 ? 6.299  -13.762 -21.110 1.00 35.07  ? 456 LEU A CD1   1 
ATOM   3579 C CD2   . LEU A 1 456 ? 4.878  -12.106 -22.292 1.00 30.52  ? 456 LEU A CD2   1 
ATOM   3580 N N     . VAL A 1 457 ? 5.374  -15.957 -26.071 1.00 33.29  ? 457 VAL A N     1 
ATOM   3581 C CA    . VAL A 1 457 ? 5.977  -16.515 -27.280 1.00 35.17  ? 457 VAL A CA    1 
ATOM   3582 C C     . VAL A 1 457 ? 5.065  -16.310 -28.491 1.00 35.81  ? 457 VAL A C     1 
ATOM   3583 O O     . VAL A 1 457 ? 5.507  -15.810 -29.518 1.00 37.36  ? 457 VAL A O     1 
ATOM   3584 C CB    . VAL A 1 457 ? 6.289  -18.013 -27.107 1.00 36.55  ? 457 VAL A CB    1 
ATOM   3585 C CG1   . VAL A 1 457 ? 6.700  -18.669 -28.422 1.00 35.13  ? 457 VAL A CG1   1 
ATOM   3586 C CG2   . VAL A 1 457 ? 7.328  -18.244 -26.018 1.00 35.26  ? 457 VAL A CG2   1 
ATOM   3587 N N     . ASP A 1 458 ? 3.791  -16.689 -28.366 1.00 38.14  ? 458 ASP A N     1 
ATOM   3588 C CA    . ASP A 1 458 ? 2.837  -16.594 -29.467 1.00 41.19  ? 458 ASP A CA    1 
ATOM   3589 C C     . ASP A 1 458 ? 2.648  -15.147 -29.900 1.00 37.99  ? 458 ASP A C     1 
ATOM   3590 O O     . ASP A 1 458 ? 2.555  -14.847 -31.089 1.00 43.44  ? 458 ASP A O     1 
ATOM   3591 C CB    . ASP A 1 458 ? 1.482  -17.203 -29.099 1.00 44.36  ? 458 ASP A CB    1 
ATOM   3592 C CG    . ASP A 1 458 ? 1.528  -18.710 -28.892 1.00 51.32  ? 458 ASP A CG    1 
ATOM   3593 O OD1   . ASP A 1 458 ? 2.639  -19.297 -29.015 1.00 50.80  ? 458 ASP A OD1   1 
ATOM   3594 O OD2   . ASP A 1 458 ? 0.461  -19.288 -28.602 1.00 57.57  ? 458 ASP A OD2   1 
ATOM   3595 N N     . GLU A 1 459 ? 2.612  -14.241 -28.930 1.00 40.83  ? 459 GLU A N     1 
ATOM   3596 C CA    . GLU A 1 459 ? 2.340  -12.847 -29.234 1.00 44.52  ? 459 GLU A CA    1 
ATOM   3597 C C     . GLU A 1 459 ? 3.594  -12.178 -29.789 1.00 41.62  ? 459 GLU A C     1 
ATOM   3598 O O     . GLU A 1 459 ? 3.487  -11.240 -30.573 1.00 46.36  ? 459 GLU A O     1 
ATOM   3599 C CB    . GLU A 1 459 ? 1.769  -12.144 -28.002 1.00 44.84  ? 459 GLU A CB    1 
ATOM   3600 C CG    . GLU A 1 459 ? 0.385  -12.655 -27.645 1.00 45.55  ? 459 GLU A CG    1 
ATOM   3601 C CD    . GLU A 1 459 ? -0.265 -11.910 -26.496 1.00 48.87  ? 459 GLU A CD    1 
ATOM   3602 O OE1   . GLU A 1 459 ? 0.456  -11.292 -25.709 1.00 50.84  ? 459 GLU A OE1   1 
ATOM   3603 O OE2   . GLU A 1 459 ? -1.494 -11.924 -26.426 1.00 59.78  ? 459 GLU A OE2   1 
ATOM   3604 N N     . ALA A 1 460 ? 4.773  -12.669 -29.395 1.00 35.50  ? 460 ALA A N     1 
ATOM   3605 C CA    . ALA A 1 460 ? 6.012  -12.199 -29.989 1.00 34.31  ? 460 ALA A CA    1 
ATOM   3606 C C     . ALA A 1 460 ? 6.129  -12.682 -31.439 1.00 30.43  ? 460 ALA A C     1 
ATOM   3607 O O     . ALA A 1 460 ? 6.406  -11.889 -32.334 1.00 29.19  ? 460 ALA A O     1 
ATOM   3608 C CB    . ALA A 1 460 ? 7.185  -12.637 -29.144 1.00 36.71  ? 460 ALA A CB    1 
ATOM   3609 N N     . ALA A 1 461 ? 5.899  -13.974 -31.687 1.00 28.10  ? 461 ALA A N     1 
ATOM   3610 C CA    . ALA A 1 461 ? 5.982  -14.515 -33.040 1.00 31.44  ? 461 ALA A CA    1 
ATOM   3611 C C     . ALA A 1 461 ? 5.015  -13.801 -33.992 1.00 35.74  ? 461 ALA A C     1 
ATOM   3612 O O     . ALA A 1 461 ? 5.353  -13.555 -35.152 1.00 35.77  ? 461 ALA A O     1 
ATOM   3613 C CB    . ALA A 1 461 ? 5.719  -16.002 -33.029 1.00 29.84  ? 461 ALA A CB    1 
ATOM   3614 N N     . ALA A 1 462 ? 3.804  -13.489 -33.516 1.00 38.05  ? 462 ALA A N     1 
ATOM   3615 C CA    . ALA A 1 462 ? 2.826  -12.784 -34.334 1.00 41.21  ? 462 ALA A CA    1 
ATOM   3616 C C     . ALA A 1 462 ? 3.378  -11.440 -34.798 1.00 41.57  ? 462 ALA A C     1 
ATOM   3617 O O     . ALA A 1 462 ? 2.919  -10.933 -35.812 1.00 41.14  ? 462 ALA A O     1 
ATOM   3618 C CB    . ALA A 1 462 ? 1.535  -12.591 -33.583 1.00 42.24  ? 462 ALA A CB    1 
ATOM   3619 N N     . GLU A 1 463 ? 4.366  -10.874 -34.087 1.00 38.52  ? 463 GLU A N     1 
ATOM   3620 C CA    . GLU A 1 463 ? 4.958  -9.606  -34.500 1.00 38.69  ? 463 GLU A CA    1 
ATOM   3621 C C     . GLU A 1 463 ? 6.274  -9.778  -35.270 1.00 34.04  ? 463 GLU A C     1 
ATOM   3622 O O     . GLU A 1 463 ? 6.972  -8.801  -35.506 1.00 34.44  ? 463 GLU A O     1 
ATOM   3623 C CB    . GLU A 1 463 ? 5.234  -8.742  -33.272 1.00 41.34  ? 463 GLU A CB    1 
ATOM   3624 C CG    . GLU A 1 463 ? 4.016  -8.470  -32.418 1.00 47.20  ? 463 GLU A CG    1 
ATOM   3625 C CD    . GLU A 1 463 ? 2.926  -7.632  -33.070 1.00 51.64  ? 463 GLU A CD    1 
ATOM   3626 O OE1   . GLU A 1 463 ? 3.256  -6.559  -33.672 1.00 44.87  ? 463 GLU A OE1   1 
ATOM   3627 O OE2   . GLU A 1 463 ? 1.745  -8.032  -32.934 1.00 47.95  ? 463 GLU A OE2   1 
ATOM   3628 N N     . GLY A 1 464 ? 6.658  -11.009 -35.616 1.00 33.64  ? 464 GLY A N     1 
ATOM   3629 C CA    . GLY A 1 464 ? 7.968  -11.264 -36.213 1.00 35.60  ? 464 GLY A CA    1 
ATOM   3630 C C     . GLY A 1 464 ? 9.168  -11.223 -35.247 1.00 31.10  ? 464 GLY A C     1 
ATOM   3631 O O     . GLY A 1 464 ? 10.294 -10.995 -35.690 1.00 28.92  ? 464 GLY A O     1 
ATOM   3632 N N     . TYR A 1 465 ? 8.940  -11.466 -33.946 1.00 29.57  ? 465 TYR A N     1 
ATOM   3633 C CA    . TYR A 1 465 ? 9.998  -11.461 -32.937 1.00 28.35  ? 465 TYR A CA    1 
ATOM   3634 C C     . TYR A 1 465 ? 10.281 -12.894 -32.512 1.00 26.01  ? 465 TYR A C     1 
ATOM   3635 O O     . TYR A 1 465 ? 9.373  -13.591 -32.098 1.00 26.37  ? 465 TYR A O     1 
ATOM   3636 C CB    . TYR A 1 465 ? 9.629  -10.680 -31.670 1.00 27.87  ? 465 TYR A CB    1 
ATOM   3637 C CG    . TYR A 1 465 ? 9.299  -9.236  -31.899 1.00 28.82  ? 465 TYR A CG    1 
ATOM   3638 C CD1   . TYR A 1 465 ? 10.000 -8.491  -32.834 1.00 30.14  ? 465 TYR A CD1   1 
ATOM   3639 C CD2   . TYR A 1 465 ? 8.269  -8.607  -31.199 1.00 28.28  ? 465 TYR A CD2   1 
ATOM   3640 C CE1   . TYR A 1 465 ? 9.682  -7.159  -33.080 1.00 29.76  ? 465 TYR A CE1   1 
ATOM   3641 C CE2   . TYR A 1 465 ? 7.960  -7.272  -31.411 1.00 24.86  ? 465 TYR A CE2   1 
ATOM   3642 C CZ    . TYR A 1 465 ? 8.667  -6.547  -32.361 1.00 29.25  ? 465 TYR A CZ    1 
ATOM   3643 O OH    . TYR A 1 465 ? 8.399  -5.222  -32.641 1.00 30.42  ? 465 TYR A OH    1 
ATOM   3644 N N     . GLY A 1 466 ? 11.535 -13.338 -32.663 1.00 27.19  ? 466 GLY A N     1 
ATOM   3645 C CA    . GLY A 1 466 ? 11.911 -14.710 -32.353 1.00 23.98  ? 466 GLY A CA    1 
ATOM   3646 C C     . GLY A 1 466 ? 12.913 -14.773 -31.204 1.00 24.67  ? 466 GLY A C     1 
ATOM   3647 O O     . GLY A 1 466 ? 13.822 -13.942 -31.095 1.00 25.11  ? 466 GLY A O     1 
ATOM   3648 N N     . GLU A 1 467 ? 12.772 -15.818 -30.396 1.00 22.74  ? 467 GLU A N     1 
ATOM   3649 C CA    . GLU A 1 467 ? 13.670 -16.079 -29.292 1.00 26.87  ? 467 GLU A CA    1 
ATOM   3650 C C     . GLU A 1 467 ? 14.955 -16.739 -29.809 1.00 27.18  ? 467 GLU A C     1 
ATOM   3651 O O     . GLU A 1 467 ? 14.914 -17.505 -30.762 1.00 22.49  ? 467 GLU A O     1 
ATOM   3652 C CB    . GLU A 1 467 ? 12.883 -16.924 -28.288 1.00 33.27  ? 467 GLU A CB    1 
ATOM   3653 C CG    . GLU A 1 467 ? 13.700 -17.505 -27.168 1.00 38.88  ? 467 GLU A CG    1 
ATOM   3654 C CD    . GLU A 1 467 ? 14.014 -16.522 -26.056 1.00 51.17  ? 467 GLU A CD    1 
ATOM   3655 O OE1   . GLU A 1 467 ? 14.826 -15.585 -26.348 1.00 42.49  ? 467 GLU A OE1   1 
ATOM   3656 O OE2   . GLU A 1 467 ? 13.473 -16.727 -24.878 1.00 53.63  ? 467 GLU A OE2   1 
ATOM   3657 N N     . TYR A 1 468 ? 16.100 -16.455 -29.157 1.00 30.57  ? 468 TYR A N     1 
ATOM   3658 C CA    . TYR A 1 468 ? 17.396 -16.959 -29.601 1.00 32.72  ? 468 TYR A CA    1 
ATOM   3659 C C     . TYR A 1 468 ? 17.983 -17.987 -28.627 1.00 31.47  ? 468 TYR A C     1 
ATOM   3660 O O     . TYR A 1 468 ? 18.959 -18.669 -28.962 1.00 30.05  ? 468 TYR A O     1 
ATOM   3661 C CB    . TYR A 1 468 ? 18.398 -15.818 -29.799 1.00 33.79  ? 468 TYR A CB    1 
ATOM   3662 C CG    . TYR A 1 468 ? 19.000 -15.319 -28.522 1.00 32.92  ? 468 TYR A CG    1 
ATOM   3663 C CD1   . TYR A 1 468 ? 18.274 -14.504 -27.683 1.00 36.13  ? 468 TYR A CD1   1 
ATOM   3664 C CD2   . TYR A 1 468 ? 20.259 -15.725 -28.118 1.00 35.99  ? 468 TYR A CD2   1 
ATOM   3665 C CE1   . TYR A 1 468 ? 18.805 -14.058 -26.487 1.00 41.32  ? 468 TYR A CE1   1 
ATOM   3666 C CE2   . TYR A 1 468 ? 20.809 -15.297 -26.922 1.00 37.27  ? 468 TYR A CE2   1 
ATOM   3667 C CZ    . TYR A 1 468 ? 20.074 -14.457 -26.103 1.00 41.79  ? 468 TYR A CZ    1 
ATOM   3668 O OH    . TYR A 1 468 ? 20.574 -13.974 -24.927 1.00 40.14  ? 468 TYR A OH    1 
ATOM   3669 N N     . ARG A 1 469 ? 17.375 -18.096 -27.442 1.00 27.48  ? 469 ARG A N     1 
ATOM   3670 C CA    . ARG A 1 469 ? 17.786 -19.042 -26.426 1.00 27.65  ? 469 ARG A CA    1 
ATOM   3671 C C     . ARG A 1 469 ? 16.587 -19.321 -25.524 1.00 29.22  ? 469 ARG A C     1 
ATOM   3672 O O     . ARG A 1 469 ? 15.910 -18.384 -25.147 1.00 32.34  ? 469 ARG A O     1 
ATOM   3673 C CB    . ARG A 1 469 ? 18.941 -18.389 -25.669 1.00 26.55  ? 469 ARG A CB    1 
ATOM   3674 C CG    . ARG A 1 469 ? 19.654 -19.299 -24.690 1.00 27.73  ? 469 ARG A CG    1 
ATOM   3675 C CD    . ARG A 1 469 ? 20.779 -18.559 -23.973 1.00 28.75  ? 469 ARG A CD    1 
ATOM   3676 N NE    . ARG A 1 469 ? 21.448 -19.450 -23.029 1.00 29.75  ? 469 ARG A NE    1 
ATOM   3677 C CZ    . ARG A 1 469 ? 22.381 -19.086 -22.155 1.00 30.79  ? 469 ARG A CZ    1 
ATOM   3678 N NH1   . ARG A 1 469 ? 22.716 -17.817 -22.012 1.00 29.74  ? 469 ARG A NH1   1 
ATOM   3679 N NH2   . ARG A 1 469 ? 22.977 -20.008 -21.416 1.00 33.14  ? 469 ARG A NH2   1 
ATOM   3680 N N     . THR A 1 470 ? 16.328 -20.574 -25.138 1.00 30.00  ? 470 THR A N     1 
ATOM   3681 C CA    . THR A 1 470 ? 15.162 -20.857 -24.303 1.00 29.79  ? 470 THR A CA    1 
ATOM   3682 C C     . THR A 1 470 ? 15.391 -22.030 -23.352 1.00 27.64  ? 470 THR A C     1 
ATOM   3683 O O     . THR A 1 470 ? 16.400 -22.714 -23.395 1.00 27.30  ? 470 THR A O     1 
ATOM   3684 C CB    . THR A 1 470 ? 13.906 -21.120 -25.145 1.00 31.78  ? 470 THR A CB    1 
ATOM   3685 O OG1   . THR A 1 470 ? 12.797 -21.187 -24.242 1.00 33.88  ? 470 THR A OG1   1 
ATOM   3686 C CG2   . THR A 1 470 ? 14.016 -22.378 -25.979 1.00 31.48  ? 470 THR A CG2   1 
ATOM   3687 N N     . HIS A 1 471 ? 14.409 -22.258 -22.485 1.00 29.18  ? 471 HIS A N     1 
ATOM   3688 C CA    . HIS A 1 471 ? 14.458 -23.318 -21.488 1.00 29.31  ? 471 HIS A CA    1 
ATOM   3689 C C     . HIS A 1 471 ? 14.039 -24.620 -22.170 1.00 27.76  ? 471 HIS A C     1 
ATOM   3690 O O     . HIS A 1 471 ? 13.289 -24.598 -23.138 1.00 29.40  ? 471 HIS A O     1 
ATOM   3691 C CB    . HIS A 1 471 ? 13.638 -22.849 -20.278 1.00 30.87  ? 471 HIS A CB    1 
ATOM   3692 C CG    . HIS A 1 471 ? 13.387 -23.830 -19.192 1.00 34.29  ? 471 HIS A CG    1 
ATOM   3693 N ND1   . HIS A 1 471 ? 12.602 -24.958 -19.344 1.00 32.45  ? 471 HIS A ND1   1 
ATOM   3694 C CD2   . HIS A 1 471 ? 13.751 -23.780 -17.900 1.00 32.84  ? 471 HIS A CD2   1 
ATOM   3695 C CE1   . HIS A 1 471 ? 12.522 -25.576 -18.178 1.00 33.53  ? 471 HIS A CE1   1 
ATOM   3696 N NE2   . HIS A 1 471 ? 13.214 -24.882 -17.289 1.00 34.15  ? 471 HIS A NE2   1 
ATOM   3697 N N     . ILE A 1 472 ? 14.560 -25.743 -21.685 1.00 26.88  ? 472 ILE A N     1 
ATOM   3698 C CA    . ILE A 1 472 ? 14.318 -27.046 -22.272 1.00 30.38  ? 472 ILE A CA    1 
ATOM   3699 C C     . ILE A 1 472 ? 12.836 -27.285 -22.510 1.00 32.80  ? 472 ILE A C     1 
ATOM   3700 O O     . ILE A 1 472 ? 12.467 -27.933 -23.494 1.00 32.80  ? 472 ILE A O     1 
ATOM   3701 C CB    . ILE A 1 472 ? 14.911 -28.157 -21.386 1.00 35.06  ? 472 ILE A CB    1 
ATOM   3702 C CG1   . ILE A 1 472 ? 14.417 -28.041 -19.937 1.00 38.86  ? 472 ILE A CG1   1 
ATOM   3703 C CG2   . ILE A 1 472 ? 16.428 -28.155 -21.484 1.00 29.58  ? 472 ILE A CG2   1 
ATOM   3704 C CD1   . ILE A 1 472 ? 14.963 -29.094 -19.000 1.00 39.63  ? 472 ILE A CD1   1 
ATOM   3705 N N     . ARG A 1 473 ? 11.986 -26.779 -21.610 1.00 34.31  ? 473 ARG A N     1 
ATOM   3706 C CA    . ARG A 1 473 ? 10.554 -27.001 -21.733 1.00 35.50  ? 473 ARG A CA    1 
ATOM   3707 C C     . ARG A 1 473 ? 9.977  -26.403 -23.027 1.00 30.62  ? 473 ARG A C     1 
ATOM   3708 O O     . ARG A 1 473 ? 8.970  -26.886 -23.530 1.00 29.34  ? 473 ARG A O     1 
ATOM   3709 C CB    . ARG A 1 473 ? 9.840  -26.451 -20.491 1.00 40.74  ? 473 ARG A CB    1 
ATOM   3710 C CG    . ARG A 1 473 ? 8.321  -26.487 -20.599 1.00 43.00  ? 473 ARG A CG    1 
ATOM   3711 C CD    . ARG A 1 473 ? 7.600  -26.123 -19.321 1.00 46.93  ? 473 ARG A CD    1 
ATOM   3712 N NE    . ARG A 1 473 ? 6.161  -26.335 -19.469 1.00 50.82  ? 473 ARG A NE    1 
ATOM   3713 C CZ    . ARG A 1 473 ? 5.535  -27.510 -19.362 1.00 49.65  ? 473 ARG A CZ    1 
ATOM   3714 N NH1   . ARG A 1 473 ? 6.200  -28.618 -19.076 1.00 48.12  ? 473 ARG A NH1   1 
ATOM   3715 N NH2   . ARG A 1 473 ? 4.227  -27.564 -19.532 1.00 48.99  ? 473 ARG A NH2   1 
ATOM   3716 N N     . TYR A 1 474 ? 10.608 -25.372 -23.591 1.00 30.17  ? 474 TYR A N     1 
ATOM   3717 C CA    . TYR A 1 474 ? 9.991  -24.576 -24.650 1.00 31.50  ? 474 TYR A CA    1 
ATOM   3718 C C     . TYR A 1 474 ? 10.734 -24.698 -25.977 1.00 28.38  ? 474 TYR A C     1 
ATOM   3719 O O     . TYR A 1 474 ? 10.433 -23.990 -26.927 1.00 28.69  ? 474 TYR A O     1 
ATOM   3720 C CB    . TYR A 1 474 ? 9.936  -23.120 -24.183 1.00 33.04  ? 474 TYR A CB    1 
ATOM   3721 C CG    . TYR A 1 474 ? 9.097  -22.953 -22.945 1.00 35.60  ? 474 TYR A CG    1 
ATOM   3722 C CD1   . TYR A 1 474 ? 7.753  -23.305 -22.952 1.00 36.41  ? 474 TYR A CD1   1 
ATOM   3723 C CD2   . TYR A 1 474 ? 9.648  -22.507 -21.756 1.00 40.37  ? 474 TYR A CD2   1 
ATOM   3724 C CE1   . TYR A 1 474 ? 6.965  -23.182 -21.819 1.00 40.75  ? 474 TYR A CE1   1 
ATOM   3725 C CE2   . TYR A 1 474 ? 8.879  -22.391 -20.606 1.00 43.81  ? 474 TYR A CE2   1 
ATOM   3726 C CZ    . TYR A 1 474 ? 7.531  -22.727 -20.638 1.00 44.06  ? 474 TYR A CZ    1 
ATOM   3727 O OH    . TYR A 1 474 ? 6.757  -22.593 -19.514 1.00 40.00  ? 474 TYR A OH    1 
ATOM   3728 N N     . MET A 1 475 ? 11.676 -25.635 -26.054 1.00 30.51  ? 475 MET A N     1 
ATOM   3729 C CA    . MET A 1 475 ? 12.602 -25.706 -27.178 1.00 29.55  ? 475 MET A CA    1 
ATOM   3730 C C     . MET A 1 475 ? 11.862 -26.131 -28.444 1.00 27.96  ? 475 MET A C     1 
ATOM   3731 O O     . MET A 1 475 ? 12.091 -25.570 -29.512 1.00 26.80  ? 475 MET A O     1 
ATOM   3732 C CB    . MET A 1 475 ? 13.749 -26.681 -26.874 1.00 28.93  ? 475 MET A CB    1 
ATOM   3733 C CG    . MET A 1 475 ? 14.866 -26.051 -26.056 1.00 29.60  ? 475 MET A CG    1 
ATOM   3734 S SD    . MET A 1 475 ? 16.141 -27.237 -25.563 1.00 29.94  ? 475 MET A SD    1 
ATOM   3735 C CE    . MET A 1 475 ? 17.092 -26.182 -24.466 1.00 29.64  ? 475 MET A CE    1 
ATOM   3736 N N     . ASP A 1 476 ? 10.957 -27.106 -28.321 1.00 31.37  ? 476 ASP A N     1 
ATOM   3737 C CA    . ASP A 1 476 ? 10.079 -27.447 -29.429 1.00 32.82  ? 476 ASP A CA    1 
ATOM   3738 C C     . ASP A 1 476 ? 9.245  -26.235 -29.811 1.00 32.21  ? 476 ASP A C     1 
ATOM   3739 O O     . ASP A 1 476 ? 9.121  -25.953 -30.993 1.00 30.03  ? 476 ASP A O     1 
ATOM   3740 C CB    . ASP A 1 476 ? 9.108  -28.572 -29.095 1.00 35.77  ? 476 ASP A CB    1 
ATOM   3741 C CG    . ASP A 1 476 ? 9.662  -29.952 -29.344 1.00 38.17  ? 476 ASP A CG    1 
ATOM   3742 O OD1   . ASP A 1 476 ? 10.641 -30.044 -30.084 1.00 41.88  ? 476 ASP A OD1   1 
ATOM   3743 O OD2   . ASP A 1 476 ? 9.116  -30.907 -28.771 1.00 43.49  ? 476 ASP A OD2   1 
ATOM   3744 N N     . ARG A 1 477 ? 8.689  -25.528 -28.809 1.00 32.68  ? 477 ARG A N     1 
ATOM   3745 C CA    . ARG A 1 477 ? 7.778  -24.445 -29.119 1.00 32.61  ? 477 ARG A CA    1 
ATOM   3746 C C     . ARG A 1 477 ? 8.537  -23.345 -29.858 1.00 29.94  ? 477 ARG A C     1 
ATOM   3747 O O     . ARG A 1 477 ? 8.023  -22.784 -30.815 1.00 24.23  ? 477 ARG A O     1 
ATOM   3748 C CB    . ARG A 1 477 ? 7.027  -23.903 -27.899 1.00 36.29  ? 477 ARG A CB    1 
ATOM   3749 C CG    . ARG A 1 477 ? 5.890  -22.966 -28.293 1.00 42.27  ? 477 ARG A CG    1 
ATOM   3750 C CD    . ARG A 1 477 ? 5.015  -22.533 -27.141 1.00 57.53  ? 477 ARG A CD    1 
ATOM   3751 N NE    . ARG A 1 477 ? 3.686  -22.077 -27.552 1.00 67.80  ? 477 ARG A NE    1 
ATOM   3752 C CZ    . ARG A 1 477 ? 2.540  -22.666 -27.208 1.00 72.97  ? 477 ARG A CZ    1 
ATOM   3753 N NH1   . ARG A 1 477 ? 2.560  -23.749 -26.448 1.00 69.03  ? 477 ARG A NH1   1 
ATOM   3754 N NH2   . ARG A 1 477 ? 1.380  -22.181 -27.629 1.00 71.67  ? 477 ARG A NH2   1 
ATOM   3755 N N     . ILE A 1 478 ? 9.760  -23.033 -29.429 1.00 29.86  ? 478 ILE A N     1 
ATOM   3756 C CA    . ILE A 1 478 ? 10.511 -21.988 -30.110 1.00 29.17  ? 478 ILE A CA    1 
ATOM   3757 C C     . ILE A 1 478 ? 10.904 -22.449 -31.519 1.00 29.95  ? 478 ILE A C     1 
ATOM   3758 O O     . ILE A 1 478 ? 10.815 -21.675 -32.482 1.00 30.36  ? 478 ILE A O     1 
ATOM   3759 C CB    . ILE A 1 478 ? 11.749 -21.579 -29.296 1.00 30.51  ? 478 ILE A CB    1 
ATOM   3760 C CG1   . ILE A 1 478 ? 11.400 -21.116 -27.874 1.00 35.03  ? 478 ILE A CG1   1 
ATOM   3761 C CG2   . ILE A 1 478 ? 12.533 -20.525 -30.054 1.00 29.83  ? 478 ILE A CG2   1 
ATOM   3762 C CD1   . ILE A 1 478 ? 10.289 -20.102 -27.789 1.00 36.33  ? 478 ILE A CD1   1 
ATOM   3763 N N     . ALA A 1 479 ? 11.340 -23.709 -31.651 1.00 28.53  ? 479 ALA A N     1 
ATOM   3764 C CA    . ALA A 1 479 ? 11.711 -24.231 -32.962 1.00 30.95  ? 479 ALA A CA    1 
ATOM   3765 C C     . ALA A 1 479 ? 10.573 -24.047 -33.956 1.00 26.15  ? 479 ALA A C     1 
ATOM   3766 O O     . ALA A 1 479 ? 10.806 -23.709 -35.112 1.00 26.63  ? 479 ALA A O     1 
ATOM   3767 C CB    . ALA A 1 479 ? 12.126 -25.680 -32.900 1.00 30.83  ? 479 ALA A CB    1 
ATOM   3768 N N     . LYS A 1 480 ? 9.348  -24.257 -33.496 1.00 28.86  ? 480 LYS A N     1 
ATOM   3769 C CA    . LYS A 1 480 ? 8.201  -24.268 -34.398 1.00 31.42  ? 480 LYS A CA    1 
ATOM   3770 C C     . LYS A 1 480 ? 7.875  -22.858 -34.883 1.00 26.70  ? 480 LYS A C     1 
ATOM   3771 O O     . LYS A 1 480 ? 7.123  -22.712 -35.845 1.00 24.77  ? 480 LYS A O     1 
ATOM   3772 C CB    . LYS A 1 480 ? 6.955  -24.871 -33.743 1.00 34.05  ? 480 LYS A CB    1 
ATOM   3773 C CG    . LYS A 1 480 ? 6.949  -26.386 -33.599 1.00 37.79  ? 480 LYS A CG    1 
ATOM   3774 C CD    . LYS A 1 480 ? 5.640  -26.868 -33.008 1.00 43.98  ? 480 LYS A CD    1 
ATOM   3775 C CE    . LYS A 1 480 ? 5.725  -28.235 -32.372 1.00 47.15  ? 480 LYS A CE    1 
ATOM   3776 N NZ    . LYS A 1 480 ? 6.090  -29.254 -33.377 1.00 51.54  ? 480 LYS A NZ    1 
ATOM   3777 N N     . THR A 1 481 ? 8.458  -21.829 -34.258 1.00 24.20  ? 481 THR A N     1 
ATOM   3778 C CA    . THR A 1 481 ? 8.224  -20.465 -34.711 1.00 25.72  ? 481 THR A CA    1 
ATOM   3779 C C     . THR A 1 481 ? 9.094  -20.127 -35.924 1.00 25.78  ? 481 THR A C     1 
ATOM   3780 O O     . THR A 1 481 ? 8.809  -19.153 -36.627 1.00 28.57  ? 481 THR A O     1 
ATOM   3781 C CB    . THR A 1 481 ? 8.422  -19.445 -33.574 1.00 29.51  ? 481 THR A CB    1 
ATOM   3782 O OG1   . THR A 1 481 ? 9.815  -19.313 -33.278 1.00 31.81  ? 481 THR A OG1   1 
ATOM   3783 C CG2   . THR A 1 481 ? 7.671  -19.798 -32.304 1.00 26.37  ? 481 THR A CG2   1 
ATOM   3784 N N     . TYR A 1 482 ? 10.141 -20.925 -36.191 1.00 25.27  ? 482 TYR A N     1 
ATOM   3785 C CA    . TYR A 1 482 ? 11.056 -20.647 -37.292 1.00 27.36  ? 482 TYR A CA    1 
ATOM   3786 C C     . TYR A 1 482 ? 10.637 -21.445 -38.527 1.00 29.05  ? 482 TYR A C     1 
ATOM   3787 O O     . TYR A 1 482 ? 11.435 -22.165 -39.127 1.00 31.19  ? 482 TYR A O     1 
ATOM   3788 C CB    . TYR A 1 482 ? 12.498 -20.898 -36.842 1.00 27.89  ? 482 TYR A CB    1 
ATOM   3789 C CG    . TYR A 1 482 ? 13.020 -19.880 -35.862 1.00 28.11  ? 482 TYR A CG    1 
ATOM   3790 C CD1   . TYR A 1 482 ? 13.517 -18.662 -36.306 1.00 31.00  ? 482 TYR A CD1   1 
ATOM   3791 C CD2   . TYR A 1 482 ? 12.965 -20.093 -34.497 1.00 28.04  ? 482 TYR A CD2   1 
ATOM   3792 C CE1   . TYR A 1 482 ? 13.971 -17.688 -35.428 1.00 29.02  ? 482 TYR A CE1   1 
ATOM   3793 C CE2   . TYR A 1 482 ? 13.419 -19.131 -33.605 1.00 28.95  ? 482 TYR A CE2   1 
ATOM   3794 C CZ    . TYR A 1 482 ? 13.933 -17.931 -34.072 1.00 28.56  ? 482 TYR A CZ    1 
ATOM   3795 O OH    . TYR A 1 482 ? 14.421 -16.966 -33.228 1.00 26.90  ? 482 TYR A OH    1 
ATOM   3796 N N     . SER A 1 483 ? 9.394  -21.204 -38.970 1.00 31.24  ? 483 SER A N     1 
ATOM   3797 C CA    . SER A 1 483 ? 8.660  -22.124 -39.824 1.00 32.80  ? 483 SER A CA    1 
ATOM   3798 C C     . SER A 1 483 ? 8.695  -21.737 -41.305 1.00 29.03  ? 483 SER A C     1 
ATOM   3799 O O     . SER A 1 483 ? 7.970  -22.332 -42.094 1.00 29.81  ? 483 SER A O     1 
ATOM   3800 C CB    . SER A 1 483 ? 7.226  -22.209 -39.340 1.00 34.93  ? 483 SER A CB    1 
ATOM   3801 O OG    . SER A 1 483 ? 6.582  -20.932 -39.442 1.00 38.00  ? 483 SER A OG    1 
ATOM   3802 N N     . TRP A 1 484 ? 9.499  -20.745 -41.705 1.00 27.80  ? 484 TRP A N     1 
ATOM   3803 C CA    . TRP A 1 484 ? 9.505  -20.305 -43.100 1.00 27.14  ? 484 TRP A CA    1 
ATOM   3804 C C     . TRP A 1 484 ? 9.626  -21.495 -44.052 1.00 26.51  ? 484 TRP A C     1 
ATOM   3805 O O     . TRP A 1 484 ? 10.433 -22.394 -43.837 1.00 26.62  ? 484 TRP A O     1 
ATOM   3806 C CB    . TRP A 1 484 ? 10.633 -19.306 -43.356 1.00 27.34  ? 484 TRP A CB    1 
ATOM   3807 C CG    . TRP A 1 484 ? 10.618 -18.694 -44.722 1.00 27.01  ? 484 TRP A CG    1 
ATOM   3808 C CD1   . TRP A 1 484 ? 9.858  -17.646 -45.136 1.00 28.44  ? 484 TRP A CD1   1 
ATOM   3809 C CD2   . TRP A 1 484 ? 11.416 -19.069 -45.854 1.00 26.74  ? 484 TRP A CD2   1 
ATOM   3810 N NE1   . TRP A 1 484 ? 10.141 -17.328 -46.434 1.00 29.13  ? 484 TRP A NE1   1 
ATOM   3811 C CE2   . TRP A 1 484 ? 11.076 -18.195 -46.910 1.00 27.32  ? 484 TRP A CE2   1 
ATOM   3812 C CE3   . TRP A 1 484 ? 12.406 -20.032 -46.070 1.00 24.45  ? 484 TRP A CE3   1 
ATOM   3813 C CZ2   . TRP A 1 484 ? 11.672 -18.262 -48.166 1.00 27.46  ? 484 TRP A CZ2   1 
ATOM   3814 C CZ3   . TRP A 1 484 ? 12.981 -20.122 -47.318 1.00 25.84  ? 484 TRP A CZ3   1 
ATOM   3815 C CH2   . TRP A 1 484 ? 12.626 -19.240 -48.346 1.00 28.84  ? 484 TRP A CH2   1 
ATOM   3816 N N     . ASN A 1 485 ? 8.798  -21.479 -45.103 1.00 29.19  ? 485 ASN A N     1 
ATOM   3817 C CA    . ASN A 1 485 ? 8.774  -22.487 -46.159 1.00 29.00  ? 485 ASN A CA    1 
ATOM   3818 C C     . ASN A 1 485 ? 8.565  -23.880 -45.571 1.00 31.09  ? 485 ASN A C     1 
ATOM   3819 O O     . ASN A 1 485 ? 9.334  -24.806 -45.867 1.00 25.86  ? 485 ASN A O     1 
ATOM   3820 C CB    . ASN A 1 485 ? 10.031 -22.438 -47.025 1.00 29.33  ? 485 ASN A CB    1 
ATOM   3821 C CG    . ASN A 1 485 ? 9.919  -23.327 -48.243 1.00 29.45  ? 485 ASN A CG    1 
ATOM   3822 O OD1   . ASN A 1 485 ? 8.822  -23.506 -48.756 1.00 29.12  ? 485 ASN A OD1   1 
ATOM   3823 N ND2   . ASN A 1 485 ? 11.030 -23.896 -48.691 1.00 26.22  ? 485 ASN A ND2   1 
ATOM   3824 N N     . ASP A 1 486 ? 7.514  -23.986 -44.739 1.00 30.86  ? 486 ASP A N     1 
ATOM   3825 C CA    . ASP A 1 486 ? 7.063  -25.242 -44.155 1.00 35.71  ? 486 ASP A CA    1 
ATOM   3826 C C     . ASP A 1 486 ? 8.221  -25.904 -43.394 1.00 33.31  ? 486 ASP A C     1 
ATOM   3827 O O     . ASP A 1 486 ? 8.533  -27.080 -43.584 1.00 32.75  ? 486 ASP A O     1 
ATOM   3828 C CB    . ASP A 1 486 ? 6.341  -26.126 -45.192 1.00 40.34  ? 486 ASP A CB    1 
ATOM   3829 C CG    . ASP A 1 486 ? 5.696  -27.378 -44.592 1.00 52.59  ? 486 ASP A CG    1 
ATOM   3830 O OD1   . ASP A 1 486 ? 5.098  -27.277 -43.490 1.00 59.98  ? 486 ASP A OD1   1 
ATOM   3831 O OD2   . ASP A 1 486 ? 5.812  -28.467 -45.203 1.00 59.27  ? 486 ASP A OD2   1 
ATOM   3832 N N     . ASN A 1 487 ? 8.830  -25.128 -42.494 1.00 29.06  ? 487 ASN A N     1 
ATOM   3833 C CA    . ASN A 1 487 ? 9.829  -25.627 -41.567 1.00 28.55  ? 487 ASN A CA    1 
ATOM   3834 C C     . ASN A 1 487 ? 11.054 -26.121 -42.327 1.00 24.97  ? 487 ASN A C     1 
ATOM   3835 O O     . ASN A 1 487 ? 11.655 -27.125 -41.958 1.00 27.20  ? 487 ASN A O     1 
ATOM   3836 C CB    . ASN A 1 487 ? 9.260  -26.696 -40.628 1.00 29.00  ? 487 ASN A CB    1 
ATOM   3837 C CG    . ASN A 1 487 ? 8.105  -26.146 -39.826 1.00 31.10  ? 487 ASN A CG    1 
ATOM   3838 O OD1   . ASN A 1 487 ? 6.960  -26.436 -40.143 1.00 32.42  ? 487 ASN A OD1   1 
ATOM   3839 N ND2   . ASN A 1 487 ? 8.382  -25.280 -38.862 1.00 30.28  ? 487 ASN A ND2   1 
ATOM   3840 N N     . ALA A 1 488 ? 11.474 -25.370 -43.342 1.00 23.85  ? 488 ALA A N     1 
ATOM   3841 C CA    . ALA A 1 488 ? 12.590 -25.796 -44.173 1.00 22.85  ? 488 ALA A CA    1 
ATOM   3842 C C     . ALA A 1 488 ? 13.840 -25.965 -43.320 1.00 21.72  ? 488 ALA A C     1 
ATOM   3843 O O     . ALA A 1 488 ? 14.600 -26.903 -43.526 1.00 22.08  ? 488 ALA A O     1 
ATOM   3844 C CB    . ALA A 1 488 ? 12.826 -24.809 -45.299 1.00 23.74  ? 488 ALA A CB    1 
ATOM   3845 N N     . LEU A 1 489 ? 14.061 -25.049 -42.375 1.00 23.27  ? 489 LEU A N     1 
ATOM   3846 C CA    . LEU A 1 489 ? 15.343 -25.001 -41.702 1.00 24.67  ? 489 LEU A CA    1 
ATOM   3847 C C     . LEU A 1 489 ? 15.492 -26.197 -40.761 1.00 23.56  ? 489 LEU A C     1 
ATOM   3848 O O     . LEU A 1 489 ? 16.562 -26.800 -40.718 1.00 25.02  ? 489 LEU A O     1 
ATOM   3849 C CB    . LEU A 1 489 ? 15.533 -23.650 -41.002 1.00 26.15  ? 489 LEU A CB    1 
ATOM   3850 C CG    . LEU A 1 489 ? 16.804 -23.540 -40.148 1.00 27.47  ? 489 LEU A CG    1 
ATOM   3851 C CD1   . LEU A 1 489 ? 18.049 -23.696 -40.994 1.00 27.54  ? 489 LEU A CD1   1 
ATOM   3852 C CD2   . LEU A 1 489 ? 16.862 -22.226 -39.390 1.00 28.80  ? 489 LEU A CD2   1 
ATOM   3853 N N     . TRP A 1 490 ? 14.440 -26.552 -40.015 1.00 25.47  ? 490 TRP A N     1 
ATOM   3854 C CA    . TRP A 1 490 ? 14.517 -27.693 -39.104 1.00 25.39  ? 490 TRP A CA    1 
ATOM   3855 C C     . TRP A 1 490 ? 14.596 -29.016 -39.880 1.00 26.63  ? 490 TRP A C     1 
ATOM   3856 O O     . TRP A 1 490 ? 15.248 -29.955 -39.425 1.00 25.65  ? 490 TRP A O     1 
ATOM   3857 C CB    . TRP A 1 490 ? 13.400 -27.676 -38.038 1.00 27.44  ? 490 TRP A CB    1 
ATOM   3858 C CG    . TRP A 1 490 ? 13.930 -27.235 -36.709 1.00 26.35  ? 490 TRP A CG    1 
ATOM   3859 C CD1   . TRP A 1 490 ? 14.105 -28.007 -35.594 1.00 25.18  ? 490 TRP A CD1   1 
ATOM   3860 C CD2   . TRP A 1 490 ? 14.490 -25.947 -36.401 1.00 26.39  ? 490 TRP A CD2   1 
ATOM   3861 N NE1   . TRP A 1 490 ? 14.726 -27.281 -34.614 1.00 25.74  ? 490 TRP A NE1   1 
ATOM   3862 C CE2   . TRP A 1 490 ? 14.976 -26.014 -35.080 1.00 25.92  ? 490 TRP A CE2   1 
ATOM   3863 C CE3   . TRP A 1 490 ? 14.612 -24.739 -37.100 1.00 28.59  ? 490 TRP A CE3   1 
ATOM   3864 C CZ2   . TRP A 1 490 ? 15.569 -24.914 -34.453 1.00 25.87  ? 490 TRP A CZ2   1 
ATOM   3865 C CZ3   . TRP A 1 490 ? 15.210 -23.659 -36.481 1.00 26.58  ? 490 TRP A CZ3   1 
ATOM   3866 C CH2   . TRP A 1 490 ? 15.681 -23.746 -35.174 1.00 24.60  ? 490 TRP A CH2   1 
ATOM   3867 N N     . LYS A 1 491 ? 13.995 -29.073 -41.076 1.00 26.78  ? 491 LYS A N     1 
ATOM   3868 C CA    . LYS A 1 491 ? 14.121 -30.239 -41.938 1.00 28.38  ? 491 LYS A CA    1 
ATOM   3869 C C     . LYS A 1 491 ? 15.583 -30.484 -42.320 1.00 29.53  ? 491 LYS A C     1 
ATOM   3870 O O     . LYS A 1 491 ? 16.023 -31.635 -42.413 1.00 26.05  ? 491 LYS A O     1 
ATOM   3871 C CB    . LYS A 1 491 ? 13.258 -30.095 -43.200 1.00 27.97  ? 491 LYS A CB    1 
ATOM   3872 C CG    . LYS A 1 491 ? 11.785 -30.465 -43.040 1.00 30.51  ? 491 LYS A CG    1 
ATOM   3873 C CD    . LYS A 1 491 ? 10.899 -29.819 -44.076 1.00 32.90  ? 491 LYS A CD    1 
ATOM   3874 C CE    . LYS A 1 491 ? 9.449  -30.232 -43.996 1.00 34.08  ? 491 LYS A CE    1 
ATOM   3875 N NZ    . LYS A 1 491 ? 8.684  -29.601 -45.098 1.00 35.40  ? 491 LYS A NZ    1 
ATOM   3876 N N     . MET A 1 492 ? 16.330 -29.393 -42.562 1.00 29.59  ? 492 MET A N     1 
ATOM   3877 C CA    . MET A 1 492 ? 17.749 -29.509 -42.845 1.00 26.28  ? 492 MET A CA    1 
ATOM   3878 C C     . MET A 1 492 ? 18.536 -29.879 -41.583 1.00 25.31  ? 492 MET A C     1 
ATOM   3879 O O     . MET A 1 492 ? 19.469 -30.683 -41.661 1.00 22.94  ? 492 MET A O     1 
ATOM   3880 C CB    . MET A 1 492 ? 18.302 -28.204 -43.395 1.00 26.69  ? 492 MET A CB    1 
ATOM   3881 C CG    . MET A 1 492 ? 19.744 -28.345 -43.816 1.00 27.17  ? 492 MET A CG    1 
ATOM   3882 S SD    . MET A 1 492 ? 20.439 -26.789 -44.278 1.00 30.30  ? 492 MET A SD    1 
ATOM   3883 C CE    . MET A 1 492 ? 20.914 -26.148 -42.676 1.00 34.33  ? 492 MET A CE    1 
ATOM   3884 N N     . HIS A 1 493 ? 18.176 -29.277 -40.430 1.00 25.92  ? 493 HIS A N     1 
ATOM   3885 C CA    . HIS A 1 493 ? 18.794 -29.649 -39.168 1.00 25.80  ? 493 HIS A CA    1 
ATOM   3886 C C     . HIS A 1 493 ? 18.606 -31.146 -38.942 1.00 26.99  ? 493 HIS A C     1 
ATOM   3887 O O     . HIS A 1 493 ? 19.570 -31.808 -38.563 1.00 25.58  ? 493 HIS A O     1 
ATOM   3888 C CB    . HIS A 1 493 ? 18.288 -28.835 -37.969 1.00 23.74  ? 493 HIS A CB    1 
ATOM   3889 C CG    . HIS A 1 493 ? 18.708 -27.417 -37.940 1.00 24.49  ? 493 HIS A CG    1 
ATOM   3890 N ND1   . HIS A 1 493 ? 19.873 -26.912 -38.482 1.00 26.68  ? 493 HIS A ND1   1 
ATOM   3891 C CD2   . HIS A 1 493 ? 18.077 -26.375 -37.375 1.00 25.76  ? 493 HIS A CD2   1 
ATOM   3892 C CE1   . HIS A 1 493 ? 19.918 -25.606 -38.264 1.00 26.71  ? 493 HIS A CE1   1 
ATOM   3893 N NE2   . HIS A 1 493 ? 18.831 -25.257 -37.598 1.00 25.45  ? 493 HIS A NE2   1 
ATOM   3894 N N     . GLU A 1 494 ? 17.391 -31.665 -39.212 1.00 28.47  ? 494 GLU A N     1 
ATOM   3895 C CA    . GLU A 1 494 ? 17.077 -33.075 -38.984 1.00 32.15  ? 494 GLU A CA    1 
ATOM   3896 C C     . GLU A 1 494 ? 17.854 -33.988 -39.960 1.00 29.31  ? 494 GLU A C     1 
ATOM   3897 O O     . GLU A 1 494 ? 18.250 -35.101 -39.620 1.00 26.88  ? 494 GLU A O     1 
ATOM   3898 C CB    . GLU A 1 494 ? 15.563 -33.302 -39.059 1.00 36.49  ? 494 GLU A CB    1 
ATOM   3899 C CG    . GLU A 1 494 ? 14.740 -32.715 -37.909 1.00 41.49  ? 494 GLU A CG    1 
ATOM   3900 C CD    . GLU A 1 494 ? 14.687 -33.445 -36.560 1.00 50.71  ? 494 GLU A CD    1 
ATOM   3901 O OE1   . GLU A 1 494 ? 15.312 -34.526 -36.414 1.00 46.44  ? 494 GLU A OE1   1 
ATOM   3902 O OE2   . GLU A 1 494 ? 13.986 -32.929 -35.615 1.00 55.79  ? 494 GLU A OE2   1 
ATOM   3903 N N     . THR A 1 495 ? 18.090 -33.528 -41.186 1.00 28.52  ? 495 THR A N     1 
ATOM   3904 C CA    . THR A 1 495 ? 18.912 -34.250 -42.148 1.00 27.82  ? 495 THR A CA    1 
ATOM   3905 C C     . THR A 1 495 ? 20.349 -34.401 -41.632 1.00 29.48  ? 495 THR A C     1 
ATOM   3906 O O     . THR A 1 495 ? 20.956 -35.470 -41.734 1.00 28.54  ? 495 THR A O     1 
ATOM   3907 C CB    . THR A 1 495 ? 18.913 -33.525 -43.502 1.00 29.00  ? 495 THR A CB    1 
ATOM   3908 O OG1   . THR A 1 495 ? 17.574 -33.457 -44.002 1.00 26.33  ? 495 THR A OG1   1 
ATOM   3909 C CG2   . THR A 1 495 ? 19.791 -34.201 -44.533 1.00 29.79  ? 495 THR A CG2   1 
ATOM   3910 N N     . ILE A 1 496 ? 20.898 -33.325 -41.060 1.00 27.68  ? 496 ILE A N     1 
ATOM   3911 C CA    . ILE A 1 496 ? 22.268 -33.364 -40.578 1.00 28.46  ? 496 ILE A CA    1 
ATOM   3912 C C     . ILE A 1 496 ? 22.328 -34.254 -39.333 1.00 27.66  ? 496 ILE A C     1 
ATOM   3913 O O     . ILE A 1 496 ? 23.254 -35.054 -39.170 1.00 26.70  ? 496 ILE A O     1 
ATOM   3914 C CB    . ILE A 1 496 ? 22.776 -31.925 -40.335 1.00 30.96  ? 496 ILE A CB    1 
ATOM   3915 C CG1   . ILE A 1 496 ? 22.883 -31.153 -41.653 1.00 29.81  ? 496 ILE A CG1   1 
ATOM   3916 C CG2   . ILE A 1 496 ? 24.093 -31.896 -39.558 1.00 31.10  ? 496 ILE A CG2   1 
ATOM   3917 C CD1   . ILE A 1 496 ? 22.932 -29.649 -41.468 1.00 29.96  ? 496 ILE A CD1   1 
ATOM   3918 N N     . LYS A 1 497 ? 21.320 -34.118 -38.467 1.00 25.27  ? 497 LYS A N     1 
ATOM   3919 C CA    . LYS A 1 497 ? 21.208 -34.932 -37.266 1.00 26.13  ? 497 LYS A CA    1 
ATOM   3920 C C     . LYS A 1 497 ? 21.301 -36.424 -37.602 1.00 25.91  ? 497 LYS A C     1 
ATOM   3921 O O     . LYS A 1 497 ? 21.952 -37.181 -36.893 1.00 24.32  ? 497 LYS A O     1 
ATOM   3922 C CB    . LYS A 1 497 ? 19.893 -34.614 -36.550 1.00 24.89  ? 497 LYS A CB    1 
ATOM   3923 C CG    . LYS A 1 497 ? 19.612 -35.429 -35.295 1.00 24.18  ? 497 LYS A CG    1 
ATOM   3924 C CD    . LYS A 1 497 ? 20.647 -35.274 -34.233 1.00 24.73  ? 497 LYS A CD    1 
ATOM   3925 C CE    . LYS A 1 497 ? 20.176 -35.783 -32.896 1.00 24.90  ? 497 LYS A CE    1 
ATOM   3926 N NZ    . LYS A 1 497 ? 21.253 -35.713 -31.872 1.00 26.39  ? 497 LYS A NZ    1 
ATOM   3927 N N     . ASP A 1 498 ? 20.621 -36.844 -38.668 1.00 29.29  ? 498 ASP A N     1 
ATOM   3928 C CA    . ASP A 1 498 ? 20.470 -38.260 -38.976 1.00 30.85  ? 498 ASP A CA    1 
ATOM   3929 C C     . ASP A 1 498 ? 21.771 -38.797 -39.572 1.00 30.00  ? 498 ASP A C     1 
ATOM   3930 O O     . ASP A 1 498 ? 22.149 -39.948 -39.343 1.00 34.07  ? 498 ASP A O     1 
ATOM   3931 C CB    . ASP A 1 498 ? 19.233 -38.465 -39.856 1.00 30.77  ? 498 ASP A CB    1 
ATOM   3932 C CG    . ASP A 1 498 ? 17.915 -38.322 -39.095 1.00 32.58  ? 498 ASP A CG    1 
ATOM   3933 O OD1   . ASP A 1 498 ? 17.922 -38.393 -37.840 1.00 34.99  ? 498 ASP A OD1   1 
ATOM   3934 O OD2   . ASP A 1 498 ? 16.889 -38.124 -39.753 1.00 33.43  ? 498 ASP A OD2   1 
ATOM   3935 N N     . ALA A 1 499 ? 22.471 -37.937 -40.304 1.00 25.60  ? 499 ALA A N     1 
ATOM   3936 C CA    . ALA A 1 499 ? 23.748 -38.294 -40.883 1.00 25.14  ? 499 ALA A CA    1 
ATOM   3937 C C     . ALA A 1 499 ? 24.809 -38.464 -39.790 1.00 26.38  ? 499 ALA A C     1 
ATOM   3938 O O     . ALA A 1 499 ? 25.557 -39.432 -39.786 1.00 25.63  ? 499 ALA A O     1 
ATOM   3939 C CB    . ALA A 1 499 ? 24.142 -37.226 -41.868 1.00 24.92  ? 499 ALA A CB    1 
ATOM   3940 N N     . LEU A 1 500 ? 24.904 -37.503 -38.869 1.00 26.64  ? 500 LEU A N     1 
ATOM   3941 C CA    . LEU A 1 500 ? 25.922 -37.553 -37.839 1.00 27.07  ? 500 LEU A CA    1 
ATOM   3942 C C     . LEU A 1 500 ? 25.515 -38.449 -36.670 1.00 27.37  ? 500 LEU A C     1 
ATOM   3943 O O     . LEU A 1 500 ? 26.383 -38.940 -35.954 1.00 25.11  ? 500 LEU A O     1 
ATOM   3944 C CB    . LEU A 1 500 ? 26.155 -36.130 -37.350 1.00 28.08  ? 500 LEU A CB    1 
ATOM   3945 C CG    . LEU A 1 500 ? 26.774 -35.194 -38.385 1.00 27.82  ? 500 LEU A CG    1 
ATOM   3946 C CD1   . LEU A 1 500 ? 26.799 -33.764 -37.845 1.00 26.63  ? 500 LEU A CD1   1 
ATOM   3947 C CD2   . LEU A 1 500 ? 28.169 -35.677 -38.768 1.00 25.94  ? 500 LEU A CD2   1 
ATOM   3948 N N     . ASP A 1 501 ? 24.206 -38.595 -36.428 1.00 28.21  ? 501 ASP A N     1 
ATOM   3949 C CA    . ASP A 1 501 ? 23.725 -39.301 -35.250 1.00 27.90  ? 501 ASP A CA    1 
ATOM   3950 C C     . ASP A 1 501 ? 22.555 -40.202 -35.624 1.00 28.05  ? 501 ASP A C     1 
ATOM   3951 O O     . ASP A 1 501 ? 21.482 -40.094 -35.042 1.00 29.32  ? 501 ASP A O     1 
ATOM   3952 C CB    . ASP A 1 501 ? 23.314 -38.315 -34.159 1.00 27.92  ? 501 ASP A CB    1 
ATOM   3953 C CG    . ASP A 1 501 ? 22.952 -38.938 -32.826 1.00 29.59  ? 501 ASP A CG    1 
ATOM   3954 O OD1   . ASP A 1 501 ? 23.211 -40.161 -32.656 1.00 26.05  ? 501 ASP A OD1   1 
ATOM   3955 O OD2   . ASP A 1 501 ? 22.418 -38.184 -31.953 1.00 29.11  ? 501 ASP A OD2   1 
ATOM   3956 N N     . PRO A 1 502 ? 22.756 -41.206 -36.505 1.00 30.24  ? 502 PRO A N     1 
ATOM   3957 C CA    . PRO A 1 502 ? 21.650 -42.071 -36.924 1.00 30.40  ? 502 PRO A CA    1 
ATOM   3958 C C     . PRO A 1 502 ? 20.886 -42.745 -35.772 1.00 29.92  ? 502 PRO A C     1 
ATOM   3959 O O     . PRO A 1 502 ? 19.670 -42.908 -35.865 1.00 27.08  ? 502 PRO A O     1 
ATOM   3960 C CB    . PRO A 1 502 ? 22.331 -43.086 -37.872 1.00 30.67  ? 502 PRO A CB    1 
ATOM   3961 C CG    . PRO A 1 502 ? 23.830 -42.985 -37.623 1.00 28.06  ? 502 PRO A CG    1 
ATOM   3962 C CD    . PRO A 1 502 ? 24.055 -41.595 -37.090 1.00 29.06  ? 502 PRO A CD    1 
ATOM   3963 N N     . ASN A 1 503 ? 21.586 -43.115 -34.677 1.00 30.91  ? 503 ASN A N     1 
ATOM   3964 C CA    . ASN A 1 503 ? 20.954 -43.768 -33.529 1.00 28.86  ? 503 ASN A CA    1 
ATOM   3965 C C     . ASN A 1 503 ? 20.298 -42.747 -32.593 1.00 31.60  ? 503 ASN A C     1 
ATOM   3966 O O     . ASN A 1 503 ? 19.618 -43.120 -31.633 1.00 27.18  ? 503 ASN A O     1 
ATOM   3967 C CB    . ASN A 1 503 ? 21.950 -44.647 -32.756 1.00 26.99  ? 503 ASN A CB    1 
ATOM   3968 C CG    . ASN A 1 503 ? 22.492 -45.770 -33.617 1.00 25.71  ? 503 ASN A CG    1 
ATOM   3969 O OD1   . ASN A 1 503 ? 21.755 -46.383 -34.384 1.00 25.56  ? 503 ASN A OD1   1 
ATOM   3970 N ND2   . ASN A 1 503 ? 23.780 -46.030 -33.540 1.00 24.74  ? 503 ASN A ND2   1 
ATOM   3971 N N     . GLY A 1 504 ? 20.541 -41.453 -32.838 1.00 30.60  ? 504 GLY A N     1 
ATOM   3972 C CA    . GLY A 1 504 ? 19.851 -40.402 -32.109 1.00 30.98  ? 504 GLY A CA    1 
ATOM   3973 C C     . GLY A 1 504 ? 20.139 -40.413 -30.612 1.00 33.06  ? 504 GLY A C     1 
ATOM   3974 O O     . GLY A 1 504 ? 19.262 -40.059 -29.832 1.00 37.29  ? 504 GLY A O     1 
ATOM   3975 N N     . ILE A 1 505 ? 21.391 -40.714 -30.234 1.00 34.96  ? 505 ILE A N     1 
ATOM   3976 C CA    . ILE A 1 505 ? 21.784 -40.860 -28.835 1.00 34.00  ? 505 ILE A CA    1 
ATOM   3977 C C     . ILE A 1 505 ? 22.329 -39.562 -28.202 1.00 32.00  ? 505 ILE A C     1 
ATOM   3978 O O     . ILE A 1 505 ? 22.632 -39.587 -27.011 1.00 31.94  ? 505 ILE A O     1 
ATOM   3979 C CB    . ILE A 1 505 ? 22.775 -42.040 -28.650 1.00 34.49  ? 505 ILE A CB    1 
ATOM   3980 C CG1   . ILE A 1 505 ? 23.976 -41.991 -29.599 1.00 32.56  ? 505 ILE A CG1   1 
ATOM   3981 C CG2   . ILE A 1 505 ? 22.050 -43.386 -28.749 1.00 36.56  ? 505 ILE A CG2   1 
ATOM   3982 C CD1   . ILE A 1 505 ? 25.069 -41.027 -29.188 1.00 34.08  ? 505 ILE A CD1   1 
ATOM   3983 N N     . LEU A 1 506 ? 22.473 -38.440 -28.933 1.00 27.66  ? 506 LEU A N     1 
ATOM   3984 C CA    . LEU A 1 506 ? 22.839 -37.187 -28.274 1.00 30.10  ? 506 LEU A CA    1 
ATOM   3985 C C     . LEU A 1 506 ? 21.626 -36.276 -28.072 1.00 29.23  ? 506 LEU A C     1 
ATOM   3986 O O     . LEU A 1 506 ? 21.018 -35.827 -29.039 1.00 29.63  ? 506 LEU A O     1 
ATOM   3987 C CB    . LEU A 1 506 ? 23.881 -36.411 -29.079 1.00 32.92  ? 506 LEU A CB    1 
ATOM   3988 C CG    . LEU A 1 506 ? 25.283 -36.996 -29.199 1.00 35.28  ? 506 LEU A CG    1 
ATOM   3989 C CD1   . LEU A 1 506 ? 26.217 -35.904 -29.693 1.00 36.21  ? 506 LEU A CD1   1 
ATOM   3990 C CD2   . LEU A 1 506 ? 25.790 -37.583 -27.884 1.00 35.93  ? 506 LEU A CD2   1 
ATOM   3991 N N     . ALA A 1 507 ? 21.333 -35.977 -26.798 1.00 31.74  ? 507 ALA A N     1 
ATOM   3992 C CA    . ALA A 1 507 ? 20.421 -34.917 -26.360 1.00 31.18  ? 507 ALA A CA    1 
ATOM   3993 C C     . ALA A 1 507 ? 19.239 -34.764 -27.306 1.00 28.68  ? 507 ALA A C     1 
ATOM   3994 O O     . ALA A 1 507 ? 19.030 -33.708 -27.896 1.00 29.15  ? 507 ALA A O     1 
ATOM   3995 C CB    . ALA A 1 507 ? 21.161 -33.616 -26.191 1.00 29.24  ? 507 ALA A CB    1 
ATOM   3996 N N     . PRO A 1 508 ? 18.420 -35.817 -27.455 1.00 27.61  ? 508 PRO A N     1 
ATOM   3997 C CA    . PRO A 1 508 ? 17.217 -35.735 -28.261 1.00 29.05  ? 508 PRO A CA    1 
ATOM   3998 C C     . PRO A 1 508 ? 16.401 -34.570 -27.737 1.00 29.40  ? 508 PRO A C     1 
ATOM   3999 O O     . PRO A 1 508 ? 16.225 -34.450 -26.527 1.00 29.14  ? 508 PRO A O     1 
ATOM   4000 C CB    . PRO A 1 508 ? 16.501 -37.080 -28.059 1.00 29.44  ? 508 PRO A CB    1 
ATOM   4001 C CG    . PRO A 1 508 ? 17.187 -37.712 -26.881 1.00 30.11  ? 508 PRO A CG    1 
ATOM   4002 C CD    . PRO A 1 508 ? 18.583 -37.134 -26.840 1.00 30.30  ? 508 PRO A CD    1 
ATOM   4003 N N     . GLY A 1 509 ? 15.997 -33.689 -28.664 1.00 29.35  ? 509 GLY A N     1 
ATOM   4004 C CA    . GLY A 1 509 ? 15.103 -32.595 -28.350 1.00 28.84  ? 509 GLY A CA    1 
ATOM   4005 C C     . GLY A 1 509 ? 15.811 -31.262 -28.144 1.00 28.55  ? 509 GLY A C     1 
ATOM   4006 O O     . GLY A 1 509 ? 15.158 -30.225 -28.131 1.00 32.16  ? 509 GLY A O     1 
ATOM   4007 N N     . LYS A 1 510 ? 17.131 -31.270 -27.976 1.00 29.72  ? 510 LYS A N     1 
ATOM   4008 C CA    . LYS A 1 510 ? 17.868 -30.015 -27.924 1.00 28.33  ? 510 LYS A CA    1 
ATOM   4009 C C     . LYS A 1 510 ? 17.536 -29.173 -29.160 1.00 27.08  ? 510 LYS A C     1 
ATOM   4010 O O     . LYS A 1 510 ? 17.546 -29.688 -30.275 1.00 21.34  ? 510 LYS A O     1 
ATOM   4011 C CB    . LYS A 1 510 ? 19.368 -30.276 -27.807 1.00 28.45  ? 510 LYS A CB    1 
ATOM   4012 C CG    . LYS A 1 510 ? 20.243 -29.030 -27.836 1.00 32.48  ? 510 LYS A CG    1 
ATOM   4013 C CD    . LYS A 1 510 ? 20.014 -28.028 -26.710 1.00 34.53  ? 510 LYS A CD    1 
ATOM   4014 C CE    . LYS A 1 510 ? 20.930 -26.828 -26.858 1.00 35.78  ? 510 LYS A CE    1 
ATOM   4015 N NZ    . LYS A 1 510 ? 20.667 -25.777 -25.848 1.00 35.75  ? 510 LYS A NZ    1 
ATOM   4016 N N     . SER A 1 511 ? 17.168 -27.900 -28.910 1.00 26.64  ? 511 SER A N     1 
ATOM   4017 C CA    . SER A 1 511 ? 16.816 -26.930 -29.931 1.00 27.73  ? 511 SER A CA    1 
ATOM   4018 C C     . SER A 1 511 ? 15.704 -27.445 -30.840 1.00 27.12  ? 511 SER A C     1 
ATOM   4019 O O     . SER A 1 511 ? 15.614 -27.029 -31.996 1.00 23.94  ? 511 SER A O     1 
ATOM   4020 C CB    . SER A 1 511 ? 18.031 -26.529 -30.750 1.00 28.62  ? 511 SER A CB    1 
ATOM   4021 O OG    . SER A 1 511 ? 19.094 -26.052 -29.920 1.00 29.49  ? 511 SER A OG    1 
ATOM   4022 N N     . GLY A 1 512 ? 14.854 -28.334 -30.317 1.00 27.05  ? 512 GLY A N     1 
ATOM   4023 C CA    . GLY A 1 512 ? 13.764 -28.906 -31.094 1.00 26.71  ? 512 GLY A CA    1 
ATOM   4024 C C     . GLY A 1 512 ? 14.190 -29.916 -32.168 1.00 26.71  ? 512 GLY A C     1 
ATOM   4025 O O     . GLY A 1 512 ? 13.417 -30.176 -33.091 1.00 25.92  ? 512 GLY A O     1 
ATOM   4026 N N     . ILE A 1 513 ? 15.370 -30.531 -32.004 1.00 27.70  ? 513 ILE A N     1 
ATOM   4027 C CA    . ILE A 1 513 ? 15.935 -31.473 -32.966 1.00 27.34  ? 513 ILE A CA    1 
ATOM   4028 C C     . ILE A 1 513 ? 15.941 -32.896 -32.394 1.00 27.32  ? 513 ILE A C     1 
ATOM   4029 O O     . ILE A 1 513 ? 16.583 -33.152 -31.383 1.00 29.29  ? 513 ILE A O     1 
ATOM   4030 C CB    . ILE A 1 513 ? 17.366 -31.038 -33.322 1.00 27.79  ? 513 ILE A CB    1 
ATOM   4031 C CG1   . ILE A 1 513 ? 17.400 -29.608 -33.864 1.00 25.91  ? 513 ILE A CG1   1 
ATOM   4032 C CG2   . ILE A 1 513 ? 17.998 -32.043 -34.276 1.00 30.64  ? 513 ILE A CG2   1 
ATOM   4033 C CD1   . ILE A 1 513 ? 18.782 -29.063 -34.058 1.00 25.83  ? 513 ILE A CD1   1 
ATOM   4034 N N     . TRP A 1 514 ? 15.305 -33.843 -33.093 1.00 29.55  ? 514 TRP A N     1 
ATOM   4035 C CA    . TRP A 1 514 ? 14.886 -35.094 -32.482 1.00 29.81  ? 514 TRP A CA    1 
ATOM   4036 C C     . TRP A 1 514 ? 15.555 -36.339 -33.074 1.00 31.54  ? 514 TRP A C     1 
ATOM   4037 O O     . TRP A 1 514 ? 15.841 -37.288 -32.333 1.00 40.26  ? 514 TRP A O     1 
ATOM   4038 C CB    . TRP A 1 514 ? 13.355 -35.171 -32.507 1.00 27.13  ? 514 TRP A CB    1 
ATOM   4039 C CG    . TRP A 1 514 ? 12.739 -34.390 -31.388 1.00 25.41  ? 514 TRP A CG    1 
ATOM   4040 C CD1   . TRP A 1 514 ? 12.207 -33.132 -31.441 1.00 24.50  ? 514 TRP A CD1   1 
ATOM   4041 C CD2   . TRP A 1 514 ? 12.623 -34.812 -30.017 1.00 26.37  ? 514 TRP A CD2   1 
ATOM   4042 N NE1   . TRP A 1 514 ? 11.749 -32.750 -30.201 1.00 24.03  ? 514 TRP A NE1   1 
ATOM   4043 C CE2   . TRP A 1 514 ? 11.992 -33.756 -29.307 1.00 23.75  ? 514 TRP A CE2   1 
ATOM   4044 C CE3   . TRP A 1 514 ? 12.973 -35.983 -29.327 1.00 25.44  ? 514 TRP A CE3   1 
ATOM   4045 C CZ2   . TRP A 1 514 ? 11.706 -33.837 -27.950 1.00 22.45  ? 514 TRP A CZ2   1 
ATOM   4046 C CZ3   . TRP A 1 514 ? 12.696 -36.057 -27.978 1.00 26.30  ? 514 TRP A CZ3   1 
ATOM   4047 C CH2   . TRP A 1 514 ? 12.070 -34.996 -27.305 1.00 24.89  ? 514 TRP A CH2   1 
ATOM   4048 N N     . GLY A 1 515 ? 15.764 -36.379 -34.388 1.00 31.07  ? 515 GLY A N     1 
ATOM   4049 C CA    . GLY A 1 515 ? 16.358 -37.554 -35.020 1.00 33.03  ? 515 GLY A CA    1 
ATOM   4050 C C     . GLY A 1 515 ? 15.303 -38.568 -35.476 1.00 30.59  ? 515 GLY A C     1 
ATOM   4051 O O     . GLY A 1 515 ? 14.242 -38.627 -34.875 1.00 30.58  ? 515 GLY A O     1 
ATOM   4052 N N     . LYS A 1 516 ? 15.601 -39.361 -36.519 1.00 30.91  ? 516 LYS A N     1 
ATOM   4053 C CA    . LYS A 1 516 ? 14.582 -40.152 -37.195 1.00 37.17  ? 516 LYS A CA    1 
ATOM   4054 C C     . LYS A 1 516 ? 13.877 -41.124 -36.239 1.00 39.26  ? 516 LYS A C     1 
ATOM   4055 O O     . LYS A 1 516 ? 12.679 -41.338 -36.379 1.00 39.51  ? 516 LYS A O     1 
ATOM   4056 C CB    . LYS A 1 516 ? 15.124 -40.894 -38.422 1.00 40.79  ? 516 LYS A CB    1 
ATOM   4057 C CG    . LYS A 1 516 ? 16.321 -41.821 -38.231 1.00 46.46  ? 516 LYS A CG    1 
ATOM   4058 C CD    . LYS A 1 516 ? 16.525 -42.761 -39.434 1.00 52.66  ? 516 LYS A CD    1 
ATOM   4059 C CE    . LYS A 1 516 ? 17.953 -43.210 -39.685 1.00 54.79  ? 516 LYS A CE    1 
ATOM   4060 N NZ    . LYS A 1 516 ? 18.567 -43.824 -38.481 1.00 58.42  ? 516 LYS A NZ    1 
ATOM   4061 N N     . ASN A 1 517 ? 14.581 -41.682 -35.248 1.00 36.28  ? 517 ASN A N     1 
ATOM   4062 C CA    . ASN A 1 517 ? 13.957 -42.651 -34.354 1.00 40.48  ? 517 ASN A CA    1 
ATOM   4063 C C     . ASN A 1 517 ? 12.870 -42.035 -33.470 1.00 40.07  ? 517 ASN A C     1 
ATOM   4064 O O     . ASN A 1 517 ? 12.070 -42.778 -32.924 1.00 44.28  ? 517 ASN A O     1 
ATOM   4065 C CB    . ASN A 1 517 ? 14.955 -43.338 -33.417 1.00 37.73  ? 517 ASN A CB    1 
ATOM   4066 C CG    . ASN A 1 517 ? 15.993 -44.162 -34.151 1.00 38.93  ? 517 ASN A CG    1 
ATOM   4067 O OD1   . ASN A 1 517 ? 15.842 -44.507 -35.319 1.00 38.87  ? 517 ASN A OD1   1 
ATOM   4068 N ND2   . ASN A 1 517 ? 17.058 -44.500 -33.456 1.00 39.72  ? 517 ASN A ND2   1 
ATOM   4069 N N     . ARG A 1 518 ? 12.826 -40.709 -33.291 1.00 40.21  ? 518 ARG A N     1 
ATOM   4070 C CA    . ARG A 1 518 ? 11.900 -40.161 -32.313 1.00 40.48  ? 518 ARG A CA    1 
ATOM   4071 C C     . ARG A 1 518 ? 10.951 -39.093 -32.871 1.00 40.57  ? 518 ARG A C     1 
ATOM   4072 O O     . ARG A 1 518 ? 10.066 -38.663 -32.142 1.00 45.38  ? 518 ARG A O     1 
ATOM   4073 C CB    . ARG A 1 518 ? 12.680 -39.639 -31.104 1.00 39.73  ? 518 ARG A CB    1 
ATOM   4074 C CG    . ARG A 1 518 ? 13.348 -40.732 -30.281 1.00 39.14  ? 518 ARG A CG    1 
ATOM   4075 C CD    . ARG A 1 518 ? 14.033 -40.129 -29.077 1.00 40.05  ? 518 ARG A CD    1 
ATOM   4076 N NE    . ARG A 1 518 ? 14.846 -41.087 -28.351 1.00 46.20  ? 518 ARG A NE    1 
ATOM   4077 C CZ    . ARG A 1 518 ? 14.369 -41.991 -27.496 1.00 50.00  ? 518 ARG A CZ    1 
ATOM   4078 N NH1   . ARG A 1 518 ? 13.091 -41.978 -27.148 1.00 47.63  ? 518 ARG A NH1   1 
ATOM   4079 N NH2   . ARG A 1 518 ? 15.180 -42.901 -26.980 1.00 50.21  ? 518 ARG A NH2   1 
ATOM   4080 N N     . ARG A 1 519 ? 11.047 -38.664 -34.133 1.00 37.87  ? 519 ARG A N     1 
ATOM   4081 C CA    . ARG A 1 519 ? 10.057 -37.681 -34.555 1.00 45.15  ? 519 ARG A CA    1 
ATOM   4082 C C     . ARG A 1 519 ? 8.844  -38.377 -35.188 1.00 45.35  ? 519 ARG A C     1 
ATOM   4083 O O     . ARG A 1 519 ? 9.085  -39.388 -35.884 1.00 45.25  ? 519 ARG A O     1 
ATOM   4084 C CB    . ARG A 1 519 ? 10.684 -36.595 -35.433 1.00 47.73  ? 519 ARG A CB    1 
ATOM   4085 C CG    . ARG A 1 519 ? 11.825 -37.033 -36.328 1.00 45.23  ? 519 ARG A CG    1 
ATOM   4086 C CD    . ARG A 1 519 ? 12.122 -35.966 -37.364 1.00 43.98  ? 519 ARG A CD    1 
ATOM   4087 N NE    . ARG A 1 519 ? 12.674 -36.567 -38.580 1.00 46.12  ? 519 ARG A NE    1 
ATOM   4088 C CZ    . ARG A 1 519 ? 13.939 -36.968 -38.766 1.00 39.88  ? 519 ARG A CZ    1 
ATOM   4089 N NH1   . ARG A 1 519 ? 14.921 -36.505 -38.014 1.00 37.45  ? 519 ARG A NH1   1 
ATOM   4090 N NH2   . ARG A 1 519 ? 14.232 -37.771 -39.777 1.00 33.70  ? 519 ARG A NH2   1 
ATOM   4091 N N     . MET B 1 1   ? 41.392 -28.247 -77.327 1.00 62.98  ? 1   MET B N     1 
ATOM   4092 C CA    . MET B 1 1   ? 40.341 -29.289 -77.501 1.00 61.57  ? 1   MET B CA    1 
ATOM   4093 C C     . MET B 1 1   ? 39.129 -29.004 -76.609 1.00 55.70  ? 1   MET B C     1 
ATOM   4094 O O     . MET B 1 1   ? 39.168 -28.173 -75.702 1.00 55.34  ? 1   MET B O     1 
ATOM   4095 C CB    . MET B 1 1   ? 40.867 -30.699 -77.189 1.00 64.02  ? 1   MET B CB    1 
ATOM   4096 C CG    . MET B 1 1   ? 42.030 -30.752 -76.221 1.00 67.12  ? 1   MET B CG    1 
ATOM   4097 S SD    . MET B 1 1   ? 42.180 -32.373 -75.423 1.00 75.21  ? 1   MET B SD    1 
ATOM   4098 C CE    . MET B 1 1   ? 40.811 -32.291 -74.269 1.00 83.30  ? 1   MET B CE    1 
ATOM   4099 N N     . ALA B 1 2   ? 38.046 -29.740 -76.885 1.00 46.70  ? 2   ALA B N     1 
ATOM   4100 C CA    . ALA B 1 2   ? 36.795 -29.637 -76.161 1.00 39.70  ? 2   ALA B CA    1 
ATOM   4101 C C     . ALA B 1 2   ? 36.907 -30.310 -74.788 1.00 38.94  ? 2   ALA B C     1 
ATOM   4102 O O     . ALA B 1 2   ? 37.707 -31.231 -74.584 1.00 38.67  ? 2   ALA B O     1 
ATOM   4103 C CB    . ALA B 1 2   ? 35.702 -30.263 -76.990 1.00 37.75  ? 2   ALA B CB    1 
ATOM   4104 N N     . ALA B 1 3   ? 36.082 -29.836 -73.845 1.00 32.91  ? 3   ALA B N     1 
ATOM   4105 C CA    . ALA B 1 3   ? 35.932 -30.470 -72.548 1.00 32.12  ? 3   ALA B CA    1 
ATOM   4106 C C     . ALA B 1 3   ? 35.396 -31.893 -72.722 1.00 31.33  ? 3   ALA B C     1 
ATOM   4107 O O     . ALA B 1 3   ? 34.474 -32.132 -73.495 1.00 31.70  ? 3   ALA B O     1 
ATOM   4108 C CB    . ALA B 1 3   ? 35.020 -29.630 -71.684 1.00 30.86  ? 3   ALA B CB    1 
ATOM   4109 N N     . PRO B 1 4   ? 35.916 -32.892 -71.983 1.00 29.71  ? 4   PRO B N     1 
ATOM   4110 C CA    . PRO B 1 4   ? 35.296 -34.207 -71.951 1.00 29.99  ? 4   PRO B CA    1 
ATOM   4111 C C     . PRO B 1 4   ? 34.021 -34.145 -71.125 1.00 31.08  ? 4   PRO B C     1 
ATOM   4112 O O     . PRO B 1 4   ? 33.855 -33.240 -70.313 1.00 31.67  ? 4   PRO B O     1 
ATOM   4113 C CB    . PRO B 1 4   ? 36.336 -35.097 -71.252 1.00 32.05  ? 4   PRO B CB    1 
ATOM   4114 C CG    . PRO B 1 4   ? 37.112 -34.140 -70.380 1.00 32.45  ? 4   PRO B CG    1 
ATOM   4115 C CD    . PRO B 1 4   ? 37.111 -32.823 -71.136 1.00 32.67  ? 4   PRO B CD    1 
ATOM   4116 N N     . LEU B 1 5   ? 33.139 -35.126 -71.332 1.00 31.34  ? 5   LEU B N     1 
ATOM   4117 C CA    . LEU B 1 5   ? 32.026 -35.349 -70.436 1.00 31.38  ? 5   LEU B CA    1 
ATOM   4118 C C     . LEU B 1 5   ? 32.574 -35.679 -69.054 1.00 37.45  ? 5   LEU B C     1 
ATOM   4119 O O     . LEU B 1 5   ? 33.665 -36.238 -68.930 1.00 37.68  ? 5   LEU B O     1 
ATOM   4120 C CB    . LEU B 1 5   ? 31.185 -36.502 -70.963 1.00 30.86  ? 5   LEU B CB    1 
ATOM   4121 C CG    . LEU B 1 5   ? 30.414 -36.196 -72.238 1.00 33.13  ? 5   LEU B CG    1 
ATOM   4122 C CD1   . LEU B 1 5   ? 29.902 -37.480 -72.878 1.00 33.83  ? 5   LEU B CD1   1 
ATOM   4123 C CD2   . LEU B 1 5   ? 29.255 -35.252 -71.941 1.00 33.72  ? 5   LEU B CD2   1 
ATOM   4124 N N     . PRO B 1 6   ? 31.826 -35.351 -67.976 1.00 39.36  ? 6   PRO B N     1 
ATOM   4125 C CA    . PRO B 1 6   ? 32.167 -35.836 -66.649 1.00 37.86  ? 6   PRO B CA    1 
ATOM   4126 C C     . PRO B 1 6   ? 31.934 -37.339 -66.665 1.00 39.49  ? 6   PRO B C     1 
ATOM   4127 O O     . PRO B 1 6   ? 31.025 -37.817 -67.341 1.00 36.50  ? 6   PRO B O     1 
ATOM   4128 C CB    . PRO B 1 6   ? 31.213 -35.068 -65.735 1.00 38.27  ? 6   PRO B CB    1 
ATOM   4129 C CG    . PRO B 1 6   ? 30.015 -34.783 -66.601 1.00 37.37  ? 6   PRO B CG    1 
ATOM   4130 C CD    . PRO B 1 6   ? 30.579 -34.569 -67.986 1.00 37.65  ? 6   PRO B CD    1 
ATOM   4131 N N     . GLU B 1 7   ? 32.778 -38.064 -65.927 1.00 43.72  ? 7   GLU B N     1 
ATOM   4132 C CA    . GLU B 1 7   ? 32.712 -39.512 -65.876 1.00 41.82  ? 7   GLU B CA    1 
ATOM   4133 C C     . GLU B 1 7   ? 31.397 -39.916 -65.230 1.00 38.27  ? 7   GLU B C     1 
ATOM   4134 O O     . GLU B 1 7   ? 30.943 -39.279 -64.279 1.00 34.90  ? 7   GLU B O     1 
ATOM   4135 C CB    . GLU B 1 7   ? 33.903 -40.069 -65.101 1.00 47.72  ? 7   GLU B CB    1 
ATOM   4136 C CG    . GLU B 1 7   ? 33.894 -41.580 -64.965 1.00 54.29  ? 7   GLU B CG    1 
ATOM   4137 C CD    . GLU B 1 7   ? 35.153 -42.139 -64.319 1.00 66.69  ? 7   GLU B CD    1 
ATOM   4138 O OE1   . GLU B 1 7   ? 36.021 -41.337 -63.898 1.00 66.24  ? 7   GLU B OE1   1 
ATOM   4139 O OE2   . GLU B 1 7   ? 35.273 -43.377 -64.245 1.00 76.07  ? 7   GLU B OE2   1 
ATOM   4140 N N     . GLY B 1 8   ? 30.806 -40.974 -65.789 1.00 35.92  ? 8   GLY B N     1 
ATOM   4141 C CA    . GLY B 1 8   ? 29.538 -41.507 -65.340 1.00 33.27  ? 8   GLY B CA    1 
ATOM   4142 C C     . GLY B 1 8   ? 28.355 -40.877 -66.058 1.00 35.41  ? 8   GLY B C     1 
ATOM   4143 O O     . GLY B 1 8   ? 27.223 -41.172 -65.714 1.00 43.28  ? 8   GLY B O     1 
ATOM   4144 N N     . VAL B 1 9   ? 28.607 -39.982 -67.013 1.00 36.39  ? 9   VAL B N     1 
ATOM   4145 C CA    . VAL B 1 9   ? 27.532 -39.285 -67.704 1.00 37.25  ? 9   VAL B CA    1 
ATOM   4146 C C     . VAL B 1 9   ? 27.724 -39.411 -69.212 1.00 39.38  ? 9   VAL B C     1 
ATOM   4147 O O     . VAL B 1 9   ? 28.773 -39.040 -69.762 1.00 40.62  ? 9   VAL B O     1 
ATOM   4148 C CB    . VAL B 1 9   ? 27.447 -37.807 -67.296 1.00 37.71  ? 9   VAL B CB    1 
ATOM   4149 C CG1   . VAL B 1 9   ? 26.492 -37.031 -68.181 1.00 36.98  ? 9   VAL B CG1   1 
ATOM   4150 C CG2   . VAL B 1 9   ? 27.068 -37.656 -65.836 1.00 43.71  ? 9   VAL B CG2   1 
ATOM   4151 N N     . SER B 1 10  ? 26.664 -39.911 -69.854 1.00 39.02  ? 10  SER B N     1 
ATOM   4152 C CA    . SER B 1 10  ? 26.653 -40.177 -71.283 1.00 39.59  ? 10  SER B CA    1 
ATOM   4153 C C     . SER B 1 10  ? 26.375 -38.882 -72.038 1.00 38.58  ? 10  SER B C     1 
ATOM   4154 O O     . SER B 1 10  ? 25.917 -37.906 -71.453 1.00 34.90  ? 10  SER B O     1 
ATOM   4155 C CB    . SER B 1 10  ? 25.607 -41.214 -71.602 1.00 40.19  ? 10  SER B CB    1 
ATOM   4156 O OG    . SER B 1 10  ? 24.317 -40.799 -71.148 1.00 42.81  ? 10  SER B OG    1 
ATOM   4157 N N     . ALA B 1 11  ? 26.614 -38.909 -73.349 1.00 41.04  ? 11  ALA B N     1 
ATOM   4158 C CA    . ALA B 1 11  ? 26.331 -37.780 -74.217 1.00 43.59  ? 11  ALA B CA    1 
ATOM   4159 C C     . ALA B 1 11  ? 24.836 -37.474 -74.195 1.00 42.93  ? 11  ALA B C     1 
ATOM   4160 O O     . ALA B 1 11  ? 24.443 -36.319 -74.192 1.00 42.73  ? 11  ALA B O     1 
ATOM   4161 C CB    . ALA B 1 11  ? 26.811 -38.084 -75.612 1.00 42.48  ? 11  ALA B CB    1 
ATOM   4162 N N     . GLU B 1 12  ? 24.019 -38.529 -74.136 1.00 45.17  ? 12  GLU B N     1 
ATOM   4163 C CA    . GLU B 1 12  ? 22.568 -38.419 -74.172 1.00 46.40  ? 12  GLU B CA    1 
ATOM   4164 C C     . GLU B 1 12  ? 22.050 -37.755 -72.891 1.00 40.74  ? 12  GLU B C     1 
ATOM   4165 O O     . GLU B 1 12  ? 21.122 -36.959 -72.940 1.00 33.72  ? 12  GLU B O     1 
ATOM   4166 C CB    . GLU B 1 12  ? 21.938 -39.801 -74.403 1.00 50.70  ? 12  GLU B CB    1 
ATOM   4167 C CG    . GLU B 1 12  ? 22.338 -40.453 -75.739 1.00 60.44  ? 12  GLU B CG    1 
ATOM   4168 C CD    . GLU B 1 12  ? 23.767 -40.993 -75.898 1.00 66.81  ? 12  GLU B CD    1 
ATOM   4169 O OE1   . GLU B 1 12  ? 24.423 -41.354 -74.873 1.00 61.64  ? 12  GLU B OE1   1 
ATOM   4170 O OE2   . GLU B 1 12  ? 24.249 -41.038 -77.057 1.00 61.10  ? 12  GLU B OE2   1 
ATOM   4171 N N     . ALA B 1 13  ? 22.640 -38.076 -71.733 1.00 36.04  ? 13  ALA B N     1 
ATOM   4172 C CA    . ALA B 1 13  ? 22.225 -37.448 -70.493 1.00 37.56  ? 13  ALA B CA    1 
ATOM   4173 C C     . ALA B 1 13  ? 22.646 -35.974 -70.484 1.00 36.96  ? 13  ALA B C     1 
ATOM   4174 O O     . ALA B 1 13  ? 21.895 -35.107 -70.037 1.00 35.01  ? 13  ALA B O     1 
ATOM   4175 C CB    . ALA B 1 13  ? 22.802 -38.216 -69.330 1.00 39.04  ? 13  ALA B CB    1 
ATOM   4176 N N     . MET B 1 14  ? 23.835 -35.682 -71.023 1.00 35.76  ? 14  MET B N     1 
ATOM   4177 C CA    . MET B 1 14  ? 24.352 -34.326 -70.998 1.00 38.05  ? 14  MET B CA    1 
ATOM   4178 C C     . MET B 1 14  ? 23.484 -33.475 -71.918 1.00 36.44  ? 14  MET B C     1 
ATOM   4179 O O     . MET B 1 14  ? 22.950 -32.432 -71.524 1.00 36.75  ? 14  MET B O     1 
ATOM   4180 C CB    . MET B 1 14  ? 25.824 -34.275 -71.433 1.00 37.11  ? 14  MET B CB    1 
ATOM   4181 C CG    . MET B 1 14  ? 26.412 -32.858 -71.493 1.00 38.12  ? 14  MET B CG    1 
ATOM   4182 S SD    . MET B 1 14  ? 26.326 -31.940 -69.907 1.00 33.58  ? 14  MET B SD    1 
ATOM   4183 C CE    . MET B 1 14  ? 27.710 -32.719 -69.083 1.00 33.99  ? 14  MET B CE    1 
ATOM   4184 N N     . SER B 1 15  ? 23.340 -33.968 -73.144 1.00 34.71  ? 15  SER B N     1 
ATOM   4185 C CA    . SER B 1 15  ? 22.545 -33.321 -74.177 1.00 34.56  ? 15  SER B CA    1 
ATOM   4186 C C     . SER B 1 15  ? 21.146 -32.983 -73.667 1.00 31.41  ? 15  SER B C     1 
ATOM   4187 O O     . SER B 1 15  ? 20.654 -31.891 -73.908 1.00 31.45  ? 15  SER B O     1 
ATOM   4188 C CB    . SER B 1 15  ? 22.496 -34.198 -75.401 1.00 34.98  ? 15  SER B CB    1 
ATOM   4189 O OG    . SER B 1 15  ? 21.434 -33.799 -76.238 1.00 39.98  ? 15  SER B OG    1 
ATOM   4190 N N     . SER B 1 16  ? 20.527 -33.924 -72.942 1.00 32.31  ? 16  SER B N     1 
ATOM   4191 C CA    . SER B 1 16  ? 19.189 -33.760 -72.396 1.00 33.22  ? 16  SER B CA    1 
ATOM   4192 C C     . SER B 1 16  ? 19.153 -32.726 -71.268 1.00 33.14  ? 16  SER B C     1 
ATOM   4193 O O     . SER B 1 16  ? 18.280 -31.841 -71.241 1.00 33.09  ? 16  SER B O     1 
ATOM   4194 C CB    . SER B 1 16  ? 18.669 -35.073 -71.909 1.00 34.90  ? 16  SER B CB    1 
ATOM   4195 O OG    . SER B 1 16  ? 18.328 -35.900 -73.000 1.00 38.47  ? 16  SER B OG    1 
ATOM   4196 N N     . ALA B 1 17  ? 20.076 -32.875 -70.309 1.00 29.50  ? 17  ALA B N     1 
ATOM   4197 C CA    . ALA B 1 17  ? 20.235 -31.866 -69.270 1.00 28.85  ? 17  ALA B CA    1 
ATOM   4198 C C     . ALA B 1 17  ? 20.378 -30.475 -69.888 1.00 25.91  ? 17  ALA B C     1 
ATOM   4199 O O     . ALA B 1 17  ? 19.666 -29.564 -69.490 1.00 24.77  ? 17  ALA B O     1 
ATOM   4200 C CB    . ALA B 1 17  ? 21.395 -32.195 -68.359 1.00 29.02  ? 17  ALA B CB    1 
ATOM   4201 N N     . LEU B 1 18  ? 21.264 -30.308 -70.869 1.00 25.30  ? 18  LEU B N     1 
ATOM   4202 C CA    . LEU B 1 18  ? 21.496 -28.983 -71.428 1.00 27.87  ? 18  LEU B CA    1 
ATOM   4203 C C     . LEU B 1 18  ? 20.242 -28.413 -72.096 1.00 30.08  ? 18  LEU B C     1 
ATOM   4204 O O     . LEU B 1 18  ? 19.936 -27.230 -71.923 1.00 29.94  ? 18  LEU B O     1 
ATOM   4205 C CB    . LEU B 1 18  ? 22.664 -29.042 -72.415 1.00 30.04  ? 18  LEU B CB    1 
ATOM   4206 C CG    . LEU B 1 18  ? 24.045 -29.312 -71.810 1.00 30.29  ? 18  LEU B CG    1 
ATOM   4207 C CD1   . LEU B 1 18  ? 25.129 -29.144 -72.876 1.00 31.20  ? 18  LEU B CD1   1 
ATOM   4208 C CD2   . LEU B 1 18  ? 24.309 -28.405 -70.620 1.00 27.97  ? 18  LEU B CD2   1 
ATOM   4209 N N     . ASP B 1 19  ? 19.484 -29.247 -72.824 1.00 32.85  ? 19  ASP B N     1 
ATOM   4210 C CA    . ASP B 1 19  ? 18.235 -28.775 -73.405 1.00 33.73  ? 19  ASP B CA    1 
ATOM   4211 C C     . ASP B 1 19  ? 17.213 -28.473 -72.294 1.00 31.72  ? 19  ASP B C     1 
ATOM   4212 O O     . ASP B 1 19  ? 16.483 -27.487 -72.394 1.00 31.81  ? 19  ASP B O     1 
ATOM   4213 C CB    . ASP B 1 19  ? 17.716 -29.695 -74.521 1.00 36.19  ? 19  ASP B CB    1 
ATOM   4214 C CG    . ASP B 1 19  ? 16.464 -29.135 -75.193 1.00 41.65  ? 19  ASP B CG    1 
