data_5DF0
# 
_entry.id   5DF0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.285 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5DF0         
WWPDB D_1000213110 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          5DEZ 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5DF0 
_pdbx_database_status.recvd_initial_deposition_date   2015-08-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Mou, T.-C.'   1 
'Sprang, S.R.' 2 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of AcMNPV Chitinase A' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Mou, T.-C.'   1 
primary 'Sprang, S.R.' 2 
# 
_cell.entry_id           5DF0 
_cell.length_a           96.712 
_cell.length_b           112.766 
_cell.length_c           129.591 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5DF0 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 Ac-ChiA                                                                                             60875.121 2  
3.2.1.14 ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                                                                              221.208   6  
?        ? ? ? 
3 non-polymer syn '2-deoxy-2-(ethanethioylamino)-beta-D-glucopyranose'                                                237.273   2  
?        ? ? ? 
4 non-polymer syn '(2R,3aR,5R,6R,7R,7aR)-5-(hydroxymethyl)-2-methylhexahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol' 221.274   2  
?        ? ? ? 
5 non-polymer man 'CHLORIDE ION'                                                                                      35.453    1  
?        ? ? ? 
6 non-polymer man 'SULFATE ION'                                                                                       96.063    5  
?        ? ? ? 
7 water       nat water                                                                                               18.015    16 
?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Chitinase 
# 
_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       
;MLYKLLNVLWLVAVSNAIPGTPVIDWADRNYALVEINYEATAYENLIKPKEQVDVQVSWNVWNGDIGDIAYVLFDEQQVW
KGDAESKRATIKVLVSGQFNMRVKLCNEDGCSVSDPVLVKVADTDGGHLAPLEYTWLENNKPGRREDKIVAAYFVEWGVY
GRNFPVDKVPLPNLSHLLYGFIPICGGDGINDALKTISGSFESLQRSCKGREDFKVAIHDPWAAVQKPQKSVSAWNEPYK
GNFGQLMAAKLANPHLKILPSIGGWTLSDPFYFMHDVEKRNVFVDSVKEFLQVWKFFDGVDVDWEFPGGKGANPSLGDAE
RDAKTYILLLEELRAMLDDLEAQTGRVYELTSAISAGYDKIAVVNYAEAQKSLGKIFLMSYDFKGAWSNTDLGYQTTVYA
PSWNSEELYTTHYAVDALLKQGVDPNKIIVGVAMYGRGWTGVTNYTNDNYFSGTGNGPVSGTWEDGVVDYRQIQKDLNNY
VYTFDSAAQASYVFDKSKGDLISFDSVDSVLGKVKYVDRNKLGGLFAWEIDADNGDLLNAINAQF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLYKLLNVLWLVAVSNAIPGTPVIDWADRNYALVEINYEATAYENLIKPKEQVDVQVSWNVWNGDIGDIAYVLFDEQQVW
KGDAESKRATIKVLVSGQFNMRVKLCNEDGCSVSDPVLVKVADTDGGHLAPLEYTWLENNKPGRREDKIVAAYFVEWGVY
GRNFPVDKVPLPNLSHLLYGFIPICGGDGINDALKTISGSFESLQRSCKGREDFKVAIHDPWAAVQKPQKSVSAWNEPYK
GNFGQLMAAKLANPHLKILPSIGGWTLSDPFYFMHDVEKRNVFVDSVKEFLQVWKFFDGVDVDWEFPGGKGANPSLGDAE
RDAKTYILLLEELRAMLDDLEAQTGRVYELTSAISAGYDKIAVVNYAEAQKSLGKIFLMSYDFKGAWSNTDLGYQTTVYA
PSWNSEELYTTHYAVDALLKQGVDPNKIIVGVAMYGRGWTGVTNYTNDNYFSGTGNGPVSGTWEDGVVDYRQIQKDLNNY
VYTFDSAAQASYVFDKSKGDLISFDSVDSVLGKVKYVDRNKLGGLFAWEIDADNGDLLNAINAQF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   LEU n 
1 3   TYR n 
1 4   LYS n 
1 5   LEU n 
1 6   LEU n 
1 7   ASN n 
1 8   VAL n 
1 9   LEU n 
1 10  TRP n 
1 11  LEU n 
1 12  VAL n 
1 13  ALA n 
1 14  VAL n 
1 15  SER n 
1 16  ASN n 
1 17  ALA n 
1 18  ILE n 
1 19  PRO n 
1 20  GLY n 
1 21  THR n 
1 22  PRO n 
1 23  VAL n 
1 24  ILE n 
1 25  ASP n 
1 26  TRP n 
1 27  ALA n 
1 28  ASP n 
1 29  ARG n 
1 30  ASN n 
1 31  TYR n 
1 32  ALA n 
1 33  LEU n 
1 34  VAL n 
1 35  GLU n 
1 36  ILE n 
1 37  ASN n 
1 38  TYR n 
1 39  GLU n 
1 40  ALA n 
1 41  THR n 
1 42  ALA n 
1 43  TYR n 
1 44  GLU n 
1 45  ASN n 
1 46  LEU n 
1 47  ILE n 
1 48  LYS n 
1 49  PRO n 
1 50  LYS n 
1 51  GLU n 
1 52  GLN n 
1 53  VAL n 
1 54  ASP n 
1 55  VAL n 
1 56  GLN n 
1 57  VAL n 
1 58  SER n 
1 59  TRP n 
1 60  ASN n 
1 61  VAL n 
1 62  TRP n 
1 63  ASN n 
1 64  GLY n 
1 65  ASP n 
1 66  ILE n 
1 67  GLY n 
1 68  ASP n 
1 69  ILE n 
1 70  ALA n 
1 71  TYR n 
1 72  VAL n 
1 73  LEU n 
1 74  PHE n 
1 75  ASP n 
1 76  GLU n 
1 77  GLN n 
1 78  GLN n 
1 79  VAL n 
1 80  TRP n 
1 81  LYS n 
1 82  GLY n 
1 83  ASP n 
1 84  ALA n 
1 85  GLU n 
1 86  SER n 
1 87  LYS n 
1 88  ARG n 
1 89  ALA n 
1 90  THR n 
1 91  ILE n 
1 92  LYS n 
1 93  VAL n 
1 94  LEU n 
1 95  VAL n 
1 96  SER n 
1 97  GLY n 
1 98  GLN n 
1 99  PHE n 
1 100 ASN n 
1 101 MET n 
1 102 ARG n 
1 103 VAL n 
1 104 LYS n 
1 105 LEU n 
1 106 CYS n 
1 107 ASN n 
1 108 GLU n 
1 109 ASP n 
1 110 GLY n 
1 111 CYS n 
1 112 SER n 
1 113 VAL n 
1 114 SER n 
1 115 ASP n 
1 116 PRO n 
1 117 VAL n 
1 118 LEU n 
1 119 VAL n 
1 120 LYS n 
1 121 VAL n 
1 122 ALA n 
1 123 ASP n 
1 124 THR n 
1 125 ASP n 
1 126 GLY n 
1 127 GLY n 
1 128 HIS n 
1 129 LEU n 
1 130 ALA n 
1 131 PRO n 
1 132 LEU n 
1 133 GLU n 
1 134 TYR n 
1 135 THR n 
1 136 TRP n 
1 137 LEU n 
1 138 GLU n 
1 139 ASN n 
1 140 ASN n 
1 141 LYS n 
1 142 PRO n 
1 143 GLY n 
1 144 ARG n 
1 145 ARG n 
1 146 GLU n 
1 147 ASP n 
1 148 LYS n 
1 149 ILE n 
1 150 VAL n 
1 151 ALA n 
1 152 ALA n 
1 153 TYR n 
1 154 PHE n 
1 155 VAL n 
1 156 GLU n 
1 157 TRP n 
1 158 GLY n 
1 159 VAL n 
1 160 TYR n 
1 161 GLY n 
1 162 ARG n 
1 163 ASN n 
1 164 PHE n 
1 165 PRO n 
1 166 VAL n 
1 167 ASP n 
1 168 LYS n 
1 169 VAL n 
1 170 PRO n 
1 171 LEU n 
1 172 PRO n 
1 173 ASN n 
1 174 LEU n 
1 175 SER n 
1 176 HIS n 
1 177 LEU n 
1 178 LEU n 
1 179 TYR n 
1 180 GLY n 
1 181 PHE n 
1 182 ILE n 
1 183 PRO n 
1 184 ILE n 
1 185 CYS n 
1 186 GLY n 
1 187 GLY n 
1 188 ASP n 
1 189 GLY n 
1 190 ILE n 
1 191 ASN n 
1 192 ASP n 
1 193 ALA n 
1 194 LEU n 
1 195 LYS n 
1 196 THR n 
1 197 ILE n 
1 198 SER n 
1 199 GLY n 
1 200 SER n 
1 201 PHE n 
1 202 GLU n 
1 203 SER n 
1 204 LEU n 
1 205 GLN n 
1 206 ARG n 
1 207 SER n 
1 208 CYS n 
1 209 LYS n 
1 210 GLY n 
1 211 ARG n 
1 212 GLU n 
1 213 ASP n 
1 214 PHE n 
1 215 LYS n 
1 216 VAL n 
1 217 ALA n 
1 218 ILE n 
1 219 HIS n 
1 220 ASP n 
1 221 PRO n 
1 222 TRP n 
1 223 ALA n 
1 224 ALA n 
1 225 VAL n 
1 226 GLN n 
1 227 LYS n 
1 228 PRO n 
1 229 GLN n 
1 230 LYS n 
1 231 SER n 
1 232 VAL n 
1 233 SER n 
1 234 ALA n 
1 235 TRP n 
1 236 ASN n 
1 237 GLU n 
1 238 PRO n 
1 239 TYR n 
1 240 LYS n 
1 241 GLY n 
1 242 ASN n 
1 243 PHE n 
1 244 GLY n 
1 245 GLN n 
1 246 LEU n 
1 247 MET n 
1 248 ALA n 
1 249 ALA n 
1 250 LYS n 
1 251 LEU n 
1 252 ALA n 
1 253 ASN n 
1 254 PRO n 
1 255 HIS n 
1 256 LEU n 
1 257 LYS n 
1 258 ILE n 
1 259 LEU n 
1 260 PRO n 
1 261 SER n 
1 262 ILE n 
1 263 GLY n 
1 264 GLY n 
1 265 TRP n 
1 266 THR n 
1 267 LEU n 
1 268 SER n 
1 269 ASP n 
1 270 PRO n 
1 271 PHE n 
1 272 TYR n 
1 273 PHE n 
1 274 MET n 
1 275 HIS n 
1 276 ASP n 
1 277 VAL n 
1 278 GLU n 
1 279 LYS n 
1 280 ARG n 
1 281 ASN n 
1 282 VAL n 
1 283 PHE n 
1 284 VAL n 
1 285 ASP n 
1 286 SER n 
1 287 VAL n 
1 288 LYS n 
1 289 GLU n 
1 290 PHE n 
1 291 LEU n 
1 292 GLN n 
1 293 VAL n 
1 294 TRP n 
1 295 LYS n 
1 296 PHE n 
1 297 PHE n 
1 298 ASP n 
1 299 GLY n 
1 300 VAL n 
1 301 ASP n 
1 302 VAL n 
1 303 ASP n 
1 304 TRP n 
1 305 GLU n 
1 306 PHE n 
1 307 PRO n 
1 308 GLY n 
1 309 GLY n 
1 310 LYS n 
1 311 GLY n 
1 312 ALA n 
1 313 ASN n 
1 314 PRO n 
1 315 SER n 
1 316 LEU n 
1 317 GLY n 
1 318 ASP n 
1 319 ALA n 
1 320 GLU n 
1 321 ARG n 
1 322 ASP n 
1 323 ALA n 
1 324 LYS n 
1 325 THR n 
1 326 TYR n 
1 327 ILE n 
1 328 LEU n 
1 329 LEU n 
1 330 LEU n 
1 331 GLU n 
1 332 GLU n 
1 333 LEU n 
1 334 ARG n 
1 335 ALA n 
1 336 MET n 
1 337 LEU n 
1 338 ASP n 
1 339 ASP n 
1 340 LEU n 
1 341 GLU n 
1 342 ALA n 
1 343 GLN n 
1 344 THR n 
1 345 GLY n 
1 346 ARG n 
1 347 VAL n 
1 348 TYR n 
1 349 GLU n 
1 350 LEU n 
1 351 THR n 
1 352 SER n 
1 353 ALA n 
1 354 ILE n 
1 355 SER n 
1 356 ALA n 
1 357 GLY n 
1 358 TYR n 
1 359 ASP n 
1 360 LYS n 
1 361 ILE n 
1 362 ALA n 
1 363 VAL n 
1 364 VAL n 
1 365 ASN n 
1 366 TYR n 
1 367 ALA n 
1 368 GLU n 
1 369 ALA n 
1 370 GLN n 
1 371 LYS n 
1 372 SER n 
1 373 LEU n 
1 374 GLY n 
1 375 LYS n 
1 376 ILE n 
1 377 PHE n 
1 378 LEU n 
1 379 MET n 
1 380 SER n 
1 381 TYR n 
1 382 ASP n 
1 383 PHE n 
1 384 LYS n 
1 385 GLY n 
1 386 ALA n 
1 387 TRP n 
1 388 SER n 
1 389 ASN n 
1 390 THR n 
1 391 ASP n 
1 392 LEU n 
1 393 GLY n 
1 394 TYR n 
1 395 GLN n 
1 396 THR n 
1 397 THR n 
1 398 VAL n 
1 399 TYR n 
1 400 ALA n 
1 401 PRO n 
1 402 SER n 
1 403 TRP n 
1 404 ASN n 
1 405 SER n 
1 406 GLU n 
1 407 GLU n 
1 408 LEU n 
1 409 TYR n 
1 410 THR n 
1 411 THR n 
1 412 HIS n 
1 413 TYR n 
1 414 ALA n 
1 415 VAL n 
1 416 ASP n 
1 417 ALA n 
1 418 LEU n 
1 419 LEU n 
1 420 LYS n 
1 421 GLN n 
1 422 GLY n 
1 423 VAL n 
1 424 ASP n 
1 425 PRO n 
1 426 ASN n 
1 427 LYS n 
1 428 ILE n 
1 429 ILE n 
1 430 VAL n 
1 431 GLY n 
1 432 VAL n 
1 433 ALA n 
1 434 MET n 
1 435 TYR n 
1 436 GLY n 
1 437 ARG n 
1 438 GLY n 
1 439 TRP n 
1 440 THR n 
1 441 GLY n 
1 442 VAL n 
1 443 THR n 
1 444 ASN n 
1 445 TYR n 
1 446 THR n 
1 447 ASN n 
1 448 ASP n 
1 449 ASN n 
1 450 TYR n 
1 451 PHE n 
1 452 SER n 
1 453 GLY n 
1 454 THR n 
1 455 GLY n 
1 456 ASN n 
1 457 GLY n 
1 458 PRO n 
1 459 VAL n 
1 460 SER n 
1 461 GLY n 
1 462 THR n 
1 463 TRP n 
1 464 GLU n 
1 465 ASP n 
1 466 GLY n 
1 467 VAL n 
1 468 VAL n 
1 469 ASP n 
1 470 TYR n 
1 471 ARG n 
1 472 GLN n 
1 473 ILE n 
1 474 GLN n 
1 475 LYS n 
1 476 ASP n 
1 477 LEU n 
1 478 ASN n 
1 479 ASN n 
1 480 TYR n 
1 481 VAL n 
1 482 TYR n 
1 483 THR n 
1 484 PHE n 
1 485 ASP n 
1 486 SER n 
1 487 ALA n 
1 488 ALA n 
1 489 GLN n 
1 490 ALA n 
1 491 SER n 
1 492 TYR n 
1 493 VAL n 
1 494 PHE n 
1 495 ASP n 
1 496 LYS n 
1 497 SER n 
1 498 LYS n 
1 499 GLY n 
1 500 ASP n 
1 501 LEU n 
1 502 ILE n 
1 503 SER n 
1 504 PHE n 
1 505 ASP n 
1 506 SER n 
1 507 VAL n 
1 508 ASP n 
1 509 SER n 
1 510 VAL n 
1 511 LEU n 
1 512 GLY n 
1 513 LYS n 
1 514 VAL n 
1 515 LYS n 
1 516 TYR n 
1 517 VAL n 
1 518 ASP n 
1 519 ARG n 
1 520 ASN n 
1 521 LYS n 
1 522 LEU n 
1 523 GLY n 
1 524 GLY n 
1 525 LEU n 
1 526 PHE n 
1 527 ALA n 
1 528 TRP n 
1 529 GLU n 
1 530 ILE n 
1 531 ASP n 
1 532 ALA n 
1 533 ASP n 
1 534 ASN n 
1 535 GLY n 
1 536 ASP n 
1 537 LEU n 
1 538 LEU n 
1 539 ASN n 
1 540 ALA n 
1 541 ILE n 
1 542 ASN n 
1 543 ALA n 
1 544 GLN n 
1 545 PHE 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                   545 
_entity_src_gen.gene_src_common_name               AcMNPV 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ChiA, Ac-ChiA' 
_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      'Autographa californica nuclear polyhedrosis virus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     46015 
_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      Alphabaculovirus 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     558016 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q70SQ1_NPVAC 
_struct_ref.pdbx_db_accession          Q70SQ1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLYKLLNVLWLVAVSNAIPGTPVIDWADRNYALVEINYEATAYENLIKPKEQVDVQVSWNVWNGDIGDIAYVLFDEQQVW
KGDAESKRATIKVLVSGQFNMRVKLCNEDGCSVSDPVLVKVADTDGGHLAPLEYTWLENNKPGRREDKIVAAYFVEWGVY
GRNFPVDKVPLPNLSHLLYGFIPICGGDGINDALKTISGSFESLQRSCKGREDFKVAIHDPWAAVQKPQKSVSAWNEPYK
GNFGQLMAAKLANPHLKILPSIGGWTLSDPFYFMHDVEKRNVFVDSVKEFLQVWKFFDGVDVDWEFPGGKGANPSLGDAE
RDAKTYILLLEELRAMLDDLEAQTGRVYELTSAISAGYDKIAVVNYAEAQKSLGKIFLMSYDFKGAWSNTDLGYQTTVYA
PSWNSEELYTTHYAVDALLKQGVDPNKIIVGVAMYGRGWTGVTNYTNDNYFSGTGNGPVSGTWEDGVVDYRQIQKDLNNY
VYTFDSAAQASYVFDKSKGDLISFDSVDSVLGKVKYVDRNKLGGLFAWEIDADNGDLLNAINAQF
;
_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 5DF0 A 1 ? 545 ? Q70SQ1 1 ? 545 ? 1 545 
2 1 5DF0 B 1 ? 545 ? Q70SQ1 1 ? 545 ? 1 545 
# 
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 
58Y non-polymer         . '(2R,3aR,5R,6R,7R,7aR)-5-(hydroxymethyl)-2-methylhexahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol' ? 
'C8 H15 N O4 S'  221.274 
ALA 'L-peptide linking' y ALANINE                                                                                             ? 
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                                                            ? 
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                          ? 
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                     ? 
'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                                                                                      ? 
'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                                                                            ? 
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                           ? 
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                     ? 
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                                                             ? 
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                           ? 
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                                               ? 
'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                          ? 
'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                             ? 
'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                                                              ? 
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                                          ? 
'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                                                                              ? 
'C8 H15 N O6'    221.208 
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 
SN5 non-polymer         . '2-deoxy-2-(ethanethioylamino)-beta-D-glucopyranose'                                                ? 
'C8 H15 N O5 S'  237.273 
SO4 non-polymer         . 'SULFATE ION'                                                                                       ? 
'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                                                                           ? 
'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                          ? 
'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                            ? 
'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                                                              ? 
'C5 H11 N O2'    117.146 
# 
_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                   5DF0 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.87 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         57.14 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Ammonium sulfate, MES' 
_exptl_crystal_grow.pdbx_pH_range   6.5 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-07-16 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Si (111)' 
_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   0.979 
_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                        'SSRL BEAMLINE BL11-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL11-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5DF0 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.251 
_reflns.d_resolution_low                 28.09 
_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                       20513 
_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             89.64 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  5.4 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.125 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            3.58 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.251 
_reflns_shell.d_res_low                   3.367 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2.13 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        81.95 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_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             2.3 
_reflns_shell.pdbx_Rsym_value             0.127 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5DF0 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     20291 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.43 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             14.978 
_refine.ls_d_res_high                            3.251 
_refine.ls_percent_reflns_obs                    89.58 
_refine.ls_R_factor_obs                          0.2318 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2259 
_refine.ls_R_factor_R_free                       0.2856 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.75 
_refine.ls_number_reflns_R_free                  1978 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1EDQ 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.43 
_refine.pdbx_overall_phase_error                 25.47 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8334 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         171 
_refine_hist.number_atoms_solvent             16 
_refine_hist.number_atoms_total               8521 
_refine_hist.d_res_high                       3.251 
_refine_hist.d_res_low                        14.978 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.002  ? ? 8724  'X-RAY DIFFRACTION' ? 
f_angle_d          0.485  ? ? 11878 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 10.238 ? ? 5008  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.043  ? ? 1285  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 1520  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 3.2506 3.3310  1174 0.3003 81.00 0.3855 . . 126 . . . . 
'X-RAY DIFFRACTION' . 3.3310 3.4200  1203 0.2818 85.00 0.3361 . . 131 . . . . 
'X-RAY DIFFRACTION' . 3.4200 3.5194  1247 0.2783 85.00 0.3410 . . 134 . . . . 
'X-RAY DIFFRACTION' . 3.5194 3.6314  1175 0.2809 83.00 0.3663 . . 128 . . . . 
'X-RAY DIFFRACTION' . 3.6314 3.7593  1196 0.2591 82.00 0.3383 . . 128 . . . . 
'X-RAY DIFFRACTION' . 3.7593 3.9072  1345 0.2283 92.00 0.2829 . . 146 . . . . 
'X-RAY DIFFRACTION' . 3.9072 4.0816  1347 0.2169 94.00 0.2600 . . 146 . . . . 
'X-RAY DIFFRACTION' . 4.0816 4.2920  1377 0.2014 95.00 0.2872 . . 149 . . . . 
'X-RAY DIFFRACTION' . 4.2920 4.5538  1370 0.2003 94.00 0.2631 . . 147 . . . . 
'X-RAY DIFFRACTION' . 4.5538 4.8940  1363 0.1888 92.00 0.2379 . . 147 . . . . 
'X-RAY DIFFRACTION' . 4.8940 5.3658  1328 0.1977 91.00 0.2688 . . 144 . . . . 
'X-RAY DIFFRACTION' . 5.3658 6.0960  1337 0.2212 91.00 0.2782 . . 144 . . . . 
'X-RAY DIFFRACTION' . 6.0960 7.5152  1428 0.2167 95.00 0.2714 . . 155 . . . . 
'X-RAY DIFFRACTION' . 7.5152 14.9781 1423 0.1959 92.00 0.2241 . . 153 . . . . 
# 
_struct.entry_id                     5DF0 
_struct.title                        'Crystal structure of AcMNPV Chitinase A in complex WITH CHITOTRIO-THIAZOLINE DITHIOAMIDE' 
_struct.pdbx_descriptor              'Ac-ChiA (E.C.3.2.1.14)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5DF0 
_struct_keywords.text            'Chitinase, AcMNPV, chitin, Glycosidase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
K N N 6 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 7 ? 
T N N 7 ? 
# 
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 TRP A 157 ? TYR A 160 ? TRP A 157 TYR A 160 5 ? 4  
HELX_P HELX_P2  AA2 PRO A 165 ? VAL A 169 ? PRO A 165 VAL A 169 5 ? 5  
HELX_P HELX_P3  AA3 PRO A 170 ? LEU A 174 ? PRO A 170 LEU A 174 5 ? 5  
HELX_P HELX_P4  AA4 ASN A 191 ? ILE A 197 ? ASN A 191 ILE A 197 5 ? 7  
HELX_P HELX_P5  AA5 GLY A 199 ? CYS A 208 ? GLY A 199 CYS A 208 1 ? 10 
HELX_P HELX_P6  AA6 ASP A 220 ? GLN A 226 ? ASP A 220 GLN A 226 1 ? 7  
HELX_P HELX_P7  AA7 LYS A 240 ? ASN A 253 ? LYS A 240 ASN A 253 1 ? 14 
HELX_P HELX_P8  AA8 SER A 268 ? MET A 274 ? SER A 268 MET A 274 5 ? 7  
HELX_P HELX_P9  AA9 GLU A 278 ? TRP A 294 ? GLU A 278 TRP A 294 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 318 ? GLY A 345 ? ASP A 318 GLY A 345 1 ? 28 
HELX_P HELX_P11 AB2 GLY A 357 ? ALA A 362 ? GLY A 357 ALA A 362 1 ? 6  
HELX_P HELX_P12 AB3 ASN A 365 ? GLN A 370 ? ASN A 365 GLN A 370 1 ? 6  
HELX_P HELX_P13 AB4 THR A 410 ? GLN A 421 ? THR A 410 GLN A 421 1 ? 12 
HELX_P HELX_P14 AB5 ASP A 424 ? ASN A 426 ? ASP A 424 ASN A 426 5 ? 3  
HELX_P HELX_P15 AB6 TYR A 470 ? ASP A 476 ? TYR A 470 ASP A 476 1 ? 7  
HELX_P HELX_P16 AB7 LEU A 477 ? TYR A 480 ? LEU A 477 TYR A 480 5 ? 4  
HELX_P HELX_P17 AB8 SER A 506 ? ARG A 519 ? SER A 506 ARG A 519 1 ? 14 
HELX_P HELX_P18 AB9 GLU A 529 ? ASP A 533 ? GLU A 529 ASP A 533 5 ? 5  
HELX_P HELX_P19 AC1 GLY A 535 ? ASN A 542 ? GLY A 535 ASN A 542 1 ? 8  
HELX_P HELX_P20 AC2 ALA B 42  ? LEU B 46  ? ALA B 42  LEU B 46  1 ? 5  
HELX_P HELX_P21 AC3 TRP B 157 ? TYR B 160 ? TRP B 157 TYR B 160 5 ? 4  
HELX_P HELX_P22 AC4 PRO B 165 ? VAL B 169 ? PRO B 165 VAL B 169 5 ? 5  
HELX_P HELX_P23 AC5 PRO B 170 ? LEU B 174 ? PRO B 170 LEU B 174 5 ? 5  
HELX_P HELX_P24 AC6 ASN B 191 ? ILE B 197 ? ASN B 191 ILE B 197 5 ? 7  
HELX_P HELX_P25 AC7 GLY B 199 ? CYS B 208 ? GLY B 199 CYS B 208 1 ? 10 
HELX_P HELX_P26 AC8 ASP B 220 ? GLN B 226 ? ASP B 220 GLN B 226 1 ? 7  
HELX_P HELX_P27 AC9 LYS B 240 ? ASN B 253 ? LYS B 240 ASN B 253 1 ? 14 
HELX_P HELX_P28 AD1 SER B 268 ? MET B 274 ? SER B 268 MET B 274 5 ? 7  
HELX_P HELX_P29 AD2 ASP B 276 ? TRP B 294 ? ASP B 276 TRP B 294 1 ? 19 
HELX_P HELX_P30 AD3 ASP B 318 ? GLY B 345 ? ASP B 318 GLY B 345 1 ? 28 
HELX_P HELX_P31 AD4 GLY B 357 ? ALA B 362 ? GLY B 357 ALA B 362 1 ? 6  
HELX_P HELX_P32 AD5 GLU B 368 ? SER B 372 ? GLU B 368 SER B 372 5 ? 5  
HELX_P HELX_P33 AD6 THR B 410 ? LYS B 420 ? THR B 410 LYS B 420 1 ? 11 
HELX_P HELX_P34 AD7 TYR B 470 ? ASP B 476 ? TYR B 470 ASP B 476 1 ? 7  
HELX_P HELX_P35 AD8 LEU B 477 ? TYR B 480 ? LEU B 477 TYR B 480 5 ? 4  
HELX_P HELX_P36 AD9 SER B 506 ? ASN B 520 ? SER B 506 ASN B 520 1 ? 15 
HELX_P HELX_P37 AE1 GLU B 529 ? ASP B 533 ? GLU B 529 ASP B 533 5 ? 5  
HELX_P HELX_P38 AE2 GLY B 535 ? ASN B 542 ? GLY B 535 ASN B 542 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ?   ? A CYS 106 SG  ? ? ? 1_555 A CYS 111 SG ? ? A CYS 106 A CYS 111 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf2 disulf ?   ? A CYS 185 SG  ? ? ? 1_555 A CYS 208 SG ? ? A CYS 185 A CYS 208 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf3 disulf ?   ? B CYS 106 SG  ? ? ? 1_555 B CYS 111 SG ? ? B CYS 106 B CYS 111 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf4 disulf ?   ? B CYS 185 SG  ? ? ? 1_555 B CYS 208 SG ? ? B CYS 185 B CYS 208 1_555 ? ? ? ? ? ? ? 2.033 ? 
covale1 covale one ? B ASN 444 ND2 ? ? ? 1_555 N NAG .   C1 ? ? B ASN 444 B NAG 603 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale2 covale one ? F SN5 .   C1  ? ? ? 1_555 G 58Y .   O4 ? ? A SN5 604 A 58Y 605 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale3 covale one ? O SN5 .   C1  ? ? ? 1_555 P 58Y .   O4 ? ? B SN5 604 B 58Y 605 1_555 ? ? ? ? ? ? ? 1.444 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 142 A . ? PRO 142 A GLY 143 A ? GLY 143 A 1 1.88  
2 GLY 180 A . ? GLY 180 A PHE 181 A ? PHE 181 A 1 0.46  
3 GLU 305 A . ? GLU 305 A PHE 306 A ? PHE 306 A 1 -2.71 
4 TRP 528 A . ? TRP 528 A GLU 529 A ? GLU 529 A 1 -3.95 
5 GLY 180 B . ? GLY 180 B PHE 181 B ? PHE 181 B 1 0.94  
6 GLU 305 B . ? GLU 305 B PHE 306 B ? PHE 306 B 1 -3.84 
7 TRP 528 B . ? TRP 528 B GLU 529 B ? GLU 529 B 1 -2.42 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 9 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 5 ? 
AA9 ? 4 ? 
AB1 ? 2 ? 
AB2 ? 9 ? 
AB3 ? 5 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA5 7 8 ? parallel      
AA5 8 9 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB2 5 6 ? parallel      
AB2 6 7 ? parallel      
AB2 7 8 ? parallel      
AB2 8 9 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? 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 THR A 21  ? ILE A 24  ? THR A 21  ILE A 24  
AA1 2 VAL A 53  ? TRP A 62  ? VAL A 53  TRP A 62  
AA1 3 ARG A 88  ? VAL A 93  ? ARG A 88  VAL A 93  
AA2 1 ASN A 30  ? ALA A 32  ? ASN A 30  ALA A 32  
AA2 2 VAL A 117 ? ALA A 122 ? VAL A 117 ALA A 122 
AA2 3 GLY A 97  ? CYS A 106 ? GLY A 97  CYS A 106 
AA2 4 ILE A 69  ? LEU A 73  ? ILE A 69  LEU A 73  
AA2 5 GLN A 78  ? ASP A 83  ? GLN A 78  ASP A 83  
AA3 1 ASN A 30  ? ALA A 32  ? ASN A 30  ALA A 32  
AA3 2 VAL A 117 ? ALA A 122 ? VAL A 117 ALA A 122 
AA3 3 GLY A 97  ? CYS A 106 ? GLY A 97  CYS A 106 
AA3 4 CYS A 111 ? VAL A 113 ? CYS A 111 VAL A 113 
AA4 1 VAL A 34  ? ILE A 36  ? VAL A 34  ILE A 36  
AA4 2 ILE A 47  ? PRO A 49  ? ILE A 47  PRO A 49  
AA5 1 ILE A 149 ? VAL A 155 ? ILE A 149 VAL A 155 
AA5 2 HIS A 176 ? ILE A 182 ? HIS A 176 ILE A 182 
AA5 3 LYS A 257 ? GLY A 263 ? LYS A 257 GLY A 263 
AA5 4 GLY A 299 ? ASP A 303 ? GLY A 299 ASP A 303 
AA5 5 GLU A 349 ? SER A 355 ? GLU A 349 SER A 355 
AA5 6 LYS A 375 ? MET A 379 ? LYS A 375 MET A 379 
AA5 7 ILE A 428 ? ALA A 433 ? ILE A 428 ALA A 433 
AA5 8 GLY A 524 ? TRP A 528 ? GLY A 524 TRP A 528 
AA5 9 ILE A 149 ? VAL A 155 ? ILE A 149 VAL A 155 
AA6 1 VAL A 467 ? ASP A 469 ? VAL A 467 ASP A 469 
AA6 2 TYR A 435 ? TRP A 439 ? TYR A 435 TRP A 439 
AA6 3 ASP A 500 ? PHE A 504 ? ASP A 500 PHE A 504 
AA6 4 ALA A 490 ? ASP A 495 ? ALA A 490 ASP A 495 
AA6 5 VAL A 481 ? ASP A 485 ? VAL A 481 ASP A 485 
AA7 1 THR B 21  ? ILE B 24  ? THR B 21  ILE B 24  
AA7 2 VAL B 53  ? TRP B 62  ? VAL B 53  TRP B 62  
AA7 3 ARG B 88  ? VAL B 93  ? ARG B 88  VAL B 93  
AA8 1 ASN B 30  ? ALA B 32  ? ASN B 30  ALA B 32  
AA8 2 VAL B 117 ? ALA B 122 ? VAL B 117 ALA B 122 
AA8 3 GLY B 97  ? CYS B 106 ? GLY B 97  CYS B 106 
AA8 4 ILE B 69  ? PHE B 74  ? ILE B 69  PHE B 74  
AA8 5 GLN B 77  ? GLY B 82  ? GLN B 77  GLY B 82  
AA9 1 ASN B 30  ? ALA B 32  ? ASN B 30  ALA B 32  
AA9 2 VAL B 117 ? ALA B 122 ? VAL B 117 ALA B 122 
AA9 3 GLY B 97  ? CYS B 106 ? GLY B 97  CYS B 106 
AA9 4 CYS B 111 ? VAL B 113 ? CYS B 111 VAL B 113 
AB1 1 VAL B 34  ? ILE B 36  ? VAL B 34  ILE B 36  
AB1 2 ILE B 47  ? PRO B 49  ? ILE B 47  PRO B 49  
AB2 1 ILE B 149 ? VAL B 155 ? ILE B 149 VAL B 155 
AB2 2 HIS B 176 ? ILE B 182 ? HIS B 176 ILE B 182 
AB2 3 LYS B 257 ? GLY B 264 ? LYS B 257 GLY B 264 
AB2 4 GLY B 299 ? TRP B 304 ? GLY B 299 TRP B 304 
AB2 5 GLU B 349 ? SER B 355 ? GLU B 349 SER B 355 
AB2 6 LYS B 375 ? MET B 379 ? LYS B 375 MET B 379 
AB2 7 ILE B 428 ? ALA B 433 ? ILE B 428 ALA B 433 
AB2 8 GLY B 524 ? TRP B 528 ? GLY B 524 TRP B 528 
AB2 9 ILE B 149 ? VAL B 155 ? ILE B 149 VAL B 155 
AB3 1 VAL B 467 ? ASP B 469 ? VAL B 467 ASP B 469 
AB3 2 TYR B 435 ? TRP B 439 ? TYR B 435 TRP B 439 
AB3 3 ASP B 500 ? PHE B 504 ? ASP B 500 PHE B 504 
AB3 4 ALA B 490 ? ASP B 495 ? ALA B 490 ASP B 495 
AB3 5 VAL B 481 ? ASP B 485 ? VAL B 481 ASP B 485 
# 
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 VAL A 23  ? N VAL A 23  O ASN A 60  ? O ASN A 60  
AA1 2 3 N VAL A 55  ? N VAL A 55  O ILE A 91  ? O ILE A 91  
AA2 1 2 N TYR A 31  ? N TYR A 31  O LYS A 120 ? O LYS A 120 
AA2 2 3 O VAL A 117 ? O VAL A 117 N MET A 101 ? N MET A 101 
AA2 3 4 O CYS A 106 ? O CYS A 106 N ILE A 69  ? N ILE A 69  
AA2 4 5 N VAL A 72  ? N VAL A 72  O VAL A 79  ? O VAL A 79  
AA3 1 2 N TYR A 31  ? N TYR A 31  O LYS A 120 ? O LYS A 120 
AA3 2 3 O VAL A 117 ? O VAL A 117 N MET A 101 ? N MET A 101 
AA3 3 4 N LEU A 105 ? N LEU A 105 O SER A 112 ? O SER A 112 
AA4 1 2 N GLU A 35  ? N GLU A 35  O LYS A 48  ? O LYS A 48  
AA5 1 2 N PHE A 154 ? N PHE A 154 O LEU A 178 ? O LEU A 178 
AA5 2 3 N ILE A 182 ? N ILE A 182 O SER A 261 ? O SER A 261 
AA5 3 4 N ILE A 262 ? N ILE A 262 O ASP A 301 ? O ASP A 301 
AA5 4 5 N VAL A 300 ? N VAL A 300 O GLU A 349 ? O GLU A 349 
AA5 5 6 N ILE A 354 ? N ILE A 354 O MET A 379 ? O MET A 379 
AA5 6 7 N LEU A 378 ? N LEU A 378 O ILE A 429 ? O ILE A 429 
AA5 7 8 N VAL A 432 ? N VAL A 432 O PHE A 526 ? O PHE A 526 
AA5 8 9 O LEU A 525 ? O LEU A 525 N ILE A 149 ? N ILE A 149 
AA6 1 2 O VAL A 468 ? O VAL A 468 N GLY A 436 ? N GLY A 436 
AA6 2 3 N ARG A 437 ? N ARG A 437 O SER A 503 ? O SER A 503 
AA6 3 4 O ILE A 502 ? O ILE A 502 N VAL A 493 ? N VAL A 493 
AA6 4 5 O ALA A 490 ? O ALA A 490 N ASP A 485 ? N ASP A 485 
AA7 1 2 N VAL B 23  ? N VAL B 23  O ASN B 60  ? O ASN B 60  
AA7 2 3 N VAL B 53  ? N VAL B 53  O VAL B 93  ? O VAL B 93  
AA8 1 2 N TYR B 31  ? N TYR B 31  O LYS B 120 ? O LYS B 120 
AA8 2 3 O VAL B 119 ? O VAL B 119 N PHE B 99  ? N PHE B 99  
AA8 3 4 O LYS B 104 ? O LYS B 104 N TYR B 71  ? N TYR B 71  
AA8 4 5 N ALA B 70  ? N ALA B 70  O GLY B 82  ? O GLY B 82  
AA9 1 2 N TYR B 31  ? N TYR B 31  O LYS B 120 ? O LYS B 120 
AA9 2 3 O VAL B 119 ? O VAL B 119 N PHE B 99  ? N PHE B 99  
AA9 3 4 N LEU B 105 ? N LEU B 105 O SER B 112 ? O SER B 112 
AB1 1 2 N GLU B 35  ? N GLU B 35  O LYS B 48  ? O LYS B 48  
AB2 1 2 N ALA B 152 ? N ALA B 152 O LEU B 178 ? O LEU B 178 
AB2 2 3 N ILE B 182 ? N ILE B 182 O SER B 261 ? O SER B 261 
AB2 3 4 N ILE B 262 ? N ILE B 262 O ASP B 301 ? O ASP B 301 
AB2 4 5 N VAL B 300 ? N VAL B 300 O THR B 351 ? O THR B 351 
AB2 5 6 N ILE B 354 ? N ILE B 354 O MET B 379 ? O MET B 379 
AB2 6 7 N ILE B 376 ? N ILE B 376 O ILE B 429 ? O ILE B 429 
AB2 7 8 N VAL B 432 ? N VAL B 432 O PHE B 526 ? O PHE B 526 
AB2 8 9 O LEU B 525 ? O LEU B 525 N ILE B 149 ? N ILE B 149 
AB3 1 2 O VAL B 468 ? O VAL B 468 N GLY B 436 ? N GLY B 436 
AB3 2 3 N ARG B 437 ? N ARG B 437 O SER B 503 ? O SER B 503 
AB3 3 4 O ILE B 502 ? O ILE B 502 N VAL B 493 ? N VAL B 493 
AB3 4 5 O ALA B 490 ? O ALA B 490 N ASP B 485 ? N ASP B 485 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A NAG 601 ? 5  'binding site for residue NAG A 601'                            
AC2 Software A NAG 602 ? 8  'binding site for residue NAG A 602'                            
AC3 Software A NAG 603 ? 6  'binding site for residue NAG A 603'                            
AC4 Software A CL  606 ? 1  'binding site for residue CL A 606'                             
AC5 Software A SO4 607 ? 2  'binding site for residue SO4 A 607'                            
AC6 Software A SO4 608 ? 3  'binding site for residue SO4 A 608'                            
AC7 Software A SO4 609 ? 3  'binding site for residue SO4 A 609'                            
AC8 Software B NAG 601 ? 5  'binding site for residue NAG B 601'                            
AC9 Software B NAG 602 ? 7  'binding site for residue NAG B 602'                            
AD1 Software B SO4 606 ? 2  'binding site for residue SO4 B 606'                            
AD2 Software B SO4 607 ? 3  'binding site for residue SO4 B 607'                            
AD3 Software B NAG 603 ? 2  'binding site for Mono-Saccharide NAG B 603 bound to ASN B 444' 
AD4 Software A SN5 604 ? 15 'binding site for residues SN5 A 604 and 58Y A 605'             
AD5 Software B SN5 604 ? 14 'binding site for residues SN5 B 604 and 58Y B 605'             
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5  ASP A 125 ? ASP A 125 . ? 1_555 ? 
2  AC1 5  LYS A 250 ? LYS A 250 . ? 1_555 ? 
3  AC1 5  LYS A 295 ? LYS A 295 . ? 1_555 ? 
4  AC1 5  ASP A 298 ? ASP A 298 . ? 1_555 ? 
5  AC1 5  ARG A 346 ? ARG A 346 . ? 1_555 ? 
6  AC2 8  TRP A 26  ? TRP A 26  . ? 1_555 ? 
7  AC2 8  ASP A 28  ? ASP A 28  . ? 1_555 ? 
8  AC2 8  ARG A 29  ? ARG A 29  . ? 1_555 ? 
9  AC2 8  ASN A 30  ? ASN A 30  . ? 1_555 ? 
10 AC2 8  TRP A 235 ? TRP A 235 . ? 1_555 ? 
11 AC2 8  ASN A 236 ? ASN A 236 . ? 1_555 ? 
12 AC2 8  GLU B 133 ? GLU B 133 . ? 1_555 ? 
13 AC2 8  TRP B 136 ? TRP B 136 . ? 1_555 ? 
14 AC3 6  TRP A 265 ? TRP A 265 . ? 1_555 ? 
15 AC3 6  ASP A 382 ? ASP A 382 . ? 1_555 ? 
16 AC3 6  TRP A 387 ? TRP A 387 . ? 1_555 ? 
17 AC3 6  ARG A 437 ? ARG A 437 . ? 1_555 ? 
18 AC3 6  SN5 F .   ? SN5 A 604 . ? 1_555 ? 
19 AC3 6  58Y G .   ? 58Y A 605 . ? 1_555 ? 
20 AC4 1  VAL A 53  ? VAL A 53  . ? 1_555 ? 
21 AC5 2  PRO A 49  ? PRO A 49  . ? 1_555 ? 
22 AC5 2  GLU A 289 ? GLU A 289 . ? 1_555 ? 
23 AC6 3  ARG A 211 ? ARG A 211 . ? 1_555 ? 
24 AC6 3  LYS A 215 ? LYS A 215 . ? 1_555 ? 
25 AC6 3  GLU A 289 ? GLU A 289 . ? 1_555 ? 
26 AC7 3  TRP A 80  ? TRP A 80  . ? 1_555 ? 
27 AC7 3  ALA A 89  ? ALA A 89  . ? 1_555 ? 
28 AC7 3  THR A 90  ? THR A 90  . ? 1_555 ? 
29 AC8 5  ASP B 382 ? ASP B 382 . ? 1_555 ? 
30 AC8 5  TRP B 387 ? TRP B 387 . ? 1_555 ? 
31 AC8 5  ARG B 437 ? ARG B 437 . ? 1_555 ? 
32 AC8 5  SN5 O .   ? SN5 B 604 . ? 1_555 ? 
33 AC8 5  58Y P .   ? 58Y B 605 . ? 1_555 ? 
34 AC9 7  TYR B 358 ? TYR B 358 . ? 1_555 ? 
35 AC9 7  PHE B 383 ? PHE B 383 . ? 1_555 ? 
36 AC9 7  LYS B 384 ? LYS B 384 . ? 1_555 ? 
37 AC9 7  ASP B 391 ? ASP B 391 . ? 1_555 ? 
38 AC9 7  GLU B 407 ? GLU B 407 . ? 1_555 ? 
39 AC9 7  LEU B 408 ? LEU B 408 . ? 1_555 ? 
40 AC9 7  TYR B 409 ? TYR B 409 . ? 1_555 ? 
41 AD1 2  LYS B 168 ? LYS B 168 . ? 1_555 ? 
42 AD1 2  ARG B 471 ? ARG B 471 . ? 1_555 ? 
43 AD2 3  ARG B 211 ? ARG B 211 . ? 1_555 ? 
44 AD2 3  SER B 286 ? SER B 286 . ? 1_555 ? 
45 AD2 3  GLU B 289 ? GLU B 289 . ? 1_555 ? 
46 AD3 2  ASN B 444 ? ASN B 444 . ? 1_555 ? 
47 AD3 2  THR B 454 ? THR B 454 . ? 1_555 ? 
48 AD4 15 TYR A 153 ? TYR A 153 . ? 1_555 ? 
49 AD4 15 PHE A 181 ? PHE A 181 . ? 1_555 ? 
50 AD4 15 ILE A 197 ? ILE A 197 . ? 1_555 ? 
51 AD4 15 TRP A 265 ? TRP A 265 . ? 1_555 ? 
52 AD4 15 THR A 266 ? THR A 266 . ? 1_555 ? 
53 AD4 15 GLU A 305 ? GLU A 305 . ? 1_555 ? 
54 AD4 15 MET A 379 ? MET A 379 . ? 1_555 ? 
55 AD4 15 TYR A 381 ? TYR A 381 . ? 1_555 ? 
56 AD4 15 ASP A 382 ? ASP A 382 . ? 1_555 ? 
57 AD4 15 TYR A 435 ? TYR A 435 . ? 1_555 ? 
58 AD4 15 ARG A 437 ? ARG A 437 . ? 1_555 ? 
59 AD4 15 VAL A 467 ? VAL A 467 . ? 1_555 ? 
60 AD4 15 TRP A 528 ? TRP A 528 . ? 1_555 ? 
61 AD4 15 GLU A 529 ? GLU A 529 . ? 1_555 ? 
62 AD4 15 NAG E .   ? NAG A 603 . ? 1_555 ? 
63 AD5 14 TYR B 153 ? TYR B 153 . ? 1_555 ? 
64 AD5 14 PHE B 181 ? PHE B 181 . ? 1_555 ? 
65 AD5 14 ILE B 197 ? ILE B 197 . ? 1_555 ? 
66 AD5 14 TRP B 265 ? TRP B 265 . ? 1_555 ? 
67 AD5 14 THR B 266 ? THR B 266 . ? 1_555 ? 
68 AD5 14 GLU B 305 ? GLU B 305 . ? 1_555 ? 
69 AD5 14 MET B 379 ? MET B 379 . ? 1_555 ? 
70 AD5 14 TYR B 381 ? TYR B 381 . ? 1_555 ? 
71 AD5 14 ASP B 382 ? ASP B 382 . ? 1_555 ? 
72 AD5 14 TYR B 435 ? TYR B 435 . ? 1_555 ? 
73 AD5 14 VAL B 467 ? VAL B 467 . ? 1_555 ? 
74 AD5 14 TRP B 528 ? TRP B 528 . ? 1_555 ? 
75 AD5 14 GLU B 529 ? GLU B 529 . ? 1_555 ? 
76 AD5 14 NAG L .   ? NAG B 601 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5DF0 
_atom_sites.fract_transf_matrix[1][1]   0.010340 
_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]   0.008868 
_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]   0.007717 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
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   . ILE A 1 18  ? -51.220  24.389  263.866 1.00 43.39  ? 18  ILE A N   1 
ATOM   2    C  CA  . ILE A 1 18  ? -52.404  24.532  264.701 1.00 37.86  ? 18  ILE A CA  1 
ATOM   3    C  C   . ILE A 1 18  ? -51.990  24.737  266.154 1.00 34.44  ? 18  ILE A C   1 
ATOM   4    O  O   . ILE A 1 18  ? -50.905  24.315  266.556 1.00 40.50  ? 18  ILE A O   1 
ATOM   5    C  CB  . ILE A 1 18  ? -53.338  23.312  264.559 1.00 42.40  ? 18  ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 18  ? -52.687  22.063  265.157 1.00 59.57  ? 18  ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 18  ? -53.696  23.084  263.099 1.00 51.39  ? 18  ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 18  ? -53.643  20.905  265.338 1.00 42.57  ? 18  ILE A CD1 1 
ATOM   9    N  N   . PRO A 1 19  ? -52.840  25.392  266.940 1.00 34.79  ? 19  PRO A N   1 
ATOM   10   C  CA  . PRO A 1 19  ? -52.556  25.540  268.370 1.00 35.76  ? 19  PRO A CA  1 
ATOM   11   C  C   . PRO A 1 19  ? -52.577  24.192  269.073 1.00 37.81  ? 19  PRO A C   1 
ATOM   12   O  O   . PRO A 1 19  ? -52.893  23.151  268.494 1.00 38.61  ? 19  PRO A O   1 
ATOM   13   C  CB  . PRO A 1 19  ? -53.681  26.449  268.877 1.00 39.30  ? 19  PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 19  ? -54.244  27.094  267.659 1.00 50.02  ? 19  PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 19  ? -54.064  26.110  266.547 1.00 46.43  ? 19  PRO A CD  1 
ATOM   16   N  N   . GLY A 1 20  ? -52.231  24.229  270.356 1.00 41.97  ? 20  GLY A N   1 
ATOM   17   C  CA  . GLY A 1 20  ? -52.221  23.010  271.140 1.00 39.64  ? 20  GLY A CA  1 
ATOM   18   C  C   . GLY A 1 20  ? -53.610  22.422  271.290 1.00 36.51  ? 20  GLY A C   1 
ATOM   19   O  O   . GLY A 1 20  ? -54.622  23.122  271.219 1.00 37.76  ? 20  GLY A O   1 
ATOM   20   N  N   . THR A 1 21  ? -53.654  21.114  271.489 1.00 37.80  ? 21  THR A N   1 
ATOM   21   C  CA  . THR A 1 21  ? -54.926  20.443  271.719 1.00 32.01  ? 21  THR A CA  1 
ATOM   22   C  C   . THR A 1 21  ? -55.461  20.823  273.094 1.00 32.59  ? 21  THR A C   1 
ATOM   23   O  O   . THR A 1 21  ? -54.756  20.645  274.097 1.00 34.56  ? 21  THR A O   1 
ATOM   24   C  CB  . THR A 1 21  ? -54.773  18.926  271.593 1.00 34.01  ? 21  THR A CB  1 
ATOM   25   O  OG1 . THR A 1 21  ? -55.956  18.279  272.078 1.00 34.08  ? 21  THR A OG1 1 
ATOM   26   C  CG2 . THR A 1 21  ? -53.556  18.421  272.362 1.00 46.75  ? 21  THR A CG2 1 
ATOM   27   N  N   . PRO A 1 22  ? -56.670  21.362  273.192 1.00 30.88  ? 22  PRO A N   1 
ATOM   28   C  CA  . PRO A 1 22  ? -57.203  21.739  274.502 1.00 29.81  ? 22  PRO A CA  1 
ATOM   29   C  C   . PRO A 1 22  ? -57.830  20.553  275.214 1.00 27.75  ? 22  PRO A C   1 
ATOM   30   O  O   . PRO A 1 22  ? -58.399  19.650  274.597 1.00 25.27  ? 22  PRO A O   1 
ATOM   31   C  CB  . PRO A 1 22  ? -58.252  22.806  274.162 1.00 27.18  ? 22  PRO A CB  1 
ATOM   32   C  CG  . PRO A 1 22  ? -58.596  22.586  272.700 1.00 26.53  ? 22  PRO A CG  1 
ATOM   33   C  CD  . PRO A 1 22  ? -57.650  21.572  272.115 1.00 27.96  ? 22  PRO A CD  1 
ATOM   34   N  N   . VAL A 1 23  ? -57.703  20.560  276.538 1.00 27.49  ? 23  VAL A N   1 
ATOM   35   C  CA  . VAL A 1 23  ? -58.239  19.503  277.387 1.00 26.59  ? 23  VAL A CA  1 
ATOM   36   C  C   . VAL A 1 23  ? -59.085  20.162  278.465 1.00 25.33  ? 23  VAL A C   1 
ATOM   37   O  O   . VAL A 1 23  ? -58.548  20.806  279.374 1.00 24.69  ? 23  VAL A O   1 
ATOM   38   C  CB  . VAL A 1 23  ? -57.140  18.640  278.016 1.00 27.57  ? 23  VAL A CB  1 
ATOM   39   C  CG1 . VAL A 1 23  ? -57.762  17.619  278.950 1.00 32.39  ? 23  VAL A CG1 1 
ATOM   40   C  CG2 . VAL A 1 23  ? -56.319  17.954  276.935 1.00 32.97  ? 23  VAL A CG2 1 
ATOM   41   N  N   . ILE A 1 24  ? -60.403  19.990  278.374 1.00 26.16  ? 24  ILE A N   1 
ATOM   42   C  CA  . ILE A 1 24  ? -61.312  20.596  279.337 1.00 28.02  ? 24  ILE A CA  1 
ATOM   43   C  C   . ILE A 1 24  ? -61.128  19.934  280.695 1.00 26.46  ? 24  ILE A C   1 
ATOM   44   O  O   . ILE A 1 24  ? -61.209  18.705  280.822 1.00 25.87  ? 24  ILE A O   1 
ATOM   45   C  CB  . ILE A 1 24  ? -62.762  20.477  278.848 1.00 29.08  ? 24  ILE A CB  1 
ATOM   46   C  CG1 . ILE A 1 24  ? -62.911  21.120  277.469 1.00 29.17  ? 24  ILE A CG1 1 
ATOM   47   C  CG2 . ILE A 1 24  ? -63.708  21.128  279.833 1.00 28.39  ? 24  ILE A CG2 1 
ATOM   48   C  CD1 . ILE A 1 24  ? -64.321  21.086  276.929 1.00 22.57  ? 24  ILE A CD1 1 
ATOM   49   N  N   . ASP A 1 25  ? -60.876  20.746  281.718 1.00 24.60  ? 25  ASP A N   1 
ATOM   50   C  CA  . ASP A 1 25  ? -60.696  20.224  283.064 1.00 26.77  ? 25  ASP A CA  1 
ATOM   51   C  C   . ASP A 1 25  ? -61.994  19.614  283.581 1.00 30.29  ? 25  ASP A C   1 
ATOM   52   O  O   . ASP A 1 25  ? -63.094  20.019  283.199 1.00 32.81  ? 25  ASP A O   1 
ATOM   53   C  CB  . ASP A 1 25  ? -60.228  21.329  284.009 1.00 31.02  ? 25  ASP A CB  1 
ATOM   54   C  CG  . ASP A 1 25  ? -58.989  22.040  283.505 1.00 51.07  ? 25  ASP A CG  1 
ATOM   55   O  OD1 . ASP A 1 25  ? -58.224  21.427  282.731 1.00 51.58  ? 25  ASP A OD1 1 
ATOM   56   O  OD2 . ASP A 1 25  ? -58.779  23.211  283.884 1.00 37.85  ? 25  ASP A OD2 1 
ATOM   57   N  N   . TRP A 1 26  ? -61.855  18.627  284.462 1.00 32.33  ? 26  TRP A N   1 
ATOM   58   C  CA  . TRP A 1 26  ? -63.014  17.926  284.991 1.00 28.46  ? 26  TRP A CA  1 
ATOM   59   C  C   . TRP A 1 26  ? -63.696  18.749  286.074 1.00 30.69  ? 26  TRP A C   1 
ATOM   60   O  O   . TRP A 1 26  ? -63.039  19.342  286.934 1.00 30.19  ? 26  TRP A O   1 
ATOM   61   C  CB  . TRP A 1 26  ? -62.615  16.562  285.555 1.00 29.18  ? 26  TRP A CB  1 
ATOM   62   C  CG  . TRP A 1 26  ? -63.792  15.770  286.037 1.00 28.76  ? 26  TRP A CG  1 
ATOM   63   C  CD1 . TRP A 1 26  ? -64.538  14.887  285.312 1.00 30.65  ? 26  TRP A CD1 1 
ATOM   64   C  CD2 . TRP A 1 26  ? -64.372  15.802  287.347 1.00 32.94  ? 26  TRP A CD2 1 
ATOM   65   N  NE1 . TRP A 1 26  ? -65.540  14.362  286.090 1.00 38.20  ? 26  TRP A NE1 1 
ATOM   66   C  CE2 . TRP A 1 26  ? -65.461  14.908  287.344 1.00 36.59  ? 26  TRP A CE2 1 
ATOM   67   C  CE3 . TRP A 1 26  ? -64.074  16.498  288.523 1.00 35.97  ? 26  TRP A CE3 1 
ATOM   68   C  CZ2 . TRP A 1 26  ? -66.252  14.692  288.471 1.00 38.92  ? 26  TRP A CZ2 1 
ATOM   69   C  CZ3 . TRP A 1 26  ? -64.861  16.281  289.640 1.00 46.58  ? 26  TRP A CZ3 1 
ATOM   70   C  CH2 . TRP A 1 26  ? -65.937  15.386  289.606 1.00 42.97  ? 26  TRP A CH2 1 
ATOM   71   N  N   . ALA A 1 27  ? -65.024  18.771  286.027 1.00 35.60  ? 27  ALA A N   1 
ATOM   72   C  CA  . ALA A 1 27  ? -65.851  19.450  287.016 1.00 35.03  ? 27  ALA A CA  1 
ATOM   73   C  C   . ALA A 1 27  ? -67.285  18.984  286.812 1.00 33.95  ? 27  ALA A C   1 
ATOM   74   O  O   . ALA A 1 27  ? -67.622  18.387  285.786 1.00 33.23  ? 27  ALA A O   1 
ATOM   75   C  CB  . ALA A 1 27  ? -65.746  20.973  286.900 1.00 36.03  ? 27  ALA A CB  1 
ATOM   76   N  N   . ASP A 1 28  ? -68.127  19.260  287.804 1.00 36.63  ? 28  ASP A N   1 
ATOM   77   C  CA  . ASP A 1 28  ? -69.541  18.929  287.691 1.00 40.67  ? 28  ASP A CA  1 
ATOM   78   C  C   . ASP A 1 28  ? -70.222  19.904  286.741 1.00 37.93  ? 28  ASP A C   1 
ATOM   79   O  O   . ASP A 1 28  ? -70.234  21.115  286.985 1.00 63.40  ? 28  ASP A O   1 
ATOM   80   C  CB  . ASP A 1 28  ? -70.216  18.961  289.059 1.00 49.01  ? 28  ASP A CB  1 
ATOM   81   C  CG  . ASP A 1 28  ? -71.730  18.973  288.955 1.00 54.62  ? 28  ASP A CG  1 
ATOM   82   O  OD1 . ASP A 1 28  ? -72.291  18.039  288.345 1.00 72.82  ? 28  ASP A OD1 1 
ATOM   83   O  OD2 . ASP A 1 28  ? -72.358  19.916  289.481 1.00 45.44  ? 28  ASP A OD2 1 
ATOM   84   N  N   . ARG A 1 29  ? -70.792  19.378  285.660 1.00 35.33  ? 29  ARG A N   1 
ATOM   85   C  CA  . ARG A 1 29  ? -71.490  20.185  284.670 1.00 31.85  ? 29  ARG A CA  1 
ATOM   86   C  C   . ARG A 1 29  ? -72.978  19.857  284.623 1.00 32.03  ? 29  ARG A C   1 
ATOM   87   O  O   . ARG A 1 29  ? -73.618  19.970  283.575 1.00 29.62  ? 29  ARG A O   1 
ATOM   88   C  CB  . ARG A 1 29  ? -70.835  20.015  283.301 1.00 28.23  ? 29  ARG A CB  1 
ATOM   89   C  CG  . ARG A 1 29  ? -69.474  20.682  283.255 1.00 33.22  ? 29  ARG A CG  1 
ATOM   90   C  CD  . ARG A 1 29  ? -68.640  20.287  282.057 1.00 37.13  ? 29  ARG A CD  1 
ATOM   91   N  NE  . ARG A 1 29  ? -67.387  21.035  282.061 1.00 44.25  ? 29  ARG A NE  1 
ATOM   92   C  CZ  . ARG A 1 29  ? -66.290  20.647  282.703 1.00 45.34  ? 29  ARG A CZ  1 
ATOM   93   N  NH1 . ARG A 1 29  ? -66.289  19.512  283.388 1.00 49.01  ? 29  ARG A NH1 1 
ATOM   94   N  NH2 . ARG A 1 29  ? -65.196  21.394  282.663 1.00 31.67  ? 29  ARG A NH2 1 
ATOM   95   N  N   . ASN A 1 30  ? -73.533  19.448  285.761 1.00 33.22  ? 30  ASN A N   1 
ATOM   96   C  CA  . ASN A 1 30  ? -74.971  19.270  285.931 1.00 33.00  ? 30  ASN A CA  1 
ATOM   97   C  C   . ASN A 1 30  ? -75.502  20.534  286.595 1.00 35.35  ? 30  ASN A C   1 
ATOM   98   O  O   . ASN A 1 30  ? -75.308  20.747  287.795 1.00 29.36  ? 30  ASN A O   1 
ATOM   99   C  CB  . ASN A 1 30  ? -75.276  18.028  286.761 1.00 41.53  ? 30  ASN A CB  1 
ATOM   100  C  CG  . ASN A 1 30  ? -74.877  16.747  286.059 1.00 45.07  ? 30  ASN A CG  1 
ATOM   101  O  OD1 . ASN A 1 30  ? -73.915  16.720  285.293 1.00 44.97  ? 30  ASN A OD1 1 
ATOM   102  N  ND2 . ASN A 1 30  ? -75.618  15.676  286.316 1.00 57.74  ? 30  ASN A ND2 1 
ATOM   103  N  N   . TYR A 1 31  ? -76.163  21.377  285.810 1.00 31.66  ? 31  TYR A N   1 
ATOM   104  C  CA  . TYR A 1 31  ? -76.662  22.658  286.280 1.00 30.24  ? 31  TYR A CA  1 
ATOM   105  C  C   . TYR A 1 31  ? -78.182  22.633  286.370 1.00 26.89  ? 31  TYR A C   1 
ATOM   106  O  O   . TYR A 1 31  ? -78.854  21.830  285.717 1.00 26.37  ? 31  TYR A O   1 
ATOM   107  C  CB  . TYR A 1 31  ? -76.205  23.791  285.357 1.00 39.36  ? 31  TYR A CB  1 
ATOM   108  C  CG  . TYR A 1 31  ? -74.707  23.996  285.343 1.00 23.57  ? 31  TYR A CG  1 
ATOM   109  C  CD1 . TYR A 1 31  ? -74.042  24.474  286.464 1.00 23.23  ? 31  TYR A CD1 1 
ATOM   110  C  CD2 . TYR A 1 31  ? -73.958  23.713  284.209 1.00 23.60  ? 31  TYR A CD2 1 
ATOM   111  C  CE1 . TYR A 1 31  ? -72.674  24.664  286.457 1.00 23.87  ? 31  TYR A CE1 1 
ATOM   112  C  CE2 . TYR A 1 31  ? -72.590  23.899  284.192 1.00 23.93  ? 31  TYR A CE2 1 
ATOM   113  C  CZ  . TYR A 1 31  ? -71.953  24.375  285.319 1.00 23.28  ? 31  TYR A CZ  1 
ATOM   114  O  OH  . TYR A 1 31  ? -70.590  24.561  285.307 1.00 22.69  ? 31  TYR A OH  1 
ATOM   115  N  N   . ALA A 1 32  ? -78.720  23.529  287.194 1.00 26.67  ? 32  ALA A N   1 
ATOM   116  C  CA  . ALA A 1 32  ? -80.156  23.599  287.426 1.00 28.28  ? 32  ALA A CA  1 
ATOM   117  C  C   . ALA A 1 32  ? -80.587  25.053  287.524 1.00 23.51  ? 32  ALA A C   1 
ATOM   118  O  O   . ALA A 1 32  ? -79.995  25.827  288.282 1.00 25.12  ? 32  ALA A O   1 
ATOM   119  C  CB  . ALA A 1 32  ? -80.546  22.847  288.703 1.00 39.71  ? 32  ALA A CB  1 
ATOM   120  N  N   . LEU A 1 33  ? -81.621  25.420  286.763 1.00 25.50  ? 33  LEU A N   1 
ATOM   121  C  CA  . LEU A 1 33  ? -82.158  26.773  286.842 1.00 25.74  ? 33  LEU A CA  1 
ATOM   122  C  C   . LEU A 1 33  ? -82.950  27.003  288.121 1.00 31.56  ? 33  LEU A C   1 
ATOM   123  O  O   . LEU A 1 33  ? -83.205  28.159  288.476 1.00 37.91  ? 33  LEU A O   1 
ATOM   124  C  CB  . LEU A 1 33  ? -83.035  27.062  285.623 1.00 25.53  ? 33  LEU A CB  1 
ATOM   125  C  CG  . LEU A 1 33  ? -82.290  27.253  284.301 1.00 23.72  ? 33  LEU A CG  1 
ATOM   126  C  CD1 . LEU A 1 33  ? -83.192  26.991  283.104 1.00 22.52  ? 33  LEU A CD1 1 
ATOM   127  C  CD2 . LEU A 1 33  ? -81.703  28.654  284.228 1.00 30.69  ? 33  LEU A CD2 1 
ATOM   128  N  N   . VAL A 1 34  ? -83.353  25.936  288.810 1.00 29.03  ? 34  VAL A N   1 
ATOM   129  C  CA  . VAL A 1 34  ? -84.021  26.017  290.107 1.00 23.08  ? 34  VAL A CA  1 
ATOM   130  C  C   . VAL A 1 34  ? -83.375  24.950  290.984 1.00 22.64  ? 34  VAL A C   1 
ATOM   131  O  O   . VAL A 1 34  ? -83.713  23.766  290.881 1.00 23.85  ? 34  VAL A O   1 
ATOM   132  C  CB  . VAL A 1 34  ? -85.538  25.806  290.007 1.00 22.01  ? 34  VAL A CB  1 
ATOM   133  C  CG1 . VAL A 1 34  ? -86.185  25.909  291.377 1.00 21.65  ? 34  VAL A CG1 1 
ATOM   134  C  CG2 . VAL A 1 34  ? -86.163  26.815  289.053 1.00 27.55  ? 34  VAL A CG2 1 
ATOM   135  N  N   . GLU A 1 35  ? -82.453  25.360  291.851 1.00 22.32  ? 35  GLU A N   1 
ATOM   136  C  CA  . GLU A 1 35  ? -81.818  24.410  292.754 1.00 22.68  ? 35  GLU A CA  1 
ATOM   137  C  C   . GLU A 1 35  ? -82.824  23.867  293.760 1.00 22.23  ? 35  GLU A C   1 
ATOM   138  O  O   . GLU A 1 35  ? -83.804  24.527  294.113 1.00 24.52  ? 35  GLU A O   1 
ATOM   139  C  CB  . GLU A 1 35  ? -80.654  25.059  293.501 1.00 30.66  ? 35  GLU A CB  1 
ATOM   140  C  CG  . GLU A 1 35  ? -79.479  25.486  292.640 1.00 39.34  ? 35  GLU A CG  1 
ATOM   141  C  CD  . GLU A 1 35  ? -78.305  25.953  293.482 1.00 40.69  ? 35  GLU A CD  1 
ATOM   142  O  OE1 . GLU A 1 35  ? -78.244  25.576  294.670 1.00 47.54  ? 35  GLU A OE1 1 
ATOM   143  O  OE2 . GLU A 1 35  ? -77.436  26.681  292.960 1.00 44.14  ? 35  GLU A OE2 1 
ATOM   144  N  N   . ILE A 1 36  ? -82.563  22.650  294.228 1.00 20.23  ? 36  ILE A N   1 
ATOM   145  C  CA  . ILE A 1 36  ? -83.391  21.982  295.223 1.00 21.69  ? 36  ILE A CA  1 
ATOM   146  C  C   . ILE A 1 36  ? -82.490  21.545  296.368 1.00 22.15  ? 36  ILE A C   1 
ATOM   147  O  O   . ILE A 1 36  ? -81.596  20.713  296.176 1.00 25.06  ? 36  ILE A O   1 
ATOM   148  C  CB  . ILE A 1 36  ? -84.139  20.774  294.637 1.00 23.54  ? 36  ILE A CB  1 
ATOM   149  C  CG1 . ILE A 1 36  ? -85.066  21.216  293.504 1.00 24.05  ? 36  ILE A CG1 1 
ATOM   150  C  CG2 . ILE A 1 36  ? -84.917  20.058  295.725 1.00 22.83  ? 36  ILE A CG2 1 
ATOM   151  C  CD1 . ILE A 1 36  ? -86.126  22.200  293.938 1.00 47.52  ? 36  ILE A CD1 1 
ATOM   152  N  N   . ASN A 1 37  ? -82.716  22.111  297.549 1.00 22.65  ? 37  ASN A N   1 
ATOM   153  C  CA  . ASN A 1 37  ? -82.010  21.691  298.753 1.00 22.82  ? 37  ASN A CA  1 
ATOM   154  C  C   . ASN A 1 37  ? -82.750  20.484  299.316 1.00 25.52  ? 37  ASN A C   1 
ATOM   155  O  O   . ASN A 1 37  ? -83.883  20.608  299.790 1.00 42.79  ? 37  ASN A O   1 
ATOM   156  C  CB  . ASN A 1 37  ? -81.943  22.844  299.753 1.00 25.23  ? 37  ASN A CB  1 
ATOM   157  C  CG  . ASN A 1 37  ? -81.292  22.460  301.081 1.00 34.20  ? 37  ASN A CG  1 
ATOM   158  O  OD1 . ASN A 1 37  ? -81.171  21.286  301.429 1.00 37.38  ? 37  ASN A OD1 1 
ATOM   159  N  ND2 . ASN A 1 37  ? -80.867  23.469  301.832 1.00 34.45  ? 37  ASN A ND2 1 
ATOM   160  N  N   . TYR A 1 38  ? -82.113  19.316  299.264 1.00 24.94  ? 38  TYR A N   1 
ATOM   161  C  CA  . TYR A 1 38  ? -82.745  18.071  299.679 1.00 27.42  ? 38  TYR A CA  1 
ATOM   162  C  C   . TYR A 1 38  ? -82.664  17.827  301.181 1.00 28.38  ? 38  TYR A C   1 
ATOM   163  O  O   . TYR A 1 38  ? -83.033  16.740  301.638 1.00 28.29  ? 38  TYR A O   1 
ATOM   164  C  CB  . TYR A 1 38  ? -82.126  16.894  298.921 1.00 25.99  ? 38  TYR A CB  1 
ATOM   165  C  CG  . TYR A 1 38  ? -82.580  16.810  297.484 1.00 22.32  ? 38  TYR A CG  1 
ATOM   166  C  CD1 . TYR A 1 38  ? -83.700  16.070  297.133 1.00 23.99  ? 38  TYR A CD1 1 
ATOM   167  C  CD2 . TYR A 1 38  ? -81.897  17.481  296.478 1.00 22.27  ? 38  TYR A CD2 1 
ATOM   168  C  CE1 . TYR A 1 38  ? -84.124  15.993  295.822 1.00 25.63  ? 38  TYR A CE1 1 
ATOM   169  C  CE2 . TYR A 1 38  ? -82.314  17.410  295.163 1.00 24.12  ? 38  TYR A CE2 1 
ATOM   170  C  CZ  . TYR A 1 38  ? -83.428  16.665  294.841 1.00 27.18  ? 38  TYR A CZ  1 
ATOM   171  O  OH  . TYR A 1 38  ? -83.851  16.588  293.535 1.00 25.64  ? 38  TYR A OH  1 
ATOM   172  N  N   . GLU A 1 39  ? -82.194  18.805  301.955 1.00 31.25  ? 39  GLU A N   1 
ATOM   173  C  CA  . GLU A 1 39  ? -82.195  18.711  303.407 1.00 29.77  ? 39  GLU A CA  1 
ATOM   174  C  C   . GLU A 1 39  ? -83.129  19.711  304.070 1.00 29.35  ? 39  GLU A C   1 
ATOM   175  O  O   . GLU A 1 39  ? -83.323  19.637  305.288 1.00 30.74  ? 39  GLU A O   1 
ATOM   176  C  CB  . GLU A 1 39  ? -80.774  18.907  303.961 1.00 34.27  ? 39  GLU A CB  1 
ATOM   177  C  CG  . GLU A 1 39  ? -79.776  17.834  303.545 1.00 42.67  ? 39  GLU A CG  1 
ATOM   178  C  CD  . GLU A 1 39  ? -79.052  18.167  302.254 1.00 64.26  ? 39  GLU A CD  1 
ATOM   179  O  OE1 . GLU A 1 39  ? -79.368  19.207  301.641 1.00 45.50  ? 39  GLU A OE1 1 
ATOM   180  O  OE2 . GLU A 1 39  ? -78.159  17.390  301.855 1.00 47.34  ? 39  GLU A OE2 1 
ATOM   181  N  N   . ALA A 1 40  ? -83.714  20.631  303.310 1.00 25.46  ? 40  ALA A N   1 
ATOM   182  C  CA  . ALA A 1 40  ? -84.545  21.674  303.884 1.00 26.46  ? 40  ALA A CA  1 
ATOM   183  C  C   . ALA A 1 40  ? -85.965  21.172  304.129 1.00 31.93  ? 40  ALA A C   1 
ATOM   184  O  O   . ALA A 1 40  ? -86.437  20.218  303.504 1.00 41.07  ? 40  ALA A O   1 
ATOM   185  C  CB  . ALA A 1 40  ? -84.578  22.899  302.969 1.00 29.46  ? 40  ALA A CB  1 
ATOM   186  N  N   . THR A 1 41  ? -86.644  21.834  305.064 1.00 35.78  ? 41  THR A N   1 
ATOM   187  C  CA  . THR A 1 41  ? -88.044  21.566  305.362 1.00 29.35  ? 41  THR A CA  1 
ATOM   188  C  C   . THR A 1 41  ? -88.967  22.718  305.005 1.00 26.92  ? 41  THR A C   1 
ATOM   189  O  O   . THR A 1 41  ? -90.124  22.479  304.656 1.00 27.92  ? 41  THR A O   1 
ATOM   190  C  CB  . THR A 1 41  ? -88.222  21.236  306.850 1.00 40.35  ? 41  THR A CB  1 
ATOM   191  O  OG1 . THR A 1 41  ? -87.385  22.094  307.636 1.00 49.27  ? 41  THR A OG1 1 
ATOM   192  C  CG2 . THR A 1 41  ? -87.848  19.788  307.124 1.00 33.98  ? 41  THR A CG2 1 
ATOM   193  N  N   . ALA A 1 42  ? -88.485  23.955  305.084 1.00 28.96  ? 42  ALA A N   1 