ATOM   4215 O OD1   . ASP B 1 19  ? 16.569 -28.089 -75.885 1.00 43.33  ? 19  ASP B OD1   1 
ATOM   4216 O OD2   . ASP B 1 19  ? 15.363 -29.691 -74.956 1.00 43.97  ? 19  ASP B OD2   1 
ATOM   4217 N N     . ARG B 1 20  ? 17.183 -29.248 -71.205 1.00 29.71  ? 20  ARG B N     1 
ATOM   4218 C CA    . ARG B 1 20  ? 16.248 -28.966 -70.116 1.00 30.62  ? 20  ARG B CA    1 
ATOM   4219 C C     . ARG B 1 20  ? 16.619 -27.669 -69.396 1.00 28.67  ? 20  ARG B C     1 
ATOM   4220 O O     . ARG B 1 20  ? 15.762 -26.887 -68.965 1.00 27.90  ? 20  ARG B O     1 
ATOM   4221 C CB    . ARG B 1 20  ? 16.214 -30.131 -69.122 1.00 31.95  ? 20  ARG B CB    1 
ATOM   4222 C CG    . ARG B 1 20  ? 15.683 -31.437 -69.699 1.00 33.99  ? 20  ARG B CG    1 
ATOM   4223 C CD    . ARG B 1 20  ? 14.168 -31.521 -69.749 1.00 33.32  ? 20  ARG B CD    1 
ATOM   4224 N NE    . ARG B 1 20  ? 13.552 -31.282 -68.454 1.00 35.90  ? 20  ARG B NE    1 
ATOM   4225 C CZ    . ARG B 1 20  ? 13.524 -32.139 -67.436 1.00 35.85  ? 20  ARG B CZ    1 
ATOM   4226 N NH1   . ARG B 1 20  ? 13.986 -33.369 -67.599 1.00 36.32  ? 20  ARG B NH1   1 
ATOM   4227 N NH2   . ARG B 1 20  ? 12.973 -31.776 -66.280 1.00 32.24  ? 20  ARG B NH2   1 
ATOM   4228 N N     . PHE B 1 21  ? 17.918 -27.442 -69.256 1.00 28.23  ? 21  PHE B N     1 
ATOM   4229 C CA    . PHE B 1 21  ? 18.387 -26.206 -68.669 1.00 27.86  ? 21  PHE B CA    1 
ATOM   4230 C C     . PHE B 1 21  ? 17.851 -25.067 -69.516 1.00 29.77  ? 21  PHE B C     1 
ATOM   4231 O O     . PHE B 1 21  ? 17.298 -24.120 -68.971 1.00 29.45  ? 21  PHE B O     1 
ATOM   4232 C CB    . PHE B 1 21  ? 19.915 -26.167 -68.582 1.00 27.22  ? 21  PHE B CB    1 
ATOM   4233 C CG    . PHE B 1 21  ? 20.554 -27.061 -67.549 1.00 24.42  ? 21  PHE B CG    1 
ATOM   4234 C CD1   . PHE B 1 21  ? 19.890 -27.448 -66.404 1.00 25.25  ? 21  PHE B CD1   1 
ATOM   4235 C CD2   . PHE B 1 21  ? 21.831 -27.540 -67.751 1.00 26.70  ? 21  PHE B CD2   1 
ATOM   4236 C CE1   . PHE B 1 21  ? 20.485 -28.290 -65.479 1.00 25.96  ? 21  PHE B CE1   1 
ATOM   4237 C CE2   . PHE B 1 21  ? 22.429 -28.385 -66.830 1.00 28.37  ? 21  PHE B CE2   1 
ATOM   4238 C CZ    . PHE B 1 21  ? 21.758 -28.756 -65.691 1.00 27.35  ? 21  PHE B CZ    1 
ATOM   4239 N N     . ALA B 1 22  ? 17.967 -25.206 -70.844 1.00 30.18  ? 22  ALA B N     1 
ATOM   4240 C CA    . ALA B 1 22  ? 17.542 -24.161 -71.768 1.00 28.71  ? 22  ALA B CA    1 
ATOM   4241 C C     . ALA B 1 22  ? 16.042 -23.872 -71.643 1.00 29.17  ? 22  ALA B C     1 
ATOM   4242 O O     . ALA B 1 22  ? 15.626 -22.722 -71.759 1.00 29.87  ? 22  ALA B O     1 
ATOM   4243 C CB    . ALA B 1 22  ? 17.928 -24.524 -73.181 1.00 27.92  ? 22  ALA B CB    1 
ATOM   4244 N N     . ARG B 1 23  ? 15.230 -24.894 -71.371 1.00 28.20  ? 23  ARG B N     1 
ATOM   4245 C CA    . ARG B 1 23  ? 13.800 -24.685 -71.194 1.00 30.22  ? 23  ARG B CA    1 
ATOM   4246 C C     . ARG B 1 23  ? 13.552 -23.855 -69.931 1.00 30.21  ? 23  ARG B C     1 
ATOM   4247 O O     . ARG B 1 23  ? 12.551 -23.165 -69.819 1.00 30.37  ? 23  ARG B O     1 
ATOM   4248 C CB    . ARG B 1 23  ? 13.029 -26.001 -71.055 1.00 34.82  ? 23  ARG B CB    1 
ATOM   4249 C CG    . ARG B 1 23  ? 13.254 -27.039 -72.149 1.00 39.94  ? 23  ARG B CG    1 
ATOM   4250 C CD    . ARG B 1 23  ? 12.742 -26.594 -73.501 1.00 44.56  ? 23  ARG B CD    1 
ATOM   4251 N NE    . ARG B 1 23  ? 12.968 -27.528 -74.604 1.00 47.93  ? 23  ARG B NE    1 
ATOM   4252 C CZ    . ARG B 1 23  ? 12.544 -27.323 -75.853 1.00 43.15  ? 23  ARG B CZ    1 
ATOM   4253 N NH1   . ARG B 1 23  ? 11.656 -26.387 -76.112 1.00 35.29  ? 23  ARG B NH1   1 
ATOM   4254 N NH2   . ARG B 1 23  ? 12.994 -28.074 -76.841 1.00 51.53  ? 23  ARG B NH2   1 
ATOM   4255 N N     . ILE B 1 24  ? 14.464 -23.935 -68.963 1.00 30.50  ? 24  ILE B N     1 
ATOM   4256 C CA    . ILE B 1 24  ? 14.350 -23.195 -67.718 1.00 28.27  ? 24  ILE B CA    1 
ATOM   4257 C C     . ILE B 1 24  ? 14.805 -21.741 -67.895 1.00 27.97  ? 24  ILE B C     1 
ATOM   4258 O O     . ILE B 1 24  ? 14.070 -20.845 -67.522 1.00 27.14  ? 24  ILE B O     1 
ATOM   4259 C CB    . ILE B 1 24  ? 15.148 -23.905 -66.614 1.00 27.58  ? 24  ILE B CB    1 
ATOM   4260 C CG1   . ILE B 1 24  ? 14.602 -25.309 -66.352 1.00 28.35  ? 24  ILE B CG1   1 
ATOM   4261 C CG2   . ILE B 1 24  ? 15.180 -23.057 -65.359 1.00 29.14  ? 24  ILE B CG2   1 
ATOM   4262 C CD1   . ILE B 1 24  ? 15.561 -26.207 -65.609 1.00 28.63  ? 24  ILE B CD1   1 
ATOM   4263 N N     . VAL B 1 25  ? 15.990 -21.483 -68.467 1.00 28.66  ? 25  VAL B N     1 
ATOM   4264 C CA    . VAL B 1 25  ? 16.570 -20.141 -68.425 1.00 28.98  ? 25  VAL B CA    1 
ATOM   4265 C C     . VAL B 1 25  ? 16.392 -19.398 -69.748 1.00 27.27  ? 25  VAL B C     1 
ATOM   4266 O O     . VAL B 1 25  ? 16.544 -18.181 -69.763 1.00 28.03  ? 25  VAL B O     1 
ATOM   4267 C CB    . VAL B 1 25  ? 18.057 -20.153 -68.019 1.00 29.33  ? 25  VAL B CB    1 
ATOM   4268 C CG1   . VAL B 1 25  ? 18.238 -20.734 -66.640 1.00 29.46  ? 25  VAL B CG1   1 
ATOM   4269 C CG2   . VAL B 1 25  ? 18.945 -20.894 -69.014 1.00 31.72  ? 25  VAL B CG2   1 
ATOM   4270 N N     . GLY B 1 26  ? 16.054 -20.123 -70.824 1.00 27.87  ? 26  GLY B N     1 
ATOM   4271 C CA    . GLY B 1 26  ? 16.045 -19.597 -72.180 1.00 28.86  ? 26  GLY B CA    1 
ATOM   4272 C C     . GLY B 1 26  ? 17.273 -20.078 -72.957 1.00 31.76  ? 26  GLY B C     1 
ATOM   4273 O O     . GLY B 1 26  ? 18.340 -20.280 -72.374 1.00 32.00  ? 26  GLY B O     1 
ATOM   4274 N N     . ALA B 1 27  ? 17.149 -20.228 -74.278 1.00 31.49  ? 27  ALA B N     1 
ATOM   4275 C CA    . ALA B 1 27  ? 18.246 -20.776 -75.062 1.00 32.04  ? 27  ALA B CA    1 
ATOM   4276 C C     . ALA B 1 27  ? 19.410 -19.781 -75.105 1.00 30.58  ? 27  ALA B C     1 
ATOM   4277 O O     . ALA B 1 27  ? 20.561 -20.168 -75.275 1.00 30.58  ? 27  ALA B O     1 
ATOM   4278 C CB    . ALA B 1 27  ? 17.762 -21.160 -76.448 1.00 33.51  ? 27  ALA B CB    1 
ATOM   4279 N N     . ASP B 1 28  ? 19.148 -18.491 -74.895 1.00 32.57  ? 28  ASP B N     1 
ATOM   4280 C CA    . ASP B 1 28  ? 20.224 -17.510 -74.949 1.00 31.21  ? 28  ASP B CA    1 
ATOM   4281 C C     . ASP B 1 28  ? 21.114 -17.604 -73.713 1.00 28.61  ? 28  ASP B C     1 
ATOM   4282 O O     . ASP B 1 28  ? 22.148 -16.947 -73.645 1.00 28.15  ? 28  ASP B O     1 
ATOM   4283 C CB    . ASP B 1 28  ? 19.680 -16.087 -75.115 1.00 35.83  ? 28  ASP B CB    1 
ATOM   4284 C CG    . ASP B 1 28  ? 18.729 -15.906 -76.304 1.00 40.47  ? 28  ASP B CG    1 
ATOM   4285 O OD1   . ASP B 1 28  ? 18.958 -16.531 -77.348 1.00 36.15  ? 28  ASP B OD1   1 
ATOM   4286 O OD2   . ASP B 1 28  ? 17.771 -15.110 -76.185 1.00 44.56  ? 28  ASP B OD2   1 
ATOM   4287 N N     . TRP B 1 29  ? 20.727 -18.430 -72.732 1.00 30.37  ? 29  TRP B N     1 
ATOM   4288 C CA    . TRP B 1 29  ? 21.377 -18.418 -71.428 1.00 28.95  ? 29  TRP B CA    1 
ATOM   4289 C C     . TRP B 1 29  ? 22.007 -19.766 -71.086 1.00 28.49  ? 29  TRP B C     1 
ATOM   4290 O O     . TRP B 1 29  ? 22.338 -20.021 -69.927 1.00 23.94  ? 29  TRP B O     1 
ATOM   4291 C CB    . TRP B 1 29  ? 20.388 -17.907 -70.378 1.00 27.07  ? 29  TRP B CB    1 
ATOM   4292 C CG    . TRP B 1 29  ? 19.972 -16.497 -70.681 1.00 27.95  ? 29  TRP B CG    1 
ATOM   4293 C CD1   . TRP B 1 29  ? 18.724 -16.070 -71.033 1.00 28.54  ? 29  TRP B CD1   1 
ATOM   4294 C CD2   . TRP B 1 29  ? 20.817 -15.330 -70.737 1.00 25.95  ? 29  TRP B CD2   1 
ATOM   4295 N NE1   . TRP B 1 29  ? 18.732 -14.718 -71.270 1.00 30.50  ? 29  TRP B NE1   1 
ATOM   4296 C CE2   . TRP B 1 29  ? 19.996 -14.234 -71.081 1.00 25.84  ? 29  TRP B CE2   1 
ATOM   4297 C CE3   . TRP B 1 29  ? 22.167 -15.083 -70.464 1.00 29.17  ? 29  TRP B CE3   1 
ATOM   4298 C CZ2   . TRP B 1 29  ? 20.477 -12.930 -71.185 1.00 26.39  ? 29  TRP B CZ2   1 
ATOM   4299 C CZ3   . TRP B 1 29  ? 22.648 -13.784 -70.560 1.00 28.62  ? 29  TRP B CZ3   1 
ATOM   4300 C CH2   . TRP B 1 29  ? 21.814 -12.722 -70.923 1.00 26.85  ? 29  TRP B CH2   1 
ATOM   4301 N N     . VAL B 1 30  ? 22.270 -20.575 -72.124 1.00 29.37  ? 30  VAL B N     1 
ATOM   4302 C CA    . VAL B 1 30  ? 23.081 -21.777 -71.963 1.00 31.30  ? 30  VAL B CA    1 
ATOM   4303 C C     . VAL B 1 30  ? 24.250 -21.640 -72.923 1.00 30.56  ? 30  VAL B C     1 
ATOM   4304 O O     . VAL B 1 30  ? 24.043 -21.278 -74.068 1.00 32.51  ? 30  VAL B O     1 
ATOM   4305 C CB    . VAL B 1 30  ? 22.298 -23.082 -72.217 1.00 28.26  ? 30  VAL B CB    1 
ATOM   4306 C CG1   . VAL B 1 30  ? 23.207 -24.297 -72.128 1.00 28.52  ? 30  VAL B CG1   1 
ATOM   4307 C CG2   . VAL B 1 30  ? 21.122 -23.226 -71.266 1.00 27.39  ? 30  VAL B CG2   1 
ATOM   4308 N N     . PHE B 1 31  ? 25.462 -21.918 -72.446 1.00 29.19  ? 31  PHE B N     1 
ATOM   4309 C CA    . PHE B 1 31  ? 26.649 -21.598 -73.211 1.00 29.58  ? 31  PHE B CA    1 
ATOM   4310 C C     . PHE B 1 31  ? 27.448 -22.877 -73.396 1.00 31.36  ? 31  PHE B C     1 
ATOM   4311 O O     . PHE B 1 31  ? 27.814 -23.511 -72.407 1.00 31.82  ? 31  PHE B O     1 
ATOM   4312 C CB    . PHE B 1 31  ? 27.442 -20.474 -72.538 1.00 30.34  ? 31  PHE B CB    1 
ATOM   4313 C CG    . PHE B 1 31  ? 26.635 -19.224 -72.293 1.00 31.71  ? 31  PHE B CG    1 
ATOM   4314 C CD1   . PHE B 1 31  ? 26.326 -18.363 -73.332 1.00 34.08  ? 31  PHE B CD1   1 
ATOM   4315 C CD2   . PHE B 1 31  ? 26.110 -18.949 -71.043 1.00 35.01  ? 31  PHE B CD2   1 
ATOM   4316 C CE1   . PHE B 1 31  ? 25.537 -17.243 -73.124 1.00 33.22  ? 31  PHE B CE1   1 
ATOM   4317 C CE2   . PHE B 1 31  ? 25.350 -17.813 -70.826 1.00 36.61  ? 31  PHE B CE2   1 
ATOM   4318 C CZ    . PHE B 1 31  ? 25.059 -16.966 -71.870 1.00 35.74  ? 31  PHE B CZ    1 
ATOM   4319 N N     . THR B 1 32  ? 27.702 -23.205 -74.673 1.00 30.61  ? 32  THR B N     1 
ATOM   4320 C CA    . THR B 1 32  ? 28.397 -24.413 -75.082 1.00 36.07  ? 32  THR B CA    1 
ATOM   4321 C C     . THR B 1 32  ? 29.430 -24.042 -76.131 1.00 35.65  ? 32  THR B C     1 
ATOM   4322 O O     . THR B 1 32  ? 29.485 -22.891 -76.535 1.00 36.05  ? 32  THR B O     1 
ATOM   4323 C CB    . THR B 1 32  ? 27.415 -25.457 -75.632 1.00 37.38  ? 32  THR B CB    1 
ATOM   4324 O OG1   . THR B 1 32  ? 26.524 -24.815 -76.538 1.00 35.27  ? 32  THR B OG1   1 
ATOM   4325 C CG2   . THR B 1 32  ? 26.583 -26.101 -74.547 1.00 38.33  ? 32  THR B CG2   1 
ATOM   4326 N N     . GLU B 1 33  ? 30.249 -25.017 -76.529 1.00 42.89  ? 33  GLU B N     1 
ATOM   4327 C CA    . GLU B 1 33  ? 31.166 -24.878 -77.656 1.00 48.88  ? 33  GLU B CA    1 
ATOM   4328 C C     . GLU B 1 33  ? 32.005 -23.615 -77.473 1.00 47.55  ? 33  GLU B C     1 
ATOM   4329 O O     . GLU B 1 33  ? 32.676 -23.481 -76.456 1.00 50.19  ? 33  GLU B O     1 
ATOM   4330 C CB    . GLU B 1 33  ? 30.385 -24.969 -78.974 1.00 55.02  ? 33  GLU B CB    1 
ATOM   4331 C CG    . GLU B 1 33  ? 29.732 -26.333 -79.159 1.00 64.33  ? 33  GLU B CG    1 
ATOM   4332 C CD    . GLU B 1 33  ? 29.014 -26.584 -80.477 1.00 75.15  ? 33  GLU B CD    1 
ATOM   4333 O OE1   . GLU B 1 33  ? 29.301 -27.628 -81.094 1.00 82.51  ? 33  GLU B OE1   1 
ATOM   4334 O OE2   . GLU B 1 33  ? 28.161 -25.757 -80.882 1.00 69.95  ? 33  GLU B OE2   1 
ATOM   4335 N N     . ASP B 1 34  ? 31.953 -22.683 -78.432 1.00 47.94  ? 34  ASP B N     1 
ATOM   4336 C CA    . ASP B 1 34  ? 32.872 -21.554 -78.447 1.00 53.15  ? 34  ASP B CA    1 
ATOM   4337 C C     . ASP B 1 34  ? 32.487 -20.541 -77.369 1.00 48.22  ? 34  ASP B C     1 
ATOM   4338 O O     . ASP B 1 34  ? 33.322 -19.737 -76.954 1.00 47.14  ? 34  ASP B O     1 
ATOM   4339 C CB    . ASP B 1 34  ? 32.927 -20.890 -79.829 1.00 63.69  ? 34  ASP B CB    1 
ATOM   4340 C CG    . ASP B 1 34  ? 33.427 -21.793 -80.952 1.00 78.91  ? 34  ASP B CG    1 
ATOM   4341 O OD1   . ASP B 1 34  ? 33.489 -23.028 -80.753 1.00 84.31  ? 34  ASP B OD1   1 
ATOM   4342 O OD2   . ASP B 1 34  ? 33.770 -21.254 -82.025 1.00 88.72  ? 34  ASP B OD2   1 
ATOM   4343 N N     . LYS B 1 35  ? 31.234 -20.594 -76.896 1.00 42.14  ? 35  LYS B N     1 
ATOM   4344 C CA    . LYS B 1 35  ? 30.749 -19.652 -75.900 1.00 43.57  ? 35  LYS B CA    1 
ATOM   4345 C C     . LYS B 1 35  ? 31.262 -19.998 -74.494 1.00 38.07  ? 35  LYS B C     1 
ATOM   4346 O O     . LYS B 1 35  ? 30.966 -19.283 -73.540 1.00 34.06  ? 35  LYS B O     1 
ATOM   4347 C CB    . LYS B 1 35  ? 29.215 -19.626 -75.932 1.00 50.71  ? 35  LYS B CB    1 
ATOM   4348 C CG    . LYS B 1 35  ? 28.588 -19.073 -77.209 1.00 57.84  ? 35  LYS B CG    1 
ATOM   4349 C CD    . LYS B 1 35  ? 28.005 -17.666 -77.101 1.00 64.51  ? 35  LYS B CD    1 
ATOM   4350 C CE    . LYS B 1 35  ? 26.489 -17.630 -77.114 1.00 69.48  ? 35  LYS B CE    1 
ATOM   4351 N NZ    . LYS B 1 35  ? 25.954 -16.250 -76.957 1.00 71.90  ? 35  LYS B NZ    1 
ATOM   4352 N N     . ILE B 1 36  ? 32.013 -21.097 -74.338 1.00 35.76  ? 36  ILE B N     1 
ATOM   4353 C CA    . ILE B 1 36  ? 32.400 -21.558 -73.017 1.00 34.76  ? 36  ILE B CA    1 
ATOM   4354 C C     . ILE B 1 36  ? 33.714 -20.908 -72.585 1.00 32.96  ? 36  ILE B C     1 
ATOM   4355 O O     . ILE B 1 36  ? 34.060 -20.990 -71.406 1.00 30.50  ? 36  ILE B O     1 
ATOM   4356 C CB    . ILE B 1 36  ? 32.469 -23.105 -72.945 1.00 35.90  ? 36  ILE B CB    1 
ATOM   4357 C CG1   . ILE B 1 36  ? 32.373 -23.644 -71.513 1.00 34.53  ? 36  ILE B CG1   1 
ATOM   4358 C CG2   . ILE B 1 36  ? 33.730 -23.646 -73.616 1.00 36.78  ? 36  ILE B CG2   1 
ATOM   4359 C CD1   . ILE B 1 36  ? 31.317 -22.996 -70.655 1.00 38.81  ? 36  ILE B CD1   1 
ATOM   4360 N N     . THR B 1 37  ? 34.442 -20.248 -73.497 1.00 32.76  ? 37  THR B N     1 
ATOM   4361 C CA    . THR B 1 37  ? 35.838 -19.968 -73.198 1.00 37.98  ? 37  THR B CA    1 
ATOM   4362 C C     . THR B 1 37  ? 35.985 -18.859 -72.142 1.00 33.43  ? 37  THR B C     1 
ATOM   4363 O O     . THR B 1 37  ? 36.950 -18.891 -71.399 1.00 32.56  ? 37  THR B O     1 
ATOM   4364 C CB    . THR B 1 37  ? 36.718 -19.780 -74.451 1.00 43.20  ? 37  THR B CB    1 
ATOM   4365 O OG1   . THR B 1 37  ? 36.634 -18.440 -74.894 1.00 40.01  ? 37  THR B OG1   1 
ATOM   4366 C CG2   . THR B 1 37  ? 36.398 -20.714 -75.604 1.00 45.80  ? 37  THR B CG2   1 
ATOM   4367 N N     . PRO B 1 38  ? 35.079 -17.870 -71.958 1.00 31.63  ? 38  PRO B N     1 
ATOM   4368 C CA    . PRO B 1 38  ? 35.139 -17.032 -70.750 1.00 32.02  ? 38  PRO B CA    1 
ATOM   4369 C C     . PRO B 1 38  ? 35.122 -17.799 -69.413 1.00 30.30  ? 38  PRO B C     1 
ATOM   4370 O O     . PRO B 1 38  ? 35.522 -17.262 -68.379 1.00 29.08  ? 38  PRO B O     1 
ATOM   4371 C CB    . PRO B 1 38  ? 33.889 -16.132 -70.875 1.00 31.18  ? 38  PRO B CB    1 
ATOM   4372 C CG    . PRO B 1 38  ? 33.564 -16.097 -72.372 1.00 28.14  ? 38  PRO B CG    1 
ATOM   4373 C CD    . PRO B 1 38  ? 33.998 -17.460 -72.877 1.00 30.15  ? 38  PRO B CD    1 
ATOM   4374 N N     . TYR B 1 39  ? 34.674 -19.061 -69.424 1.00 28.12  ? 39  TYR B N     1 
ATOM   4375 C CA    . TYR B 1 39  ? 34.471 -19.807 -68.192 1.00 28.83  ? 39  TYR B CA    1 
ATOM   4376 C C     . TYR B 1 39  ? 35.729 -20.608 -67.851 1.00 30.52  ? 39  TYR B C     1 
ATOM   4377 O O     . TYR B 1 39  ? 35.828 -21.176 -66.756 1.00 31.00  ? 39  TYR B O     1 
ATOM   4378 C CB    . TYR B 1 39  ? 33.184 -20.630 -68.285 1.00 28.17  ? 39  TYR B CB    1 
ATOM   4379 C CG    . TYR B 1 39  ? 31.924 -19.794 -68.199 1.00 31.53  ? 39  TYR B CG    1 
ATOM   4380 C CD1   . TYR B 1 39  ? 31.387 -19.399 -66.977 1.00 31.26  ? 39  TYR B CD1   1 
ATOM   4381 C CD2   . TYR B 1 39  ? 31.285 -19.357 -69.350 1.00 34.78  ? 39  TYR B CD2   1 
ATOM   4382 C CE1   . TYR B 1 39  ? 30.248 -18.612 -66.899 1.00 30.96  ? 39  TYR B CE1   1 
ATOM   4383 C CE2   . TYR B 1 39  ? 30.159 -18.548 -69.295 1.00 33.97  ? 39  TYR B CE2   1 
ATOM   4384 C CZ    . TYR B 1 39  ? 29.642 -18.171 -68.068 1.00 33.91  ? 39  TYR B CZ    1 
ATOM   4385 O OH    . TYR B 1 39  ? 28.524 -17.371 -68.083 1.00 33.02  ? 39  TYR B OH    1 
ATOM   4386 N N     . GLU B 1 40  ? 36.721 -20.571 -68.757 1.00 28.17  ? 40  GLU B N     1 
ATOM   4387 C CA    . GLU B 1 40  ? 38.012 -21.199 -68.524 1.00 28.74  ? 40  GLU B CA    1 
ATOM   4388 C C     . GLU B 1 40  ? 38.807 -20.346 -67.535 1.00 28.18  ? 40  GLU B C     1 
ATOM   4389 O O     . GLU B 1 40  ? 38.602 -19.130 -67.467 1.00 25.58  ? 40  GLU B O     1 
ATOM   4390 C CB    . GLU B 1 40  ? 38.822 -21.304 -69.812 1.00 29.45  ? 40  GLU B CB    1 
ATOM   4391 C CG    . GLU B 1 40  ? 38.068 -21.879 -71.004 1.00 32.57  ? 40  GLU B CG    1 
ATOM   4392 C CD    . GLU B 1 40  ? 37.966 -23.393 -71.079 1.00 33.69  ? 40  GLU B CD    1 
ATOM   4393 O OE1   . GLU B 1 40  ? 38.438 -24.059 -70.136 1.00 34.51  ? 40  GLU B OE1   1 
ATOM   4394 O OE2   . GLU B 1 40  ? 37.417 -23.896 -72.091 1.00 36.48  ? 40  GLU B OE2   1 
ATOM   4395 N N     . ASP B 1 41  ? 39.719 -20.991 -66.787 1.00 26.46  ? 41  ASP B N     1 
ATOM   4396 C CA    . ASP B 1 41  ? 40.653 -20.265 -65.943 1.00 27.50  ? 41  ASP B CA    1 
ATOM   4397 C C     . ASP B 1 41  ? 41.482 -19.371 -66.865 1.00 26.83  ? 41  ASP B C     1 
ATOM   4398 O O     . ASP B 1 41  ? 42.140 -19.862 -67.771 1.00 26.76  ? 41  ASP B O     1 
ATOM   4399 C CB    . ASP B 1 41  ? 41.505 -21.212 -65.088 1.00 27.61  ? 41  ASP B CB    1 
ATOM   4400 C CG    . ASP B 1 41  ? 42.566 -20.538 -64.222 1.00 28.60  ? 41  ASP B CG    1 
ATOM   4401 O OD1   . ASP B 1 41  ? 42.562 -19.309 -64.123 1.00 27.64  ? 41  ASP B OD1   1 
ATOM   4402 O OD2   . ASP B 1 41  ? 43.414 -21.260 -63.645 1.00 34.03  ? 41  ASP B OD2   1 
ATOM   4403 N N     . PRO B 1 42  ? 41.430 -18.029 -66.722 1.00 26.00  ? 42  PRO B N     1 
ATOM   4404 C CA    . PRO B 1 42  ? 42.256 -17.161 -67.545 1.00 28.78  ? 42  PRO B CA    1 
ATOM   4405 C C     . PRO B 1 42  ? 43.745 -17.373 -67.290 1.00 29.94  ? 42  PRO B C     1 
ATOM   4406 O O     . PRO B 1 42  ? 44.526 -17.066 -68.175 1.00 30.72  ? 42  PRO B O     1 
ATOM   4407 C CB    . PRO B 1 42  ? 41.848 -15.733 -67.156 1.00 27.14  ? 42  PRO B CB    1 
ATOM   4408 C CG    . PRO B 1 42  ? 41.264 -15.893 -65.759 1.00 28.20  ? 42  PRO B CG    1 
ATOM   4409 C CD    . PRO B 1 42  ? 40.611 -17.264 -65.766 1.00 27.34  ? 42  PRO B CD    1 
ATOM   4410 N N     . TYR B 1 43  ? 44.116 -17.879 -66.103 1.00 29.96  ? 43  TYR B N     1 
ATOM   4411 C CA    . TYR B 1 43  ? 45.513 -18.039 -65.711 1.00 30.39  ? 43  TYR B CA    1 
ATOM   4412 C C     . TYR B 1 43  ? 45.911 -19.520 -65.666 1.00 29.65  ? 43  TYR B C     1 
ATOM   4413 O O     . TYR B 1 43  ? 46.254 -20.063 -64.609 1.00 25.43  ? 43  TYR B O     1 
ATOM   4414 C CB    . TYR B 1 43  ? 45.740 -17.376 -64.353 1.00 30.48  ? 43  TYR B CB    1 
ATOM   4415 C CG    . TYR B 1 43  ? 45.300 -15.937 -64.208 1.00 29.42  ? 43  TYR B CG    1 
ATOM   4416 C CD1   . TYR B 1 43  ? 45.236 -15.058 -65.281 1.00 28.31  ? 43  TYR B CD1   1 
ATOM   4417 C CD2   . TYR B 1 43  ? 44.983 -15.447 -62.953 1.00 26.41  ? 43  TYR B CD2   1 
ATOM   4418 C CE1   . TYR B 1 43  ? 44.856 -13.732 -65.109 1.00 28.34  ? 43  TYR B CE1   1 
ATOM   4419 C CE2   . TYR B 1 43  ? 44.577 -14.140 -62.767 1.00 28.28  ? 43  TYR B CE2   1 
ATOM   4420 C CZ    . TYR B 1 43  ? 44.522 -13.276 -63.844 1.00 29.87  ? 43  TYR B CZ    1 
ATOM   4421 O OH    . TYR B 1 43  ? 44.132 -11.991 -63.585 1.00 29.93  ? 43  TYR B OH    1 
ATOM   4422 N N     . THR B 1 44  ? 45.865 -20.165 -66.839 1.00 31.29  ? 44  THR B N     1 
ATOM   4423 C CA    . THR B 1 44  ? 46.055 -21.608 -67.004 1.00 32.80  ? 44  THR B CA    1 
ATOM   4424 C C     . THR B 1 44  ? 47.294 -22.126 -66.274 1.00 32.79  ? 44  THR B C     1 
ATOM   4425 O O     . THR B 1 44  ? 48.348 -21.493 -66.377 1.00 34.46  ? 44  THR B O     1 
ATOM   4426 C CB    . THR B 1 44  ? 46.278 -21.956 -68.482 1.00 32.52  ? 44  THR B CB    1 
ATOM   4427 O OG1   . THR B 1 44  ? 45.371 -21.182 -69.278 1.00 31.88  ? 44  THR B OG1   1 
ATOM   4428 C CG2   . THR B 1 44  ? 46.139 -23.442 -68.747 1.00 32.43  ? 44  THR B CG2   1 
ATOM   4429 N N     . ILE B 1 45  ? 47.169 -23.286 -65.594 1.00 32.14  ? 45  ILE B N     1 
ATOM   4430 C CA    . ILE B 1 45  ? 48.297 -23.904 -64.895 1.00 33.42  ? 45  ILE B CA    1 
ATOM   4431 C C     . ILE B 1 45  ? 48.633 -25.292 -65.447 1.00 33.06  ? 45  ILE B C     1 
ATOM   4432 O O     . ILE B 1 45  ? 49.797 -25.581 -65.680 1.00 41.06  ? 45  ILE B O     1 
ATOM   4433 C CB    . ILE B 1 45  ? 48.081 -23.974 -63.372 1.00 33.46  ? 45  ILE B CB    1 
ATOM   4434 C CG1   . ILE B 1 45  ? 48.008 -22.583 -62.736 1.00 33.57  ? 45  ILE B CG1   1 
ATOM   4435 C CG2   . ILE B 1 45  ? 49.177 -24.823 -62.726 1.00 35.90  ? 45  ILE B CG2   1 
ATOM   4436 C CD1   . ILE B 1 45  ? 47.637 -22.575 -61.261 1.00 32.02  ? 45  ILE B CD1   1 
ATOM   4437 N N     . SER B 1 46  ? 47.644 -26.177 -65.599 1.00 38.01  ? 46  SER B N     1 
ATOM   4438 C CA    . SER B 1 46  ? 47.871 -27.492 -66.194 1.00 36.53  ? 46  SER B CA    1 
ATOM   4439 C C     . SER B 1 46  ? 48.394 -27.349 -67.615 1.00 35.34  ? 46  SER B C     1 
ATOM   4440 O O     . SER B 1 46  ? 47.941 -26.474 -68.357 1.00 37.64  ? 46  SER B O     1 
ATOM   4441 C CB    . SER B 1 46  ? 46.612 -28.322 -66.204 1.00 37.34  ? 46  SER B CB    1 
ATOM   4442 O OG    . SER B 1 46  ? 46.914 -29.697 -66.364 1.00 36.64  ? 46  SER B OG    1 
ATOM   4443 N N     . ASN B 1 47  ? 49.352 -28.215 -67.961 1.00 37.08  ? 47  ASN B N     1 
ATOM   4444 C CA    . ASN B 1 47  ? 49.742 -28.443 -69.348 1.00 40.30  ? 47  ASN B CA    1 
ATOM   4445 C C     . ASN B 1 47  ? 48.862 -29.540 -69.960 1.00 38.91  ? 47  ASN B C     1 
ATOM   4446 O O     . ASN B 1 47  ? 48.901 -29.774 -71.169 1.00 41.35  ? 47  ASN B O     1 
ATOM   4447 C CB    . ASN B 1 47  ? 51.243 -28.751 -69.470 1.00 36.93  ? 47  ASN B CB    1 
ATOM   4448 C CG    . ASN B 1 47  ? 52.084 -27.496 -69.361 1.00 39.24  ? 47  ASN B CG    1 
ATOM   4449 O OD1   . ASN B 1 47  ? 51.712 -26.447 -69.876 1.00 38.28  ? 47  ASN B OD1   1 
ATOM   4450 N ND2   . ASN B 1 47  ? 53.199 -27.571 -68.658 1.00 42.07  ? 47  ASN B ND2   1 
ATOM   4451 N N     . ASP B 1 48  ? 48.045 -30.182 -69.119 1.00 35.47  ? 48  ASP B N     1 
ATOM   4452 C CA    . ASP B 1 48  ? 47.129 -31.216 -69.557 1.00 36.65  ? 48  ASP B CA    1 
ATOM   4453 C C     . ASP B 1 48  ? 45.761 -30.587 -69.827 1.00 38.16  ? 48  ASP B C     1 
ATOM   4454 O O     . ASP B 1 48  ? 45.066 -30.192 -68.893 1.00 41.01  ? 48  ASP B O     1 
ATOM   4455 C CB    . ASP B 1 48  ? 47.097 -32.329 -68.512 1.00 35.96  ? 48  ASP B CB    1 
ATOM   4456 C CG    . ASP B 1 48  ? 46.135 -33.446 -68.865 1.00 38.90  ? 48  ASP B CG    1 
ATOM   4457 O OD1   . ASP B 1 48  ? 45.362 -33.267 -69.837 1.00 41.87  ? 48  ASP B OD1   1 
ATOM   4458 O OD2   . ASP B 1 48  ? 46.165 -34.473 -68.166 1.00 36.22  ? 48  ASP B OD2   1 
ATOM   4459 N N     . GLU B 1 49  ? 45.353 -30.541 -71.106 1.00 38.96  ? 49  GLU B N     1 
ATOM   4460 C CA    . GLU B 1 49  ? 44.174 -29.798 -71.535 1.00 37.15  ? 49  GLU B CA    1 
ATOM   4461 C C     . GLU B 1 49  ? 42.848 -30.507 -71.219 1.00 34.64  ? 49  GLU B C     1 
ATOM   4462 O O     . GLU B 1 49  ? 41.799 -29.955 -71.533 1.00 31.40  ? 49  GLU B O     1 
ATOM   4463 C CB    . GLU B 1 49  ? 44.234 -29.527 -73.033 1.00 39.80  ? 49  GLU B CB    1 
ATOM   4464 C CG    . GLU B 1 49  ? 45.327 -28.561 -73.419 1.00 49.21  ? 49  GLU B CG    1 
ATOM   4465 C CD    . GLU B 1 49  ? 45.311 -28.232 -74.898 1.00 54.62  ? 49  GLU B CD    1 
ATOM   4466 O OE1   . GLU B 1 49  ? 45.173 -27.042 -75.236 1.00 64.45  ? 49  GLU B OE1   1 
ATOM   4467 O OE2   . GLU B 1 49  ? 45.405 -29.181 -75.698 1.00 59.19  ? 49  GLU B OE2   1 
ATOM   4468 N N     . THR B 1 50  ? 42.881 -31.704 -70.616 1.00 32.57  ? 50  THR B N     1 
ATOM   4469 C CA    . THR B 1 50  ? 41.668 -32.387 -70.197 1.00 36.97  ? 50  THR B CA    1 
ATOM   4470 C C     . THR B 1 50  ? 41.254 -31.969 -68.776 1.00 37.90  ? 50  THR B C     1 
ATOM   4471 O O     . THR B 1 50  ? 40.197 -32.380 -68.302 1.00 33.98  ? 50  THR B O     1 
ATOM   4472 C CB    . THR B 1 50  ? 41.848 -33.910 -70.232 1.00 39.12  ? 50  THR B CB    1 
ATOM   4473 O OG1   . THR B 1 50  ? 42.765 -34.303 -69.204 1.00 44.08  ? 50  THR B OG1   1 
ATOM   4474 C CG2   . THR B 1 50  ? 42.348 -34.411 -71.566 1.00 41.59  ? 50  THR B CG2   1 
ATOM   4475 N N     . GLU B 1 51  ? 42.106 -31.206 -68.078 1.00 36.74  ? 51  GLU B N     1 
ATOM   4476 C CA    . GLU B 1 51  ? 41.866 -30.877 -66.680 1.00 38.30  ? 51  GLU B CA    1 
ATOM   4477 C C     . GLU B 1 51  ? 41.206 -29.505 -66.534 1.00 32.97  ? 51  GLU B C     1 
ATOM   4478 O O     . GLU B 1 51  ? 41.584 -28.537 -67.206 1.00 34.48  ? 51  GLU B O     1 
ATOM   4479 C CB    . GLU B 1 51  ? 43.166 -30.893 -65.882 1.00 40.58  ? 51  GLU B CB    1 
ATOM   4480 C CG    . GLU B 1 51  ? 43.612 -32.281 -65.454 1.00 42.60  ? 51  GLU B CG    1 
ATOM   4481 C CD    . GLU B 1 51  ? 44.950 -32.277 -64.729 1.00 44.94  ? 51  GLU B CD    1 
ATOM   4482 O OE1   . GLU B 1 51  ? 45.890 -31.630 -65.226 1.00 41.44  ? 51  GLU B OE1   1 
ATOM   4483 O OE2   . GLU B 1 51  ? 45.051 -32.916 -63.669 1.00 53.53  ? 51  GLU B OE2   1 
ATOM   4484 N N     . HIS B 1 52  ? 40.226 -29.452 -65.625 1.00 30.83  ? 52  HIS B N     1 
ATOM   4485 C CA    . HIS B 1 52  ? 39.622 -28.205 -65.149 1.00 34.77  ? 52  HIS B CA    1 
ATOM   4486 C C     . HIS B 1 52  ? 38.825 -27.520 -66.259 1.00 30.28  ? 52  HIS B C     1 
ATOM   4487 O O     . HIS B 1 52  ? 38.711 -26.302 -66.270 1.00 31.23  ? 52  HIS B O     1 
ATOM   4488 C CB    . HIS B 1 52  ? 40.638 -27.247 -64.490 1.00 29.36  ? 52  HIS B CB    1 
ATOM   4489 C CG    . HIS B 1 52  ? 41.575 -27.907 -63.524 1.00 30.49  ? 52  HIS B CG    1 
ATOM   4490 N ND1   . HIS B 1 52  ? 41.145 -28.673 -62.464 1.00 33.52  ? 52  HIS B ND1   1 
ATOM   4491 C CD2   . HIS B 1 52  ? 42.927 -27.952 -63.484 1.00 32.04  ? 52  HIS B CD2   1 
ATOM   4492 C CE1   . HIS B 1 52  ? 42.198 -29.166 -61.811 1.00 33.29  ? 52  HIS B CE1   1 
ATOM   4493 N NE2   . HIS B 1 52  ? 43.291 -28.752 -62.419 1.00 33.64  ? 52  HIS B NE2   1 
ATOM   4494 N N     . ARG B 1 53  ? 38.176 -28.311 -67.113 1.00 30.97  ? 53  ARG B N     1 
ATOM   4495 C CA    . ARG B 1 53  ? 37.495 -27.785 -68.289 1.00 31.62  ? 53  ARG B CA    1 
ATOM   4496 C C     . ARG B 1 53  ? 35.996 -27.780 -68.038 1.00 27.66  ? 53  ARG B C     1 
ATOM   4497 O O     . ARG B 1 53  ? 35.413 -28.838 -67.875 1.00 30.84  ? 53  ARG B O     1 
ATOM   4498 C CB    . ARG B 1 53  ? 37.811 -28.653 -69.515 1.00 34.47  ? 53  ARG B CB    1 
ATOM   4499 C CG    . ARG B 1 53  ? 39.301 -28.899 -69.743 1.00 34.03  ? 53  ARG B CG    1 
ATOM   4500 C CD    . ARG B 1 53  ? 40.087 -27.616 -69.966 1.00 31.37  ? 53  ARG B CD    1 
ATOM   4501 N NE    . ARG B 1 53  ? 39.479 -26.833 -71.031 1.00 33.65  ? 53  ARG B NE    1 
ATOM   4502 C CZ    . ARG B 1 53  ? 39.480 -27.174 -72.324 1.00 36.81  ? 53  ARG B CZ    1 
ATOM   4503 N NH1   . ARG B 1 53  ? 40.184 -28.215 -72.752 1.00 38.14  ? 53  ARG B NH1   1 
ATOM   4504 N NH2   . ARG B 1 53  ? 38.807 -26.452 -73.202 1.00 32.75  ? 53  ARG B NH2   1 
ATOM   4505 N N     . PRO B 1 54  ? 35.326 -26.613 -67.986 1.00 25.96  ? 54  PRO B N     1 
ATOM   4506 C CA    . PRO B 1 54  ? 33.869 -26.570 -67.880 1.00 24.83  ? 54  PRO B CA    1 
ATOM   4507 C C     . PRO B 1 54  ? 33.230 -27.068 -69.168 1.00 25.67  ? 54  PRO B C     1 
ATOM   4508 O O     . PRO B 1 54  ? 33.671 -26.717 -70.269 1.00 26.42  ? 54  PRO B O     1 
ATOM   4509 C CB    . PRO B 1 54  ? 33.555 -25.084 -67.634 1.00 24.54  ? 54  PRO B CB    1 
ATOM   4510 C CG    . PRO B 1 54  ? 34.738 -24.346 -68.194 1.00 25.40  ? 54  PRO B CG    1 
ATOM   4511 C CD    . PRO B 1 54  ? 35.921 -25.274 -68.032 1.00 26.79  ? 54  PRO B CD    1 
ATOM   4512 N N     . TYR B 1 55  ? 32.197 -27.907 -69.025 1.00 26.89  ? 55  TYR B N     1 
ATOM   4513 C CA    . TYR B 1 55  ? 31.505 -28.451 -70.183 1.00 27.26  ? 55  TYR B CA    1 
ATOM   4514 C C     . TYR B 1 55  ? 30.594 -27.412 -70.820 1.00 27.43  ? 55  TYR B C     1 
ATOM   4515 O O     . TYR B 1 55  ? 30.490 -27.322 -72.038 1.00 32.38  ? 55  TYR B O     1 
ATOM   4516 C CB    . TYR B 1 55  ? 30.637 -29.656 -69.831 1.00 29.71  ? 55  TYR B CB    1 
ATOM   4517 C CG    . TYR B 1 55  ? 30.330 -30.467 -71.054 1.00 31.92  ? 55  TYR B CG    1 
ATOM   4518 C CD1   . TYR B 1 55  ? 31.290 -31.326 -71.572 1.00 36.58  ? 55  TYR B CD1   1 
ATOM   4519 C CD2   . TYR B 1 55  ? 29.155 -30.278 -71.775 1.00 35.46  ? 55  TYR B CD2   1 
ATOM   4520 C CE1   . TYR B 1 55  ? 31.057 -32.054 -72.731 1.00 39.06  ? 55  TYR B CE1   1 
ATOM   4521 C CE2   . TYR B 1 55  ? 28.906 -30.995 -72.943 1.00 37.26  ? 55  TYR B CE2   1 
ATOM   4522 C CZ    . TYR B 1 55  ? 29.862 -31.887 -73.420 1.00 37.61  ? 55  TYR B CZ    1 
ATOM   4523 O OH    . TYR B 1 55  ? 29.661 -32.628 -74.555 1.00 34.32  ? 55  TYR B OH    1 
ATOM   4524 N N     . ALA B 1 56  ? 29.888 -26.676 -69.966 1.00 27.48  ? 56  ALA B N     1 
ATOM   4525 C CA    . ALA B 1 56  ? 28.928 -25.677 -70.384 1.00 26.46  ? 56  ALA B CA    1 
ATOM   4526 C C     . ALA B 1 56  ? 28.683 -24.747 -69.206 1.00 26.22  ? 56  ALA B C     1 
ATOM   4527 O O     . ALA B 1 56  ? 29.234 -24.994 -68.123 1.00 25.75  ? 56  ALA B O     1 
ATOM   4528 C CB    . ALA B 1 56  ? 27.662 -26.366 -70.816 1.00 26.33  ? 56  ALA B CB    1 
ATOM   4529 N N     . ALA B 1 57  ? 27.875 -23.703 -69.456 1.00 24.71  ? 57  ALA B N     1 
ATOM   4530 C CA    . ALA B 1 57  ? 27.446 -22.759 -68.435 1.00 26.26  ? 57  ALA B CA    1 
ATOM   4531 C C     . ALA B 1 57  ? 25.947 -22.470 -68.565 1.00 26.87  ? 57  ALA B C     1 
ATOM   4532 O O     . ALA B 1 57  ? 25.449 -22.382 -69.678 1.00 27.79  ? 57  ALA B O     1 
ATOM   4533 C CB    . ALA B 1 57  ? 28.240 -21.488 -68.561 1.00 23.35  ? 57  ALA B CB    1 
ATOM   4534 N N     . VAL B 1 58  ? 25.258 -22.309 -67.422 1.00 26.47  ? 58  VAL B N     1 
ATOM   4535 C CA    . VAL B 1 58  ? 23.858 -21.923 -67.351 1.00 28.34  ? 58  VAL B CA    1 
ATOM   4536 C C     . VAL B 1 58  ? 23.778 -20.646 -66.521 1.00 29.45  ? 58  VAL B C     1 
ATOM   4537 O O     . VAL B 1 58  ? 24.356 -20.574 -65.436 1.00 28.32  ? 58  VAL B O     1 
ATOM   4538 C CB    . VAL B 1 58  ? 22.975 -23.003 -66.687 1.00 33.11  ? 58  VAL B CB    1 
ATOM   4539 C CG1   . VAL B 1 58  ? 21.505 -22.631 -66.729 1.00 34.75  ? 58  VAL B CG1   1 
ATOM   4540 C CG2   . VAL B 1 58  ? 23.149 -24.382 -67.291 1.00 37.03  ? 58  VAL B CG2   1 
ATOM   4541 N N     . ALA B 1 59  ? 22.970 -19.690 -66.982 1.00 26.71  ? 59  ALA B N     1 
ATOM   4542 C CA    . ALA B 1 59  ? 22.885 -18.395 -66.337 1.00 25.66  ? 59  ALA B CA    1 
ATOM   4543 C C     . ALA B 1 59  ? 21.438 -18.074 -65.947 1.00 24.11  ? 59  ALA B C     1 
ATOM   4544 O O     . ALA B 1 59  ? 20.705 -17.421 -66.680 1.00 23.03  ? 59  ALA B O     1 
ATOM   4545 C CB    . ALA B 1 59  ? 23.487 -17.350 -67.247 1.00 25.50  ? 59  ALA B CB    1 
ATOM   4546 N N     . PRO B 1 60  ? 20.965 -18.509 -64.763 1.00 24.14  ? 60  PRO B N     1 
ATOM   4547 C CA    . PRO B 1 60  ? 19.601 -18.204 -64.347 1.00 23.85  ? 60  PRO B CA    1 
ATOM   4548 C C     . PRO B 1 60  ? 19.392 -16.754 -63.956 1.00 23.27  ? 60  PRO B C     1 
ATOM   4549 O O     . PRO B 1 60  ? 20.344 -16.062 -63.596 1.00 26.42  ? 60  PRO B O     1 
ATOM   4550 C CB    . PRO B 1 60  ? 19.402 -19.064 -63.103 1.00 25.03  ? 60  PRO B CB    1 
ATOM   4551 C CG    . PRO B 1 60  ? 20.814 -19.252 -62.567 1.00 25.36  ? 60  PRO B CG    1 
ATOM   4552 C CD    . PRO B 1 60  ? 21.679 -19.361 -63.799 1.00 24.33  ? 60  PRO B CD    1 
ATOM   4553 N N     . ALA B 1 61  ? 18.120 -16.362 -63.971 1.00 23.06  ? 61  ALA B N     1 
ATOM   4554 C CA    . ALA B 1 61  ? 17.669 -15.034 -63.607 1.00 24.00  ? 61  ALA B CA    1 
ATOM   4555 C C     . ALA B 1 61  ? 16.909 -15.001 -62.277 1.00 25.02  ? 61  ALA B C     1 
ATOM   4556 O O     . ALA B 1 61  ? 16.408 -13.940 -61.897 1.00 26.24  ? 61  ALA B O     1 
ATOM   4557 C CB    . ALA B 1 61  ? 16.782 -14.505 -64.708 1.00 25.64  ? 61  ALA B CB    1 
ATOM   4558 N N     . SER B 1 62  ? 16.808 -16.119 -61.550 1.00 25.83  ? 62  SER B N     1 
ATOM   4559 C CA    . SER B 1 62  ? 16.057 -16.094 -60.302 1.00 26.00  ? 62  SER B CA    1 
ATOM   4560 C C     . SER B 1 62  ? 16.357 -17.327 -59.462 1.00 27.55  ? 62  SER B C     1 
ATOM   4561 O O     . SER B 1 62  ? 16.895 -18.329 -59.958 1.00 26.34  ? 62  SER B O     1 
ATOM   4562 C CB    . SER B 1 62  ? 14.590 -16.038 -60.571 1.00 26.65  ? 62  SER B CB    1 
ATOM   4563 O OG    . SER B 1 62  ? 14.185 -17.270 -61.185 1.00 27.76  ? 62  SER B OG    1 
ATOM   4564 N N     . THR B 1 63  ? 15.898 -17.260 -58.206 1.00 27.61  ? 63  THR B N     1 
ATOM   4565 C CA    . THR B 1 63  ? 16.007 -18.382 -57.293 1.00 29.07  ? 63  THR B CA    1 
ATOM   4566 C C     . THR B 1 63  ? 15.203 -19.546 -57.861 1.00 28.01  ? 63  THR B C     1 
ATOM   4567 O O     . THR B 1 63  ? 15.682 -20.677 -57.880 1.00 26.66  ? 63  THR B O     1 
ATOM   4568 C CB    . THR B 1 63  ? 15.607 -17.997 -55.862 1.00 28.55  ? 63  THR B CB    1 
ATOM   4569 O OG1   . THR B 1 63  ? 16.541 -17.022 -55.406 1.00 27.22  ? 63  THR B OG1   1 
ATOM   4570 C CG2   . THR B 1 63  ? 15.636 -19.162 -54.895 1.00 28.32  ? 63  THR B CG2   1 
ATOM   4571 N N     . GLU B 1 64  ? 14.018 -19.264 -58.388 1.00 29.98  ? 64  GLU B N     1 
ATOM   4572 C CA    . GLU B 1 64  ? 13.164 -20.354 -58.856 1.00 36.64  ? 64  GLU B CA    1 
ATOM   4573 C C     . GLU B 1 64  ? 13.827 -21.083 -60.040 1.00 30.37  ? 64  GLU B C     1 
ATOM   4574 O O     . GLU B 1 64  ? 13.739 -22.311 -60.122 1.00 23.92  ? 64  GLU B O     1 
ATOM   4575 C CB    . GLU B 1 64  ? 11.697 -19.939 -59.079 1.00 40.95  ? 64  GLU B CB    1 
ATOM   4576 C CG    . GLU B 1 64  ? 11.451 -18.450 -59.276 1.00 52.08  ? 64  GLU B CG    1 
ATOM   4577 C CD    . GLU B 1 64  ? 11.487 -17.567 -58.034 1.00 46.80  ? 64  GLU B CD    1 
ATOM   4578 O OE1   . GLU B 1 64  ? 12.462 -16.789 -57.886 1.00 43.02  ? 64  GLU B OE1   1 
ATOM   4579 O OE2   . GLU B 1 64  ? 10.520 -17.614 -57.260 1.00 41.68  ? 64  GLU B OE2   1 
ATOM   4580 N N     . GLU B 1 65  ? 14.605 -20.372 -60.867 1.00 27.57  ? 65  GLU B N     1 
ATOM   4581 C CA    . GLU B 1 65  ? 15.324 -21.034 -61.944 1.00 27.70  ? 65  GLU B CA    1 
ATOM   4582 C C     . GLU B 1 65  ? 16.481 -21.881 -61.407 1.00 25.58  ? 65  GLU B C     1 
ATOM   4583 O O     . GLU B 1 65  ? 16.673 -23.018 -61.850 1.00 21.39  ? 65  GLU B O     1 
ATOM   4584 C CB    . GLU B 1 65  ? 15.750 -20.019 -63.001 1.00 30.69  ? 65  GLU B CB    1 
ATOM   4585 C CG    . GLU B 1 65  ? 14.562 -19.453 -63.750 1.00 29.04  ? 65  GLU B CG    1 
ATOM   4586 C CD    . GLU B 1 65  ? 14.883 -18.417 -64.804 1.00 31.29  ? 65  GLU B CD    1 
ATOM   4587 O OE1   . GLU B 1 65  ? 16.090 -18.209 -65.106 1.00 28.08  ? 65  GLU B OE1   1 
ATOM   4588 O OE2   . GLU B 1 65  ? 13.912 -17.822 -65.318 1.00 36.41  ? 65  GLU B OE2   1 
ATOM   4589 N N     . VAL B 1 66  ? 17.215 -21.351 -60.421 1.00 26.75  ? 66  VAL B N     1 
ATOM   4590 C CA    . VAL B 1 66  ? 18.272 -22.112 -59.769 1.00 24.97  ? 66  VAL B CA    1 
ATOM   4591 C C     . VAL B 1 66  ? 17.700 -23.429 -59.255 1.00 23.96  ? 66  VAL B C     1 
ATOM   4592 O O     . VAL B 1 66  ? 18.300 -24.487 -59.430 1.00 23.59  ? 66  VAL B O     1 
ATOM   4593 C CB    . VAL B 1 66  ? 18.952 -21.320 -58.630 1.00 25.03  ? 66  VAL B CB    1 
ATOM   4594 C CG1   . VAL B 1 66  ? 19.870 -22.215 -57.804 1.00 25.24  ? 66  VAL B CG1   1 
ATOM   4595 C CG2   . VAL B 1 66  ? 19.722 -20.100 -59.142 1.00 24.23  ? 66  VAL B CG2   1 
ATOM   4596 N N     . GLN B 1 67  ? 16.554 -23.362 -58.588 1.00 23.61  ? 67  GLN B N     1 
ATOM   4597 C CA    . GLN B 1 67  ? 15.978 -24.560 -57.996 1.00 25.47  ? 67  GLN B CA    1 
ATOM   4598 C C     . GLN B 1 67  ? 15.677 -25.603 -59.071 1.00 26.88  ? 67  GLN B C     1 
ATOM   4599 O O     . GLN B 1 67  ? 15.900 -26.797 -58.845 1.00 25.52  ? 67  GLN B O     1 
ATOM   4600 C CB    . GLN B 1 67  ? 14.681 -24.236 -57.253 1.00 25.55  ? 67  GLN B CB    1 
ATOM   4601 C CG    . GLN B 1 67  ? 14.870 -23.289 -56.080 1.00 27.75  ? 67  GLN B CG    1 
ATOM   4602 C CD    . GLN B 1 67  ? 13.551 -23.033 -55.396 1.00 30.11  ? 67  GLN B CD    1 
ATOM   4603 O OE1   . GLN B 1 67  ? 12.899 -22.022 -55.639 1.00 31.39  ? 67  GLN B OE1   1 
ATOM   4604 N NE2   . GLN B 1 67  ? 13.128 -23.987 -54.580 1.00 29.76  ? 67  GLN B NE2   1 
ATOM   4605 N N     . GLU B 1 68  ? 15.134 -25.149 -60.215 1.00 26.63  ? 68  GLU B N     1 
ATOM   4606 C CA    . GLU B 1 68  ? 14.766 -26.059 -61.287 1.00 31.55  ? 68  GLU B CA    1 
ATOM   4607 C C     . GLU B 1 68  ? 16.034 -26.659 -61.895 1.00 29.16  ? 68  GLU B C     1 
ATOM   4608 O O     . GLU B 1 68  ? 16.089 -27.851 -62.177 1.00 32.41  ? 68  GLU B O     1 
ATOM   4609 C CB    . GLU B 1 68  ? 13.831 -25.395 -62.312 1.00 39.58  ? 68  GLU B CB    1 
ATOM   4610 C CG    . GLU B 1 68  ? 12.361 -25.840 -62.209 1.00 53.48  ? 68  GLU B CG    1 
ATOM   4611 C CD    . GLU B 1 68  ? 12.073 -27.355 -62.205 1.00 61.43  ? 68  GLU B CD    1 
ATOM   4612 O OE1   . GLU B 1 68  ? 11.308 -27.822 -61.306 1.00 55.91  ? 68  GLU B OE1   1 
ATOM   4613 O OE2   . GLU B 1 68  ? 12.620 -28.096 -63.087 1.00 56.63  ? 68  GLU B OE2   1 
ATOM   4614 N N     . ILE B 1 69  ? 17.074 -25.845 -62.067 1.00 28.88  ? 69  ILE B N     1 
ATOM   4615 C CA    . ILE B 1 69  ? 18.328 -26.329 -62.618 1.00 28.78  ? 69  ILE B CA    1 
ATOM   4616 C C     . ILE B 1 69  ? 18.873 -27.452 -61.746 1.00 28.35  ? 69  ILE B C     1 
ATOM   4617 O O     . ILE B 1 69  ? 19.350 -28.461 -62.261 1.00 28.60  ? 69  ILE B O     1 
ATOM   4618 C CB    . ILE B 1 69  ? 19.330 -25.171 -62.755 1.00 28.06  ? 69  ILE B CB    1 
ATOM   4619 C CG1   . ILE B 1 69  ? 18.907 -24.230 -63.880 1.00 29.71  ? 69  ILE B CG1   1 
ATOM   4620 C CG2   . ILE B 1 69  ? 20.746 -25.677 -62.946 1.00 27.28  ? 69  ILE B CG2   1 
ATOM   4621 C CD1   . ILE B 1 69  ? 19.613 -22.897 -63.848 1.00 31.63  ? 69  ILE B CD1   1 
ATOM   4622 N N     . VAL B 1 70  ? 18.799 -27.259 -60.429 1.00 28.22  ? 70  VAL B N     1 
ATOM   4623 C CA    . VAL B 1 70  ? 19.382 -28.205 -59.490 1.00 29.32  ? 70  VAL B CA    1 
ATOM   4624 C C     . VAL B 1 70  ? 18.607 -29.521 -59.543 1.00 31.05  ? 70  VAL B C     1 
ATOM   4625 O O     . VAL B 1 70  ? 19.221 -30.589 -59.441 1.00 34.94  ? 70  VAL B O     1 
ATOM   4626 C CB    . VAL B 1 70  ? 19.459 -27.620 -58.062 1.00 26.64  ? 70  VAL B CB    1 
ATOM   4627 C CG1   . VAL B 1 70  ? 19.676 -28.674 -56.980 1.00 25.33  ? 70  VAL B CG1   1 
ATOM   4628 C CG2   . VAL B 1 70  ? 20.536 -26.558 -57.973 1.00 27.70  ? 70  VAL B CG2   1 
ATOM   4629 N N     . ARG B 1 71  ? 17.273 -29.436 -59.663 1.00 30.07  ? 71  ARG B N     1 
ATOM   4630 C CA    . ARG B 1 71  ? 16.448 -30.619 -59.856 1.00 29.74  ? 71  ARG B CA    1 
ATOM   4631 C C     . ARG B 1 71  ? 16.874 -31.349 -61.123 1.00 28.44  ? 71  ARG B C     1 
ATOM   4632 O O     . ARG B 1 71  ? 17.023 -32.568 -61.103 1.00 25.81  ? 71  ARG B O     1 
ATOM   4633 C CB    . ARG B 1 71  ? 14.965 -30.284 -59.967 1.00 32.59  ? 71  ARG B CB    1 
ATOM   4634 C CG    . ARG B 1 71  ? 14.283 -29.993 -58.639 1.00 35.91  ? 71  ARG B CG    1 
ATOM   4635 C CD    . ARG B 1 71  ? 12.860 -29.472 -58.809 1.00 36.01  ? 71  ARG B CD    1 
ATOM   4636 N NE    . ARG B 1 71  ? 12.426 -28.850 -57.559 1.00 39.69  ? 71  ARG B NE    1 
ATOM   4637 C CZ    . ARG B 1 71  ? 11.945 -27.612 -57.435 1.00 38.10  ? 71  ARG B CZ    1 
ATOM   4638 N NH1   . ARG B 1 71  ? 11.638 -26.895 -58.507 1.00 35.61  ? 71  ARG B NH1   1 
ATOM   4639 N NH2   . ARG B 1 71  ? 11.719 -27.127 -56.225 1.00 38.65  ? 71  ARG B NH2   1 
ATOM   4640 N N     . VAL B 1 72  ? 17.138 -30.602 -62.200 1.00 27.87  ? 72  VAL B N     1 
ATOM   4641 C CA    . VAL B 1 72  ? 17.492 -31.246 -63.455 1.00 27.51  ? 72  VAL B CA    1 
ATOM   4642 C C     . VAL B 1 72  ? 18.882 -31.872 -63.328 1.00 26.60  ? 72  VAL B C     1 
ATOM   4643 O O     . VAL B 1 72  ? 19.096 -32.984 -63.811 1.00 25.65  ? 72  VAL B O     1 
ATOM   4644 C CB    . VAL B 1 72  ? 17.351 -30.291 -64.656 1.00 28.61  ? 72  VAL B CB    1 
ATOM   4645 C CG1   . VAL B 1 72  ? 17.962 -30.853 -65.919 1.00 27.99  ? 72  VAL B CG1   1 
ATOM   4646 C CG2   . VAL B 1 72  ? 15.899 -29.931 -64.913 1.00 30.78  ? 72  VAL B CG2   1 
ATOM   4647 N N     . ALA B 1 73  ? 19.797 -31.216 -62.599 1.00 25.83  ? 73  ALA B N     1 
ATOM   4648 C CA    . ALA B 1 73  ? 21.129 -31.775 -62.396 1.00 25.27  ? 73  ALA B CA    1 
ATOM   4649 C C     . ALA B 1 73  ? 21.056 -33.153 -61.726 1.00 26.30  ? 73  ALA B C     1 
ATOM   4650 O O     . ALA B 1 73  ? 21.732 -34.096 -62.155 1.00 27.89  ? 73  ALA B O     1 
ATOM   4651 C CB    . ALA B 1 73  ? 21.986 -30.803 -61.622 1.00 24.65  ? 73  ALA B CB    1 
ATOM   4652 N N     . ASN B 1 74  ? 20.188 -33.278 -60.715 1.00 26.85  ? 74  ASN B N     1 
ATOM   4653 C CA    . ASN B 1 74  ? 19.977 -34.530 -59.995 1.00 27.44  ? 74  ASN B CA    1 
ATOM   4654 C C     . ASN B 1 74  ? 19.362 -35.599 -60.893 1.00 27.92  ? 74  ASN B C     1 
ATOM   4655 O O     . ASN B 1 74  ? 19.734 -36.769 -60.831 1.00 29.05  ? 74  ASN B O     1 
ATOM   4656 C CB    . ASN B 1 74  ? 19.007 -34.359 -58.831 1.00 28.02  ? 74  ASN B CB    1 
ATOM   4657 C CG    . ASN B 1 74  ? 19.656 -33.874 -57.557 1.00 28.59  ? 74  ASN B CG    1 
ATOM   4658 O OD1   . ASN B 1 74  ? 20.290 -34.644 -56.841 1.00 29.33  ? 74  ASN B OD1   1 
ATOM   4659 N ND2   . ASN B 1 74  ? 19.454 -32.610 -57.247 1.00 29.36  ? 74  ASN B ND2   1 
ATOM   4660 N N     . GLU B 1 75  ? 18.399 -35.192 -61.717 1.00 28.73  ? 75  GLU B N     1 
ATOM   4661 C CA    . GLU B 1 75  ? 17.747 -36.110 -62.638 1.00 32.27  ? 75  GLU B CA    1 
ATOM   4662 C C     . GLU B 1 75  ? 18.806 -36.800 -63.507 1.00 32.04  ? 75  GLU B C     1 
ATOM   4663 O O     . GLU B 1 75  ? 18.738 -38.006 -63.705 1.00 28.27  ? 75  GLU B O     1 
ATOM   4664 C CB    . GLU B 1 75  ? 16.699 -35.326 -63.430 1.00 34.53  ? 75  GLU B CB    1 
ATOM   4665 C CG    . GLU B 1 75  ? 15.909 -36.163 -64.401 1.00 38.65  ? 75  GLU B CG    1 
ATOM   4666 C CD    . GLU B 1 75  ? 14.709 -35.483 -65.047 1.00 41.36  ? 75  GLU B CD    1 
ATOM   4667 O OE1   . GLU B 1 75  ? 14.145 -36.107 -65.959 1.00 43.80  ? 75  GLU B OE1   1 
ATOM   4668 O OE2   . GLU B 1 75  ? 14.313 -34.359 -64.620 1.00 40.86  ? 75  GLU B OE2   1 
ATOM   4669 N N     . PHE B 1 76  ? 19.832 -36.054 -63.951 1.00 31.22  ? 76  PHE B N     1 
ATOM   4670 C CA    . PHE B 1 76  ? 20.732 -36.540 -64.989 1.00 33.26  ? 76  PHE B CA    1 
ATOM   4671 C C     . PHE B 1 76  ? 22.138 -36.846 -64.480 1.00 33.36  ? 76  PHE B C     1 
ATOM   4672 O O     . PHE B 1 76  ? 22.997 -37.210 -65.285 1.00 28.79  ? 76  PHE B O     1 
ATOM   4673 C CB    . PHE B 1 76  ? 20.816 -35.515 -66.118 1.00 32.25  ? 76  PHE B CB    1 
ATOM   4674 C CG    . PHE B 1 76  ? 19.579 -35.513 -66.971 1.00 35.07  ? 76  PHE B CG    1 
ATOM   4675 C CD1   . PHE B 1 76  ? 19.260 -36.629 -67.730 1.00 35.68  ? 76  PHE B CD1   1 
ATOM   4676 C CD2   . PHE B 1 76  ? 18.711 -34.438 -66.960 1.00 33.36  ? 76  PHE B CD2   1 
ATOM   4677 C CE1   . PHE B 1 76  ? 18.123 -36.649 -68.506 1.00 34.78  ? 76  PHE B CE1   1 
ATOM   4678 C CE2   . PHE B 1 76  ? 17.571 -34.459 -67.733 1.00 35.10  ? 76  PHE B CE2   1 
ATOM   4679 C CZ    . PHE B 1 76  ? 17.284 -35.562 -68.509 1.00 40.76  ? 76  PHE B CZ    1 
ATOM   4680 N N     . GLY B 1 77  ? 22.357 -36.660 -63.166 1.00 33.24  ? 77  GLY B N     1 
ATOM   4681 C CA    . GLY B 1 77  ? 23.666 -36.809 -62.539 1.00 30.30  ? 77  GLY B CA    1 
ATOM   4682 C C     . GLY B 1 77  ? 24.733 -35.907 -63.152 1.00 25.64  ? 77  GLY B C     1 
ATOM   4683 O O     . GLY B 1 77  ? 25.876 -36.297 -63.232 1.00 27.59  ? 77  GLY B O     1 
ATOM   4684 N N     . VAL B 1 78  ? 24.343 -34.724 -63.610 1.00 24.71  ? 78  VAL B N     1 
ATOM   4685 C CA    . VAL B 1 78  ? 25.253 -33.782 -64.231 1.00 25.88  ? 78  VAL B CA    1 
ATOM   4686 C C     . VAL B 1 78  ? 25.701 -32.769 -63.185 1.00 27.03  ? 78  VAL B C     1 
ATOM   4687 O O     . VAL B 1 78  ? 24.877 -32.058 -62.625 1.00 24.56  ? 78  VAL B O     1 
ATOM   4688 C CB    . VAL B 1 78  ? 24.546 -33.065 -65.389 1.00 30.03  ? 78  VAL B CB    1 
ATOM   4689 C CG1   . VAL B 1 78  ? 25.254 -31.776 -65.768 1.00 30.49  ? 78  VAL B CG1   1 
ATOM   4690 C CG2   . VAL B 1 78  ? 24.391 -33.999 -66.584 1.00 32.34  ? 78  VAL B CG2   1 
ATOM   4691 N N     . PRO B 1 79  ? 27.001 -32.690 -62.839 1.00 28.88  ? 79  PRO B N     1 
ATOM   4692 C CA    . PRO B 1 79  ? 27.419 -31.807 -61.749 1.00 27.24  ? 79  PRO B CA    1 
ATOM   4693 C C     . PRO B 1 79  ? 27.487 -30.337 -62.164 1.00 24.89  ? 79  PRO B C     1 
ATOM   4694 O O     . PRO B 1 79  ? 27.740 -30.019 -63.320 1.00 22.96  ? 79  PRO B O     1 
ATOM   4695 C CB    . PRO B 1 79  ? 28.762 -32.426 -61.322 1.00 28.50  ? 79  PRO B CB    1 
ATOM   4696 C CG    . PRO B 1 79  ? 29.301 -33.100 -62.572 1.00 31.45  ? 79  PRO B CG    1 
ATOM   4697 C CD    . PRO B 1 79  ? 28.097 -33.494 -63.403 1.00 29.47  ? 79  PRO B CD    1 
ATOM   4698 N N     . LEU B 1 80  ? 27.200 -29.457 -61.194 1.00 24.85  ? 80  LEU B N     1 
ATOM   4699 C CA    . LEU B 1 80  ? 27.176 -28.013 -61.363 1.00 24.37  ? 80  LEU B CA    1 
ATOM   4700 C C     . LEU B 1 80  ? 28.316 -27.363 -60.579 1.00 24.20  ? 80  LEU B C     1 
ATOM   4701 O O     . LEU B 1 80  ? 28.746 -27.845 -59.537 1.00 22.79  ? 80  LEU B O     1 
ATOM   4702 C CB    . LEU B 1 80  ? 25.857 -27.466 -60.807 1.00 26.77  ? 80  LEU B CB    1 
ATOM   4703 C CG    . LEU B 1 80  ? 24.557 -27.950 -61.445 1.00 28.02  ? 80  LEU B CG    1 
ATOM   4704 C CD1   . LEU B 1 80  ? 23.360 -27.489 -60.628 1.00 26.77  ? 80  LEU B CD1   1 
ATOM   4705 C CD2   . LEU B 1 80  ? 24.437 -27.443 -62.868 1.00 30.42  ? 80  LEU B CD2   1 
ATOM   4706 N N     . TRP B 1 81  ? 28.759 -26.196 -61.036 1.00 23.58  ? 81  TRP B N     1 
ATOM   4707 C CA    . TRP B 1 81  ? 29.770 -25.466 -60.314 1.00 22.28  ? 81  TRP B CA    1 
ATOM   4708 C C     . TRP B 1 81  ? 29.247 -24.059 -60.063 1.00 23.02  ? 81  TRP B C     1 
ATOM   4709 O O     . TRP B 1 81  ? 29.379 -23.174 -60.895 1.00 20.84  ? 81  TRP B O     1 
ATOM   4710 C CB    . TRP B 1 81  ? 31.088 -25.486 -61.091 1.00 24.33  ? 81  TRP B CB    1 
ATOM   4711 C CG    . TRP B 1 81  ? 32.214 -24.828 -60.354 1.00 23.86  ? 81  TRP B CG    1 
ATOM   4712 C CD1   . TRP B 1 81  ? 32.541 -23.506 -60.345 1.00 26.27  ? 81  TRP B CD1   1 
ATOM   4713 C CD2   . TRP B 1 81  ? 33.107 -25.457 -59.432 1.00 22.76  ? 81  TRP B CD2   1 
ATOM   4714 N NE1   . TRP B 1 81  ? 33.605 -23.274 -59.512 1.00 25.92  ? 81  TRP B NE1   1 
ATOM   4715 C CE2   . TRP B 1 81  ? 33.969 -24.457 -58.939 1.00 24.08  ? 81  TRP B CE2   1 
ATOM   4716 C CE3   . TRP B 1 81  ? 33.288 -26.773 -59.019 1.00 24.74  ? 81  TRP B CE3   1 
ATOM   4717 C CZ2   . TRP B 1 81  ? 34.991 -24.733 -58.044 1.00 24.62  ? 81  TRP B CZ2   1 
ATOM   4718 C CZ3   . TRP B 1 81  ? 34.296 -27.049 -58.126 1.00 25.86  ? 81  TRP B CZ3   1 
ATOM   4719 C CH2   . TRP B 1 81  ? 35.129 -26.040 -57.646 1.00 25.05  ? 81  TRP B CH2   1 
ATOM   4720 N N     . PRO B 1 82  ? 28.601 -23.819 -58.909 1.00 24.31  ? 82  PRO B N     1 
ATOM   4721 C CA    . PRO B 1 82  ? 28.001 -22.519 -58.626 1.00 25.23  ? 82  PRO B CA    1 
ATOM   4722 C C     . PRO B 1 82  ? 29.037 -21.413 -58.454 1.00 25.40  ? 82  PRO B C     1 
ATOM   4723 O O     . PRO B 1 82  ? 29.995 -21.589 -57.712 1.00 27.81  ? 82  PRO B O     1 
ATOM   4724 C CB    . PRO B 1 82  ? 27.237 -22.760 -57.319 1.00 26.08  ? 82  PRO B CB    1 
ATOM   4725 C CG    . PRO B 1 82  ? 27.061 -24.266 -57.266 1.00 26.46  ? 82  PRO B CG    1 
ATOM   4726 C CD    . PRO B 1 82  ? 28.346 -24.804 -57.850 1.00 24.67  ? 82  PRO B CD    1 
ATOM   4727 N N     . VAL B 1 83  ? 28.859 -20.319 -59.209 1.00 25.23  ? 83  VAL B N     1 
ATOM   4728 C CA    . VAL B 1 83  ? 29.621 -19.100 -59.037 1.00 27.86  ? 83  VAL B CA    1 
ATOM   4729 C C     . VAL B 1 83  ? 28.626 -17.944 -58.995 1.00 28.30  ? 83  VAL B C     1 
ATOM   4730 O O     . VAL B 1 83  ? 27.574 -18.014 -59.639 1.00 25.95  ? 83  VAL B O     1 
ATOM   4731 C CB    . VAL B 1 83  ? 30.706 -18.909 -60.123 1.00 30.04  ? 83  VAL B CB    1 
ATOM   4732 C CG1   . VAL B 1 83  ? 31.627 -20.118 -60.213 1.00 30.47  ? 83  VAL B CG1   1 
ATOM   4733 C CG2   . VAL B 1 83  ? 30.136 -18.595 -61.495 1.00 32.30  ? 83  VAL B CG2   1 
ATOM   4734 N N     . SER B 1 84  ? 28.984 -16.910 -58.219 1.00 25.82  ? 84  SER B N     1 
ATOM   4735 C CA    . SER B 1 84  ? 28.149 -15.734 -58.053 1.00 27.03  ? 84  SER B CA    1 
ATOM   4736 C C     . SER B 1 84  ? 28.403 -14.772 -59.213 1.00 27.49  ? 84  SER B C     1 
ATOM   4737 O O     . SER B 1 84  ? 27.480 -14.365 -59.916 1.00 28.02  ? 84  SER B O     1 
ATOM   4738 C CB    . SER B 1 84  ? 28.410 -15.072 -56.717 1.00 27.64  ? 84  SER B CB    1 
ATOM   4739 O OG    . SER B 1 84  ? 27.922 -15.869 -55.642 1.00 26.12  ? 84  SER B OG    1 
ATOM   4740 N N     . ARG B 1 85  ? 29.668 -14.414 -59.430 1.00 25.80  ? 85  ARG B N     1 
ATOM   4741 C CA    . ARG B 1 85  ? 30.033 -13.762 -60.677 1.00 26.61  ? 85  ARG B CA    1 
ATOM   4742 C C     . ARG B 1 85  ? 31.183 -14.477 -61.383 1.00 25.19  ? 85  ARG B C     1 
ATOM   4743 O O     . ARG B 1 85  ? 31.497 -14.133 -62.504 1.00 25.73  ? 85  ARG B O     1 
ATOM   4744 C CB    . ARG B 1 85  ? 30.385 -12.300 -60.419 1.00 28.10  ? 85  ARG B CB    1 
ATOM   4745 C CG    . ARG B 1 85  ? 29.161 -11.437 -60.159 1.00 29.07  ? 85  ARG B CG    1 
ATOM   4746 C CD    . ARG B 1 85  ? 29.584 -10.073 -59.671 1.00 28.67  ? 85  ARG B CD    1 
ATOM   4747 N NE    . ARG B 1 85  ? 30.373 -9.388  -60.670 1.00 29.37  ? 85  ARG B NE    1 
ATOM   4748 C CZ    . ARG B 1 85  ? 29.879 -8.768  -61.743 1.00 31.84  ? 85  ARG B CZ    1 
ATOM   4749 N NH1   . ARG B 1 85  ? 28.577 -8.696  -61.952 1.00 32.29  ? 85  ARG B NH1   1 
ATOM   4750 N NH2   . ARG B 1 85  ? 30.704 -8.194  -62.602 1.00 31.64  ? 85  ARG B NH2   1 
ATOM   4751 N N     . GLY B 1 86  ? 31.860 -15.412 -60.724 1.00 24.59  ? 86  GLY B N     1 
ATOM   4752 C CA    . GLY B 1 86  ? 32.815 -16.245 -61.422 1.00 26.33  ? 86  GLY B CA    1 
ATOM   4753 C C     . GLY B 1 86  ? 34.105 -15.520 -61.782 1.00 27.07  ? 86  GLY B C     1 
ATOM   4754 O O     . GLY B 1 86  ? 34.822 -15.983 -62.656 1.00 26.93  ? 86  GLY B O     1 
ATOM   4755 N N     . LYS B 1 87  ? 34.448 -14.481 -61.007 1.00 28.22  ? 87  LYS B N     1 
ATOM   4756 C CA    . LYS B 1 87  ? 35.649 -13.695 -61.219 1.00 27.29  ? 87  LYS B CA    1 
ATOM   4757 C C     . LYS B 1 87  ? 36.752 -14.061 -60.235 1.00 24.17  ? 87  LYS B C     1 
ATOM   4758 O O     . LYS B 1 87  ? 37.565 -13.209 -59.898 1.00 20.27  ? 87  LYS B O     1 
ATOM   4759 C CB    . LYS B 1 87  ? 35.294 -12.218 -61.082 1.00 30.75  ? 87  LYS B CB    1 
ATOM   4760 C CG    . LYS B 1 87  ? 34.176 -11.770 -62.018 1.00 35.01  ? 87  LYS B CG    1 
ATOM   4761 C CD    . LYS B 1 87  ? 34.652 -11.074 -63.267 1.00 39.28  ? 87  LYS B CD    1 
ATOM   4762 C CE    . LYS B 1 87  ? 33.527 -10.615 -64.172 1.00 44.23  ? 87  LYS B CE    1 
ATOM   4763 N NZ    . LYS B 1 87  ? 33.201 -11.651 -65.184 1.00 48.73  ? 87  LYS B NZ    1 
ATOM   4764 N N     . ASN B 1 88  ? 36.807 -15.337 -59.824 1.00 24.17  ? 88  ASN B N     1 
ATOM   4765 C CA    . ASN B 1 88  ? 37.772 -15.802 -58.826 1.00 24.54  ? 88  ASN B CA    1 
ATOM   4766 C C     . ASN B 1 88  ? 39.142 -15.994 -59.484 1.00 25.15  ? 88  ASN B C     1 
ATOM   4767 O O     . ASN B 1 88  ? 39.755 -17.051 -59.367 1.00 23.70  ? 88  ASN B O     1 
ATOM   4768 C CB    . ASN B 1 88  ? 37.298 -17.106 -58.154 1.00 23.08  ? 88  ASN B CB    1 
ATOM   4769 C CG    . ASN B 1 88  ? 37.733 -17.280 -56.711 1.00 22.82  ? 88  ASN B CG    1 
ATOM   4770 O OD1   . ASN B 1 88  ? 38.219 -16.351 -56.059 1.00 22.17  ? 88  ASN B OD1   1 
ATOM   4771 N ND2   . ASN B 1 88  ? 37.551 -18.482 -56.194 1.00 22.82  ? 88  ASN B ND2   1 
ATOM   4772 N N     . PHE B 1 89  ? 39.616 -14.968 -60.198 1.00 26.56  ? 89  PHE B N     1 
ATOM   4773 C CA    . PHE B 1 89  ? 40.925 -15.027 -60.831 1.00 27.49  ? 89  PHE B CA    1 
ATOM   4774 C C     . PHE B 1 89  ? 42.011 -15.049 -59.749 1.00 28.21  ? 89  PHE B C     1 
ATOM   4775 O O     . PHE B 1 89  ? 41.935 -14.278 -58.779 1.00 25.00  ? 89  PHE B O     1 
ATOM   4776 C CB    . PHE B 1 89  ? 41.065 -13.863 -61.816 1.00 28.71  ? 89  PHE B CB    1 
ATOM   4777 C CG    . PHE B 1 89  ? 39.886 -13.701 -62.741 1.00 30.26  ? 89  PHE B CG    1 
ATOM   4778 C CD1   . PHE B 1 89  ? 39.243 -14.811 -63.276 1.00 34.11  ? 89  PHE B CD1   1 
ATOM   4779 C CD2   . PHE B 1 89  ? 39.404 -12.453 -63.073 1.00 32.86  ? 89  PHE B CD2   1 
ATOM   4780 C CE1   . PHE B 1 89  ? 38.166 -14.673 -64.136 1.00 34.95  ? 89  PHE B CE1   1 
ATOM   4781 C CE2   . PHE B 1 89  ? 38.316 -12.320 -63.924 1.00 33.58  ? 89  PHE B CE2   1 
ATOM   4782 C CZ    . PHE B 1 89  ? 37.699 -13.425 -64.453 1.00 32.98  ? 89  PHE B CZ    1 
ATOM   4783 N N     . ALA B 1 90  ? 43.003 -15.937 -59.967 1.00 24.71  ? 90  ALA B N     1 
ATOM   4784 C CA    . ALA B 1 90  ? 44.024 -16.362 -59.015 1.00 25.69  ? 90  ALA B CA    1 
ATOM   4785 C C     . ALA B 1 90  ? 43.644 -17.716 -58.437 1.00 24.20  ? 90  ALA B C     1 
ATOM   4786 O O     . ALA B 1 90  ? 44.502 -18.422 -57.908 1.00 23.28  ? 90  ALA B O     1 
ATOM   4787 C CB    . ALA B 1 90  ? 44.271 -15.382 -57.876 1.00 25.99  ? 90  ALA B CB    1 
ATOM   4788 N N     . TYR B 1 91  ? 42.356 -18.059 -58.484 1.00 24.72  ? 91  TYR B N     1 
ATOM   4789 C CA    . TYR B 1 91  ? 41.912 -19.314 -57.870 1.00 27.37  ? 91  TYR B CA    1 
ATOM   4790 C C     . TYR B 1 91  ? 41.210 -20.215 -58.894 1.00 26.21  ? 91  TYR B C     1 
ATOM   4791 O O     . TYR B 1 91  ? 40.622 -21.227 -58.519 1.00 25.39  ? 91  TYR B O     1 
ATOM   4792 C CB    . TYR B 1 91  ? 41.027 -19.007 -56.652 1.00 28.49  ? 91  TYR B CB    1 
ATOM   4793 C CG    . TYR B 1 91  ? 41.714 -18.256 -55.532 1.00 28.16  ? 91  TYR B CG    1 
ATOM   4794 C CD1   . TYR B 1 91  ? 42.563 -18.903 -54.659 1.00 28.46  ? 91  TYR B CD1   1 
ATOM   4795 C CD2   . TYR B 1 91  ? 41.536 -16.891 -55.355 1.00 28.17  ? 91  TYR B CD2   1 
ATOM   4796 C CE1   . TYR B 1 91  ? 43.204 -18.232 -53.634 1.00 29.36  ? 91  TYR B CE1   1 
ATOM   4797 C CE2   . TYR B 1 91  ? 42.167 -16.199 -54.337 1.00 26.42  ? 91  TYR B CE2   1 
ATOM   4798 C CZ    . TYR B 1 91  ? 43.005 -16.875 -53.472 1.00 28.00  ? 91  TYR B CZ    1 
ATOM   4799 O OH    . TYR B 1 91  ? 43.645 -16.225 -52.462 1.00 27.12  ? 91  TYR B OH    1 
ATOM   4800 N N     . GLY B 1 92  ? 41.284 -19.847 -60.186 1.00 26.76  ? 92  GLY B N     1 
ATOM   4801 C CA    . GLY B 1 92  ? 40.692 -20.648 -61.245 1.00 27.57  ? 92  GLY B CA    1 
ATOM   4802 C C     . GLY B 1 92  ? 39.591 -19.956 -62.048 1.00 26.73  ? 92  GLY B C     1 
ATOM   4803 O O     . GLY B 1 92  ? 39.023 -20.581 -62.930 1.00 23.84  ? 92  GLY B O     1 
ATOM   4804 N N     . GLY B 1 93  ? 39.306 -18.672 -61.769 1.00 28.34  ? 93  GLY B N     1 
ATOM   4805 C CA    . GLY B 1 93  ? 38.169 -17.983 -62.363 1.00 24.11  ? 93  GLY B CA    1 
ATOM   4806 C C     . GLY B 1 93  ? 36.871 -18.746 -62.115 1.00 25.47  ? 93  GLY B C     1 
ATOM   4807 O O     . GLY B 1 93  ? 36.585 -19.110 -60.982 1.00 28.27  ? 93  GLY B O     1 
ATOM   4808 N N     . ALA B 1 94  ? 36.119 -19.043 -63.181 1.00 23.83  ? 94  ALA B N     1 
ATOM   4809 C CA    . ALA B 1 94  ? 34.864 -19.753 -63.052 1.00 25.97  ? 94  ALA B CA    1 
ATOM   4810 C C     . ALA B 1 94  ? 35.017 -21.240 -63.365 1.00 26.01  ? 94  ALA B C     1 
ATOM   4811 O O     . ALA B 1 94  ? 34.030 -21.936 -63.541 1.00 28.52  ? 94  ALA B O     1 
ATOM   4812 C CB    . ALA B 1 94  ? 33.839 -19.110 -63.955 1.00 27.92  ? 94  ALA B CB    1 
ATOM   4813 N N     . ALA B 1 95  ? 36.244 -21.748 -63.380 1.00 26.98  ? 95  ALA B N     1 
ATOM   4814 C CA    . ALA B 1 95  ? 36.501 -23.112 -63.816 1.00 25.93  ? 95  ALA B CA    1 
ATOM   4815 C C     . ALA B 1 95  ? 36.303 -24.087 -62.659 1.00 25.66  ? 95  ALA B C     1 
ATOM   4816 O O     . ALA B 1 95  ? 36.619 -23.776 -61.517 1.00 29.43  ? 95  ALA B O     1 
ATOM   4817 C CB    . ALA B 1 95  ? 37.898 -23.214 -64.388 1.00 25.28  ? 95  ALA B CB    1 
ATOM   4818 N N     . PRO B 1 96  ? 35.771 -25.300 -62.913 1.00 25.00  ? 96  PRO B N     1 
ATOM   4819 C CA    . PRO B 1 96  ? 35.622 -26.309 -61.864 1.00 23.90  ? 96  PRO B CA    1 
ATOM   4820 C C     . PRO B 1 96  ? 36.849 -27.194 -61.689 1.00 24.25  ? 96  PRO B C     1 
ATOM   4821 O O     . PRO B 1 96  ? 37.669 -27.322 -62.589 1.00 23.60  ? 96  PRO B O     1 
ATOM   4822 C CB    . PRO B 1 96  ? 34.499 -27.183 -62.403 1.00 23.93  ? 96  PRO B CB    1 
ATOM   4823 C CG    . PRO B 1 96  ? 34.758 -27.154 -63.904 1.00 24.90  ? 96  PRO B CG    1 
ATOM   4824 C CD    . PRO B 1 96  ? 35.268 -25.759 -64.215 1.00 23.75  ? 96  PRO B CD    1 
ATOM   4825 N N     . VAL B 1 97  ? 36.946 -27.811 -60.513 1.00 23.72  ? 97  VAL B N     1 
ATOM   4826 C CA    . VAL B 1 97  ? 37.959 -28.809 -60.259 1.00 24.08  ? 97  VAL B CA    1 
ATOM   4827 C C     . VAL B 1 97  ? 37.860 -29.934 -61.289 1.00 25.80  ? 97  VAL B C     1 
ATOM   4828 O O     . VAL B 1 97  ? 38.867 -30.361 -61.852 1.00 27.21  ? 97  VAL B O     1 
ATOM   4829 C CB    . VAL B 1 97  ? 37.833 -29.375 -58.842 1.00 23.46  ? 97  VAL B CB    1 
ATOM   4830 C CG1   . VAL B 1 97  ? 38.781 -30.550 -58.682 1.00 23.48  ? 97  VAL B CG1   1 
ATOM   4831 C CG2   . VAL B 1 97  ? 38.071 -28.318 -57.759 1.00 23.11  ? 97  VAL B CG2   1 
ATOM   4832 N N     . MET B 1 98  ? 36.647 -30.446 -61.507 1.00 25.08  ? 98  MET B N     1 
ATOM   4833 C CA    . MET B 1 98  ? 36.486 -31.648 -62.312 1.00 26.22  ? 98  MET B CA    1 
ATOM   4834 C C     . MET B 1 98  ? 35.911 -31.298 -63.681 1.00 24.69  ? 98  MET B C     1 
ATOM   4835 O O     . MET B 1 98  ? 34.817 -30.762 -63.815 1.00 24.95  ? 98  MET B O     1 
ATOM   4836 C CB    . MET B 1 98  ? 35.570 -32.657 -61.611 1.00 27.49  ? 98  MET B CB    1 
ATOM   4837 C CG    . MET B 1 98  ? 35.416 -33.961 -62.375 1.00 27.04  ? 98  MET B CG    1 
ATOM   4838 S SD    . MET B 1 98  ? 34.152 -35.023 -61.647 1.00 30.64  ? 98  MET B SD    1 
ATOM   4839 C CE    . MET B 1 98  ? 32.679 -34.367 -62.440 1.00 28.20  ? 98  MET B CE    1 
ATOM   4840 N N     . SER B 1 99  ? 36.672 -31.638 -64.711 1.00 26.28  ? 99  SER B N     1 
ATOM   4841 C CA    . SER B 1 99  ? 36.241 -31.467 -66.084 1.00 26.35  ? 99  SER B CA    1 
ATOM   4842 C C     . SER B 1 99  ? 34.881 -32.118 -66.328 1.00 25.22  ? 99  SER B C     1 
ATOM   4843 O O     . SER B 1 99  ? 34.575 -33.186 -65.800 1.00 27.44  ? 99  SER B O     1 
ATOM   4844 C CB    . SER B 1 99  ? 37.271 -32.034 -67.007 1.00 25.56  ? 99  SER B CB    1 
ATOM   4845 O OG    . SER B 1 99  ? 38.359 -31.151 -67.111 1.00 26.66  ? 99  SER B OG    1 
ATOM   4846 N N     . GLY B 1 100 ? 34.071 -31.471 -67.153 1.00 24.31  ? 100 GLY B N     1 
ATOM   4847 C CA    . GLY B 1 100 ? 32.736 -31.978 -67.418 1.00 28.25  ? 100 GLY B CA    1 
ATOM   4848 C C     . GLY B 1 100 ? 31.659 -31.339 -66.536 1.00 28.22  ? 100 GLY B C     1 
ATOM   4849 O O     . GLY B 1 100 ? 30.470 -31.485 -66.823 1.00 28.32  ? 100 GLY B O     1 
ATOM   4850 N N     . THR B 1 101 ? 32.069 -30.635 -65.468 1.00 25.00  ? 101 THR B N     1 
ATOM   4851 C CA    . THR B 1 101 ? 31.114 -29.950 -64.627 1.00 22.96  ? 101 THR B CA    1 
ATOM   4852 C C     . THR B 1 101 ? 30.546 -28.762 -65.406 1.00 22.01  ? 101 THR B C     1 
ATOM   4853 O O     . THR B 1 101 ? 31.251 -28.168 -66.220 1.00 23.71  ? 101 THR B O     1 
ATOM   4854 C CB    . THR B 1 101 ? 31.762 -29.520 -63.307 1.00 22.95  ? 101 THR B CB    1 
ATOM   4855 O OG1   . THR B 1 101 ? 32.407 -30.639 -62.704 1.00 20.88  ? 101 THR B OG1   1 
ATOM   4856 C CG2   . THR B 1 101 ? 30.759 -28.915 -62.347 1.00 22.90  ? 101 THR B CG2   1 
ATOM   4857 N N     . VAL B 1 102 ? 29.274 -28.439 -65.148 1.00 22.94  ? 102 VAL B N     1 
ATOM   4858 C CA    . VAL B 1 102 ? 28.583 -27.315 -65.771 1.00 23.91  ? 102 VAL B CA    1 
ATOM   4859 C C     . VAL B 1 102 ? 28.558 -26.137 -64.799 1.00 21.34  ? 102 VAL B C     1 
ATOM   4860 O O     . VAL B 1 102 ? 28.176 -26.275 -63.657 1.00 23.34  ? 102 VAL B O     1 
ATOM   4861 C CB    . VAL B 1 102 ? 27.158 -27.704 -66.205 1.00 25.49  ? 102 VAL B CB    1 
ATOM   4862 C CG1   . VAL B 1 102 ? 26.356 -26.511 -66.700 1.00 25.99  ? 102 VAL B CG1   1 
ATOM   4863 C CG2   . VAL B 1 102 ? 27.182 -28.797 -67.266 1.00 27.82  ? 102 VAL B CG2   1 
ATOM   4864 N N     . VAL B 1 103 ? 28.951 -24.961 -65.266 1.00 21.60  ? 103 VAL B N     1 
ATOM   4865 C CA    . VAL B 1 103 ? 29.006 -23.810 -64.404 1.00 22.17  ? 103 VAL B CA    1 
ATOM   4866 C C     . VAL B 1 103 ? 27.590 -23.291 -64.266 1.00 22.66  ? 103 VAL B C     1 
ATOM   4867 O O     . VAL B 1 103 ? 26.922 -23.061 -65.269 1.00 23.99  ? 103 VAL B O     1 
ATOM   4868 C CB    . VAL B 1 103 ? 29.940 -22.729 -64.965 1.00 22.25  ? 103 VAL B CB    1 
ATOM   4869 C CG1   . VAL B 1 103 ? 29.829 -21.420 -64.182 1.00 21.34  ? 103 VAL B CG1   1 
ATOM   4870 C CG2   . VAL B 1 103 ? 31.378 -23.223 -65.018 1.00 22.42  ? 103 VAL B CG2   1 
ATOM   4871 N N     . LEU B 1 104 ? 27.167 -23.115 -63.016 1.00 23.90  ? 104 LEU B N     1 
ATOM   4872 C CA    . LEU B 1 104 ? 25.948 -22.391 -62.711 1.00 24.23  ? 104 LEU B CA    1 
ATOM   4873 C C     . LEU B 1 104 ? 26.328 -20.978 -62.317 1.00 25.05  ? 104 LEU B C     1 
ATOM   4874 O O     . LEU B 1 104 ? 26.764 -20.746 -61.201 1.00 25.56  ? 104 LEU B O     1 
ATOM   4875 C CB    . LEU B 1 104 ? 25.195 -23.104 -61.595 1.00 24.16  ? 104 LEU B CB    1 
ATOM   4876 C CG    . LEU B 1 104 ? 24.018 -22.333 -61.017 1.00 26.04  ? 104 LEU B CG    1 
ATOM   4877 C CD1   . LEU B 1 104 ? 22.914 -22.228 -62.038 1.00 27.31  ? 104 LEU B CD1   1 
ATOM   4878 C CD2   . LEU B 1 104 ? 23.516 -23.019 -59.757 1.00 29.07  ? 104 LEU B CD2   1 
ATOM   4879 N N     . ASP B 1 105 ? 26.177 -20.067 -63.280 1.00 27.70  ? 105 ASP B N     1 
ATOM   4880 C CA    . ASP B 1 105 ? 26.644 -18.698 -63.196 1.00 26.25  ? 105 ASP B CA    1 
ATOM   4881 C C     . ASP B 1 105 ? 25.479 -17.794 -62.801 1.00 26.88  ? 105 ASP B C     1 
ATOM   4882 O O     . ASP B 1 105 ? 24.571 -17.575 -63.597 1.00 24.48  ? 105 ASP B O     1 
ATOM   4883 C CB    . ASP B 1 105 ? 27.207 -18.285 -64.547 1.00 28.10  ? 105 ASP B CB    1 
ATOM   4884 C CG    . ASP B 1 105 ? 27.634 -16.833 -64.649 1.00 31.06  ? 105 ASP B CG    1 
ATOM   4885 O OD1   . ASP B 1 105 ? 27.518 -16.096 -63.640 1.00 27.55  ? 105 ASP B OD1   1 
ATOM   4886 O OD2   . ASP B 1 105 ? 28.051 -16.448 -65.768 1.00 35.97  ? 105 ASP B OD2   1 
ATOM   4887 N N     . MET B 1 106 ? 25.551 -17.199 -61.603 1.00 25.26  ? 106 MET B N     1 
ATOM   4888 C CA    . MET B 1 106 ? 24.415 -16.457 -61.102 1.00 26.53  ? 106 MET B CA    1 
ATOM   4889 C C     . MET B 1 106 ? 24.545 -14.943 -61.318 1.00 24.75  ? 106 MET B C     1 
ATOM   4890 O O     . MET B 1 106 ? 23.777 -14.173 -60.751 1.00 24.10  ? 106 MET B O     1 
ATOM   4891 C CB    . MET B 1 106 ? 24.204 -16.847 -59.640 1.00 26.78  ? 106 MET B CB    1 
ATOM   4892 C CG    . MET B 1 106 ? 23.528 -18.191 -59.576 1.00 27.99  ? 106 MET B CG    1 
ATOM   4893 S SD    . MET B 1 106 ? 23.256 -18.808 -57.921 1.00 31.16  ? 106 MET B SD    1 
ATOM   4894 C CE    . MET B 1 106 ? 24.946 -18.848 -57.335 1.00 32.70  ? 106 MET B CE    1 
ATOM   4895 N N     . ASN B 1 107 ? 25.387 -14.509 -62.259 1.00 27.23  ? 107 ASN B N     1 
ATOM   4896 C CA    . ASN B 1 107 ? 25.704 -13.087 -62.381 1.00 29.50  ? 107 ASN B CA    1 
ATOM   4897 C C     . ASN B 1 107 ? 24.461 -12.266 -62.732 1.00 26.90  ? 107 ASN B C     1 
ATOM   4898 O O     . ASN B 1 107 ? 24.379 -11.101 -62.363 1.00 24.70  ? 107 ASN B O     1 
ATOM   4899 C CB    . ASN B 1 107 ? 26.885 -12.822 -63.328 1.00 33.86  ? 107 ASN B CB    1 
ATOM   4900 C CG    . ASN B 1 107 ? 26.505 -12.854 -64.784 1.00 40.15  ? 107 ASN B CG    1 
ATOM   4901 O OD1   . ASN B 1 107 ? 26.762 -13.833 -65.493 1.00 53.60  ? 107 ASN B OD1   1 
ATOM   4902 N ND2   . ASN B 1 107 ? 25.865 -11.789 -65.227 1.00 41.22  ? 107 ASN B ND2   1 
ATOM   4903 N N     . ARG B 1 108 ? 23.464 -12.865 -63.387 1.00 26.50  ? 108 ARG B N     1 
ATOM   4904 C CA    . ARG B 1 108 ? 22.288 -12.111 -63.791 1.00 25.39  ? 108 ARG B CA    1 
ATOM   4905 C C     . ARG B 1 108 ? 21.338 -11.872 -62.619 1.00 26.50  ? 108 ARG B C     1 
ATOM   4906 O O     . ARG B 1 108 ? 20.508 -10.988 -62.698 1.00 30.33  ? 108 ARG B O     1 
ATOM   4907 C CB    . ARG B 1 108 ? 21.536 -12.822 -64.910 1.00 24.36  ? 108 ARG B CB    1 
ATOM   4908 C CG    . ARG B 1 108 ? 22.380 -13.049 -66.148 1.00 25.57  ? 108 ARG B CG    1 
ATOM   4909 C CD    . ARG B 1 108 ? 21.636 -13.898 -67.165 1.00 27.52  ? 108 ARG B CD    1 
ATOM   4910 N NE    . ARG B 1 108 ? 20.355 -13.334 -67.569 1.00 27.98  ? 108 ARG B NE    1 
ATOM   4911 C CZ    . ARG B 1 108 ? 19.227 -14.026 -67.701 1.00 27.86  ? 108 ARG B CZ    1 
ATOM   4912 N NH1   . ARG B 1 108 ? 19.200 -15.313 -67.398 1.00 27.98  ? 108 ARG B NH1   1 
ATOM   4913 N NH2   . ARG B 1 108 ? 18.136 -13.437 -68.165 1.00 27.34  ? 108 ARG B NH2   1 
ATOM   4914 N N     . MET B 1 109 ? 21.439 -12.638 -61.534 1.00 26.95  ? 109 MET B N     1 
ATOM   4915 C CA    . MET B 1 109 ? 20.651 -12.366 -60.342 1.00 26.72  ? 109 MET B CA    1 
ATOM   4916 C C     . MET B 1 109 ? 21.385 -11.284 -59.551 1.00 26.35  ? 109 MET B C     1 
ATOM   4917 O O     . MET B 1 109 ? 22.226 -11.551 -58.687 1.00 27.64  ? 109 MET B O     1 
ATOM   4918 C CB    . MET B 1 109 ? 20.464 -13.629 -59.500 1.00 26.21  ? 109 MET B CB    1 
ATOM   4919 C CG    . MET B 1 109 ? 19.715 -14.758 -60.238 1.00 28.12  ? 109 MET B CG    1 
ATOM   4920 S SD    . MET B 1 109 ? 19.970 -16.369 -59.394 1.00 28.59  ? 109 MET B SD    1 
ATOM   4921 C CE    . MET B 1 109 ? 19.322 -15.970 -57.769 1.00 27.92  ? 109 MET B CE    1 
ATOM   4922 N N     . ASN B 1 110 ? 21.085 -10.040 -59.903 1.00 24.90  ? 110 ASN B N     1 
ATOM   4923 C CA    . ASN B 1 110 ? 21.875 -8.916  -59.449 1.00 27.73  ? 110 ASN B CA    1 
ATOM   4924 C C     . ASN B 1 110 ? 20.999 -7.871  -58.778 1.00 25.17  ? 110 ASN B C     1 
ATOM   4925 O O     . ASN B 1 110 ? 21.345 -6.718  -58.847 1.00 27.13  ? 110 ASN B O     1 
ATOM   4926 C CB    . ASN B 1 110 ? 22.639 -8.276  -60.609 1.00 32.10  ? 110 ASN B CB    1 
ATOM   4927 C CG    . ASN B 1 110 ? 21.725 -7.714  -61.686 1.00 33.66  ? 110 ASN B CG    1 
ATOM   4928 O OD1   . ASN B 1 110 ? 20.505 -7.904  -61.666 1.00 30.64  ? 110 ASN B OD1   1 
ATOM   4929 N ND2   . ASN B 1 110 ? 22.328 -7.000  -62.618 1.00 34.94  ? 110 ASN B ND2   1 
ATOM   4930 N N     . ARG B 1 111 ? 19.897 -8.270  -58.140 1.00 25.82  ? 111 ARG B N     1 
ATOM   4931 C CA    . ARG B 1 111 ? 19.087 -7.357  -57.356 1.00 28.34  ? 111 ARG B CA    1 
ATOM   4932 C C     . ARG B 1 111 ? 19.817 -6.987  -56.056 1.00 28.23  ? 111 ARG B C     1 
ATOM   4933 O O     . ARG B 1 111 ? 20.225 -7.840  -55.255 1.00 25.17  ? 111 ARG B O     1 
ATOM   4934 C CB    . ARG B 1 111 ? 17.718 -7.966  -57.026 1.00 33.66  ? 111 ARG B CB    1 
ATOM   4935 C CG    . ARG B 1 111 ? 16.860 -8.318  -58.235 1.00 39.91  ? 111 ARG B CG    1 
ATOM   4936 C CD    . ARG B 1 111 ? 15.870 -9.443  -57.954 1.00 48.24  ? 111 ARG B CD    1 
ATOM   4937 N NE    . ARG B 1 111 ? 15.245 -9.982  -59.163 1.00 62.02  ? 111 ARG B NE    1 
ATOM   4938 C CZ    . ARG B 1 111 ? 15.697 -11.016 -59.886 1.00 65.28  ? 111 ARG B CZ    1 
ATOM   4939 N NH1   . ARG B 1 111 ? 16.874 -11.568 -59.629 1.00 63.07  ? 111 ARG B NH1   1 
ATOM   4940 N NH2   . ARG B 1 111 ? 14.978 -11.469 -60.900 1.00 56.54  ? 111 ARG B NH2   1 
ATOM   4941 N N     . ILE B 1 112 ? 19.961 -5.673  -55.855 1.00 27.13  ? 112 ILE B N     1 
ATOM   4942 C CA    . ILE B 1 112 ? 20.150 -5.115  -54.536 1.00 24.47  ? 112 ILE B CA    1 
ATOM   4943 C C     . ILE B 1 112 ? 18.789 -5.054  -53.852 1.00 23.51  ? 112 ILE B C     1 
ATOM   4944 O O     . ILE B 1 112 ? 18.008 -4.177  -54.134 1.00 27.25  ? 112 ILE B O     1 
ATOM   4945 C CB    . ILE B 1 112 ? 20.824 -3.742  -54.651 1.00 24.20  ? 112 ILE B CB    1 
ATOM   4946 C CG1   . ILE B 1 112 ? 22.125 -3.851  -55.449 1.00 25.82  ? 112 ILE B CG1   1 
ATOM   4947 C CG2   . ILE B 1 112 ? 21.034 -3.147  -53.277 1.00 24.13  ? 112 ILE B CG2   1 
ATOM   4948 C CD1   . ILE B 1 112 ? 22.835 -2.543  -55.685 1.00 26.14  ? 112 ILE B CD1   1 
ATOM   4949 N N     . LEU B 1 113 ? 18.515 -5.982  -52.942 1.00 24.45  ? 113 LEU B N     1 
ATOM   4950 C CA    . LEU B 1 113 ? 17.197 -6.120  -52.349 1.00 28.87  ? 113 LEU B CA    1 
ATOM   4951 C C     . LEU B 1 113 ? 16.976 -5.099  -51.233 1.00 30.75  ? 113 LEU B C     1 
ATOM   4952 O O     . LEU B 1 113 ? 15.853 -4.633  -51.057 1.00 31.43  ? 113 LEU B O     1 
ATOM   4953 C CB    . LEU B 1 113 ? 17.048 -7.556  -51.838 1.00 30.85  ? 113 LEU B CB    1 
ATOM   4954 C CG    . LEU B 1 113 ? 17.184 -8.618  -52.934 1.00 35.62  ? 113 LEU B CG    1 
ATOM   4955 C CD1   . LEU B 1 113 ? 17.237 -10.025 -52.348 1.00 36.78  ? 113 LEU B CD1   1 
ATOM   4956 C CD2   . LEU B 1 113 ? 16.045 -8.496  -53.948 1.00 34.25  ? 113 LEU B CD2   1 
ATOM   4957 N N     . GLU B 1 114 ? 18.023 -4.785  -50.460 1.00 29.23  ? 114 GLU B N     1 
ATOM   4958 C CA    . GLU B 1 114 ? 17.932 -3.723  -49.473 1.00 29.54  ? 114 GLU B CA    1 
ATOM   4959 C C     . GLU B 1 114 ? 19.313 -3.146  -49.197 1.00 25.80  ? 114 GLU B C     1 
ATOM   4960 O O     . GLU B 1 114 ? 20.297 -3.868  -49.185 1.00 29.76  ? 114 GLU B O     1 
ATOM   4961 C CB    . GLU B 1 114 ? 17.296 -4.218  -48.173 1.00 33.50  ? 114 GLU B CB    1 
ATOM   4962 C CG    . GLU B 1 114 ? 16.579 -3.088  -47.452 1.00 38.47  ? 114 GLU B CG    1 
ATOM   4963 C CD    . GLU B 1 114 ? 16.150 -3.368  -46.023 1.00 38.59  ? 114 GLU B CD    1 
ATOM   4964 O OE1   . GLU B 1 114 ? 15.849 -4.537  -45.743 1.00 39.74  ? 114 GLU B OE1   1 
ATOM   4965 O OE2   . GLU B 1 114 ? 16.056 -2.397  -45.233 1.00 38.45  ? 114 GLU B OE2   1 
ATOM   4966 N N     . VAL B 1 115 ? 19.382 -1.830  -49.061 1.00 24.71  ? 115 VAL B N     1 
ATOM   4967 C CA    . VAL B 1 115 ? 20.483 -1.186  -48.382 1.00 27.49  ? 115 VAL B CA    1 
ATOM   4968 C C     . VAL B 1 115 ? 19.880 -0.327  -47.281 1.00 28.53  ? 115 VAL B C     1 
ATOM   4969 O O     . VAL B 1 115 ? 19.036 0.512   -47.554 1.00 29.74  ? 115 VAL B O     1 
ATOM   4970 C CB    . VAL B 1 115 ? 21.368 -0.358  -49.330 1.00 28.04  ? 115 VAL B CB    1 
ATOM   4971 C CG1   . VAL B 1 115 ? 22.526 0.268   -48.570 1.00 28.28  ? 115 VAL B CG1   1 
ATOM   4972 C CG2   . VAL B 1 115 ? 21.889 -1.162  -50.517 1.00 27.18  ? 115 VAL B CG2   1 
ATOM   4973 N N     . ASN B 1 116 ? 20.321 -0.570  -46.040 1.00 32.91  ? 116 ASN B N     1 
ATOM   4974 C CA    . ASN B 1 116 ? 19.753 0.011   -44.831 1.00 28.37  ? 116 ASN B CA    1 
ATOM   4975 C C     . ASN B 1 116 ? 20.818 0.874   -44.162 1.00 27.61  ? 116 ASN B C     1 
ATOM   4976 O O     . ASN B 1 116 ? 21.815 0.365   -43.652 1.00 26.74  ? 116 ASN B O     1 
ATOM   4977 C CB    . ASN B 1 116 ? 19.282 -1.079  -43.875 1.00 28.51  ? 116 ASN B CB    1 
ATOM   4978 C CG    . ASN B 1 116 ? 18.358 -0.548  -42.793 1.00 29.58  ? 116 ASN B CG    1 
ATOM   4979 O OD1   . ASN B 1 116 ? 18.793 0.216   -41.938 1.00 28.12  ? 116 ASN B OD1   1 
ATOM   4980 N ND2   . ASN B 1 116 ? 17.097 -0.973  -42.801 1.00 26.51  ? 116 ASN B ND2   1 
ATOM   4981 N N     . GLU B 1 117 ? 20.605 2.190   -44.181 1.00 29.48  ? 117 GLU B N     1 
ATOM   4982 C CA    . GLU B 1 117 ? 21.595 3.129   -43.686 1.00 29.91  ? 117 GLU B CA    1 
ATOM   4983 C C     . GLU B 1 117 ? 21.644 3.086   -42.161 1.00 30.99  ? 117 GLU B C     1 
ATOM   4984 O O     . GLU B 1 117 ? 22.735 2.967   -41.608 1.00 30.95  ? 117 GLU B O     1 
ATOM   4985 C CB    . GLU B 1 117 ? 21.275 4.531   -44.181 1.00 32.19  ? 117 GLU B CB    1 
ATOM   4986 C CG    . GLU B 1 117 ? 22.292 5.573   -43.757 1.00 35.13  ? 117 GLU B CG    1 
ATOM   4987 C CD    . GLU B 1 117 ? 21.988 6.960   -44.302 1.00 35.89  ? 117 GLU B CD    1 
ATOM   4988 O OE1   . GLU B 1 117 ? 20.841 7.399   -44.187 1.00 43.03  ? 117 GLU B OE1   1 
ATOM   4989 O OE2   . GLU B 1 117 ? 22.899 7.595   -44.835 1.00 39.04  ? 117 GLU B OE2   1 
ATOM   4990 N N     . GLU B 1 118 ? 20.466 3.141   -41.512 1.00 30.83  ? 118 GLU B N     1 
ATOM   4991 C CA    . GLU B 1 118 ? 20.377 3.283   -40.065 1.00 34.00  ? 118 GLU B CA    1 
ATOM   4992 C C     . GLU B 1 118 ? 20.945 2.035   -39.386 1.00 31.50  ? 118 GLU B C     1 
ATOM   4993 O O     . GLU B 1 118 ? 21.621 2.161   -38.380 1.00 28.93  ? 118 GLU B O     1 
ATOM   4994 C CB    . GLU B 1 118 ? 18.950 3.630   -39.608 1.00 37.79  ? 118 GLU B CB    1 
ATOM   4995 C CG    . GLU B 1 118 ? 17.915 2.571   -39.944 1.00 46.72  ? 118 GLU B CG    1 
ATOM   4996 C CD    . GLU B 1 118 ? 16.501 2.756   -39.401 1.00 55.08  ? 118 GLU B CD    1 
ATOM   4997 O OE1   . GLU B 1 118 ? 16.306 3.637   -38.529 1.00 53.90  ? 118 GLU B OE1   1 
ATOM   4998 O OE2   . GLU B 1 118 ? 15.585 1.997   -39.853 1.00 57.27  ? 118 GLU B OE2   1 
ATOM   4999 N N     . PHE B 1 119 ? 20.744 0.845   -39.967 1.00 31.38  ? 119 PHE B N     1 
ATOM   5000 C CA    . PHE B 1 119 ? 21.289 -0.382  -39.393 1.00 31.38  ? 119 PHE B CA    1 
ATOM   5001 C C     . PHE B 1 119 ? 22.601 -0.804  -40.054 1.00 28.24  ? 119 PHE B C     1 
ATOM   5002 O O     . PHE B 1 119 ? 23.208 -1.755  -39.590 1.00 26.26  ? 119 PHE B O     1 
ATOM   5003 C CB    . PHE B 1 119 ? 20.260 -1.513  -39.459 1.00 32.20  ? 119 PHE B CB    1 
ATOM   5004 C CG    . PHE B 1 119 ? 19.071 -1.286  -38.559 1.00 36.36  ? 119 PHE B CG    1 
ATOM   5005 C CD1   . PHE B 1 119 ? 19.229 -1.280  -37.180 1.00 39.29  ? 119 PHE B CD1   1 
ATOM   5006 C CD2   . PHE B 1 119 ? 17.802 -1.070  -39.081 1.00 38.67  ? 119 PHE B CD2   1 
ATOM   5007 C CE1   . PHE B 1 119 ? 18.137 -1.092  -36.345 1.00 40.21  ? 119 PHE B CE1   1 
ATOM   5008 C CE2   . PHE B 1 119 ? 16.713 -0.860  -38.245 1.00 39.49  ? 119 PHE B CE2   1 
ATOM   5009 C CZ    . PHE B 1 119 ? 16.891 -0.850  -36.879 1.00 40.22  ? 119 PHE B CZ    1 
ATOM   5010 N N     . GLY B 1 120 ? 23.032 -0.119  -41.125 1.00 25.96  ? 120 GLY B N     1 
ATOM   5011 C CA    . GLY B 1 120 ? 24.313 -0.397  -41.756 1.00 24.83  ? 120 GLY B CA    1 
ATOM   5012 C C     . GLY B 1 120 ? 24.412 -1.817  -42.318 1.00 26.16  ? 120 GLY B C     1 
ATOM   5013 O O     . GLY B 1 120 ? 25.283 -2.573  -41.889 1.00 26.27  ? 120 GLY B O     1 
ATOM   5014 N N     . TYR B 1 121 ? 23.528 -2.168  -43.271 1.00 23.39  ? 121 TYR B N     1 
ATOM   5015 C CA    . TYR B 1 121 ? 23.604 -3.453  -43.935 1.00 23.73  ? 121 TYR B CA    1 
ATOM   5016 C C     . TYR B 1 121 ? 23.038 -3.414  -45.352 1.00 25.19  ? 121 TYR B C     1 
ATOM   5017 O O     . TYR B 1 121 ? 22.349 -2.478  -45.728 1.00 27.66  ? 121 TYR B O     1 
ATOM   5018 C CB    . TYR B 1 121 ? 22.914 -4.523  -43.092 1.00 23.95  ? 121 TYR B CB    1 
ATOM   5019 C CG    . TYR B 1 121 ? 21.418 -4.505  -43.107 1.00 22.39  ? 121 TYR B CG    1 
ATOM   5020 C CD1   . TYR B 1 121 ? 20.721 -4.900  -44.233 1.00 22.93  ? 121 TYR B CD1   1 
ATOM   5021 C CD2   . TYR B 1 121 ? 20.690 -4.114  -41.989 1.00 21.92  ? 121 TYR B CD2   1 
ATOM   5022 C CE1   . TYR B 1 121 ? 19.336 -4.936  -44.248 1.00 22.32  ? 121 TYR B CE1   1 
ATOM   5023 C CE2   . TYR B 1 121 ? 19.305 -4.097  -42.002 1.00 21.56  ? 121 TYR B CE2   1 
ATOM   5024 C CZ    . TYR B 1 121 ? 18.622 -4.524  -43.136 1.00 22.97  ? 121 TYR B CZ    1 
ATOM   5025 O OH    . TYR B 1 121 ? 17.237 -4.559  -43.207 1.00 23.01  ? 121 TYR B OH    1 
ATOM   5026 N N     . ALA B 1 122 ? 23.394 -4.444  -46.145 1.00 25.29  ? 122 ALA B N     1 
ATOM   5027 C CA    . ALA B 1 122 ? 22.806 -4.713  -47.445 1.00 22.02  ? 122 ALA B CA    1 
ATOM   5028 C C     . ALA B 1 122 ? 22.379 -6.173  -47.507 1.00 23.32  ? 122 ALA B C     1 
ATOM   5029 O O     . ALA B 1 122 ? 23.005 -7.011  -46.858 1.00 22.44  ? 122 ALA B O     1 
ATOM   5030 C CB    . ALA B 1 122 ? 23.787 -4.401  -48.539 1.00 21.33  ? 122 ALA B CB    1 
ATOM   5031 N N     . LEU B 1 123 ? 21.281 -6.428  -48.242 1.00 22.85  ? 123 LEU B N     1 
ATOM   5032 C CA    . LEU B 1 123 ? 20.860 -7.759  -48.650 1.00 24.58  ? 123 LEU B CA    1 
ATOM   5033 C C     . LEU B 1 123 ? 20.940 -7.841  -50.176 1.00 26.11  ? 123 LEU B C     1 
ATOM   5034 O O     . LEU B 1 123 ? 20.241 -7.105  -50.874 1.00 24.52  ? 123 LEU B O     1 
ATOM   5035 C CB    . LEU B 1 123 ? 19.440 -8.009  -48.142 1.00 26.00  ? 123 LEU B CB    1 
ATOM   5036 C CG    . LEU B 1 123 ? 18.750 -9.288  -48.637 1.00 26.68  ? 123 LEU B CG    1 
ATOM   5037 C CD1   . LEU B 1 123 ? 19.485 -10.505 -48.149 1.00 26.02  ? 123 LEU B CD1   1 
ATOM   5038 C CD2   . LEU B 1 123 ? 17.279 -9.372  -48.167 1.00 24.91  ? 123 LEU B CD2   1 
ATOM   5039 N N     . VAL B 1 124 ? 21.845 -8.696  -50.681 1.00 26.06  ? 124 VAL B N     1 
ATOM   5040 C CA    . VAL B 1 124 ? 22.190 -8.719  -52.096 1.00 26.21  ? 124 VAL B CA    1 
ATOM   5041 C C     . VAL B 1 124 ? 22.005 -10.121 -52.659 1.00 25.99  ? 124 VAL B C     1 
ATOM   5042 O O     . VAL B 1 124 ? 22.075 -11.113 -51.935 1.00 26.63  ? 124 VAL B O     1 
ATOM   5043 C CB    . VAL B 1 124 ? 23.636 -8.257  -52.337 1.00 25.97  ? 124 VAL B CB    1 
ATOM   5044 C CG1   . VAL B 1 124 ? 23.794 -6.747  -52.246 1.00 26.72  ? 124 VAL B CG1   1 
ATOM   5045 C CG2   . VAL B 1 124 ? 24.600 -8.950  -51.394 1.00 26.50  ? 124 VAL B CG2   1 
ATOM   5046 N N     . GLU B 1 125 ? 21.809 -10.171 -53.982 1.00 26.11  ? 125 GLU B N     1 
ATOM   5047 C CA    . GLU B 1 125 ? 21.885 -11.406 -54.741 1.00 25.11  ? 125 GLU B CA    1 
ATOM   5048 C C     . GLU B 1 125 ? 23.321 -11.625 -55.232 1.00 22.70  ? 125 GLU B C     1 
ATOM   5049 O O     . GLU B 1 125 ? 24.149 -10.716 -55.236 1.00 21.74  ? 125 GLU B O     1 
ATOM   5050 C CB    . GLU B 1 125 ? 20.892 -11.343 -55.900 1.00 27.58  ? 125 GLU B CB    1 
ATOM   5051 C CG    . GLU B 1 125 ? 19.431 -11.453 -55.504 1.00 29.24  ? 125 GLU B CG    1 
ATOM   5052 C CD    . GLU B 1 125 ? 18.507 -11.606 -56.704 1.00 28.14  ? 125 GLU B CD    1 
ATOM   5053 O OE1   . GLU B 1 125 ? 18.781 -10.939 -57.736 1.00 27.53  ? 125 GLU B OE1   1 
ATOM   5054 O OE2   . GLU B 1 125 ? 17.550 -12.407 -56.624 1.00 25.17  ? 125 GLU B OE2   1 
ATOM   5055 N N     . PRO B 1 126 ? 23.685 -12.853 -55.657 1.00 22.31  ? 126 PRO B N     1 
ATOM   5056 C CA    . PRO B 1 126 ? 25.068 -13.178 -56.015 1.00 21.77  ? 126 PRO B CA    1 
ATOM   5057 C C     . PRO B 1 126 ? 25.684 -12.344 -57.132 1.00 20.15  ? 126 PRO B C     1 
ATOM   5058 O O     . PRO B 1 126 ? 26.867 -12.055 -57.115 1.00 20.58  ? 126 PRO B O     1 
ATOM   5059 C CB    . PRO B 1 126 ? 24.932 -14.630 -56.460 1.00 22.93  ? 126 PRO B CB    1 
ATOM   5060 C CG    . PRO B 1 126 ? 23.809 -15.126 -55.616 1.00 23.16  ? 126 PRO B CG    1 
ATOM   5061 C CD    . PRO B 1 126 ? 22.801 -14.019 -55.765 1.00 23.44  ? 126 PRO B CD    1 
ATOM   5062 N N     . GLY B 1 127 ? 24.859 -11.899 -58.065 1.00 21.32  ? 127 GLY B N     1 
ATOM   5063 C CA    . GLY B 1 127 ? 25.357 -11.172 -59.212 1.00 22.14  ? 127 GLY B CA    1 
ATOM   5064 C C     . GLY B 1 127 ? 25.788 -9.749  -58.905 1.00 23.26  ? 127 GLY B C     1 
ATOM   5065 O O     . GLY B 1 127 ? 26.381 -9.095  -59.747 1.00 26.56  ? 127 GLY B O     1 
ATOM   5066 N N     . VAL B 1 128 ? 25.486 -9.239  -57.714 1.00 28.13  ? 128 VAL B N     1 
ATOM   5067 C CA    . VAL B 1 128 ? 25.847 -7.863  -57.399 1.00 26.36  ? 128 VAL B CA    1 
ATOM   5068 C C     . VAL B 1 128 ? 27.356 -7.780  -57.187 1.00 26.58  ? 128 VAL B C     1 
ATOM   5069 O O     . VAL B 1 128 ? 27.916 -8.453  -56.323 1.00 27.35  ? 128 VAL B O     1 
ATOM   5070 C CB    . VAL B 1 128 ? 25.094 -7.324  -56.171 1.00 27.11  ? 128 VAL B CB    1 
ATOM   5071 C CG1   . VAL B 1 128 ? 25.489 -5.875  -55.906 1.00 28.11  ? 128 VAL B CG1   1 
ATOM   5072 C CG2   . VAL B 1 128 ? 23.581 -7.476  -56.325 1.00 26.22  ? 128 VAL B CG2   1 
ATOM   5073 N N     . SER B 1 129 ? 27.988 -6.914  -57.980 1.00 25.10  ? 129 SER B N     1 
ATOM   5074 C CA    . SER B 1 129 ? 29.404 -6.634  -57.860 1.00 23.92  ? 129 SER B CA    1 
ATOM   5075 C C     . SER B 1 129 ? 29.638 -5.529  -56.838 1.00 21.49  ? 129 SER B C     1 
ATOM   5076 O O     . SER B 1 129 ? 28.712 -4.814  -56.479 1.00 22.23  ? 129 SER B O     1 
ATOM   5077 C CB    . SER B 1 129 ? 29.953 -6.195  -59.182 1.00 22.92  ? 129 SER B CB    1 
ATOM   5078 O OG    . SER B 1 129 ? 29.686 -4.811  -59.394 1.00 22.69  ? 129 SER B OG    1 
ATOM   5079 N N     . TYR B 1 130 ? 30.907 -5.312  -56.489 1.00 20.72  ? 130 TYR B N     1 
ATOM   5080 C CA    . TYR B 1 130 ? 31.270 -4.255  -55.563 1.00 21.15  ? 130 TYR B CA    1 
ATOM   5081 C C     . TYR B 1 130 ? 31.039 -2.886  -56.201 1.00 22.66  ? 130 TYR B C     1 
ATOM   5082 O O     . TYR B 1 130 ? 30.548 -1.989  -55.515 1.00 22.80  ? 130 TYR B O     1 
ATOM   5083 C CB    . TYR B 1 130 ? 32.709 -4.438  -55.096 1.00 20.95  ? 130 TYR B CB    1 
ATOM   5084 C CG    . TYR B 1 130 ? 32.984 -5.651  -54.248 1.00 22.23  ? 130 TYR B CG    1 
ATOM   5085 C CD1   . TYR B 1 130 ? 32.735 -5.641  -52.873 1.00 24.01  ? 130 TYR B CD1   1 
ATOM   5086 C CD2   . TYR B 1 130 ? 33.564 -6.786  -54.794 1.00 21.90  ? 130 TYR B CD2   1 
ATOM   5087 C CE1   . TYR B 1 130 ? 33.010 -6.745  -52.075 1.00 22.99  ? 130 TYR B CE1   1 
ATOM   5088 C CE2   . TYR B 1 130 ? 33.841 -7.898  -54.012 1.00 22.04  ? 130 TYR B CE2   1 
ATOM   5089 C CZ    . TYR B 1 130 ? 33.584 -7.871  -52.648 1.00 23.68  ? 130 TYR B CZ    1 
ATOM   5090 O OH    . TYR B 1 130 ? 33.861 -8.964  -51.872 1.00 23.30  ? 130 TYR B OH    1 
ATOM   5091 N N     . PHE B 1 131 ? 31.368 -2.730  -57.503 1.00 24.96  ? 131 PHE B N     1 
ATOM   5092 C CA    . PHE B 1 131 ? 31.045 -1.518  -58.253 1.00 26.86  ? 131 PHE B CA    1 
ATOM   5093 C C     . PHE B 1 131 ? 29.561 -1.208  -58.126 1.00 25.51  ? 131 PHE B C     1 
ATOM   5094 O O     . PHE B 1 131 ? 29.196 -0.074  -57.835 1.00 25.96  ? 131 PHE B O     1 
ATOM   5095 C CB    . PHE B 1 131 ? 31.366 -1.623  -59.748 1.00 30.65  ? 131 PHE B CB    1 
ATOM   5096 C CG    . PHE B 1 131 ? 32.835 -1.568  -60.071 1.00 37.13  ? 131 PHE B CG    1 
ATOM   5097 C CD1   . PHE B 1 131 ? 33.581 -0.427  -59.795 1.00 39.92  ? 131 PHE B CD1   1 
ATOM   5098 C CD2   . PHE B 1 131 ? 33.491 -2.672  -60.605 1.00 41.04  ? 131 PHE B CD2   1 
ATOM   5099 C CE1   . PHE B 1 131 ? 34.950 -0.397  -60.033 1.00 42.03  ? 131 PHE B CE1   1 
ATOM   5100 C CE2   . PHE B 1 131 ? 34.862 -2.638  -60.838 1.00 40.94  ? 131 PHE B CE2   1 
ATOM   5101 C CZ    . PHE B 1 131 ? 35.584 -1.494  -60.581 1.00 39.32  ? 131 PHE B CZ    1 
ATOM   5102 N N     . GLU B 1 132 ? 28.711 -2.221  -58.347 1.00 24.52  ? 132 GLU B N     1 
ATOM   5103 C CA    . GLU B 1 132 ? 27.279 -1.984  -58.371 1.00 28.06  ? 132 GLU B CA    1 
ATOM   5104 C C     . GLU B 1 132 ? 26.783 -1.488  -57.013 1.00 27.34  ? 132 GLU B C     1 
ATOM   5105 O O     . GLU B 1 132 ? 25.985 -0.568  -56.962 1.00 26.21  ? 132 GLU B O     1 
ATOM   5106 C CB    . GLU B 1 132 ? 26.515 -3.234  -58.802 1.00 31.18  ? 132 GLU B CB    1 
ATOM   5107 C CG    . GLU B 1 132 ? 26.423 -3.379  -60.318 1.00 36.14  ? 132 GLU B CG    1 
ATOM   5108 C CD    . GLU B 1 132 ? 26.006 -4.755  -60.809 1.00 36.15  ? 132 GLU B CD    1 
ATOM   5109 O OE1   . GLU B 1 132 ? 25.959 -5.681  -60.007 1.00 34.63  ? 132 GLU B OE1   1 
ATOM   5110 O OE2   . GLU B 1 132 ? 25.734 -4.887  -61.994 1.00 52.15  ? 132 GLU B OE2   1 
ATOM   5111 N N     . LEU B 1 133 ? 27.225 -2.124  -55.920 1.00 26.67  ? 133 LEU B N     1 
ATOM   5112 C CA    . LEU B 1 133 ? 26.733 -1.782  -54.596 1.00 24.64  ? 133 LEU B CA    1 
ATOM   5113 C C     . LEU B 1 133 ? 27.297 -0.424  -54.198 1.00 22.19  ? 133 LEU B C     1 
ATOM   5114 O O     . LEU B 1 133 ? 26.573 0.385   -53.625 1.00 21.36  ? 133 LEU B O     1 
ATOM   5115 C CB    . LEU B 1 133 ? 27.133 -2.890  -53.617 1.00 25.27  ? 133 LEU B CB    1 
ATOM   5116 C CG    . LEU B 1 133 ? 26.786 -2.643  -52.156 1.00 26.22  ? 133 LEU B CG    1 
ATOM   5117 C CD1   . LEU B 1 133 ? 25.267 -2.572  -51.979 1.00 25.91  ? 133 LEU B CD1   1 
ATOM   5118 C CD2   . LEU B 1 133 ? 27.402 -3.725  -51.263 1.00 25.24  ? 133 LEU B CD2   1 
ATOM   5119 N N     . TYR B 1 134 ? 28.552 -0.157  -54.585 1.00 21.13  ? 134 TYR B N     1 
ATOM   5120 C CA    . TYR B 1 134 ? 29.168 1.134   -54.327 1.00 22.74  ? 134 TYR B CA    1 
ATOM   5121 C C     . TYR B 1 134 ? 28.406 2.214   -55.081 1.00 25.18  ? 134 TYR B C     1 
ATOM   5122 O O     . TYR B 1 134 ? 28.044 3.212   -54.478 1.00 28.08  ? 134 TYR B O     1 
ATOM   5123 C CB    . TYR B 1 134 ? 30.646 1.129   -54.714 1.00 22.99  ? 134 TYR B CB    1 
ATOM   5124 C CG    . TYR B 1 134 ? 31.368 2.442   -54.541 1.00 24.38  ? 134 TYR B CG    1 
ATOM   5125 C CD1   . TYR B 1 134 ? 31.947 2.789   -53.332 1.00 24.00  ? 134 TYR B CD1   1 
ATOM   5126 C CD2   . TYR B 1 134 ? 31.504 3.331   -55.604 1.00 25.43  ? 134 TYR B CD2   1 
ATOM   5127 C CE1   . TYR B 1 134 ? 32.618 3.996   -53.171 1.00 24.56  ? 134 TYR B CE1   1 
ATOM   5128 C CE2   . TYR B 1 134 ? 32.163 4.544   -55.461 1.00 24.83  ? 134 TYR B CE2   1 
ATOM   5129 C CZ    . TYR B 1 134 ? 32.718 4.881   -54.235 1.00 27.20  ? 134 TYR B CZ    1 
ATOM   5130 O OH    . TYR B 1 134 ? 33.388 6.074   -54.070 1.00 28.45  ? 134 TYR B OH    1 
ATOM   5131 N N     . ASP B 1 135 ? 28.139 1.988   -56.377 1.00 27.20  ? 135 ASP B N     1 
ATOM   5132 C CA    . ASP B 1 135 ? 27.427 2.958   -57.190 1.00 31.34  ? 135 ASP B CA    1 
ATOM   5133 C C     . ASP B 1 135 ? 26.065 3.277   -56.578 1.00 28.00  ? 135 ASP B C     1 
ATOM   5134 O O     . ASP B 1 135 ? 25.727 4.443   -56.450 1.00 28.03  ? 135 ASP B O     1 
ATOM   5135 C CB    . ASP B 1 135 ? 27.321 2.517   -58.653 1.00 35.52  ? 135 ASP B CB    1 
ATOM   5136 C CG    . ASP B 1 135 ? 28.644 2.600   -59.402 1.00 43.23  ? 135 ASP B CG    1 
ATOM   5137 O OD1   . ASP B 1 135 ? 29.619 3.158   -58.827 1.00 41.88  ? 135 ASP B OD1   1 
ATOM   5138 O OD2   . ASP B 1 135 ? 28.708 2.078   -60.549 1.00 49.91  ? 135 ASP B OD2   1 
ATOM   5139 N N     . TYR B 1 136 ? 25.302 2.255   -56.178 1.00 27.06  ? 136 TYR B N     1 
ATOM   5140 C CA    . TYR B 1 136 ? 23.978 2.448   -55.606 1.00 28.54  ? 136 TYR B CA    1 
ATOM   5141 C C     . TYR B 1 136 ? 24.060 3.322   -54.352 1.00 31.47  ? 136 TYR B C     1 
ATOM   5142 O O     . TYR B 1 136 ? 23.307 4.280   -54.227 1.00 33.05  ? 136 TYR B O     1 
ATOM   5143 C CB    . TYR B 1 136 ? 23.320 1.092   -55.355 1.00 30.08  ? 136 TYR B CB    1 
ATOM   5144 C CG    . TYR B 1 136 ? 21.978 1.122   -54.672 1.00 32.81  ? 136 TYR B CG    1 
ATOM   5145 C CD1   . TYR B 1 136 ? 21.870 1.300   -53.302 1.00 34.33  ? 136 TYR B CD1   1 
ATOM   5146 C CD2   . TYR B 1 136 ? 20.803 0.939   -55.401 1.00 36.86  ? 136 TYR B CD2   1 
ATOM   5147 C CE1   . TYR B 1 136 ? 20.631 1.293   -52.669 1.00 38.96  ? 136 TYR B CE1   1 
ATOM   5148 C CE2   . TYR B 1 136 ? 19.557 0.952   -54.794 1.00 37.75  ? 136 TYR B CE2   1 
ATOM   5149 C CZ    . TYR B 1 136 ? 19.472 1.123   -53.420 1.00 42.61  ? 136 TYR B CZ    1 
ATOM   5150 O OH    . TYR B 1 136 ? 18.243 1.147   -52.822 1.00 43.91  ? 136 TYR B OH    1 
ATOM   5151 N N     . ILE B 1 137 ? 25.012 3.028   -53.454 1.00 32.53  ? 137 ILE B N     1 
ATOM   5152 C CA    . ILE B 1 137 ? 25.207 3.828   -52.250 1.00 30.61  ? 137 ILE B CA    1 
ATOM   5153 C C     . ILE B 1 137 ? 25.487 5.304   -52.576 1.00 30.34  ? 137 ILE B C     1 
ATOM   5154 O O     . ILE B 1 137 ? 24.899 6.183   -51.940 1.00 27.08  ? 137 ILE B O     1 
ATOM   5155 C CB    . ILE B 1 137 ? 26.302 3.205   -51.360 1.00 27.29  ? 137 ILE B CB    1 
ATOM   5156 C CG1   . ILE B 1 137 ? 25.804 1.896   -50.740 1.00 27.11  ? 137 ILE B CG1   1 
ATOM   5157 C CG2   . ILE B 1 137 ? 26.778 4.198   -50.299 1.00 26.65  ? 137 ILE B CG2   1 
ATOM   5158 C CD1   . ILE B 1 137 ? 26.871 1.087   -50.043 1.00 25.89  ? 137 ILE B CD1   1 
ATOM   5159 N N     . GLN B 1 138 ? 26.411 5.581   -53.510 1.00 31.88  ? 138 GLN B N     1 
ATOM   5160 C CA    . GLN B 1 138 ? 26.763 6.954   -53.858 1.00 35.32  ? 138 GLN B CA    1 
ATOM   5161 C C     . GLN B 1 138 ? 25.562 7.687   -54.454 1.00 38.13  ? 138 GLN B C     1 
ATOM   5162 O O     . GLN B 1 138 ? 25.284 8.816   -54.059 1.00 40.61  ? 138 GLN B O     1 
ATOM   5163 C CB    . GLN B 1 138 ? 27.916 7.028   -54.858 1.00 38.04  ? 138 GLN B CB    1 
ATOM   5164 C CG    . GLN B 1 138 ? 29.224 6.436   -54.354 1.00 43.11  ? 138 GLN B CG    1 
ATOM   5165 C CD    . GLN B 1 138 ? 29.619 6.859   -52.956 1.00 44.87  ? 138 GLN B CD    1 
ATOM   5166 O OE1   . GLN B 1 138 ? 30.006 7.994   -52.720 1.00 41.41  ? 138 GLN B OE1   1 
ATOM   5167 N NE2   . GLN B 1 138 ? 29.561 5.930   -52.014 1.00 48.42  ? 138 GLN B NE2   1 
ATOM   5168 N N     . GLU B 1 139 ? 24.825 7.025   -55.355 1.00 40.51  ? 139 GLU B N     1 
ATOM   5169 C CA    . GLU B 1 139 ? 23.692 7.639   -56.032 1.00 46.24  ? 139 GLU B CA    1 
ATOM   5170 C C     . GLU B 1 139 ? 22.578 7.972   -55.041 1.00 41.66  ? 139 GLU B C     1 
ATOM   5171 O O     . GLU B 1 139 ? 21.908 8.982   -55.215 1.00 38.26  ? 139 GLU B O     1 
ATOM   5172 C CB    . GLU B 1 139 ? 23.180 6.770   -57.190 1.00 51.59  ? 139 GLU B CB    1 
ATOM   5173 C CG    . GLU B 1 139 ? 23.737 7.189   -58.546 1.00 63.61  ? 139 GLU B CG    1 
ATOM   5174 C CD    . GLU B 1 139 ? 24.100 6.068   -59.515 1.00 79.83  ? 139 GLU B CD    1 
ATOM   5175 O OE1   . GLU B 1 139 ? 23.284 5.124   -59.675 1.00 85.25  ? 139 GLU B OE1   1 
ATOM   5176 O OE2   . GLU B 1 139 ? 25.206 6.143   -60.120 1.00 85.08  ? 139 GLU B OE2   1 
ATOM   5177 N N     . LYS B 1 140 ? 22.385 7.149   -54.002 1.00 39.47  ? 140 LYS B N     1 
ATOM   5178 C CA    . LYS B 1 140 ? 21.351 7.417   -53.013 1.00 35.61  ? 140 LYS B CA    1 
ATOM   5179 C C     . LYS B 1 140 ? 21.881 8.314   -51.896 1.00 32.31  ? 140 LYS B C     1 
ATOM   5180 O O     . LYS B 1 140 ? 21.120 8.700   -51.016 1.00 32.25  ? 140 LYS B O     1 
ATOM   5181 C CB    . LYS B 1 140 ? 20.810 6.120   -52.418 1.00 39.30  ? 140 LYS B CB    1 
ATOM   5182 C CG    . LYS B 1 140 ? 20.204 5.156   -53.419 1.00 45.37  ? 140 LYS B CG    1 
ATOM   5183 C CD    . LYS B 1 140 ? 18.901 5.617   -54.030 1.00 53.61  ? 140 LYS B CD    1 
ATOM   5184 C CE    . LYS B 1 140 ? 18.455 4.690   -55.145 1.00 59.17  ? 140 LYS B CE    1 
ATOM   5185 N NZ    . LYS B 1 140 ? 17.036 4.899   -55.501 1.00 59.60  ? 140 LYS B NZ    1 
ATOM   5186 N N     . GLY B 1 141 ? 23.176 8.639   -51.923 1.00 29.44  ? 141 GLY B N     1 
ATOM   5187 C CA    . GLY B 1 141 ? 23.768 9.475   -50.894 1.00 30.95  ? 141 GLY B CA    1 
ATOM   5188 C C     . GLY B 1 141 ? 23.795 8.846   -49.492 1.00 30.46  ? 141 GLY B C     1 
ATOM   5189 O O     . GLY B 1 141 ? 23.998 9.556   -48.511 1.00 31.37  ? 141 GLY B O     1 
ATOM   5190 N N     . LEU B 1 142 ? 23.694 7.515   -49.382 1.00 28.59  ? 142 LEU B N     1 
ATOM   5191 C CA    . LEU B 1 142 ? 23.734 6.875   -48.071 1.00 30.10  ? 142 LEU B CA    1 
ATOM   5192 C C     . LEU B 1 142 ? 25.142 7.002   -47.459 1.00 28.16  ? 142 LEU B C     1 
ATOM   5193 O O     . LEU B 1 142 ? 26.143 6.857   -48.149 1.00 28.11  ? 142 LEU B O     1 
ATOM   5194 C CB    . LEU B 1 142 ? 23.293 5.411   -48.203 1.00 28.39  ? 142 LEU B CB    1 
ATOM   5195 C CG    . LEU B 1 142 ? 21.992 5.164   -48.972 1.00 29.93  ? 142 LEU B CG    1 
ATOM   5196 C CD1   . LEU B 1 142 ? 21.719 3.679   -49.116 1.00 31.01  ? 142 LEU B CD1   1 
ATOM   5197 C CD2   . LEU B 1 142 ? 20.805 5.823   -48.302 1.00 29.72  ? 142 LEU B CD2   1 
ATOM   5198 N N     . LYS B 1 143 ? 25.206 7.235   -46.146 1.00 27.57  ? 143 LYS B N     1 
ATOM   5199 C CA    . LYS B 1 143 ? 26.460 7.398   -45.425 1.00 33.67  ? 143 LYS B CA    1 
ATOM   5200 C C     . LYS B 1 143 ? 27.011 6.046   -44.958 1.00 32.45  ? 143 LYS B C     1 
ATOM   5201 O O     . LYS B 1 143 ? 27.090 5.761   -43.753 1.00 29.73  ? 143 LYS B O     1 
ATOM   5202 C CB    . LYS B 1 143 ? 26.262 8.320   -44.212 1.00 42.07  ? 143 LYS B CB    1 
ATOM   5203 C CG    . LYS B 1 143 ? 25.540 9.640   -44.463 1.00 46.32  ? 143 LYS B CG    1 
ATOM   5204 C CD    . LYS B 1 143 ? 26.285 10.608  -45.353 1.00 58.17  ? 143 LYS B CD    1 
ATOM   5205 C CE    . LYS B 1 143 ? 25.768 12.028  -45.240 1.00 66.41  ? 143 LYS B CE    1 
ATOM   5206 N NZ    . LYS B 1 143 ? 25.819 12.498  -43.832 1.00 67.24  ? 143 LYS B NZ    1 
ATOM   5207 N N     . LEU B 1 144 ? 27.449 5.238   -45.934 1.00 30.80  ? 144 LEU B N     1 
ATOM   5208 C CA    . LEU B 1 144 ? 27.936 3.887   -45.691 1.00 26.74  ? 144 LEU B CA    1 
ATOM   5209 C C     . LEU B 1 144 ? 29.142 3.621   -46.574 1.00 25.11  ? 144 LEU B C     1 
ATOM   5210 O O     . LEU B 1 144 ? 29.194 4.081   -47.711 1.00 25.12  ? 144 LEU B O     1 
ATOM   5211 C CB    . LEU B 1 144 ? 26.860 2.869   -46.077 1.00 25.75  ? 144 LEU B CB    1 
ATOM   5212 C CG    . LEU B 1 144 ? 25.551 2.853   -45.293 1.00 23.39  ? 144 LEU B CG    1 
ATOM   5213 C CD1   . LEU B 1 144 ? 24.573 1.919   -45.967 1.00 23.11  ? 144 LEU B CD1   1 
ATOM   5214 C CD2   . LEU B 1 144 ? 25.756 2.401   -43.864 1.00 23.87  ? 144 LEU B CD2   1 
ATOM   5215 N N     . TRP B 1 145 ? 30.064 2.803   -46.075 1.00 24.65  ? 145 TRP B N     1 
ATOM   5216 C CA    . TRP B 1 145 ? 31.160 2.318   -46.883 1.00 23.53  ? 145 TRP B CA    1 
ATOM   5217 C C     . TRP B 1 145 ? 30.961 0.833   -47.161 1.00 24.37  ? 145 TRP B C     1 
ATOM   5218 O O     . TRP B 1 145 ? 30.316 0.101   -46.394 1.00 24.08  ? 145 TRP B O     1 
ATOM   5219 C CB    . TRP B 1 145 ? 32.507 2.588   -46.210 1.00 24.59  ? 145 TRP B CB    1 
ATOM   5220 C CG    . TRP B 1 145 ? 32.931 4.021   -46.229 1.00 26.17  ? 145 TRP B CG    1 
ATOM   5221 C CD1   . TRP B 1 145 ? 32.239 5.097   -46.706 1.00 26.25  ? 145 TRP B CD1   1 
ATOM   5222 C CD2   . TRP B 1 145 ? 34.177 4.539   -45.730 1.00 26.69  ? 145 TRP B CD2   1 
ATOM   5223 N NE1   . TRP B 1 145 ? 32.968 6.244   -46.533 1.00 27.18  ? 145 TRP B NE1   1 
ATOM   5224 C CE2   . TRP B 1 145 ? 34.153 5.934   -45.927 1.00 25.82  ? 145 TRP B CE2   1 
ATOM   5225 C CE3   . TRP B 1 145 ? 35.304 3.954   -45.147 1.00 26.27  ? 145 TRP B CE3   1 
ATOM   5226 C CZ2   . TRP B 1 145 ? 35.211 6.752   -45.557 1.00 28.60  ? 145 TRP B CZ2   1 
ATOM   5227 C CZ3   . TRP B 1 145 ? 36.348 4.766   -44.774 1.00 26.85  ? 145 TRP B CZ3   1 
ATOM   5228 C CH2   . TRP B 1 145 ? 36.299 6.145   -44.973 1.00 28.86  ? 145 TRP B CH2   1 
ATOM   5229 N N     . ILE B 1 146 ? 31.552 0.386   -48.272 1.00 24.54  ? 146 ILE B N     1 
ATOM   5230 C CA    . ILE B 1 146 ? 31.703 -1.040  -48.472 1.00 24.77  ? 146 ILE B CA    1 
ATOM   5231 C C     . ILE B 1 146 ? 33.143 -1.410  -48.132 1.00 23.84  ? 146 ILE B C     1 
ATOM   5232 O O     . ILE B 1 146 ? 33.974 -0.549  -47.883 1.00 22.45  ? 146 ILE B O     1 
ATOM   5233 C CB    . ILE B 1 146 ? 31.280 -1.444  -49.894 1.00 25.76  ? 146 ILE B CB    1 
ATOM   5234 C CG1   . ILE B 1 146 ? 32.158 -0.826  -50.976 1.00 28.74  ? 146 ILE B CG1   1 
ATOM   5235 C CG2   . ILE B 1 146 ? 29.820 -1.124  -50.142 1.00 26.54  ? 146 ILE B CG2   1 
ATOM   5236 C CD1   . ILE B 1 146 ? 31.889 -1.440  -52.357 1.00 30.49  ? 146 ILE B CD1   1 
ATOM   5237 N N     . ASP B 1 147 ? 33.421 -2.708  -48.100 1.00 24.74  ? 147 ASP B N     1 
ATOM   5238 C CA    . ASP B 1 147 ? 34.783 -3.185  -47.974 1.00 24.84  ? 147 ASP B CA    1 
ATOM   5239 C C     . ASP B 1 147 ? 35.087 -4.017  -49.220 1.00 23.40  ? 147 ASP B C     1 
ATOM   5240 O O     . ASP B 1 147 ? 34.438 -5.012  -49.470 1.00 24.57  ? 147 ASP B O     1 
ATOM   5241 C CB    . ASP B 1 147 ? 34.964 -3.950  -46.660 1.00 25.42  ? 147 ASP B CB    1 
ATOM   5242 C CG    . ASP B 1 147 ? 36.391 -4.417  -46.457 1.00 27.59  ? 147 ASP B CG    1 
ATOM   5243 O OD1   . ASP B 1 147 ? 36.831 -5.258  -47.276 1.00 27.12  ? 147 ASP B OD1   1 
ATOM   5244 O OD2   . ASP B 1 147 ? 37.065 -3.909  -45.508 1.00 29.08  ? 147 ASP B OD2   1 
ATOM   5245 N N     . VAL B 1 148 ? 36.070 -3.581  -49.994 1.00 22.23  ? 148 VAL B N     1 
ATOM   5246 C CA    . VAL B 1 148 ? 36.358 -4.159  -51.286 1.00 23.80  ? 148 VAL B CA    1 
ATOM   5247 C C     . VAL B 1 148 ? 37.685 -4.912  -51.224 1.00 24.39  ? 148 VAL B C     1 
ATOM   5248 O O     . VAL B 1 148 ? 38.639 -4.446  -50.588 1.00 21.77  ? 148 VAL B O     1 
ATOM   5249 C CB    . VAL B 1 148 ? 36.438 -3.077  -52.378 1.00 24.58  ? 148 VAL B CB    1 
ATOM   5250 C CG1   . VAL B 1 148 ? 35.102 -2.409  -52.556 1.00 29.34  ? 148 VAL B CG1   1 
ATOM   5251 C CG2   . VAL B 1 148 ? 37.520 -2.040  -52.099 1.00 24.00  ? 148 VAL B CG2   1 
ATOM   5252 N N     . PRO B 1 149 ? 37.822 -5.999  -52.019 1.00 24.60  ? 149 PRO B N     1 
ATOM   5253 C CA    . PRO B 1 149 ? 39.136 -6.563  -52.326 1.00 27.35  ? 149 PRO B CA    1 
ATOM   5254 C C     . PRO B 1 149 ? 39.912 -5.545  -53.158 1.00 26.88  ? 149 PRO B C     1 
ATOM   5255 O O     . PRO B 1 149 ? 39.411 -4.478  -53.490 1.00 30.73  ? 149 PRO B O     1 
ATOM   5256 C CB    . PRO B 1 149 ? 38.833 -7.828  -53.140 1.00 29.03  ? 149 PRO B CB    1 
ATOM   5257 C CG    . PRO B 1 149 ? 37.331 -8.023  -53.017 1.00 28.51  ? 149 PRO B CG    1 
ATOM   5258 C CD    . PRO B 1 149 ? 36.746 -6.648  -52.778 1.00 25.62  ? 149 PRO B CD    1 
ATOM   5259 N N     . ASP B 1 150 ? 41.131 -5.869  -53.539 1.00 29.92  ? 150 ASP B N     1 
ATOM   5260 C CA    . ASP B 1 150 ? 41.943 -4.925  -54.301 1.00 30.82  ? 150 ASP B CA    1 
ATOM   5261 C C     . ASP B 1 150 ? 41.297 -4.597  -55.650 1.00 29.72  ? 150 ASP B C     1 
ATOM   5262 O O     . ASP B 1 150 ? 41.649 -3.598  -56.247 1.00 32.47  ? 150 ASP B O     1 
ATOM   5263 C CB    . ASP B 1 150 ? 43.357 -5.474  -54.499 1.00 34.06  ? 150 ASP B CB    1 
ATOM   5264 C CG    . ASP B 1 150 ? 44.294 -5.225  -53.327 1.00 38.38  ? 150 ASP B CG    1 
ATOM   5265 O OD1   . ASP B 1 150 ? 44.050 -4.251  -52.574 1.00 38.35  ? 150 ASP B OD1   1 
ATOM   5266 O OD2   . ASP B 1 150 ? 45.263 -5.995  -53.186 1.00 44.48  ? 150 ASP B OD2   1 
ATOM   5267 N N     . ILE B 1 151 ? 40.358 -5.437  -56.112 1.00 27.42  ? 151 ILE B N     1 
ATOM   5268 C CA    . ILE B 1 151 ? 39.732 -5.330  -57.412 1.00 25.53  ? 151 ILE B CA    1 
ATOM   5269 C C     . ILE B 1 151 ? 38.232 -5.432  -57.172 1.00 24.77  ? 151 ILE B C     1 
ATOM   5270 O O     . ILE B 1 151 ? 37.827 -6.157  -56.270 1.00 25.66  ? 151 ILE B O     1 
ATOM   5271 C CB    . ILE B 1 151 ? 40.299 -6.410  -58.363 1.00 31.24  ? 151 ILE B CB    1 
ATOM   5272 C CG1   . ILE B 1 151 ? 40.322 -7.823  -57.769 1.00 36.51  ? 151 ILE B CG1   1 
ATOM   5273 C CG2   . ILE B 1 151 ? 41.707 -6.034  -58.802 1.00 32.63  ? 151 ILE B CG2   1 
ATOM   5274 C CD1   . ILE B 1 151 ? 39.119 -8.635  -58.052 1.00 42.42  ? 151 ILE B CD1   1 
ATOM   5275 N N     . GLY B 1 152 ? 37.421 -4.676  -57.927 1.00 22.38  ? 152 GLY B N     1 
ATOM   5276 C CA    . GLY B 1 152 ? 36.023 -4.470  -57.568 1.00 23.44  ? 152 GLY B CA    1 
ATOM   5277 C C     . GLY B 1 152 ? 34.963 -5.098  -58.487 1.00 23.80  ? 152 GLY B C     1 
ATOM   5278 O O     . GLY B 1 152 ? 33.772 -4.877  -58.288 1.00 23.71  ? 152 GLY B O     1 
ATOM   5279 N N     . TRP B 1 153 ? 35.346 -5.912  -59.469 1.00 23.00  ? 153 TRP B N     1 
ATOM   5280 C CA    . TRP B 1 153 ? 34.363 -6.488  -60.380 1.00 21.90  ? 153 TRP B CA    1 
ATOM   5281 C C     . TRP B 1 153 ? 33.832 -7.842  -59.893 1.00 21.57  ? 153 TRP B C     1 
ATOM   5282 O O     . TRP B 1 153 ? 32.986 -8.448  -60.549 1.00 23.06  ? 153 TRP B O     1 
ATOM   5283 C CB    . TRP B 1 153 ? 34.931 -6.564  -61.804 1.00 20.84  ? 153 TRP B CB    1 
ATOM   5284 C CG    . TRP B 1 153 ? 36.118 -7.452  -62.024 1.00 24.64  ? 153 TRP B CG    1 
ATOM   5285 C CD1   . TRP B 1 153 ? 36.738 -8.290  -61.134 1.00 26.01  ? 153 TRP B CD1   1 
ATOM   5286 C CD2   . TRP B 1 153 ? 36.821 -7.612  -63.274 1.00 26.59  ? 153 TRP B CD2   1 
ATOM   5287 N NE1   . TRP B 1 153 ? 37.762 -8.964  -61.746 1.00 27.40  ? 153 TRP B NE1   1 
ATOM   5288 C CE2   . TRP B 1 153 ? 37.828 -8.584  -63.064 1.00 27.69  ? 153 TRP B CE2   1 
ATOM   5289 C CE3   . TRP B 1 153 ? 36.695 -7.027  -64.542 1.00 25.85  ? 153 TRP B CE3   1 
ATOM   5290 C CZ2   . TRP B 1 153 ? 38.725 -8.954  -64.071 1.00 29.25  ? 153 TRP B CZ2   1 
ATOM   5291 C CZ3   . TRP B 1 153 ? 37.547 -7.434  -65.549 1.00 28.33  ? 153 TRP B CZ3   1 
ATOM   5292 C CH2   . TRP B 1 153 ? 38.560 -8.375  -65.313 1.00 28.82  ? 153 TRP B CH2   1 
ATOM   5293 N N     . GLY B 1 154 ? 34.291 -8.315  -58.735 1.00 20.27  ? 154 GLY B N     1 
ATOM   5294 C CA    . GLY B 1 154 ? 33.775 -9.553  -58.170 1.00 21.81  ? 154 GLY B CA    1 
ATOM   5295 C C     . GLY B 1 154 ? 32.458 -9.371  -57.411 1.00 22.07  ? 154 GLY B C     1 
ATOM   5296 O O     . GLY B 1 154 ? 31.843 -8.310  -57.467 1.00 24.77  ? 154 GLY B O     1 
ATOM   5297 N N     . SER B 1 155 ? 32.041 -10.428 -56.699 1.00 21.57  ? 155 SER B N     1 
ATOM   5298 C CA    . SER B 1 155 ? 30.728 -10.513 -56.073 1.00 20.92  ? 155 SER B CA    1 
ATOM   5299 C C     . SER B 1 155 ? 30.827 -10.249 -54.580 1.00 19.43  ? 155 SER B C     1 
ATOM   5300 O O     . SER B 1 155 ? 31.569 -10.931 -53.889 1.00 17.77  ? 155 SER B O     1 
ATOM   5301 C CB    . SER B 1 155 ? 30.106 -11.874 -56.274 1.00 21.56  ? 155 SER B CB    1 
ATOM   5302 O OG    . SER B 1 155 ? 28.942 -12.033 -55.446 1.00 22.92  ? 155 SER B OG    1 
ATOM   5303 N N     . VAL B 1 156 ? 29.950 -9.387  -54.065 1.00 20.15  ? 156 VAL B N     1 
ATOM   5304 C CA    . VAL B 1 156 ? 29.887 -9.197  -52.627 1.00 21.08  ? 156 VAL B CA    1 
ATOM   5305 C C     . VAL B 1 156 ? 29.641 -10.555 -51.972 1.00 21.83  ? 156 VAL B C     1 
ATOM   5306 O O     . VAL B 1 156 ? 30.263 -10.873 -50.951 1.00 23.04  ? 156 VAL B O     1 
ATOM   5307 C CB    . VAL B 1 156 ? 28.837 -8.153  -52.206 1.00 21.29  ? 156 VAL B CB    1 
ATOM   5308 C CG1   . VAL B 1 156 ? 28.738 -8.051  -50.698 1.00 20.95  ? 156 VAL B CG1   1 
ATOM   5309 C CG2   . VAL B 1 156 ? 29.110 -6.779  -52.797 1.00 22.12  ? 156 VAL B CG2   1 
ATOM   5310 N N     . VAL B 1 157 ? 28.762 -11.356 -52.595 1.00 21.81  ? 157 VAL B N     1 
ATOM   5311 C CA    . VAL B 1 157 ? 28.434 -12.683 -52.094 1.00 21.71  ? 157 VAL B CA    1 
ATOM   5312 C C     . VAL B 1 157 ? 29.569 -13.685 -52.309 1.00 21.57  ? 157 VAL B C     1 
ATOM   5313 O O     . VAL B 1 157 ? 30.032 -14.292 -51.345 1.00 23.32  ? 157 VAL B O     1 
ATOM   5314 C CB    . VAL B 1 157 ? 27.127 -13.215 -52.687 1.00 20.53  ? 157 VAL B CB    1 
ATOM   5315 C CG1   . VAL B 1 157 ? 26.891 -14.642 -52.231 1.00 21.08  ? 157 VAL B CG1   1 
ATOM   5316 C CG2   . VAL B 1 157 ? 25.974 -12.325 -52.287 1.00 20.42  ? 157 VAL B CG2   1 
ATOM   5317 N N     . GLY B 1 158 ? 29.993 -13.881 -53.559 1.00 21.93  ? 158 GLY B N     1 
ATOM   5318 C CA    . GLY B 1 158 ? 30.920 -14.960 -53.914 1.00 21.23  ? 158 GLY B CA    1 
ATOM   5319 C C     . GLY B 1 158 ? 32.239 -14.842 -53.154 1.00 19.72  ? 158 GLY B C     1 
ATOM   5320 O O     . GLY B 1 158 ? 32.758 -15.810 -52.608 1.00 19.59  ? 158 GLY B O     1 
ATOM   5321 N N     . ASN B 1 159 ? 32.738 -13.616 -53.088 1.00 19.55  ? 159 ASN B N     1 
ATOM   5322 C CA    . ASN B 1 159 ? 33.977 -13.324 -52.403 1.00 21.13  ? 159 ASN B CA    1 
ATOM   5323 C C     . ASN B 1 159 ? 33.839 -13.712 -50.930 1.00 19.87  ? 159 ASN B C     1 
ATOM   5324 O O     . ASN B 1 159 ? 34.629 -14.487 -50.388 1.00 19.59  ? 159 ASN B O     1 
ATOM   5325 C CB    . ASN B 1 159 ? 34.393 -11.872 -52.670 1.00 22.70  ? 159 ASN B CB    1 
ATOM   5326 C CG    . ASN B 1 159 ? 35.633 -11.464 -51.903 1.00 24.97  ? 159 ASN B CG    1 
ATOM   5327 O OD1   . ASN B 1 159 ? 35.563 -11.208 -50.708 1.00 27.31  ? 159 ASN B OD1   1 
ATOM   5328 N ND2   . ASN B 1 159 ? 36.768 -11.385 -52.566 1.00 26.40  ? 159 ASN B ND2   1 
ATOM   5329 N N     . ALA B 1 160 ? 32.798 -13.206 -50.282 1.00 19.27  ? 160 ALA B N     1 
ATOM   5330 C CA    . ALA B 1 160 ? 32.587 -13.518 -48.882 1.00 19.87  ? 160 ALA B CA    1 
ATOM   5331 C C     . ALA B 1 160 ? 32.575 -15.028 -48.678 1.00 20.43  ? 160 ALA B C     1 
ATOM   5332 O O     . ALA B 1 160 ? 33.173 -15.520 -47.716 1.00 20.78  ? 160 ALA B O     1 
ATOM   5333 C CB    . ALA B 1 160 ? 31.320 -12.869 -48.380 1.00 19.57  ? 160 ALA B CB    1 
ATOM   5334 N N     . LEU B 1 161 ? 31.890 -15.745 -49.581 1.00 20.54  ? 161 LEU B N     1 
ATOM   5335 C CA    . LEU B 1 161 ? 31.707 -17.173 -49.412 1.00 21.93  ? 161 LEU B CA    1 
ATOM   5336 C C     . LEU B 1 161 ? 33.035 -17.891 -49.534 1.00 21.04  ? 161 LEU B C     1 
ATOM   5337 O O     . LEU B 1 161 ? 33.192 -18.927 -48.928 1.00 23.74  ? 161 LEU B O     1 
ATOM   5338 C CB    . LEU B 1 161 ? 30.715 -17.722 -50.434 1.00 22.53  ? 161 LEU B CB    1 
ATOM   5339 C CG    . LEU B 1 161 ? 29.250 -17.331 -50.216 1.00 23.34  ? 161 LEU B CG    1 
ATOM   5340 C CD1   . LEU B 1 161 ? 28.387 -17.874 -51.344 1.00 22.91  ? 161 LEU B CD1   1 
ATOM   5341 C CD2   . LEU B 1 161 ? 28.722 -17.823 -48.871 1.00 22.38  ? 161 LEU B CD2   1 
ATOM   5342 N N     . ASP B 1 162 ? 33.972 -17.362 -50.315 1.00 20.28  ? 162 ASP B N     1 
ATOM   5343 C CA    . ASP B 1 162 ? 35.280 -17.986 -50.435 1.00 20.79  ? 162 ASP B CA    1 
ATOM   5344 C C     . ASP B 1 162 ? 36.244 -17.448 -49.367 1.00 19.65  ? 162 ASP B C     1 
ATOM   5345 O O     . ASP B 1 162 ? 37.422 -17.729 -49.440 1.00 19.38  ? 162 ASP B O     1 
ATOM   5346 C CB    . ASP B 1 162 ? 35.883 -17.809 -51.832 1.00 21.75  ? 162 ASP B CB    1 
ATOM   5347 C CG    . ASP B 1 162 ? 36.802 -18.941 -52.295 1.00 24.90  ? 162 ASP B CG    1 
ATOM   5348 O OD1   . ASP B 1 162 ? 36.680 -20.096 -51.768 1.00 24.42  ? 162 ASP B OD1   1 
ATOM   5349 O OD2   . ASP B 1 162 ? 37.658 -18.671 -53.193 1.00 25.67  ? 162 ASP B OD2   1 
ATOM   5350 N N     . HIS B 1 163 ? 35.730 -16.728 -48.366 1.00 19.01  ? 163 HIS B N     1 
ATOM   5351 C CA    . HIS B 1 163 ? 36.488 -16.202 -47.239 1.00 19.75  ? 163 HIS B CA    1 
ATOM   5352 C C     . HIS B 1 163 ? 37.431 -15.104 -47.693 1.00 20.63  ? 163 HIS B C     1 
ATOM   5353 O O     . HIS B 1 163 ? 38.544 -14.992 -47.183 1.00 20.06  ? 163 HIS B O     1 
ATOM   5354 C CB    . HIS B 1 163 ? 37.232 -17.280 -46.444 1.00 20.19  ? 163 HIS B CB    1 
ATOM   5355 C CG    . HIS B 1 163 ? 36.320 -18.289 -45.835 1.00 19.91  ? 163 HIS B CG    1 
ATOM   5356 N ND1   . HIS B 1 163 ? 36.770 -19.519 -45.402 1.00 19.05  ? 163 HIS B ND1   1 
ATOM   5357 C CD2   . HIS B 1 163 ? 34.997 -18.276 -45.663 1.00 19.36  ? 163 HIS B CD2   1 
ATOM   5358 C CE1   . HIS B 1 163 ? 35.735 -20.207 -44.959 1.00 20.05  ? 163 HIS B CE1   1 
ATOM   5359 N NE2   . HIS B 1 163 ? 34.645 -19.479 -45.110 1.00 20.04  ? 163 HIS B NE2   1 
ATOM   5360 N N     . GLY B 1 164 ? 36.949 -14.268 -48.624 1.00 21.79  ? 164 GLY B N     1 
ATOM   5361 C CA    . GLY B 1 164 ? 37.751 -13.165 -49.124 1.00 21.51  ? 164 GLY B CA    1 
ATOM   5362 C C     . GLY B 1 164 ? 37.904 -12.073 -48.082 1.00 21.04  ? 164 GLY B C     1 
ATOM   5363 O O     . GLY B 1 164 ? 37.232 -12.083 -47.046 1.00 20.57  ? 164 GLY B O     1 
ATOM   5364 N N     . ILE B 1 165 ? 38.784 -11.128 -48.407 1.00 22.93  ? 165 ILE B N     1 
ATOM   5365 C CA    . ILE B 1 165 ? 39.178 -10.069 -47.492 1.00 23.93  ? 165 ILE B CA    1 
ATOM   5366 C C     . ILE B 1 165 ? 39.274 -8.733  -48.223 1.00 22.71  ? 165 ILE B C     1 
ATOM   5367 O O     . ILE B 1 165 ? 39.544 -8.650  -49.437 1.00 23.38  ? 165 ILE B O     1 
ATOM   5368 C CB    . ILE B 1 165 ? 40.533 -10.401 -46.843 1.00 25.90  ? 165 ILE B CB    1 
ATOM   5369 C CG1   . ILE B 1 165 ? 41.611 -10.558 -47.909 1.00 28.95  ? 165 ILE B CG1   1 
ATOM   5370 C CG2   . ILE B 1 165 ? 40.430 -11.644 -45.971 1.00 27.21  ? 165 ILE B CG2   1 
ATOM   5371 C CD1   . ILE B 1 165 ? 42.998 -10.474 -47.366 1.00 34.14  ? 165 ILE B CD1   1 
ATOM   5372 N N     . GLY B 1 166 ? 39.172 -7.684  -47.415 1.00 20.43  ? 166 GLY B N     1 
ATOM   5373 C CA    . GLY B 1 166 ? 39.366 -6.326  -47.874 1.00 20.52  ? 166 GLY B CA    1 
ATOM   5374 C C     . GLY B 1 166 ? 40.203 -5.580  -46.851 1.00 21.89  ? 166 GLY B C     1 
ATOM   5375 O O     . GLY B 1 166 ? 40.835 -6.212  -46.025 1.00 21.16  ? 166 GLY B O     1 
ATOM   5376 N N     . TYR B 1 167 ? 40.192 -4.250  -46.915 1.00 22.86  ? 167 TYR B N     1 
ATOM   5377 C CA    . TYR B 1 167 ? 41.258 -3.471  -46.316 1.00 23.36  ? 167 TYR B CA    1 
ATOM   5378 C C     . TYR B 1 167 ? 40.671 -2.296  -45.519 1.00 22.36  ? 167 TYR B C     1 
ATOM   5379 O O     . TYR B 1 167 ? 41.378 -1.316  -45.304 1.00 21.68  ? 167 TYR B O     1 
ATOM   5380 C CB    . TYR B 1 167 ? 42.254 -3.080  -47.407 1.00 23.84  ? 167 TYR B CB    1 
ATOM   5381 C CG    . TYR B 1 167 ? 42.804 -4.272  -48.145 1.00 27.17  ? 167 TYR B CG    1 
ATOM   5382 C CD1   . TYR B 1 167 ? 43.856 -5.021  -47.631 1.00 31.71  ? 167 TYR B CD1   1 
ATOM   5383 C CD2   . TYR B 1 167 ? 42.233 -4.691  -49.335 1.00 27.61  ? 167 TYR B CD2   1 
ATOM   5384 C CE1   . TYR B 1 167 ? 44.330 -6.149  -48.283 1.00 33.52  ? 167 TYR B CE1   1 
ATOM   5385 C CE2   . TYR B 1 167 ? 42.702 -5.808  -50.004 1.00 30.04  ? 167 TYR B CE2   1 
ATOM   5386 C CZ    . TYR B 1 167 ? 43.747 -6.545  -49.476 1.00 33.99  ? 167 TYR B CZ    1 
ATOM   5387 O OH    . TYR B 1 167 ? 44.193 -7.658  -50.153 1.00 42.60  ? 167 TYR B OH    1 
ATOM   5388 N N     . THR B 1 168 ? 39.434 -2.449  -45.010 1.00 19.17  ? 168 THR B N     1 
ATOM   5389 C CA    . THR B 1 168 ? 38.870 -1.538  -44.028 1.00 20.42  ? 168 THR B CA    1 
ATOM   5390 C C     . THR B 1 168 ? 38.632 -2.316  -42.726 1.00 20.62  ? 168 THR B C     1 
ATOM   5391 O O     . THR B 1 168 ? 38.932 -3.503  -42.640 1.00 20.43  ? 168 THR B O     1 
ATOM   5392 C CB    . THR B 1 168 ? 37.586 -0.869  -44.566 1.00 21.10  ? 168 THR B CB    1 
ATOM   5393 O OG1   . THR B 1 168 ? 36.428 -1.675  -44.301 1.00 20.15  ? 168 THR B OG1   1 
ATOM   5394 C CG2   . THR B 1 168 ? 37.666 -0.560  -46.049 1.00 20.63  ? 168 THR B CG2   1 
ATOM   5395 N N     . PRO B 1 169 ? 38.069 -1.704  -41.662 1.00 20.75  ? 169 PRO B N     1 
ATOM   5396 C CA    . PRO B 1 169 ? 37.741 -2.462  -40.456 1.00 21.34  ? 169 PRO B CA    1 
ATOM   5397 C C     . PRO B 1 169 ? 36.798 -3.632  -40.718 1.00 19.38  ? 169 PRO B C     1 
ATOM   5398 O O     . PRO B 1 169 ? 36.786 -4.578  -39.958 1.00 18.43  ? 169 PRO B O     1 
ATOM   5399 C CB    . PRO B 1 169 ? 37.151 -1.405  -39.513 1.00 20.72  ? 169 PRO B CB    1 
ATOM   5400 C CG    . PRO B 1 169 ? 37.770 -0.108  -40.014 1.00 21.41  ? 169 PRO B CG    1 
ATOM   5401 C CD    . PRO B 1 169 ? 37.789 -0.267  -41.517 1.00 20.94  ? 169 PRO B CD    1 
ATOM   5402 N N     . TYR B 1 170 ? 36.043 -3.590  -41.817 1.00 20.30  ? 170 TYR B N     1 
ATOM   5403 C CA    . TYR B 1 170 ? 35.157 -4.680  -42.182 1.00 21.46  ? 170 TYR B CA    1 
ATOM   5404 C C     . TYR B 1 170 ? 35.824 -5.617  -43.209 1.00 21.17  ? 170 TYR B C     1 
ATOM   5405 O O     . TYR B 1 170 ? 35.149 -6.175  -44.076 1.00 21.61  ? 170 TYR B O     1 
ATOM   5406 C CB    . TYR B 1 170 ? 33.847 -4.071  -42.714 1.00 23.44  ? 170 TYR B CB    1 
ATOM   5407 C CG    . TYR B 1 170 ? 32.857 -3.557  -41.693 1.00 22.94  ? 170 TYR B CG    1 
ATOM   5408 C CD1   . TYR B 1 170 ? 33.224 -2.685  -40.683 1.00 26.06  ? 170 TYR B CD1   1 
ATOM   5409 C CD2   . TYR B 1 170 ? 31.526 -3.894  -41.782 1.00 22.86  ? 170 TYR B CD2   1 
ATOM   5410 C CE1   . TYR B 1 170 ? 32.305 -2.216  -39.760 1.00 26.10  ? 170 TYR B CE1   1 
ATOM   5411 C CE2   . TYR B 1 170 ? 30.591 -3.443  -40.868 1.00 23.65  ? 170 TYR B CE2   1 
ATOM   5412 C CZ    . TYR B 1 170 ? 30.976 -2.579  -39.868 1.00 25.14  ? 170 TYR B CZ    1 
ATOM   5413 O OH    . TYR B 1 170 ? 30.035 -2.133  -38.978 1.00 26.73  ? 170 TYR B OH    1 
ATOM   5414 N N     . GLY B 1 171 ? 37.143 -5.829  -43.100 1.00 19.72  ? 171 GLY B N     1 
ATOM   5415 C CA    . GLY B 1 171 ? 37.906 -6.577  -44.088 1.00 20.95  ? 171 GLY B CA    1 
ATOM   5416 C C     . GLY B 1 171 ? 37.745 -8.105  -44.070 1.00 23.16  ? 171 GLY B C     1 
ATOM   5417 O O     . GLY B 1 171 ? 38.226 -8.774  -44.988 1.00 25.42  ? 171 GLY B O     1 
ATOM   5418 N N     . ASP B 1 172 ? 37.138 -8.681  -43.021 1.00 23.05  ? 172 ASP B N     1 
ATOM   5419 C CA    . ASP B 1 172 ? 36.843 -10.106 -42.981 1.00 22.93  ? 172 ASP B CA    1 
ATOM   5420 C C     . ASP B 1 172 ? 35.413 -10.289 -43.480 1.00 22.60  ? 172 ASP B C     1 
ATOM   5421 O O     . ASP B 1 172 ? 34.435 -10.191 -42.724 1.00 23.62  ? 172 ASP B O     1 
ATOM   5422 C CB    . ASP B 1 172 ? 37.128 -10.670 -41.583 1.00 25.52  ? 172 ASP B CB    1 
ATOM   5423 C CG    . ASP B 1 172 ? 36.881 -12.160 -41.402 1.00 25.59  ? 172 ASP B CG    1 
ATOM   5424 O OD1   . ASP B 1 172 ? 36.304 -12.780 -42.311 1.00 25.19  ? 172 ASP B OD1   1 
ATOM   5425 O OD2   . ASP B 1 172 ? 37.292 -12.682 -40.356 1.00 25.11  ? 172 ASP B OD2   1 
ATOM   5426 N N     . HIS B 1 173 ? 35.290 -10.510 -44.790 1.00 21.97  ? 173 HIS B N     1 
ATOM   5427 C CA    . HIS B 1 173 ? 33.996 -10.361 -45.443 1.00 21.10  ? 173 HIS B CA    1 
ATOM   5428 C C     . HIS B 1 173 ? 32.979 -11.361 -44.901 1.00 19.78  ? 173 HIS B C     1 
ATOM   5429 O O     . HIS B 1 173 ? 31.814 -10.996 -44.679 1.00 17.75  ? 173 HIS B O     1 
ATOM   5430 C CB    . HIS B 1 173 ? 34.131 -10.496 -46.955 1.00 23.34  ? 173 HIS B CB    1 
ATOM   5431 C CG    . HIS B 1 173 ? 34.850 -9.359  -47.575 1.00 25.39  ? 173 HIS B CG    1 
ATOM   5432 N ND1   . HIS B 1 173 ? 35.294 -9.438  -48.869 1.00 27.25  ? 173 HIS B ND1   1 
ATOM   5433 C CD2   . HIS B 1 173 ? 35.216 -8.154  -47.130 1.00 28.42  ? 173 HIS B CD2   1 
ATOM   5434 C CE1   . HIS B 1 173 ? 35.934 -8.319  -49.176 1.00 28.02  ? 173 HIS B CE1   1 
ATOM   5435 N NE2   . HIS B 1 173 ? 35.878 -7.513  -48.145 1.00 27.96  ? 173 HIS B NE2   1 
ATOM   5436 N N     . PHE B 1 174 ? 33.406 -12.611 -44.670 1.00 18.75  ? 174 PHE B N     1 
ATOM   5437 C CA    . PHE B 1 174 ? 32.442 -13.602 -44.213 1.00 19.86  ? 174 PHE B CA    1 
ATOM   5438 C C     . PHE B 1 174 ? 32.019 -13.320 -42.770 1.00 20.32  ? 174 PHE B C     1 
ATOM   5439 O O     . PHE B 1 174 ? 30.902 -13.645 -42.376 1.00 20.46  ? 174 PHE B O     1 
ATOM   5440 C CB    . PHE B 1 174 ? 32.951 -15.029 -44.349 1.00 19.94  ? 174 PHE B CB    1 
ATOM   5441 C CG    . PHE B 1 174 ? 31.834 -16.016 -44.158 1.00 21.42  ? 174 PHE B CG    1 
ATOM   5442 C CD1   . PHE B 1 174 ? 30.788 -16.060 -45.068 1.00 22.06  ? 174 PHE B CD1   1 
ATOM   5443 C CD2   . PHE B 1 174 ? 31.781 -16.829 -43.027 1.00 22.43  ? 174 PHE B CD2   1 
ATOM   5444 C CE1   . PHE B 1 174 ? 29.728 -16.920 -44.867 1.00 22.76  ? 174 PHE B CE1   1 
ATOM   5445 C CE2   . PHE B 1 174 ? 30.716 -17.688 -42.820 1.00 21.05  ? 174 PHE B CE2   1 
ATOM   5446 C CZ    . PHE B 1 174 ? 29.680 -17.706 -43.724 1.00 24.31  ? 174 PHE B CZ    1 
ATOM   5447 N N     . ALA B 1 175 ? 32.886 -12.672 -41.989 1.00 20.84  ? 175 ALA B N     1 
ATOM   5448 C CA    . ALA B 1 175 ? 32.578 -12.411 -40.594 1.00 21.62  ? 175 ALA B CA    1 
ATOM   5449 C C     . ALA B 1 175 ? 31.461 -11.371 -40.517 1.00 22.98  ? 175 ALA B C     1 
ATOM   5450 O O     . ALA B 1 175 ? 30.649 -11.411 -39.599 1.00 26.25  ? 175 ALA B O     1 
ATOM   5451 C CB    . ALA B 1 175 ? 33.817 -12.010 -39.839 1.00 21.94  ? 175 ALA B CB    1 
ATOM   5452 N N     . MET B 1 176 ? 31.350 -10.551 -41.566 1.00 22.42  ? 176 MET B N     1 
ATOM   5453 C CA    . MET B 1 176 ? 30.370 -9.497  -41.672 1.00 20.13  ? 176 MET B CA    1 
ATOM   5454 C C     . MET B 1 176 ? 29.097 -9.987  -42.355 1.00 21.26  ? 176 MET B C     1 
ATOM   5455 O O     . MET B 1 176 ? 28.136 -9.252  -42.468 1.00 23.80  ? 176 MET B O     1 
ATOM   5456 C CB    . MET B 1 176 ? 30.951 -8.334  -42.473 1.00 21.13  ? 176 MET B CB    1 
ATOM   5457 C CG    . MET B 1 176 ? 32.146 -7.672  -41.836 1.00 22.70  ? 176 MET B CG    1 
ATOM   5458 S SD    . MET B 1 176 ? 31.871 -6.993  -40.186 1.00 29.82  ? 176 MET B SD    1 
ATOM   5459 C CE    . MET B 1 176 ? 32.487 -8.338  -39.176 1.00 30.81  ? 176 MET B CE    1 
ATOM   5460 N N     . GLN B 1 177 ? 29.040 -11.251 -42.741 1.00 23.35  ? 177 GLN B N     1 
ATOM   5461 C CA    . GLN B 1 177 ? 27.841 -11.842 -43.308 1.00 22.84  ? 177 GLN B CA    1 
ATOM   5462 C C     . GLN B 1 177 ? 26.752 -11.998 -42.242 1.00 24.21  ? 177 GLN B C     1 
ATOM   5463 O O     . GLN B 1 177 ? 27.055 -12.292 -41.083 1.00 21.85  ? 177 GLN B O     1 
ATOM   5464 C CB    . GLN B 1 177 ? 28.231 -13.178 -43.945 1.00 21.77  ? 177 GLN B CB    1 
ATOM   5465 C CG    . GLN B 1 177 ? 27.057 -13.918 -44.542 1.00 21.36  ? 177 GLN B CG    1 
ATOM   5466 C CD    . GLN B 1 177 ? 26.414 -14.858 -43.560 1.00 24.17  ? 177 GLN B CD    1 
ATOM   5467 O OE1   . GLN B 1 177 ? 27.043 -15.333 -42.614 1.00 25.34  ? 177 GLN B OE1   1 
ATOM   5468 N NE2   . GLN B 1 177 ? 25.157 -15.186 -43.815 1.00 26.88  ? 177 GLN B NE2   1 
ATOM   5469 N N     . CYS B 1 178 ? 25.472 -11.803 -42.635 1.00 23.73  ? 178 CYS B N     1 
ATOM   5470 C CA    . CYS B 1 178 ? 24.367 -11.957 -41.693 1.00 23.02  ? 178 CYS B CA    1 
ATOM   5471 C C     . CYS B 1 178 ? 23.091 -12.347 -42.443 1.00 23.32  ? 178 CYS B C     1 
ATOM   5472 O O     . CYS B 1 178 ? 22.537 -11.554 -43.184 1.00 23.54  ? 178 CYS B O     1 
ATOM   5473 C CB    . CYS B 1 178 ? 24.152 -10.695 -40.862 1.00 22.88  ? 178 CYS B CB    1 
ATOM   5474 S SG    . CYS B 1 178 ? 22.948 -10.890 -39.517 1.00 24.62  ? 178 CYS B SG    1 
ATOM   5475 N N     . GLY B 1 179 ? 22.626 -13.582 -42.227 1.00 21.49  ? 179 GLY B N     1 
ATOM   5476 C CA    . GLY B 1 179 ? 21.475 -14.107 -42.926 1.00 20.72  ? 179 GLY B CA    1 
ATOM   5477 C C     . GLY B 1 179 ? 21.845 -14.561 -44.333 1.00 21.23  ? 179 GLY B C     1 
ATOM   5478 O O     . GLY B 1 179 ? 22.633 -13.893 -45.016 1.00 22.05  ? 179 GLY B O     1 
ATOM   5479 N N     . MET B 1 180 ? 21.304 -15.715 -44.743 1.00 20.20  ? 180 MET B N     1 
ATOM   5480 C CA    . MET B 1 180 ? 21.362 -16.095 -46.145 1.00 21.97  ? 180 MET B CA    1 
ATOM   5481 C C     . MET B 1 180 ? 20.186 -17.007 -46.537 1.00 20.74  ? 180 MET B C     1 
ATOM   5482 O O     . MET B 1 180 ? 19.508 -17.630 -45.713 1.00 19.08  ? 180 MET B O     1 
ATOM   5483 C CB    . MET B 1 180 ? 22.690 -16.797 -46.471 1.00 24.00  ? 180 MET B CB    1 
ATOM   5484 C CG    . MET B 1 180 ? 22.940 -18.089 -45.681 1.00 25.86  ? 180 MET B CG    1 
ATOM   5485 S SD    . MET B 1 180 ? 24.377 -19.057 -46.306 1.00 29.75  ? 180 MET B SD    1 
ATOM   5486 C CE    . MET B 1 180 ? 25.703 -17.897 -45.958 1.00 29.48  ? 180 MET B CE    1 
ATOM   5487 N N     . GLU B 1 181 ? 19.991 -17.094 -47.848 1.00 22.12  ? 181 GLU B N     1 