ATOM   194  C  CA  . ALA A 1 42  ? -89.285  25.112  304.721 1.00 25.79  ? 42  ALA A CA  1 
ATOM   195  C  C   . ALA A 1 42  ? -89.205  25.363  303.220 1.00 25.27  ? 42  ALA A C   1 
ATOM   196  O  O   . ALA A 1 42  ? -88.249  24.970  302.548 1.00 26.15  ? 42  ALA A O   1 
ATOM   197  C  CB  . ALA A 1 42  ? -88.823  26.351  305.487 1.00 27.33  ? 42  ALA A CB  1 
ATOM   198  N  N   . TYR A 1 43  ? -90.230  26.040  302.696 1.00 22.49  ? 43  TYR A N   1 
ATOM   199  C  CA  . TYR A 1 43  ? -90.321  26.233  301.253 1.00 27.76  ? 43  TYR A CA  1 
ATOM   200  C  C   . TYR A 1 43  ? -89.336  27.288  300.763 1.00 31.39  ? 43  TYR A C   1 
ATOM   201  O  O   . TYR A 1 43  ? -88.778  27.159  299.667 1.00 38.13  ? 43  TYR A O   1 
ATOM   202  C  CB  . TYR A 1 43  ? -91.749  26.611  300.862 1.00 23.76  ? 43  TYR A CB  1 
ATOM   203  C  CG  . TYR A 1 43  ? -91.951  26.763  299.371 1.00 21.10  ? 43  TYR A CG  1 
ATOM   204  C  CD1 . TYR A 1 43  ? -92.186  25.656  298.567 1.00 20.31  ? 43  TYR A CD1 1 
ATOM   205  C  CD2 . TYR A 1 43  ? -91.908  28.012  298.768 1.00 21.47  ? 43  TYR A CD2 1 
ATOM   206  C  CE1 . TYR A 1 43  ? -92.370  25.789  297.205 1.00 20.27  ? 43  TYR A CE1 1 
ATOM   207  C  CE2 . TYR A 1 43  ? -92.092  28.155  297.406 1.00 22.39  ? 43  TYR A CE2 1 
ATOM   208  C  CZ  . TYR A 1 43  ? -92.323  27.040  296.630 1.00 19.68  ? 43  TYR A CZ  1 
ATOM   209  O  OH  . TYR A 1 43  ? -92.507  27.176  295.274 1.00 19.39  ? 43  TYR A OH  1 
ATOM   210  N  N   . GLU A 1 44  ? -89.112  28.341  301.553 1.00 35.55  ? 44  GLU A N   1 
ATOM   211  C  CA  . GLU A 1 44  ? -88.205  29.400  301.120 1.00 29.06  ? 44  GLU A CA  1 
ATOM   212  C  C   . GLU A 1 44  ? -86.764  28.915  301.043 1.00 33.60  ? 44  GLU A C   1 
ATOM   213  O  O   . GLU A 1 44  ? -85.978  29.438  300.245 1.00 28.34  ? 44  GLU A O   1 
ATOM   214  C  CB  . GLU A 1 44  ? -88.314  30.604  302.055 1.00 30.89  ? 44  GLU A CB  1 
ATOM   215  C  CG  . GLU A 1 44  ? -89.646  31.325  301.967 1.00 31.29  ? 44  GLU A CG  1 
ATOM   216  C  CD  . GLU A 1 44  ? -89.559  32.771  302.412 1.00 38.32  ? 44  GLU A CD  1 
ATOM   217  O  OE1 . GLU A 1 44  ? -88.733  33.072  303.298 1.00 60.75  ? 44  GLU A OE1 1 
ATOM   218  O  OE2 . GLU A 1 44  ? -90.316  33.607  301.874 1.00 38.42  ? 44  GLU A OE2 1 
ATOM   219  N  N   . ASN A 1 45  ? -86.398  27.926  301.855 1.00 29.76  ? 45  ASN A N   1 
ATOM   220  C  CA  . ASN A 1 45  ? -85.078  27.315  301.796 1.00 30.48  ? 45  ASN A CA  1 
ATOM   221  C  C   . ASN A 1 45  ? -85.071  26.011  301.011 1.00 30.17  ? 45  ASN A C   1 
ATOM   222  O  O   . ASN A 1 45  ? -84.012  25.391  300.874 1.00 29.06  ? 45  ASN A O   1 
ATOM   223  C  CB  . ASN A 1 45  ? -84.542  27.077  303.211 1.00 28.95  ? 45  ASN A CB  1 
ATOM   224  C  CG  . ASN A 1 45  ? -84.548  28.337  304.053 1.00 39.78  ? 45  ASN A CG  1 
ATOM   225  O  OD1 . ASN A 1 45  ? -84.386  29.443  303.536 1.00 37.94  ? 45  ASN A OD1 1 
ATOM   226  N  ND2 . ASN A 1 45  ? -84.732  28.178  305.359 1.00 52.62  ? 45  ASN A ND2 1 
ATOM   227  N  N   . LEU A 1 46  ? -86.224  25.584  300.495 1.00 28.84  ? 46  LEU A N   1 
ATOM   228  C  CA  . LEU A 1 46  ? -86.280  24.379  299.675 1.00 28.48  ? 46  LEU A CA  1 
ATOM   229  C  C   . LEU A 1 46  ? -85.781  24.646  298.261 1.00 24.16  ? 46  LEU A C   1 
ATOM   230  O  O   . LEU A 1 46  ? -84.995  23.865  297.712 1.00 22.67  ? 46  LEU A O   1 
ATOM   231  C  CB  . LEU A 1 46  ? -87.709  23.837  299.631 1.00 23.86  ? 46  LEU A CB  1 
ATOM   232  C  CG  . LEU A 1 46  ? -87.966  22.742  298.593 1.00 23.77  ? 46  LEU A CG  1 
ATOM   233  C  CD1 . LEU A 1 46  ? -87.241  21.461  298.965 1.00 25.02  ? 46  LEU A CD1 1 
ATOM   234  C  CD2 . LEU A 1 46  ? -89.457  22.501  298.413 1.00 28.88  ? 46  LEU A CD2 1 
ATOM   235  N  N   . ILE A 1 47  ? -86.234  25.738  297.654 1.00 23.84  ? 47  ILE A N   1 
ATOM   236  C  CA  . ILE A 1 47  ? -85.950  26.028  296.259 1.00 27.83  ? 47  ILE A CA  1 
ATOM   237  C  C   . ILE A 1 47  ? -85.055  27.256  296.167 1.00 29.04  ? 47  ILE A C   1 
ATOM   238  O  O   . ILE A 1 47  ? -84.974  28.078  297.085 1.00 36.07  ? 47  ILE A O   1 
ATOM   239  C  CB  . ILE A 1 47  ? -87.243  26.236  295.446 1.00 25.62  ? 47  ILE A CB  1 
ATOM   240  C  CG1 . ILE A 1 47  ? -88.006  27.455  295.967 1.00 21.17  ? 47  ILE A CG1 1 
ATOM   241  C  CG2 . ILE A 1 47  ? -88.114  24.993  295.511 1.00 23.71  ? 47  ILE A CG2 1 
ATOM   242  C  CD1 . ILE A 1 47  ? -89.214  27.818  295.136 1.00 29.98  ? 47  ILE A CD1 1 
ATOM   243  N  N   . LYS A 1 48  ? -84.372  27.370  295.032 1.00 24.60  ? 48  LYS A N   1 
ATOM   244  C  CA  . LYS A 1 48  ? -83.524  28.522  294.727 1.00 24.92  ? 48  LYS A CA  1 
ATOM   245  C  C   . LYS A 1 48  ? -83.677  28.842  293.249 1.00 28.01  ? 48  LYS A C   1 
ATOM   246  O  O   . LYS A 1 48  ? -82.861  28.429  292.416 1.00 27.29  ? 48  LYS A O   1 
ATOM   247  C  CB  . LYS A 1 48  ? -82.063  28.246  295.089 1.00 36.77  ? 48  LYS A CB  1 
ATOM   248  C  CG  . LYS A 1 48  ? -81.156  29.462  294.984 1.00 69.37  ? 48  LYS A CG  1 
ATOM   249  C  CD  . LYS A 1 48  ? -79.705  29.099  295.257 1.00 46.67  ? 48  LYS A CD  1 
ATOM   250  C  CE  . LYS A 1 48  ? -78.862  30.340  295.505 1.00 50.34  ? 48  LYS A CE  1 
ATOM   251  N  NZ  . LYS A 1 48  ? -77.459  29.997  295.869 1.00 62.11  ? 48  LYS A NZ  1 
ATOM   252  N  N   . PRO A 1 49  ? -84.733  29.569  292.881 1.00 32.19  ? 49  PRO A N   1 
ATOM   253  C  CA  . PRO A 1 49  ? -84.919  29.930  291.470 1.00 29.20  ? 49  PRO A CA  1 
ATOM   254  C  C   . PRO A 1 49  ? -83.819  30.867  291.001 1.00 32.96  ? 49  PRO A C   1 
ATOM   255  O  O   . PRO A 1 49  ? -83.370  31.746  291.740 1.00 31.61  ? 49  PRO A O   1 
ATOM   256  C  CB  . PRO A 1 49  ? -86.290  30.619  291.452 1.00 29.68  ? 49  PRO A CB  1 
ATOM   257  C  CG  . PRO A 1 49  ? -86.946  30.231  292.746 1.00 27.15  ? 49  PRO A CG  1 
ATOM   258  C  CD  . PRO A 1 49  ? -85.833  30.057  293.726 1.00 34.65  ? 49  PRO A CD  1 
ATOM   259  N  N   . LYS A 1 50  ? -83.384  30.672  289.759 1.00 34.25  ? 50  LYS A N   1 
ATOM   260  C  CA  . LYS A 1 50  ? -82.265  31.420  289.203 1.00 38.43  ? 50  LYS A CA  1 
ATOM   261  C  C   . LYS A 1 50  ? -82.705  32.227  287.994 1.00 42.06  ? 50  LYS A C   1 
ATOM   262  O  O   . LYS A 1 50  ? -83.432  31.725  287.131 1.00 38.27  ? 50  LYS A O   1 
ATOM   263  C  CB  . LYS A 1 50  ? -81.113  30.494  288.811 1.00 36.24  ? 50  LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 50  ? -80.367  29.912  289.989 1.00 34.54  ? 50  LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 50  ? -79.109  29.206  289.531 1.00 33.48  ? 50  LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 50  ? -78.487  28.429  290.667 1.00 37.34  ? 50  LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 50  ? -77.904  29.330  291.699 1.00 43.15  ? 50  LYS A NZ  1 
ATOM   268  N  N   . GLU A 1 51  ? -82.256  33.482  287.949 1.00 49.09  ? 51  GLU A N   1 
ATOM   269  C  CA  . GLU A 1 51  ? -82.398  34.302  286.753 1.00 50.33  ? 51  GLU A CA  1 
ATOM   270  C  C   . GLU A 1 51  ? -81.762  33.619  285.548 1.00 52.70  ? 51  GLU A C   1 
ATOM   271  O  O   . GLU A 1 51  ? -82.348  33.567  284.461 1.00 42.91  ? 51  GLU A O   1 
ATOM   272  C  CB  . GLU A 1 51  ? -81.768  35.680  286.997 1.00 66.17  ? 51  GLU A CB  1 
ATOM   273  C  CG  . GLU A 1 51  ? -80.303  35.665  287.487 1.00 82.19  ? 51  GLU A CG  1 
ATOM   274  C  CD  . GLU A 1 51  ? -80.129  35.168  288.920 1.00 74.37  ? 51  GLU A CD  1 
ATOM   275  O  OE1 . GLU A 1 51  ? -81.145  34.881  289.588 1.00 87.79  ? 51  GLU A OE1 1 
ATOM   276  O  OE2 . GLU A 1 51  ? -78.970  35.042  289.370 1.00 55.07  ? 51  GLU A OE2 1 
ATOM   277  N  N   . GLN A 1 52  ? -80.562  33.075  285.733 1.00 58.81  ? 52  GLN A N   1 
ATOM   278  C  CA  . GLN A 1 52  ? -79.821  32.406  284.675 1.00 36.68  ? 52  GLN A CA  1 
ATOM   279  C  C   . GLN A 1 52  ? -78.908  31.375  285.322 1.00 35.32  ? 52  GLN A C   1 
ATOM   280  O  O   . GLN A 1 52  ? -78.821  31.277  286.549 1.00 39.71  ? 52  GLN A O   1 
ATOM   281  C  CB  . GLN A 1 52  ? -79.015  33.408  283.842 1.00 37.39  ? 52  GLN A CB  1 
ATOM   282  C  CG  . GLN A 1 52  ? -77.911  34.097  284.631 1.00 40.33  ? 52  GLN A CG  1 
ATOM   283  C  CD  . GLN A 1 52  ? -77.413  35.367  283.971 1.00 36.25  ? 52  GLN A CD  1 
ATOM   284  O  OE1 . GLN A 1 52  ? -78.196  36.149  283.433 1.00 36.27  ? 52  GLN A OE1 1 
ATOM   285  N  NE2 . GLN A 1 52  ? -76.103  35.579  284.011 1.00 48.85  ? 52  GLN A NE2 1 
ATOM   286  N  N   . VAL A 1 53  ? -78.219  30.604  284.487 1.00 29.79  ? 53  VAL A N   1 
ATOM   287  C  CA  . VAL A 1 53  ? -77.207  29.665  284.949 1.00 30.97  ? 53  VAL A CA  1 
ATOM   288  C  C   . VAL A 1 53  ? -75.928  29.925  284.168 1.00 25.73  ? 53  VAL A C   1 
ATOM   289  O  O   . VAL A 1 53  ? -75.971  30.281  282.984 1.00 35.63  ? 53  VAL A O   1 
ATOM   290  C  CB  . VAL A 1 53  ? -77.667  28.196  284.808 1.00 30.72  ? 53  VAL A CB  1 
ATOM   291  C  CG1 . VAL A 1 53  ? -77.743  27.778  283.348 1.00 24.24  ? 53  VAL A CG1 1 
ATOM   292  C  CG2 . VAL A 1 53  ? -76.752  27.276  285.597 1.00 28.88  ? 53  VAL A CG2 1 
ATOM   293  N  N   . ASP A 1 54  ? -74.790  29.774  284.837 1.00 24.76  ? 54  ASP A N   1 
ATOM   294  C  CA  . ASP A 1 54  ? -73.485  30.092  284.265 1.00 29.28  ? 54  ASP A CA  1 
ATOM   295  C  C   . ASP A 1 54  ? -72.701  28.795  284.099 1.00 25.12  ? 54  ASP A C   1 
ATOM   296  O  O   . ASP A 1 54  ? -72.193  28.236  285.075 1.00 22.23  ? 54  ASP A O   1 
ATOM   297  C  CB  . ASP A 1 54  ? -72.739  31.090  285.145 1.00 28.85  ? 54  ASP A CB  1 
ATOM   298  C  CG  . ASP A 1 54  ? -73.401  32.452  285.168 1.00 34.18  ? 54  ASP A CG  1 
ATOM   299  O  OD1 . ASP A 1 54  ? -73.325  33.170  284.149 1.00 27.79  ? 54  ASP A OD1 1 
ATOM   300  O  OD2 . ASP A 1 54  ? -74.002  32.802  286.205 1.00 41.27  ? 54  ASP A OD2 1 
ATOM   301  N  N   . VAL A 1 55  ? -72.606  28.322  282.860 1.00 22.27  ? 55  VAL A N   1 
ATOM   302  C  CA  . VAL A 1 55  ? -71.825  27.131  282.545 1.00 22.29  ? 55  VAL A CA  1 
ATOM   303  C  C   . VAL A 1 55  ? -70.354  27.530  282.510 1.00 25.32  ? 55  VAL A C   1 
ATOM   304  O  O   . VAL A 1 55  ? -69.932  28.304  281.648 1.00 46.98  ? 55  VAL A O   1 
ATOM   305  C  CB  . VAL A 1 55  ? -72.263  26.506  281.216 1.00 23.81  ? 55  VAL A CB  1 
ATOM   306  C  CG1 . VAL A 1 55  ? -71.329  25.369  280.832 1.00 28.98  ? 55  VAL A CG1 1 
ATOM   307  C  CG2 . VAL A 1 55  ? -73.696  26.012  281.312 1.00 24.40  ? 55  VAL A CG2 1 
ATOM   308  N  N   . GLN A 1 56  ? -69.573  27.005  283.449 1.00 31.27  ? 56  GLN A N   1 
ATOM   309  C  CA  . GLN A 1 56  ? -68.157  27.321  283.559 1.00 25.99  ? 56  GLN A CA  1 
ATOM   310  C  C   . GLN A 1 56  ? -67.322  26.207  282.943 1.00 26.32  ? 56  GLN A C   1 
ATOM   311  O  O   . GLN A 1 56  ? -67.583  25.022  283.171 1.00 30.64  ? 56  GLN A O   1 
ATOM   312  C  CB  . GLN A 1 56  ? -67.757  27.526  285.021 1.00 26.15  ? 56  GLN A CB  1 
ATOM   313  C  CG  . GLN A 1 56  ? -68.298  28.805  285.636 1.00 28.86  ? 56  GLN A CG  1 
ATOM   314  C  CD  . GLN A 1 56  ? -67.982  28.919  287.114 1.00 38.26  ? 56  GLN A CD  1 
ATOM   315  O  OE1 . GLN A 1 56  ? -67.738  27.918  287.786 1.00 61.94  ? 56  GLN A OE1 1 
ATOM   316  N  NE2 . GLN A 1 56  ? -67.988  30.143  287.628 1.00 42.56  ? 56  GLN A NE2 1 
ATOM   317  N  N   . VAL A 1 57  ? -66.316  26.596  282.162 1.00 26.51  ? 57  VAL A N   1 
ATOM   318  C  CA  . VAL A 1 57  ? -65.426  25.651  281.497 1.00 30.74  ? 57  VAL A CA  1 
ATOM   319  C  C   . VAL A 1 57  ? -64.000  26.177  281.584 1.00 30.26  ? 57  VAL A C   1 
ATOM   320  O  O   . VAL A 1 57  ? -63.750  27.360  281.326 1.00 39.67  ? 57  VAL A O   1 
ATOM   321  C  CB  . VAL A 1 57  ? -65.835  25.415  280.029 1.00 30.15  ? 57  VAL A CB  1 
ATOM   322  C  CG1 . VAL A 1 57  ? -66.113  26.733  279.329 1.00 27.70  ? 57  VAL A CG1 1 
ATOM   323  C  CG2 . VAL A 1 57  ? -64.760  24.632  279.290 1.00 28.95  ? 57  VAL A CG2 1 
ATOM   324  N  N   . SER A 1 58  ? -63.070  25.302  281.961 1.00 27.36  ? 58  SER A N   1 
ATOM   325  C  CA  . SER A 1 58  ? -61.654  25.626  282.016 1.00 29.88  ? 58  SER A CA  1 
ATOM   326  C  C   . SER A 1 58  ? -60.865  24.497  281.372 1.00 30.36  ? 58  SER A C   1 
ATOM   327  O  O   . SER A 1 58  ? -61.299  23.342  281.369 1.00 31.00  ? 58  SER A O   1 
ATOM   328  C  CB  . SER A 1 58  ? -61.182  25.847  283.457 1.00 31.57  ? 58  SER A CB  1 
ATOM   329  O  OG  . SER A 1 58  ? -62.114  26.636  284.177 1.00 33.86  ? 58  SER A OG  1 
ATOM   330  N  N   . TRP A 1 59  ? -59.699  24.835  280.826 1.00 28.71  ? 59  TRP A N   1 
ATOM   331  C  CA  . TRP A 1 59  ? -58.925  23.856  280.080 1.00 28.67  ? 59  TRP A CA  1 
ATOM   332  C  C   . TRP A 1 59  ? -57.439  24.155  280.203 1.00 30.56  ? 59  TRP A C   1 
ATOM   333  O  O   . TRP A 1 59  ? -57.030  25.257  280.577 1.00 31.11  ? 59  TRP A O   1 
ATOM   334  C  CB  . TRP A 1 59  ? -59.336  23.828  278.603 1.00 39.94  ? 59  TRP A CB  1 
ATOM   335  C  CG  . TRP A 1 59  ? -58.996  25.080  277.853 1.00 33.31  ? 59  TRP A CG  1 
ATOM   336  C  CD1 . TRP A 1 59  ? -57.891  25.300  277.083 1.00 30.78  ? 59  TRP A CD1 1 
ATOM   337  C  CD2 . TRP A 1 59  ? -59.768  26.286  277.800 1.00 33.45  ? 59  TRP A CD2 1 
ATOM   338  N  NE1 . TRP A 1 59  ? -57.927  26.567  276.554 1.00 32.54  ? 59  TRP A NE1 1 
ATOM   339  C  CE2 . TRP A 1 59  ? -59.069  27.193  276.979 1.00 35.48  ? 59  TRP A CE2 1 
ATOM   340  C  CE3 . TRP A 1 59  ? -60.982  26.686  278.366 1.00 39.19  ? 59  TRP A CE3 1 
ATOM   341  C  CZ2 . TRP A 1 59  ? -59.544  28.475  276.710 1.00 40.08  ? 59  TRP A CZ2 1 
ATOM   342  C  CZ3 . TRP A 1 59  ? -61.451  27.960  278.099 1.00 31.57  ? 59  TRP A CZ3 1 
ATOM   343  C  CH2 . TRP A 1 59  ? -60.733  28.839  277.279 1.00 31.91  ? 59  TRP A CH2 1 
ATOM   344  N  N   . ASN A 1 60  ? -56.636  23.143  279.885 1.00 31.15  ? 60  ASN A N   1 
ATOM   345  C  CA  . ASN A 1 60  ? -55.192  23.265  279.775 1.00 27.55  ? 60  ASN A CA  1 
ATOM   346  C  C   . ASN A 1 60  ? -54.773  22.884  278.362 1.00 28.95  ? 60  ASN A C   1 
ATOM   347  O  O   . ASN A 1 60  ? -55.499  22.193  277.642 1.00 35.71  ? 60  ASN A O   1 
ATOM   348  C  CB  . ASN A 1 60  ? -54.474  22.382  280.802 1.00 26.76  ? 60  ASN A CB  1 
ATOM   349  C  CG  . ASN A 1 60  ? -54.781  22.784  282.229 1.00 30.73  ? 60  ASN A CG  1 
ATOM   350  O  OD1 . ASN A 1 60  ? -54.903  23.969  282.539 1.00 31.76  ? 60  ASN A OD1 1 
ATOM   351  N  ND2 . ASN A 1 60  ? -54.907  21.798  283.109 1.00 47.41  ? 60  ASN A ND2 1 
ATOM   352  N  N   . VAL A 1 61  ? -53.588  23.340  277.965 1.00 26.57  ? 61  VAL A N   1 
ATOM   353  C  CA  . VAL A 1 61  ? -53.109  23.197  276.596 1.00 28.45  ? 61  VAL A CA  1 
ATOM   354  C  C   . VAL A 1 61  ? -51.898  22.275  276.582 1.00 34.97  ? 61  VAL A C   1 
ATOM   355  O  O   . VAL A 1 61  ? -50.942  22.478  277.340 1.00 37.22  ? 61  VAL A O   1 
ATOM   356  C  CB  . VAL A 1 61  ? -52.767  24.562  275.977 1.00 36.38  ? 61  VAL A CB  1 
ATOM   357  C  CG1 . VAL A 1 61  ? -52.381  24.398  274.521 1.00 44.43  ? 61  VAL A CG1 1 
ATOM   358  C  CG2 . VAL A 1 61  ? -53.947  25.510  276.111 1.00 67.96  ? 61  VAL A CG2 1 
ATOM   359  N  N   . TRP A 1 62  ? -51.946  21.263  275.721 1.00 38.66  ? 62  TRP A N   1 
ATOM   360  C  CA  . TRP A 1 62  ? -50.819  20.388  275.445 1.00 51.99  ? 62  TRP A CA  1 
ATOM   361  C  C   . TRP A 1 62  ? -50.567  20.386  273.943 1.00 50.34  ? 62  TRP A C   1 
ATOM   362  O  O   . TRP A 1 62  ? -51.448  20.724  273.150 1.00 43.75  ? 62  TRP A O   1 
ATOM   363  C  CB  . TRP A 1 62  ? -51.075  18.955  275.941 1.00 44.50  ? 62  TRP A CB  1 
ATOM   364  C  CG  . TRP A 1 62  ? -51.535  18.871  277.372 1.00 40.88  ? 62  TRP A CG  1 
ATOM   365  C  CD1 . TRP A 1 62  ? -52.794  19.106  277.846 1.00 38.21  ? 62  TRP A CD1 1 
ATOM   366  C  CD2 . TRP A 1 62  ? -50.743  18.506  278.509 1.00 46.07  ? 62  TRP A CD2 1 
ATOM   367  N  NE1 . TRP A 1 62  ? -52.831  18.923  279.207 1.00 37.90  ? 62  TRP A NE1 1 
ATOM   368  C  CE2 . TRP A 1 62  ? -51.584  18.553  279.638 1.00 42.30  ? 62  TRP A CE2 1 
ATOM   369  C  CE3 . TRP A 1 62  ? -49.402  18.150  278.681 1.00 64.52  ? 62  TRP A CE3 1 
ATOM   370  C  CZ2 . TRP A 1 62  ? -51.129  18.256  280.921 1.00 49.51  ? 62  TRP A CZ2 1 
ATOM   371  C  CZ3 . TRP A 1 62  ? -48.953  17.857  279.954 1.00 79.05  ? 62  TRP A CZ3 1 
ATOM   372  C  CH2 . TRP A 1 62  ? -49.813  17.911  281.058 1.00 58.60  ? 62  TRP A CH2 1 
ATOM   373  N  N   . ASN A 1 63  ? -49.347  20.003  273.560 1.00 47.07  ? 63  ASN A N   1 
ATOM   374  C  CA  . ASN A 1 63  ? -48.971  19.809  272.158 1.00 51.90  ? 63  ASN A CA  1 
ATOM   375  C  C   . ASN A 1 63  ? -49.055  21.131  271.389 1.00 62.47  ? 63  ASN A C   1 
ATOM   376  O  O   . ASN A 1 63  ? -49.777  21.276  270.398 1.00 92.84  ? 63  ASN A O   1 
ATOM   377  C  CB  . ASN A 1 63  ? -49.827  18.712  271.513 1.00 56.75  ? 63  ASN A CB  1 
ATOM   378  C  CG  . ASN A 1 63  ? -49.520  18.508  270.038 1.00 65.35  ? 63  ASN A CG  1 
ATOM   379  O  OD1 . ASN A 1 63  ? -48.478  18.929  269.534 1.00 72.24  ? 63  ASN A OD1 1 
ATOM   380  N  ND2 . ASN A 1 63  ? -50.453  17.885  269.332 1.00 58.62  ? 63  ASN A ND2 1 
ATOM   381  N  N   . GLY A 1 64  ? -48.310  22.112  271.884 1.00 49.08  ? 64  GLY A N   1 
ATOM   382  C  CA  . GLY A 1 64  ? -48.148  23.385  271.213 1.00 44.59  ? 64  GLY A CA  1 
ATOM   383  C  C   . GLY A 1 64  ? -48.559  24.555  272.089 1.00 42.06  ? 64  GLY A C   1 
ATOM   384  O  O   . GLY A 1 64  ? -48.672  24.456  273.316 1.00 41.46  ? 64  GLY A O   1 
ATOM   385  N  N   . ASP A 1 65  ? -48.769  25.691  271.429 1.00 41.86  ? 65  ASP A N   1 
ATOM   386  C  CA  . ASP A 1 65  ? -49.098  26.924  272.119 1.00 45.55  ? 65  ASP A CA  1 
ATOM   387  C  C   . ASP A 1 65  ? -50.600  27.010  272.389 1.00 40.73  ? 65  ASP A C   1 
ATOM   388  O  O   . ASP A 1 65  ? -51.390  26.153  271.984 1.00 48.96  ? 65  ASP A O   1 
ATOM   389  C  CB  . ASP A 1 65  ? -48.623  28.125  271.308 1.00 46.71  ? 65  ASP A CB  1 
ATOM   390  C  CG  . ASP A 1 65  ? -49.266  28.199  269.937 1.00 57.43  ? 65  ASP A CG  1 
ATOM   391  O  OD1 . ASP A 1 65  ? -48.750  27.561  269.002 1.00 85.33  ? 65  ASP A OD1 1 
ATOM   392  O  OD2 . ASP A 1 65  ? -50.286  28.909  269.795 1.00 51.54  ? 65  ASP A OD2 1 
ATOM   393  N  N   . ILE A 1 66  ? -51.002  28.080  273.082 1.00 38.67  ? 66  ILE A N   1 
ATOM   394  C  CA  . ILE A 1 66  ? -52.390  28.233  273.516 1.00 35.66  ? 66  ILE A CA  1 
ATOM   395  C  C   . ILE A 1 66  ? -53.292  28.843  272.457 1.00 38.02  ? 66  ILE A C   1 
ATOM   396  O  O   . ILE A 1 66  ? -54.508  28.924  272.669 1.00 38.24  ? 66  ILE A O   1 
ATOM   397  C  CB  . ILE A 1 66  ? -52.462  29.093  274.791 1.00 33.39  ? 66  ILE A CB  1 
ATOM   398  C  CG1 . ILE A 1 66  ? -51.829  30.461  274.540 1.00 33.53  ? 66  ILE A CG1 1 
ATOM   399  C  CG2 . ILE A 1 66  ? -51.762  28.393  275.944 1.00 31.24  ? 66  ILE A CG2 1 
ATOM   400  C  CD1 . ILE A 1 66  ? -51.951  31.401  275.707 1.00 36.45  ? 66  ILE A CD1 1 
ATOM   401  N  N   . GLY A 1 67  ? -52.744  29.274  271.329 1.00 37.20  ? 67  GLY A N   1 
ATOM   402  C  CA  . GLY A 1 67  ? -53.541  29.860  270.274 1.00 35.46  ? 67  GLY A CA  1 
ATOM   403  C  C   . GLY A 1 67  ? -53.833  31.332  270.510 1.00 34.02  ? 67  GLY A C   1 
ATOM   404  O  O   . GLY A 1 67  ? -53.677  31.868  271.606 1.00 35.44  ? 67  GLY A O   1 
ATOM   405  N  N   . ASP A 1 68  ? -54.275  31.996  269.440 1.00 32.52  ? 68  ASP A N   1 
ATOM   406  C  CA  . ASP A 1 68  ? -54.527  33.432  269.510 1.00 35.46  ? 68  ASP A CA  1 
ATOM   407  C  C   . ASP A 1 68  ? -55.913  33.742  270.064 1.00 42.98  ? 68  ASP A C   1 
ATOM   408  O  O   . ASP A 1 68  ? -56.070  34.678  270.855 1.00 71.41  ? 68  ASP A O   1 
ATOM   409  C  CB  . ASP A 1 68  ? -54.352  34.062  268.128 1.00 38.37  ? 68  ASP A CB  1 
ATOM   410  C  CG  . ASP A 1 68  ? -52.934  33.938  267.607 1.00 38.87  ? 68  ASP A CG  1 
ATOM   411  O  OD1 . ASP A 1 68  ? -52.012  33.765  268.431 1.00 41.79  ? 68  ASP A OD1 1 
ATOM   412  O  OD2 . ASP A 1 68  ? -52.740  34.014  266.376 1.00 40.16  ? 68  ASP A OD2 1 
ATOM   413  N  N   . ILE A 1 69  ? -56.927  32.976  269.663 1.00 33.73  ? 69  ILE A N   1 
ATOM   414  C  CA  . ILE A 1 69  ? -58.300  33.212  270.093 1.00 31.61  ? 69  ILE A CA  1 
ATOM   415  C  C   . ILE A 1 69  ? -58.924  31.882  270.493 1.00 30.67  ? 69  ILE A C   1 
ATOM   416  O  O   . ILE A 1 69  ? -58.550  30.819  269.987 1.00 31.49  ? 69  ILE A O   1 
ATOM   417  C  CB  . ILE A 1 69  ? -59.127  33.917  268.991 1.00 31.16  ? 69  ILE A CB  1 
ATOM   418  C  CG1 . ILE A 1 69  ? -60.425  34.489  269.565 1.00 31.50  ? 69  ILE A CG1 1 
ATOM   419  C  CG2 . ILE A 1 69  ? -59.409  32.970  267.834 1.00 34.85  ? 69  ILE A CG2 1 
ATOM   420  C  CD1 . ILE A 1 69  ? -61.084  35.518  268.672 1.00 39.53  ? 69  ILE A CD1 1 
ATOM   421  N  N   . ALA A 1 70  ? -59.877  31.944  271.421 1.00 30.40  ? 70  ALA A N   1 
ATOM   422  C  CA  . ALA A 1 70  ? -60.509  30.762  271.989 1.00 29.85  ? 70  ALA A CA  1 
ATOM   423  C  C   . ALA A 1 70  ? -62.018  30.834  271.811 1.00 30.25  ? 70  ALA A C   1 
ATOM   424  O  O   . ALA A 1 70  ? -62.629  31.882  272.038 1.00 32.29  ? 70  ALA A O   1 
ATOM   425  C  CB  . ALA A 1 70  ? -60.169  30.623  273.476 1.00 29.17  ? 70  ALA A CB  1 
ATOM   426  N  N   . TYR A 1 71  ? -62.616  29.713  271.413 1.00 28.93  ? 71  TYR A N   1 
ATOM   427  C  CA  . TYR A 1 71  ? -64.057  29.598  271.254 1.00 27.68  ? 71  TYR A CA  1 
ATOM   428  C  C   . TYR A 1 71  ? -64.595  28.469  272.122 1.00 26.24  ? 71  TYR A C   1 
ATOM   429  O  O   . TYR A 1 71  ? -63.875  27.534  272.483 1.00 27.12  ? 71  TYR A O   1 
ATOM   430  C  CB  . TYR A 1 71  ? -64.449  29.338  269.792 1.00 28.23  ? 71  TYR A CB  1 
ATOM   431  C  CG  . TYR A 1 71  ? -63.926  30.350  268.800 1.00 28.23  ? 71  TYR A CG  1 
ATOM   432  C  CD1 . TYR A 1 71  ? -64.560  31.573  268.627 1.00 29.69  ? 71  TYR A CD1 1 
ATOM   433  C  CD2 . TYR A 1 71  ? -62.813  30.074  268.019 1.00 29.60  ? 71  TYR A CD2 1 
ATOM   434  C  CE1 . TYR A 1 71  ? -64.091  32.498  267.715 1.00 32.82  ? 71  TYR A CE1 1 
ATOM   435  C  CE2 . TYR A 1 71  ? -62.337  30.991  267.103 1.00 33.11  ? 71  TYR A CE2 1 
ATOM   436  C  CZ  . TYR A 1 71  ? -62.980  32.202  266.955 1.00 34.41  ? 71  TYR A CZ  1 
ATOM   437  O  OH  . TYR A 1 71  ? -62.510  33.119  266.045 1.00 44.52  ? 71  TYR A OH  1 
ATOM   438  N  N   . VAL A 1 72  ? -65.880  28.570  272.453 1.00 26.21  ? 72  VAL A N   1 
ATOM   439  C  CA  . VAL A 1 72  ? -66.626  27.511  273.121 1.00 26.32  ? 72  VAL A CA  1 
ATOM   440  C  C   . VAL A 1 72  ? -67.809  27.151  272.236 1.00 26.66  ? 72  VAL A C   1 
ATOM   441  O  O   . VAL A 1 72  ? -68.486  28.038  271.704 1.00 26.35  ? 72  VAL A O   1 
ATOM   442  C  CB  . VAL A 1 72  ? -67.094  27.935  274.529 1.00 23.77  ? 72  VAL A CB  1 
ATOM   443  C  CG1 . VAL A 1 72  ? -67.954  26.851  275.156 1.00 23.47  ? 72  VAL A CG1 1 
ATOM   444  C  CG2 . VAL A 1 72  ? -65.897  28.243  275.412 1.00 21.57  ? 72  VAL A CG2 1 
ATOM   445  N  N   . LEU A 1 73  ? -68.053  25.853  272.068 1.00 26.50  ? 73  LEU A N   1 
ATOM   446  C  CA  . LEU A 1 73  ? -69.023  25.356  271.100 1.00 29.88  ? 73  LEU A CA  1 
ATOM   447  C  C   . LEU A 1 73  ? -70.085  24.527  271.809 1.00 33.39  ? 73  LEU A C   1 
ATOM   448  O  O   . LEU A 1 73  ? -69.761  23.547  272.488 1.00 37.07  ? 73  LEU A O   1 
ATOM   449  C  CB  . LEU A 1 73  ? -68.328  24.529  270.017 1.00 27.63  ? 73  LEU A CB  1 
ATOM   450  C  CG  . LEU A 1 73  ? -67.255  25.270  269.214 1.00 27.68  ? 73  LEU A CG  1 
ATOM   451  C  CD1 . LEU A 1 73  ? -66.711  24.393  268.098 1.00 33.25  ? 73  LEU A CD1 1 
ATOM   452  C  CD2 . LEU A 1 73  ? -67.798  26.577  268.660 1.00 30.45  ? 73  LEU A CD2 1 
ATOM   453  N  N   . PHE A 1 74  ? -71.350  24.919  271.643 1.00 32.59  ? 74  PHE A N   1 
ATOM   454  C  CA  . PHE A 1 74  ? -72.480  24.166  272.178 1.00 33.75  ? 74  PHE A CA  1 
ATOM   455  C  C   . PHE A 1 74  ? -73.330  23.566  271.065 1.00 46.99  ? 74  PHE A C   1 
ATOM   456  O  O   . PHE A 1 74  ? -74.521  23.882  270.990 1.00 102.62 ? 74  PHE A O   1 
ATOM   457  C  CB  . PHE A 1 74  ? -73.387  25.051  273.040 1.00 32.78  ? 74  PHE A CB  1 
ATOM   458  C  CG  . PHE A 1 74  ? -72.813  25.425  274.376 1.00 29.87  ? 74  PHE A CG  1 
ATOM   459  C  CD1 . PHE A 1 74  ? -71.579  24.960  274.789 1.00 28.35  ? 74  PHE A CD1 1 
ATOM   460  C  CD2 . PHE A 1 74  ? -73.536  26.241  275.231 1.00 28.60  ? 74  PHE A CD2 1 
ATOM   461  C  CE1 . PHE A 1 74  ? -71.075  25.316  276.025 1.00 41.95  ? 74  PHE A CE1 1 
ATOM   462  C  CE2 . PHE A 1 74  ? -73.037  26.595  276.465 1.00 30.64  ? 74  PHE A CE2 1 
ATOM   463  C  CZ  . PHE A 1 74  ? -71.805  26.133  276.864 1.00 45.97  ? 74  PHE A CZ  1 
ATOM   464  N  N   . ASP A 1 75  ? -72.718  22.720  270.218 1.00 44.94  ? 75  ASP A N   1 
ATOM   465  C  CA  . ASP A 1 75  ? -73.279  21.977  269.079 1.00 54.34  ? 75  ASP A CA  1 
ATOM   466  C  C   . ASP A 1 75  ? -72.434  22.217  267.835 1.00 50.64  ? 75  ASP A C   1 
ATOM   467  O  O   . ASP A 1 75  ? -72.956  22.181  266.716 1.00 53.84  ? 75  ASP A O   1 
ATOM   468  C  CB  . ASP A 1 75  ? -74.730  22.344  268.737 1.00 79.14  ? 75  ASP A CB  1 
ATOM   469  C  CG  . ASP A 1 75  ? -75.740  21.672  269.647 1.00 77.56  ? 75  ASP A CG  1 
ATOM   470  O  OD1 . ASP A 1 75  ? -75.457  20.561  270.142 1.00 54.12  ? 75  ASP A OD1 1 
ATOM   471  O  OD2 . ASP A 1 75  ? -76.818  22.264  269.869 1.00 58.70  ? 75  ASP A OD2 1 
ATOM   472  N  N   . GLU A 1 76  ? -71.136  22.458  268.021 1.00 45.05  ? 76  GLU A N   1 
ATOM   473  C  CA  . GLU A 1 76  ? -70.236  22.931  266.968 1.00 48.29  ? 76  GLU A CA  1 
ATOM   474  C  C   . GLU A 1 76  ? -70.647  24.301  266.438 1.00 59.14  ? 76  GLU A C   1 
ATOM   475  O  O   . GLU A 1 76  ? -70.280  24.674  265.319 1.00 83.42  ? 76  GLU A O   1 
ATOM   476  C  CB  . GLU A 1 76  ? -70.129  21.929  265.810 1.00 53.32  ? 76  GLU A CB  1 
ATOM   477  C  CG  . GLU A 1 76  ? -69.677  20.538  266.215 1.00 52.06  ? 76  GLU A CG  1 
ATOM   478  C  CD  . GLU A 1 76  ? -69.812  19.535  265.085 1.00 44.76  ? 76  GLU A CD  1 
ATOM   479  O  OE1 . GLU A 1 76  ? -69.178  19.739  264.028 1.00 51.57  ? 76  GLU A OE1 1 
ATOM   480  O  OE2 . GLU A 1 76  ? -70.554  18.545  265.252 1.00 43.48  ? 76  GLU A OE2 1 
ATOM   481  N  N   . GLN A 1 77  ? -71.410  25.057  267.224 1.00 47.22  ? 77  GLN A N   1 
ATOM   482  C  CA  . GLN A 1 77  ? -71.788  26.424  266.898 1.00 50.43  ? 77  GLN A CA  1 
ATOM   483  C  C   . GLN A 1 77  ? -71.351  27.344  268.029 1.00 36.94  ? 77  GLN A C   1 
ATOM   484  O  O   . GLN A 1 77  ? -71.445  26.984  269.207 1.00 34.73  ? 77  GLN A O   1 
ATOM   485  C  CB  . GLN A 1 77  ? -73.299  26.545  266.659 1.00 52.26  ? 77  GLN A CB  1 
ATOM   486  C  CG  . GLN A 1 77  ? -73.811  25.740  265.468 1.00 57.76  ? 77  GLN A CG  1 
ATOM   487  C  CD  . GLN A 1 77  ? -73.522  26.405  264.131 1.00 73.81  ? 77  GLN A CD  1 
ATOM   488  O  OE1 . GLN A 1 77  ? -72.858  27.440  264.067 1.00 87.98  ? 77  GLN A OE1 1 
ATOM   489  N  NE2 . GLN A 1 77  ? -74.021  25.808  263.054 1.00 57.83  ? 77  GLN A NE2 1 
ATOM   490  N  N   . GLN A 1 78  ? -70.879  28.533  267.662 1.00 35.01  ? 78  GLN A N   1 
ATOM   491  C  CA  . GLN A 1 78  ? -70.227  29.423  268.614 1.00 31.78  ? 78  GLN A CA  1 
ATOM   492  C  C   . GLN A 1 78  ? -71.198  29.909  269.684 1.00 29.16  ? 78  GLN A C   1 
ATOM   493  O  O   . GLN A 1 78  ? -72.351  30.242  269.397 1.00 30.90  ? 78  GLN A O   1 
ATOM   494  C  CB  . GLN A 1 78  ? -69.625  30.619  267.880 1.00 33.43  ? 78  GLN A CB  1 
ATOM   495  C  CG  . GLN A 1 78  ? -68.564  31.366  268.664 1.00 31.23  ? 78  GLN A CG  1 
ATOM   496  C  CD  . GLN A 1 78  ? -68.262  32.726  268.072 1.00 37.31  ? 78  GLN A CD  1 
ATOM   497  O  OE1 . GLN A 1 78  ? -68.930  33.712  268.382 1.00 53.90  ? 78  GLN A OE1 1 
ATOM   498  N  NE2 . GLN A 1 78  ? -67.260  32.784  267.204 1.00 45.39  ? 78  GLN A NE2 1 
ATOM   499  N  N   . VAL A 1 79  ? -70.720  29.946  270.929 1.00 30.14  ? 79  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 79  ? -71.497  30.472  272.048 1.00 29.19  ? 79  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 79  ? -70.617  31.352  272.927 1.00 38.53  ? 79  VAL A C   1 
ATOM   502  O  O   . VAL A 1 79  ? -71.100  31.966  273.885 1.00 53.92  ? 79  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 79  ? -72.132  29.344  272.885 1.00 27.15  ? 79  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 79  ? -73.016  28.455  272.024 1.00 44.85  ? 79  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 79  ? -71.056  28.528  273.581 1.00 29.04  ? 79  VAL A CG2 1 
ATOM   506  N  N   . TRP A 1 80  ? -69.323  31.420  272.616 1.00 31.52  ? 80  TRP A N   1 
ATOM   507  C  CA  . TRP A 1 80  ? -68.396  32.187  273.437 1.00 27.97  ? 80  TRP A CA  1 
ATOM   508  C  C   . TRP A 1 80  ? -67.114  32.436  272.656 1.00 27.93  ? 80  TRP A C   1 
ATOM   509  O  O   . TRP A 1 80  ? -66.744  31.652  271.779 1.00 41.55  ? 80  TRP A O   1 
ATOM   510  C  CB  . TRP A 1 80  ? -68.084  31.461  274.753 1.00 27.43  ? 80  TRP A CB  1 
ATOM   511  C  CG  . TRP A 1 80  ? -67.232  32.248  275.707 1.00 26.90  ? 80  TRP A CG  1 
ATOM   512  C  CD1 . TRP A 1 80  ? -67.666  33.108  276.673 1.00 37.89  ? 80  TRP A CD1 1 
ATOM   513  C  CD2 . TRP A 1 80  ? -65.802  32.239  275.792 1.00 25.72  ? 80  TRP A CD2 1 
ATOM   514  N  NE1 . TRP A 1 80  ? -66.596  33.638  277.351 1.00 28.46  ? 80  TRP A NE1 1 
ATOM   515  C  CE2 . TRP A 1 80  ? -65.440  33.121  276.829 1.00 25.95  ? 80  TRP A CE2 1 
ATOM   516  C  CE3 . TRP A 1 80  ? -64.792  31.573  275.091 1.00 29.88  ? 80  TRP A CE3 1 
ATOM   517  C  CZ2 . TRP A 1 80  ? -64.112  33.354  277.182 1.00 30.18  ? 80  TRP A CZ2 1 
ATOM   518  C  CZ3 . TRP A 1 80  ? -63.475  31.806  275.443 1.00 27.60  ? 80  TRP A CZ3 1 
ATOM   519  C  CH2 . TRP A 1 80  ? -63.147  32.688  276.479 1.00 28.49  ? 80  TRP A CH2 1 
ATOM   520  N  N   . LYS A 1 81  ? -66.447  33.541  272.985 1.00 30.72  ? 81  LYS A N   1 
ATOM   521  C  CA  . LYS A 1 81  ? -65.129  33.839  272.444 1.00 29.83  ? 81  LYS A CA  1 
ATOM   522  C  C   . LYS A 1 81  ? -64.425  34.806  273.384 1.00 28.60  ? 81  LYS A C   1 
ATOM   523  O  O   . LYS A 1 81  ? -65.070  35.583  274.092 1.00 29.71  ? 81  LYS A O   1 
ATOM   524  C  CB  . LYS A 1 81  ? -65.204  34.424  271.028 1.00 32.26  ? 81  LYS A CB  1 
ATOM   525  C  CG  . LYS A 1 81  ? -65.837  35.801  270.940 1.00 38.06  ? 81  LYS A CG  1 
ATOM   526  C  CD  . LYS A 1 81  ? -65.472  36.476  269.628 1.00 48.95  ? 81  LYS A CD  1 
ATOM   527  C  CE  . LYS A 1 81  ? -66.080  37.863  269.525 1.00 60.23  ? 81  LYS A CE  1 
ATOM   528  N  NZ  . LYS A 1 81  ? -67.564  37.813  269.420 1.00 92.76  ? 81  LYS A NZ  1 
ATOM   529  N  N   . GLY A 1 82  ? -63.095  34.742  273.388 1.00 27.81  ? 82  GLY A N   1 
ATOM   530  C  CA  . GLY A 1 82  ? -62.303  35.602  274.248 1.00 33.96  ? 82  GLY A CA  1 
ATOM   531  C  C   . GLY A 1 82  ? -60.811  35.363  274.141 1.00 37.28  ? 82  GLY A C   1 
ATOM   532  O  O   . GLY A 1 82  ? -60.306  35.021  273.068 1.00 55.85  ? 82  GLY A O   1 
ATOM   533  N  N   . ASP A 1 83  ? -60.094  35.540  275.249 1.00 35.76  ? 83  ASP A N   1 
ATOM   534  C  CA  . ASP A 1 83  ? -58.650  35.354  275.276 1.00 37.74  ? 83  ASP A CA  1 
ATOM   535  C  C   . ASP A 1 83  ? -58.315  33.912  275.635 1.00 36.07  ? 83  ASP A C   1 
ATOM   536  O  O   . ASP A 1 83  ? -58.855  33.363  276.602 1.00 38.06  ? 83  ASP A O   1 
ATOM   537  C  CB  . ASP A 1 83  ? -58.000  36.309  276.278 1.00 47.11  ? 83  ASP A CB  1 
ATOM   538  C  CG  . ASP A 1 83  ? -58.462  37.740  276.102 1.00 66.25  ? 83  ASP A CG  1 
ATOM   539  O  OD1 . ASP A 1 83  ? -59.273  37.995  275.186 1.00 72.08  ? 83  ASP A OD1 1 
ATOM   540  O  OD2 . ASP A 1 83  ? -58.015  38.612  276.876 1.00 56.17  ? 83  ASP A OD2 1 
ATOM   541  N  N   . ALA A 1 84  ? -57.421  33.304  274.854 1.00 35.09  ? 84  ALA A N   1 
ATOM   542  C  CA  . ALA A 1 84  ? -56.978  31.945  275.134 1.00 30.78  ? 84  ALA A CA  1 
ATOM   543  C  C   . ALA A 1 84  ? -56.000  31.877  276.297 1.00 32.56  ? 84  ALA A C   1 
ATOM   544  O  O   . ALA A 1 84  ? -55.793  30.792  276.851 1.00 32.14  ? 84  ALA A O   1 
ATOM   545  C  CB  . ALA A 1 84  ? -56.339  31.332  273.887 1.00 33.90  ? 84  ALA A CB  1 
ATOM   546  N  N   . GLU A 1 85  ? -55.393  33.005  276.674 1.00 38.99  ? 85  GLU A N   1 
ATOM   547  C  CA  . GLU A 1 85  ? -54.498  33.016  277.826 1.00 38.44  ? 85  GLU A CA  1 
ATOM   548  C  C   . GLU A 1 85  ? -55.252  32.749  279.120 1.00 37.40  ? 85  GLU A C   1 
ATOM   549  O  O   . GLU A 1 85  ? -54.689  32.173  280.058 1.00 48.97  ? 85  GLU A O   1 
ATOM   550  C  CB  . GLU A 1 85  ? -53.763  34.356  277.918 1.00 40.80  ? 85  GLU A CB  1 
ATOM   551  C  CG  . GLU A 1 85  ? -52.869  34.690  276.730 1.00 42.33  ? 85  GLU A CG  1 
ATOM   552  C  CD  . GLU A 1 85  ? -53.640  35.205  275.529 1.00 51.46  ? 85  GLU A CD  1 
ATOM   553  O  OE1 . GLU A 1 85  ? -54.872  35.382  275.637 1.00 77.74  ? 85  GLU A OE1 1 
ATOM   554  O  OE2 . GLU A 1 85  ? -53.012  35.433  274.474 1.00 51.76  ? 85  GLU A OE2 1 
ATOM   555  N  N   . SER A 1 86  ? -56.521  33.158  279.189 1.00 40.09  ? 86  SER A N   1 
ATOM   556  C  CA  . SER A 1 86  ? -57.297  32.974  280.409 1.00 40.18  ? 86  SER A CA  1 
ATOM   557  C  C   . SER A 1 86  ? -57.572  31.504  280.691 1.00 36.39  ? 86  SER A C   1 
ATOM   558  O  O   . SER A 1 86  ? -57.670  31.109  281.858 1.00 36.62  ? 86  SER A O   1 
ATOM   559  C  CB  . SER A 1 86  ? -58.611  33.748  280.312 1.00 35.79  ? 86  SER A CB  1 
ATOM   560  O  OG  . SER A 1 86  ? -59.302  33.422  279.119 1.00 32.23  ? 86  SER A OG  1 
ATOM   561  N  N   . LYS A 1 87  ? -57.697  30.686  279.643 1.00 34.17  ? 87  LYS A N   1 
ATOM   562  C  CA  . LYS A 1 87  ? -58.008  29.262  279.775 1.00 33.42  ? 87  LYS A CA  1 
ATOM   563  C  C   . LYS A 1 87  ? -59.286  29.035  280.576 1.00 32.11  ? 87  LYS A C   1 
ATOM   564  O  O   . LYS A 1 87  ? -59.431  28.022  281.264 1.00 39.25  ? 87  LYS A O   1 
ATOM   565  C  CB  . LYS A 1 87  ? -56.841  28.490  280.399 1.00 47.41  ? 87  LYS A CB  1 
ATOM   566  C  CG  . LYS A 1 87  ? -55.548  28.560  279.604 1.00 33.80  ? 87  LYS A CG  1 
ATOM   567  C  CD  . LYS A 1 87  ? -54.459  27.728  280.261 1.00 30.25  ? 87  LYS A CD  1 
ATOM   568  C  CE  . LYS A 1 87  ? -53.168  27.777  279.464 1.00 34.86  ? 87  LYS A CE  1 
ATOM   569  N  NZ  . LYS A 1 87  ? -52.116  26.908  280.060 1.00 34.13  ? 87  LYS A NZ  1 
ATOM   570  N  N   . ARG A 1 88  ? -60.222  29.978  280.492 1.00 33.09  ? 88  ARG A N   1 
ATOM   571  C  CA  . ARG A 1 88  ? -61.468  29.902  281.238 1.00 33.68  ? 88  ARG A CA  1 
ATOM   572  C  C   . ARG A 1 88  ? -62.560  30.600  280.443 1.00 31.99  ? 88  ARG A C   1 
ATOM   573  O  O   . ARG A 1 88  ? -62.302  31.570  279.725 1.00 30.16  ? 88  ARG A O   1 
ATOM   574  C  CB  . ARG A 1 88  ? -61.333  30.539  282.626 1.00 39.23  ? 88  ARG A CB  1 
ATOM   575  C  CG  . ARG A 1 88  ? -62.537  30.334  283.531 1.00 32.50  ? 88  ARG A CG  1 
ATOM   576  C  CD  . ARG A 1 88  ? -62.456  31.221  284.758 1.00 35.38  ? 88  ARG A CD  1 
ATOM   577  N  NE  . ARG A 1 88  ? -63.434  30.848  285.775 1.00 37.27  ? 88  ARG A NE  1 
ATOM   578  C  CZ  . ARG A 1 88  ? -63.463  31.355  287.003 1.00 47.70  ? 88  ARG A CZ  1 
ATOM   579  N  NH1 . ARG A 1 88  ? -62.565  32.259  287.371 1.00 56.30  ? 88  ARG A NH1 1 
ATOM   580  N  NH2 . ARG A 1 88  ? -64.389  30.959  287.866 1.00 43.24  ? 88  ARG A NH2 1 
ATOM   581  N  N   . ALA A 1 89  ? -63.784  30.096  280.578 1.00 33.68  ? 89  ALA A N   1 
ATOM   582  C  CA  . ALA A 1 89  ? -64.931  30.686  279.907 1.00 30.92  ? 89  ALA A CA  1 
ATOM   583  C  C   . ALA A 1 89  ? -66.174  30.450  280.750 1.00 29.47  ? 89  ALA A C   1 
ATOM   584  O  O   . ALA A 1 89  ? -66.338  29.380  281.343 1.00 30.73  ? 89  ALA A O   1 
ATOM   585  C  CB  . ALA A 1 89  ? -65.122  30.103  278.503 1.00 27.82  ? 89  ALA A CB  1 
ATOM   586  N  N   . THR A 1 90  ? -67.040  31.459  280.803 1.00 27.64  ? 90  THR A N   1 
ATOM   587  C  CA  . THR A 1 90  ? -68.310  31.378  281.514 1.00 24.35  ? 90  THR A CA  1 
ATOM   588  C  C   . THR A 1 90  ? -69.420  31.737  280.539 1.00 23.60  ? 90  THR A C   1 
ATOM   589  O  O   . THR A 1 90  ? -69.436  32.847  279.997 1.00 26.18  ? 90  THR A O   1 
ATOM   590  C  CB  . THR A 1 90  ? -68.332  32.313  282.726 1.00 24.22  ? 90  THR A CB  1 
ATOM   591  O  OG1 . THR A 1 90  ? -67.247  31.984  283.603 1.00 28.10  ? 90  THR A OG1 1 
ATOM   592  C  CG2 . THR A 1 90  ? -69.644  32.178  283.479 1.00 26.34  ? 90  THR A CG2 1 
ATOM   593  N  N   . ILE A 1 91  ? -70.339  30.803  280.314 1.00 22.51  ? 91  ILE A N   1 
ATOM   594  C  CA  . ILE A 1 91  ? -71.392  30.952  279.316 1.00 25.63  ? 91  ILE A CA  1 
ATOM   595  C  C   . ILE A 1 91  ? -72.732  31.056  280.028 1.00 24.46  ? 91  ILE A C   1 
ATOM   596  O  O   . ILE A 1 91  ? -73.050  30.234  280.896 1.00 22.80  ? 91  ILE A O   1 
ATOM   597  C  CB  . ILE A 1 91  ? -71.392  29.784  278.315 1.00 25.70  ? 91  ILE A CB  1 
ATOM   598  C  CG1 . ILE A 1 91  ? -70.025  29.653  277.639 1.00 27.14  ? 91  ILE A CG1 1 
ATOM   599  C  CG2 . ILE A 1 91  ? -72.478  29.982  277.271 1.00 26.20  ? 91  ILE A CG2 1 
ATOM   600  C  CD1 . ILE A 1 91  ? -69.120  28.617  278.274 1.00 25.72  ? 91  ILE A CD1 1 
ATOM   601  N  N   . LYS A 1 92  ? -73.515  32.065  279.656 1.00 28.05  ? 92  LYS A N   1 
ATOM   602  C  CA  . LYS A 1 92  ? -74.850  32.253  280.207 1.00 24.53  ? 92  LYS A CA  1 
ATOM   603  C  C   . LYS A 1 92  ? -75.842  31.388  279.438 1.00 22.47  ? 92  LYS A C   1 
ATOM   604  O  O   . LYS A 1 92  ? -75.944  31.493  278.211 1.00 26.87  ? 92  LYS A O   1 
ATOM   605  C  CB  . LYS A 1 92  ? -75.249  33.724  280.132 1.00 26.10  ? 92  LYS A CB  1 
ATOM   606  C  CG  . LYS A 1 92  ? -76.624  34.029  280.695 1.00 31.24  ? 92  LYS A CG  1 
ATOM   607  C  CD  . LYS A 1 92  ? -76.975  35.494  280.511 1.00 26.35  ? 92  LYS A CD  1 
ATOM   608  C  CE  . LYS A 1 92  ? -77.093  35.848  279.037 1.00 26.28  ? 92  LYS A CE  1 
ATOM   609  N  NZ  . LYS A 1 92  ? -77.401  37.289  278.832 1.00 34.64  ? 92  LYS A NZ  1 
ATOM   610  N  N   . VAL A 1 93  ? -76.570  30.537  280.155 1.00 24.20  ? 93  VAL A N   1 
ATOM   611  C  CA  . VAL A 1 93  ? -77.579  29.663  279.567 1.00 22.87  ? 93  VAL A CA  1 
ATOM   612  C  C   . VAL A 1 93  ? -78.915  29.969  280.228 1.00 23.75  ? 93  VAL A C   1 
ATOM   613  O  O   . VAL A 1 93  ? -78.998  30.052  281.458 1.00 22.78  ? 93  VAL A O   1 
ATOM   614  C  CB  . VAL A 1 93  ? -77.209  28.177  279.730 1.00 23.15  ? 93  VAL A CB  1 
ATOM   615  C  CG1 . VAL A 1 93  ? -78.347  27.290  279.254 1.00 24.22  ? 93  VAL A CG1 1 
ATOM   616  C  CG2 . VAL A 1 93  ? -75.931  27.863  278.967 1.00 24.86  ? 93  VAL A CG2 1 
ATOM   617  N  N   . LEU A 1 94  ? -79.956  30.140  279.410 1.00 28.12  ? 94  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 94  ? -81.275  30.510  279.903 1.00 27.09  ? 94  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 94  ? -82.305  29.394  279.822 1.00 27.75  ? 94  LEU A C   1 
ATOM   620  O  O   . LEU A 1 94  ? -83.321  29.468  280.520 1.00 30.20  ? 94  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 94  ? -81.812  31.727  279.134 1.00 29.07  ? 94  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 94  ? -81.571  33.121  279.720 1.00 24.99  ? 94  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 94  ? -80.127  33.306  280.155 1.00 27.21  ? 94  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 94  ? -81.969  34.191  278.714 1.00 35.58  ? 94  LEU A CD2 1 
ATOM   625  N  N   . VAL A 1 95  ? -82.080  28.375  278.998 1.00 26.91  ? 95  VAL A N   1 
ATOM   626  C  CA  . VAL A 1 95  ? -83.051  27.308  278.801 1.00 25.87  ? 95  VAL A CA  1 
ATOM   627  C  C   . VAL A 1 95  ? -82.418  25.977  279.176 1.00 28.39  ? 95  VAL A C   1 
ATOM   628  O  O   . VAL A 1 95  ? -81.203  25.787  279.065 1.00 25.29  ? 95  VAL A O   1 
ATOM   629  C  CB  . VAL A 1 95  ? -83.573  27.273  277.349 1.00 20.23  ? 95  VAL A CB  1 
ATOM   630  C  CG1 . VAL A 1 95  ? -84.446  28.484  277.073 1.00 30.28  ? 95  VAL A CG1 1 
ATOM   631  C  CG2 . VAL A 1 95  ? -82.411  27.214  276.371 1.00 26.46  ? 95  VAL A CG2 1 
ATOM   632  N  N   . SER A 1 96  ? -83.260  25.050  279.624 1.00 33.18  ? 96  SER A N   1 
ATOM   633  C  CA  . SER A 1 96  ? -82.792  23.726  279.998 1.00 29.88  ? 96  SER A CA  1 
ATOM   634  C  C   . SER A 1 96  ? -82.442  22.908  278.759 1.00 29.28  ? 96  SER A C   1 
ATOM   635  O  O   . SER A 1 96  ? -82.838  23.226  277.634 1.00 37.93  ? 96  SER A O   1 
ATOM   636  C  CB  . SER A 1 96  ? -83.854  22.998  280.820 1.00 26.76  ? 96  SER A CB  1 
ATOM   637  O  OG  . SER A 1 96  ? -85.127  23.104  280.208 1.00 27.42  ? 96  SER A OG  1 
ATOM   638  N  N   . GLY A 1 97  ? -81.692  21.844  278.978 1.00 25.96  ? 97  GLY A N   1 
ATOM   639  C  CA  . GLY A 1 97  ? -81.306  20.956  277.898 1.00 28.24  ? 97  GLY A CA  1 
ATOM   640  C  C   . GLY A 1 97  ? -79.918  20.398  278.121 1.00 29.96  ? 97  GLY A C   1 
ATOM   641  O  O   . GLY A 1 97  ? -79.175  20.827  279.002 1.00 26.81  ? 97  GLY A O   1 
ATOM   642  N  N   . GLN A 1 98  ? -79.577  19.416  277.291 1.00 31.03  ? 98  GLN A N   1 
ATOM   643  C  CA  . GLN A 1 98  ? -78.279  18.760  277.322 1.00 27.12  ? 98  GLN A CA  1 
ATOM   644  C  C   . GLN A 1 98  ? -77.561  18.998  276.002 1.00 25.74  ? 98  GLN A C   1 
ATOM   645  O  O   . GLN A 1 98  ? -78.177  18.953  274.932 1.00 25.77  ? 98  GLN A O   1 
ATOM   646  C  CB  . GLN A 1 98  ? -78.427  17.259  277.582 1.00 27.13  ? 98  GLN A CB  1 
ATOM   647  C  CG  . GLN A 1 98  ? -79.060  16.928  278.925 1.00 43.85  ? 98  GLN A CG  1 
ATOM   648  C  CD  . GLN A 1 98  ? -79.290  15.443  279.110 1.00 50.47  ? 98  GLN A CD  1 
ATOM   649  O  OE1 . GLN A 1 98  ? -79.370  14.692  278.139 1.00 52.20  ? 98  GLN A OE1 1 
ATOM   650  N  NE2 . GLN A 1 98  ? -79.393  15.009  280.361 1.00 35.10  ? 98  GLN A NE2 1 
ATOM   651  N  N   . PHE A 1 99  ? -76.257  19.252  276.080 1.00 23.04  ? 99  PHE A N   1 
ATOM   652  C  CA  . PHE A 1 99  ? -75.479  19.586  274.896 1.00 20.76  ? 99  PHE A CA  1 
ATOM   653  C  C   . PHE A 1 99  ? -74.012  19.290  275.162 1.00 18.69  ? 99  PHE A C   1 
ATOM   654  O  O   . PHE A 1 99  ? -73.561  19.267  276.311 1.00 20.59  ? 99  PHE A O   1 
ATOM   655  C  CB  . PHE A 1 99  ? -75.674  21.054  274.500 1.00 25.59  ? 99  PHE A CB  1 
ATOM   656  C  CG  . PHE A 1 99  ? -75.575  22.012  275.654 1.00 26.87  ? 99  PHE A CG  1 
ATOM   657  C  CD1 . PHE A 1 99  ? -74.341  22.442  276.114 1.00 25.68  ? 99  PHE A CD1 1 
ATOM   658  C  CD2 . PHE A 1 99  ? -76.717  22.481  276.281 1.00 33.66  ? 99  PHE A CD2 1 
ATOM   659  C  CE1 . PHE A 1 99  ? -74.250  23.321  277.176 1.00 24.22  ? 99  PHE A CE1 1 
ATOM   660  C  CE2 . PHE A 1 99  ? -76.632  23.360  277.343 1.00 26.42  ? 99  PHE A CE2 1 
ATOM   661  C  CZ  . PHE A 1 99  ? -75.396  23.781  277.791 1.00 23.96  ? 99  PHE A CZ  1 
ATOM   662  N  N   . ASN A 1 100 ? -73.272  19.067  274.079 1.00 19.11  ? 100 ASN A N   1 
ATOM   663  C  CA  . ASN A 1 100 ? -71.841  18.808  274.154 1.00 18.53  ? 100 ASN A CA  1 
ATOM   664  C  C   . ASN A 1 100 ? -71.075  20.121  274.067 1.00 22.67  ? 100 ASN A C   1 
ATOM   665  O  O   . ASN A 1 100 ? -71.300  20.921  273.153 1.00 23.16  ? 100 ASN A O   1 
ATOM   666  C  CB  . ASN A 1 100 ? -71.399  17.865  273.035 1.00 15.99  ? 100 ASN A CB  1 
ATOM   667  C  CG  . ASN A 1 100 ? -72.003  16.482  273.165 1.00 14.15  ? 100 ASN A CG  1 
ATOM   668  O  OD1 . ASN A 1 100 ? -72.310  16.026  274.267 1.00 16.87  ? 100 ASN A OD1 1 
ATOM   669  N  ND2 . ASN A 1 100 ? -72.176  15.804  272.037 1.00 12.97  ? 100 ASN A ND2 1 
ATOM   670  N  N   . MET A 1 101 ? -70.170  20.336  275.017 1.00 22.76  ? 101 MET A N   1 
ATOM   671  C  CA  . MET A 1 101 ? -69.358  21.542  275.079 1.00 21.55  ? 101 MET A CA  1 
ATOM   672  C  C   . MET A 1 101 ? -67.919  21.216  274.708 1.00 21.97  ? 101 MET A C   1 
ATOM   673  O  O   . MET A 1 101 ? -67.319  20.294  275.273 1.00 21.12  ? 101 MET A O   1 
ATOM   674  C  CB  . MET A 1 101 ? -69.415  22.173  276.471 1.00 21.17  ? 101 MET A CB  1 
ATOM   675  C  CG  . MET A 1 101 ? -68.454  23.331  276.659 1.00 21.59  ? 101 MET A CG  1 
ATOM   676  S  SD  . MET A 1 101 ? -68.632  24.105  278.273 1.00 12.72  ? 101 MET A SD  1 
ATOM   677  C  CE  . MET A 1 101 ? -68.268  22.724  279.347 1.00 23.56  ? 101 MET A CE  1 
ATOM   678  N  N   . ARG A 1 102 ? -67.371  21.974  273.762 1.00 25.24  ? 102 ARG A N   1 
ATOM   679  C  CA  . ARG A 1 102 ? -65.992  21.823  273.330 1.00 23.51  ? 102 ARG A CA  1 
ATOM   680  C  C   . ARG A 1 102 ? -65.298  23.176  273.364 1.00 23.97  ? 102 ARG A C   1 
ATOM   681  O  O   . ARG A 1 102 ? -65.927  24.220  273.176 1.00 24.05  ? 102 ARG A O   1 
ATOM   682  C  CB  . ARG A 1 102 ? -65.901  21.236  271.915 1.00 21.77  ? 102 ARG A CB  1 
ATOM   683  C  CG  . ARG A 1 102 ? -66.349  19.793  271.799 1.00 21.85  ? 102 ARG A CG  1 
ATOM   684  C  CD  . ARG A 1 102 ? -66.409  19.361  270.344 1.00 28.09  ? 102 ARG A CD  1 
ATOM   685  N  NE  . ARG A 1 102 ? -65.686  18.115  270.110 1.00 36.24  ? 102 ARG A NE  1 
ATOM   686  C  CZ  . ARG A 1 102 ? -65.756  17.410  268.986 1.00 58.30  ? 102 ARG A CZ  1 
ATOM   687  N  NH1 . ARG A 1 102 ? -66.519  17.829  267.985 1.00 50.08  ? 102 ARG A NH1 1 
ATOM   688  N  NH2 . ARG A 1 102 ? -65.063  16.287  268.861 1.00 50.10  ? 102 ARG A NH2 1 
ATOM   689  N  N   . VAL A 1 103 ? -63.991  23.146  273.608 1.00 24.26  ? 103 VAL A N   1 
ATOM   690  C  CA  . VAL A 1 103 ? -63.144  24.330  273.531 1.00 25.59  ? 103 VAL A CA  1 
ATOM   691  C  C   . VAL A 1 103 ? -62.365  24.268  272.227 1.00 25.81  ? 103 VAL A C   1 
ATOM   692  O  O   . VAL A 1 103 ? -61.743  23.245  271.914 1.00 25.04  ? 103 VAL A O   1 
ATOM   693  C  CB  . VAL A 1 103 ? -62.198  24.423  274.740 1.00 30.41  ? 103 VAL A CB  1 
ATOM   694  C  CG1 . VAL A 1 103 ? -61.305  25.648  274.620 1.00 26.57  ? 103 VAL A CG1 1 
ATOM   695  C  CG2 . VAL A 1 103 ? -62.996  24.470  276.031 1.00 33.18  ? 103 VAL A CG2 1 
ATOM   696  N  N   . LYS A 1 104 ? -62.402  25.355  271.463 1.00 26.60  ? 104 LYS A N   1 
ATOM   697  C  CA  . LYS A 1 104 ? -61.779  25.416  270.143 1.00 26.49  ? 104 LYS A CA  1 
ATOM   698  C  C   . LYS A 1 104 ? -60.798  26.583  270.121 1.00 28.05  ? 104 LYS A C   1 
ATOM   699  O  O   . LYS A 1 104 ? -61.208  27.746  270.045 1.00 27.81  ? 104 LYS A O   1 
ATOM   700  C  CB  . LYS A 1 104 ? -62.836  25.552  269.051 1.00 26.50  ? 104 LYS A CB  1 
ATOM   701  C  CG  . LYS A 1 104 ? -62.290  25.477  267.635 1.00 26.51  ? 104 LYS A CG  1 
ATOM   702  C  CD  . LYS A 1 104 ? -63.419  25.420  266.618 1.00 26.59  ? 104 LYS A CD  1 
ATOM   703  C  CE  . LYS A 1 104 ? -62.889  25.474  265.196 1.00 26.81  ? 104 LYS A CE  1 
ATOM   704  N  NZ  . LYS A 1 104 ? -63.985  25.485  264.190 1.00 27.14  ? 104 LYS A NZ  1 
ATOM   705  N  N   . LEU A 1 105 ? -59.507  26.270  270.187 1.00 28.57  ? 105 LEU A N   1 
ATOM   706  C  CA  . LEU A 1 105 ? -58.455  27.272  270.093 1.00 29.71  ? 105 LEU A CA  1 
ATOM   707  C  C   . LEU A 1 105 ? -58.063  27.453  268.632 1.00 31.41  ? 105 LEU A C   1 
ATOM   708  O  O   . LEU A 1 105 ? -57.736  26.480  267.947 1.00 31.22  ? 105 LEU A O   1 
ATOM   709  C  CB  . LEU A 1 105 ? -57.239  26.860  270.923 1.00 31.29  ? 105 LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 105 ? -57.498  26.495  272.387 1.00 30.02  ? 105 LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 105 ? -56.198  26.144  273.094 1.00 46.55  ? 105 LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 105 ? -58.210  27.624  273.107 1.00 27.14  ? 105 LEU A CD2 1 
ATOM   713  N  N   . CYS A 1 106 ? -58.097  28.697  268.160 1.00 32.40  ? 106 CYS A N   1 
ATOM   714  C  CA  . CYS A 1 106 ? -57.826  29.007  266.765 1.00 36.47  ? 106 CYS A CA  1 
ATOM   715  C  C   . CYS A 1 106 ? -56.744  30.072  266.667 1.00 39.34  ? 106 CYS A C   1 
ATOM   716  O  O   . CYS A 1 106 ? -56.584  30.904  267.565 1.00 52.66  ? 106 CYS A O   1 
ATOM   717  C  CB  . CYS A 1 106 ? -59.085  29.504  266.044 1.00 34.61  ? 106 CYS A CB  1 
ATOM   718  S  SG  . CYS A 1 106 ? -60.342  28.253  265.699 1.00 36.28  ? 106 CYS A SG  1 
ATOM   719  N  N   . ASN A 1 107 ? -56.006  30.041  265.562 1.00 40.19  ? 107 ASN A N   1 
ATOM   720  C  CA  . ASN A 1 107 ? -55.028  31.079  265.257 1.00 49.06  ? 107 ASN A CA  1 
ATOM   721  C  C   . ASN A 1 107 ? -54.811  31.099  263.744 1.00 48.41  ? 107 ASN A C   1 
ATOM   722  O  O   . ASN A 1 107 ? -55.658  30.620  262.981 1.00 44.80  ? 107 ASN A O   1 
ATOM   723  C  CB  . ASN A 1 107 ? -53.730  30.858  266.054 1.00 51.68  ? 107 ASN A CB  1 
ATOM   724  C  CG  . ASN A 1 107 ? -53.030  29.561  265.695 1.00 43.25  ? 107 ASN A CG  1 
ATOM   725  O  OD1 . ASN A 1 107 ? -53.503  28.789  264.862 1.00 44.12  ? 107 ASN A OD1 1 
ATOM   726  N  ND2 . ASN A 1 107 ? -51.891  29.314  266.330 1.00 45.14  ? 107 ASN A ND2 1 
ATOM   727  N  N   . GLU A 1 108 ? -53.672  31.647  263.312 1.00 50.80  ? 108 GLU A N   1 
ATOM   728  C  CA  . GLU A 1 108 ? -53.400  31.766  261.883 1.00 43.96  ? 108 GLU A CA  1 
ATOM   729  C  C   . GLU A 1 108 ? -53.193  30.402  261.237 1.00 43.06  ? 108 GLU A C   1 
ATOM   730  O  O   . GLU A 1 108 ? -53.601  30.186  260.090 1.00 45.37  ? 108 GLU A O   1 
ATOM   731  C  CB  . GLU A 1 108 ? -52.180  32.659  261.658 1.00 42.02  ? 108 GLU A CB  1 
ATOM   732  C  CG  . GLU A 1 108 ? -51.998  33.141  260.225 1.00 51.33  ? 108 GLU A CG  1 
ATOM   733  C  CD  . GLU A 1 108 ? -51.247  32.146  259.360 1.00 41.22  ? 108 GLU A CD  1 
ATOM   734  O  OE1 . GLU A 1 108 ? -51.615  31.987  258.177 1.00 44.45  ? 108 GLU A OE1 1 
ATOM   735  O  OE2 . GLU A 1 108 ? -50.289  31.523  259.863 1.00 45.73  ? 108 GLU A OE2 1 
ATOM   736  N  N   . ASP A 1 109 ? -52.559  29.473  261.951 1.00 47.53  ? 109 ASP A N   1 
ATOM   737  C  CA  . ASP A 1 109 ? -52.289  28.145  261.412 1.00 48.27  ? 109 ASP A CA  1 
ATOM   738  C  C   . ASP A 1 109 ? -53.587  27.402  261.127 1.00 49.24  ? 109 ASP A C   1 
ATOM   739  O  O   . ASP A 1 109 ? -53.957  27.203  259.965 1.00 41.91  ? 109 ASP A O   1 
ATOM   740  C  CB  . ASP A 1 109 ? -51.422  27.337  262.380 1.00 56.81  ? 109 ASP A CB  1 
ATOM   741  C  CG  . ASP A 1 109 ? -50.357  28.180  263.053 1.00 84.27  ? 109 ASP A CG  1 
ATOM   742  O  OD1 . ASP A 1 109 ? -49.327  28.468  262.408 1.00 94.76  ? 109 ASP A OD1 1 
ATOM   743  O  OD2 . ASP A 1 109 ? -50.549  28.551  264.229 1.00 80.97  ? 109 ASP A OD2 1 
ATOM   744  N  N   . GLY A 1 110 ? -54.276  26.993  262.176 1.00 56.99  ? 110 GLY A N   1 
ATOM   745  C  CA  . GLY A 1 110 ? -55.540  26.297  262.042 1.00 43.14  ? 110 GLY A CA  1 
ATOM   746  C  C   . GLY A 1 110 ? -56.307  26.378  263.337 1.00 38.87  ? 110 GLY A C   1 
ATOM   747  O  O   . GLY A 1 110 ? -56.197  27.352  264.085 1.00 48.14  ? 110 GLY A O   1 
ATOM   748  N  N   . CYS A 1 111 ? -57.093  25.340  263.611 1.00 36.67  ? 111 CYS A N   1 
ATOM   749  C  CA  . CYS A 1 111 ? -57.880  25.274  264.833 1.00 32.14  ? 111 CYS A CA  1 
ATOM   750  C  C   . CYS A 1 111 ? -57.781  23.877  265.424 1.00 39.02  ? 111 CYS A C   1 
ATOM   751  O  O   . CYS A 1 111 ? -57.715  22.887  264.690 1.00 36.51  ? 111 CYS A O   1 
ATOM   752  C  CB  . CYS A 1 111 ? -59.349  25.622  264.576 1.00 35.35  ? 111 CYS A CB  1 
ATOM   753  S  SG  . CYS A 1 111 ? -59.663  27.316  264.029 1.00 47.48  ? 111 CYS A SG  1 
ATOM   754  N  N   . SER A 1 112 ? -57.770  23.806  266.751 1.00 35.16  ? 112 SER A N   1 
ATOM   755  C  CA  . SER A 1 112 ? -57.766  22.545  267.477 1.00 30.41  ? 112 SER A CA  1 
ATOM   756  C  C   . SER A 1 112 ? -59.059  22.421  268.269 1.00 26.15  ? 112 SER A C   1 
ATOM   757  O  O   . SER A 1 112 ? -59.564  23.411  268.807 1.00 26.63  ? 112 SER A O   1 
ATOM   758  C  CB  . SER A 1 112 ? -56.561  22.449  268.417 1.00 32.54  ? 112 SER A CB  1 
ATOM   759  O  OG  . SER A 1 112 ? -56.605  23.458  269.411 1.00 34.49  ? 112 SER A OG  1 
ATOM   760  N  N   . VAL A 1 113 ? -59.590  21.204  268.340 1.00 28.72  ? 113 VAL A N   1 
ATOM   761  C  CA  . VAL A 1 113 ? -60.866  20.935  268.992 1.00 24.69  ? 113 VAL A CA  1 
ATOM   762  C  C   . VAL A 1 113 ? -60.627  19.992  270.163 1.00 24.51  ? 113 VAL A C   1 
ATOM   763  O  O   . VAL A 1 113 ? -59.954  18.966  270.014 1.00 26.95  ? 113 VAL A O   1 