ATOM   5488 C CA    . GLU B 1 181 ? 19.052 -18.019 -48.467 1.00 24.48  ? 181 GLU B CA    1 
ATOM   5489 C C     . GLU B 1 181 ? 19.861 -18.979 -49.314 1.00 23.51  ? 181 GLU B C     1 
ATOM   5490 O O     . GLU B 1 181 ? 20.740 -18.570 -50.062 1.00 23.71  ? 181 GLU B O     1 
ATOM   5491 C CB    . GLU B 1 181 ? 18.046 -17.271 -49.341 1.00 25.99  ? 181 GLU B CB    1 
ATOM   5492 C CG    . GLU B 1 181 ? 17.039 -18.148 -50.058 1.00 27.15  ? 181 GLU B CG    1 
ATOM   5493 C CD    . GLU B 1 181 ? 16.123 -17.337 -50.971 1.00 28.63  ? 181 GLU B CD    1 
ATOM   5494 O OE1   . GLU B 1 181 ? 15.114 -16.812 -50.462 1.00 30.25  ? 181 GLU B OE1   1 
ATOM   5495 O OE2   . GLU B 1 181 ? 16.472 -17.147 -52.172 1.00 26.51  ? 181 GLU B OE2   1 
ATOM   5496 N N     . VAL B 1 182 ? 19.553 -20.254 -49.163 1.00 23.83  ? 182 VAL B N     1 
ATOM   5497 C CA    . VAL B 1 182 ? 20.305 -21.293 -49.817 1.00 24.64  ? 182 VAL B CA    1 
ATOM   5498 C C     . VAL B 1 182 ? 19.339 -22.196 -50.551 1.00 26.39  ? 182 VAL B C     1 
ATOM   5499 O O     . VAL B 1 182 ? 18.310 -22.598 -49.978 1.00 27.43  ? 182 VAL B O     1 
ATOM   5500 C CB    . VAL B 1 182 ? 21.085 -22.100 -48.774 1.00 27.69  ? 182 VAL B CB    1 
ATOM   5501 C CG1   . VAL B 1 182 ? 21.920 -23.201 -49.423 1.00 28.65  ? 182 VAL B CG1   1 
ATOM   5502 C CG2   . VAL B 1 182 ? 21.939 -21.176 -47.930 1.00 29.95  ? 182 VAL B CG2   1 
ATOM   5503 N N     . VAL B 1 183 ? 19.732 -22.566 -51.779 1.00 23.98  ? 183 VAL B N     1 
ATOM   5504 C CA    . VAL B 1 183 ? 19.096 -23.686 -52.448 1.00 22.72  ? 183 VAL B CA    1 
ATOM   5505 C C     . VAL B 1 183 ? 19.938 -24.918 -52.147 1.00 22.81  ? 183 VAL B C     1 
ATOM   5506 O O     . VAL B 1 183 ? 21.105 -24.984 -52.510 1.00 24.04  ? 183 VAL B O     1 
ATOM   5507 C CB    . VAL B 1 183 ? 18.931 -23.475 -53.962 1.00 24.00  ? 183 VAL B CB    1 
ATOM   5508 C CG1   . VAL B 1 183 ? 18.344 -24.716 -54.632 1.00 24.94  ? 183 VAL B CG1   1 
ATOM   5509 C CG2   . VAL B 1 183 ? 18.088 -22.248 -54.275 1.00 24.12  ? 183 VAL B CG2   1 
ATOM   5510 N N     . LEU B 1 184 ? 19.327 -25.876 -51.459 1.00 23.16  ? 184 LEU B N     1 
ATOM   5511 C CA    . LEU B 1 184 ? 19.997 -27.089 -51.050 1.00 23.63  ? 184 LEU B CA    1 
ATOM   5512 C C     . LEU B 1 184 ? 20.155 -27.967 -52.275 1.00 25.43  ? 184 LEU B C     1 
ATOM   5513 O O     . LEU B 1 184 ? 19.528 -27.707 -53.299 1.00 24.60  ? 184 LEU B O     1 
ATOM   5514 C CB    . LEU B 1 184 ? 19.167 -27.757 -49.945 1.00 23.47  ? 184 LEU B CB    1 
ATOM   5515 C CG    . LEU B 1 184 ? 19.118 -26.981 -48.631 1.00 24.54  ? 184 LEU B CG    1 
ATOM   5516 C CD1   . LEU B 1 184 ? 18.256 -27.674 -47.600 1.00 28.12  ? 184 LEU B CD1   1 
ATOM   5517 C CD2   . LEU B 1 184 ? 20.501 -26.793 -48.070 1.00 26.41  ? 184 LEU B CD2   1 
ATOM   5518 N N     . PRO B 1 185 ? 20.996 -29.022 -52.207 1.00 25.32  ? 185 PRO B N     1 
ATOM   5519 C CA    . PRO B 1 185 ? 21.282 -29.845 -53.377 1.00 26.47  ? 185 PRO B CA    1 
ATOM   5520 C C     . PRO B 1 185 ? 20.074 -30.605 -53.917 1.00 27.83  ? 185 PRO B C     1 
ATOM   5521 O O     . PRO B 1 185 ? 20.140 -31.120 -55.024 1.00 29.84  ? 185 PRO B O     1 
ATOM   5522 C CB    . PRO B 1 185 ? 22.373 -30.800 -52.876 1.00 25.93  ? 185 PRO B CB    1 
ATOM   5523 C CG    . PRO B 1 185 ? 22.955 -30.093 -51.674 1.00 25.08  ? 185 PRO B CG    1 
ATOM   5524 C CD    . PRO B 1 185 ? 21.747 -29.459 -51.030 1.00 24.22  ? 185 PRO B CD    1 
ATOM   5525 N N     . ASN B 1 186 ? 18.973 -30.665 -53.164 1.00 26.93  ? 186 ASN B N     1 
ATOM   5526 C CA    . ASN B 1 186 ? 17.763 -31.273 -53.691 1.00 26.70  ? 186 ASN B CA    1 
ATOM   5527 C C     . ASN B 1 186 ? 16.830 -30.227 -54.312 1.00 28.73  ? 186 ASN B C     1 
ATOM   5528 O O     . ASN B 1 186 ? 15.741 -30.568 -54.748 1.00 31.87  ? 186 ASN B O     1 
ATOM   5529 C CB    . ASN B 1 186 ? 17.007 -32.020 -52.595 1.00 27.67  ? 186 ASN B CB    1 
ATOM   5530 C CG    . ASN B 1 186 ? 16.492 -31.105 -51.502 1.00 29.39  ? 186 ASN B CG    1 
ATOM   5531 O OD1   . ASN B 1 186 ? 16.799 -29.916 -51.474 1.00 29.34  ? 186 ASN B OD1   1 
ATOM   5532 N ND2   . ASN B 1 186 ? 15.717 -31.645 -50.579 1.00 30.45  ? 186 ASN B ND2   1 
ATOM   5533 N N     . GLY B 1 187 ? 17.170 -28.934 -54.242 1.00 30.06  ? 187 GLY B N     1 
ATOM   5534 C CA    . GLY B 1 187 ? 16.388 -27.900 -54.905 1.00 28.03  ? 187 GLY B CA    1 
ATOM   5535 C C     . GLY B 1 187 ? 15.381 -27.204 -53.997 1.00 28.63  ? 187 GLY B C     1 
ATOM   5536 O O     . GLY B 1 187 ? 14.706 -26.257 -54.416 1.00 28.99  ? 187 GLY B O     1 
ATOM   5537 N N     . GLU B 1 188 ? 15.285 -27.668 -52.752 1.00 28.75  ? 188 GLU B N     1 
ATOM   5538 C CA    . GLU B 1 188 ? 14.466 -26.992 -51.764 1.00 29.57  ? 188 GLU B CA    1 
ATOM   5539 C C     . GLU B 1 188 ? 15.246 -25.769 -51.281 1.00 30.55  ? 188 GLU B C     1 
ATOM   5540 O O     . GLU B 1 188 ? 16.468 -25.719 -51.426 1.00 28.51  ? 188 GLU B O     1 
ATOM   5541 C CB    . GLU B 1 188 ? 14.103 -27.953 -50.631 1.00 32.85  ? 188 GLU B CB    1 
ATOM   5542 C CG    . GLU B 1 188 ? 13.198 -29.106 -51.058 1.00 37.71  ? 188 GLU B CG    1 
ATOM   5543 C CD    . GLU B 1 188 ? 11.889 -28.667 -51.690 1.00 46.85  ? 188 GLU B CD    1 
ATOM   5544 O OE1   . GLU B 1 188 ? 11.033 -28.105 -50.956 1.00 47.68  ? 188 GLU B OE1   1 
ATOM   5545 O OE2   . GLU B 1 188 ? 11.750 -28.833 -52.928 1.00 53.17  ? 188 GLU B OE2   1 
ATOM   5546 N N     . VAL B 1 189 ? 14.537 -24.780 -50.719 1.00 27.35  ? 189 VAL B N     1 
ATOM   5547 C CA    . VAL B 1 189 ? 15.166 -23.529 -50.360 1.00 27.25  ? 189 VAL B CA    1 
ATOM   5548 C C     . VAL B 1 189 ? 15.011 -23.309 -48.852 1.00 28.69  ? 189 VAL B C     1 
ATOM   5549 O O     . VAL B 1 189 ? 13.984 -23.656 -48.275 1.00 30.43  ? 189 VAL B O     1 
ATOM   5550 C CB    . VAL B 1 189 ? 14.617 -22.382 -51.237 1.00 28.47  ? 189 VAL B CB    1 
ATOM   5551 C CG1   . VAL B 1 189 ? 13.119 -22.218 -51.116 1.00 33.48  ? 189 VAL B CG1   1 
ATOM   5552 C CG2   . VAL B 1 189 ? 15.294 -21.062 -50.934 1.00 28.90  ? 189 VAL B CG2   1 
ATOM   5553 N N     . VAL B 1 190 ? 16.055 -22.762 -48.204 1.00 28.62  ? 190 VAL B N     1 
ATOM   5554 C CA    . VAL B 1 190 ? 16.025 -22.504 -46.772 1.00 29.22  ? 190 VAL B CA    1 
ATOM   5555 C C     . VAL B 1 190 ? 16.571 -21.112 -46.510 1.00 24.97  ? 190 VAL B C     1 
ATOM   5556 O O     . VAL B 1 190 ? 17.445 -20.647 -47.221 1.00 21.94  ? 190 VAL B O     1 
ATOM   5557 C CB    . VAL B 1 190 ? 16.834 -23.540 -45.959 1.00 33.83  ? 190 VAL B CB    1 
ATOM   5558 C CG1   . VAL B 1 190 ? 16.281 -24.939 -46.100 1.00 38.21  ? 190 VAL B CG1   1 
ATOM   5559 C CG2   . VAL B 1 190 ? 18.297 -23.559 -46.342 1.00 36.57  ? 190 VAL B CG2   1 
ATOM   5560 N N     . ARG B 1 191 ? 16.109 -20.491 -45.426 1.00 25.40  ? 191 ARG B N     1 
ATOM   5561 C CA    . ARG B 1 191 ? 16.769 -19.300 -44.917 1.00 25.33  ? 191 ARG B CA    1 
ATOM   5562 C C     . ARG B 1 191 ? 17.311 -19.548 -43.509 1.00 24.03  ? 191 ARG B C     1 
ATOM   5563 O O     . ARG B 1 191 ? 16.704 -20.255 -42.700 1.00 23.15  ? 191 ARG B O     1 
ATOM   5564 C CB    . ARG B 1 191 ? 15.795 -18.118 -44.928 1.00 27.74  ? 191 ARG B CB    1 
ATOM   5565 C CG    . ARG B 1 191 ? 15.272 -17.778 -46.312 1.00 27.12  ? 191 ARG B CG    1 
ATOM   5566 C CD    . ARG B 1 191 ? 14.310 -16.620 -46.306 1.00 27.15  ? 191 ARG B CD    1 
ATOM   5567 N NE    . ARG B 1 191 ? 14.066 -16.238 -47.684 1.00 29.01  ? 191 ARG B NE    1 
ATOM   5568 C CZ    . ARG B 1 191 ? 13.522 -15.090 -48.057 1.00 29.76  ? 191 ARG B CZ    1 
ATOM   5569 N NH1   . ARG B 1 191 ? 13.054 -14.249 -47.149 1.00 27.53  ? 191 ARG B NH1   1 
ATOM   5570 N NH2   . ARG B 1 191 ? 13.468 -14.782 -49.338 1.00 31.20  ? 191 ARG B NH2   1 
ATOM   5571 N N     . THR B 1 192 ? 18.472 -18.934 -43.241 1.00 25.18  ? 192 THR B N     1 
ATOM   5572 C CA    . THR B 1 192 ? 19.168 -19.064 -41.968 1.00 24.69  ? 192 THR B CA    1 
ATOM   5573 C C     . THR B 1 192 ? 18.821 -17.911 -41.027 1.00 23.92  ? 192 THR B C     1 
ATOM   5574 O O     . THR B 1 192 ? 18.332 -16.872 -41.445 1.00 23.24  ? 192 THR B O     1 
ATOM   5575 C CB    . THR B 1 192 ? 20.687 -19.129 -42.170 1.00 21.96  ? 192 THR B CB    1 
ATOM   5576 O OG1   . THR B 1 192 ? 21.110 -17.866 -42.679 1.00 23.30  ? 192 THR B OG1   1 
ATOM   5577 C CG2   . THR B 1 192 ? 21.096 -20.235 -43.113 1.00 22.45  ? 192 THR B CG2   1 
ATOM   5578 N N     . GLY B 1 193 ? 19.117 -18.139 -39.745 1.00 25.69  ? 193 GLY B N     1 
ATOM   5579 C CA    . GLY B 1 193 ? 18.982 -17.145 -38.699 1.00 26.61  ? 193 GLY B CA    1 
ATOM   5580 C C     . GLY B 1 193 ? 17.532 -16.714 -38.531 1.00 25.41  ? 193 GLY B C     1 
ATOM   5581 O O     . GLY B 1 193 ? 16.620 -17.539 -38.553 1.00 23.41  ? 193 GLY B O     1 
ATOM   5582 N N     . MET B 1 194 ? 17.340 -15.394 -38.466 1.00 25.91  ? 194 MET B N     1 
ATOM   5583 C CA    . MET B 1 194 ? 16.028 -14.813 -38.247 1.00 23.70  ? 194 MET B CA    1 
ATOM   5584 C C     . MET B 1 194 ? 15.210 -14.893 -39.535 1.00 24.28  ? 194 MET B C     1 
ATOM   5585 O O     . MET B 1 194 ? 13.991 -14.905 -39.491 1.00 24.33  ? 194 MET B O     1 
ATOM   5586 C CB    . MET B 1 194 ? 16.173 -13.373 -37.762 1.00 23.91  ? 194 MET B CB    1 
ATOM   5587 C CG    . MET B 1 194 ? 16.980 -13.278 -36.474 1.00 24.40  ? 194 MET B CG    1 
ATOM   5588 S SD    . MET B 1 194 ? 16.300 -14.282 -35.118 1.00 28.33  ? 194 MET B SD    1 
ATOM   5589 C CE    . MET B 1 194 ? 14.572 -13.817 -35.167 1.00 26.60  ? 194 MET B CE    1 
ATOM   5590 N N     . GLY B 1 195 ? 15.869 -15.120 -40.669 1.00 24.89  ? 195 GLY B N     1 
ATOM   5591 C CA    . GLY B 1 195 ? 15.155 -15.333 -41.919 1.00 26.76  ? 195 GLY B CA    1 
ATOM   5592 C C     . GLY B 1 195 ? 14.202 -16.524 -41.863 1.00 27.78  ? 195 GLY B C     1 
ATOM   5593 O O     . GLY B 1 195 ? 13.249 -16.595 -42.640 1.00 28.46  ? 195 GLY B O     1 
ATOM   5594 N N     . ALA B 1 196 ? 14.511 -17.482 -40.980 1.00 28.22  ? 196 ALA B N     1 
ATOM   5595 C CA    . ALA B 1 196 ? 13.675 -18.653 -40.788 1.00 29.65  ? 196 ALA B CA    1 
ATOM   5596 C C     . ALA B 1 196 ? 12.343 -18.289 -40.127 1.00 30.72  ? 196 ALA B C     1 
ATOM   5597 O O     . ALA B 1 196 ? 11.412 -19.094 -40.121 1.00 31.50  ? 196 ALA B O     1 
ATOM   5598 C CB    . ALA B 1 196 ? 14.409 -19.658 -39.949 1.00 29.71  ? 196 ALA B CB    1 
ATOM   5599 N N     . MET B 1 197 ? 12.244 -17.095 -39.541 1.00 29.97  ? 197 MET B N     1 
ATOM   5600 C CA    . MET B 1 197 ? 10.984 -16.708 -38.926 1.00 31.74  ? 197 MET B CA    1 
ATOM   5601 C C     . MET B 1 197 ? 10.159 -15.845 -39.871 1.00 27.59  ? 197 MET B C     1 
ATOM   5602 O O     . MET B 1 197 ? 10.634 -14.788 -40.289 1.00 28.18  ? 197 MET B O     1 
ATOM   5603 C CB    . MET B 1 197 ? 11.169 -15.902 -37.646 1.00 34.57  ? 197 MET B CB    1 
ATOM   5604 C CG    . MET B 1 197 ? 9.919  -15.152 -37.339 1.00 37.79  ? 197 MET B CG    1 
ATOM   5605 S SD    . MET B 1 197 ? 9.804  -14.657 -35.672 1.00 46.52  ? 197 MET B SD    1 
ATOM   5606 C CE    . MET B 1 197 ? 9.452  -16.208 -34.844 1.00 42.93  ? 197 MET B CE    1 
ATOM   5607 N N     . PRO B 1 198 ? 8.875  -16.209 -40.136 1.00 27.41  ? 198 PRO B N     1 
ATOM   5608 C CA    . PRO B 1 198 ? 7.996  -15.409 -40.995 1.00 27.22  ? 198 PRO B CA    1 
ATOM   5609 C C     . PRO B 1 198 ? 7.701  -14.045 -40.392 1.00 27.42  ? 198 PRO B C     1 
ATOM   5610 O O     . PRO B 1 198 ? 7.377  -13.943 -39.213 1.00 32.72  ? 198 PRO B O     1 
ATOM   5611 C CB    . PRO B 1 198 ? 6.701  -16.231 -41.093 1.00 27.30  ? 198 PRO B CB    1 
ATOM   5612 C CG    . PRO B 1 198 ? 7.114  -17.643 -40.687 1.00 27.42  ? 198 PRO B CG    1 
ATOM   5613 C CD    . PRO B 1 198 ? 8.188  -17.416 -39.644 1.00 26.82  ? 198 PRO B CD    1 
ATOM   5614 N N     . GLY B 1 199 ? 7.861  -13.001 -41.201 1.00 26.29  ? 199 GLY B N     1 
ATOM   5615 C CA    . GLY B 1 199 ? 7.489  -11.656 -40.801 1.00 26.49  ? 199 GLY B CA    1 
ATOM   5616 C C     . GLY B 1 199 ? 8.574  -10.979 -39.970 1.00 29.01  ? 199 GLY B C     1 
ATOM   5617 O O     . GLY B 1 199 ? 8.338  -9.922  -39.384 1.00 29.88  ? 199 GLY B O     1 
ATOM   5618 N N     . ASN B 1 200 ? 9.757  -11.601 -39.903 1.00 28.17  ? 200 ASN B N     1 
ATOM   5619 C CA    . ASN B 1 200 ? 10.865 -11.032 -39.152 1.00 28.25  ? 200 ASN B CA    1 
ATOM   5620 C C     . ASN B 1 200 ? 11.306 -9.748  -39.827 1.00 27.93  ? 200 ASN B C     1 
ATOM   5621 O O     . ASN B 1 200 ? 11.194 -9.614  -41.041 1.00 29.21  ? 200 ASN B O     1 
ATOM   5622 C CB    . ASN B 1 200 ? 12.074 -11.968 -39.096 1.00 26.47  ? 200 ASN B CB    1 
ATOM   5623 C CG    . ASN B 1 200 ? 12.817 -11.980 -40.410 1.00 25.64  ? 200 ASN B CG    1 
ATOM   5624 O OD1   . ASN B 1 200 ? 13.647 -11.105 -40.666 1.00 24.62  ? 200 ASN B OD1   1 
ATOM   5625 N ND2   . ASN B 1 200 ? 12.483 -12.940 -41.262 1.00 24.87  ? 200 ASN B ND2   1 
ATOM   5626 N N     . ASN B 1 201 ? 11.872 -8.836  -39.048 1.00 29.58  ? 201 ASN B N     1 
ATOM   5627 C CA    . ASN B 1 201 ? 12.605 -7.729  -39.645 1.00 34.27  ? 201 ASN B CA    1 
ATOM   5628 C C     . ASN B 1 201 ? 14.019 -7.721  -39.058 1.00 32.36  ? 201 ASN B C     1 
ATOM   5629 O O     . ASN B 1 201 ? 14.606 -6.657  -38.906 1.00 39.06  ? 201 ASN B O     1 
ATOM   5630 C CB    . ASN B 1 201 ? 11.842 -6.396  -39.505 1.00 39.69  ? 201 ASN B CB    1 
ATOM   5631 C CG    . ASN B 1 201 ? 10.592 -6.272  -40.379 1.00 42.92  ? 201 ASN B CG    1 
ATOM   5632 O OD1   . ASN B 1 201 ? 10.647 -5.837  -41.534 1.00 37.45  ? 201 ASN B OD1   1 
ATOM   5633 N ND2   . ASN B 1 201 ? 9.434  -6.606  -39.824 1.00 41.80  ? 201 ASN B ND2   1 
ATOM   5634 N N     . THR B 1 202 ? 14.578 -8.913  -38.779 1.00 29.26  ? 202 THR B N     1 
ATOM   5635 C CA    . THR B 1 202 ? 15.879 -9.035  -38.126 1.00 28.81  ? 202 THR B CA    1 
ATOM   5636 C C     . THR B 1 202 ? 16.905 -9.893  -38.886 1.00 25.76  ? 202 THR B C     1 
ATOM   5637 O O     . THR B 1 202 ? 18.018 -10.039 -38.408 1.00 26.83  ? 202 THR B O     1 
ATOM   5638 C CB    . THR B 1 202 ? 15.685 -9.570  -36.702 1.00 29.96  ? 202 THR B CB    1 
ATOM   5639 O OG1   . THR B 1 202 ? 14.742 -10.642 -36.750 1.00 25.55  ? 202 THR B OG1   1 
ATOM   5640 C CG2   . THR B 1 202 ? 15.213 -8.484  -35.755 1.00 30.93  ? 202 THR B CG2   1 
ATOM   5641 N N     . TRP B 1 203 ? 16.570 -10.426 -40.068 1.00 25.17  ? 203 TRP B N     1 
ATOM   5642 C CA    . TRP B 1 203 ? 17.453 -11.300 -40.840 1.00 24.31  ? 203 TRP B CA    1 
ATOM   5643 C C     . TRP B 1 203 ? 18.877 -10.749 -40.901 1.00 22.84  ? 203 TRP B C     1 
ATOM   5644 O O     . TRP B 1 203 ? 19.839 -11.494 -40.740 1.00 27.65  ? 203 TRP B O     1 
ATOM   5645 C CB    . TRP B 1 203 ? 16.917 -11.485 -42.268 1.00 24.97  ? 203 TRP B CB    1 
ATOM   5646 C CG    . TRP B 1 203 ? 17.375 -12.714 -42.995 1.00 25.63  ? 203 TRP B CG    1 
ATOM   5647 C CD1   . TRP B 1 203 ? 18.029 -13.801 -42.479 1.00 25.62  ? 203 TRP B CD1   1 
ATOM   5648 C CD2   . TRP B 1 203 ? 17.109 -13.025 -44.375 1.00 23.61  ? 203 TRP B CD2   1 
ATOM   5649 N NE1   . TRP B 1 203 ? 18.215 -14.752 -43.447 1.00 25.82  ? 203 TRP B NE1   1 
ATOM   5650 C CE2   . TRP B 1 203 ? 17.661 -14.302 -44.624 1.00 24.46  ? 203 TRP B CE2   1 
ATOM   5651 C CE3   . TRP B 1 203 ? 16.519 -12.324 -45.435 1.00 23.41  ? 203 TRP B CE3   1 
ATOM   5652 C CZ2   . TRP B 1 203 ? 17.604 -14.902 -45.881 1.00 22.08  ? 203 TRP B CZ2   1 
ATOM   5653 C CZ3   . TRP B 1 203 ? 16.467 -12.912 -46.679 1.00 23.64  ? 203 TRP B CZ3   1 
ATOM   5654 C CH2   . TRP B 1 203 ? 17.006 -14.187 -46.892 1.00 23.69  ? 203 TRP B CH2   1 
ATOM   5655 N N     . GLN B 1 204 ? 19.014 -9.444  -41.151 1.00 22.47  ? 204 GLN B N     1 
ATOM   5656 C CA    . GLN B 1 204 ? 20.322 -8.826  -41.328 1.00 21.98  ? 204 GLN B CA    1 
ATOM   5657 C C     . GLN B 1 204 ? 20.803 -8.150  -40.043 1.00 21.72  ? 204 GLN B C     1 
ATOM   5658 O O     . GLN B 1 204 ? 21.784 -7.429  -40.081 1.00 21.95  ? 204 GLN B O     1 
ATOM   5659 C CB    . GLN B 1 204 ? 20.324 -7.828  -42.492 1.00 21.20  ? 204 GLN B CB    1 
ATOM   5660 C CG    . GLN B 1 204 ? 20.659 -8.459  -43.839 1.00 22.36  ? 204 GLN B CG    1 
ATOM   5661 C CD    . GLN B 1 204 ? 19.619 -9.483  -44.224 1.00 24.77  ? 204 GLN B CD    1 
ATOM   5662 O OE1   . GLN B 1 204 ? 18.480 -9.153  -44.555 1.00 24.44  ? 204 GLN B OE1   1 
ATOM   5663 N NE2   . GLN B 1 204 ? 19.983 -10.749 -44.108 1.00 26.52  ? 204 GLN B NE2   1 
ATOM   5664 N N     . LEU B 1 205 ? 20.191 -8.445  -38.897 1.00 22.69  ? 205 LEU B N     1 
ATOM   5665 C CA    . LEU B 1 205 ? 20.554 -7.766  -37.665 1.00 24.99  ? 205 LEU B CA    1 
ATOM   5666 C C     . LEU B 1 205 ? 21.178 -8.733  -36.663 1.00 25.55  ? 205 LEU B C     1 
ATOM   5667 O O     . LEU B 1 205 ? 21.895 -8.296  -35.770 1.00 24.76  ? 205 LEU B O     1 
ATOM   5668 C CB    . LEU B 1 205 ? 19.298 -7.122  -37.063 1.00 24.70  ? 205 LEU B CB    1 
ATOM   5669 C CG    . LEU B 1 205 ? 18.627 -6.040  -37.910 1.00 23.34  ? 205 LEU B CG    1 
ATOM   5670 C CD1   . LEU B 1 205 ? 17.520 -5.399  -37.114 1.00 22.91  ? 205 LEU B CD1   1 
ATOM   5671 C CD2   . LEU B 1 205 ? 19.622 -4.984  -38.365 1.00 23.18  ? 205 LEU B CD2   1 
ATOM   5672 N N     . PHE B 1 206 ? 20.873 -10.028 -36.777 1.00 26.79  ? 206 PHE B N     1 
ATOM   5673 C CA    . PHE B 1 206 ? 21.270 -10.994 -35.752 1.00 27.18  ? 206 PHE B CA    1 
ATOM   5674 C C     . PHE B 1 206 ? 21.649 -12.317 -36.405 1.00 26.19  ? 206 PHE B C     1 
ATOM   5675 O O     . PHE B 1 206 ? 20.805 -12.967 -37.023 1.00 25.80  ? 206 PHE B O     1 
ATOM   5676 C CB    . PHE B 1 206 ? 20.130 -11.256 -34.767 1.00 25.43  ? 206 PHE B CB    1 
ATOM   5677 C CG    . PHE B 1 206 ? 20.502 -12.181 -33.645 1.00 25.23  ? 206 PHE B CG    1 
ATOM   5678 C CD1   . PHE B 1 206 ? 21.556 -11.872 -32.799 1.00 29.33  ? 206 PHE B CD1   1 
ATOM   5679 C CD2   . PHE B 1 206 ? 19.780 -13.330 -33.404 1.00 24.49  ? 206 PHE B CD2   1 
ATOM   5680 C CE1   . PHE B 1 206 ? 21.902 -12.716 -31.750 1.00 27.89  ? 206 PHE B CE1   1 
ATOM   5681 C CE2   . PHE B 1 206 ? 20.129 -14.179 -32.370 1.00 25.83  ? 206 PHE B CE2   1 
ATOM   5682 C CZ    . PHE B 1 206 ? 21.194 -13.873 -31.546 1.00 27.26  ? 206 PHE B CZ    1 
ATOM   5683 N N     . LYS B 1 207 ? 22.916 -12.700 -36.253 1.00 26.97  ? 207 LYS B N     1 
ATOM   5684 C CA    . LYS B 1 207 ? 23.509 -13.779 -37.025 1.00 26.71  ? 207 LYS B CA    1 
ATOM   5685 C C     . LYS B 1 207 ? 22.842 -15.125 -36.745 1.00 26.39  ? 207 LYS B C     1 
ATOM   5686 O O     . LYS B 1 207 ? 22.479 -15.829 -37.687 1.00 26.74  ? 207 LYS B O     1 
ATOM   5687 C CB    . LYS B 1 207 ? 25.004 -13.865 -36.728 1.00 28.45  ? 207 LYS B CB    1 
ATOM   5688 C CG    . LYS B 1 207 ? 25.864 -12.844 -37.450 1.00 29.81  ? 207 LYS B CG    1 
ATOM   5689 C CD    . LYS B 1 207 ? 27.280 -12.842 -36.928 1.00 35.06  ? 207 LYS B CD    1 
ATOM   5690 C CE    . LYS B 1 207 ? 28.303 -12.271 -37.890 1.00 36.88  ? 207 LYS B CE    1 
ATOM   5691 N NZ    . LYS B 1 207 ? 28.682 -13.263 -38.929 1.00 36.84  ? 207 LYS B NZ    1 
ATOM   5692 N N     . TYR B 1 208 ? 22.641 -15.461 -35.468 1.00 24.99  ? 208 TYR B N     1 
ATOM   5693 C CA    . TYR B 1 208 ? 22.500 -16.855 -35.084 1.00 24.80  ? 208 TYR B CA    1 
ATOM   5694 C C     . TYR B 1 208 ? 21.112 -17.376 -35.406 1.00 26.39  ? 208 TYR B C     1 
ATOM   5695 O O     . TYR B 1 208 ? 20.959 -18.530 -35.812 1.00 29.09  ? 208 TYR B O     1 
ATOM   5696 C CB    . TYR B 1 208 ? 22.765 -17.062 -33.591 1.00 26.65  ? 208 TYR B CB    1 
ATOM   5697 C CG    . TYR B 1 208 ? 24.148 -16.671 -33.120 1.00 28.98  ? 208 TYR B CG    1 
ATOM   5698 C CD1   . TYR B 1 208 ? 25.282 -17.067 -33.810 1.00 28.10  ? 208 TYR B CD1   1 
ATOM   5699 C CD2   . TYR B 1 208 ? 24.334 -15.946 -31.955 1.00 29.15  ? 208 TYR B CD2   1 
ATOM   5700 C CE1   . TYR B 1 208 ? 26.550 -16.721 -33.380 1.00 29.78  ? 208 TYR B CE1   1 
ATOM   5701 C CE2   . TYR B 1 208 ? 25.599 -15.620 -31.489 1.00 28.25  ? 208 TYR B CE2   1 
ATOM   5702 C CZ    . TYR B 1 208 ? 26.712 -15.981 -32.220 1.00 28.31  ? 208 TYR B CZ    1 
ATOM   5703 O OH    . TYR B 1 208 ? 27.974 -15.666 -31.791 1.00 25.64  ? 208 TYR B OH    1 
ATOM   5704 N N     . GLY B 1 209 ? 20.110 -16.529 -35.175 1.00 28.60  ? 209 GLY B N     1 
ATOM   5705 C CA    . GLY B 1 209 ? 18.750 -17.003 -34.967 1.00 27.13  ? 209 GLY B CA    1 
ATOM   5706 C C     . GLY B 1 209 ? 18.707 -17.967 -33.789 1.00 25.25  ? 209 GLY B C     1 
ATOM   5707 O O     . GLY B 1 209 ? 19.270 -17.675 -32.745 1.00 26.36  ? 209 GLY B O     1 
ATOM   5708 N N     . TYR B 1 210 ? 18.145 -19.154 -34.008 1.00 25.08  ? 210 TYR B N     1 
ATOM   5709 C CA    . TYR B 1 210 ? 18.005 -20.141 -32.956 1.00 25.14  ? 210 TYR B CA    1 
ATOM   5710 C C     . TYR B 1 210 ? 18.491 -21.496 -33.442 1.00 26.01  ? 210 TYR B C     1 
ATOM   5711 O O     . TYR B 1 210 ? 18.278 -21.838 -34.609 1.00 28.92  ? 210 TYR B O     1 
ATOM   5712 C CB    . TYR B 1 210 ? 16.536 -20.231 -32.554 1.00 25.52  ? 210 TYR B CB    1 
ATOM   5713 C CG    . TYR B 1 210 ? 16.195 -21.321 -31.574 1.00 25.88  ? 210 TYR B CG    1 
ATOM   5714 C CD1   . TYR B 1 210 ? 16.706 -21.321 -30.284 1.00 26.56  ? 210 TYR B CD1   1 
ATOM   5715 C CD2   . TYR B 1 210 ? 15.328 -22.339 -31.940 1.00 24.10  ? 210 TYR B CD2   1 
ATOM   5716 C CE1   . TYR B 1 210 ? 16.350 -22.312 -29.382 1.00 28.32  ? 210 TYR B CE1   1 
ATOM   5717 C CE2   . TYR B 1 210 ? 14.977 -23.338 -31.061 1.00 24.29  ? 210 TYR B CE2   1 
ATOM   5718 C CZ    . TYR B 1 210 ? 15.459 -23.304 -29.770 1.00 25.95  ? 210 TYR B CZ    1 
ATOM   5719 O OH    . TYR B 1 210 ? 15.039 -24.288 -28.927 1.00 24.84  ? 210 TYR B OH    1 
ATOM   5720 N N     . GLY B 1 211 ? 19.131 -22.259 -32.539 1.00 24.98  ? 211 GLY B N     1 
ATOM   5721 C CA    . GLY B 1 211 ? 19.632 -23.592 -32.866 1.00 24.32  ? 211 GLY B CA    1 
ATOM   5722 C C     . GLY B 1 211 ? 21.022 -23.556 -33.502 1.00 24.58  ? 211 GLY B C     1 
ATOM   5723 O O     . GLY B 1 211 ? 21.734 -22.562 -33.351 1.00 23.03  ? 211 GLY B O     1 
ATOM   5724 N N     . PRO B 1 212 ? 21.434 -24.627 -34.234 1.00 24.92  ? 212 PRO B N     1 
ATOM   5725 C CA    . PRO B 1 212 ? 22.746 -24.694 -34.873 1.00 24.55  ? 212 PRO B CA    1 
ATOM   5726 C C     . PRO B 1 212 ? 23.005 -23.542 -35.830 1.00 22.88  ? 212 PRO B C     1 
ATOM   5727 O O     . PRO B 1 212 ? 22.143 -23.184 -36.642 1.00 22.15  ? 212 PRO B O     1 
ATOM   5728 C CB    . PRO B 1 212 ? 22.705 -26.011 -35.659 1.00 26.77  ? 212 PRO B CB    1 
ATOM   5729 C CG    . PRO B 1 212 ? 21.725 -26.851 -34.879 1.00 27.80  ? 212 PRO B CG    1 
ATOM   5730 C CD    . PRO B 1 212 ? 20.657 -25.856 -34.478 1.00 27.51  ? 212 PRO B CD    1 
ATOM   5731 N N     . TYR B 1 213 ? 24.182 -22.943 -35.682 1.00 21.22  ? 213 TYR B N     1 
ATOM   5732 C CA    . TYR B 1 213 ? 24.592 -21.843 -36.538 1.00 23.25  ? 213 TYR B CA    1 
ATOM   5733 C C     . TYR B 1 213 ? 25.227 -22.457 -37.779 1.00 25.01  ? 213 TYR B C     1 
ATOM   5734 O O     . TYR B 1 213 ? 26.293 -23.049 -37.666 1.00 27.00  ? 213 TYR B O     1 
ATOM   5735 C CB    . TYR B 1 213 ? 25.539 -20.921 -35.769 1.00 23.48  ? 213 TYR B CB    1 
ATOM   5736 C CG    . TYR B 1 213 ? 26.029 -19.702 -36.510 1.00 24.45  ? 213 TYR B CG    1 
ATOM   5737 C CD1   . TYR B 1 213 ? 25.233 -19.016 -37.400 1.00 25.43  ? 213 TYR B CD1   1 
ATOM   5738 C CD2   . TYR B 1 213 ? 27.274 -19.171 -36.238 1.00 27.78  ? 213 TYR B CD2   1 
ATOM   5739 C CE1   . TYR B 1 213 ? 25.694 -17.901 -38.072 1.00 28.30  ? 213 TYR B CE1   1 
ATOM   5740 C CE2   . TYR B 1 213 ? 27.740 -18.032 -36.868 1.00 28.10  ? 213 TYR B CE2   1 
ATOM   5741 C CZ    . TYR B 1 213 ? 26.955 -17.402 -37.809 1.00 29.61  ? 213 TYR B CZ    1 
ATOM   5742 O OH    . TYR B 1 213 ? 27.423 -16.267 -38.432 1.00 32.99  ? 213 TYR B OH    1 
ATOM   5743 N N     . VAL B 1 214 ? 24.528 -22.387 -38.928 1.00 25.36  ? 214 VAL B N     1 
ATOM   5744 C CA    . VAL B 1 214 ? 24.868 -23.204 -40.090 1.00 23.79  ? 214 VAL B CA    1 
ATOM   5745 C C     . VAL B 1 214 ? 25.364 -22.380 -41.285 1.00 26.75  ? 214 VAL B C     1 
ATOM   5746 O O     . VAL B 1 214 ? 25.821 -22.985 -42.245 1.00 27.57  ? 214 VAL B O     1 
ATOM   5747 C CB    . VAL B 1 214 ? 23.683 -24.089 -40.510 1.00 21.76  ? 214 VAL B CB    1 
ATOM   5748 C CG1   . VAL B 1 214 ? 23.416 -25.134 -39.451 1.00 19.98  ? 214 VAL B CG1   1 
ATOM   5749 C CG2   . VAL B 1 214 ? 22.426 -23.278 -40.832 1.00 21.56  ? 214 VAL B CG2   1 
ATOM   5750 N N     . ASP B 1 215 ? 25.308 -21.033 -41.229 1.00 27.08  ? 215 ASP B N     1 
ATOM   5751 C CA    . ASP B 1 215 ? 25.694 -20.180 -42.348 1.00 28.22  ? 215 ASP B CA    1 
ATOM   5752 C C     . ASP B 1 215 ? 27.089 -20.573 -42.858 1.00 27.83  ? 215 ASP B C     1 
ATOM   5753 O O     . ASP B 1 215 ? 27.312 -20.718 -44.070 1.00 24.01  ? 215 ASP B O     1 
ATOM   5754 C CB    . ASP B 1 215 ? 25.669 -18.694 -41.956 1.00 28.10  ? 215 ASP B CB    1 
ATOM   5755 C CG    . ASP B 1 215 ? 24.285 -18.138 -41.654 1.00 30.70  ? 215 ASP B CG    1 
ATOM   5756 O OD1   . ASP B 1 215 ? 23.652 -18.618 -40.684 1.00 27.60  ? 215 ASP B OD1   1 
ATOM   5757 O OD2   . ASP B 1 215 ? 23.842 -17.230 -42.401 1.00 33.33  ? 215 ASP B OD2   1 
ATOM   5758 N N     . GLY B 1 216 ? 28.013 -20.733 -41.900 1.00 25.75  ? 216 GLY B N     1 
ATOM   5759 C CA    . GLY B 1 216 ? 29.391 -21.140 -42.147 1.00 25.23  ? 216 GLY B CA    1 
ATOM   5760 C C     . GLY B 1 216 ? 29.554 -22.382 -43.033 1.00 22.98  ? 216 GLY B C     1 
ATOM   5761 O O     . GLY B 1 216 ? 30.489 -22.439 -43.828 1.00 23.60  ? 216 GLY B O     1 
ATOM   5762 N N     . ILE B 1 217 ? 28.651 -23.362 -42.948 1.00 20.71  ? 217 ILE B N     1 
ATOM   5763 C CA    . ILE B 1 217 ? 28.824 -24.572 -43.735 1.00 21.30  ? 217 ILE B CA    1 
ATOM   5764 C C     . ILE B 1 217 ? 28.613 -24.319 -45.236 1.00 21.86  ? 217 ILE B C     1 
ATOM   5765 O O     . ILE B 1 217 ? 28.950 -25.194 -46.034 1.00 22.13  ? 217 ILE B O     1 
ATOM   5766 C CB    . ILE B 1 217 ? 27.936 -25.736 -43.243 1.00 23.08  ? 217 ILE B CB    1 
ATOM   5767 C CG1   . ILE B 1 217 ? 26.514 -25.687 -43.804 1.00 23.47  ? 217 ILE B CG1   1 
ATOM   5768 C CG2   . ILE B 1 217 ? 27.917 -25.869 -41.726 1.00 23.51  ? 217 ILE B CG2   1 
ATOM   5769 C CD1   . ILE B 1 217 ? 25.623 -26.777 -43.218 1.00 24.03  ? 217 ILE B CD1   1 
ATOM   5770 N N     . PHE B 1 218 ? 28.079 -23.157 -45.645 1.00 19.43  ? 218 PHE B N     1 
ATOM   5771 C CA    . PHE B 1 218 ? 27.857 -22.905 -47.059 1.00 20.28  ? 218 PHE B CA    1 
ATOM   5772 C C     . PHE B 1 218 ? 28.942 -21.980 -47.612 1.00 22.75  ? 218 PHE B C     1 
ATOM   5773 O O     . PHE B 1 218 ? 28.890 -21.590 -48.775 1.00 24.11  ? 218 PHE B O     1 
ATOM   5774 C CB    . PHE B 1 218 ? 26.447 -22.360 -47.309 1.00 19.85  ? 218 PHE B CB    1 
ATOM   5775 C CG    . PHE B 1 218 ? 25.346 -23.296 -46.884 1.00 20.07  ? 218 PHE B CG    1 
ATOM   5776 C CD1   . PHE B 1 218 ? 25.052 -24.428 -47.616 1.00 20.74  ? 218 PHE B CD1   1 
ATOM   5777 C CD2   . PHE B 1 218 ? 24.637 -23.078 -45.721 1.00 20.50  ? 218 PHE B CD2   1 
ATOM   5778 C CE1   . PHE B 1 218 ? 24.063 -25.296 -47.204 1.00 21.24  ? 218 PHE B CE1   1 
ATOM   5779 C CE2   . PHE B 1 218 ? 23.659 -23.959 -45.299 1.00 20.90  ? 218 PHE B CE2   1 
ATOM   5780 C CZ    . PHE B 1 218 ? 23.395 -25.088 -46.027 1.00 21.87  ? 218 PHE B CZ    1 
ATOM   5781 N N     . SER B 1 219 ? 29.945 -21.662 -46.785 1.00 22.70  ? 219 SER B N     1 
ATOM   5782 C CA    . SER B 1 219 ? 31.157 -21.003 -47.247 1.00 21.67  ? 219 SER B CA    1 
ATOM   5783 C C     . SER B 1 219 ? 32.231 -22.051 -47.552 1.00 21.80  ? 219 SER B C     1 
ATOM   5784 O O     . SER B 1 219 ? 32.324 -23.064 -46.846 1.00 23.08  ? 219 SER B O     1 
ATOM   5785 C CB    . SER B 1 219 ? 31.627 -20.033 -46.191 1.00 22.39  ? 219 SER B CB    1 
ATOM   5786 O OG    . SER B 1 219 ? 31.933 -20.705 -44.972 1.00 21.01  ? 219 SER B OG    1 
ATOM   5787 N N     . GLN B 1 220 ? 33.079 -21.741 -48.547 1.00 21.31  ? 220 GLN B N     1 
ATOM   5788 C CA    . GLN B 1 220 ? 34.094 -22.617 -49.135 1.00 19.91  ? 220 GLN B CA    1 
ATOM   5789 C C     . GLN B 1 220 ? 33.567 -24.034 -49.175 1.00 19.60  ? 220 GLN B C     1 
ATOM   5790 O O     . GLN B 1 220 ? 34.223 -24.942 -48.664 1.00 17.97  ? 220 GLN B O     1 
ATOM   5791 C CB    . GLN B 1 220 ? 35.435 -22.570 -48.388 1.00 21.61  ? 220 GLN B CB    1 
ATOM   5792 C CG    . GLN B 1 220 ? 36.264 -21.310 -48.645 1.00 21.47  ? 220 GLN B CG    1 
ATOM   5793 C CD    . GLN B 1 220 ? 37.673 -21.379 -48.090 1.00 23.70  ? 220 GLN B CD    1 
ATOM   5794 O OE1   . GLN B 1 220 ? 38.070 -22.335 -47.415 1.00 27.64  ? 220 GLN B OE1   1 
ATOM   5795 N NE2   . GLN B 1 220 ? 38.465 -20.359 -48.396 1.00 22.01  ? 220 GLN B NE2   1 
ATOM   5796 N N     . SER B 1 221 ? 32.385 -24.190 -49.800 1.00 20.63  ? 221 SER B N     1 
ATOM   5797 C CA    . SER B 1 221 ? 31.571 -25.384 -49.635 1.00 22.16  ? 221 SER B CA    1 
ATOM   5798 C C     . SER B 1 221 ? 30.908 -25.791 -50.950 1.00 21.95  ? 221 SER B C     1 
ATOM   5799 O O     . SER B 1 221 ? 30.772 -24.981 -51.855 1.00 23.77  ? 221 SER B O     1 
ATOM   5800 C CB    . SER B 1 221 ? 30.527 -25.106 -48.574 1.00 24.25  ? 221 SER B CB    1 
ATOM   5801 O OG    . SER B 1 221 ? 29.671 -26.208 -48.363 1.00 25.04  ? 221 SER B OG    1 
ATOM   5802 N N     . ASN B 1 222 ? 30.400 -27.030 -50.981 1.00 22.50  ? 222 ASN B N     1 
ATOM   5803 C CA    . ASN B 1 222 ? 29.538 -27.547 -52.040 1.00 22.85  ? 222 ASN B CA    1 
ATOM   5804 C C     . ASN B 1 222 ? 28.326 -28.228 -51.403 1.00 22.82  ? 222 ASN B C     1 
ATOM   5805 O O     . ASN B 1 222 ? 27.855 -29.276 -51.849 1.00 23.92  ? 222 ASN B O     1 
ATOM   5806 C CB    . ASN B 1 222 ? 30.298 -28.518 -52.957 1.00 23.56  ? 222 ASN B CB    1 
ATOM   5807 C CG    . ASN B 1 222 ? 31.010 -29.627 -52.206 1.00 22.48  ? 222 ASN B CG    1 
ATOM   5808 O OD1   . ASN B 1 222 ? 30.662 -29.925 -51.070 1.00 22.67  ? 222 ASN B OD1   1 
ATOM   5809 N ND2   . ASN B 1 222 ? 31.970 -30.281 -52.846 1.00 24.45  ? 222 ASN B ND2   1 
ATOM   5810 N N     . PHE B 1 223 ? 27.825 -27.617 -50.334 1.00 22.34  ? 223 PHE B N     1 
ATOM   5811 C CA    . PHE B 1 223 ? 26.658 -28.119 -49.643 1.00 21.84  ? 223 PHE B CA    1 
ATOM   5812 C C     . PHE B 1 223 ? 25.393 -27.410 -50.102 1.00 20.78  ? 223 PHE B C     1 
ATOM   5813 O O     . PHE B 1 223 ? 24.326 -27.789 -49.664 1.00 22.71  ? 223 PHE B O     1 
ATOM   5814 C CB    . PHE B 1 223 ? 26.840 -27.915 -48.136 1.00 22.70  ? 223 PHE B CB    1 
ATOM   5815 C CG    . PHE B 1 223 ? 27.945 -28.711 -47.487 1.00 22.62  ? 223 PHE B CG    1 
ATOM   5816 C CD1   . PHE B 1 223 ? 28.597 -29.739 -48.153 1.00 22.92  ? 223 PHE B CD1   1 
ATOM   5817 C CD2   . PHE B 1 223 ? 28.335 -28.419 -46.194 1.00 23.68  ? 223 PHE B CD2   1 
ATOM   5818 C CE1   . PHE B 1 223 ? 29.587 -30.477 -47.525 1.00 23.75  ? 223 PHE B CE1   1 
ATOM   5819 C CE2   . PHE B 1 223 ? 29.340 -29.147 -45.577 1.00 25.71  ? 223 PHE B CE2   1 
ATOM   5820 C CZ    . PHE B 1 223 ? 29.961 -30.177 -46.240 1.00 24.09  ? 223 PHE B CZ    1 
ATOM   5821 N N     . GLY B 1 224 ? 25.499 -26.352 -50.912 1.00 21.66  ? 224 GLY B N     1 
ATOM   5822 C CA    . GLY B 1 224 ? 24.337 -25.532 -51.216 1.00 21.33  ? 224 GLY B CA    1 
ATOM   5823 C C     . GLY B 1 224 ? 24.670 -24.414 -52.194 1.00 22.92  ? 224 GLY B C     1 
ATOM   5824 O O     . GLY B 1 224 ? 25.835 -24.138 -52.445 1.00 24.67  ? 224 GLY B O     1 
ATOM   5825 N N     . VAL B 1 225 ? 23.629 -23.806 -52.767 1.00 24.12  ? 225 VAL B N     1 
ATOM   5826 C CA    . VAL B 1 225 ? 23.775 -22.668 -53.654 1.00 23.97  ? 225 VAL B CA    1 
ATOM   5827 C C     . VAL B 1 225 ? 23.124 -21.473 -52.966 1.00 25.99  ? 225 VAL B C     1 
ATOM   5828 O O     . VAL B 1 225 ? 21.915 -21.442 -52.731 1.00 24.46  ? 225 VAL B O     1 
ATOM   5829 C CB    . VAL B 1 225 ? 23.148 -22.969 -55.023 1.00 26.44  ? 225 VAL B CB    1 
ATOM   5830 C CG1   . VAL B 1 225 ? 23.272 -21.807 -55.981 1.00 29.06  ? 225 VAL B CG1   1 
ATOM   5831 C CG2   . VAL B 1 225 ? 23.756 -24.212 -55.638 1.00 27.09  ? 225 VAL B CG2   1 
ATOM   5832 N N     . VAL B 1 226 ? 23.965 -20.510 -52.585 1.00 26.59  ? 226 VAL B N     1 
ATOM   5833 C CA    . VAL B 1 226 ? 23.484 -19.292 -51.969 1.00 25.63  ? 226 VAL B CA    1 
ATOM   5834 C C     . VAL B 1 226 ? 22.877 -18.362 -53.023 1.00 26.53  ? 226 VAL B C     1 
ATOM   5835 O O     . VAL B 1 226 ? 23.521 -17.968 -54.013 1.00 25.35  ? 226 VAL B O     1 
ATOM   5836 C CB    . VAL B 1 226 ? 24.606 -18.596 -51.184 1.00 25.43  ? 226 VAL B CB    1 
ATOM   5837 C CG1   . VAL B 1 226 ? 24.119 -17.273 -50.623 1.00 23.35  ? 226 VAL B CG1   1 
ATOM   5838 C CG2   . VAL B 1 226 ? 25.156 -19.493 -50.069 1.00 26.82  ? 226 VAL B CG2   1 
ATOM   5839 N N     . THR B 1 227 ? 21.643 -17.936 -52.733 1.00 25.81  ? 227 THR B N     1 
ATOM   5840 C CA    . THR B 1 227 ? 20.889 -17.115 -53.664 1.00 25.31  ? 227 THR B CA    1 
ATOM   5841 C C     . THR B 1 227 ? 20.600 -15.742 -53.081 1.00 23.58  ? 227 THR B C     1 
ATOM   5842 O O     . THR B 1 227 ? 20.268 -14.849 -53.837 1.00 24.12  ? 227 THR B O     1 
ATOM   5843 C CB    . THR B 1 227 ? 19.619 -17.855 -54.103 1.00 24.43  ? 227 THR B CB    1 
ATOM   5844 O OG1   . THR B 1 227 ? 18.879 -18.189 -52.930 1.00 23.55  ? 227 THR B OG1   1 
ATOM   5845 C CG2   . THR B 1 227 ? 19.956 -19.105 -54.888 1.00 23.75  ? 227 THR B CG2   1 
ATOM   5846 N N     . LYS B 1 228 ? 20.708 -15.574 -51.757 1.00 24.86  ? 228 LYS B N     1 
ATOM   5847 C CA    . LYS B 1 228 ? 20.615 -14.258 -51.125 1.00 24.59  ? 228 LYS B CA    1 
ATOM   5848 C C     . LYS B 1 228 ? 21.544 -14.226 -49.917 1.00 23.42  ? 228 LYS B C     1 
ATOM   5849 O O     . LYS B 1 228 ? 21.655 -15.224 -49.207 1.00 22.52  ? 228 LYS B O     1 
ATOM   5850 C CB    . LYS B 1 228 ? 19.190 -13.920 -50.667 1.00 25.53  ? 228 LYS B CB    1 
ATOM   5851 C CG    . LYS B 1 228 ? 18.125 -13.896 -51.758 1.00 26.59  ? 228 LYS B CG    1 
ATOM   5852 C CD    . LYS B 1 228 ? 16.698 -13.689 -51.216 1.00 28.48  ? 228 LYS B CD    1 
ATOM   5853 C CE    . LYS B 1 228 ? 15.627 -13.574 -52.284 1.00 26.35  ? 228 LYS B CE    1 
ATOM   5854 N NZ    . LYS B 1 228 ? 15.593 -14.807 -53.102 1.00 27.83  ? 228 LYS B NZ    1 
ATOM   5855 N N     . MET B 1 229 ? 22.197 -13.073 -49.686 1.00 24.31  ? 229 MET B N     1 
ATOM   5856 C CA    . MET B 1 229 ? 23.097 -12.937 -48.555 1.00 22.76  ? 229 MET B CA    1 
ATOM   5857 C C     . MET B 1 229 ? 23.032 -11.521 -48.012 1.00 22.11  ? 229 MET B C     1 
ATOM   5858 O O     . MET B 1 229 ? 23.084 -10.563 -48.765 1.00 23.52  ? 229 MET B O     1 
ATOM   5859 C CB    . MET B 1 229 ? 24.538 -13.255 -48.935 1.00 21.62  ? 229 MET B CB    1 
ATOM   5860 C CG    . MET B 1 229 ? 25.424 -13.637 -47.735 1.00 22.09  ? 229 MET B CG    1 
ATOM   5861 S SD    . MET B 1 229 ? 27.207 -13.655 -48.202 1.00 24.71  ? 229 MET B SD    1 
ATOM   5862 C CE    . MET B 1 229 ? 27.624 -11.913 -48.229 1.00 23.27  ? 229 MET B CE    1 
ATOM   5863 N N     . GLY B 1 230 ? 22.928 -11.412 -46.691 1.00 22.24  ? 230 GLY B N     1 
ATOM   5864 C CA    . GLY B 1 230 ? 23.065 -10.137 -46.018 1.00 21.74  ? 230 GLY B CA    1 
ATOM   5865 C C     . GLY B 1 230 ? 24.501 -9.863  -45.592 1.00 21.84  ? 230 GLY B C     1 
ATOM   5866 O O     . GLY B 1 230 ? 25.259 -10.785 -45.313 1.00 22.92  ? 230 GLY B O     1 
ATOM   5867 N N     . ILE B 1 231 ? 24.874 -8.579  -45.541 1.00 22.66  ? 231 ILE B N     1 
ATOM   5868 C CA    . ILE B 1 231 ? 26.211 -8.202  -45.111 1.00 22.00  ? 231 ILE B CA    1 
ATOM   5869 C C     . ILE B 1 231 ? 26.174 -6.860  -44.383 1.00 22.92  ? 231 ILE B C     1 
ATOM   5870 O O     . ILE B 1 231 ? 25.506 -5.906  -44.801 1.00 22.39  ? 231 ILE B O     1 
ATOM   5871 C CB    . ILE B 1 231 ? 27.221 -8.185  -46.284 1.00 23.14  ? 231 ILE B CB    1 
ATOM   5872 C CG1   . ILE B 1 231 ? 28.651 -8.094  -45.750 1.00 23.75  ? 231 ILE B CG1   1 
ATOM   5873 C CG2   . ILE B 1 231 ? 26.936 -7.082  -47.300 1.00 22.63  ? 231 ILE B CG2   1 
ATOM   5874 C CD1   . ILE B 1 231 ? 29.714 -8.425  -46.750 1.00 25.56  ? 231 ILE B CD1   1 
ATOM   5875 N N     . TRP B 1 232 ? 26.956 -6.783  -43.301 1.00 23.09  ? 232 TRP B N     1 
ATOM   5876 C CA    . TRP B 1 232 ? 27.039 -5.557  -42.535 1.00 21.88  ? 232 TRP B CA    1 
ATOM   5877 C C     . TRP B 1 232 ? 27.915 -4.601  -43.319 1.00 23.07  ? 232 TRP B C     1 
ATOM   5878 O O     . TRP B 1 232 ? 28.898 -5.029  -43.946 1.00 23.30  ? 232 TRP B O     1 
ATOM   5879 C CB    . TRP B 1 232 ? 27.522 -5.824  -41.109 1.00 20.65  ? 232 TRP B CB    1 
ATOM   5880 C CG    . TRP B 1 232 ? 26.536 -6.600  -40.293 1.00 21.29  ? 232 TRP B CG    1 
ATOM   5881 C CD1   . TRP B 1 232 ? 25.205 -6.759  -40.545 1.00 22.11  ? 232 TRP B CD1   1 
ATOM   5882 C CD2   . TRP B 1 232 ? 26.806 -7.398  -39.127 1.00 22.82  ? 232 TRP B CD2   1 
ATOM   5883 N NE1   . TRP B 1 232 ? 24.620 -7.531  -39.578 1.00 22.38  ? 232 TRP B NE1   1 
ATOM   5884 C CE2   . TRP B 1 232 ? 25.581 -7.956  -38.710 1.00 23.07  ? 232 TRP B CE2   1 
ATOM   5885 C CE3   . TRP B 1 232 ? 27.957 -7.698  -38.399 1.00 23.86  ? 232 TRP B CE3   1 
ATOM   5886 C CZ2   . TRP B 1 232 ? 25.481 -8.795  -37.604 1.00 25.92  ? 232 TRP B CZ2   1 
ATOM   5887 C CZ3   . TRP B 1 232 ? 27.862 -8.521  -37.306 1.00 24.21  ? 232 TRP B CZ3   1 
ATOM   5888 C CH2   . TRP B 1 232 ? 26.642 -9.073  -36.922 1.00 26.34  ? 232 TRP B CH2   1 
ATOM   5889 N N     . LEU B 1 233 ? 27.481 -3.335  -43.323 1.00 22.43  ? 233 LEU B N     1 
ATOM   5890 C CA    . LEU B 1 233 ? 28.231 -2.247  -43.918 1.00 23.21  ? 233 LEU B CA    1 
ATOM   5891 C C     . LEU B 1 233 ? 28.650 -1.255  -42.841 1.00 22.88  ? 233 LEU B C     1 
ATOM   5892 O O     . LEU B 1 233 ? 27.903 -1.004  -41.915 1.00 24.81  ? 233 LEU B O     1 
ATOM   5893 C CB    . LEU B 1 233 ? 27.332 -1.589  -44.966 1.00 24.66  ? 233 LEU B CB    1 
ATOM   5894 C CG    . LEU B 1 233 ? 27.010 -2.463  -46.180 1.00 25.02  ? 233 LEU B CG    1 
ATOM   5895 C CD1   . LEU B 1 233 ? 26.122 -1.729  -47.178 1.00 26.36  ? 233 LEU B CD1   1 
ATOM   5896 C CD2   . LEU B 1 233 ? 28.281 -2.925  -46.850 1.00 24.02  ? 233 LEU B CD2   1 
ATOM   5897 N N     . MET B 1 234 ? 29.845 -0.689  -42.979 1.00 24.76  ? 234 MET B N     1 
ATOM   5898 C CA    . MET B 1 234 ? 30.394 0.218   -41.993 1.00 24.68  ? 234 MET B CA    1 
ATOM   5899 C C     . MET B 1 234 ? 29.796 1.605   -42.197 1.00 25.43  ? 234 MET B C     1 
ATOM   5900 O O     . MET B 1 234 ? 29.868 2.168   -43.292 1.00 23.45  ? 234 MET B O     1 
ATOM   5901 C CB    . MET B 1 234 ? 31.916 0.314   -42.134 1.00 26.31  ? 234 MET B CB    1 
ATOM   5902 C CG    . MET B 1 234 ? 32.577 1.125   -41.033 1.00 26.32  ? 234 MET B CG    1 
ATOM   5903 S SD    . MET B 1 234 ? 34.386 1.192   -41.072 1.00 26.86  ? 234 MET B SD    1 
ATOM   5904 C CE    . MET B 1 234 ? 34.628 2.115   -42.580 1.00 29.17  ? 234 MET B CE    1 
ATOM   5905 N N     . PRO B 1 235 ? 29.226 2.224   -41.140 1.00 25.99  ? 235 PRO B N     1 
ATOM   5906 C CA    . PRO B 1 235 ? 28.843 3.635   -41.199 1.00 26.90  ? 235 PRO B CA    1 
ATOM   5907 C C     . PRO B 1 235 ? 30.029 4.516   -41.570 1.00 24.88  ? 235 PRO B C     1 
ATOM   5908 O O     . PRO B 1 235 ? 31.175 4.197   -41.254 1.00 24.19  ? 235 PRO B O     1 
ATOM   5909 C CB    . PRO B 1 235 ? 28.326 3.957   -39.791 1.00 26.88  ? 235 PRO B CB    1 
ATOM   5910 C CG    . PRO B 1 235 ? 27.907 2.592   -39.243 1.00 29.18  ? 235 PRO B CG    1 
ATOM   5911 C CD    . PRO B 1 235 ? 28.903 1.614   -39.843 1.00 29.10  ? 235 PRO B CD    1 
ATOM   5912 N N     . GLU B 1 236 ? 29.751 5.579   -42.322 1.00 25.10  ? 236 GLU B N     1 
ATOM   5913 C CA    . GLU B 1 236 ? 30.815 6.479   -42.742 1.00 29.50  ? 236 GLU B CA    1 
ATOM   5914 C C     . GLU B 1 236 ? 31.484 7.061   -41.493 1.00 30.68  ? 236 GLU B C     1 
ATOM   5915 O O     . GLU B 1 236 ? 30.811 7.619   -40.619 1.00 28.02  ? 236 GLU B O     1 
ATOM   5916 C CB    . GLU B 1 236 ? 30.250 7.572   -43.644 1.00 33.00  ? 236 GLU B CB    1 
ATOM   5917 C CG    . GLU B 1 236 ? 31.273 8.588   -44.110 1.00 40.59  ? 236 GLU B CG    1 
ATOM   5918 C CD    . GLU B 1 236 ? 30.670 9.726   -44.923 1.00 46.72  ? 236 GLU B CD    1 
ATOM   5919 O OE1   . GLU B 1 236 ? 29.458 9.983   -44.777 1.00 51.26  ? 236 GLU B OE1   1 
ATOM   5920 O OE2   . GLU B 1 236 ? 31.406 10.341  -45.707 1.00 51.37  ? 236 GLU B OE2   1 
ATOM   5921 N N     . PRO B 1 237 ? 32.821 6.931   -41.363 1.00 27.91  ? 237 PRO B N     1 
ATOM   5922 C CA    . PRO B 1 237 ? 33.531 7.420   -40.195 1.00 29.30  ? 237 PRO B CA    1 
ATOM   5923 C C     . PRO B 1 237 ? 33.638 8.938   -40.184 1.00 29.11  ? 237 PRO B C     1 
ATOM   5924 O O     . PRO B 1 237 ? 33.475 9.590   -41.214 1.00 26.83  ? 237 PRO B O     1 
ATOM   5925 C CB    . PRO B 1 237 ? 34.923 6.793   -40.346 1.00 28.68  ? 237 PRO B CB    1 
ATOM   5926 C CG    . PRO B 1 237 ? 35.100 6.705   -41.827 1.00 28.43  ? 237 PRO B CG    1 
ATOM   5927 C CD    . PRO B 1 237 ? 33.733 6.294   -42.324 1.00 29.87  ? 237 PRO B CD    1 
ATOM   5928 N N     . ALA B 1 238 ? 33.929 9.473   -38.996 1.00 29.72  ? 238 ALA B N     1 
ATOM   5929 C CA    . ALA B 1 238 ? 34.031 10.910  -38.826 1.00 30.71  ? 238 ALA B CA    1 
ATOM   5930 C C     . ALA B 1 238 ? 35.404 11.396  -39.270 1.00 31.88  ? 238 ALA B C     1 
ATOM   5931 O O     . ALA B 1 238 ? 35.632 12.593  -39.336 1.00 41.48  ? 238 ALA B O     1 
ATOM   5932 C CB    . ALA B 1 238 ? 33.740 11.277  -37.398 1.00 29.07  ? 238 ALA B CB    1 
ATOM   5933 N N     . GLY B 1 239 ? 36.320 10.481  -39.584 1.00 30.00  ? 239 GLY B N     1 
ATOM   5934 C CA    . GLY B 1 239 ? 37.587 10.862  -40.182 1.00 28.53  ? 239 GLY B CA    1 
ATOM   5935 C C     . GLY B 1 239 ? 38.294 9.662   -40.789 1.00 27.46  ? 239 GLY B C     1 
ATOM   5936 O O     . GLY B 1 239 ? 37.891 8.524   -40.563 1.00 33.11  ? 239 GLY B O     1 
ATOM   5937 N N     . TYR B 1 240 ? 39.364 9.921   -41.535 1.00 26.74  ? 240 TYR B N     1 
ATOM   5938 C CA    . TYR B 1 240 ? 39.999 8.885   -42.330 1.00 26.12  ? 240 TYR B CA    1 
ATOM   5939 C C     . TYR B 1 240 ? 41.377 9.371   -42.724 1.00 27.69  ? 240 TYR B C     1 
ATOM   5940 O O     . TYR B 1 240 ? 41.464 10.397  -43.386 1.00 28.29  ? 240 TYR B O     1 
ATOM   5941 C CB    . TYR B 1 240 ? 39.231 8.595   -43.622 1.00 26.14  ? 240 TYR B CB    1 
ATOM   5942 C CG    . TYR B 1 240 ? 39.946 7.624   -44.527 1.00 26.62  ? 240 TYR B CG    1 
ATOM   5943 C CD1   . TYR B 1 240 ? 40.291 6.348   -44.084 1.00 27.94  ? 240 TYR B CD1   1 
ATOM   5944 C CD2   . TYR B 1 240 ? 40.333 7.989   -45.799 1.00 25.61  ? 240 TYR B CD2   1 
ATOM   5945 C CE1   . TYR B 1 240 ? 40.964 5.457   -44.902 1.00 27.32  ? 240 TYR B CE1   1 
ATOM   5946 C CE2   . TYR B 1 240 ? 40.997 7.104   -46.633 1.00 28.11  ? 240 TYR B CE2   1 
ATOM   5947 C CZ    . TYR B 1 240 ? 41.306 5.832   -46.187 1.00 26.90  ? 240 TYR B CZ    1 
ATOM   5948 O OH    . TYR B 1 240 ? 41.993 4.993   -47.018 1.00 26.19  ? 240 TYR B OH    1 
ATOM   5949 N N     . ARG B 1 241 ? 42.417 8.651   -42.276 1.00 29.13  ? 241 ARG B N     1 
ATOM   5950 C CA    . ARG B 1 241 ? 43.792 9.049   -42.513 1.00 29.43  ? 241 ARG B CA    1 
ATOM   5951 C C     . ARG B 1 241 ? 44.624 7.822   -42.906 1.00 27.81  ? 241 ARG B C     1 
ATOM   5952 O O     . ARG B 1 241 ? 45.080 7.051   -42.060 1.00 26.23  ? 241 ARG B O     1 
ATOM   5953 C CB    . ARG B 1 241 ? 44.347 9.785   -41.288 1.00 33.90  ? 241 ARG B CB    1 
ATOM   5954 C CG    . ARG B 1 241 ? 43.862 11.224  -41.120 1.00 35.97  ? 241 ARG B CG    1 
ATOM   5955 C CD    . ARG B 1 241 ? 44.456 12.203  -42.125 1.00 41.29  ? 241 ARG B CD    1 
ATOM   5956 N NE    . ARG B 1 241 ? 45.827 12.657  -41.857 1.00 41.13  ? 241 ARG B NE    1 
ATOM   5957 C CZ    . ARG B 1 241 ? 46.642 13.226  -42.752 1.00 42.12  ? 241 ARG B CZ    1 
ATOM   5958 N NH1   . ARG B 1 241 ? 46.321 13.273  -44.036 1.00 43.75  ? 241 ARG B NH1   1 
ATOM   5959 N NH2   . ARG B 1 241 ? 47.807 13.718  -42.367 1.00 41.19  ? 241 ARG B NH2   1 
ATOM   5960 N N     . PRO B 1 242 ? 44.855 7.612   -44.223 1.00 27.19  ? 242 PRO B N     1 
ATOM   5961 C CA    . PRO B 1 242 ? 45.705 6.523   -44.700 1.00 27.87  ? 242 PRO B CA    1 
ATOM   5962 C C     . PRO B 1 242 ? 47.191 6.829   -44.576 1.00 26.25  ? 242 PRO B C     1 
ATOM   5963 O O     . PRO B 1 242 ? 47.568 7.981   -44.746 1.00 25.10  ? 242 PRO B O     1 
ATOM   5964 C CB    . PRO B 1 242 ? 45.276 6.370   -46.163 1.00 27.10  ? 242 PRO B CB    1 
ATOM   5965 C CG    . PRO B 1 242 ? 44.767 7.730   -46.571 1.00 27.45  ? 242 PRO B CG    1 
ATOM   5966 C CD    . PRO B 1 242 ? 44.264 8.395   -45.320 1.00 26.90  ? 242 PRO B CD    1 
ATOM   5967 N N     . TYR B 1 243 ? 48.007 5.796   -44.281 1.00 24.49  ? 243 TYR B N     1 
ATOM   5968 C CA    . TYR B 1 243 ? 49.437 5.983   -44.050 1.00 26.86  ? 243 TYR B CA    1 
ATOM   5969 C C     . TYR B 1 243 ? 50.274 4.844   -44.652 1.00 26.05  ? 243 TYR B C     1 
ATOM   5970 O O     . TYR B 1 243 ? 49.828 3.700   -44.785 1.00 22.61  ? 243 TYR B O     1 
ATOM   5971 C CB    . TYR B 1 243 ? 49.736 6.144   -42.546 1.00 25.59  ? 243 TYR B CB    1 
ATOM   5972 C CG    . TYR B 1 243 ? 49.365 4.959   -41.696 1.00 26.15  ? 243 TYR B CG    1 
ATOM   5973 C CD1   . TYR B 1 243 ? 50.159 3.822   -41.629 1.00 27.23  ? 243 TYR B CD1   1 
ATOM   5974 C CD2   . TYR B 1 243 ? 48.165 4.935   -41.017 1.00 29.19  ? 243 TYR B CD2   1 
ATOM   5975 C CE1   . TYR B 1 243 ? 49.797 2.723   -40.859 1.00 28.02  ? 243 TYR B CE1   1 
ATOM   5976 C CE2   . TYR B 1 243 ? 47.785 3.848   -40.244 1.00 30.42  ? 243 TYR B CE2   1 
ATOM   5977 C CZ    . TYR B 1 243 ? 48.602 2.732   -40.159 1.00 29.56  ? 243 TYR B CZ    1 
ATOM   5978 O OH    . TYR B 1 243 ? 48.161 1.661   -39.404 1.00 28.40  ? 243 TYR B OH    1 
ATOM   5979 N N     . LEU B 1 244 ? 51.533 5.180   -44.956 1.00 26.94  ? 244 LEU B N     1 
ATOM   5980 C CA    . LEU B 1 244 ? 52.532 4.204   -45.369 1.00 27.36  ? 244 LEU B CA    1 
ATOM   5981 C C     . LEU B 1 244 ? 53.772 4.317   -44.481 1.00 26.16  ? 244 LEU B C     1 
ATOM   5982 O O     . LEU B 1 244 ? 54.298 5.412   -44.285 1.00 26.87  ? 244 LEU B O     1 
ATOM   5983 C CB    . LEU B 1 244 ? 52.894 4.467   -46.834 1.00 28.43  ? 244 LEU B CB    1 
ATOM   5984 C CG    . LEU B 1 244 ? 54.089 3.688   -47.390 1.00 28.24  ? 244 LEU B CG    1 
ATOM   5985 C CD1   . LEU B 1 244 ? 53.790 2.207   -47.461 1.00 29.55  ? 244 LEU B CD1   1 
ATOM   5986 C CD2   . LEU B 1 244 ? 54.449 4.213   -48.764 1.00 30.54  ? 244 LEU B CD2   1 
ATOM   5987 N N     . ILE B 1 245 ? 54.242 3.168   -43.980 1.00 27.77  ? 245 ILE B N     1 
ATOM   5988 C CA    . ILE B 1 245 ? 55.483 3.052   -43.218 1.00 27.89  ? 245 ILE B CA    1 
ATOM   5989 C C     . ILE B 1 245 ? 56.422 2.108   -43.972 1.00 26.61  ? 245 ILE B C     1 
ATOM   5990 O O     . ILE B 1 245 ? 56.073 0.974   -44.220 1.00 30.95  ? 245 ILE B O     1 
ATOM   5991 C CB    . ILE B 1 245 ? 55.194 2.567   -41.780 1.00 26.13  ? 245 ILE B CB    1 
ATOM   5992 C CG1   . ILE B 1 245 ? 54.015 3.339   -41.177 1.00 24.54  ? 245 ILE B CG1   1 
ATOM   5993 C CG2   . ILE B 1 245 ? 56.451 2.635   -40.903 1.00 27.36  ? 245 ILE B CG2   1 
ATOM   5994 C CD1   . ILE B 1 245 ? 53.837 3.186   -39.701 1.00 23.20  ? 245 ILE B CD1   1 
ATOM   5995 N N     . THR B 1 246 ? 57.599 2.585   -44.374 1.00 27.52  ? 246 THR B N     1 
ATOM   5996 C CA    . THR B 1 246 ? 58.511 1.798   -45.193 1.00 28.03  ? 246 THR B CA    1 
ATOM   5997 C C     . THR B 1 246 ? 59.769 1.462   -44.397 1.00 29.58  ? 246 THR B C     1 
ATOM   5998 O O     . THR B 1 246 ? 60.173 2.187   -43.493 1.00 26.09  ? 246 THR B O     1 
ATOM   5999 C CB    . THR B 1 246 ? 58.890 2.500   -46.507 1.00 28.45  ? 246 THR B CB    1 
ATOM   6000 O OG1   . THR B 1 246 ? 59.775 3.604   -46.296 1.00 31.05  ? 246 THR B OG1   1 
ATOM   6001 C CG2   . THR B 1 246 ? 57.675 3.003   -47.252 1.00 30.90  ? 246 THR B CG2   1 
ATOM   6002 N N     . PHE B 1 247 ? 60.381 0.338   -44.764 1.00 31.51  ? 247 PHE B N     1 
ATOM   6003 C CA    . PHE B 1 247 ? 61.517 -0.199  -44.043 1.00 32.04  ? 247 PHE B CA    1 
ATOM   6004 C C     . PHE B 1 247 ? 62.581 -0.503  -45.086 1.00 35.03  ? 247 PHE B C     1 
ATOM   6005 O O     . PHE B 1 247 ? 62.230 -0.964  -46.174 1.00 33.65  ? 247 PHE B O     1 
ATOM   6006 C CB    . PHE B 1 247 ? 61.086 -1.434  -43.248 1.00 29.77  ? 247 PHE B CB    1 
ATOM   6007 C CG    . PHE B 1 247 ? 59.980 -1.158  -42.266 1.00 29.38  ? 247 PHE B CG    1 
ATOM   6008 C CD1   . PHE B 1 247 ? 60.242 -0.506  -41.070 1.00 28.59  ? 247 PHE B CD1   1 
ATOM   6009 C CD2   . PHE B 1 247 ? 58.672 -1.498  -42.562 1.00 27.69  ? 247 PHE B CD2   1 
ATOM   6010 C CE1   . PHE B 1 247 ? 59.225 -0.258  -40.168 1.00 28.22  ? 247 PHE B CE1   1 
ATOM   6011 C CE2   . PHE B 1 247 ? 57.649 -1.216  -41.668 1.00 27.55  ? 247 PHE B CE2   1 
ATOM   6012 C CZ    . PHE B 1 247 ? 57.926 -0.598  -40.476 1.00 28.48  ? 247 PHE B CZ    1 
ATOM   6013 N N     . GLU B 1 248 ? 63.856 -0.234  -44.760 1.00 34.74  ? 248 GLU B N     1 
ATOM   6014 C CA    . GLU B 1 248 ? 64.867 -0.226  -45.798 1.00 37.50  ? 248 GLU B CA    1 
ATOM   6015 C C     . GLU B 1 248 ? 65.496 -1.617  -45.959 1.00 34.32  ? 248 GLU B C     1 
ATOM   6016 O O     . GLU B 1 248 ? 65.912 -1.945  -47.064 1.00 33.04  ? 248 GLU B O     1 
ATOM   6017 C CB    . GLU B 1 248 ? 65.841 0.932   -45.592 1.00 45.49  ? 248 GLU B CB    1 
ATOM   6018 C CG    . GLU B 1 248 ? 65.158 2.302   -45.289 1.00 62.09  ? 248 GLU B CG    1 
ATOM   6019 C CD    . GLU B 1 248 ? 64.092 2.971   -46.183 1.00 62.53  ? 248 GLU B CD    1 
ATOM   6020 O OE1   . GLU B 1 248 ? 64.471 3.636   -47.176 1.00 49.79  ? 248 GLU B OE1   1 
ATOM   6021 O OE2   . GLU B 1 248 ? 62.856 2.921   -45.829 1.00 53.46  ? 248 GLU B OE2   1 
ATOM   6022 N N     . ASN B 1 249 ? 65.466 -2.485  -44.939 1.00 34.15  ? 249 ASN B N     1 
ATOM   6023 C CA    . ASN B 1 249 ? 66.114 -3.799  -45.033 1.00 36.70  ? 249 ASN B CA    1 
ATOM   6024 C C     . ASN B 1 249 ? 65.123 -4.960  -44.979 1.00 34.30  ? 249 ASN B C     1 
ATOM   6025 O O     . ASN B 1 249 ? 64.153 -4.909  -44.231 1.00 33.98  ? 249 ASN B O     1 
ATOM   6026 C CB    . ASN B 1 249 ? 67.116 -4.022  -43.903 1.00 38.80  ? 249 ASN B CB    1 
ATOM   6027 C CG    . ASN B 1 249 ? 68.072 -2.854  -43.811 1.00 42.67  ? 249 ASN B CG    1 
ATOM   6028 O OD1   . ASN B 1 249 ? 68.759 -2.534  -44.779 1.00 46.62  ? 249 ASN B OD1   1 
ATOM   6029 N ND2   . ASN B 1 249 ? 68.047 -2.157  -42.691 1.00 42.91  ? 249 ASN B ND2   1 
ATOM   6030 N N     . GLU B 1 250 ? 65.424 -6.036  -45.725 1.00 36.34  ? 250 GLU B N     1 
ATOM   6031 C CA    . GLU B 1 250 ? 64.580 -7.227  -45.782 1.00 35.28  ? 250 GLU B CA    1 
ATOM   6032 C C     . GLU B 1 250 ? 64.451 -7.865  -44.399 1.00 33.36  ? 250 GLU B C     1 
ATOM   6033 O O     . GLU B 1 250 ? 63.378 -8.372  -44.062 1.00 31.90  ? 250 GLU B O     1 
ATOM   6034 C CB    . GLU B 1 250 ? 65.073 -8.239  -46.820 1.00 41.77  ? 250 GLU B CB    1 
ATOM   6035 C CG    . GLU B 1 250 ? 66.570 -8.501  -46.783 1.00 53.16  ? 250 GLU B CG    1 
ATOM   6036 C CD    . GLU B 1 250 ? 67.071 -9.779  -47.454 1.00 60.28  ? 250 GLU B CD    1 
ATOM   6037 O OE1   . GLU B 1 250 ? 66.534 -10.160 -48.520 1.00 55.73  ? 250 GLU B OE1   1 
ATOM   6038 O OE2   . GLU B 1 250 ? 68.021 -10.389 -46.913 1.00 63.25  ? 250 GLU B OE2   1 
ATOM   6039 N N     . ASP B 1 251 ? 65.501 -7.769  -43.574 1.00 31.06  ? 251 ASP B N     1 
ATOM   6040 C CA    . ASP B 1 251 ? 65.508 -8.356  -42.245 1.00 33.41  ? 251 ASP B CA    1 
ATOM   6041 C C     . ASP B 1 251 ? 64.635 -7.582  -41.254 1.00 32.45  ? 251 ASP B C     1 
ATOM   6042 O O     . ASP B 1 251 ? 64.360 -8.106  -40.169 1.00 30.55  ? 251 ASP B O     1 
ATOM   6043 C CB    . ASP B 1 251 ? 66.926 -8.445  -41.682 1.00 39.18  ? 251 ASP B CB    1 
ATOM   6044 C CG    . ASP B 1 251 ? 67.741 -9.577  -42.282 1.00 47.08  ? 251 ASP B CG    1 
ATOM   6045 O OD1   . ASP B 1 251 ? 67.151 -10.397 -43.034 1.00 42.04  ? 251 ASP B OD1   1 
ATOM   6046 O OD2   . ASP B 1 251 ? 68.965 -9.621  -41.996 1.00 53.97  ? 251 ASP B OD2   1 
ATOM   6047 N N     . ASP B 1 252 ? 64.205 -6.355  -41.612 1.00 30.01  ? 252 ASP B N     1 
ATOM   6048 C CA    . ASP B 1 252 ? 63.342 -5.545  -40.751 1.00 29.27  ? 252 ASP B CA    1 
ATOM   6049 C C     . ASP B 1 252 ? 61.998 -6.212  -40.477 1.00 27.96  ? 252 ASP B C     1 
ATOM   6050 O O     . ASP B 1 252 ? 61.364 -5.895  -39.480 1.00 26.65  ? 252 ASP B O     1 
ATOM   6051 C CB    . ASP B 1 252 ? 63.053 -4.174  -41.354 1.00 32.87  ? 252 ASP B CB    1 
ATOM   6052 C CG    . ASP B 1 252 ? 64.251 -3.248  -41.341 1.00 33.19  ? 252 ASP B CG    1 
ATOM   6053 O OD1   . ASP B 1 252 ? 65.142 -3.495  -40.506 1.00 35.67  ? 252 ASP B OD1   1 
ATOM   6054 O OD2   . ASP B 1 252 ? 64.272 -2.286  -42.166 1.00 29.82  ? 252 ASP B OD2   1 
ATOM   6055 N N     . ILE B 1 253 ? 61.578 -7.151  -41.336 1.00 28.37  ? 253 ILE B N     1 
ATOM   6056 C CA    . ILE B 1 253 ? 60.277 -7.775  -41.201 1.00 27.07  ? 253 ILE B CA    1 
ATOM   6057 C C     . ILE B 1 253 ? 60.181 -8.503  -39.867 1.00 26.61  ? 253 ILE B C     1 
ATOM   6058 O O     . ILE B 1 253 ? 59.085 -8.646  -39.338 1.00 30.91  ? 253 ILE B O     1 
ATOM   6059 C CB    . ILE B 1 253 ? 59.965 -8.698  -42.400 1.00 27.76  ? 253 ILE B CB    1 
ATOM   6060 C CG1   . ILE B 1 253 ? 58.470 -8.971  -42.525 1.00 27.75  ? 253 ILE B CG1   1 
ATOM   6061 C CG2   . ILE B 1 253 ? 60.739 -10.001 -42.344 1.00 28.91  ? 253 ILE B CG2   1 
ATOM   6062 C CD1   . ILE B 1 253 ? 57.608 -7.729  -42.553 1.00 30.03  ? 253 ILE B CD1   1 
ATOM   6063 N N     . GLU B 1 254 ? 61.307 -8.967  -39.328 1.00 26.18  ? 254 GLU B N     1 
ATOM   6064 C CA    . GLU B 1 254 ? 61.286 -9.681  -38.056 1.00 28.22  ? 254 GLU B CA    1 
ATOM   6065 C C     . GLU B 1 254 ? 60.807 -8.746  -36.941 1.00 27.28  ? 254 GLU B C     1 
ATOM   6066 O O     . GLU B 1 254 ? 59.840 -9.048  -36.249 1.00 29.53  ? 254 GLU B O     1 
ATOM   6067 C CB    . GLU B 1 254 ? 62.638 -10.343 -37.758 1.00 26.94  ? 254 GLU B CB    1 
ATOM   6068 C CG    . GLU B 1 254 ? 62.665 -11.039 -36.413 1.00 30.20  ? 254 GLU B CG    1 
ATOM   6069 C CD    . GLU B 1 254 ? 63.817 -12.000 -36.111 1.00 33.90  ? 254 GLU B CD    1 
ATOM   6070 O OE1   . GLU B 1 254 ? 64.670 -12.221 -36.991 1.00 31.90  ? 254 GLU B OE1   1 
ATOM   6071 O OE2   . GLU B 1 254 ? 63.858 -12.535 -34.964 1.00 34.11  ? 254 GLU B OE2   1 
ATOM   6072 N N     . THR B 1 255 ? 61.463 -7.594  -36.771 1.00 28.02  ? 255 THR B N     1 
ATOM   6073 C CA    . THR B 1 255 ? 61.128 -6.708  -35.672 1.00 27.32  ? 255 THR B CA    1 
ATOM   6074 C C     . THR B 1 255 ? 59.788 -6.045  -35.976 1.00 27.21  ? 255 THR B C     1 
ATOM   6075 O O     . THR B 1 255 ? 58.984 -5.846  -35.072 1.00 26.38  ? 255 THR B O     1 
ATOM   6076 C CB    . THR B 1 255 ? 62.294 -5.757  -35.352 1.00 28.48  ? 255 THR B CB    1 
ATOM   6077 O OG1   . THR B 1 255 ? 62.128 -5.263  -34.017 1.00 27.85  ? 255 THR B OG1   1 
ATOM   6078 C CG2   . THR B 1 255 ? 62.403 -4.605  -36.326 1.00 27.80  ? 255 THR B CG2   1 
ATOM   6079 N N     . VAL B 1 256 ? 59.531 -5.754  -37.258 1.00 28.62  ? 256 VAL B N     1 
ATOM   6080 C CA    . VAL B 1 256 ? 58.267 -5.157  -37.658 1.00 28.73  ? 256 VAL B CA    1 
ATOM   6081 C C     . VAL B 1 256 ? 57.097 -6.024  -37.197 1.00 27.72  ? 256 VAL B C     1 
ATOM   6082 O O     . VAL B 1 256 ? 56.142 -5.496  -36.624 1.00 27.64  ? 256 VAL B O     1 
ATOM   6083 C CB    . VAL B 1 256 ? 58.201 -4.914  -39.173 1.00 30.52  ? 256 VAL B CB    1 
ATOM   6084 C CG1   . VAL B 1 256 ? 56.769 -4.742  -39.640 1.00 28.78  ? 256 VAL B CG1   1 
ATOM   6085 C CG2   . VAL B 1 256 ? 59.054 -3.722  -39.583 1.00 29.91  ? 256 VAL B CG2   1 
ATOM   6086 N N     . THR B 1 257 ? 57.181 -7.347  -37.409 1.00 25.22  ? 257 THR B N     1 
ATOM   6087 C CA    . THR B 1 257 ? 56.064 -8.218  -37.070 1.00 26.34  ? 257 THR B CA    1 
ATOM   6088 C C     . THR B 1 257 ? 55.842 -8.296  -35.555 1.00 27.24  ? 257 THR B C     1 
ATOM   6089 O O     . THR B 1 257 ? 54.689 -8.413  -35.113 1.00 25.30  ? 257 THR B O     1 
ATOM   6090 C CB    . THR B 1 257 ? 56.241 -9.615  -37.671 1.00 28.12  ? 257 THR B CB    1 
ATOM   6091 O OG1   . THR B 1 257 ? 56.353 -9.447  -39.084 1.00 30.05  ? 257 THR B OG1   1 
ATOM   6092 C CG2   . THR B 1 257 ? 55.085 -10.543 -37.356 1.00 28.85  ? 257 THR B CG2   1 
ATOM   6093 N N     . GLU B 1 258 ? 56.937 -8.257  -34.770 1.00 26.78  ? 258 GLU B N     1 
ATOM   6094 C CA    . GLU B 1 258 ? 56.856 -8.239  -33.312 1.00 27.23  ? 258 GLU B CA    1 
ATOM   6095 C C     . GLU B 1 258 ? 56.099 -7.015  -32.816 1.00 26.63  ? 258 GLU B C     1 
ATOM   6096 O O     . GLU B 1 258 ? 55.336 -7.111  -31.861 1.00 28.26  ? 258 GLU B O     1 
ATOM   6097 C CB    . GLU B 1 258 ? 58.223 -8.138  -32.622 1.00 29.10  ? 258 GLU B CB    1 
ATOM   6098 C CG    . GLU B 1 258 ? 59.077 -9.398  -32.622 1.00 30.36  ? 258 GLU B CG    1 
ATOM   6099 C CD    . GLU B 1 258 ? 58.459 -10.584 -31.905 1.00 32.36  ? 258 GLU B CD    1 
ATOM   6100 O OE1   . GLU B 1 258 ? 58.349 -10.529 -30.648 1.00 29.42  ? 258 GLU B OE1   1 
ATOM   6101 O OE2   . GLU B 1 258 ? 58.033 -11.533 -32.632 1.00 30.13  ? 258 GLU B OE2   1 
ATOM   6102 N N     . ARG B 1 259 ? 56.357 -5.861  -33.439 1.00 27.20  ? 259 ARG B N     1 
ATOM   6103 C CA    . ARG B 1 259 ? 55.719 -4.612  -33.046 1.00 27.73  ? 259 ARG B CA    1 
ATOM   6104 C C     . ARG B 1 259 ? 54.263 -4.582  -33.516 1.00 27.92  ? 259 ARG B C     1 
ATOM   6105 O O     . ARG B 1 259 ? 53.412 -4.051  -32.800 1.00 27.96  ? 259 ARG B O     1 
ATOM   6106 C CB    . ARG B 1 259 ? 56.519 -3.422  -33.581 1.00 27.05  ? 259 ARG B CB    1 
ATOM   6107 C CG    . ARG B 1 259 ? 57.922 -3.338  -33.003 1.00 29.77  ? 259 ARG B CG    1 
ATOM   6108 C CD    . ARG B 1 259 ? 58.890 -2.776  -34.025 1.00 36.57  ? 259 ARG B CD    1 
ATOM   6109 N NE    . ARG B 1 259 ? 60.276 -2.869  -33.580 1.00 45.49  ? 259 ARG B NE    1 
ATOM   6110 C CZ    . ARG B 1 259 ? 61.005 -1.866  -33.086 1.00 44.79  ? 259 ARG B CZ    1 
ATOM   6111 N NH1   . ARG B 1 259 ? 60.484 -0.670  -32.886 1.00 42.59  ? 259 ARG B NH1   1 
ATOM   6112 N NH2   . ARG B 1 259 ? 62.267 -2.077  -32.775 1.00 44.07  ? 259 ARG B NH2   1 
ATOM   6113 N N     . LEU B 1 260 ? 53.972 -5.178  -34.688 1.00 26.23  ? 260 LEU B N     1 
ATOM   6114 C CA    . LEU B 1 260 ? 52.591 -5.273  -35.174 1.00 24.34  ? 260 LEU B CA    1 
ATOM   6115 C C     . LEU B 1 260 ? 51.714 -6.097  -34.229 1.00 23.70  ? 260 LEU B C     1 
ATOM   6116 O O     . LEU B 1 260 ? 50.556 -5.763  -34.038 1.00 26.17  ? 260 LEU B O     1 
ATOM   6117 C CB    . LEU B 1 260 ? 52.568 -5.878  -36.581 1.00 23.58  ? 260 LEU B CB    1 
ATOM   6118 C CG    . LEU B 1 260 ? 52.976 -4.943  -37.715 1.00 22.56  ? 260 LEU B CG    1 
ATOM   6119 C CD1   . LEU B 1 260 ? 53.171 -5.708  -38.997 1.00 21.90  ? 260 LEU B CD1   1 
ATOM   6120 C CD2   . LEU B 1 260 ? 51.940 -3.846  -37.897 1.00 23.43  ? 260 LEU B CD2   1 
ATOM   6121 N N     . ARG B 1 261 ? 52.252 -7.148  -33.596 1.00 23.99  ? 261 ARG B N     1 
ATOM   6122 C CA    . ARG B 1 261 ? 51.411 -8.077  -32.848 1.00 23.69  ? 261 ARG B CA    1 
ATOM   6123 C C     . ARG B 1 261 ? 50.539 -7.381  -31.802 1.00 23.78  ? 261 ARG B C     1 
ATOM   6124 O O     . ARG B 1 261 ? 49.334 -7.556  -31.823 1.00 27.14  ? 261 ARG B O     1 
ATOM   6125 C CB    . ARG B 1 261 ? 52.229 -9.167  -32.160 1.00 23.57  ? 261 ARG B CB    1 
ATOM   6126 C CG    . ARG B 1 261 ? 51.397 -10.111 -31.304 1.00 24.52  ? 261 ARG B CG    1 
ATOM   6127 C CD    . ARG B 1 261 ? 52.288 -11.177 -30.680 1.00 26.12  ? 261 ARG B CD    1 
ATOM   6128 N NE    . ARG B 1 261 ? 53.465 -10.663 -29.977 1.00 24.94  ? 261 ARG B NE    1 
ATOM   6129 C CZ    . ARG B 1 261 ? 54.728 -10.932 -30.288 1.00 25.75  ? 261 ARG B CZ    1 
ATOM   6130 N NH1   . ARG B 1 261 ? 55.020 -11.603 -31.384 1.00 25.67  ? 261 ARG B NH1   1 
ATOM   6131 N NH2   . ARG B 1 261 ? 55.713 -10.528 -29.504 1.00 26.80  ? 261 ARG B NH2   1 
ATOM   6132 N N     . PRO B 1 262 ? 51.058 -6.641  -30.793 1.00 24.49  ? 262 PRO B N     1 
ATOM   6133 C CA    . PRO B 1 262 ? 50.178 -6.117  -29.740 1.00 23.30  ? 262 PRO B CA    1 
ATOM   6134 C C     . PRO B 1 262 ? 49.224 -5.041  -30.290 1.00 22.75  ? 262 PRO B C     1 
ATOM   6135 O O     . PRO B 1 262 ? 48.088 -4.943  -29.837 1.00 23.94  ? 262 PRO B O     1 
ATOM   6136 C CB    . PRO B 1 262 ? 51.190 -5.661  -28.676 1.00 20.82  ? 262 PRO B CB    1 
ATOM   6137 C CG    . PRO B 1 262 ? 52.374 -5.216  -29.497 1.00 21.29  ? 262 PRO B CG    1 
ATOM   6138 C CD    . PRO B 1 262 ? 52.458 -6.229  -30.614 1.00 23.04  ? 262 PRO B CD    1 
ATOM   6139 N N     . LEU B 1 263 ? 49.635 -4.319  -31.342 1.00 21.55  ? 263 LEU B N     1 
ATOM   6140 C CA    . LEU B 1 263 ? 48.814 -3.285  -31.955 1.00 23.14  ? 263 LEU B CA    1 
ATOM   6141 C C     . LEU B 1 263 ? 47.582 -3.872  -32.641 1.00 26.07  ? 263 LEU B C     1 
ATOM   6142 O O     . LEU B 1 263 ? 46.537 -3.216  -32.676 1.00 28.31  ? 263 LEU B O     1 
ATOM   6143 C CB    . LEU B 1 263 ? 49.639 -2.531  -32.998 1.00 24.24  ? 263 LEU B CB    1 
ATOM   6144 C CG    . LEU B 1 263 ? 50.785 -1.670  -32.475 1.00 23.32  ? 263 LEU B CG    1 
ATOM   6145 C CD1   . LEU B 1 263 ? 51.579 -1.087  -33.627 1.00 23.07  ? 263 LEU B CD1   1 
ATOM   6146 C CD2   . LEU B 1 263 ? 50.264 -0.566  -31.600 1.00 24.34  ? 263 LEU B CD2   1 
ATOM   6147 N N     . LYS B 1 264 ? 47.718 -5.066  -33.241 1.00 26.76  ? 264 LYS B N     1 
ATOM   6148 C CA    . LYS B 1 264 ? 46.596 -5.723  -33.901 1.00 26.60  ? 264 LYS B CA    1 
ATOM   6149 C C     . LYS B 1 264 ? 45.703 -6.452  -32.903 1.00 26.72  ? 264 LYS B C     1 
ATOM   6150 O O     . LYS B 1 264 ? 44.497 -6.475  -33.050 1.00 26.74  ? 264 LYS B O     1 
ATOM   6151 C CB    . LYS B 1 264 ? 47.091 -6.743  -34.925 1.00 29.07  ? 264 LYS B CB    1 
ATOM   6152 C CG    . LYS B 1 264 ? 47.505 -6.186  -36.285 1.00 32.16  ? 264 LYS B CG    1 
ATOM   6153 C CD    . LYS B 1 264 ? 46.397 -5.538  -37.080 1.00 35.31  ? 264 LYS B CD    1 
ATOM   6154 C CE    . LYS B 1 264 ? 45.101 -6.314  -37.151 1.00 35.15  ? 264 LYS B CE    1 
ATOM   6155 N NZ    . LYS B 1 264 ? 44.025 -5.515  -37.783 1.00 33.31  ? 264 LYS B NZ    1 
ATOM   6156 N N     . VAL B 1 265 ? 46.302 -7.117  -31.913 1.00 29.14  ? 265 VAL B N     1 
ATOM   6157 C CA    . VAL B 1 265 ? 45.551 -7.912  -30.964 1.00 26.60  ? 265 VAL B CA    1 
ATOM   6158 C C     . VAL B 1 265 ? 44.679 -6.983  -30.125 1.00 27.69  ? 265 VAL B C     1 
ATOM   6159 O O     . VAL B 1 265 ? 43.538 -7.317  -29.827 1.00 28.66  ? 265 VAL B O     1 
ATOM   6160 C CB    . VAL B 1 265 ? 46.506 -8.751  -30.097 1.00 28.74  ? 265 VAL B CB    1 
ATOM   6161 C CG1   . VAL B 1 265 ? 45.780 -9.501  -28.996 1.00 27.73  ? 265 VAL B CG1   1 
ATOM   6162 C CG2   . VAL B 1 265 ? 47.321 -9.730  -30.941 1.00 31.39  ? 265 VAL B CG2   1 
ATOM   6163 N N     . ALA B 1 266 ? 45.216 -5.815  -29.762 1.00 27.32  ? 266 ALA B N     1 
ATOM   6164 C CA    . ALA B 1 266 ? 44.492 -4.845  -28.945 1.00 29.06  ? 266 ALA B CA    1 
ATOM   6165 C C     . ALA B 1 266 ? 43.574 -3.989  -29.805 1.00 30.39  ? 266 ALA B C     1 
ATOM   6166 O O     . ALA B 1 266 ? 42.740 -3.277  -29.263 1.00 36.56  ? 266 ALA B O     1 
ATOM   6167 C CB    . ALA B 1 266 ? 45.447 -3.958  -28.193 1.00 28.01  ? 266 ALA B CB    1 
ATOM   6168 N N     . GLY B 1 267 ? 43.750 -4.052  -31.129 1.00 29.90  ? 267 GLY B N     1 
ATOM   6169 C CA    . GLY B 1 267 ? 42.881 -3.366  -32.067 1.00 28.97  ? 267 GLY B CA    1 
ATOM   6170 C C     . GLY B 1 267 ? 43.271 -1.907  -32.294 1.00 27.43  ? 267 GLY B C     1 
ATOM   6171 O O     . GLY B 1 267 ? 42.442 -1.119  -32.747 1.00 28.89  ? 267 GLY B O     1 
ATOM   6172 N N     . VAL B 1 268 ? 44.531 -1.563  -32.034 1.00 26.62  ? 268 VAL B N     1 
ATOM   6173 C CA    . VAL B 1 268 ? 45.031 -0.216  -32.266 1.00 28.83  ? 268 VAL B CA    1 
ATOM   6174 C C     . VAL B 1 268 ? 45.124 0.064   -33.771 1.00 28.45  ? 268 VAL B C     1 
ATOM   6175 O O     . VAL B 1 268 ? 44.748 1.132   -34.250 1.00 28.89  ? 268 VAL B O     1 
ATOM   6176 C CB    . VAL B 1 268 ? 46.384 -0.025  -31.564 1.00 29.75  ? 268 VAL B CB    1 
ATOM   6177 C CG1   . VAL B 1 268 ? 47.028 1.300   -31.929 1.00 30.76  ? 268 VAL B CG1   1 
ATOM   6178 C CG2   . VAL B 1 268 ? 46.211 -0.163  -30.056 1.00 30.77  ? 268 VAL B CG2   1 
ATOM   6179 N N     . ILE B 1 269 ? 45.617 -0.911  -34.526 1.00 26.76  ? 269 ILE B N     1 
ATOM   6180 C CA    . ILE B 1 269 ? 45.470 -0.874  -35.971 1.00 25.58  ? 269 ILE B CA    1 
ATOM   6181 C C     . ILE B 1 269 ? 44.062 -1.363  -36.304 1.00 24.24  ? 269 ILE B C     1 
ATOM   6182 O O     . ILE B 1 269 ? 43.700 -2.466  -35.919 1.00 24.83  ? 269 ILE B O     1 
ATOM   6183 C CB    . ILE B 1 269 ? 46.569 -1.719  -36.641 1.00 24.81  ? 269 ILE B CB    1 
ATOM   6184 C CG1   . ILE B 1 269 ? 47.939 -1.088  -36.392 1.00 24.27  ? 269 ILE B CG1   1 
ATOM   6185 C CG2   . ILE B 1 269 ? 46.266 -1.899  -38.123 1.00 24.68  ? 269 ILE B CG2   1 
ATOM   6186 C CD1   . ILE B 1 269 ? 49.133 -1.911  -36.833 1.00 25.37  ? 269 ILE B CD1   1 
ATOM   6187 N N     . GLN B 1 270 ? 43.262 -0.533  -36.983 1.00 24.43  ? 270 GLN B N     1 
ATOM   6188 C CA    . GLN B 1 270 ? 41.830 -0.765  -37.059 1.00 24.74  ? 270 GLN B CA    1 
ATOM   6189 C C     . GLN B 1 270 ? 41.437 -1.607  -38.282 1.00 25.58  ? 270 GLN B C     1 
ATOM   6190 O O     . GLN B 1 270 ? 40.370 -2.227  -38.278 1.00 24.09  ? 270 GLN B O     1 
ATOM   6191 C CB    . GLN B 1 270 ? 41.077 0.558   -37.101 1.00 24.66  ? 270 GLN B CB    1 
ATOM   6192 C CG    . GLN B 1 270 ? 41.116 1.371   -35.814 1.00 25.69  ? 270 GLN B CG    1 
ATOM   6193 C CD    . GLN B 1 270 ? 40.900 2.830   -36.140 1.00 25.56  ? 270 GLN B CD    1 
ATOM   6194 O OE1   . GLN B 1 270 ? 41.735 3.468   -36.778 1.00 30.35  ? 270 GLN B OE1   1 
ATOM   6195 N NE2   . GLN B 1 270 ? 39.764 3.366   -35.750 1.00 23.56  ? 270 GLN B NE2   1 
ATOM   6196 N N     . ASN B 1 271 ? 42.232 -1.554  -39.356 1.00 25.31  ? 271 ASN B N     1 
ATOM   6197 C CA    . ASN B 1 271 ? 42.000 -2.404  -40.516 1.00 26.34  ? 271 ASN B CA    1 
ATOM   6198 C C     . ASN B 1 271 ? 43.045 -3.513  -40.511 1.00 29.31  ? 271 ASN B C     1 
ATOM   6199 O O     . ASN B 1 271 ? 43.903 -3.558  -39.626 1.00 30.77  ? 271 ASN B O     1 
ATOM   6200 C CB    . ASN B 1 271 ? 42.005 -1.623  -41.837 1.00 24.45  ? 271 ASN B CB    1 
ATOM   6201 C CG    . ASN B 1 271 ? 43.250 -0.796  -42.115 1.00 26.44  ? 271 ASN B CG    1 
ATOM   6202 O OD1   . ASN B 1 271 ? 44.030 -0.437  -41.229 1.00 26.40  ? 271 ASN B OD1   1 
ATOM   6203 N ND2   . ASN B 1 271 ? 43.425 -0.425  -43.368 1.00 25.39  ? 271 ASN B ND2   1 
ATOM   6204 N N     . GLY B 1 272 ? 42.940 -4.410  -41.499 1.00 32.27  ? 272 GLY B N     1 
ATOM   6205 C CA    . GLY B 1 272 ? 43.973 -5.380  -41.798 1.00 32.11  ? 272 GLY B CA    1 
ATOM   6206 C C     . GLY B 1 272 ? 45.312 -4.689  -42.049 1.00 36.51  ? 272 GLY B C     1 
ATOM   6207 O O     . GLY B 1 272 ? 45.374 -3.690  -42.765 1.00 39.61  ? 272 GLY B O     1 
ATOM   6208 N N     . ALA B 1 273 ? 46.366 -5.246  -41.427 1.00 39.94  ? 273 ALA B N     1 
ATOM   6209 C CA    . ALA B 1 273 ? 47.746 -4.827  -41.636 1.00 40.71  ? 273 ALA B CA    1 
ATOM   6210 C C     . ALA B 1 273 ? 48.319 -5.593  -42.825 1.00 38.81  ? 273 ALA B C     1 
ATOM   6211 O O     . ALA B 1 273 ? 48.276 -6.822  -42.857 1.00 42.28  ? 273 ALA B O     1 
ATOM   6212 C CB    . ALA B 1 273 ? 48.581 -5.072  -40.394 1.00 37.41  ? 273 ALA B CB    1 
ATOM   6213 N N     . THR B 1 274 ? 48.844 -4.848  -43.793 1.00 36.91  ? 274 THR B N     1 
ATOM   6214 C CA    . THR B 1 274 ? 49.453 -5.432  -44.971 1.00 38.10  ? 274 THR B CA    1 
ATOM   6215 C C     . THR B 1 274 ? 50.838 -4.819  -45.069 1.00 31.01  ? 274 THR B C     1 
ATOM   6216 O O     . THR B 1 274 ? 50.951 -3.609  -45.150 1.00 27.12  ? 274 THR B O     1 
ATOM   6217 C CB    . THR B 1 274 ? 48.618 -5.177  -46.238 1.00 41.20  ? 274 THR B CB    1 
ATOM   6218 O OG1   . THR B 1 274 ? 48.951 -3.887  -46.756 1.00 52.03  ? 274 THR B OG1   1 
ATOM   6219 C CG2   . THR B 1 274 ? 47.127 -5.240  -45.981 1.00 43.53  ? 274 THR B CG2   1 
ATOM   6220 N N     . VAL B 1 275 ? 51.865 -5.665  -45.053 1.00 29.43  ? 275 VAL B N     1 
ATOM   6221 C CA    . VAL B 1 275 ? 53.220 -5.202  -45.240 1.00 31.30  ? 275 VAL B CA    1 
ATOM   6222 C C     . VAL B 1 275 ? 53.752 -5.798  -46.537 1.00 29.29  ? 275 VAL B C     1 
ATOM   6223 O O     . VAL B 1 275 ? 54.174 -6.939  -46.553 1.00 30.13  ? 275 VAL B O     1 
ATOM   6224 C CB    . VAL B 1 275 ? 54.090 -5.583  -44.028 1.00 31.94  ? 275 VAL B CB    1 
ATOM   6225 C CG1   . VAL B 1 275 ? 55.474 -4.969  -44.144 1.00 33.73  ? 275 VAL B CG1   1 
ATOM   6226 C CG2   . VAL B 1 275 ? 53.420 -5.189  -42.722 1.00 32.05  ? 275 VAL B CG2   1 
ATOM   6227 N N     . ARG B 1 276 ? 53.785 -5.005  -47.606 1.00 29.88  ? 276 ARG B N     1 
ATOM   6228 C CA    . ARG B 1 276 ? 54.115 -5.549  -48.911 1.00 33.16  ? 276 ARG B CA    1 
ATOM   6229 C C     . ARG B 1 276 ? 55.590 -5.324  -49.263 1.00 29.50  ? 276 ARG B C     1 
ATOM   6230 O O     . ARG B 1 276 ? 56.208 -4.314  -48.916 1.00 27.01  ? 276 ARG B O     1 
ATOM   6231 C CB    . ARG B 1 276 ? 53.136 -4.979  -49.939 1.00 37.01  ? 276 ARG B CB    1 
ATOM   6232 C CG    . ARG B 1 276 ? 51.676 -5.234  -49.597 1.00 38.70  ? 276 ARG B CG    1 
ATOM   6233 C CD    . ARG B 1 276 ? 50.724 -4.261  -50.266 1.00 45.05  ? 276 ARG B CD    1 
ATOM   6234 N NE    . ARG B 1 276 ? 50.264 -4.760  -51.543 1.00 52.70  ? 276 ARG B NE    1 
ATOM   6235 C CZ    . ARG B 1 276 ? 49.073 -5.319  -51.742 1.00 61.40  ? 276 ARG B CZ    1 
ATOM   6236 N NH1   . ARG B 1 276 ? 48.169 -5.301  -50.775 1.00 66.28  ? 276 ARG B NH1   1 
ATOM   6237 N NH2   . ARG B 1 276 ? 48.792 -5.893  -52.904 1.00 58.64  ? 276 ARG B NH2   1 
ATOM   6238 N N     . SER B 1 277 ? 56.143 -6.324  -49.957 1.00 27.67  ? 277 SER B N     1 
ATOM   6239 C CA    . SER B 1 277 ? 57.524 -6.320  -50.421 1.00 27.11  ? 277 SER B CA    1 
ATOM   6240 C C     . SER B 1 277 ? 57.694 -5.347  -51.589 1.00 29.91  ? 277 SER B C     1 
ATOM   6241 O O     . SER B 1 277 ? 56.722 -4.952  -52.250 1.00 32.15  ? 277 SER B O     1 
ATOM   6242 C CB    . SER B 1 277 ? 57.958 -7.724  -50.808 1.00 27.00  ? 277 SER B CB    1 
ATOM   6243 O OG    . SER B 1 277 ? 57.409 -8.138  -52.066 1.00 26.41  ? 277 SER B OG    1 
ATOM   6244 N N     . LEU B 1 278 ? 58.955 -4.998  -51.860 1.00 31.45  ? 278 LEU B N     1 
ATOM   6245 C CA    . LEU B 1 278 ? 59.294 -3.951  -52.816 1.00 30.93  ? 278 LEU B CA    1 
ATOM   6246 C C     . LEU B 1 278 ? 58.673 -4.210  -54.182 1.00 28.71  ? 278 LEU B C     1 
ATOM   6247 O O     . LEU B 1 278 ? 57.995 -3.360  -54.731 1.00 30.55  ? 278 LEU B O     1 
ATOM   6248 C CB    . LEU B 1 278 ? 60.817 -3.886  -52.914 1.00 34.12  ? 278 LEU B CB    1 
ATOM   6249 C CG    . LEU B 1 278 ? 61.392 -2.963  -53.985 1.00 35.33  ? 278 LEU B CG    1 
ATOM   6250 C CD1   . LEU B 1 278 ? 60.888 -1.536  -53.826 1.00 35.12  ? 278 LEU B CD1   1 
ATOM   6251 C CD2   . LEU B 1 278 ? 62.906 -3.003  -53.922 1.00 35.02  ? 278 LEU B CD2   1 
ATOM   6252 N N     . VAL B 1 279 ? 58.896 -5.396  -54.739 1.00 29.54  ? 279 VAL B N     1 
ATOM   6253 C CA    . VAL B 1 279 ? 58.534 -5.635  -56.124 1.00 28.06  ? 279 VAL B CA    1 
ATOM   6254 C C     . VAL B 1 279 ? 57.017 -5.678  -56.265 1.00 28.51  ? 279 VAL B C     1 
ATOM   6255 O O     . VAL B 1 279 ? 56.476 -5.253  -57.278 1.00 33.11  ? 279 VAL B O     1 
ATOM   6256 C CB    . VAL B 1 279 ? 59.178 -6.928  -56.648 1.00 29.09  ? 279 VAL B CB    1 
ATOM   6257 C CG1   . VAL B 1 279 ? 58.752 -7.233  -58.089 1.00 27.42  ? 279 VAL B CG1   1 
ATOM   6258 C CG2   . VAL B 1 279 ? 60.692 -6.869  -56.509 1.00 28.62  ? 279 VAL B CG2   1 
ATOM   6259 N N     . LEU B 1 280 ? 56.322 -6.214  -55.267 1.00 27.65  ? 280 LEU B N     1 
ATOM   6260 C CA    . LEU B 1 280 ? 54.868 -6.235  -55.329 1.00 29.31  ? 280 LEU B CA    1 
ATOM   6261 C C     . LEU B 1 280 ? 54.301 -4.819  -55.341 1.00 27.92  ? 280 LEU B C     1 
ATOM   6262 O O     . LEU B 1 280 ? 53.370 -4.527  -56.070 1.00 27.50  ? 280 LEU B O     1 
ATOM   6263 C CB    . LEU B 1 280 ? 54.324 -7.012  -54.131 1.00 30.64  ? 280 LEU B CB    1 
ATOM   6264 C CG    . LEU B 1 280 ? 52.805 -7.127  -54.068 1.00 29.70  ? 280 LEU B CG    1 
ATOM   6265 C CD1   . LEU B 1 280 ? 52.256 -7.780  -55.319 1.00 30.08  ? 280 LEU B CD1   1 
ATOM   6266 C CD2   . LEU B 1 280 ? 52.404 -7.923  -52.843 1.00 32.22  ? 280 LEU B CD2   1 
ATOM   6267 N N     . ASP B 1 281 ? 54.818 -3.952  -54.478 1.00 31.47  ? 281 ASP B N     1 
ATOM   6268 C CA    . ASP B 1 281 ? 54.366 -2.576  -54.489 1.00 33.89  ? 281 ASP B CA    1 
ATOM   6269 C C     . ASP B 1 281 ? 54.853 -1.916  -55.776 1.00 32.30  ? 281 ASP B C     1 
ATOM   6270 O O     . ASP B 1 281 ? 54.068 -1.257  -56.444 1.00 32.99  ? 281 ASP B O     1 
ATOM   6271 C CB    . ASP B 1 281 ? 54.748 -1.839  -53.203 1.00 36.45  ? 281 ASP B CB    1 
ATOM   6272 C CG    . ASP B 1 281 ? 53.769 -2.081  -52.061 1.00 42.69  ? 281 ASP B CG    1 
ATOM   6273 O OD1   . ASP B 1 281 ? 52.537 -2.161  -52.330 1.00 47.47  ? 281 ASP B OD1   1 
ATOM   6274 O OD2   . ASP B 1 281 ? 54.228 -2.169  -50.893 1.00 44.42  ? 281 ASP B OD2   1 
ATOM   6275 N N     . ALA B 1 282 ? 56.112 -2.141  -56.173 1.00 30.18  ? 282 ALA B N     1 
ATOM   6276 C CA    . ALA B 1 282 ? 56.633 -1.469  -57.358 1.00 32.30  ? 282 ALA B CA    1 
ATOM   6277 C C     . ALA B 1 282 ? 55.861 -1.859  -58.624 1.00 31.63  ? 282 ALA B C     1 
ATOM   6278 O O     . ALA B 1 282 ? 55.719 -1.039  -59.542 1.00 31.94  ? 282 ALA B O     1 
ATOM   6279 C CB    . ALA B 1 282 ? 58.096 -1.758  -57.514 1.00 33.27  ? 282 ALA B CB    1 
ATOM   6280 N N     . ALA B 1 283 ? 55.332 -3.092  -58.685 1.00 29.51  ? 283 ALA B N     1 
ATOM   6281 C CA    . ALA B 1 283 ? 54.680 -3.554  -59.909 1.00 32.07  ? 283 ALA B CA    1 
ATOM   6282 C C     . ALA B 1 283 ? 53.344 -2.852  -60.143 1.00 31.50  ? 283 ALA B C     1 
ATOM   6283 O O     . ALA B 1 283 ? 52.757 -3.040  -61.188 1.00 30.93  ? 283 ALA B O     1 
ATOM   6284 C CB    . ALA B 1 283 ? 54.482 -5.050  -59.903 1.00 32.12  ? 283 ALA B CB    1 
ATOM   6285 N N     . ILE B 1 284 ? 52.842 -2.087  -59.169 1.00 36.39  ? 284 ILE B N     1 
ATOM   6286 C CA    . ILE B 1 284 ? 51.628 -1.302  -59.350 1.00 41.42  ? 284 ILE B CA    1 
ATOM   6287 C C     . ILE B 1 284 ? 51.846 -0.204  -60.402 1.00 44.08  ? 284 ILE B C     1 
ATOM   6288 O O     . ILE B 1 284 ? 50.981 -0.029  -61.256 1.00 46.08  ? 284 ILE B O     1 
ATOM   6289 C CB    . ILE B 1 284 ? 51.134 -0.745  -57.992 1.00 44.21  ? 284 ILE B CB    1 
ATOM   6290 C CG1   . ILE B 1 284 ? 50.688 -1.857  -57.037 1.00 42.15  ? 284 ILE B CG1   1 
ATOM   6291 C CG2   . ILE B 1 284 ? 50.024 0.279   -58.170 1.00 45.96  ? 284 ILE B CG2   1 
ATOM   6292 C CD1   . ILE B 1 284 ? 49.483 -2.640  -57.518 1.00 41.59  ? 284 ILE B CD1   1 
ATOM   6293 N N     . THR B 1 285 ? 53.002 0.491   -60.370 1.00 45.02  ? 285 THR B N     1 
ATOM   6294 C CA    . THR B 1 285 ? 53.251 1.634   -61.244 1.00 45.29  ? 285 THR B CA    1 
ATOM   6295 C C     . THR B 1 285 ? 54.437 1.435   -62.199 1.00 45.78  ? 285 THR B C     1 
ATOM   6296 O O     . THR B 1 285 ? 54.780 2.371   -62.908 1.00 43.94  ? 285 THR B O     1 
ATOM   6297 C CB    . THR B 1 285 ? 53.490 2.922   -60.441 1.00 46.98  ? 285 THR B CB    1 
ATOM   6298 O OG1   . THR B 1 285 ? 54.736 2.839   -59.753 1.00 46.85  ? 285 THR B OG1   1 
ATOM   6299 C CG2   . THR B 1 285 ? 52.404 3.227   -59.431 1.00 49.92  ? 285 THR B CG2   1 
ATOM   6300 N N     . ARG B 1 286 ? 55.054 0.242   -62.259 1.00 44.21  ? 286 ARG B N     1 
ATOM   6301 C CA    . ARG B 1 286 ? 56.312 0.085   -62.976 1.00 37.44  ? 286 ARG B CA    1 
ATOM   6302 C C     . ARG B 1 286 ? 56.475 -1.340  -63.499 1.00 37.49  ? 286 ARG B C     1 
ATOM   6303 O O     . ARG B 1 286 ? 55.882 -2.271  -62.962 1.00 34.72  ? 286 ARG B O     1 
ATOM   6304 C CB    . ARG B 1 286 ? 57.490 0.359   -62.039 1.00 38.68  ? 286 ARG B CB    1 
ATOM   6305 C CG    . ARG B 1 286 ? 57.728 1.812   -61.670 1.00 42.79  ? 286 ARG B CG    1 
ATOM   6306 C CD    . ARG B 1 286 ? 58.165 2.666   -62.853 1.00 44.53  ? 286 ARG B CD    1 
ATOM   6307 N NE    . ARG B 1 286 ? 58.392 4.065   -62.498 1.00 43.50  ? 286 ARG B NE    1 
ATOM   6308 C CZ    . ARG B 1 286 ? 57.447 4.929   -62.131 1.00 44.81  ? 286 ARG B CZ    1 
ATOM   6309 N NH1   . ARG B 1 286 ? 56.174 4.577   -62.134 1.00 45.56  ? 286 ARG B NH1   1 
ATOM   6310 N NH2   . ARG B 1 286 ? 57.779 6.146   -61.738 1.00 44.58  ? 286 ARG B NH2   1 
ATOM   6311 N N     . THR B 1 287 ? 57.324 -1.514  -64.522 1.00 38.35  ? 287 THR B N     1 
ATOM   6312 C CA    . THR B 1 287 ? 57.687 -2.845  -64.995 1.00 39.07  ? 287 THR B CA    1 
ATOM   6313 C C     . THR B 1 287 ? 59.176 -3.121  -64.800 1.00 37.48  ? 287 THR B C     1 
ATOM   6314 O O     . THR B 1 287 ? 59.998 -2.201  -64.706 1.00 36.30  ? 287 THR B O     1 
ATOM   6315 C CB    . THR B 1 287 ? 57.311 -3.033  -66.463 1.00 39.18  ? 287 THR B CB    1 
ATOM   6316 O OG1   . THR B 1 287 ? 58.256 -2.296  -67.246 1.00 40.29  ? 287 THR B OG1   1 
ATOM   6317 C CG2   . THR B 1 287 ? 55.888 -2.592  -66.717 1.00 37.53  ? 287 THR B CG2   1 
ATOM   6318 N N     . LYS B 1 288 ? 59.506 -4.417  -64.739 1.00 38.26  ? 288 LYS B N     1 
ATOM   6319 C CA    . LYS B 1 288 ? 60.880 -4.844  -64.515 1.00 37.80  ? 288 LYS B CA    1 
ATOM   6320 C C     . LYS B 1 288 ? 61.791 -4.195  -65.554 1.00 37.01  ? 288 LYS B C     1 
ATOM   6321 O O     . LYS B 1 288 ? 62.841 -3.662  -65.205 1.00 36.72  ? 288 LYS B O     1 
ATOM   6322 C CB    . LYS B 1 288 ? 61.017 -6.363  -64.601 1.00 36.31  ? 288 LYS B CB    1 
ATOM   6323 C CG    . LYS B 1 288 ? 62.320 -6.914  -64.041 1.00 40.14  ? 288 LYS B CG    1 
ATOM   6324 C CD    . LYS B 1 288 ? 62.422 -8.435  -64.040 1.00 42.09  ? 288 LYS B CD    1 
ATOM   6325 C CE    . LYS B 1 288 ? 62.639 -9.004  -65.422 1.00 45.47  ? 288 LYS B CE    1 
ATOM   6326 N NZ    . LYS B 1 288 ? 62.903 -10.464 -65.392 1.00 46.86  ? 288 LYS B NZ    1 
ATOM   6327 N N     . SER B 1 289 ? 61.329 -4.228  -66.807 1.00 39.61  ? 289 SER B N     1 
ATOM   6328 C CA    . SER B 1 289 ? 62.075 -3.783  -67.972 1.00 45.26  ? 289 SER B CA    1 
ATOM   6329 C C     . SER B 1 289 ? 62.557 -2.337  -67.822 1.00 48.06  ? 289 SER B C     1 
ATOM   6330 O O     . SER B 1 289 ? 63.556 -1.987  -68.441 1.00 54.61  ? 289 SER B O     1 
ATOM   6331 C CB    . SER B 1 289 ? 61.269 -3.995  -69.263 1.00 46.26  ? 289 SER B CB    1 
ATOM   6332 O OG    . SER B 1 289 ? 60.091 -3.187  -69.331 1.00 44.07  ? 289 SER B OG    1 
ATOM   6333 N N     . GLN B 1 290 ? 61.896 -1.523  -66.979 1.00 41.82  ? 290 GLN B N     1 
ATOM   6334 C CA    . GLN B 1 290 ? 62.263 -0.122  -66.813 1.00 40.99  ? 290 GLN B CA    1 
ATOM   6335 C C     . GLN B 1 290 ? 63.462 0.041   -65.876 1.00 44.73  ? 290 GLN B C     1 
ATOM   6336 O O     . GLN B 1 290 ? 63.927 1.165   -65.670 1.00 44.06  ? 290 GLN B O     1 
ATOM   6337 C CB    . GLN B 1 290 ? 61.113 0.720   -66.238 1.00 38.07  ? 290 GLN B CB    1 
ATOM   6338 C CG    . GLN B 1 290 ? 59.826 0.720   -67.053 1.00 39.69  ? 290 GLN B CG    1 
ATOM   6339 C CD    . GLN B 1 290 ? 58.744 1.528   -66.366 1.00 45.07  ? 290 GLN B CD    1 
ATOM   6340 O OE1   . GLN B 1 290 ? 57.972 1.037   -65.545 1.00 47.73  ? 290 GLN B OE1   1 
ATOM   6341 N NE2   . GLN B 1 290 ? 58.716 2.816   -66.642 1.00 43.29  ? 290 GLN B NE2   1 
ATOM   6342 N N     . TYR B 1 291 ? 63.921 -1.055  -65.256 1.00 48.70  ? 291 TYR B N     1 
ATOM   6343 C CA    . TYR B 1 291 ? 65.028 -1.008  -64.310 1.00 45.61  ? 291 TYR B CA    1 
ATOM   6344 C C     . TYR B 1 291 ? 66.120 -2.032  -64.624 1.00 44.69  ? 291 TYR B C     1 
ATOM   6345 O O     . TYR B 1 291 ? 67.205 -1.938  -64.049 1.00 42.46  ? 291 TYR B O     1 
ATOM   6346 C CB    . TYR B 1 291 ? 64.534 -1.303  -62.894 1.00 46.63  ? 291 TYR B CB    1 
ATOM   6347 C CG    . TYR B 1 291 ? 63.667 -0.230  -62.298 1.00 42.02  ? 291 TYR B CG    1 
ATOM   6348 C CD1   . TYR B 1 291 ? 64.220 0.929   -61.790 1.00 37.99  ? 291 TYR B CD1   1 
ATOM   6349 C CD2   . TYR B 1 291 ? 62.290 -0.381  -62.230 1.00 40.24  ? 291 TYR B CD2   1 
ATOM   6350 C CE1   . TYR B 1 291 ? 63.420 1.918   -61.237 1.00 39.20  ? 291 TYR B CE1   1 
ATOM   6351 C CE2   . TYR B 1 291 ? 61.477 0.603   -61.692 1.00 38.88  ? 291 TYR B CE2   1 
ATOM   6352 C CZ    . TYR B 1 291 ? 62.044 1.760   -61.194 1.00 38.19  ? 291 TYR B CZ    1 
ATOM   6353 O OH    . TYR B 1 291 ? 61.240 2.741   -60.653 1.00 40.83  ? 291 TYR B OH    1 
ATOM   6354 N N     . TYR B 1 292 ? 65.838 -3.015  -65.493 1.00 43.51  ? 292 TYR B N     1 
ATOM   6355 C CA    . TYR B 1 292 ? 66.643 -4.224  -65.552 1.00 48.60  ? 292 TYR B CA    1 
ATOM   6356 C C     . TYR B 1 292 ? 66.390 -4.968  -66.862 1.00 51.16  ? 292 TYR B C     1 
ATOM   6357 O O     . TYR B 1 292 ? 65.232 -5.212  -67.195 1.00 54.11  ? 292 TYR B O     1 
ATOM   6358 C CB    . TYR B 1 292 ? 66.333 -5.086  -64.322 1.00 50.75  ? 292 TYR B CB    1 
ATOM   6359 C CG    . TYR B 1 292 ? 67.163 -6.339  -64.206 1.00 53.10  ? 292 TYR B CG    1 
ATOM   6360 C CD1   . TYR B 1 292 ? 68.549 -6.279  -64.253 1.00 54.97  ? 292 TYR B CD1   1 
ATOM   6361 C CD2   . TYR B 1 292 ? 66.568 -7.587  -64.058 1.00 53.05  ? 292 TYR B CD2   1 
ATOM   6362 C CE1   . TYR B 1 292 ? 69.321 -7.427  -64.171 1.00 56.26  ? 292 TYR B CE1   1 
ATOM   6363 C CE2   . TYR B 1 292 ? 67.325 -8.744  -63.966 1.00 49.74  ? 292 TYR B CE2   1 
ATOM   6364 C CZ    . TYR B 1 292 ? 68.707 -8.660  -64.023 1.00 52.82  ? 292 TYR B CZ    1 
ATOM   6365 O OH    . TYR B 1 292 ? 69.486 -9.786  -63.937 1.00 48.43  ? 292 TYR B OH    1 
ATOM   6366 N N     . ASP B 1 293 ? 67.477 -5.326  -67.579 1.00 57.92  ? 293 ASP B N     1 
ATOM   6367 C CA    . ASP B 1 293 ? 67.405 -5.982  -68.887 1.00 60.12  ? 293 ASP B CA    1 
ATOM   6368 C C     . ASP B 1 293 ? 67.375 -7.499  -68.721 1.00 55.20  ? 293 ASP B C     1 
ATOM   6369 O O     . ASP B 1 293 ? 67.038 -8.226  -69.652 1.00 51.35  ? 293 ASP B O     1 
ATOM   6370 C CB    . ASP B 1 293 ? 68.612 -5.717  -69.803 1.00 67.57  ? 293 ASP B CB    1 
ATOM   6371 C CG    . ASP B 1 293 ? 69.247 -4.337  -69.714 1.00 77.86  ? 293 ASP B CG    1 
ATOM   6372 O OD1   . ASP B 1 293 ? 68.569 -3.340  -70.049 1.00 79.62  ? 293 ASP B OD1   1 
ATOM   6373 O OD2   . ASP B 1 293 ? 70.428 -4.274  -69.321 1.00 75.49  ? 293 ASP B OD2   1 
ATOM   6374 N N     . GLY B 1 294 ? 67.745 -7.982  -67.533 1.00 54.41  ? 294 GLY B N     1 
ATOM   6375 C CA    . GLY B 1 294 ? 67.878 -9.413  -67.310 1.00 60.19  ? 294 GLY B CA    1 
ATOM   6376 C C     . GLY B 1 294 ? 66.594 -10.202 -67.558 1.00 62.01  ? 294 GLY B C     1 
ATOM   6377 O O     . GLY B 1 294 ? 65.478 -9.678  -67.505 1.00 60.60  ? 294 GLY B O     1 
ATOM   6378 N N     . ASP B 1 295 ? 66.786 -11.500 -67.793 1.00 62.53  ? 295 ASP B N     1 
ATOM   6379 C CA    . ASP B 1 295 ? 65.689 -12.415 -68.041 1.00 65.81  ? 295 ASP B CA    1 
ATOM   6380 C C     . ASP B 1 295 ? 65.099 -12.846 -66.699 1.00 62.38  ? 295 ASP B C     1 
ATOM   6381 O O     . ASP B 1 295 ? 63.899 -13.090 -66.592 1.00 66.22  ? 295 ASP B O     1 
ATOM   6382 C CB    . ASP B 1 295 ? 66.183 -13.590 -68.889 1.00 72.93  ? 295 ASP B CB    1 
ATOM   6383 C CG    . ASP B 1 295 ? 65.130 -14.185 -69.806 1.00 83.57  ? 295 ASP B CG    1 
ATOM   6384 O OD1   . ASP B 1 295 ? 64.377 -13.397 -70.408 1.00 92.17  ? 295 ASP B OD1   1 
ATOM   6385 O OD2   . ASP B 1 295 ? 65.111 -15.425 -69.951 1.00 93.35  ? 295 ASP B OD2   1 
ATOM   6386 N N     . GLY B 1 296 ? 65.941 -12.912 -65.663 1.00 51.45  ? 296 GLY B N     1 
ATOM   6387 C CA    . GLY B 1 296 ? 65.519 -13.484 -64.396 1.00 49.96  ? 296 GLY B CA    1 
ATOM   6388 C C     . GLY B 1 296 ? 65.033 -12.454 -63.370 1.00 49.00  ? 296 GLY B C     1 
ATOM   6389 O O     . GLY B 1 296 ? 64.694 -11.307 -63.670 1.00 43.52  ? 296 GLY B O     1 
ATOM   6390 N N     . PRO B 1 297 ? 64.961 -12.857 -62.089 1.00 41.55  ? 297 PRO B N     1 
ATOM   6391 C CA    . PRO B 1 297 ? 64.592 -11.936 -61.021 1.00 39.27  ? 297 PRO B CA    1 
ATOM   6392 C C     . PRO B 1 297 ? 65.638 -10.845 -60.775 1.00 37.80  ? 297 PRO B C     1 
ATOM   6393 O O     . PRO B 1 297 ? 66.782 -10.943 -61.191 1.00 42.66  ? 297 PRO B O     1 
ATOM   6394 C CB    . PRO B 1 297 ? 64.433 -12.879 -59.818 1.00 40.51  ? 297 PRO B CB    1 
ATOM   6395 C CG    . PRO B 1 297 ? 65.313 -14.052 -60.118 1.00 40.26  ? 297 PRO B CG    1 
ATOM   6396 C CD    . PRO B 1 297 ? 65.216 -14.225 -61.616 1.00 41.76  ? 297 PRO B CD    1 
ATOM   6397 N N     . ILE B 1 298 ? 65.238 -9.784  -60.086 1.00 37.57  ? 298 ILE B N     1 
ATOM   6398 C CA    . ILE B 1 298 ? 66.086 -8.612  -59.989 1.00 37.74  ? 298 ILE B CA    1 
ATOM   6399 C C     . ILE B 1 298 ? 67.214 -8.932  -59.024 1.00 40.28  ? 298 ILE B C     1 
ATOM   6400 O O     . ILE B 1 298 ? 67.034 -9.709  -58.081 1.00 38.59  ? 298 ILE B O     1 
ATOM   6401 C CB    . ILE B 1 298 ? 65.307 -7.345  -59.564 1.00 35.84  ? 298 ILE B CB    1 
ATOM   6402 C CG1   . ILE B 1 298 ? 64.702 -7.432  -58.159 1.00 34.59  ? 298 ILE B CG1   1 
ATOM   6403 C CG2   . ILE B 1 298 ? 64.240 -7.014  -60.593 1.00 39.34  ? 298 ILE B CG2   1 
ATOM   6404 C CD1   . ILE B 1 298 ? 64.295 -6.086  -57.595 1.00 35.52  ? 298 ILE B CD1   1 
ATOM   6405 N N     . PRO B 1 299 ? 68.393 -8.303  -59.233 1.00 41.01  ? 299 PRO B N     1 
ATOM   6406 C CA    . PRO B 1 299 ? 69.488 -8.358  -58.272 1.00 39.06  ? 299 PRO B CA    1 
ATOM   6407 C C     . PRO B 1 299 ? 69.392 -7.244  -57.236 1.00 42.05  ? 299 PRO B C     1 
ATOM   6408 O O     . PRO B 1 299 ? 68.615 -6.299  -57.394 1.00 43.40  ? 299 PRO B O     1 
ATOM   6409 C CB    . PRO B 1 299 ? 70.689 -8.179  -59.197 1.00 41.15  ? 299 PRO B CB    1 
ATOM   6410 C CG    . PRO B 1 299 ? 70.202 -7.193  -60.232 1.00 41.37  ? 299 PRO B CG    1 
ATOM   6411 C CD    . PRO B 1 299 ? 68.738 -7.524  -60.430 1.00 41.01  ? 299 PRO B CD    1 
ATOM   6412 N N     . PRO B 1 300 ? 70.173 -7.333  -56.134 1.00 41.58  ? 300 PRO B N     1 
ATOM   6413 C CA    . PRO B 1 300 ? 70.114 -6.333  -55.064 1.00 40.93  ? 300 PRO B CA    1 
ATOM   6414 C C     . PRO B 1 300 ? 70.359 -4.886  -55.498 1.00 43.34  ? 300 PRO B C     1 
ATOM   6415 O O     . PRO B 1 300 ? 69.799 -3.958  -54.924 1.00 46.69  ? 300 PRO B O     1 
ATOM   6416 C CB    . PRO B 1 300 ? 71.209 -6.805  -54.088 1.00 38.35  ? 300 PRO B CB    1 
ATOM   6417 C CG    . PRO B 1 300 ? 71.296 -8.296  -54.329 1.00 38.32  ? 300 PRO B CG    1 
ATOM   6418 C CD    . PRO B 1 300 ? 71.091 -8.447  -55.825 1.00 39.59  ? 300 PRO B CD    1 
ATOM   6419 N N     . SER B 1 301 ? 71.213 -4.679  -56.500 1.00 44.87  ? 301 SER B N     1 
ATOM   6420 C CA    . SER B 1 301 ? 71.544 -3.329  -56.926 1.00 43.92  ? 301 SER B CA    1 
ATOM   6421 C C     . SER B 1 301 ? 70.320 -2.664  -57.547 1.00 38.93  ? 301 SER B C     1 
ATOM   6422 O O     . SER B 1 301 ? 70.103 -1.474  -57.368 1.00 37.15  ? 301 SER B O     1 
ATOM   6423 C CB    . SER B 1 301 ? 72.705 -3.331  -57.884 1.00 45.70  ? 301 SER B CB    1 
ATOM   6424 O OG    . SER B 1 301 ? 72.397 -4.127  -59.011 1.00 47.39  ? 301 SER B OG    1 
ATOM   6425 N N     . VAL B 1 302 ? 69.514 -3.437  -58.277 1.00 40.86  ? 302 VAL B N     1 
ATOM   6426 C CA    . VAL B 1 302 ? 68.293 -2.897  -58.861 1.00 42.16  ? 302 VAL B CA    1 
ATOM   6427 C C     . VAL B 1 302 ? 67.288 -2.549  -57.765 1.00 41.86  ? 302 VAL B C     1 
ATOM   6428 O O     . VAL B 1 302 ? 66.614 -1.533  -57.839 1.00 43.53  ? 302 VAL B O     1 
ATOM   6429 C CB    . VAL B 1 302 ? 67.685 -3.884  -59.861 1.00 42.03  ? 302 VAL B CB    1 
ATOM   6430 C CG1   . VAL B 1 302 ? 66.260 -3.491  -60.228 1.00 45.05  ? 302 VAL B CG1   1 
ATOM   6431 C CG2   . VAL B 1 302 ? 68.572 -4.001  -61.094 1.00 44.63  ? 302 VAL B CG2   1 
ATOM   6432 N N     . ALA B 1 303 ? 67.199 -3.408  -56.754 1.00 38.50  ? 303 ALA B N     1 
ATOM   6433 C CA    . ALA B 1 303 ? 66.285 -3.196  -55.655 1.00 37.88  ? 303 ALA B CA    1 
ATOM   6434 C C     . ALA B 1 303 ? 66.522 -1.824  -55.032 1.00 38.73  ? 303 ALA B C     1 
ATOM   6435 O O     . ALA B 1 303 ? 65.561 -1.096  -54.794 1.00 38.57  ? 303 ALA B O     1 
ATOM   6436 C CB    . ALA B 1 303 ? 66.450 -4.323  -54.661 1.00 40.10  ? 303 ALA B CB    1 
ATOM   6437 N N     . LYS B 1 304 ? 67.795 -1.480  -54.781 1.00 43.78  ? 304 LYS B N     1 
ATOM   6438 C CA    . LYS B 1 304 ? 68.174 -0.210  -54.161 1.00 45.41  ? 304 LYS B CA    1 
ATOM   6439 C C     . LYS B 1 304 ? 67.807 0.971   -55.061 1.00 41.57  ? 304 LYS B C     1 
ATOM   6440 O O     . LYS B 1 304 ? 67.324 1.976   -54.561 1.00 45.48  ? 304 LYS B O     1 
ATOM   6441 C CB    . LYS B 1 304 ? 69.677 -0.125  -53.869 1.00 51.45  ? 304 LYS B CB    1 
ATOM   6442 C CG    . LYS B 1 304 ? 70.198 -0.893  -52.657 1.00 60.59  ? 304 LYS B CG    1 
ATOM   6443 C CD    . LYS B 1 304 ? 71.710 -0.669  -52.476 1.00 76.22  ? 304 LYS B CD    1 
ATOM   6444 C CE    . LYS B 1 304 ? 72.305 -1.128  -51.156 1.00 80.50  ? 304 LYS B CE    1 
ATOM   6445 N NZ    . LYS B 1 304 ? 72.765 -2.538  -51.192 1.00 78.67  ? 304 LYS B NZ    1 
ATOM   6446 N N     . THR B 1 305 ? 68.038 0.850   -56.376 1.00 41.60  ? 305 THR B N     1 
ATOM   6447 C CA    . THR B 1 305 ? 67.550 1.811   -57.362 1.00 45.56  ? 305 THR B CA    1 
ATOM   6448 C C     . THR B 1 305 ? 66.047 2.051   -57.169 1.00 47.36  ? 305 THR B C     1 
ATOM   6449 O O     . THR B 1 305 ? 65.614 3.151   -56.831 1.00 50.10  ? 305 THR B O     1 
ATOM   6450 C CB    . THR B 1 305 ? 67.850 1.330   -58.793 1.00 45.29  ? 305 THR B CB    1 
ATOM   6451 O OG1   . THR B 1 305 ? 69.242 1.076   -58.903 1.00 44.68  ? 305 THR B OG1   1 
ATOM   6452 C CG2   . THR B 1 305 ? 67.494 2.315   -59.883 1.00 46.55  ? 305 THR B CG2   1 
ATOM   6453 N N     . MET B 1 306 ? 65.254 0.991   -57.346 1.00 49.06  ? 306 MET B N     1 
ATOM   6454 C CA    . MET B 1 306 ? 63.801 1.062   -57.267 1.00 43.96  ? 306 MET B CA    1 
ATOM   6455 C C     . MET B 1 306 ? 63.342 1.765   -55.991 1.00 39.20  ? 306 MET B C     1 
ATOM   6456 O O     . MET B 1 306 ? 62.443 2.593   -56.029 1.00 42.61  ? 306 MET B O     1 
ATOM   6457 C CB    . MET B 1 306 ? 63.225 -0.353  -57.309 1.00 44.76  ? 306 MET B CB    1 
ATOM   6458 C CG    . MET B 1 306 ? 63.188 -0.928  -58.701 1.00 44.10  ? 306 MET B CG    1 
ATOM   6459 S SD    . MET B 1 306 ? 62.804 -2.686  -58.695 1.00 44.35  ? 306 MET B SD    1 
ATOM   6460 C CE    . MET B 1 306 ? 61.089 -2.604  -58.199 1.00 46.35  ? 306 MET B CE    1 
ATOM   6461 N N     . MET B 1 307 ? 63.965 1.436   -54.860 1.00 39.39  ? 307 MET B N     1 
ATOM   6462 C CA    . MET B 1 307 ? 63.551 1.977   -53.579 1.00 42.26  ? 307 MET B CA    1 
ATOM   6463 C C     . MET B 1 307 ? 63.596 3.497   -53.631 1.00 46.36  ? 307 MET B C     1 
ATOM   6464 O O     . MET B 1 307 ? 62.742 4.151   -53.052 1.00 49.76  ? 307 MET B O     1 
ATOM   6465 C CB    . MET B 1 307 ? 64.457 1.507   -52.435 1.00 41.92  ? 307 MET B CB    1 
ATOM   6466 C CG    . MET B 1 307 ? 64.149 0.108   -51.928 1.00 44.06  ? 307 MET B CG    1 
ATOM   6467 S SD    . MET B 1 307 ? 65.453 -0.535  -50.836 1.00 42.74  ? 307 MET B SD    1 
ATOM   6468 C CE    . MET B 1 307 ? 65.050 0.367   -49.347 1.00 51.31  ? 307 MET B CE    1 
ATOM   6469 N N     . ALA B 1 308 ? 64.624 4.044   -54.288 1.00 52.49  ? 308 ALA B N     1 
ATOM   6470 C CA    . ALA B 1 308 ? 64.869 5.477   -54.265 1.00 53.76  ? 308 ALA B CA    1 
ATOM   6471 C C     . ALA B 1 308 ? 64.052 6.181   -55.351 1.00 43.08  ? 308 ALA B C     1 
ATOM   6472 O O     . ALA B 1 308 ? 63.596 7.295   -55.126 1.00 44.14  ? 308 ALA B O     1 
ATOM   6473 C CB    . ALA B 1 308 ? 66.352 5.753   -54.393 1.00 59.40  ? 308 ALA B CB    1 
ATOM   6474 N N     . ASP B 1 309 ? 63.877 5.537   -56.511 1.00 37.07  ? 309 ASP B N     1 
ATOM   6475 C CA    . ASP B 1 309 ? 62.983 6.032   -57.546 1.00 40.24  ? 309 ASP B CA    1 
ATOM   6476 C C     . ASP B 1 309 ? 61.585 6.234   -56.959 1.00 43.01  ? 309 ASP B C     1 
ATOM   6477 O O     . ASP B 1 309 ? 61.016 7.306   -57.146 1.00 48.49  ? 309 ASP B O     1 
ATOM   6478 C CB    . ASP B 1 309 ? 62.953 5.104   -58.768 1.00 44.91  ? 309 ASP B CB    1 
ATOM   6479 C CG    . ASP B 1 309 ? 62.557 5.778   -60.079 1.00 48.17  ? 309 ASP B CG    1 
ATOM   6480 O OD1   . ASP B 1 309 ? 63.253 6.731   -60.455 1.00 60.09  ? 309 ASP B OD1   1 
ATOM   6481 O OD2   . ASP B 1 309 ? 61.583 5.331   -60.751 1.00 45.32  ? 309 ASP B OD2   1 
ATOM   6482 N N     . LEU B 1 310 ? 61.060 5.237   -56.212 1.00 41.60  ? 310 LEU B N     1 
ATOM   6483 C CA    . LEU B 1 310 ? 59.643 5.169   -55.855 1.00 38.58  ? 310 LEU B CA    1 
ATOM   6484 C C     . LEU B 1 310 ? 59.399 5.568   -54.399 1.00 36.13  ? 310 LEU B C     1 
ATOM   6485 O O     . LEU B 1 310 ? 58.261 5.681   -53.957 1.00 35.52  ? 310 LEU B O     1 
ATOM   6486 C CB    . LEU B 1 310 ? 59.160 3.739   -56.122 1.00 36.45  ? 310 LEU B CB    1 
ATOM   6487 C CG    . LEU B 1 310 ? 59.436 3.237   -57.537 1.00 39.12  ? 310 LEU B CG    1 
ATOM   6488 C CD1   . LEU B 1 310 ? 59.057 1.782   -57.709 1.00 38.86  ? 310 LEU B CD1   1 
ATOM   6489 C CD2   . LEU B 1 310 ? 58.685 4.076   -58.554 1.00 42.84  ? 310 LEU B CD2   1 
ATOM   6490 N N     . ASP B 1 311 ? 60.466 5.802   -53.635 1.00 36.61  ? 311 ASP B N     1 
ATOM   6491 C CA    . ASP B 1 311 ? 60.324 6.049   -52.209 1.00 38.77  ? 311 ASP B CA    1 
ATOM   6492 C C     . ASP B 1 311 ? 59.566 4.891   -51.564 1.00 36.50  ? 311 ASP B C     1 
ATOM   6493 O O     . ASP B 1 311 ? 58.563 5.081   -50.891 1.00 34.08  ? 311 ASP B O     1 
ATOM   6494 C CB    . ASP B 1 311 ? 59.575 7.347   -51.906 1.00 47.48  ? 311 ASP B CB    1 
ATOM   6495 C CG    . ASP B 1 311 ? 60.130 8.609   -52.542 1.00 52.08  ? 311 ASP B CG    1 
ATOM   6496 O OD1   . ASP B 1 311 ? 61.165 8.527   -53.250 1.00 50.90  ? 311 ASP B OD1   1 
ATOM   6497 O OD2   . ASP B 1 311 ? 59.495 9.671   -52.327 1.00 61.04  ? 311 ASP B OD2   1 
ATOM   6498 N N     . LEU B 1 312 ? 60.049 3.675   -51.802 1.00 34.83  ? 312 LEU B N     1 
ATOM   6499 C CA    . LEU B 1 312 ? 59.492 2.495   -51.174 1.00 33.58  ? 312 LEU B CA    1 
ATOM   6500 C C     . LEU B 1 312 ? 60.622 1.841   -50.403 1.00 30.78  ? 312 LEU B C     1 
ATOM   6501 O O     . LEU B 1 312 ? 61.776 2.010   -50.765 1.00 31.22  ? 312 LEU B O     1 
ATOM   6502 C CB    . LEU B 1 312 ? 58.963 1.554   -52.264 1.00 33.29  ? 312 LEU B CB    1 
ATOM   6503 C CG    . LEU B 1 312 ? 57.718 2.031   -53.012 1.00 30.68  ? 312 LEU B CG    1 
ATOM   6504 C CD1   . LEU B 1 312 ? 57.385 1.064   -54.130 1.00 31.19  ? 312 LEU B CD1   1 
ATOM   6505 C CD2   . LEU B 1 312 ? 56.535 2.184   -52.067 1.00 30.73  ? 312 LEU B CD2   1 
ATOM   6506 N N     . GLY B 1 313 ? 60.274 1.070   -49.378 1.00 29.71  ? 313 GLY B N     1 
ATOM   6507 C CA    . GLY B 1 313 ? 61.231 0.204   -48.715 1.00 30.72  ? 313 GLY B CA    1 
ATOM   6508 C C     . GLY B 1 313 ? 61.230 -1.198  -49.318 1.00 30.75  ? 313 GLY B C     1 
ATOM   6509 O O     . GLY B 1 313 ? 60.559 -1.463  -50.309 1.00 31.91  ? 313 GLY B O     1 
ATOM   6510 N N     . MET B 1 314 ? 61.993 -2.092  -48.696 1.00 33.27  ? 314 MET B N     1 
ATOM   6511 C CA    . MET B 1 314 ? 61.942 -3.511  -49.017 1.00 31.01  ? 314 MET B CA    1 
ATOM   6512 C C     . MET B 1 314 ? 60.632 -4.078  -48.484 1.00 30.24  ? 314 MET B C     1 
ATOM   6513 O O     . MET B 1 314 ? 60.163 -5.093  -48.966 1.00 31.14  ? 314 MET B O     1 
ATOM   6514 C CB    . MET B 1 314 ? 63.115 -4.264  -48.375 1.00 30.63  ? 314 MET B CB    1 
ATOM   6515 C CG    . MET B 1 314 ? 64.478 -3.927  -48.971 1.00 32.55  ? 314 MET B CG    1 
ATOM   6516 S SD    . MET B 1 314 ? 64.632 -4.282  -50.731 1.00 38.43  ? 314 MET B SD    1 
ATOM   6517 C CE    . MET B 1 314 ? 63.988 -5.947  -50.848 1.00 40.24  ? 314 MET B CE    1 
ATOM   6518 N N     . TRP B 1 315 ? 60.091 -3.424  -47.452 1.00 29.79  ? 315 TRP B N     1 
ATOM   6519 C CA    . TRP B 1 315 ? 58.827 -3.774  -46.834 1.00 30.66  ? 315 TRP B CA    1 
ATOM   6520 C C     . TRP B 1 315 ? 58.017 -2.503  -46.646 1.00 31.54  ? 315 TRP B C     1 
ATOM   6521 O O     . TRP B 1 315 ? 58.566 -1.518  -46.154 1.00 28.44  ? 315 TRP B O     1 
ATOM   6522 C CB    . TRP B 1 315 ? 59.068 -4.426  -45.479 1.00 31.20  ? 315 TRP B CB    1 
ATOM   6523 C CG    . TRP B 1 315 ? 59.652 -5.789  -45.608 1.00 31.98  ? 315 TRP B CG    1 
ATOM   6524 C CD1   . TRP B 1 315 ? 60.897 -6.189  -45.240 1.00 33.59  ? 315 TRP B CD1   1 
ATOM   6525 C CD2   . TRP B 1 315 ? 59.006 -6.933  -46.175 1.00 31.93  ? 315 TRP B CD2   1 
ATOM   6526 N NE1   . TRP B 1 315 ? 61.066 -7.510  -45.526 1.00 34.27  ? 315 TRP B NE1   1 
ATOM   6527 C CE2   . TRP B 1 315 ? 59.923 -7.998  -46.092 1.00 33.38  ? 315 TRP B CE2   1 
ATOM   6528 C CE3   . TRP B 1 315 ? 57.745 -7.165  -46.730 1.00 31.78  ? 315 TRP B CE3   1 
ATOM   6529 C CZ2   . TRP B 1 315 ? 59.626 -9.276  -46.556 1.00 33.63  ? 315 TRP B CZ2   1 
ATOM   6530 C CZ3   . TRP B 1 315 ? 57.449 -8.433  -47.178 1.00 34.86  ? 315 TRP B CZ3   1 
ATOM   6531 C CH2   . TRP B 1 315 ? 58.379 -9.470  -47.097 1.00 32.60  ? 315 TRP B CH2   1 
ATOM   6532 N N     . ASN B 1 316 ? 56.726 -2.568  -47.002 1.00 29.02  ? 316 ASN B N     1 
ATOM   6533 C CA    . ASN B 1 316 ? 55.882 -1.392  -47.060 1.00 29.23  ? 316 ASN B CA    1 
ATOM   6534 C C     . ASN B 1 316 ? 54.543 -1.675  -46.383 1.00 31.31  ? 316 ASN B C     1 
ATOM   6535 O O     . ASN B 1 316 ? 53.660 -2.324  -46.951 1.00 32.08  ? 316 ASN B O     1 
ATOM   6536 C CB    . ASN B 1 316 ? 55.674 -0.954  -48.504 1.00 28.53  ? 316 ASN B CB    1 
ATOM   6537 C CG    . ASN B 1 316 ? 56.980 -0.718  -49.227 1.00 29.64  ? 316 ASN B CG    1 
ATOM   6538 O OD1   . ASN B 1 316 ? 57.625 0.306   -49.026 1.00 30.96  ? 316 ASN B OD1   1 
ATOM   6539 N ND2   . ASN B 1 316 ? 57.368 -1.643  -50.087 1.00 28.86  ? 316 ASN B ND2   1 
ATOM   6540 N N     . PHE B 1 317 ? 54.400 -1.137  -45.173 1.00 31.56  ? 317 PHE B N     1 
ATOM   6541 C CA    . PHE B 1 317 ? 53.208 -1.313  -44.354 1.00 31.84  ? 317 PHE B CA    1 
ATOM   6542 C C     . PHE B 1 317 ? 52.217 -0.185  -44.641 1.00 33.17  ? 317 PHE B C     1 
ATOM   6543 O O     . PHE B 1 317 ? 52.496 0.975   -44.332 1.00 29.81  ? 317 PHE B O     1 
ATOM   6544 C CB    . PHE B 1 317 ? 53.641 -1.392  -42.889 1.00 31.07  ? 317 PHE B CB    1 
ATOM   6545 C CG    . PHE B 1 317 ? 52.565 -1.204  -41.861 1.00 31.17  ? 317 PHE B CG    1 
ATOM   6546 C CD1   . PHE B 1 317 ? 51.286 -1.691  -42.057 1.00 33.17  ? 317 PHE B CD1   1 
ATOM   6547 C CD2   . PHE B 1 317 ? 52.845 -0.559  -40.668 1.00 33.40  ? 317 PHE B CD2   1 
ATOM   6548 C CE1   . PHE B 1 317 ? 50.312 -1.534  -41.086 1.00 31.90  ? 317 PHE B CE1   1 
ATOM   6549 C CE2   . PHE B 1 317 ? 51.863 -0.405  -39.696 1.00 34.24  ? 317 PHE B CE2   1 
ATOM   6550 C CZ    . PHE B 1 317 ? 50.605 -0.905  -39.900 1.00 31.87  ? 317 PHE B CZ    1 
ATOM   6551 N N     . CYS B 1 318 ? 51.098 -0.546  -45.293 1.00 32.98  ? 318 CYS B N     1 
ATOM   6552 C CA    . CYS B 1 318 ? 49.952 0.331   -45.445 1.00 33.88  ? 318 CYS B CA    1 
ATOM   6553 C C     . CYS B 1 318 ? 48.878 -0.037  -44.438 1.00 31.03  ? 318 CYS B C     1 
ATOM   6554 O O     . CYS B 1 318 ? 48.544 -1.205  -44.252 1.00 32.74  ? 318 CYS B O     1 
ATOM   6555 C CB    . CYS B 1 318 ? 49.288 0.257   -46.809 1.00 37.23  ? 318 CYS B CB    1 
ATOM   6556 S SG    . CYS B 1 318 ? 50.224 1.110   -48.094 1.00 49.10  ? 318 CYS B SG    1 
ATOM   6557 N N     . GLY B 1 319 ? 48.342 1.017   -43.833 1.00 31.38  ? 319 GLY B N     1 
ATOM   6558 C CA    . GLY B 1 319 ? 47.226 0.949   -42.907 1.00 29.70  ? 319 GLY B CA    1 
ATOM   6559 C C     . GLY B 1 319 ? 46.495 2.280   -42.959 1.00 26.87  ? 319 GLY B C     1 
ATOM   6560 O O     . GLY B 1 319 ? 46.864 3.147   -43.760 1.00 25.83  ? 319 GLY B O     1 
ATOM   6561 N N     . ALA B 1 320 ? 45.463 2.401   -42.118 1.00 26.17  ? 320 ALA B N     1 
ATOM   6562 C CA    . ALA B 1 320 ? 44.644 3.597   -42.068 1.00 24.69  ? 320 ALA B CA    1 
ATOM   6563 C C     . ALA B 1 320 ? 44.039 3.770   -40.680 1.00 24.68  ? 320 ALA B C     1 
ATOM   6564 O O     . ALA B 1 320 ? 43.771 2.798   -39.985 1.00 23.49  ? 320 ALA B O     1 
ATOM   6565 C CB    . ALA B 1 320 ? 43.582 3.566   -43.140 1.00 22.98  ? 320 ALA B CB    1 
ATOM   6566 N N     . LEU B 1 321 ? 43.866 5.051   -40.322 1.00 29.11  ? 321 LEU B N     1 
ATOM   6567 C CA    . LEU B 1 321 ? 43.176 5.500   -39.125 1.00 29.73  ? 321 LEU B CA    1 
ATOM   6568 C C     . LEU B 1 321 ? 41.770 5.918   -39.521 1.00 26.98  ? 321 LEU B C     1 
ATOM   6569 O O     . LEU B 1 321 ? 41.577 6.548   -40.554 1.00 30.53  ? 321 LEU B O     1 
ATOM   6570 C CB    . LEU B 1 321 ? 43.937 6.695   -38.542 1.00 32.11  ? 321 LEU B CB    1 
ATOM   6571 C CG    . LEU B 1 321 ? 45.433 6.495   -38.304 1.00 30.42  ? 321 LEU B CG    1 
ATOM   6572 C CD1   . LEU B 1 321 ? 46.136 7.827   -38.154 1.00 28.85  ? 321 LEU B CD1   1 
ATOM   6573 C CD2   . LEU B 1 321 ? 45.687 5.619   -37.073 1.00 32.16  ? 321 LEU B CD2   1 
ATOM   6574 N N     . TYR B 1 322 ? 40.801 5.535   -38.702 1.00 26.68  ? 322 TYR B N     1 
ATOM   6575 C CA    . TYR B 1 322 ? 39.407 5.859   -38.922 1.00 26.55  ? 322 TYR B CA    1 
ATOM   6576 C C     . TYR B 1 322 ? 38.823 6.453   -37.642 1.00 28.25  ? 322 TYR B C     1 
ATOM   6577 O O     . TYR B 1 322 ? 39.099 5.952   -36.554 1.00 24.33  ? 322 TYR B O     1 
ATOM   6578 C CB    . TYR B 1 322 ? 38.616 4.608   -39.296 1.00 26.62  ? 322 TYR B CB    1 
ATOM   6579 C CG    . TYR B 1 322 ? 39.184 3.794   -40.430 1.00 28.19  ? 322 TYR B CG    1 
ATOM   6580 C CD1   . TYR B 1 322 ? 40.227 2.906   -40.230 1.00 29.77  ? 322 TYR B CD1   1 
ATOM   6581 C CD2   . TYR B 1 322 ? 38.661 3.897   -41.710 1.00 30.83  ? 322 TYR B CD2   1 
ATOM   6582 C CE1   . TYR B 1 322 ? 40.719 2.128   -41.266 1.00 31.72  ? 322 TYR B CE1   1 
ATOM   6583 C CE2   . TYR B 1 322 ? 39.163 3.151   -42.764 1.00 29.89  ? 322 TYR B CE2   1 
ATOM   6584 C CZ    . TYR B 1 322 ? 40.192 2.259   -42.540 1.00 30.56  ? 322 TYR B CZ    1 
ATOM   6585 O OH    . TYR B 1 322 ? 40.665 1.514   -43.581 1.00 29.45  ? 322 TYR B OH    1 
ATOM   6586 N N     . GLY B 1 323 ? 38.041 7.537   -37.788 1.00 29.24  ? 323 GLY B N     1 
ATOM   6587 C CA    . GLY B 1 323 ? 37.253 8.096   -36.699 1.00 28.95  ? 323 GLY B CA    1 
ATOM   6588 C C     . GLY B 1 323 ? 37.587 9.560   -36.435 1.00 29.75  ? 323 GLY B C     1 
ATOM   6589 O O     . GLY B 1 323 ? 38.297 10.185  -37.222 1.00 32.61  ? 323 GLY B O     1 
ATOM   6590 N N     . PRO B 1 324 ? 37.086 10.145  -35.318 1.00 31.60  ? 324 PRO B N     1 
ATOM   6591 C CA    . PRO B 1 324 ? 37.300 11.565  -34.999 1.00 29.11  ? 324 PRO B CA    1 
ATOM   6592 C C     . PRO B 1 324 ? 38.781 11.895  -34.893 1.00 28.68  ? 324 PRO B C     1 
ATOM   6593 O O     . PRO B 1 324 ? 39.559 11.060  -34.437 1.00 32.66  ? 324 PRO B O     1 
ATOM   6594 C CB    . PRO B 1 324 ? 36.671 11.733  -33.606 1.00 30.26  ? 324 PRO B CB    1 
ATOM   6595 C CG    . PRO B 1 324 ? 35.711 10.582  -33.460 1.00 31.03  ? 324 PRO B CG    1 
ATOM   6596 C CD    . PRO B 1 324 ? 36.292 9.454   -34.288 1.00 31.92  ? 324 PRO B CD    1 
ATOM   6597 N N     . PRO B 1 325 ? 39.246 13.099  -35.280 1.00 31.44  ? 325 PRO B N     1 
ATOM   6598 C CA    . PRO B 1 325 ? 40.657 13.441  -35.117 1.00 30.72  ? 325 PRO B CA    1 
ATOM   6599 C C     . PRO B 1 325 ? 41.284 13.015  -33.791 1.00 32.10  ? 325 PRO B C     1 
ATOM   6600 O O     . PRO B 1 325 ? 42.379 12.452  -33.821 1.00 38.23  ? 325 PRO B O     1 
ATOM   6601 C CB    . PRO B 1 325 ? 40.687 14.961  -35.343 1.00 31.79  ? 325 PRO B CB    1 
ATOM   6602 C CG    . PRO B 1 325 ? 39.562 15.191  -36.344 1.00 34.19  ? 325 PRO B CG    1 
ATOM   6603 C CD    . PRO B 1 325 ? 38.502 14.151  -36.000 1.00 34.34  ? 325 PRO B CD    1 
ATOM   6604 N N     . PRO B 1 326 ? 40.685 13.241  -32.593 1.00 31.41  ? 326 PRO B N     1 
ATOM   6605 C CA    . PRO B 1 326 ? 41.348 12.873  -31.343 1.00 32.79  ? 326 PRO B CA    1 
ATOM   6606 C C     . PRO B 1 326 ? 41.637 11.378  -31.218 1.00 32.91  ? 326 PRO B C     1 
ATOM   6607 O O     . PRO B 1 326 ? 42.655 11.005  -30.634 1.00 34.00  ? 326 PRO B O     1 
ATOM   6608 C CB    . PRO B 1 326 ? 40.388 13.355  -30.235 1.00 33.12  ? 326 PRO B CB    1 
ATOM   6609 C CG    . PRO B 1 326 ? 39.523 14.375  -30.895 1.00 29.79  ? 326 PRO B CG    1 
ATOM   6610 C CD    . PRO B 1 326 ? 39.411 13.920  -32.337 1.00 31.96  ? 326 PRO B CD    1 
ATOM   6611 N N     . VAL B 1 327 ? 40.763 10.527  -31.774 1.00 32.98  ? 327 VAL B N     1 
ATOM   6612 C CA    . VAL B 1 327 ? 40.997 9.085   -31.752 1.00 33.92  ? 327 VAL B CA    1 
ATOM   6613 C C     . VAL B 1 327 ? 42.137 8.734   -32.708 1.00 31.21  ? 327 VAL B C     1 
ATOM   6614 O O     . VAL B 1 327 ? 43.117 8.079   -32.349 1.00 30.93  ? 327 VAL B O     1 
ATOM   6615 C CB    . VAL B 1 327 ? 39.726 8.297   -32.105 1.00 35.95  ? 327 VAL B CB    1 
ATOM   6616 C CG1   . VAL B 1 327 ? 40.037 6.834   -32.350 1.00 36.32  ? 327 VAL B CG1   1 
ATOM   6617 C CG2   . VAL B 1 327 ? 38.655 8.447   -31.035 1.00 36.30  ? 327 VAL B CG2   1 
ATOM   6618 N N     . MET B 1 328 ? 42.031 9.214   -33.939 1.00 31.01  ? 328 MET B N     1 
ATOM   6619 C CA    . MET B 1 328 ? 43.061 8.936   -34.925 1.00 32.26  ? 328 MET B CA    1 
ATOM   6620 C C     . MET B 1 328 ? 44.442 9.340   -34.395 1.00 30.93  ? 328 MET B C     1 
ATOM   6621 O O     . MET B 1 328 ? 45.420 8.613   -34.590 1.00 28.48  ? 328 MET B O     1 
ATOM   6622 C CB    . MET B 1 328 ? 42.740 9.656   -36.238 1.00 31.18  ? 328 MET B CB    1 
ATOM   6623 C CG    . MET B 1 328 ? 41.557 9.026   -36.939 1.00 32.87  ? 328 MET B CG    1 
ATOM   6624 S SD    . MET B 1 328 ? 41.378 9.498   -38.665 1.00 34.86  ? 328 MET B SD    1 
ATOM   6625 C CE    . MET B 1 328 ? 41.133 11.264  -38.470 1.00 39.98  ? 328 MET B CE    1 
ATOM   6626 N N     . ASP B 1 329 ? 44.519 10.485  -33.711 1.00 28.46  ? 329 ASP B N     1 
ATOM   6627 C CA    . ASP B 1 329 ? 45.800 11.016  -33.249 1.00 31.02  ? 329 ASP B CA    1 
ATOM   6628 C C     . ASP B 1 329 ? 46.383 10.139  -32.153 1.00 30.21  ? 329 ASP B C     1 
ATOM   6629 O O     . ASP B 1 329 ? 47.583 9.902   -32.169 1.00 34.62  ? 329 ASP B O     1 
ATOM   6630 C CB    . ASP B 1 329 ? 45.697 12.451  -32.712 1.00 32.40  ? 329 ASP B CB    1 
ATOM   6631 C CG    . ASP B 1 329 ? 45.466 13.460  -33.811 1.00 34.76  ? 329 ASP B CG    1 
ATOM   6632 O OD1   . ASP B 1 329 ? 45.729 13.095  -34.989 1.00 45.08  ? 329 ASP B OD1   1 
ATOM   6633 O OD2   . ASP B 1 329 ? 45.002 14.572  -33.501 1.00 37.54  ? 329 ASP B OD2   1 
ATOM   6634 N N     . THR B 1 330 ? 45.533 9.694   -31.215 1.00 30.06  ? 330 THR B N     1 
ATOM   6635 C CA    . THR B 1 330 ? 45.940 8.778   -30.159 1.00 31.95  ? 330 THR B CA    1 
ATOM   6636 C C     . THR B 1 330 ? 46.451 7.469   -30.757 1.00 32.97  ? 330 THR B C     1 
ATOM   6637 O O     . THR B 1 330 ? 47.520 6.998   -30.371 1.00 35.83  ? 330 THR B O     1 
ATOM   6638 C CB    . THR B 1 330 ? 44.814 8.465   -29.157 1.00 32.24  ? 330 THR B CB    1 
ATOM   6639 O OG1   . THR B 1 330 ? 44.285 9.683   -28.634 1.00 30.60  ? 330 THR B OG1   1 
ATOM   6640 C CG2   . THR B 1 330 ? 45.281 7.600   -28.001 1.00 29.33  ? 330 THR B CG2   1 
ATOM   6641 N N     . LEU B 1 331 ? 45.693 6.873   -31.688 1.00 30.24  ? 331 LEU B N     1 
ATOM   6642 C CA    . LEU B 1 331 ? 46.111 5.596   -32.249 1.00 29.26  ? 331 LEU B CA    1 
ATOM   6643 C C     . LEU B 1 331 ? 47.422 5.760   -33.032 1.00 27.99  ? 331 LEU B C     1 
ATOM   6644 O O     . LEU B 1 331 ? 48.302 4.895   -32.993 1.00 25.27  ? 331 LEU B O     1 
ATOM   6645 C CB    . LEU B 1 331 ? 44.988 5.033   -33.125 1.00 29.42  ? 331 LEU B CB    1 
ATOM   6646 C CG    . LEU B 1 331 ? 43.631 4.840   -32.450 1.00 30.04  ? 331 LEU B CG    1 
ATOM   6647 C CD1   . LEU B 1 331 ? 42.639 4.249   -33.442 1.00 30.39  ? 331 LEU B CD1   1 
ATOM   6648 C CD2   . LEU B 1 331 ? 43.732 3.972   -31.197 1.00 30.76  ? 331 LEU B CD2   1 
ATOM   6649 N N     . TRP B 1 332 ? 47.582 6.908   -33.697 1.00 28.04  ? 332 TRP B N     1 
ATOM   6650 C CA    . TRP B 1 332 ? 48.760 7.147   -34.514 1.00 28.11  ? 332 TRP B CA    1 
ATOM   6651 C C     . TRP B 1 332 ? 50.014 7.216   -33.660 1.00 29.44  ? 332 TRP B C     1 
ATOM   6652 O O     . TRP B 1 332 ? 51.042 6.680   -34.037 1.00 32.96  ? 332 TRP B O     1 
ATOM   6653 C CB    . TRP B 1 332 ? 48.622 8.429   -35.326 1.00 28.30  ? 332 TRP B CB    1 
ATOM   6654 C CG    . TRP B 1 332 ? 49.852 8.694   -36.129 1.00 28.80  ? 332 TRP B CG    1 
ATOM   6655 C CD1   . TRP B 1 332 ? 50.670 9.778   -36.046 1.00 28.60  ? 332 TRP B CD1   1 
ATOM   6656 C CD2   . TRP B 1 332 ? 50.429 7.827   -37.119 1.00 27.29  ? 332 TRP B CD2   1 
ATOM   6657 N NE1   . TRP B 1 332 ? 51.716 9.646   -36.914 1.00 28.60  ? 332 TRP B NE1   1 
ATOM   6658 C CE2   . TRP B 1 332 ? 51.601 8.460   -37.582 1.00 28.45  ? 332 TRP B CE2   1 
ATOM   6659 C CE3   . TRP B 1 332 ? 50.071 6.586   -37.657 1.00 26.58  ? 332 TRP B CE3   1 
ATOM   6660 C CZ2   . TRP B 1 332 ? 52.425 7.886   -38.552 1.00 28.54  ? 332 TRP B CZ2   1 
ATOM   6661 C CZ3   . TRP B 1 332 ? 50.878 6.020   -38.617 1.00 26.07  ? 332 TRP B CZ3   1 
ATOM   6662 C CH2   . TRP B 1 332 ? 52.025 6.671   -39.069 1.00 28.71  ? 332 TRP B CH2   1 
ATOM   6663 N N     . THR B 1 333 ? 49.922 7.923   -32.533 1.00 32.85  ? 333 THR B N     1 
ATOM   6664 C CA    . THR B 1 333 ? 50.999 8.014   -31.560 1.00 32.67  ? 333 THR B CA    1 
ATOM   6665 C C     . THR B 1 333 ? 51.511 6.613   -31.220 1.00 30.49  ? 333 THR B C     1 
ATOM   6666 O O     . THR B 1 333 ? 52.706 6.348   -31.282 1.00 32.68  ? 333 THR B O     1 
ATOM   6667 C CB    . THR B 1 333 ? 50.513 8.767   -30.313 1.00 31.98  ? 333 THR B CB    1 
ATOM   6668 O OG1   . THR B 1 333 ? 50.329 10.128  -30.694 1.00 28.41  ? 333 THR B OG1   1 
ATOM   6669 C CG2   . THR B 1 333 ? 51.465 8.665   -29.146 1.00 30.65  ? 333 THR B CG2   1 
ATOM   6670 N N     . ALA B 1 334 ? 50.594 5.708   -30.888 1.00 30.55  ? 334 ALA B N     1 
ATOM   6671 C CA    . ALA B 1 334 ? 50.958 4.348   -30.524 1.00 30.35  ? 334 ALA B CA    1 
ATOM   6672 C C     . ALA B 1 334 ? 51.606 3.617   -31.701 1.00 30.14  ? 334 ALA B C     1 
ATOM   6673 O O     . ALA B 1 334 ? 52.548 2.839   -31.503 1.00 33.78  ? 334 ALA B O     1 
ATOM   6674 C CB    . ALA B 1 334 ? 49.734 3.613   -30.029 1.00 30.32  ? 334 ALA B CB    1 
ATOM   6675 N N     . ILE B 1 335 ? 51.094 3.850   -32.917 1.00 28.47  ? 335 ILE B N     1 
ATOM   6676 C CA    . ILE B 1 335 ? 51.588 3.141   -34.095 1.00 30.42  ? 335 ILE B CA    1 
ATOM   6677 C C     . ILE B 1 335 ? 52.968 3.665   -34.472 1.00 30.41  ? 335 ILE B C     1 
ATOM   6678 O O     . ILE B 1 335 ? 53.902 2.874   -34.588 1.00 29.32  ? 335 ILE B O     1 
ATOM   6679 C CB    . ILE B 1 335 ? 50.601 3.230   -35.276 1.00 29.76  ? 335 ILE B CB    1 
ATOM   6680 C CG1   . ILE B 1 335 ? 49.343 2.419   -34.979 1.00 31.50  ? 335 ILE B CG1   1 
ATOM   6681 C CG2   . ILE B 1 335 ? 51.256 2.773   -36.570 1.00 33.72  ? 335 ILE B CG2   1 
ATOM   6682 C CD1   . ILE B 1 335 ? 48.170 2.721   -35.880 1.00 33.40  ? 335 ILE B CD1   1 
ATOM   6683 N N     . ARG B 1 336 ? 53.078 4.993   -34.657 1.00 31.94  ? 336 ARG B N     1 
ATOM   6684 C CA    . ARG B 1 336 ? 54.332 5.621   -35.050 1.00 34.30  ? 336 ARG B CA    1 
ATOM   6685 C C     . ARG B 1 336 ? 55.433 5.271   -34.053 1.00 32.76  ? 336 ARG B C     1 
ATOM   6686 O O     . ARG B 1 336 ? 56.526 4.893   -34.470 1.00 31.16  ? 336 ARG B O     1 
ATOM   6687 C CB    . ARG B 1 336 ? 54.204 7.144   -35.141 1.00 38.23  ? 336 ARG B CB    1 
ATOM   6688 C CG    . ARG B 1 336 ? 55.428 7.833   -35.738 1.00 42.10  ? 336 ARG B CG    1 
ATOM   6689 C CD    . ARG B 1 336 ? 55.484 9.339   -35.513 1.00 42.95  ? 336 ARG B CD    1 
ATOM   6690 N NE    . ARG B 1 336 ? 56.332 10.001  -36.507 1.00 44.18  ? 336 ARG B NE    1 
ATOM   6691 C CZ    . ARG B 1 336 ? 57.667 10.069  -36.483 1.00 45.12  ? 336 ARG B CZ    1 
ATOM   6692 N NH1   . ARG B 1 336 ? 58.367 9.529   -35.496 1.00 50.37  ? 336 ARG B NH1   1 
ATOM   6693 N NH2   . ARG B 1 336 ? 58.310 10.692  -37.455 1.00 40.02  ? 336 ARG B NH2   1 
ATOM   6694 N N     . ASP B 1 337 ? 55.124 5.372   -32.749 1.00 30.74  ? 337 ASP B N     1 
ATOM   6695 C CA    . ASP B 1 337 ? 56.107 5.115   -31.703 1.00 34.19  ? 337 ASP B CA    1 
ATOM   6696 C C     . ASP B 1 337 ? 56.556 3.659   -31.678 1.00 33.18  ? 337 ASP B C     1 
ATOM   6697 O O     . ASP B 1 337 ? 57.642 3.399   -31.165 1.00 32.79  ? 337 ASP B O     1 
ATOM   6698 C CB    . ASP B 1 337 ? 55.601 5.474   -30.300 1.00 37.94  ? 337 ASP B CB    1 
ATOM   6699 C CG    . ASP B 1 337 ? 55.482 6.968   -30.057 1.00 41.62  ? 337 ASP B CG    1 
ATOM   6700 O OD1   . ASP B 1 337 ? 55.931 7.729   -30.935 1.00 44.81  ? 337 ASP B OD1   1 
ATOM   6701 O OD2   . ASP B 1 337 ? 54.891 7.359   -29.025 1.00 44.74  ? 337 ASP B OD2   1 
ATOM   6702 N N     . SER B 1 338 ? 55.734 2.726   -32.193 1.00 31.08  ? 338 SER B N     1 
ATOM   6703 C CA    . SER B 1 338 ? 56.112 1.322   -32.231 1.00 30.90  ? 338 SER B CA    1 
ATOM   6704 C C     . SER B 1 338 ? 57.213 1.084   -33.261 1.00 30.53  ? 338 SER B C     1 
ATOM   6705 O O     . SER B 1 338 ? 57.859 0.040   -33.191 1.00 32.83  ? 338 SER B O     1 
ATOM   6706 C CB    . SER B 1 338 ? 54.949 0.398   -32.536 1.00 31.75  ? 338 SER B CB    1 
ATOM   6707 O OG    . SER B 1 338 ? 53.945 0.432   -31.532 1.00 33.53  ? 338 SER B OG    1 
ATOM   6708 N N     . PHE B 1 339 ? 57.405 2.005   -34.223 1.00 28.72  ? 339 PHE B N     1 
ATOM   6709 C CA    . PHE B 1 339 ? 58.345 1.765   -35.317 1.00 29.54  ? 339 PHE B CA    1 
ATOM   6710 C C     . PHE B 1 339 ? 59.469 2.798   -35.421 1.00 27.42  ? 339 PHE B C     1 
ATOM   6711 O O     . PHE B 1 339 ? 60.361 2.601   -36.246 1.00 22.90  ? 339 PHE B O     1 
ATOM   6712 C CB    . PHE B 1 339 ? 57.605 1.707   -36.661 1.00 29.89  ? 339 PHE B CB    1 
ATOM   6713 C CG    . PHE B 1 339 ? 56.558 0.629   -36.702 1.00 30.60  ? 339 PHE B CG    1 
ATOM   6714 C CD1   . PHE B 1 339 ? 56.916 -0.697  -36.919 1.00 32.95  ? 339 PHE B CD1   1 
ATOM   6715 C CD2   . PHE B 1 339 ? 55.237 0.921   -36.420 1.00 28.62  ? 339 PHE B CD2   1 
ATOM   6716 C CE1   . PHE B 1 339 ? 55.964 -1.706  -36.883 1.00 30.48  ? 339 PHE B CE1   1 
ATOM   6717 C CE2   . PHE B 1 339 ? 54.286 -0.084  -36.414 1.00 31.91  ? 339 PHE B CE2   1 
ATOM   6718 C CZ    . PHE B 1 339 ? 54.647 -1.394  -36.654 1.00 32.42  ? 339 PHE B CZ    1 
ATOM   6719 N N     . ALA B 1 340 ? 59.452 3.857   -34.591 1.00 30.90  ? 340 ALA B N     1 
ATOM   6720 C CA    . ALA B 1 340 ? 60.306 5.032   -34.805 1.00 33.32  ? 340 ALA B CA    1 
ATOM   6721 C C     . ALA B 1 340 ? 61.808 4.730   -34.676 1.00 32.66  ? 340 ALA B C     1 
ATOM   6722 O O     . ALA B 1 340 ? 62.613 5.266   -35.428 1.00 37.74  ? 340 ALA B O     1 
ATOM   6723 C CB    . ALA B 1 340 ? 59.900 6.142   -33.869 1.00 31.95  ? 340 ALA B CB    1 
ATOM   6724 N N     . ASP B 1 341 ? 62.201 3.820   -33.784 1.00 35.53  ? 341 ASP B N     1 
ATOM   6725 C CA    . ASP B 1 341 ? 63.611 3.581   -33.511 1.00 37.86  ? 341 ASP B CA    1 
ATOM   6726 C C     . ASP B 1 341 ? 64.245 2.603   -34.511 1.00 38.38  ? 341 ASP B C     1 
ATOM   6727 O O     . ASP B 1 341 ? 65.404 2.228   -34.336 1.00 36.77  ? 341 ASP B O     1 
ATOM   6728 C CB    . ASP B 1 341 ? 63.789 3.041   -32.090 1.00 40.19  ? 341 ASP B CB    1 
ATOM   6729 C CG    . ASP B 1 341 ? 63.226 1.640   -31.931 1.00 47.08  ? 341 ASP B CG    1 
ATOM   6730 O OD1   . ASP B 1 341 ? 63.652 0.739   -32.679 1.00 50.09  ? 341 ASP B OD1   1 
ATOM   6731 O OD2   . ASP B 1 341 ? 62.370 1.465   -31.073 1.00 56.39  ? 341 ASP B OD2   1 
ATOM   6732 N N     . ILE B 1 342 ? 63.510 2.157   -35.541 1.00 32.18  ? 342 ILE B N     1 
ATOM   6733 C CA    . ILE B 1 342 ? 64.063 1.204   -36.490 1.00 31.57  ? 342 ILE B CA    1 
ATOM   6734 C C     . ILE B 1 342 ? 64.917 1.961   -37.499 1.00 30.64  ? 342 ILE B C     1 
ATOM   6735 O O     . ILE B 1 342 ? 64.405 2.734   -38.293 1.00 30.12  ? 342 ILE B O     1 
ATOM   6736 C CB    . ILE B 1 342 ? 62.990 0.352   -37.197 1.00 30.81  ? 342 ILE B CB    1 
ATOM   6737 C CG1   . ILE B 1 342 ? 62.266 -0.569  -36.220 1.00 36.01  ? 342 ILE B CG1   1 
ATOM   6738 C CG2   . ILE B 1 342 ? 63.602 -0.454  -38.317 1.00 32.13  ? 342 ILE B CG2   1 
ATOM   6739 C CD1   . ILE B 1 342 ? 61.012 -1.171  -36.784 1.00 38.27  ? 342 ILE B CD1   1 
ATOM   6740 N N     . PRO B 1 343 ? 66.241 1.716   -37.538 1.00 31.45  ? 343 PRO B N     1 
ATOM   6741 C CA    . PRO B 1 343 ? 67.102 2.368   -38.522 1.00 31.93  ? 343 PRO B CA    1 
ATOM   6742 C C     . PRO B 1 343 ? 66.476 2.314   -39.912 1.00 30.09  ? 343 PRO B C     1 
ATOM   6743 O O     . PRO B 1 343 ? 66.061 1.244   -40.354 1.00 32.67  ? 343 PRO B O     1 
ATOM   6744 C CB    . PRO B 1 343 ? 68.389 1.536   -38.455 1.00 33.77  ? 343 PRO B CB    1 
ATOM   6745 C CG    . PRO B 1 343 ? 68.414 1.009   -37.027 1.00 33.08  ? 343 PRO B CG    1 
ATOM   6746 C CD    . PRO B 1 343 ? 66.965 0.792   -36.654 1.00 30.12  ? 343 PRO B CD    1 
ATOM   6747 N N     . GLY B 1 344 ? 66.346 3.484   -40.548 1.00 27.47  ? 344 GLY B N     1 
ATOM   6748 C CA    . GLY B 1 344 ? 65.905 3.597   -41.934 1.00 27.72  ? 344 GLY B CA    1 
ATOM   6749 C C     . GLY B 1 344 ? 64.387 3.743   -42.112 1.00 26.72  ? 344 GLY B C     1 
ATOM   6750 O O     . GLY B 1 344 ? 63.920 3.976   -43.219 1.00 28.34  ? 344 GLY B O     1 
ATOM   6751 N N     . VAL B 1 345 ? 63.597 3.611   -41.047 1.00 26.54  ? 345 VAL B N     1 
ATOM   6752 C CA    . VAL B 1 345 ? 62.163 3.718   -41.191 1.00 29.42  ? 345 VAL B CA    1 
ATOM   6753 C C     . VAL B 1 345 ? 61.787 5.079   -41.762 1.00 32.02  ? 345 VAL B C     1 
ATOM   6754 O O     . VAL B 1 345 ? 62.413 6.070   -41.417 1.00 35.45  ? 345 VAL B O     1 
ATOM   6755 C CB    . VAL B 1 345 ? 61.455 3.489   -39.852 1.00 31.32  ? 345 VAL B CB    1 
ATOM   6756 C CG1   . VAL B 1 345 ? 61.718 4.610   -38.862 1.00 30.66  ? 345 VAL B CG1   1 
ATOM   6757 C CG2   . VAL B 1 345 ? 59.968 3.299   -40.073 1.00 30.81  ? 345 VAL B CG2   1 
ATOM   6758 N N     . LYS B 1 346 ? 60.733 5.100   -42.595 1.00 35.05  ? 346 LYS B N     1 
ATOM   6759 C CA    . LYS B 1 346 ? 60.127 6.312   -43.129 1.00 36.16  ? 346 LYS B CA    1 
ATOM   6760 C C     . LYS B 1 346 ? 58.608 6.281   -42.900 1.00 35.71  ? 346 LYS B C     1 
ATOM   6761 O O     . LYS B 1 346 ? 57.964 5.227   -42.954 1.00 31.73  ? 346 LYS B O     1 