ATOM   764  C  CB  . VAL A 1 113 ? -61.890  20.335  268.011 1.00 23.07  ? 113 VAL A CB  1 
ATOM   765  C  CG1 . VAL A 1 113 ? -63.256  20.230  268.670 1.00 27.76  ? 113 VAL A CG1 1 
ATOM   766  C  CG2 . VAL A 1 113 ? -61.968  21.174  266.747 1.00 25.45  ? 113 VAL A CG2 1 
ATOM   767  N  N   . SER A 1 114 ? -61.180  20.340  271.320 1.00 23.21  ? 114 SER A N   1 
ATOM   768  C  CA  . SER A 1 114 ? -61.057  19.507  272.503 1.00 23.21  ? 114 SER A CA  1 
ATOM   769  C  C   . SER A 1 114 ? -62.000  18.311  272.414 1.00 22.72  ? 114 SER A C   1 
ATOM   770  O  O   . SER A 1 114 ? -62.906  18.256  271.578 1.00 25.41  ? 114 SER A O   1 
ATOM   771  C  CB  . SER A 1 114 ? -61.357  20.320  273.761 1.00 24.34  ? 114 SER A CB  1 
ATOM   772  O  OG  . SER A 1 114 ? -62.725  20.685  273.812 1.00 23.93  ? 114 SER A OG  1 
ATOM   773  N  N   . ASP A 1 115 ? -61.775  17.338  273.290 1.00 25.48  ? 115 ASP A N   1 
ATOM   774  C  CA  . ASP A 1 115 ? -62.712  16.234  273.411 1.00 26.44  ? 115 ASP A CA  1 
ATOM   775  C  C   . ASP A 1 115 ? -63.994  16.725  274.079 1.00 29.66  ? 115 ASP A C   1 
ATOM   776  O  O   . ASP A 1 115 ? -63.936  17.451  275.076 1.00 28.25  ? 115 ASP A O   1 
ATOM   777  C  CB  . ASP A 1 115 ? -62.103  15.086  274.214 1.00 26.90  ? 115 ASP A CB  1 
ATOM   778  C  CG  . ASP A 1 115 ? -61.141  14.247  273.395 1.00 30.08  ? 115 ASP A CG  1 
ATOM   779  O  OD1 . ASP A 1 115 ? -61.293  14.206  272.155 1.00 32.29  ? 115 ASP A OD1 1 
ATOM   780  O  OD2 . ASP A 1 115 ? -60.238  13.623  273.990 1.00 29.17  ? 115 ASP A OD2 1 
ATOM   781  N  N   . PRO A 1 116 ? -65.159  16.356  273.554 1.00 30.62  ? 116 PRO A N   1 
ATOM   782  C  CA  . PRO A 1 116 ? -66.408  16.922  274.071 1.00 28.25  ? 116 PRO A CA  1 
ATOM   783  C  C   . PRO A 1 116 ? -66.788  16.348  275.426 1.00 24.02  ? 116 PRO A C   1 
ATOM   784  O  O   . PRO A 1 116 ? -66.510  15.189  275.744 1.00 24.84  ? 116 PRO A O   1 
ATOM   785  C  CB  . PRO A 1 116 ? -67.437  16.540  273.001 1.00 25.62  ? 116 PRO A CB  1 
ATOM   786  C  CG  . PRO A 1 116 ? -66.880  15.309  272.377 1.00 23.20  ? 116 PRO A CG  1 
ATOM   787  C  CD  . PRO A 1 116 ? -65.385  15.468  272.401 1.00 26.19  ? 116 PRO A CD  1 
ATOM   788  N  N   . VAL A 1 117 ? -67.428  17.192  276.232 1.00 23.09  ? 117 VAL A N   1 
ATOM   789  C  CA  . VAL A 1 117 ? -68.072  16.780  277.470 1.00 25.18  ? 117 VAL A CA  1 
ATOM   790  C  C   . VAL A 1 117 ? -69.537  17.183  277.384 1.00 21.39  ? 117 VAL A C   1 
ATOM   791  O  O   . VAL A 1 117 ? -69.912  18.103  276.654 1.00 19.93  ? 117 VAL A O   1 
ATOM   792  C  CB  . VAL A 1 117 ? -67.408  17.393  278.721 1.00 24.74  ? 117 VAL A CB  1 
ATOM   793  C  CG1 . VAL A 1 117 ? -65.968  16.921  278.846 1.00 23.74  ? 117 VAL A CG1 1 
ATOM   794  C  CG2 . VAL A 1 117 ? -67.479  18.911  278.672 1.00 22.79  ? 117 VAL A CG2 1 
ATOM   795  N  N   . LEU A 1 118 ? -70.372  16.477  278.138 1.00 22.47  ? 118 LEU A N   1 
ATOM   796  C  CA  . LEU A 1 118 ? -71.811  16.698  278.118 1.00 22.63  ? 118 LEU A CA  1 
ATOM   797  C  C   . LEU A 1 118 ? -72.227  17.536  279.320 1.00 22.67  ? 118 LEU A C   1 
ATOM   798  O  O   . LEU A 1 118 ? -71.865  17.222  280.459 1.00 22.13  ? 118 LEU A O   1 
ATOM   799  C  CB  . LEU A 1 118 ? -72.566  15.368  278.098 1.00 22.78  ? 118 LEU A CB  1 
ATOM   800  C  CG  . LEU A 1 118 ? -74.087  15.422  278.251 1.00 18.81  ? 118 LEU A CG  1 
ATOM   801  C  CD1 . LEU A 1 118 ? -74.750  14.460  277.290 1.00 25.75  ? 118 LEU A CD1 1 
ATOM   802  C  CD2 . LEU A 1 118 ? -74.478  15.077  279.672 1.00 22.76  ? 118 LEU A CD2 1 
ATOM   803  N  N   . VAL A 1 119 ? -72.988  18.596  279.059 1.00 26.15  ? 119 VAL A N   1 
ATOM   804  C  CA  . VAL A 1 119 ? -73.477  19.506  280.087 1.00 24.58  ? 119 VAL A CA  1 
ATOM   805  C  C   . VAL A 1 119 ? -74.982  19.320  280.218 1.00 23.62  ? 119 VAL A C   1 
ATOM   806  O  O   . VAL A 1 119 ? -75.689  19.183  279.213 1.00 28.21  ? 119 VAL A O   1 
ATOM   807  C  CB  . VAL A 1 119 ? -73.133  20.971  279.751 1.00 21.24  ? 119 VAL A CB  1 
ATOM   808  C  CG1 . VAL A 1 119 ? -73.531  21.893  280.894 1.00 24.27  ? 119 VAL A CG1 1 
ATOM   809  C  CG2 . VAL A 1 119 ? -71.653  21.109  279.434 1.00 21.80  ? 119 VAL A CG2 1 
ATOM   810  N  N   . LYS A 1 120 ? -75.470  19.311  281.457 1.00 23.12  ? 120 LYS A N   1 
ATOM   811  C  CA  . LYS A 1 120 ? -76.894  19.189  281.743 1.00 25.28  ? 120 LYS A CA  1 
ATOM   812  C  C   . LYS A 1 120 ? -77.374  20.453  282.441 1.00 25.38  ? 120 LYS A C   1 
ATOM   813  O  O   . LYS A 1 120 ? -76.849  20.820  283.498 1.00 23.03  ? 120 LYS A O   1 
ATOM   814  C  CB  . LYS A 1 120 ? -77.189  17.962  282.609 1.00 32.85  ? 120 LYS A CB  1 
ATOM   815  C  CG  . LYS A 1 120 ? -76.636  16.656  282.071 1.00 39.15  ? 120 LYS A CG  1 
ATOM   816  C  CD  . LYS A 1 120 ? -77.091  15.481  282.923 1.00 39.13  ? 120 LYS A CD  1 
ATOM   817  C  CE  . LYS A 1 120 ? -76.227  14.253  282.689 1.00 50.86  ? 120 LYS A CE  1 
ATOM   818  N  NZ  . LYS A 1 120 ? -76.644  13.102  283.536 1.00 56.84  ? 120 LYS A NZ  1 
ATOM   819  N  N   . VAL A 1 121 ? -78.368  21.110  281.852 1.00 25.14  ? 121 VAL A N   1 
ATOM   820  C  CA  . VAL A 1 121 ? -79.030  22.262  282.451 1.00 25.27  ? 121 VAL A CA  1 
ATOM   821  C  C   . VAL A 1 121 ? -80.457  21.847  282.776 1.00 24.51  ? 121 VAL A C   1 
ATOM   822  O  O   . VAL A 1 121 ? -81.226  21.489  281.876 1.00 25.54  ? 121 VAL A O   1 
ATOM   823  C  CB  . VAL A 1 121 ? -79.004  23.483  281.520 1.00 25.88  ? 121 VAL A CB  1 
ATOM   824  C  CG1 . VAL A 1 121 ? -79.645  24.681  282.202 1.00 31.90  ? 121 VAL A CG1 1 
ATOM   825  C  CG2 . VAL A 1 121 ? -77.576  23.801  281.105 1.00 25.30  ? 121 VAL A CG2 1 
ATOM   826  N  N   . ALA A 1 122 ? -80.809  21.889  284.056 1.00 25.92  ? 122 ALA A N   1 
ATOM   827  C  CA  . ALA A 1 122 ? -82.092  21.391  284.524 1.00 28.57  ? 122 ALA A CA  1 
ATOM   828  C  C   . ALA A 1 122 ? -83.065  22.534  284.784 1.00 29.33  ? 122 ALA A C   1 
ATOM   829  O  O   . ALA A 1 122 ? -82.673  23.641  285.162 1.00 36.87  ? 122 ALA A O   1 
ATOM   830  C  CB  . ALA A 1 122 ? -81.922  20.560  285.796 1.00 25.91  ? 122 ALA A CB  1 
ATOM   831  N  N   . ASP A 1 123 ? -84.347  22.246  284.576 1.00 28.04  ? 123 ASP A N   1 
ATOM   832  C  CA  . ASP A 1 123 ? -85.420  23.193  284.836 1.00 26.03  ? 123 ASP A CA  1 
ATOM   833  C  C   . ASP A 1 123 ? -86.710  22.402  284.982 1.00 24.46  ? 123 ASP A C   1 
ATOM   834  O  O   . ASP A 1 123 ? -86.788  21.235  284.591 1.00 53.30  ? 123 ASP A O   1 
ATOM   835  C  CB  . ASP A 1 123 ? -85.533  24.239  283.720 1.00 26.41  ? 123 ASP A CB  1 
ATOM   836  C  CG  . ASP A 1 123 ? -86.366  25.438  284.124 1.00 26.09  ? 123 ASP A CG  1 
ATOM   837  O  OD1 . ASP A 1 123 ? -86.660  25.581  285.329 1.00 37.57  ? 123 ASP A OD1 1 
ATOM   838  O  OD2 . ASP A 1 123 ? -86.722  26.241  283.236 1.00 21.74  ? 123 ASP A OD2 1 
ATOM   839  N  N   . THR A 1 124 ? -87.727  23.051  285.549 1.00 22.55  ? 124 THR A N   1 
ATOM   840  C  CA  . THR A 1 124 ? -88.977  22.352  285.826 1.00 23.55  ? 124 THR A CA  1 
ATOM   841  C  C   . THR A 1 124 ? -89.807  22.079  284.579 1.00 21.62  ? 124 THR A C   1 
ATOM   842  O  O   . THR A 1 124 ? -90.925  21.569  284.709 1.00 23.20  ? 124 THR A O   1 
ATOM   843  C  CB  . THR A 1 124 ? -89.812  23.138  286.838 1.00 20.84  ? 124 THR A CB  1 
ATOM   844  O  OG1 . THR A 1 124 ? -90.124  24.432  286.306 1.00 20.57  ? 124 THR A OG1 1 
ATOM   845  C  CG2 . THR A 1 124 ? -89.046  23.288  288.145 1.00 19.74  ? 124 THR A CG2 1 
ATOM   846  N  N   . ASP A 1 125 ? -89.306  22.395  283.385 1.00 21.05  ? 125 ASP A N   1 
ATOM   847  C  CA  . ASP A 1 125 ? -90.001  22.011  282.164 1.00 27.04  ? 125 ASP A CA  1 
ATOM   848  C  C   . ASP A 1 125 ? -89.664  20.594  281.716 1.00 28.03  ? 125 ASP A C   1 
ATOM   849  O  O   . ASP A 1 125 ? -90.266  20.107  280.753 1.00 29.64  ? 125 ASP A O   1 
ATOM   850  C  CB  . ASP A 1 125 ? -89.689  23.001  281.037 1.00 37.50  ? 125 ASP A CB  1 
ATOM   851  C  CG  . ASP A 1 125 ? -88.200  23.231  280.848 1.00 39.44  ? 125 ASP A CG  1 
ATOM   852  O  OD1 . ASP A 1 125 ? -87.395  22.372  281.262 1.00 44.72  ? 125 ASP A OD1 1 
ATOM   853  O  OD2 . ASP A 1 125 ? -87.835  24.276  280.269 1.00 29.25  ? 125 ASP A OD2 1 
ATOM   854  N  N   . GLY A 1 126 ? -88.723  19.929  282.382 1.00 25.56  ? 126 GLY A N   1 
ATOM   855  C  CA  . GLY A 1 126 ? -88.386  18.562  282.043 1.00 29.21  ? 126 GLY A CA  1 
ATOM   856  C  C   . GLY A 1 126 ? -87.492  18.397  280.838 1.00 24.46  ? 126 GLY A C   1 
ATOM   857  O  O   . GLY A 1 126 ? -87.389  17.286  280.308 1.00 22.71  ? 126 GLY A O   1 
ATOM   858  N  N   . GLY A 1 127 ? -86.834  19.467  280.387 1.00 27.74  ? 127 GLY A N   1 
ATOM   859  C  CA  . GLY A 1 127 ? -85.963  19.370  279.228 1.00 26.71  ? 127 GLY A CA  1 
ATOM   860  C  C   . GLY A 1 127 ? -84.749  18.491  279.441 1.00 34.49  ? 127 GLY A C   1 
ATOM   861  O  O   . GLY A 1 127 ? -84.129  18.055  278.465 1.00 37.19  ? 127 GLY A O   1 
ATOM   862  N  N   . HIS A 1 128 ? -84.393  18.222  280.695 1.00 32.80  ? 128 HIS A N   1 
ATOM   863  C  CA  . HIS A 1 128 ? -83.264  17.365  281.025 1.00 26.31  ? 128 HIS A CA  1 
ATOM   864  C  C   . HIS A 1 128 ? -83.679  15.930  281.320 1.00 28.92  ? 128 HIS A C   1 
ATOM   865  O  O   . HIS A 1 128 ? -82.810  15.082  281.547 1.00 44.33  ? 128 HIS A O   1 
ATOM   866  C  CB  . HIS A 1 128 ? -82.511  17.933  282.230 1.00 24.17  ? 128 HIS A CB  1 
ATOM   867  C  CG  . HIS A 1 128 ? -83.283  17.857  283.511 1.00 27.13  ? 128 HIS A CG  1 
ATOM   868  N  ND1 . HIS A 1 128 ? -84.333  18.702  283.798 1.00 25.22  ? 128 HIS A ND1 1 
ATOM   869  C  CD2 . HIS A 1 128 ? -83.162  17.031  284.577 1.00 29.30  ? 128 HIS A CD2 1 
ATOM   870  C  CE1 . HIS A 1 128 ? -84.824  18.403  284.987 1.00 27.93  ? 128 HIS A CE1 1 
ATOM   871  N  NE2 . HIS A 1 128 ? -84.131  17.392  285.481 1.00 25.72  ? 128 HIS A NE2 1 
ATOM   872  N  N   . LEU A 1 129 ? -84.975  15.638  281.320 1.00 26.69  ? 129 LEU A N   1 
ATOM   873  C  CA  . LEU A 1 129 ? -85.492  14.336  281.708 1.00 23.70  ? 129 LEU A CA  1 
ATOM   874  C  C   . LEU A 1 129 ? -85.939  13.544  280.486 1.00 21.35  ? 129 LEU A C   1 
ATOM   875  O  O   . LEU A 1 129 ? -86.229  14.099  279.423 1.00 19.64  ? 129 LEU A O   1 
ATOM   876  C  CB  . LEU A 1 129 ? -86.664  14.484  282.684 1.00 22.33  ? 129 LEU A CB  1 
ATOM   877  C  CG  . LEU A 1 129 ? -86.336  15.043  284.069 1.00 26.10  ? 129 LEU A CG  1 
ATOM   878  C  CD1 . LEU A 1 129 ? -87.583  15.083  284.936 1.00 26.36  ? 129 LEU A CD1 1 
ATOM   879  C  CD2 . LEU A 1 129 ? -85.248  14.217  284.733 1.00 25.26  ? 129 LEU A CD2 1 
ATOM   880  N  N   . ALA A 1 130 ? -85.989  12.224  280.658 1.00 21.66  ? 130 ALA A N   1 
ATOM   881  C  CA  . ALA A 1 130 ? -86.483  11.255  279.698 1.00 22.60  ? 130 ALA A CA  1 
ATOM   882  C  C   . ALA A 1 130 ? -87.933  10.899  280.007 1.00 23.04  ? 130 ALA A C   1 
ATOM   883  O  O   . ALA A 1 130 ? -88.350  10.934  281.169 1.00 27.24  ? 130 ALA A O   1 
ATOM   884  C  CB  . ALA A 1 130 ? -85.628  9.984   279.719 1.00 35.96  ? 130 ALA A CB  1 
ATOM   885  N  N   . PRO A 1 131 ? -88.722  10.564  278.986 1.00 25.52  ? 131 PRO A N   1 
ATOM   886  C  CA  . PRO A 1 131 ? -90.145  10.282  279.214 1.00 21.25  ? 131 PRO A CA  1 
ATOM   887  C  C   . PRO A 1 131 ? -90.357  9.155   280.215 1.00 22.16  ? 131 PRO A C   1 
ATOM   888  O  O   . PRO A 1 131 ? -89.693  8.117   280.165 1.00 18.39  ? 131 PRO A O   1 
ATOM   889  C  CB  . PRO A 1 131 ? -90.651  9.895   277.821 1.00 20.71  ? 131 PRO A CB  1 
ATOM   890  C  CG  . PRO A 1 131 ? -89.755  10.640  276.895 1.00 24.15  ? 131 PRO A CG  1 
ATOM   891  C  CD  . PRO A 1 131 ? -88.398  10.607  277.549 1.00 31.36  ? 131 PRO A CD  1 
ATOM   892  N  N   . LEU A 1 132 ? -91.292  9.377   281.136 1.00 23.47  ? 132 LEU A N   1 
ATOM   893  C  CA  . LEU A 1 132 ? -91.706  8.371   282.114 1.00 22.56  ? 132 LEU A CA  1 
ATOM   894  C  C   . LEU A 1 132 ? -93.039  7.805   281.638 1.00 21.90  ? 132 LEU A C   1 
ATOM   895  O  O   . LEU A 1 132 ? -94.105  8.356   281.913 1.00 21.71  ? 132 LEU A O   1 
ATOM   896  C  CB  . LEU A 1 132 ? -91.810  8.973   283.511 1.00 20.24  ? 132 LEU A CB  1 
ATOM   897  C  CG  . LEU A 1 132 ? -92.344  8.057   284.615 1.00 16.10  ? 132 LEU A CG  1 
ATOM   898  C  CD1 . LEU A 1 132 ? -91.548  6.763   284.674 1.00 47.85  ? 132 LEU A CD1 1 
ATOM   899  C  CD2 . LEU A 1 132 ? -92.329  8.765   285.961 1.00 14.89  ? 132 LEU A CD2 1 
ATOM   900  N  N   . GLU A 1 133 ? -92.973  6.694   280.911 1.00 26.24  ? 133 GLU A N   1 
ATOM   901  C  CA  . GLU A 1 133 ? -94.169  6.090   280.344 1.00 28.28  ? 133 GLU A CA  1 
ATOM   902  C  C   . GLU A 1 133 ? -94.901  5.261   281.391 1.00 29.88  ? 133 GLU A C   1 
ATOM   903  O  O   . GLU A 1 133 ? -94.281  4.613   282.239 1.00 32.26  ? 133 GLU A O   1 
ATOM   904  C  CB  . GLU A 1 133 ? -93.809  5.215   279.145 1.00 27.28  ? 133 GLU A CB  1 
ATOM   905  C  CG  . GLU A 1 133 ? -93.105  5.962   278.028 1.00 29.46  ? 133 GLU A CG  1 
ATOM   906  C  CD  . GLU A 1 133 ? -92.773  5.066   276.854 1.00 55.44  ? 133 GLU A CD  1 
ATOM   907  O  OE1 . GLU A 1 133 ? -91.594  4.676   276.719 1.00 52.93  ? 133 GLU A OE1 1 
ATOM   908  O  OE2 . GLU A 1 133 ? -93.689  4.752   276.066 1.00 56.88  ? 133 GLU A OE2 1 
ATOM   909  N  N   . TYR A 1 134 ? -96.228  5.285   281.323 1.00 27.33  ? 134 TYR A N   1 
ATOM   910  C  CA  . TYR A 1 134 ? -97.057  4.518   282.243 1.00 27.93  ? 134 TYR A CA  1 
ATOM   911  C  C   . TYR A 1 134 ? -97.157  3.073   281.770 1.00 28.47  ? 134 TYR A C   1 
ATOM   912  O  O   . TYR A 1 134 ? -97.679  2.804   280.683 1.00 32.35  ? 134 TYR A O   1 
ATOM   913  C  CB  . TYR A 1 134 ? -98.446  5.142   282.354 1.00 26.19  ? 134 TYR A CB  1 
ATOM   914  C  CG  . TYR A 1 134 ? -99.437  4.287   283.113 1.00 41.35  ? 134 TYR A CG  1 
ATOM   915  C  CD1 . TYR A 1 134 ? -99.343  4.134   284.489 1.00 37.78  ? 134 TYR A CD1 1 
ATOM   916  C  CD2 . TYR A 1 134 ? -100.468 3.633   282.450 1.00 29.37  ? 134 TYR A CD2 1 
ATOM   917  C  CE1 . TYR A 1 134 ? -100.247 3.352   285.184 1.00 19.81  ? 134 TYR A CE1 1 
ATOM   918  C  CE2 . TYR A 1 134 ? -101.376 2.851   283.137 1.00 22.24  ? 134 TYR A CE2 1 
ATOM   919  C  CZ  . TYR A 1 134 ? -101.261 2.714   284.504 1.00 20.14  ? 134 TYR A CZ  1 
ATOM   920  O  OH  . TYR A 1 134 ? -102.162 1.936   285.193 1.00 27.00  ? 134 TYR A OH  1 
ATOM   921  N  N   . THR A 1 135 ? -96.652  2.147   282.581 1.00 24.65  ? 135 THR A N   1 
ATOM   922  C  CA  . THR A 1 135 ? -96.854  0.729   282.326 1.00 26.36  ? 135 THR A CA  1 
ATOM   923  C  C   . THR A 1 135 ? -98.225  0.320   282.848 1.00 35.54  ? 135 THR A C   1 
ATOM   924  O  O   . THR A 1 135 ? -98.555  0.571   284.011 1.00 49.92  ? 135 THR A O   1 
ATOM   925  C  CB  . THR A 1 135 ? -95.758  -0.103  282.991 1.00 28.29  ? 135 THR A CB  1 
ATOM   926  O  OG1 . THR A 1 135 ? -95.937  -0.086  284.412 1.00 37.76  ? 135 THR A OG1 1 
ATOM   927  C  CG2 . THR A 1 135 ? -94.386  0.462   282.651 1.00 47.53  ? 135 THR A CG2 1 
ATOM   928  N  N   . TRP A 1 136 ? -99.023  -0.304  281.985 1.00 28.16  ? 136 TRP A N   1 
ATOM   929  C  CA  . TRP A 1 136 ? -100.420 -0.579  282.301 1.00 26.79  ? 136 TRP A CA  1 
ATOM   930  C  C   . TRP A 1 136 ? -100.528 -1.566  283.459 1.00 23.04  ? 136 TRP A C   1 
ATOM   931  O  O   . TRP A 1 136 ? -100.103 -2.721  283.347 1.00 30.40  ? 136 TRP A O   1 
ATOM   932  C  CB  . TRP A 1 136 ? -101.139 -1.108  281.064 1.00 24.58  ? 136 TRP A CB  1 
ATOM   933  C  CG  . TRP A 1 136 ? -101.177 -0.106  279.954 1.00 25.28  ? 136 TRP A CG  1 
ATOM   934  C  CD1 . TRP A 1 136 ? -100.302 -0.001  278.913 1.00 26.67  ? 136 TRP A CD1 1 
ATOM   935  C  CD2 . TRP A 1 136 ? -102.127 0.952   279.787 1.00 31.09  ? 136 TRP A CD2 1 
ATOM   936  N  NE1 . TRP A 1 136 ? -100.656 1.049   278.101 1.00 36.19  ? 136 TRP A NE1 1 
ATOM   937  C  CE2 . TRP A 1 136 ? -101.773 1.651   278.617 1.00 33.37  ? 136 TRP A CE2 1 
ATOM   938  C  CE3 . TRP A 1 136 ? -103.247 1.373   280.511 1.00 28.24  ? 136 TRP A CE3 1 
ATOM   939  C  CZ2 . TRP A 1 136 ? -102.496 2.747   278.155 1.00 28.86  ? 136 TRP A CZ2 1 
ATOM   940  C  CZ3 . TRP A 1 136 ? -103.964 2.459   280.050 1.00 30.34  ? 136 TRP A CZ3 1 
ATOM   941  C  CH2 . TRP A 1 136 ? -103.587 3.134   278.883 1.00 44.26  ? 136 TRP A CH2 1 
ATOM   942  N  N   . LEU A 1 137 ? -101.104 -1.110  284.566 1.00 20.54  ? 137 LEU A N   1 
ATOM   943  C  CA  . LEU A 1 137 ? -101.272 -1.909  285.769 1.00 22.22  ? 137 LEU A CA  1 
ATOM   944  C  C   . LEU A 1 137 ? -102.748 -2.189  286.017 1.00 22.14  ? 137 LEU A C   1 
ATOM   945  O  O   . LEU A 1 137 ? -103.630 -1.455  285.561 1.00 21.18  ? 137 LEU A O   1 
ATOM   946  C  CB  . LEU A 1 137 ? -100.672 -1.201  286.988 1.00 25.69  ? 137 LEU A CB  1 
ATOM   947  C  CG  . LEU A 1 137 ? -99.227  -0.715  286.879 1.00 30.75  ? 137 LEU A CG  1 
ATOM   948  C  CD1 . LEU A 1 137 ? -98.809  0.001   288.153 1.00 68.49  ? 137 LEU A CD1 1 
ATOM   949  C  CD2 . LEU A 1 137 ? -98.291  -1.874  286.578 1.00 56.23  ? 137 LEU A CD2 1 
ATOM   950  N  N   . GLU A 1 138 ? -103.000 -3.268  286.756 1.00 23.18  ? 138 GLU A N   1 
ATOM   951  C  CA  . GLU A 1 138 ? -104.344 -3.673  287.192 1.00 18.50  ? 138 GLU A CA  1 
ATOM   952  C  C   . GLU A 1 138 ? -105.208 -3.877  285.949 1.00 18.59  ? 138 GLU A C   1 
ATOM   953  O  O   . GLU A 1 138 ? -104.790 -4.606  285.035 1.00 19.01  ? 138 GLU A O   1 
ATOM   954  C  CB  . GLU A 1 138 ? -104.870 -2.660  288.201 1.00 17.92  ? 138 GLU A CB  1 
ATOM   955  C  CG  . GLU A 1 138 ? -103.926 -2.390  289.357 1.00 19.19  ? 138 GLU A CG  1 
ATOM   956  C  CD  . GLU A 1 138 ? -104.542 -1.492  290.409 1.00 36.09  ? 138 GLU A CD  1 
ATOM   957  O  OE1 . GLU A 1 138 ? -105.295 -2.009  291.261 1.00 19.77  ? 138 GLU A OE1 1 
ATOM   958  O  OE2 . GLU A 1 138 ? -104.278 -0.272  290.385 1.00 38.28  ? 138 GLU A OE2 1 
ATOM   959  N  N   . ASN A 1 139 ? -106.393 -3.272  285.864 1.00 21.12  ? 139 ASN A N   1 
ATOM   960  C  CA  . ASN A 1 139 ? -107.309 -3.490  284.753 1.00 22.92  ? 139 ASN A CA  1 
ATOM   961  C  C   . ASN A 1 139 ? -107.391 -2.294  283.811 1.00 20.80  ? 139 ASN A C   1 
ATOM   962  O  O   . ASN A 1 139 ? -108.288 -2.248  282.963 1.00 24.99  ? 139 ASN A O   1 
ATOM   963  C  CB  . ASN A 1 139 ? -108.702 -3.837  285.283 1.00 22.78  ? 139 ASN A CB  1 
ATOM   964  C  CG  . ASN A 1 139 ? -108.692 -5.044  286.201 1.00 32.14  ? 139 ASN A CG  1 
ATOM   965  O  OD1 . ASN A 1 139 ? -107.843 -5.927  286.075 1.00 24.24  ? 139 ASN A OD1 1 
ATOM   966  N  ND2 . ASN A 1 139 ? -109.637 -5.087  287.133 1.00 40.12  ? 139 ASN A ND2 1 
ATOM   967  N  N   . ASN A 1 140 ? -106.484 -1.330  283.938 1.00 18.62  ? 140 ASN A N   1 
ATOM   968  C  CA  . ASN A 1 140 ? -106.481 -0.184  283.039 1.00 23.10  ? 140 ASN A CA  1 
ATOM   969  C  C   . ASN A 1 140 ? -106.082 -0.620  281.635 1.00 24.34  ? 140 ASN A C   1 
ATOM   970  O  O   . ASN A 1 140 ? -105.107 -1.356  281.457 1.00 42.17  ? 140 ASN A O   1 
ATOM   971  C  CB  . ASN A 1 140 ? -105.522 0.890   283.550 1.00 30.53  ? 140 ASN A CB  1 
ATOM   972  C  CG  . ASN A 1 140 ? -106.000 1.539   284.833 1.00 27.00  ? 140 ASN A CG  1 
ATOM   973  O  OD1 . ASN A 1 140 ? -106.794 2.479   284.808 1.00 19.21  ? 140 ASN A OD1 1 
ATOM   974  N  ND2 . ASN A 1 140 ? -105.514 1.042   285.965 1.00 22.42  ? 140 ASN A ND2 1 
ATOM   975  N  N   . LYS A 1 141 ? -106.837 -0.169  280.637 1.00 26.55  ? 141 LYS A N   1 
ATOM   976  C  CA  . LYS A 1 141 ? -106.528 -0.464  279.246 1.00 33.09  ? 141 LYS A CA  1 
ATOM   977  C  C   . LYS A 1 141 ? -106.936 0.727   278.394 1.00 38.59  ? 141 LYS A C   1 
ATOM   978  O  O   . LYS A 1 141 ? -107.880 1.443   278.749 1.00 43.84  ? 141 LYS A O   1 
ATOM   979  C  CB  . LYS A 1 141 ? -107.241 -1.737  278.759 1.00 32.63  ? 141 LYS A CB  1 
ATOM   980  C  CG  . LYS A 1 141 ? -108.592 -1.999  279.397 1.00 31.87  ? 141 LYS A CG  1 
ATOM   981  C  CD  . LYS A 1 141 ? -109.236 -3.249  278.811 1.00 36.07  ? 141 LYS A CD  1 
ATOM   982  C  CE  . LYS A 1 141 ? -110.456 -3.682  279.610 1.00 39.16  ? 141 LYS A CE  1 
ATOM   983  N  NZ  . LYS A 1 141 ? -111.532 -2.653  279.593 1.00 35.01  ? 141 LYS A NZ  1 
ATOM   984  N  N   . PRO A 1 142 ? -106.239 0.976   277.272 1.00 35.65  ? 142 PRO A N   1 
ATOM   985  C  CA  . PRO A 1 142 ? -106.538 2.067   276.332 1.00 38.42  ? 142 PRO A CA  1 
ATOM   986  C  C   . PRO A 1 142 ? -107.973 2.019   275.805 1.00 46.67  ? 142 PRO A C   1 
ATOM   987  O  O   . PRO A 1 142 ? -108.556 0.936   275.758 1.00 88.38  ? 142 PRO A O   1 
ATOM   988  C  CB  . PRO A 1 142 ? -105.534 1.834   275.195 1.00 52.94  ? 142 PRO A CB  1 
ATOM   989  C  CG  . PRO A 1 142 ? -104.431 1.061   275.809 1.00 38.58  ? 142 PRO A CG  1 
ATOM   990  C  CD  . PRO A 1 142 ? -105.059 0.198   276.853 1.00 32.54  ? 142 PRO A CD  1 
ATOM   991  N  N   . GLY A 1 143 ? -108.533 3.162   275.410 1.00 47.73  ? 143 GLY A N   1 
ATOM   992  C  CA  . GLY A 1 143 ? -107.827 4.432   275.423 1.00 43.03  ? 143 GLY A CA  1 
ATOM   993  C  C   . GLY A 1 143 ? -108.502 5.522   276.233 1.00 50.27  ? 143 GLY A C   1 
ATOM   994  O  O   . GLY A 1 143 ? -108.967 5.283   277.347 1.00 67.70  ? 143 GLY A O   1 
ATOM   995  N  N   . ARG A 1 144 ? -108.562 6.725   275.665 1.00 37.52  ? 144 ARG A N   1 
ATOM   996  C  CA  . ARG A 1 144 ? -109.048 7.902   276.369 1.00 34.95  ? 144 ARG A CA  1 
ATOM   997  C  C   . ARG A 1 144 ? -110.181 8.554   275.588 1.00 36.82  ? 144 ARG A C   1 
ATOM   998  O  O   . ARG A 1 144 ? -110.189 8.554   274.354 1.00 51.75  ? 144 ARG A O   1 
ATOM   999  C  CB  . ARG A 1 144 ? -107.916 8.919   276.591 1.00 32.96  ? 144 ARG A CB  1 
ATOM   1000 C  CG  . ARG A 1 144 ? -108.291 10.105  277.465 1.00 36.53  ? 144 ARG A CG  1 
ATOM   1001 C  CD  . ARG A 1 144 ? -107.163 11.126  277.542 1.00 36.17  ? 144 ARG A CD  1 
ATOM   1002 N  NE  . ARG A 1 144 ? -106.971 11.839  276.282 1.00 27.06  ? 144 ARG A NE  1 
ATOM   1003 C  CZ  . ARG A 1 144 ? -106.032 11.543  275.389 1.00 24.43  ? 144 ARG A CZ  1 
ATOM   1004 N  NH1 . ARG A 1 144 ? -105.188 10.546  275.616 1.00 23.92  ? 144 ARG A NH1 1 
ATOM   1005 N  NH2 . ARG A 1 144 ? -105.933 12.247  274.270 1.00 24.72  ? 144 ARG A NH2 1 
ATOM   1006 N  N   . ARG A 1 145 ? -111.142 9.108   276.326 1.00 37.31  ? 145 ARG A N   1 
ATOM   1007 C  CA  . ARG A 1 145 ? -112.231 9.882   275.740 1.00 40.46  ? 145 ARG A CA  1 
ATOM   1008 C  C   . ARG A 1 145 ? -111.706 11.277  275.418 1.00 39.44  ? 145 ARG A C   1 
ATOM   1009 O  O   . ARG A 1 145 ? -111.491 12.090  276.322 1.00 37.92  ? 145 ARG A O   1 
ATOM   1010 C  CB  . ARG A 1 145 ? -113.414 9.942   276.702 1.00 45.97  ? 145 ARG A CB  1 
ATOM   1011 C  CG  . ARG A 1 145 ? -114.618 10.708  276.182 1.00 78.63  ? 145 ARG A CG  1 
ATOM   1012 C  CD  . ARG A 1 145 ? -115.335 9.936   275.088 1.00 70.73  ? 145 ARG A CD  1 
ATOM   1013 N  NE  . ARG A 1 145 ? -116.489 10.668  274.572 1.00 72.75  ? 145 ARG A NE  1 
ATOM   1014 C  CZ  . ARG A 1 145 ? -117.732 10.510  275.015 1.00 67.00  ? 145 ARG A CZ  1 
ATOM   1015 N  NH1 . ARG A 1 145 ? -117.986 9.643   275.986 1.00 70.86  ? 145 ARG A NH1 1 
ATOM   1016 N  NH2 . ARG A 1 145 ? -118.721 11.218  274.488 1.00 57.39  ? 145 ARG A NH2 1 
ATOM   1017 N  N   . GLU A 1 146 ? -111.502 11.559  274.131 1.00 38.24  ? 146 GLU A N   1 
ATOM   1018 C  CA  . GLU A 1 146 ? -110.786 12.763  273.726 1.00 36.43  ? 146 GLU A CA  1 
ATOM   1019 C  C   . GLU A 1 146 ? -111.689 13.973  273.529 1.00 41.00  ? 146 GLU A C   1 
ATOM   1020 O  O   . GLU A 1 146 ? -111.233 15.107  273.714 1.00 47.61  ? 146 GLU A O   1 
ATOM   1021 C  CB  . GLU A 1 146 ? -110.002 12.496  272.438 1.00 37.70  ? 146 GLU A CB  1 
ATOM   1022 C  CG  . GLU A 1 146 ? -108.887 11.477  272.606 1.00 38.00  ? 146 GLU A CG  1 
ATOM   1023 C  CD  . GLU A 1 146 ? -107.894 11.502  271.464 1.00 36.45  ? 146 GLU A CD  1 
ATOM   1024 O  OE1 . GLU A 1 146 ? -108.111 12.267  270.502 1.00 35.87  ? 146 GLU A OE1 1 
ATOM   1025 O  OE2 . GLU A 1 146 ? -106.895 10.754  271.529 1.00 61.01  ? 146 GLU A OE2 1 
ATOM   1026 N  N   . ASP A 1 147 ? -112.951 13.772  273.156 1.00 45.12  ? 147 ASP A N   1 
ATOM   1027 C  CA  . ASP A 1 147 ? -113.858 14.896  272.964 1.00 43.48  ? 147 ASP A CA  1 
ATOM   1028 C  C   . ASP A 1 147 ? -114.481 15.383  274.265 1.00 39.51  ? 147 ASP A C   1 
ATOM   1029 O  O   . ASP A 1 147 ? -115.196 16.391  274.250 1.00 51.75  ? 147 ASP A O   1 
ATOM   1030 C  CB  . ASP A 1 147 ? -114.964 14.526  271.972 1.00 46.04  ? 147 ASP A CB  1 
ATOM   1031 C  CG  . ASP A 1 147 ? -115.784 13.339  272.432 1.00 58.62  ? 147 ASP A CG  1 
ATOM   1032 O  OD1 . ASP A 1 147 ? -115.212 12.439  273.080 1.00 66.25  ? 147 ASP A OD1 1 
ATOM   1033 O  OD2 . ASP A 1 147 ? -116.998 13.307  272.144 1.00 74.17  ? 147 ASP A OD2 1 
ATOM   1034 N  N   . LYS A 1 148 ? -114.232 14.701  275.380 1.00 40.35  ? 148 LYS A N   1 
ATOM   1035 C  CA  . LYS A 1 148 ? -114.759 15.095  276.677 1.00 36.74  ? 148 LYS A CA  1 
ATOM   1036 C  C   . LYS A 1 148 ? -113.627 15.127  277.695 1.00 31.22  ? 148 LYS A C   1 
ATOM   1037 O  O   . LYS A 1 148 ? -112.604 14.454  277.541 1.00 31.46  ? 148 LYS A O   1 
ATOM   1038 C  CB  . LYS A 1 148 ? -115.869 14.144  277.149 1.00 41.35  ? 148 LYS A CB  1 
ATOM   1039 C  CG  . LYS A 1 148 ? -117.049 14.046  276.193 1.00 45.92  ? 148 LYS A CG  1 
ATOM   1040 C  CD  . LYS A 1 148 ? -117.830 15.350  276.140 1.00 50.29  ? 148 LYS A CD  1 
ATOM   1041 C  CE  . LYS A 1 148 ? -119.067 15.218  275.267 1.00 43.68  ? 148 LYS A CE  1 
ATOM   1042 N  NZ  . LYS A 1 148 ? -119.811 16.504  275.163 1.00 40.67  ? 148 LYS A NZ  1 
ATOM   1043 N  N   . ILE A 1 149 ? -113.823 15.919  278.744 1.00 30.00  ? 149 ILE A N   1 
ATOM   1044 C  CA  . ILE A 1 149 ? -112.803 16.104  279.770 1.00 26.79  ? 149 ILE A CA  1 
ATOM   1045 C  C   . ILE A 1 149 ? -112.801 14.894  280.695 1.00 23.42  ? 149 ILE A C   1 
ATOM   1046 O  O   . ILE A 1 149 ? -113.822 14.562  281.305 1.00 22.26  ? 149 ILE A O   1 
ATOM   1047 C  CB  . ILE A 1 149 ? -113.039 17.400  280.559 1.00 26.40  ? 149 ILE A CB  1 
ATOM   1048 C  CG1 . ILE A 1 149 ? -112.989 18.609  279.624 1.00 29.08  ? 149 ILE A CG1 1 
ATOM   1049 C  CG2 . ILE A 1 149 ? -112.015 17.539  281.674 1.00 26.30  ? 149 ILE A CG2 1 
ATOM   1050 C  CD1 . ILE A 1 149 ? -111.669 18.773  278.907 1.00 31.62  ? 149 ILE A CD1 1 
ATOM   1051 N  N   . VAL A 1 150 ? -111.651 14.234  280.802 1.00 22.43  ? 150 VAL A N   1 
ATOM   1052 C  CA  . VAL A 1 150 ? -111.461 13.104  281.705 1.00 23.03  ? 150 VAL A CA  1 
ATOM   1053 C  C   . VAL A 1 150 ? -110.357 13.504  282.676 1.00 24.09  ? 150 VAL A C   1 
ATOM   1054 O  O   . VAL A 1 150 ? -109.167 13.390  282.360 1.00 23.55  ? 150 VAL A O   1 
ATOM   1055 C  CB  . VAL A 1 150 ? -111.109 11.813  280.960 1.00 25.73  ? 150 VAL A CB  1 
ATOM   1056 C  CG1 . VAL A 1 150 ? -111.018 10.648  281.934 1.00 23.63  ? 150 VAL A CG1 1 
ATOM   1057 C  CG2 . VAL A 1 150 ? -112.137 11.529  279.876 1.00 28.93  ? 150 VAL A CG2 1 
ATOM   1058 N  N   . ALA A 1 151 ? -110.744 13.975  283.855 1.00 24.23  ? 151 ALA A N   1 
ATOM   1059 C  CA  . ALA A 1 151 ? -109.808 14.439  284.866 1.00 21.42  ? 151 ALA A CA  1 
ATOM   1060 C  C   . ALA A 1 151 ? -109.770 13.470  286.039 1.00 19.12  ? 151 ALA A C   1 
ATOM   1061 O  O   . ALA A 1 151 ? -110.638 12.607  286.199 1.00 21.20  ? 151 ALA A O   1 
ATOM   1062 C  CB  . ALA A 1 151 ? -110.181 15.845  285.350 1.00 23.23  ? 151 ALA A CB  1 
ATOM   1063 N  N   . ALA A 1 152 ? -108.740 13.625  286.866 1.00 15.94  ? 152 ALA A N   1 
ATOM   1064 C  CA  . ALA A 1 152 ? -108.575 12.802  288.054 1.00 16.22  ? 152 ALA A CA  1 
ATOM   1065 C  C   . ALA A 1 152 ? -107.690 13.547  289.039 1.00 18.58  ? 152 ALA A C   1 
ATOM   1066 O  O   . ALA A 1 152 ? -106.862 14.374  288.648 1.00 22.07  ? 152 ALA A O   1 
ATOM   1067 C  CB  . ALA A 1 152 ? -107.972 11.434  287.718 1.00 14.91  ? 152 ALA A CB  1 
ATOM   1068 N  N   . TYR A 1 153 ? -107.877 13.246  290.319 1.00 15.31  ? 153 TYR A N   1 
ATOM   1069 C  CA  . TYR A 1 153 ? -107.130 13.886  291.392 1.00 15.35  ? 153 TYR A CA  1 
ATOM   1070 C  C   . TYR A 1 153 ? -106.028 12.960  291.885 1.00 18.95  ? 153 TYR A C   1 
ATOM   1071 O  O   . TYR A 1 153 ? -106.289 11.803  292.231 1.00 22.02  ? 153 TYR A O   1 
ATOM   1072 C  CB  . TYR A 1 153 ? -108.051 14.258  292.552 1.00 16.75  ? 153 TYR A CB  1 
ATOM   1073 C  CG  . TYR A 1 153 ? -108.665 15.634  292.454 1.00 21.67  ? 153 TYR A CG  1 
ATOM   1074 C  CD1 . TYR A 1 153 ? -107.978 16.753  292.904 1.00 23.47  ? 153 TYR A CD1 1 
ATOM   1075 C  CD2 . TYR A 1 153 ? -109.939 15.814  291.932 1.00 37.06  ? 153 TYR A CD2 1 
ATOM   1076 C  CE1 . TYR A 1 153 ? -108.535 18.014  292.824 1.00 24.87  ? 153 TYR A CE1 1 
ATOM   1077 C  CE2 . TYR A 1 153 ? -110.507 17.072  291.851 1.00 23.51  ? 153 TYR A CE2 1 
ATOM   1078 C  CZ  . TYR A 1 153 ? -109.799 18.168  292.296 1.00 25.77  ? 153 TYR A CZ  1 
ATOM   1079 O  OH  . TYR A 1 153 ? -110.356 19.423  292.217 1.00 34.03  ? 153 TYR A OH  1 
ATOM   1080 N  N   . PHE A 1 154 ? -104.803 13.476  291.924 1.00 17.60  ? 154 PHE A N   1 
ATOM   1081 C  CA  . PHE A 1 154 ? -103.662 12.765  292.485 1.00 14.07  ? 154 PHE A CA  1 
ATOM   1082 C  C   . PHE A 1 154 ? -103.345 13.358  293.851 1.00 12.85  ? 154 PHE A C   1 
ATOM   1083 O  O   . PHE A 1 154 ? -103.108 14.565  293.967 1.00 13.44  ? 154 PHE A O   1 
ATOM   1084 C  CB  . PHE A 1 154 ? -102.452 12.857  291.556 1.00 15.60  ? 154 PHE A CB  1 
ATOM   1085 C  CG  . PHE A 1 154 ? -101.224 12.176  292.091 1.00 16.20  ? 154 PHE A CG  1 
ATOM   1086 C  CD1 . PHE A 1 154 ? -101.059 10.809  291.953 1.00 16.23  ? 154 PHE A CD1 1 
ATOM   1087 C  CD2 . PHE A 1 154 ? -100.228 12.905  292.721 1.00 14.86  ? 154 PHE A CD2 1 
ATOM   1088 C  CE1 . PHE A 1 154 ? -99.929  10.180  292.438 1.00 16.48  ? 154 PHE A CE1 1 
ATOM   1089 C  CE2 . PHE A 1 154 ? -99.097  12.282  293.209 1.00 14.20  ? 154 PHE A CE2 1 
ATOM   1090 C  CZ  . PHE A 1 154 ? -98.947  10.917  293.067 1.00 17.49  ? 154 PHE A CZ  1 
ATOM   1091 N  N   . VAL A 1 155 ? -103.345 12.517  294.876 1.00 13.80  ? 155 VAL A N   1 
ATOM   1092 C  CA  . VAL A 1 155 ? -103.094 12.977  296.236 1.00 17.56  ? 155 VAL A CA  1 
ATOM   1093 C  C   . VAL A 1 155 ? -101.593 13.080  296.467 1.00 18.72  ? 155 VAL A C   1 
ATOM   1094 O  O   . VAL A 1 155 ? -100.815 12.228  296.018 1.00 20.14  ? 155 VAL A O   1 
ATOM   1095 C  CB  . VAL A 1 155 ? -103.760 12.037  297.256 1.00 20.40  ? 155 VAL A CB  1 
ATOM   1096 C  CG1 . VAL A 1 155 ? -105.269 12.206  297.219 1.00 24.68  ? 155 VAL A CG1 1 
ATOM   1097 C  CG2 . VAL A 1 155 ? -103.379 10.595  296.977 1.00 24.54  ? 155 VAL A CG2 1 
ATOM   1098 N  N   . GLU A 1 156 ? -101.180 14.137  297.168 1.00 18.18  ? 156 GLU A N   1 
ATOM   1099 C  CA  . GLU A 1 156 ? -99.762  14.327  297.456 1.00 16.83  ? 156 GLU A CA  1 
ATOM   1100 C  C   . GLU A 1 156 ? -99.250  13.276  298.433 1.00 17.92  ? 156 GLU A C   1 
ATOM   1101 O  O   . GLU A 1 156 ? -98.122  12.789  298.295 1.00 18.10  ? 156 GLU A O   1 
ATOM   1102 C  CB  . GLU A 1 156 ? -99.528  15.734  298.006 1.00 15.50  ? 156 GLU A CB  1 
ATOM   1103 C  CG  . GLU A 1 156 ? -98.111  15.996  298.485 1.00 16.55  ? 156 GLU A CG  1 
ATOM   1104 C  CD  . GLU A 1 156 ? -97.865  17.460  298.791 1.00 18.90  ? 156 GLU A CD  1 
ATOM   1105 O  OE1 . GLU A 1 156 ? -97.904  17.836  299.981 1.00 19.55  ? 156 GLU A OE1 1 
ATOM   1106 O  OE2 . GLU A 1 156 ? -97.634  18.236  297.840 1.00 16.80  ? 156 GLU A OE2 1 
ATOM   1107 N  N   . TRP A 1 157 ? -100.065 12.909  299.418 1.00 19.54  ? 157 TRP A N   1 
ATOM   1108 C  CA  . TRP A 1 157 ? -99.687  11.932  300.430 1.00 18.98  ? 157 TRP A CA  1 
ATOM   1109 C  C   . TRP A 1 157 ? -99.888  10.492  299.973 1.00 20.07  ? 157 TRP A C   1 
ATOM   1110 O  O   . TRP A 1 157 ? -99.851  9.584   300.809 1.00 19.78  ? 157 TRP A O   1 
ATOM   1111 C  CB  . TRP A 1 157 ? -100.477 12.182  301.718 1.00 21.97  ? 157 TRP A CB  1 
ATOM   1112 C  CG  . TRP A 1 157 ? -101.964 12.093  301.537 1.00 26.97  ? 157 TRP A CG  1 
ATOM   1113 C  CD1 . TRP A 1 157 ? -102.761 11.022  301.818 1.00 42.08  ? 157 TRP A CD1 1 
ATOM   1114 C  CD2 . TRP A 1 157 ? -102.832 13.117  301.033 1.00 25.68  ? 157 TRP A CD2 1 
ATOM   1115 N  NE1 . TRP A 1 157 ? -104.070 11.315  301.522 1.00 41.00  ? 157 TRP A NE1 1 
ATOM   1116 C  CE2 . TRP A 1 157 ? -104.141 12.595  301.038 1.00 27.81  ? 157 TRP A CE2 1 
ATOM   1117 C  CE3 . TRP A 1 157 ? -102.630 14.424  300.579 1.00 22.79  ? 157 TRP A CE3 1 
ATOM   1118 C  CZ2 . TRP A 1 157 ? -105.240 13.333  300.607 1.00 29.03  ? 157 TRP A CZ2 1 
ATOM   1119 C  CZ3 . TRP A 1 157 ? -103.724 15.154  300.151 1.00 20.98  ? 157 TRP A CZ3 1 
ATOM   1120 C  CH2 . TRP A 1 157 ? -105.012 14.607  300.168 1.00 23.91  ? 157 TRP A CH2 1 
ATOM   1121 N  N   . GLY A 1 158 ? -100.097 10.262  298.677 1.00 18.54  ? 158 GLY A N   1 
ATOM   1122 C  CA  . GLY A 1 158 ? -100.333 8.921   298.178 1.00 16.40  ? 158 GLY A CA  1 
ATOM   1123 C  C   . GLY A 1 158 ? -99.105  8.048   298.054 1.00 17.63  ? 158 GLY A C   1 
ATOM   1124 O  O   . GLY A 1 158 ? -99.240  6.850   297.788 1.00 16.63  ? 158 GLY A O   1 
ATOM   1125 N  N   . VAL A 1 159 ? -97.909  8.614   298.240 1.00 19.64  ? 159 VAL A N   1 
ATOM   1126 C  CA  . VAL A 1 159 ? -96.681  7.829   298.126 1.00 20.41  ? 159 VAL A CA  1 
ATOM   1127 C  C   . VAL A 1 159 ? -96.347  7.062   299.392 1.00 23.12  ? 159 VAL A C   1 
ATOM   1128 O  O   . VAL A 1 159 ? -95.436  6.226   299.374 1.00 23.70  ? 159 VAL A O   1 
ATOM   1129 C  CB  . VAL A 1 159 ? -95.482  8.726   297.766 1.00 23.54  ? 159 VAL A CB  1 
ATOM   1130 C  CG1 . VAL A 1 159 ? -95.707  9.402   296.423 1.00 24.73  ? 159 VAL A CG1 1 
ATOM   1131 C  CG2 . VAL A 1 159 ? -95.249  9.752   298.859 1.00 22.19  ? 159 VAL A CG2 1 
ATOM   1132 N  N   . TYR A 1 160 ? -97.054  7.318   300.492 1.00 22.13  ? 160 TYR A N   1 
ATOM   1133 C  CA  . TYR A 1 160 ? -96.772  6.639   301.750 1.00 18.49  ? 160 TYR A CA  1 
ATOM   1134 C  C   . TYR A 1 160 ? -97.538  5.326   301.852 1.00 20.04  ? 160 TYR A C   1 
ATOM   1135 O  O   . TYR A 1 160 ? -97.220  4.360   301.151 1.00 23.16  ? 160 TYR A O   1 
ATOM   1136 C  CB  . TYR A 1 160 ? -97.111  7.545   302.934 1.00 17.90  ? 160 TYR A CB  1 
ATOM   1137 C  CG  . TYR A 1 160 ? -96.284  8.808   302.990 1.00 21.15  ? 160 TYR A CG  1 
ATOM   1138 C  CD1 . TYR A 1 160 ? -94.917  8.754   303.224 1.00 19.76  ? 160 TYR A CD1 1 
ATOM   1139 C  CD2 . TYR A 1 160 ? -96.868  10.054  302.811 1.00 25.95  ? 160 TYR A CD2 1 
ATOM   1140 C  CE1 . TYR A 1 160 ? -94.155  9.904   303.277 1.00 20.12  ? 160 TYR A CE1 1 
ATOM   1141 C  CE2 . TYR A 1 160 ? -96.114  11.211  302.862 1.00 25.13  ? 160 TYR A CE2 1 
ATOM   1142 C  CZ  . TYR A 1 160 ? -94.758  11.129  303.096 1.00 23.63  ? 160 TYR A CZ  1 
ATOM   1143 O  OH  . TYR A 1 160 ? -94.001  12.276  303.148 1.00 35.98  ? 160 TYR A OH  1 
ATOM   1144 N  N   . GLY A 1 161 ? -98.546  5.285   302.726 1.00 15.98  ? 161 GLY A N   1 
ATOM   1145 C  CA  . GLY A 1 161 ? -99.288  4.050   302.929 1.00 15.49  ? 161 GLY A CA  1 
ATOM   1146 C  C   . GLY A 1 161 ? -99.997  3.575   301.676 1.00 19.74  ? 161 GLY A C   1 
ATOM   1147 O  O   . GLY A 1 161 ? -100.081 2.372   301.417 1.00 24.77  ? 161 GLY A O   1 
ATOM   1148 N  N   . ARG A 1 162 ? -100.515 4.512   300.878 1.00 19.29  ? 162 ARG A N   1 
ATOM   1149 C  CA  . ARG A 1 162 ? -101.198 4.131   299.646 1.00 17.89  ? 162 ARG A CA  1 
ATOM   1150 C  C   . ARG A 1 162 ? -100.231 3.558   298.619 1.00 17.72  ? 162 ARG A C   1 
ATOM   1151 O  O   . ARG A 1 162 ? -100.625 2.707   297.812 1.00 18.45  ? 162 ARG A O   1 
ATOM   1152 C  CB  . ARG A 1 162 ? -101.944 5.333   299.067 1.00 23.16  ? 162 ARG A CB  1 
ATOM   1153 C  CG  . ARG A 1 162 ? -103.194 5.713   299.842 1.00 21.18  ? 162 ARG A CG  1 
ATOM   1154 C  CD  . ARG A 1 162 ? -103.846 6.961   299.271 1.00 17.40  ? 162 ARG A CD  1 
ATOM   1155 N  NE  . ARG A 1 162 ? -105.186 7.175   299.810 1.00 22.29  ? 162 ARG A NE  1 
ATOM   1156 C  CZ  . ARG A 1 162 ? -105.439 7.706   301.002 1.00 24.22  ? 162 ARG A CZ  1 
ATOM   1157 N  NH1 . ARG A 1 162 ? -104.442 8.080   301.792 1.00 24.91  ? 162 ARG A NH1 1 
ATOM   1158 N  NH2 . ARG A 1 162 ? -106.693 7.862   301.406 1.00 24.03  ? 162 ARG A NH2 1 
ATOM   1159 N  N   . ASN A 1 163 ? -98.975  4.002   298.635 1.00 18.45  ? 163 ASN A N   1 
ATOM   1160 C  CA  . ASN A 1 163 ? -97.934  3.514   297.731 1.00 21.05  ? 163 ASN A CA  1 
ATOM   1161 C  C   . ASN A 1 163 ? -98.375  3.637   296.272 1.00 17.75  ? 163 ASN A C   1 
ATOM   1162 O  O   . ASN A 1 163 ? -98.462  2.658   295.529 1.00 17.35  ? 163 ASN A O   1 
ATOM   1163 C  CB  . ASN A 1 163 ? -97.548  2.072   298.072 1.00 28.86  ? 163 ASN A CB  1 
ATOM   1164 C  CG  . ASN A 1 163 ? -96.272  1.631   297.383 1.00 29.30  ? 163 ASN A CG  1 
ATOM   1165 O  OD1 . ASN A 1 163 ? -95.343  2.419   297.206 1.00 23.58  ? 163 ASN A OD1 1 
ATOM   1166 N  ND2 . ASN A 1 163 ? -96.221  0.364   296.986 1.00 50.25  ? 163 ASN A ND2 1 
ATOM   1167 N  N   . PHE A 1 164 ? -98.656  4.873   295.871 1.00 16.68  ? 164 PHE A N   1 
ATOM   1168 C  CA  . PHE A 1 164 ? -99.153  5.172   294.528 1.00 15.15  ? 164 PHE A CA  1 
ATOM   1169 C  C   . PHE A 1 164 ? -98.459  6.418   294.002 1.00 15.69  ? 164 PHE A C   1 
ATOM   1170 O  O   . PHE A 1 164 ? -99.016  7.522   294.031 1.00 13.71  ? 164 PHE A O   1 
ATOM   1171 C  CB  . PHE A 1 164 ? -100.673 5.349   294.535 1.00 16.88  ? 164 PHE A CB  1 
ATOM   1172 C  CG  . PHE A 1 164 ? -101.317 5.132   293.197 1.00 16.40  ? 164 PHE A CG  1 
ATOM   1173 C  CD1 . PHE A 1 164 ? -101.379 6.156   292.268 1.00 18.22  ? 164 PHE A CD1 1 
ATOM   1174 C  CD2 . PHE A 1 164 ? -101.871 3.906   292.873 1.00 15.99  ? 164 PHE A CD2 1 
ATOM   1175 C  CE1 . PHE A 1 164 ? -101.975 5.959   291.038 1.00 15.60  ? 164 PHE A CE1 1 
ATOM   1176 C  CE2 . PHE A 1 164 ? -102.469 3.703   291.644 1.00 15.52  ? 164 PHE A CE2 1 
ATOM   1177 C  CZ  . PHE A 1 164 ? -102.521 4.731   290.727 1.00 15.39  ? 164 PHE A CZ  1 
ATOM   1178 N  N   . PRO A 1 165 ? -97.233  6.281   293.513 1.00 17.69  ? 165 PRO A N   1 
ATOM   1179 C  CA  . PRO A 1 165 ? -96.528  7.418   292.915 1.00 21.73  ? 165 PRO A CA  1 
ATOM   1180 C  C   . PRO A 1 165 ? -97.065  7.711   291.517 1.00 20.76  ? 165 PRO A C   1 
ATOM   1181 O  O   . PRO A 1 165 ? -97.977  7.052   291.022 1.00 18.64  ? 165 PRO A O   1 
ATOM   1182 C  CB  . PRO A 1 165 ? -95.073  6.945   292.878 1.00 17.10  ? 165 PRO A CB  1 
ATOM   1183 C  CG  . PRO A 1 165 ? -95.172  5.466   292.781 1.00 14.22  ? 165 PRO A CG  1 
ATOM   1184 C  CD  . PRO A 1 165 ? -96.389  5.075   293.569 1.00 17.33  ? 165 PRO A CD  1 
ATOM   1185 N  N   . VAL A 1 166 ? -96.467  8.722   290.880 1.00 13.62  ? 166 VAL A N   1 
ATOM   1186 C  CA  . VAL A 1 166 ? -96.947  9.180   289.579 1.00 13.49  ? 166 VAL A CA  1 
ATOM   1187 C  C   . VAL A 1 166 ? -96.807  8.091   288.525 1.00 16.08  ? 166 VAL A C   1 
ATOM   1188 O  O   . VAL A 1 166 ? -97.644  7.979   287.620 1.00 16.07  ? 166 VAL A O   1 
ATOM   1189 C  CB  . VAL A 1 166 ? -96.203  10.463  289.163 1.00 14.27  ? 166 VAL A CB  1 
ATOM   1190 C  CG1 . VAL A 1 166 ? -96.724  10.974  287.830 1.00 11.54  ? 166 VAL A CG1 1 
ATOM   1191 C  CG2 . VAL A 1 166 ? -96.341  11.525  290.241 1.00 42.50  ? 166 VAL A CG2 1 
ATOM   1192 N  N   . ASP A 1 167 ? -95.764  7.264   288.624 1.00 15.51  ? 167 ASP A N   1 
ATOM   1193 C  CA  . ASP A 1 167 ? -95.553  6.202   287.646 1.00 14.45  ? 167 ASP A CA  1 
ATOM   1194 C  C   . ASP A 1 167 ? -96.649  5.144   287.672 1.00 15.51  ? 167 ASP A C   1 
ATOM   1195 O  O   . ASP A 1 167 ? -96.642  4.250   286.818 1.00 14.04  ? 167 ASP A O   1 
ATOM   1196 C  CB  . ASP A 1 167 ? -94.189  5.550   287.873 1.00 12.85  ? 167 ASP A CB  1 
ATOM   1197 C  CG  . ASP A 1 167 ? -94.013  5.047   289.289 1.00 14.07  ? 167 ASP A CG  1 
ATOM   1198 O  OD1 . ASP A 1 167 ? -94.453  3.916   289.579 1.00 35.89  ? 167 ASP A OD1 1 
ATOM   1199 O  OD2 . ASP A 1 167 ? -93.432  5.785   290.113 1.00 13.96  ? 167 ASP A OD2 1 
ATOM   1200 N  N   . LYS A 1 168 ? -97.583  5.219   288.620 1.00 13.85  ? 168 LYS A N   1 
ATOM   1201 C  CA  . LYS A 1 168 ? -98.736  4.331   288.657 1.00 15.48  ? 168 LYS A CA  1 
ATOM   1202 C  C   . LYS A 1 168 ? -100.013 4.990   288.156 1.00 15.94  ? 168 LYS A C   1 
ATOM   1203 O  O   . LYS A 1 168 ? -101.038 4.310   288.042 1.00 14.77  ? 168 LYS A O   1 
ATOM   1204 C  CB  . LYS A 1 168 ? -98.967  3.818   290.083 1.00 14.34  ? 168 LYS A CB  1 
ATOM   1205 C  CG  . LYS A 1 168 ? -97.890  2.888   290.609 1.00 12.82  ? 168 LYS A CG  1 
ATOM   1206 C  CD  . LYS A 1 168 ? -98.280  2.344   291.973 1.00 14.75  ? 168 LYS A CD  1 
ATOM   1207 C  CE  . LYS A 1 168 ? -97.314  1.276   292.449 1.00 20.51  ? 168 LYS A CE  1 
ATOM   1208 N  NZ  . LYS A 1 168 ? -97.745  0.691   293.749 1.00 44.32  ? 168 LYS A NZ  1 
ATOM   1209 N  N   . VAL A 1 169 ? -99.980  6.281   287.854 1.00 15.54  ? 169 VAL A N   1 
ATOM   1210 C  CA  . VAL A 1 169 ? -101.199 7.011   287.501 1.00 15.86  ? 169 VAL A CA  1 
ATOM   1211 C  C   . VAL A 1 169 ? -101.533 6.735   286.037 1.00 20.17  ? 169 VAL A C   1 
ATOM   1212 O  O   . VAL A 1 169 ? -100.664 6.907   285.169 1.00 21.15  ? 169 VAL A O   1 
ATOM   1213 C  CB  . VAL A 1 169 ? -101.020 8.504   287.751 1.00 14.49  ? 169 VAL A CB  1 
ATOM   1214 C  CG1 . VAL A 1 169 ? -102.292 9.256   287.396 1.00 15.43  ? 169 VAL A CG1 1 
ATOM   1215 C  CG2 . VAL A 1 169 ? -100.631 8.752   289.196 1.00 13.73  ? 169 VAL A CG2 1 
ATOM   1216 N  N   . PRO A 1 170 ? -102.764 6.322   285.724 1.00 19.69  ? 170 PRO A N   1 
ATOM   1217 C  CA  . PRO A 1 170 ? -103.116 6.033   284.327 1.00 18.39  ? 170 PRO A CA  1 
ATOM   1218 C  C   . PRO A 1 170 ? -103.254 7.296   283.491 1.00 19.82  ? 170 PRO A C   1 
ATOM   1219 O  O   . PRO A 1 170 ? -104.358 7.663   283.079 1.00 19.87  ? 170 PRO A O   1 
ATOM   1220 C  CB  . PRO A 1 170 ? -104.456 5.291   284.442 1.00 22.79  ? 170 PRO A CB  1 
ATOM   1221 C  CG  . PRO A 1 170 ? -104.633 4.985   285.911 1.00 22.64  ? 170 PRO A CG  1 
ATOM   1222 C  CD  . PRO A 1 170 ? -103.877 6.038   286.642 1.00 16.17  ? 170 PRO A CD  1 
ATOM   1223 N  N   . LEU A 1 171 ? -102.129 7.959   283.234 1.00 20.71  ? 171 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 171 ? -102.161 9.213   282.485 1.00 20.47  ? 171 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 171 ? -102.634 9.073   281.041 1.00 23.58  ? 171 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 171 ? -103.306 10.002  280.559 1.00 30.05  ? 171 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 171 ? -100.777 9.869   282.541 1.00 18.54  ? 171 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 171 ? -100.319 10.212  283.958 1.00 21.66  ? 171 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 171 ? -98.904  10.745  283.945 1.00 18.26  ? 171 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 171 ? -101.267 11.219  284.586 1.00 17.19  ? 171 LEU A CD2 1 
ATOM   1231 N  N   . PRO A 1 172 ? -102.323 8.003   280.296 1.00 22.98  ? 172 PRO A N   1 
ATOM   1232 C  CA  . PRO A 1 172 ? -102.859 7.899   278.926 1.00 24.09  ? 172 PRO A CA  1 
ATOM   1233 C  C   . PRO A 1 172 ? -104.375 7.979   278.842 1.00 25.19  ? 172 PRO A C   1 
ATOM   1234 O  O   . PRO A 1 172 ? -104.899 8.349   277.785 1.00 34.80  ? 172 PRO A O   1 
ATOM   1235 C  CB  . PRO A 1 172 ? -102.344 6.534   278.454 1.00 23.44  ? 172 PRO A CB  1 
ATOM   1236 C  CG  . PRO A 1 172 ? -101.086 6.346   279.202 1.00 23.43  ? 172 PRO A CG  1 
ATOM   1237 C  CD  . PRO A 1 172 ? -101.317 6.955   280.556 1.00 21.23  ? 172 PRO A CD  1 
ATOM   1238 N  N   . ASN A 1 173 ? -105.096 7.650   279.913 1.00 23.34  ? 173 ASN A N   1 
ATOM   1239 C  CA  . ASN A 1 173 ? -106.549 7.745   279.936 1.00 24.07  ? 173 ASN A CA  1 
ATOM   1240 C  C   . ASN A 1 173 ? -107.039 9.007   280.636 1.00 23.02  ? 173 ASN A C   1 
ATOM   1241 O  O   . ASN A 1 173 ? -108.195 9.059   281.069 1.00 25.65  ? 173 ASN A O   1 
ATOM   1242 C  CB  . ASN A 1 173 ? -107.151 6.508   280.606 1.00 26.17  ? 173 ASN A CB  1 
ATOM   1243 C  CG  . ASN A 1 173 ? -106.861 5.232   279.843 1.00 28.26  ? 173 ASN A CG  1 
ATOM   1244 O  OD1 . ASN A 1 173 ? -106.493 5.265   278.670 1.00 27.80  ? 173 ASN A OD1 1 
ATOM   1245 N  ND2 . ASN A 1 173 ? -107.033 4.095   280.508 1.00 26.10  ? 173 ASN A ND2 1 
ATOM   1246 N  N   . LEU A 1 174 ? -106.188 10.024  280.755 1.00 20.19  ? 174 LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 174 ? -106.528 11.247  281.467 1.00 21.52  ? 174 LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 174 ? -106.150 12.463  280.636 1.00 26.26  ? 174 LEU A C   1 
ATOM   1249 O  O   . LEU A 1 174 ? -105.072 12.507  280.036 1.00 32.34  ? 174 LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 174 ? -105.821 11.317  282.825 1.00 17.87  ? 174 LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 174 ? -106.212 10.267  283.863 1.00 16.57  ? 174 LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 174 ? -105.416 10.462  285.142 1.00 15.82  ? 174 LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 174 ? -107.702 10.330  284.143 1.00 16.10  ? 174 LEU A CD2 1 
ATOM   1254 N  N   . SER A 1 175 ? -107.045 13.449  280.608 1.00 25.79  ? 175 SER A N   1 
ATOM   1255 C  CA  . SER A 1 175 ? -106.761 14.740  279.997 1.00 24.99  ? 175 SER A CA  1 
ATOM   1256 C  C   . SER A 1 175 ? -106.290 15.777  281.004 1.00 26.84  ? 175 SER A C   1 
ATOM   1257 O  O   . SER A 1 175 ? -105.556 16.699  280.632 1.00 40.78  ? 175 SER A O   1 
ATOM   1258 C  CB  . SER A 1 175 ? -108.001 15.271  279.271 1.00 25.95  ? 175 SER A CB  1 
ATOM   1259 O  OG  . SER A 1 175 ? -109.052 15.528  280.185 1.00 41.71  ? 175 SER A OG  1 
ATOM   1260 N  N   . HIS A 1 176 ? -106.696 15.649  282.265 1.00 22.83  ? 176 HIS A N   1 
ATOM   1261 C  CA  . HIS A 1 176 ? -106.224 16.506  283.342 1.00 21.79  ? 176 HIS A CA  1 
ATOM   1262 C  C   . HIS A 1 176 ? -105.746 15.650  284.503 1.00 20.13  ? 176 HIS A C   1 
ATOM   1263 O  O   . HIS A 1 176 ? -106.360 14.630  284.829 1.00 19.16  ? 176 HIS A O   1 
ATOM   1264 C  CB  . HIS A 1 176 ? -107.314 17.463  283.839 1.00 26.86  ? 176 HIS A CB  1 
ATOM   1265 C  CG  . HIS A 1 176 ? -107.760 18.466  282.822 1.00 26.75  ? 176 HIS A CG  1 
ATOM   1266 N  ND1 . HIS A 1 176 ? -108.636 18.156  281.805 1.00 39.90  ? 176 HIS A ND1 1 
ATOM   1267 C  CD2 . HIS A 1 176 ? -107.459 19.777  282.674 1.00 23.61  ? 176 HIS A CD2 1 
ATOM   1268 C  CE1 . HIS A 1 176 ? -108.854 19.233  281.072 1.00 40.74  ? 176 HIS A CE1 1 
ATOM   1269 N  NE2 . HIS A 1 176 ? -108.151 20.230  281.577 1.00 30.01  ? 176 HIS A NE2 1 
ATOM   1270 N  N   . LEU A 1 177 ? -104.648 16.073  285.122 1.00 20.21  ? 177 LEU A N   1 
ATOM   1271 C  CA  . LEU A 1 177 ? -104.147 15.478  286.355 1.00 18.47  ? 177 LEU A CA  1 
ATOM   1272 C  C   . LEU A 1 177 ? -104.127 16.581  287.404 1.00 19.35  ? 177 LEU A C   1 
ATOM   1273 O  O   . LEU A 1 177 ? -103.343 17.530  287.299 1.00 25.53  ? 177 LEU A O   1 
ATOM   1274 C  CB  . LEU A 1 177 ? -102.761 14.867  286.154 1.00 19.50  ? 177 LEU A CB  1 
ATOM   1275 C  CG  . LEU A 1 177 ? -102.263 13.861  287.198 1.00 17.47  ? 177 LEU A CG  1 
ATOM   1276 C  CD1 . LEU A 1 177 ? -101.647 14.560  288.401 1.00 16.68  ? 177 LEU A CD1 1 
ATOM   1277 C  CD2 . LEU A 1 177 ? -103.392 12.938  287.633 1.00 20.53  ? 177 LEU A CD2 1 
ATOM   1278 N  N   . LEU A 1 178 ? -104.993 16.464  288.404 1.00 19.24  ? 178 LEU A N   1 
ATOM   1279 C  CA  . LEU A 1 178 ? -105.175 17.505  289.408 1.00 20.11  ? 178 LEU A CA  1 
ATOM   1280 C  C   . LEU A 1 178 ? -104.353 17.143  290.639 1.00 17.86  ? 178 LEU A C   1 
ATOM   1281 O  O   . LEU A 1 178 ? -104.628 16.143  291.308 1.00 20.46  ? 178 LEU A O   1 
ATOM   1282 C  CB  . LEU A 1 178 ? -106.656 17.665  289.743 1.00 22.43  ? 178 LEU A CB  1 
ATOM   1283 C  CG  . LEU A 1 178 ? -107.534 17.980  288.527 1.00 24.75  ? 178 LEU A CG  1 
ATOM   1284 C  CD1 . LEU A 1 178 ? -108.984 18.180  288.925 1.00 24.07  ? 178 LEU A CD1 1 
ATOM   1285 C  CD2 . LEU A 1 178 ? -107.012 19.204  287.790 1.00 23.47  ? 178 LEU A CD2 1 
ATOM   1286 N  N   . TYR A 1 179 ? -103.350 17.965  290.937 1.00 17.75  ? 179 TYR A N   1 
ATOM   1287 C  CA  . TYR A 1 179 ? -102.432 17.718  292.043 1.00 17.16  ? 179 TYR A CA  1 
ATOM   1288 C  C   . TYR A 1 179 ? -102.981 18.380  293.301 1.00 14.22  ? 179 TYR A C   1 
ATOM   1289 O  O   . TYR A 1 179 ? -102.983 19.610  293.414 1.00 15.40  ? 179 TYR A O   1 
ATOM   1290 C  CB  . TYR A 1 179 ? -101.038 18.243  291.709 1.00 15.78  ? 179 TYR A CB  1 
ATOM   1291 C  CG  . TYR A 1 179 ? -100.009 17.997  292.790 1.00 13.97  ? 179 TYR A CG  1 
ATOM   1292 C  CD1 . TYR A 1 179 ? -99.262  16.827  292.811 1.00 14.71  ? 179 TYR A CD1 1 
ATOM   1293 C  CD2 . TYR A 1 179 ? -99.777  18.939  293.783 1.00 14.16  ? 179 TYR A CD2 1 
ATOM   1294 C  CE1 . TYR A 1 179 ? -98.320  16.600  293.794 1.00 14.50  ? 179 TYR A CE1 1 
ATOM   1295 C  CE2 . TYR A 1 179 ? -98.839  18.720  294.770 1.00 17.83  ? 179 TYR A CE2 1 
ATOM   1296 C  CZ  . TYR A 1 179 ? -98.113  17.550  294.770 1.00 14.17  ? 179 TYR A CZ  1 
ATOM   1297 O  OH  . TYR A 1 179 ? -97.176  17.330  295.750 1.00 13.33  ? 179 TYR A OH  1 
ATOM   1298 N  N   . GLY A 1 180 ? -103.439 17.567  294.245 1.00 15.01  ? 180 GLY A N   1 
ATOM   1299 C  CA  . GLY A 1 180 ? -103.943 18.075  295.505 1.00 15.13  ? 180 GLY A CA  1 
ATOM   1300 C  C   . GLY A 1 180 ? -103.104 17.641  296.691 1.00 15.90  ? 180 GLY A C   1 
ATOM   1301 O  O   . GLY A 1 180 ? -102.762 16.465  296.813 1.00 17.55  ? 180 GLY A O   1 
ATOM   1302 N  N   . PHE A 1 181 ? -102.770 18.584  297.567 1.00 16.96  ? 181 PHE A N   1 
ATOM   1303 C  CA  . PHE A 1 181 ? -103.189 19.973  297.418 1.00 20.52  ? 181 PHE A CA  1 
ATOM   1304 C  C   . PHE A 1 181 ? -102.026 20.936  297.630 1.00 22.62  ? 181 PHE A C   1 
ATOM   1305 O  O   . PHE A 1 181 ? -101.057 20.614  298.317 1.00 21.24  ? 181 PHE A O   1 
ATOM   1306 C  CB  . PHE A 1 181 ? -104.312 20.304  298.402 1.00 19.81  ? 181 PHE A CB  1 
ATOM   1307 C  CG  . PHE A 1 181 ? -105.626 19.661  298.067 1.00 20.45  ? 181 PHE A CG  1 
ATOM   1308 C  CD1 . PHE A 1 181 ? -106.383 20.116  297.001 1.00 21.15  ? 181 PHE A CD1 1 
ATOM   1309 C  CD2 . PHE A 1 181 ? -106.109 18.607  298.823 1.00 20.97  ? 181 PHE A CD2 1 
ATOM   1310 C  CE1 . PHE A 1 181 ? -107.592 19.528  296.690 1.00 19.33  ? 181 PHE A CE1 1 
ATOM   1311 C  CE2 . PHE A 1 181 ? -107.318 18.015  298.518 1.00 24.59  ? 181 PHE A CE2 1 
ATOM   1312 C  CZ  . PHE A 1 181 ? -108.060 18.477  297.450 1.00 22.89  ? 181 PHE A CZ  1 
ATOM   1313 N  N   . ILE A 1 182 ? -102.132 22.119  297.036 1.00 22.47  ? 182 ILE A N   1 
ATOM   1314 C  CA  . ILE A 1 182 ? -101.157 23.187  297.231 1.00 21.24  ? 182 ILE A CA  1 
ATOM   1315 C  C   . ILE A 1 182 ? -101.651 24.062  298.380 1.00 22.06  ? 182 ILE A C   1 
ATOM   1316 O  O   . ILE A 1 182 ? -102.706 24.701  298.243 1.00 23.57  ? 182 ILE A O   1 
ATOM   1317 C  CB  . ILE A 1 182 ? -100.964 24.014  295.956 1.00 19.76  ? 182 ILE A CB  1 
ATOM   1318 C  CG1 . ILE A 1 182 ? -100.393 23.138  294.839 1.00 21.17  ? 182 ILE A CG1 1 
ATOM   1319 C  CG2 . ILE A 1 182 ? -100.055 25.202  296.228 1.00 22.23  ? 182 ILE A CG2 1 
ATOM   1320 C  CD1 . ILE A 1 182 ? -99.096  22.453  295.206 1.00 22.57  ? 182 ILE A CD1 1 
ATOM   1321 N  N   . PRO A 1 183 ? -100.941 24.122  299.499 1.00 21.85  ? 183 PRO A N   1 
ATOM   1322 C  CA  . PRO A 1 183 ? -101.459 24.826  300.674 1.00 22.83  ? 183 PRO A CA  1 
ATOM   1323 C  C   . PRO A 1 183 ? -101.261 26.333  300.574 1.00 23.23  ? 183 PRO A C   1 
ATOM   1324 O  O   . PRO A 1 183 ? -100.581 26.851  299.688 1.00 23.74  ? 183 PRO A O   1 
ATOM   1325 C  CB  . PRO A 1 183 ? -100.627 24.241  301.816 1.00 24.17  ? 183 PRO A CB  1 
ATOM   1326 C  CG  . PRO A 1 183 ? -99.321  23.929  301.174 1.00 23.80  ? 183 PRO A CG  1 
ATOM   1327 C  CD  . PRO A 1 183 ? -99.643  23.481  299.769 1.00 22.64  ? 183 PRO A CD  1 
ATOM   1328 N  N   . ILE A 1 184 ? -101.886 27.033  301.518 1.00 25.90  ? 184 ILE A N   1 
ATOM   1329 C  CA  . ILE A 1 184 ? -101.697 28.464  301.715 1.00 27.13  ? 184 ILE A CA  1 
ATOM   1330 C  C   . ILE A 1 184 ? -101.135 28.668  303.113 1.00 25.93  ? 184 ILE A C   1 
ATOM   1331 O  O   . ILE A 1 184 ? -101.704 28.173  304.093 1.00 25.09  ? 184 ILE A O   1 
ATOM   1332 C  CB  . ILE A 1 184 ? -103.008 29.249  301.533 1.00 24.45  ? 184 ILE A CB  1 
ATOM   1333 C  CG1 . ILE A 1 184 ? -103.609 28.958  300.161 1.00 25.13  ? 184 ILE A CG1 1 
ATOM   1334 C  CG2 . ILE A 1 184 ? -102.755 30.738  301.681 1.00 22.99  ? 184 ILE A CG2 1 
ATOM   1335 C  CD1 . ILE A 1 184 ? -102.689 29.324  299.033 1.00 24.80  ? 184 ILE A CD1 1 
ATOM   1336 N  N   . CYS A 1 185 ? -100.022 29.390  303.202 1.00 26.51  ? 185 CYS A N   1 
ATOM   1337 C  CA  . CYS A 1 185 ? -99.341  29.556  304.477 1.00 29.82  ? 185 CYS A CA  1 
ATOM   1338 C  C   . CYS A 1 185 ? -100.219 30.316  305.466 1.00 30.47  ? 185 CYS A C   1 
ATOM   1339 O  O   . CYS A 1 185 ? -101.029 31.167  305.091 1.00 32.08  ? 185 CYS A O   1 
ATOM   1340 C  CB  . CYS A 1 185 ? -98.014  30.286  304.278 1.00 33.25  ? 185 CYS A CB  1 
ATOM   1341 S  SG  . CYS A 1 185 ? -96.723  29.275  303.514 1.00 37.89  ? 185 CYS A SG  1 
ATOM   1342 N  N   . GLY A 1 186 ? -100.051 29.991  306.744 1.00 29.73  ? 186 GLY A N   1 
ATOM   1343 C  CA  . GLY A 1 186 ? -100.827 30.610  307.798 1.00 24.69  ? 186 GLY A CA  1 
ATOM   1344 C  C   . GLY A 1 186 ? -100.738 29.844  309.101 1.00 25.62  ? 186 GLY A C   1 
ATOM   1345 O  O   . GLY A 1 186 ? -100.639 28.613  309.097 1.00 25.16  ? 186 GLY A O   1 
ATOM   1346 N  N   . GLY A 1 187 ? -100.768 30.556  310.217 1.00 27.41  ? 187 GLY A N   1 
ATOM   1347 C  CA  . GLY A 1 187 ? -100.666 29.960  311.538 1.00 44.96  ? 187 GLY A CA  1 
ATOM   1348 C  C   . GLY A 1 187 ? -102.019 29.767  312.186 1.00 27.45  ? 187 GLY A C   1 
ATOM   1349 O  O   . GLY A 1 187 ? -102.985 29.344  311.540 1.00 26.30  ? 187 GLY A O   1 
ATOM   1350 N  N   . ASP A 1 188 ? -102.090 30.078  313.479 1.00 26.42  ? 188 ASP A N   1 
ATOM   1351 C  CA  . ASP A 1 188 ? -103.339 29.940  314.214 1.00 25.69  ? 188 ASP A CA  1 
ATOM   1352 C  C   . ASP A 1 188 ? -104.395 30.883  313.652 1.00 24.67  ? 188 ASP A C   1 
ATOM   1353 O  O   . ASP A 1 188 ? -104.122 32.052  313.366 1.00 23.24  ? 188 ASP A O   1 
ATOM   1354 C  CB  . ASP A 1 188 ? -103.115 30.224  315.699 1.00 25.68  ? 188 ASP A CB  1 
ATOM   1355 C  CG  . ASP A 1 188 ? -102.280 29.156  316.377 1.00 32.30  ? 188 ASP A CG  1 
ATOM   1356 O  OD1 . ASP A 1 188 ? -102.403 27.973  315.995 1.00 44.37  ? 188 ASP A OD1 1 
ATOM   1357 O  OD2 . ASP A 1 188 ? -101.502 29.499  317.291 1.00 33.27  ? 188 ASP A OD2 1 
ATOM   1358 N  N   . GLY A 1 189 ? -105.613 30.365  313.493 1.00 26.14  ? 189 GLY A N   1 
ATOM   1359 C  CA  . GLY A 1 189 ? -106.702 31.121  312.921 1.00 25.35  ? 189 GLY A CA  1 
ATOM   1360 C  C   . GLY A 1 189 ? -106.750 31.137  311.410 1.00 27.15  ? 189 GLY A C   1 
ATOM   1361 O  O   . GLY A 1 189 ? -107.822 31.374  310.842 1.00 27.51  ? 189 GLY A O   1 
ATOM   1362 N  N   . ILE A 1 190 ? -105.628 30.889  310.737 1.00 26.25  ? 190 ILE A N   1 
ATOM   1363 C  CA  . ILE A 1 190 ? -105.592 30.899  309.280 1.00 26.31  ? 190 ILE A CA  1 
ATOM   1364 C  C   . ILE A 1 190 ? -105.658 29.495  308.685 1.00 38.96  ? 190 ILE A C   1 
ATOM   1365 O  O   . ILE A 1 190 ? -106.086 29.345  307.530 1.00 26.69  ? 190 ILE A O   1 
ATOM   1366 C  CB  . ILE A 1 190 ? -104.335 31.639  308.777 1.00 23.36  ? 190 ILE A CB  1 
ATOM   1367 C  CG1 . ILE A 1 190 ? -104.115 32.906  309.602 1.00 25.09  ? 190 ILE A CG1 1 
ATOM   1368 C  CG2 . ILE A 1 190 ? -104.468 31.996  307.305 1.00 26.84  ? 190 ILE A CG2 1 
ATOM   1369 C  CD1 . ILE A 1 190 ? -102.894 33.690  309.198 1.00 43.32  ? 190 ILE A CD1 1 
ATOM   1370 N  N   . ASN A 1 191 ? -105.256 28.471  309.431 1.00 49.00  ? 191 ASN A N   1 
ATOM   1371 C  CA  . ASN A 1 191 ? -105.355 27.090  308.970 1.00 30.78  ? 191 ASN A CA  1 
ATOM   1372 C  C   . ASN A 1 191 ? -105.677 26.176  310.151 1.00 30.07  ? 191 ASN A C   1 
ATOM   1373 O  O   . ASN A 1 191 ? -105.038 25.144  310.362 1.00 29.77  ? 191 ASN A O   1 
ATOM   1374 C  CB  . ASN A 1 191 ? -104.073 26.656  308.260 1.00 27.67  ? 191 ASN A CB  1 
ATOM   1375 C  CG  . ASN A 1 191 ? -103.974 27.200  306.851 1.00 25.87  ? 191 ASN A CG  1 
ATOM   1376 O  OD1 . ASN A 1 191 ? -104.661 26.731  305.945 1.00 24.66  ? 191 ASN A OD1 1 
ATOM   1377 N  ND2 . ASN A 1 191 ? -103.115 28.193  306.657 1.00 34.38  ? 191 ASN A ND2 1 
ATOM   1378 N  N   . ASP A 1 192 ? -106.685 26.554  310.942 1.00 30.08  ? 192 ASP A N   1 
ATOM   1379 C  CA  . ASP A 1 192 ? -107.106 25.720  312.062 1.00 30.68  ? 192 ASP A CA  1 
ATOM   1380 C  C   . ASP A 1 192 ? -107.689 24.390  311.608 1.00 31.76  ? 192 ASP A C   1 
ATOM   1381 O  O   . ASP A 1 192 ? -107.692 23.432  312.389 1.00 30.26  ? 192 ASP A O   1 
ATOM   1382 C  CB  . ASP A 1 192 ? -108.133 26.459  312.921 1.00 30.08  ? 192 ASP A CB  1 
ATOM   1383 C  CG  . ASP A 1 192 ? -107.582 27.735  313.520 1.00 31.08  ? 192 ASP A CG  1 
ATOM   1384 O  OD1 . ASP A 1 192 ? -106.343 27.881  313.575 1.00 31.57  ? 192 ASP A OD1 1 
ATOM   1385 O  OD2 . ASP A 1 192 ? -108.390 28.589  313.943 1.00 48.41  ? 192 ASP A OD2 1 
ATOM   1386 N  N   . ALA A 1 193 ? -108.180 24.309  310.369 1.00 32.24  ? 193 ALA A N   1 
ATOM   1387 C  CA  . ALA A 1 193 ? -108.764 23.064  309.883 1.00 30.10  ? 193 ALA A CA  1 
ATOM   1388 C  C   . ALA A 1 193 ? -107.732 21.949  309.805 1.00 38.68  ? 193 ALA A C   1 
ATOM   1389 O  O   . ALA A 1 193 ? -108.084 20.769  309.921 1.00 38.54  ? 193 ALA A O   1 
ATOM   1390 C  CB  . ALA A 1 193 ? -109.408 23.287  308.515 1.00 29.19  ? 193 ALA A CB  1 
ATOM   1391 N  N   . LEU A 1 194 ? -106.457 22.295  309.610 1.00 36.02  ? 194 LEU A N   1 
ATOM   1392 C  CA  . LEU A 1 194 ? -105.412 21.280  309.582 1.00 33.01  ? 194 LEU A CA  1 
ATOM   1393 C  C   . LEU A 1 194 ? -105.197 20.641  310.945 1.00 34.61  ? 194 LEU A C   1 
ATOM   1394 O  O   . LEU A 1 194 ? -104.700 19.512  311.015 1.00 37.76  ? 194 LEU A O   1 
ATOM   1395 C  CB  . LEU A 1 194 ? -104.094 21.874  309.085 1.00 34.88  ? 194 LEU A CB  1 
ATOM   1396 C  CG  . LEU A 1 194 ? -103.923 22.089  307.581 1.00 45.44  ? 194 LEU A CG  1 
ATOM   1397 C  CD1 . LEU A 1 194 ? -104.723 23.289  307.109 1.00 50.76  ? 194 LEU A CD1 1 
ATOM   1398 C  CD2 . LEU A 1 194 ? -102.451 22.245  307.230 1.00 33.20  ? 194 LEU A CD2 1 
ATOM   1399 N  N   . LYS A 1 195 ? -105.557 21.334  312.027 1.00 28.04  ? 195 LYS A N   1 
ATOM   1400 C  CA  . LYS A 1 195 ? -105.425 20.766  313.362 1.00 29.30  ? 195 LYS A CA  1 
ATOM   1401 C  C   . LYS A 1 195 ? -106.344 19.574  313.586 1.00 30.25  ? 195 LYS A C   1 
ATOM   1402 O  O   . LYS A 1 195 ? -106.170 18.859  314.579 1.00 38.13  ? 195 LYS A O   1 
ATOM   1403 C  CB  . LYS A 1 195 ? -105.692 21.841  314.417 1.00 29.52  ? 195 LYS A CB  1 
ATOM   1404 C  CG  . LYS A 1 195 ? -104.753 23.032  314.320 1.00 29.60  ? 195 LYS A CG  1 
ATOM   1405 C  CD  . LYS A 1 195 ? -105.106 24.109  315.330 1.00 28.95  ? 195 LYS A CD  1 
ATOM   1406 C  CE  . LYS A 1 195 ? -104.066 25.216  315.330 1.00 28.09  ? 195 LYS A CE  1 
ATOM   1407 N  NZ  . LYS A 1 195 ? -104.444 26.335  316.234 1.00 32.63  ? 195 LYS A NZ  1 
ATOM   1408 N  N   . THR A 1 196 ? -107.313 19.344  312.696 1.00 29.05  ? 196 THR A N   1 
ATOM   1409 C  CA  . THR A 1 196 ? -108.123 18.134  312.781 1.00 32.87  ? 196 THR A CA  1 
ATOM   1410 C  C   . THR A 1 196 ? -107.294 16.889  312.495 1.00 34.14  ? 196 THR A C   1 
ATOM   1411 O  O   . THR A 1 196 ? -107.635 15.797  312.963 1.00 37.37  ? 196 THR A O   1 
ATOM   1412 C  CB  . THR A 1 196 ? -109.302 18.220  311.811 1.00 33.42  ? 196 THR A CB  1 
ATOM   1413 O  OG1 . THR A 1 196 ? -108.812 18.317  310.468 1.00 34.77  ? 196 THR A OG1 1 
ATOM   1414 C  CG2 . THR A 1 196 ? -110.157 19.439  312.121 1.00 34.75  ? 196 THR A CG2 1 
ATOM   1415 N  N   . ILE A 1 197 ? -106.212 17.030  311.734 1.00 31.66  ? 197 ILE A N   1 
ATOM   1416 C  CA  . ILE A 1 197 ? -105.291 15.940  311.439 1.00 29.54  ? 197 ILE A CA  1 
ATOM   1417 C  C   . ILE A 1 197 ? -104.013 16.174  312.232 1.00 35.92  ? 197 ILE A C   1 
ATOM   1418 O  O   . ILE A 1 197 ? -103.409 17.250  312.143 1.00 40.51  ? 197 ILE A O   1 
ATOM   1419 C  CB  . ILE A 1 197 ? -104.994 15.842  309.933 1.00 28.02  ? 197 ILE A CB  1 
ATOM   1420 C  CG1 . ILE A 1 197 ? -106.296 15.720  309.140 1.00 29.81  ? 197 ILE A CG1 1 
ATOM   1421 C  CG2 . ILE A 1 197 ? -104.078 14.663  309.645 1.00 32.10  ? 197 ILE A CG2 1 
ATOM   1422 C  CD1 . ILE A 1 197 ? -106.093 15.655  307.642 1.00 29.43  ? 197 ILE A CD1 1 
ATOM   1423 N  N   . SER A 1 198 ? -103.604 15.171  313.005 1.00 29.68  ? 198 SER A N   1 
ATOM   1424 C  CA  . SER A 1 198 ? -102.415 15.304  313.836 1.00 32.11  ? 198 SER A CA  1 
ATOM   1425 C  C   . SER A 1 198 ? -101.164 15.374  312.969 1.00 31.80  ? 198 SER A C   1 
ATOM   1426 O  O   . SER A 1 198 ? -100.970 14.552  312.069 1.00 30.21  ? 198 SER A O   1 
ATOM   1427 C  CB  . SER A 1 198 ? -102.318 14.134  314.813 1.00 39.91  ? 198 SER A CB  1 
ATOM   1428 O  OG  . SER A 1 198 ? -101.515 13.094  314.284 1.00 54.88  ? 198 SER A OG  1 
ATOM   1429 N  N   . GLY A 1 199 ? -100.313 16.363  313.245 1.00 33.10  ? 199 GLY A N   1 
ATOM   1430 C  CA  . GLY A 1 199 ? -99.090  16.560  312.500 1.00 35.57  ? 199 GLY A CA  1 
ATOM   1431 C  C   . GLY A 1 199 ? -99.243  17.286  311.183 1.00 34.82  ? 199 GLY A C   1 
ATOM   1432 O  O   . GLY A 1 199 ? -98.239  17.746  310.626 1.00 35.02  ? 199 GLY A O   1 
ATOM   1433 N  N   . SER A 1 200 ? -100.466 17.408  310.663 1.00 32.28  ? 200 SER A N   1 
ATOM   1434 C  CA  . SER A 1 200 ? -100.657 18.076  309.380 1.00 31.29  ? 200 SER A CA  1 
ATOM   1435 C  C   . SER A 1 200 ? -100.520 19.588  309.518 1.00 33.85  ? 200 SER A C   1 
ATOM   1436 O  O   . SER A 1 200 ? -99.949  20.249  308.643 1.00 36.36  ? 200 SER A O   1 
ATOM   1437 C  CB  . SER A 1 200 ? -102.020 17.706  308.798 1.00 31.00  ? 200 SER A CB  1 
ATOM   1438 O  OG  . SER A 1 200 ? -102.245 18.374  307.571 1.00 34.37  ? 200 SER A OG  1 
ATOM   1439 N  N   . PHE A 1 201 ? -101.039 20.153  310.611 1.00 36.97  ? 201 PHE A N   1 
ATOM   1440 C  CA  . PHE A 1 201 ? -100.908 21.590  310.832 1.00 33.79  ? 201 PHE A CA  1 
ATOM   1441 C  C   . PHE A 1 201 ? -99.459  21.977  311.094 1.00 42.79  ? 201 PHE A C   1 
ATOM   1442 O  O   . PHE A 1 201 ? -98.975  22.988  310.571 1.00 52.31  ? 201 PHE A O   1 
ATOM   1443 C  CB  . PHE A 1 201 ? -101.803 22.024  311.993 1.00 44.15  ? 201 PHE A CB  1 
ATOM   1444 C  CG  . PHE A 1 201 ? -101.594 23.449  312.421 1.00 34.58  ? 201 PHE A CG  1 
ATOM   1445 C  CD1 . PHE A 1 201 ? -102.211 24.485  311.742 1.00 32.22  ? 201 PHE A CD1 1 
ATOM   1446 C  CD2 . PHE A 1 201 ? -100.793 23.751  313.510 1.00 34.95  ? 201 PHE A CD2 1 
ATOM   1447 C  CE1 . PHE A 1 201 ? -102.025 25.797  312.133 1.00 32.30  ? 201 PHE A CE1 1 
ATOM   1448 C  CE2 . PHE A 1 201 ? -100.603 25.060  313.906 1.00 33.12  ? 201 PHE A CE2 1 
ATOM   1449 C  CZ  . PHE A 1 201 ? -101.220 26.084  313.217 1.00 32.65  ? 201 PHE A CZ  1 
ATOM   1450 N  N   . GLU A 1 202 ? -98.751  21.186  311.902 1.00 41.27  ? 202 GLU A N   1 
ATOM   1451 C  CA  . GLU A 1 202 ? -97.356  21.489  312.200 1.00 41.28  ? 202 GLU A CA  1 
ATOM   1452 C  C   . GLU A 1 202 ? -96.474  21.326  310.971 1.00 37.60  ? 202 GLU A C   1 
ATOM   1453 O  O   . GLU A 1 202 ? -95.465  22.028  310.836 1.00 37.83  ? 202 GLU A O   1 
ATOM   1454 C  CB  . GLU A 1 202 ? -96.854  20.600  313.339 1.00 55.68  ? 202 GLU A CB  1 
ATOM   1455 C  CG  . GLU A 1 202 ? -97.550  20.824  314.679 1.00 52.61  ? 202 GLU A CG  1 
ATOM   1456 C  CD  . GLU A 1 202 ? -98.958  20.255  314.724 1.00 44.00  ? 202 GLU A CD  1 
ATOM   1457 O  OE1 . GLU A 1 202 ? -99.331  19.504  313.799 1.00 48.86  ? 202 GLU A OE1 1 
ATOM   1458 O  OE2 . GLU A 1 202 ? -99.695  20.565  315.683 1.00 42.35  ? 202 GLU A OE2 1 
ATOM   1459 N  N   . SER A 1 203 ? -96.834  20.413  310.066 1.00 38.21  ? 203 SER A N   1 
ATOM   1460 C  CA  . SER A 1 203 ? -96.053  20.234  308.848 1.00 39.52  ? 203 SER A CA  1 
ATOM   1461 C  C   . SER A 1 203 ? -96.129  21.468  307.958 1.00 30.99  ? 203 SER A C   1 
ATOM   1462 O  O   . SER A 1 203 ? -95.150  21.819  307.289 1.00 32.83  ? 203 SER A O   1 
ATOM   1463 C  CB  . SER A 1 203 ? -96.535  18.996  308.092 1.00 35.36  ? 203 SER A CB  1 
ATOM   1464 O  OG  . SER A 1 203 ? -95.635  18.651  307.053 1.00 42.98  ? 203 SER A OG  1 
ATOM   1465 N  N   . LEU A 1 204 ? -97.281  22.142  307.939 1.00 29.99  ? 204 LEU A N   1 
ATOM   1466 C  CA  . LEU A 1 204 ? -97.407  23.359  307.146 1.00 29.25  ? 204 LEU A CA  1 
ATOM   1467 C  C   . LEU A 1 204 ? -96.643  24.518  307.772 1.00 29.51  ? 204 LEU A C   1 
ATOM   1468 O  O   . LEU A 1 204 ? -96.108  25.367  307.050 1.00 39.46  ? 204 LEU A O   1 
ATOM   1469 C  CB  . LEU A 1 204 ? -98.880  23.727  306.975 1.00 29.86  ? 204 LEU A CB  1 
ATOM   1470 C  CG  . LEU A 1 204 ? -99.153  24.972  306.130 1.00 29.91  ? 204 LEU A CG  1 
ATOM   1471 C  CD1 . LEU A 1 204 ? -98.595  24.789  304.729 1.00 26.26  ? 204 LEU A CD1 1 
ATOM   1472 C  CD2 . LEU A 1 204 ? -100.640 25.279  306.082 1.00 58.89  ? 204 LEU A CD2 1 
ATOM   1473 N  N   . GLN A 1 205 ? -96.580  24.571  309.104 1.00 30.26  ? 205 GLN A N   1 
ATOM   1474 C  CA  . GLN A 1 205 ? -95.846  25.644  309.767 1.00 31.57  ? 205 GLN A CA  1 
ATOM   1475 C  C   . GLN A 1 205 ? -94.353  25.545  309.478 1.00 33.99  ? 205 GLN A C   1 
ATOM   1476 O  O   . GLN A 1 205 ? -93.713  26.540  309.118 1.00 28.94  ? 205 GLN A O   1 
ATOM   1477 C  CB  . GLN A 1 205 ? -96.112  25.608  311.271 1.00 32.98  ? 205 GLN A CB  1 
ATOM   1478 C  CG  . GLN A 1 205 ? -97.575  25.779  311.641 1.00 34.52  ? 205 GLN A CG  1 
ATOM   1479 C  CD  . GLN A 1 205 ? -98.206  26.982  310.969 1.00 42.50  ? 205 GLN A CD  1 
ATOM   1480 O  OE1 . GLN A 1 205 ? -97.686  28.095  311.046 1.00 52.46  ? 205 GLN A OE1 1 
ATOM   1481 N  NE2 . GLN A 1 205 ? -99.335  26.764  310.305 1.00 39.47  ? 205 GLN A NE2 1 
ATOM   1482 N  N   . ARG A 1 206 ? -93.779  24.348  309.627 1.00 31.07  ? 206 ARG A N   1 
ATOM   1483 C  CA  . ARG A 1 206 ? -92.365  24.167  309.327 1.00 32.16  ? 206 ARG A CA  1 
ATOM   1484 C  C   . ARG A 1 206 ? -92.081  24.231  307.833 1.00 30.96  ? 206 ARG A C   1 
ATOM   1485 O  O   . ARG A 1 206 ? -90.923  24.415  307.443 1.00 47.93  ? 206 ARG A O   1 
ATOM   1486 C  CB  . ARG A 1 206 ? -91.865  22.841  309.905 1.00 32.58  ? 206 ARG A CB  1 
ATOM   1487 C  CG  . ARG A 1 206 ? -92.579  21.609  309.378 1.00 34.42  ? 206 ARG A CG  1 
ATOM   1488 C  CD  . ARG A 1 206 ? -92.135  20.363  310.130 1.00 36.88  ? 206 ARG A CD  1 
ATOM   1489 N  NE  . ARG A 1 206 ? -92.836  19.166  309.676 1.00 41.49  ? 206 ARG A NE  1 
ATOM   1490 C  CZ  . ARG A 1 206 ? -92.333  18.286  308.816 1.00 38.10  ? 206 ARG A CZ  1 
ATOM   1491 N  NH1 . ARG A 1 206 ? -91.120  18.467  308.312 1.00 33.84  ? 206 ARG A NH1 1 
ATOM   1492 N  NH2 . ARG A 1 206 ? -93.043  17.225  308.460 1.00 34.33  ? 206 ARG A NH2 1 
ATOM   1493 N  N   . SER A 1 207 ? -93.105  24.082  306.991 1.00 27.65  ? 207 SER A N   1 
ATOM   1494 C  CA  . SER A 1 207 ? -92.929  24.305  305.561 1.00 25.51  ? 207 SER A CA  1 
ATOM   1495 C  C   . SER A 1 207 ? -92.998  25.785  305.213 1.00 25.02  ? 207 SER A C   1 
ATOM   1496 O  O   . SER A 1 207 ? -92.417  26.211  304.209 1.00 31.85  ? 207 SER A O   1 
ATOM   1497 C  CB  . SER A 1 207 ? -93.980  23.528  304.768 1.00 24.06  ? 207 SER A CB  1 
ATOM   1498 O  OG  . SER A 1 207 ? -93.806  22.131  304.921 1.00 36.06  ? 207 SER A OG  1 
ATOM   1499 N  N   . CYS A 1 208 ? -93.701  26.576  306.024 1.00 22.28  ? 208 CYS A N   1 
ATOM   1500 C  CA  . CYS A 1 208 ? -93.769  28.021  305.859 1.00 25.66  ? 208 CYS A CA  1 
ATOM   1501 C  C   . CYS A 1 208 ? -92.851  28.758  306.832 1.00 26.10  ? 208 CYS A C   1 
ATOM   1502 O  O   . CYS A 1 208 ? -93.165  29.873  307.254 1.00 27.19  ? 208 CYS A O   1 
ATOM   1503 C  CB  . CYS A 1 208 ? -95.211  28.508  306.016 1.00 35.79  ? 208 CYS A CB  1 
ATOM   1504 S  SG  . CYS A 1 208 ? -96.403  27.787  304.860 1.00 28.73  ? 208 CYS A SG  1 
ATOM   1505 N  N   . LYS A 1 209 ? -91.726  28.153  307.206 1.00 27.16  ? 209 LYS A N   1 
ATOM   1506 C  CA  . LYS A 1 209 ? -90.794  28.805  308.116 1.00 26.67  ? 209 LYS A CA  1 
ATOM   1507 C  C   . LYS A 1 209 ? -90.063  29.924  307.384 1.00 26.53  ? 209 LYS A C   1 
ATOM   1508 O  O   . LYS A 1 209 ? -89.512  29.713  306.298 1.00 43.21  ? 209 LYS A O   1 
ATOM   1509 C  CB  . LYS A 1 209 ? -89.807  27.781  308.684 1.00 25.69  ? 209 LYS A CB  1 
ATOM   1510 C  CG  . LYS A 1 209 ? -89.234  28.167  310.039 1.00 25.51  ? 209 LYS A CG  1 
ATOM   1511 C  CD  . LYS A 1 209 ? -90.338  28.340  311.068 1.00 25.84  ? 209 LYS A CD  1 
ATOM   1512 C  CE  . LYS A 1 209 ? -89.773  28.683  312.434 1.00 24.45  ? 209 LYS A CE  1 
ATOM   1513 N  NZ  . LYS A 1 209 ? -90.840  28.703  313.470 1.00 37.18  ? 209 LYS A NZ  1 
ATOM   1514 N  N   . GLY A 1 210 ? -90.073  31.123  307.969 1.00 26.73  ? 210 GLY A N   1 
ATOM   1515 C  CA  . GLY A 1 210 ? -89.531  32.291  307.322 1.00 35.50  ? 210 GLY A CA  1 
ATOM   1516 C  C   . GLY A 1 210 ? -90.422  32.880  306.245 1.00 29.69  ? 210 GLY A C   1 
ATOM   1517 O  O   . GLY A 1 210 ? -90.249  34.046  305.885 1.00 37.51  ? 210 GLY A O   1 
ATOM   1518 N  N   . ARG A 1 211 ? -91.381  32.118  305.733 1.00 30.27  ? 211 ARG A N   1 
ATOM   1519 C  CA  . ARG A 1 211 ? -92.372  32.610  304.787 1.00 31.00  ? 211 ARG A CA  1 
ATOM   1520 C  C   . ARG A 1 211 ? -93.624  33.009  305.554 1.00 30.70  ? 211 ARG A C   1 
ATOM   1521 O  O   . ARG A 1 211 ? -94.147  32.220  306.347 1.00 45.66  ? 211 ARG A O   1 
ATOM   1522 C  CB  . ARG A 1 211 ? -92.703  31.534  303.752 1.00 28.94  ? 211 ARG A CB  1 
ATOM   1523 C  CG  . ARG A 1 211 ? -93.434  32.025  302.498 1.00 28.76  ? 211 ARG A CG  1 
ATOM   1524 C  CD  . ARG A 1 211 ? -93.927  30.816  301.712 1.00 30.78  ? 211 ARG A CD  1 
ATOM   1525 N  NE  . ARG A 1 211 ? -94.254  31.154  300.337 1.00 28.51  ? 211 ARG A NE  1 
ATOM   1526 C  CZ  . ARG A 1 211 ? -93.355  31.295  299.373 1.00 30.85  ? 211 ARG A CZ  1 
ATOM   1527 N  NH1 . ARG A 1 211 ? -92.066  31.130  299.631 1.00 40.51  ? 211 ARG A NH1 1 
ATOM   1528 N  NH2 . ARG A 1 211 ? -93.750  31.613  298.152 1.00 35.22  ? 211 ARG A NH2 1 
ATOM   1529 N  N   . GLU A 1 212 ? -94.118  34.215  305.307 1.00 30.35  ? 212 GLU A N   1 
ATOM   1530 C  CA  . GLU A 1 212 ? -95.261  34.692  306.068 1.00 41.36  ? 212 GLU A CA  1 
ATOM   1531 C  C   . GLU A 1 212 ? -96.567  34.480  305.303 1.00 33.13  ? 212 GLU A C   1 
ATOM   1532 O  O   . GLU A 1 212 ? -96.584  34.106  304.130 1.00 30.32  ? 212 GLU A O   1 
ATOM   1533 C  CB  . GLU A 1 212 ? -95.077  36.156  306.472 1.00 62.33  ? 212 GLU A CB  1 
ATOM   1534 C  CG  . GLU A 1 212 ? -93.950  36.332  307.486 1.00 48.49  ? 212 GLU A CG  1 
ATOM   1535 C  CD  . GLU A 1 212 ? -94.405  36.955  308.789 1.00 64.49  ? 212 GLU A CD  1 
ATOM   1536 O  OE1 . GLU A 1 212 ? -95.617  37.208  308.933 1.00 63.33  ? 212 GLU A OE1 1 
ATOM   1537 O  OE2 . GLU A 1 212 ? -93.550  37.164  309.678 1.00 54.13  ? 212 GLU A OE2 1 
ATOM   1538 N  N   . ASP A 1 213 ? -97.671  34.747  305.997 1.00 31.69  ? 213 ASP A N   1 
ATOM   1539 C  CA  . ASP A 1 213 ? -98.957  34.133  305.697 1.00 27.95  ? 213 ASP A CA  1 
ATOM   1540 C  C   . ASP A 1 213 ? -99.491  34.531  304.321 1.00 29.18  ? 213 ASP A C   1 
ATOM   1541 O  O   . ASP A 1 213 ? -99.051  35.503  303.701 1.00 29.74  ? 213 ASP A O   1 
ATOM   1542 C  CB  . ASP A 1 213 ? -99.975  34.502  306.774 1.00 24.17  ? 213 ASP A CB  1 
ATOM   1543 C  CG  . ASP A 1 213 ? -99.514  34.102  308.160 1.00 25.62  ? 213 ASP A CG  1 
ATOM   1544 O  OD1 . ASP A 1 213 ? -98.782  33.098  308.273 1.00 37.08  ? 213 ASP A OD1 1 
ATOM   1545 O  OD2 . ASP A 1 213 ? -99.864  34.802  309.133 1.00 25.53  ? 213 ASP A OD2 1 
ATOM   1546 N  N   . PHE A 1 214 ? -100.454 33.734  303.846 1.00 35.62  ? 214 PHE A N   1 
ATOM   1547 C  CA  . PHE A 1 214 ? -101.226 33.975  302.628 1.00 27.91  ? 214 PHE A CA  1 
ATOM   1548 C  C   . PHE A 1 214 ? -100.391 33.862  301.358 1.00 28.11  ? 214 PHE A C   1 
ATOM   1549 O  O   . PHE A 1 214 ? -100.749 34.437  300.328 1.00 26.42  ? 214 PHE A O   1 
ATOM   1550 C  CB  . PHE A 1 214 ? -101.938 35.330  302.690 1.00 27.72  ? 214 PHE A CB  1 
ATOM   1551 C  CG  . PHE A 1 214 ? -103.006 35.391  303.741 1.00 32.01  ? 214 PHE A CG  1 
ATOM   1552 C  CD1 . PHE A 1 214 ? -104.281 34.918  303.482 1.00 36.89  ? 214 PHE A CD1 1 
ATOM   1553 C  CD2 . PHE A 1 214 ? -102.723 35.881  305.005 1.00 37.21  ? 214 PHE A CD2 1 
ATOM   1554 C  CE1 . PHE A 1 214 ? -105.260 34.959  304.455 1.00 44.33  ? 214 PHE A CE1 1 
ATOM   1555 C  CE2 . PHE A 1 214 ? -103.697 35.921  305.983 1.00 29.08  ? 214 PHE A CE2 1 
ATOM   1556 C  CZ  . PHE A 1 214 ? -104.967 35.462  305.707 1.00 36.33  ? 214 PHE A CZ  1 
ATOM   1557 N  N   . LYS A 1 215 ? -99.291  33.115  301.407 1.00 27.32  ? 215 LYS A N   1 
ATOM   1558 C  CA  . LYS A 1 215 ? -98.491  32.795  300.234 1.00 25.93  ? 215 LYS A CA  1 
ATOM   1559 C  C   . LYS A 1 215 ? -98.551  31.297  299.982 1.00 26.74  ? 215 LYS A C   1 
ATOM   1560 O  O   . LYS A 1 215 ? -98.602  30.502  300.927 1.00 25.10  ? 215 LYS A O   1 
ATOM   1561 C  CB  . LYS A 1 215 ? -97.034  33.235  300.411 1.00 30.65  ? 215 LYS A CB  1 
ATOM   1562 C  CG  . LYS A 1 215 ? -96.730  34.622  299.880 1.00 34.79  ? 215 LYS A CG  1 
ATOM   1563 C  CD  . LYS A 1 215 ? -95.299  35.029  300.177 1.00 41.34  ? 215 LYS A CD  1 
ATOM   1564 C  CE  . LYS A 1 215 ? -94.997  36.412  299.627 1.00 55.07  ? 215 LYS A CE  1 
ATOM   1565 N  NZ  . LYS A 1 215 ? -93.606  36.840  299.941 1.00 67.88  ? 215 LYS A NZ  1 
ATOM   1566 N  N   . VAL A 1 216 ? -98.545  30.912  298.705 1.00 26.93  ? 216 VAL A N   1 
ATOM   1567 C  CA  . VAL A 1 216 ? -98.579  29.497  298.365 1.00 23.54  ? 216 VAL A CA  1 
ATOM   1568 C  C   . VAL A 1 216 ? -97.250  28.848  298.733 1.00 27.54  ? 216 VAL A C   1 
ATOM   1569 O  O   . VAL A 1 216 ? -96.201  29.504  298.792 1.00 31.25  ? 216 VAL A O   1 
ATOM   1570 C  CB  . VAL A 1 216 ? -98.901  29.293  296.873 1.00 20.40  ? 216 VAL A CB  1 
ATOM   1571 C  CG1 . VAL A 1 216 ? -100.192 29.997  296.510 1.00 19.53  ? 216 VAL A CG1 1 
ATOM   1572 C  CG2 . VAL A 1 216 ? -97.755  29.784  296.004 1.00 23.85  ? 216 VAL A CG2 1 
ATOM   1573 N  N   . ALA A 1 217 ? -97.296  27.547  298.990 1.00 21.94  ? 217 ALA A N   1 
ATOM   1574 C  CA  . ALA A 1 217 ? -96.106  26.790  299.350 1.00 19.41  ? 217 ALA A CA  1 
ATOM   1575 C  C   . ALA A 1 217 ? -96.366  25.323  299.017 1.00 20.38  ? 217 ALA A C   1 
ATOM   1576 O  O   . ALA A 1 217 ? -97.216  25.010  298.177 1.00 22.62  ? 217 ALA A O   1 
ATOM   1577 C  CB  . ALA A 1 217 ? -95.753  27.013  300.830 1.00 19.51  ? 217 ALA A CB  1 
ATOM   1578 N  N   . ILE A 1 218 ? -95.632  24.428  299.671 1.00 19.39  ? 218 ILE A N   1 
ATOM   1579 C  CA  . ILE A 1 218 ? -95.814  22.991  299.522 1.00 19.81  ? 218 ILE A CA  1 
ATOM   1580 C  C   . ILE A 1 218 ? -96.000  22.396  300.909 1.00 22.58  ? 218 ILE A C   1 
ATOM   1581 O  O   . ILE A 1 218 ? -95.216  22.682  301.820 1.00 21.78  ? 218 ILE A O   1 
ATOM   1582 C  CB  . ILE A 1 218 ? -94.624  22.331  298.801 1.00 18.87  ? 218 ILE A CB  1 
ATOM   1583 C  CG1 . ILE A 1 218 ? -94.447  22.929  297.405 1.00 18.61  ? 218 ILE A CG1 1 
ATOM   1584 C  CG2 . ILE A 1 218 ? -94.822  20.827  298.716 1.00 30.25  ? 218 ILE A CG2 1 
ATOM   1585 C  CD1 . ILE A 1 218 ? -93.277  22.353  296.643 1.00 19.67  ? 218 ILE A CD1 1 
ATOM   1586 N  N   . HIS A 1 219 ? -97.041  21.576  301.068 1.00 21.94  ? 219 HIS A N   1 
ATOM   1587 C  CA  . HIS A 1 219 ? -97.333  20.996  302.375 1.00 24.61  ? 219 HIS A CA  1 
ATOM   1588 C  C   . HIS A 1 219 ? -96.211  20.069  302.825 1.00 28.05  ? 219 HIS A C   1 
ATOM   1589 O  O   . HIS A 1 219 ? -95.710  20.180  303.950 1.00 33.57  ? 219 HIS A O   1 
ATOM   1590 C  CB  . HIS A 1 219 ? -98.666  20.250  302.328 1.00 27.81  ? 219 HIS A CB  1 
ATOM   1591 C  CG  . HIS A 1 219 ? -99.269  20.008  303.676 1.00 28.74  ? 219 HIS A CG  1 
ATOM   1592 N  ND1 . HIS A 1 219 ? -100.398 19.240  303.859 1.00 27.34  ? 219 HIS A ND1 1 
ATOM   1593 C  CD2 . HIS A 1 219 ? -98.901  20.435  304.907 1.00 29.32  ? 219 HIS A CD2 1 
ATOM   1594 C  CE1 . HIS A 1 219 ? -100.700 19.203  305.144 1.00 27.89  ? 219 HIS A CE1 1 
ATOM   1595 N  NE2 . HIS A 1 219 ? -99.808  19.921  305.802 1.00 30.29  ? 219 HIS A NE2 1 
ATOM   1596 N  N   . ASP A 1 220 ? -95.802  19.147  301.958 1.00 26.40  ? 220 ASP A N   1 
ATOM   1597 C  CA  . ASP A 1 220 ? -94.714  18.218  302.252 1.00 26.70  ? 220 ASP A CA  1 
ATOM   1598 C  C   . ASP A 1 220 ? -93.699  18.284  301.120 1.00 31.60  ? 220 ASP A C   1 
ATOM   1599 O  O   . ASP A 1 220 ? -93.945  17.740  300.029 1.00 30.50  ? 220 ASP A O   1 
ATOM   1600 C  CB  . ASP A 1 220 ? -95.231  16.796  302.433 1.00 26.42  ? 220 ASP A CB  1 
ATOM   1601 C  CG  . ASP A 1 220 ? -94.137  15.825  302.825 1.00 29.73  ? 220 ASP A CG  1 
ATOM   1602 O  OD1 . ASP A 1 220 ? -93.088  16.279  303.330 1.00 28.88  ? 220 ASP A OD1 1 
ATOM   1603 O  OD2 . ASP A 1 220 ? -94.324  14.606  302.626 1.00 59.21  ? 220 ASP A OD2 1 
ATOM   1604 N  N   . PRO A 1 221 ? -92.554  18.938  301.333 1.00 28.07  ? 221 PRO A N   1 
ATOM   1605 C  CA  . PRO A 1 221 ? -91.538  18.998  300.272 1.00 26.68  ? 221 PRO A CA  1 
ATOM   1606 C  C   . PRO A 1 221 ? -90.852  17.670  300.013 1.00 37.26  ? 221 PRO A C   1 
ATOM   1607 O  O   . PRO A 1 221 ? -90.241  17.507  298.950 1.00 30.62  ? 221 PRO A O   1 
ATOM   1608 C  CB  . PRO A 1 221 ? -90.548  20.045  300.797 1.00 26.30  ? 221 PRO A CB  1 
ATOM   1609 C  CG  . PRO A 1 221 ? -90.678  19.955  302.281 1.00 26.87  ? 221 PRO A CG  1 
ATOM   1610 C  CD  . PRO A 1 221 ? -92.130  19.657  302.547 1.00 27.53  ? 221 PRO A CD  1 
ATOM   1611 N  N   . TRP A 1 222 ? -90.932  16.719  300.946 1.00 25.93  ? 222 TRP A N   1 
ATOM   1612 C  CA  . TRP A 1 222 ? -90.299  15.420  300.741 1.00 24.07  ? 222 TRP A CA  1 
ATOM   1613 C  C   . TRP A 1 222 ? -90.969  14.657  299.605 1.00 24.60  ? 222 TRP A C   1 
ATOM   1614 O  O   . TRP A 1 222 ? -90.334  14.340  298.592 1.00 24.96  ? 222 TRP A O   1 
ATOM   1615 C  CB  . TRP A 1 222 ? -90.339  14.604  302.033 1.00 29.02  ? 222 TRP A CB  1 
ATOM   1616 C  CG  . TRP A 1 222 ? -89.888  13.191  301.845 1.00 30.29  ? 222 TRP A CG  1 
ATOM   1617 C  CD1 . TRP A 1 222 ? -90.674  12.076  301.818 1.00 41.19  ? 222 TRP A CD1 1 
ATOM   1618 C  CD2 . TRP A 1 222 ? -88.545  12.740  301.639 1.00 27.75  ? 222 TRP A CD2 1 
ATOM   1619 N  NE1 . TRP A 1 222 ? -89.902  10.957  301.616 1.00 35.58  ? 222 TRP A NE1 1 
ATOM   1620 C  CE2 . TRP A 1 222 ? -88.591  11.339  301.503 1.00 28.63  ? 222 TRP A CE2 1 
ATOM   1621 C  CE3 . TRP A 1 222 ? -87.307  13.385  301.561 1.00 30.87  ? 222 TRP A CE3 1 
ATOM   1622 C  CZ2 . TRP A 1 222 ? -87.448  10.572  301.293 1.00 30.59  ? 222 TRP A CZ2 1 
ATOM   1623 C  CZ3 . TRP A 1 222 ? -86.174  12.622  301.352 1.00 55.34  ? 222 TRP A CZ3 1 
ATOM   1624 C  CH2 . TRP A 1 222 ? -86.252  11.230  301.220 1.00 41.72  ? 222 TRP A CH2 1 
ATOM   1625 N  N   . ALA A 1 223 ? -92.258  14.349  299.758 1.00 25.44  ? 223 ALA A N   1 
ATOM   1626 C  CA  . ALA A 1 223 ? -92.977  13.612  298.728 1.00 25.04  ? 223 ALA A CA  1 
ATOM   1627 C  C   . ALA A 1 223 ? -93.121  14.406  297.438 1.00 22.69  ? 223 ALA A C   1 
ATOM   1628 O  O   . ALA A 1 223 ? -93.305  13.807  296.374 1.00 21.68  ? 223 ALA A O   1 
ATOM   1629 C  CB  . ALA A 1 223 ? -94.357  13.206  299.242 1.00 22.15  ? 223 ALA A CB  1 
ATOM   1630 N  N   . ALA A 1 224 ? -93.031  15.734  297.506 1.00 21.81  ? 224 ALA A N   1 
ATOM   1631 C  CA  . ALA A 1 224 ? -93.282  16.557  296.330 1.00 20.84  ? 224 ALA A CA  1 
ATOM   1632 C  C   . ALA A 1 224 ? -92.081  16.586  295.391 1.00 21.73  ? 224 ALA A C   1 
ATOM   1633 O  O   . ALA A 1 224 ? -92.231  16.402  294.179 1.00 26.39  ? 224 ALA A O   1 
ATOM   1634 C  CB  . ALA A 1 224 ? -93.662  17.975  296.755 1.00 21.74  ? 224 ALA A CB  1 
ATOM   1635 N  N   . VAL A 1 225 ? -90.882  16.811  295.928 1.00 20.78  ? 225 VAL A N   1 
ATOM   1636 C  CA  . VAL A 1 225 ? -89.726  17.067  295.074 1.00 20.67  ? 225 VAL A CA  1 
ATOM   1637 C  C   . VAL A 1 225 ? -88.477  16.364  295.597 1.00 24.42  ? 225 VAL A C   1 
ATOM   1638 O  O   . VAL A 1 225 ? -87.457  16.297  294.902 1.00 28.47  ? 225 VAL A O   1 
ATOM   1639 C  CB  . VAL A 1 225 ? -89.484  18.582  294.939 1.00 21.74  ? 225 VAL A CB  1 
ATOM   1640 C  CG1 . VAL A 1 225 ? -88.781  19.121  296.175 1.00 23.41  ? 225 VAL A CG1 1 
ATOM   1641 C  CG2 . VAL A 1 225 ? -88.696  18.896  293.675 1.00 29.44  ? 225 VAL A CG2 1 
ATOM   1642 N  N   . GLN A 1 226 ? -88.541  15.825  296.815 1.00 29.92  ? 226 GLN A N   1 
ATOM   1643 C  CA  . GLN A 1 226 ? -87.368  15.226  297.442 1.00 21.51  ? 226 GLN A CA  1 
ATOM   1644 C  C   . GLN A 1 226 ? -87.362  13.705  297.450 1.00 22.70  ? 226 GLN A C   1 
ATOM   1645 O  O   . GLN A 1 226 ? -86.289  13.111  297.337 1.00 27.20  ? 226 GLN A O   1 
ATOM   1646 C  CB  . GLN A 1 226 ? -87.224  15.716  298.888 1.00 21.93  ? 226 GLN A CB  1 
ATOM   1647 C  CG  . GLN A 1 226 ? -86.965  17.203  299.026 1.00 21.97  ? 226 GLN A CG  1 
ATOM   1648 C  CD  . GLN A 1 226 ? -86.754  17.624  300.467 1.00 22.72  ? 226 GLN A CD  1 
ATOM   1649 O  OE1 . GLN A 1 226 ? -87.074  16.883  301.397 1.00 26.60  ? 226 GLN A OE1 1 
ATOM   1650 N  NE2 . GLN A 1 226 ? -86.206  18.815  300.658 1.00 22.52  ? 226 GLN A NE2 1 
ATOM   1651 N  N   . LYS A 1 227 ? -88.514  13.062  297.586 1.00 23.28  ? 227 LYS A N   1 
ATOM   1652 C  CA  . LYS A 1 227 ? -88.537  11.611  297.755 1.00 29.73  ? 227 LYS A CA  1 
ATOM   1653 C  C   . LYS A 1 227 ? -88.062  10.916  296.482 1.00 23.85  ? 227 LYS A C   1 
ATOM   1654 O  O   . LYS A 1 227 ? -88.554  11.226  295.393 1.00 28.56  ? 227 LYS A O   1 
ATOM   1655 C  CB  . LYS A 1 227 ? -89.939  11.134  298.123 1.00 25.64  ? 227 LYS A CB  1 
ATOM   1656 C  CG  . LYS A 1 227 ? -90.028  9.641   298.403 1.00 22.17  ? 227 LYS A CG  1 
ATOM   1657 C  CD  . LYS A 1 227 ? -91.430  9.237   298.824 1.00 22.81  ? 227 LYS A CD  1 
ATOM   1658 C  CE  . LYS A 1 227 ? -91.456  7.807   299.335 1.00 20.80  ? 227 LYS A CE  1 
ATOM   1659 N  NZ  . LYS A 1 227 ? -90.660  7.653   300.583 1.00 20.70  ? 227 LYS A NZ  1 
ATOM   1660 N  N   . PRO A 1 228 ? -87.113  9.983   296.574 1.00 20.66  ? 228 PRO A N   1 
ATOM   1661 C  CA  . PRO A 1 228 ? -86.662  9.264   295.374 1.00 22.45  ? 228 PRO A CA  1 
ATOM   1662 C  C   . PRO A 1 228 ? -87.765  8.366   294.833 1.00 26.32  ? 228 PRO A C   1 
ATOM   1663 O  O   . PRO A 1 228 ? -88.368  7.585   295.573 1.00 46.69  ? 228 PRO A O   1 
ATOM   1664 C  CB  . PRO A 1 228 ? -85.466  8.445   295.876 1.00 23.38  ? 228 PRO A CB  1 
ATOM   1665 C  CG  . PRO A 1 228 ? -85.064  9.085   297.169 1.00 22.97  ? 228 PRO A CG  1 
ATOM   1666 C  CD  . PRO A 1 228 ? -86.331  9.613   297.764 1.00 23.00  ? 228 PRO A CD  1 
ATOM   1667 N  N   . GLN A 1 229 ? -88.025  8.482   293.533 1.00 24.62  ? 229 GLN A N   1 
ATOM   1668 C  CA  . GLN A 1 229 ? -89.051  7.698   292.860 1.00 18.60  ? 229 GLN A CA  1 
ATOM   1669 C  C   . GLN A 1 229 ? -88.492  7.165   291.547 1.00 17.76  ? 229 GLN A C   1 
ATOM   1670 O  O   . GLN A 1 229 ? -87.322  7.372   291.215 1.00 21.82  ? 229 GLN A O   1 
ATOM   1671 C  CB  . GLN A 1 229 ? -90.318  8.529   292.614 1.00 17.66  ? 229 GLN A CB  1 
ATOM   1672 C  CG  . GLN A 1 229 ? -91.002  9.032   293.876 1.00 20.95  ? 229 GLN A CG  1 
ATOM   1673 C  CD  . GLN A 1 229 ? -91.715  7.938   294.649 1.00 21.61  ? 229 GLN A CD  1 
ATOM   1674 O  OE1 . GLN A 1 229 ? -91.698  6.768   294.264 1.00 22.15  ? 229 GLN A OE1 1 
ATOM   1675 N  NE2 . GLN A 1 229 ? -92.344  8.316   295.754 1.00 21.89  ? 229 GLN A NE2 1 
ATOM   1676 N  N   . LYS A 1 230 ? -89.346  6.473   290.799 1.00 15.16  ? 230 LYS A N   1 
ATOM   1677 C  CA  . LYS A 1 230 ? -88.928  5.873   289.541 1.00 15.28  ? 230 LYS A CA  1 
ATOM   1678 C  C   . LYS A 1 230 ? -88.564  6.951   288.528 1.00 17.20  ? 230 LYS A C   1 
ATOM   1679 O  O   . LYS A 1 230 ? -89.216  7.994   288.445 1.00 19.37  ? 230 LYS A O   1 
ATOM   1680 C  CB  . LYS A 1 230 ? -90.040  4.968   289.004 1.00 12.55  ? 230 LYS A CB  1 
ATOM   1681 C  CG  . LYS A 1 230 ? -89.715  4.247   287.709 1.00 12.15  ? 230 LYS A CG  1 
ATOM   1682 C  CD  . LYS A 1 230 ? -90.650  3.070   287.468 1.00 11.11  ? 230 LYS A CD  1 
ATOM   1683 C  CE  . LYS A 1 230 ? -90.720  2.155   288.691 1.00 18.72  ? 230 LYS A CE  1 
ATOM   1684 N  NZ  . LYS A 1 230 ? -91.606  0.978   288.452 1.00 24.98  ? 230 LYS A NZ  1 
ATOM   1685 N  N   . SER A 1 231 ? -87.484  6.702   287.784 1.00 16.38  ? 231 SER A N   1 
ATOM   1686 C  CA  . SER A 1 231 ? -86.984  7.580   286.731 1.00 19.48  ? 231 SER A CA  1 
ATOM   1687 C  C   . SER A 1 231 ? -86.448  8.891   287.298 1.00 19.54  ? 231 SER A C   1 
ATOM   1688 O  O   . SER A 1 231 ? -85.987  9.755   286.547 1.00 18.47  ? 231 SER A O   1 
ATOM   1689 C  CB  . SER A 1 231 ? -88.071  7.847   285.682 1.00 15.29  ? 231 SER A CB  1 
ATOM   1690 O  OG  . SER A 1 231 ? -89.114  8.644   286.213 1.00 18.75  ? 231 SER A OG  1 
ATOM   1691 N  N   . VAL A 1 232 ? -86.469  9.040   288.621 1.00 22.11  ? 232 VAL A N   1 
ATOM   1692 C  CA  . VAL A 1 232 ? -85.871  10.202  289.271 1.00 27.02  ? 232 VAL A CA  1 
ATOM   1693 C  C   . VAL A 1 232 ? -85.181  9.746   290.551 1.00 35.96  ? 232 VAL A C   1 
ATOM   1694 O  O   . VAL A 1 232 ? -85.264  10.409  291.592 1.00 42.36  ? 232 VAL A O   1 
ATOM   1695 C  CB  . VAL A 1 232 ? -86.922  11.291  289.559 1.00 23.59  ? 232 VAL A CB  1 
ATOM   1696 C  CG1 . VAL A 1 232 ? -87.202  12.098  288.299 1.00 23.13  ? 232 VAL A CG1 1 
ATOM   1697 C  CG2 . VAL A 1 232 ? -88.198  10.674  290.110 1.00 24.28  ? 232 VAL A CG2 1 
ATOM   1698 N  N   . SER A 1 233 ? -84.499  8.604   290.484 1.00 28.44  ? 233 SER A N   1 
ATOM   1699 C  CA  . SER A 1 233 ? -83.865  8.004   291.650 1.00 33.13  ? 233 SER A CA  1 
ATOM   1700 C  C   . SER A 1 233 ? -82.371  8.289   291.732 1.00 43.68  ? 233 SER A C   1 
ATOM   1701 O  O   . SER A 1 233 ? -81.706  7.771   292.636 1.00 45.95  ? 233 SER A O   1 
ATOM   1702 C  CB  . SER A 1 233 ? -84.103  6.488   291.658 1.00 37.92  ? 233 SER A CB  1 
ATOM   1703 O  OG  . SER A 1 233 ? -83.632  5.902   292.860 1.00 68.57  ? 233 SER A OG  1 
ATOM   1704 N  N   . ALA A 1 234 ? -81.830  9.097   290.825 1.00 34.59  ? 234 ALA A N   1 
ATOM   1705 C  CA  . ALA A 1 234 ? -80.405  9.387   290.838 1.00 36.82  ? 234 ALA A CA  1 
ATOM   1706 C  C   . ALA A 1 234 ? -80.030  10.205  292.071 1.00 37.94  ? 234 ALA A C   1 
ATOM   1707 O  O   . ALA A 1 234 ? -80.852  10.910  292.661 1.00 37.91  ? 234 ALA A O   1 
ATOM   1708 C  CB  . ALA A 1 234 ? -79.994  10.132  289.567 1.00 39.44  ? 234 ALA A CB  1 
ATOM   1709 N  N   . TRP A 1 235 ? -78.758  10.096  292.461 1.00 38.31  ? 235 TRP A N   1 
ATOM   1710 C  CA  . TRP A 1 235 ? -78.278  10.827  293.628 1.00 42.68  ? 235 TRP A CA  1 
ATOM   1711 C  C   . TRP A 1 235 ? -78.129  12.313  293.328 1.00 40.63  ? 235 TRP A C   1 
ATOM   1712 O  O   . TRP A 1 235 ? -78.404  13.157  294.190 1.00 43.71  ? 235 TRP A O   1 
ATOM   1713 C  CB  . TRP A 1 235 ? -76.954  10.231  294.105 1.00 46.63  ? 235 TRP A CB  1 
ATOM   1714 C  CG  . TRP A 1 235 ? -75.870  10.283  293.074 1.00 59.86  ? 235 TRP A CG  1 
ATOM   1715 C  CD1 . TRP A 1 235 ? -75.647  9.380   292.075 1.00 67.59  ? 235 TRP A CD1 1 
ATOM   1716 C  CD2 . TRP A 1 235 ? -74.852  11.282  292.946 1.00 53.86  ? 235 TRP A CD2 1 
ATOM   1717 N  NE1 . TRP A 1 235 ? -74.558  9.759   291.329 1.00 57.68  ? 235 TRP A NE1 1 
ATOM   1718 C  CE2 . TRP A 1 235 ? -74.051  10.923  291.844 1.00 50.57  ? 235 TRP A CE2 1 
ATOM   1719 C  CE3 . TRP A 1 235 ? -74.542  12.447  293.655 1.00 51.60  ? 235 TRP A CE3 1 
ATOM   1720 C  CZ2 . TRP A 1 235 ? -72.961  11.687  291.434 1.00 55.87  ? 235 TRP A CZ2 1 
ATOM   1721 C  CZ3 . TRP A 1 235 ? -73.459  13.203  293.246 1.00 53.73  ? 235 TRP A CZ3 1 
ATOM   1722 C  CH2 . TRP A 1 235 ? -72.681  12.819  292.147 1.00 53.45  ? 235 TRP A CH2 1 
ATOM   1723 N  N   . ASN A 1 236 ? -77.697  12.654  292.115 1.00 39.89  ? 236 ASN A N   1 
ATOM   1724 C  CA  . ASN A 1 236 ? -77.597  14.038  291.678 1.00 40.90  ? 236 ASN A CA  1 
ATOM   1725 C  C   . ASN A 1 236 ? -78.847  14.505  290.944 1.00 39.53  ? 236 ASN A C   1 
ATOM   1726 O  O   . ASN A 1 236 ? -78.775  15.460  290.160 1.00 36.13  ? 236 ASN A O   1 
ATOM   1727 C  CB  . ASN A 1 236 ? -76.369  14.222  290.787 1.00 46.96  ? 236 ASN A CB  1 
ATOM   1728 C  CG  . ASN A 1 236 ? -76.376  13.296  289.588 1.00 44.34  ? 236 ASN A CG  1 
ATOM   1729 O  OD1 . ASN A 1 236 ? -77.055  12.270  289.586 1.00 42.67  ? 236 ASN A OD1 1 
ATOM   1730 N  ND2 . ASN A 1 236 ? -75.620  13.655  288.558 1.00 51.03  ? 236 ASN A ND2 1 
ATOM   1731 N  N   . GLU A 1 237 ? -79.978  13.853  291.174 1.00 54.95  ? 237 GLU A N   1 
ATOM   1732 C  CA  . GLU A 1 237 ? -81.211  14.192  290.474 1.00 35.95  ? 237 GLU A CA  1 
ATOM   1733 C  C   . GLU A 1 237 ? -81.663  15.592  290.863 1.00 32.73  ? 237 GLU A C   1 
ATOM   1734 O  O   . GLU A 1 237 ? -81.888  15.852  292.053 1.00 45.40  ? 237 GLU A O   1 
ATOM   1735 C  CB  . GLU A 1 237 ? -82.298  13.173  290.798 1.00 31.76  ? 237 GLU A CB  1 
ATOM   1736 C  CG  . GLU A 1 237 ? -83.458  13.172  289.819 1.00 48.51  ? 237 GLU A CG  1 
ATOM   1737 C  CD  . GLU A 1 237 ? -83.011  12.941  288.389 1.00 34.63  ? 237 GLU A CD  1 
ATOM   1738 O  OE1 . GLU A 1 237 ? -82.327  11.929  288.136 1.00 39.94  ? 237 GLU A OE1 1 
ATOM   1739 O  OE2 . GLU A 1 237 ? -83.345  13.772  287.519 1.00 49.16  ? 237 GLU A OE2 1 
ATOM   1740 N  N   . PRO A 1 238 ? -81.800  16.519  289.912 1.00 30.70  ? 238 PRO A N   1 
ATOM   1741 C  CA  . PRO A 1 238 ? -82.226  17.879  290.282 1.00 30.09  ? 238 PRO A CA  1 
ATOM   1742 C  C   . PRO A 1 238 ? -83.632  17.933  290.852 1.00 32.11  ? 238 PRO A C   1 
ATOM   1743 O  O   . PRO A 1 238 ? -83.891  18.713  291.776 1.00 32.86  ? 238 PRO A O   1 
ATOM   1744 C  CB  . PRO A 1 238 ? -82.117  18.651  288.959 1.00 26.71  ? 238 PRO A CB  1 
ATOM   1745 C  CG  . PRO A 1 238 ? -81.222  17.818  288.088 1.00 33.12  ? 238 PRO A CG  1 
ATOM   1746 C  CD  . PRO A 1 238 ? -81.488  16.403  288.480 1.00 32.28  ? 238 PRO A CD  1 
ATOM   1747 N  N   . TYR A 1 239 ? -84.549  17.119  290.332 1.00 28.67  ? 239 TYR A N   1 
ATOM   1748 C  CA  . TYR A 1 239 ? -85.937  17.117  290.778 1.00 25.51  ? 239 TYR A CA  1 
ATOM   1749 C  C   . TYR A 1 239 ? -86.396  15.680  290.964 1.00 27.14  ? 239 TYR A C   1 
ATOM   1750 O  O   . TYR A 1 239 ? -86.348  14.883  290.021 1.00 28.03  ? 239 TYR A O   1 
ATOM   1751 C  CB  . TYR A 1 239 ? -86.838  17.844  289.777 1.00 24.97  ? 239 TYR A CB  1 
ATOM   1752 C  CG  . TYR A 1 239 ? -86.334  19.215  289.388 1.00 27.59  ? 239 TYR A CG  1 
ATOM   1753 C  CD1 . TYR A 1 239 ? -86.310  20.254  290.309 1.00 27.81  ? 239 TYR A CD1 1 
ATOM   1754 C  CD2 . TYR A 1 239 ? -85.880  19.470  288.101 1.00 25.98  ? 239 TYR A CD2 1 
ATOM   1755 C  CE1 . TYR A 1 239 ? -85.848  21.508  289.959 1.00 26.26  ? 239 TYR A CE1 1 
ATOM   1756 C  CE2 . TYR A 1 239 ? -85.417  20.721  287.742 1.00 26.38  ? 239 TYR A CE2 1 
ATOM   1757 C  CZ  . TYR A 1 239 ? -85.403  21.736  288.674 1.00 25.35  ? 239 TYR A CZ  1 
ATOM   1758 O  OH  . TYR A 1 239 ? -84.943  22.984  288.321 1.00 22.18  ? 239 TYR A OH  1 
ATOM   1759 N  N   . LYS A 1 240 ? -86.838  15.352  292.178 1.00 29.17  ? 240 LYS A N   1 
ATOM   1760 C  CA  . LYS A 1 240 ? -87.384  14.032  292.469 1.00 24.79  ? 240 LYS A CA  1 
ATOM   1761 C  C   . LYS A 1 240 ? -88.846  14.152  292.879 1.00 26.57  ? 240 LYS A C   1 
ATOM   1762 O  O   . LYS A 1 240 ? -89.523  15.116  292.506 1.00 21.71  ? 240 LYS A O   1 
ATOM   1763 C  CB  . LYS A 1 240 ? -86.576  13.342  293.570 1.00 23.19  ? 240 LYS A CB  1 
ATOM   1764 C  CG  . LYS A 1 240 ? -85.073  13.355  293.349 1.00 26.00  ? 240 LYS A CG  1 
ATOM   1765 C  CD  . LYS A 1 240 ? -84.345  12.669  294.496 1.00 30.89  ? 240 LYS A CD  1 
ATOM   1766 C  CE  . LYS A 1 240 ? -82.839  12.843  294.382 1.00 35.20  ? 240 LYS A CE  1 
ATOM   1767 N  NZ  . LYS A 1 240 ? -82.129  12.375  295.605 1.00 46.06  ? 240 LYS A NZ  1 
ATOM   1768 N  N   . GLY A 1 241 ? -89.339  13.180  293.643 1.00 27.48  ? 241 GLY A N   1 
ATOM   1769 C  CA  . GLY A 1 241 ? -90.677  13.230  294.197 1.00 22.73  ? 241 GLY A CA  1 
ATOM   1770 C  C   . GLY A 1 241 ? -91.775  13.255  293.142 1.00 19.03  ? 241 GLY A C   1 
ATOM   1771 O  O   . GLY A 1 241 ? -91.591  12.869  291.985 1.00 15.68  ? 241 GLY A O   1 
ATOM   1772 N  N   . ASN A 1 242 ? -92.945  13.727  293.578 1.00 16.88  ? 242 ASN A N   1 
ATOM   1773 C  CA  . ASN A 1 242 ? -94.089  13.817  292.677 1.00 17.01  ? 242 ASN A CA  1 
ATOM   1774 C  C   . ASN A 1 242 ? -93.849  14.842  291.577 1.00 18.09  ? 242 ASN A C   1 
ATOM   1775 O  O   . ASN A 1 242 ? -94.229  14.621  290.422 1.00 17.20  ? 242 ASN A O   1 
ATOM   1776 C  CB  . ASN A 1 242 ? -95.353  14.166  293.463 1.00 16.45  ? 242 ASN A CB  1 
ATOM   1777 C  CG  . ASN A 1 242 ? -95.636  13.180  294.577 1.00 15.52  ? 242 ASN A CG  1 
ATOM   1778 O  OD1 . ASN A 1 242 ? -95.237  12.019  294.509 1.00 24.28  ? 242 ASN A OD1 1 
ATOM   1779 N  ND2 . ASN A 1 242 ? -96.327  13.640  295.613 1.00 11.88  ? 242 ASN A ND2 1 
ATOM   1780 N  N   . PHE A 1 243 ? -93.217  15.969  291.915 1.00 20.08  ? 243 PHE A N   1 
ATOM   1781 C  CA  . PHE A 1 243 ? -92.997  17.016  290.922 1.00 23.23  ? 243 PHE A CA  1 
ATOM   1782 C  C   . PHE A 1 243 ? -92.038  16.556  289.832 1.00 25.28  ? 243 PHE A C   1 
ATOM   1783 O  O   . PHE A 1 243 ? -92.261  16.830  288.647 1.00 50.47  ? 243 PHE A O   1 
ATOM   1784 C  CB  . PHE A 1 243 ? -92.472  18.282  291.597 1.00 24.21  ? 243 PHE A CB  1 
ATOM   1785 C  CG  . PHE A 1 243 ? -93.537  19.097  292.273 1.00 23.00  ? 243 PHE A CG  1 
ATOM   1786 C  CD1 . PHE A 1 243 ? -94.852  18.665  292.297 1.00 21.19  ? 243 PHE A CD1 1 
ATOM   1787 C  CD2 . PHE A 1 243 ? -93.223  20.303  292.873 1.00 22.58  ? 243 PHE A CD2 1 
ATOM   1788 C  CE1 . PHE A 1 243 ? -95.832  19.417  292.915 1.00 19.34  ? 243 PHE A CE1 1 
ATOM   1789 C  CE2 . PHE A 1 243 ? -94.198  21.060  293.492 1.00 22.37  ? 243 PHE A CE2 1 
ATOM   1790 C  CZ  . PHE A 1 243 ? -95.503  20.616  293.513 1.00 20.16  ? 243 PHE A CZ  1 
ATOM   1791 N  N   . GLY A 1 244 ? -90.966  15.858  290.211 1.00 20.55  ? 244 GLY A N   1 
ATOM   1792 C  CA  . GLY A 1 244 ? -90.009  15.398  289.217 1.00 23.93  ? 244 GLY A CA  1 
ATOM   1793 C  C   . GLY A 1 244 ? -90.609  14.405  288.240 1.00 29.95  ? 244 GLY A C   1 
ATOM   1794 O  O   . GLY A 1 244 ? -90.344  14.466  287.037 1.00 29.95  ? 244 GLY A O   1 
ATOM   1795 N  N   . GLN A 1 245 ? -91.428  13.479  288.743 1.00 23.46  ? 245 GLN A N   1 
ATOM   1796 C  CA  . GLN A 1 245 ? -92.064  12.504  287.863 1.00 19.45  ? 245 GLN A CA  1 
ATOM   1797 C  C   . GLN A 1 245 ? -93.061  13.171  286.926 1.00 17.12  ? 245 GLN A C   1 
ATOM   1798 O  O   . GLN A 1 245 ? -93.178  12.782  285.758 1.00 16.64  ? 245 GLN A O   1 
ATOM   1799 C  CB  . GLN A 1 245 ? -92.750  11.417  288.690 1.00 16.69  ? 245 GLN A CB  1 
ATOM   1800 C  CG  . GLN A 1 245 ? -91.797  10.418  289.319 1.00 17.45  ? 245 GLN A CG  1 
ATOM   1801 C  CD  . GLN A 1 245 ? -92.523  9.278   290.005 1.00 14.74  ? 245 GLN A CD  1 
ATOM   1802 O  OE1 . GLN A 1 245 ? -93.487  9.494   290.740 1.00 15.40  ? 245 GLN A OE1 1 
ATOM   1803 N  NE2 . GLN A 1 245 ? -92.067  8.056   289.763 1.00 13.83  ? 245 GLN A NE2 1 
ATOM   1804 N  N   . LEU A 1 246 ? -93.787  14.179  287.416 1.00 19.15  ? 246 LEU A N   1 
ATOM   1805 C  CA  . LEU A 1 246 ? -94.759  14.866  286.571 1.00 22.73  ? 246 LEU A CA  1 
ATOM   1806 C  C   . LEU A 1 246 ? -94.082  15.608  285.425 1.00 21.55  ? 246 LEU A C   1 
ATOM   1807 O  O   . LEU A 1 246 ? -94.690  15.791  284.364 1.00 18.88  ? 246 LEU A O   1 
ATOM   1808 C  CB  . LEU A 1 246 ? -95.600  15.828  287.410 1.00 16.14  ? 246 LEU A CB  1 
ATOM   1809 C  CG  . LEU A 1 246 ? -96.593  15.187  288.384 1.00 15.15  ? 246 LEU A CG  1 
ATOM   1810 C  CD1 . LEU A 1 246 ? -97.172  16.228  289.330 1.00 13.92  ? 246 LEU A CD1 1 
ATOM   1811 C  CD2 . LEU A 1 246 ? -97.701  14.458  287.642 1.00 15.48  ? 246 LEU A CD2 1 
ATOM   1812 N  N   . MET A 1 247 ? -92.834  16.042  285.616 1.00 18.64  ? 247 MET A N   1 
ATOM   1813 C  CA  . MET A 1 247 ? -92.085  16.641  284.516 1.00 18.07  ? 247 MET A CA  1 
ATOM   1814 C  C   . MET A 1 247 ? -91.810  15.614  283.426 1.00 17.18  ? 247 MET A C   1 
ATOM   1815 O  O   . MET A 1 247 ? -92.034  15.877  282.238 1.00 18.57  ? 247 MET A O   1 
ATOM   1816 C  CB  . MET A 1 247 ? -90.772  17.234  285.028 1.00 21.93  ? 247 MET A CB  1 
ATOM   1817 C  CG  . MET A 1 247 ? -90.921  18.229  286.162 1.00 19.64  ? 247 MET A CG  1 
ATOM   1818 S  SD  . MET A 1 247 ? -89.324  18.719  286.835 1.00 15.77  ? 247 MET A SD  1 
ATOM   1819 C  CE  . MET A 1 247 ? -89.832  19.598  288.309 1.00 20.19  ? 247 MET A CE  1 
ATOM   1820 N  N   . ALA A 1 248 ? -91.322  14.434  283.814 1.00 16.86  ? 248 ALA A N   1 
ATOM   1821 C  CA  . ALA A 1 248 ? -91.039  13.391  282.836 1.00 18.22  ? 248 ALA A CA  1 
ATOM   1822 C  C   . ALA A 1 248 ? -92.317  12.766  282.293 1.00 19.77  ? 248 ALA A C   1 
ATOM   1823 O  O   . ALA A 1 248 ? -92.323  12.246  281.172 1.00 20.47  ? 248 ALA A O   1 
ATOM   1824 C  CB  . ALA A 1 248 ? -90.147  12.318  283.459 1.00 18.69  ? 248 ALA A CB  1 
ATOM   1825 N  N   . ALA A 1 249 ? -93.402  12.808  283.068 1.00 20.91  ? 249 ALA A N   1 
ATOM   1826 C  CA  . ALA A 1 249 ? -94.655  12.212  282.619 1.00 19.59  ? 249 ALA A CA  1 
ATOM   1827 C  C   . ALA A 1 249 ? -95.277  13.015  281.484 1.00 19.14  ? 249 ALA A C   1 
ATOM   1828 O  O   . ALA A 1 249 ? -95.835  12.438  280.543 1.00 17.74  ? 249 ALA A O   1 
ATOM   1829 C  CB  . ALA A 1 249 ? -95.627  12.095  283.791 1.00 18.36  ? 249 ALA A CB  1 
ATOM   1830 N  N   . LYS A 1 250 ? -95.193  14.346  281.554 1.00 19.05  ? 250 LYS A N   1 
ATOM   1831 C  CA  . LYS A 1 250 ? -95.725  15.182  280.483 1.00 20.79  ? 250 LYS A CA  1 
ATOM   1832 C  C   . LYS A 1 250 ? -95.004  14.954  279.163 1.00 21.18  ? 250 LYS A C   1 
ATOM   1833 O  O   . LYS A 1 250 ? -95.566  15.248  278.103 1.00 22.79  ? 250 LYS A O   1 
ATOM   1834 C  CB  . LYS A 1 250 ? -95.640  16.658  280.871 1.00 22.79  ? 250 LYS A CB  1 
ATOM   1835 C  CG  . LYS A 1 250 ? -96.613  17.066  281.960 1.00 28.39  ? 250 LYS A CG  1 
ATOM   1836 C  CD  . LYS A 1 250 ? -96.689  18.578  282.099 1.00 26.07  ? 250 LYS A CD  1 
ATOM   1837 C  CE  . LYS A 1 250 ? -97.144  19.230  280.804 1.00 29.67  ? 250 LYS A CE  1 
ATOM   1838 N  NZ  . LYS A 1 250 ? -97.236  20.711  280.932 1.00 27.62  ? 250 LYS A NZ  1 
ATOM   1839 N  N   . LEU A 1 251 ? -93.773  14.443  279.202 1.00 22.83  ? 251 LEU A N   1 
ATOM   1840 C  CA  . LEU A 1 251 ? -93.068  14.116  277.969 1.00 21.45  ? 251 LEU A CA  1 
ATOM   1841 C  C   . LEU A 1 251 ? -93.593  12.822  277.361 1.00 21.61  ? 251 LEU A C   1 
ATOM   1842 O  O   . LEU A 1 251 ? -93.765  12.731  276.140 1.00 26.83  ? 251 LEU A O   1 
ATOM   1843 C  CB  . LEU A 1 251 ? -91.567  14.014  278.237 1.00 19.35  ? 251 LEU A CB  1 
ATOM   1844 C  CG  . LEU A 1 251 ? -90.942  15.231  278.919 1.00 18.32  ? 251 LEU A CG  1 
ATOM   1845 C  CD1 . LEU A 1 251 ? -89.477  14.977  279.223 1.00 46.18  ? 251 LEU A CD1 1 
ATOM   1846 C  CD2 . LEU A 1 251 ? -91.110  16.472  278.058 1.00 25.59  ? 251 LEU A CD2 1 
ATOM   1847 N  N   . ALA A 1 252 ? -93.851  11.812  278.195 1.00 19.77  ? 252 ALA A N   1 
ATOM   1848 C  CA  . ALA A 1 252 ? -94.449  10.579  277.698 1.00 16.81  ? 252 ALA A CA  1 
ATOM   1849 C  C   . ALA A 1 252 ? -95.923  10.767  277.370 1.00 17.75  ? 252 ALA A C   1 
ATOM   1850 O  O   . ALA A 1 252 ? -96.465  10.051  276.521 1.00 20.62  ? 252 ALA A O   1 
ATOM   1851 C  CB  . ALA A 1 252 ? -94.272  9.457   278.720 1.00 18.49  ? 252 ALA A CB  1 
ATOM   1852 N  N   . ASN A 1 253 ? -96.585  11.721  278.028 1.00 19.16  ? 253 ASN A N   1 
ATOM   1853 C  CA  . ASN A 1 253 ? -97.989  12.041  277.787 1.00 18.74  ? 253 ASN A CA  1 
ATOM   1854 C  C   . ASN A 1 253 ? -98.076  13.514  277.404 1.00 20.40  ? 253 ASN A C   1 
ATOM   1855 O  O   . ASN A 1 253 ? -98.421  14.364  278.239 1.00 31.30  ? 253 ASN A O   1 
ATOM   1856 C  CB  . ASN A 1 253 ? -98.849  11.736  279.013 1.00 16.13  ? 253 ASN A CB  1 
ATOM   1857 C  CG  . ASN A 1 253 ? -98.677  10.313  279.505 1.00 17.11  ? 253 ASN A CG  1 
ATOM   1858 O  OD1 . ASN A 1 253 ? -99.336  9.393   279.022 1.00 31.91  ? 253 ASN A OD1 1 
ATOM   1859 N  ND2 . ASN A 1 253 ? -97.788  10.126  280.473 1.00 15.75  ? 253 ASN A ND2 1 
ATOM   1860 N  N   . PRO A 1 254 ? -97.765  13.855  276.151 1.00 21.55  ? 254 PRO A N   1 
ATOM   1861 C  CA  . PRO A 1 254 ? -97.836  15.268  275.748 1.00 20.94  ? 254 PRO A CA  1 
ATOM   1862 C  C   . PRO A 1 254 ? -99.251  15.813  275.744 1.00 20.29  ? 254 PRO A C   1 
ATOM   1863 O  O   . PRO A 1 254 ? -99.437  17.026  275.903 1.00 34.94  ? 254 PRO A O   1 
ATOM   1864 C  CB  . PRO A 1 254 ? -97.224  15.260  274.342 1.00 19.22  ? 254 PRO A CB  1 
ATOM   1865 C  CG  . PRO A 1 254 ? -97.514  13.888  273.831 1.00 25.30  ? 254 PRO A CG  1 
ATOM   1866 C  CD  . PRO A 1 254 ? -97.403  12.977  275.025 1.00 26.00  ? 254 PRO A CD  1 
ATOM   1867 N  N   . HIS A 1 255 ? -100.255 14.952  275.568 1.00 18.72  ? 255 HIS A N   1 
ATOM   1868 C  CA  . HIS A 1 255 ? -101.640 15.399  275.654 1.00 18.83  ? 255 HIS A CA  1 
ATOM   1869 C  C   . HIS A 1 255 ? -101.997 15.843  277.065 1.00 19.29  ? 255 HIS A C   1 
ATOM   1870 O  O   . HIS A 1 255 ? -102.856 16.714  277.242 1.00 20.52  ? 255 HIS A O   1 
ATOM   1871 C  CB  . HIS A 1 255 ? -102.576 14.274  275.218 1.00 21.66  ? 255 HIS A CB  1 
ATOM   1872 C  CG  . HIS A 1 255 ? -102.687 13.168  276.220 1.00 20.45  ? 255 HIS A CG  1 
ATOM   1873 N  ND1 . HIS A 1 255 ? -101.820 12.097  276.246 1.00 29.14  ? 255 HIS A ND1 1 
ATOM   1874 C  CD2 . HIS A 1 255 ? -103.555 12.975  277.242 1.00 21.36  ? 255 HIS A CD2 1 
ATOM   1875 C  CE1 . HIS A 1 255 ? -102.152 11.289  277.237 1.00 24.21  ? 255 HIS A CE1 1 
ATOM   1876 N  NE2 . HIS A 1 255 ? -103.202 11.798  277.856 1.00 21.42  ? 255 HIS A NE2 1 
ATOM   1877 N  N   . LEU A 1 256 ? -101.351 15.259  278.071 1.00 21.53  ? 256 LEU A N   1 
ATOM   1878 C  CA  . LEU A 1 256 ? -101.741 15.483  279.454 1.00 30.03  ? 256 LEU A CA  1 
ATOM   1879 C  C   . LEU A 1 256 ? -101.481 16.924  279.874 1.00 24.14  ? 256 LEU A C   1 
ATOM   1880 O  O   . LEU A 1 256 ? -100.452 17.515  279.535 1.00 24.24  ? 256 LEU A O   1 
ATOM   1881 C  CB  . LEU A 1 256 ? -100.985 14.528  280.377 1.00 24.34  ? 256 LEU A CB  1 
ATOM   1882 C  CG  . LEU A 1 256 ? -101.207 14.723  281.877 1.00 20.62  ? 256 LEU A CG  1 
ATOM   1883 C  CD1 . LEU A 1 256 ? -102.579 14.210  282.292 1.00 19.55  ? 256 LEU A CD1 1 
ATOM   1884 C  CD2 . LEU A 1 256 ? -100.107 14.049  282.675 1.00 19.23  ? 256 LEU A CD2 1 
ATOM   1885 N  N   . LYS A 1 257 ? -102.430 17.485  280.616 1.00 23.00  ? 257 LYS A N   1 
ATOM   1886 C  CA  . LYS A 1 257 ? -102.317 18.811  281.204 1.00 20.45  ? 257 LYS A CA  1 
ATOM   1887 C  C   . LYS A 1 257 ? -102.466 18.685  282.713 1.00 16.94  ? 257 LYS A C   1 
ATOM   1888 O  O   . LYS A 1 257 ? -103.396 18.031  283.196 1.00 17.84  ? 257 LYS A O   1 
ATOM   1889 C  CB  . LYS A 1 257 ? -103.375 19.750  280.623 1.00 25.62  ? 257 LYS A CB  1 
ATOM   1890 C  CG  . LYS A 1 257 ? -103.532 19.616  279.114 1.00 44.83  ? 257 LYS A CG  1 
ATOM   1891 C  CD  . LYS A 1 257 ? -104.553 20.595  278.564 1.00 38.89  ? 257 LYS A CD  1 
ATOM   1892 C  CE  . LYS A 1 257 ? -105.881 20.449  279.285 1.00 36.98  ? 257 LYS A CE  1 
ATOM   1893 N  NZ  . LYS A 1 257 ? -106.335 19.032  279.306 1.00 80.15  ? 257 LYS A NZ  1 
ATOM   1894 N  N   . ILE A 1 258 ? -101.547 19.298  283.453 1.00 16.32  ? 258 ILE A N   1 
ATOM   1895 C  CA  . ILE A 1 258 ? -101.481 19.167  284.903 1.00 15.45  ? 258 ILE A CA  1 
ATOM   1896 C  C   . ILE A 1 258 ? -101.861 20.500  285.529 1.00 16.16  ? 258 ILE A C   1 
ATOM   1897 O  O   . ILE A 1 258 ? -101.389 21.556  285.091 1.00 17.28  ? 258 ILE A O   1 
ATOM   1898 C  CB  . ILE A 1 258 ? -100.083 18.719  285.360 1.00 14.62  ? 258 ILE A CB  1 
ATOM   1899 C  CG1 . ILE A 1 258 ? -99.699  17.413  284.668 1.00 13.81  ? 258 ILE A CG1 1 
ATOM   1900 C  CG2 . ILE A 1 258 ? -100.044 18.549  286.870 1.00 12.24  ? 258 ILE A CG2 1 
ATOM   1901 C  CD1 . ILE A 1 258 ? -98.357  16.879  285.088 1.00 15.91  ? 258 ILE A CD1 1 
ATOM   1902 N  N   . LEU A 1 259 ? -102.713 20.449  286.551 1.00 18.55  ? 259 LEU A N   1 
ATOM   1903 C  CA  . LEU A 1 259 ? -103.178 21.642  287.234 1.00 20.31  ? 259 LEU A CA  1 
ATOM   1904 C  C   . LEU A 1 259 ? -102.935 21.515  288.731 1.00 18.82  ? 259 LEU A C   1 
ATOM   1905 O  O   . LEU A 1 259 ? -103.196 20.458  289.317 1.00 16.42  ? 259 LEU A O   1 
ATOM   1906 C  CB  . LEU A 1 259 ? -104.673 21.876  286.974 1.00 20.55  ? 259 LEU A CB  1 