ATOM   6762 C CB    . LYS B 1 346 ? 60.418 6.448   -44.627 1.00 41.11  ? 346 LYS B CB    1 
ATOM   6763 C CG    . LYS B 1 346 ? 61.862 6.743   -45.024 1.00 45.59  ? 346 LYS B CG    1 
ATOM   6764 C CD    . LYS B 1 346 ? 62.290 8.204   -44.902 1.00 56.74  ? 346 LYS B CD    1 
ATOM   6765 C CE    . LYS B 1 346 ? 61.380 9.205   -45.607 1.00 63.06  ? 346 LYS B CE    1 
ATOM   6766 N NZ    . LYS B 1 346 ? 61.944 10.583  -45.690 1.00 58.10  ? 346 LYS B NZ    1 
ATOM   6767 N N     . PHE B 1 347 ? 58.039 7.464   -42.631 1.00 33.16  ? 347 PHE B N     1 
ATOM   6768 C CA    . PHE B 1 347 ? 56.617 7.614   -42.370 1.00 32.53  ? 347 PHE B CA    1 
ATOM   6769 C C     . PHE B 1 347 ? 56.009 8.584   -43.381 1.00 31.14  ? 347 PHE B C     1 
ATOM   6770 O O     . PHE B 1 347 ? 56.575 9.635   -43.668 1.00 29.86  ? 347 PHE B O     1 
ATOM   6771 C CB    . PHE B 1 347 ? 56.358 8.111   -40.946 1.00 30.34  ? 347 PHE B CB    1 
ATOM   6772 C CG    . PHE B 1 347 ? 56.881 7.231   -39.847 1.00 31.98  ? 347 PHE B CG    1 
ATOM   6773 C CD1   . PHE B 1 347 ? 56.121 6.193   -39.337 1.00 35.82  ? 347 PHE B CD1   1 
ATOM   6774 C CD2   . PHE B 1 347 ? 58.138 7.439   -39.307 1.00 34.11  ? 347 PHE B CD2   1 
ATOM   6775 C CE1   . PHE B 1 347 ? 56.601 5.403   -38.299 1.00 34.30  ? 347 PHE B CE1   1 
ATOM   6776 C CE2   . PHE B 1 347 ? 58.615 6.650   -38.270 1.00 33.84  ? 347 PHE B CE2   1 
ATOM   6777 C CZ    . PHE B 1 347 ? 57.849 5.627   -37.772 1.00 33.66  ? 347 PHE B CZ    1 
ATOM   6778 N N     . TYR B 1 348 ? 54.832 8.219   -43.899 1.00 29.50  ? 348 TYR B N     1 
ATOM   6779 C CA    . TYR B 1 348 ? 54.193 8.989   -44.946 1.00 28.12  ? 348 TYR B CA    1 
ATOM   6780 C C     . TYR B 1 348 ? 52.677 9.029   -44.771 1.00 27.16  ? 348 TYR B C     1 
ATOM   6781 O O     . TYR B 1 348 ? 52.030 8.008   -44.518 1.00 26.01  ? 348 TYR B O     1 
ATOM   6782 C CB    . TYR B 1 348 ? 54.470 8.364   -46.311 1.00 28.96  ? 348 TYR B CB    1 
ATOM   6783 C CG    . TYR B 1 348 ? 55.908 8.282   -46.746 1.00 27.04  ? 348 TYR B CG    1 
ATOM   6784 C CD1   . TYR B 1 348 ? 56.551 9.346   -47.363 1.00 26.61  ? 348 TYR B CD1   1 
ATOM   6785 C CD2   . TYR B 1 348 ? 56.603 7.094   -46.605 1.00 27.76  ? 348 TYR B CD2   1 
ATOM   6786 C CE1   . TYR B 1 348 ? 57.865 9.229   -47.805 1.00 27.44  ? 348 TYR B CE1   1 
ATOM   6787 C CE2   . TYR B 1 348 ? 57.908 6.961   -47.049 1.00 26.67  ? 348 TYR B CE2   1 
ATOM   6788 C CZ    . TYR B 1 348 ? 58.535 8.029   -47.653 1.00 26.08  ? 348 TYR B CZ    1 
ATOM   6789 O OH    . TYR B 1 348 ? 59.809 7.832   -48.059 1.00 32.70  ? 348 TYR B OH    1 
ATOM   6790 N N     . PHE B 1 349 ? 52.140 10.241  -44.947 1.00 28.66  ? 349 PHE B N     1 
ATOM   6791 C CA    . PHE B 1 349 ? 50.726 10.486  -45.161 1.00 29.32  ? 349 PHE B CA    1 
ATOM   6792 C C     . PHE B 1 349 ? 50.572 10.930  -46.608 1.00 29.53  ? 349 PHE B C     1 
ATOM   6793 O O     . PHE B 1 349 ? 51.576 11.213  -47.249 1.00 30.19  ? 349 PHE B O     1 
ATOM   6794 C CB    . PHE B 1 349 ? 50.216 11.479  -44.116 1.00 30.50  ? 349 PHE B CB    1 
ATOM   6795 C CG    . PHE B 1 349 ? 49.987 10.833  -42.778 1.00 32.60  ? 349 PHE B CG    1 
ATOM   6796 C CD1   . PHE B 1 349 ? 48.892 10.012  -42.577 1.00 35.72  ? 349 PHE B CD1   1 
ATOM   6797 C CD2   . PHE B 1 349 ? 50.876 11.014  -41.734 1.00 33.03  ? 349 PHE B CD2   1 
ATOM   6798 C CE1   . PHE B 1 349 ? 48.674 9.412   -41.345 1.00 39.26  ? 349 PHE B CE1   1 
ATOM   6799 C CE2   . PHE B 1 349 ? 50.666 10.405  -40.510 1.00 35.23  ? 349 PHE B CE2   1 
ATOM   6800 C CZ    . PHE B 1 349 ? 49.569 9.600   -40.314 1.00 36.79  ? 349 PHE B CZ    1 
ATOM   6801 N N     . PRO B 1 350 ? 49.359 10.919  -47.207 1.00 30.63  ? 350 PRO B N     1 
ATOM   6802 C CA    . PRO B 1 350 ? 49.223 11.175  -48.639 1.00 31.22  ? 350 PRO B CA    1 
ATOM   6803 C C     . PRO B 1 350 ? 49.922 12.462  -49.057 1.00 28.91  ? 350 PRO B C     1 
ATOM   6804 O O     . PRO B 1 350 ? 50.640 12.451  -50.050 1.00 29.81  ? 350 PRO B O     1 
ATOM   6805 C CB    . PRO B 1 350 ? 47.708 11.213  -48.884 1.00 29.19  ? 350 PRO B CB    1 
ATOM   6806 C CG    . PRO B 1 350 ? 47.172 10.336  -47.779 1.00 31.36  ? 350 PRO B CG    1 
ATOM   6807 C CD    . PRO B 1 350 ? 48.062 10.637  -46.581 1.00 31.15  ? 350 PRO B CD    1 
ATOM   6808 N N     . GLU B 1 351 ? 49.790 13.526  -48.255 1.00 29.91  ? 351 GLU B N     1 
ATOM   6809 C CA    . GLU B 1 351 ? 50.398 14.811  -48.606 1.00 32.00  ? 351 GLU B CA    1 
ATOM   6810 C C     . GLU B 1 351 ? 51.936 14.766  -48.580 1.00 32.71  ? 351 GLU B C     1 
ATOM   6811 O O     . GLU B 1 351 ? 52.572 15.662  -49.108 1.00 37.98  ? 351 GLU B O     1 
ATOM   6812 C CB    . GLU B 1 351 ? 49.839 15.934  -47.732 1.00 31.69  ? 351 GLU B CB    1 
ATOM   6813 C CG    . GLU B 1 351 ? 50.255 15.883  -46.271 1.00 36.32  ? 351 GLU B CG    1 
ATOM   6814 C CD    . GLU B 1 351 ? 49.439 14.976  -45.354 1.00 38.62  ? 351 GLU B CD    1 
ATOM   6815 O OE1   . GLU B 1 351 ? 48.526 14.231  -45.858 1.00 36.98  ? 351 GLU B OE1   1 
ATOM   6816 O OE2   . GLU B 1 351 ? 49.709 15.021  -44.127 1.00 34.04  ? 351 GLU B OE2   1 
ATOM   6817 N N     . ASP B 1 352 ? 52.551 13.706  -48.041 1.00 35.75  ? 352 ASP B N     1 
ATOM   6818 C CA    . ASP B 1 352 ? 54.001 13.550  -48.008 1.00 35.91  ? 352 ASP B CA    1 
ATOM   6819 C C     . ASP B 1 352 ? 54.539 12.816  -49.237 1.00 39.36  ? 352 ASP B C     1 
ATOM   6820 O O     . ASP B 1 352 ? 55.741 12.585  -49.316 1.00 45.21  ? 352 ASP B O     1 
ATOM   6821 C CB    . ASP B 1 352 ? 54.455 12.745  -46.786 1.00 33.67  ? 352 ASP B CB    1 
ATOM   6822 C CG    . ASP B 1 352 ? 54.087 13.399  -45.470 1.00 34.27  ? 352 ASP B CG    1 
ATOM   6823 O OD1   . ASP B 1 352 ? 54.527 14.531  -45.260 1.00 38.03  ? 352 ASP B OD1   1 
ATOM   6824 O OD2   . ASP B 1 352 ? 53.370 12.768  -44.664 1.00 36.17  ? 352 ASP B OD2   1 
ATOM   6825 N N     . ARG B 1 353 ? 53.674 12.406  -50.173 1.00 39.83  ? 353 ARG B N     1 
ATOM   6826 C CA    . ARG B 1 353 ? 54.109 11.581  -51.292 1.00 37.17  ? 353 ARG B CA    1 
ATOM   6827 C C     . ARG B 1 353 ? 54.299 12.448  -52.526 1.00 37.40  ? 353 ARG B C     1 
ATOM   6828 O O     . ARG B 1 353 ? 53.338 12.995  -53.044 1.00 47.02  ? 353 ARG B O     1 
ATOM   6829 C CB    . ARG B 1 353 ? 53.073 10.498  -51.622 1.00 36.43  ? 353 ARG B CB    1 
ATOM   6830 C CG    . ARG B 1 353 ? 52.792 9.532   -50.480 1.00 36.34  ? 353 ARG B CG    1 
ATOM   6831 C CD    . ARG B 1 353 ? 54.008 8.718   -50.087 1.00 34.20  ? 353 ARG B CD    1 
ATOM   6832 N NE    . ARG B 1 353 ? 54.437 7.824   -51.143 1.00 31.57  ? 353 ARG B NE    1 
ATOM   6833 C CZ    . ARG B 1 353 ? 55.491 7.014   -51.097 1.00 32.58  ? 353 ARG B CZ    1 
ATOM   6834 N NH1   . ARG B 1 353 ? 56.297 7.014   -50.052 1.00 33.03  ? 353 ARG B NH1   1 
ATOM   6835 N NH2   . ARG B 1 353 ? 55.744 6.199   -52.109 1.00 34.28  ? 353 ARG B NH2   1 
ATOM   6836 N N     . ARG B 1 354 ? 55.516 12.465  -53.054 1.00 38.51  ? 354 ARG B N     1 
ATOM   6837 C CA    . ARG B 1 354 ? 55.881 13.380  -54.115 1.00 43.64  ? 354 ARG B CA    1 
ATOM   6838 C C     . ARG B 1 354 ? 55.486 12.912  -55.519 1.00 47.46  ? 354 ARG B C     1 
ATOM   6839 O O     . ARG B 1 354 ? 55.619 13.703  -56.436 1.00 49.07  ? 354 ARG B O     1 
ATOM   6840 C CB    . ARG B 1 354 ? 57.383 13.683  -54.045 1.00 51.06  ? 354 ARG B CB    1 
ATOM   6841 C CG    . ARG B 1 354 ? 58.339 12.516  -54.255 1.00 52.31  ? 354 ARG B CG    1 
ATOM   6842 C CD    . ARG B 1 354 ? 59.767 12.990  -53.987 1.00 58.27  ? 354 ARG B CD    1 
ATOM   6843 N NE    . ARG B 1 354 ? 60.784 11.942  -54.032 1.00 68.28  ? 354 ARG B NE    1 
ATOM   6844 C CZ    . ARG B 1 354 ? 61.190 11.287  -55.125 1.00 71.80  ? 354 ARG B CZ    1 
ATOM   6845 N NH1   . ARG B 1 354 ? 60.873 11.731  -56.329 1.00 73.82  ? 354 ARG B NH1   1 
ATOM   6846 N NH2   . ARG B 1 354 ? 61.948 10.205  -55.013 1.00 70.38  ? 354 ARG B NH2   1 
ATOM   6847 N N     . HIS B 1 355 ? 55.015 11.675  -55.732 1.00 53.92  ? 355 HIS B N     1 
ATOM   6848 C CA    . HIS B 1 355 ? 54.579 11.258  -57.065 1.00 52.81  ? 355 HIS B CA    1 
ATOM   6849 C C     . HIS B 1 355 ? 53.059 11.370  -57.204 1.00 53.40  ? 355 HIS B C     1 
ATOM   6850 O O     . HIS B 1 355 ? 52.326 11.014  -56.284 1.00 50.40  ? 355 HIS B O     1 
ATOM   6851 C CB    . HIS B 1 355 ? 54.921 9.794   -57.363 1.00 55.21  ? 355 HIS B CB    1 
ATOM   6852 C CG    . HIS B 1 355 ? 56.344 9.425   -57.147 1.00 55.02  ? 355 HIS B CG    1 
ATOM   6853 N ND1   . HIS B 1 355 ? 57.168 9.076   -58.192 1.00 57.34  ? 355 HIS B ND1   1 
ATOM   6854 C CD2   . HIS B 1 355 ? 57.082 9.328   -56.035 1.00 53.39  ? 355 HIS B CD2   1 
ATOM   6855 C CE1   . HIS B 1 355 ? 58.370 8.788   -57.720 1.00 55.06  ? 355 HIS B CE1   1 
ATOM   6856 N NE2   . HIS B 1 355 ? 58.338 8.931   -56.414 1.00 51.56  ? 355 HIS B NE2   1 
ATOM   6857 N N     . LYS B 1 356 ? 52.591 11.816  -58.379 1.00 59.49  ? 356 LYS B N     1 
ATOM   6858 C CA    . LYS B 1 356 ? 51.162 11.908  -58.664 1.00 61.06  ? 356 LYS B CA    1 
ATOM   6859 C C     . LYS B 1 356 ? 50.545 10.505  -58.715 1.00 52.15  ? 356 LYS B C     1 
ATOM   6860 O O     . LYS B 1 356 ? 49.399 10.335  -58.314 1.00 47.47  ? 356 LYS B O     1 
ATOM   6861 C CB    . LYS B 1 356 ? 50.896 12.627  -59.994 1.00 65.28  ? 356 LYS B CB    1 
ATOM   6862 C CG    . LYS B 1 356 ? 49.449 13.074  -60.184 1.00 75.69  ? 356 LYS B CG    1 
ATOM   6863 C CD    . LYS B 1 356 ? 48.790 12.621  -61.496 1.00 83.13  ? 356 LYS B CD    1 
ATOM   6864 C CE    . LYS B 1 356 ? 47.280 12.478  -61.370 1.00 83.51  ? 356 LYS B CE    1 
ATOM   6865 N NZ    . LYS B 1 356 ? 46.692 11.547  -62.365 1.00 76.05  ? 356 LYS B NZ    1 
ATOM   6866 N N     . VAL B 1 357 ? 51.310 9.534   -59.246 1.00 42.57  ? 357 VAL B N     1 
ATOM   6867 C CA    . VAL B 1 357 ? 50.932 8.139   -59.342 1.00 37.23  ? 357 VAL B CA    1 
ATOM   6868 C C     . VAL B 1 357 ? 51.770 7.364   -58.336 1.00 37.18  ? 357 VAL B C     1 
ATOM   6869 O O     . VAL B 1 357 ? 52.986 7.232   -58.505 1.00 37.19  ? 357 VAL B O     1 
ATOM   6870 C CB    . VAL B 1 357 ? 51.176 7.593   -60.765 1.00 39.28  ? 357 VAL B CB    1 
ATOM   6871 C CG1   . VAL B 1 357 ? 50.821 6.112   -60.882 1.00 36.62  ? 357 VAL B CG1   1 
ATOM   6872 C CG2   . VAL B 1 357 ? 50.464 8.417   -61.825 1.00 37.77  ? 357 VAL B CG2   1 
ATOM   6873 N N     . ASP B 1 358 ? 51.117 6.819   -57.306 1.00 35.78  ? 358 ASP B N     1 
ATOM   6874 C CA    . ASP B 1 358 ? 51.839 6.459   -56.098 1.00 31.42  ? 358 ASP B CA    1 
ATOM   6875 C C     . ASP B 1 358 ? 51.123 5.392   -55.297 1.00 29.31  ? 358 ASP B C     1 
ATOM   6876 O O     . ASP B 1 358 ? 49.902 5.388   -55.225 1.00 31.02  ? 358 ASP B O     1 
ATOM   6877 C CB    . ASP B 1 358 ? 51.954 7.659   -55.174 1.00 35.15  ? 358 ASP B CB    1 
ATOM   6878 C CG    . ASP B 1 358 ? 52.642 7.308   -53.875 1.00 36.06  ? 358 ASP B CG    1 
ATOM   6879 O OD1   . ASP B 1 358 ? 53.854 6.962   -53.952 1.00 34.08  ? 358 ASP B OD1   1 
ATOM   6880 O OD2   . ASP B 1 358 ? 51.947 7.344   -52.819 1.00 33.58  ? 358 ASP B OD2   1 
ATOM   6881 N N     . LEU B 1 359 ? 51.912 4.547   -54.641 1.00 28.49  ? 359 LEU B N     1 
ATOM   6882 C CA    . LEU B 1 359 ? 51.386 3.388   -53.960 1.00 28.93  ? 359 LEU B CA    1 
ATOM   6883 C C     . LEU B 1 359 ? 50.418 3.779   -52.845 1.00 29.42  ? 359 LEU B C     1 
ATOM   6884 O O     . LEU B 1 359 ? 49.396 3.118   -52.662 1.00 26.20  ? 359 LEU B O     1 
ATOM   6885 C CB    . LEU B 1 359 ? 52.537 2.573   -53.369 1.00 32.35  ? 359 LEU B CB    1 
ATOM   6886 C CG    . LEU B 1 359 ? 52.048 1.419   -52.490 1.00 36.47  ? 359 LEU B CG    1 
ATOM   6887 C CD1   . LEU B 1 359 ? 51.634 0.245   -53.356 1.00 36.03  ? 359 LEU B CD1   1 
ATOM   6888 C CD2   . LEU B 1 359 ? 53.079 1.022   -51.467 1.00 40.73  ? 359 LEU B CD2   1 
ATOM   6889 N N     . LEU B 1 360 ? 50.751 4.811   -52.063 1.00 30.20  ? 360 LEU B N     1 
ATOM   6890 C CA    . LEU B 1 360 ? 49.891 5.141   -50.942 1.00 31.77  ? 360 LEU B CA    1 
ATOM   6891 C C     . LEU B 1 360 ? 48.589 5.754   -51.456 1.00 30.71  ? 360 LEU B C     1 
ATOM   6892 O O     . LEU B 1 360 ? 47.522 5.479   -50.912 1.00 31.92  ? 360 LEU B O     1 
ATOM   6893 C CB    . LEU B 1 360 ? 50.614 6.036   -49.927 1.00 31.75  ? 360 LEU B CB    1 
ATOM   6894 C CG    . LEU B 1 360 ? 49.735 6.565   -48.785 1.00 30.25  ? 360 LEU B CG    1 
ATOM   6895 C CD1   . LEU B 1 360 ? 49.123 5.422   -47.978 1.00 31.50  ? 360 LEU B CD1   1 
ATOM   6896 C CD2   . LEU B 1 360 ? 50.513 7.503   -47.856 1.00 29.56  ? 360 LEU B CD2   1 
ATOM   6897 N N     . LEU B 1 361 ? 48.650 6.567   -52.508 1.00 32.01  ? 361 LEU B N     1 
ATOM   6898 C CA    . LEU B 1 361 ? 47.424 7.133   -53.052 1.00 32.91  ? 361 LEU B CA    1 
ATOM   6899 C C     . LEU B 1 361 ? 46.571 5.992   -53.601 1.00 31.00  ? 361 LEU B C     1 
ATOM   6900 O O     . LEU B 1 361 ? 45.354 6.002   -53.470 1.00 30.80  ? 361 LEU B O     1 
ATOM   6901 C CB    . LEU B 1 361 ? 47.741 8.167   -54.136 1.00 36.67  ? 361 LEU B CB    1 
ATOM   6902 C CG    . LEU B 1 361 ? 48.680 9.315   -53.740 1.00 46.65  ? 361 LEU B CG    1 
ATOM   6903 C CD1   . LEU B 1 361 ? 48.755 10.354  -54.853 1.00 46.88  ? 361 LEU B CD1   1 
ATOM   6904 C CD2   . LEU B 1 361 ? 48.266 9.983   -52.431 1.00 48.72  ? 361 LEU B CD2   1 
ATOM   6905 N N     . HIS B 1 362 ? 47.221 4.987   -54.188 1.00 29.83  ? 362 HIS B N     1 
ATOM   6906 C CA    . HIS B 1 362 ? 46.522 3.832   -54.731 1.00 30.15  ? 362 HIS B CA    1 
ATOM   6907 C C     . HIS B 1 362 ? 45.820 3.074   -53.600 1.00 28.72  ? 362 HIS B C     1 
ATOM   6908 O O     . HIS B 1 362 ? 44.627 2.797   -53.687 1.00 29.06  ? 362 HIS B O     1 
ATOM   6909 C CB    . HIS B 1 362 ? 47.466 3.003   -55.618 1.00 29.96  ? 362 HIS B CB    1 
ATOM   6910 C CG    . HIS B 1 362 ? 46.920 1.700   -56.100 1.00 31.58  ? 362 HIS B CG    1 
ATOM   6911 N ND1   . HIS B 1 362 ? 47.026 0.554   -55.342 1.00 35.52  ? 362 HIS B ND1   1 
ATOM   6912 C CD2   . HIS B 1 362 ? 46.337 1.317   -57.256 1.00 35.56  ? 362 HIS B CD2   1 
ATOM   6913 C CE1   . HIS B 1 362 ? 46.489 -0.468  -55.998 1.00 35.28  ? 362 HIS B CE1   1 
ATOM   6914 N NE2   . HIS B 1 362 ? 46.060 -0.032  -57.169 1.00 33.96  ? 362 HIS B NE2   1 
ATOM   6915 N N     . ARG B 1 363 ? 46.536 2.764   -52.519 1.00 27.50  ? 363 ARG B N     1 
ATOM   6916 C CA    . ARG B 1 363 ? 45.965 1.909   -51.494 1.00 29.01  ? 363 ARG B CA    1 
ATOM   6917 C C     . ARG B 1 363 ? 45.002 2.704   -50.613 1.00 28.17  ? 363 ARG B C     1 
ATOM   6918 O O     . ARG B 1 363 ? 44.062 2.144   -50.055 1.00 26.78  ? 363 ARG B O     1 
ATOM   6919 C CB    . ARG B 1 363 ? 47.065 1.175   -50.727 1.00 32.13  ? 363 ARG B CB    1 
ATOM   6920 C CG    . ARG B 1 363 ? 47.793 0.140   -51.571 1.00 38.53  ? 363 ARG B CG    1 
ATOM   6921 C CD    . ARG B 1 363 ? 48.333 -1.050  -50.784 1.00 48.69  ? 363 ARG B CD    1 
ATOM   6922 N NE    . ARG B 1 363 ? 47.288 -1.795  -50.077 1.00 66.63  ? 363 ARG B NE    1 
ATOM   6923 C CZ    . ARG B 1 363 ? 46.342 -2.545  -50.653 1.00 68.68  ? 363 ARG B CZ    1 
ATOM   6924 N NH1   . ARG B 1 363 ? 46.350 -2.755  -51.961 1.00 66.09  ? 363 ARG B NH1   1 
ATOM   6925 N NH2   . ARG B 1 363 ? 45.409 -3.118  -49.907 1.00 65.83  ? 363 ARG B NH2   1 
ATOM   6926 N N     . ALA B 1 364 ? 45.179 4.023   -50.544 1.00 27.39  ? 364 ALA B N     1 
ATOM   6927 C CA    . ALA B 1 364 ? 44.243 4.854   -49.813 1.00 26.54  ? 364 ALA B CA    1 
ATOM   6928 C C     . ALA B 1 364 ? 42.820 4.653   -50.327 1.00 27.43  ? 364 ALA B C     1 
ATOM   6929 O O     . ALA B 1 364 ? 41.862 4.790   -49.564 1.00 28.43  ? 364 ALA B O     1 
ATOM   6930 C CB    . ALA B 1 364 ? 44.636 6.305   -49.915 1.00 26.84  ? 364 ALA B CB    1 
ATOM   6931 N N     . GLU B 1 365 ? 42.668 4.387   -51.626 1.00 27.97  ? 365 GLU B N     1 
ATOM   6932 C CA    . GLU B 1 365 ? 41.333 4.281   -52.204 1.00 31.32  ? 365 GLU B CA    1 
ATOM   6933 C C     . GLU B 1 365 ? 40.667 3.012   -51.679 1.00 28.16  ? 365 GLU B C     1 
ATOM   6934 O O     . GLU B 1 365 ? 39.501 3.009   -51.335 1.00 28.26  ? 365 GLU B O     1 
ATOM   6935 C CB    . GLU B 1 365 ? 41.402 4.292   -53.732 1.00 35.77  ? 365 GLU B CB    1 
ATOM   6936 C CG    . GLU B 1 365 ? 41.931 5.591   -54.313 1.00 42.24  ? 365 GLU B CG    1 
ATOM   6937 C CD    . GLU B 1 365 ? 40.881 6.673   -54.457 1.00 54.49  ? 365 GLU B CD    1 
ATOM   6938 O OE1   . GLU B 1 365 ? 40.660 7.434   -53.477 1.00 64.45  ? 365 GLU B OE1   1 
ATOM   6939 O OE2   . GLU B 1 365 ? 40.254 6.717   -55.543 1.00 62.12  ? 365 GLU B OE2   1 
ATOM   6940 N N     . THR B 1 366 ? 41.465 1.950   -51.583 1.00 27.99  ? 366 THR B N     1 
ATOM   6941 C CA    . THR B 1 366 ? 41.012 0.623   -51.222 1.00 25.73  ? 366 THR B CA    1 
ATOM   6942 C C     . THR B 1 366 ? 40.636 0.553   -49.751 1.00 23.29  ? 366 THR B C     1 
ATOM   6943 O O     . THR B 1 366 ? 39.771 -0.227  -49.360 1.00 22.24  ? 366 THR B O     1 
ATOM   6944 C CB    . THR B 1 366 ? 42.125 -0.375  -51.540 1.00 25.90  ? 366 THR B CB    1 
ATOM   6945 O OG1   . THR B 1 366 ? 42.469 -0.207  -52.918 1.00 29.89  ? 366 THR B OG1   1 
ATOM   6946 C CG2   . THR B 1 366 ? 41.709 -1.799  -51.289 1.00 26.93  ? 366 THR B CG2   1 
ATOM   6947 N N     . MET B 1 367 ? 41.346 1.340   -48.945 1.00 23.72  ? 367 MET B N     1 
ATOM   6948 C CA    . MET B 1 367 ? 41.193 1.316   -47.504 1.00 24.77  ? 367 MET B CA    1 
ATOM   6949 C C     . MET B 1 367 ? 40.023 2.230   -47.121 1.00 24.40  ? 367 MET B C     1 
ATOM   6950 O O     . MET B 1 367 ? 39.644 2.276   -45.957 1.00 24.14  ? 367 MET B O     1 
ATOM   6951 C CB    . MET B 1 367 ? 42.507 1.749   -46.825 1.00 26.65  ? 367 MET B CB    1 
ATOM   6952 C CG    . MET B 1 367 ? 43.572 0.645   -46.797 1.00 25.82  ? 367 MET B CG    1 
ATOM   6953 S SD    . MET B 1 367 ? 45.162 1.051   -46.017 1.00 25.95  ? 367 MET B SD    1 
ATOM   6954 C CE    . MET B 1 367 ? 45.551 2.619   -46.794 1.00 29.01  ? 367 MET B CE    1 
ATOM   6955 N N     . LYS B 1 368 ? 39.414 2.922   -48.096 1.00 23.50  ? 368 LYS B N     1 
ATOM   6956 C CA    . LYS B 1 368 ? 38.132 3.548   -47.826 1.00 27.91  ? 368 LYS B CA    1 
ATOM   6957 C C     . LYS B 1 368 ? 37.040 2.913   -48.680 1.00 27.43  ? 368 LYS B C     1 
ATOM   6958 O O     . LYS B 1 368 ? 35.941 3.437   -48.747 1.00 27.78  ? 368 LYS B O     1 
ATOM   6959 C CB    . LYS B 1 368 ? 38.166 5.079   -47.922 1.00 30.47  ? 368 LYS B CB    1 
ATOM   6960 C CG    . LYS B 1 368 ? 38.174 5.705   -49.309 1.00 37.37  ? 368 LYS B CG    1 
ATOM   6961 C CD    . LYS B 1 368 ? 38.260 7.233   -49.271 1.00 42.62  ? 368 LYS B CD    1 
ATOM   6962 C CE    . LYS B 1 368 ? 38.507 7.848   -50.634 1.00 53.37  ? 368 LYS B CE    1 
ATOM   6963 N NZ    . LYS B 1 368 ? 39.331 9.088   -50.577 1.00 58.82  ? 368 LYS B NZ    1 
ATOM   6964 N N     . GLY B 1 369 ? 37.298 1.738   -49.253 1.00 28.36  ? 369 GLY B N     1 
ATOM   6965 C CA    . GLY B 1 369 ? 36.216 0.961   -49.852 1.00 29.10  ? 369 GLY B CA    1 
ATOM   6966 C C     . GLY B 1 369 ? 35.812 1.429   -51.256 1.00 27.10  ? 369 GLY B C     1 
ATOM   6967 O O     . GLY B 1 369 ? 34.660 1.252   -51.617 1.00 24.50  ? 369 GLY B O     1 
ATOM   6968 N N     . VAL B 1 370 ? 36.761 1.954   -52.054 1.00 25.17  ? 370 VAL B N     1 
ATOM   6969 C CA    . VAL B 1 370 ? 36.503 2.369   -53.431 1.00 25.52  ? 370 VAL B CA    1 
ATOM   6970 C C     . VAL B 1 370 ? 36.893 1.243   -54.390 1.00 26.93  ? 370 VAL B C     1 
ATOM   6971 O O     . VAL B 1 370 ? 38.046 0.830   -54.418 1.00 23.96  ? 370 VAL B O     1 
ATOM   6972 C CB    . VAL B 1 370 ? 37.258 3.664   -53.804 1.00 25.66  ? 370 VAL B CB    1 
ATOM   6973 C CG1   . VAL B 1 370 ? 36.927 4.092   -55.221 1.00 25.33  ? 370 VAL B CG1   1 
ATOM   6974 C CG2   . VAL B 1 370 ? 36.959 4.807   -52.835 1.00 27.12  ? 370 VAL B CG2   1 
ATOM   6975 N N     . PRO B 1 371 ? 35.959 0.709   -55.210 1.00 28.36  ? 371 PRO B N     1 
ATOM   6976 C CA    . PRO B 1 371 ? 36.290 -0.352  -56.155 1.00 29.96  ? 371 PRO B CA    1 
ATOM   6977 C C     . PRO B 1 371 ? 36.998 0.185   -57.393 1.00 29.99  ? 371 PRO B C     1 
ATOM   6978 O O     . PRO B 1 371 ? 36.640 1.246   -57.896 1.00 30.59  ? 371 PRO B O     1 
ATOM   6979 C CB    . PRO B 1 371 ? 34.919 -0.943  -56.521 1.00 29.90  ? 371 PRO B CB    1 
ATOM   6980 C CG    . PRO B 1 371 ? 33.958 0.215   -56.366 1.00 29.19  ? 371 PRO B CG    1 
ATOM   6981 C CD    . PRO B 1 371 ? 34.530 1.060   -55.247 1.00 29.17  ? 371 PRO B CD    1 
ATOM   6982 N N     . LYS B 1 372 ? 38.000 -0.573  -57.857 1.00 30.98  ? 372 LYS B N     1 
ATOM   6983 C CA    . LYS B 1 372 ? 38.827 -0.219  -59.003 1.00 31.11  ? 372 LYS B CA    1 
ATOM   6984 C C     . LYS B 1 372 ? 39.354 -1.501  -59.655 1.00 26.23  ? 372 LYS B C     1 
ATOM   6985 O O     . LYS B 1 372 ? 39.095 -2.593  -59.171 1.00 23.39  ? 372 LYS B O     1 
ATOM   6986 C CB    . LYS B 1 372 ? 39.931 0.741   -58.551 1.00 33.47  ? 372 LYS B CB    1 
ATOM   6987 C CG    . LYS B 1 372 ? 39.475 2.182   -58.376 1.00 37.96  ? 372 LYS B CG    1 
ATOM   6988 C CD    . LYS B 1 372 ? 40.594 3.163   -58.242 1.00 44.67  ? 372 LYS B CD    1 
ATOM   6989 C CE    . LYS B 1 372 ? 40.159 4.586   -58.527 1.00 55.27  ? 372 LYS B CE    1 
ATOM   6990 N NZ    . LYS B 1 372 ? 41.220 5.566   -58.170 1.00 62.73  ? 372 LYS B NZ    1 
ATOM   6991 N N     . LEU B 1 373 ? 40.048 -1.369  -60.788 1.00 25.55  ? 373 LEU B N     1 
ATOM   6992 C CA    . LEU B 1 373 ? 40.624 -2.519  -61.476 1.00 26.53  ? 373 LEU B CA    1 
ATOM   6993 C C     . LEU B 1 373 ? 42.096 -2.304  -61.823 1.00 26.64  ? 373 LEU B C     1 
ATOM   6994 O O     . LEU B 1 373 ? 42.685 -3.131  -62.502 1.00 28.90  ? 373 LEU B O     1 
ATOM   6995 C CB    . LEU B 1 373 ? 39.782 -2.786  -62.729 1.00 27.36  ? 373 LEU B CB    1 
ATOM   6996 C CG    . LEU B 1 373 ? 38.405 -3.379  -62.435 1.00 25.28  ? 373 LEU B CG    1 
ATOM   6997 C CD1   . LEU B 1 373 ? 37.496 -3.304  -63.651 1.00 25.62  ? 373 LEU B CD1   1 
ATOM   6998 C CD2   . LEU B 1 373 ? 38.533 -4.805  -61.920 1.00 23.17  ? 373 LEU B CD2   1 
ATOM   6999 N N     . THR B 1 374 ? 42.692 -1.237  -61.281 1.00 28.42  ? 374 THR B N     1 
ATOM   7000 C CA    . THR B 1 374 ? 44.082 -0.876  -61.480 1.00 28.03  ? 374 THR B CA    1 
ATOM   7001 C C     . THR B 1 374 ? 45.031 -1.939  -60.956 1.00 29.06  ? 374 THR B C     1 
ATOM   7002 O O     . THR B 1 374 ? 46.123 -2.093  -61.501 1.00 30.39  ? 374 THR B O     1 
ATOM   7003 C CB    . THR B 1 374 ? 44.380 0.447   -60.780 1.00 29.33  ? 374 THR B CB    1 
ATOM   7004 O OG1   . THR B 1 374 ? 43.822 0.382   -59.464 1.00 30.24  ? 374 THR B OG1   1 
ATOM   7005 C CG2   . THR B 1 374 ? 43.792 1.624   -61.535 1.00 29.77  ? 374 THR B CG2   1 
ATOM   7006 N N     . GLU B 1 375 ? 44.632 -2.672  -59.904 1.00 29.26  ? 375 GLU B N     1 
ATOM   7007 C CA    . GLU B 1 375 ? 45.530 -3.670  -59.336 1.00 28.65  ? 375 GLU B CA    1 
ATOM   7008 C C     . GLU B 1 375 ? 46.034 -4.627  -60.421 1.00 27.73  ? 375 GLU B C     1 
ATOM   7009 O O     . GLU B 1 375 ? 47.157 -5.087  -60.325 1.00 27.01  ? 375 GLU B O     1 
ATOM   7010 C CB    . GLU B 1 375 ? 44.861 -4.469  -58.215 1.00 31.82  ? 375 GLU B CB    1 
ATOM   7011 C CG    . GLU B 1 375 ? 45.843 -5.114  -57.242 1.00 33.08  ? 375 GLU B CG    1 
ATOM   7012 C CD    . GLU B 1 375 ? 46.496 -4.185  -56.219 1.00 35.11  ? 375 GLU B CD    1 
ATOM   7013 O OE1   . GLU B 1 375 ? 46.225 -2.972  -56.254 1.00 40.64  ? 375 GLU B OE1   1 
ATOM   7014 O OE2   . GLU B 1 375 ? 47.275 -4.678  -55.380 1.00 35.95  ? 375 GLU B OE2   1 
ATOM   7015 N N     . PHE B 1 376 ? 45.234 -4.920  -61.463 1.00 28.95  ? 376 PHE B N     1 
ATOM   7016 C CA    . PHE B 1 376 ? 45.647 -5.866  -62.500 1.00 28.71  ? 376 PHE B CA    1 
ATOM   7017 C C     . PHE B 1 376 ? 46.912 -5.419  -63.231 1.00 30.15  ? 376 PHE B C     1 
ATOM   7018 O O     . PHE B 1 376 ? 47.548 -6.248  -63.888 1.00 31.56  ? 376 PHE B O     1 
ATOM   7019 C CB    . PHE B 1 376 ? 44.522 -6.121  -63.506 1.00 28.01  ? 376 PHE B CB    1 
ATOM   7020 C CG    . PHE B 1 376 ? 43.476 -7.074  -62.987 1.00 29.16  ? 376 PHE B CG    1 
ATOM   7021 C CD1   . PHE B 1 376 ? 43.774 -8.415  -62.813 1.00 28.80  ? 376 PHE B CD1   1 
ATOM   7022 C CD2   . PHE B 1 376 ? 42.231 -6.617  -62.597 1.00 28.17  ? 376 PHE B CD2   1 
ATOM   7023 C CE1   . PHE B 1 376 ? 42.834 -9.292  -62.308 1.00 28.21  ? 376 PHE B CE1   1 
ATOM   7024 C CE2   . PHE B 1 376 ? 41.289 -7.490  -62.087 1.00 29.11  ? 376 PHE B CE2   1 
ATOM   7025 C CZ    . PHE B 1 376 ? 41.591 -8.829  -61.953 1.00 31.01  ? 376 PHE B CZ    1 
ATOM   7026 N N     . ASN B 1 377 ? 47.288 -4.135  -63.124 1.00 29.61  ? 377 ASN B N     1 
ATOM   7027 C CA    . ASN B 1 377 ? 48.493 -3.649  -63.786 1.00 32.11  ? 377 ASN B CA    1 
ATOM   7028 C C     . ASN B 1 377 ? 49.768 -4.301  -63.231 1.00 30.42  ? 377 ASN B C     1 
ATOM   7029 O O     . ASN B 1 377 ? 50.761 -4.353  -63.947 1.00 27.66  ? 377 ASN B O     1 
ATOM   7030 C CB    . ASN B 1 377 ? 48.578 -2.120  -63.766 1.00 35.22  ? 377 ASN B CB    1 
ATOM   7031 C CG    . ASN B 1 377 ? 47.626 -1.517  -64.778 1.00 35.49  ? 377 ASN B CG    1 
ATOM   7032 O OD1   . ASN B 1 377 ? 47.802 -1.705  -65.977 1.00 35.58  ? 377 ASN B OD1   1 
ATOM   7033 N ND2   . ASN B 1 377 ? 46.585 -0.849  -64.310 1.00 35.76  ? 377 ASN B ND2   1 
ATOM   7034 N N     . PHE B 1 378 ? 49.740 -4.856  -62.009 1.00 28.47  ? 378 PHE B N     1 
ATOM   7035 C CA    . PHE B 1 378 ? 50.930 -5.480  -61.457 1.00 30.31  ? 378 PHE B CA    1 
ATOM   7036 C C     . PHE B 1 378 ? 51.294 -6.756  -62.209 1.00 29.54  ? 378 PHE B C     1 
ATOM   7037 O O     . PHE B 1 378 ? 52.430 -7.176  -62.099 1.00 28.60  ? 378 PHE B O     1 
ATOM   7038 C CB    . PHE B 1 378 ? 50.806 -5.750  -59.959 1.00 34.76  ? 378 PHE B CB    1 
ATOM   7039 C CG    . PHE B 1 378 ? 50.311 -7.119  -59.564 1.00 39.75  ? 378 PHE B CG    1 
ATOM   7040 C CD1   . PHE B 1 378 ? 48.991 -7.486  -59.744 1.00 46.02  ? 378 PHE B CD1   1 
ATOM   7041 C CD2   . PHE B 1 378 ? 51.166 -8.038  -58.982 1.00 44.14  ? 378 PHE B CD2   1 
ATOM   7042 C CE1   . PHE B 1 378 ? 48.547 -8.748  -59.385 1.00 49.05  ? 378 PHE B CE1   1 
ATOM   7043 C CE2   . PHE B 1 378 ? 50.716 -9.297  -58.619 1.00 48.60  ? 378 PHE B CE2   1 
ATOM   7044 C CZ    . PHE B 1 378 ? 49.406 -9.652  -58.822 1.00 46.38  ? 378 PHE B CZ    1 
ATOM   7045 N N     . LEU B 1 379 ? 50.350 -7.341  -62.964 1.00 29.56  ? 379 LEU B N     1 
ATOM   7046 C CA    . LEU B 1 379 ? 50.579 -8.520  -63.793 1.00 31.84  ? 379 LEU B CA    1 
ATOM   7047 C C     . LEU B 1 379 ? 51.559 -8.242  -64.937 1.00 32.98  ? 379 LEU B C     1 
ATOM   7048 O O     . LEU B 1 379 ? 52.064 -9.176  -65.552 1.00 33.78  ? 379 LEU B O     1 
ATOM   7049 C CB    . LEU B 1 379 ? 49.241 -8.975  -64.390 1.00 32.73  ? 379 LEU B CB    1 
ATOM   7050 C CG    . LEU B 1 379 ? 48.259 -9.598  -63.404 1.00 33.73  ? 379 LEU B CG    1 
ATOM   7051 C CD1   . LEU B 1 379 ? 47.014 -10.092 -64.124 1.00 30.19  ? 379 LEU B CD1   1 
ATOM   7052 C CD2   . LEU B 1 379 ? 48.922 -10.742 -62.641 1.00 37.43  ? 379 LEU B CD2   1 
ATOM   7053 N N     . ASN B 1 380 ? 51.797 -6.966  -65.250 1.00 33.38  ? 380 ASN B N     1 
ATOM   7054 C CA    . ASN B 1 380 ? 52.725 -6.609  -66.310 1.00 36.36  ? 380 ASN B CA    1 
ATOM   7055 C C     . ASN B 1 380 ? 54.153 -6.492  -65.796 1.00 34.18  ? 380 ASN B C     1 
ATOM   7056 O O     . ASN B 1 380 ? 54.997 -6.018  -66.542 1.00 39.12  ? 380 ASN B O     1 
ATOM   7057 C CB    . ASN B 1 380 ? 52.358 -5.284  -66.990 1.00 37.91  ? 380 ASN B CB    1 
ATOM   7058 C CG    . ASN B 1 380 ? 51.085 -5.379  -67.801 1.00 38.66  ? 380 ASN B CG    1 
ATOM   7059 O OD1   . ASN B 1 380 ? 50.867 -6.350  -68.527 1.00 42.72  ? 380 ASN B OD1   1 
ATOM   7060 N ND2   . ASN B 1 380 ? 50.216 -4.402  -67.637 1.00 38.16  ? 380 ASN B ND2   1 
ATOM   7061 N N     . TRP B 1 381 ? 54.442 -6.908  -64.557 1.00 34.71  ? 381 TRP B N     1 
ATOM   7062 C CA    . TRP B 1 381 ? 55.800 -6.793  -64.032 1.00 34.32  ? 381 TRP B CA    1 
ATOM   7063 C C     . TRP B 1 381 ? 56.814 -7.355  -65.032 1.00 36.50  ? 381 TRP B C     1 
ATOM   7064 O O     . TRP B 1 381 ? 57.787 -6.681  -65.353 1.00 35.94  ? 381 TRP B O     1 
ATOM   7065 C CB    . TRP B 1 381 ? 55.952 -7.496  -62.679 1.00 33.27  ? 381 TRP B CB    1 
ATOM   7066 C CG    . TRP B 1 381 ? 57.349 -7.418  -62.139 1.00 35.98  ? 381 TRP B CG    1 
ATOM   7067 C CD1   . TRP B 1 381 ? 58.218 -8.452  -61.948 1.00 33.60  ? 381 TRP B CD1   1 
ATOM   7068 C CD2   . TRP B 1 381 ? 58.065 -6.225  -61.765 1.00 35.20  ? 381 TRP B CD2   1 
ATOM   7069 N NE1   . TRP B 1 381 ? 59.398 -7.991  -61.439 1.00 34.03  ? 381 TRP B NE1   1 
ATOM   7070 C CE2   . TRP B 1 381 ? 59.341 -6.629  -61.338 1.00 32.60  ? 381 TRP B CE2   1 
ATOM   7071 C CE3   . TRP B 1 381 ? 57.744 -4.864  -61.750 1.00 35.84  ? 381 TRP B CE3   1 
ATOM   7072 C CZ2   . TRP B 1 381 ? 60.290 -5.727  -60.872 1.00 33.49  ? 381 TRP B CZ2   1 
ATOM   7073 C CZ3   . TRP B 1 381 ? 58.686 -3.969  -61.305 1.00 35.92  ? 381 TRP B CZ3   1 
ATOM   7074 C CH2   . TRP B 1 381 ? 59.940 -4.400  -60.868 1.00 37.10  ? 381 TRP B CH2   1 
ATOM   7075 N N     . ASP B 1 382 ? 56.559 -8.577  -65.527 1.00 39.39  ? 382 ASP B N     1 
ATOM   7076 C CA    . ASP B 1 382 ? 57.532 -9.320  -66.314 1.00 43.42  ? 382 ASP B CA    1 
ATOM   7077 C C     . ASP B 1 382 ? 57.009 -9.523  -67.731 1.00 39.76  ? 382 ASP B C     1 
ATOM   7078 O O     . ASP B 1 382 ? 57.170 -10.581 -68.318 1.00 40.69  ? 382 ASP B O     1 
ATOM   7079 C CB    . ASP B 1 382 ? 57.848 -10.684 -65.682 1.00 48.70  ? 382 ASP B CB    1 
ATOM   7080 C CG    . ASP B 1 382 ? 59.334 -10.948 -65.501 1.00 58.29  ? 382 ASP B CG    1 
ATOM   7081 O OD1   . ASP B 1 382 ? 60.120 -10.513 -66.367 1.00 64.17  ? 382 ASP B OD1   1 
ATOM   7082 O OD2   . ASP B 1 382 ? 59.698 -11.578 -64.482 1.00 72.04  ? 382 ASP B OD2   1 
ATOM   7083 N N     . GLY B 1 383 ? 56.350 -8.519  -68.285 1.00 36.76  ? 383 GLY B N     1 
ATOM   7084 C CA    . GLY B 1 383 ? 55.900 -8.651  -69.653 1.00 40.01  ? 383 GLY B CA    1 
ATOM   7085 C C     . GLY B 1 383 ? 54.395 -8.856  -69.768 1.00 44.32  ? 383 GLY B C     1 
ATOM   7086 O O     . GLY B 1 383 ? 53.805 -8.459  -70.768 1.00 49.63  ? 383 GLY B O     1 
ATOM   7087 N N     . GLY B 1 384 ? 53.778 -9.459  -68.748 1.00 41.95  ? 384 GLY B N     1 
ATOM   7088 C CA    . GLY B 1 384 ? 52.362 -9.776  -68.798 1.00 38.85  ? 384 GLY B CA    1 
ATOM   7089 C C     . GLY B 1 384 ? 52.163 -11.234 -68.423 1.00 39.39  ? 384 GLY B C     1 
ATOM   7090 O O     . GLY B 1 384 ? 52.823 -12.105 -68.978 1.00 41.97  ? 384 GLY B O     1 
ATOM   7091 N N     . GLY B 1 385 ? 51.286 -11.493 -67.453 1.00 36.24  ? 385 GLY B N     1 
ATOM   7092 C CA    . GLY B 1 385 ? 50.992 -12.867 -67.092 1.00 35.01  ? 385 GLY B CA    1 
ATOM   7093 C C     . GLY B 1 385 ? 49.716 -12.977 -66.271 1.00 33.50  ? 385 GLY B C     1 
ATOM   7094 O O     . GLY B 1 385 ? 48.943 -12.032 -66.206 1.00 32.68  ? 385 GLY B O     1 
ATOM   7095 N N     . GLY B 1 386 ? 49.506 -14.166 -65.695 1.00 32.84  ? 386 GLY B N     1 
ATOM   7096 C CA    . GLY B 1 386 ? 48.515 -14.378 -64.654 1.00 30.58  ? 386 GLY B CA    1 
ATOM   7097 C C     . GLY B 1 386 ? 49.182 -14.444 -63.282 1.00 26.50  ? 386 GLY B C     1 
ATOM   7098 O O     . GLY B 1 386 ? 50.390 -14.283 -63.159 1.00 26.78  ? 386 GLY B O     1 
ATOM   7099 N N     . HIS B 1 387 ? 48.377 -14.648 -62.249 1.00 24.94  ? 387 HIS B N     1 
ATOM   7100 C CA    . HIS B 1 387 ? 48.894 -14.812 -60.905 1.00 25.65  ? 387 HIS B CA    1 
ATOM   7101 C C     . HIS B 1 387 ? 48.177 -15.953 -60.178 1.00 24.79  ? 387 HIS B C     1 
ATOM   7102 O O     . HIS B 1 387 ? 47.064 -16.349 -60.517 1.00 28.04  ? 387 HIS B O     1 
ATOM   7103 C CB    . HIS B 1 387 ? 48.830 -13.487 -60.136 1.00 25.66  ? 387 HIS B CB    1 
ATOM   7104 C CG    . HIS B 1 387 ? 47.477 -12.991 -59.688 1.00 25.57  ? 387 HIS B CG    1 
ATOM   7105 N ND1   . HIS B 1 387 ? 47.179 -12.901 -58.339 1.00 25.62  ? 387 HIS B ND1   1 
ATOM   7106 C CD2   . HIS B 1 387 ? 46.416 -12.476 -60.352 1.00 28.36  ? 387 HIS B CD2   1 
ATOM   7107 C CE1   . HIS B 1 387 ? 45.961 -12.397 -58.157 1.00 26.70  ? 387 HIS B CE1   1 
ATOM   7108 N NE2   . HIS B 1 387 ? 45.420 -12.094 -59.399 1.00 28.76  ? 387 HIS B NE2   1 
ATOM   7109 N N     . VAL B 1 388 ? 48.868 -16.476 -59.169 1.00 24.70  ? 388 VAL B N     1 
ATOM   7110 C CA    . VAL B 1 388 ? 48.322 -17.417 -58.213 1.00 24.11  ? 388 VAL B CA    1 
ATOM   7111 C C     . VAL B 1 388 ? 49.032 -17.110 -56.906 1.00 25.12  ? 388 VAL B C     1 
ATOM   7112 O O     . VAL B 1 388 ? 50.129 -16.577 -56.935 1.00 26.41  ? 388 VAL B O     1 
ATOM   7113 C CB    . VAL B 1 388 ? 48.563 -18.867 -58.664 1.00 24.94  ? 388 VAL B CB    1 
ATOM   7114 C CG1   . VAL B 1 388 ? 50.043 -19.219 -58.646 1.00 25.07  ? 388 VAL B CG1   1 
ATOM   7115 C CG2   . VAL B 1 388 ? 47.780 -19.852 -57.829 1.00 25.66  ? 388 VAL B CG2   1 
ATOM   7116 N N     . GLY B 1 389 ? 48.388 -17.400 -55.778 1.00 26.16  ? 389 GLY B N     1 
ATOM   7117 C CA    . GLY B 1 389 ? 48.878 -16.989 -54.481 1.00 23.33  ? 389 GLY B CA    1 
ATOM   7118 C C     . GLY B 1 389 ? 48.913 -18.159 -53.512 1.00 26.00  ? 389 GLY B C     1 
ATOM   7119 O O     . GLY B 1 389 ? 48.285 -19.193 -53.726 1.00 24.92  ? 389 GLY B O     1 
ATOM   7120 N N     . PHE B 1 390 ? 49.701 -17.997 -52.451 1.00 29.60  ? 390 PHE B N     1 
ATOM   7121 C CA    . PHE B 1 390 ? 49.805 -19.008 -51.421 1.00 30.30  ? 390 PHE B CA    1 
ATOM   7122 C C     . PHE B 1 390 ? 49.832 -18.224 -50.128 1.00 29.92  ? 390 PHE B C     1 
ATOM   7123 O O     . PHE B 1 390 ? 50.703 -17.384 -49.973 1.00 33.83  ? 390 PHE B O     1 
ATOM   7124 C CB    . PHE B 1 390 ? 51.034 -19.905 -51.649 1.00 32.14  ? 390 PHE B CB    1 
ATOM   7125 C CG    . PHE B 1 390 ? 51.229 -20.955 -50.580 1.00 34.08  ? 390 PHE B CG    1 
ATOM   7126 C CD1   . PHE B 1 390 ? 50.251 -21.913 -50.343 1.00 36.94  ? 390 PHE B CD1   1 
ATOM   7127 C CD2   . PHE B 1 390 ? 52.354 -20.947 -49.765 1.00 32.57  ? 390 PHE B CD2   1 
ATOM   7128 C CE1   . PHE B 1 390 ? 50.395 -22.843 -49.321 1.00 38.81  ? 390 PHE B CE1   1 
ATOM   7129 C CE2   . PHE B 1 390 ? 52.500 -21.878 -48.751 1.00 32.33  ? 390 PHE B CE2   1 
ATOM   7130 C CZ    . PHE B 1 390 ? 51.525 -22.829 -48.537 1.00 36.79  ? 390 PHE B CZ    1 
ATOM   7131 N N     . SER B 1 391 ? 48.851 -18.475 -49.259 1.00 31.15  ? 391 SER B N     1 
ATOM   7132 C CA    . SER B 1 391 ? 48.514 -17.577 -48.166 1.00 31.33  ? 391 SER B CA    1 
ATOM   7133 C C     . SER B 1 391 ? 48.250 -18.340 -46.859 1.00 30.22  ? 391 SER B C     1 
ATOM   7134 O O     . SER B 1 391 ? 47.285 -18.073 -46.151 1.00 28.20  ? 391 SER B O     1 
ATOM   7135 C CB    . SER B 1 391 ? 47.336 -16.745 -48.567 1.00 32.31  ? 391 SER B CB    1 
ATOM   7136 O OG    . SER B 1 391 ? 46.259 -17.590 -48.938 1.00 34.81  ? 391 SER B OG    1 
ATOM   7137 N N     . PRO B 1 392 ? 49.180 -19.204 -46.396 1.00 29.26  ? 392 PRO B N     1 
ATOM   7138 C CA    . PRO B 1 392 ? 48.960 -19.944 -45.159 1.00 26.61  ? 392 PRO B CA    1 
ATOM   7139 C C     . PRO B 1 392 ? 48.990 -19.043 -43.926 1.00 26.93  ? 392 PRO B C     1 
ATOM   7140 O O     . PRO B 1 392 ? 49.449 -17.911 -43.964 1.00 30.36  ? 392 PRO B O     1 
ATOM   7141 C CB    . PRO B 1 392 ? 50.159 -20.890 -45.167 1.00 26.57  ? 392 PRO B CB    1 
ATOM   7142 C CG    . PRO B 1 392 ? 51.254 -20.030 -45.772 1.00 24.91  ? 392 PRO B CG    1 
ATOM   7143 C CD    . PRO B 1 392 ? 50.541 -19.394 -46.940 1.00 26.27  ? 392 PRO B CD    1 
ATOM   7144 N N     . VAL B 1 393 ? 48.531 -19.614 -42.827 1.00 26.76  ? 393 VAL B N     1 
ATOM   7145 C CA    . VAL B 1 393 ? 48.405 -18.967 -41.538 1.00 27.42  ? 393 VAL B CA    1 
ATOM   7146 C C     . VAL B 1 393 ? 49.594 -19.351 -40.647 1.00 27.38  ? 393 VAL B C     1 
ATOM   7147 O O     . VAL B 1 393 ? 49.928 -20.535 -40.545 1.00 22.03  ? 393 VAL B O     1 
ATOM   7148 C CB    . VAL B 1 393 ? 47.099 -19.434 -40.878 1.00 27.08  ? 393 VAL B CB    1 
ATOM   7149 C CG1   . VAL B 1 393 ? 46.851 -18.694 -39.591 1.00 29.57  ? 393 VAL B CG1   1 
ATOM   7150 C CG2   . VAL B 1 393 ? 45.916 -19.310 -41.818 1.00 31.21  ? 393 VAL B CG2   1 
ATOM   7151 N N     . SER B 1 394 ? 50.176 -18.337 -39.980 1.00 26.39  ? 394 SER B N     1 
ATOM   7152 C CA    . SER B 1 394 ? 51.240 -18.506 -39.006 1.00 25.76  ? 394 SER B CA    1 
ATOM   7153 C C     . SER B 1 394 ? 50.953 -17.611 -37.809 1.00 27.48  ? 394 SER B C     1 
ATOM   7154 O O     . SER B 1 394 ? 50.231 -16.625 -37.933 1.00 30.53  ? 394 SER B O     1 
ATOM   7155 C CB    . SER B 1 394 ? 52.569 -18.127 -39.612 1.00 26.50  ? 394 SER B CB    1 
ATOM   7156 O OG    . SER B 1 394 ? 52.563 -16.769 -40.044 1.00 26.64  ? 394 SER B OG    1 
ATOM   7157 N N     . PRO B 1 395 ? 51.543 -17.874 -36.629 1.00 28.35  ? 395 PRO B N     1 
ATOM   7158 C CA    . PRO B 1 395 ? 51.490 -16.916 -35.518 1.00 29.28  ? 395 PRO B CA    1 
ATOM   7159 C C     . PRO B 1 395 ? 52.111 -15.574 -35.904 1.00 29.35  ? 395 PRO B C     1 
ATOM   7160 O O     . PRO B 1 395 ? 53.051 -15.562 -36.698 1.00 27.76  ? 395 PRO B O     1 
ATOM   7161 C CB    . PRO B 1 395 ? 52.301 -17.574 -34.392 1.00 28.55  ? 395 PRO B CB    1 
ATOM   7162 C CG    . PRO B 1 395 ? 52.403 -19.044 -34.780 1.00 29.41  ? 395 PRO B CG    1 
ATOM   7163 C CD    . PRO B 1 395 ? 52.251 -19.111 -36.288 1.00 29.26  ? 395 PRO B CD    1 
ATOM   7164 N N     . ILE B 1 396 ? 51.586 -14.465 -35.347 1.00 31.14  ? 396 ILE B N     1 
ATOM   7165 C CA    . ILE B 1 396 ? 52.165 -13.140 -35.572 1.00 30.50  ? 396 ILE B CA    1 
ATOM   7166 C C     . ILE B 1 396 ? 53.447 -13.044 -34.750 1.00 31.10  ? 396 ILE B C     1 
ATOM   7167 O O     . ILE B 1 396 ? 53.457 -12.496 -33.655 1.00 28.10  ? 396 ILE B O     1 
ATOM   7168 C CB    . ILE B 1 396 ? 51.229 -11.971 -35.206 1.00 29.84  ? 396 ILE B CB    1 
ATOM   7169 C CG1   . ILE B 1 396 ? 49.807 -12.139 -35.734 1.00 32.95  ? 396 ILE B CG1   1 
ATOM   7170 C CG2   . ILE B 1 396 ? 51.822 -10.658 -35.682 1.00 29.98  ? 396 ILE B CG2   1 
ATOM   7171 C CD1   . ILE B 1 396 ? 48.795 -11.322 -34.965 1.00 32.71  ? 396 ILE B CD1   1 
ATOM   7172 N N     . THR B 1 397 ? 54.530 -13.576 -35.313 1.00 31.59  ? 397 THR B N     1 
ATOM   7173 C CA    . THR B 1 397 ? 55.822 -13.632 -34.659 1.00 30.01  ? 397 THR B CA    1 
ATOM   7174 C C     . THR B 1 397 ? 56.850 -13.168 -35.683 1.00 28.83  ? 397 THR B C     1 
ATOM   7175 O O     . THR B 1 397 ? 56.690 -13.451 -36.863 1.00 23.62  ? 397 THR B O     1 
ATOM   7176 C CB    . THR B 1 397 ? 56.009 -15.058 -34.130 1.00 31.16  ? 397 THR B CB    1 
ATOM   7177 O OG1   . THR B 1 397 ? 55.546 -15.159 -32.787 1.00 31.84  ? 397 THR B OG1   1 
ATOM   7178 C CG2   . THR B 1 397 ? 57.417 -15.567 -34.172 1.00 29.81  ? 397 THR B CG2   1 
ATOM   7179 N N     . GLY B 1 398 ? 57.876 -12.444 -35.219 1.00 28.73  ? 398 GLY B N     1 
ATOM   7180 C CA    . GLY B 1 398 ? 59.024 -12.113 -36.040 1.00 29.08  ? 398 GLY B CA    1 
ATOM   7181 C C     . GLY B 1 398 ? 59.678 -13.343 -36.675 1.00 29.95  ? 398 GLY B C     1 
ATOM   7182 O O     . GLY B 1 398 ? 59.978 -13.333 -37.877 1.00 25.78  ? 398 GLY B O     1 
ATOM   7183 N N     . LYS B 1 399 ? 59.900 -14.383 -35.859 1.00 30.69  ? 399 LYS B N     1 
ATOM   7184 C CA    . LYS B 1 399 ? 60.541 -15.611 -36.317 1.00 34.30  ? 399 LYS B CA    1 
ATOM   7185 C C     . LYS B 1 399 ? 59.726 -16.276 -37.422 1.00 28.76  ? 399 LYS B C     1 
ATOM   7186 O O     . LYS B 1 399 ? 60.292 -16.725 -38.415 1.00 28.71  ? 399 LYS B O     1 
ATOM   7187 C CB    . LYS B 1 399 ? 60.761 -16.589 -35.157 1.00 40.65  ? 399 LYS B CB    1 
ATOM   7188 C CG    . LYS B 1 399 ? 61.864 -16.150 -34.208 1.00 53.05  ? 399 LYS B CG    1 
ATOM   7189 C CD    . LYS B 1 399 ? 62.168 -17.138 -33.117 1.00 63.67  ? 399 LYS B CD    1 
ATOM   7190 C CE    . LYS B 1 399 ? 63.158 -16.594 -32.108 1.00 70.06  ? 399 LYS B CE    1 
ATOM   7191 N NZ    . LYS B 1 399 ? 62.921 -17.192 -30.771 1.00 75.98  ? 399 LYS B NZ    1 
ATOM   7192 N N     . ASP B 1 400 ? 58.407 -16.355 -37.251 1.00 26.41  ? 400 ASP B N     1 
ATOM   7193 C CA    . ASP B 1 400 ? 57.558 -16.974 -38.262 1.00 26.80  ? 400 ASP B CA    1 
ATOM   7194 C C     . ASP B 1 400 ? 57.583 -16.139 -39.528 1.00 25.20  ? 400 ASP B C     1 
ATOM   7195 O O     . ASP B 1 400 ? 57.560 -16.679 -40.630 1.00 23.51  ? 400 ASP B O     1 
ATOM   7196 C CB    . ASP B 1 400 ? 56.110 -17.133 -37.808 1.00 25.96  ? 400 ASP B CB    1 
ATOM   7197 C CG    . ASP B 1 400 ? 55.980 -18.134 -36.680 1.00 26.68  ? 400 ASP B CG    1 
ATOM   7198 O OD1   . ASP B 1 400 ? 56.129 -19.350 -36.949 1.00 24.46  ? 400 ASP B OD1   1 
ATOM   7199 O OD2   . ASP B 1 400 ? 55.749 -17.684 -35.542 1.00 27.24  ? 400 ASP B OD2   1 
ATOM   7200 N N     . ALA B 1 401 ? 57.650 -14.821 -39.363 1.00 27.16  ? 401 ALA B N     1 
ATOM   7201 C CA    . ALA B 1 401 ? 57.563 -13.946 -40.519 1.00 31.46  ? 401 ALA B CA    1 
ATOM   7202 C C     . ALA B 1 401 ? 58.826 -14.084 -41.366 1.00 29.39  ? 401 ALA B C     1 
ATOM   7203 O O     . ALA B 1 401 ? 58.742 -14.182 -42.581 1.00 30.65  ? 401 ALA B O     1 
ATOM   7204 C CB    . ALA B 1 401 ? 57.311 -12.513 -40.096 1.00 31.76  ? 401 ALA B CB    1 
ATOM   7205 N N     . ILE B 1 402 ? 59.995 -14.097 -40.729 1.00 29.75  ? 402 ILE B N     1 
ATOM   7206 C CA    . ILE B 1 402 ? 61.234 -14.082 -41.480 1.00 29.32  ? 402 ILE B CA    1 
ATOM   7207 C C     . ILE B 1 402 ? 61.596 -15.491 -41.955 1.00 28.37  ? 402 ILE B C     1 
ATOM   7208 O O     . ILE B 1 402 ? 62.217 -15.644 -43.007 1.00 27.70  ? 402 ILE B O     1 
ATOM   7209 C CB    . ILE B 1 402 ? 62.371 -13.413 -40.684 1.00 33.16  ? 402 ILE B CB    1 
ATOM   7210 C CG1   . ILE B 1 402 ? 63.500 -13.002 -41.637 1.00 36.12  ? 402 ILE B CG1   1 
ATOM   7211 C CG2   . ILE B 1 402 ? 62.852 -14.295 -39.538 1.00 30.31  ? 402 ILE B CG2   1 
ATOM   7212 C CD1   . ILE B 1 402 ? 64.708 -12.473 -40.946 1.00 40.38  ? 402 ILE B CD1   1 
ATOM   7213 N N     . LYS B 1 403 ? 61.214 -16.520 -41.194 1.00 26.82  ? 403 LYS B N     1 
ATOM   7214 C CA    . LYS B 1 403 ? 61.377 -17.877 -41.678 1.00 30.07  ? 403 LYS B CA    1 
ATOM   7215 C C     . LYS B 1 403 ? 60.660 -18.034 -43.023 1.00 31.81  ? 403 LYS B C     1 
ATOM   7216 O O     . LYS B 1 403 ? 61.255 -18.489 -44.002 1.00 28.63  ? 403 LYS B O     1 
ATOM   7217 C CB    . LYS B 1 403 ? 60.836 -18.886 -40.671 1.00 34.38  ? 403 LYS B CB    1 
ATOM   7218 C CG    . LYS B 1 403 ? 61.227 -20.322 -40.972 1.00 37.70  ? 403 LYS B CG    1 
ATOM   7219 C CD    . LYS B 1 403 ? 60.218 -21.304 -40.461 1.00 46.30  ? 403 LYS B CD    1 
ATOM   7220 C CE    . LYS B 1 403 ? 60.219 -21.485 -38.955 1.00 51.51  ? 403 LYS B CE    1 
ATOM   7221 N NZ    . LYS B 1 403 ? 59.176 -22.474 -38.562 1.00 52.96  ? 403 LYS B NZ    1 
ATOM   7222 N N     . GLN B 1 404 ? 59.390 -17.606 -43.075 1.00 30.60  ? 404 GLN B N     1 
ATOM   7223 C CA    . GLN B 1 404 ? 58.580 -17.748 -44.282 1.00 30.79  ? 404 GLN B CA    1 
ATOM   7224 C C     . GLN B 1 404 ? 59.120 -16.905 -45.444 1.00 30.95  ? 404 GLN B C     1 
ATOM   7225 O O     . GLN B 1 404 ? 59.208 -17.385 -46.569 1.00 33.26  ? 404 GLN B O     1 
ATOM   7226 C CB    . GLN B 1 404 ? 57.129 -17.426 -43.947 1.00 27.37  ? 404 GLN B CB    1 
ATOM   7227 C CG    . GLN B 1 404 ? 56.435 -18.574 -43.245 1.00 27.55  ? 404 GLN B CG    1 
ATOM   7228 C CD    . GLN B 1 404 ? 55.051 -18.168 -42.805 1.00 29.71  ? 404 GLN B CD    1 
ATOM   7229 O OE1   . GLN B 1 404 ? 54.042 -18.410 -43.478 1.00 29.57  ? 404 GLN B OE1   1 
ATOM   7230 N NE2   . GLN B 1 404 ? 55.009 -17.492 -41.666 1.00 30.86  ? 404 GLN B NE2   1 
ATOM   7231 N N     . TYR B 1 405 ? 59.492 -15.651 -45.185 1.00 29.70  ? 405 TYR B N     1 
ATOM   7232 C CA    . TYR B 1 405 ? 60.109 -14.839 -46.215 1.00 30.37  ? 405 TYR B CA    1 
ATOM   7233 C C     . TYR B 1 405 ? 61.377 -15.538 -46.747 1.00 30.14  ? 405 TYR B C     1 
ATOM   7234 O O     . TYR B 1 405 ? 61.571 -15.659 -47.948 1.00 26.31  ? 405 TYR B O     1 
ATOM   7235 C CB    . TYR B 1 405 ? 60.373 -13.422 -45.686 1.00 31.49  ? 405 TYR B CB    1 
ATOM   7236 C CG    . TYR B 1 405 ? 61.400 -12.683 -46.509 1.00 33.00  ? 405 TYR B CG    1 
ATOM   7237 C CD1   . TYR B 1 405 ? 61.122 -12.300 -47.812 1.00 34.20  ? 405 TYR B CD1   1 
ATOM   7238 C CD2   . TYR B 1 405 ? 62.680 -12.463 -46.033 1.00 36.57  ? 405 TYR B CD2   1 
ATOM   7239 C CE1   . TYR B 1 405 ? 62.068 -11.671 -48.603 1.00 34.25  ? 405 TYR B CE1   1 
ATOM   7240 C CE2   . TYR B 1 405 ? 63.637 -11.824 -46.809 1.00 39.42  ? 405 TYR B CE2   1 
ATOM   7241 C CZ    . TYR B 1 405 ? 63.331 -11.438 -48.102 1.00 36.63  ? 405 TYR B CZ    1 
ATOM   7242 O OH    . TYR B 1 405 ? 64.268 -10.832 -48.891 1.00 36.13  ? 405 TYR B OH    1 
ATOM   7243 N N     . ASN B 1 406 ? 62.279 -15.976 -45.861 1.00 31.27  ? 406 ASN B N     1 
ATOM   7244 C CA    . ASN B 1 406 ? 63.472 -16.698 -46.285 1.00 31.28  ? 406 ASN B CA    1 
ATOM   7245 C C     . ASN B 1 406 ? 63.095 -17.939 -47.104 1.00 31.08  ? 406 ASN B C     1 
ATOM   7246 O O     . ASN B 1 406 ? 63.584 -18.096 -48.223 1.00 32.22  ? 406 ASN B O     1 
ATOM   7247 C CB    . ASN B 1 406 ? 64.361 -17.041 -45.087 1.00 31.65  ? 406 ASN B CB    1 
ATOM   7248 C CG    . ASN B 1 406 ? 65.119 -15.846 -44.549 1.00 34.31  ? 406 ASN B CG    1 
ATOM   7249 O OD1   . ASN B 1 406 ? 65.437 -14.906 -45.273 1.00 35.58  ? 406 ASN B OD1   1 
ATOM   7250 N ND2   . ASN B 1 406 ? 65.459 -15.887 -43.274 1.00 37.64  ? 406 ASN B ND2   1 
ATOM   7251 N N     . MET B 1 407 ? 62.208 -18.789 -46.564 1.00 31.54  ? 407 MET B N     1 
ATOM   7252 C CA    . MET B 1 407 ? 61.754 -20.014 -47.224 1.00 36.05  ? 407 MET B CA    1 
ATOM   7253 C C     . MET B 1 407 ? 61.280 -19.750 -48.657 1.00 37.15  ? 407 MET B C     1 
ATOM   7254 O O     . MET B 1 407 ? 61.655 -20.459 -49.595 1.00 40.89  ? 407 MET B O     1 
ATOM   7255 C CB    . MET B 1 407 ? 60.551 -20.629 -46.502 1.00 36.74  ? 407 MET B CB    1 
ATOM   7256 C CG    . MET B 1 407 ? 60.887 -21.513 -45.363 1.00 39.40  ? 407 MET B CG    1 
ATOM   7257 S SD    . MET B 1 407 ? 59.370 -21.973 -44.482 1.00 38.61  ? 407 MET B SD    1 
ATOM   7258 C CE    . MET B 1 407 ? 59.011 -23.506 -45.332 1.00 35.78  ? 407 MET B CE    1 
ATOM   7259 N N     . VAL B 1 408 ? 60.393 -18.764 -48.808 1.00 35.62  ? 408 VAL B N     1 
ATOM   7260 C CA    . VAL B 1 408 ? 59.628 -18.598 -50.035 1.00 35.37  ? 408 VAL B CA    1 
ATOM   7261 C C     . VAL B 1 408 ? 60.431 -17.825 -51.094 1.00 37.78  ? 408 VAL B C     1 
ATOM   7262 O O     . VAL B 1 408 ? 60.465 -18.226 -52.258 1.00 36.62  ? 408 VAL B O     1 
ATOM   7263 C CB    . VAL B 1 408 ? 58.274 -17.933 -49.727 1.00 34.03  ? 408 VAL B CB    1 
ATOM   7264 C CG1   . VAL B 1 408 ? 57.518 -17.595 -51.003 1.00 35.94  ? 408 VAL B CG1   1 
ATOM   7265 C CG2   . VAL B 1 408 ? 57.414 -18.789 -48.796 1.00 30.87  ? 408 VAL B CG2   1 
ATOM   7266 N N     . SER B 1 409 ? 61.095 -16.728 -50.709 1.00 35.19  ? 409 SER B N     1 
ATOM   7267 C CA    . SER B 1 409 ? 61.754 -15.894 -51.701 1.00 38.90  ? 409 SER B CA    1 
ATOM   7268 C C     . SER B 1 409 ? 62.891 -16.653 -52.386 1.00 37.79  ? 409 SER B C     1 
ATOM   7269 O O     . SER B 1 409 ? 63.165 -16.412 -53.552 1.00 35.58  ? 409 SER B O     1 
ATOM   7270 C CB    . SER B 1 409 ? 62.236 -14.582 -51.120 1.00 38.80  ? 409 SER B CB    1 
ATOM   7271 O OG    . SER B 1 409 ? 63.150 -14.796 -50.066 1.00 39.12  ? 409 SER B OG    1 
ATOM   7272 N N     . SER B 1 410 ? 63.567 -17.537 -51.644 1.00 39.98  ? 410 SER B N     1 
ATOM   7273 C CA    . SER B 1 410 ? 64.619 -18.386 -52.194 1.00 39.76  ? 410 SER B CA    1 
ATOM   7274 C C     . SER B 1 410 ? 64.046 -19.340 -53.249 1.00 34.41  ? 410 SER B C     1 
ATOM   7275 O O     . SER B 1 410 ? 64.627 -19.472 -54.333 1.00 29.12  ? 410 SER B O     1 
ATOM   7276 C CB    . SER B 1 410 ? 65.316 -19.155 -51.100 1.00 37.58  ? 410 SER B CB    1 
ATOM   7277 O OG    . SER B 1 410 ? 64.355 -19.908 -50.382 1.00 42.75  ? 410 SER B OG    1 
ATOM   7278 N N     . ARG B 1 411 ? 62.905 -19.967 -52.915 1.00 29.42  ? 411 ARG B N     1 
ATOM   7279 C CA    . ARG B 1 411 ? 62.267 -20.966 -53.758 1.00 30.25  ? 411 ARG B CA    1 
ATOM   7280 C C     . ARG B 1 411 ? 61.695 -20.354 -55.026 1.00 28.63  ? 411 ARG B C     1 
ATOM   7281 O O     . ARG B 1 411 ? 61.795 -20.928 -56.099 1.00 28.52  ? 411 ARG B O     1 
ATOM   7282 C CB    . ARG B 1 411 ? 61.098 -21.638 -53.034 1.00 31.78  ? 411 ARG B CB    1 
ATOM   7283 C CG    . ARG B 1 411 ? 61.531 -22.686 -52.027 1.00 33.31  ? 411 ARG B CG    1 
ATOM   7284 C CD    . ARG B 1 411 ? 62.315 -23.800 -52.682 1.00 33.07  ? 411 ARG B CD    1 
ATOM   7285 N NE    . ARG B 1 411 ? 62.642 -24.809 -51.689 1.00 33.38  ? 411 ARG B NE    1 
ATOM   7286 C CZ    . ARG B 1 411 ? 63.619 -25.692 -51.821 1.00 33.03  ? 411 ARG B CZ    1 
ATOM   7287 N NH1   . ARG B 1 411 ? 64.362 -25.713 -52.911 1.00 35.91  ? 411 ARG B NH1   1 
ATOM   7288 N NH2   . ARG B 1 411 ? 63.869 -26.540 -50.848 1.00 33.66  ? 411 ARG B NH2   1 
ATOM   7289 N N     . VAL B 1 412 ? 61.038 -19.213 -54.877 1.00 28.68  ? 412 VAL B N     1 
ATOM   7290 C CA    . VAL B 1 412 ? 60.379 -18.560 -55.993 1.00 29.68  ? 412 VAL B CA    1 
ATOM   7291 C C     . VAL B 1 412 ? 61.429 -18.112 -57.006 1.00 29.24  ? 412 VAL B C     1 
ATOM   7292 O O     . VAL B 1 412 ? 61.262 -18.283 -58.203 1.00 27.89  ? 412 VAL B O     1 
ATOM   7293 C CB    . VAL B 1 412 ? 59.540 -17.391 -55.452 1.00 32.33  ? 412 VAL B CB    1 
ATOM   7294 C CG1   . VAL B 1 412 ? 59.369 -16.281 -56.465 1.00 38.16  ? 412 VAL B CG1   1 
ATOM   7295 C CG2   . VAL B 1 412 ? 58.201 -17.864 -54.912 1.00 29.04  ? 412 VAL B CG2   1 
ATOM   7296 N N     . ARG B 1 413 ? 62.535 -17.559 -56.512 1.00 29.88  ? 413 ARG B N     1 
ATOM   7297 C CA    . ARG B 1 413 ? 63.588 -17.037 -57.368 1.00 30.10  ? 413 ARG B CA    1 
ATOM   7298 C C     . ARG B 1 413 ? 64.321 -18.185 -58.063 1.00 32.89  ? 413 ARG B C     1 
ATOM   7299 O O     . ARG B 1 413 ? 64.749 -18.046 -59.209 1.00 34.68  ? 413 ARG B O     1 
ATOM   7300 C CB    . ARG B 1 413 ? 64.495 -16.131 -56.529 1.00 30.02  ? 413 ARG B CB    1 
ATOM   7301 C CG    . ARG B 1 413 ? 63.840 -14.797 -56.197 1.00 29.78  ? 413 ARG B CG    1 
ATOM   7302 C CD    . ARG B 1 413 ? 64.580 -14.036 -55.124 1.00 31.99  ? 413 ARG B CD    1 
ATOM   7303 N NE    . ARG B 1 413 ? 65.966 -13.799 -55.490 1.00 37.94  ? 413 ARG B NE    1 
ATOM   7304 C CZ    . ARG B 1 413 ? 66.391 -12.876 -56.350 1.00 37.88  ? 413 ARG B CZ    1 
ATOM   7305 N NH1   . ARG B 1 413 ? 65.565 -11.971 -56.833 1.00 41.80  ? 413 ARG B NH1   1 
ATOM   7306 N NH2   . ARG B 1 413 ? 67.660 -12.842 -56.707 1.00 36.81  ? 413 ARG B NH2   1 
ATOM   7307 N N     . GLU B 1 414 ? 64.419 -19.321 -57.360 1.00 34.75  ? 414 GLU B N     1 
ATOM   7308 C CA    . GLU B 1 414 ? 64.990 -20.558 -57.865 1.00 34.67  ? 414 GLU B CA    1 
ATOM   7309 C C     . GLU B 1 414 ? 64.238 -20.989 -59.122 1.00 35.79  ? 414 GLU B C     1 
ATOM   7310 O O     . GLU B 1 414 ? 64.805 -21.663 -59.986 1.00 36.76  ? 414 GLU B O     1 
ATOM   7311 C CB    . GLU B 1 414 ? 64.939 -21.616 -56.757 1.00 35.87  ? 414 GLU B CB    1 
ATOM   7312 C CG    . GLU B 1 414 ? 65.503 -22.957 -57.159 1.00 39.62  ? 414 GLU B CG    1 
ATOM   7313 C CD    . GLU B 1 414 ? 65.210 -24.133 -56.238 1.00 41.88  ? 414 GLU B CD    1 
ATOM   7314 O OE1   . GLU B 1 414 ? 64.725 -23.929 -55.110 1.00 37.94  ? 414 GLU B OE1   1 
ATOM   7315 O OE2   . GLU B 1 414 ? 65.443 -25.273 -56.678 1.00 45.82  ? 414 GLU B OE2   1 
ATOM   7316 N N     . TYR B 1 415 ? 62.972 -20.567 -59.248 1.00 31.27  ? 415 TYR B N     1 
ATOM   7317 C CA    . TYR B 1 415 ? 62.210 -20.889 -60.440 1.00 32.13  ? 415 TYR B CA    1 
ATOM   7318 C C     . TYR B 1 415 ? 62.059 -19.685 -61.359 1.00 30.33  ? 415 TYR B C     1 
ATOM   7319 O O     . TYR B 1 415 ? 61.276 -19.736 -62.295 1.00 28.41  ? 415 TYR B O     1 
ATOM   7320 C CB    . TYR B 1 415 ? 60.856 -21.490 -60.069 1.00 32.04  ? 415 TYR B CB    1 
ATOM   7321 C CG    . TYR B 1 415 ? 60.966 -22.915 -59.597 1.00 28.75  ? 415 TYR B CG    1 
ATOM   7322 C CD1   . TYR B 1 415 ? 61.429 -23.196 -58.327 1.00 27.57  ? 415 TYR B CD1   1 
ATOM   7323 C CD2   . TYR B 1 415 ? 60.673 -23.977 -60.440 1.00 26.70  ? 415 TYR B CD2   1 
ATOM   7324 C CE1   . TYR B 1 415 ? 61.548 -24.504 -57.880 1.00 29.51  ? 415 TYR B CE1   1 
ATOM   7325 C CE2   . TYR B 1 415 ? 60.751 -25.287 -59.994 1.00 27.46  ? 415 TYR B CE2   1 
ATOM   7326 C CZ    . TYR B 1 415 ? 61.207 -25.551 -58.716 1.00 27.16  ? 415 TYR B CZ    1 
ATOM   7327 O OH    . TYR B 1 415 ? 61.346 -26.816 -58.231 1.00 27.75  ? 415 TYR B OH    1 
ATOM   7328 N N     . GLY B 1 416 ? 62.832 -18.632 -61.101 1.00 29.80  ? 416 GLY B N     1 
ATOM   7329 C CA    . GLY B 1 416 ? 62.970 -17.545 -62.053 1.00 33.96  ? 416 GLY B CA    1 
ATOM   7330 C C     . GLY B 1 416 ? 61.927 -16.440 -61.893 1.00 34.30  ? 416 GLY B C     1 
ATOM   7331 O O     . GLY B 1 416 ? 61.900 -15.532 -62.718 1.00 36.08  ? 416 GLY B O     1 
ATOM   7332 N N     . PHE B 1 417 ? 61.102 -16.508 -60.835 1.00 31.30  ? 417 PHE B N     1 
ATOM   7333 C CA    . PHE B 1 417 ? 60.070 -15.507 -60.596 1.00 29.21  ? 417 PHE B CA    1 
ATOM   7334 C C     . PHE B 1 417 ? 60.590 -14.496 -59.585 1.00 27.85  ? 417 PHE B C     1 
ATOM   7335 O O     . PHE B 1 417 ? 61.362 -14.824 -58.696 1.00 30.23  ? 417 PHE B O     1 
ATOM   7336 C CB    . PHE B 1 417 ? 58.780 -16.157 -60.084 1.00 25.67  ? 417 PHE B CB    1 
ATOM   7337 C CG    . PHE B 1 417 ? 58.200 -17.226 -60.976 1.00 24.43  ? 417 PHE B CG    1 
ATOM   7338 C CD1   . PHE B 1 417 ? 57.675 -16.912 -62.216 1.00 24.59  ? 417 PHE B CD1   1 
ATOM   7339 C CD2   . PHE B 1 417 ? 58.209 -18.559 -60.590 1.00 26.13  ? 417 PHE B CD2   1 
ATOM   7340 C CE1   . PHE B 1 417 ? 57.187 -17.902 -63.048 1.00 24.15  ? 417 PHE B CE1   1 
ATOM   7341 C CE2   . PHE B 1 417 ? 57.671 -19.548 -61.398 1.00 23.90  ? 417 PHE B CE2   1 
ATOM   7342 C CZ    . PHE B 1 417 ? 57.163 -19.215 -62.624 1.00 24.76  ? 417 PHE B CZ    1 
ATOM   7343 N N     . ASP B 1 418 ? 60.176 -13.249 -59.708 1.00 28.71  ? 418 ASP B N     1 
ATOM   7344 C CA    . ASP B 1 418 ? 60.497 -12.305 -58.656 1.00 30.96  ? 418 ASP B CA    1 
ATOM   7345 C C     . ASP B 1 418 ? 59.686 -12.655 -57.408 1.00 33.19  ? 418 ASP B C     1 
ATOM   7346 O O     . ASP B 1 418 ? 58.545 -13.121 -57.487 1.00 31.28  ? 418 ASP B O     1 
ATOM   7347 C CB    . ASP B 1 418 ? 60.304 -10.868 -59.114 1.00 31.54  ? 418 ASP B CB    1 
ATOM   7348 C CG    . ASP B 1 418 ? 61.578 -10.227 -59.629 1.00 33.93  ? 418 ASP B CG    1 
ATOM   7349 O OD1   . ASP B 1 418 ? 62.542 -10.121 -58.829 1.00 38.45  ? 418 ASP B OD1   1 
ATOM   7350 O OD2   . ASP B 1 418 ? 61.579 -9.815  -60.797 1.00 32.49  ? 418 ASP B OD2   1 
ATOM   7351 N N     . TYR B 1 419 ? 60.327 -12.459 -56.253 1.00 34.30  ? 419 TYR B N     1 
ATOM   7352 C CA    . TYR B 1 419 ? 59.633 -12.548 -54.982 1.00 34.88  ? 419 TYR B CA    1 
ATOM   7353 C C     . TYR B 1 419 ? 58.687 -11.364 -54.871 1.00 30.46  ? 419 TYR B C     1 
ATOM   7354 O O     . TYR B 1 419 ? 59.127 -10.231 -54.936 1.00 30.40  ? 419 TYR B O     1 
ATOM   7355 C CB    . TYR B 1 419 ? 60.598 -12.545 -53.792 1.00 34.43  ? 419 TYR B CB    1 
ATOM   7356 C CG    . TYR B 1 419 ? 59.874 -12.492 -52.478 1.00 35.08  ? 419 TYR B CG    1 
ATOM   7357 C CD1   . TYR B 1 419 ? 59.108 -13.562 -52.049 1.00 36.05  ? 419 TYR B CD1   1 
ATOM   7358 C CD2   . TYR B 1 419 ? 59.853 -11.335 -51.718 1.00 37.83  ? 419 TYR B CD2   1 
ATOM   7359 C CE1   . TYR B 1 419 ? 58.399 -13.511 -50.861 1.00 36.59  ? 419 TYR B CE1   1 
ATOM   7360 C CE2   . TYR B 1 419 ? 59.137 -11.264 -50.535 1.00 37.00  ? 419 TYR B CE2   1 
ATOM   7361 C CZ    . TYR B 1 419 ? 58.415 -12.357 -50.100 1.00 36.92  ? 419 TYR B CZ    1 
ATOM   7362 O OH    . TYR B 1 419 ? 57.716 -12.300 -48.923 1.00 38.15  ? 419 TYR B OH    1 
ATOM   7363 N N     . MET B 1 420 ? 57.399 -11.656 -54.726 1.00 32.01  ? 420 MET B N     1 
ATOM   7364 C CA    . MET B 1 420 ? 56.376 -10.656 -54.486 1.00 34.92  ? 420 MET B CA    1 
ATOM   7365 C C     . MET B 1 420 ? 55.567 -11.155 -53.297 1.00 37.68  ? 420 MET B C     1 
ATOM   7366 O O     . MET B 1 420 ? 54.679 -11.980 -53.436 1.00 49.88  ? 420 MET B O     1 
ATOM   7367 C CB    . MET B 1 420 ? 55.439 -10.500 -55.688 1.00 34.42  ? 420 MET B CB    1 
ATOM   7368 C CG    . MET B 1 420 ? 55.962 -9.654  -56.824 1.00 33.93  ? 420 MET B CG    1 
ATOM   7369 S SD    . MET B 1 420 ? 54.924 -9.944  -58.286 1.00 36.76  ? 420 MET B SD    1 
ATOM   7370 C CE    . MET B 1 420 ? 55.796 -8.997  -59.525 1.00 36.92  ? 420 MET B CE    1 
ATOM   7371 N N     . GLY B 1 421 ? 55.936 -10.712 -52.109 1.00 40.24  ? 421 GLY B N     1 
ATOM   7372 C CA    . GLY B 1 421 ? 55.333 -11.240 -50.909 1.00 35.97  ? 421 GLY B CA    1 
ATOM   7373 C C     . GLY B 1 421 ? 54.670 -10.139 -50.103 1.00 34.80  ? 421 GLY B C     1 
ATOM   7374 O O     . GLY B 1 421 ? 54.807 -8.954  -50.376 1.00 36.68  ? 421 GLY B O     1 
ATOM   7375 N N     . LEU B 1 422 ? 54.002 -10.573 -49.050 1.00 35.92  ? 422 LEU B N     1 
ATOM   7376 C CA    . LEU B 1 422 ? 53.145 -9.709  -48.276 1.00 37.22  ? 422 LEU B CA    1 
ATOM   7377 C C     . LEU B 1 422 ? 52.939 -10.419 -46.940 1.00 36.20  ? 422 LEU B C     1 
ATOM   7378 O O     . LEU B 1 422 ? 52.702 -11.634 -46.912 1.00 32.48  ? 422 LEU B O     1 
ATOM   7379 C CB    . LEU B 1 422 ? 51.923 -9.548  -49.188 1.00 43.21  ? 422 LEU B CB    1 
ATOM   7380 C CG    . LEU B 1 422 ? 50.587 -9.126  -48.609 1.00 42.45  ? 422 LEU B CG    1 
ATOM   7381 C CD1   . LEU B 1 422 ? 49.609 -8.933  -49.755 1.00 43.08  ? 422 LEU B CD1   1 
ATOM   7382 C CD2   . LEU B 1 422 ? 50.057 -10.152 -47.627 1.00 41.01  ? 422 LEU B CD2   1 
ATOM   7383 N N     . LEU B 1 423 ? 53.186 -9.702  -45.834 1.00 32.35  ? 423 LEU B N     1 
ATOM   7384 C CA    . LEU B 1 423 ? 52.787 -10.217 -44.535 1.00 34.32  ? 423 LEU B CA    1 
ATOM   7385 C C     . LEU B 1 423 ? 51.535 -9.481  -44.092 1.00 33.20  ? 423 LEU B C     1 
ATOM   7386 O O     . LEU B 1 423 ? 51.557 -8.265  -44.006 1.00 36.27  ? 423 LEU B O     1 
ATOM   7387 C CB    . LEU B 1 423 ? 53.958 -10.134 -43.553 1.00 36.21  ? 423 LEU B CB    1 
ATOM   7388 C CG    . LEU B 1 423 ? 55.015 -11.204 -43.852 1.00 39.98  ? 423 LEU B CG    1 
ATOM   7389 C CD1   . LEU B 1 423 ? 56.286 -10.583 -44.402 1.00 40.19  ? 423 LEU B CD1   1 
ATOM   7390 C CD2   . LEU B 1 423 ? 55.304 -12.104 -42.658 1.00 40.46  ? 423 LEU B CD2   1 
ATOM   7391 N N     . ALA B 1 424 ? 50.439 -10.244 -43.930 1.00 34.67  ? 424 ALA B N     1 
ATOM   7392 C CA    . ALA B 1 424 ? 49.108 -9.718  -43.637 1.00 34.69  ? 424 ALA B CA    1 
ATOM   7393 C C     . ALA B 1 424 ? 48.645 -10.230 -42.280 1.00 34.19  ? 424 ALA B C     1 
ATOM   7394 O O     . ALA B 1 424 ? 48.949 -11.357 -41.908 1.00 40.49  ? 424 ALA B O     1 
ATOM   7395 C CB    . ALA B 1 424 ? 48.108 -10.086 -44.706 1.00 32.56  ? 424 ALA B CB    1 
ATOM   7396 N N     . ILE B 1 425 ? 47.945 -9.371  -41.538 1.00 34.76  ? 425 ILE B N     1 
ATOM   7397 C CA    . ILE B 1 425 ? 47.416 -9.722  -40.233 1.00 35.74  ? 425 ILE B CA    1 
ATOM   7398 C C     . ILE B 1 425 ? 45.942 -9.334  -40.199 1.00 32.68  ? 425 ILE B C     1 
ATOM   7399 O O     . ILE B 1 425 ? 45.583 -8.201  -40.517 1.00 30.98  ? 425 ILE B O     1 
ATOM   7400 C CB    . ILE B 1 425 ? 48.202 -9.043  -39.093 1.00 40.65  ? 425 ILE B CB    1 
ATOM   7401 C CG1   . ILE B 1 425 ? 49.712 -9.260  -39.219 1.00 40.15  ? 425 ILE B CG1   1 
ATOM   7402 C CG2   . ILE B 1 425 ? 47.675 -9.501  -37.735 1.00 40.78  ? 425 ILE B CG2   1 
ATOM   7403 C CD1   . ILE B 1 425 ? 50.511 -8.456  -38.224 1.00 41.61  ? 425 ILE B CD1   1 
ATOM   7404 N N     . GLY B 1 426 ? 45.097 -10.294 -39.820 1.00 32.27  ? 426 GLY B N     1 
ATOM   7405 C CA    . GLY B 1 426 ? 43.672 -10.044 -39.757 1.00 32.38  ? 426 GLY B CA    1 
ATOM   7406 C C     . GLY B 1 426 ? 43.325 -9.442  -38.404 1.00 35.07  ? 426 GLY B C     1 
ATOM   7407 O O     . GLY B 1 426 ? 43.028 -8.247  -38.288 1.00 33.70  ? 426 GLY B O     1 
ATOM   7408 N N     . TRP B 1 427 ? 43.354 -10.321 -37.404 1.00 32.82  ? 427 TRP B N     1 
ATOM   7409 C CA    . TRP B 1 427 ? 43.234 -9.936  -36.016 1.00 30.80  ? 427 TRP B CA    1 
ATOM   7410 C C     . TRP B 1 427 ? 44.353 -10.623 -35.226 1.00 30.95  ? 427 TRP B C     1 
ATOM   7411 O O     . TRP B 1 427 ? 45.211 -9.927  -34.689 1.00 34.66  ? 427 TRP B O     1 
ATOM   7412 C CB    . TRP B 1 427 ? 41.829 -10.236 -35.488 1.00 29.65  ? 427 TRP B CB    1 
ATOM   7413 C CG    . TRP B 1 427 ? 41.536 -9.601  -34.159 1.00 31.80  ? 427 TRP B CG    1 
ATOM   7414 C CD1   . TRP B 1 427 ? 42.401 -8.871  -33.390 1.00 29.96  ? 427 TRP B CD1   1 
ATOM   7415 C CD2   . TRP B 1 427 ? 40.289 -9.643  -33.428 1.00 33.11  ? 427 TRP B CD2   1 
ATOM   7416 N NE1   . TRP B 1 427 ? 41.771 -8.432  -32.258 1.00 30.55  ? 427 TRP B NE1   1 
ATOM   7417 C CE2   . TRP B 1 427 ? 40.475 -8.882  -32.252 1.00 31.50  ? 427 TRP B CE2   1 
ATOM   7418 C CE3   . TRP B 1 427 ? 39.034 -10.238 -33.650 1.00 35.28  ? 427 TRP B CE3   1 
ATOM   7419 C CZ2   . TRP B 1 427 ? 39.468 -8.738  -31.292 1.00 31.90  ? 427 TRP B CZ2   1 
ATOM   7420 C CZ3   . TRP B 1 427 ? 38.028 -10.069 -32.718 1.00 34.50  ? 427 TRP B CZ3   1 
ATOM   7421 C CH2   . TRP B 1 427 ? 38.250 -9.335  -31.549 1.00 34.63  ? 427 TRP B CH2   1 
ATOM   7422 N N     . ARG B 1 428 ? 44.393 -11.966 -35.205 1.00 26.24  ? 428 ARG B N     1 
ATOM   7423 C CA    . ARG B 1 428 ? 45.405 -12.679 -34.433 1.00 27.08  ? 428 ARG B CA    1 
ATOM   7424 C C     . ARG B 1 428 ? 46.238 -13.573 -35.348 1.00 26.65  ? 428 ARG B C     1 
ATOM   7425 O O     . ARG B 1 428 ? 47.119 -14.300 -34.881 1.00 27.21  ? 428 ARG B O     1 
ATOM   7426 C CB    . ARG B 1 428 ? 44.745 -13.497 -33.318 1.00 26.01  ? 428 ARG B CB    1 
ATOM   7427 C CG    . ARG B 1 428 ? 44.299 -12.677 -32.115 1.00 26.40  ? 428 ARG B CG    1 
ATOM   7428 C CD    . ARG B 1 428 ? 43.379 -13.523 -31.258 1.00 27.28  ? 428 ARG B CD    1 
ATOM   7429 N NE    . ARG B 1 428 ? 43.132 -12.950 -29.950 1.00 27.08  ? 428 ARG B NE    1 
ATOM   7430 C CZ    . ARG B 1 428 ? 42.379 -11.890 -29.694 1.00 27.66  ? 428 ARG B CZ    1 
ATOM   7431 N NH1   . ARG B 1 428 ? 41.663 -11.321 -30.641 1.00 28.10  ? 428 ARG B NH1   1 
ATOM   7432 N NH2   . ARG B 1 428 ? 42.340 -11.401 -28.466 1.00 29.99  ? 428 ARG B NH2   1 
ATOM   7433 N N     . ASP B 1 429 ? 45.975 -13.474 -36.654 1.00 24.05  ? 429 ASP B N     1 
ATOM   7434 C CA    . ASP B 1 429 ? 46.538 -14.386 -37.625 1.00 23.82  ? 429 ASP B CA    1 
ATOM   7435 C C     . ASP B 1 429 ? 47.461 -13.626 -38.561 1.00 27.58  ? 429 ASP B C     1 
ATOM   7436 O O     . ASP B 1 429 ? 47.057 -12.634 -39.167 1.00 28.42  ? 429 ASP B O     1 
ATOM   7437 C CB    . ASP B 1 429 ? 45.442 -15.037 -38.449 1.00 23.62  ? 429 ASP B CB    1 
ATOM   7438 C CG    . ASP B 1 429 ? 44.504 -14.040 -39.100 1.00 23.71  ? 429 ASP B CG    1 
ATOM   7439 O OD1   . ASP B 1 429 ? 44.030 -13.132 -38.404 1.00 24.51  ? 429 ASP B OD1   1 
ATOM   7440 O OD2   . ASP B 1 429 ? 44.233 -14.204 -40.275 1.00 23.75  ? 429 ASP B OD2   1 
ATOM   7441 N N     . LEU B 1 430 ? 48.687 -14.134 -38.689 1.00 29.47  ? 430 LEU B N     1 
ATOM   7442 C CA    . LEU B 1 430 ? 49.605 -13.679 -39.719 1.00 32.52  ? 430 LEU B CA    1 
ATOM   7443 C C     . LEU B 1 430 ? 49.478 -14.612 -40.929 1.00 33.25  ? 430 LEU B C     1 
ATOM   7444 O O     . LEU B 1 430 ? 49.275 -15.832 -40.787 1.00 27.72  ? 430 LEU B O     1 
ATOM   7445 C CB    . LEU B 1 430 ? 51.018 -13.676 -39.113 1.00 34.01  ? 430 LEU B CB    1 
ATOM   7446 C CG    . LEU B 1 430 ? 52.189 -13.352 -40.048 1.00 36.41  ? 430 LEU B CG    1 
ATOM   7447 C CD1   . LEU B 1 430 ? 52.232 -11.875 -40.413 1.00 36.45  ? 430 LEU B CD1   1 
ATOM   7448 C CD2   . LEU B 1 430 ? 53.507 -13.763 -39.418 1.00 35.34  ? 430 LEU B CD2   1 
ATOM   7449 N N     . HIS B 1 431 ? 49.581 -14.002 -42.114 1.00 32.23  ? 431 HIS B N     1 
ATOM   7450 C CA    . HIS B 1 431 ? 49.766 -14.729 -43.365 1.00 34.16  ? 431 HIS B CA    1 
ATOM   7451 C C     . HIS B 1 431 ? 50.964 -14.165 -44.117 1.00 31.21  ? 431 HIS B C     1 
ATOM   7452 O O     . HIS B 1 431 ? 50.976 -12.989 -44.475 1.00 35.47  ? 431 HIS B O     1 
ATOM   7453 C CB    . HIS B 1 431 ? 48.552 -14.627 -44.293 1.00 34.10  ? 431 HIS B CB    1 
ATOM   7454 C CG    . HIS B 1 431 ? 47.277 -14.906 -43.595 1.00 34.75  ? 431 HIS B CG    1 
ATOM   7455 N ND1   . HIS B 1 431 ? 46.463 -15.955 -43.955 1.00 36.96  ? 431 HIS B ND1   1 
ATOM   7456 C CD2   . HIS B 1 431 ? 46.681 -14.289 -42.562 1.00 35.21  ? 431 HIS B CD2   1 
ATOM   7457 C CE1   . HIS B 1 431 ? 45.392 -15.957 -43.168 1.00 38.27  ? 431 HIS B CE1   1 
ATOM   7458 N NE2   . HIS B 1 431 ? 45.506 -14.952 -42.317 1.00 36.86  ? 431 HIS B NE2   1 
ATOM   7459 N N     . HIS B 1 432 ? 51.983 -15.006 -44.315 1.00 30.52  ? 432 HIS B N     1 
ATOM   7460 C CA    . HIS B 1 432 ? 52.928 -14.789 -45.389 1.00 28.28  ? 432 HIS B CA    1 
ATOM   7461 C C     . HIS B 1 432 ? 52.211 -15.172 -46.673 1.00 31.04  ? 432 HIS B C     1 
ATOM   7462 O O     . HIS B 1 432 ? 51.866 -16.343 -46.860 1.00 39.32  ? 432 HIS B O     1 
ATOM   7463 C CB    . HIS B 1 432 ? 54.238 -15.566 -45.203 1.00 26.80  ? 432 HIS B CB    1 
ATOM   7464 C CG    . HIS B 1 432 ? 55.181 -15.203 -46.302 1.00 26.50  ? 432 HIS B CG    1 
ATOM   7465 N ND1   . HIS B 1 432 ? 55.114 -15.783 -47.538 1.00 28.72  ? 432 HIS B ND1   1 
ATOM   7466 C CD2   . HIS B 1 432 ? 56.151 -14.292 -46.395 1.00 28.33  ? 432 HIS B CD2   1 
ATOM   7467 C CE1   . HIS B 1 432 ? 56.019 -15.231 -48.336 1.00 29.83  ? 432 HIS B CE1   1 
ATOM   7468 N NE2   . HIS B 1 432 ? 56.647 -14.321 -47.669 1.00 28.71  ? 432 HIS B NE2   1 
ATOM   7469 N N     . VAL B 1 433 ? 51.956 -14.173 -47.525 1.00 29.07  ? 433 VAL B N     1 
ATOM   7470 C CA    . VAL B 1 433 ? 51.326 -14.408 -48.808 1.00 28.92  ? 433 VAL B CA    1 
ATOM   7471 C C     . VAL B 1 433 ? 52.374 -14.285 -49.910 1.00 32.43  ? 433 VAL B C     1 
ATOM   7472 O O     . VAL B 1 433 ? 52.903 -13.181 -50.143 1.00 33.11  ? 433 VAL B O     1 
ATOM   7473 C CB    . VAL B 1 433 ? 50.164 -13.432 -49.074 1.00 29.51  ? 433 VAL B CB    1 
ATOM   7474 C CG1   . VAL B 1 433 ? 49.555 -13.651 -50.457 1.00 27.08  ? 433 VAL B CG1   1 
ATOM   7475 C CG2   . VAL B 1 433 ? 49.114 -13.532 -47.974 1.00 31.36  ? 433 VAL B CG2   1 
ATOM   7476 N N     . THR B 1 434 ? 52.581 -15.408 -50.616 1.00 30.09  ? 434 THR B N     1 
ATOM   7477 C CA    . THR B 1 434 ? 53.377 -15.464 -51.833 1.00 31.69  ? 434 THR B CA    1 
ATOM   7478 C C     . THR B 1 434 ? 52.463 -15.164 -53.025 1.00 31.29  ? 434 THR B C     1 
ATOM   7479 O O     . THR B 1 434 ? 51.411 -15.765 -53.156 1.00 32.24  ? 434 THR B O     1 
ATOM   7480 C CB    . THR B 1 434 ? 54.054 -16.842 -51.954 1.00 35.42  ? 434 THR B CB    1 
ATOM   7481 O OG1   . THR B 1 434 ? 54.669 -17.231 -50.717 1.00 38.67  ? 434 THR B OG1   1 
ATOM   7482 C CG2   . THR B 1 434 ? 55.106 -16.875 -53.041 1.00 37.01  ? 434 THR B CG2   1 
ATOM   7483 N N     . VAL B 1 435 ? 52.864 -14.221 -53.884 1.00 31.20  ? 435 VAL B N     1 
ATOM   7484 C CA    . VAL B 1 435 ? 52.157 -13.876 -55.109 1.00 29.10  ? 435 VAL B CA    1 
ATOM   7485 C C     . VAL B 1 435 ? 53.094 -14.190 -56.273 1.00 27.71  ? 435 VAL B C     1 
ATOM   7486 O O     . VAL B 1 435 ? 54.196 -13.638 -56.350 1.00 27.86  ? 435 VAL B O     1 
ATOM   7487 C CB    . VAL B 1 435 ? 51.787 -12.381 -55.131 1.00 32.57  ? 435 VAL B CB    1 
ATOM   7488 C CG1   . VAL B 1 435 ? 50.986 -12.005 -56.361 1.00 34.67  ? 435 VAL B CG1   1 
ATOM   7489 C CG2   . VAL B 1 435 ? 51.054 -11.963 -53.882 1.00 35.75  ? 435 VAL B CG2   1 
ATOM   7490 N N     . ILE B 1 436 ? 52.665 -15.083 -57.166 1.00 25.55  ? 436 ILE B N     1 
ATOM   7491 C CA    . ILE B 1 436 ? 53.514 -15.521 -58.260 1.00 24.61  ? 436 ILE B CA    1 
ATOM   7492 C C     . ILE B 1 436 ? 52.865 -15.145 -59.581 1.00 23.82  ? 436 ILE B C     1 
ATOM   7493 O O     . ILE B 1 436 ? 51.789 -15.639 -59.906 1.00 26.43  ? 436 ILE B O     1 
ATOM   7494 C CB    . ILE B 1 436 ? 53.810 -17.030 -58.200 1.00 25.01  ? 436 ILE B CB    1 
ATOM   7495 C CG1   . ILE B 1 436 ? 54.242 -17.466 -56.803 1.00 26.97  ? 436 ILE B CG1   1 
ATOM   7496 C CG2   . ILE B 1 436 ? 54.863 -17.400 -59.233 1.00 26.90  ? 436 ILE B CG2   1 
ATOM   7497 C CD1   . ILE B 1 436 ? 54.372 -18.964 -56.670 1.00 28.26  ? 436 ILE B CD1   1 
ATOM   7498 N N     . VAL B 1 437 ? 53.573 -14.303 -60.335 1.00 24.61  ? 437 VAL B N     1 
ATOM   7499 C CA    . VAL B 1 437 ? 53.161 -13.830 -61.643 1.00 24.79  ? 437 VAL B CA    1 
ATOM   7500 C C     . VAL B 1 437 ? 53.903 -14.657 -62.684 1.00 26.61  ? 437 VAL B C     1 
ATOM   7501 O O     . VAL B 1 437 ? 55.116 -14.815 -62.585 1.00 27.55  ? 437 VAL B O     1 
ATOM   7502 C CB    . VAL B 1 437 ? 53.482 -12.326 -61.758 1.00 26.33  ? 437 VAL B CB    1 
ATOM   7503 C CG1   . VAL B 1 437 ? 53.202 -11.752 -63.136 1.00 26.28  ? 437 VAL B CG1   1 
ATOM   7504 C CG2   . VAL B 1 437 ? 52.724 -11.539 -60.701 1.00 27.97  ? 437 VAL B CG2   1 
ATOM   7505 N N     . TYR B 1 438 ? 53.181 -15.174 -63.683 1.00 27.87  ? 438 TYR B N     1 
ATOM   7506 C CA    . TYR B 1 438 ? 53.749 -16.160 -64.570 1.00 28.55  ? 438 TYR B CA    1 
ATOM   7507 C C     . TYR B 1 438 ? 53.144 -16.039 -65.952 1.00 32.30  ? 438 TYR B C     1 
ATOM   7508 O O     . TYR B 1 438 ? 51.968 -15.712 -66.067 1.00 38.98  ? 438 TYR B O     1 
ATOM   7509 C CB    . TYR B 1 438 ? 53.537 -17.576 -64.026 1.00 30.78  ? 438 TYR B CB    1 
ATOM   7510 C CG    . TYR B 1 438 ? 52.106 -18.011 -63.812 1.00 33.67  ? 438 TYR B CG    1 
ATOM   7511 C CD1   . TYR B 1 438 ? 51.407 -17.628 -62.677 1.00 34.06  ? 438 TYR B CD1   1 
ATOM   7512 C CD2   . TYR B 1 438 ? 51.462 -18.846 -64.717 1.00 31.60  ? 438 TYR B CD2   1 
ATOM   7513 C CE1   . TYR B 1 438 ? 50.105 -18.050 -62.456 1.00 35.17  ? 438 TYR B CE1   1 
ATOM   7514 C CE2   . TYR B 1 438 ? 50.155 -19.264 -64.518 1.00 30.83  ? 438 TYR B CE2   1 
ATOM   7515 C CZ    . TYR B 1 438 ? 49.477 -18.875 -63.378 1.00 34.18  ? 438 TYR B CZ    1 
ATOM   7516 O OH    . TYR B 1 438 ? 48.189 -19.293 -63.138 1.00 32.69  ? 438 TYR B OH    1 
ATOM   7517 N N     . ASP B 1 439 ? 53.956 -16.341 -66.978 1.00 31.72  ? 439 ASP B N     1 
ATOM   7518 C CA    . ASP B 1 439 ? 53.449 -16.433 -68.334 1.00 37.10  ? 439 ASP B CA    1 
ATOM   7519 C C     . ASP B 1 439 ? 52.621 -17.714 -68.485 1.00 36.85  ? 439 ASP B C     1 
ATOM   7520 O O     . ASP B 1 439 ? 53.129 -18.810 -68.678 1.00 37.94  ? 439 ASP B O     1 
ATOM   7521 C CB    . ASP B 1 439 ? 54.550 -16.353 -69.392 1.00 37.39  ? 439 ASP B CB    1 
ATOM   7522 C CG    . ASP B 1 439 ? 53.997 -16.295 -70.807 1.00 36.58  ? 439 ASP B CG    1 
ATOM   7523 O OD1   . ASP B 1 439 ? 52.756 -16.183 -70.961 1.00 33.29  ? 439 ASP B OD1   1 
ATOM   7524 O OD2   . ASP B 1 439 ? 54.808 -16.388 -71.744 1.00 41.67  ? 439 ASP B OD2   1 
ATOM   7525 N N     . LYS B 1 440 ? 51.315 -17.504 -68.464 1.00 36.55  ? 440 LYS B N     1 
ATOM   7526 C CA    . LYS B 1 440 ? 50.295 -18.520 -68.531 1.00 35.97  ? 440 LYS B CA    1 
ATOM   7527 C C     . LYS B 1 440 ? 50.237 -19.161 -69.922 1.00 36.09  ? 440 LYS B C     1 
ATOM   7528 O O     . LYS B 1 440 ? 49.639 -20.218 -70.093 1.00 30.91  ? 440 LYS B O     1 
ATOM   7529 C CB    . LYS B 1 440 ? 49.006 -17.791 -68.147 1.00 39.26  ? 440 LYS B CB    1 
ATOM   7530 C CG    . LYS B 1 440 ? 47.829 -18.001 -69.081 1.00 45.54  ? 440 LYS B CG    1 
ATOM   7531 C CD    . LYS B 1 440 ? 46.915 -16.805 -69.163 1.00 50.90  ? 440 LYS B CD    1 
ATOM   7532 C CE    . LYS B 1 440 ? 46.758 -16.225 -70.555 1.00 52.92  ? 440 LYS B CE    1 
ATOM   7533 N NZ    . LYS B 1 440 ? 45.960 -17.129 -71.422 1.00 49.30  ? 440 LYS B NZ    1 
ATOM   7534 N N     . THR B 1 441 ? 50.817 -18.513 -70.937 1.00 36.36  ? 441 THR B N     1 
ATOM   7535 C CA    . THR B 1 441 ? 50.780 -19.062 -72.280 1.00 33.50  ? 441 THR B CA    1 
ATOM   7536 C C     . THR B 1 441 ? 51.915 -20.068 -72.469 1.00 33.87  ? 441 THR B C     1 
ATOM   7537 O O     . THR B 1 441 ? 51.867 -20.863 -73.398 1.00 36.43  ? 441 THR B O     1 
ATOM   7538 C CB    . THR B 1 441 ? 50.851 -17.964 -73.350 1.00 34.58  ? 441 THR B CB    1 
ATOM   7539 O OG1   . THR B 1 441 ? 52.188 -17.461 -73.427 1.00 35.83  ? 441 THR B OG1   1 
ATOM   7540 C CG2   . THR B 1 441 ? 49.889 -16.821 -73.106 1.00 33.80  ? 441 THR B CG2   1 
ATOM   7541 N N     . ASP B 1 442 ? 52.947 -20.017 -71.620 1.00 34.03  ? 442 ASP B N     1 
ATOM   7542 C CA    . ASP B 1 442 ? 54.161 -20.787 -71.848 1.00 36.30  ? 442 ASP B CA    1 
ATOM   7543 C C     . ASP B 1 442 ? 54.082 -22.102 -71.080 1.00 35.40  ? 442 ASP B C     1 
ATOM   7544 O O     . ASP B 1 442 ? 54.139 -22.124 -69.853 1.00 32.86  ? 442 ASP B O     1 
ATOM   7545 C CB    . ASP B 1 442 ? 55.409 -19.974 -71.479 1.00 43.10  ? 442 ASP B CB    1 
ATOM   7546 C CG    . ASP B 1 442 ? 56.759 -20.654 -71.713 1.00 43.96  ? 442 ASP B CG    1 
ATOM   7547 O OD1   . ASP B 1 442 ? 56.785 -21.851 -71.993 1.00 44.46  ? 442 ASP B OD1   1 
ATOM   7548 O OD2   . ASP B 1 442 ? 57.789 -19.961 -71.616 1.00 44.79  ? 442 ASP B OD2   1 
ATOM   7549 N N     . PRO B 1 443 ? 54.036 -23.259 -71.775 1.00 38.20  ? 443 PRO B N     1 
ATOM   7550 C CA    . PRO B 1 443 ? 53.905 -24.543 -71.095 1.00 38.75  ? 443 PRO B CA    1 
ATOM   7551 C C     . PRO B 1 443 ? 55.021 -24.780 -70.088 1.00 37.82  ? 443 PRO B C     1 
ATOM   7552 O O     . PRO B 1 443 ? 54.802 -25.498 -69.119 1.00 37.53  ? 443 PRO B O     1 
ATOM   7553 C CB    . PRO B 1 443 ? 53.932 -25.616 -72.199 1.00 37.99  ? 443 PRO B CB    1 
ATOM   7554 C CG    . PRO B 1 443 ? 54.376 -24.878 -73.460 1.00 38.78  ? 443 PRO B CG    1 
ATOM   7555 C CD    . PRO B 1 443 ? 54.097 -23.403 -73.237 1.00 37.95  ? 443 PRO B CD    1 
ATOM   7556 N N     . ASP B 1 444 ? 56.197 -24.187 -70.342 1.00 41.67  ? 444 ASP B N     1 
ATOM   7557 C CA    . ASP B 1 444 ? 57.375 -24.397 -69.514 1.00 43.85  ? 444 ASP B CA    1 
ATOM   7558 C C     . ASP B 1 444 ? 57.302 -23.540 -68.256 1.00 37.31  ? 444 ASP B C     1 
ATOM   7559 O O     . ASP B 1 444 ? 57.758 -23.972 -67.207 1.00 37.29  ? 444 ASP B O     1 
ATOM   7560 C CB    . ASP B 1 444 ? 58.682 -24.169 -70.285 1.00 47.32  ? 444 ASP B CB    1 
ATOM   7561 C CG    . ASP B 1 444 ? 59.060 -25.351 -71.165 1.00 57.93  ? 444 ASP B CG    1 
ATOM   7562 O OD1   . ASP B 1 444 ? 59.249 -26.471 -70.619 1.00 70.04  ? 444 ASP B OD1   1 
ATOM   7563 O OD2   . ASP B 1 444 ? 59.158 -25.153 -72.386 1.00 60.66  ? 444 ASP B OD2   1 
ATOM   7564 N N     . GLU B 1 445 ? 56.784 -22.317 -68.357 1.00 35.28  ? 445 GLU B N     1 
ATOM   7565 C CA    . GLU B 1 445 ? 56.577 -21.523 -67.157 1.00 35.49  ? 445 GLU B CA    1 
ATOM   7566 C C     . GLU B 1 445 ? 55.486 -22.191 -66.319 1.00 31.82  ? 445 GLU B C     1 
ATOM   7567 O O     . GLU B 1 445 ? 55.600 -22.262 -65.096 1.00 25.40  ? 445 GLU B O     1 
ATOM   7568 C CB    . GLU B 1 445 ? 56.239 -20.071 -67.505 1.00 39.00  ? 445 GLU B CB    1 
ATOM   7569 C CG    . GLU B 1 445 ? 57.383 -19.339 -68.184 1.00 44.54  ? 445 GLU B CG    1 
ATOM   7570 C CD    . GLU B 1 445 ? 58.634 -19.201 -67.327 1.00 48.02  ? 445 GLU B CD    1 
ATOM   7571 O OE1   . GLU B 1 445 ? 58.541 -18.583 -66.237 1.00 50.00  ? 445 GLU B OE1   1 
ATOM   7572 O OE2   . GLU B 1 445 ? 59.684 -19.746 -67.732 1.00 44.12  ? 445 GLU B OE2   1 
ATOM   7573 N N     . ARG B 1 446 ? 54.471 -22.731 -67.006 1.00 30.31  ? 446 ARG B N     1 
ATOM   7574 C CA    . ARG B 1 446 ? 53.360 -23.390 -66.339 1.00 32.32  ? 446 ARG B CA    1 
ATOM   7575 C C     . ARG B 1 446 ? 53.893 -24.568 -65.528 1.00 30.64  ? 446 ARG B C     1 
ATOM   7576 O O     . ARG B 1 446 ? 53.530 -24.746 -64.366 1.00 27.07  ? 446 ARG B O     1 
ATOM   7577 C CB    . ARG B 1 446 ? 52.266 -23.825 -67.329 1.00 31.60  ? 446 ARG B CB    1 
ATOM   7578 C CG    . ARG B 1 446 ? 51.493 -22.685 -67.968 1.00 31.94  ? 446 ARG B CG    1 
ATOM   7579 C CD    . ARG B 1 446 ? 50.124 -23.064 -68.496 1.00 33.34  ? 446 ARG B CD    1 
ATOM   7580 N NE    . ARG B 1 446 ? 50.183 -24.062 -69.544 1.00 38.01  ? 446 ARG B NE    1 
ATOM   7581 C CZ    . ARG B 1 446 ? 49.916 -23.850 -70.835 1.00 40.35  ? 446 ARG B CZ    1 
ATOM   7582 N NH1   . ARG B 1 446 ? 49.643 -22.631 -71.275 1.00 35.71  ? 446 ARG B NH1   1 
ATOM   7583 N NH2   . ARG B 1 446 ? 49.960 -24.866 -71.688 1.00 37.94  ? 446 ARG B NH2   1 
ATOM   7584 N N     . LYS B 1 447 ? 54.792 -25.340 -66.141 1.00 33.50  ? 447 LYS B N     1 
ATOM   7585 C CA    . LYS B 1 447 ? 55.364 -26.527 -65.520 1.00 32.47  ? 447 LYS B CA    1 
ATOM   7586 C C     . LYS B 1 447 ? 56.165 -26.123 -64.278 1.00 28.93  ? 447 LYS B C     1 
ATOM   7587 O O     . LYS B 1 447 ? 56.058 -26.742 -63.229 1.00 24.45  ? 447 LYS B O     1 
ATOM   7588 C CB    . LYS B 1 447 ? 56.205 -27.242 -66.579 1.00 37.67  ? 447 LYS B CB    1 
ATOM   7589 C CG    . LYS B 1 447 ? 56.843 -28.567 -66.176 1.00 46.74  ? 447 LYS B CG    1 
ATOM   7590 C CD    . LYS B 1 447 ? 57.850 -29.048 -67.225 1.00 54.13  ? 447 LYS B CD    1 
ATOM   7591 C CE    . LYS B 1 447 ? 58.044 -30.550 -67.236 1.00 58.21  ? 447 LYS B CE    1 
ATOM   7592 N NZ    . LYS B 1 447 ? 58.659 -31.006 -65.972 1.00 58.38  ? 447 LYS B NZ    1 
ATOM   7593 N N     . LYS B 1 448 ? 56.979 -25.074 -64.396 1.00 30.63  ? 448 LYS B N     1 
ATOM   7594 C CA    . LYS B 1 448 ? 57.754 -24.561 -63.273 1.00 30.93  ? 448 LYS B CA    1 
ATOM   7595 C C     . LYS B 1 448 ? 56.843 -24.067 -62.147 1.00 29.11  ? 448 LYS B C     1 
ATOM   7596 O O     . LYS B 1 448 ? 57.116 -24.306 -60.983 1.00 26.34  ? 448 LYS B O     1 
ATOM   7597 C CB    . LYS B 1 448 ? 58.648 -23.417 -63.749 1.00 31.88  ? 448 LYS B CB    1 
ATOM   7598 C CG    . LYS B 1 448 ? 59.811 -23.859 -64.617 1.00 34.27  ? 448 LYS B CG    1 
ATOM   7599 C CD    . LYS B 1 448 ? 60.469 -22.735 -65.387 1.00 35.98  ? 448 LYS B CD    1 
ATOM   7600 C CE    . LYS B 1 448 ? 60.982 -21.614 -64.520 1.00 35.07  ? 448 LYS B CE    1 
ATOM   7601 N NZ    . LYS B 1 448 ? 61.781 -20.653 -65.315 1.00 36.00  ? 448 LYS B NZ    1 
ATOM   7602 N N     . LEU B 1 449 ? 55.747 -23.389 -62.497 1.00 29.29  ? 449 LEU B N     1 
ATOM   7603 C CA    . LEU B 1 449 ? 54.829 -22.896 -61.490 1.00 32.79  ? 449 LEU B CA    1 
ATOM   7604 C C     . LEU B 1 449 ? 54.241 -24.050 -60.674 1.00 31.09  ? 449 LEU B C     1 
ATOM   7605 O O     . LEU B 1 449 ? 54.213 -24.014 -59.446 1.00 32.90  ? 449 LEU B O     1 
ATOM   7606 C CB    . LEU B 1 449 ? 53.698 -22.102 -62.149 1.00 36.31  ? 449 LEU B CB    1 
ATOM   7607 C CG    . LEU B 1 449 ? 52.674 -21.606 -61.129 1.00 40.97  ? 449 LEU B CG    1 
ATOM   7608 C CD1   . LEU B 1 449 ? 53.158 -20.326 -60.458 1.00 39.61  ? 449 LEU B CD1   1 
ATOM   7609 C CD2   . LEU B 1 449 ? 51.315 -21.428 -61.766 1.00 43.83  ? 449 LEU B CD2   1 
ATOM   7610 N N     . ASP B 1 450 ? 53.718 -25.054 -61.367 1.00 29.32  ? 450 ASP B N     1 
ATOM   7611 C CA    . ASP B 1 450 ? 53.059 -26.161 -60.705 1.00 31.29  ? 450 ASP B CA    1 
ATOM   7612 C C     . ASP B 1 450 ? 54.059 -26.767 -59.731 1.00 28.72  ? 450 ASP B C     1 
ATOM   7613 O O     . ASP B 1 450 ? 53.734 -26.975 -58.572 1.00 30.83  ? 450 ASP B O     1 
ATOM   7614 C CB    . ASP B 1 450 ? 52.448 -27.116 -61.743 1.00 35.00  ? 450 ASP B CB    1 
ATOM   7615 C CG    . ASP B 1 450 ? 51.577 -28.220 -61.165 1.00 41.47  ? 450 ASP B CG    1 
ATOM   7616 O OD1   . ASP B 1 450 ? 50.706 -27.916 -60.301 1.00 38.97  ? 450 ASP B OD1   1 
ATOM   7617 O OD2   . ASP B 1 450 ? 51.736 -29.373 -61.628 1.00 45.88  ? 450 ASP B OD2   1 
ATOM   7618 N N     . GLU B 1 451 ? 55.304 -26.964 -60.171 1.00 27.62  ? 451 GLU B N     1 
ATOM   7619 C CA    . GLU B 1 451 ? 56.274 -27.650 -59.337 1.00 27.51  ? 451 GLU B CA    1 
ATOM   7620 C C     . GLU B 1 451 ? 56.582 -26.796 -58.101 1.00 26.75  ? 451 GLU B C     1 
ATOM   7621 O O     . GLU B 1 451 ? 56.547 -27.292 -56.978 1.00 26.77  ? 451 GLU B O     1 
ATOM   7622 C CB    . GLU B 1 451 ? 57.486 -28.050 -60.177 1.00 27.93  ? 451 GLU B CB    1 
ATOM   7623 C CG    . GLU B 1 451 ? 58.631 -28.639 -59.366 1.00 30.52  ? 451 GLU B CG    1 
ATOM   7624 C CD    . GLU B 1 451 ? 59.801 -29.061 -60.242 1.00 34.67  ? 451 GLU B CD    1 
ATOM   7625 O OE1   . GLU B 1 451 ? 59.548 -29.820 -61.182 1.00 40.34  ? 451 GLU B OE1   1 
ATOM   7626 O OE2   . GLU B 1 451 ? 60.945 -28.594 -60.021 1.00 34.36  ? 451 GLU B OE2   1 
ATOM   7627 N N     . LEU B 1 452 ? 56.846 -25.505 -58.310 1.00 24.59  ? 452 LEU B N     1 
ATOM   7628 C CA    . LEU B 1 452 ? 57.101 -24.566 -57.222 1.00 26.48  ? 452 LEU B CA    1 
ATOM   7629 C C     . LEU B 1 452 ? 55.958 -24.563 -56.197 1.00 26.43  ? 452 LEU B C     1 
ATOM   7630 O O     . LEU B 1 452 ? 56.183 -24.602 -54.981 1.00 24.41  ? 452 LEU B O     1 
ATOM   7631 C CB    . LEU B 1 452 ? 57.296 -23.169 -57.829 1.00 24.32  ? 452 LEU B CB    1 
ATOM   7632 C CG    . LEU B 1 452 ? 57.354 -22.005 -56.841 1.00 23.50  ? 452 LEU B CG    1 
ATOM   7633 C CD1   . LEU B 1 452 ? 58.538 -22.138 -55.914 1.00 24.47  ? 452 LEU B CD1   1 
ATOM   7634 C CD2   . LEU B 1 452 ? 57.416 -20.669 -57.568 1.00 23.36  ? 452 LEU B CD2   1 
ATOM   7635 N N     . PHE B 1 453 ? 54.726 -24.499 -56.705 1.00 24.54  ? 453 PHE B N     1 
ATOM   7636 C CA    . PHE B 1 453 ? 53.566 -24.389 -55.844 1.00 26.18  ? 453 PHE B CA    1 
ATOM   7637 C C     . PHE B 1 453 ? 53.503 -25.577 -54.881 1.00 26.28  ? 453 PHE B C     1 
ATOM   7638 O O     . PHE B 1 453 ? 53.230 -25.395 -53.694 1.00 28.26  ? 453 PHE B O     1 
ATOM   7639 C CB    . PHE B 1 453 ? 52.309 -24.185 -56.691 1.00 25.58  ? 453 PHE B CB    1 
ATOM   7640 C CG    . PHE B 1 453 ? 51.173 -23.647 -55.875 1.00 28.10  ? 453 PHE B CG    1 
ATOM   7641 C CD1   . PHE B 1 453 ? 50.416 -24.490 -55.080 1.00 29.45  ? 453 PHE B CD1   1 
ATOM   7642 C CD2   . PHE B 1 453 ? 50.908 -22.286 -55.848 1.00 29.97  ? 453 PHE B CD2   1 
ATOM   7643 C CE1   . PHE B 1 453 ? 49.392 -23.982 -54.293 1.00 31.23  ? 453 PHE B CE1   1 
ATOM   7644 C CE2   . PHE B 1 453 ? 49.897 -21.774 -55.045 1.00 30.27  ? 453 PHE B CE2   1 
ATOM   7645 C CZ    . PHE B 1 453 ? 49.150 -22.624 -54.263 1.00 31.97  ? 453 PHE B CZ    1 
ATOM   7646 N N     . ASN B 1 454 ? 53.793 -26.782 -55.381 1.00 25.20  ? 454 ASN B N     1 
ATOM   7647 C CA    . ASN B 1 454 ? 53.708 -27.991 -54.579 1.00 26.03  ? 454 ASN B CA    1 
ATOM   7648 C C     . ASN B 1 454 ? 54.792 -27.971 -53.496 1.00 26.54  ? 454 ASN B C     1 
ATOM   7649 O O     . ASN B 1 454 ? 54.544 -28.380 -52.356 1.00 25.15  ? 454 ASN B O     1 
ATOM   7650 C CB    . ASN B 1 454 ? 53.765 -29.258 -55.451 1.00 29.71  ? 454 ASN B CB    1 
ATOM   7651 C CG    . ASN B 1 454 ? 52.481 -29.525 -56.221 1.00 31.64  ? 454 ASN B CG    1 
ATOM   7652 O OD1   . ASN B 1 454 ? 51.401 -29.562 -55.646 1.00 44.32  ? 454 ASN B OD1   1 
ATOM   7653 N ND2   . ASN B 1 454 ? 52.554 -29.707 -57.521 1.00 27.97  ? 454 ASN B ND2   1 
ATOM   7654 N N     . ILE B 1 455 ? 55.988 -27.470 -53.838 1.00 26.44  ? 455 ILE B N     1 
ATOM   7655 C CA    . ILE B 1 455 ? 57.078 -27.340 -52.882 1.00 25.86  ? 455 ILE B CA    1 
ATOM   7656 C C     . ILE B 1 455 ? 56.663 -26.415 -51.738 1.00 26.23  ? 455 ILE B C     1 
ATOM   7657 O O     . ILE B 1 455 ? 56.939 -26.701 -50.572 1.00 28.98  ? 455 ILE B O     1 
ATOM   7658 C CB    . ILE B 1 455 ? 58.369 -26.840 -53.569 1.00 26.39  ? 455 ILE B CB    1 
ATOM   7659 C CG1   . ILE B 1 455 ? 58.915 -27.866 -54.549 1.00 27.12  ? 455 ILE B CG1   1 
ATOM   7660 C CG2   . ILE B 1 455 ? 59.460 -26.465 -52.559 1.00 27.38  ? 455 ILE B CG2   1 
ATOM   7661 C CD1   . ILE B 1 455 ? 59.986 -27.295 -55.433 1.00 31.14  ? 455 ILE B CD1   1 
ATOM   7662 N N     . LEU B 1 456 ? 56.057 -25.276 -52.085 1.00 26.13  ? 456 LEU B N     1 
ATOM   7663 C CA    . LEU B 1 456 ? 55.665 -24.295 -51.089 1.00 27.32  ? 456 LEU B CA    1 
ATOM   7664 C C     . LEU B 1 456 ? 54.651 -24.902 -50.116 1.00 27.55  ? 456 LEU B C     1 
ATOM   7665 O O     . LEU B 1 456 ? 54.783 -24.695 -48.901 1.00 26.37  ? 456 LEU B O     1 
ATOM   7666 C CB    . LEU B 1 456 ? 55.079 -23.068 -51.793 1.00 27.52  ? 456 LEU B CB    1 
ATOM   7667 C CG    . LEU B 1 456 ? 56.056 -22.231 -52.604 1.00 26.49  ? 456 LEU B CG    1 
ATOM   7668 C CD1   . LEU B 1 456 ? 55.349 -21.051 -53.239 1.00 27.35  ? 456 LEU B CD1   1 
ATOM   7669 C CD2   . LEU B 1 456 ? 57.215 -21.758 -51.743 1.00 28.38  ? 456 LEU B CD2   1 
ATOM   7670 N N     . VAL B 1 457 ? 53.654 -25.632 -50.650 1.00 25.34  ? 457 VAL B N     1 
ATOM   7671 C CA    . VAL B 1 457 ? 52.627 -26.235 -49.807 1.00 26.65  ? 457 VAL B CA    1 
ATOM   7672 C C     . VAL B 1 457 ? 53.267 -27.176 -48.790 1.00 27.46  ? 457 VAL B C     1 
ATOM   7673 O O     . VAL B 1 457 ? 52.987 -27.076 -47.598 1.00 31.72  ? 457 VAL B O     1 
ATOM   7674 C CB    . VAL B 1 457 ? 51.534 -26.944 -50.628 1.00 26.40  ? 457 VAL B CB    1 
ATOM   7675 C CG1   . VAL B 1 457 ? 50.646 -27.840 -49.778 1.00 27.67  ? 457 VAL B CG1   1 
ATOM   7676 C CG2   . VAL B 1 457 ? 50.684 -25.941 -51.389 1.00 26.59  ? 457 VAL B CG2   1 
ATOM   7677 N N     . ASP B 1 458 ? 54.148 -28.059 -49.261 1.00 31.55  ? 458 ASP B N     1 
ATOM   7678 C CA    . ASP B 1 458 ? 54.719 -29.122 -48.446 1.00 31.55  ? 458 ASP B CA    1 
ATOM   7679 C C     . ASP B 1 458 ? 55.664 -28.555 -47.393 1.00 28.44  ? 458 ASP B C     1 
ATOM   7680 O O     . ASP B 1 458 ? 55.664 -29.016 -46.260 1.00 29.97  ? 458 ASP B O     1 
ATOM   7681 C CB    . ASP B 1 458 ? 55.493 -30.128 -49.305 1.00 36.26  ? 458 ASP B CB    1 
ATOM   7682 C CG    . ASP B 1 458 ? 54.627 -30.952 -50.244 1.00 38.81  ? 458 ASP B CG    1 
ATOM   7683 O OD1   . ASP B 1 458 ? 53.394 -30.924 -50.090 1.00 46.14  ? 458 ASP B OD1   1 
ATOM   7684 O OD2   . ASP B 1 458 ? 55.194 -31.586 -51.147 1.00 44.42  ? 458 ASP B OD2   1 
ATOM   7685 N N     . GLU B 1 459 ? 56.477 -27.570 -47.776 1.00 27.97  ? 459 GLU B N     1 
ATOM   7686 C CA    . GLU B 1 459 ? 57.460 -26.999 -46.868 1.00 29.62  ? 459 GLU B CA    1 
ATOM   7687 C C     . GLU B 1 459 ? 56.753 -26.190 -45.787 1.00 28.43  ? 459 GLU B C     1 
ATOM   7688 O O     . GLU B 1 459 ? 57.174 -26.222 -44.639 1.00 26.38  ? 459 GLU B O     1 
ATOM   7689 C CB    . GLU B 1 459 ? 58.520 -26.208 -47.640 1.00 30.90  ? 459 GLU B CB    1 
ATOM   7690 C CG    . GLU B 1 459 ? 59.480 -27.132 -48.385 1.00 34.08  ? 459 GLU B CG    1 
ATOM   7691 C CD    . GLU B 1 459 ? 60.675 -26.503 -49.088 1.00 38.24  ? 459 GLU B CD    1 
ATOM   7692 O OE1   . GLU B 1 459 ? 60.785 -25.269 -49.097 1.00 37.67  ? 459 GLU B OE1   1 
ATOM   7693 O OE2   . GLU B 1 459 ? 61.501 -27.269 -49.633 1.00 48.79  ? 459 GLU B OE2   1 
ATOM   7694 N N     . ALA B 1 460 ? 55.641 -25.538 -46.145 1.00 28.95  ? 460 ALA B N     1 
ATOM   7695 C CA    . ALA B 1 460 ? 54.849 -24.801 -45.176 1.00 29.21  ? 460 ALA B CA    1 
ATOM   7696 C C     . ALA B 1 460 ? 54.125 -25.773 -44.235 1.00 25.35  ? 460 ALA B C     1 
ATOM   7697 O O     . ALA B 1 460 ? 54.144 -25.593 -43.019 1.00 20.04  ? 460 ALA B O     1 
ATOM   7698 C CB    . ALA B 1 460 ? 53.901 -23.866 -45.900 1.00 30.15  ? 460 ALA B CB    1 
ATOM   7699 N N     . ALA B 1 461 ? 53.489 -26.802 -44.803 1.00 22.54  ? 461 ALA B N     1 
ATOM   7700 C CA    . ALA B 1 461 ? 52.820 -27.810 -43.995 1.00 22.88  ? 461 ALA B CA    1 
ATOM   7701 C C     . ALA B 1 461 ? 53.799 -28.479 -43.025 1.00 24.18  ? 461 ALA B C     1 
ATOM   7702 O O     . ALA B 1 461 ? 53.442 -28.777 -41.886 1.00 20.85  ? 461 ALA B O     1 
ATOM   7703 C CB    . ALA B 1 461 ? 52.148 -28.825 -44.878 1.00 22.11  ? 461 ALA B CB    1 
ATOM   7704 N N     . ALA B 1 462 ? 55.042 -28.690 -43.461 1.00 24.80  ? 462 ALA B N     1 
ATOM   7705 C CA    . ALA B 1 462 ? 56.042 -29.269 -42.577 1.00 28.02  ? 462 ALA B CA    1 
ATOM   7706 C C     . ALA B 1 462 ? 56.282 -28.359 -41.383 1.00 26.58  ? 462 ALA B C     1 
ATOM   7707 O O     . ALA B 1 462 ? 56.631 -28.859 -40.319 1.00 28.85  ? 462 ALA B O     1 
ATOM   7708 C CB    . ALA B 1 462 ? 57.353 -29.533 -43.291 1.00 28.05  ? 462 ALA B CB    1 
ATOM   7709 N N     . GLU B 1 463 ? 56.103 -27.046 -41.546 1.00 27.20  ? 463 GLU B N     1 
ATOM   7710 C CA    . GLU B 1 463 ? 56.275 -26.117 -40.423 1.00 28.72  ? 463 GLU B CA    1 
ATOM   7711 C C     . GLU B 1 463 ? 54.979 -25.879 -39.644 1.00 25.31  ? 463 GLU B C     1 
ATOM   7712 O O     . GLU B 1 463 ? 54.974 -25.032 -38.767 1.00 25.94  ? 463 GLU B O     1 
ATOM   7713 C CB    . GLU B 1 463 ? 56.768 -24.749 -40.898 1.00 30.40  ? 463 GLU B CB    1 
ATOM   7714 C CG    . GLU B 1 463 ? 58.077 -24.813 -41.661 1.00 35.51  ? 463 GLU B CG    1 
ATOM   7715 C CD    . GLU B 1 463 ? 59.189 -25.449 -40.855 1.00 39.05  ? 463 GLU B CD    1 
ATOM   7716 O OE1   . GLU B 1 463 ? 59.439 -24.958 -39.740 1.00 38.44  ? 463 GLU B OE1   1 
ATOM   7717 O OE2   . GLU B 1 463 ? 59.782 -26.431 -41.341 1.00 44.49  ? 463 GLU B OE2   1 
ATOM   7718 N N     . GLY B 1 464 ? 53.891 -26.594 -39.972 1.00 23.65  ? 464 GLY B N     1 
ATOM   7719 C CA    . GLY B 1 464 ? 52.587 -26.364 -39.370 1.00 23.52  ? 464 GLY B CA    1 
ATOM   7720 C C     . GLY B 1 464 ? 51.866 -25.096 -39.866 1.00 21.90  ? 464 GLY B C     1 
ATOM   7721 O O     . GLY B 1 464 ? 50.980 -24.569 -39.196 1.00 21.30  ? 464 GLY B O     1 
ATOM   7722 N N     . TYR B 1 465 ? 52.220 -24.626 -41.057 1.00 22.72  ? 465 TYR B N     1 
ATOM   7723 C CA    . TYR B 1 465 ? 51.535 -23.519 -41.708 1.00 23.01  ? 465 TYR B CA    1 
ATOM   7724 C C     . TYR B 1 465 ? 50.522 -24.016 -42.744 1.00 22.59  ? 465 TYR B C     1 
ATOM   7725 O O     . TYR B 1 465 ? 50.916 -24.603 -43.752 1.00 23.49  ? 465 TYR B O     1 
ATOM   7726 C CB    . TYR B 1 465 ? 52.559 -22.624 -42.411 1.00 22.61  ? 465 TYR B CB    1 
ATOM   7727 C CG    . TYR B 1 465 ? 53.649 -22.062 -41.531 1.00 21.80  ? 465 TYR B CG    1 
ATOM   7728 C CD1   . TYR B 1 465 ? 53.405 -21.672 -40.219 1.00 22.14  ? 465 TYR B CD1   1 
ATOM   7729 C CD2   . TYR B 1 465 ? 54.914 -21.856 -42.044 1.00 21.41  ? 465 TYR B CD2   1 
ATOM   7730 C CE1   . TYR B 1 465 ? 54.408 -21.146 -39.420 1.00 22.41  ? 465 TYR B CE1   1 
ATOM   7731 C CE2   . TYR B 1 465 ? 55.927 -21.321 -41.271 1.00 22.67  ? 465 TYR B CE2   1 
ATOM   7732 C CZ    . TYR B 1 465 ? 55.666 -20.961 -39.960 1.00 23.36  ? 465 TYR B CZ    1 
ATOM   7733 O OH    . TYR B 1 465 ? 56.667 -20.415 -39.236 1.00 24.39  ? 465 TYR B OH    1 
ATOM   7734 N N     . GLY B 1 466 ? 49.238 -23.679 -42.542 1.00 22.53  ? 466 GLY B N     1 
ATOM   7735 C CA    . GLY B 1 466 ? 48.158 -24.174 -43.383 1.00 23.16  ? 466 GLY B CA    1 
ATOM   7736 C C     . GLY B 1 466 ? 47.453 -23.077 -44.183 1.00 24.91  ? 466 GLY B C     1 
ATOM   7737 O O     . GLY B 1 466 ? 47.171 -21.981 -43.679 1.00 26.07  ? 466 GLY B O     1 
ATOM   7738 N N     . GLU B 1 467 ? 47.132 -23.429 -45.428 1.00 24.20  ? 467 GLU B N     1 
ATOM   7739 C CA    . GLU B 1 467 ? 46.470 -22.552 -46.377 1.00 23.43  ? 467 GLU B CA    1 
ATOM   7740 C C     . GLU B 1 467 ? 44.984 -22.558 -46.077 1.00 22.35  ? 467 GLU B C     1 
ATOM   7741 O O     . GLU B 1 467 ? 44.453 -23.585 -45.650 1.00 23.74  ? 467 GLU B O     1 
ATOM   7742 C CB    . GLU B 1 467 ? 46.642 -23.066 -47.807 1.00 25.49  ? 467 GLU B CB    1 
ATOM   7743 C CG    . GLU B 1 467 ? 45.971 -22.198 -48.865 1.00 28.01  ? 467 GLU B CG    1 
ATOM   7744 C CD    . GLU B 1 467 ? 46.405 -20.732 -48.875 1.00 30.10  ? 467 GLU B CD    1 
ATOM   7745 O OE1   . GLU B 1 467 ? 47.242 -20.364 -49.752 1.00 31.19  ? 467 GLU B OE1   1 
ATOM   7746 O OE2   . GLU B 1 467 ? 45.853 -19.927 -48.056 1.00 26.25  ? 467 GLU B OE2   1 
ATOM   7747 N N     . TYR B 1 468 ? 44.349 -21.407 -46.286 1.00 21.47  ? 468 TYR B N     1 
ATOM   7748 C CA    . TYR B 1 468 ? 42.947 -21.225 -45.952 1.00 23.50  ? 468 TYR B CA    1 
ATOM   7749 C C     . TYR B 1 468 ? 42.108 -20.898 -47.192 1.00 22.90  ? 468 TYR B C     1 
ATOM   7750 O O     . TYR B 1 468 ? 40.893 -20.845 -47.082 1.00 22.73  ? 468 TYR B O     1 
ATOM   7751 C CB    . TYR B 1 468 ? 42.786 -20.079 -44.952 1.00 24.14  ? 468 TYR B CB    1 
ATOM   7752 C CG    . TYR B 1 468 ? 42.835 -18.710 -45.578 1.00 23.41  ? 468 TYR B CG    1 
ATOM   7753 C CD1   . TYR B 1 468 ? 44.037 -18.114 -45.885 1.00 25.23  ? 468 TYR B CD1   1 
ATOM   7754 C CD2   . TYR B 1 468 ? 41.670 -18.032 -45.902 1.00 25.39  ? 468 TYR B CD2   1 
ATOM   7755 C CE1   . TYR B 1 468 ? 44.092 -16.864 -46.481 1.00 26.78  ? 468 TYR B CE1   1 
ATOM   7756 C CE2   . TYR B 1 468 ? 41.696 -16.775 -46.485 1.00 26.68  ? 468 TYR B CE2   1 
ATOM   7757 C CZ    . TYR B 1 468 ? 42.916 -16.202 -46.795 1.00 28.17  ? 468 TYR B CZ    1 
ATOM   7758 O OH    . TYR B 1 468 ? 42.946 -14.960 -47.336 1.00 30.50  ? 468 TYR B OH    1 
ATOM   7759 N N     . ARG B 1 469 ? 42.758 -20.616 -48.329 1.00 21.95  ? 469 ARG B N     1 
ATOM   7760 C CA    . ARG B 1 469 ? 42.087 -20.409 -49.595 1.00 23.74  ? 469 ARG B CA    1 
ATOM   7761 C C     . ARG B 1 469 ? 43.041 -20.771 -50.732 1.00 25.43  ? 469 ARG B C     1 
ATOM   7762 O O     . ARG B 1 469 ? 44.237 -20.515 -50.639 1.00 22.86  ? 469 ARG B O     1 
ATOM   7763 C CB    . ARG B 1 469 ? 41.633 -18.955 -49.705 1.00 24.11  ? 469 ARG B CB    1 
ATOM   7764 C CG    . ARG B 1 469 ? 40.751 -18.675 -50.907 1.00 26.44  ? 469 ARG B CG    1 
ATOM   7765 C CD    . ARG B 1 469 ? 40.355 -17.213 -50.892 1.00 27.25  ? 469 ARG B CD    1 
ATOM   7766 N NE    . ARG B 1 469 ? 39.467 -16.838 -51.974 1.00 26.34  ? 469 ARG B NE    1 
ATOM   7767 C CZ    . ARG B 1 469 ? 39.248 -15.583 -52.343 1.00 27.70  ? 469 ARG B CZ    1 
ATOM   7768 N NH1   . ARG B 1 469 ? 39.783 -14.593 -51.653 1.00 25.81  ? 469 ARG B NH1   1 
ATOM   7769 N NH2   . ARG B 1 469 ? 38.495 -15.319 -53.396 1.00 30.41  ? 469 ARG B NH2   1 
ATOM   7770 N N     . THR B 1 470 ? 42.518 -21.433 -51.778 1.00 27.70  ? 470 THR B N     1 
ATOM   7771 C CA    . THR B 1 470 ? 43.383 -21.976 -52.815 1.00 25.75  ? 470 THR B CA    1 
ATOM   7772 C C     . THR B 1 470 ? 42.653 -22.120 -54.146 1.00 25.23  ? 470 THR B C     1 
ATOM   7773 O O     . THR B 1 470 ? 41.419 -22.109 -54.217 1.00 24.54  ? 470 THR B O     1 
ATOM   7774 C CB    . THR B 1 470 ? 43.996 -23.315 -52.394 1.00 24.81  ? 470 THR B CB    1 
ATOM   7775 O OG1   . THR B 1 470 ? 45.233 -23.478 -53.097 1.00 27.09  ? 470 THR B OG1   1 
ATOM   7776 C CG2   . THR B 1 470 ? 43.091 -24.504 -52.637 1.00 25.95  ? 470 THR B CG2   1 
ATOM   7777 N N     . HIS B 1 471 ? 43.485 -22.214 -55.187 1.00 25.52  ? 471 HIS B N     1 
ATOM   7778 C CA    . HIS B 1 471 ? 43.096 -22.491 -56.563 1.00 26.37  ? 471 HIS B CA    1 
ATOM   7779 C C     . HIS B 1 471 ? 42.497 -23.894 -56.682 1.00 23.61  ? 471 HIS B C     1 
ATOM   7780 O O     . HIS B 1 471 ? 42.878 -24.810 -55.962 1.00 24.02  ? 471 HIS B O     1 
ATOM   7781 C CB    . HIS B 1 471 ? 44.341 -22.344 -57.447 1.00 26.57  ? 471 HIS B CB    1 
ATOM   7782 C CG    . HIS B 1 471 ? 44.134 -22.324 -58.919 1.00 26.19  ? 471 HIS B CG    1 
ATOM   7783 N ND1   . HIS B 1 471 ? 43.798 -23.433 -59.669 1.00 25.72  ? 471 HIS B ND1   1 
ATOM   7784 C CD2   . HIS B 1 471 ? 44.260 -21.293 -59.782 1.00 25.31  ? 471 HIS B CD2   1 
ATOM   7785 C CE1   . HIS B 1 471 ? 43.713 -23.066 -60.949 1.00 28.78  ? 471 HIS B CE1   1 
ATOM   7786 N NE2   . HIS B 1 471 ? 43.994 -21.769 -61.043 1.00 26.67  ? 471 HIS B NE2   1 
ATOM   7787 N N     . ILE B 1 472 ? 41.573 -24.051 -57.631 1.00 23.68  ? 472 ILE B N     1 
ATOM   7788 C CA    . ILE B 1 472 ? 40.884 -25.312 -57.887 1.00 23.74  ? 472 ILE B CA    1 
ATOM   7789 C C     . ILE B 1 472 ? 41.868 -26.471 -58.030 1.00 24.26  ? 472 ILE B C     1 
ATOM   7790 O O     . ILE B 1 472 ? 41.580 -27.586 -57.594 1.00 22.66  ? 472 ILE B O     1 
ATOM   7791 C CB    . ILE B 1 472 ? 39.991 -25.195 -59.136 1.00 22.72  ? 472 ILE B CB    1 
ATOM   7792 C CG1   . ILE B 1 472 ? 40.760 -24.711 -60.363 1.00 26.27  ? 472 ILE B CG1   1 
ATOM   7793 C CG2   . ILE B 1 472 ? 38.804 -24.298 -58.867 1.00 24.50  ? 472 ILE B CG2   1 
ATOM   7794 C CD1   . ILE B 1 472 ? 39.929 -24.672 -61.631 1.00 27.83  ? 472 ILE B CD1   1 
ATOM   7795 N N     . ARG B 1 473 ? 43.014 -26.209 -58.670 1.00 23.72  ? 473 ARG B N     1 
ATOM   7796 C CA    . ARG B 1 473 ? 44.003 -27.243 -58.907 1.00 25.72  ? 473 ARG B CA    1 
ATOM   7797 C C     . ARG B 1 473 ? 44.538 -27.812 -57.588 1.00 25.60  ? 473 ARG B C     1 
ATOM   7798 O O     . ARG B 1 473 ? 44.835 -29.000 -57.533 1.00 23.24  ? 473 ARG B O     1 
ATOM   7799 C CB    . ARG B 1 473 ? 45.125 -26.696 -59.790 1.00 26.87  ? 473 ARG B CB    1 
ATOM   7800 C CG    . ARG B 1 473 ? 46.120 -27.748 -60.255 1.00 28.50  ? 473 ARG B CG    1 
ATOM   7801 C CD    . ARG B 1 473 ? 47.005 -27.196 -61.365 1.00 31.53  ? 473 ARG B CD    1 
ATOM   7802 N NE    . ARG B 1 473 ? 48.070 -28.124 -61.705 1.00 33.80  ? 473 ARG B NE    1 
ATOM   7803 C CZ    . ARG B 1 473 ? 47.914 -29.249 -62.382 1.00 36.34  ? 473 ARG B CZ    1 
ATOM   7804 N NH1   . ARG B 1 473 ? 46.778 -29.510 -62.999 1.00 39.28  ? 473 ARG B NH1   1 
ATOM   7805 N NH2   . ARG B 1 473 ? 48.927 -30.088 -62.489 1.00 37.26  ? 473 ARG B NH2   1 
ATOM   7806 N N     . TYR B 1 474 ? 44.590 -27.012 -56.509 1.00 25.39  ? 474 TYR B N     1 
ATOM   7807 C CA    . TYR B 1 474 ? 45.294 -27.436 -55.301 1.00 24.53  ? 474 TYR B CA    1 
ATOM   7808 C C     . TYR B 1 474 ? 44.345 -27.764 -54.161 1.00 23.42  ? 474 TYR B C     1 
ATOM   7809 O O     . TYR B 1 474 ? 44.796 -28.007 -53.043 1.00 25.49  ? 474 TYR B O     1 
ATOM   7810 C CB    . TYR B 1 474 ? 46.304 -26.361 -54.919 1.00 24.27  ? 474 TYR B CB    1 
ATOM   7811 C CG    . TYR B 1 474 ? 47.267 -26.105 -56.042 1.00 24.21  ? 474 TYR B CG    1 
ATOM   7812 C CD1   . TYR B 1 474 ? 48.115 -27.106 -56.484 1.00 26.66  ? 474 TYR B CD1   1 
ATOM   7813 C CD2   . TYR B 1 474 ? 47.295 -24.899 -56.707 1.00 26.10  ? 474 TYR B CD2   1 
ATOM   7814 C CE1   . TYR B 1 474 ? 48.983 -26.907 -57.549 1.00 27.99  ? 474 TYR B CE1   1 
ATOM   7815 C CE2   . TYR B 1 474 ? 48.178 -24.668 -57.756 1.00 27.80  ? 474 TYR B CE2   1 
ATOM   7816 C CZ    . TYR B 1 474 ? 49.011 -25.685 -58.195 1.00 27.69  ? 474 TYR B CZ    1 
ATOM   7817 O OH    . TYR B 1 474 ? 49.869 -25.483 -59.245 1.00 28.76  ? 474 TYR B OH    1 
ATOM   7818 N N     . MET B 1 475 ? 43.048 -27.852 -54.462 1.00 23.56  ? 475 MET B N     1 
ATOM   7819 C CA    . MET B 1 475 ? 42.045 -27.987 -53.411 1.00 24.90  ? 475 MET B CA    1 
ATOM   7820 C C     . MET B 1 475 ? 42.215 -29.327 -52.704 1.00 25.08  ? 475 MET B C     1 
ATOM   7821 O O     . MET B 1 475 ? 42.164 -29.370 -51.479 1.00 24.08  ? 475 MET B O     1 
ATOM   7822 C CB    . MET B 1 475 ? 40.607 -27.813 -53.930 1.00 22.13  ? 475 MET B CB    1 
ATOM   7823 C CG    . MET B 1 475 ? 40.269 -26.338 -54.118 1.00 22.55  ? 475 MET B CG    1 
ATOM   7824 S SD    . MET B 1 475 ? 38.650 -25.973 -54.855 1.00 20.97  ? 475 MET B SD    1 
ATOM   7825 C CE    . MET B 1 475 ? 38.725 -24.191 -55.047 1.00 23.42  ? 475 MET B CE    1 
ATOM   7826 N N     . ASP B 1 476 ? 42.482 -30.394 -53.473 1.00 26.95  ? 476 ASP B N     1 
ATOM   7827 C CA    . ASP B 1 476 ? 42.748 -31.706 -52.892 1.00 27.00  ? 476 ASP B CA    1 
ATOM   7828 C C     . ASP B 1 476 ? 44.044 -31.672 -52.089 1.00 25.60  ? 476 ASP B C     1 
ATOM   7829 O O     . ASP B 1 476 ? 44.086 -32.171 -50.969 1.00 25.97  ? 476 ASP B O     1 
ATOM   7830 C CB    . ASP B 1 476 ? 42.813 -32.818 -53.945 1.00 26.77  ? 476 ASP B CB    1 
ATOM   7831 C CG    . ASP B 1 476 ? 41.471 -33.414 -54.334 1.00 27.94  ? 476 ASP B CG    1 
ATOM   7832 O OD1   . ASP B 1 476 ? 40.438 -33.009 -53.763 1.00 28.20  ? 476 ASP B OD1   1 
ATOM   7833 O OD2   . ASP B 1 476 ? 41.459 -34.261 -55.244 1.00 33.51  ? 476 ASP B OD2   1 
ATOM   7834 N N     . ARG B 1 477 ? 45.096 -31.058 -52.636 1.00 27.04  ? 477 ARG B N     1 
ATOM   7835 C CA    . ARG B 1 477 ? 46.365 -31.049 -51.935 1.00 30.06  ? 477 ARG B CA    1 
ATOM   7836 C C     . ARG B 1 477 ? 46.227 -30.342 -50.587 1.00 28.05  ? 477 ARG B C     1 
ATOM   7837 O O     . ARG B 1 477 ? 46.795 -30.786 -49.590 1.00 26.28  ? 477 ARG B O     1 
ATOM   7838 C CB    . ARG B 1 477 ? 47.483 -30.419 -52.767 1.00 35.60  ? 477 ARG B CB    1 
ATOM   7839 C CG    . ARG B 1 477 ? 48.853 -30.976 -52.400 1.00 44.51  ? 477 ARG B CG    1 
ATOM   7840 C CD    . ARG B 1 477 ? 49.952 -30.411 -53.277 1.00 57.35  ? 477 ARG B CD    1 
ATOM   7841 N NE    . ARG B 1 477 ? 50.875 -31.437 -53.768 1.00 59.64  ? 477 ARG B NE    1 
ATOM   7842 C CZ    . ARG B 1 477 ? 52.125 -31.564 -53.354 1.00 63.64  ? 477 ARG B CZ    1 
ATOM   7843 N NH1   . ARG B 1 477 ? 52.593 -30.732 -52.438 1.00 67.93  ? 477 ARG B NH1   1 
ATOM   7844 N NH2   . ARG B 1 477 ? 52.891 -32.524 -53.840 1.00 64.34  ? 477 ARG B NH2   1 
ATOM   7845 N N     . ILE B 1 478 ? 45.507 -29.215 -50.562 1.00 26.55  ? 478 ILE B N     1 
ATOM   7846 C CA    . ILE B 1 478 ? 45.396 -28.464 -49.324 1.00 24.36  ? 478 ILE B CA    1 
ATOM   7847 C C     . ILE B 1 478 ? 44.535 -29.249 -48.338 1.00 23.14  ? 478 ILE B C     1 
ATOM   7848 O O     . ILE B 1 478 ? 44.880 -29.321 -47.152 1.00 22.29  ? 478 ILE B O     1 
ATOM   7849 C CB    . ILE B 1 478 ? 44.836 -27.047 -49.556 1.00 24.22  ? 478 ILE B CB    1 
ATOM   7850 C CG1   . ILE B 1 478 ? 45.728 -26.201 -50.479 1.00 22.93  ? 478 ILE B CG1   1 
ATOM   7851 C CG2   . ILE B 1 478 ? 44.572 -26.387 -48.208 1.00 23.72  ? 478 ILE B CG2   1 
ATOM   7852 C CD1   . ILE B 1 478 ? 47.203 -26.280 -50.155 1.00 23.42  ? 478 ILE B CD1   1 
ATOM   7853 N N     . ALA B 1 479 ? 43.429 -29.843 -48.818 1.00 21.16  ? 479 ALA B N     1 
ATOM   7854 C CA    . ALA B 1 479 ? 42.580 -30.623 -47.925 1.00 22.88  ? 479 ALA B CA    1 
ATOM   7855 C C     . ALA B 1 479 ? 43.393 -31.698 -47.214 1.00 24.37  ? 479 ALA B C     1 
ATOM   7856 O O     . ALA B 1 479 ? 43.162 -31.934 -46.022 1.00 23.74  ? 479 ALA B O     1 
ATOM   7857 C CB    . ALA B 1 479 ? 41.415 -31.247 -48.648 1.00 23.50  ? 479 ALA B CB    1 
ATOM   7858 N N     . LYS B 1 480 ? 44.347 -32.323 -47.941 1.00 23.99  ? 480 LYS B N     1 
ATOM   7859 C CA    . LYS B 1 480 ? 45.103 -33.434 -47.379 1.00 24.96  ? 480 LYS B CA    1 
ATOM   7860 C C     . LYS B 1 480 ? 46.103 -32.972 -46.327 1.00 25.33  ? 480 LYS B C     1 
ATOM   7861 O O     . LYS B 1 480 ? 46.561 -33.811 -45.561 1.00 26.39  ? 480 LYS B O     1 
ATOM   7862 C CB    . LYS B 1 480 ? 45.837 -34.223 -48.465 1.00 29.30  ? 480 LYS B CB    1 
ATOM   7863 C CG    . LYS B 1 480 ? 44.938 -35.089 -49.332 1.00 32.10  ? 480 LYS B CG    1 
ATOM   7864 C CD    . LYS B 1 480 ? 45.608 -35.576 -50.578 1.00 40.06  ? 480 LYS B CD    1 
ATOM   7865 C CE    . LYS B 1 480 ? 44.668 -36.337 -51.498 1.00 51.51  ? 480 LYS B CE    1 
ATOM   7866 N NZ    . LYS B 1 480 ? 45.117 -36.251 -52.916 1.00 58.05  ? 480 LYS B NZ    1 
ATOM   7867 N N     . THR B 1 481 ? 46.413 -31.666 -46.243 1.00 23.96  ? 481 THR B N     1 
ATOM   7868 C CA    . THR B 1 481 ? 47.285 -31.179 -45.178 1.00 24.07  ? 481 THR B CA    1 
ATOM   7869 C C     . THR B 1 481 ? 46.550 -31.086 -43.832 1.00 25.03  ? 481 THR B C     1 
ATOM   7870 O O     . THR B 1 481 ? 47.200 -31.107 -42.786 1.00 23.77  ? 481 THR B O     1 
ATOM   7871 C CB    . THR B 1 481 ? 47.945 -29.852 -45.564 1.00 23.59  ? 481 THR B CB    1 
ATOM   7872 O OG1   . THR B 1 481 ? 46.996 -28.788 -45.573 1.00 22.69  ? 481 THR B OG1   1 
ATOM   7873 C CG2   . THR B 1 481 ? 48.608 -29.930 -46.920 1.00 22.29  ? 481 THR B CG2   1 
ATOM   7874 N N     . TYR B 1 482 ? 45.203 -31.045 -43.842 1.00 23.83  ? 482 TYR B N     1 
ATOM   7875 C CA    . TYR B 1 482 ? 44.422 -30.987 -42.609 1.00 23.09  ? 482 TYR B CA    1 
ATOM   7876 C C     . TYR B 1 482 ? 44.111 -32.410 -42.121 1.00 26.54  ? 482 TYR B C     1 
ATOM   7877 O O     . TYR B 1 482 ? 42.949 -32.758 -41.913 1.00 25.92  ? 482 TYR B O     1 
ATOM   7878 C CB    . TYR B 1 482 ? 43.195 -30.087 -42.823 1.00 21.07  ? 482 TYR B CB    1 
ATOM   7879 C CG    . TYR B 1 482 ? 43.554 -28.630 -42.977 1.00 20.33  ? 482 TYR B CG    1 
ATOM   7880 C CD1   . TYR B 1 482 ? 43.804 -27.820 -41.861 1.00 19.92  ? 482 TYR B CD1   1 
ATOM   7881 C CD2   . TYR B 1 482 ? 43.753 -28.074 -44.233 1.00 18.34  ? 482 TYR B CD2   1 
ATOM   7882 C CE1   . TYR B 1 482 ? 44.191 -26.493 -42.002 1.00 18.45  ? 482 TYR B CE1   1 
ATOM   7883 C CE2   . TYR B 1 482 ? 44.157 -26.759 -44.384 1.00 18.94  ? 482 TYR B CE2   1 
ATOM   7884 C CZ    . TYR B 1 482 ? 44.369 -25.963 -43.266 1.00 19.57  ? 482 TYR B CZ    1 
ATOM   7885 O OH    . TYR B 1 482 ? 44.782 -24.661 -43.428 1.00 22.88  ? 482 TYR B OH    1 
ATOM   7886 N N     . SER B 1 483 ? 45.174 -33.191 -41.842 1.00 26.15  ? 483 SER B N     1 
ATOM   7887 C CA    . SER B 1 483 ? 45.085 -34.639 -41.708 1.00 26.73  ? 483 SER B CA    1 
ATOM   7888 C C     . SER B 1 483 ? 44.974 -35.126 -40.259 1.00 27.18  ? 483 SER B C     1 
ATOM   7889 O O     . SER B 1 483 ? 44.960 -36.333 -40.025 1.00 25.95  ? 483 SER B O     1 
ATOM   7890 C CB    . SER B 1 483 ? 46.262 -35.303 -42.377 1.00 25.08  ? 483 SER B CB    1 
ATOM   7891 O OG    . SER B 1 483 ? 47.464 -34.918 -41.743 1.00 25.70  ? 483 SER B OG    1 
ATOM   7892 N N     . TRP B 1 484 ? 44.851 -34.227 -39.279 1.00 27.02  ? 484 TRP B N     1 
ATOM   7893 C CA    . TRP B 1 484 ? 44.728 -34.655 -37.890 1.00 26.37  ? 484 TRP B CA    1 
ATOM   7894 C C     . TRP B 1 484 ? 43.781 -35.857 -37.742 1.00 23.04  ? 484 TRP B C     1 
ATOM   7895 O O     . TRP B 1 484 ? 42.667 -35.857 -38.258 1.00 19.91  ? 484 TRP B O     1 
ATOM   7896 C CB    . TRP B 1 484 ? 44.272 -33.494 -36.999 1.00 27.39  ? 484 TRP B CB    1 
ATOM   7897 C CG    . TRP B 1 484 ? 44.421 -33.829 -35.545 1.00 30.40  ? 484 TRP B CG    1 
ATOM   7898 C CD1   . TRP B 1 484 ? 45.593 -33.870 -34.841 1.00 30.59  ? 484 TRP B CD1   1 
ATOM   7899 C CD2   . TRP B 1 484 ? 43.389 -34.258 -34.638 1.00 27.30  ? 484 TRP B CD2   1 
ATOM   7900 N NE1   . TRP B 1 484 ? 45.353 -34.254 -33.550 1.00 30.32  ? 484 TRP B NE1   1 
ATOM   7901 C CE2   . TRP B 1 484 ? 44.022 -34.526 -33.396 1.00 27.92  ? 484 TRP B CE2   1 
ATOM   7902 C CE3   . TRP B 1 484 ? 41.999 -34.422 -34.740 1.00 28.12  ? 484 TRP B CE3   1 
ATOM   7903 C CZ2   . TRP B 1 484 ? 43.317 -34.940 -32.263 1.00 26.13  ? 484 TRP B CZ2   1 
ATOM   7904 C CZ3   . TRP B 1 484 ? 41.294 -34.833 -33.622 1.00 28.24  ? 484 TRP B CZ3   1 
ATOM   7905 C CH2   . TRP B 1 484 ? 41.950 -35.074 -32.398 1.00 28.79  ? 484 TRP B CH2   1 
ATOM   7906 N N     . ASN B 1 485 ? 44.253 -36.875 -37.012 1.00 22.56  ? 485 ASN B N     1 
ATOM   7907 C CA    . ASN B 1 485 ? 43.493 -38.069 -36.674 1.00 24.21  ? 485 ASN B CA    1 
ATOM   7908 C C     . ASN B 1 485 ? 42.997 -38.788 -37.925 1.00 26.74  ? 485 ASN B C     1 
ATOM   7909 O O     . ASN B 1 485 ? 41.806 -39.085 -38.061 1.00 27.56  ? 485 ASN B O     1 
ATOM   7910 C CB    . ASN B 1 485 ? 42.327 -37.728 -35.740 1.00 25.06  ? 485 ASN B CB    1 
ATOM   7911 C CG    . ASN B 1 485 ? 41.723 -38.981 -35.163 1.00 26.35  ? 485 ASN B CG    1 
ATOM   7912 O OD1   . ASN B 1 485 ? 42.436 -39.967 -34.969 1.00 27.70  ? 485 ASN B OD1   1 
ATOM   7913 N ND2   . ASN B 1 485 ? 40.424 -38.969 -34.921 1.00 26.98  ? 485 ASN B ND2   1 
ATOM   7914 N N     . ASP B 1 486 ? 43.915 -39.009 -38.869 1.00 28.97  ? 486 ASP B N     1 
ATOM   7915 C CA    . ASP B 1 486 ? 43.626 -39.731 -40.102 1.00 32.86  ? 486 ASP B CA    1 
ATOM   7916 C C     . ASP B 1 486 ? 42.472 -39.069 -40.874 1.00 29.72  ? 486 ASP B C     1 
ATOM   7917 O O     . ASP B 1 486 ? 41.534 -39.728 -41.307 1.00 28.05  ? 486 ASP B O     1 
ATOM   7918 C CB    . ASP B 1 486 ? 43.454 -41.233 -39.824 1.00 38.27  ? 486 ASP B CB    1 
ATOM   7919 C CG    . ASP B 1 486 ? 43.461 -42.068 -41.100 1.00 52.61  ? 486 ASP B CG    1 
ATOM   7920 O OD1   . ASP B 1 486 ? 44.314 -41.782 -41.992 1.00 55.97  ? 486 ASP B OD1   1 
ATOM   7921 O OD2   . ASP B 1 486 ? 42.599 -42.981 -41.224 1.00 58.46  ? 486 ASP B OD2   1 
ATOM   7922 N N     . ASN B 1 487 ? 42.587 -37.753 -41.095 1.00 29.38  ? 487 ASN B N     1 
ATOM   7923 C CA    . ASN B 1 487 ? 41.683 -36.970 -41.930 1.00 25.94  ? 487 ASN B CA    1 
ATOM   7924 C C     . ASN B 1 487 ? 40.262 -36.972 -41.361 1.00 24.28  ? 487 ASN B C     1 
ATOM   7925 O O     . ASN B 1 487 ? 39.288 -36.981 -42.113 1.00 22.54  ? 487 ASN B O     1 
ATOM   7926 C CB    . ASN B 1 487 ? 41.694 -37.446 -43.382 1.00 25.11  ? 487 ASN B CB    1 
ATOM   7927 C CG    . ASN B 1 487 ? 43.090 -37.533 -43.953 1.00 25.08  ? 487 ASN B CG    1 
ATOM   7928 O OD1   . ASN B 1 487 ? 43.682 -38.599 -43.968 1.00 28.18  ? 487 ASN B OD1   1 
ATOM   7929 N ND2   . ASN B 1 487 ? 43.659 -36.411 -44.344 1.00 24.40  ? 487 ASN B ND2   1 
ATOM   7930 N N     . ALA B 1 488 ? 40.150 -36.902 -40.028 1.00 25.57  ? 488 ALA B N     1 
ATOM   7931 C CA    . ALA B 1 488 ? 38.860 -36.959 -39.351 1.00 25.66  ? 488 ALA B CA    1 
ATOM   7932 C C     . ALA B 1 488 ? 37.908 -35.864 -39.838 1.00 26.52  ? 488 ALA B C     1 
ATOM   7933 O O     . ALA B 1 488 ? 36.727 -36.138 -40.016 1.00 25.21  ? 488 ALA B O     1 
ATOM   7934 C CB    . ALA B 1 488 ? 39.053 -36.865 -37.862 1.00 26.72  ? 488 ALA B CB    1 
ATOM   7935 N N     . LEU B 1 489 ? 38.414 -34.638 -40.059 1.00 25.96  ? 489 LEU B N     1 
ATOM   7936 C CA    . LEU B 1 489 ? 37.547 -33.519 -40.389 1.00 26.01  ? 489 LEU B CA    1 
ATOM   7937 C C     . LEU B 1 489 ? 36.919 -33.677 -41.775 1.00 25.95  ? 489 LEU B C     1 
ATOM   7938 O O     . LEU B 1 489 ? 35.716 -33.459 -41.950 1.00 24.44  ? 489 LEU B O     1 
ATOM   7939 C CB    . LEU B 1 489 ? 38.351 -32.220 -40.301 1.00 28.87  ? 489 LEU B CB    1 
ATOM   7940 C CG    . LEU B 1 489 ? 37.563 -30.948 -40.618 1.00 30.23  ? 489 LEU B CG    1 
ATOM   7941 C CD1   . LEU B 1 489 ? 36.332 -30.856 -39.744 1.00 29.76  ? 489 LEU B CD1   1 
ATOM   7942 C CD2   . LEU B 1 489 ? 38.422 -29.706 -40.425 1.00 32.85  ? 489 LEU B CD2   1 
ATOM   7943 N N     . TRP B 1 490 ? 37.733 -34.040 -42.772 1.00 23.86  ? 490 TRP B N     1 
ATOM   7944 C CA    . TRP B 1 490 ? 37.191 -34.257 -44.095 1.00 24.24  ? 490 TRP B CA    1 
ATOM   7945 C C     . TRP B 1 490 ? 36.236 -35.441 -44.092 1.00 24.45  ? 490 TRP B C     1 
ATOM   7946 O O     . TRP B 1 490 ? 35.268 -35.435 -44.832 1.00 21.51  ? 490 TRP B O     1 
ATOM   7947 C CB    . TRP B 1 490 ? 38.284 -34.373 -45.163 1.00 23.87  ? 490 TRP B CB    1 
ATOM   7948 C CG    . TRP B 1 490 ? 38.376 -33.080 -45.912 1.00 25.38  ? 490 TRP B CG    1 
ATOM   7949 C CD1   . TRP B 1 490 ? 37.965 -32.845 -47.191 1.00 25.26  ? 490 TRP B CD1   1 
ATOM   7950 C CD2   . TRP B 1 490 ? 38.779 -31.804 -45.380 1.00 25.53  ? 490 TRP B CD2   1 
ATOM   7951 N NE1   . TRP B 1 490 ? 38.129 -31.529 -47.504 1.00 25.02  ? 490 TRP B NE1   1 
ATOM   7952 C CE2   . TRP B 1 490 ? 38.631 -30.864 -46.419 1.00 25.05  ? 490 TRP B CE2   1 
ATOM   7953 C CE3   . TRP B 1 490 ? 39.276 -31.373 -44.141 1.00 26.86  ? 490 TRP B CE3   1 
ATOM   7954 C CZ2   . TRP B 1 490 ? 38.992 -29.525 -46.269 1.00 25.68  ? 490 TRP B CZ2   1 
ATOM   7955 C CZ3   . TRP B 1 490 ? 39.610 -30.045 -43.983 1.00 25.32  ? 490 TRP B CZ3   1 
ATOM   7956 C CH2   . TRP B 1 490 ? 39.474 -29.140 -45.036 1.00 26.26  ? 490 TRP B CH2   1 
ATOM   7957 N N     . LYS B 1 491 ? 36.472 -36.427 -43.226 1.00 25.69  ? 491 LYS B N     1 
ATOM   7958 C CA    . LYS B 1 491 ? 35.552 -37.549 -43.160 1.00 26.16  ? 491 LYS B CA    1 
ATOM   7959 C C     . LYS B 1 491 ? 34.189 -37.039 -42.725 1.00 23.79  ? 491 LYS B C     1 
ATOM   7960 O O     . LYS B 1 491 ? 33.180 -37.520 -43.229 1.00 30.16  ? 491 LYS B O     1 
ATOM   7961 C CB    . LYS B 1 491 ? 36.062 -38.662 -42.247 1.00 27.06  ? 491 LYS B CB    1 
ATOM   7962 C CG    . LYS B 1 491 ? 37.155 -39.524 -42.859 1.00 28.13  ? 491 LYS B CG    1 
ATOM   7963 C CD    . LYS B 1 491 ? 37.721 -40.516 -41.855 1.00 27.92  ? 491 LYS B CD    1 
ATOM   7964 C CE    . LYS B 1 491 ? 38.913 -41.266 -42.402 1.00 27.89  ? 491 LYS B CE    1 
ATOM   7965 N NZ    . LYS B 1 491 ? 39.552 -42.059 -41.329 1.00 29.26  ? 491 LYS B NZ    1 
ATOM   7966 N N     . MET B 1 492 ? 34.178 -36.059 -41.823 1.00 22.28  ? 492 MET B N     1 
ATOM   7967 C CA    . MET B 1 492 ? 32.937 -35.446 -41.376 1.00 22.84  ? 492 MET B CA    1 
ATOM   7968 C C     . MET B 1 492 ? 32.368 -34.571 -42.490 1.00 22.64  ? 492 MET B C     1 
ATOM   7969 O O     . MET B 1 492 ? 31.156 -34.548 -42.677 1.00 24.22  ? 492 MET B O     1 
ATOM   7970 C CB    . MET B 1 492 ? 33.128 -34.595 -40.125 1.00 23.86  ? 492 MET B CB    1 
ATOM   7971 C CG    . MET B 1 492 ? 31.831 -34.073 -39.545 1.00 28.23  ? 492 MET B CG    1 
ATOM   7972 S SD    . MET B 1 492 ? 32.079 -32.784 -38.266 1.00 29.36  ? 492 MET B SD    1 
ATOM   7973 C CE    . MET B 1 492 ? 32.382 -31.388 -39.344 1.00 27.94  ? 492 MET B CE    1 
ATOM   7974 N N     . HIS B 1 493 ? 33.215 -33.889 -43.268 1.00 21.87  ? 493 HIS B N     1 
ATOM   7975 C CA    . HIS B 1 493 ? 32.668 -33.070 -44.340 1.00 22.62  ? 493 HIS B CA    1 
ATOM   7976 C C     . HIS B 1 493 ? 31.955 -33.953 -45.360 1.00 22.55  ? 493 HIS B C     1 
ATOM   7977 O O     . HIS B 1 493 ? 30.870 -33.604 -45.819 1.00 23.32  ? 493 HIS B O     1 
ATOM   7978 C CB    . HIS B 1 493 ? 33.725 -32.223 -45.045 1.00 21.85  ? 493 HIS B CB    1 
ATOM   7979 C CG    . HIS B 1 493 ? 34.306 -31.124 -44.255 1.00 22.68  ? 493 HIS B CG    1 
ATOM   7980 N ND1   . HIS B 1 493 ? 33.552 -30.269 -43.489 1.00 26.17  ? 493 HIS B ND1   1 
ATOM   7981 C CD2   . HIS B 1 493 ? 35.579 -30.694 -44.164 1.00 22.42  ? 493 HIS B CD2   1 
ATOM   7982 C CE1   . HIS B 1 493 ? 34.372 -29.366 -42.954 1.00 26.87  ? 493 HIS B CE1   1 
ATOM   7983 N NE2   . HIS B 1 493 ? 35.606 -29.608 -43.352 1.00 21.67  ? 493 HIS B NE2   1 
ATOM   7984 N N     . GLU B 1 494 ? 32.559 -35.110 -45.662 1.00 25.25  ? 494 GLU B N     1 
ATOM   7985 C CA    . GLU B 1 494 ? 32.047 -36.060 -46.642 1.00 26.71  ? 494 GLU B CA    1 
ATOM   7986 C C     . GLU B 1 494 ? 30.716 -36.640 -46.146 1.00 26.77  ? 494 GLU B C     1 
ATOM   7987 O O     . GLU B 1 494 ? 29.801 -36.883 -46.946 1.00 23.80  ? 494 GLU B O     1 
ATOM   7988 C CB    . GLU B 1 494 ? 33.085 -37.160 -46.935 1.00 27.51  ? 494 GLU B CB    1 
ATOM   7989 C CG    . GLU B 1 494 ? 34.322 -36.755 -47.761 1.00 30.37  ? 494 GLU B CG    1 
ATOM   7990 C CD    . GLU B 1 494 ? 34.217 -36.396 -49.251 1.00 40.11  ? 494 GLU B CD    1 
ATOM   7991 O OE1   . GLU B 1 494 ? 33.099 -36.524 -49.853 1.00 35.61  ? 494 GLU B OE1   1 
ATOM   7992 O OE2   . GLU B 1 494 ? 35.307 -36.000 -49.866 1.00 46.14  ? 494 GLU B OE2   1 
ATOM   7993 N N     . THR B 1 495 ? 30.613 -36.869 -44.819 1.00 25.37  ? 495 THR B N     1 
ATOM   7994 C CA    . THR B 1 495 ? 29.377 -37.365 -44.239 1.00 24.80  ? 495 THR B CA    1 
ATOM   7995 C C     . THR B 1 495 ? 28.234 -36.375 -44.472 1.00 26.87  ? 495 THR B C     1 
ATOM   7996 O O     . THR B 1 495 ? 27.139 -36.778 -44.856 1.00 28.32  ? 495 THR B O     1 
ATOM   7997 C CB    . THR B 1 495 ? 29.535 -37.657 -42.749 1.00 24.72  ? 495 THR B CB    1 
ATOM   7998 O OG1   . THR B 1 495 ? 30.471 -38.714 -42.596 1.00 25.02  ? 495 THR B OG1   1 
ATOM   7999 C CG2   . THR B 1 495 ? 28.242 -38.054 -42.075 1.00 24.55  ? 495 THR B CG2   1 
ATOM   8000 N N     . ILE B 1 496 ? 28.491 -35.084 -44.233 1.00 26.68  ? 496 ILE B N     1 
ATOM   8001 C CA    . ILE B 1 496 ? 27.484 -34.049 -44.396 1.00 26.75  ? 496 ILE B CA    1 
ATOM   8002 C C     . ILE B 1 496 ? 27.145 -33.915 -45.877 1.00 26.85  ? 496 ILE B C     1 
ATOM   8003 O O     . ILE B 1 496 ? 25.991 -33.756 -46.264 1.00 33.28  ? 496 ILE B O     1 
ATOM   8004 C CB    . ILE B 1 496 ? 27.992 -32.720 -43.790 1.00 26.69  ? 496 ILE B CB    1 
ATOM   8005 C CG1   . ILE B 1 496 ? 28.117 -32.814 -42.267 1.00 27.34  ? 496 ILE B CG1   1 
ATOM   8006 C CG2   . ILE B 1 496 ? 27.109 -31.553 -44.204 1.00 26.72  ? 496 ILE B CG2   1 
ATOM   8007 C CD1   . ILE B 1 496 ? 28.865 -31.663 -41.601 1.00 27.46  ? 496 ILE B CD1   1 
ATOM   8008 N N     . LYS B 1 497 ? 28.171 -33.981 -46.714 1.00 25.95  ? 497 LYS B N     1 
ATOM   8009 C CA    . LYS B 1 497 ? 27.991 -33.906 -48.153 1.00 23.90  ? 497 LYS B CA    1 
ATOM   8010 C C     . LYS B 1 497 ? 27.044 -35.006 -48.631 1.00 24.45  ? 497 LYS B C     1 
ATOM   8011 O O     . LYS B 1 497 ? 26.192 -34.781 -49.488 1.00 24.41  ? 497 LYS B O     1 
ATOM   8012 C CB    . LYS B 1 497 ? 29.356 -34.075 -48.825 1.00 24.35  ? 497 LYS B CB    1 
ATOM   8013 C CG    . LYS B 1 497 ? 29.344 -34.194 -50.340 1.00 23.26  ? 497 LYS B CG    1 
ATOM   8014 C CD    . LYS B 1 497 ? 28.852 -32.958 -50.995 1.00 24.22  ? 497 LYS B CD    1 
ATOM   8015 C CE    . LYS B 1 497 ? 29.162 -32.881 -52.475 1.00 26.77  ? 497 LYS B CE    1 
ATOM   8016 N NZ    . LYS B 1 497 ? 28.585 -31.644 -53.072 1.00 27.49  ? 497 LYS B NZ    1 
ATOM   8017 N N     . ASP B 1 498 ? 27.246 -36.226 -48.121 1.00 23.76  ? 498 ASP B N     1 
ATOM   8018 C CA    . ASP B 1 498 ? 26.470 -37.367 -48.585 1.00 25.21  ? 498 ASP B CA    1 
ATOM   8019 C C     . ASP B 1 498 ? 25.004 -37.199 -48.184 1.00 23.12  ? 498 ASP B C     1 
ATOM   8020 O O     . ASP B 1 498 ? 24.118 -37.536 -48.952 1.00 22.12  ? 498 ASP B O     1 
ATOM   8021 C CB    . ASP B 1 498 ? 27.125 -38.681 -48.135 1.00 27.15  ? 498 ASP B CB    1 
ATOM   8022 C CG    . ASP B 1 498 ? 28.337 -39.080 -48.982 1.00 28.56  ? 498 ASP B CG    1 
ATOM   8023 O OD1   . ASP B 1 498 ? 28.516 -38.527 -50.113 1.00 27.49  ? 498 ASP B OD1   1 
ATOM   8024 O OD2   . ASP B 1 498 ? 29.138 -39.891 -48.493 1.00 31.40  ? 498 ASP B OD2   1 
ATOM   8025 N N     . ALA B 1 499 ? 24.763 -36.583 -47.023 1.00 22.97  ? 499 ALA B N     1 
ATOM   8026 C CA    . ALA B 1 499 ? 23.430 -36.366 -46.494 1.00 22.32  ? 499 ALA B CA    1 
ATOM   8027 C C     . ALA B 1 499 ? 22.684 -35.238 -47.234 1.00 23.59  ? 499 ALA B C     1 
ATOM   8028 O O     . ALA B 1 499 ? 21.531 -35.391 -47.600 1.00 24.50  ? 499 ALA B O     1 
ATOM   8029 C CB    . ALA B 1 499 ? 23.575 -36.091 -45.015 1.00 22.17  ? 499 ALA B CB    1 
ATOM   8030 N N     . LEU B 1 500 ? 23.326 -34.096 -47.466 1.00 24.12  ? 500 LEU B N     1 
ATOM   8031 C CA    . LEU B 1 500 ? 22.689 -32.998 -48.172 1.00 24.85  ? 500 LEU B CA    1 
ATOM   8032 C C     . LEU B 1 500 ? 22.664 -33.241 -49.678 1.00 25.02  ? 500 LEU B C     1 
ATOM   8033 O O     . LEU B 1 500 ? 21.765 -32.733 -50.329 1.00 25.45  ? 500 LEU B O     1 
ATOM   8034 C CB    . LEU B 1 500 ? 23.446 -31.690 -47.912 1.00 25.92  ? 500 LEU B CB    1 