ATOM   1907 C  CG  . LEU A 1 259 ? -105.071 22.179  285.530 1.00 21.73  ? 259 LEU A CG  1 
ATOM   1908 C  CD1 . LEU A 1 259 ? -106.580 22.324  285.409 1.00 26.73  ? 259 LEU A CD1 1 
ATOM   1909 C  CD2 . LEU A 1 259 ? -104.364 23.424  285.027 1.00 18.71  ? 259 LEU A CD2 1 
ATOM   1910 N  N   . PRO A 1 260 ? -102.431 22.568  289.374 1.00 18.10  ? 260 PRO A N   1 
ATOM   1911 C  CA  . PRO A 1 260 ? -102.248 22.527  290.829 1.00 17.13  ? 260 PRO A CA  1 
ATOM   1912 C  C   . PRO A 1 260 ? -103.515 22.907  291.578 1.00 18.27  ? 260 PRO A C   1 
ATOM   1913 O  O   . PRO A 1 260 ? -104.074 23.988  291.364 1.00 18.46  ? 260 PRO A O   1 
ATOM   1914 C  CB  . PRO A 1 260 ? -101.126 23.543  291.061 1.00 16.48  ? 260 PRO A CB  1 
ATOM   1915 C  CG  . PRO A 1 260 ? -101.336 24.553  289.978 1.00 18.44  ? 260 PRO A CG  1 
ATOM   1916 C  CD  . PRO A 1 260 ? -101.870 23.794  288.781 1.00 18.26  ? 260 PRO A CD  1 
ATOM   1917 N  N   . SER A 1 261 ? -103.979 22.024  292.457 1.00 15.91  ? 261 SER A N   1 
ATOM   1918 C  CA  . SER A 1 261 ? -105.198 22.258  293.222 1.00 17.13  ? 261 SER A CA  1 
ATOM   1919 C  C   . SER A 1 261 ? -104.837 22.991  294.508 1.00 17.01  ? 261 SER A C   1 
ATOM   1920 O  O   . SER A 1 261 ? -104.174 22.431  295.388 1.00 16.67  ? 261 SER A O   1 
ATOM   1921 C  CB  . SER A 1 261 ? -105.914 20.942  293.513 1.00 20.04  ? 261 SER A CB  1 
ATOM   1922 O  OG  . SER A 1 261 ? -106.560 20.451  292.351 1.00 25.75  ? 261 SER A OG  1 
ATOM   1923 N  N   . ILE A 1 262 ? -105.269 24.242  294.614 1.00 17.09  ? 262 ILE A N   1 
ATOM   1924 C  CA  . ILE A 1 262 ? -105.005 25.075  295.780 1.00 16.68  ? 262 ILE A CA  1 
ATOM   1925 C  C   . ILE A 1 262 ? -106.202 24.967  296.713 1.00 20.06  ? 262 ILE A C   1 
ATOM   1926 O  O   . ILE A 1 262 ? -107.299 25.435  296.388 1.00 22.31  ? 262 ILE A O   1 
ATOM   1927 C  CB  . ILE A 1 262 ? -104.740 26.533  295.383 1.00 17.10  ? 262 ILE A CB  1 
ATOM   1928 C  CG1 . ILE A 1 262 ? -103.655 26.608  294.307 1.00 22.23  ? 262 ILE A CG1 1 
ATOM   1929 C  CG2 . ILE A 1 262 ? -104.350 27.351  296.599 1.00 16.69  ? 262 ILE A CG2 1 
ATOM   1930 C  CD1 . ILE A 1 262 ? -103.344 28.021  293.863 1.00 17.12  ? 262 ILE A CD1 1 
ATOM   1931 N  N   . GLY A 1 263 ? -105.998 24.358  297.877 1.00 19.43  ? 263 GLY A N   1 
ATOM   1932 C  CA  . GLY A 1 263 ? -107.051 24.274  298.869 1.00 18.89  ? 263 GLY A CA  1 
ATOM   1933 C  C   . GLY A 1 263 ? -107.419 22.860  299.265 1.00 21.39  ? 263 GLY A C   1 
ATOM   1934 O  O   . GLY A 1 263 ? -106.578 22.101  299.753 1.00 20.83  ? 263 GLY A O   1 
ATOM   1935 N  N   . GLY A 1 264 ? -108.674 22.494  299.052 1.00 20.56  ? 264 GLY A N   1 
ATOM   1936 C  CA  . GLY A 1 264 ? -109.180 21.213  299.490 1.00 20.22  ? 264 GLY A CA  1 
ATOM   1937 C  C   . GLY A 1 264 ? -110.055 21.339  300.719 1.00 24.16  ? 264 GLY A C   1 
ATOM   1938 O  O   . GLY A 1 264 ? -110.522 22.418  301.087 1.00 24.84  ? 264 GLY A O   1 
ATOM   1939 N  N   . TRP A 1 265 ? -110.273 20.197  301.371 1.00 25.63  ? 265 TRP A N   1 
ATOM   1940 C  CA  . TRP A 1 265 ? -111.130 20.188  302.551 1.00 27.66  ? 265 TRP A CA  1 
ATOM   1941 C  C   . TRP A 1 265 ? -110.457 20.873  303.734 1.00 25.26  ? 265 TRP A C   1 
ATOM   1942 O  O   . TRP A 1 265 ? -111.092 21.659  304.446 1.00 31.26  ? 265 TRP A O   1 
ATOM   1943 C  CB  . TRP A 1 265 ? -111.518 18.754  302.912 1.00 27.03  ? 265 TRP A CB  1 
ATOM   1944 C  CG  . TRP A 1 265 ? -112.343 18.659  304.159 1.00 28.74  ? 265 TRP A CG  1 
ATOM   1945 C  CD1 . TRP A 1 265 ? -111.939 18.192  305.375 1.00 30.75  ? 265 TRP A CD1 1 
ATOM   1946 C  CD2 . TRP A 1 265 ? -113.712 19.050  304.314 1.00 29.77  ? 265 TRP A CD2 1 
ATOM   1947 N  NE1 . TRP A 1 265 ? -112.972 18.263  306.277 1.00 32.57  ? 265 TRP A NE1 1 
ATOM   1948 C  CE2 . TRP A 1 265 ? -114.072 18.787  305.651 1.00 35.40  ? 265 TRP A CE2 1 
ATOM   1949 C  CE3 . TRP A 1 265 ? -114.669 19.595  303.453 1.00 34.04  ? 265 TRP A CE3 1 
ATOM   1950 C  CZ2 . TRP A 1 265 ? -115.347 19.051  306.146 1.00 41.29  ? 265 TRP A CZ2 1 
ATOM   1951 C  CZ3 . TRP A 1 265 ? -115.935 19.856  303.947 1.00 36.06  ? 265 TRP A CZ3 1 
ATOM   1952 C  CH2 . TRP A 1 265 ? -116.262 19.584  305.281 1.00 37.04  ? 265 TRP A CH2 1 
ATOM   1953 N  N   . THR A 1 266 ? -109.173 20.599  303.953 1.00 22.28  ? 266 THR A N   1 
ATOM   1954 C  CA  . THR A 1 266 ? -108.478 21.126  305.120 1.00 26.95  ? 266 THR A CA  1 
ATOM   1955 C  C   . THR A 1 266 ? -107.777 22.452  304.853 1.00 32.90  ? 266 THR A C   1 
ATOM   1956 O  O   . THR A 1 266 ? -107.622 23.256  305.778 1.00 31.96  ? 266 THR A O   1 
ATOM   1957 C  CB  . THR A 1 266 ? -107.454 20.107  305.628 1.00 26.98  ? 266 THR A CB  1 
ATOM   1958 O  OG1 . THR A 1 266 ? -106.495 19.835  304.599 1.00 24.61  ? 266 THR A OG1 1 
ATOM   1959 C  CG2 . THR A 1 266 ? -108.144 18.810  306.021 1.00 24.97  ? 266 THR A CG2 1 
ATOM   1960 N  N   . LEU A 1 267 ? -107.358 22.706  303.613 1.00 25.72  ? 267 LEU A N   1 
ATOM   1961 C  CA  . LEU A 1 267 ? -106.559 23.878  303.282 1.00 20.61  ? 267 LEU A CA  1 
ATOM   1962 C  C   . LEU A 1 267 ? -107.392 25.022  302.712 1.00 24.68  ? 267 LEU A C   1 
ATOM   1963 O  O   . LEU A 1 267 ? -106.844 25.898  302.035 1.00 35.10  ? 267 LEU A O   1 
ATOM   1964 C  CB  . LEU A 1 267 ? -105.454 23.495  302.297 1.00 20.05  ? 267 LEU A CB  1 
ATOM   1965 C  CG  . LEU A 1 267 ? -104.384 22.518  302.785 1.00 23.08  ? 267 LEU A CG  1 
ATOM   1966 C  CD1 . LEU A 1 267 ? -103.585 21.982  301.611 1.00 30.98  ? 267 LEU A CD1 1 
ATOM   1967 C  CD2 . LEU A 1 267 ? -103.467 23.194  303.782 1.00 25.62  ? 267 LEU A CD2 1 
ATOM   1968 N  N   . SER A 1 268 ? -108.698 25.039  302.972 1.00 22.41  ? 268 SER A N   1 
ATOM   1969 C  CA  . SER A 1 268 ? -109.568 26.079  302.439 1.00 22.33  ? 268 SER A CA  1 
ATOM   1970 C  C   . SER A 1 268 ? -109.720 27.276  303.367 1.00 24.55  ? 268 SER A C   1 
ATOM   1971 O  O   . SER A 1 268 ? -110.305 28.283  302.957 1.00 27.79  ? 268 SER A O   1 
ATOM   1972 C  CB  . SER A 1 268 ? -110.956 25.506  302.132 1.00 24.37  ? 268 SER A CB  1 
ATOM   1973 O  OG  . SER A 1 268 ? -110.893 24.543  301.097 1.00 25.79  ? 268 SER A OG  1 
ATOM   1974 N  N   . ASP A 1 269 ? -109.206 27.194  304.593 1.00 25.46  ? 269 ASP A N   1 
ATOM   1975 C  CA  . ASP A 1 269 ? -109.419 28.270  305.559 1.00 27.93  ? 269 ASP A CA  1 
ATOM   1976 C  C   . ASP A 1 269 ? -108.864 29.624  305.121 1.00 24.32  ? 269 ASP A C   1 
ATOM   1977 O  O   . ASP A 1 269 ? -109.563 30.632  305.326 1.00 36.52  ? 269 ASP A O   1 
ATOM   1978 C  CB  . ASP A 1 269 ? -108.838 27.860  306.918 1.00 29.28  ? 269 ASP A CB  1 
ATOM   1979 C  CG  . ASP A 1 269 ? -109.726 26.879  307.656 1.00 31.90  ? 269 ASP A CG  1 
ATOM   1980 O  OD1 . ASP A 1 269 ? -110.465 26.128  306.987 1.00 30.23  ? 269 ASP A OD1 1 
ATOM   1981 O  OD2 . ASP A 1 269 ? -109.686 26.861  308.904 1.00 31.41  ? 269 ASP A OD2 1 
ATOM   1982 N  N   . PRO A 1 270 ? -107.661 29.740  304.546 1.00 21.27  ? 270 PRO A N   1 
ATOM   1983 C  CA  . PRO A 1 270 ? -107.169 31.076  304.168 1.00 23.22  ? 270 PRO A CA  1 
ATOM   1984 C  C   . PRO A 1 270 ? -107.997 31.763  303.096 1.00 27.68  ? 270 PRO A C   1 
ATOM   1985 O  O   . PRO A 1 270 ? -107.851 32.978  302.912 1.00 31.44  ? 270 PRO A O   1 
ATOM   1986 C  CB  . PRO A 1 270 ? -105.742 30.800  303.675 1.00 21.12  ? 270 PRO A CB  1 
ATOM   1987 C  CG  . PRO A 1 270 ? -105.355 29.535  304.344 1.00 31.00  ? 270 PRO A CG  1 
ATOM   1988 C  CD  . PRO A 1 270 ? -106.610 28.721  304.371 1.00 32.68  ? 270 PRO A CD  1 
ATOM   1989 N  N   . PHE A 1 271 ? -108.855 31.033  302.379 1.00 24.87  ? 271 PHE A N   1 
ATOM   1990 C  CA  . PHE A 1 271 ? -109.696 31.665  301.367 1.00 20.78  ? 271 PHE A CA  1 
ATOM   1991 C  C   . PHE A 1 271 ? -110.673 32.651  301.992 1.00 21.76  ? 271 PHE A C   1 
ATOM   1992 O  O   . PHE A 1 271 ? -110.932 33.721  301.430 1.00 21.74  ? 271 PHE A O   1 
ATOM   1993 C  CB  . PHE A 1 271 ? -110.453 30.602  300.573 1.00 20.19  ? 271 PHE A CB  1 
ATOM   1994 C  CG  . PHE A 1 271 ? -109.628 29.922  299.522 1.00 19.86  ? 271 PHE A CG  1 
ATOM   1995 C  CD1 . PHE A 1 271 ? -108.822 30.659  298.672 1.00 19.93  ? 271 PHE A CD1 1 
ATOM   1996 C  CD2 . PHE A 1 271 ? -109.663 28.547  299.380 1.00 18.65  ? 271 PHE A CD2 1 
ATOM   1997 C  CE1 . PHE A 1 271 ? -108.064 30.035  297.700 1.00 18.23  ? 271 PHE A CE1 1 
ATOM   1998 C  CE2 . PHE A 1 271 ? -108.907 27.917  298.411 1.00 18.81  ? 271 PHE A CE2 1 
ATOM   1999 C  CZ  . PHE A 1 271 ? -108.107 28.662  297.570 1.00 17.16  ? 271 PHE A CZ  1 
ATOM   2000 N  N   . TYR A 1 272 ? -111.225 32.309  303.159 1.00 26.30  ? 272 TYR A N   1 
ATOM   2001 C  CA  . TYR A 1 272 ? -112.237 33.151  303.789 1.00 23.81  ? 272 TYR A CA  1 
ATOM   2002 C  C   . TYR A 1 272 ? -111.693 34.514  304.193 1.00 23.42  ? 272 TYR A C   1 
ATOM   2003 O  O   . TYR A 1 272 ? -112.479 35.447  304.390 1.00 22.01  ? 272 TYR A O   1 
ATOM   2004 C  CB  . TYR A 1 272 ? -112.819 32.443  305.015 1.00 31.72  ? 272 TYR A CB  1 
ATOM   2005 C  CG  . TYR A 1 272 ? -113.458 31.105  304.715 1.00 24.16  ? 272 TYR A CG  1 
ATOM   2006 C  CD1 . TYR A 1 272 ? -112.706 29.938  304.718 1.00 23.21  ? 272 TYR A CD1 1 
ATOM   2007 C  CD2 . TYR A 1 272 ? -114.814 31.008  304.435 1.00 26.85  ? 272 TYR A CD2 1 
ATOM   2008 C  CE1 . TYR A 1 272 ? -113.285 28.714  304.447 1.00 25.09  ? 272 TYR A CE1 1 
ATOM   2009 C  CE2 . TYR A 1 272 ? -115.402 29.788  304.163 1.00 25.65  ? 272 TYR A CE2 1 
ATOM   2010 C  CZ  . TYR A 1 272 ? -114.632 28.644  304.170 1.00 26.64  ? 272 TYR A CZ  1 
ATOM   2011 O  OH  . TYR A 1 272 ? -115.211 27.426  303.900 1.00 27.12  ? 272 TYR A OH  1 
ATOM   2012 N  N   . PHE A 1 273 ? -110.375 34.654  304.320 1.00 22.78  ? 273 PHE A N   1 
ATOM   2013 C  CA  . PHE A 1 273 ? -109.767 35.913  304.725 1.00 22.47  ? 273 PHE A CA  1 
ATOM   2014 C  C   . PHE A 1 273 ? -109.393 36.807  303.552 1.00 21.01  ? 273 PHE A C   1 
ATOM   2015 O  O   . PHE A 1 273 ? -108.972 37.947  303.775 1.00 23.15  ? 273 PHE A O   1 
ATOM   2016 C  CB  . PHE A 1 273 ? -108.515 35.652  305.567 1.00 22.13  ? 273 PHE A CB  1 
ATOM   2017 C  CG  . PHE A 1 273 ? -108.785 34.923  306.848 1.00 24.77  ? 273 PHE A CG  1 
ATOM   2018 C  CD1 . PHE A 1 273 ? -109.273 35.597  307.954 1.00 27.47  ? 273 PHE A CD1 1 
ATOM   2019 C  CD2 . PHE A 1 273 ? -108.543 33.564  306.950 1.00 24.51  ? 273 PHE A CD2 1 
ATOM   2020 C  CE1 . PHE A 1 273 ? -109.520 34.930  309.136 1.00 30.62  ? 273 PHE A CE1 1 
ATOM   2021 C  CE2 . PHE A 1 273 ? -108.787 32.891  308.130 1.00 25.76  ? 273 PHE A CE2 1 
ATOM   2022 C  CZ  . PHE A 1 273 ? -109.277 33.575  309.224 1.00 33.45  ? 273 PHE A CZ  1 
ATOM   2023 N  N   . MET A 1 274 ? -109.532 36.330  302.317 1.00 20.70  ? 274 MET A N   1 
ATOM   2024 C  CA  . MET A 1 274 ? -109.088 37.090  301.156 1.00 19.64  ? 274 MET A CA  1 
ATOM   2025 C  C   . MET A 1 274 ? -110.056 38.195  300.757 1.00 21.20  ? 274 MET A C   1 
ATOM   2026 O  O   . MET A 1 274 ? -109.912 38.766  299.671 1.00 23.77  ? 274 MET A O   1 
ATOM   2027 C  CB  . MET A 1 274 ? -108.837 36.149  299.978 1.00 18.99  ? 274 MET A CB  1 
ATOM   2028 C  CG  . MET A 1 274 ? -107.690 35.190  300.235 1.00 18.68  ? 274 MET A CG  1 
ATOM   2029 S  SD  . MET A 1 274 ? -107.110 34.333  298.765 1.00 13.28  ? 274 MET A SD  1 
ATOM   2030 C  CE  . MET A 1 274 ? -105.963 33.174  299.505 1.00 21.13  ? 274 MET A CE  1 
ATOM   2031 N  N   . HIS A 1 275 ? -111.039 38.507  301.602 1.00 21.90  ? 275 HIS A N   1 
ATOM   2032 C  CA  . HIS A 1 275 ? -111.792 39.740  301.428 1.00 22.90  ? 275 HIS A CA  1 
ATOM   2033 C  C   . HIS A 1 275 ? -110.948 40.958  301.776 1.00 28.33  ? 275 HIS A C   1 
ATOM   2034 O  O   . HIS A 1 275 ? -111.244 42.062  301.308 1.00 32.38  ? 275 HIS A O   1 
ATOM   2035 C  CB  . HIS A 1 275 ? -113.046 39.716  302.301 1.00 20.28  ? 275 HIS A CB  1 
ATOM   2036 C  CG  . HIS A 1 275 ? -112.757 39.534  303.758 1.00 22.07  ? 275 HIS A CG  1 
ATOM   2037 N  ND1 . HIS A 1 275 ? -112.452 38.308  304.309 1.00 32.63  ? 275 HIS A ND1 1 
ATOM   2038 C  CD2 . HIS A 1 275 ? -112.711 40.425  304.777 1.00 26.15  ? 275 HIS A CD2 1 
ATOM   2039 C  CE1 . HIS A 1 275 ? -112.238 38.451  305.604 1.00 25.81  ? 275 HIS A CE1 1 
ATOM   2040 N  NE2 . HIS A 1 275 ? -112.389 39.726  305.914 1.00 25.27  ? 275 HIS A NE2 1 
ATOM   2041 N  N   . ASP A 1 276 ? -109.900 40.772  302.576 1.00 35.16  ? 276 ASP A N   1 
ATOM   2042 C  CA  . ASP A 1 276 ? -109.097 41.869  303.089 1.00 36.98  ? 276 ASP A CA  1 
ATOM   2043 C  C   . ASP A 1 276 ? -108.223 42.450  301.976 1.00 38.63  ? 276 ASP A C   1 
ATOM   2044 O  O   . ASP A 1 276 ? -108.082 41.865  300.899 1.00 33.12  ? 276 ASP A O   1 
ATOM   2045 C  CB  . ASP A 1 276 ? -108.258 41.385  304.275 1.00 50.82  ? 276 ASP A CB  1 
ATOM   2046 C  CG  . ASP A 1 276 ? -107.591 42.520  305.028 1.00 65.15  ? 276 ASP A CG  1 
ATOM   2047 O  OD1 . ASP A 1 276 ? -107.863 43.690  304.705 1.00 64.96  ? 276 ASP A OD1 1 
ATOM   2048 O  OD2 . ASP A 1 276 ? -106.809 42.247  305.960 1.00 69.36  ? 276 ASP A OD2 1 
ATOM   2049 N  N   . VAL A 1 277 ? -107.624 43.615  302.271 1.00 49.38  ? 277 VAL A N   1 
ATOM   2050 C  CA  . VAL A 1 277 ? -106.924 44.505  301.338 1.00 71.35  ? 277 VAL A CA  1 
ATOM   2051 C  C   . VAL A 1 277 ? -106.594 43.852  299.998 1.00 48.38  ? 277 VAL A C   1 
ATOM   2052 O  O   . VAL A 1 277 ? -107.041 44.324  298.945 1.00 45.84  ? 277 VAL A O   1 
ATOM   2053 C  CB  . VAL A 1 277 ? -105.660 45.110  302.003 1.00 104.44 ? 277 VAL A CB  1 
ATOM   2054 C  CG1 . VAL A 1 277 ? -106.009 45.699  303.344 1.00 81.54  ? 277 VAL A CG1 1 
ATOM   2055 C  CG2 . VAL A 1 277 ? -104.546 44.085  302.226 1.00 69.28  ? 277 VAL A CG2 1 
ATOM   2056 N  N   . GLU A 1 278 ? -105.867 42.736  300.048 1.00 42.29  ? 278 GLU A N   1 
ATOM   2057 C  CA  . GLU A 1 278 ? -105.355 41.975  298.918 1.00 45.99  ? 278 GLU A CA  1 
ATOM   2058 C  C   . GLU A 1 278 ? -104.192 41.134  299.424 1.00 44.77  ? 278 GLU A C   1 
ATOM   2059 O  O   . GLU A 1 278 ? -103.125 41.088  298.802 1.00 41.77  ? 278 GLU A O   1 
ATOM   2060 C  CB  . GLU A 1 278 ? -104.909 42.857  297.747 1.00 52.23  ? 278 GLU A CB  1 
ATOM   2061 C  CG  . GLU A 1 278 ? -104.829 42.099  296.429 1.00 56.92  ? 278 GLU A CG  1 
ATOM   2062 C  CD  . GLU A 1 278 ? -105.519 42.792  295.273 1.00 94.04  ? 278 GLU A CD  1 
ATOM   2063 O  OE1 . GLU A 1 278 ? -105.572 44.039  295.265 1.00 106.36 ? 278 GLU A OE1 1 
ATOM   2064 O  OE2 . GLU A 1 278 ? -105.990 42.084  294.358 1.00 117.96 ? 278 GLU A OE2 1 
ATOM   2065 N  N   . LYS A 1 279 ? -104.379 40.486  300.578 1.00 35.10  ? 279 LYS A N   1 
ATOM   2066 C  CA  . LYS A 1 279 ? -103.640 39.258  300.833 1.00 31.60  ? 279 LYS A CA  1 
ATOM   2067 C  C   . LYS A 1 279 ? -103.837 38.296  299.676 1.00 33.59  ? 279 LYS A C   1 
ATOM   2068 O  O   . LYS A 1 279 ? -103.037 37.373  299.488 1.00 58.55  ? 279 LYS A O   1 
ATOM   2069 C  CB  . LYS A 1 279 ? -104.103 38.621  302.145 1.00 29.75  ? 279 LYS A CB  1 
ATOM   2070 C  CG  . LYS A 1 279 ? -104.415 39.619  303.248 1.00 32.72  ? 279 LYS A CG  1 
ATOM   2071 C  CD  . LYS A 1 279 ? -104.367 38.954  304.609 1.00 29.89  ? 279 LYS A CD  1 
ATOM   2072 C  CE  . LYS A 1 279 ? -105.396 39.545  305.550 1.00 32.76  ? 279 LYS A CE  1 
ATOM   2073 N  NZ  . LYS A 1 279 ? -105.388 38.902  306.890 1.00 28.62  ? 279 LYS A NZ  1 
ATOM   2074 N  N   . ARG A 1 280 ? -104.920 38.496  298.923 1.00 28.54  ? 280 ARG A N   1 
ATOM   2075 C  CA  . ARG A 1 280 ? -105.085 37.932  297.591 1.00 35.65  ? 280 ARG A CA  1 
ATOM   2076 C  C   . ARG A 1 280 ? -103.840 38.135  296.731 1.00 49.68  ? 280 ARG A C   1 
ATOM   2077 O  O   . ARG A 1 280 ? -103.396 37.211  296.045 1.00 43.30  ? 280 ARG A O   1 
ATOM   2078 C  CB  . ARG A 1 280 ? -106.310 38.584  296.950 1.00 33.73  ? 280 ARG A CB  1 
ATOM   2079 C  CG  . ARG A 1 280 ? -107.005 37.802  295.870 1.00 42.70  ? 280 ARG A CG  1 
ATOM   2080 C  CD  . ARG A 1 280 ? -108.487 38.146  295.902 1.00 31.84  ? 280 ARG A CD  1 
ATOM   2081 N  NE  . ARG A 1 280 ? -108.729 39.555  295.588 1.00 31.48  ? 280 ARG A NE  1 
ATOM   2082 C  CZ  . ARG A 1 280 ? -109.248 40.433  296.442 1.00 32.33  ? 280 ARG A CZ  1 
ATOM   2083 N  NH1 . ARG A 1 280 ? -109.585 40.052  297.668 1.00 28.63  ? 280 ARG A NH1 1 
ATOM   2084 N  NH2 . ARG A 1 280 ? -109.435 41.692  296.071 1.00 31.46  ? 280 ARG A NH2 1 
ATOM   2085 N  N   . ASN A 1 281 ? -103.266 39.345  296.736 1.00 42.22  ? 281 ASN A N   1 
ATOM   2086 C  CA  . ASN A 1 281 ? -102.017 39.553  296.001 1.00 46.14  ? 281 ASN A CA  1 
ATOM   2087 C  C   . ASN A 1 281 ? -100.886 38.739  296.611 1.00 36.12  ? 281 ASN A C   1 
ATOM   2088 O  O   . ASN A 1 281 ? -100.121 38.088  295.892 1.00 36.90  ? 281 ASN A O   1 
ATOM   2089 C  CB  . ASN A 1 281 ? -101.639 41.035  295.958 1.00 55.55  ? 281 ASN A CB  1 
ATOM   2090 C  CG  . ASN A 1 281 ? -101.991 41.684  294.635 1.00 71.44  ? 281 ASN A CG  1 
ATOM   2091 O  OD1 . ASN A 1 281 ? -102.048 41.018  293.602 1.00 107.89 ? 281 ASN A OD1 1 
ATOM   2092 N  ND2 . ASN A 1 281 ? -102.207 42.994  294.655 1.00 71.91  ? 281 ASN A ND2 1 
ATOM   2093 N  N   . VAL A 1 282 ? -100.764 38.766  297.941 1.00 31.70  ? 282 VAL A N   1 
ATOM   2094 C  CA  . VAL A 1 282 ? -99.856  37.850  298.624 1.00 30.09  ? 282 VAL A CA  1 
ATOM   2095 C  C   . VAL A 1 282 ? -100.125 36.422  298.175 1.00 45.51  ? 282 VAL A C   1 
ATOM   2096 O  O   . VAL A 1 282 ? -99.202  35.604  298.068 1.00 70.02  ? 282 VAL A O   1 
ATOM   2097 C  CB  . VAL A 1 282 ? -100.000 38.009  300.152 1.00 28.93  ? 282 VAL A CB  1 
ATOM   2098 C  CG1 . VAL A 1 282 ? -98.999  37.145  300.885 1.00 33.59  ? 282 VAL A CG1 1 
ATOM   2099 C  CG2 . VAL A 1 282 ? -99.852  39.473  300.550 1.00 32.99  ? 282 VAL A CG2 1 
ATOM   2100 N  N   . PHE A 1 283 ? -101.387 36.108  297.882 1.00 29.62  ? 283 PHE A N   1 
ATOM   2101 C  CA  . PHE A 1 283 ? -101.749 34.827  297.288 1.00 27.74  ? 283 PHE A CA  1 
ATOM   2102 C  C   . PHE A 1 283 ? -101.452 34.801  295.790 1.00 28.98  ? 283 PHE A C   1 
ATOM   2103 O  O   . PHE A 1 283 ? -100.693 33.951  295.315 1.00 33.15  ? 283 PHE A O   1 
ATOM   2104 C  CB  . PHE A 1 283 ? -103.229 34.540  297.558 1.00 26.19  ? 283 PHE A CB  1 
ATOM   2105 C  CG  . PHE A 1 283 ? -103.795 33.416  296.742 1.00 26.48  ? 283 PHE A CG  1 
ATOM   2106 C  CD1 . PHE A 1 283 ? -103.494 32.100  297.038 1.00 24.92  ? 283 PHE A CD1 1 
ATOM   2107 C  CD2 . PHE A 1 283 ? -104.640 33.683  295.678 1.00 26.31  ? 283 PHE A CD2 1 
ATOM   2108 C  CE1 . PHE A 1 283 ? -104.024 31.069  296.284 1.00 23.19  ? 283 PHE A CE1 1 
ATOM   2109 C  CE2 . PHE A 1 283 ? -105.170 32.658  294.922 1.00 24.28  ? 283 PHE A CE2 1 
ATOM   2110 C  CZ  . PHE A 1 283 ? -104.862 31.350  295.225 1.00 24.66  ? 283 PHE A CZ  1 
ATOM   2111 N  N   . VAL A 1 284 ? -102.031 35.740  295.035 1.00 29.47  ? 284 VAL A N   1 
ATOM   2112 C  CA  . VAL A 1 284 ? -101.939 35.696  293.574 1.00 28.27  ? 284 VAL A CA  1 
ATOM   2113 C  C   . VAL A 1 284 ? -100.492 35.839  293.116 1.00 30.52  ? 284 VAL A C   1 
ATOM   2114 O  O   . VAL A 1 284 ? -100.014 35.070  292.273 1.00 33.33  ? 284 VAL A O   1 
ATOM   2115 C  CB  . VAL A 1 284 ? -102.838 36.774  292.941 1.00 28.45  ? 284 VAL A CB  1 
ATOM   2116 C  CG1 . VAL A 1 284 ? -102.588 36.858  291.447 1.00 28.75  ? 284 VAL A CG1 1 
ATOM   2117 C  CG2 . VAL A 1 284 ? -104.304 36.469  293.205 1.00 27.60  ? 284 VAL A CG2 1 
ATOM   2118 N  N   . ASP A 1 285 ? -99.775  36.833  293.651 1.00 33.12  ? 285 ASP A N   1 
ATOM   2119 C  CA  . ASP A 1 285 ? -98.378  37.011  293.261 1.00 32.34  ? 285 ASP A CA  1 
ATOM   2120 C  C   . ASP A 1 285 ? -97.547  35.782  293.599 1.00 32.04  ? 285 ASP A C   1 
ATOM   2121 O  O   . ASP A 1 285 ? -96.578  35.475  292.895 1.00 54.02  ? 285 ASP A O   1 
ATOM   2122 C  CB  . ASP A 1 285 ? -97.786  38.251  293.931 1.00 37.17  ? 285 ASP A CB  1 
ATOM   2123 C  CG  . ASP A 1 285 ? -98.554  39.514  293.600 1.00 43.45  ? 285 ASP A CG  1 
ATOM   2124 O  OD1 . ASP A 1 285 ? -99.610  39.413  292.942 1.00 43.51  ? 285 ASP A OD1 1 
ATOM   2125 O  OD2 . ASP A 1 285 ? -98.100  40.608  293.996 1.00 72.47  ? 285 ASP A OD2 1 
ATOM   2126 N  N   . SER A 1 286 ? -97.908  35.067  294.666 1.00 28.06  ? 286 SER A N   1 
ATOM   2127 C  CA  . SER A 1 286 ? -97.246  33.800  294.952 1.00 30.54  ? 286 SER A CA  1 
ATOM   2128 C  C   . SER A 1 286 ? -97.668  32.728  293.956 1.00 26.61  ? 286 SER A C   1 
ATOM   2129 O  O   . SER A 1 286 ? -96.852  31.889  293.558 1.00 26.80  ? 286 SER A O   1 
ATOM   2130 C  CB  . SER A 1 286 ? -97.548  33.359  296.384 1.00 30.46  ? 286 SER A CB  1 
ATOM   2131 O  OG  . SER A 1 286 ? -98.933  33.130  296.565 1.00 28.31  ? 286 SER A OG  1 
ATOM   2132 N  N   . VAL A 1 287 ? -98.938  32.741  293.540 1.00 26.71  ? 287 VAL A N   1 
ATOM   2133 C  CA  . VAL A 1 287 ? -99.387  31.818  292.501 1.00 26.16  ? 287 VAL A CA  1 
ATOM   2134 C  C   . VAL A 1 287 ? -98.656  32.093  291.195 1.00 26.24  ? 287 VAL A C   1 
ATOM   2135 O  O   . VAL A 1 287 ? -98.298  31.166  290.459 1.00 49.78  ? 287 VAL A O   1 
ATOM   2136 C  CB  . VAL A 1 287 ? -100.915 31.907  292.320 1.00 23.48  ? 287 VAL A CB  1 
ATOM   2137 C  CG1 . VAL A 1 287 ? -101.371 30.995  291.194 1.00 18.63  ? 287 VAL A CG1 1 
ATOM   2138 C  CG2 . VAL A 1 287 ? -101.628 31.532  293.603 1.00 23.31  ? 287 VAL A CG2 1 
ATOM   2139 N  N   . LYS A 1 288 ? -98.412  33.370  290.890 1.00 25.86  ? 288 LYS A N   1 
ATOM   2140 C  CA  . LYS A 1 288 ? -97.760  33.703  289.628 1.00 26.82  ? 288 LYS A CA  1 
ATOM   2141 C  C   . LYS A 1 288 ? -96.298  33.276  289.621 1.00 29.19  ? 288 LYS A C   1 
ATOM   2142 O  O   . LYS A 1 288 ? -95.765  32.925  288.563 1.00 35.60  ? 288 LYS A O   1 
ATOM   2143 C  CB  . LYS A 1 288 ? -97.892  35.201  289.341 1.00 34.70  ? 288 LYS A CB  1 
ATOM   2144 C  CG  . LYS A 1 288 ? -96.595  35.990  289.411 1.00 41.52  ? 288 LYS A CG  1 
ATOM   2145 C  CD  . LYS A 1 288 ? -96.729  37.318  288.683 1.00 64.84  ? 288 LYS A CD  1 
ATOM   2146 C  CE  . LYS A 1 288 ? -95.369  37.905  288.344 1.00 93.63  ? 288 LYS A CE  1 
ATOM   2147 N  NZ  . LYS A 1 288 ? -95.485  39.087  287.446 1.00 93.11  ? 288 LYS A NZ  1 
ATOM   2148 N  N   . GLU A 1 289 ? -95.637  33.288  290.781 1.00 28.64  ? 289 GLU A N   1 
ATOM   2149 C  CA  . GLU A 1 289 ? -94.279  32.764  290.850 1.00 28.67  ? 289 GLU A CA  1 
ATOM   2150 C  C   . GLU A 1 289 ? -94.270  31.247  290.969 1.00 24.53  ? 289 GLU A C   1 
ATOM   2151 O  O   . GLU A 1 289 ? -93.369  30.593  290.435 1.00 24.30  ? 289 GLU A O   1 
ATOM   2152 C  CB  . GLU A 1 289 ? -93.519  33.394  292.020 1.00 38.75  ? 289 GLU A CB  1 
ATOM   2153 C  CG  . GLU A 1 289 ? -92.093  32.875  292.174 1.00 49.80  ? 289 GLU A CG  1 
ATOM   2154 C  CD  . GLU A 1 289 ? -91.116  33.948  292.611 1.00 46.53  ? 289 GLU A CD  1 
ATOM   2155 O  OE1 . GLU A 1 289 ? -91.404  34.652  293.600 1.00 70.23  ? 289 GLU A OE1 1 
ATOM   2156 O  OE2 . GLU A 1 289 ? -90.055  34.084  291.964 1.00 44.36  ? 289 GLU A OE2 1 
ATOM   2157 N  N   . PHE A 1 290 ? -95.268  30.676  291.648 1.00 23.10  ? 290 PHE A N   1 
ATOM   2158 C  CA  . PHE A 1 290 ? -95.372  29.225  291.745 1.00 24.42  ? 290 PHE A CA  1 
ATOM   2159 C  C   . PHE A 1 290 ? -95.477  28.575  290.372 1.00 24.59  ? 290 PHE A C   1 
ATOM   2160 O  O   . PHE A 1 290 ? -94.992  27.456  290.176 1.00 38.76  ? 290 PHE A O   1 
ATOM   2161 C  CB  . PHE A 1 290 ? -96.580  28.851  292.606 1.00 23.46  ? 290 PHE A CB  1 
ATOM   2162 C  CG  . PHE A 1 290 ? -96.611  27.409  293.024 1.00 23.79  ? 290 PHE A CG  1 
ATOM   2163 C  CD1 . PHE A 1 290 ? -97.189  26.449  292.210 1.00 24.58  ? 290 PHE A CD1 1 
ATOM   2164 C  CD2 . PHE A 1 290 ? -96.071  27.015  294.236 1.00 24.30  ? 290 PHE A CD2 1 
ATOM   2165 C  CE1 . PHE A 1 290 ? -97.221  25.124  292.594 1.00 21.90  ? 290 PHE A CE1 1 
ATOM   2166 C  CE2 . PHE A 1 290 ? -96.101  25.691  294.625 1.00 23.76  ? 290 PHE A CE2 1 
ATOM   2167 C  CZ  . PHE A 1 290 ? -96.676  24.744  293.803 1.00 23.35  ? 290 PHE A CZ  1 
ATOM   2168 N  N   . LEU A 1 291 ? -96.096  29.259  289.410 1.00 21.44  ? 291 LEU A N   1 
ATOM   2169 C  CA  . LEU A 1 291 ? -96.300  28.691  288.085 1.00 21.60  ? 291 LEU A CA  1 
ATOM   2170 C  C   . LEU A 1 291 ? -95.122  28.909  287.147 1.00 21.51  ? 291 LEU A C   1 
ATOM   2171 O  O   . LEU A 1 291 ? -94.977  28.157  286.177 1.00 28.63  ? 291 LEU A O   1 
ATOM   2172 C  CB  . LEU A 1 291 ? -97.567  29.269  287.452 1.00 22.69  ? 291 LEU A CB  1 
ATOM   2173 C  CG  . LEU A 1 291 ? -98.868  28.893  288.162 1.00 20.22  ? 291 LEU A CG  1 
ATOM   2174 C  CD1 . LEU A 1 291 ? -100.061 29.406  287.382 1.00 21.93  ? 291 LEU A CD1 1 
ATOM   2175 C  CD2 . LEU A 1 291 ? -98.958  27.388  288.366 1.00 19.35  ? 291 LEU A CD2 1 
ATOM   2176 N  N   . GLN A 1 292 ? -94.286  29.917  287.396 1.00 23.53  ? 292 GLN A N   1 
ATOM   2177 C  CA  . GLN A 1 292 ? -93.063  30.076  286.620 1.00 24.40  ? 292 GLN A CA  1 
ATOM   2178 C  C   . GLN A 1 292 ? -91.863  29.414  287.279 1.00 18.62  ? 292 GLN A C   1 
ATOM   2179 O  O   . GLN A 1 292 ? -90.881  29.117  286.590 1.00 19.31  ? 292 GLN A O   1 
ATOM   2180 C  CB  . GLN A 1 292 ? -92.767  31.559  286.372 1.00 29.32  ? 292 GLN A CB  1 
ATOM   2181 C  CG  . GLN A 1 292 ? -92.759  32.424  287.613 1.00 41.22  ? 292 GLN A CG  1 
ATOM   2182 C  CD  . GLN A 1 292 ? -92.976  33.890  287.293 1.00 30.10  ? 292 GLN A CD  1 
ATOM   2183 O  OE1 . GLN A 1 292 ? -93.089  34.272  286.128 1.00 25.39  ? 292 GLN A OE1 1 
ATOM   2184 N  NE2 . GLN A 1 292 ? -93.039  34.720  288.328 1.00 41.98  ? 292 GLN A NE2 1 
ATOM   2185 N  N   . VAL A 1 293 ? -91.916  29.180  288.591 1.00 18.97  ? 293 VAL A N   1 
ATOM   2186 C  CA  . VAL A 1 293 ? -90.928  28.312  289.224 1.00 21.29  ? 293 VAL A CA  1 
ATOM   2187 C  C   . VAL A 1 293 ? -91.161  26.867  288.805 1.00 20.52  ? 293 VAL A C   1 
ATOM   2188 O  O   . VAL A 1 293 ? -90.244  26.183  288.337 1.00 24.29  ? 293 VAL A O   1 
ATOM   2189 C  CB  . VAL A 1 293 ? -90.969  28.471  290.754 1.00 20.66  ? 293 VAL A CB  1 
ATOM   2190 C  CG1 . VAL A 1 293 ? -90.256  27.309  291.426 1.00 19.37  ? 293 VAL A CG1 1 
ATOM   2191 C  CG2 . VAL A 1 293 ? -90.338  29.790  291.165 1.00 24.53  ? 293 VAL A CG2 1 
ATOM   2192 N  N   . TRP A 1 294 ? -92.394  26.388  288.954 1.00 19.42  ? 294 TRP A N   1 
ATOM   2193 C  CA  . TRP A 1 294 ? -92.787  25.048  288.527 1.00 19.55  ? 294 TRP A CA  1 
ATOM   2194 C  C   . TRP A 1 294 ? -93.524  25.189  287.200 1.00 16.55  ? 294 TRP A C   1 
ATOM   2195 O  O   . TRP A 1 294 ? -94.721  25.485  287.171 1.00 17.93  ? 294 TRP A O   1 
ATOM   2196 C  CB  . TRP A 1 294 ? -93.656  24.373  289.582 1.00 18.67  ? 294 TRP A CB  1 
ATOM   2197 C  CG  . TRP A 1 294 ? -93.097  24.467  290.964 1.00 21.00  ? 294 TRP A CG  1 
ATOM   2198 C  CD1 . TRP A 1 294 ? -93.494  25.320  291.952 1.00 23.16  ? 294 TRP A CD1 1 
ATOM   2199 C  CD2 . TRP A 1 294 ? -92.034  23.682  291.515 1.00 19.87  ? 294 TRP A CD2 1 
ATOM   2200 N  NE1 . TRP A 1 294 ? -92.747  25.113  293.085 1.00 26.24  ? 294 TRP A NE1 1 
ATOM   2201 C  CE2 . TRP A 1 294 ? -91.842  24.113  292.843 1.00 20.21  ? 294 TRP A CE2 1 
ATOM   2202 C  CE3 . TRP A 1 294 ? -91.226  22.657  291.016 1.00 21.34  ? 294 TRP A CE3 1 
ATOM   2203 C  CZ2 . TRP A 1 294 ? -90.877  23.554  293.677 1.00 19.30  ? 294 TRP A CZ2 1 
ATOM   2204 C  CZ3 . TRP A 1 294 ? -90.268  22.104  291.846 1.00 21.66  ? 294 TRP A CZ3 1 
ATOM   2205 C  CH2 . TRP A 1 294 ? -90.102  22.553  293.161 1.00 21.08  ? 294 TRP A CH2 1 
ATOM   2206 N  N   . LYS A 1 295 ? -92.805  24.976  286.098 1.00 18.42  ? 295 LYS A N   1 
ATOM   2207 C  CA  . LYS A 1 295 ? -93.376  25.198  284.776 1.00 17.89  ? 295 LYS A CA  1 
ATOM   2208 C  C   . LYS A 1 295 ? -94.230  24.035  284.289 1.00 19.58  ? 295 LYS A C   1 
ATOM   2209 O  O   . LYS A 1 295 ? -95.014  24.216  283.351 1.00 21.42  ? 295 LYS A O   1 
ATOM   2210 C  CB  . LYS A 1 295 ? -92.263  25.476  283.764 1.00 18.33  ? 295 LYS A CB  1 
ATOM   2211 C  CG  . LYS A 1 295 ? -91.416  26.688  284.106 1.00 20.47  ? 295 LYS A CG  1 
ATOM   2212 C  CD  . LYS A 1 295 ? -90.259  26.852  283.137 1.00 24.69  ? 295 LYS A CD  1 
ATOM   2213 C  CE  . LYS A 1 295 ? -89.409  28.058  283.502 1.00 32.18  ? 295 LYS A CE  1 
ATOM   2214 N  NZ  . LYS A 1 295 ? -88.178  28.143  282.669 1.00 72.80  ? 295 LYS A NZ  1 
ATOM   2215 N  N   . PHE A 1 296 ? -94.106  22.854  284.898 1.00 19.52  ? 296 PHE A N   1 
ATOM   2216 C  CA  . PHE A 1 296 ? -94.878  21.703  284.445 1.00 21.19  ? 296 PHE A CA  1 
ATOM   2217 C  C   . PHE A 1 296 ? -96.366  21.829  284.745 1.00 20.78  ? 296 PHE A C   1 
ATOM   2218 O  O   . PHE A 1 296 ? -97.155  21.053  284.196 1.00 37.84  ? 296 PHE A O   1 
ATOM   2219 C  CB  . PHE A 1 296 ? -94.321  20.417  285.062 1.00 22.15  ? 296 PHE A CB  1 
ATOM   2220 C  CG  . PHE A 1 296 ? -94.383  20.381  286.562 1.00 22.40  ? 296 PHE A CG  1 
ATOM   2221 C  CD1 . PHE A 1 296 ? -93.342  20.887  287.321 1.00 22.12  ? 296 PHE A CD1 1 
ATOM   2222 C  CD2 . PHE A 1 296 ? -95.471  19.825  287.212 1.00 20.11  ? 296 PHE A CD2 1 
ATOM   2223 C  CE1 . PHE A 1 296 ? -93.392  20.852  288.700 1.00 19.54  ? 296 PHE A CE1 1 
ATOM   2224 C  CE2 . PHE A 1 296 ? -95.525  19.787  288.590 1.00 19.67  ? 296 PHE A CE2 1 
ATOM   2225 C  CZ  . PHE A 1 296 ? -94.485  20.302  289.334 1.00 17.50  ? 296 PHE A CZ  1 
ATOM   2226 N  N   . PHE A 1 297 ? -96.768  22.771  285.594 1.00 17.37  ? 297 PHE A N   1 
ATOM   2227 C  CA  . PHE A 1 297 ? -98.180  23.062  285.779 1.00 17.10  ? 297 PHE A CA  1 
ATOM   2228 C  C   . PHE A 1 297 ? -98.704  23.880  284.604 1.00 17.90  ? 297 PHE A C   1 
ATOM   2229 O  O   . PHE A 1 297 ? -97.959  24.617  283.952 1.00 19.82  ? 297 PHE A O   1 
ATOM   2230 C  CB  . PHE A 1 297 ? -98.414  23.816  287.087 1.00 16.28  ? 297 PHE A CB  1 
ATOM   2231 C  CG  . PHE A 1 297 ? -98.170  22.989  288.315 1.00 14.49  ? 297 PHE A CG  1 
ATOM   2232 C  CD1 . PHE A 1 297 ? -98.942  21.870  288.575 1.00 15.41  ? 297 PHE A CD1 1 
ATOM   2233 C  CD2 . PHE A 1 297 ? -97.177  23.334  289.215 1.00 16.93  ? 297 PHE A CD2 1 
ATOM   2234 C  CE1 . PHE A 1 297 ? -98.725  21.108  289.706 1.00 17.98  ? 297 PHE A CE1 1 
ATOM   2235 C  CE2 . PHE A 1 297 ? -96.955  22.575  290.347 1.00 17.90  ? 297 PHE A CE2 1 
ATOM   2236 C  CZ  . PHE A 1 297 ? -97.731  21.462  290.594 1.00 17.15  ? 297 PHE A CZ  1 
ATOM   2237 N  N   . ASP A 1 298 ? -100.004 23.745  284.336 1.00 18.29  ? 298 ASP A N   1 
ATOM   2238 C  CA  . ASP A 1 298 ? -100.621 24.386  283.181 1.00 22.14  ? 298 ASP A CA  1 
ATOM   2239 C  C   . ASP A 1 298 ? -101.758 25.325  283.569 1.00 23.47  ? 298 ASP A C   1 
ATOM   2240 O  O   . ASP A 1 298 ? -102.602 25.646  282.726 1.00 26.81  ? 298 ASP A O   1 
ATOM   2241 C  CB  . ASP A 1 298 ? -101.122 23.332  282.192 1.00 25.21  ? 298 ASP A CB  1 
ATOM   2242 C  CG  . ASP A 1 298 ? -100.010 22.436  281.686 1.00 31.23  ? 298 ASP A CG  1 
ATOM   2243 O  OD1 . ASP A 1 298 ? -99.168  22.919  280.900 1.00 38.95  ? 298 ASP A OD1 1 
ATOM   2244 O  OD2 . ASP A 1 298 ? -99.979  21.250  282.073 1.00 21.97  ? 298 ASP A OD2 1 
ATOM   2245 N  N   . GLY A 1 299 ? -101.803 25.775  284.814 1.00 24.71  ? 299 GLY A N   1 
ATOM   2246 C  CA  . GLY A 1 299 ? -102.842 26.716  285.204 1.00 23.52  ? 299 GLY A CA  1 
ATOM   2247 C  C   . GLY A 1 299 ? -103.007 26.759  286.715 1.00 19.30  ? 299 GLY A C   1 
ATOM   2248 O  O   . GLY A 1 299 ? -102.047 26.571  287.461 1.00 20.83  ? 299 GLY A O   1 
ATOM   2249 N  N   . VAL A 1 300 ? -104.240 27.041  287.136 1.00 15.66  ? 300 VAL A N   1 
ATOM   2250 C  CA  . VAL A 1 300 ? -104.603 27.125  288.548 1.00 15.03  ? 300 VAL A CA  1 
ATOM   2251 C  C   . VAL A 1 300 ? -105.941 26.429  288.748 1.00 21.15  ? 300 VAL A C   1 
ATOM   2252 O  O   . VAL A 1 300 ? -106.827 26.504  287.890 1.00 22.64  ? 300 VAL A O   1 
ATOM   2253 C  CB  . VAL A 1 300 ? -104.689 28.586  289.046 1.00 14.91  ? 300 VAL A CB  1 
ATOM   2254 C  CG1 . VAL A 1 300 ? -104.796 28.627  290.562 1.00 16.10  ? 300 VAL A CG1 1 
ATOM   2255 C  CG2 . VAL A 1 300 ? -103.496 29.401  288.581 1.00 17.98  ? 300 VAL A CG2 1 
ATOM   2256 N  N   . ASP A 1 301 ? -106.089 25.753  289.886 1.00 21.59  ? 301 ASP A N   1 
ATOM   2257 C  CA  . ASP A 1 301 ? -107.358 25.162  290.295 1.00 21.87  ? 301 ASP A CA  1 
ATOM   2258 C  C   . ASP A 1 301 ? -107.686 25.656  291.695 1.00 21.62  ? 301 ASP A C   1 
ATOM   2259 O  O   . ASP A 1 301 ? -106.919 25.418  292.634 1.00 26.50  ? 301 ASP A O   1 
ATOM   2260 C  CB  . ASP A 1 301 ? -107.300 23.633  290.263 1.00 22.28  ? 301 ASP A CB  1 
ATOM   2261 C  CG  . ASP A 1 301 ? -108.634 22.995  290.597 1.00 24.98  ? 301 ASP A CG  1 
ATOM   2262 O  OD1 . ASP A 1 301 ? -109.677 23.552  290.195 1.00 21.89  ? 301 ASP A OD1 1 
ATOM   2263 O  OD2 . ASP A 1 301 ? -108.640 21.936  291.260 1.00 25.44  ? 301 ASP A OD2 1 
ATOM   2264 N  N   . VAL A 1 302 ? -108.816 26.340  291.834 1.00 20.96  ? 302 VAL A N   1 
ATOM   2265 C  CA  . VAL A 1 302 ? -109.230 26.937  293.098 1.00 18.39  ? 302 VAL A CA  1 
ATOM   2266 C  C   . VAL A 1 302 ? -110.264 26.017  293.733 1.00 17.10  ? 302 VAL A C   1 
ATOM   2267 O  O   . VAL A 1 302 ? -111.381 25.877  293.227 1.00 17.30  ? 302 VAL A O   1 
ATOM   2268 C  CB  . VAL A 1 302 ? -109.792 28.350  292.898 1.00 21.01  ? 302 VAL A CB  1 
ATOM   2269 C  CG1 . VAL A 1 302 ? -110.170 28.964  294.237 1.00 18.63  ? 302 VAL A CG1 1 
ATOM   2270 C  CG2 . VAL A 1 302 ? -108.783 29.218  292.170 1.00 22.43  ? 302 VAL A CG2 1 
ATOM   2271 N  N   . ASP A 1 303 ? -109.901 25.398  294.851 1.00 15.69  ? 303 ASP A N   1 
ATOM   2272 C  CA  . ASP A 1 303 ? -110.775 24.466  295.550 1.00 15.22  ? 303 ASP A CA  1 
ATOM   2273 C  C   . ASP A 1 303 ? -111.190 25.069  296.889 1.00 16.31  ? 303 ASP A C   1 
ATOM   2274 O  O   . ASP A 1 303 ? -110.827 24.581  297.961 1.00 22.88  ? 303 ASP A O   1 
ATOM   2275 C  CB  . ASP A 1 303 ? -110.070 23.120  295.733 1.00 16.59  ? 303 ASP A CB  1 
ATOM   2276 C  CG  . ASP A 1 303 ? -109.634 22.510  294.417 1.00 18.68  ? 303 ASP A CG  1 
ATOM   2277 O  OD1 . ASP A 1 303 ? -110.362 21.647  293.887 1.00 20.27  ? 303 ASP A OD1 1 
ATOM   2278 O  OD2 . ASP A 1 303 ? -108.563 22.900  293.908 1.00 27.97  ? 303 ASP A OD2 1 
ATOM   2279 N  N   . TRP A 1 304 ? -111.965 26.149  296.819 1.00 17.36  ? 304 TRP A N   1 
ATOM   2280 C  CA  . TRP A 1 304 ? -112.485 26.786  298.022 1.00 19.04  ? 304 TRP A CA  1 
ATOM   2281 C  C   . TRP A 1 304 ? -113.665 25.974  298.540 1.00 19.73  ? 304 TRP A C   1 
ATOM   2282 O  O   . TRP A 1 304 ? -114.683 25.838  297.852 1.00 19.35  ? 304 TRP A O   1 
ATOM   2283 C  CB  . TRP A 1 304 ? -112.899 28.228  297.737 1.00 18.13  ? 304 TRP A CB  1 
ATOM   2284 C  CG  . TRP A 1 304 ? -113.278 29.015  298.967 1.00 19.88  ? 304 TRP A CG  1 
ATOM   2285 C  CD1 . TRP A 1 304 ? -113.353 28.552  300.251 1.00 21.80  ? 304 TRP A CD1 1 
ATOM   2286 C  CD2 . TRP A 1 304 ? -113.627 30.403  299.024 1.00 23.70  ? 304 TRP A CD2 1 
ATOM   2287 N  NE1 . TRP A 1 304 ? -113.730 29.563  301.099 1.00 23.00  ? 304 TRP A NE1 1 
ATOM   2288 C  CE2 . TRP A 1 304 ? -113.904 30.710  300.371 1.00 24.06  ? 304 TRP A CE2 1 
ATOM   2289 C  CE3 . TRP A 1 304 ? -113.733 31.417  298.067 1.00 24.74  ? 304 TRP A CE3 1 
ATOM   2290 C  CZ2 . TRP A 1 304 ? -114.278 31.986  300.784 1.00 25.12  ? 304 TRP A CZ2 1 
ATOM   2291 C  CZ3 . TRP A 1 304 ? -114.106 32.683  298.479 1.00 23.75  ? 304 TRP A CZ3 1 
ATOM   2292 C  CH2 . TRP A 1 304 ? -114.373 32.956  299.825 1.00 25.92  ? 304 TRP A CH2 1 
ATOM   2293 N  N   . GLU A 1 305 ? -113.529 25.439  299.748 1.00 20.14  ? 305 GLU A N   1 
ATOM   2294 C  CA  . GLU A 1 305 ? -114.567 24.606  300.341 1.00 24.27  ? 305 GLU A CA  1 
ATOM   2295 C  C   . GLU A 1 305 ? -114.958 25.101  301.731 1.00 28.11  ? 305 GLU A C   1 
ATOM   2296 O  O   . GLU A 1 305 ? -114.290 24.776  302.712 1.00 27.65  ? 305 GLU A O   1 
ATOM   2297 C  CB  . GLU A 1 305 ? -114.100 23.151  300.429 1.00 22.15  ? 305 GLU A CB  1 
ATOM   2298 C  CG  . GLU A 1 305 ? -113.775 22.510  299.091 1.00 25.11  ? 305 GLU A CG  1 
ATOM   2299 C  CD  . GLU A 1 305 ? -113.351 21.061  299.232 1.00 21.98  ? 305 GLU A CD  1 
ATOM   2300 O  OE1 . GLU A 1 305 ? -113.596 20.471  300.305 1.00 21.99  ? 305 GLU A OE1 1 
ATOM   2301 O  OE2 . GLU A 1 305 ? -112.771 20.513  298.271 1.00 37.37  ? 305 GLU A OE2 1 
ATOM   2302 N  N   . PHE A 1 306 ? -116.031 25.883  301.825 1.00 26.20  ? 306 PHE A N   1 
ATOM   2303 C  CA  . PHE A 1 306 ? -116.810 26.333  300.674 1.00 26.66  ? 306 PHE A CA  1 
ATOM   2304 C  C   . PHE A 1 306 ? -117.106 27.823  300.827 1.00 30.36  ? 306 PHE A C   1 
ATOM   2305 O  O   . PHE A 1 306 ? -117.111 28.339  301.944 1.00 45.34  ? 306 PHE A O   1 
ATOM   2306 C  CB  . PHE A 1 306 ? -118.119 25.543  300.549 1.00 28.97  ? 306 PHE A CB  1 
ATOM   2307 C  CG  . PHE A 1 306 ? -117.932 24.054  300.511 1.00 25.06  ? 306 PHE A CG  1 
ATOM   2308 C  CD1 . PHE A 1 306 ? -117.698 23.404  299.311 1.00 20.68  ? 306 PHE A CD1 1 
ATOM   2309 C  CD2 . PHE A 1 306 ? -117.999 23.304  301.672 1.00 27.13  ? 306 PHE A CD2 1 
ATOM   2310 C  CE1 . PHE A 1 306 ? -117.525 22.035  299.272 1.00 24.00  ? 306 PHE A CE1 1 
ATOM   2311 C  CE2 . PHE A 1 306 ? -117.829 21.934  301.639 1.00 26.78  ? 306 PHE A CE2 1 
ATOM   2312 C  CZ  . PHE A 1 306 ? -117.593 21.299  300.437 1.00 28.20  ? 306 PHE A CZ  1 
ATOM   2313 N  N   . PRO A 1 307 ? -117.351 28.521  299.713 1.00 28.05  ? 307 PRO A N   1 
ATOM   2314 C  CA  . PRO A 1 307 ? -117.716 29.941  299.812 1.00 26.32  ? 307 PRO A CA  1 
ATOM   2315 C  C   . PRO A 1 307 ? -119.042 30.138  300.527 1.00 29.39  ? 307 PRO A C   1 
ATOM   2316 O  O   . PRO A 1 307 ? -120.107 29.863  299.966 1.00 35.14  ? 307 PRO A O   1 
ATOM   2317 C  CB  . PRO A 1 307 ? -117.789 30.396  298.348 1.00 22.18  ? 307 PRO A CB  1 
ATOM   2318 C  CG  . PRO A 1 307 ? -117.059 29.352  297.569 1.00 24.54  ? 307 PRO A CG  1 
ATOM   2319 C  CD  . PRO A 1 307 ? -117.243 28.073  298.315 1.00 28.91  ? 307 PRO A CD  1 
ATOM   2320 N  N   . GLY A 1 308 ? -118.986 30.608  301.771 1.00 27.75  ? 308 GLY A N   1 
ATOM   2321 C  CA  . GLY A 1 308 ? -120.183 30.810  302.561 1.00 31.27  ? 308 GLY A CA  1 
ATOM   2322 C  C   . GLY A 1 308 ? -120.239 29.914  303.780 1.00 34.26  ? 308 GLY A C   1 
ATOM   2323 O  O   . GLY A 1 308 ? -121.300 29.744  304.389 1.00 35.05  ? 308 GLY A O   1 
ATOM   2324 N  N   . GLY A 1 309 ? -119.099 29.331  304.143 1.00 40.47  ? 309 GLY A N   1 
ATOM   2325 C  CA  . GLY A 1 309 ? -119.025 28.453  305.295 1.00 40.27  ? 309 GLY A CA  1 
ATOM   2326 C  C   . GLY A 1 309 ? -118.980 26.986  304.921 1.00 41.45  ? 309 GLY A C   1 
ATOM   2327 O  O   . GLY A 1 309 ? -118.353 26.612  303.926 1.00 69.70  ? 309 GLY A O   1 
ATOM   2328 N  N   . LYS A 1 310 ? -119.641 26.146  305.724 1.00 42.36  ? 310 LYS A N   1 
ATOM   2329 C  CA  . LYS A 1 310 ? -119.802 24.714  305.471 1.00 43.49  ? 310 LYS A CA  1 
ATOM   2330 C  C   . LYS A 1 310 ? -118.478 23.957  305.417 1.00 43.12  ? 310 LYS A C   1 
ATOM   2331 O  O   . LYS A 1 310 ? -118.471 22.732  305.262 1.00 39.38  ? 310 LYS A O   1 
ATOM   2332 C  CB  . LYS A 1 310 ? -120.563 24.472  304.163 1.00 45.95  ? 310 LYS A CB  1 
ATOM   2333 C  CG  . LYS A 1 310 ? -121.587 25.532  303.802 1.00 64.70  ? 310 LYS A CG  1 
ATOM   2334 C  CD  . LYS A 1 310 ? -121.762 25.582  302.302 1.00 72.37  ? 310 LYS A CD  1 
ATOM   2335 C  CE  . LYS A 1 310 ? -122.097 26.976  301.814 1.00 62.87  ? 310 LYS A CE  1 
ATOM   2336 N  NZ  . LYS A 1 310 ? -120.856 27.764  301.591 1.00 41.83  ? 310 LYS A NZ  1 
ATOM   2337 N  N   . GLY A 1 311 ? -117.359 24.661  305.544 1.00 67.68  ? 311 GLY A N   1 
ATOM   2338 C  CA  . GLY A 1 311 ? -116.061 24.046  305.388 1.00 64.08  ? 311 GLY A CA  1 
ATOM   2339 C  C   . GLY A 1 311 ? -115.690 23.170  306.572 1.00 34.97  ? 311 GLY A C   1 
ATOM   2340 O  O   . GLY A 1 311 ? -116.500 22.841  307.439 1.00 35.41  ? 311 GLY A O   1 
ATOM   2341 N  N   . ALA A 1 312 ? -114.413 22.781  306.591 1.00 35.11  ? 312 ALA A N   1 
ATOM   2342 C  CA  . ALA A 1 312 ? -113.903 21.995  307.708 1.00 35.72  ? 312 ALA A CA  1 
ATOM   2343 C  C   . ALA A 1 312 ? -113.923 22.794  309.002 1.00 34.95  ? 312 ALA A C   1 
ATOM   2344 O  O   . ALA A 1 312 ? -114.071 22.219  310.086 1.00 33.33  ? 312 ALA A O   1 
ATOM   2345 C  CB  . ALA A 1 312 ? -112.488 21.502  307.406 1.00 35.00  ? 312 ALA A CB  1 
ATOM   2346 N  N   . ASN A 1 313 ? -113.779 24.115  308.909 1.00 31.10  ? 313 ASN A N   1 
ATOM   2347 C  CA  . ASN A 1 313 ? -113.860 24.981  310.073 1.00 31.57  ? 313 ASN A CA  1 
ATOM   2348 C  C   . ASN A 1 313 ? -115.248 25.597  310.126 1.00 31.52  ? 313 ASN A C   1 
ATOM   2349 O  O   . ASN A 1 313 ? -115.566 26.453  309.287 1.00 38.30  ? 313 ASN A O   1 
ATOM   2350 C  CB  . ASN A 1 313 ? -112.794 26.072  310.009 1.00 31.72  ? 313 ASN A CB  1 
ATOM   2351 C  CG  . ASN A 1 313 ? -112.579 26.757  311.342 1.00 30.50  ? 313 ASN A CG  1 
ATOM   2352 O  OD1 . ASN A 1 313 ? -113.374 26.602  312.269 1.00 37.26  ? 313 ASN A OD1 1 
ATOM   2353 N  ND2 . ASN A 1 313 ? -111.500 27.522  311.445 1.00 32.07  ? 313 ASN A ND2 1 
ATOM   2354 N  N   . PRO A 1 314 ? -116.106 25.202  311.072 1.00 30.91  ? 314 PRO A N   1 
ATOM   2355 C  CA  . PRO A 1 314 ? -117.457 25.781  311.130 1.00 33.20  ? 314 PRO A CA  1 
ATOM   2356 C  C   . PRO A 1 314 ? -117.485 27.229  311.587 1.00 31.56  ? 314 PRO A C   1 
ATOM   2357 O  O   . PRO A 1 314 ? -118.526 27.882  311.435 1.00 37.88  ? 314 PRO A O   1 
ATOM   2358 C  CB  . PRO A 1 314 ? -118.182 24.873  312.131 1.00 31.31  ? 314 PRO A CB  1 
ATOM   2359 C  CG  . PRO A 1 314 ? -117.093 24.358  313.011 1.00 30.24  ? 314 PRO A CG  1 
ATOM   2360 C  CD  . PRO A 1 314 ? -115.888 24.194  312.124 1.00 31.57  ? 314 PRO A CD  1 
ATOM   2361 N  N   . SER A 1 315 ? -116.386 27.751  312.136 1.00 30.91  ? 315 SER A N   1 
ATOM   2362 C  CA  . SER A 1 315 ? -116.387 29.125  312.628 1.00 31.66  ? 315 SER A CA  1 
ATOM   2363 C  C   . SER A 1 315 ? -116.382 30.135  311.489 1.00 29.70  ? 315 SER A C   1 
ATOM   2364 O  O   . SER A 1 315 ? -116.841 31.269  311.667 1.00 31.00  ? 315 SER A O   1 
ATOM   2365 C  CB  . SER A 1 315 ? -115.184 29.356  313.541 1.00 31.46  ? 315 SER A CB  1 
ATOM   2366 O  OG  . SER A 1 315 ? -115.179 28.438  314.620 1.00 39.18  ? 315 SER A OG  1 
ATOM   2367 N  N   . LEU A 1 316 ? -115.877 29.750  310.322 1.00 34.82  ? 316 LEU A N   1 
ATOM   2368 C  CA  . LEU A 1 316 ? -115.770 30.656  309.190 1.00 31.14  ? 316 LEU A CA  1 
ATOM   2369 C  C   . LEU A 1 316 ? -117.023 30.595  308.328 1.00 29.38  ? 316 LEU A C   1 
ATOM   2370 O  O   . LEU A 1 316 ? -117.720 29.578  308.278 1.00 29.00  ? 316 LEU A O   1 
ATOM   2371 C  CB  . LEU A 1 316 ? -114.541 30.318  308.346 1.00 32.97  ? 316 LEU A CB  1 
ATOM   2372 C  CG  . LEU A 1 316 ? -113.244 30.095  309.125 1.00 33.48  ? 316 LEU A CG  1 
ATOM   2373 C  CD1 . LEU A 1 316 ? -112.144 29.583  308.209 1.00 44.72  ? 316 LEU A CD1 1 
ATOM   2374 C  CD2 . LEU A 1 316 ? -112.813 31.375  309.823 1.00 45.85  ? 316 LEU A CD2 1 
ATOM   2375 N  N   . GLY A 1 317 ? -117.303 31.701  307.644 1.00 29.14  ? 317 GLY A N   1 
ATOM   2376 C  CA  . GLY A 1 317 ? -118.440 31.760  306.749 1.00 29.96  ? 317 GLY A CA  1 
ATOM   2377 C  C   . GLY A 1 317 ? -119.150 33.097  306.736 1.00 31.44  ? 317 GLY A C   1 
ATOM   2378 O  O   . GLY A 1 317 ? -119.440 33.671  307.789 1.00 43.50  ? 317 GLY A O   1 
ATOM   2379 N  N   . ASP A 1 318 ? -119.429 33.603  305.538 1.00 29.94  ? 318 ASP A N   1 
ATOM   2380 C  CA  . ASP A 1 318 ? -120.224 34.818  305.379 1.00 30.59  ? 318 ASP A CA  1 
ATOM   2381 C  C   . ASP A 1 318 ? -120.856 34.762  303.999 1.00 31.04  ? 318 ASP A C   1 
ATOM   2382 O  O   . ASP A 1 318 ? -120.142 34.615  303.002 1.00 30.81  ? 318 ASP A O   1 
ATOM   2383 C  CB  . ASP A 1 318 ? -119.363 36.071  305.548 1.00 30.26  ? 318 ASP A CB  1 
ATOM   2384 C  CG  . ASP A 1 318 ? -120.193 37.333  305.694 1.00 30.80  ? 318 ASP A CG  1 
ATOM   2385 O  OD1 . ASP A 1 318 ? -121.429 37.221  305.823 1.00 37.44  ? 318 ASP A OD1 1 
ATOM   2386 O  OD2 . ASP A 1 318 ? -119.608 38.435  305.702 1.00 38.34  ? 318 ASP A OD2 1 
ATOM   2387 N  N   . ALA A 1 319 ? -122.185 34.873  303.946 1.00 30.64  ? 319 ALA A N   1 
ATOM   2388 C  CA  . ALA A 1 319 ? -122.926 34.569  302.724 1.00 31.94  ? 319 ALA A CA  1 
ATOM   2389 C  C   . ALA A 1 319 ? -122.449 35.417  301.550 1.00 34.43  ? 319 ALA A C   1 
ATOM   2390 O  O   . ALA A 1 319 ? -121.901 34.896  300.572 1.00 33.84  ? 319 ALA A O   1 
ATOM   2391 C  CB  . ALA A 1 319 ? -124.424 34.770  302.960 1.00 66.38  ? 319 ALA A CB  1 
ATOM   2392 N  N   . GLU A 1 320 ? -122.650 36.730  301.628 1.00 51.36  ? 320 GLU A N   1 
ATOM   2393 C  CA  . GLU A 1 320 ? -122.382 37.613  300.502 1.00 43.41  ? 320 GLU A CA  1 
ATOM   2394 C  C   . GLU A 1 320 ? -121.031 38.313  300.596 1.00 44.47  ? 320 GLU A C   1 
ATOM   2395 O  O   . GLU A 1 320 ? -120.736 39.176  299.764 1.00 65.92  ? 320 GLU A O   1 
ATOM   2396 C  CB  . GLU A 1 320 ? -123.511 38.634  300.358 1.00 48.94  ? 320 GLU A CB  1 
ATOM   2397 C  CG  . GLU A 1 320 ? -124.830 38.001  299.930 1.00 62.37  ? 320 GLU A CG  1 
ATOM   2398 C  CD  . GLU A 1 320 ? -125.964 39.000  299.827 1.00 65.65  ? 320 GLU A CD  1 
ATOM   2399 O  OE1 . GLU A 1 320 ? -125.779 40.160  300.249 1.00 55.55  ? 320 GLU A OE1 1 
ATOM   2400 O  OE2 . GLU A 1 320 ? -127.043 38.623  299.323 1.00 67.50  ? 320 GLU A OE2 1 
ATOM   2401 N  N   . ARG A 1 321 ? -120.204 37.965  301.584 1.00 36.07  ? 321 ARG A N   1 
ATOM   2402 C  CA  . ARG A 1 321 ? -118.797 38.346  301.516 1.00 28.75  ? 321 ARG A CA  1 
ATOM   2403 C  C   . ARG A 1 321 ? -118.015 37.360  300.660 1.00 36.33  ? 321 ARG A C   1 
ATOM   2404 O  O   . ARG A 1 321 ? -117.257 37.760  299.769 1.00 40.23  ? 321 ARG A O   1 
ATOM   2405 C  CB  . ARG A 1 321 ? -118.182 38.419  302.914 1.00 26.29  ? 321 ARG A CB  1 
ATOM   2406 C  CG  . ARG A 1 321 ? -116.934 39.287  302.971 1.00 26.15  ? 321 ARG A CG  1 
ATOM   2407 C  CD  . ARG A 1 321 ? -116.186 39.157  304.289 1.00 26.03  ? 321 ARG A CD  1 
ATOM   2408 N  NE  . ARG A 1 321 ? -117.047 38.752  305.395 1.00 42.63  ? 321 ARG A NE  1 
ATOM   2409 C  CZ  . ARG A 1 321 ? -116.602 38.481  306.617 1.00 34.79  ? 321 ARG A CZ  1 
ATOM   2410 N  NH1 . ARG A 1 321 ? -115.307 38.572  306.886 1.00 27.70  ? 321 ARG A NH1 1 
ATOM   2411 N  NH2 . ARG A 1 321 ? -117.448 38.118  307.570 1.00 32.86  ? 321 ARG A NH2 1 
ATOM   2412 N  N   . ASP A 1 322 ? -118.194 36.064  300.921 1.00 37.88  ? 322 ASP A N   1 
ATOM   2413 C  CA  . ASP A 1 322 ? -117.507 35.041  300.145 1.00 27.32  ? 322 ASP A CA  1 
ATOM   2414 C  C   . ASP A 1 322 ? -117.983 35.019  298.700 1.00 26.94  ? 322 ASP A C   1 
ATOM   2415 O  O   . ASP A 1 322 ? -117.195 34.725  297.796 1.00 24.12  ? 322 ASP A O   1 
ATOM   2416 C  CB  . ASP A 1 322 ? -117.716 33.673  300.791 1.00 29.70  ? 322 ASP A CB  1 
ATOM   2417 C  CG  . ASP A 1 322 ? -117.131 33.594  302.185 1.00 33.53  ? 322 ASP A CG  1 
ATOM   2418 O  OD1 . ASP A 1 322 ? -116.239 34.408  302.503 1.00 39.24  ? 322 ASP A OD1 1 
ATOM   2419 O  OD2 . ASP A 1 322 ? -117.566 32.721  302.965 1.00 34.70  ? 322 ASP A OD2 1 
ATOM   2420 N  N   . ALA A 1 323 ? -119.260 35.331  298.466 1.00 30.18  ? 323 ALA A N   1 
ATOM   2421 C  CA  . ALA A 1 323 ? -119.800 35.284  297.111 1.00 28.78  ? 323 ALA A CA  1 
ATOM   2422 C  C   . ALA A 1 323 ? -119.108 36.292  296.204 1.00 23.81  ? 323 ALA A C   1 
ATOM   2423 O  O   . ALA A 1 323 ? -118.905 36.029  295.013 1.00 18.45  ? 323 ALA A O   1 
ATOM   2424 C  CB  . ALA A 1 323 ? -121.307 35.533  297.138 1.00 34.74  ? 323 ALA A CB  1 
ATOM   2425 N  N   . LYS A 1 324 ? -118.742 37.454  296.745 1.00 26.31  ? 324 LYS A N   1 
ATOM   2426 C  CA  . LYS A 1 324 ? -118.010 38.447  295.970 1.00 25.18  ? 324 LYS A CA  1 
ATOM   2427 C  C   . LYS A 1 324 ? -116.508 38.194  295.996 1.00 22.22  ? 324 LYS A C   1 
ATOM   2428 O  O   . LYS A 1 324 ? -115.824 38.423  294.992 1.00 21.61  ? 324 LYS A O   1 
ATOM   2429 C  CB  . LYS A 1 324 ? -118.316 39.854  296.489 1.00 23.11  ? 324 LYS A CB  1 
ATOM   2430 C  CG  . LYS A 1 324 ? -117.718 40.965  295.644 1.00 20.66  ? 324 LYS A CG  1 
ATOM   2431 C  CD  . LYS A 1 324 ? -118.283 40.946  294.233 1.00 20.62  ? 324 LYS A CD  1 
ATOM   2432 C  CE  . LYS A 1 324 ? -117.489 41.851  293.305 1.00 23.44  ? 324 LYS A CE  1 
ATOM   2433 N  NZ  . LYS A 1 324 ? -117.368 43.233  293.843 1.00 34.85  ? 324 LYS A NZ  1 
ATOM   2434 N  N   . THR A 1 325 ? -115.982 37.723  297.130 1.00 23.51  ? 325 THR A N   1 
ATOM   2435 C  CA  . THR A 1 325 ? -114.570 37.363  297.198 1.00 24.56  ? 325 THR A CA  1 
ATOM   2436 C  C   . THR A 1 325 ? -114.247 36.236  296.225 1.00 26.60  ? 325 THR A C   1 
ATOM   2437 O  O   . THR A 1 325 ? -113.200 36.252  295.567 1.00 20.25  ? 325 THR A O   1 
ATOM   2438 C  CB  . THR A 1 325 ? -114.197 36.961  298.625 1.00 22.18  ? 325 THR A CB  1 
ATOM   2439 O  OG1 . THR A 1 325 ? -114.528 38.025  299.526 1.00 20.98  ? 325 THR A OG1 1 
ATOM   2440 C  CG2 . THR A 1 325 ? -112.709 36.667  298.727 1.00 19.26  ? 325 THR A CG2 1 
ATOM   2441 N  N   . TYR A 1 326 ? -115.142 35.250  296.118 1.00 21.82  ? 326 TYR A N   1 
ATOM   2442 C  CA  . TYR A 1 326 ? -114.950 34.167  295.160 1.00 19.22  ? 326 TYR A CA  1 
ATOM   2443 C  C   . TYR A 1 326 ? -114.917 34.685  293.729 1.00 19.56  ? 326 TYR A C   1 
ATOM   2444 O  O   . TYR A 1 326 ? -114.201 34.134  292.886 1.00 20.15  ? 326 TYR A O   1 
ATOM   2445 C  CB  . TYR A 1 326 ? -116.060 33.128  295.329 1.00 19.27  ? 326 TYR A CB  1 
ATOM   2446 C  CG  . TYR A 1 326 ? -115.895 31.877  294.498 1.00 20.67  ? 326 TYR A CG  1 
ATOM   2447 C  CD1 . TYR A 1 326 ? -115.110 30.823  294.942 1.00 16.62  ? 326 TYR A CD1 1 
ATOM   2448 C  CD2 . TYR A 1 326 ? -116.542 31.743  293.278 1.00 23.16  ? 326 TYR A CD2 1 
ATOM   2449 C  CE1 . TYR A 1 326 ? -114.965 29.675  294.188 1.00 16.41  ? 326 TYR A CE1 1 
ATOM   2450 C  CE2 . TYR A 1 326 ? -116.405 30.599  292.519 1.00 19.36  ? 326 TYR A CE2 1 
ATOM   2451 C  CZ  . TYR A 1 326 ? -115.615 29.569  292.977 1.00 17.37  ? 326 TYR A CZ  1 
ATOM   2452 O  OH  . TYR A 1 326 ? -115.475 28.429  292.221 1.00 20.23  ? 326 TYR A OH  1 
ATOM   2453 N  N   . ILE A 1 327 ? -115.676 35.742  293.437 1.00 20.59  ? 327 ILE A N   1 
ATOM   2454 C  CA  . ILE A 1 327 ? -115.658 36.326  292.101 1.00 19.45  ? 327 ILE A CA  1 
ATOM   2455 C  C   . ILE A 1 327 ? -114.383 37.128  291.885 1.00 21.90  ? 327 ILE A C   1 
ATOM   2456 O  O   . ILE A 1 327 ? -113.711 36.987  290.857 1.00 22.12  ? 327 ILE A O   1 
ATOM   2457 C  CB  . ILE A 1 327 ? -116.912 37.192  291.879 1.00 20.64  ? 327 ILE A CB  1 
ATOM   2458 C  CG1 . ILE A 1 327 ? -118.173 36.330  291.925 1.00 21.58  ? 327 ILE A CG1 1 
ATOM   2459 C  CG2 . ILE A 1 327 ? -116.820 37.928  290.552 1.00 21.92  ? 327 ILE A CG2 1 
ATOM   2460 C  CD1 . ILE A 1 327 ? -118.190 35.221  290.902 1.00 27.98  ? 327 ILE A CD1 1 
ATOM   2461 N  N   . LEU A 1 328 ? -114.030 37.979  292.852 1.00 23.97  ? 328 LEU A N   1 
ATOM   2462 C  CA  . LEU A 1 328 ? -112.822 38.788  292.723 1.00 26.64  ? 328 LEU A CA  1 
ATOM   2463 C  C   . LEU A 1 328 ? -111.571 37.925  292.648 1.00 31.93  ? 328 LEU A C   1 
ATOM   2464 O  O   . LEU A 1 328 ? -110.611 38.283  291.957 1.00 25.07  ? 328 LEU A O   1 
ATOM   2465 C  CB  . LEU A 1 328 ? -112.720 39.768  293.892 1.00 23.68  ? 328 LEU A CB  1 
ATOM   2466 C  CG  . LEU A 1 328 ? -113.775 40.873  293.958 1.00 26.11  ? 328 LEU A CG  1 
ATOM   2467 C  CD1 . LEU A 1 328 ? -113.619 41.687  295.232 1.00 27.76  ? 328 LEU A CD1 1 
ATOM   2468 C  CD2 . LEU A 1 328 ? -113.693 41.771  292.732 1.00 28.03  ? 328 LEU A CD2 1 
ATOM   2469 N  N   . LEU A 1 329 ? -111.562 36.789  293.350 1.00 46.11  ? 329 LEU A N   1 
ATOM   2470 C  CA  . LEU A 1 329 ? -110.409 35.896  293.312 1.00 26.66  ? 329 LEU A CA  1 
ATOM   2471 C  C   . LEU A 1 329 ? -110.201 35.326  291.914 1.00 23.78  ? 329 LEU A C   1 
ATOM   2472 O  O   . LEU A 1 329 ? -109.075 35.296  291.404 1.00 23.21  ? 329 LEU A O   1 
ATOM   2473 C  CB  . LEU A 1 329 ? -110.589 34.772  294.334 1.00 24.68  ? 329 LEU A CB  1 
ATOM   2474 C  CG  . LEU A 1 329 ? -109.406 33.836  294.581 1.00 22.27  ? 329 LEU A CG  1 
ATOM   2475 C  CD1 . LEU A 1 329 ? -108.163 34.619  294.945 1.00 21.68  ? 329 LEU A CD1 1 
ATOM   2476 C  CD2 . LEU A 1 329 ? -109.745 32.839  295.676 1.00 25.89  ? 329 LEU A CD2 1 
ATOM   2477 N  N   . LEU A 1 330 ? -111.281 34.873  291.275 1.00 22.91  ? 330 LEU A N   1 
ATOM   2478 C  CA  . LEU A 1 330 ? -111.157 34.283  289.946 1.00 23.60  ? 330 LEU A CA  1 