ATOM   8035 C CG    . LEU B 1 500 ? 23.563 -31.286 -46.453 1.00 24.88  ? 500 LEU B CG    1 
ATOM   8036 C CD1   . LEU B 1 500 ? 24.338 -29.991 -46.324 1.00 26.37  ? 500 LEU B CD1   1 
ATOM   8037 C CD2   . LEU B 1 500 ? 22.183 -31.147 -45.827 1.00 25.60  ? 500 LEU B CD2   1 
ATOM   8038 N N     . ASP B 1 501 ? 23.678 -33.919 -50.237 1.00 26.19  ? 501 ASP B N     1 
ATOM   8039 C CA    . ASP B 1 501 ? 23.844 -34.009 -51.685 1.00 26.34  ? 501 ASP B CA    1 
ATOM   8040 C C     . ASP B 1 501 ? 24.121 -35.456 -52.072 1.00 25.84  ? 501 ASP B C     1 
ATOM   8041 O O     . ASP B 1 501 ? 25.188 -35.764 -52.587 1.00 27.06  ? 501 ASP B O     1 
ATOM   8042 C CB    . ASP B 1 501 ? 24.976 -33.100 -52.180 1.00 27.04  ? 501 ASP B CB    1 
ATOM   8043 C CG    . ASP B 1 501 ? 25.189 -32.998 -53.688 1.00 28.23  ? 501 ASP B CG    1 
ATOM   8044 O OD1   . ASP B 1 501 ? 24.326 -33.470 -54.481 1.00 30.37  ? 501 ASP B OD1   1 
ATOM   8045 O OD2   . ASP B 1 501 ? 26.229 -32.426 -54.071 1.00 29.70  ? 501 ASP B OD2   1 
ATOM   8046 N N     . PRO B 1 502 ? 23.165 -36.390 -51.888 1.00 26.26  ? 502 PRO B N     1 
ATOM   8047 C CA    . PRO B 1 502 ? 23.444 -37.809 -52.134 1.00 27.12  ? 502 PRO B CA    1 
ATOM   8048 C C     . PRO B 1 502 ? 23.922 -38.138 -53.551 1.00 27.12  ? 502 PRO B C     1 
ATOM   8049 O O     . PRO B 1 502 ? 24.786 -38.990 -53.719 1.00 27.85  ? 502 PRO B O     1 
ATOM   8050 C CB    . PRO B 1 502 ? 22.134 -38.511 -51.776 1.00 27.11  ? 502 PRO B CB    1 
ATOM   8051 C CG    . PRO B 1 502 ? 21.084 -37.418 -51.769 1.00 27.91  ? 502 PRO B CG    1 
ATOM   8052 C CD    . PRO B 1 502 ? 21.799 -36.128 -51.423 1.00 26.45  ? 502 PRO B CD    1 
ATOM   8053 N N     . ASN B 1 503 ? 23.474 -37.372 -54.554 1.00 27.77  ? 503 ASN B N     1 
ATOM   8054 C CA    . ASN B 1 503 ? 23.865 -37.604 -55.937 1.00 26.19  ? 503 ASN B CA    1 
ATOM   8055 C C     . ASN B 1 503 ? 25.149 -36.888 -56.353 1.00 27.29  ? 503 ASN B C     1 
ATOM   8056 O O     . ASN B 1 503 ? 25.543 -37.002 -57.515 1.00 25.11  ? 503 ASN B O     1 
ATOM   8057 C CB    . ASN B 1 503 ? 22.760 -37.170 -56.896 1.00 27.09  ? 503 ASN B CB    1 
ATOM   8058 C CG    . ASN B 1 503 ? 21.511 -37.998 -56.704 1.00 27.60  ? 503 ASN B CG    1 
ATOM   8059 O OD1   . ASN B 1 503 ? 21.595 -39.211 -56.542 1.00 28.09  ? 503 ASN B OD1   1 
ATOM   8060 N ND2   . ASN B 1 503 ? 20.366 -37.343 -56.661 1.00 26.71  ? 503 ASN B ND2   1 
ATOM   8061 N N     . GLY B 1 504 ? 25.721 -36.057 -55.467 1.00 27.84  ? 504 GLY B N     1 
ATOM   8062 C CA    . GLY B 1 504 ? 26.993 -35.397 -55.724 1.00 26.40  ? 504 GLY B CA    1 
ATOM   8063 C C     . GLY B 1 504 ? 26.932 -34.369 -56.854 1.00 27.79  ? 504 GLY B C     1 
ATOM   8064 O O     . GLY B 1 504 ? 27.882 -34.236 -57.628 1.00 24.59  ? 504 GLY B O     1 
ATOM   8065 N N     . ILE B 1 505 ? 25.830 -33.624 -56.962 1.00 28.62  ? 505 ILE B N     1 
ATOM   8066 C CA    . ILE B 1 505 ? 25.697 -32.770 -58.138 1.00 29.94  ? 505 ILE B CA    1 
ATOM   8067 C C     . ILE B 1 505 ? 26.127 -31.321 -57.873 1.00 28.98  ? 505 ILE B C     1 
ATOM   8068 O O     . ILE B 1 505 ? 26.117 -30.544 -58.827 1.00 26.27  ? 505 ILE B O     1 
ATOM   8069 C CB    . ILE B 1 505 ? 24.312 -32.880 -58.827 1.00 32.04  ? 505 ILE B CB    1 
ATOM   8070 C CG1   . ILE B 1 505 ? 23.124 -32.723 -57.884 1.00 33.56  ? 505 ILE B CG1   1 
ATOM   8071 C CG2   . ILE B 1 505 ? 24.223 -34.194 -59.600 1.00 34.84  ? 505 ILE B CG2   1 
ATOM   8072 C CD1   . ILE B 1 505 ? 23.020 -31.353 -57.260 1.00 37.55  ? 505 ILE B CD1   1 
ATOM   8073 N N     . LEU B 1 506 ? 26.583 -30.947 -56.650 1.00 29.82  ? 506 LEU B N     1 
ATOM   8074 C CA    . LEU B 1 506 ? 27.162 -29.610 -56.474 1.00 27.05  ? 506 LEU B CA    1 
ATOM   8075 C C     . LEU B 1 506 ? 28.688 -29.676 -56.344 1.00 25.12  ? 506 LEU B C     1 
ATOM   8076 O O     . LEU B 1 506 ? 29.205 -30.263 -55.401 1.00 24.01  ? 506 LEU B O     1 
ATOM   8077 C CB    . LEU B 1 506 ? 26.597 -28.917 -55.235 1.00 26.69  ? 506 LEU B CB    1 
ATOM   8078 C CG    . LEU B 1 506 ? 25.104 -28.610 -55.194 1.00 27.80  ? 506 LEU B CG    1 
ATOM   8079 C CD1   . LEU B 1 506 ? 24.826 -27.688 -54.010 1.00 29.39  ? 506 LEU B CD1   1 
ATOM   8080 C CD2   . LEU B 1 506 ? 24.598 -27.994 -56.485 1.00 26.51  ? 506 LEU B CD2   1 
ATOM   8081 N N     . ALA B 1 507 ? 29.384 -29.019 -57.284 1.00 24.97  ? 507 ALA B N     1 
ATOM   8082 C CA    . ALA B 1 507 ? 30.814 -28.714 -57.247 1.00 24.39  ? 507 ALA B CA    1 
ATOM   8083 C C     . ALA B 1 507 ? 31.661 -29.855 -56.666 1.00 24.87  ? 507 ALA B C     1 
ATOM   8084 O O     . ALA B 1 507 ? 32.331 -29.720 -55.639 1.00 24.40  ? 507 ALA B O     1 
ATOM   8085 C CB    . ALA B 1 507 ? 31.016 -27.416 -56.518 1.00 21.40  ? 507 ALA B CB    1 
ATOM   8086 N N     . PRO B 1 508 ? 31.690 -31.019 -57.342 1.00 25.30  ? 508 PRO B N     1 
ATOM   8087 C CA    . PRO B 1 508 ? 32.610 -32.097 -56.981 1.00 24.38  ? 508 PRO B CA    1 
ATOM   8088 C C     . PRO B 1 508 ? 34.044 -31.597 -56.936 1.00 22.58  ? 508 PRO B C     1 
ATOM   8089 O O     . PRO B 1 508 ? 34.510 -31.006 -57.907 1.00 21.76  ? 508 PRO B O     1 
ATOM   8090 C CB    . PRO B 1 508 ? 32.477 -33.120 -58.127 1.00 26.28  ? 508 PRO B CB    1 
ATOM   8091 C CG    . PRO B 1 508 ? 31.159 -32.800 -58.799 1.00 26.49  ? 508 PRO B CG    1 
ATOM   8092 C CD    . PRO B 1 508 ? 30.856 -31.342 -58.509 1.00 25.82  ? 508 PRO B CD    1 
ATOM   8093 N N     . GLY B 1 509 ? 34.701 -31.796 -55.785 1.00 23.76  ? 509 GLY B N     1 
ATOM   8094 C CA    . GLY B 1 509 ? 36.104 -31.461 -55.585 1.00 22.09  ? 509 GLY B CA    1 
ATOM   8095 C C     . GLY B 1 509 ? 36.338 -30.123 -54.875 1.00 22.55  ? 509 GLY B C     1 
ATOM   8096 O O     . GLY B 1 509 ? 37.459 -29.845 -54.460 1.00 24.24  ? 509 GLY B O     1 
ATOM   8097 N N     . LYS B 1 510 ? 35.301 -29.292 -54.725 1.00 22.62  ? 510 LYS B N     1 
ATOM   8098 C CA    . LYS B 1 510 ? 35.432 -28.021 -54.020 1.00 22.11  ? 510 LYS B CA    1 
ATOM   8099 C C     . LYS B 1 510 ? 35.913 -28.259 -52.581 1.00 20.78  ? 510 LYS B C     1 
ATOM   8100 O O     . LYS B 1 510 ? 35.405 -29.134 -51.890 1.00 19.28  ? 510 LYS B O     1 
ATOM   8101 C CB    . LYS B 1 510 ? 34.107 -27.252 -54.061 1.00 21.90  ? 510 LYS B CB    1 
ATOM   8102 C CG    . LYS B 1 510 ? 34.032 -25.970 -53.234 1.00 22.34  ? 510 LYS B CG    1 
ATOM   8103 C CD    . LYS B 1 510 ? 34.896 -24.854 -53.753 1.00 22.63  ? 510 LYS B CD    1 
ATOM   8104 C CE    . LYS B 1 510 ? 35.042 -23.695 -52.785 1.00 22.16  ? 510 LYS B CE    1 
ATOM   8105 N NZ    . LYS B 1 510 ? 36.100 -22.760 -53.242 1.00 21.11  ? 510 LYS B NZ    1 
ATOM   8106 N N     . SER B 1 511 ? 36.941 -27.507 -52.159 1.00 18.99  ? 511 SER B N     1 
ATOM   8107 C CA    . SER B 1 511 ? 37.548 -27.694 -50.854 1.00 19.48  ? 511 SER B CA    1 
ATOM   8108 C C     . SER B 1 511 ? 37.967 -29.156 -50.631 1.00 22.20  ? 511 SER B C     1 
ATOM   8109 O O     . SER B 1 511 ? 38.095 -29.623 -49.503 1.00 21.58  ? 511 SER B O     1 
ATOM   8110 C CB    . SER B 1 511 ? 36.603 -27.185 -49.769 1.00 20.62  ? 511 SER B CB    1 
ATOM   8111 O OG    . SER B 1 511 ? 36.388 -25.770 -49.872 1.00 20.03  ? 511 SER B OG    1 
ATOM   8112 N N     . GLY B 1 512 ? 38.191 -29.911 -51.714 1.00 24.40  ? 512 GLY B N     1 
ATOM   8113 C CA    . GLY B 1 512 ? 38.552 -31.315 -51.599 1.00 24.55  ? 512 GLY B CA    1 
ATOM   8114 C C     . GLY B 1 512 ? 37.435 -32.221 -51.070 1.00 23.72  ? 512 GLY B C     1 
ATOM   8115 O O     . GLY B 1 512 ? 37.713 -33.306 -50.576 1.00 25.63  ? 512 GLY B O     1 
ATOM   8116 N N     . ILE B 1 513 ? 36.178 -31.803 -51.217 1.00 23.98  ? 513 ILE B N     1 
ATOM   8117 C CA    . ILE B 1 513 ? 35.032 -32.614 -50.821 1.00 23.68  ? 513 ILE B CA    1 
ATOM   8118 C C     . ILE B 1 513 ? 34.408 -33.209 -52.075 1.00 24.21  ? 513 ILE B C     1 
ATOM   8119 O O     . ILE B 1 513 ? 34.025 -32.443 -52.954 1.00 26.44  ? 513 ILE B O     1 
ATOM   8120 C CB    . ILE B 1 513 ? 34.025 -31.733 -50.049 1.00 21.71  ? 513 ILE B CB    1 
ATOM   8121 C CG1   . ILE B 1 513 ? 34.670 -31.129 -48.798 1.00 22.00  ? 513 ILE B CG1   1 
ATOM   8122 C CG2   . ILE B 1 513 ? 32.778 -32.512 -49.699 1.00 21.26  ? 513 ILE B CG2   1 
ATOM   8123 C CD1   . ILE B 1 513 ? 33.804 -30.120 -48.079 1.00 22.97  ? 513 ILE B CD1   1 
ATOM   8124 N N     . TRP B 1 514 ? 34.236 -34.539 -52.135 1.00 26.18  ? 514 TRP B N     1 
ATOM   8125 C CA    . TRP B 1 514 ? 33.846 -35.175 -53.397 1.00 28.05  ? 514 TRP B CA    1 
ATOM   8126 C C     . TRP B 1 514 ? 32.450 -35.811 -53.410 1.00 29.57  ? 514 TRP B C     1 
ATOM   8127 O O     . TRP B 1 514 ? 31.788 -35.784 -54.463 1.00 35.55  ? 514 TRP B O     1 
ATOM   8128 C CB    . TRP B 1 514 ? 34.912 -36.183 -53.835 1.00 25.18  ? 514 TRP B CB    1 
ATOM   8129 C CG    . TRP B 1 514 ? 36.120 -35.498 -54.375 1.00 23.60  ? 514 TRP B CG    1 
ATOM   8130 C CD1   . TRP B 1 514 ? 37.190 -35.034 -53.670 1.00 22.75  ? 514 TRP B CD1   1 
ATOM   8131 C CD2   . TRP B 1 514 ? 36.328 -35.105 -55.740 1.00 22.50  ? 514 TRP B CD2   1 
ATOM   8132 N NE1   . TRP B 1 514 ? 38.081 -34.430 -54.520 1.00 23.16  ? 514 TRP B NE1   1 
ATOM   8133 C CE2   . TRP B 1 514 ? 37.573 -34.453 -55.797 1.00 22.38  ? 514 TRP B CE2   1 
ATOM   8134 C CE3   . TRP B 1 514 ? 35.594 -35.249 -56.917 1.00 24.97  ? 514 TRP B CE3   1 
ATOM   8135 C CZ2   . TRP B 1 514 ? 38.089 -33.932 -56.985 1.00 23.30  ? 514 TRP B CZ2   1 
ATOM   8136 C CZ3   . TRP B 1 514 ? 36.115 -34.754 -58.096 1.00 26.13  ? 514 TRP B CZ3   1 
ATOM   8137 C CH2   . TRP B 1 514 ? 37.346 -34.101 -58.128 1.00 23.31  ? 514 TRP B CH2   1 
ATOM   8138 N N     . GLY B 1 515 ? 32.043 -36.458 -52.315 1.00 28.24  ? 515 GLY B N     1 
ATOM   8139 C CA    . GLY B 1 515 ? 30.777 -37.189 -52.308 1.00 30.36  ? 515 GLY B CA    1 
ATOM   8140 C C     . GLY B 1 515 ? 30.941 -38.670 -52.674 1.00 28.92  ? 515 GLY B C     1 
ATOM   8141 O O     . GLY B 1 515 ? 31.834 -39.027 -53.422 1.00 27.38  ? 515 GLY B O     1 
ATOM   8142 N N     . LYS B 1 516 ? 30.044 -39.523 -52.179 1.00 31.71  ? 516 LYS B N     1 
ATOM   8143 C CA    . LYS B 1 516 ? 30.265 -40.960 -52.201 1.00 36.75  ? 516 LYS B CA    1 
ATOM   8144 C C     . LYS B 1 516 ? 30.416 -41.487 -53.624 1.00 36.53  ? 516 LYS B C     1 
ATOM   8145 O O     . LYS B 1 516 ? 31.166 -42.435 -53.834 1.00 34.63  ? 516 LYS B O     1 
ATOM   8146 C CB    . LYS B 1 516 ? 29.162 -41.747 -51.489 1.00 41.85  ? 516 LYS B CB    1 
ATOM   8147 C CG    . LYS B 1 516 ? 27.721 -41.516 -51.941 1.00 50.31  ? 516 LYS B CG    1 
ATOM   8148 C CD    . LYS B 1 516 ? 26.761 -42.529 -51.304 1.00 55.38  ? 516 LYS B CD    1 
ATOM   8149 C CE    . LYS B 1 516 ? 25.427 -41.958 -50.860 1.00 58.81  ? 516 LYS B CE    1 
ATOM   8150 N NZ    . LYS B 1 516 ? 24.549 -41.660 -52.010 1.00 61.98  ? 516 LYS B NZ    1 
ATOM   8151 N N     . ASN B 1 517 ? 29.734 -40.887 -54.604 1.00 34.58  ? 517 ASN B N     1 
ATOM   8152 C CA    . ASN B 1 517 ? 29.784 -41.440 -55.947 1.00 36.47  ? 517 ASN B CA    1 
ATOM   8153 C C     . ASN B 1 517 ? 31.159 -41.271 -56.581 1.00 39.97  ? 517 ASN B C     1 
ATOM   8154 O O     . ASN B 1 517 ? 31.471 -42.032 -57.490 1.00 41.30  ? 517 ASN B O     1 
ATOM   8155 C CB    . ASN B 1 517 ? 28.733 -40.839 -56.879 1.00 36.52  ? 517 ASN B CB    1 
ATOM   8156 C CG    . ASN B 1 517 ? 27.345 -41.285 -56.503 1.00 35.56  ? 517 ASN B CG    1 
ATOM   8157 O OD1   . ASN B 1 517 ? 27.174 -42.328 -55.883 1.00 41.37  ? 517 ASN B OD1   1 
ATOM   8158 N ND2   . ASN B 1 517 ? 26.354 -40.489 -56.839 1.00 37.90  ? 517 ASN B ND2   1 
ATOM   8159 N N     . ARG B 1 518 ? 31.944 -40.266 -56.152 1.00 41.02  ? 518 ARG B N     1 
ATOM   8160 C CA    . ARG B 1 518 ? 33.191 -39.962 -56.833 1.00 38.76  ? 518 ARG B CA    1 
ATOM   8161 C C     . ARG B 1 518 ? 34.419 -40.286 -55.981 1.00 39.22  ? 518 ARG B C     1 
ATOM   8162 O O     . ARG B 1 518 ? 35.481 -40.519 -56.536 1.00 42.84  ? 518 ARG B O     1 
ATOM   8163 C CB    . ARG B 1 518 ? 33.174 -38.529 -57.368 1.00 36.53  ? 518 ARG B CB    1 
ATOM   8164 C CG    . ARG B 1 518 ? 32.229 -38.377 -58.549 1.00 38.17  ? 518 ARG B CG    1 
ATOM   8165 C CD    . ARG B 1 518 ? 32.191 -36.981 -59.117 1.00 39.53  ? 518 ARG B CD    1 
ATOM   8166 N NE    . ARG B 1 518 ? 31.102 -36.795 -60.064 1.00 41.99  ? 518 ARG B NE    1 
ATOM   8167 C CZ    . ARG B 1 518 ? 31.072 -37.263 -61.317 1.00 46.47  ? 518 ARG B CZ    1 
ATOM   8168 N NH1   . ARG B 1 518 ? 32.064 -37.988 -61.815 1.00 39.46  ? 518 ARG B NH1   1 
ATOM   8169 N NH2   . ARG B 1 518 ? 30.026 -36.994 -62.081 1.00 49.91  ? 518 ARG B NH2   1 
ATOM   8170 N N     . ARG B 1 519 ? 34.323 -40.351 -54.659 1.00 40.80  ? 519 ARG B N     1 
ATOM   8171 C CA    . ARG B 1 519 ? 35.497 -40.780 -53.907 1.00 47.43  ? 519 ARG B CA    1 
ATOM   8172 C C     . ARG B 1 519 ? 35.493 -42.312 -53.832 1.00 43.68  ? 519 ARG B C     1 
ATOM   8173 O O     . ARG B 1 519 ? 36.606 -42.831 -53.892 1.00 49.55  ? 519 ARG B O     1 
ATOM   8174 C CB    . ARG B 1 519 ? 35.612 -40.097 -52.531 1.00 44.74  ? 519 ARG B CB    1 
ATOM   8175 C CG    . ARG B 1 519 ? 34.352 -40.116 -51.685 1.00 42.50  ? 519 ARG B CG    1 
ATOM   8176 C CD    . ARG B 1 519 ? 34.571 -39.821 -50.207 1.00 41.84  ? 519 ARG B CD    1 
ATOM   8177 N NE    . ARG B 1 519 ? 33.645 -40.625 -49.395 1.00 37.06  ? 519 ARG B NE    1 
ATOM   8178 C CZ    . ARG B 1 519 ? 32.341 -40.409 -49.228 1.00 35.52  ? 519 ARG B CZ    1 
ATOM   8179 N NH1   . ARG B 1 519 ? 31.794 -39.241 -49.502 1.00 39.19  ? 519 ARG B NH1   1 
ATOM   8180 N NH2   . ARG B 1 519 ? 31.588 -41.348 -48.690 1.00 35.86  ? 519 ARG B NH2   1 
HETATM 8181 P PA    . FAD C 2 .   ? 26.012 -25.641 -19.541 1.00 32.16  ? 601 FAD A PA    1 
HETATM 8182 O O1A   . FAD C 2 .   ? 24.802 -25.795 -18.685 1.00 27.57  ? 601 FAD A O1A   1 
HETATM 8183 O O2A   . FAD C 2 .   ? 27.095 -26.625 -19.225 1.00 35.50  ? 601 FAD A O2A   1 
HETATM 8184 O O5B   . FAD C 2 .   ? 25.659 -25.701 -21.112 1.00 28.77  ? 601 FAD A O5B   1 
HETATM 8185 C C5B   . FAD C 2 .   ? 24.383 -25.239 -21.600 1.00 30.99  ? 601 FAD A C5B   1 
HETATM 8186 C C4B   . FAD C 2 .   ? 23.922 -26.141 -22.719 1.00 34.18  ? 601 FAD A C4B   1 
HETATM 8187 O O4B   . FAD C 2 .   ? 24.899 -26.136 -23.793 1.00 34.37  ? 601 FAD A O4B   1 
HETATM 8188 C C3B   . FAD C 2 .   ? 23.755 -27.622 -22.358 1.00 36.26  ? 601 FAD A C3B   1 
HETATM 8189 O O3B   . FAD C 2 .   ? 22.520 -27.877 -21.693 1.00 30.42  ? 601 FAD A O3B   1 
HETATM 8190 C C2B   . FAD C 2 .   ? 23.904 -28.282 -23.732 1.00 34.47  ? 601 FAD A C2B   1 
HETATM 8191 O O2B   . FAD C 2 .   ? 22.723 -28.262 -24.503 1.00 31.46  ? 601 FAD A O2B   1 
HETATM 8192 C C1B   . FAD C 2 .   ? 25.021 -27.432 -24.346 1.00 35.81  ? 601 FAD A C1B   1 
HETATM 8193 N N9A   . FAD C 2 .   ? 26.399 -27.879 -24.077 1.00 35.40  ? 601 FAD A N9A   1 
HETATM 8194 C C8A   . FAD C 2 .   ? 27.183 -27.487 -23.006 1.00 34.66  ? 601 FAD A C8A   1 
HETATM 8195 N N7A   . FAD C 2 .   ? 28.375 -28.028 -23.027 1.00 33.09  ? 601 FAD A N7A   1 
HETATM 8196 C C5A   . FAD C 2 .   ? 28.381 -28.791 -24.188 1.00 33.31  ? 601 FAD A C5A   1 
HETATM 8197 C C6A   . FAD C 2 .   ? 29.377 -29.584 -24.770 1.00 31.08  ? 601 FAD A C6A   1 
HETATM 8198 N N6A   . FAD C 2 .   ? 30.572 -29.731 -24.214 1.00 29.42  ? 601 FAD A N6A   1 
HETATM 8199 N N1A   . FAD C 2 .   ? 29.074 -30.234 -25.923 1.00 30.52  ? 601 FAD A N1A   1 
HETATM 8200 C C2A   . FAD C 2 .   ? 27.863 -30.039 -26.455 1.00 33.68  ? 601 FAD A C2A   1 
HETATM 8201 N N3A   . FAD C 2 .   ? 26.846 -29.310 -25.993 1.00 36.70  ? 601 FAD A N3A   1 
HETATM 8202 C C4A   . FAD C 2 .   ? 27.179 -28.696 -24.851 1.00 32.10  ? 601 FAD A C4A   1 
HETATM 8203 N N1    . FAD C 2 .   ? 23.583 -16.351 -19.370 1.00 33.71  ? 601 FAD A N1    1 
HETATM 8204 C C2    . FAD C 2 .   ? 24.277 -15.497 -20.114 1.00 34.20  ? 601 FAD A C2    1 
HETATM 8205 O O2    . FAD C 2 .   ? 24.710 -15.856 -21.213 1.00 29.73  ? 601 FAD A O2    1 
HETATM 8206 N N3    . FAD C 2 .   ? 24.570 -14.209 -19.673 1.00 40.05  ? 601 FAD A N3    1 
HETATM 8207 C C4    . FAD C 2 .   ? 24.144 -13.726 -18.443 1.00 40.21  ? 601 FAD A C4    1 
HETATM 8208 O O4    . FAD C 2 .   ? 24.414 -12.573 -18.084 1.00 30.20  ? 601 FAD A O4    1 
HETATM 8209 C C4X   . FAD C 2 .   ? 23.386 -14.626 -17.639 1.00 38.24  ? 601 FAD A C4X   1 
HETATM 8210 N N5    . FAD C 2 .   ? 22.975 -14.218 -16.464 1.00 30.95  ? 601 FAD A N5    1 
HETATM 8211 C C5X   . FAD C 2 .   ? 22.240 -15.102 -15.728 1.00 33.44  ? 601 FAD A C5X   1 
HETATM 8212 C C6    . FAD C 2 .   ? 21.764 -14.698 -14.467 1.00 36.56  ? 601 FAD A C6    1 
HETATM 8213 C C7    . FAD C 2 .   ? 20.999 -15.534 -13.675 1.00 34.45  ? 601 FAD A C7    1 
HETATM 8214 C C7M   . FAD C 2 .   ? 20.520 -15.077 -12.321 1.00 36.91  ? 601 FAD A C7M   1 
HETATM 8215 C C8    . FAD C 2 .   ? 20.664 -16.809 -14.144 1.00 32.18  ? 601 FAD A C8    1 
HETATM 8216 C C8M   . FAD C 2 .   ? 19.911 -17.779 -13.270 1.00 34.55  ? 601 FAD A C8M   1 
HETATM 8217 C C9    . FAD C 2 .   ? 21.138 -17.233 -15.361 1.00 33.11  ? 601 FAD A C9    1 
HETATM 8218 C C9A   . FAD C 2 .   ? 21.939 -16.410 -16.168 1.00 35.23  ? 601 FAD A C9A   1 
HETATM 8219 N N10   . FAD C 2 .   ? 22.427 -16.828 -17.401 1.00 35.98  ? 601 FAD A N10   1 
HETATM 8220 C C10   . FAD C 2 .   ? 23.147 -15.946 -18.194 1.00 37.55  ? 601 FAD A C10   1 
HETATM 8221 C "C1'" . FAD C 2 .   ? 22.074 -18.172 -17.904 1.00 35.32  ? 601 FAD A "C1'" 1 
HETATM 8222 C "C2'" . FAD C 2 .   ? 22.994 -19.265 -17.415 1.00 35.09  ? 601 FAD A "C2'" 1 
HETATM 8223 O "O2'" . FAD C 2 .   ? 22.898 -19.462 -16.010 1.00 33.55  ? 601 FAD A "O2'" 1 
HETATM 8224 C "C3'" . FAD C 2 .   ? 24.455 -18.996 -17.798 1.00 32.92  ? 601 FAD A "C3'" 1 
HETATM 8225 O "O3'" . FAD C 2 .   ? 24.529 -18.619 -19.182 1.00 27.18  ? 601 FAD A "O3'" 1 
HETATM 8226 C "C4'" . FAD C 2 .   ? 25.350 -20.203 -17.512 1.00 30.43  ? 601 FAD A "C4'" 1 
HETATM 8227 O "O4'" . FAD C 2 .   ? 26.684 -19.797 -17.764 1.00 30.44  ? 601 FAD A "O4'" 1 
HETATM 8228 C "C5'" . FAD C 2 .   ? 25.036 -21.419 -18.362 1.00 32.38  ? 601 FAD A "C5'" 1 
HETATM 8229 O "O5'" . FAD C 2 .   ? 25.417 -22.700 -17.738 1.00 31.44  ? 601 FAD A "O5'" 1 
HETATM 8230 P P     . FAD C 2 .   ? 26.871 -23.330 -18.029 1.00 32.96  ? 601 FAD A P     1 
HETATM 8231 O O1P   . FAD C 2 .   ? 27.841 -22.211 -18.263 1.00 25.65  ? 601 FAD A O1P   1 
HETATM 8232 O O2P   . FAD C 2 .   ? 27.160 -24.291 -16.918 1.00 29.06  ? 601 FAD A O2P   1 
HETATM 8233 O O3P   . FAD C 2 .   ? 26.602 -24.148 -19.385 1.00 31.39  ? 601 FAD A O3P   1 
HETATM 8234 C C1    . PEG D 3 .   ? 32.517 -38.590 -38.927 1.00 57.09  ? 602 PEG A C1    1 
HETATM 8235 O O1    . PEG D 3 .   ? 33.570 -39.447 -39.319 1.00 54.84  ? 602 PEG A O1    1 
HETATM 8236 C C2    . PEG D 3 .   ? 31.178 -39.013 -39.455 1.00 57.33  ? 602 PEG A C2    1 
HETATM 8237 O O2    . PEG D 3 .   ? 30.373 -39.501 -38.383 1.00 61.14  ? 602 PEG A O2    1 
HETATM 8238 C C3    . PEG D 3 .   ? 29.093 -39.960 -38.804 1.00 66.26  ? 602 PEG A C3    1 
HETATM 8239 C C4    . PEG D 3 .   ? 29.178 -41.346 -39.378 1.00 62.50  ? 602 PEG A C4    1 
HETATM 8240 O O4    . PEG D 3 .   ? 28.093 -42.138 -38.946 1.00 62.03  ? 602 PEG A O4    1 
HETATM 8241 C C1    . PEG E 3 .   ? 40.383 1.867   -31.152 1.00 52.10  ? 603 PEG A C1    1 
HETATM 8242 O O1    . PEG E 3 .   ? 40.625 0.886   -30.141 1.00 48.33  ? 603 PEG A O1    1 
HETATM 8243 C C2    . PEG E 3 .   ? 38.917 2.094   -31.430 1.00 53.98  ? 603 PEG A C2    1 
HETATM 8244 O O2    . PEG E 3 .   ? 38.418 3.186   -30.655 1.00 51.57  ? 603 PEG A O2    1 
HETATM 8245 C C3    . PEG E 3 .   ? 37.243 3.809   -31.185 1.00 48.48  ? 603 PEG A C3    1 
HETATM 8246 C C4    . PEG E 3 .   ? 36.042 2.910   -31.071 1.00 47.67  ? 603 PEG A C4    1 
HETATM 8247 O O4    . PEG E 3 .   ? 35.003 3.296   -31.947 1.00 45.89  ? 603 PEG A O4    1 
HETATM 8248 P PA    . FAD F 2 .   ? 32.988 -16.070 -57.339 1.00 25.61  ? 601 FAD B PA    1 
HETATM 8249 O O1A   . FAD F 2 .   ? 33.957 -16.445 -58.413 1.00 25.66  ? 601 FAD B O1A   1 
HETATM 8250 O O2A   . FAD F 2 .   ? 31.566 -15.853 -57.718 1.00 28.54  ? 601 FAD B O2A   1 
HETATM 8251 O O5B   . FAD F 2 .   ? 33.026 -17.127 -56.141 1.00 22.55  ? 601 FAD B O5B   1 
HETATM 8252 C C5B   . FAD F 2 .   ? 34.235 -17.799 -55.693 1.00 23.08  ? 601 FAD B C5B   1 
HETATM 8253 C C4B   . FAD F 2 .   ? 33.901 -19.236 -55.354 1.00 23.62  ? 601 FAD B C4B   1 
HETATM 8254 O O4B   . FAD F 2 .   ? 32.955 -19.286 -54.252 1.00 24.22  ? 601 FAD B O4B   1 
HETATM 8255 C C3B   . FAD F 2 .   ? 33.230 -20.067 -56.456 1.00 22.90  ? 601 FAD B C3B   1 
HETATM 8256 O O3B   . FAD F 2 .   ? 34.209 -20.634 -57.315 1.00 24.93  ? 601 FAD B O3B   1 
HETATM 8257 C C2B   . FAD F 2 .   ? 32.515 -21.123 -55.617 1.00 22.36  ? 601 FAD B C2B   1 
HETATM 8258 O O2B   . FAD F 2 .   ? 33.381 -22.077 -55.047 1.00 23.23  ? 601 FAD B O2B   1 
HETATM 8259 C C1B   . FAD F 2 .   ? 31.995 -20.298 -54.450 1.00 23.93  ? 601 FAD B C1B   1 
HETATM 8260 N N9A   . FAD F 2 .   ? 30.700 -19.648 -54.600 1.00 26.71  ? 601 FAD B N9A   1 
HETATM 8261 C C8A   . FAD F 2 .   ? 30.488 -18.395 -55.104 1.00 28.07  ? 601 FAD B C8A   1 
HETATM 8262 N N7A   . FAD F 2 .   ? 29.227 -18.046 -55.090 1.00 27.80  ? 601 FAD B N7A   1 
HETATM 8263 C C5A   . FAD F 2 .   ? 28.580 -19.126 -54.524 1.00 26.00  ? 601 FAD B C5A   1 
HETATM 8264 C C6A   . FAD F 2 .   ? 27.230 -19.342 -54.226 1.00 23.88  ? 601 FAD B C6A   1 
HETATM 8265 N N6A   . FAD F 2 .   ? 26.296 -18.436 -54.476 1.00 26.77  ? 601 FAD B N6A   1 
HETATM 8266 N N1A   . FAD F 2 .   ? 26.893 -20.534 -53.676 1.00 23.92  ? 601 FAD B N1A   1 
HETATM 8267 C C2A   . FAD F 2 .   ? 27.878 -21.412 -53.412 1.00 25.89  ? 601 FAD B C2A   1 
HETATM 8268 N N3A   . FAD F 2 .   ? 29.188 -21.317 -53.662 1.00 26.80  ? 601 FAD B N3A   1 
HETATM 8269 C C4A   . FAD F 2 .   ? 29.477 -20.129 -54.219 1.00 26.74  ? 601 FAD B C4A   1 
HETATM 8270 N N1    . FAD F 2 .   ? 40.513 -11.715 -53.312 1.00 21.90  ? 601 FAD B N1    1 
HETATM 8271 C C2    . FAD F 2 .   ? 40.280 -11.160 -52.116 1.00 24.30  ? 601 FAD B C2    1 
HETATM 8272 O O2    . FAD F 2 .   ? 39.501 -11.698 -51.298 1.00 26.85  ? 601 FAD B O2    1 
HETATM 8273 N N3    . FAD F 2 .   ? 40.865 -9.983  -51.747 1.00 23.99  ? 601 FAD B N3    1 
HETATM 8274 C C4    . FAD F 2 .   ? 41.709 -9.292  -52.583 1.00 24.88  ? 601 FAD B C4    1 
HETATM 8275 O O4    . FAD F 2 .   ? 42.196 -8.216  -52.235 1.00 25.50  ? 601 FAD B O4    1 
HETATM 8276 C C4X   . FAD F 2 .   ? 41.972 -9.843  -53.827 1.00 23.75  ? 601 FAD B C4X   1 
HETATM 8277 N N5    . FAD F 2 .   ? 42.788 -9.199  -54.609 1.00 24.17  ? 601 FAD B N5    1 
HETATM 8278 C C5X   . FAD F 2 .   ? 43.048 -9.745  -55.832 1.00 23.83  ? 601 FAD B C5X   1 
HETATM 8279 C C6    . FAD F 2 .   ? 43.917 -9.046  -56.689 1.00 24.72  ? 601 FAD B C6    1 
HETATM 8280 C C7    . FAD F 2 .   ? 44.276 -9.547  -57.917 1.00 24.54  ? 601 FAD B C7    1 
HETATM 8281 C C7M   . FAD F 2 .   ? 45.215 -8.764  -58.801 1.00 24.32  ? 601 FAD B C7M   1 
HETATM 8282 C C8    . FAD F 2 .   ? 43.724 -10.779 -58.336 1.00 25.09  ? 601 FAD B C8    1 
HETATM 8283 C C8M   . FAD F 2 .   ? 44.133 -11.405 -59.651 1.00 26.08  ? 601 FAD B C8M   1 
HETATM 8284 C C9    . FAD F 2 .   ? 42.879 -11.478 -57.495 1.00 23.29  ? 601 FAD B C9    1 
HETATM 8285 C C9A   . FAD F 2 .   ? 42.511 -10.985 -56.236 1.00 23.52  ? 601 FAD B C9A   1 
HETATM 8286 N N10   . FAD F 2 .   ? 41.606 -11.630 -55.383 1.00 21.98  ? 601 FAD B N10   1 
HETATM 8287 C C10   . FAD F 2 .   ? 41.323 -11.088 -54.139 1.00 22.37  ? 601 FAD B C10   1 
HETATM 8288 C "C1'" . FAD F 2 .   ? 41.046 -12.952 -55.730 1.00 21.47  ? 601 FAD B "C1'" 1 
HETATM 8289 C "C2'" . FAD F 2 .   ? 39.743 -12.894 -56.516 1.00 22.95  ? 601 FAD B "C2'" 1 
HETATM 8290 O "O2'" . FAD F 2 .   ? 39.989 -12.447 -57.842 1.00 22.04  ? 601 FAD B "O2'" 1 
HETATM 8291 C "C3'" . FAD F 2 .   ? 38.638 -12.065 -55.840 1.00 23.90  ? 601 FAD B "C3'" 1 
HETATM 8292 O "O3'" . FAD F 2 .   ? 38.434 -12.550 -54.522 1.00 22.59  ? 601 FAD B "O3'" 1 
HETATM 8293 C "C4'" . FAD F 2 .   ? 37.291 -12.120 -56.567 1.00 26.00  ? 601 FAD B "C4'" 1 
HETATM 8294 O "O4'" . FAD F 2 .   ? 36.453 -11.058 -56.110 1.00 24.68  ? 601 FAD B "O4'" 1 
HETATM 8295 C "C5'" . FAD F 2 .   ? 36.574 -13.447 -56.398 1.00 26.30  ? 601 FAD B "C5'" 1 
HETATM 8296 O "O5'" . FAD F 2 .   ? 35.640 -13.692 -57.500 1.00 22.90  ? 601 FAD B "O5'" 1 
HETATM 8297 P P     . FAD F 2 .   ? 34.080 -13.390 -57.292 1.00 26.42  ? 601 FAD B P     1 
HETATM 8298 O O1P   . FAD F 2 .   ? 33.926 -12.280 -56.292 1.00 27.70  ? 601 FAD B O1P   1 
HETATM 8299 O O2P   . FAD F 2 .   ? 33.428 -13.258 -58.631 1.00 27.49  ? 601 FAD B O2P   1 
HETATM 8300 O O3P   . FAD F 2 .   ? 33.546 -14.741 -56.628 1.00 25.70  ? 601 FAD B O3P   1 
HETATM 8301 C C1    . PEG G 3 .   ? 34.213 -2.463  -36.151 1.00 53.10  ? 602 PEG B C1    1 
HETATM 8302 O O1    . PEG G 3 .   ? 34.308 -1.530  -35.089 1.00 58.98  ? 602 PEG B O1    1 
HETATM 8303 C C2    . PEG G 3 .   ? 35.284 -3.496  -36.098 1.00 53.02  ? 602 PEG B C2    1 
HETATM 8304 O O2    . PEG G 3 .   ? 34.843 -4.686  -36.747 1.00 56.80  ? 602 PEG B O2    1 
HETATM 8305 C C3    . PEG G 3 .   ? 35.635 -5.829  -36.415 1.00 66.25  ? 602 PEG B C3    1 
HETATM 8306 C C4    . PEG G 3 .   ? 34.779 -7.079  -36.365 1.00 69.60  ? 602 PEG B C4    1 
HETATM 8307 O O4    . PEG G 3 .   ? 34.360 -7.432  -35.045 1.00 64.08  ? 602 PEG B O4    1 
HETATM 8308 C C1    . GOL H 4 .   ? 44.385 -25.530 -71.191 1.00 57.05  ? 603 GOL B C1    1 
HETATM 8309 O O1    . GOL H 4 .   ? 43.733 -26.387 -70.258 1.00 47.93  ? 603 GOL B O1    1 
HETATM 8310 C C2    . GOL H 4 .   ? 43.420 -24.786 -72.095 1.00 56.44  ? 603 GOL B C2    1 
HETATM 8311 O O2    . GOL H 4 .   ? 43.090 -25.591 -73.220 1.00 60.64  ? 603 GOL B O2    1 
HETATM 8312 C C3    . GOL H 4 .   ? 42.140 -24.357 -71.416 1.00 54.11  ? 603 GOL B C3    1 
HETATM 8313 O O3    . GOL H 4 .   ? 41.586 -23.213 -72.058 1.00 51.49  ? 603 GOL B O3    1 
HETATM 8314 O O     . HOH I 5 .   ? 41.056 0.355   -27.879 1.00 47.87  ? 701 HOH A O     1 
HETATM 8315 O O     . HOH I 5 .   ? 41.189 -7.144  -28.755 1.00 25.66  ? 702 HOH A O     1 
HETATM 8316 O O     . HOH I 5 .   ? 23.174 -27.522 -18.922 1.00 27.62  ? 703 HOH A O     1 
HETATM 8317 O O     . HOH I 5 .   ? 38.445 -10.420 -16.238 1.00 27.86  ? 704 HOH A O     1 
HETATM 8318 O O     . HOH I 5 .   ? 35.350 -20.426 -34.674 1.00 22.33  ? 705 HOH A O     1 
HETATM 8319 O O     . HOH I 5 .   ? 11.808 12.313  -20.197 1.00 37.71  ? 706 HOH A O     1 
HETATM 8320 O O     . HOH I 5 .   ? 31.205 -9.624  -18.584 1.00 23.25  ? 707 HOH A O     1 
HETATM 8321 O O     . HOH I 5 .   ? 35.253 -25.092 -38.789 1.00 35.86  ? 708 HOH A O     1 
HETATM 8322 O O     . HOH I 5 .   ? 41.290 -22.638 -35.656 1.00 21.59  ? 709 HOH A O     1 
HETATM 8323 O O     . HOH I 5 .   ? 16.646 9.605   -14.166 1.00 27.70  ? 710 HOH A O     1 
HETATM 8324 O O     . HOH I 5 .   ? 10.252 6.650   -32.479 1.00 33.06  ? 711 HOH A O     1 
HETATM 8325 O O     . HOH I 5 .   ? 14.305 10.714  -18.143 1.00 31.38  ? 712 HOH A O     1 
HETATM 8326 O O     . HOH I 5 .   ? 34.000 -44.425 -32.323 1.00 30.95  ? 713 HOH A O     1 
HETATM 8327 O O     . HOH I 5 .   ? 36.615 -27.137 -42.562 1.00 19.10  ? 714 HOH A O     1 
HETATM 8328 O O     . HOH I 5 .   ? 33.215 -34.872 -15.415 1.00 35.57  ? 715 HOH A O     1 
HETATM 8329 O O     . HOH I 5 .   ? 24.376 -42.321 -33.543 1.00 22.49  ? 716 HOH A O     1 
HETATM 8330 O O     . HOH I 5 .   ? 18.880 8.316   -10.885 1.00 30.50  ? 717 HOH A O     1 
HETATM 8331 O O     . HOH I 5 .   ? 32.547 -18.869 -33.434 1.00 31.23  ? 718 HOH A O     1 
HETATM 8332 O O     . HOH I 5 .   ? 42.525 -13.826 -36.082 1.00 25.65  ? 719 HOH A O     1 
HETATM 8333 O O     . HOH I 5 .   ? 5.940  4.341   -1.648  1.00 25.79  ? 720 HOH A O     1 
HETATM 8334 O O     . HOH I 5 .   ? 5.839  -24.464 -37.338 1.00 29.97  ? 721 HOH A O     1 
HETATM 8335 O O     . HOH I 5 .   ? 40.406 -32.585 -37.296 1.00 22.42  ? 722 HOH A O     1 
HETATM 8336 O O     . HOH I 5 .   ? 8.409  -26.941 -26.107 1.00 28.16  ? 723 HOH A O     1 
HETATM 8337 O O     . HOH I 5 .   ? 19.809 -1.560  -6.758  1.00 38.78  ? 724 HOH A O     1 
HETATM 8338 O O     . HOH I 5 .   ? 41.094 -11.078 -15.959 1.00 39.19  ? 725 HOH A O     1 
HETATM 8339 O O     . HOH I 5 .   ? 20.338 -28.778 -12.686 1.00 27.30  ? 726 HOH A O     1 
HETATM 8340 O O     . HOH I 5 .   ? 10.847 0.406   -16.849 1.00 35.10  ? 727 HOH A O     1 
HETATM 8341 O O     . HOH I 5 .   ? 6.524  -17.857 -36.244 1.00 23.26  ? 728 HOH A O     1 
HETATM 8342 O O     . HOH I 5 .   ? 24.038 -30.709 -26.652 1.00 41.28  ? 729 HOH A O     1 
HETATM 8343 O O     . HOH I 5 .   ? 40.230 -43.932 -18.780 1.00 32.33  ? 730 HOH A O     1 
HETATM 8344 O O     . HOH I 5 .   ? 40.574 -46.817 -22.622 1.00 30.62  ? 731 HOH A O     1 
HETATM 8345 O O     . HOH I 5 .   ? 10.532 -25.347 -37.217 1.00 24.34  ? 732 HOH A O     1 
HETATM 8346 O O     . HOH I 5 .   ? 20.379 -15.277 -20.321 1.00 36.75  ? 733 HOH A O     1 
HETATM 8347 O O     . HOH I 5 .   ? 31.166 3.487   7.064   1.00 35.70  ? 734 HOH A O     1 
HETATM 8348 O O     . HOH I 5 .   ? 37.041 -40.990 -14.733 1.00 40.26  ? 735 HOH A O     1 
HETATM 8349 O O     . HOH I 5 .   ? 12.284 -22.479 -41.881 1.00 17.81  ? 736 HOH A O     1 
HETATM 8350 O O     . HOH I 5 .   ? 47.518 -9.245  -24.775 1.00 36.04  ? 737 HOH A O     1 
HETATM 8351 O O     . HOH I 5 .   ? 37.153 -22.197 -35.184 1.00 23.20  ? 738 HOH A O     1 
HETATM 8352 O O     . HOH I 5 .   ? 10.553 8.474   -25.377 1.00 34.77  ? 739 HOH A O     1 
HETATM 8353 O O     . HOH I 5 .   ? 18.214 -24.975 -27.592 1.00 28.10  ? 740 HOH A O     1 
HETATM 8354 O O     . HOH I 5 .   ? 16.700 -35.085 -23.927 1.00 29.39  ? 741 HOH A O     1 
HETATM 8355 O O     . HOH I 5 .   ? 33.958 -13.852 -24.590 1.00 23.45  ? 742 HOH A O     1 
HETATM 8356 O O     . HOH I 5 .   ? 6.318  -4.540  -12.116 1.00 36.28  ? 743 HOH A O     1 
HETATM 8357 O O     . HOH I 5 .   ? 7.661  -10.197 -0.597  1.00 35.53  ? 744 HOH A O     1 
HETATM 8358 O O     . HOH I 5 .   ? 36.601 -13.484 -23.828 1.00 28.21  ? 745 HOH A O     1 
HETATM 8359 O O     . HOH I 5 .   ? 36.685 -9.077  -21.573 1.00 23.43  ? 746 HOH A O     1 
HETATM 8360 O O     . HOH I 5 .   ? 10.977 -28.822 -25.637 1.00 34.43  ? 747 HOH A O     1 
HETATM 8361 O O     . HOH I 5 .   ? 5.235  7.887   -4.321  1.00 34.51  ? 748 HOH A O     1 
HETATM 8362 O O     . HOH I 5 .   ? 37.778 -11.290 -22.939 1.00 19.39  ? 749 HOH A O     1 
HETATM 8363 O O     . HOH I 5 .   ? 18.773 8.503   -33.674 1.00 30.38  ? 750 HOH A O     1 
HETATM 8364 O O     . HOH I 5 .   ? 40.488 -26.536 -41.425 1.00 25.03  ? 751 HOH A O     1 
HETATM 8365 O O     . HOH I 5 .   ? 17.243 9.940   -6.982  1.00 38.87  ? 752 HOH A O     1 
HETATM 8366 O O     . HOH I 5 .   ? 27.434 -15.993 -27.941 1.00 19.79  ? 753 HOH A O     1 
HETATM 8367 O O     . HOH I 5 .   ? 17.241 -41.331 -34.496 1.00 40.07  ? 754 HOH A O     1 
HETATM 8368 O O     . HOH I 5 .   ? 9.878  -27.445 -46.600 1.00 32.28  ? 755 HOH A O     1 
HETATM 8369 O O     . HOH I 5 .   ? 39.458 -32.374 -23.344 1.00 23.93  ? 756 HOH A O     1 
HETATM 8370 O O     . HOH I 5 .   ? 32.180 -54.347 -20.298 1.00 33.77  ? 757 HOH A O     1 
HETATM 8371 O O     . HOH I 5 .   ? 28.158 -42.677 -7.324  1.00 49.72  ? 758 HOH A O     1 
HETATM 8372 O O     . HOH I 5 .   ? 45.797 -30.364 -33.449 1.00 26.52  ? 759 HOH A O     1 
HETATM 8373 O O     . HOH I 5 .   ? 22.879 9.018   -30.718 1.00 28.24  ? 760 HOH A O     1 
HETATM 8374 O O     . HOH I 5 .   ? 32.728 13.119  -29.665 1.00 38.92  ? 761 HOH A O     1 
HETATM 8375 O O     . HOH I 5 .   ? 6.584  -9.548  -7.065  1.00 42.77  ? 762 HOH A O     1 
HETATM 8376 O O     . HOH I 5 .   ? 14.274 -31.972 -13.679 1.00 36.19  ? 763 HOH A O     1 
HETATM 8377 O O     . HOH I 5 .   ? 20.235 -26.995 -23.118 1.00 32.34  ? 764 HOH A O     1 
HETATM 8378 O O     . HOH I 5 .   ? 25.637 -27.193 -28.270 1.00 32.10  ? 765 HOH A O     1 
HETATM 8379 O O     . HOH I 5 .   ? 23.976 7.962   -5.963  1.00 34.10  ? 766 HOH A O     1 
HETATM 8380 O O     . HOH I 5 .   ? 25.913 -3.727  -18.012 1.00 44.77  ? 767 HOH A O     1 
HETATM 8381 O O     . HOH I 5 .   ? 37.160 -49.581 -14.570 1.00 40.60  ? 768 HOH A O     1 
HETATM 8382 O O     . HOH I 5 .   ? 2.953  -10.212 -24.834 1.00 38.36  ? 769 HOH A O     1 
HETATM 8383 O O     . HOH I 5 .   ? 40.959 -35.199 -22.319 1.00 35.09  ? 770 HOH A O     1 
HETATM 8384 O O     . HOH I 5 .   ? 19.863 5.793   -37.165 1.00 30.37  ? 771 HOH A O     1 
HETATM 8385 O O     . HOH I 5 .   ? 50.216 -19.921 -30.665 1.00 35.11  ? 772 HOH A O     1 
HETATM 8386 O O     . HOH I 5 .   ? 31.893 -9.675  -28.799 1.00 26.56  ? 773 HOH A O     1 
HETATM 8387 O O     . HOH I 5 .   ? 21.546 16.626  -18.974 1.00 34.85  ? 774 HOH A O     1 
HETATM 8388 O O     . HOH I 5 .   ? 6.958  6.274   -15.903 1.00 34.44  ? 775 HOH A O     1 
HETATM 8389 O O     . HOH I 5 .   ? 9.872  -9.193  -0.390  1.00 30.91  ? 776 HOH A O     1 
HETATM 8390 O O     . HOH I 5 .   ? 11.101 -40.534 -22.734 1.00 40.86  ? 777 HOH A O     1 
HETATM 8391 O O     . HOH I 5 .   ? 28.645 12.604  -13.549 1.00 46.08  ? 778 HOH A O     1 
HETATM 8392 O O     . HOH I 5 .   ? 30.307 14.325  -18.243 1.00 32.83  ? 779 HOH A O     1 
HETATM 8393 O O     . HOH I 5 .   ? 37.272 -35.155 -9.797  1.00 38.63  ? 780 HOH A O     1 
HETATM 8394 O O     . HOH I 5 .   ? 8.709  -15.419 -48.217 1.00 38.14  ? 781 HOH A O     1 
HETATM 8395 O O     . HOH I 5 .   ? 39.978 -15.610 -37.296 1.00 25.98  ? 782 HOH A O     1 
HETATM 8396 O O     . HOH I 5 .   ? 4.604  -20.213 -37.325 1.00 38.92  ? 783 HOH A O     1 
HETATM 8397 O O     . HOH I 5 .   ? 40.818 4.323   -16.292 1.00 33.95  ? 784 HOH A O     1 
HETATM 8398 O O     . HOH I 5 .   ? 25.346 -33.047 -27.886 1.00 36.13  ? 785 HOH A O     1 
HETATM 8399 O O     . HOH I 5 .   ? 22.988 14.112  -14.249 1.00 30.53  ? 786 HOH A O     1 
HETATM 8400 O O     . HOH I 5 .   ? 37.604 -5.638  -9.040  1.00 43.24  ? 787 HOH A O     1 
HETATM 8401 O O     . HOH I 5 .   ? 26.649 -30.066 -30.622 1.00 31.58  ? 788 HOH A O     1 
HETATM 8402 O O     . HOH I 5 .   ? 40.155 -41.629 -31.559 1.00 33.09  ? 789 HOH A O     1 
HETATM 8403 O O     . HOH I 5 .   ? 29.754 -27.519 -9.054  1.00 37.40  ? 790 HOH A O     1 
HETATM 8404 O O     . HOH I 5 .   ? 8.915  -31.775 -47.211 1.00 35.93  ? 791 HOH A O     1 
HETATM 8405 O O     . HOH I 5 .   ? 30.030 -12.969 -5.522  1.00 30.73  ? 792 HOH A O     1 
HETATM 8406 O O     . HOH I 5 .   ? 32.039 1.709   -37.279 1.00 37.05  ? 793 HOH A O     1 
HETATM 8407 O O     . HOH I 5 .   ? 44.554 -26.329 -15.220 1.00 30.45  ? 794 HOH A O     1 
HETATM 8408 O O     . HOH I 5 .   ? 7.032  -5.618  -35.802 1.00 38.91  ? 795 HOH A O     1 
HETATM 8409 O O     . HOH I 5 .   ? 33.597 -15.698 -22.449 1.00 24.38  ? 796 HOH A O     1 
HETATM 8410 O O     . HOH I 5 .   ? 36.031 -14.962 -21.600 1.00 21.32  ? 797 HOH A O     1 
HETATM 8411 O O     . HOH I 5 .   ? 43.728 0.493   -24.655 1.00 21.84  ? 798 HOH A O     1 
HETATM 8412 O O     . HOH I 5 .   ? 5.264  -21.921 -44.422 1.00 33.44  ? 799 HOH A O     1 
HETATM 8413 O O     . HOH I 5 .   ? 37.291 -14.707 -7.774  1.00 36.57  ? 800 HOH A O     1 
HETATM 8414 O O     . HOH I 5 .   ? 29.314 -5.928  -28.081 1.00 28.83  ? 801 HOH A O     1 
HETATM 8415 O O     . HOH I 5 .   ? 47.057 -21.290 -31.485 1.00 31.17  ? 802 HOH A O     1 
HETATM 8416 O O     . HOH I 5 .   ? 9.168  -30.837 -25.687 1.00 38.13  ? 803 HOH A O     1 
HETATM 8417 O O     . HOH I 5 .   ? 20.155 -10.529 -16.024 1.00 40.33  ? 804 HOH A O     1 
HETATM 8418 O O     . HOH I 5 .   ? 6.996  7.726   -26.339 1.00 46.68  ? 805 HOH A O     1 
HETATM 8419 O O     . HOH I 5 .   ? 42.344 -35.875 -28.251 1.00 40.13  ? 806 HOH A O     1 
HETATM 8420 O O     . HOH I 5 .   ? 25.246 -7.585  -23.552 1.00 33.21  ? 807 HOH A O     1 
HETATM 8421 O O     . HOH I 5 .   ? 43.417 -7.886  -15.200 1.00 36.90  ? 808 HOH A O     1 
HETATM 8422 O O     . HOH I 5 .   ? 10.756 -40.011 -28.030 1.00 42.99  ? 809 HOH A O     1 
HETATM 8423 O O     . HOH I 5 .   ? 23.862 -14.137 -28.696 1.00 39.07  ? 810 HOH A O     1 
HETATM 8424 O O     . HOH I 5 .   ? 9.509  -15.380 -5.910  1.00 37.81  ? 811 HOH A O     1 
HETATM 8425 O O     . HOH I 5 .   ? 42.951 -0.101  -16.809 1.00 42.89  ? 812 HOH A O     1 
HETATM 8426 O O     . HOH I 5 .   ? 17.869 -31.703 -46.733 1.00 32.86  ? 813 HOH A O     1 
HETATM 8427 O O     . HOH I 5 .   ? 33.992 -15.469 -38.466 1.00 36.58  ? 814 HOH A O     1 
HETATM 8428 O O     . HOH I 5 .   ? 25.638 -29.529 -11.885 1.00 35.48  ? 815 HOH A O     1 
HETATM 8429 O O     . HOH I 5 .   ? 51.066 -22.845 -28.819 1.00 44.83  ? 816 HOH A O     1 
HETATM 8430 O O     . HOH I 5 .   ? 19.520 -15.245 -18.103 1.00 33.64  ? 817 HOH A O     1 
HETATM 8431 O O     . HOH I 5 .   ? 6.725  -1.633  -12.777 1.00 39.17  ? 818 HOH A O     1 
HETATM 8432 O O     . HOH I 5 .   ? 4.816  -25.856 -23.885 1.00 41.03  ? 819 HOH A O     1 
HETATM 8433 O O     . HOH I 5 .   ? 10.099 -29.278 -33.542 1.00 35.61  ? 820 HOH A O     1 
HETATM 8434 O O     . HOH I 5 .   ? 7.990  -20.242 -49.635 1.00 39.04  ? 821 HOH A O     1 
HETATM 8435 O O     . HOH I 5 .   ? 46.683 -29.287 -28.203 1.00 36.74  ? 822 HOH A O     1 
HETATM 8436 O O     . HOH I 5 .   ? 13.859 15.304  -26.020 1.00 50.66  ? 823 HOH A O     1 
HETATM 8437 O O     . HOH I 5 .   ? 35.248 9.909   -18.240 1.00 37.34  ? 824 HOH A O     1 
HETATM 8438 O O     . HOH I 5 .   ? 16.382 -55.213 -15.360 1.00 45.00  ? 825 HOH A O     1 
HETATM 8439 O O     . HOH I 5 .   ? 29.206 -9.455  -32.450 1.00 35.14  ? 826 HOH A O     1 
HETATM 8440 O O     . HOH I 5 .   ? 48.351 -31.172 -33.571 1.00 23.57  ? 827 HOH A O     1 
HETATM 8441 O O     . HOH I 5 .   ? 11.752 -52.439 -24.030 1.00 41.92  ? 828 HOH A O     1 
HETATM 8442 O O     . HOH I 5 .   ? 52.816 -28.004 -32.371 1.00 43.72  ? 829 HOH A O     1 
HETATM 8443 O O     . HOH I 5 .   ? 8.924  -35.207 -32.789 1.00 40.88  ? 830 HOH A O     1 
HETATM 8444 O O     . HOH I 5 .   ? 31.719 -16.500 -36.844 1.00 39.87  ? 831 HOH A O     1 
HETATM 8445 O O     . HOH I 5 .   ? 16.237 -42.775 -11.166 1.00 46.68  ? 832 HOH A O     1 
HETATM 8446 O O     . HOH I 5 .   ? 28.221 -45.621 -33.955 1.00 41.81  ? 833 HOH A O     1 
HETATM 8447 O O     . HOH I 5 .   ? 38.831 9.186   -18.901 1.00 37.39  ? 834 HOH A O     1 
HETATM 8448 O O     . HOH I 5 .   ? 12.284 -30.386 -13.772 1.00 34.80  ? 835 HOH A O     1 
HETATM 8449 O O     . HOH I 5 .   ? 18.587 -8.875  -2.026  1.00 41.25  ? 836 HOH A O     1 
HETATM 8450 O O     . HOH I 5 .   ? 9.659  -20.834 -51.531 1.00 40.47  ? 837 HOH A O     1 
HETATM 8451 O O     . HOH I 5 .   ? 54.576 -31.532 -38.061 1.00 41.29  ? 838 HOH A O     1 
HETATM 8452 O O     . HOH I 5 .   ? 6.330  5.719   -12.207 1.00 49.69  ? 839 HOH A O     1 
HETATM 8453 O O     . HOH I 5 .   ? 30.398 -34.423 -9.991  1.00 42.33  ? 840 HOH A O     1 
HETATM 8454 O O     . HOH I 5 .   ? 35.954 -6.301  -30.383 1.00 32.81  ? 841 HOH A O     1 
HETATM 8455 O O     . HOH I 5 .   ? 42.360 -1.889  -15.666 1.00 50.85  ? 842 HOH A O     1 
HETATM 8456 O O     . HOH I 5 .   ? 31.773 -3.950  -31.942 1.00 40.72  ? 843 HOH A O     1 
HETATM 8457 O O     . HOH I 5 .   ? 27.877 8.510   -33.836 1.00 43.27  ? 844 HOH A O     1 
HETATM 8458 O O     . HOH I 5 .   ? 10.453 -30.536 -38.726 1.00 32.92  ? 845 HOH A O     1 
HETATM 8459 O O     . HOH I 5 .   ? 4.974  4.314   -13.362 1.00 56.28  ? 846 HOH A O     1 
HETATM 8460 O O     . HOH I 5 .   ? 9.999  -28.317 -35.654 1.00 36.50  ? 847 HOH A O     1 
HETATM 8461 O O     . HOH I 5 .   ? 32.444 -32.970 -9.680  1.00 40.09  ? 848 HOH A O     1 
HETATM 8462 O O     . HOH I 5 .   ? 32.223 9.956   -32.585 1.00 46.21  ? 849 HOH A O     1 
HETATM 8463 O O     . HOH J 5 .   ? 12.608 -30.410 -62.910 1.00 58.40  ? 701 HOH B O     1 
HETATM 8464 O O     . HOH J 5 .   ? 56.595 -17.073 -66.196 1.00 31.23  ? 702 HOH B O     1 
HETATM 8465 O O     . HOH J 5 .   ? 39.363 -20.418 -45.125 1.00 24.10  ? 703 HOH B O     1 
HETATM 8466 O O     . HOH J 5 .   ? 25.798 -15.279 -40.102 1.00 26.15  ? 704 HOH B O     1 
HETATM 8467 O O     . HOH J 5 .   ? 13.623 -32.778 -62.757 1.00 37.04  ? 705 HOH B O     1 
HETATM 8468 O O     . HOH J 5 .   ? 43.550 -10.504 -65.562 1.00 28.07  ? 706 HOH B O     1 
HETATM 8469 O O     . HOH J 5 .   ? 34.405 -18.925 -59.210 1.00 23.49  ? 707 HOH B O     1 
HETATM 8470 O O     . HOH J 5 .   ? 20.925 -18.143 -30.846 1.00 22.64  ? 708 HOH B O     1 
HETATM 8471 O O     . HOH J 5 .   ? 48.947 -22.593 -39.374 1.00 23.49  ? 709 HOH B O     1 
HETATM 8472 O O     . HOH J 5 .   ? 17.672 -14.420 -55.033 1.00 21.08  ? 710 HOH B O     1 
HETATM 8473 O O     . HOH J 5 .   ? 13.182 -29.861 -54.800 1.00 27.36  ? 711 HOH B O     1 
HETATM 8474 O O     . HOH J 5 .   ? 54.942 5.563   -58.343 1.00 30.71  ? 712 HOH B O     1 
HETATM 8475 O O     . HOH J 5 .   ? 44.748 -30.718 -55.603 1.00 23.95  ? 713 HOH B O     1 
HETATM 8476 O O     . HOH J 5 .   ? 40.930 -14.358 -48.857 1.00 38.89  ? 714 HOH B O     1 
HETATM 8477 O O     . HOH J 5 .   ? 60.605 4.948   -48.360 1.00 34.00  ? 715 HOH B O     1 
HETATM 8478 O O     . HOH J 5 .   ? 47.040 -3.819  -67.296 1.00 32.81  ? 716 HOH B O     1 
HETATM 8479 O O     . HOH J 5 .   ? 38.549 -2.517  -48.836 1.00 22.91  ? 717 HOH B O     1 
HETATM 8480 O O     . HOH J 5 .   ? 23.171 -15.569 -40.189 1.00 18.98  ? 718 HOH B O     1 
HETATM 8481 O O     . HOH J 5 .   ? 12.911 -10.840 -34.900 1.00 40.73  ? 719 HOH B O     1 
HETATM 8482 O O     . HOH J 5 .   ? 19.461 -22.738 -36.760 1.00 24.62  ? 720 HOH B O     1 
HETATM 8483 O O     . HOH J 5 .   ? 22.990 -15.558 -64.117 1.00 21.66  ? 721 HOH B O     1 
HETATM 8484 O O     . HOH J 5 .   ? 27.442 -37.197 -52.098 1.00 28.08  ? 722 HOH B O     1 
HETATM 8485 O O     . HOH J 5 .   ? 16.610 -16.766 -67.557 1.00 31.58  ? 723 HOH B O     1 
HETATM 8486 O O     . HOH J 5 .   ? 42.197 -2.143  -58.359 1.00 26.47  ? 724 HOH B O     1 
HETATM 8487 O O     . HOH J 5 .   ? 46.900 -21.371 -52.153 1.00 29.13  ? 725 HOH B O     1 
HETATM 8488 O O     . HOH J 5 .   ? 39.561 -31.136 -55.382 1.00 21.90  ? 726 HOH B O     1 
HETATM 8489 O O     . HOH J 5 .   ? 17.969 6.996   -56.778 1.00 36.55  ? 727 HOH B O     1 
HETATM 8490 O O     . HOH J 5 .   ? 22.560 -20.406 -34.604 1.00 26.90  ? 728 HOH B O     1 
HETATM 8491 O O     . HOH J 5 .   ? 50.946 -14.475 -70.105 1.00 36.78  ? 729 HOH B O     1 
HETATM 8492 O O     . HOH J 5 .   ? 42.870 -22.190 -68.763 1.00 25.49  ? 730 HOH B O     1 
HETATM 8493 O O     . HOH J 5 .   ? 56.619 -14.408 -55.658 1.00 24.83  ? 731 HOH B O     1 
HETATM 8494 O O     . HOH J 5 .   ? 41.448 -33.905 -39.543 1.00 18.73  ? 732 HOH B O     1 
HETATM 8495 O O     . HOH J 5 .   ? 24.815 3.965   -40.326 1.00 38.63  ? 733 HOH B O     1 
HETATM 8496 O O     . HOH J 5 .   ? 26.775 -10.048 -54.549 1.00 19.53  ? 734 HOH B O     1 
HETATM 8497 O O     . HOH J 5 .   ? 21.272 -30.011 -75.664 1.00 32.38  ? 735 HOH B O     1 
HETATM 8498 O O     . HOH J 5 .   ? 30.598 -0.291  -37.164 1.00 24.04  ? 736 HOH B O     1 
HETATM 8499 O O     . HOH J 5 .   ? 32.910 2.471   -50.047 1.00 19.39  ? 737 HOH B O     1 
HETATM 8500 O O     . HOH J 5 .   ? 54.016 -2.216  -30.985 1.00 27.52  ? 738 HOH B O     1 
HETATM 8501 O O     . HOH J 5 .   ? 34.048 -29.778 -60.212 1.00 20.28  ? 739 HOH B O     1 
HETATM 8502 O O     . HOH J 5 .   ? 37.965 -24.489 -51.584 1.00 28.28  ? 740 HOH B O     1 
HETATM 8503 O O     . HOH J 5 .   ? 14.278 -21.050 -43.462 1.00 19.47  ? 741 HOH B O     1 
HETATM 8504 O O     . HOH J 5 .   ? 29.228 -15.152 -40.951 1.00 29.09  ? 742 HOH B O     1 
HETATM 8505 O O     . HOH J 5 .   ? 36.400 -8.314  -56.922 1.00 22.56  ? 743 HOH B O     1 
HETATM 8506 O O     . HOH J 5 .   ? 25.881 6.257   -41.427 1.00 31.97  ? 744 HOH B O     1 
HETATM 8507 O O     . HOH J 5 .   ? 43.083 -18.339 -61.692 1.00 17.23  ? 745 HOH B O     1 
HETATM 8508 O O     . HOH J 5 .   ? 34.082 -0.606  -44.996 1.00 19.08  ? 746 HOH B O     1 
HETATM 8509 O O     . HOH J 5 .   ? 12.232 -14.750 -44.282 1.00 28.01  ? 747 HOH B O     1 
HETATM 8510 O O     . HOH J 5 .   ? 62.357 -7.232  -32.218 1.00 35.96  ? 748 HOH B O     1 
HETATM 8511 O O     . HOH J 5 .   ? 59.249 -6.035  -67.514 1.00 29.61  ? 749 HOH B O     1 
HETATM 8512 O O     . HOH J 5 .   ? 30.045 -24.094 -54.292 1.00 43.14  ? 750 HOH B O     1 
HETATM 8513 O O     . HOH J 5 .   ? 24.022 -7.897  -34.164 1.00 26.23  ? 751 HOH B O     1 
HETATM 8514 O O     . HOH J 5 .   ? 21.955 -34.751 -54.544 1.00 27.47  ? 752 HOH B O     1 
HETATM 8515 O O     . HOH J 5 .   ? 35.851 -26.083 -71.723 1.00 29.82  ? 753 HOH B O     1 
HETATM 8516 O O     . HOH J 5 .   ? 63.891 0.362   -41.831 1.00 24.79  ? 754 HOH B O     1 
HETATM 8517 O O     . HOH J 5 .   ? 6.063  -15.352 -37.326 1.00 36.82  ? 755 HOH B O     1 
HETATM 8518 O O     . HOH J 5 .   ? 61.388 -7.500  -49.029 1.00 27.89  ? 756 HOH B O     1 
HETATM 8519 O O     . HOH J 5 .   ? 59.749 -8.070  -53.416 1.00 28.35  ? 757 HOH B O     1 
HETATM 8520 O O     . HOH J 5 .   ? 15.648 -14.704 -57.360 1.00 32.53  ? 758 HOH B O     1 
HETATM 8521 O O     . HOH J 5 .   ? 36.187 -21.591 -59.978 1.00 23.52  ? 759 HOH B O     1 
HETATM 8522 O O     . HOH J 5 .   ? 32.368 -9.376  -49.648 1.00 17.19  ? 760 HOH B O     1 
HETATM 8523 O O     . HOH J 5 .   ? 25.954 -39.209 -44.663 1.00 34.26  ? 761 HOH B O     1 
HETATM 8524 O O     . HOH J 5 .   ? 19.730 -13.829 -39.359 1.00 20.92  ? 762 HOH B O     1 
HETATM 8525 O O     . HOH J 5 .   ? 31.114 -4.605  -45.454 1.00 23.77  ? 763 HOH B O     1 
HETATM 8526 O O     . HOH J 5 .   ? 31.571 -1.882  -45.028 1.00 19.01  ? 764 HOH B O     1 
HETATM 8527 O O     . HOH J 5 .   ? 40.555 -0.349  -54.843 1.00 30.06  ? 765 HOH B O     1 
HETATM 8528 O O     . HOH J 5 .   ? 39.823 -24.130 -67.468 1.00 32.02  ? 766 HOH B O     1 
HETATM 8529 O O     . HOH J 5 .   ? 56.425 -22.637 -48.215 1.00 36.00  ? 767 HOH B O     1 
HETATM 8530 O O     . HOH J 5 .   ? 66.916 -18.056 -54.742 1.00 31.16  ? 768 HOH B O     1 
HETATM 8531 O O     . HOH J 5 .   ? 42.048 -34.370 -45.155 1.00 21.63  ? 769 HOH B O     1 
HETATM 8532 O O     . HOH J 5 .   ? 49.917 -31.324 -42.842 1.00 13.12  ? 770 HOH B O     1 
HETATM 8533 O O     . HOH J 5 .   ? 36.057 -22.129 -55.894 1.00 27.12  ? 771 HOH B O     1 
HETATM 8534 O O     . HOH J 5 .   ? 22.423 -20.369 -38.985 1.00 33.48  ? 772 HOH B O     1 
HETATM 8535 O O     . HOH J 5 .   ? 16.751 -17.237 -74.503 1.00 31.97  ? 773 HOH B O     1 
HETATM 8536 O O     . HOH J 5 .   ? 50.710 -25.900 -46.150 1.00 22.08  ? 774 HOH B O     1 
HETATM 8537 O O     . HOH J 5 .   ? 36.098 -13.673 -45.127 1.00 24.47  ? 775 HOH B O     1 
HETATM 8538 O O     . HOH J 5 .   ? 38.994 -10.896 -60.247 1.00 25.45  ? 776 HOH B O     1 
HETATM 8539 O O     . HOH J 5 .   ? 23.872 -0.325  -58.690 1.00 36.51  ? 777 HOH B O     1 
HETATM 8540 O O     . HOH J 5 .   ? 54.498 -18.035 -74.786 1.00 48.57  ? 778 HOH B O     1 
HETATM 8541 O O     . HOH J 5 .   ? 46.194 -36.534 -45.629 1.00 27.55  ? 779 HOH B O     1 
HETATM 8542 O O     . HOH J 5 .   ? 56.138 -6.279  -29.351 1.00 35.49  ? 780 HOH B O     1 
HETATM 8543 O O     . HOH J 5 .   ? 27.591 -25.563 -54.033 1.00 30.44  ? 781 HOH B O     1 
HETATM 8544 O O     . HOH J 5 .   ? 32.670 -6.833  -48.377 1.00 16.31  ? 782 HOH B O     1 
HETATM 8545 O O     . HOH J 5 .   ? 62.997 -10.658 -56.151 1.00 30.19  ? 783 HOH B O     1 
HETATM 8546 O O     . HOH J 5 .   ? 32.178 4.254   -38.670 1.00 33.91  ? 784 HOH B O     1 
HETATM 8547 O O     . HOH J 5 .   ? 40.742 -34.211 -42.764 1.00 22.12  ? 785 HOH B O     1 
HETATM 8548 O O     . HOH J 5 .   ? 19.980 -20.144 -37.850 1.00 31.51  ? 786 HOH B O     1 
HETATM 8549 O O     . HOH J 5 .   ? 38.812 -21.200 -53.288 1.00 23.09  ? 787 HOH B O     1 
HETATM 8550 O O     . HOH J 5 .   ? 59.638 -13.796 -32.879 1.00 30.17  ? 788 HOH B O     1 
HETATM 8551 O O     . HOH J 5 .   ? 33.877 7.056   -51.508 1.00 37.53  ? 789 HOH B O     1 
HETATM 8552 O O     . HOH J 5 .   ? 46.582 -31.798 -73.270 1.00 39.29  ? 790 HOH B O     1 
HETATM 8553 O O     . HOH J 5 .   ? 51.422 -30.463 -40.953 1.00 25.43  ? 791 HOH B O     1 
HETATM 8554 O O     . HOH J 5 .   ? 46.811 -34.413 -54.173 1.00 41.70  ? 792 HOH B O     1 
HETATM 8555 O O     . HOH J 5 .   ? 60.940 -29.873 -50.502 1.00 34.02  ? 793 HOH B O     1 
HETATM 8556 O O     . HOH J 5 .   ? 16.998 -7.515  -41.409 1.00 30.06  ? 794 HOH B O     1 
HETATM 8557 O O     . HOH J 5 .   ? 34.733 -16.008 -65.458 1.00 30.17  ? 795 HOH B O     1 
HETATM 8558 O O     . HOH J 5 .   ? 46.336 -33.098 -61.183 1.00 35.71  ? 796 HOH B O     1 
HETATM 8559 O O     . HOH J 5 .   ? 11.693 -25.379 -50.996 1.00 23.45  ? 797 HOH B O     1 
HETATM 8560 O O     . HOH J 5 .   ? 24.474 12.317  -48.314 1.00 43.34  ? 798 HOH B O     1 
HETATM 8561 O O     . HOH J 5 .   ? 41.008 -4.545  -27.447 1.00 25.30  ? 799 HOH B O     1 
HETATM 8562 O O     . HOH J 5 .   ? 30.703 -21.855 -50.914 1.00 23.92  ? 800 HOH B O     1 
HETATM 8563 O O     . HOH J 5 .   ? 12.277 -29.099 -65.728 1.00 35.54  ? 801 HOH B O     1 
HETATM 8564 O O     . HOH J 5 .   ? 39.584 -40.734 -38.664 1.00 36.40  ? 802 HOH B O     1 
HETATM 8565 O O     . HOH J 5 .   ? 25.328 -7.650  -62.480 1.00 31.52  ? 803 HOH B O     1 
HETATM 8566 O O     . HOH J 5 .   ? 36.720 -17.783 -65.650 1.00 22.13  ? 804 HOH B O     1 
HETATM 8567 O O     . HOH J 5 .   ? 34.707 -27.361 -74.070 1.00 31.37  ? 805 HOH B O     1 
HETATM 8568 O O     . HOH J 5 .   ? 55.754 -12.749 -69.489 1.00 42.83  ? 806 HOH B O     1 
HETATM 8569 O O     . HOH J 5 .   ? 41.933 -30.279 -56.756 1.00 24.92  ? 807 HOH B O     1 
HETATM 8570 O O     . HOH J 5 .   ? 39.845 -31.949 -64.000 1.00 33.59  ? 808 HOH B O     1 
HETATM 8571 O O     . HOH J 5 .   ? 24.556 -11.000 -34.667 1.00 26.76  ? 809 HOH B O     1 
HETATM 8572 O O     . HOH J 5 .   ? 57.960 -12.646 -61.388 1.00 31.41  ? 810 HOH B O     1 
HETATM 8573 O O     . HOH J 5 .   ? 18.680 -34.387 -76.724 1.00 38.88  ? 811 HOH B O     1 
HETATM 8574 O O     . HOH J 5 .   ? 11.781 -19.966 -53.998 1.00 43.87  ? 812 HOH B O     1 
HETATM 8575 O O     . HOH J 5 .   ? 31.222 -4.530  -48.308 1.00 16.83  ? 813 HOH B O     1 
HETATM 8576 O O     . HOH J 5 .   ? 16.948 -19.683 -36.559 1.00 22.97  ? 814 HOH B O     1 
HETATM 8577 O O     . HOH J 5 .   ? 51.441 -22.676 -37.076 1.00 33.32  ? 815 HOH B O     1 
HETATM 8578 O O     . HOH J 5 .   ? 27.376 -6.178  -63.984 1.00 39.85  ? 816 HOH B O     1 
HETATM 8579 O O     . HOH J 5 .   ? 56.184 -12.895 -59.139 1.00 30.24  ? 817 HOH B O     1 
HETATM 8580 O O     . HOH J 5 .   ? 36.254 -7.401  -40.294 1.00 21.00  ? 818 HOH B O     1 
HETATM 8581 O O     . HOH J 5 .   ? 12.867 -17.031 -52.281 1.00 29.70  ? 819 HOH B O     1 
HETATM 8582 O O     . HOH J 5 .   ? 48.629 -32.414 -64.652 1.00 36.73  ? 820 HOH B O     1 
HETATM 8583 O O     . HOH J 5 .   ? 27.936 -38.600 -54.488 1.00 30.87  ? 821 HOH B O     1 
HETATM 8584 O O     . HOH J 5 .   ? 38.600 -40.620 -33.334 1.00 29.61  ? 822 HOH B O     1 
HETATM 8585 O O     . HOH J 5 .   ? 46.608 -37.762 -35.509 1.00 33.86  ? 823 HOH B O     1 
HETATM 8586 O O     . HOH J 5 .   ? 55.478 9.939   -27.763 1.00 40.02  ? 824 HOH B O     1 
HETATM 8587 O O     . HOH J 5 .   ? 11.722 -7.813  -36.299 1.00 41.38  ? 825 HOH B O     1 
HETATM 8588 O O     . HOH J 5 .   ? 48.071 -26.073 -46.317 1.00 23.09  ? 826 HOH B O     1 
HETATM 8589 O O     . HOH J 5 .   ? 26.255 -14.274 -68.366 1.00 37.33  ? 827 HOH B O     1 
HETATM 8590 O O     . HOH J 5 .   ? 49.456 -23.780 -74.393 1.00 45.17  ? 828 HOH B O     1 
HETATM 8591 O O     . HOH J 5 .   ? 33.574 7.928   -36.481 1.00 26.58  ? 829 HOH B O     1 
HETATM 8592 O O     . HOH J 5 .   ? 27.866 7.601   -40.210 1.00 33.79  ? 830 HOH B O     1 
HETATM 8593 O O     . HOH J 5 .   ? 18.066 2.994   -45.514 1.00 33.54  ? 831 HOH B O     1 
HETATM 8594 O O     . HOH J 5 .   ? 61.447 9.944   -49.394 1.00 49.30  ? 832 HOH B O     1 
HETATM 8595 O O     . HOH J 5 .   ? 32.756 -6.743  -45.776 1.00 19.64  ? 833 HOH B O     1 
HETATM 8596 O O     . HOH J 5 .   ? 48.817 -30.762 -56.554 1.00 29.59  ? 834 HOH B O     1 
HETATM 8597 O O     . HOH J 5 .   ? 37.743 -21.107 -57.688 1.00 23.02  ? 835 HOH B O     1 
HETATM 8598 O O     . HOH J 5 .   ? 52.864 -8.966  -27.575 1.00 35.99  ? 836 HOH B O     1 
HETATM 8599 O O     . HOH J 5 .   ? 36.764 -14.528 -68.378 1.00 32.70  ? 837 HOH B O     1 
HETATM 8600 O O     . HOH J 5 .   ? 48.596 -2.380  -53.947 1.00 33.10  ? 838 HOH B O     1 
HETATM 8601 O O     . HOH J 5 .   ? 29.909 -37.718 -55.865 1.00 34.91  ? 839 HOH B O     1 
HETATM 8602 O O     . HOH J 5 .   ? 69.000 -15.503 -56.091 1.00 36.84  ? 840 HOH B O     1 
HETATM 8603 O O     . HOH J 5 .   ? 58.913 11.310  -44.681 1.00 33.40  ? 841 HOH B O     1 
HETATM 8604 O O     . HOH J 5 .   ? 19.042 -31.826 -49.271 1.00 36.77  ? 842 HOH B O     1 
HETATM 8605 O O     . HOH J 5 .   ? 30.125 -27.787 -75.041 1.00 40.58  ? 843 HOH B O     1 
HETATM 8606 O O     . HOH J 5 .   ? 54.635 -12.892 -66.638 1.00 30.86  ? 844 HOH B O     1 
HETATM 8607 O O     . HOH J 5 .   ? 25.840 -40.452 -63.075 1.00 38.35  ? 845 HOH B O     1 
HETATM 8608 O O     . HOH J 5 .   ? 26.036 -21.593 -76.686 1.00 34.47  ? 846 HOH B O     1 
HETATM 8609 O O     . HOH J 5 .   ? 21.250 9.866   -46.087 1.00 42.66  ? 847 HOH B O     1 
HETATM 8610 O O     . HOH J 5 .   ? 47.524 -8.007  -54.741 1.00 45.45  ? 848 HOH B O     1 
HETATM 8611 O O     . HOH J 5 .   ? 43.239 1.243   -55.964 1.00 42.80  ? 849 HOH B O     1 
HETATM 8612 O O     . HOH J 5 .   ? 39.749 12.935  -42.133 1.00 34.05  ? 850 HOH B O     1 
HETATM 8613 O O     . HOH J 5 .   ? 14.972 -3.904  -40.288 1.00 39.11  ? 851 HOH B O     1 
HETATM 8614 O O     . HOH J 5 .   ? 49.563 -30.396 -58.813 1.00 35.59  ? 852 HOH B O     1 
HETATM 8615 O O     . HOH J 5 .   ? 37.644 -10.951 -37.780 1.00 41.12  ? 853 HOH B O     1 
HETATM 8616 O O     . HOH J 5 .   ? 28.287 -19.924 -38.884 1.00 33.18  ? 854 HOH B O     1 
HETATM 8617 O O     . HOH J 5 .   ? 26.283 -13.275 -76.004 1.00 42.31  ? 855 HOH B O     1 
HETATM 8618 O O     . HOH J 5 .   ? 30.253 -4.334  -62.450 1.00 34.02  ? 856 HOH B O     1 
HETATM 8619 O O     . HOH J 5 .   ? 53.922 9.795   -60.979 1.00 35.59  ? 857 HOH B O     1 
HETATM 8620 O O     . HOH J 5 .   ? 46.827 11.857  -37.669 1.00 34.92  ? 858 HOH B O     1 
HETATM 8621 O O     . HOH J 5 .   ? 17.693 3.685   -42.908 1.00 38.03  ? 859 HOH B O     1 
HETATM 8622 O O     . HOH J 5 .   ? 67.752 -0.877  -68.207 1.00 49.14  ? 860 HOH B O     1 
HETATM 8623 O O     . HOH J 5 .   ? 69.351 -11.846 -59.522 1.00 42.56  ? 861 HOH B O     1 
HETATM 8624 O O     . HOH J 5 .   ? 28.709 -15.367 -70.564 1.00 37.87  ? 862 HOH B O     1 
HETATM 8625 O O     . HOH J 5 .   ? 39.417 -22.181 -51.324 1.00 25.36  ? 863 HOH B O     1 
HETATM 8626 O O     . HOH J 5 .   ? 33.176 -40.400 -44.692 1.00 40.66  ? 864 HOH B O     1 
HETATM 8627 O O     . HOH J 5 .   ? 40.610 -6.497  -39.525 1.00 34.43  ? 865 HOH B O     1 
HETATM 8628 O O     . HOH J 5 .   ? 39.670 -14.897 -44.143 1.00 43.71  ? 866 HOH B O     1 
HETATM 8629 O O     . HOH J 5 .   ? 32.864 -14.747 -66.133 1.00 29.61  ? 867 HOH B O     1 
HETATM 8630 O O     . HOH J 5 .   ? 37.650 8.672   -53.652 1.00 40.97  ? 868 HOH B O     1 
HETATM 8631 O O     . HOH J 5 .   ? 44.044 -24.249 -64.879 1.00 47.47  ? 869 HOH B O     1 
HETATM 8632 O O     . HOH J 5 .   ? 54.478 10.231  -32.529 1.00 38.58  ? 870 HOH B O     1 
HETATM 8633 O O     . HOH J 5 .   ? 35.364 -36.409 -64.694 1.00 39.47  ? 871 HOH B O     1 
HETATM 8634 O O     . HOH J 5 .   ? 20.215 -10.067 -68.112 1.00 40.34  ? 872 HOH B O     1 
HETATM 8635 O O     . HOH J 5 .   ? 16.258 -12.692 -72.172 1.00 41.10  ? 873 HOH B O     1 
HETATM 8636 O O     . HOH J 5 .   ? 14.598 -8.463  -42.451 1.00 35.28  ? 874 HOH B O     1 
HETATM 8637 O O     . HOH J 5 .   ? 44.807 -12.940 -44.907 1.00 54.96  ? 875 HOH B O     1 
HETATM 8638 O O     . HOH J 5 .   ? 49.767 -33.797 -46.598 1.00 29.64  ? 876 HOH B O     1 
HETATM 8639 O O     . HOH J 5 .   ? 42.545 -18.723 -70.926 1.00 37.15  ? 877 HOH B O     1 
HETATM 8640 O O     . HOH J 5 .   ? 30.556 11.266  -40.712 1.00 42.65  ? 878 HOH B O     1 
HETATM 8641 O O     . HOH J 5 .   ? 47.653 6.319   -57.626 1.00 36.67  ? 879 HOH B O     1 
HETATM 8642 O O     . HOH J 5 .   ? 10.692 -23.615 -58.282 1.00 39.86  ? 880 HOH B O     1 
HETATM 8643 O O     . HOH J 5 .   ? 9.411  -13.637 -44.184 1.00 28.75  ? 881 HOH B O     1 
HETATM 8644 O O     . HOH J 5 .   ? 17.216 -34.727 -55.314 1.00 37.73  ? 882 HOH B O     1 
HETATM 8645 O O     . HOH J 5 .   ? 53.458 2.063   -28.260 1.00 37.15  ? 883 HOH B O     1 
HETATM 8646 O O     . HOH J 5 .   ? 35.490 1.252   -36.806 1.00 38.19  ? 884 HOH B O     1 
HETATM 8647 O O     . HOH J 5 .   ? 19.543 -40.026 -59.614 1.00 38.17  ? 885 HOH B O     1 
HETATM 8648 O O     . HOH J 5 .   ? 40.769 -35.046 -50.384 1.00 33.54  ? 886 HOH B O     1 
HETATM 8649 O O     . HOH J 5 .   ? 61.165 12.206  -50.518 1.00 42.55  ? 887 HOH B O     1 
HETATM 8650 O O     . HOH J 5 .   ? 14.370 -23.107 -75.232 1.00 41.00  ? 888 HOH B O     1 
HETATM 8651 O O     . HOH J 5 .   ? 41.967 -13.748 -43.830 1.00 38.18  ? 889 HOH B O     1 
HETATM 8652 O O     . HOH J 5 .   ? 16.982 -10.206 -64.058 1.00 43.54  ? 890 HOH B O     1 
HETATM 8653 O O     . HOH J 5 .   ? 45.702 -13.606 -50.432 1.00 35.25  ? 891 HOH B O     1 
HETATM 8654 O O     . HOH J 5 .   ? 30.485 -41.760 -61.273 1.00 39.03  ? 892 HOH B O     1 
HETATM 8655 O O     . HOH J 5 .   ? 38.355 -38.685 -54.547 1.00 32.76  ? 893 HOH B O     1 
HETATM 8656 O O     . HOH J 5 .   ? 44.343 -11.721 -50.891 1.00 42.37  ? 894 HOH B O     1 
HETATM 8657 O O     . HOH J 5 .   ? 35.458 4.296   -36.553 1.00 36.75  ? 895 HOH B O     1 
HETATM 8658 O O     . HOH J 5 .   ? 11.006 -21.483 -62.931 1.00 45.90  ? 896 HOH B O     1 
HETATM 8659 O O     . HOH J 5 .   ? 45.034 6.569   -57.454 1.00 36.77  ? 897 HOH B O     1 
HETATM 8660 O O     . HOH J 5 .   ? 42.442 -31.911 -58.910 1.00 36.20  ? 898 HOH B O     1 
HETATM 8661 O O     . HOH J 5 .   ? 42.402 -24.138 -67.181 1.00 34.77  ? 899 HOH B O     1 
HETATM 8662 O O     . HOH J 5 .   ? 18.364 -35.118 -50.276 1.00 38.66  ? 900 HOH B O     1 
HETATM 8663 O O     . HOH J 5 .   ? 39.205 -5.884  -34.321 1.00 46.07  ? 901 HOH B O     1 
HETATM 8664 O O     . HOH J 5 .   ? 66.660 7.464   -39.269 1.00 41.39  ? 902 HOH B O     1 
HETATM 8665 O O     . HOH J 5 .   ? 68.710 -16.700 -58.817 1.00 41.72  ? 903 HOH B O     1 
HETATM 8666 O O     . HOH J 5 .   ? 61.789 -8.228  -51.654 1.00 28.22  ? 904 HOH B O     1 
HETATM 8667 O O     . HOH J 5 .   ? 41.565 -10.778 -66.898 1.00 41.04  ? 905 HOH B O     1 
HETATM 8668 O O     . HOH J 5 .   ? 40.996 -35.435 -47.808 1.00 32.70  ? 906 HOH B O     1 
HETATM 8669 O O     . HOH J 5 .   ? 68.271 -4.521  -50.589 1.00 37.28  ? 907 HOH B O     1 
HETATM 8670 O O     . HOH J 5 .   ? 64.100 -8.672  -53.899 1.00 42.08  ? 908 HOH B O     1 
HETATM 8671 O O     . HOH J 5 .   ? 37.255 -12.286 -67.962 1.00 31.81  ? 909 HOH B O     1 
# 