ATOM   2479 C  C   . LEU A 1 330 ? -110.844 35.340  288.895 1.00 26.83  ? 330 LEU A C   1 
ATOM   2480 O  O   . LEU A 1 330 ? -110.075 35.084  287.961 1.00 25.58  ? 330 LEU A O   1 
ATOM   2481 C  CB  . LEU A 1 330 ? -112.439 33.534  289.587 1.00 24.38  ? 330 LEU A CB  1 
ATOM   2482 C  CG  . LEU A 1 330 ? -112.836 32.396  290.526 1.00 26.28  ? 330 LEU A CG  1 
ATOM   2483 C  CD1 . LEU A 1 330 ? -114.159 31.792  290.090 1.00 26.91  ? 330 LEU A CD1 1 
ATOM   2484 C  CD2 . LEU A 1 330 ? -111.746 31.336  290.587 1.00 22.63  ? 330 LEU A CD2 1 
ATOM   2485 N  N   . GLU A 1 331 ? -111.437 36.529  289.024 1.00 28.61  ? 331 GLU A N   1 
ATOM   2486 C  CA  . GLU A 1 331 ? -111.179 37.592  288.058 1.00 26.99  ? 331 GLU A CA  1 
ATOM   2487 C  C   . GLU A 1 331 ? -109.710 37.993  288.059 1.00 27.47  ? 331 GLU A C   1 
ATOM   2488 O  O   . GLU A 1 331 ? -109.110 38.188  286.995 1.00 24.76  ? 331 GLU A O   1 
ATOM   2489 C  CB  . GLU A 1 331 ? -112.064 38.802  288.358 1.00 26.63  ? 331 GLU A CB  1 
ATOM   2490 C  CG  . GLU A 1 331 ? -113.546 38.567  288.123 1.00 33.54  ? 331 GLU A CG  1 
ATOM   2491 C  CD  . GLU A 1 331 ? -114.386 39.780  288.466 1.00 27.43  ? 331 GLU A CD  1 
ATOM   2492 O  OE1 . GLU A 1 331 ? -113.859 40.703  289.122 1.00 23.19  ? 331 GLU A OE1 1 
ATOM   2493 O  OE2 . GLU A 1 331 ? -115.573 39.812  288.080 1.00 21.79  ? 331 GLU A OE2 1 
ATOM   2494 N  N   . GLU A 1 332 ? -109.112 38.116  289.244 1.00 27.75  ? 332 GLU A N   1 
ATOM   2495 C  CA  . GLU A 1 332 ? -107.713 38.516  289.330 1.00 27.98  ? 332 GLU A CA  1 
ATOM   2496 C  C   . GLU A 1 332 ? -106.770 37.375  288.972 1.00 26.19  ? 332 GLU A C   1 
ATOM   2497 O  O   . GLU A 1 332 ? -105.694 37.620  288.413 1.00 24.49  ? 332 GLU A O   1 
ATOM   2498 C  CB  . GLU A 1 332 ? -107.407 39.042  290.733 1.00 27.12  ? 332 GLU A CB  1 
ATOM   2499 C  CG  . GLU A 1 332 ? -108.225 40.265  291.114 1.00 28.81  ? 332 GLU A CG  1 
ATOM   2500 C  CD  . GLU A 1 332 ? -108.262 40.495  292.609 1.00 30.48  ? 332 GLU A CD  1 
ATOM   2501 O  OE1 . GLU A 1 332 ? -107.620 39.717  293.342 1.00 35.88  ? 332 GLU A OE1 1 
ATOM   2502 O  OE2 . GLU A 1 332 ? -108.940 41.445  293.053 1.00 31.84  ? 332 GLU A OE2 1 
ATOM   2503 N  N   . LEU A 1 333 ? -107.147 36.132  289.280 1.00 26.67  ? 333 LEU A N   1 
ATOM   2504 C  CA  . LEU A 1 333 ? -106.328 34.996  288.872 1.00 25.29  ? 333 LEU A CA  1 
ATOM   2505 C  C   . LEU A 1 333 ? -106.348 34.819  287.359 1.00 24.06  ? 333 LEU A C   1 
ATOM   2506 O  O   . LEU A 1 333 ? -105.314 34.522  286.751 1.00 25.17  ? 333 LEU A O   1 
ATOM   2507 C  CB  . LEU A 1 333 ? -106.806 33.722  289.568 1.00 22.47  ? 333 LEU A CB  1 
ATOM   2508 C  CG  . LEU A 1 333 ? -106.383 33.549  291.027 1.00 18.32  ? 333 LEU A CG  1 
ATOM   2509 C  CD1 . LEU A 1 333 ? -106.941 32.259  291.588 1.00 21.96  ? 333 LEU A CD1 1 
ATOM   2510 C  CD2 . LEU A 1 333 ? -104.871 33.561  291.141 1.00 19.53  ? 333 LEU A CD2 1 
ATOM   2511 N  N   . ARG A 1 334 ? -107.515 34.999  286.735 1.00 23.78  ? 334 ARG A N   1 
ATOM   2512 C  CA  . ARG A 1 334 ? -107.597 34.896  285.282 1.00 25.81  ? 334 ARG A CA  1 
ATOM   2513 C  C   . ARG A 1 334 ? -106.766 35.980  284.609 1.00 28.89  ? 334 ARG A C   1 
ATOM   2514 O  O   . ARG A 1 334 ? -106.067 35.715  283.624 1.00 26.52  ? 334 ARG A O   1 
ATOM   2515 C  CB  . ARG A 1 334 ? -109.055 34.978  284.833 1.00 27.04  ? 334 ARG A CB  1 
ATOM   2516 C  CG  . ARG A 1 334 ? -109.267 34.798  283.337 1.00 23.67  ? 334 ARG A CG  1 
ATOM   2517 C  CD  . ARG A 1 334 ? -108.965 33.375  282.894 1.00 27.76  ? 334 ARG A CD  1 
ATOM   2518 N  NE  . ARG A 1 334 ? -107.607 33.227  282.379 1.00 28.03  ? 334 ARG A NE  1 
ATOM   2519 C  CZ  . ARG A 1 334 ? -107.072 32.066  282.015 1.00 25.70  ? 334 ARG A CZ  1 
ATOM   2520 N  NH1 . ARG A 1 334 ? -107.778 30.949  282.113 1.00 22.27  ? 334 ARG A NH1 1 
ATOM   2521 N  NH2 . ARG A 1 334 ? -105.830 32.021  281.554 1.00 37.32  ? 334 ARG A NH2 1 
ATOM   2522 N  N   . ALA A 1 335 ? -106.828 37.208  285.128 1.00 26.59  ? 335 ALA A N   1 
ATOM   2523 C  CA  . ALA A 1 335 ? -106.016 38.286  284.574 1.00 24.56  ? 335 ALA A CA  1 
ATOM   2524 C  C   . ALA A 1 335 ? -104.531 38.018  284.779 1.00 23.83  ? 335 ALA A C   1 
ATOM   2525 O  O   . ALA A 1 335 ? -103.711 38.332  283.908 1.00 27.45  ? 335 ALA A O   1 
ATOM   2526 C  CB  . ALA A 1 335 ? -106.414 39.621  285.202 1.00 25.36  ? 335 ALA A CB  1 
ATOM   2527 N  N   . MET A 1 336 ? -104.167 37.437  285.924 1.00 22.14  ? 336 MET A N   1 
ATOM   2528 C  CA  . MET A 1 336 ? -102.772 37.081  286.157 1.00 22.28  ? 336 MET A CA  1 
ATOM   2529 C  C   . MET A 1 336 ? -102.319 35.989  285.197 1.00 24.42  ? 336 MET A C   1 
ATOM   2530 O  O   . MET A 1 336 ? -101.196 36.034  284.682 1.00 26.69  ? 336 MET A O   1 
ATOM   2531 C  CB  . MET A 1 336 ? -102.582 36.647  287.613 1.00 19.50  ? 336 MET A CB  1 
ATOM   2532 C  CG  . MET A 1 336 ? -101.189 36.135  287.961 1.00 18.54  ? 336 MET A CG  1 
ATOM   2533 S  SD  . MET A 1 336 ? -100.944 34.379  287.623 1.00 19.15  ? 336 MET A SD  1 
ATOM   2534 C  CE  . MET A 1 336 ? -102.347 33.672  288.480 1.00 22.92  ? 336 MET A CE  1 
ATOM   2535 N  N   . LEU A 1 337 ? -103.179 34.998  284.946 1.00 24.08  ? 337 LEU A N   1 
ATOM   2536 C  CA  . LEU A 1 337 ? -102.840 33.953  283.987 1.00 23.03  ? 337 LEU A CA  1 
ATOM   2537 C  C   . LEU A 1 337 ? -102.737 34.502  282.570 1.00 25.85  ? 337 LEU A C   1 
ATOM   2538 O  O   . LEU A 1 337 ? -101.931 34.007  281.775 1.00 25.17  ? 337 LEU A O   1 
ATOM   2539 C  CB  . LEU A 1 337 ? -103.872 32.829  284.044 1.00 22.16  ? 337 LEU A CB  1 
ATOM   2540 C  CG  . LEU A 1 337 ? -103.912 32.002  285.329 1.00 21.18  ? 337 LEU A CG  1 
ATOM   2541 C  CD1 . LEU A 1 337 ? -104.999 30.945  285.246 1.00 22.91  ? 337 LEU A CD1 1 
ATOM   2542 C  CD2 . LEU A 1 337 ? -102.562 31.365  285.584 1.00 19.52  ? 337 LEU A CD2 1 
ATOM   2543 N  N   . ASP A 1 338 ? -103.540 35.516  282.236 1.00 27.92  ? 338 ASP A N   1 
ATOM   2544 C  CA  . ASP A 1 338 ? -103.436 36.133  280.918 1.00 27.63  ? 338 ASP A CA  1 
ATOM   2545 C  C   . ASP A 1 338 ? -102.077 36.787  280.715 1.00 28.29  ? 338 ASP A C   1 
ATOM   2546 O  O   . ASP A 1 338 ? -101.568 36.826  279.589 1.00 31.75  ? 338 ASP A O   1 
ATOM   2547 C  CB  . ASP A 1 338 ? -104.554 37.157  280.724 1.00 25.75  ? 338 ASP A CB  1 
ATOM   2548 C  CG  . ASP A 1 338 ? -105.930 36.525  280.726 1.00 33.95  ? 338 ASP A CG  1 
ATOM   2549 O  OD1 . ASP A 1 338 ? -106.032 35.318  280.420 1.00 39.26  ? 338 ASP A OD1 1 
ATOM   2550 O  OD2 . ASP A 1 338 ? -106.911 37.234  281.033 1.00 42.17  ? 338 ASP A OD2 1 
ATOM   2551 N  N   . ASP A 1 339 ? -101.476 37.307  281.788 1.00 24.91  ? 339 ASP A N   1 
ATOM   2552 C  CA  . ASP A 1 339 ? -100.126 37.849  281.682 1.00 25.85  ? 339 ASP A CA  1 
ATOM   2553 C  C   . ASP A 1 339 ? -99.109  36.740  281.450 1.00 28.16  ? 339 ASP A C   1 
ATOM   2554 O  O   . ASP A 1 339 ? -98.163  36.910  280.672 1.00 30.66  ? 339 ASP A O   1 
ATOM   2555 C  CB  . ASP A 1 339 ? -99.780  38.646  282.938 1.00 30.44  ? 339 ASP A CB  1 
ATOM   2556 C  CG  . ASP A 1 339 ? -100.680 39.850  283.129 1.00 44.59  ? 339 ASP A CG  1 
ATOM   2557 O  OD1 . ASP A 1 339 ? -100.747 40.695  282.212 1.00 55.16  ? 339 ASP A OD1 1 
ATOM   2558 O  OD2 . ASP A 1 339 ? -101.321 39.952  284.197 1.00 42.17  ? 339 ASP A OD2 1 
ATOM   2559 N  N   . LEU A 1 340 ? -99.289  35.596  282.115 1.00 26.22  ? 340 LEU A N   1 
ATOM   2560 C  CA  . LEU A 1 340 ? -98.417  34.454  281.868 1.00 28.78  ? 340 LEU A CA  1 
ATOM   2561 C  C   . LEU A 1 340 ? -98.576  33.931  280.448 1.00 25.64  ? 340 LEU A C   1 
ATOM   2562 O  O   . LEU A 1 340 ? -97.604  33.460  279.847 1.00 37.57  ? 340 LEU A O   1 
ATOM   2563 C  CB  . LEU A 1 340 ? -98.708  33.341  282.876 1.00 23.79  ? 340 LEU A CB  1 
ATOM   2564 C  CG  . LEU A 1 340 ? -98.009  33.420  284.234 1.00 22.70  ? 340 LEU A CG  1 
ATOM   2565 C  CD1 . LEU A 1 340 ? -98.436  32.261  285.119 1.00 19.56  ? 340 LEU A CD1 1 
ATOM   2566 C  CD2 . LEU A 1 340 ? -96.500  33.432  284.059 1.00 28.34  ? 340 LEU A CD2 1 
ATOM   2567 N  N   . GLU A 1 341 ? -99.789  34.007  279.896 1.00 24.40  ? 341 GLU A N   1 
ATOM   2568 C  CA  . GLU A 1 341 ? -100.019 33.512  278.543 1.00 26.52  ? 341 GLU A CA  1 
ATOM   2569 C  C   . GLU A 1 341 ? -99.263  34.341  277.513 1.00 27.65  ? 341 GLU A C   1 
ATOM   2570 O  O   . GLU A 1 341 ? -98.732  33.797  276.538 1.00 34.27  ? 341 GLU A O   1 
ATOM   2571 C  CB  . GLU A 1 341 ? -101.516 33.510  278.234 1.00 29.56  ? 341 GLU A CB  1 
ATOM   2572 C  CG  . GLU A 1 341 ? -102.308 32.463  279.000 1.00 28.66  ? 341 GLU A CG  1 
ATOM   2573 C  CD  . GLU A 1 341 ? -103.765 32.420  278.588 1.00 27.97  ? 341 GLU A CD  1 
ATOM   2574 O  OE1 . GLU A 1 341 ? -104.175 33.269  277.770 1.00 30.44  ? 341 GLU A OE1 1 
ATOM   2575 O  OE2 . GLU A 1 341 ? -104.499 31.539  279.081 1.00 24.03  ? 341 GLU A OE2 1 
ATOM   2576 N  N   . ALA A 1 342 ? -99.204  35.659  277.708 1.00 28.37  ? 342 ALA A N   1 
ATOM   2577 C  CA  . ALA A 1 342 ? -98.483  36.512  276.771 1.00 39.21  ? 342 ALA A CA  1 
ATOM   2578 C  C   . ALA A 1 342 ? -96.983  36.503  277.029 1.00 34.75  ? 342 ALA A C   1 
ATOM   2579 O  O   . ALA A 1 342 ? -96.197  36.711  276.097 1.00 30.11  ? 342 ALA A O   1 
ATOM   2580 C  CB  . ALA A 1 342 ? -99.019  37.943  276.843 1.00 43.72  ? 342 ALA A CB  1 
ATOM   2581 N  N   . GLN A 1 343 ? -96.568  36.262  278.273 1.00 40.28  ? 343 GLN A N   1 
ATOM   2582 C  CA  . GLN A 1 343 ? -95.147  36.268  278.601 1.00 35.64  ? 343 GLN A CA  1 
ATOM   2583 C  C   . GLN A 1 343 ? -94.483  34.942  278.249 1.00 29.97  ? 343 GLN A C   1 
ATOM   2584 O  O   . GLN A 1 343 ? -93.336  34.922  277.787 1.00 33.49  ? 343 GLN A O   1 
ATOM   2585 C  CB  . GLN A 1 343 ? -94.960  36.597  280.085 1.00 35.83  ? 343 GLN A CB  1 
ATOM   2586 C  CG  . GLN A 1 343 ? -93.633  36.154  280.678 1.00 50.72  ? 343 GLN A CG  1 
ATOM   2587 C  CD  . GLN A 1 343 ? -93.522  36.481  282.155 1.00 56.24  ? 343 GLN A CD  1 
ATOM   2588 O  OE1 . GLN A 1 343 ? -94.312  37.259  282.691 1.00 53.30  ? 343 GLN A OE1 1 
ATOM   2589 N  NE2 . GLN A 1 343 ? -92.538  35.888  282.821 1.00 51.55  ? 343 GLN A NE2 1 
ATOM   2590 N  N   . THR A 1 344 ? -95.188  33.827  278.446 1.00 29.03  ? 344 THR A N   1 
ATOM   2591 C  CA  . THR A 1 344 ? -94.640  32.510  278.152 1.00 26.36  ? 344 THR A CA  1 
ATOM   2592 C  C   . THR A 1 344 ? -95.079  31.957  276.803 1.00 25.93  ? 344 THR A C   1 
ATOM   2593 O  O   . THR A 1 344 ? -94.468  30.996  276.321 1.00 27.45  ? 344 THR A O   1 
ATOM   2594 C  CB  . THR A 1 344 ? -95.037  31.510  279.245 1.00 27.13  ? 344 THR A CB  1 
ATOM   2595 O  OG1 . THR A 1 344 ? -96.444  31.252  279.172 1.00 26.14  ? 344 THR A OG1 1 
ATOM   2596 C  CG2 . THR A 1 344 ? -94.700  32.063  280.620 1.00 43.65  ? 344 THR A CG2 1 
ATOM   2597 N  N   . GLY A 1 345 ? -96.109  32.530  276.186 1.00 26.38  ? 345 GLY A N   1 
ATOM   2598 C  CA  . GLY A 1 345 ? -96.627  32.003  274.941 1.00 26.65  ? 345 GLY A CA  1 
ATOM   2599 C  C   . GLY A 1 345 ? -97.487  30.769  275.082 1.00 26.44  ? 345 GLY A C   1 
ATOM   2600 O  O   . GLY A 1 345 ? -97.879  30.185  274.066 1.00 24.90  ? 345 GLY A O   1 
ATOM   2601 N  N   . ARG A 1 346 ? -97.795  30.356  276.307 1.00 25.84  ? 346 ARG A N   1 
ATOM   2602 C  CA  . ARG A 1 346 ? -98.585  29.167  276.573 1.00 25.02  ? 346 ARG A CA  1 
ATOM   2603 C  C   . ARG A 1 346 ? -100.037 29.552  276.839 1.00 24.65  ? 346 ARG A C   1 
ATOM   2604 O  O   . ARG A 1 346 ? -100.399 30.730  276.890 1.00 25.35  ? 346 ARG A O   1 
ATOM   2605 C  CB  . ARG A 1 346 ? -98.000  28.402  277.761 1.00 27.06  ? 346 ARG A CB  1 
ATOM   2606 C  CG  . ARG A 1 346 ? -96.540  28.021  277.601 1.00 43.63  ? 346 ARG A CG  1 
ATOM   2607 C  CD  . ARG A 1 346 ? -95.965  27.497  278.906 1.00 39.24  ? 346 ARG A CD  1 
ATOM   2608 N  NE  . ARG A 1 346 ? -96.807  26.464  279.501 1.00 43.48  ? 346 ARG A NE  1 
ATOM   2609 C  CZ  . ARG A 1 346 ? -96.576  25.902  280.683 1.00 40.21  ? 346 ARG A CZ  1 
ATOM   2610 N  NH1 . ARG A 1 346 ? -95.526  26.276  281.402 1.00 32.90  ? 346 ARG A NH1 1 
ATOM   2611 N  NH2 . ARG A 1 346 ? -97.394  24.968  281.148 1.00 29.26  ? 346 ARG A NH2 1 
ATOM   2612 N  N   . VAL A 1 347 ? -100.880 28.537  277.011 1.00 22.92  ? 347 VAL A N   1 
ATOM   2613 C  CA  . VAL A 1 347 ? -102.252 28.718  277.466 1.00 25.25  ? 347 VAL A CA  1 
ATOM   2614 C  C   . VAL A 1 347 ? -102.344 28.191  278.893 1.00 24.42  ? 347 VAL A C   1 
ATOM   2615 O  O   . VAL A 1 347 ? -101.809 27.120  279.209 1.00 23.24  ? 347 VAL A O   1 
ATOM   2616 C  CB  . VAL A 1 347 ? -103.265 28.035  276.526 1.00 25.17  ? 347 VAL A CB  1 
ATOM   2617 C  CG1 . VAL A 1 347 ? -102.971 28.409  275.082 1.00 22.45  ? 347 VAL A CG1 1 
ATOM   2618 C  CG2 . VAL A 1 347 ? -103.252 26.522  276.682 1.00 30.64  ? 347 VAL A CG2 1 
ATOM   2619 N  N   . TYR A 1 348 ? -102.978 28.970  279.765 1.00 27.02  ? 348 TYR A N   1 
ATOM   2620 C  CA  . TYR A 1 348 ? -103.096 28.642  281.178 1.00 28.97  ? 348 TYR A CA  1 
ATOM   2621 C  C   . TYR A 1 348 ? -104.569 28.619  281.554 1.00 29.74  ? 348 TYR A C   1 
ATOM   2622 O  O   . TYR A 1 348 ? -105.323 29.523  281.178 1.00 35.90  ? 348 TYR A O   1 
ATOM   2623 C  CB  . TYR A 1 348 ? -102.332 29.650  282.043 1.00 26.57  ? 348 TYR A CB  1 
ATOM   2624 C  CG  . TYR A 1 348 ? -100.840 29.401  282.109 1.00 26.05  ? 348 TYR A CG  1 
ATOM   2625 C  CD1 . TYR A 1 348 ? -100.292 28.613  283.112 1.00 26.47  ? 348 TYR A CD1 1 
ATOM   2626 C  CD2 . TYR A 1 348 ? -99.980  29.955  281.169 1.00 24.49  ? 348 TYR A CD2 1 
ATOM   2627 C  CE1 . TYR A 1 348 ? -98.930  28.384  283.179 1.00 31.99  ? 348 TYR A CE1 1 
ATOM   2628 C  CE2 . TYR A 1 348 ? -98.616  29.730  281.227 1.00 25.12  ? 348 TYR A CE2 1 
ATOM   2629 C  CZ  . TYR A 1 348 ? -98.097  28.944  282.234 1.00 29.10  ? 348 TYR A CZ  1 
ATOM   2630 O  OH  . TYR A 1 348 ? -96.742  28.715  282.299 1.00 26.14  ? 348 TYR A OH  1 
ATOM   2631 N  N   . GLU A 1 349 ? -104.972 27.590  282.290 1.00 25.31  ? 349 GLU A N   1 
ATOM   2632 C  CA  . GLU A 1 349 ? -106.368 27.374  282.633 1.00 27.58  ? 349 GLU A CA  1 
ATOM   2633 C  C   . GLU A 1 349 ? -106.639 27.760  284.081 1.00 24.51  ? 349 GLU A C   1 
ATOM   2634 O  O   . GLU A 1 349 ? -105.761 27.681  284.942 1.00 23.97  ? 349 GLU A O   1 
ATOM   2635 C  CB  . GLU A 1 349 ? -106.758 25.913  282.402 1.00 27.09  ? 349 GLU A CB  1 
ATOM   2636 C  CG  . GLU A 1 349 ? -106.707 25.494  280.946 1.00 32.50  ? 349 GLU A CG  1 
ATOM   2637 C  CD  . GLU A 1 349 ? -106.961 24.015  280.753 1.00 24.89  ? 349 GLU A CD  1 
ATOM   2638 O  OE1 . GLU A 1 349 ? -107.586 23.394  281.638 1.00 24.64  ? 349 GLU A OE1 1 
ATOM   2639 O  OE2 . GLU A 1 349 ? -106.536 23.475  279.712 1.00 26.22  ? 349 GLU A OE2 1 
ATOM   2640 N  N   . LEU A 1 350 ? -107.874 28.180  284.339 1.00 23.05  ? 350 LEU A N   1 
ATOM   2641 C  CA  . LEU A 1 350 ? -108.321 28.545  285.681 1.00 21.00  ? 350 LEU A CA  1 
ATOM   2642 C  C   . LEU A 1 350 ? -109.594 27.757  285.966 1.00 22.31  ? 350 LEU A C   1 
ATOM   2643 O  O   . LEU A 1 350 ? -110.668 28.099  285.465 1.00 22.60  ? 350 LEU A O   1 
ATOM   2644 C  CB  . LEU A 1 350 ? -108.555 30.047  285.799 1.00 21.41  ? 350 LEU A CB  1 
ATOM   2645 C  CG  . LEU A 1 350 ? -109.114 30.536  287.134 1.00 22.21  ? 350 LEU A CG  1 
ATOM   2646 C  CD1 . LEU A 1 350 ? -108.237 30.075  288.287 1.00 17.98  ? 350 LEU A CD1 1 
ATOM   2647 C  CD2 . LEU A 1 350 ? -109.246 32.048  287.129 1.00 27.12  ? 350 LEU A CD2 1 
ATOM   2648 N  N   . THR A 1 351 ? -109.470 26.700  286.759 1.00 23.92  ? 351 THR A N   1 
ATOM   2649 C  CA  . THR A 1 351 ? -110.589 25.836  287.099 1.00 25.92  ? 351 THR A CA  1 
ATOM   2650 C  C   . THR A 1 351 ? -110.944 25.993  288.571 1.00 23.17  ? 351 THR A C   1 
ATOM   2651 O  O   . THR A 1 351 ? -110.240 26.650  289.342 1.00 21.49  ? 351 THR A O   1 
ATOM   2652 C  CB  . THR A 1 351 ? -110.263 24.372  286.785 1.00 29.43  ? 351 THR A CB  1 
ATOM   2653 O  OG1 . THR A 1 351 ? -109.234 23.911  287.668 1.00 27.08  ? 351 THR A OG1 1 
ATOM   2654 C  CG2 . THR A 1 351 ? -109.791 24.229  285.347 1.00 49.02  ? 351 THR A CG2 1 
ATOM   2655 N  N   . SER A 1 352 ? -112.056 25.371  288.955 1.00 23.38  ? 352 SER A N   1 
ATOM   2656 C  CA  . SER A 1 352 ? -112.519 25.435  290.335 1.00 21.40  ? 352 SER A CA  1 
ATOM   2657 C  C   . SER A 1 352 ? -113.459 24.272  290.603 1.00 20.05  ? 352 SER A C   1 
ATOM   2658 O  O   . SER A 1 352 ? -114.351 23.996  289.796 1.00 21.98  ? 352 SER A O   1 
ATOM   2659 C  CB  . SER A 1 352 ? -113.226 26.763  290.621 1.00 21.01  ? 352 SER A CB  1 
ATOM   2660 O  OG  . SER A 1 352 ? -113.818 26.753  291.908 1.00 17.50  ? 352 SER A OG  1 
ATOM   2661 N  N   . ALA A 1 353 ? -113.256 23.600  291.731 1.00 18.92  ? 353 ALA A N   1 
ATOM   2662 C  CA  . ALA A 1 353 ? -114.159 22.551  292.178 1.00 22.06  ? 353 ALA A CA  1 
ATOM   2663 C  C   . ALA A 1 353 ? -115.188 23.150  293.126 1.00 21.06  ? 353 ALA A C   1 
ATOM   2664 O  O   . ALA A 1 353 ? -114.831 23.844  294.083 1.00 21.34  ? 353 ALA A O   1 
ATOM   2665 C  CB  . ALA A 1 353 ? -113.392 21.423  292.867 1.00 21.57  ? 353 ALA A CB  1 
ATOM   2666 N  N   . ILE A 1 354 ? -116.463 22.889  292.851 1.00 19.97  ? 354 ILE A N   1 
ATOM   2667 C  CA  . ILE A 1 354 ? -117.555 23.442  293.636 1.00 21.50  ? 354 ILE A CA  1 
ATOM   2668 C  C   . ILE A 1 354 ? -118.354 22.298  294.242 1.00 21.97  ? 354 ILE A C   1 
ATOM   2669 O  O   . ILE A 1 354 ? -118.291 21.152  293.790 1.00 23.70  ? 354 ILE A O   1 
ATOM   2670 C  CB  . ILE A 1 354 ? -118.470 24.352  292.794 1.00 26.99  ? 354 ILE A CB  1 
ATOM   2671 C  CG1 . ILE A 1 354 ? -119.271 23.516  291.795 1.00 25.15  ? 354 ILE A CG1 1 
ATOM   2672 C  CG2 . ILE A 1 354 ? -117.644 25.390  292.059 1.00 27.68  ? 354 ILE A CG2 1 
ATOM   2673 C  CD1 . ILE A 1 354 ? -120.406 24.270  291.142 1.00 38.81  ? 354 ILE A CD1 1 
ATOM   2674 N  N   . SER A 1 355 ? -119.113 22.624  295.281 1.00 23.98  ? 355 SER A N   1 
ATOM   2675 C  CA  . SER A 1 355 ? -119.977 21.641  295.911 1.00 23.46  ? 355 SER A CA  1 
ATOM   2676 C  C   . SER A 1 355 ? -121.211 21.389  295.055 1.00 23.24  ? 355 SER A C   1 
ATOM   2677 O  O   . SER A 1 355 ? -121.638 22.243  294.273 1.00 26.47  ? 355 SER A O   1 
ATOM   2678 C  CB  . SER A 1 355 ? -120.401 22.105  297.303 1.00 23.94  ? 355 SER A CB  1 
ATOM   2679 O  OG  . SER A 1 355 ? -121.132 21.089  297.965 1.00 24.42  ? 355 SER A OG  1 
ATOM   2680 N  N   . ALA A 1 356 ? -121.781 20.196  295.209 1.00 22.04  ? 356 ALA A N   1 
ATOM   2681 C  CA  . ALA A 1 356 ? -123.006 19.823  294.517 1.00 21.83  ? 356 ALA A CA  1 
ATOM   2682 C  C   . ALA A 1 356 ? -124.244 20.032  295.377 1.00 23.02  ? 356 ALA A C   1 
ATOM   2683 O  O   . ALA A 1 356 ? -125.323 19.548  295.022 1.00 24.77  ? 356 ALA A O   1 
ATOM   2684 C  CB  . ALA A 1 356 ? -122.929 18.369  294.052 1.00 23.06  ? 356 ALA A CB  1 
ATOM   2685 N  N   . GLY A 1 357 ? -124.112 20.735  296.500 1.00 24.52  ? 357 GLY A N   1 
ATOM   2686 C  CA  . GLY A 1 357 ? -125.246 21.017  297.359 1.00 25.57  ? 357 GLY A CA  1 
ATOM   2687 C  C   . GLY A 1 357 ? -125.956 22.279  296.914 1.00 27.89  ? 357 GLY A C   1 
ATOM   2688 O  O   . GLY A 1 357 ? -125.334 23.334  296.767 1.00 30.30  ? 357 GLY A O   1 
ATOM   2689 N  N   . TYR A 1 358 ? -127.270 22.165  296.700 1.00 23.94  ? 358 TYR A N   1 
ATOM   2690 C  CA  . TYR A 1 358 ? -128.046 23.304  296.221 1.00 29.49  ? 358 TYR A CA  1 
ATOM   2691 C  C   . TYR A 1 358 ? -127.996 24.463  297.208 1.00 34.98  ? 358 TYR A C   1 
ATOM   2692 O  O   . TYR A 1 358 ? -127.952 25.631  296.803 1.00 38.48  ? 358 TYR A O   1 
ATOM   2693 C  CB  . TYR A 1 358 ? -129.492 22.881  295.963 1.00 26.98  ? 358 TYR A CB  1 
ATOM   2694 C  CG  . TYR A 1 358 ? -130.272 22.562  297.218 1.00 24.41  ? 358 TYR A CG  1 
ATOM   2695 C  CD1 . TYR A 1 358 ? -130.198 21.306  297.804 1.00 24.69  ? 358 TYR A CD1 1 
ATOM   2696 C  CD2 . TYR A 1 358 ? -131.085 23.517  297.817 1.00 24.94  ? 358 TYR A CD2 1 
ATOM   2697 C  CE1 . TYR A 1 358 ? -130.907 21.010  298.952 1.00 23.89  ? 358 TYR A CE1 1 
ATOM   2698 C  CE2 . TYR A 1 358 ? -131.796 23.230  298.964 1.00 24.13  ? 358 TYR A CE2 1 
ATOM   2699 C  CZ  . TYR A 1 358 ? -131.704 21.975  299.527 1.00 22.20  ? 358 TYR A CZ  1 
ATOM   2700 O  OH  . TYR A 1 358 ? -132.412 21.684  300.669 1.00 26.89  ? 358 TYR A OH  1 
ATOM   2701 N  N   . ASP A 1 359 ? -128.001 24.161  298.508 1.00 28.63  ? 359 ASP A N   1 
ATOM   2702 C  CA  . ASP A 1 359 ? -127.889 25.206  299.518 1.00 29.32  ? 359 ASP A CA  1 
ATOM   2703 C  C   . ASP A 1 359 ? -126.556 25.933  299.436 1.00 32.71  ? 359 ASP A C   1 
ATOM   2704 O  O   . ASP A 1 359 ? -126.425 27.034  299.982 1.00 48.25  ? 359 ASP A O   1 
ATOM   2705 C  CB  . ASP A 1 359 ? -128.068 24.606  300.912 1.00 29.73  ? 359 ASP A CB  1 
ATOM   2706 C  CG  . ASP A 1 359 ? -127.045 23.531  301.215 1.00 34.06  ? 359 ASP A CG  1 
ATOM   2707 O  OD1 . ASP A 1 359 ? -126.658 22.801  300.278 1.00 30.29  ? 359 ASP A OD1 1 
ATOM   2708 O  OD2 . ASP A 1 359 ? -126.624 23.418  302.385 1.00 55.99  ? 359 ASP A OD2 1 
ATOM   2709 N  N   . LYS A 1 360 ? -125.571 25.343  298.765 1.00 30.90  ? 360 LYS A N   1 
ATOM   2710 C  CA  . LYS A 1 360 ? -124.241 25.916  298.620 1.00 29.04  ? 360 LYS A CA  1 
ATOM   2711 C  C   . LYS A 1 360 ? -124.012 26.522  297.243 1.00 29.43  ? 360 LYS A C   1 
ATOM   2712 O  O   . LYS A 1 360 ? -123.322 27.539  297.125 1.00 27.41  ? 360 LYS A O   1 
ATOM   2713 C  CB  . LYS A 1 360 ? -123.190 24.840  298.895 1.00 31.52  ? 360 LYS A CB  1 
ATOM   2714 C  CG  . LYS A 1 360 ? -123.609 23.886  300.003 1.00 43.85  ? 360 LYS A CG  1 
ATOM   2715 C  CD  . LYS A 1 360 ? -122.670 22.706  300.127 1.00 35.74  ? 360 LYS A CD  1 
ATOM   2716 C  CE  . LYS A 1 360 ? -123.116 21.766  301.235 1.00 44.75  ? 360 LYS A CE  1 
ATOM   2717 N  NZ  . LYS A 1 360 ? -122.316 20.511  301.253 1.00 43.87  ? 360 LYS A NZ  1 
ATOM   2718 N  N   . ILE A 1 361 ? -124.583 25.917  296.199 1.00 30.02  ? 361 ILE A N   1 
ATOM   2719 C  CA  . ILE A 1 361 ? -124.503 26.491  294.860 1.00 28.29  ? 361 ILE A CA  1 
ATOM   2720 C  C   . ILE A 1 361 ? -125.225 27.829  294.805 1.00 30.21  ? 361 ILE A C   1 
ATOM   2721 O  O   . ILE A 1 361 ? -124.808 28.740  294.080 1.00 41.21  ? 361 ILE A O   1 
ATOM   2722 C  CB  . ILE A 1 361 ? -125.068 25.497  293.825 1.00 22.27  ? 361 ILE A CB  1 
ATOM   2723 C  CG1 . ILE A 1 361 ? -124.279 24.188  293.854 1.00 23.68  ? 361 ILE A CG1 1 
ATOM   2724 C  CG2 . ILE A 1 361 ? -125.047 26.096  292.429 1.00 22.47  ? 361 ILE A CG2 1 
ATOM   2725 C  CD1 . ILE A 1 361 ? -124.741 23.179  292.828 1.00 24.72  ? 361 ILE A CD1 1 
ATOM   2726 N  N   . ALA A 1 362 ? -126.307 27.979  295.573 1.00 28.51  ? 362 ALA A N   1 
ATOM   2727 C  CA  . ALA A 1 362 ? -127.059 29.228  295.573 1.00 50.98  ? 362 ALA A CA  1 
ATOM   2728 C  C   . ALA A 1 362 ? -126.255 30.397  296.127 1.00 31.63  ? 362 ALA A C   1 
ATOM   2729 O  O   . ALA A 1 362 ? -126.583 31.551  295.833 1.00 34.68  ? 362 ALA A O   1 
ATOM   2730 C  CB  . ALA A 1 362 ? -128.350 29.064  296.375 1.00 33.43  ? 362 ALA A CB  1 
ATOM   2731 N  N   . VAL A 1 363 ? -125.212 30.129  296.916 1.00 23.65  ? 363 VAL A N   1 
ATOM   2732 C  CA  . VAL A 1 363 ? -124.425 31.213  297.494 1.00 27.72  ? 363 VAL A CA  1 
ATOM   2733 C  C   . VAL A 1 363 ? -123.620 31.927  296.415 1.00 30.45  ? 363 VAL A C   1 
ATOM   2734 O  O   . VAL A 1 363 ? -123.556 33.161  296.382 1.00 31.02  ? 363 VAL A O   1 
ATOM   2735 C  CB  . VAL A 1 363 ? -123.517 30.674  298.614 1.00 28.39  ? 363 VAL A CB  1 
ATOM   2736 C  CG1 . VAL A 1 363 ? -122.662 31.793  299.191 1.00 26.44  ? 363 VAL A CG1 1 
ATOM   2737 C  CG2 . VAL A 1 363 ? -124.352 30.022  299.704 1.00 37.41  ? 363 VAL A CG2 1 
ATOM   2738 N  N   . VAL A 1 364 ? -123.002 31.168  295.515 1.00 26.45  ? 364 VAL A N   1 
ATOM   2739 C  CA  . VAL A 1 364 ? -122.143 31.715  294.472 1.00 23.45  ? 364 VAL A CA  1 
ATOM   2740 C  C   . VAL A 1 364 ? -122.933 31.800  293.175 1.00 21.98  ? 364 VAL A C   1 
ATOM   2741 O  O   . VAL A 1 364 ? -123.605 30.839  292.783 1.00 26.34  ? 364 VAL A O   1 
ATOM   2742 C  CB  . VAL A 1 364 ? -120.880 30.858  294.287 1.00 27.52  ? 364 VAL A CB  1 
ATOM   2743 C  CG1 . VAL A 1 364 ? -120.022 31.414  293.165 1.00 39.43  ? 364 VAL A CG1 1 
ATOM   2744 C  CG2 . VAL A 1 364 ? -120.095 30.787  295.584 1.00 35.50  ? 364 VAL A CG2 1 
ATOM   2745 N  N   . ASN A 1 365 ? -122.850 32.946  292.506 1.00 19.99  ? 365 ASN A N   1 
ATOM   2746 C  CA  . ASN A 1 365 ? -123.477 33.131  291.199 1.00 23.65  ? 365 ASN A CA  1 
ATOM   2747 C  C   . ASN A 1 365 ? -122.445 32.777  290.138 1.00 22.75  ? 365 ASN A C   1 
ATOM   2748 O  O   . ASN A 1 365 ? -121.564 33.580  289.817 1.00 22.35  ? 365 ASN A O   1 
ATOM   2749 C  CB  . ASN A 1 365 ? -123.986 34.559  291.038 1.00 33.55  ? 365 ASN A CB  1 
ATOM   2750 C  CG  . ASN A 1 365 ? -124.386 34.877  289.610 1.00 26.64  ? 365 ASN A CG  1 
ATOM   2751 O  OD1 . ASN A 1 365 ? -124.930 34.030  288.902 1.00 44.54  ? 365 ASN A OD1 1 
ATOM   2752 N  ND2 . ASN A 1 365 ? -124.116 36.104  289.179 1.00 25.13  ? 365 ASN A ND2 1 
ATOM   2753 N  N   . TYR A 1 366 ? -122.551 31.570  289.588 1.00 22.91  ? 366 TYR A N   1 
ATOM   2754 C  CA  . TYR A 1 366 ? -121.570 31.081  288.629 1.00 23.91  ? 366 TYR A CA  1 
ATOM   2755 C  C   . TYR A 1 366 ? -121.801 31.598  287.216 1.00 25.25  ? 366 TYR A C   1 
ATOM   2756 O  O   . TYR A 1 366 ? -121.000 31.291  286.327 1.00 26.07  ? 366 TYR A O   1 
ATOM   2757 C  CB  . TYR A 1 366 ? -121.556 29.551  288.629 1.00 24.98  ? 366 TYR A CB  1 
ATOM   2758 C  CG  . TYR A 1 366 ? -121.230 28.959  289.979 1.00 25.55  ? 366 TYR A CG  1 
ATOM   2759 C  CD1 . TYR A 1 366 ? -119.915 28.726  290.353 1.00 24.07  ? 366 TYR A CD1 1 
ATOM   2760 C  CD2 . TYR A 1 366 ? -122.235 28.635  290.879 1.00 25.21  ? 366 TYR A CD2 1 
ATOM   2761 C  CE1 . TYR A 1 366 ? -119.609 28.189  291.586 1.00 26.19  ? 366 TYR A CE1 1 
ATOM   2762 C  CE2 . TYR A 1 366 ? -121.939 28.095  292.115 1.00 26.50  ? 366 TYR A CE2 1 
ATOM   2763 C  CZ  . TYR A 1 366 ? -120.624 27.873  292.462 1.00 29.62  ? 366 TYR A CZ  1 
ATOM   2764 O  OH  . TYR A 1 366 ? -120.321 27.335  293.692 1.00 32.84  ? 366 TYR A OH  1 
ATOM   2765 N  N   . ALA A 1 367 ? -122.868 32.365  286.980 1.00 24.01  ? 367 ALA A N   1 
ATOM   2766 C  CA  . ALA A 1 367 ? -123.010 33.033  285.692 1.00 22.66  ? 367 ALA A CA  1 
ATOM   2767 C  C   . ALA A 1 367 ? -121.912 34.067  285.489 1.00 21.76  ? 367 ALA A C   1 
ATOM   2768 O  O   . ALA A 1 367 ? -121.454 34.276  284.359 1.00 22.11  ? 367 ALA A O   1 
ATOM   2769 C  CB  . ALA A 1 367 ? -124.386 33.688  285.585 1.00 24.16  ? 367 ALA A CB  1 
ATOM   2770 N  N   . GLU A 1 368 ? -121.479 34.718  286.567 1.00 20.53  ? 368 GLU A N   1 
ATOM   2771 C  CA  . GLU A 1 368 ? -120.357 35.643  286.519 1.00 21.58  ? 368 GLU A CA  1 
ATOM   2772 C  C   . GLU A 1 368 ? -119.018 34.938  286.676 1.00 23.91  ? 368 GLU A C   1 
ATOM   2773 O  O   . GLU A 1 368 ? -118.019 35.381  286.098 1.00 29.99  ? 368 GLU A O   1 
ATOM   2774 C  CB  . GLU A 1 368 ? -120.508 36.706  287.612 1.00 22.66  ? 368 GLU A CB  1 
ATOM   2775 C  CG  . GLU A 1 368 ? -119.448 37.795  287.591 1.00 25.18  ? 368 GLU A CG  1 
ATOM   2776 C  CD  . GLU A 1 368 ? -119.715 38.852  286.540 1.00 26.37  ? 368 GLU A CD  1 
ATOM   2777 O  OE1 . GLU A 1 368 ? -120.795 38.813  285.915 1.00 20.76  ? 368 GLU A OE1 1 
ATOM   2778 O  OE2 . GLU A 1 368 ? -118.846 39.727  286.342 1.00 21.25  ? 368 GLU A OE2 1 
ATOM   2779 N  N   . ALA A 1 369 ? -118.980 33.842  287.438 1.00 22.75  ? 369 ALA A N   1 
ATOM   2780 C  CA  . ALA A 1 369 ? -117.724 33.134  287.653 1.00 24.19  ? 369 ALA A CA  1 
ATOM   2781 C  C   . ALA A 1 369 ? -117.300 32.341  286.424 1.00 26.65  ? 369 ALA A C   1 
ATOM   2782 O  O   . ALA A 1 369 ? -116.105 32.089  286.235 1.00 33.60  ? 369 ALA A O   1 
ATOM   2783 C  CB  . ALA A 1 369 ? -117.843 32.207  288.862 1.00 24.18  ? 369 ALA A CB  1 
ATOM   2784 N  N   . GLN A 1 370 ? -118.254 31.942  285.579 1.00 25.82  ? 370 GLN A N   1 
ATOM   2785 C  CA  . GLN A 1 370 ? -117.918 31.109  284.431 1.00 30.26  ? 370 GLN A CA  1 
ATOM   2786 C  C   . GLN A 1 370 ? -117.145 31.868  283.361 1.00 35.62  ? 370 GLN A C   1 
ATOM   2787 O  O   . GLN A 1 370 ? -116.510 31.235  282.512 1.00 31.81  ? 370 GLN A O   1 
ATOM   2788 C  CB  . GLN A 1 370 ? -119.183 30.505  283.820 1.00 33.05  ? 370 GLN A CB  1 
ATOM   2789 C  CG  . GLN A 1 370 ? -120.023 31.486  283.025 1.00 29.45  ? 370 GLN A CG  1 
ATOM   2790 C  CD  . GLN A 1 370 ? -121.161 30.808  282.290 1.00 36.24  ? 370 GLN A CD  1 
ATOM   2791 O  OE1 . GLN A 1 370 ? -121.204 29.582  282.187 1.00 34.37  ? 370 GLN A OE1 1 
ATOM   2792 N  NE2 . GLN A 1 370 ? -122.088 31.603  281.773 1.00 54.59  ? 370 GLN A NE2 1 
ATOM   2793 N  N   . LYS A 1 371 ? -117.184 33.200  283.371 1.00 29.97  ? 371 LYS A N   1 
ATOM   2794 C  CA  . LYS A 1 371 ? -116.385 33.961  282.421 1.00 33.05  ? 371 LYS A CA  1 
ATOM   2795 C  C   . LYS A 1 371 ? -114.931 34.087  282.861 1.00 31.84  ? 371 LYS A C   1 
ATOM   2796 O  O   . LYS A 1 371 ? -114.106 34.598  282.096 1.00 35.15  ? 371 LYS A O   1 
ATOM   2797 C  CB  . LYS A 1 371 ? -117.007 35.344  282.200 1.00 42.29  ? 371 LYS A CB  1 
ATOM   2798 C  CG  . LYS A 1 371 ? -116.560 36.029  280.915 1.00 74.73  ? 371 LYS A CG  1 
ATOM   2799 C  CD  . LYS A 1 371 ? -117.686 36.831  280.286 1.00 83.11  ? 371 LYS A CD  1 
ATOM   2800 C  CE  . LYS A 1 371 ? -118.582 35.940  279.440 1.00 73.20  ? 371 LYS A CE  1 
ATOM   2801 N  NZ  . LYS A 1 371 ? -117.798 35.102  278.489 1.00 55.65  ? 371 LYS A NZ  1 
ATOM   2802 N  N   . SER A 1 372 ? -114.601 33.627  284.069 1.00 29.03  ? 372 SER A N   1 
ATOM   2803 C  CA  . SER A 1 372 ? -113.220 33.486  284.501 1.00 47.24  ? 372 SER A CA  1 
ATOM   2804 C  C   . SER A 1 372 ? -112.775 32.036  284.616 1.00 33.28  ? 372 SER A C   1 
ATOM   2805 O  O   . SER A 1 372 ? -111.574 31.766  284.525 1.00 28.58  ? 372 SER A O   1 
ATOM   2806 C  CB  . SER A 1 372 ? -113.006 34.182  285.853 1.00 32.89  ? 372 SER A CB  1 
ATOM   2807 O  OG  . SER A 1 372 ? -113.315 35.562  285.768 1.00 27.97  ? 372 SER A OG  1 
ATOM   2808 N  N   . LEU A 1 373 ? -113.707 31.106  284.808 1.00 28.37  ? 373 LEU A N   1 
ATOM   2809 C  CA  . LEU A 1 373 ? -113.393 29.687  284.871 1.00 26.27  ? 373 LEU A CA  1 
ATOM   2810 C  C   . LEU A 1 373 ? -113.544 29.052  283.497 1.00 25.04  ? 373 LEU A C   1 
ATOM   2811 O  O   . LEU A 1 373 ? -114.479 29.364  282.754 1.00 26.77  ? 373 LEU A O   1 
ATOM   2812 C  CB  . LEU A 1 373 ? -114.304 28.976  285.872 1.00 32.27  ? 373 LEU A CB  1 
ATOM   2813 C  CG  . LEU A 1 373 ? -114.178 29.388  287.338 1.00 29.90  ? 373 LEU A CG  1 
ATOM   2814 C  CD1 . LEU A 1 373 ? -115.182 28.630  288.190 1.00 24.09  ? 373 LEU A CD1 1 
ATOM   2815 C  CD2 . LEU A 1 373 ? -112.762 29.142  287.831 1.00 27.47  ? 373 LEU A CD2 1 
ATOM   2816 N  N   . GLY A 1 374 ? -112.617 28.161  283.162 1.00 29.20  ? 374 GLY A N   1 
ATOM   2817 C  CA  . GLY A 1 374 ? -112.710 27.423  281.920 1.00 32.19  ? 374 GLY A CA  1 
ATOM   2818 C  C   . GLY A 1 374 ? -113.525 26.159  282.087 1.00 29.73  ? 374 GLY A C   1 
ATOM   2819 O  O   . GLY A 1 374 ? -114.211 25.719  281.160 1.00 41.73  ? 374 GLY A O   1 
ATOM   2820 N  N   . LYS A 1 375 ? -113.456 25.570  283.279 1.00 30.01  ? 375 LYS A N   1 
ATOM   2821 C  CA  . LYS A 1 375 ? -114.191 24.357  283.599 1.00 34.10  ? 375 LYS A CA  1 
ATOM   2822 C  C   . LYS A 1 375 ? -114.606 24.409  285.061 1.00 32.06  ? 375 LYS A C   1 
ATOM   2823 O  O   . LYS A 1 375 ? -113.971 25.082  285.877 1.00 29.96  ? 375 LYS A O   1 
ATOM   2824 C  CB  . LYS A 1 375 ? -113.355 23.099  283.327 1.00 31.49  ? 375 LYS A CB  1 
ATOM   2825 C  CG  . LYS A 1 375 ? -113.174 22.776  281.853 1.00 36.03  ? 375 LYS A CG  1 
ATOM   2826 C  CD  . LYS A 1 375 ? -112.141 21.685  281.647 1.00 43.21  ? 375 LYS A CD  1 
ATOM   2827 C  CE  . LYS A 1 375 ? -110.744 22.273  281.547 1.00 50.50  ? 375 LYS A CE  1 
ATOM   2828 N  NZ  . LYS A 1 375 ? -110.638 23.267  280.444 1.00 48.15  ? 375 LYS A NZ  1 
ATOM   2829 N  N   . ILE A 1 376 ? -115.679 23.691  285.384 1.00 30.58  ? 376 ILE A N   1 
ATOM   2830 C  CA  . ILE A 1 376 ? -116.209 23.627  286.741 1.00 27.79  ? 376 ILE A CA  1 
ATOM   2831 C  C   . ILE A 1 376 ? -116.293 22.164  287.146 1.00 26.11  ? 376 ILE A C   1 
ATOM   2832 O  O   . ILE A 1 376 ? -117.018 21.383  286.517 1.00 25.39  ? 376 ILE A O   1 
ATOM   2833 C  CB  . ILE A 1 376 ? -117.588 24.298  286.856 1.00 27.33  ? 376 ILE A CB  1 
ATOM   2834 C  CG1 . ILE A 1 376 ? -117.481 25.793  286.548 1.00 31.87  ? 376 ILE A CG1 1 
ATOM   2835 C  CG2 . ILE A 1 376 ? -118.171 24.075  288.240 1.00 23.55  ? 376 ILE A CG2 1 
ATOM   2836 C  CD1 . ILE A 1 376 ? -118.799 26.529  286.634 1.00 30.33  ? 376 ILE A CD1 1 
ATOM   2837 N  N   . PHE A 1 377 ? -115.558 21.793  288.191 1.00 22.08  ? 377 PHE A N   1 
ATOM   2838 C  CA  . PHE A 1 377 ? -115.550 20.421  288.694 1.00 22.26  ? 377 PHE A CA  1 
ATOM   2839 C  C   . PHE A 1 377 ? -116.645 20.290  289.745 1.00 26.85  ? 377 PHE A C   1 
ATOM   2840 O  O   . PHE A 1 377 ? -116.451 20.640  290.911 1.00 39.26  ? 377 PHE A O   1 
ATOM   2841 C  CB  . PHE A 1 377 ? -114.181 20.061  289.262 1.00 23.00  ? 377 PHE A CB  1 
ATOM   2842 C  CG  . PHE A 1 377 ? -113.083 20.063  288.239 1.00 22.21  ? 377 PHE A CG  1 
ATOM   2843 C  CD1 . PHE A 1 377 ? -113.079 19.140  287.206 1.00 22.12  ? 377 PHE A CD1 1 
ATOM   2844 C  CD2 . PHE A 1 377 ? -112.052 20.984  288.311 1.00 23.04  ? 377 PHE A CD2 1 
ATOM   2845 C  CE1 . PHE A 1 377 ? -112.070 19.138  286.263 1.00 24.73  ? 377 PHE A CE1 1 
ATOM   2846 C  CE2 . PHE A 1 377 ? -111.040 20.985  287.371 1.00 27.50  ? 377 PHE A CE2 1 
ATOM   2847 C  CZ  . PHE A 1 377 ? -111.049 20.062  286.346 1.00 31.23  ? 377 PHE A CZ  1 
ATOM   2848 N  N   . LEU A 1 378 ? -117.803 19.782  289.330 1.00 25.72  ? 378 LEU A N   1 
ATOM   2849 C  CA  . LEU A 1 378 ? -118.942 19.618  290.227 1.00 23.90  ? 378 LEU A CA  1 
ATOM   2850 C  C   . LEU A 1 378 ? -118.725 18.374  291.079 1.00 23.70  ? 378 LEU A C   1 
ATOM   2851 O  O   . LEU A 1 378 ? -118.849 17.247  290.588 1.00 23.91  ? 378 LEU A O   1 
ATOM   2852 C  CB  . LEU A 1 378 ? -120.237 19.522  289.427 1.00 23.43  ? 378 LEU A CB  1 
ATOM   2853 C  CG  . LEU A 1 378 ? -121.526 19.336  290.227 1.00 22.65  ? 378 LEU A CG  1 
ATOM   2854 C  CD1 . LEU A 1 378 ? -121.763 20.530  291.133 1.00 30.68  ? 378 LEU A CD1 1 
ATOM   2855 C  CD2 . LEU A 1 378 ? -122.707 19.124  289.294 1.00 22.23  ? 378 LEU A CD2 1 
ATOM   2856 N  N   . MET A 1 379 ? -118.401 18.575  292.356 1.00 22.51  ? 379 MET A N   1 
ATOM   2857 C  CA  . MET A 1 379 ? -118.124 17.471  293.275 1.00 22.64  ? 379 MET A CA  1 
ATOM   2858 C  C   . MET A 1 379 ? -119.438 16.778  293.624 1.00 26.28  ? 379 MET A C   1 
ATOM   2859 O  O   . MET A 1 379 ? -120.058 17.023  294.661 1.00 25.87  ? 379 MET A O   1 
ATOM   2860 C  CB  . MET A 1 379 ? -117.411 17.977  294.523 1.00 19.83  ? 379 MET A CB  1 
ATOM   2861 C  CG  . MET A 1 379 ? -115.990 18.450  294.274 1.00 16.47  ? 379 MET A CG  1 
ATOM   2862 S  SD  . MET A 1 379 ? -115.176 19.034  295.771 1.00 12.18  ? 379 MET A SD  1 
ATOM   2863 C  CE  . MET A 1 379 ? -116.274 20.355  296.270 1.00 26.88  ? 379 MET A CE  1 
ATOM   2864 N  N   . SER A 1 380 ? -119.864 15.886  292.733 1.00 25.79  ? 380 SER A N   1 
ATOM   2865 C  CA  . SER A 1 380 ? -121.121 15.157  292.902 1.00 23.72  ? 380 SER A CA  1 
ATOM   2866 C  C   . SER A 1 380 ? -120.896 13.874  293.706 1.00 24.68  ? 380 SER A C   1 
ATOM   2867 O  O   . SER A 1 380 ? -121.111 12.757  293.236 1.00 22.93  ? 380 SER A O   1 
ATOM   2868 C  CB  . SER A 1 380 ? -121.744 14.859  291.544 1.00 25.97  ? 380 SER A CB  1 
ATOM   2869 O  OG  . SER A 1 380 ? -120.876 14.071  290.749 1.00 23.26  ? 380 SER A OG  1 
ATOM   2870 N  N   . TYR A 1 381 ? -120.451 14.060  294.944 1.00 29.32  ? 381 TYR A N   1 
ATOM   2871 C  CA  . TYR A 1 381 ? -120.258 12.954  295.873 1.00 27.88  ? 381 TYR A CA  1 
ATOM   2872 C  C   . TYR A 1 381 ? -120.298 13.510  297.291 1.00 27.45  ? 381 TYR A C   1 
ATOM   2873 O  O   . TYR A 1 381 ? -120.500 14.709  297.503 1.00 43.62  ? 381 TYR A O   1 
ATOM   2874 C  CB  . TYR A 1 381 ? -118.951 12.204  295.589 1.00 25.31  ? 381 TYR A CB  1 
ATOM   2875 C  CG  . TYR A 1 381 ? -117.771 13.093  295.266 1.00 23.23  ? 381 TYR A CG  1 
ATOM   2876 C  CD1 . TYR A 1 381 ? -117.005 13.661  296.275 1.00 22.36  ? 381 TYR A CD1 1 
ATOM   2877 C  CD2 . TYR A 1 381 ? -117.416 13.354  293.949 1.00 22.93  ? 381 TYR A CD2 1 
ATOM   2878 C  CE1 . TYR A 1 381 ? -115.923 14.470  295.982 1.00 22.18  ? 381 TYR A CE1 1 
ATOM   2879 C  CE2 . TYR A 1 381 ? -116.337 14.162  293.646 1.00 22.66  ? 381 TYR A CE2 1 
ATOM   2880 C  CZ  . TYR A 1 381 ? -115.594 14.716  294.665 1.00 21.01  ? 381 TYR A CZ  1 
ATOM   2881 O  OH  . TYR A 1 381 ? -114.519 15.520  294.366 1.00 17.94  ? 381 TYR A OH  1 
ATOM   2882 N  N   . ASP A 1 382 ? -120.111 12.617  298.264 1.00 25.56  ? 382 ASP A N   1 
ATOM   2883 C  CA  . ASP A 1 382 ? -120.163 12.959  299.686 1.00 24.16  ? 382 ASP A CA  1 
ATOM   2884 C  C   . ASP A 1 382 ? -121.522 13.528  300.080 1.00 29.34  ? 382 ASP A C   1 
ATOM   2885 O  O   . ASP A 1 382 ? -121.623 14.346  300.998 1.00 40.79  ? 382 ASP A O   1 
ATOM   2886 C  CB  . ASP A 1 382 ? -119.042 13.930  300.068 1.00 26.17  ? 382 ASP A CB  1 
ATOM   2887 C  CG  . ASP A 1 382 ? -117.667 13.323  299.895 1.00 38.43  ? 382 ASP A CG  1 
ATOM   2888 O  OD1 . ASP A 1 382 ? -117.554 12.082  299.972 1.00 43.92  ? 382 ASP A OD1 1 
ATOM   2889 O  OD2 . ASP A 1 382 ? -116.699 14.081  299.678 1.00 32.32  ? 382 ASP A OD2 1 
ATOM   2890 N  N   . PHE A 1 383 ? -122.579 13.099  299.386 1.00 29.69  ? 383 PHE A N   1 
ATOM   2891 C  CA  . PHE A 1 383 ? -123.926 13.525  299.750 1.00 30.88  ? 383 PHE A CA  1 
ATOM   2892 C  C   . PHE A 1 383 ? -124.336 12.947  301.098 1.00 30.50  ? 383 PHE A C   1 
ATOM   2893 O  O   . PHE A 1 383 ? -124.936 13.644  301.925 1.00 26.13  ? 383 PHE A O   1 
ATOM   2894 C  CB  . PHE A 1 383 ? -124.919 13.108  298.666 1.00 33.43  ? 383 PHE A CB  1 
ATOM   2895 C  CG  . PHE A 1 383 ? -124.714 13.807  297.353 1.00 29.93  ? 383 PHE A CG  1 
ATOM   2896 C  CD1 . PHE A 1 383 ? -124.352 15.142  297.312 1.00 29.81  ? 383 PHE A CD1 1 
ATOM   2897 C  CD2 . PHE A 1 383 ? -124.875 13.125  296.158 1.00 32.01  ? 383 PHE A CD2 1 
ATOM   2898 C  CE1 . PHE A 1 383 ? -124.163 15.786  296.106 1.00 34.18  ? 383 PHE A CE1 1 
ATOM   2899 C  CE2 . PHE A 1 383 ? -124.687 13.764  294.948 1.00 31.64  ? 383 PHE A CE2 1 
ATOM   2900 C  CZ  . PHE A 1 383 ? -124.329 15.095  294.921 1.00 28.85  ? 383 PHE A CZ  1 
ATOM   2901 N  N   . LYS A 1 384 ? -124.026 11.675  301.334 1.00 33.12  ? 384 LYS A N   1 
ATOM   2902 C  CA  . LYS A 1 384 ? -124.297 11.012  302.599 1.00 31.60  ? 384 LYS A CA  1 
ATOM   2903 C  C   . LYS A 1 384 ? -123.022 10.337  303.081 1.00 32.86  ? 384 LYS A C   1 
ATOM   2904 O  O   . LYS A 1 384 ? -122.192 9.903   302.278 1.00 32.46  ? 384 LYS A O   1 
ATOM   2905 C  CB  . LYS A 1 384 ? -125.422 9.977   302.465 1.00 34.96  ? 384 LYS A CB  1 
ATOM   2906 C  CG  . LYS A 1 384 ? -126.709 10.525  301.869 1.00 40.98  ? 384 LYS A CG  1 
ATOM   2907 C  CD  . LYS A 1 384 ? -127.373 11.536  302.787 1.00 34.27  ? 384 LYS A CD  1 
ATOM   2908 C  CE  . LYS A 1 384 ? -128.733 11.951  302.250 1.00 29.32  ? 384 LYS A CE  1 
ATOM   2909 N  NZ  . LYS A 1 384 ? -128.658 12.409  300.835 1.00 39.81  ? 384 LYS A NZ  1 
ATOM   2910 N  N   . GLY A 1 385 ? -122.871 10.250  304.399 1.00 30.07  ? 385 GLY A N   1 
ATOM   2911 C  CA  . GLY A 1 385 ? -121.660 9.672   304.947 1.00 33.06  ? 385 GLY A CA  1 
ATOM   2912 C  C   . GLY A 1 385 ? -121.877 9.135   306.344 1.00 31.88  ? 385 GLY A C   1 
ATOM   2913 O  O   . GLY A 1 385 ? -122.976 9.199   306.900 1.00 29.72  ? 385 GLY A O   1 
ATOM   2914 N  N   . ALA A 1 386 ? -120.795 8.601   306.908 1.00 32.17  ? 386 ALA A N   1 
ATOM   2915 C  CA  . ALA A 1 386 ? -120.814 8.025   308.246 1.00 34.65  ? 386 ALA A CA  1 
ATOM   2916 C  C   . ALA A 1 386 ? -120.832 9.075   309.348 1.00 35.64  ? 386 ALA A C   1 
ATOM   2917 O  O   . ALA A 1 386 ? -120.840 8.708   310.528 1.00 41.99  ? 386 ALA A O   1 
ATOM   2918 C  CB  . ALA A 1 386 ? -119.609 7.101   308.436 1.00 37.62  ? 386 ALA A CB  1 
ATOM   2919 N  N   . TRP A 1 387 ? -120.833 10.363  309.001 1.00 35.38  ? 387 TRP A N   1 
ATOM   2920 C  CA  . TRP A 1 387 ? -120.916 11.411  310.009 1.00 36.87  ? 387 TRP A CA  1 
ATOM   2921 C  C   . TRP A 1 387 ? -122.287 11.486  310.666 1.00 35.30  ? 387 TRP A C   1 
ATOM   2922 O  O   . TRP A 1 387 ? -122.421 12.142  311.704 1.00 48.97  ? 387 TRP A O   1 
ATOM   2923 C  CB  . TRP A 1 387 ? -120.564 12.766  309.391 1.00 31.93  ? 387 TRP A CB  1 
ATOM   2924 C  CG  . TRP A 1 387 ? -121.290 13.056  308.113 1.00 34.16  ? 387 TRP A CG  1 
ATOM   2925 C  CD1 . TRP A 1 387 ? -122.574 13.496  307.981 1.00 34.59  ? 387 TRP A CD1 1 
ATOM   2926 C  CD2 . TRP A 1 387 ? -120.769 12.935  306.784 1.00 32.40  ? 387 TRP A CD2 1 
ATOM   2927 N  NE1 . TRP A 1 387 ? -122.888 13.652  306.653 1.00 38.37  ? 387 TRP A NE1 1 
ATOM   2928 C  CE2 . TRP A 1 387 ? -121.796 13.314  305.897 1.00 36.08  ? 387 TRP A CE2 1 
ATOM   2929 C  CE3 . TRP A 1 387 ? -119.536 12.541  306.257 1.00 31.83  ? 387 TRP A CE3 1 
ATOM   2930 C  CZ2 . TRP A 1 387 ? -121.628 13.311  304.514 1.00 34.09  ? 387 TRP A CZ2 1 
ATOM   2931 C  CZ3 . TRP A 1 387 ? -119.370 12.538  304.884 1.00 31.99  ? 387 TRP A CZ3 1 
ATOM   2932 C  CH2 . TRP A 1 387 ? -120.410 12.920  304.028 1.00 31.41  ? 387 TRP A CH2 1 
ATOM   2933 N  N   . SER A 1 388 ? -123.298 10.835  310.094 1.00 33.92  ? 388 SER A N   1 
ATOM   2934 C  CA  . SER A 1 388 ? -124.641 10.821  310.661 1.00 38.27  ? 388 SER A CA  1 
ATOM   2935 C  C   . SER A 1 388 ? -125.206 9.416   310.534 1.00 45.71  ? 388 SER A C   1 
ATOM   2936 O  O   . SER A 1 388 ? -125.424 8.933   309.419 1.00 48.91  ? 388 SER A O   1 
ATOM   2937 C  CB  . SER A 1 388 ? -125.552 11.831  309.958 1.00 59.13  ? 388 SER A CB  1 
ATOM   2938 O  OG  . SER A 1 388 ? -126.880 11.745  310.446 1.00 38.45  ? 388 SER A OG  1 
ATOM   2939 N  N   . ASN A 1 389 ? -125.439 8.763   311.674 1.00 35.83  ? 389 ASN A N   1 
ATOM   2940 C  CA  . ASN A 1 389 ? -126.042 7.437   311.667 1.00 34.11  ? 389 ASN A CA  1 
ATOM   2941 C  C   . ASN A 1 389 ? -127.529 7.471   311.343 1.00 32.97  ? 389 ASN A C   1 
ATOM   2942 O  O   . ASN A 1 389 ? -128.108 6.416   311.062 1.00 33.53  ? 389 ASN A O   1 
ATOM   2943 C  CB  . ASN A 1 389 ? -125.825 6.754   313.018 1.00 36.41  ? 389 ASN A CB  1 
ATOM   2944 C  CG  . ASN A 1 389 ? -124.364 6.465   313.296 1.00 41.05  ? 389 ASN A CG  1 
ATOM   2945 O  OD1 . ASN A 1 389 ? -123.529 6.502   312.392 1.00 47.08  ? 389 ASN A OD1 1 
ATOM   2946 N  ND2 . ASN A 1 389 ? -124.046 6.174   314.552 1.00 48.70  ? 389 ASN A ND2 1 
ATOM   2947 N  N   . THR A 1 390 ? -128.155 8.646   311.374 1.00 32.36  ? 390 THR A N   1 
ATOM   2948 C  CA  . THR A 1 390 ? -129.579 8.774   311.081 1.00 32.98  ? 390 THR A CA  1 
ATOM   2949 C  C   . THR A 1 390 ? -129.830 8.939   309.585 1.00 31.21  ? 390 THR A C   1 
ATOM   2950 O  O   . THR A 1 390 ? -130.572 8.158   308.981 1.00 32.53  ? 390 THR A O   1 
ATOM   2951 C  CB  . THR A 1 390 ? -130.169 9.959   311.854 1.00 30.89  ? 390 THR A CB  1 
ATOM   2952 O  OG1 . THR A 1 390 ? -129.521 11.170  311.443 1.00 39.85  ? 390 THR A OG1 1 
ATOM   2953 C  CG2 . THR A 1 390 ? -129.973 9.770   313.350 1.00 34.40  ? 390 THR A CG2 1 
ATOM   2954 N  N   . ASP A 1 391 ? -129.214 9.952   308.976 1.00 33.65  ? 391 ASP A N   1 
ATOM   2955 C  CA  . ASP A 1 391 ? -129.429 10.261  307.563 1.00 35.93  ? 391 ASP A CA  1 
ATOM   2956 C  C   . ASP A 1 391 ? -128.637 9.269   306.715 1.00 33.28  ? 391 ASP A C   1 
ATOM   2957 O  O   . ASP A 1 391 ? -127.527 9.537   306.248 1.00 37.22  ? 391 ASP A O   1 
ATOM   2958 C  CB  . ASP A 1 391 ? -129.033 11.701  307.264 1.00 47.25  ? 391 ASP A CB  1 
ATOM   2959 C  CG  . ASP A 1 391 ? -129.316 12.099  305.827 1.00 33.22  ? 391 ASP A CG  1 
ATOM   2960 O  OD1 . ASP A 1 391 ? -130.084 11.385  305.149 1.00 30.63  ? 391 ASP A OD1 1 
ATOM   2961 O  OD2 . ASP A 1 391 ? -128.770 13.128  305.376 1.00 32.65  ? 391 ASP A OD2 1 
ATOM   2962 N  N   . LEU A 1 392 ? -129.229 8.095   306.516 1.00 29.71  ? 392 LEU A N   1 
ATOM   2963 C  CA  . LEU A 1 392 ? -128.661 7.089   305.632 1.00 30.31  ? 392 LEU A CA  1 
ATOM   2964 C  C   . LEU A 1 392 ? -129.158 7.313   304.210 1.00 35.15  ? 392 LEU A C   1 
ATOM   2965 O  O   . LEU A 1 392 ? -130.339 7.595   303.989 1.00 37.34  ? 392 LEU A O   1 
ATOM   2966 C  CB  . LEU A 1 392 ? -129.028 5.679   306.098 1.00 34.77  ? 392 LEU A CB  1 
ATOM   2967 C  CG  . LEU A 1 392 ? -128.673 5.292   307.535 1.00 31.89  ? 392 LEU A CG  1 
ATOM   2968 C  CD1 . LEU A 1 392 ? -128.884 3.802   307.752 1.00 33.86  ? 392 LEU A CD1 1 
ATOM   2969 C  CD2 . LEU A 1 392 ? -127.242 5.684   307.864 1.00 32.40  ? 392 LEU A CD2 1 
ATOM   2970 N  N   . GLY A 1 393 ? -128.251 7.190   303.251 1.00 33.13  ? 393 GLY A N   1 
ATOM   2971 C  CA  . GLY A 1 393 ? -128.618 7.394   301.864 1.00 31.18  ? 393 GLY A CA  1 
ATOM   2972 C  C   . GLY A 1 393 ? -127.446 7.119   300.951 1.00 32.42  ? 393 GLY A C   1 
ATOM   2973 O  O   . GLY A 1 393 ? -126.436 6.542   301.359 1.00 40.75  ? 393 GLY A O   1 
ATOM   2974 N  N   . TYR A 1 394 ? -127.597 7.544   299.700 1.00 33.09  ? 394 TYR A N   1 
ATOM   2975 C  CA  . TYR A 1 394 ? -126.558 7.345   298.699 1.00 30.14  ? 394 TYR A CA  1 
ATOM   2976 C  C   . TYR A 1 394 ? -125.511 8.447   298.805 1.00 31.04  ? 394 TYR A C   1 
ATOM   2977 O  O   . TYR A 1 394 ? -125.840 9.636   298.755 1.00 42.60  ? 394 TYR A O   1 
ATOM   2978 C  CB  . TYR A 1 394 ? -127.161 7.324   297.295 1.00 29.10  ? 394 TYR A CB  1 
ATOM   2979 C  CG  . TYR A 1 394 ? -128.089 6.158   297.028 1.00 34.20  ? 394 TYR A CG  1 
ATOM   2980 C  CD1 . TYR A 1 394 ? -128.110 5.050   297.867 1.00 34.10  ? 394 TYR A CD1 1 
ATOM   2981 C  CD2 . TYR A 1 394 ? -128.942 6.164   295.932 1.00 30.61  ? 394 TYR A CD2 1 
ATOM   2982 C  CE1 . TYR A 1 394 ? -128.956 3.985   297.623 1.00 30.82  ? 394 TYR A CE1 1 
ATOM   2983 C  CE2 . TYR A 1 394 ? -129.791 5.103   295.680 1.00 28.19  ? 394 TYR A CE2 1 
ATOM   2984 C  CZ  . TYR A 1 394 ? -129.793 4.017   296.529 1.00 28.67  ? 394 TYR A CZ  1 
ATOM   2985 O  OH  . TYR A 1 394 ? -130.637 2.958   296.281 1.00 28.63  ? 394 TYR A OH  1 
ATOM   2986 N  N   . GLN A 1 395 ? -124.246 8.046   298.955 1.00 33.57  ? 395 GLN A N   1 
ATOM   2987 C  CA  . GLN A 1 395 ? -123.161 9.021   298.991 1.00 29.34  ? 395 GLN A CA  1 
ATOM   2988 C  C   . GLN A 1 395 ? -123.032 9.746   297.658 1.00 37.20  ? 395 GLN A C   1 
ATOM   2989 O  O   . GLN A 1 395 ? -122.803 10.960  297.620 1.00 38.97  ? 395 GLN A O   1 
ATOM   2990 C  CB  . GLN A 1 395 ? -121.850 8.327   299.359 1.00 29.52  ? 395 GLN A CB  1 
ATOM   2991 C  CG  . GLN A 1 395 ? -120.607 9.004   298.810 1.00 32.10  ? 395 GLN A CG  1 
ATOM   2992 C  CD  . GLN A 1 395 ? -119.438 8.050   298.679 1.00 44.49  ? 395 GLN A CD  1 
ATOM   2993 O  OE1 . GLN A 1 395 ? -119.178 7.243   299.570 1.00 57.15  ? 395 GLN A OE1 1 
ATOM   2994 N  NE2 . GLN A 1 395 ? -118.726 8.139   297.563 1.00 48.02  ? 395 GLN A NE2 1 
ATOM   2995 N  N   . THR A 1 396 ? -123.180 9.018   296.554 1.00 32.99  ? 396 THR A N   1 
ATOM   2996 C  CA  . THR A 1 396 ? -123.157 9.601   295.222 1.00 27.63  ? 396 THR A CA  1 
ATOM   2997 C  C   . THR A 1 396 ? -124.213 8.922   294.364 1.00 26.80  ? 396 THR A C   1 
ATOM   2998 O  O   . THR A 1 396 ? -124.392 7.702   294.434 1.00 29.34  ? 396 THR A O   1 
ATOM   2999 C  CB  . THR A 1 396 ? -121.774 9.469   294.569 1.00 28.72  ? 396 THR A CB  1 
ATOM   3000 O  OG1 . THR A 1 396 ? -121.853 9.860   293.192 1.00 27.03  ? 396 THR A OG1 1 
ATOM   3001 C  CG2 . THR A 1 396 ? -121.263 8.039   294.665 1.00 27.36  ? 396 THR A CG2 1 
ATOM   3002 N  N   . THR A 1 397 ? -124.914 9.719   293.564 1.00 26.52  ? 397 THR A N   1 
ATOM   3003 C  CA  . THR A 1 397 ? -125.993 9.216   292.724 1.00 26.32  ? 397 THR A CA  1 
ATOM   3004 C  C   . THR A 1 397 ? -126.331 10.272  291.685 1.00 27.37  ? 397 THR A C   1 
ATOM   3005 O  O   . THR A 1 397 ? -126.089 11.465  291.886 1.00 27.82  ? 397 THR A O   1 
ATOM   3006 C  CB  . THR A 1 397 ? -127.237 8.866   293.548 1.00 25.16  ? 397 THR A CB  1 
ATOM   3007 O  OG1 . THR A 1 397 ? -128.333 8.590   292.667 1.00 28.87  ? 397 THR A OG1 1 
ATOM   3008 C  CG2 . THR A 1 397 ? -127.610 10.019  294.464 1.00 28.27  ? 397 THR A CG2 1 
ATOM   3009 N  N   . VAL A 1 398 ? -126.898 9.816   290.570 1.00 26.65  ? 398 VAL A N   1 
ATOM   3010 C  CA  . VAL A 1 398 ? -127.353 10.736  289.531 1.00 28.47  ? 398 VAL A CA  1 
ATOM   3011 C  C   . VAL A 1 398 ? -128.734 11.280  289.868 1.00 38.93  ? 398 VAL A C   1 
ATOM   3012 O  O   . VAL A 1 398 ? -128.937 12.496  289.962 1.00 42.40  ? 398 VAL A O   1 
ATOM   3013 C  CB  . VAL A 1 398 ? -127.345 10.044  288.157 1.00 26.91  ? 398 VAL A CB  1 
ATOM   3014 C  CG1 . VAL A 1 398 ? -127.721 11.034  287.066 1.00 31.78  ? 398 VAL A CG1 1 
ATOM   3015 C  CG2 . VAL A 1 398 ? -125.985 9.438   287.882 1.00 38.92  ? 398 VAL A CG2 1 
ATOM   3016 N  N   . TYR A 1 399 ? -129.699 10.389  290.060 1.00 33.97  ? 399 TYR A N   1 
ATOM   3017 C  CA  . TYR A 1 399 ? -131.074 10.757  290.360 1.00 33.47  ? 399 TYR A CA  1 
ATOM   3018 C  C   . TYR A 1 399 ? -131.408 10.386  291.802 1.00 30.20  ? 399 TYR A C   1 
ATOM   3019 O  O   . TYR A 1 399 ? -130.568 9.882   292.554 1.00 29.00  ? 399 TYR A O   1 
ATOM   3020 C  CB  . TYR A 1 399 ? -132.033 10.085  289.375 1.00 39.62  ? 399 TYR A CB  1 
ATOM   3021 C  CG  . TYR A 1 399 ? -131.771 10.452  287.932 1.00 33.10  ? 399 TYR A CG  1 
ATOM   3022 C  CD1 . TYR A 1 399 ? -132.141 11.693  287.433 1.00 33.34  ? 399 TYR A CD1 1 
ATOM   3023 C  CD2 . TYR A 1 399 ? -131.152 9.557   287.070 1.00 33.35  ? 399 TYR A CD2 1 
ATOM   3024 C  CE1 . TYR A 1 399 ? -131.902 12.033  286.115 1.00 36.00  ? 399 TYR A CE1 1 
ATOM   3025 C  CE2 . TYR A 1 399 ? -130.910 9.888   285.750 1.00 36.74  ? 399 TYR A CE2 1 
ATOM   3026 C  CZ  . TYR A 1 399 ? -131.285 11.127  285.278 1.00 39.19  ? 399 TYR A CZ  1 
ATOM   3027 O  OH  . TYR A 1 399 ? -131.047 11.460  283.965 1.00 38.13  ? 399 TYR A OH  1 
ATOM   3028 N  N   . ALA A 1 400 ? -132.656 10.643  292.183 1.00 27.47  ? 400 ALA A N   1 
ATOM   3029 C  CA  . ALA A 1 400 ? -133.108 10.388  293.540 1.00 25.55  ? 400 ALA A CA  1 
ATOM   3030 C  C   . ALA A 1 400 ? -133.335 8.894   293.763 1.00 25.43  ? 400 ALA A C   1 
ATOM   3031 O  O   . ALA A 1 400 ? -133.735 8.176   292.842 1.00 24.70  ? 400 ALA A O   1 
ATOM   3032 C  CB  . ALA A 1 400 ? -134.396 11.153  293.822 1.00 34.25  ? 400 ALA A CB  1 
ATOM   3033 N  N   . PRO A 1 401 ? -133.088 8.405   294.979 1.00 26.41  ? 401 PRO A N   1 
ATOM   3034 C  CA  . PRO A 1 401 ? -133.226 6.968   295.245 1.00 31.90  ? 401 PRO A CA  1 
ATOM   3035 C  C   . PRO A 1 401 ? -134.642 6.469   294.996 1.00 46.25  ? 401 PRO A C   1 
ATOM   3036 O  O   . PRO A 1 401 ? -135.607 7.236   294.939 1.00 34.18  ? 401 PRO A O   1 
ATOM   3037 C  CB  . PRO A 1 401 ? -132.850 6.844   296.727 1.00 27.52  ? 401 PRO A CB  1 
ATOM   3038 C  CG  . PRO A 1 401 ? -132.001 8.034   297.002 1.00 25.48  ? 401 PRO A CG  1 
ATOM   3039 C  CD  . PRO A 1 401 ? -132.552 9.132   296.143 1.00 23.44  ? 401 PRO A CD  1 
ATOM   3040 N  N   . SER A 1 402 ? -134.755 5.147   294.844 1.00 47.37  ? 402 SER A N   1 
ATOM   3041 C  CA  . SER A 1 402 ? -136.061 4.535   294.627 1.00 34.60  ? 402 SER A CA  1 
ATOM   3042 C  C   . SER A 1 402 ? -136.945 4.647   295.862 1.00 29.59  ? 402 SER A C   1 
ATOM   3043 O  O   . SER A 1 402 ? -138.169 4.768   295.738 1.00 31.16  ? 402 SER A O   1 
ATOM   3044 C  CB  . SER A 1 402 ? -135.893 3.070   294.224 1.00 29.59  ? 402 SER A CB  1 
ATOM   3045 O  OG  . SER A 1 402 ? -135.147 2.953   293.026 1.00 30.78  ? 402 SER A OG  1 
ATOM   3046 N  N   . TRP A 1 403 ? -136.351 4.610   297.051 1.00 30.79  ? 403 TRP A N   1 
ATOM   3047 C  CA  . TRP A 1 403 ? -137.084 4.727   298.303 1.00 28.49  ? 403 TRP A CA  1 
ATOM   3048 C  C   . TRP A 1 403 ? -137.275 6.171   298.750 1.00 30.10  ? 403 TRP A C   1 
ATOM   3049 O  O   . TRP A 1 403 ? -137.821 6.402   299.833 1.00 29.63  ? 403 TRP A O   1 
ATOM   3050 C  CB  . TRP A 1 403 ? -136.369 3.929   299.399 1.00 31.38  ? 403 TRP A CB  1 
ATOM   3051 C  CG  . TRP A 1 403 ? -134.875 4.024   299.322 1.00 32.42  ? 403 TRP A CG  1 
ATOM   3052 C  CD1 . TRP A 1 403 ? -134.035 3.179   298.656 1.00 33.30  ? 403 TRP A CD1 1 
ATOM   3053 C  CD2 . TRP A 1 403 ? -134.045 5.021   299.927 1.00 31.84  ? 403 TRP A CD2 1 
ATOM   3054 N  NE1 . TRP A 1 403 ? -132.733 3.588   298.810 1.00 34.10  ? 403 TRP A NE1 1 
ATOM   3055 C  CE2 . TRP A 1 403 ? -132.712 4.716   299.587 1.00 32.20  ? 403 TRP A CE2 1 
ATOM   3056 C  CE3 . TRP A 1 403 ? -134.298 6.141   300.724 1.00 32.67  ? 403 TRP A CE3 1 
ATOM   3057 C  CZ2 . TRP A 1 403 ? -131.637 5.490   300.015 1.00 33.84  ? 403 TRP A CZ2 1 
ATOM   3058 C  CZ3 . TRP A 1 403 ? -133.229 6.907   301.149 1.00 31.99  ? 403 TRP A CZ3 1 
ATOM   3059 C  CH2 . TRP A 1 403 ? -131.916 6.579   300.794 1.00 35.36  ? 403 TRP A CH2 1 
ATOM   3060 N  N   . ASN A 1 404 ? -136.840 7.143   297.943 1.00 28.43  ? 404 ASN A N   1 
ATOM   3061 C  CA  . ASN A 1 404 ? -137.048 8.558   298.253 1.00 28.57  ? 404 ASN A CA  1 
ATOM   3062 C  C   . ASN A 1 404 ? -136.850 9.320   296.942 1.00 30.78  ? 404 ASN A C   1 
ATOM   3063 O  O   . ASN A 1 404 ? -135.712 9.596   296.554 1.00 32.97  ? 404 ASN A O   1 
ATOM   3064 C  CB  . ASN A 1 404 ? -136.093 9.037   299.334 1.00 29.40  ? 404 ASN A CB  1 
ATOM   3065 C  CG  . ASN A 1 404 ? -136.306 10.493  299.698 1.00 39.36  ? 404 ASN A CG  1 
ATOM   3066 O  OD1 . ASN A 1 404 ? -135.902 11.395  298.964 1.00 36.47  ? 404 ASN A OD1 1 
ATOM   3067 N  ND2 . ASN A 1 404 ? -136.946 10.729  300.837 1.00 58.29  ? 404 ASN A ND2 1 
ATOM   3068 N  N   . SER A 1 405 ? -137.956 9.654   296.281 1.00 32.29  ? 405 SER A N   1 
ATOM   3069 C  CA  . SER A 1 405 ? -137.928 10.104  294.895 1.00 38.58  ? 405 SER A CA  1 
ATOM   3070 C  C   . SER A 1 405 ? -137.675 11.600  294.739 1.00 36.28  ? 405 SER A C   1 
ATOM   3071 O  O   . SER A 1 405 ? -137.812 12.120  293.626 1.00 37.85  ? 405 SER A O   1 
ATOM   3072 C  CB  . SER A 1 405 ? -139.235 9.727   294.194 1.00 73.99  ? 405 SER A CB  1 
ATOM   3073 O  OG  . SER A 1 405 ? -139.424 10.505  293.025 1.00 62.34  ? 405 SER A OG  1 
ATOM   3074 N  N   . GLU A 1 406 ? -137.314 12.305  295.805 1.00 35.08  ? 406 GLU A N   1 
ATOM   3075 C  CA  . GLU A 1 406 ? -136.828 13.673  295.653 1.00 37.47  ? 406 GLU A CA  1 
ATOM   3076 C  C   . GLU A 1 406 ? -135.840 14.007  296.769 1.00 33.80  ? 406 GLU A C   1 
ATOM   3077 O  O   . GLU A 1 406 ? -136.045 14.905  297.584 1.00 44.74  ? 406 GLU A O   1 
ATOM   3078 C  CB  . GLU A 1 406 ? -137.973 14.683  295.605 1.00 43.68  ? 406 GLU A CB  1 
ATOM   3079 C  CG  . GLU A 1 406 ? -137.563 15.972  294.892 1.00 51.71  ? 406 GLU A CG  1 
ATOM   3080 C  CD  . GLU A 1 406 ? -138.607 17.067  294.968 1.00 76.05  ? 406 GLU A CD  1 
ATOM   3081 O  OE1 . GLU A 1 406 ? -139.639 16.866  295.640 1.00 92.07  ? 406 GLU A OE1 1 
ATOM   3082 O  OE2 . GLU A 1 406 ? -138.386 18.137  294.359 1.00 57.10  ? 406 GLU A OE2 1 
ATOM   3083 N  N   . GLU A 1 407 ? -134.738 13.267  296.817 1.00 30.29  ? 407 GLU A N   1 
ATOM   3084 C  CA  . GLU A 1 407 ? -133.552 13.749  297.509 1.00 26.11  ? 407 GLU A CA  1 
ATOM   3085 C  C   . GLU A 1 407 ? -132.906 14.827  296.651 1.00 24.93  ? 407 GLU A C   1 
ATOM   3086 O  O   . GLU A 1 407 ? -132.583 14.587  295.483 1.00 24.69  ? 407 GLU A O   1 
ATOM   3087 C  CB  . GLU A 1 407 ? -132.579 12.603  297.769 1.00 25.71  ? 407 GLU A CB  1 
ATOM   3088 C  CG  . GLU A 1 407 ? -131.321 13.011  298.521 1.00 23.27  ? 407 GLU A CG  1 
ATOM   3089 C  CD  . GLU A 1 407 ? -131.611 13.525  299.918 1.00 23.57  ? 407 GLU A CD  1 
ATOM   3090 O  OE1 . GLU A 1 407 ? -132.315 12.826  300.675 1.00 27.38  ? 407 GLU A OE1 1 
ATOM   3091 O  OE2 . GLU A 1 407 ? -131.129 14.626  300.258 1.00 21.05  ? 407 GLU A OE2 1 
ATOM   3092 N  N   . LEU A 1 408 ? -132.745 16.023  297.209 1.00 24.39  ? 408 LEU A N   1 
ATOM   3093 C  CA  . LEU A 1 408 ? -132.178 17.116  296.433 1.00 24.04  ? 408 LEU A CA  1 
ATOM   3094 C  C   . LEU A 1 408 ? -130.659 17.062  296.360 1.00 22.96  ? 408 LEU A C   1 
ATOM   3095 O  O   . LEU A 1 408 ? -130.063 17.846  295.614 1.00 22.04  ? 408 LEU A O   1 
ATOM   3096 C  CB  . LEU A 1 408 ? -132.635 18.457  297.009 1.00 26.78  ? 408 LEU A CB  1 
ATOM   3097 C  CG  . LEU A 1 408 ? -134.155 18.634  297.012 1.00 26.83  ? 408 LEU A CG  1 
ATOM   3098 C  CD1 . LEU A 1 408 ? -134.599 19.558  298.135 1.00 43.63  ? 408 LEU A CD1 1 
ATOM   3099 C  CD2 . LEU A 1 408 ? -134.643 19.140  295.663 1.00 27.78  ? 408 LEU A CD2 1 
ATOM   3100 N  N   . TYR A 1 409 ? -130.025 16.156  297.104 1.00 21.59  ? 409 TYR A N   1 
ATOM   3101 C  CA  . TYR A 1 409 ? -128.580 15.943  297.014 1.00 22.66  ? 409 TYR A CA  1 
ATOM   3102 C  C   . TYR A 1 409 ? -128.293 14.847  295.987 1.00 26.56  ? 409 TYR A C   1 
ATOM   3103 O  O   . TYR A 1 409 ? -127.919 13.718  296.309 1.00 28.43  ? 409 TYR A O   1 
ATOM   3104 C  CB  . TYR A 1 409 ? -128.005 15.593  298.380 1.00 23.75  ? 409 TYR A CB  1 
ATOM   3105 C  CG  . TYR A 1 409 ? -127.464 16.775  299.151 1.00 27.66  ? 409 TYR A CG  1 
ATOM   3106 C  CD1 . TYR A 1 409 ? -127.778 18.076  298.780 1.00 30.66  ? 409 TYR A CD1 1 
ATOM   3107 C  CD2 . TYR A 1 409 ? -126.629 16.589  300.244 1.00 27.42  ? 409 TYR A CD2 1 
ATOM   3108 C  CE1 . TYR A 1 409 ? -127.281 19.157  299.484 1.00 36.10  ? 409 TYR A CE1 1 
ATOM   3109 C  CE2 . TYR A 1 409 ? -126.127 17.663  300.952 1.00 33.84  ? 409 TYR A CE2 1 
ATOM   3110 C  CZ  . TYR A 1 409 ? -126.455 18.945  300.568 1.00 34.73  ? 409 TYR A CZ  1 
ATOM   3111 O  OH  . TYR A 1 409 ? -125.957 20.018  301.271 1.00 37.18  ? 409 TYR A OH  1 
ATOM   3112 N  N   . THR A 1 410 ? -128.494 15.203  294.721 1.00 25.72  ? 410 THR A N   1 
ATOM   3113 C  CA  . THR A 1 410 ? -128.206 14.317  293.603 1.00 26.06  ? 410 THR A CA  1 
ATOM   3114 C  C   . THR A 1 410 ? -127.423 15.070  292.539 1.00 31.22  ? 410 THR A C   1 
ATOM   3115 O  O   . THR A 1 410 ? -127.392 16.303  292.512 1.00 46.04  ? 410 THR A O   1 
ATOM   3116 C  CB  . THR A 1 410 ? -129.482 13.735  292.975 1.00 28.44  ? 410 THR A CB  1 
ATOM   3117 O  OG1 . THR A 1 410 ? -130.234 14.784  292.349 1.00 28.13  ? 410 THR A OG1 1 
ATOM   3118 C  CG2 . THR A 1 410 ? -130.334 13.028  294.019 1.00 39.68  ? 410 THR A CG2 1 
ATOM   3119 N  N   . THR A 1 411 ? -126.786 14.300  291.654 1.00 32.56  ? 411 THR A N   1 
ATOM   3120 C  CA  . THR A 1 411 ? -126.052 14.902  290.546 1.00 29.81  ? 411 THR A CA  1 
ATOM   3121 C  C   . THR A 1 411 ? -126.992 15.642  289.605 1.00 31.92  ? 411 THR A C   1 
ATOM   3122 O  O   . THR A 1 411 ? -126.641 16.700  289.070 1.00 35.51  ? 411 THR A O   1 
ATOM   3123 C  CB  . THR A 1 411 ? -125.272 13.826  289.789 1.00 29.85  ? 411 THR A CB  1 
ATOM   3124 O  OG1 . THR A 1 411 ? -124.427 13.117  290.703 1.00 28.94  ? 411 THR A OG1 1 
ATOM   3125 C  CG2 . THR A 1 411 ? -124.417 14.451  288.698 1.00 28.05  ? 411 THR A CG2 1 
ATOM   3126 N  N   . HIS A 1 412 ? -128.199 15.109  289.403 1.00 38.54  ? 412 HIS A N   1 
ATOM   3127 C  CA  . HIS A 1 412 ? -129.143 15.733  288.481 1.00 32.58  ? 412 HIS A CA  1 
ATOM   3128 C  C   . HIS A 1 412 ? -129.572 17.109  288.973 1.00 28.55  ? 412 HIS A C   1 
ATOM   3129 O  O   . HIS A 1 412 ? -129.544 18.088  288.218 1.00 33.15  ? 412 HIS A O   1 
ATOM   3130 C  CB  . HIS A 1 412 ? -130.361 14.832  288.283 1.00 43.97  ? 412 HIS A CB  1 
ATOM   3131 C  CG  . HIS A 1 412 ? -131.395 15.413  287.371 1.00 33.42  ? 412 HIS A CG  1 
ATOM   3132 N  ND1 . HIS A 1 412 ? -131.236 15.465  286.003 1.00 34.70  ? 412 HIS A ND1 1 
ATOM   3133 C  CD2 . HIS A 1 412 ? -132.600 15.972  287.631 1.00 35.91  ? 412 HIS A CD2 1 
ATOM   3134 C  CE1 . HIS A 1 412 ? -132.300 16.029  285.459 1.00 44.05  ? 412 HIS A CE1 1 
ATOM   3135 N  NE2 . HIS A 1 412 ? -133.143 16.345  286.426 1.00 49.13  ? 412 HIS A NE2 1 
ATOM   3136 N  N   . TYR A 1 413 ? -129.981 17.203  290.240 1.00 25.59  ? 413 TYR A N   1 
ATOM   3137 C  CA  . TYR A 1 413 ? -130.460 18.478  290.761 1.00 27.11  ? 413 TYR A CA  1 
ATOM   3138 C  C   . TYR A 1 413 ? -129.341 19.509  290.816 1.00 25.78  ? 413 TYR A C   1 
ATOM   3139 O  O   . TYR A 1 413 ? -129.575 20.701  290.582 1.00 24.76  ? 413 TYR A O   1 
ATOM   3140 C  CB  . TYR A 1 413 ? -131.079 18.280  292.144 1.00 26.93  ? 413 TYR A CB  1 
ATOM   3141 C  CG  . TYR A 1 413 ? -131.845 19.483  292.641 1.00 22.72  ? 413 TYR A CG  1 
ATOM   3142 C  CD1 . TYR A 1 413 ? -133.124 19.755  292.173 1.00 22.26  ? 413 TYR A CD1 1 
ATOM   3143 C  CD2 . TYR A 1 413 ? -131.293 20.344  293.577 1.00 27.06  ? 413 TYR A CD2 1 
ATOM   3144 C  CE1 . TYR A 1 413 ? -133.831 20.853  292.623 1.00 23.37  ? 413 TYR A CE1 1 
ATOM   3145 C  CE2 . TYR A 1 413 ? -131.992 21.444  294.033 1.00 32.30  ? 413 TYR A CE2 1 
ATOM   3146 C  CZ  . TYR A 1 413 ? -133.259 21.694  293.554 1.00 24.37  ? 413 TYR A CZ  1 
ATOM   3147 O  OH  . TYR A 1 413 ? -133.956 22.790  294.009 1.00 23.49  ? 413 TYR A OH  1 
ATOM   3148 N  N   . ALA A 1 414 ? -128.117 19.071  291.116 1.00 26.25  ? 414 ALA A N   1 
ATOM   3149 C  CA  . ALA A 1 414 ? -126.992 19.998  291.161 1.00 22.61  ? 414 ALA A CA  1 
ATOM   3150 C  C   . ALA A 1 414 ? -126.652 20.523  289.772 1.00 22.77  ? 414 ALA A C   1 
ATOM   3151 O  O   . ALA A 1 414 ? -126.313 21.701  289.614 1.00 23.31  ? 414 ALA A O   1 
ATOM   3152 C  CB  . ALA A 1 414 ? -125.777 19.321  291.791 1.00 24.27  ? 414 ALA A CB  1 
ATOM   3153 N  N   . VAL A 1 415 ? -126.735 19.663  288.754 1.00 22.93  ? 415 VAL A N   1 
ATOM   3154 C  CA  . VAL A 1 415 ? -126.455 20.099  287.387 1.00 24.54  ? 415 VAL A CA  1 
ATOM   3155 C  C   . VAL A 1 415 ? -127.483 21.132  286.942 1.00 27.13  ? 415 VAL A C   1 
ATOM   3156 O  O   . VAL A 1 415 ? -127.133 22.198  286.421 1.00 27.06  ? 415 VAL A O   1 
ATOM   3157 C  CB  . VAL A 1 415 ? -126.416 18.892  286.433 1.00 24.40  ? 415 VAL A CB  1 
ATOM   3158 C  CG1 . VAL A 1 415 ? -126.496 19.355  284.988 1.00 27.38  ? 415 VAL A CG1 1 
ATOM   3159 C  CG2 . VAL A 1 415 ? -125.148 18.086  286.656 1.00 25.24  ? 415 VAL A CG2 1 
ATOM   3160 N  N   . ASP A 1 416 ? -128.769 20.834  287.148 1.00 28.71  ? 416 ASP A N   1 
ATOM   3161 C  CA  . ASP A 1 416 ? -129.814 21.777  286.765 1.00 44.43  ? 416 ASP A CA  1 
ATOM   3162 C  C   . ASP A 1 416 ? -129.713 23.077  287.552 1.00 32.95  ? 416 ASP A C   1 
ATOM   3163 O  O   . ASP A 1 416 ? -130.036 24.148  287.023 1.00 38.23  ? 416 ASP A O   1 
ATOM   3164 C  CB  . ASP A 1 416 ? -131.193 21.145  286.960 1.00 29.96  ? 416 ASP A CB  1 
ATOM   3165 C  CG  . ASP A 1 416 ? -131.598 20.261  285.798 1.00 35.50  ? 416 ASP A CG  1 
ATOM   3166 O  OD1 . ASP A 1 416 ? -132.454 20.690  284.995 1.00 28.91  ? 416 ASP A OD1 1 
ATOM   3167 O  OD2 . ASP A 1 416 ? -131.060 19.139  285.687 1.00 46.27  ? 416 ASP A OD2 1 
ATOM   3168 N  N   . ALA A 1 417 ? -129.272 23.007  288.810 1.00 26.76  ? 417 ALA A N   1 
ATOM   3169 C  CA  . ALA A 1 417 ? -129.101 24.223  289.600 1.00 30.60  ? 417 ALA A CA  1 
ATOM   3170 C  C   . ALA A 1 417 ? -128.096 25.162  288.948 1.00 31.07  ? 417 ALA A C   1 
ATOM   3171 O  O   . ALA A 1 417 ? -128.305 26.381  288.914 1.00 30.03  ? 417 ALA A O   1 
ATOM   3172 C  CB  . ALA A 1 417 ? -128.667 23.870  291.022 1.00 28.68  ? 417 ALA A CB  1 
ATOM   3173 N  N   . LEU A 1 418 ? -126.999 24.614  288.422 1.00 27.88  ? 418 LEU A N   1 
ATOM   3174 C  CA  . LEU A 1 418 ? -126.060 25.430  287.662 1.00 25.88  ? 418 LEU A CA  1 
ATOM   3175 C  C   . LEU A 1 418 ? -126.688 25.924  286.366 1.00 31.51  ? 418 LEU A C   1 
ATOM   3176 O  O   . LEU A 1 418 ? -126.464 27.068  285.956 1.00 32.46  ? 418 LEU A O   1 
ATOM   3177 C  CB  . LEU A 1 418 ? -124.789 24.632  287.367 1.00 27.62  ? 418 LEU A CB  1 
ATOM   3178 C  CG  . LEU A 1 418 ? -123.903 24.252  288.552 1.00 27.73  ? 418 LEU A CG  1 
ATOM   3179 C  CD1 . LEU A 1 418 ? -122.773 23.347  288.094 1.00 23.92  ? 418 LEU A CD1 1 
ATOM   3180 C  CD2 . LEU A 1 418 ? -123.352 25.497  289.225 1.00 39.81  ? 418 LEU A CD2 1 
ATOM   3181 N  N   . LEU A 1 419 ? -127.486 25.075  285.711 1.00 31.60  ? 419 LEU A N   1 
ATOM   3182 C  CA  . LEU A 1 419 ? -128.081 25.448  284.432 1.00 33.67  ? 419 LEU A CA  1 
ATOM   3183 C  C   . LEU A 1 419 ? -129.073 26.593  284.592 1.00 38.39  ? 419 LEU A C   1 
ATOM   3184 O  O   . LEU A 1 419 ? -129.135 27.488  283.741 1.00 42.33  ? 419 LEU A O   1 
ATOM   3185 C  CB  . LEU A 1 419 ? -128.761 24.234  283.800 1.00 32.91  ? 419 LEU A CB  1 
ATOM   3186 C  CG  . LEU A 1 419 ? -127.846 23.068  283.423 1.00 30.14  ? 419 LEU A CG  1 
ATOM   3187 C  CD1 . LEU A 1 419 ? -128.653 21.913  282.854 1.00 30.60  ? 419 LEU A CD1 1 
ATOM   3188 C  CD2 . LEU A 1 419 ? -126.779 23.519  282.439 1.00 42.30  ? 419 LEU A CD2 1 
ATOM   3189 N  N   . LYS A 1 420 ? -129.859 26.578  285.672 1.00 35.45  ? 420 LYS A N   1 
ATOM   3190 C  CA  . LYS A 1 420 ? -130.813 27.657  285.909 1.00 41.16  ? 420 LYS A CA  1 
ATOM   3191 C  C   . LYS A 1 420 ? -130.108 28.998  286.068 1.00 40.99  ? 420 LYS A C   1 
ATOM   3192 O  O   . LYS A 1 420 ? -130.652 30.037  285.676 1.00 72.73  ? 420 LYS A O   1 
ATOM   3193 C  CB  . LYS A 1 420 ? -131.660 27.337  287.144 1.00 46.65  ? 420 LYS A CB  1 
ATOM   3194 C  CG  . LYS A 1 420 ? -132.407 28.523  287.742 1.00 72.46  ? 420 LYS A CG  1 
ATOM   3195 C  CD  . LYS A 1 420 ? -133.840 28.591  287.239 1.00 81.33  ? 420 LYS A CD  1 
ATOM   3196 C  CE  . LYS A 1 420 ? -134.667 29.586  288.041 1.00 59.05  ? 420 LYS A CE  1 
ATOM   3197 N  NZ  . LYS A 1 420 ? -134.292 30.995  287.743 1.00 54.24  ? 420 LYS A NZ  1 
ATOM   3198 N  N   . GLN A 1 421 ? -128.894 28.993  286.619 1.00 32.99  ? 421 GLN A N   1 
ATOM   3199 C  CA  . GLN A 1 421 ? -128.119 30.216  286.773 1.00 33.08  ? 421 GLN A CA  1 
ATOM   3200 C  C   . GLN A 1 421 ? -127.508 30.704  285.466 1.00 34.63  ? 421 GLN A C   1 
ATOM   3201 O  O   . GLN A 1 421 ? -126.996 31.827  285.424 1.00 50.21  ? 421 GLN A O   1 
ATOM   3202 C  CB  . GLN A 1 421 ? -127.010 30.006  287.806 1.00 27.88  ? 421 GLN A CB  1 
ATOM   3203 C  CG  . GLN A 1 421 ? -127.515 29.624  289.185 1.00 26.20  ? 421 GLN A CG  1 
ATOM   3204 C  CD  . GLN A 1 421 ? -126.435 29.705  290.243 1.00 22.54  ? 421 GLN A CD  1 
ATOM   3205 O  OE1 . GLN A 1 421 ? -125.374 30.286  290.019 1.00 20.12  ? 421 GLN A OE1 1 
ATOM   3206 N  NE2 . GLN A 1 421 ? -126.699 29.120  291.405 1.00 25.26  ? 421 GLN A NE2 1 
ATOM   3207 N  N   . GLY A 1 422 ? -127.550 29.901  284.409 1.00 33.49  ? 422 GLY A N   1 
ATOM   3208 C  CA  . GLY A 1 422 ? -126.952 30.265  283.144 1.00 35.22  ? 422 GLY A CA  1 
ATOM   3209 C  C   . GLY A 1 422 ? -125.601 29.648  282.866 1.00 37.01  ? 422 GLY A C   1 
ATOM   3210 O  O   . GLY A 1 422 ? -124.930 30.073  281.919 1.00 33.88  ? 422 GLY A O   1 
ATOM   3211 N  N   . VAL A 1 423 ? -125.179 28.664  283.660 1.00 30.25  ? 423 VAL A N   1 
ATOM   3212 C  CA  . VAL A 1 423 ? -123.890 28.021  283.444 1.00 29.14  ? 423 VAL A CA  1 
ATOM   3213 C  C   . VAL A 1 423 ? -123.958 27.169  282.186 1.00 27.23  ? 423 VAL A C   1 
ATOM   3214 O  O   . VAL A 1 423 ? -124.899 26.387  281.996 1.00 27.19  ? 423 VAL A O   1 
ATOM   3215 C  CB  . VAL A 1 423 ? -123.499 27.178  284.667 1.00 27.90  ? 423 VAL A CB  1 
ATOM   3216 C  CG1 . VAL A 1 423 ? -122.236 26.379  284.386 1.00 26.38  ? 423 VAL A CG1 1 
ATOM   3217 C  CG2 . VAL A 1 423 ? -123.319 28.066  285.884 1.00 27.50  ? 423 VAL A CG2 1 
ATOM   3218 N  N   . ASP A 1 424 ? -122.966 27.324  281.315 1.00 25.68  ? 424 ASP A N   1 
ATOM   3219 C  CA  . ASP A 1 424 ? -122.893 26.490  280.127 1.00 25.25  ? 424 ASP A CA  1 
ATOM   3220 C  C   . ASP A 1 424 ? -122.753 25.026  280.536 1.00 27.73  ? 424 ASP A C   1 
ATOM   3221 O  O   . ASP A 1 424 ? -122.061 24.718  281.514 1.00 26.53  ? 424 ASP A O   1 
ATOM   3222 C  CB  . ASP A 1 424 ? -121.709 26.899  279.249 1.00 28.15  ? 424 ASP A CB  1 
ATOM   3223 C  CG  . ASP A 1 424 ? -121.811 28.328  278.760 1.00 47.35  ? 424 ASP A CG  1 
ATOM   3224 O  OD1 . ASP A 1 424 ? -122.897 28.929  278.897 1.00 37.24  ? 424 ASP A OD1 1 
ATOM   3225 O  OD2 . ASP A 1 424 ? -120.804 28.850  278.237 1.00 48.53  ? 424 ASP A OD2 1 
ATOM   3226 N  N   . PRO A 1 425 ? -123.397 24.100  279.823 1.00 32.75  ? 425 PRO A N   1 
ATOM   3227 C  CA  . PRO A 1 425 ? -123.214 22.684  280.165 1.00 28.97  ? 425 PRO A CA  1 
ATOM   3228 C  C   . PRO A 1 425 ? -121.849 22.158  279.763 1.00 28.73  ? 425 PRO A C   1 
ATOM   3229 O  O   . PRO A 1 425 ? -121.345 21.228  280.404 1.00 30.91  ? 425 PRO A O   1 
ATOM   3230 C  CB  . PRO A 1 425 ? -124.351 21.981  279.408 1.00 29.84  ? 425 PRO A CB  1 
ATOM   3231 C  CG  . PRO A 1 425 ? -124.830 22.960  278.370 1.00 30.34  ? 425 PRO A CG  1 
ATOM   3232 C  CD  . PRO A 1 425 ? -124.146 24.283  278.569 1.00 29.55  ? 425 PRO A CD  1 
ATOM   3233 N  N   . ASN A 1 426 ? -121.227 22.740  278.735 1.00 31.22  ? 426 ASN A N   1 
ATOM   3234 C  CA  . ASN A 1 426 ? -119.884 22.333  278.339 1.00 32.42  ? 426 ASN A CA  1 
ATOM   3235 C  C   . ASN A 1 426 ? -118.856 22.579  279.434 1.00 28.93  ? 426 ASN A C   1 
ATOM   3236 O  O   . ASN A 1 426 ? -117.806 21.928  279.442 1.00 40.93  ? 426 ASN A O   1 
ATOM   3237 C  CB  . ASN A 1 426 ? -119.466 23.072  277.067 1.00 34.64  ? 426 ASN A CB  1 
ATOM   3238 C  CG  . ASN A 1 426 ? -119.921 22.365  275.806 1.00 52.79  ? 426 ASN A CG  1 
ATOM   3239 O  OD1 . ASN A 1 426 ? -120.758 21.463  275.852 1.00 55.35  ? 426 ASN A OD1 1 
ATOM   3240 N  ND2 . ASN A 1 426 ? -119.370 22.773  274.668 1.00 41.99  ? 426 ASN A ND2 1 
ATOM   3241 N  N   . LYS A 1 427 ? -119.131 23.499  280.353 1.00 26.72  ? 427 LYS A N   1 
ATOM   3242 C  CA  . LYS A 1 427 ? -118.202 23.844  281.418 1.00 27.09  ? 427 LYS A CA  1 
ATOM   3243 C  C   . LYS A 1 427 ? -118.455 23.064  282.701 1.00 26.62  ? 427 LYS A C   1 
ATOM   3244 O  O   . LYS A 1 427 ? -117.759 23.294  283.696 1.00 25.75  ? 427 LYS A O   1 
ATOM   3245 C  CB  . LYS A 1 427 ? -118.277 25.347  281.706 1.00 25.67  ? 427 LYS A CB  1 
ATOM   3246 C  CG  . LYS A 1 427 ? -118.123 26.210  280.463 1.00 30.41  ? 427 LYS A CG  1 
ATOM   3247 C  CD  . LYS A 1 427 ? -118.314 27.687  280.767 1.00 33.39  ? 427 LYS A CD  1 
ATOM   3248 C  CE  . LYS A 1 427 ? -116.989 28.383  281.028 1.00 35.39  ? 427 LYS A CE  1 
ATOM   3249 N  NZ  . LYS A 1 427 ? -116.294 27.866  282.237 1.00 72.49  ? 427 LYS A NZ  1 
ATOM   3250 N  N   . ILE A 1 428 ? -119.425 22.153  282.704 1.00 27.49  ? 428 ILE A N   1 
ATOM   3251 C  CA  . ILE A 1 428 ? -119.786 21.380  283.887 1.00 25.77  ? 428 ILE A CA  1 
ATOM   3252 C  C   . ILE A 1 428 ? -119.113 20.019  283.805 1.00 26.46  ? 428 ILE A C   1 
ATOM   3253 O  O   . ILE A 1 428 ? -119.237 19.316  282.794 1.00 30.62  ? 428 ILE A O   1 
ATOM   3254 C  CB  . ILE A 1 428 ? -121.311 21.232  284.012 1.00 23.26  ? 428 ILE A CB  1 
ATOM   3255 C  CG1 . ILE A 1 428 ? -121.977 22.607  284.090 1.00 24.67  ? 428 ILE A CG1 1 
ATOM   3256 C  CG2 . ILE A 1 428 ? -121.668 20.396  285.231 1.00 23.04  ? 428 ILE A CG2 1 
ATOM   3257 C  CD1 . ILE A 1 428 ? -123.486 22.551  284.138 1.00 27.80  ? 428 ILE A CD1 1 
ATOM   3258 N  N   . ILE A 1 429 ? -118.404 19.644  284.866 1.00 25.76  ? 429 ILE A N   1 
ATOM   3259 C  CA  . ILE A 1 429 ? -117.714 18.362  284.951 1.00 22.51  ? 429 ILE A CA  1 
ATOM   3260 C  C   . ILE A 1 429 ? -118.319 17.583  286.109 1.00 24.42  ? 429 ILE A C   1 
ATOM   3261 O  O   . ILE A 1 429 ? -118.315 18.056  287.252 1.00 25.30  ? 429 ILE A O   1 
ATOM   3262 C  CB  . ILE A 1 429 ? -116.199 18.539  285.138 1.00 21.11  ? 429 ILE A CB  1 
ATOM   3263 C  CG1 . ILE A 1 429 ? -115.635 19.473  284.066 1.00 23.05  ? 429 ILE A CG1 1 
ATOM   3264 C  CG2 . ILE A 1 429 ? -115.498 17.193  285.083 1.00 43.66  ? 429 ILE A CG2 1 
ATOM   3265 C  CD1 . ILE A 1 429 ? -115.843 18.980  282.654 1.00 23.59  ? 429 ILE A CD1 1 
ATOM   3266 N  N   . VAL A 1 430 ? -118.834 16.392  285.815 1.00 25.35  ? 430 VAL A N   1 
ATOM   3267 C  CA  . VAL A 1 430 ? -119.521 15.580  286.813 1.00 21.87  ? 430 VAL A CA  1 
ATOM   3268 C  C   . VAL A 1 430 ? -118.500 14.794  287.623 1.00 20.65  ? 430 VAL A C   1 
ATOM   3269 O  O   . VAL A 1 430 ? -117.532 14.251  287.078 1.00 20.06  ? 430 VAL A O   1 
ATOM   3270 C  CB  . VAL A 1 430 ? -120.543 14.651  286.134 1.00 21.37  ? 430 VAL A CB  1 
ATOM   3271 C  CG1 . VAL A 1 430 ? -121.088 13.631  287.120 1.00 29.14  ? 430 VAL A CG1 1 
ATOM   3272 C  CG2 . VAL A 1 430 ? -121.673 15.472  285.546 1.00 21.93  ? 430 VAL A CG2 1 
ATOM   3273 N  N   . GLY A 1 431 ? -118.717 14.732  288.936 1.00 25.42  ? 431 GLY A N   1 
ATOM   3274 C  CA  . GLY A 1 431 ? -117.781 14.082  289.833 1.00 24.71  ? 431 GLY A CA  1 
ATOM   3275 C  C   . GLY A 1 431 ? -118.067 12.604  289.999 1.00 21.50  ? 431 GLY A C   1 
ATOM   3276 O  O   . GLY A 1 431 ? -119.212 12.203  290.224 1.00 19.11  ? 431 GLY A O   1 
ATOM   3277 N  N   . VAL A 1 432 ? -117.016 11.797  289.890 1.00 24.32  ? 432 VAL A N   1 
ATOM   3278 C  CA  . VAL A 1 432 ? -117.081 10.359  290.116 1.00 27.12  ? 432 VAL A CA  1 
ATOM   3279 C  C   . VAL A 1 432 ? -116.342 10.056  291.409 1.00 26.37  ? 432 VAL A C   1 
ATOM   3280 O  O   . VAL A 1 432 ? -115.243 10.574  291.639 1.00 25.58  ? 432 VAL A O   1 
ATOM   3281 C  CB  . VAL A 1 432 ? -116.480 9.575   288.937 1.00 24.09  ? 432 VAL A CB  1 
ATOM   3282 C  CG1 . VAL A 1 432 ? -116.523 8.081   289.213 1.00 22.75  ? 432 VAL A CG1 1 
ATOM   3283 C  CG2 . VAL A 1 432 ? -117.219 9.905   287.655 1.00 23.24  ? 432 VAL A CG2 1 
ATOM   3284 N  N   . ALA A 1 433 ? -116.945 9.227   292.256 1.00 23.18  ? 433 ALA A N   1 
ATOM   3285 C  CA  . ALA A 1 433 ? -116.352 8.841   293.530 1.00 21.46  ? 433 ALA A CA  1 
ATOM   3286 C  C   . ALA A 1 433 ? -115.687 7.478   293.375 1.00 23.18  ? 433 ALA A C   1 
ATOM   3287 O  O   . ALA A 1 433 ? -116.369 6.451   293.288 1.00 30.02  ? 433 ALA A O   1 
ATOM   3288 C  CB  . ALA A 1 433 ? -117.404 8.812   294.634 1.00 24.38  ? 433 ALA A CB  1 
ATOM   3289 N  N   . MET A 1 434 ? -114.357 7.473   293.346 1.00 22.82  ? 434 MET A N   1 
ATOM   3290 C  CA  . MET A 1 434 ? -113.571 6.240   293.311 1.00 24.87  ? 434 MET A CA  1 
ATOM   3291 C  C   . MET A 1 434 ? -113.423 5.604   294.684 1.00 25.56  ? 434 MET A C   1 
ATOM   3292 O  O   . MET A 1 434 ? -112.398 4.986   294.984 1.00 26.27  ? 434 MET A O   1 
ATOM   3293 C  CB  . MET A 1 434 ? -112.207 6.516   292.690 1.00 23.52  ? 434 MET A CB  1 
ATOM   3294 C  CG  . MET A 1 434 ? -112.266 6.777   291.191 1.00 20.65  ? 434 MET A CG  1 
ATOM   3295 S  SD  . MET A 1 434 ? -110.637 7.075   290.483 1.00 8.26   ? 434 MET A SD  1 
ATOM   3296 C  CE  . MET A 1 434 ? -110.987 6.940   288.734 1.00 15.64  ? 434 MET A CE  1 
ATOM   3297 N  N   . TYR A 1 435 ? -114.441 5.719   295.530 1.00 24.80  ? 435 TYR A N   1 
ATOM   3298 C  CA  . TYR A 1 435 ? -114.405 5.188   296.887 1.00 25.52  ? 435 TYR A CA  1 
ATOM   3299 C  C   . TYR A 1 435 ? -115.842 4.982   297.354 1.00 29.04  ? 435 TYR A C   1 
ATOM   3300 O  O   . TYR A 1 435 ? -116.793 5.157   296.586 1.00 26.27  ? 435 TYR A O   1 
ATOM   3301 C  CB  . TYR A 1 435 ? -113.629 6.126   297.818 1.00 29.49  ? 435 TYR A CB  1 
ATOM   3302 C  CG  . TYR A 1 435 ? -114.231 7.511   297.916 1.00 27.41  ? 435 TYR A CG  1 
ATOM   3303 C  CD1 . TYR A 1 435 ? -113.966 8.476   296.954 1.00 25.42  ? 435 TYR A CD1 1 
ATOM   3304 C  CD2 . TYR A 1 435 ? -115.073 7.849   298.966 1.00 29.57  ? 435 TYR A CD2 1 
ATOM   3305 C  CE1 . TYR A 1 435 ? -114.519 9.741   297.035 1.00 26.10  ? 435 TYR A CE1 1 
ATOM   3306 C  CE2 . TYR A 1 435 ? -115.630 9.111   299.057 1.00 36.37  ? 435 TYR A CE2 1 
ATOM   3307 C  CZ  . TYR A 1 435 ? -115.350 10.053  298.090 1.00 33.03  ? 435 TYR A CZ  1 
ATOM   3308 O  OH  . TYR A 1 435 ? -115.906 11.310  298.181 1.00 51.64  ? 435 TYR A OH  1 
ATOM   3309 N  N   . GLY A 1 436 ? -116.002 4.613   298.620 1.00 38.33  ? 436 GLY A N   1 
ATOM   3310 C  CA  . GLY A 1 436 ? -117.327 4.433   299.173 1.00 30.88  ? 436 GLY A CA  1 
ATOM   3311 C  C   . GLY A 1 436 ? -117.399 4.690   300.662 1.00 29.24  ? 436 GLY A C   1 
ATOM   3312 O  O   . GLY A 1 436 ? -116.524 4.254   301.415 1.00 45.68  ? 436 GLY A O   1 
ATOM   3313 N  N   . ARG A 1 437 ? -118.431 5.403   301.098 1.00 26.72  ? 437 ARG A N   1 
ATOM   3314 C  CA  . ARG A 1 437 ? -118.688 5.623   302.513 1.00 30.65  ? 437 ARG A CA  1 
ATOM   3315 C  C   . ARG A 1 437 ? -119.757 4.652   302.992 1.00 35.69  ? 437 ARG A C   1 
ATOM   3316 O  O   . ARG A 1 437 ? -120.697 4.337   302.257 1.00 39.23  ? 437 ARG A O   1 
ATOM   3317 C  CB  . ARG A 1 437 ? -119.121 7.065   302.779 1.00 34.68  ? 437 ARG A CB  1 
ATOM   3318 C  CG  . ARG A 1 437 ? -117.963 8.041   302.844 1.00 43.73  ? 437 ARG A CG  1 
ATOM   3319 C  CD  . ARG A 1 437 ? -118.417 9.420   303.279 1.00 32.39  ? 437 ARG A CD  1 
ATOM   3320 N  NE  . ARG A 1 437 ? -117.293 10.238  303.723 1.00 29.52  ? 437 ARG A NE  1 
ATOM   3321 C  CZ  . ARG A 1 437 ? -116.468 10.885  302.908 1.00 33.64  ? 437 ARG A CZ  1 
ATOM   3322 N  NH1 . ARG A 1 437 ? -116.632 10.812  301.595 1.00 36.99  ? 437 ARG A NH1 1 
ATOM   3323 N  NH2 . ARG A 1 437 ? -115.472 11.603  303.407 1.00 37.03  ? 437 ARG A NH2 1 
ATOM   3324 N  N   . GLY A 1 438 ? -119.605 4.175   304.226 1.00 36.83  ? 438 GLY A N   1 
ATOM   3325 C  CA  . GLY A 1 438 ? -120.503 3.158   304.730 1.00 34.34  ? 438 GLY A CA  1 
ATOM   3326 C  C   . GLY A 1 438 ? -120.717 3.256   306.224 1.00 39.81  ? 438 GLY A C   1 
ATOM   3327 O  O   . GLY A 1 438 ? -120.031 3.995   306.934 1.00 52.65  ? 438 GLY A O   1 
ATOM   3328 N  N   . TRP A 1 439 ? -121.693 2.483   306.691 1.00 37.91  ? 439 TRP A N   1 
ATOM   3329 C  CA  . TRP A 1 439 ? -122.043 2.398   308.099 1.00 36.51  ? 439 TRP A CA  1 
ATOM   3330 C  C   . TRP A 1 439 ? -121.996 0.940   308.531 1.00 38.68  ? 439 TRP A C   1 
ATOM   3331 O  O   . TRP A 1 439 ? -122.178 0.031   307.716 1.00 45.35  ? 439 TRP A O   1 
ATOM   3332 C  CB  . TRP A 1 439 ? -123.440 2.977   308.370 1.00 36.93  ? 439 TRP A CB  1 
ATOM   3333 C  CG  . TRP A 1 439 ? -123.649 4.365   307.835 1.00 35.19  ? 439 TRP A CG  1 
ATOM   3334 C  CD1 . TRP A 1 439 ? -123.637 5.527   308.548 1.00 37.47  ? 439 TRP A CD1 1 
ATOM   3335 C  CD2 . TRP A 1 439 ? -123.914 4.733   306.474 1.00 33.73  ? 439 TRP A CD2 1 
ATOM   3336 N  NE1 . TRP A 1 439 ? -123.872 6.596   307.718 1.00 35.71  ? 439 TRP A NE1 1 
ATOM   3337 C  CE2 . TRP A 1 439 ? -124.045 6.135   306.439 1.00 34.00  ? 439 TRP A CE2 1 
ATOM   3338 C  CE3 . TRP A 1 439 ? -124.050 4.014   305.283 1.00 33.62  ? 439 TRP A CE3 1 
ATOM   3339 C  CZ2 . TRP A 1 439 ? -124.305 6.832   305.261 1.00 28.61  ? 439 TRP A CZ2 1 
ATOM   3340 C  CZ3 . TRP A 1 439 ? -124.307 4.708   304.114 1.00 33.36  ? 439 TRP A CZ3 1 
ATOM   3341 C  CH2 . TRP A 1 439 ? -124.432 6.102   304.112 1.00 25.97  ? 439 TRP A CH2 1 
ATOM   3342 N  N   . THR A 1 440 ? -121.752 0.721   309.820 1.00 38.81  ? 440 THR A N   1 
ATOM   3343 C  CA  . THR A 1 440 ? -121.691 -0.619  310.381 1.00 39.89  ? 440 THR A CA  1 
ATOM   3344 C  C   . THR A 1 440 ? -122.804 -0.809  311.402 1.00 51.28  ? 440 THR A C   1 
ATOM   3345 O  O   . THR A 1 440 ? -123.264 0.149   312.031 1.00 60.63  ? 440 THR A O   1 
ATOM   3346 C  CB  . THR A 1 440 ? -120.332 -0.898  311.039 1.00 42.87  ? 440 THR A CB  1 
ATOM   3347 O  OG1 . THR A 1 440 ? -120.296 -2.253  311.505 1.00 44.10  ? 440 THR A OG1 1 
ATOM   3348 C  CG2 . THR A 1 440 ? -120.105 0.036   312.216 1.00 43.20  ? 440 THR A CG2 1 
ATOM   3349 N  N   . GLY A 1 441 ? -123.234 -2.059  311.556 1.00 47.21  ? 441 GLY A N   1 
ATOM   3350 C  CA  . GLY A 1 441 ? -124.274 -2.398  312.507 1.00 45.44  ? 441 GLY A CA  1 
ATOM   3351 C  C   . GLY A 1 441 ? -125.587 -1.688  312.255 1.00 43.25  ? 441 GLY A C   1 
ATOM   3352 O  O   . GLY A 1 441 ? -126.194 -1.149  313.185 1.00 50.58  ? 441 GLY A O   1 
ATOM   3353 N  N   . VAL A 1 442 ? -126.035 -1.676  311.000 1.00 40.52  ? 442 VAL A N   1 
ATOM   3354 C  CA  . VAL A 1 442 ? -127.292 -1.023  310.652 1.00 43.87  ? 442 VAL A CA  1 
ATOM   3355 C  C   . VAL A 1 442 ? -128.439 -1.789  311.300 1.00 47.26  ? 442 VAL A C   1 
ATOM   3356 O  O   . VAL A 1 442 ? -128.654 -2.973  311.016 1.00 56.66  ? 442 VAL A O   1 
ATOM   3357 C  CB  . VAL A 1 442 ? -127.465 -0.940  309.131 1.00 44.41  ? 442 VAL A CB  1 
ATOM   3358 C  CG1 . VAL A 1 442 ? -128.833 -0.374  308.783 1.00 58.44  ? 442 VAL A CG1 1 
ATOM   3359 C  CG2 . VAL A 1 442 ? -126.357 -0.096  308.517 1.00 44.77  ? 442 VAL A CG2 1 
ATOM   3360 N  N   . THR A 1 443 ? -129.180 -1.115  312.173 1.00 45.65  ? 443 THR A N   1 
ATOM   3361 C  CA  . THR A 1 443 ? -130.230 -1.737  312.965 1.00 46.15  ? 443 THR A CA  1 
ATOM   3362 C  C   . THR A 1 443 ? -131.552 -1.011  312.756 1.00 49.82  ? 443 THR A C   1 
ATOM   3363 O  O   . THR A 1 443 ? -131.612 0.067   312.157 1.00 84.36  ? 443 THR A O   1 
ATOM   3364 C  CB  . THR A 1 443 ? -129.869 -1.732  314.457 1.00 61.11  ? 443 THR A CB  1 
ATOM   3365 O  OG1 . THR A 1 443 ? -129.334 -0.451  314.815 1.00 47.72  ? 443 THR A OG1 1 
ATOM   3366 C  CG2 . THR A 1 443 ? -128.837 -2.803  314.762 1.00 54.03  ? 443 THR A CG2 1 
ATOM   3367 N  N   . ASN A 1 444 ? -132.618 -1.630  313.263 1.00 48.31  ? 444 ASN A N   1 
ATOM   3368 C  CA  . ASN A 1 444 ? -133.949 -1.030  313.347 1.00 44.32  ? 444 ASN A CA  1 
ATOM   3369 C  C   . ASN A 1 444 ? -134.428 -0.543  311.976 1.00 46.83  ? 444 ASN A C   1 
ATOM   3370 O  O   . ASN A 1 444 ? -134.559 0.651   311.710 1.00 48.08  ? 444 ASN A O   1 
ATOM   3371 C  CB  . ASN A 1 444 ? -133.956 0.109   314.371 1.00 44.82  ? 444 ASN A CB  1 
ATOM   3372 C  CG  . ASN A 1 444 ? -133.520 -0.346  315.750 1.00 40.42  ? 444 ASN A CG  1 
ATOM   3373 O  OD1 . ASN A 1 444 ? -133.744 -1.493  316.137 1.00 39.81  ? 444 ASN A OD1 1 
ATOM   3374 N  ND2 . ASN A 1 444 ? -132.892 0.552   316.499 1.00 43.71  ? 444 ASN A ND2 1 
ATOM   3375 N  N   . TYR A 1 445 ? -134.695 -1.516  311.108 1.00 47.14  ? 445 TYR A N   1 
ATOM   3376 C  CA  . TYR A 1 445 ? -135.131 -1.232  309.750 1.00 48.91  ? 445 TYR A CA  1 
ATOM   3377 C  C   . TYR A 1 445 ? -136.243 -2.192  309.358 1.00 52.55  ? 445 TYR A C   1 
ATOM   3378 O  O   . TYR A 1 445 ? -136.337 -3.307  309.880 1.00 78.05  ? 445 TYR A O   1 
ATOM   3379 C  CB  . TYR A 1 445 ? -133.969 -1.340  308.751 1.00 55.09  ? 445 TYR A CB  1 
ATOM   3380 C  CG  . TYR A 1 445 ? -133.385 -2.730  308.638 1.00 61.61  ? 445 TYR A CG  1 
ATOM   3381 C  CD1 . TYR A 1 445 ? -133.860 -3.632  307.693 1.00 63.14  ? 445 TYR A CD1 1 
ATOM   3382 C  CD2 . TYR A 1 445 ? -132.364 -3.145  309.482 1.00 65.04  ? 445 TYR A CD2 1 
ATOM   3383 C  CE1 . TYR A 1 445 ? -133.332 -4.903  307.589 1.00 84.30  ? 445 TYR A CE1 1 
ATOM   3384 C  CE2 . TYR A 1 445 ? -131.829 -4.415  309.386 1.00 70.88  ? 445 TYR A CE2 1 
ATOM   3385 C  CZ  . TYR A 1 445 ? -132.317 -5.289  308.438 1.00 82.48  ? 445 TYR A CZ  1 
ATOM   3386 O  OH  . TYR A 1 445 ? -131.787 -6.555  308.339 1.00 99.83  ? 445 TYR A OH  1 
ATOM   3387 N  N   . THR A 1 446 ? -137.080 -1.747  308.429 1.00 51.26  ? 446 THR A N   1 
ATOM   3388 C  CA  . THR A 1 446 ? -138.143 -2.564  307.867 1.00 51.24  ? 446 THR A CA  1 
ATOM   3389 C  C   . THR A 1 446 ? -137.747 -3.058  306.481 1.00 54.34  ? 446 THR A C   1 
ATOM   3390 O  O   . THR A 1 446 ? -136.809 -2.551  305.861 1.00 52.03  ? 446 THR A O   1 
ATOM   3391 C  CB  . THR A 1 446 ? -139.450 -1.774  307.776 1.00 46.29  ? 446 THR A CB  1 
ATOM   3392 O  OG1 . THR A 1 446 ? -139.281 -0.672  306.875 1.00 45.84  ? 446 THR A OG1 1 
ATOM   3393 C  CG2 . THR A 1 446 ? -139.850 -1.240  309.142 1.00 41.60  ? 446 THR A CG2 1 
ATOM   3394 N  N   . ASN A 1 447 ? -138.477 -4.062  306.007 1.00 73.69  ? 447 ASN A N   1 
ATOM   3395 C  CA  . ASN A 1 447 ? -138.334 -4.573  304.637 1.00 60.99  ? 447 ASN A CA  1 
ATOM   3396 C  C   . ASN A 1 447 ? -136.889 -5.043  304.438 1.00 55.01  ? 447 ASN A C   1 
ATOM   3397 O  O   . ASN A 1 447 ? -136.228 -5.483  305.388 1.00 57.29  ? 447 ASN A O   1 
ATOM   3398 C  CB  . ASN A 1 447 ? -138.801 -3.506  303.658 1.00 60.55  ? 447 ASN A CB  1 
ATOM   3399 C  CG  . ASN A 1 447 ? -139.055 -4.054  302.269 1.00 66.01  ? 447 ASN A CG  1 
ATOM   3400 O  OD1 . ASN A 1 447 ? -139.327 -5.240  302.100 1.00 54.73  ? 447 ASN A OD1 1 
ATOM   3401 N  ND2 . ASN A 1 447 ? -138.964 -3.188  301.265 1.00 54.04  ? 447 ASN A ND2 1 
ATOM   3402 N  N   . ASP A 1 448 ? -136.390 -4.961  303.204 1.00 54.31  ? 448 ASP A N   1 
ATOM   3403 C  CA  . ASP A 1 448 ? -134.985 -5.187  302.897 1.00 57.67  ? 448 ASP A CA  1 
ATOM   3404 C  C   . ASP A 1 448 ? -134.280 -3.893  302.505 1.00 63.22  ? 448 ASP A C   1 
ATOM   3405 O  O   . ASP A 1 448 ? -133.205 -3.931  301.898 1.00 79.73  ? 448 ASP A O   1 
ATOM   3406 C  CB  . ASP A 1 448 ? -134.839 -6.239  301.795 1.00 61.46  ? 448 ASP A CB  1 
ATOM   3407 C  CG  . ASP A 1 448 ? -135.423 -5.785  300.470 1.00 52.44  ? 448 ASP A CG  1 
ATOM   3408 O  OD1 . ASP A 1 448 ? -136.275 -4.872  300.472 1.00 58.76  ? 448 ASP A OD1 1 
ATOM   3409 O  OD2 . ASP A 1 448 ? -135.027 -6.344  299.426 1.00 41.56  ? 448 ASP A OD2 1 
ATOM   3410 N  N   . ASN A 1 449 ? -134.875 -2.748  302.829 1.00 66.06  ? 449 ASN A N   1 
ATOM   3411 C  CA  . ASN A 1 449 ? -134.253 -1.450  302.610 1.00 55.48  ? 449 ASN A CA  1 
ATOM   3412 C  C   . ASN A 1 449 ? -133.507 -1.045  303.876 1.00 67.05  ? 449 ASN A C   1 
ATOM   3413 O  O   . ASN A 1 449 ? -134.125 -0.825  304.923 1.00 65.53  ? 449 ASN A O   1 
ATOM   3414 C  CB  . ASN A 1 449 ? -135.303 -0.404  302.239 1.00 47.18  ? 449 ASN A CB  1 
ATOM   3415 C  CG  . ASN A 1 449 ? -134.723 0.991   302.133 1.00 44.51  ? 449 ASN A CG  1 
ATOM   3416 O  OD1 . ASN A 1 449 ? -133.549 1.164   301.804 1.00 52.72  ? 449 ASN A OD1 1 
ATOM   3417 N  ND2 . ASN A 1 449 ? -135.542 1.996   302.413 1.00 44.02  ? 449 ASN A ND2 1 
ATOM   3418 N  N   . TYR A 1 450 ? -132.185 -0.956  303.780 1.00 51.54  ? 450 TYR A N   1 
ATOM   3419 C  CA  . TYR A 1 450 ? -131.339 -0.699  304.937 1.00 49.43  ? 450 TYR A CA  1 
ATOM   3420 C  C   . TYR A 1 450 ? -131.026 0.778   305.131 1.00 46.98  ? 450 TYR A C   1 
ATOM   3421 O  O   . TYR A 1 450 ? -130.293 1.123   306.064 1.00 67.28  ? 450 TYR A O   1 
ATOM   3422 C  CB  . TYR A 1 450 ? -130.040 -1.499  304.817 1.00 51.49  ? 450 TYR A CB  1 
ATOM   3423 C  CG  . TYR A 1 450 ? -130.240 -2.862  304.194 1.00 54.95  ? 450 TYR A CG  1 
ATOM   3424 C  CD1 . TYR A 1 450 ? -130.694 -3.933  304.953 1.00 66.46  ? 450 TYR A CD1 1 
ATOM   3425 C  CD2 . TYR A 1 450 ? -129.978 -3.078  302.848 1.00 49.04  ? 450 TYR A CD2 1 
ATOM   3426 C  CE1 . TYR A 1 450 ? -130.883 -5.179  304.388 1.00 61.59  ? 450 TYR A CE1 1 
ATOM   3427 C  CE2 . TYR A 1 450 ? -130.161 -4.321  302.274 1.00 49.93  ? 450 TYR A CE2 1 
ATOM   3428 C  CZ  . TYR A 1 450 ? -130.614 -5.368  303.049 1.00 54.47  ? 450 TYR A CZ  1 
ATOM   3429 O  OH  . TYR A 1 450 ? -130.799 -6.608  302.483 1.00 59.51  ? 450 TYR A OH  1 
ATOM   3430 N  N   . PHE A 1 451 ? -131.557 1.653   304.280 1.00 46.90  ? 451 PHE A N   1 
ATOM   3431 C  CA  . PHE A 1 451 ? -131.389 3.090   304.444 1.00 54.27  ? 451 PHE A CA  1 
ATOM   3432 C  C   . PHE A 1 451 ? -132.496 3.722   305.274 1.00 41.07  ? 451 PHE A C   1 
ATOM   3433 O  O   . PHE A 1 451 ? -132.362 4.882   305.680 1.00 37.47  ? 451 PHE A O   1 
ATOM   3434 C  CB  . PHE A 1 451 ? -131.316 3.769   303.073 1.00 41.65  ? 451 PHE A CB  1 
ATOM   3435 C  CG  . PHE A 1 451 ? -130.254 3.202   302.176 1.00 54.72  ? 451 PHE A CG  1 
ATOM   3436 C  CD1 . PHE A 1 451 ? -128.941 3.627   302.283 1.00 62.83  ? 451 PHE A CD1 1 
ATOM   3437 C  CD2 . PHE A 1 451 ? -130.567 2.238   301.232 1.00 42.98  ? 451 PHE A CD2 1 
ATOM   3438 C  CE1 . PHE A 1 451 ? -127.959 3.107   301.461 1.00 56.44  ? 451 PHE A CE1 1 
ATOM   3439 C  CE2 . PHE A 1 451 ? -129.588 1.713   300.407 1.00 55.63  ? 451 PHE A CE2 1 
ATOM   3440 C  CZ  . PHE A 1 451 ? -128.283 2.148   300.523 1.00 42.48  ? 451 PHE A CZ  1 
ATOM   3441 N  N   . SER A 1 452 ? -133.583 2.994   305.531 1.00 41.87  ? 452 SER A N   1 
ATOM   3442 C  CA  . SER A 1 452 ? -134.628 3.467   306.427 1.00 41.57  ? 452 SER A CA  1 
ATOM   3443 C  C   . SER A 1 452 ? -134.284 3.252   307.893 1.00 42.34  ? 452 SER A C   1 
ATOM   3444 O  O   . SER A 1 452 ? -134.990 3.775   308.762 1.00 64.20  ? 452 SER A O   1 
ATOM   3445 C  CB  . SER A 1 452 ? -135.951 2.769   306.105 1.00 40.82  ? 452 SER A CB  1 
ATOM   3446 O  OG  . SER A 1 452 ? -135.790 1.362   306.090 1.00 44.78  ? 452 SER A OG  1 
ATOM   3447 N  N   . GLY A 1 453 ? -133.227 2.503   308.186 1.00 41.56  ? 453 GLY A N   1 
ATOM   3448 C  CA  . GLY A 1 453 ? -132.830 2.211   309.546 1.00 42.13  ? 453 GLY A CA  1 
ATOM   3449 C  C   . GLY A 1 453 ? -131.806 3.188   310.081 1.00 37.13  ? 453 GLY A C   1 
ATOM   3450 O  O   . GLY A 1 453 ? -131.631 4.296   309.567 1.00 34.85  ? 453 GLY A O   1 
ATOM   3451 N  N   . THR A 1 454 ? -131.123 2.764   311.142 1.00 33.32  ? 454 THR A N   1 
ATOM   3452 C  CA  . THR A 1 454 ? -130.103 3.568   311.802 1.00 34.64  ? 454 THR A CA  1 
ATOM   3453 C  C   . THR A 1 454 ? -128.865 2.716   312.033 1.00 40.21  ? 454 THR A C   1 
ATOM   3454 O  O   . THR A 1 454 ? -128.960 1.621   312.596 1.00 44.10  ? 454 THR A O   1 
ATOM   3455 C  CB  . THR A 1 454 ? -130.605 4.127   313.140 1.00 34.61  ? 454 THR A CB  1 
ATOM   3456 O  OG1 . THR A 1 454 ? -130.913 3.044   314.026 1.00 35.00  ? 454 THR A OG1 1 
ATOM   3457 C  CG2 . THR A 1 454 ? -131.846 4.985   312.939 1.00 38.13  ? 454 THR A CG2 1 
ATOM   3458 N  N   . GLY A 1 455 ? -127.708 3.219   311.599 1.00 40.00  ? 455 GLY A N   1 
ATOM   3459 C  CA  . GLY A 1 455 ? -126.459 2.534   311.847 1.00 39.87  ? 455 GLY A CA  1 
ATOM   3460 C  C   . GLY A 1 455 ? -125.892 2.847   313.219 1.00 49.12  ? 455 GLY A C   1 
ATOM   3461 O  O   . GLY A 1 455 ? -126.376 3.716   313.943 1.00 39.76  ? 455 GLY A O   1 
ATOM   3462 N  N   . ASN A 1 456 ? -124.837 2.112   313.580 1.00 46.76  ? 456 ASN A N   1 
ATOM   3463 C  CA  . ASN A 1 456 ? -124.162 2.277   314.867 1.00 45.62  ? 456 ASN A CA  1 
ATOM   3464 C  C   . ASN A 1 456 ? -122.651 2.339   314.625 1.00 37.80  ? 456 ASN A C   1 
ATOM   3465 O  O   . ASN A 1 456 ? -121.906 1.428   314.987 1.00 36.66  ? 456 ASN A O   1 
ATOM   3466 C  CB  . ASN A 1 456 ? -124.532 1.151   315.835 1.00 38.41  ? 456 ASN A CB  1 
ATOM   3467 C  CG  . ASN A 1 456 ? -123.996 1.386   317.235 1.00 38.41  ? 456 ASN A CG  1 
ATOM   3468 O  OD1 . ASN A 1 456 ? -123.240 0.574   317.768 1.00 37.73  ? 456 ASN A OD1 1 
ATOM   3469 N  ND2 . ASN A 1 456 ? -124.386 2.503   317.838 1.00 48.46  ? 456 ASN A ND2 1 
ATOM   3470 N  N   . GLY A 1 457 ? -122.204 3.428   314.005 1.00 35.54  ? 457 GLY A N   1 
ATOM   3471 C  CA  . GLY A 1 457 ? -120.794 3.655   313.798 1.00 38.71  ? 457 GLY A CA  1 
ATOM   3472 C  C   . GLY A 1 457 ? -120.381 3.556   312.344 1.00 38.51  ? 457 GLY A C   1 
ATOM   3473 O  O   . GLY A 1 457 ? -121.139 3.096   311.484 1.00 46.98  ? 457 GLY A O   1 
ATOM   3474 N  N   . PRO A 1 458 ? -119.163 3.994   312.044 1.00 36.72  ? 458 PRO A N   1 
ATOM   3475 C  CA  . PRO A 1 458 ? -118.668 3.928   310.668 1.00 37.55  ? 458 PRO A CA  1 
ATOM   3476 C  C   . PRO A 1 458 ? -118.137 2.549   310.314 1.00 36.63  ? 458 PRO A C   1 
ATOM   3477 O  O   . PRO A 1 458 ? -117.635 1.807   311.162 1.00 36.06  ? 458 PRO A O   1 
ATOM   3478 C  CB  . PRO A 1 458 ? -117.542 4.968   310.653 1.00 47.74  ? 458 PRO A CB  1 
ATOM   3479 C  CG  . PRO A 1 458 ? -117.037 4.969   312.056 1.00 41.81  ? 458 PRO A CG  1 
ATOM   3480 C  CD  . PRO A 1 458 ? -118.227 4.698   312.939 1.00 37.27  ? 458 PRO A CD  1 
ATOM   3481 N  N   . VAL A 1 459 ? -118.251 2.217   309.027 1.00 36.92  ? 459 VAL A N   1 
ATOM   3482 C  CA  . VAL A 1 459 ? -117.760 0.933   308.542 1.00 36.99  ? 459 VAL A CA  1 
ATOM   3483 C  C   . VAL A 1 459 ? -116.234 0.908   308.589 1.00 39.82  ? 459 VAL A C   1 
ATOM   3484 O  O   . VAL A 1 459 ? -115.561 1.945   308.596 1.00 50.26  ? 459 VAL A O   1 
ATOM   3485 C  CB  . VAL A 1 459 ? -118.282 0.664   307.119 1.00 37.43  ? 459 VAL A CB  1 
ATOM   3486 C  CG1 . VAL A 1 459 ? -117.570 1.554   306.110 1.00 46.02  ? 459 VAL A CG1 1 
ATOM   3487 C  CG2 . VAL A 1 459 ? -118.148 -0.810  306.749 1.00 43.20  ? 459 VAL A CG2 1 
ATOM   3488 N  N   . SER A 1 460 ? -115.683 -0.303  308.641 1.00 42.79  ? 460 SER A N   1 
ATOM   3489 C  CA  . SER A 1 460 ? -114.236 -0.476  308.599 1.00 49.13  ? 460 SER A CA  1 
ATOM   3490 C  C   . SER A 1 460 ? -113.707 -0.033  307.241 1.00 56.21  ? 460 SER A C   1 
ATOM   3491 O  O   . SER A 1 460 ? -114.147 -0.534  306.201 1.00 53.01  ? 460 SER A O   1 
ATOM   3492 C  CB  . SER A 1 460 ? -113.870 -1.933  308.871 1.00 47.93  ? 460 SER A CB  1 
ATOM   3493 O  OG  . SER A 1 460 ? -114.108 -2.740  307.731 1.00 55.95  ? 460 SER A OG  1 
ATOM   3494 N  N   . GLY A 1 461 ? -112.760 0.907   307.248 1.00 47.71  ? 461 GLY A N   1 
ATOM   3495 C  CA  . GLY A 1 461 ? -112.236 1.491   306.037 1.00 59.06  ? 461 GLY A CA  1 
ATOM   3496 C  C   . GLY A 1 461 ? -110.826 1.018   305.715 1.00 42.50  ? 461 GLY A C   1 
ATOM   3497 O  O   . GLY A 1 461 ? -110.138 0.400   306.526 1.00 38.49  ? 461 GLY A O   1 
ATOM   3498 N  N   . THR A 1 462 ? -110.406 1.329   304.489 1.00 36.22  ? 462 THR A N   1 
ATOM   3499 C  CA  . THR A 1 462 ? -109.074 0.973   304.016 1.00 33.29  ? 462 THR A CA  1 
ATOM   3500 C  C   . THR A 1 462 ? -108.011 1.760   304.770 1.00 38.41  ? 462 THR A C   1 
ATOM   3501 O  O   . THR A 1 462 ? -107.252 1.193   305.562 1.00 65.56  ? 462 THR A O   1 
ATOM   3502 C  CB  . THR A 1 462 ? -108.949 1.229   302.513 1.00 31.04  ? 462 THR A CB  1 
ATOM   3503 O  OG1 . THR A 1 462 ? -110.097 0.699   301.838 1.00 30.27  ? 462 THR A OG1 1 
ATOM   3504 C  CG2 . THR A 1 462 ? -107.695 0.565   301.965 1.00 33.53  ? 462 THR A CG2 1 
ATOM   3505 N  N   . TRP A 1 463 ? -107.949 3.067   304.525 1.00 35.35  ? 463 TRP A N   1 
ATOM   3506 C  CA  . TRP A 1 463 ? -107.020 3.953   305.214 1.00 33.32  ? 463 TRP A CA  1 
ATOM   3507 C  C   . TRP A 1 463 ? -107.683 4.728   306.342 1.00 38.80  ? 463 TRP A C   1 
ATOM   3508 O  O   . TRP A 1 463 ? -107.073 4.925   307.397 1.00 54.67  ? 463 TRP A O   1 
ATOM   3509 C  CB  . TRP A 1 463 ? -106.393 4.933   304.219 1.00 30.25  ? 463 TRP A CB  1 
ATOM   3510 C  CG  . TRP A 1 463 ? -106.050 4.297   302.910 1.00 26.73  ? 463 TRP A CG  1 
ATOM   3511 C  CD1 . TRP A 1 463 ? -106.717 4.445   301.730 1.00 26.56  ? 463 TRP A CD1 1 
ATOM   3512 C  CD2 . TRP A 1 463 ? -104.970 3.393   302.650 1.00 24.83  ? 463 TRP A CD2 1 
ATOM   3513 N  NE1 . TRP A 1 463 ? -106.114 3.698   300.747 1.00 23.04  ? 463 TRP A NE1 1 
ATOM   3514 C  CE2 . TRP A 1 463 ? -105.039 3.042   301.287 1.00 24.87  ? 463 TRP A CE2 1 
ATOM   3515 C  CE3 . TRP A 1 463 ? -103.949 2.850   303.435 1.00 25.25  ? 463 TRP A CE3 1 
ATOM   3516 C  CZ2 . TRP A 1 463 ? -104.126 2.174   300.693 1.00 25.71  ? 463 TRP A CZ2 1 
ATOM   3517 C  CZ3 . TRP A 1 463 ? -103.044 1.988   302.843 1.00 23.95  ? 463 TRP A CZ3 1 
ATOM   3518 C  CH2 . TRP A 1 463 ? -103.139 1.658   301.486 1.00 22.38  ? 463 TRP A CH2 1 
ATOM   3519 N  N   . GLU A 1 464 ? -108.921 5.171   306.140 1.00 43.93  ? 464 GLU A N   1 
ATOM   3520 C  CA  . GLU A 1 464 ? -109.715 5.821   307.172 1.00 54.46  ? 464 GLU A CA  1 
ATOM   3521 C  C   . GLU A 1 464 ? -111.052 5.105   307.276 1.00 51.11  ? 464 GLU A C   1 
ATOM   3522 O  O   . GLU A 1 464 ? -111.705 4.856   306.258 1.00 58.61  ? 464 GLU A O   1 
ATOM   3523 C  CB  . GLU A 1 464 ? -109.934 7.306   306.863 1.00 77.25  ? 464 GLU A CB  1 
ATOM   3524 C  CG  . GLU A 1 464 ? -110.860 8.011   307.845 1.00 74.95  ? 464 GLU A CG  1 
ATOM   3525 C  CD  . GLU A 1 464 ? -110.963 9.502   307.586 1.00 89.08  ? 464 GLU A CD  1 
ATOM   3526 O  OE1 . GLU A 1 464 ? -111.527 9.888   306.541 1.00 83.84  ? 464 GLU A OE1 1 
ATOM   3527 O  OE2 . GLU A 1 464 ? -110.481 10.288  308.429 1.00 108.17 ? 464 GLU A OE2 1 
ATOM   3528 N  N   . ASP A 1 465 ? -111.449 4.765   308.499 1.00 52.50  ? 465 ASP A N   1 
ATOM   3529 C  CA  . ASP A 1 465 ? -112.726 4.101   308.704 1.00 45.49  ? 465 ASP A CA  1 
ATOM   3530 C  C   . ASP A 1 465 ? -113.877 5.023   308.316 1.00 46.04  ? 465 ASP A C   1 
ATOM   3531 O  O   . ASP A 1 465 ? -113.825 6.241   308.510 1.00 45.67  ? 465 ASP A O   1 
ATOM   3532 C  CB  . ASP A 1 465 ? -112.872 3.649   310.156 1.00 44.77  ? 465 ASP A CB  1 
ATOM   3533 C  CG  . ASP A 1 465 ? -112.217 2.307   310.413 1.00 43.23  ? 465 ASP A CG  1 
ATOM   3534 O  OD1 . ASP A 1 465 ? -111.597 1.758   309.478 1.00 52.74  ? 465 ASP A OD1 1 
ATOM   3535 O  OD2 . ASP A 1 465 ? -112.323 1.799   311.548 1.00 43.22  ? 465 ASP A OD2 1 
ATOM   3536 N  N   . GLY A 1 466 ? -114.925 4.423   307.756 1.00 55.08  ? 466 GLY A N   1 
ATOM   3537 C  CA  . GLY A 1 466 ? -116.019 5.169   307.178 1.00 41.29  ? 466 GLY A CA  1 
ATOM   3538 C  C   . GLY A 1 466 ? -115.883 5.433   305.695 1.00 38.43  ? 466 GLY A C   1 
ATOM   3539 O  O   . GLY A 1 466 ? -116.864 5.845   305.063 1.00 42.88  ? 466 GLY A O   1 
ATOM   3540 N  N   . VAL A 1 467 ? -114.701 5.217   305.123 1.00 32.84  ? 467 VAL A N   1 
ATOM   3541 C  CA  . VAL A 1 467 ? -114.456 5.377   303.695 1.00 31.46  ? 467 VAL A CA  1 
ATOM   3542 C  C   . VAL A 1 467 ? -113.682 4.159   303.212 1.00 33.73  ? 467 VAL A C   1 
ATOM   3543 O  O   . VAL A 1 467 ? -112.690 3.764   303.833 1.00 35.49  ? 467 VAL A O   1 
ATOM   3544 C  CB  . VAL A 1 467 ? -113.676 6.669   303.384 1.00 36.31  ? 467 VAL A CB  1 
ATOM   3545 C  CG1 . VAL A 1 467 ? -113.411 6.781   301.891 1.00 38.10  ? 467 VAL A CG1 1 
ATOM   3546 C  CG2 . VAL A 1 467 ? -114.434 7.888   303.884 1.00 47.27  ? 467 VAL A CG2 1 
ATOM   3547 N  N   . VAL A 1 468 ? -114.133 3.565   302.110 1.00 33.86  ? 468 VAL A N   1 
ATOM   3548 C  CA  . VAL A 1 468 ? -113.523 2.361   301.560 1.00 30.46  ? 468 VAL A CA  1 
ATOM   3549 C  C   . VAL A 1 468 ? -113.156 2.625   300.107 1.00 27.20  ? 468 VAL A C   1 
ATOM   3550 O  O   . VAL A 1 468 ? -113.989 3.106   299.331 1.00 25.05  ? 468 VAL A O   1 
ATOM   3551 C  CB  . VAL A 1 468 ? -114.461 1.143   301.667 1.00 28.56  ? 468 VAL A CB  1 
ATOM   3552 C  CG1 . VAL A 1 468 ? -113.819 -0.079  301.033 1.00 36.05  ? 468 VAL A CG1 1 
ATOM   3553 C  CG2 . VAL A 1 468 ? -114.816 0.873   303.120 1.00 36.62  ? 468 VAL A CG2 1 
ATOM   3554 N  N   . ASP A 1 469 ? -111.914 2.313   299.743 1.00 26.82  ? 469 ASP A N   1 
ATOM   3555 C  CA  . ASP A 1 469 ? -111.487 2.451   298.359 1.00 26.62  ? 469 ASP A CA  1 
ATOM   3556 C  C   . ASP A 1 469 ? -112.262 1.486   297.469 1.00 27.67  ? 469 ASP A C   1 
ATOM   3557 O  O   . ASP A 1 469 ? -112.678 0.407   297.899 1.00 27.18  ? 469 ASP A O   1 
ATOM   3558 C  CB  . ASP A 1 469 ? -109.986 2.184   298.227 1.00 25.22  ? 469 ASP A CB  1 
ATOM   3559 C  CG  . ASP A 1 469 ? -109.142 3.224   298.935 1.00 25.71  ? 469 ASP A CG  1 
ATOM   3560 O  OD1 . ASP A 1 469 ? -109.397 4.432   298.748 1.00 40.94  ? 469 ASP A OD1 1 
ATOM   3561 O  OD2 . ASP A 1 469 ? -108.213 2.832   299.671 1.00 22.91  ? 469 ASP A OD2 1 
ATOM   3562 N  N   . TYR A 1 470 ? -112.454 1.886   296.210 1.00 28.90  ? 470 TYR A N   1 
ATOM   3563 C  CA  . TYR A 1 470 ? -113.175 1.030   295.274 1.00 30.27  ? 470 TYR A CA  1 
ATOM   3564 C  C   . TYR A 1 470 ? -112.430 -0.273  295.017 1.00 28.58  ? 470 TYR A C   1 
ATOM   3565 O  O   . TYR A 1 470 ? -113.059 -1.311  294.783 1.00 43.88  ? 470 TYR A O   1 
ATOM   3566 C  CB  . TYR A 1 470 ? -113.417 1.770   293.957 1.00 32.77  ? 470 TYR A CB  1 
ATOM   3567 C  CG  . TYR A 1 470 ? -113.935 0.879   292.850 1.00 31.43  ? 470 TYR A CG  1 
ATOM   3568 C  CD1 . TYR A 1 470 ? -115.276 0.529   292.787 1.00 31.05  ? 470 TYR A CD1 1 
ATOM   3569 C  CD2 . TYR A 1 470 ? -113.082 0.384   291.870 1.00 29.38  ? 470 TYR A CD2 1 
ATOM   3570 C  CE1 . TYR A 1 470 ? -115.754 -0.286  291.781 1.00 52.28  ? 470 TYR A CE1 1 
ATOM   3571 C  CE2 . TYR A 1 470 ? -113.552 -0.433  290.861 1.00 27.41  ? 470 TYR A CE2 1 
ATOM   3572 C  CZ  . TYR A 1 470 ? -114.888 -0.765  290.822 1.00 32.51  ? 470 TYR A CZ  1 
ATOM   3573 O  OH  . TYR A 1 470 ? -115.362 -1.578  289.819 1.00 45.69  ? 470 TYR A OH  1 
ATOM   3574 N  N   . ARG A 1 471 ? -111.096 -0.239  295.055 1.00 25.04  ? 471 ARG A N   1 
ATOM   3575 C  CA  . ARG A 1 471 ? -110.317 -1.444  294.789 1.00 24.94  ? 471 ARG A CA  1 
ATOM   3576 C  C   . ARG A 1 471 ? -110.545 -2.501  295.862 1.00 33.97  ? 471 ARG A C   1 
ATOM   3577 O  O   . ARG A 1 471 ? -110.679 -3.690  295.549 1.00 27.84  ? 471 ARG A O   1 
ATOM   3578 C  CB  . ARG A 1 471 ? -108.833 -1.094  294.680 1.00 24.37  ? 471 ARG A CB  1 
ATOM   3579 C  CG  . ARG A 1 471 ? -107.910 -2.299  294.634 1.00 24.72  ? 471 ARG A CG  1 
ATOM   3580 C  CD  . ARG A 1 471 ? -106.501 -1.900  294.229 1.00 20.48  ? 471 ARG A CD  1 
ATOM   3581 N  NE  . ARG A 1 471 ? -106.046 -0.698  294.921 1.00 20.49  ? 471 ARG A NE  1 
ATOM   3582 C  CZ  . ARG A 1 471 ? -105.551 0.372   294.308 1.00 20.41  ? 471 ARG A CZ  1 
ATOM   3583 N  NH1 . ARG A 1 471 ? -105.442 0.390   292.986 1.00 17.25  ? 471 ARG A NH1 1 
ATOM   3584 N  NH2 . ARG A 1 471 ? -105.160 1.423   295.015 1.00 18.74  ? 471 ARG A NH2 1 
ATOM   3585 N  N   . GLN A 1 472 ? -110.598 -2.090  297.130 1.00 29.78  ? 472 GLN A N   1 
ATOM   3586 C  CA  . GLN A 1 472 ? -110.838 -3.049  298.203 1.00 28.13  ? 472 GLN A CA  1 
ATOM   3587 C  C   . GLN A 1 472 ? -112.268 -3.574  298.169 1.00 28.34  ? 472 GLN A C   1 
ATOM   3588 O  O   . GLN A 1 472 ? -112.525 -4.701  298.610 1.00 30.35  ? 472 GLN A O   1 
ATOM   3589 C  CB  . GLN A 1 472 ? -110.527 -2.410  299.558 1.00 26.87  ? 472 GLN A CB  1 
ATOM   3590 C  CG  . GLN A 1 472 ? -110.790 -3.311  300.755 1.00 28.64  ? 472 GLN A CG  1 
ATOM   3591 C  CD  . GLN A 1 472 ? -110.693 -2.574  302.074 1.00 30.86  ? 472 GLN A CD  1 
ATOM   3592 O  OE1 . GLN A 1 472 ? -110.886 -1.361  302.136 1.00 29.81  ? 472 GLN A OE1 1 
ATOM   3593 N  NE2 . GLN A 1 472 ? -110.387 -3.306  303.139 1.00 51.97  ? 472 GLN A NE2 1 
ATOM   3594 N  N   . ILE A 1 473 ? -113.206 -2.780  297.646 1.00 28.48  ? 473 ILE A N   1 
ATOM   3595 C  CA  . ILE A 1 473 ? -114.584 -3.241  297.503 1.00 27.71  ? 473 ILE A CA  1 
ATOM   3596 C  C   . ILE A 1 473 ? -114.644 -4.464  296.597 1.00 26.99  ? 473 ILE A C   1 
ATOM   3597 O  O   . ILE A 1 473 ? -115.385 -5.418  296.863 1.00 31.60  ? 473 ILE A O   1 
ATOM   3598 C  CB  . ILE A 1 473 ? -115.477 -2.101  296.977 1.00 34.62  ? 473 ILE A CB  1 
ATOM   3599 C  CG1 . ILE A 1 473 ? -115.596 -0.993  298.024 1.00 28.76  ? 473 ILE A CG1 1 
ATOM   3600 C  CG2 . ILE A 1 473 ? -116.853 -2.625  296.594 1.00 49.77  ? 473 ILE A CG2 1 
ATOM   3601 C  CD1 . ILE A 1 473 ? -116.443 0.177   297.582 1.00 30.37  ? 473 ILE A CD1 1 
ATOM   3602 N  N   . GLN A 1 474 ? -113.857 -4.460  295.519 1.00 26.94  ? 474 GLN A N   1 
ATOM   3603 C  CA  . GLN A 1 474 ? -113.845 -5.601  294.610 1.00 27.59  ? 474 GLN A CA  1 
ATOM   3604 C  C   . GLN A 1 474 ? -113.244 -6.836  295.271 1.00 30.28  ? 474 GLN A C   1 
ATOM   3605 O  O   . GLN A 1 474 ? -113.679 -7.961  295.001 1.00 30.64  ? 474 GLN A O   1 
ATOM   3606 C  CB  . GLN A 1 474 ? -113.081 -5.245  293.335 1.00 29.24  ? 474 GLN A CB  1 
ATOM   3607 C  CG  . GLN A 1 474 ? -113.729 -4.139  292.519 1.00 32.23  ? 474 GLN A CG  1 
ATOM   3608 C  CD  . GLN A 1 474 ? -115.163 -4.457  292.145 1.00 36.21  ? 474 GLN A CD  1 
ATOM   3609 O  OE1 . GLN A 1 474 ? -115.497 -5.599  291.829 1.00 43.75  ? 474 GLN A OE1 1 
ATOM   3610 N  NE2 . GLN A 1 474 ? -116.022 -3.446  292.184 1.00 43.44  ? 474 GLN A NE2 1 
ATOM   3611 N  N   . LYS A 1 475 ? -112.243 -6.649  296.135 1.00 29.18  ? 475 LYS A N   1 
ATOM   3612 C  CA  . LYS A 1 475 ? -111.651 -7.791  296.827 1.00 31.32  ? 475 LYS A CA  1 
ATOM   3613 C  C   . LYS A 1 475 ? -112.635 -8.413  297.809 1.00 33.84  ? 475 LYS A C   1 
ATOM   3614 O  O   . LYS A 1 475 ? -112.740 -9.642  297.899 1.00 65.99  ? 475 LYS A O   1 
ATOM   3615 C  CB  . LYS A 1 475 ? -110.372 -7.369  297.550 1.00 36.92  ? 475 LYS A CB  1 
ATOM   3616 C  CG  . LYS A 1 475 ? -109.441 -6.488  296.729 1.00 50.23  ? 475 LYS A CG  1 
ATOM   3617 C  CD  . LYS A 1 475 ? -108.056 -6.377  297.365 1.00 44.88  ? 475 LYS A CD  1 
ATOM   3618 C  CE  . LYS A 1 475 ? -108.066 -6.756  298.841 1.00 46.34  ? 475 LYS A CE  1 
ATOM   3619 N  NZ  . LYS A 1 475 ? -106.907 -6.181  299.577 1.00 70.70  ? 475 LYS A NZ  1 
ATOM   3620 N  N   . ASP A 1 476 ? -113.362 -7.583  298.555 1.00 29.44  ? 476 ASP A N   1 
ATOM   3621 C  CA  . ASP A 1 476 ? -114.348 -8.052  299.516 1.00 29.82  ? 476 ASP A CA  1 
ATOM   3622 C  C   . ASP A 1 476 ? -115.741 -8.179  298.910 1.00 30.54  ? 476 ASP A C   1 
ATOM   3623 O  O   . ASP A 1 476 ? -116.732 -8.163  299.648 1.00 33.87  ? 476 ASP A O   1 
ATOM   3624 C  CB  . ASP A 1 476 ? -114.389 -7.113  300.724 1.00 30.18  ? 476 ASP A CB  1 
ATOM   3625 C  CG  . ASP A 1 476 ? -113.026 -6.917  301.355 1.00 29.14  ? 476 ASP A CG  1 
ATOM   3626 O  OD1 . ASP A 1 476 ? -112.160 -7.802  301.190 1.00 33.12  ? 476 ASP A OD1 1 
ATOM   3627 O  OD2 . ASP A 1 476 ? -112.818 -5.877  302.014 1.00 28.02  ? 476 ASP A OD2 1 
ATOM   3628 N  N   . LEU A 1 477 ? -115.835 -8.316  297.585 1.00 27.87  ? 477 LEU A N   1 
ATOM   3629 C  CA  . LEU A 1 477 ? -117.131 -8.248  296.917 1.00 30.74  ? 477 LEU A CA  1 
ATOM   3630 C  C   . LEU A 1 477 ? -118.032 -9.419  297.289 1.00 31.53  ? 477 LEU A C   1 
ATOM   3631 O  O   . LEU A 1 477 ? -119.259 -9.271  297.306 1.00 34.89  ? 477 LEU A O   1 
ATOM   3632 C  CB  . LEU A 1 477 ? -116.933 -8.185  295.402 1.00 39.98  ? 477 LEU A CB  1 
ATOM   3633 C  CG  . LEU A 1 477 ? -118.177 -7.963  294.540 1.00 25.16  ? 477 LEU A CG  1 
ATOM   3634 C  CD1 . LEU A 1 477 ? -118.921 -6.718  294.992 1.00 25.41  ? 477 LEU A CD1 1 
ATOM   3635 C  CD2 . LEU A 1 477 ? -117.797 -7.861  293.072 1.00 25.81  ? 477 LEU A CD2 1 
ATOM   3636 N  N   . ASN A 1 478 ? -117.457 -10.581 297.591 1.00 32.87  ? 478 ASN A N   1 
ATOM   3637 C  CA  . ASN A 1 478 ? -118.242 -11.748 297.971 1.00 35.21  ? 478 ASN A CA  1 
ATOM   3638 C  C   . ASN A 1 478 ? -118.519 -11.814 299.469 1.00 37.00  ? 478 ASN A C   1 
ATOM   3639 O  O   . ASN A 1 478 ? -119.052 -12.821 299.944 1.00 44.88  ? 478 ASN A O   1 
ATOM   3640 C  CB  . ASN A 1 478 ? -117.549 -13.029 297.503 1.00 39.28  ? 478 ASN A CB  1 
ATOM   3641 C  CG  . ASN A 1 478 ? -117.412 -13.092 295.995 1.00 59.69  ? 478 ASN A CG  1 
ATOM   3642 O  OD1 . ASN A 1 478 ? -118.202 -12.492 295.266 1.00 46.11  ? 478 ASN A OD1 1 
ATOM   3643 N  ND2 . ASN A 1 478 ? -116.409 -13.820 295.520 1.00 61.14  ? 478 ASN A ND2 1 
ATOM   3644 N  N   . ASN A 1 479 ? -118.165 -10.771 300.219 1.00 33.10  ? 479 ASN A N   1 
ATOM   3645 C  CA  . ASN A 1 479 ? -118.638 -10.609 301.586 1.00 34.04  ? 479 ASN A CA  1 
ATOM   3646 C  C   . ASN A 1 479 ? -119.869 -9.718  301.673 1.00 46.79  ? 479 ASN A C   1 
ATOM   3647 O  O   . ASN A 1 479 ? -120.492 -9.648  302.738 1.00 48.33  ? 479 ASN A O   1 
ATOM   3648 C  CB  . ASN A 1 479 ? -117.529 -10.032 302.477 1.00 42.20  ? 479 ASN A CB  1 
ATOM   3649 C  CG  . ASN A 1 479 ? -116.273 -10.879 302.466 1.00 39.32  ? 479 ASN A CG  1 
ATOM   3650 O  OD1 . ASN A 1 479 ? -116.326 -12.083 302.217 1.00 39.10  ? 479 ASN A OD1 1 
ATOM   3651 N  ND2 . ASN A 1 479 ? -115.135 -10.253 302.742 1.00 51.68  ? 479 ASN A ND2 1 
ATOM   3652 N  N   . TYR A 1 480 ? -120.231 -9.044  300.586 1.00 34.78  ? 480 TYR A N   1 
ATOM   3653 C  CA  . TYR A 1 480 ? -121.390 -8.169  300.534 1.00 34.22  ? 480 TYR A CA  1 
ATOM   3654 C  C   . TYR A 1 480 ? -122.379 -8.689  299.499 1.00 30.48  ? 480 TYR A C   1 
ATOM   3655 O  O   . TYR A 1 480 ? -122.088 -9.609  298.729 1.00 28.56  ? 480 TYR A O   1 
ATOM   3656 C  CB  . TYR A 1 480 ? -120.984 -6.731  300.188 1.00 44.72  ? 480 TYR A CB  1 
ATOM   3657 C  CG  . TYR A 1 480 ? -119.880 -6.155  301.046 1.00 33.63  ? 480 TYR A CG  1 
ATOM   3658 C  CD1 . TYR A 1 480 ? -120.115 -5.792  302.364 1.00 41.62  ? 480 TYR A CD1 1 
ATOM   3659 C  CD2 . TYR A 1 480 ? -118.608 -5.955  300.528 1.00 30.40  ? 480 TYR A CD2 1 
ATOM   3660 C  CE1 . TYR A 1 480 ? -119.108 -5.260  303.148 1.00 49.78  ? 480 TYR A CE1 1 
ATOM   3661 C  CE2 . TYR A 1 480 ? -117.595 -5.425  301.303 1.00 29.44  ? 480 TYR A CE2 1 
ATOM   3662 C  CZ  . TYR A 1 480 ? -117.850 -5.079  302.612 1.00 34.63  ? 480 TYR A CZ  1 
ATOM   3663 O  OH  . TYR A 1 480 ? -116.845 -4.549  303.387 1.00 34.57  ? 480 TYR A OH  1 
ATOM   3664 N  N   . VAL A 1 481 ? -123.560 -8.081  299.484 1.00 31.31  ? 481 VAL A N   1 
ATOM   3665 C  CA  . VAL A 1 481 ? -124.593 -8.369  298.495 1.00 29.15  ? 481 VAL A CA  1 
ATOM   3666 C  C   . VAL A 1 481 ? -124.755 -7.121  297.639 1.00 28.05  ? 481 VAL A C   1 
ATOM   3667 O  O   . VAL A 1 481 ? -125.211 -6.077  298.123 1.00 27.70  ? 481 VAL A O   1 
ATOM   3668 C  CB  . VAL A 1 481 ? -125.920 -8.776  299.150 1.00 29.10  ? 481 VAL A CB  1 
ATOM   3669 C  CG1 . VAL A 1 481 ? -127.030 -8.824  298.112 1.00 29.84  ? 481 VAL A CG1 1 
ATOM   3670 C  CG2 . VAL A 1 481 ? -125.775 -10.122 299.844 1.00 33.00  ? 481 VAL A CG2 1 
ATOM   3671 N  N   . TYR A 1 482 ? -124.378 -7.224  296.368 1.00 29.10  ? 482 TYR A N   1 
ATOM   3672 C  CA  . TYR A 1 482 ? -124.402 -6.070  295.480 1.00 28.66  ? 482 TYR A CA  1 
ATOM   3673 C  C   . TYR A 1 482 ? -125.833 -5.701  295.113 1.00 30.41  ? 482 TYR A C   1 
ATOM   3674 O  O   . TYR A 1 482 ? -126.696 -6.568  294.951 1.00 30.92  ? 482 TYR A O   1 
ATOM   3675 C  CB  . TYR A 1 482 ? -123.590 -6.361  294.217 1.00 32.57  ? 482 TYR A CB  1 
ATOM   3676 C  CG  . TYR A 1 482 ? -123.592 -5.241  293.201 1.00 32.87  ? 482 TYR A CG  1 
ATOM   3677 C  CD1 . TYR A 1 482 ? -122.711 -4.174  293.315 1.00 35.36  ? 482 TYR A CD1 1 
ATOM   3678 C  CD2 . TYR A 1 482 ? -124.465 -5.256  292.120 1.00 41.20  ? 482 TYR A CD2 1 
ATOM   3679 C  CE1 . TYR A 1 482 ? -122.705 -3.149  292.388 1.00 37.38  ? 482 TYR A CE1 1 
ATOM   3680 C  CE2 . TYR A 1 482 ? -124.466 -4.236  291.187 1.00 43.44  ? 482 TYR A CE2 1 
ATOM   3681 C  CZ  . TYR A 1 482 ? -123.584 -3.186  291.326 1.00 37.72  ? 482 TYR A CZ  1 
ATOM   3682 O  OH  . TYR A 1 482 ? -123.581 -2.168  290.400 1.00 33.77  ? 482 TYR A OH  1 
ATOM   3683 N  N   . THR A 1 483 ? -126.081 -4.399  294.982 1.00 36.45  ? 483 THR A N   1 
ATOM   3684 C  CA  . THR A 1 483 ? -127.395 -3.899  294.599 1.00 38.65  ? 483 THR A CA  1 
ATOM   3685 C  C   . THR A 1 483 ? -127.221 -2.615  293.804 1.00 36.11  ? 483 THR A C   1 
ATOM   3686 O  O   . THR A 1 483 ? -126.565 -1.679  294.269 1.00 34.03  ? 483 THR A O   1 
ATOM   3687 C  CB  . THR A 1 483 ? -128.278 -3.643  295.825 1.00 30.39  ? 483 THR A CB  1 
ATOM   3688 O  OG1 . THR A 1 483 ? -128.407 -4.851  296.585 1.00 32.10  ? 483 THR A OG1 1 
ATOM   3689 C  CG2 . THR A 1 483 ? -129.659 -3.177  295.391 1.00 35.24  ? 483 THR A CG2 1 
ATOM   3690 N  N   . PHE A 1 484 ? -127.807 -2.578  292.613 1.00 38.11  ? 484 PHE A N   1 
ATOM   3691 C  CA  . PHE A 1 484 ? -127.770 -1.413  291.741 1.00 39.63  ? 484 PHE A CA  1 
ATOM   3692 C  C   . PHE A 1 484 ? -129.154 -0.782  291.702 1.00 43.24  ? 484 PHE A C   1 
ATOM   3693 O  O   . PHE A 1 484 ? -130.153 -1.485  291.522 1.00 61.76  ? 484 PHE A O   1 
ATOM   3694 C  CB  . PHE A 1 484 ? -127.314 -1.803  290.333 1.00 40.07  ? 484 PHE A CB  1 
ATOM   3695 C  CG  . PHE A 1 484 ? -127.250 -0.651  289.370 1.00 36.20  ? 484 PHE A CG  1 
ATOM   3696 C  CD1 . PHE A 1 484 ? -126.384 0.407   289.590 1.00 36.48  ? 484 PHE A CD1 1 
ATOM   3697 C  CD2 . PHE A 1 484 ? -128.043 -0.635  288.236 1.00 34.45  ? 484 PHE A CD2 1 
ATOM   3698 C  CE1 . PHE A 1 484 ? -126.320 1.466   288.704 1.00 35.60  ? 484 PHE A CE1 1 
ATOM   3699 C  CE2 . PHE A 1 484 ? -127.982 0.419   287.344 1.00 43.32  ? 484 PHE A CE2 1 
ATOM   3700 C  CZ  . PHE A 1 484 ? -127.119 1.471   287.579 1.00 40.87  ? 484 PHE A CZ  1 
ATOM   3701 N  N   . ASP A 1 485 ? -129.215 0.534   291.883 1.00 40.94  ? 485 ASP A N   1 
ATOM   3702 C  CA  . ASP A 1 485 ? -130.480 1.267   291.878 1.00 30.33  ? 485 ASP A CA  1 
ATOM   3703 C  C   . ASP A 1 485 ? -130.619 1.901   290.497 1.00 33.10  ? 485 ASP A C   1 
ATOM   3704 O  O   . ASP A 1 485 ? -130.238 3.051   290.279 1.00 47.77  ? 485 ASP A O   1 
ATOM   3705 C  CB  . ASP A 1 485 ? -130.513 2.302   292.998 1.00 27.95  ? 485 ASP A CB  1 
ATOM   3706 C  CG  . ASP A 1 485 ? -131.887 2.921   293.191 1.00 29.28  ? 485 ASP A CG  1 
ATOM   3707 O  OD1 . ASP A 1 485 ? -132.676 2.973   292.225 1.00 31.98  ? 485 ASP A OD1 1 
ATOM   3708 O  OD2 . ASP A 1 485 ? -132.179 3.359   294.324 1.00 28.58  ? 485 ASP A OD2 1 
ATOM   3709 N  N   . SER A 1 486 ? -131.180 1.135   289.558 1.00 31.36  ? 486 SER A N   1 
ATOM   3710 C  CA  . SER A 1 486 ? -131.300 1.590   288.177 1.00 35.95  ? 486 SER A CA  1 
ATOM   3711 C  C   . SER A 1 486 ? -132.184 2.820   288.028 1.00 37.80  ? 486 SER A C   1 
ATOM   3712 O  O   . SER A 1 486 ? -132.151 3.459   286.971 1.00 45.23  ? 486 SER A O   1 
ATOM   3713 C  CB  . SER A 1 486 ? -131.838 0.457   287.300 1.00 38.44  ? 486 SER A CB  1 
ATOM   3714 O  OG  . SER A 1 486 ? -133.099 0.007   287.763 1.00 45.24  ? 486 SER A OG  1 
ATOM   3715 N  N   . ALA A 1 487 ? -132.972 3.166   289.047 1.00 38.11  ? 487 ALA A N   1 
ATOM   3716 C  CA  . ALA A 1 487 ? -133.760 4.391   288.988 1.00 35.80  ? 487 ALA A CA  1 
ATOM   3717 C  C   . ALA A 1 487 ? -132.911 5.612   289.318 1.00 33.12  ? 487 ALA A C   1 
ATOM   3718 O  O   . ALA A 1 487 ? -133.024 6.648   288.653 1.00 33.25  ? 487 ALA A O   1 
ATOM   3719 C  CB  . ALA A 1 487 ? -134.952 4.296   289.941 1.00 37.78  ? 487 ALA A CB  1 
ATOM   3720 N  N   . ALA A 1 488 ? -132.055 5.506   290.333 1.00 35.39  ? 488 ALA A N   1 
ATOM   3721 C  CA  . ALA A 1 488 ? -131.198 6.605   290.753 1.00 37.78  ? 488 ALA A CA  1 
ATOM   3722 C  C   . ALA A 1 488 ? -129.811 6.558   290.129 1.00 40.57  ? 488 ALA A C   1 
ATOM   3723 O  O   . ALA A 1 488 ? -129.043 7.511   290.304 1.00 36.28  ? 488 ALA A O   1 
ATOM   3724 C  CB  . ALA A 1 488 ? -131.058 6.613   292.278 1.00 32.97  ? 488 ALA A CB  1 
ATOM   3725 N  N   . GLN A 1 489 ? -129.476 5.480   289.417 1.00 35.53  ? 489 GLN A N   1 
ATOM   3726 C  CA  . GLN A 1 489 ? -128.147 5.291   288.833 1.00 32.91  ? 489 GLN A CA  1 
ATOM   3727 C  C   . GLN A 1 489 ? -127.068 5.309   289.915 1.00 28.39  ? 489 GLN A C   1 
ATOM   3728 O  O   . GLN A 1 489 ? -126.087 6.051   289.838 1.00 28.55  ? 489 GLN A O   1 
ATOM   3729 C  CB  . GLN A 1 489 ? -127.863 6.339   287.752 1.00 29.18  ? 489 GLN A CB  1 
ATOM   3730 C  CG  . GLN A 1 489 ? -128.844 6.330   286.590 1.00 28.16  ? 489 GLN A CG  1 
ATOM   3731 C  CD  . GLN A 1 489 ? -128.503 5.294   285.538 1.00 30.15  ? 489 GLN A CD  1 
ATOM   3732 O  OE1 . GLN A 1 489 ? -128.131 4.164   285.855 1.00 35.28  ? 489 GLN A OE1 1 
ATOM   3733 N  NE2 . GLN A 1 489 ? -128.626 5.677   284.272 1.00 30.51  ? 489 GLN A NE2 1 
ATOM   3734 N  N   . ALA A 1 490 ? -127.262 4.480   290.938 1.00 26.59  ? 490 ALA A N   1 
ATOM   3735 C  CA  . ALA A 1 490 ? -126.321 4.375   292.043 1.00 29.61  ? 490 ALA A CA  1 
ATOM   3736 C  C   . ALA A 1 490 ? -126.203 2.918   292.465 1.00 32.26  ? 490 ALA A C   1 
ATOM   3737 O  O   . ALA A 1 490 ? -127.051 2.084   292.140 1.00 31.66  ? 490 ALA A O   1 
ATOM   3738 C  CB  . ALA A 1 490 ? -126.747 5.239   293.236 1.00 28.47  ? 490 ALA A CB  1 
ATOM   3739 N  N   . SER A 1 491 ? -125.136 2.621   293.203 1.00 32.44  ? 491 SER A N   1 
ATOM   3740 C  CA  . SER A 1 491 ? -124.854 1.270   293.658 1.00 33.65  ? 491 SER A CA  1 
ATOM   3741 C  C   . SER A 1 491 ? -124.519 1.281   295.141 1.00 34.38  ? 491 SER A C   1 
ATOM   3742 O  O   . SER A 1 491 ? -124.058 2.289   295.684 1.00 35.09  ? 491 SER A O   1 
ATOM   3743 C  CB  . SER A 1 491 ? -123.692 0.643   292.874 1.00 45.32  ? 491 SER A CB  1 
ATOM   3744 O  OG  . SER A 1 491 ? -123.947 0.653   291.482 1.00 42.78  ? 491 SER A OG  1 
ATOM   3745 N  N   . TYR A 1 492 ? -124.759 0.146   295.792 1.00 31.26  ? 492 TYR A N   1 
ATOM   3746 C  CA  . TYR A 1 492 ? -124.380 -0.035  297.186 1.00 29.65  ? 492 TYR A CA  1 
ATOM   3747 C  C   . TYR A 1 492 ? -124.284 -1.527  297.466 1.00 33.89  ? 492 TYR A C   1 
ATOM   3748 O  O   . TYR A 1 492 ? -124.733 -2.360  296.675 1.00 39.21  ? 492 TYR A O   1 
ATOM   3749 C  CB  . TYR A 1 492 ? -125.367 0.647   298.139 1.00 29.98  ? 492 TYR A CB  1 
ATOM   3750 C  CG  . TYR A 1 492 ? -126.779 0.111   298.076 1.00 34.35  ? 492 TYR A CG  1 
ATOM   3751 C  CD1 . TYR A 1 492 ? -127.684 0.592   297.140 1.00 38.60  ? 492 TYR A CD1 1 
ATOM   3752 C  CD2 . TYR A 1 492 ? -127.211 -0.867  298.962 1.00 32.54  ? 492 TYR A CD2 1 
ATOM   3753 C  CE1 . TYR A 1 492 ? -128.976 0.109   297.082 1.00 31.19  ? 492 TYR A CE1 1 
ATOM   3754 C  CE2 . TYR A 1 492 ? -128.501 -1.357  298.911 1.00 33.92  ? 492 TYR A CE2 1 
ATOM   3755 C  CZ  . TYR A 1 492 ? -129.379 -0.865  297.970 1.00 31.69  ? 492 TYR A CZ  1 
ATOM   3756 O  OH  . TYR A 1 492 ? -130.666 -1.349  297.915 1.00 32.90  ? 492 TYR A OH  1 
ATOM   3757 N  N   . VAL A 1 493 ? -123.686 -1.854  298.609 1.00 34.05  ? 493 VAL A N   1 
ATOM   3758 C  CA  . VAL A 1 493 ? -123.482 -3.236  299.024 1.00 32.23  ? 493 VAL A CA  1 
ATOM   3759 C  C   . VAL A 1 493 ? -123.851 -3.363  300.494 1.00 33.49  ? 493 VAL A C   1 
ATOM   3760 O  O   . VAL A 1 493 ? -123.794 -2.391  301.254 1.00 33.07  ? 493 VAL A O   1 
ATOM   3761 C  CB  . VAL A 1 493 ? -122.030 -3.699  298.780 1.00 31.53  ? 493 VAL A CB  1 
ATOM   3762 C  CG1 . VAL A 1 493 ? -121.761 -3.857  297.292 1.00 32.69  ? 493 VAL A CG1 1 
ATOM   3763 C  CG2 . VAL A 1 493 ? -121.048 -2.721  299.406 1.00 46.98  ? 493 VAL A CG2 1 
ATOM   3764 N  N   . PHE A 1 494 ? -124.231 -4.575  300.897 1.00 33.39  ? 494 PHE A N   1 
ATOM   3765 C  CA  . PHE A 1 494 ? -124.675 -4.821  302.260 1.00 37.43  ? 494 PHE A CA  1 
ATOM   3766 C  C   . PHE A 1 494 ? -124.196 -6.188  302.726 1.00 36.84  ? 494 PHE A C   1 
ATOM   3767 O  O   . PHE A 1 494 ? -124.120 -7.138  301.943 1.00 35.49  ? 494 PHE A O   1 
ATOM   3768 C  CB  . PHE A 1 494 ? -126.203 -4.738  302.379 1.00 41.11  ? 494 PHE A CB  1 
ATOM   3769 C  CG  . PHE A 1 494 ? -126.703 -4.815  303.792 1.00 43.59  ? 494 PHE A CG  1 
ATOM   3770 C  CD1 . PHE A 1 494 ? -126.613 -3.717  304.631 1.00 48.88  ? 494 PHE A CD1 1 
ATOM   3771 C  CD2 . PHE A 1 494 ? -127.263 -5.982  304.282 1.00 51.30  ? 494 PHE A CD2 1 
ATOM   3772 C  CE1 . PHE A 1 494 ? -127.071 -3.782  305.933 1.00 56.76  ? 494 PHE A CE1 1 
ATOM   3773 C  CE2 . PHE A 1 494 ? -127.723 -6.051  305.584 1.00 51.86  ? 494 PHE A CE2 1 
ATOM   3774 C  CZ  . PHE A 1 494 ? -127.627 -4.951  306.410 1.00 57.28  ? 494 PHE A CZ  1 
ATOM   3775 N  N   . ASP A 1 495 ? -123.880 -6.273  304.017 1.00 39.22  ? 495 ASP A N   1 
ATOM   3776 C  CA  . ASP A 1 495 ? -123.435 -7.514  304.647 1.00 43.38  ? 495 ASP A CA  1 
ATOM   3777 C  C   . ASP A 1 495 ? -124.151 -7.640  305.984 1.00 50.42  ? 495 ASP A C   1 
ATOM   3778 O  O   . ASP A 1 495 ? -123.844 -6.901  306.924 1.00 49.88  ? 495 ASP A O   1 
ATOM   3779 C  CB  . ASP A 1 495 ? -121.918 -7.528  304.836 1.00 44.64  ? 495 ASP A CB  1 
ATOM   3780 C  CG  . ASP A 1 495 ? -121.422 -8.804  305.485 1.00 52.17  ? 495 ASP A CG  1 
ATOM   3781 O  OD1 . ASP A 1 495 ? -122.137 -9.826  305.420 1.00 76.84  ? 495 ASP A OD1 1 
ATOM   3782 O  OD2 . ASP A 1 495 ? -120.314 -8.784  306.062 1.00 58.55  ? 495 ASP A OD2 1 
ATOM   3783 N  N   . LYS A 1 496 ? -125.097 -8.577  306.071 1.00 59.40  ? 496 LYS A N   1 
ATOM   3784 C  CA  . LYS A 1 496 ? -125.893 -8.735  307.283 1.00 58.74  ? 496 LYS A CA  1 
ATOM   3785 C  C   . LYS A 1 496 ? -125.099 -9.309  308.450 1.00 54.80  ? 496 LYS A C   1 
ATOM   3786 O  O   . LYS A 1 496 ? -125.599 -9.289  309.580 1.00 54.25  ? 496 LYS A O   1 
ATOM   3787 C  CB  . LYS A 1 496 ? -127.105 -9.625  307.004 1.00 68.38  ? 496 LYS A CB  1 
ATOM   3788 C  CG  . LYS A 1 496 ? -127.641 -9.525  305.587 1.00 65.86  ? 496 LYS A CG  1 
ATOM   3789 C  CD  . LYS A 1 496 ? -128.963 -10.262 305.445 1.00 80.20  ? 496 LYS A CD  1 
ATOM   3790 C  CE  . LYS A 1 496 ? -130.079 -9.534  306.180 1.00 95.35  ? 496 LYS A CE  1 
ATOM   3791 N  NZ  . LYS A 1 496 ? -131.341 -9.499  305.390 1.00 82.53  ? 496 LYS A NZ  1 
ATOM   3792 N  N   . SER A 1 497 ? -123.889 -9.818  308.212 1.00 56.89  ? 497 SER A N   1 
ATOM   3793 C  CA  . SER A 1 497 ? -123.101 -10.390 309.300 1.00 57.32  ? 497 SER A CA  1 
ATOM   3794 C  C   . SER A 1 497 ? -122.677 -9.316  310.294 1.00 56.68  ? 497 SER A C   1 
ATOM   3795 O  O   . SER A 1 497 ? -122.837 -9.482  311.509 1.00 73.58  ? 497 SER A O   1 
ATOM   3796 C  CB  . SER A 1 497 ? -121.881 -11.119 308.738 1.00 62.06  ? 497 SER A CB  1 
ATOM   3797 O  OG  . SER A 1 497 ? -120.970 -10.210 308.148 1.00 65.29  ? 497 SER A OG  1 
ATOM   3798 N  N   . LYS A 1 498 ? -122.134 -8.204  309.797 1.00 58.11  ? 498 LYS A N   1 
ATOM   3799 C  CA  . LYS A 1 498 ? -121.721 -7.094  310.646 1.00 66.19  ? 498 LYS A CA  1 
ATOM   3800 C  C   . LYS A 1 498 ? -122.480 -5.808  310.339 1.00 50.86  ? 498 LYS A C   1 
ATOM   3801 O  O   . LYS A 1 498 ? -122.135 -4.753  310.883 1.00 55.19  ? 498 LYS A O   1 
ATOM   3802 C  CB  . LYS A 1 498 ? -120.212 -6.855  310.520 1.00 60.60  ? 498 LYS A CB  1 
ATOM   3803 C  CG  . LYS A 1 498 ? -119.413 -8.073  310.077 1.00 53.91  ? 498 LYS A CG  1 
ATOM   3804 C  CD  . LYS A 1 498 ? -119.267 -9.080  311.208 1.00 58.90  ? 498 LYS A CD  1 
ATOM   3805 C  CE  . LYS A 1 498 ? -118.364 -10.236 310.809 1.00 52.88  ? 498 LYS A CE  1 
ATOM   3806 N  NZ  . LYS A 1 498 ? -118.176 -11.209 311.921 1.00 46.47  ? 498 LYS A NZ  1 
ATOM   3807 N  N   . GLY A 1 499 ? -123.499 -5.867  309.488 1.00 48.71  ? 499 GLY A N   1 
ATOM   3808 C  CA  . GLY A 1 499 ? -124.291 -4.688  309.175 1.00 52.46  ? 499 GLY A CA  1 
ATOM   3809 C  C   . GLY A 1 499 ? -123.550 -3.622  308.398 1.00 58.65  ? 499 GLY A C   1 
ATOM   3810 O  O   . GLY A 1 499 ? -123.777 -2.426  308.624 1.00 57.62  ? 499 GLY A O   1 
ATOM   3811 N  N   . ASP A 1 500 ? -122.671 -4.023  307.483 1.00 54.71  ? 500 ASP A N   1 
ATOM   3812 C  CA  . ASP A 1 500 ? -121.866 -3.084  306.709 1.00 40.85  ? 500 ASP A CA  1 
ATOM   3813 C  C   . ASP A 1 500 ? -122.634 -2.692  305.451 1.00 38.36  ? 500 ASP A C   1 
ATOM   3814 O  O   . ASP A 1 500 ? -122.835 -3.517  304.555 1.00 40.70  ? 500 ASP A O   1 
ATOM   3815 C  CB  . ASP A 1 500 ? -120.513 -3.696  306.358 1.00 42.96  ? 500 ASP A CB  1 
ATOM   3816 C  CG  . ASP A 1 500 ? -119.645 -3.927  307.579 1.00 52.35  ? 500 ASP A CG  1 
ATOM   3817 O  OD1 . ASP A 1 500 ? -119.690 -3.093  308.507 1.00 48.89  ? 500 ASP A OD1 1 
ATOM   3818 O  OD2 . ASP A 1 500 ? -118.916 -4.941  307.608 1.00 55.53  ? 500 ASP A OD2 1 
ATOM   3819 N  N   . LEU A 1 501 ? -123.060 -1.432  305.385 1.00 36.28  ? 501 LEU A N   1 
ATOM   3820 C  CA  . LEU A 1 501 ? -123.790 -0.891  304.242 1.00 36.99  ? 501 LEU A CA  1 
ATOM   3821 C  C   . LEU A 1 501 ? -122.964 0.241   303.646 1.00 38.14  ? 501 LEU A C   1 
ATOM   3822 O  O   . LEU A 1 501 ? -122.846 1.309   304.253 1.00 36.54  ? 501 LEU A O   1 
ATOM   3823 C  CB  . LEU A 1 501 ? -125.174 -0.399  304.661 1.00 41.59  ? 501 LEU A CB  1 
ATOM   3824 C  CG  . LEU A 1 501 ? -125.946 0.434   303.636 1.00 37.02  ? 501 LEU A CG  1 
ATOM   3825 C  CD1 . LEU A 1 501 ? -126.311 -0.403  302.421 1.00 40.86  ? 501 LEU A CD1 1 
ATOM   3826 C  CD2 . LEU A 1 501 ? -127.186 1.040   304.271 1.00 42.95  ? 501 LEU A CD2 1 
ATOM   3827 N  N   . ILE A 1 502 ? -122.408 0.014   302.459 1.00 38.78  ? 502 ILE A N   1 
ATOM   3828 C  CA  . ILE A 1 502 ? -121.468 0.937   301.831 1.00 38.43  ? 502 ILE A CA  1 
ATOM   3829 C  C   . ILE A 1 502 ? -122.050 1.410   300.507 1.00 32.59  ? 502 ILE A C   1 
ATOM   3830 O  O   . ILE A 1 502 ? -122.479 0.592   299.685 1.00 31.37  ? 502 ILE A O   1 
ATOM   3831 C  CB  . ILE A 1 502 ? -120.093 0.280   301.617 1.00 37.88  ? 502 ILE A CB  1 
ATOM   3832 C  CG1 . ILE A 1 502 ? -119.490 -0.140  302.959 1.00 34.00  ? 502 ILE A CG1 1 
ATOM   3833 C  CG2 . ILE A 1 502 ? -119.157 1.223   300.878 1.00 38.47  ? 502 ILE A CG2 1 
ATOM   3834 C  CD1 . ILE A 1 502 ? -118.241 -0.978  302.827 1.00 34.19  ? 502 ILE A CD1 1 
ATOM   3835 N  N   . SER A 1 503 ? -122.055 2.724   300.300 1.00 32.32  ? 503 SER A N   1 
ATOM   3836 C  CA  . SER A 1 503 ? -122.500 3.335   299.054 1.00 30.33  ? 503 SER A CA  1 
ATOM   3837 C  C   . SER A 1 503 ? -121.290 3.845   298.286 1.00 29.89  ? 503 SER A C   1 
ATOM   3838 O  O   . SER A 1 503 ? -120.470 4.586   298.837 1.00 33.67  ? 503 SER A O   1 
ATOM   3839 C  CB  . SER A 1 503 ? -123.477 4.482   299.322 1.00 26.76  ? 503 SER A CB  1 
ATOM   3840 O  OG  . SER A 1 503 ? -123.716 5.229   298.142 1.00 27.81  ? 503 SER A OG  1 
ATOM   3841 N  N   . PHE A 1 504 ? -121.185 3.457   297.018 1.00 30.38  ? 504 PHE A N   1 
ATOM   3842 C  CA  . PHE A 1 504 ? -120.024 3.797   296.206 1.00 31.81  ? 504 PHE A CA  1 
ATOM   3843 C  C   . PHE A 1 504 ? -120.457 3.907   294.748 1.00 31.24  ? 504 PHE A C   1 
ATOM   3844 O  O   . PHE A 1 504 ? -121.647 3.837   294.426 1.00 30.00  ? 504 PHE A O   1 
ATOM   3845 C  CB  . PHE A 1 504 ? -118.910 2.760   296.400 1.00 28.26  ? 504 PHE A CB  1 
ATOM   3846 C  CG  . PHE A 1 504 ? -119.241 1.400   295.852 1.00 31.21  ? 504 PHE A CG  1 
ATOM   3847 C  CD1 . PHE A 1 504 ? -120.010 0.511   296.584 1.00 32.22  ? 504 PHE A CD1 1 
ATOM   3848 C  CD2 . PHE A 1 504 ? -118.776 1.006   294.608 1.00 34.34  ? 504 PHE A CD2 1 
ATOM   3849 C  CE1 . PHE A 1 504 ? -120.315 -0.740  296.085 1.00 31.91  ? 504 PHE A CE1 1 
ATOM   3850 C  CE2 . PHE A 1 504 ? -119.077 -0.245  294.102 1.00 32.90  ? 504 PHE A CE2 1 
ATOM   3851 C  CZ  . PHE A 1 504 ? -119.847 -1.119  294.842 1.00 29.98  ? 504 PHE A CZ  1 
ATOM   3852 N  N   . ASP A 1 505 ? -119.478 4.084   293.862 1.00 31.38  ? 505 ASP A N   1 
ATOM   3853 C  CA  . ASP A 1 505 ? -119.702 4.169   292.423 1.00 32.54  ? 505 ASP A CA  1 
ATOM   3854 C  C   . ASP A 1 505 ? -119.111 2.928   291.768 1.00 33.96  ? 505 ASP A C   1 
ATOM   3855 O  O   . ASP A 1 505 ? -117.889 2.739   291.772 1.00 41.60  ? 505 ASP A O   1 
ATOM   3856 C  CB  . ASP A 1 505 ? -119.078 5.437   291.842 1.00 31.27  ? 505 ASP A CB  1 
ATOM   3857 C  CG  . ASP A 1 505 ? -120.095 6.533   291.606 1.00 35.63  ? 505 ASP A CG  1 
ATOM   3858 O  OD1 . ASP A 1 505 ? -121.302 6.220   291.534 1.00 44.29  ? 505 ASP A OD1 1 
ATOM   3859 O  OD2 . ASP A 1 505 ? -119.688 7.707   291.485 1.00 34.48  ? 505 ASP A OD2 1 
ATOM   3860 N  N   . SER A 1 506 ? -119.974 2.086   291.208 1.00 31.00  ? 506 SER A N   1 
ATOM   3861 C  CA  . SER A 1 506 ? -119.534 0.907   290.483 1.00 29.74  ? 506 SER A CA  1 
ATOM   3862 C  C   . SER A 1 506 ? -119.421 1.231   288.995 1.00 29.70  ? 506 SER A C   1 
ATOM   3863 O  O   . SER A 1 506 ? -119.600 2.372   288.566 1.00 30.19  ? 506 SER A O   1 
ATOM   3864 C  CB  . SER A 1 506 ? -120.494 -0.256  290.723 1.00 38.80  ? 506 SER A CB  1 
ATOM   3865 O  OG  . SER A 1 506 ? -121.768 0.012   290.164 1.00 37.70  ? 506 SER A OG  1 
ATOM   3866 N  N   . VAL A 1 507 ? -119.116 0.209   288.193 1.00 32.11  ? 507 VAL A N   1 
ATOM   3867 C  CA  . VAL A 1 507 ? -119.043 0.404   286.748 1.00 33.58  ? 507 VAL A CA  1 
ATOM   3868 C  C   . VAL A 1 507 ? -120.415 0.764   286.193 1.00 37.79  ? 507 VAL A C   1 
ATOM   3869 O  O   . VAL A 1 507 ? -120.533 1.556   285.250 1.00 35.08  ? 507 VAL A O   1 
ATOM   3870 C  CB  . VAL A 1 507 ? -118.467 -0.853  286.068 1.00 36.12  ? 507 VAL A CB  1 
ATOM   3871 C  CG1 . VAL A 1 507 ? -118.310 -0.627  284.571 1.00 35.92  ? 507 VAL A CG1 1 
ATOM   3872 C  CG2 . VAL A 1 507 ? -117.138 -1.235  286.700 1.00 79.00  ? 507 VAL A CG2 1 
ATOM   3873 N  N   . ASP A 1 508 ? -121.473 0.198   286.779 1.00 34.77  ? 508 ASP A N   1 
ATOM   3874 C  CA  . ASP A 1 508 ? -122.826 0.485   286.313 1.00 33.69  ? 508 ASP A CA  1 
ATOM   3875 C  C   . ASP A 1 508 ? -123.186 1.948   286.537 1.00 37.76  ? 508 ASP A C   1 
ATOM   3876 O  O   . ASP A 1 508 ? -123.648 2.634   285.618 1.00 46.11  ? 508 ASP A O   1 
ATOM   3877 C  CB  . ASP A 1 508 ? -123.826 -0.428  287.024 1.00 33.01  ? 508 ASP A CB  1 
ATOM   3878 C  CG  . ASP A 1 508 ? -123.578 -1.897  286.746 1.00 33.94  ? 508 ASP A CG  1 
ATOM   3879 O  OD1 . ASP A 1 508 ? -123.153 -2.228  285.619 1.00 36.01  ? 508 ASP A OD1 1 
ATOM   3880 O  OD2 . ASP A 1 508 ? -123.806 -2.720  287.657 1.00 32.78  ? 508 ASP A OD2 1 
ATOM   3881 N  N   . SER A 1 509 ? -122.978 2.444   287.759 1.00 36.97  ? 509 SER A N   1 
ATOM   3882 C  CA  . SER A 1 509 ? -123.352 3.819   288.076 1.00 31.33  ? 509 SER A CA  1 
ATOM   3883 C  C   . SER A 1 509 ? -122.524 4.820   287.282 1.00 28.85  ? 509 SER A C   1 
ATOM   3884 O  O   . SER A 1 509 ? -123.046 5.845   286.830 1.00 29.65  ? 509 SER A O   1 
ATOM   3885 C  CB  . SER A 1 509 ? -123.202 4.069   289.576 1.00 31.52  ? 509 SER A CB  1 
ATOM   3886 O  OG  . SER A 1 509 ? -121.880 3.799   290.005 1.00 39.59  ? 509 SER A OG  1 
ATOM   3887 N  N   . VAL A 1 510 ? -121.231 4.541   287.101 1.00 30.40  ? 510 VAL A N   1 
ATOM   3888 C  CA  . VAL A 1 510 ? -120.381 5.444   286.332 1.00 30.35  ? 510 VAL A CA  1 
ATOM   3889 C  C   . VAL A 1 510 ? -120.819 5.477   284.874 1.00 29.83  ? 510 VAL A C   1 
ATOM   3890 O  O   . VAL A 1 510 ? -120.877 6.545   284.253 1.00 29.63  ? 510 VAL A O   1 
ATOM   3891 C  CB  . VAL A 1 510 ? -118.903 5.038   286.473 1.00 32.60  ? 510 VAL A CB  1 
ATOM   3892 C  CG1 . VAL A 1 510 ? -118.038 5.828   285.504 1.00 29.75  ? 510 VAL A CG1 1 
ATOM   3893 C  CG2 . VAL A 1 510 ? -118.433 5.257   287.901 1.00 28.76  ? 510 VAL A CG2 1 
ATOM   3894 N  N   . LEU A 1 511 ? -121.142 4.312   284.305 1.00 31.99  ? 511 LEU A N   1 
ATOM   3895 C  CA  . LEU A 1 511 ? -121.609 4.273   282.923 1.00 37.97  ? 511 LEU A CA  1 
ATOM   3896 C  C   . LEU A 1 511 ? -122.914 5.037   282.754 1.00 40.06  ? 511 LEU A C   1 
ATOM   3897 O  O   . LEU A 1 511 ? -123.146 5.643   281.701 1.00 45.72  ? 511 LEU A O   1 
ATOM   3898 C  CB  . LEU A 1 511 ? -121.771 2.825   282.462 1.00 35.61  ? 511 LEU A CB  1 
ATOM   3899 C  CG  . LEU A 1 511 ? -120.478 2.132   282.029 1.00 40.19  ? 511 LEU A CG  1 
ATOM   3900 C  CD1 . LEU A 1 511 ? -120.676 0.628   281.929 1.00 39.90  ? 511 LEU A CD1 1 
ATOM   3901 C  CD2 . LEU A 1 511 ? -119.972 2.703   280.713 1.00 66.61  ? 511 LEU A CD2 1 
ATOM   3902 N  N   . GLY A 1 512 ? -123.777 5.021   283.772 1.00 36.29  ? 512 GLY A N   1 
ATOM   3903 C  CA  . GLY A 1 512 ? -124.956 5.867   283.737 1.00 41.87  ? 512 GLY A CA  1 
ATOM   3904 C  C   . GLY A 1 512 ? -124.614 7.342   283.785 1.00 36.72  ? 512 GLY A C   1 
ATOM   3905 O  O   . GLY A 1 512 ? -125.308 8.165   283.181 1.00 44.33  ? 512 GLY A O   1 
ATOM   3906 N  N   . LYS A 1 513 ? -123.541 7.697   284.496 1.00 32.13  ? 513 LYS A N   1 
ATOM   3907 C  CA  . LYS A 1 513 ? -123.084 9.080   284.524 1.00 33.12  ? 513 LYS A CA  1 
ATOM   3908 C  C   . LYS A 1 513 ? -122.511 9.521   283.185 1.00 34.12  ? 513 LYS A C   1 
ATOM   3909 O  O   . LYS A 1 513 ? -122.483 10.724  282.904 1.00 41.28  ? 513 LYS A O   1 
ATOM   3910 C  CB  . LYS A 1 513 ? -122.032 9.267   285.619 1.00 29.38  ? 513 LYS A CB  1 
ATOM   3911 C  CG  . LYS A 1 513 ? -122.542 9.023   287.027 1.00 23.19  ? 513 LYS A CG  1 
ATOM   3912 C  CD  . LYS A 1 513 ? -121.501 9.405   288.065 1.00 22.12  ? 513 LYS A CD  1 
ATOM   3913 C  CE  . LYS A 1 513 ? -122.068 9.319   289.473 1.00 22.01  ? 513 LYS A CE  1 
ATOM   3914 N  NZ  . LYS A 1 513 ? -121.091 9.778   290.498 1.00 25.36  ? 513 LYS A NZ  1 
ATOM   3915 N  N   . VAL A 1 514 ? -122.055 8.579   282.358 1.00 35.22  ? 514 VAL A N   1 
ATOM   3916 C  CA  . VAL A 1 514 ? -121.458 8.938   281.075 1.00 36.48  ? 514 VAL A CA  1 
ATOM   3917 C  C   . VAL A 1 514 ? -122.506 9.539   280.148 1.00 47.32  ? 514 VAL A C   1 
ATOM   3918 O  O   . VAL A 1 514 ? -122.295 10.603  279.554 1.00 50.65  ? 514 VAL A O   1 
ATOM   3919 C  CB  . VAL A 1 514 ? -120.778 7.713   280.438 1.00 35.14  ? 514 VAL A CB  1 
ATOM   3920 C  CG1 . VAL A 1 514 ? -120.253 8.061   279.055 1.00 40.40  ? 514 VAL A CG1 1 
ATOM   3921 C  CG2 . VAL A 1 514 ? -119.653 7.211   281.327 1.00 35.59  ? 514 VAL A CG2 1 
ATOM   3922 N  N   . LYS A 1 515 ? -123.654 8.870   280.012 1.00 43.19  ? 515 LYS A N   1 
ATOM   3923 C  CA  . LYS A 1 515 ? -124.692 9.374   279.119 1.00 44.78  ? 515 LYS A CA  1 
ATOM   3924 C  C   . LYS A 1 515 ? -125.360 10.624  279.676 1.00 43.06  ? 515 LYS A C   1 
ATOM   3925 O  O   . LYS A 1 515 ? -125.802 11.482  278.903 1.00 44.41  ? 515 LYS A O   1 
ATOM   3926 C  CB  . LYS A 1 515 ? -125.726 8.284   278.844 1.00 66.83  ? 515 LYS A CB  1 
ATOM   3927 C  CG  . LYS A 1 515 ? -125.115 6.927   278.543 1.00 77.89  ? 515 LYS A CG  1 
ATOM   3928 C  CD  . LYS A 1 515 ? -126.013 6.107   277.635 1.00 72.70  ? 515 LYS A CD  1 
ATOM   3929 C  CE  . LYS A 1 515 ? -126.059 4.653   278.065 1.00 69.13  ? 515 LYS A CE  1 
ATOM   3930 N  NZ  . LYS A 1 515 ? -126.821 3.816   277.097 1.00 74.19  ? 515 LYS A NZ  1 
ATOM   3931 N  N   . TYR A 1 516 ? -125.447 10.749  281.004 1.00 38.54  ? 516 TYR A N   1 
ATOM   3932 C  CA  . TYR A 1 516 ? -125.899 12.010  281.583 1.00 35.88  ? 516 TYR A CA  1 
ATOM   3933 C  C   . TYR A 1 516 ? -124.968 13.153  281.206 1.00 37.01  ? 516 TYR A C   1 
ATOM   3934 O  O   . TYR A 1 516 ? -125.402 14.306  281.112 1.00 53.90  ? 516 TYR A O   1 
ATOM   3935 C  CB  . TYR A 1 516 ? -126.007 11.896  283.104 1.00 35.87  ? 516 TYR A CB  1 
ATOM   3936 C  CG  . TYR A 1 516 ? -126.676 13.092  283.741 1.00 34.54  ? 516 TYR A CG  1 
ATOM   3937 C  CD1 . TYR A 1 516 ? -128.059 13.204  283.775 1.00 45.43  ? 516 TYR A CD1 1 
ATOM   3938 C  CD2 . TYR A 1 516 ? -125.922 14.119  284.293 1.00 36.06  ? 516 TYR A CD2 1 
ATOM   3939 C  CE1 . TYR A 1 516 ? -128.673 14.301  284.349 1.00 36.12  ? 516 TYR A CE1 1 
ATOM   3940 C  CE2 . TYR A 1 516 ? -126.526 15.219  284.868 1.00 42.35  ? 516 TYR A CE2 1 
ATOM   3941 C  CZ  . TYR A 1 516 ? -127.901 15.305  284.894 1.00 36.08  ? 516 TYR A CZ  1 
ATOM   3942 O  OH  . TYR A 1 516 ? -128.503 16.401  285.466 1.00 34.89  ? 516 TYR A OH  1 
ATOM   3943 N  N   . VAL A 1 517 ? -123.688 12.854  280.990 1.00 38.41  ? 517 VAL A N   1 
ATOM   3944 C  CA  . VAL A 1 517 ? -122.760 13.863  280.498 1.00 35.58  ? 517 VAL A CA  1 
ATOM   3945 C  C   . VAL A 1 517 ? -122.871 14.000  278.983 1.00 40.80  ? 517 VAL A C   1 
ATOM   3946 O  O   . VAL A 1 517 ? -122.694 15.097  278.439 1.00 56.85  ? 517 VAL A O   1 
ATOM   3947 C  CB  . VAL A 1 517 ? -121.327 13.508  280.937 1.00 34.81  ? 517 VAL A CB  1 
ATOM   3948 C  CG1 . VAL A 1 517 ? -120.294 14.310  280.156 1.00 46.79  ? 517 VAL A CG1 1 
ATOM   3949 C  CG2 . VAL A 1 517 ? -121.160 13.724  282.432 1.00 31.48  ? 517 VAL A CG2 1 
ATOM   3950 N  N   . ASP A 1 518 ? -123.202 12.911  278.287 1.00 42.79  ? 518 ASP A N   1 
ATOM   3951 C  CA  . ASP A 1 518 ? -123.136 12.862  276.831 1.00 44.87  ? 518 ASP A CA  1 
ATOM   3952 C  C   . ASP A 1 518 ? -124.072 13.861  276.161 1.00 46.35  ? 518 ASP A C   1 
ATOM   3953 O  O   . ASP A 1 518 ? -123.607 14.821  275.538 1.00 61.50  ? 518 ASP A O   1 
ATOM   3954 C  CB  . ASP A 1 518 ? -123.435 11.445  276.339 1.00 47.48  ? 518 ASP A CB  1 
ATOM   3955 C  CG  . ASP A 1 518 ? -122.245 10.517  276.484 1.00 45.34  ? 518 ASP A CG  1 
ATOM   3956 O  OD1 . ASP A 1 518 ? -121.126 11.021  276.728 1.00 43.62  ? 518 ASP A OD1 1 
ATOM   3957 O  OD2 . ASP A 1 518 ? -122.424 9.288   276.357 1.00 47.11  ? 518 ASP A OD2 1 
ATOM   3958 N  N   . ARG A 1 519 ? -125.388 13.653  276.263 1.00 48.34  ? 519 ARG A N   1 
ATOM   3959 C  CA  . ARG A 1 519 ? -126.332 14.516  275.559 1.00 52.46  ? 519 ARG A CA  1 
ATOM   3960 C  C   . ARG A 1 519 ? -127.214 15.335  276.495 1.00 59.72  ? 519 ARG A C   1 
ATOM   3961 O  O   . ARG A 1 519 ? -128.284 15.799  276.087 1.00 74.66  ? 519 ARG A O   1 
ATOM   3962 C  CB  . ARG A 1 519 ? -127.173 13.708  274.571 1.00 68.32  ? 519 ARG A CB  1 
ATOM   3963 C  CG  . ARG A 1 519 ? -126.308 13.021  273.533 1.00 68.59  ? 519 ARG A CG  1 
ATOM   3964 C  CD  . ARG A 1 519 ? -126.625 13.520  272.135 1.00 95.14  ? 519 ARG A CD  1 
ATOM   3965 N  NE  . ARG A 1 519 ? -125.404 13.813  271.393 1.00 92.99  ? 519 ARG A NE  1 
ATOM   3966 C  CZ  . ARG A 1 519 ? -125.355 14.560  270.295 1.00 68.21  ? 519 ARG A CZ  1 
ATOM   3967 N  NH1 . ARG A 1 519 ? -126.461 15.102  269.808 1.00 68.28  ? 519 ARG A NH1 1 
ATOM   3968 N  NH2 . ARG A 1 519 ? -124.194 14.772  269.687 1.00 64.50  ? 519 ARG A NH2 1 
ATOM   3969 N  N   . ASN A 1 520 ? -126.792 15.521  277.741 1.00 43.12  ? 520 ASN A N   1 
ATOM   3970 C  CA  . ASN A 1 520 ? -127.015 16.793  278.412 1.00 37.97  ? 520 ASN A CA  1 
ATOM   3971 C  C   . ASN A 1 520 ? -125.897 17.770  278.086 1.00 38.83  ? 520 ASN A C   1 
ATOM   3972 O  O   . ASN A 1 520 ? -125.876 18.883  278.623 1.00 38.99  ? 520 ASN A O   1 
ATOM   3973 C  CB  . ASN A 1 520 ? -127.132 16.606  279.928 1.00 33.46  ? 520 ASN A CB  1 
ATOM   3974 C  CG  . ASN A 1 520 ? -128.336 15.774  280.324 1.00 35.80  ? 520 ASN A CG  1 
ATOM   3975 O  OD1 . ASN A 1 520 ? -128.225 14.573  280.567 1.00 39.76  ? 520 ASN A OD1 1 
ATOM   3976 N  ND2 . ASN A 1 520 ? -129.498 16.414  280.393 1.00 44.48  ? 520 ASN A ND2 1 
ATOM   3977 N  N   . LYS A 1 521 ? -124.968 17.352  277.222 1.00 40.18  ? 521 LYS A N   1 
ATOM   3978 C  CA  . LYS A 1 521 ? -123.874 18.180  276.718 1.00 37.11  ? 521 LYS A CA  1 
ATOM   3979 C  C   . LYS A 1 521 ? -122.995 18.698  277.851 1.00 33.17  ? 521 LYS A C   1 
ATOM   3980 O  O   . LYS A 1 521 ? -122.512 19.831  277.822 1.00 33.38  ? 521 LYS A O   1 
ATOM   3981 C  CB  . LYS A 1 521 ? -124.400 19.328  275.854 1.00 38.03  ? 521 LYS A CB  1 
ATOM   3982 C  CG  . LYS A 1 521 ? -125.047 18.870  274.547 1.00 41.00  ? 521 LYS A CG  1 
ATOM   3983 C  CD  . LYS A 1 521 ? -124.322 17.681  273.912 1.00 43.31  ? 521 LYS A CD  1 
ATOM   3984 C  CE  . LYS A 1 521 ? -122.959 18.061  273.345 1.00 51.52  ? 521 LYS A CE  1 
ATOM   3985 N  NZ  . LYS A 1 521 ? -122.148 16.855  273.013 1.00 48.25  ? 521 LYS A NZ  1 
ATOM   3986 N  N   . LEU A 1 522 ? -122.773 17.854  278.853 1.00 32.87  ? 522 LEU A N   1 
ATOM   3987 C  CA  . LEU A 1 522 ? -121.871 18.208  279.933 1.00 31.76  ? 522 LEU A CA  1 
ATOM   3988 C  C   . LEU A 1 522 ? -120.422 18.005  279.498 1.00 31.10  ? 522 LEU A C   1 
ATOM   3989 O  O   . LEU A 1 522 ? -120.122 17.239  278.577 1.00 32.16  ? 522 LEU A O   1 
ATOM   3990 C  CB  . LEU A 1 522 ? -122.186 17.392  281.186 1.00 33.53  ? 522 LEU A CB  1 
ATOM   3991 C  CG  . LEU A 1 522 ? -123.580 17.669  281.758 1.00 31.17  ? 522 LEU A CG  1 
ATOM   3992 C  CD1 . LEU A 1 522 ? -123.811 16.902  283.046 1.00 28.11  ? 522 LEU A CD1 1 
ATOM   3993 C  CD2 . LEU A 1 522 ? -123.784 19.162  281.975 1.00 30.14  ? 522 LEU A CD2 1 
ATOM   3994 N  N   . GLY A 1 523 ? -119.518 18.716  280.175 1.00 32.36  ? 523 GLY A N   1 
ATOM   3995 C  CA  . GLY A 1 523 ? -118.134 18.754  279.730 1.00 30.97  ? 523 GLY A CA  1 
ATOM   3996 C  C   . GLY A 1 523 ? -117.431 17.414  279.827 1.00 28.55  ? 523 GLY A C   1 
ATOM   3997 O  O   . GLY A 1 523 ? -116.725 17.006  278.900 1.00 34.53  ? 523 GLY A O   1 
ATOM   3998 N  N   . GLY A 1 524 ? -117.606 16.715  280.942 1.00 26.20  ? 524 GLY A N   1 
ATOM   3999 C  CA  . GLY A 1 524 ? -116.935 15.436  281.116 1.00 27.39  ? 524 GLY A CA  1 
ATOM   4000 C  C   . GLY A 1 524 ? -117.068 14.931  282.534 1.00 24.12  ? 524 GLY A C   1 
ATOM   4001 O  O   . GLY A 1 524 ? -118.053 15.219  283.224 1.00 21.85  ? 524 GLY A O   1 
ATOM   4002 N  N   . LEU A 1 525 ? -116.061 14.174  282.961 1.00 20.93  ? 525 LEU A N   1 
ATOM   4003 C  CA  . LEU A 1 525 ? -116.060 13.549  284.274 1.00 19.39  ? 525 LEU A CA  1 
ATOM   4004 C  C   . LEU A 1 525 ? -114.701 13.727  284.934 1.00 21.62  ? 525 LEU A C   1 
ATOM   4005 O  O   . LEU A 1 525 ? -113.664 13.705  284.264 1.00 23.53  ? 525 LEU A O   1 
ATOM   4006 C  CB  . LEU A 1 525 ? -116.398 12.052  284.188 1.00 21.46  ? 525 LEU A CB  1 
ATOM   4007 C  CG  . LEU A 1 525 ? -117.732 11.636  283.561 1.00 25.36  ? 525 LEU A CG  1 
ATOM   4008 C  CD1 . LEU A 1 525 ? -117.610 11.496  282.049 1.00 26.68  ? 525 LEU A CD1 1 
ATOM   4009 C  CD2 . LEU A 1 525 ? -118.236 10.343  284.178 1.00 29.21  ? 525 LEU A CD2 1 
ATOM   4010 N  N   . PHE A 1 526 ? -114.720 13.913  286.252 1.00 22.31  ? 526 PHE A N   1 
ATOM   4011 C  CA  . PHE A 1 526 ? -113.519 13.917  287.072 1.00 21.15  ? 526 PHE A CA  1 
ATOM   4012 C  C   . PHE A 1 526 ? -113.765 13.040  288.292 1.00 22.01  ? 526 PHE A C   1 
ATOM   4013 O  O   . PHE A 1 526 ? -114.909 12.795  288.682 1.00 21.71  ? 526 PHE A O   1 
ATOM   4014 C  CB  . PHE A 1 526 ? -113.117 15.340  287.494 1.00 21.62  ? 526 PHE A CB  1 
ATOM   4015 C  CG  . PHE A 1 526 ? -113.861 15.858  288.692 1.00 22.94  ? 526 PHE A CG  1 
ATOM   4016 C  CD1 . PHE A 1 526 ? -115.137 16.378  288.561 1.00 20.17  ? 526 PHE A CD1 1 
ATOM   4017 C  CD2 . PHE A 1 526 ? -113.279 15.835  289.950 1.00 23.60  ? 526 PHE A CD2 1 
ATOM   4018 C  CE1 . PHE A 1 526 ? -115.819 16.861  289.660 1.00 21.13  ? 526 PHE A CE1 1 
ATOM   4019 C  CE2 . PHE A 1 526 ? -113.959 16.313  291.054 1.00 19.99  ? 526 PHE A CE2 1 
ATOM   4020 C  CZ  . PHE A 1 526 ? -115.231 16.826  290.908 1.00 22.00  ? 526 PHE A CZ  1 
ATOM   4021 N  N   . ALA A 1 527 ? -112.678 12.561  288.895 1.00 22.16  ? 527 ALA A N   1 
ATOM   4022 C  CA  . ALA A 1 527 ? -112.790 11.552  289.936 1.00 23.69  ? 527 ALA A CA  1 
ATOM   4023 C  C   . ALA A 1 527 ? -111.833 11.836  291.084 1.00 20.88  ? 527 ALA A C   1 
ATOM   4024 O  O   . ALA A 1 527 ? -110.788 12.468  290.908 1.00 24.01  ? 527 ALA A O   1 
ATOM   4025 C  CB  . ALA A 1 527 ? -112.522 10.148  289.381 1.00 25.15  ? 527 ALA A CB  1 
ATOM   4026 N  N   . TRP A 1 528 ? -112.215 11.356  292.264 1.00 19.37  ? 528 TRP A N   1 
ATOM   4027 C  CA  . TRP A 1 528 ? -111.369 11.363  293.452 1.00 19.69  ? 528 TRP A CA  1 
ATOM   4028 C  C   . TRP A 1 528 ? -111.505 10.011  294.143 1.00 22.48  ? 528 TRP A C   1 
ATOM   4029 O  O   . TRP A 1 528 ? -112.618 9.592   294.455 1.00 35.79  ? 528 TRP A O   1 
ATOM   4030 C  CB  . TRP A 1 528 ? -111.764 12.493  294.410 1.00 19.22  ? 528 TRP A CB  1 
ATOM   4031 C  CG  . TRP A 1 528 ? -111.051 12.450  295.742 1.00 22.71  ? 528 TRP A CG  1 
ATOM   4032 C  CD1 . TRP A 1 528 ? -111.286 11.584  296.773 1.00 22.27  ? 528 TRP A CD1 1 
ATOM   4033 C  CD2 . TRP A 1 528 ? -110.009 13.326  296.190 1.00 26.69  ? 528 TRP A CD2 1 
ATOM   4034 N  NE1 . TRP A 1 528 ? -110.444 11.855  297.823 1.00 26.43  ? 528 TRP A NE1 1 
ATOM   4035 C  CE2 . TRP A 1 528 ? -109.653 12.923  297.491 1.00 28.71  ? 528 TRP A CE2 1 
ATOM   4036 C  CE3 . TRP A 1 528 ? -109.342 14.411  295.616 1.00 22.22  ? 528 TRP A CE3 1 
ATOM   4037 C  CZ2 . TRP A 1 528 ? -108.655 13.563  298.224 1.00 28.41  ? 528 TRP A CZ2 1 
ATOM   4038 C  CZ3 . TRP A 1 528 ? -108.352 15.044  296.343 1.00 20.23  ? 528 TRP A CZ3 1 
ATOM   4039 C  CH2 . TRP A 1 528 ? -108.020 14.620  297.634 1.00 23.73  ? 528 TRP A CH2 1 
ATOM   4040 N  N   . GLU A 1 529 ? -110.393 9.321   294.378 1.00 19.08  ? 529 GLU A N   1 
ATOM   4041 C  CA  . GLU A 1 529 ? -109.073 9.751   293.937 1.00 17.09  ? 529 GLU A CA  1 
ATOM   4042 C  C   . GLU A 1 529 ? -108.479 8.674   293.034 1.00 16.22  ? 529 GLU A C   1 
ATOM   4043 O  O   . GLU A 1 529 ? -108.879 7.512   293.104 1.00 19.28  ? 529 GLU A O   1 
ATOM   4044 C  CB  . GLU A 1 529 ? -108.167 10.030  295.139 1.00 18.71  ? 529 GLU A CB  1 
ATOM   4045 C  CG  . GLU A 1 529 ? -108.238 8.969   296.225 1.00 19.26  ? 529 GLU A CG  1 
ATOM   4046 C  CD  . GLU A 1 529 ? -107.596 9.416   297.525 1.00 35.04  ? 529 GLU A CD  1 
ATOM   4047 O  OE1 . GLU A 1 529 ? -106.620 8.774   297.965 1.00 41.41  ? 529 GLU A OE1 1 
ATOM   4048 O  OE2 . GLU A 1 529 ? -108.070 10.411  298.111 1.00 30.93  ? 529 GLU A OE2 1 
ATOM   4049 N  N   . ILE A 1 530 ? -107.522 9.064   292.188 1.00 13.81  ? 530 ILE A N   1 
ATOM   4050 C  CA  . ILE A 1 530 ? -107.052 8.182   291.124 1.00 13.83  ? 530 ILE A CA  1 
ATOM   4051 C  C   . ILE A 1 530 ? -106.353 6.942   291.666 1.00 15.82  ? 530 ILE A C   1 
ATOM   4052 O  O   . ILE A 1 530 ? -106.299 5.915   290.982 1.00 24.10  ? 530 ILE A O   1 
ATOM   4053 C  CB  . ILE A 1 530 ? -106.130 8.963   290.161 1.00 13.94  ? 530 ILE A CB  1 
ATOM   4054 C  CG1 . ILE A 1 530 ? -105.933 8.187   288.858 1.00 17.84  ? 530 ILE A CG1 1 
ATOM   4055 C  CG2 . ILE A 1 530 ? -104.790 9.259   290.816 1.00 14.88  ? 530 ILE A CG2 1 
ATOM   4056 C  CD1 . ILE A 1 530 ? -107.226 7.775   288.195 1.00 12.87  ? 530 ILE A CD1 1 
ATOM   4057 N  N   . ASP A 1 531 ? -105.823 7.002   292.888 1.00 15.81  ? 531 ASP A N   1 
ATOM   4058 C  CA  . ASP A 1 531 ? -105.102 5.862   293.440 1.00 14.14  ? 531 ASP A CA  1 
ATOM   4059 C  C   . ASP A 1 531 ? -106.026 4.753   293.921 1.00 17.08  ? 531 ASP A C   1 
ATOM   4060 O  O   . ASP A 1 531 ? -105.581 3.607   294.050 1.00 17.42  ? 531 ASP A O   1 
ATOM   4061 C  CB  . ASP A 1 531 ? -104.208 6.315   294.593 1.00 15.50  ? 531 ASP A CB  1 
ATOM   4062 C  CG  . ASP A 1 531 ? -104.994 6.948   295.717 1.00 20.61  ? 531 ASP A CG  1 
ATOM   4063 O  OD1 . ASP A 1 531 ? -105.471 6.206   296.601 1.00 20.50  ? 531 ASP A OD1 1 
ATOM   4064 O  OD2 . ASP A 1 531 ? -105.139 8.187   295.712 1.00 20.64  ? 531 ASP A OD2 1 
ATOM   4065 N  N   . ALA A 1 532 ? -107.294 5.060   294.191 1.00 18.28  ? 532 ALA A N   1 
ATOM   4066 C  CA  . ALA A 1 532 ? -108.215 4.063   294.719 1.00 19.54  ? 532 ALA A CA  1 
ATOM   4067 C  C   . ALA A 1 532 ? -108.875 3.223   293.635 1.00 15.81  ? 532 ALA A C   1 
ATOM   4068 O  O   . ALA A 1 532 ? -109.559 2.249   293.963 1.00 18.27  ? 532 ALA A O   1 
ATOM   4069 C  CB  . ALA A 1 532 ? -109.290 4.740   295.569 1.00 16.26  ? 532 ALA A CB  1 
ATOM   4070 N  N   . ASP A 1 533 ? -108.688 3.567   292.365 1.00 14.78  ? 533 ASP A N   1 
ATOM   4071 C  CA  . ASP A 1 533 ? -109.272 2.814   291.266 1.00 19.62  ? 533 ASP A CA  1 
ATOM   4072 C  C   . ASP A 1 533 ? -108.352 1.669   290.863 1.00 27.35  ? 533 ASP A C   1 
ATOM   4073 O  O   . ASP A 1 533 ? -107.125 1.797   290.907 1.00 51.41  ? 533 ASP A O   1 
ATOM   4074 C  CB  . ASP A 1 533 ? -109.528 3.726   290.065 1.00 18.90  ? 533 ASP A CB  1 
ATOM   4075 C  CG  . ASP A 1 533 ? -110.202 3.004   288.915 1.00 19.34  ? 533 ASP A CG  1 
ATOM   4076 O  OD1 . ASP A 1 533 ? -110.925 2.020   289.171 1.00 19.90  ? 533 ASP A OD1 1 
ATOM   4077 O  OD2 . ASP A 1 533 ? -110.005 3.421   287.754 1.00 25.96  ? 533 ASP A OD2 1 
ATOM   4078 N  N   . ASN A 1 534 ? -108.955 0.546   290.472 1.00 22.36  ? 534 ASN A N   1 
ATOM   4079 C  CA  . ASN A 1 534 ? -108.214 -0.609  289.982 1.00 20.48  ? 534 ASN A CA  1 
ATOM   4080 C  C   . ASN A 1 534 ? -108.338 -0.768  288.470 1.00 22.67  ? 534 ASN A C   1 
ATOM   4081 O  O   . ASN A 1 534 ? -108.060 -1.847  287.937 1.00 22.03  ? 534 ASN A O   1 
ATOM   4082 C  CB  . ASN A 1 534 ? -108.673 -1.881  290.698 1.00 20.02  ? 534 ASN A CB  1 
ATOM   4083 C  CG  . ASN A 1 534 ? -110.053 -2.334  290.263 1.00 25.09  ? 534 ASN A CG  1 
ATOM   4084 O  OD1 . ASN A 1 534 ? -110.864 -1.537  289.794 1.00 30.17  ? 534 ASN A OD1 1 
ATOM   4085 N  ND2 . ASN A 1 534 ? -110.326 -3.624  290.419 1.00 21.05  ? 534 ASN A ND2 1 
ATOM   4086 N  N   . GLY A 1 535 ? -108.753 0.287   287.770 1.00 24.22  ? 535 GLY A N   1 
ATOM   4087 C  CA  . GLY A 1 535 ? -108.905 0.266   286.335 1.00 22.32  ? 535 GLY A CA  1 
ATOM   4088 C  C   . GLY A 1 535 ? -110.338 0.186   285.851 1.00 22.01  ? 535 GLY A C   1 
ATOM   4089 O  O   . GLY A 1 535 ? -110.617 0.589   284.717 1.00 23.56  ? 535 GLY A O   1 
ATOM   4090 N  N   . ASP A 1 536 ? -111.254 -0.316  286.682 1.00 21.97  ? 536 ASP A N   1 
ATOM   4091 C  CA  . ASP A 1 536 ? -112.639 -0.472  286.249 1.00 24.12  ? 536 ASP A CA  1 
ATOM   4092 C  C   . ASP A 1 536 ? -113.305 0.880   286.028 1.00 26.86  ? 536 ASP A C   1 
ATOM   4093 O  O   . ASP A 1 536 ? -113.940 1.109   284.992 1.00 51.21  ? 536 ASP A O   1 
ATOM   4094 C  CB  . ASP A 1 536 ? -113.421 -1.287  287.279 1.00 25.32  ? 536 ASP A CB  1 
ATOM   4095 C  CG  . ASP A 1 536 ? -112.857 -2.677  287.475 1.00 29.95  ? 536 ASP A CG  1 
ATOM   4096 O  OD1 . ASP A 1 536 ? -112.279 -3.227  286.516 1.00 47.75  ? 536 ASP A OD1 1 
ATOM   4097 O  OD2 . ASP A 1 536 ? -112.988 -3.218  288.593 1.00 32.08  ? 536 ASP A OD2 1 
ATOM   4098 N  N   . LEU A 1 537 ? -113.166 1.791   286.993 1.00 25.25  ? 537 LEU A N   1 
ATOM   4099 C  CA  . LEU A 1 537 ? -113.924 3.037   286.951 1.00 23.32  ? 537 LEU A CA  1 
ATOM   4100 C  C   . LEU A 1 537 ? -113.431 3.959   285.842 1.00 27.75  ? 537 LEU A C   1 
ATOM   4101 O  O   . LEU A 1 537 ? -114.239 4.572   285.136 1.00 33.96  ? 537 LEU A O   1 
ATOM   4102 C  CB  . LEU A 1 537 ? -113.848 3.736   288.308 1.00 21.33  ? 537 LEU A CB  1 
ATOM   4103 C  CG  . LEU A 1 537 ? -114.355 2.906   289.489 1.00 21.60  ? 537 LEU A CG  1 
ATOM   4104 C  CD1 . LEU A 1 537 ? -114.355 3.725   290.766 1.00 23.80  ? 537 LEU A CD1 1 
ATOM   4105 C  CD2 . LEU A 1 537 ? -115.743 2.358   289.202 1.00 35.58  ? 537 LEU A CD2 1 
ATOM   4106 N  N   . LEU A 1 538 ? -112.112 4.070   285.671 1.00 23.95  ? 538 LEU A N   1 
ATOM   4107 C  CA  . LEU A 1 538 ? -111.579 4.974   284.657 1.00 24.13  ? 538 LEU A CA  1 
ATOM   4108 C  C   . LEU A 1 538 ? -111.903 4.484   283.251 1.00 27.75  ? 538 LEU A C   1 
ATOM   4109 O  O   . LEU A 1 538 ? -112.140 5.293   282.346 1.00 27.76  ? 538 LEU A O   1 
ATOM   4110 C  CB  . LEU A 1 538 ? -110.072 5.137   284.839 1.00 23.24  ? 538 LEU A CB  1 
ATOM   4111 C  CG  . LEU A 1 538 ? -109.391 6.102   283.868 1.00 24.67  ? 538 LEU A CG  1 
ATOM   4112 C  CD1 . LEU A 1 538 ? -110.033 7.476   283.947 1.00 23.60  ? 538 LEU A CD1 1 
ATOM   4113 C  CD2 . LEU A 1 538 ? -107.908 6.188   284.165 1.00 30.85  ? 538 LEU A CD2 1 
ATOM   4114 N  N   . ASN A 1 539 ? -111.916 3.165   283.047 1.00 28.79  ? 539 ASN A N   1 
ATOM   4115 C  CA  . ASN A 1 539 ? -112.294 2.623   281.745 1.00 29.78  ? 539 ASN A CA  1 
ATOM   4116 C  C   . ASN A 1 539 ? -113.752 2.924   281.426 1.00 39.82  ? 539 ASN A C   1 
ATOM   4117 O  O   . ASN A 1 539 ? -114.097 3.197   280.270 1.00 56.55  ? 539 ASN A O   1 
ATOM   4118 C  CB  . ASN A 1 539 ? -112.040 1.117   281.710 1.00 31.00  ? 539 ASN A CB  1 
ATOM   4119 C  CG  . ASN A 1 539 ? -110.566 0.776   281.746 1.00 32.54  ? 539 ASN A CG  1 
ATOM   4120 O  OD1 . ASN A 1 539 ? -109.713 1.659   281.824 1.00 29.69  ? 539 ASN A OD1 1 
ATOM   4121 N  ND2 . ASN A 1 539 ? -110.259 -0.514  281.708 1.00 36.96  ? 539 ASN A ND2 1 
ATOM   4122 N  N   . ALA A 1 540 ? -114.623 2.878   282.436 1.00 29.94  ? 540 ALA A N   1 
ATOM   4123 C  CA  . ALA A 1 540 ? -116.027 3.202   282.216 1.00 32.51  ? 540 ALA A CA  1 
ATOM   4124 C  C   . ALA A 1 540 ? -116.216 4.673   281.872 1.00 37.00  ? 540 ALA A C   1 
ATOM   4125 O  O   . ALA A 1 540 ? -117.135 5.019   281.120 1.00 52.53  ? 540 ALA A O   1 
ATOM   4126 C  CB  . ALA A 1 540 ? -116.851 2.835   283.450 1.00 34.44  ? 540 ALA A CB  1 
ATOM   4127 N  N   . ILE A 1 541 ? -115.363 5.549   282.406 1.00 36.62  ? 541 ILE A N   1 
ATOM   4128 C  CA  . ILE A 1 541 ? -115.462 6.971   282.092 1.00 34.96  ? 541 ILE A CA  1 
ATOM   4129 C  C   . ILE A 1 541 ? -115.122 7.219   280.628 1.00 33.86  ? 541 ILE A C   1 
ATOM   4130 O  O   . ILE A 1 541 ? -115.759 8.041   279.958 1.00 37.37  ? 541 ILE A O   1 
ATOM   4131 C  CB  . ILE A 1 541 ? -114.556 7.786   283.033 1.00 28.91  ? 541 ILE A CB  1 
ATOM   4132 C  CG1 . ILE A 1 541 ? -115.011 7.627   284.484 1.00 26.16  ? 541 ILE A CG1 1 
ATOM   4133 C  CG2 . ILE A 1 541 ? -114.550 9.253   282.637 1.00 26.23  ? 541 ILE A CG2 1 
ATOM   4134 C  CD1 . ILE A 1 541 ? -114.148 8.369   285.479 1.00 26.66  ? 541 ILE A CD1 1 
ATOM   4135 N  N   . ASN A 1 542 ? -114.126 6.506   280.105 1.00 33.96  ? 542 ASN A N   1 
ATOM   4136 C  CA  . ASN A 1 542 ? -113.654 6.694   278.741 1.00 40.12  ? 542 ASN A CA  1 
ATOM   4137 C  C   . ASN A 1 542 ? -114.381 5.805   277.736 1.00 44.94  ? 542 ASN A C   1 
ATOM   4138 O  O   . ASN A 1 542 ? -113.864 5.580   276.636 1.00 46.44  ? 542 ASN A O   1 
ATOM   4139 C  CB  . ASN A 1 542 ? -112.148 6.436   278.669 1.00 39.11  ? 542 ASN A CB  1 
ATOM   4140 C  CG  . ASN A 1 542 ? -111.346 7.442   279.472 1.00 37.76  ? 542 ASN A CG  1 
ATOM   4141 O  OD1 . ASN A 1 542 ? -110.977 8.503   278.969 1.00 36.13  ? 542 ASN A OD1 1 
ATOM   4142 N  ND2 . ASN A 1 542 ? -111.072 7.112   280.728 1.00 39.23  ? 542 ASN A ND2 1 
ATOM   4143 N  N   . ALA A 1 543 ? -115.562 5.302   278.085 1.00 48.27  ? 543 ALA A N   1 
ATOM   4144 C  CA  . ALA A 1 543 ? -116.275 4.383   277.208 1.00 54.35  ? 543 ALA A CA  1 
ATOM   4145 C  C   . ALA A 1 543 ? -116.850 5.124   276.008 1.00 61.99  ? 543 ALA A C   1 
ATOM   4146 O  O   . ALA A 1 543 ? -117.581 6.108   276.161 1.00 64.36  ? 543 ALA A O   1 
ATOM   4147 C  CB  . ALA A 1 543 ? -117.390 3.676   277.977 1.00 58.62  ? 543 ALA A CB  1 
ATOM   4148 N  N   . GLN A 1 544 ? -116.518 4.648   274.810 1.00 77.79  ? 544 GLN A N   1 
ATOM   4149 C  CA  . GLN A 1 544 ? -117.043 5.210   273.572 1.00 73.40  ? 544 GLN A CA  1 
ATOM   4150 C  C   . GLN A 1 544 ? -118.335 4.490   273.205 1.00 84.74  ? 544 GLN A C   1 
ATOM   4151 O  O   . GLN A 1 544 ? -118.325 3.283   272.940 1.00 91.64  ? 544 GLN A O   1 
ATOM   4152 C  CB  . GLN A 1 544 ? -116.023 5.083   272.441 1.00 72.05  ? 544 GLN A CB  1 
ATOM   4153 C  CG  . GLN A 1 544 ? -114.579 5.268   272.871 1.00 82.06  ? 544 GLN A CG  1 
ATOM   4154 C  CD  . GLN A 1 544 ? -113.612 5.162   271.708 1.00 72.27  ? 544 GLN A CD  1 
ATOM   4155 O  OE1 . GLN A 1 544 ? -113.687 5.934   270.753 1.00 67.24  ? 544 GLN A OE1 1 
ATOM   4156 N  NE2 . GLN A 1 544 ? -112.697 4.203   271.783 1.00 67.23  ? 544 GLN A NE2 1 
ATOM   4157 N  N   . PHE A 1 545 ? -119.441 5.227   273.188 1.00 89.42  ? 545 PHE A N   1 
ATOM   4158 C  CA  . PHE A 1 545 ? -120.737 4.653   272.841 1.00 86.95  ? 545 PHE A CA  1 
ATOM   4159 C  C   . PHE A 1 545 ? -121.265 5.233   271.533 1.00 78.85  ? 545 PHE A C   1 
ATOM   4160 O  O   . PHE A 1 545 ? -122.353 4.877   271.080 1.00 68.82  ? 545 PHE A O   1 
ATOM   4161 C  CB  . PHE A 1 545 ? -121.750 4.888   273.965 1.00 82.66  ? 545 PHE A CB  1 
ATOM   4162 C  CG  . PHE A 1 545 ? -121.545 4.004   275.165 1.00 82.75  ? 545 PHE A CG  1 
ATOM   4163 C  CD1 . PHE A 1 545 ? -120.569 3.020   275.165 1.00 104.56 ? 545 PHE A CD1 1 
ATOM   4164 C  CD2 . PHE A 1 545 ? -122.331 4.159   276.295 1.00 75.41  ? 545 PHE A CD2 1 
ATOM   4165 C  CE1 . PHE A 1 545 ? -120.380 2.209   276.267 1.00 113.40 ? 545 PHE A CE1 1 
ATOM   4166 C  CE2 . PHE A 1 545 ? -122.148 3.351   277.401 1.00 83.45  ? 545 PHE A CE2 1 
ATOM   4167 C  CZ  . PHE A 1 545 ? -121.171 2.374   277.386 1.00 123.98 ? 545 PHE A CZ  1 
ATOM   4168 N  N   . ILE B 1 18  ? -115.487 24.424  260.968 1.00 43.94  ? 18  ILE B N   1 
ATOM   4169 C  CA  . ILE B 1 18  ? -114.298 23.617  261.211 1.00 43.16  ? 18  ILE B CA  1 
ATOM   4170 C  C   . ILE B 1 18  ? -114.662 22.136  261.212 1.00 42.17  ? 18  ILE B C   1 
ATOM   4171 O  O   . ILE B 1 18  ? -115.791 21.770  261.544 1.00 47.65  ? 18  ILE B O   1 
ATOM   4172 C  CB  . ILE B 1 18  ? -113.614 24.020  262.533 1.00 47.32  ? 18  ILE B CB  1 
ATOM   4173 C  CG1 . ILE B 1 18  ? -114.485 23.638  263.732 1.00 42.07  ? 18  ILE B CG1 1 
ATOM   4174 C  CG2 . ILE B 1 18  ? -113.317 25.511  262.544 1.00 56.36  ? 18  ILE B CG2 1 
ATOM   4175 C  CD1 . ILE B 1 18  ? -113.757 23.693  265.056 1.00 42.60  ? 18  ILE B CD1 1 
ATOM   4176 N  N   . PRO B 1 19  ? -113.717 21.283  260.825 1.00 40.69  ? 19  PRO B N   1 
ATOM   4177 C  CA  . PRO B 1 19  ? -113.963 19.838  260.869 1.00 44.92  ? 19  PRO B CA  1 
ATOM   4178 C  C   . PRO B 1 19  ? -114.112 19.352  262.302 1.00 37.46  ? 19  PRO B C   1 
ATOM   4179 O  O   . PRO B 1 19  ? -113.781 20.042  263.269 1.00 36.34  ? 19  PRO B O   1 
ATOM   4180 C  CB  . PRO B 1 19  ? -112.720 19.238  260.203 1.00 39.65  ? 19  PRO B CB  1 
ATOM   4181 C  CG  . PRO B 1 19  ? -112.125 20.359  259.415 1.00 37.24  ? 19  PRO B CG  1 
ATOM   4182 C  CD  . PRO B 1 19  ? -112.423 21.599  260.198 1.00 38.23  ? 19  PRO B CD  1 
ATOM   4183 N  N   . GLY B 1 20  ? -114.626 18.132  262.428 1.00 40.40  ? 20  GLY B N   1 
ATOM   4184 C  CA  . GLY B 1 20  ? -114.762 17.526  263.736 1.00 48.27  ? 20  GLY B CA  1 
ATOM   4185 C  C   . GLY B 1 20  ? -113.419 17.302  264.403 1.00 41.20  ? 20  GLY B C   1 
ATOM   4186 O  O   . GLY B 1 20  ? -112.364 17.305  263.767 1.00 43.42  ? 20  GLY B O   1 
ATOM   4187 N  N   . THR B 1 21  ? -113.467 17.113  265.714 1.00 42.96  ? 21  THR B N   1 
ATOM   4188 C  CA  . THR B 1 21  ? -112.243 16.894  266.472 1.00 42.82  ? 21  THR B CA  1 
ATOM   4189 C  C   . THR B 1 21  ? -111.620 15.560  266.076 1.00 44.70  ? 21  THR B C   1 
ATOM   4190 O  O   . THR B 1 21  ? -112.313 14.535  266.063 1.00 63.35  ? 21  THR B O   1 
ATOM   4191 C  CB  . THR B 1 21  ? -112.523 16.931  267.975 1.00 54.67  ? 21  THR B CB  1 
ATOM   4192 O  OG1 . THR B 1 21  ? -111.405 16.386  268.687 1.00 61.98  ? 21  THR B OG1 1 
ATOM   4193 C  CG2 . THR B 1 21  ? -113.782 16.141  268.314 1.00 59.73  ? 21  THR B CG2 1 
ATOM   4194 N  N   . PRO B 1 22  ? -110.332 15.528  265.736 1.00 39.32  ? 22  PRO B N   1 
ATOM   4195 C  CA  . PRO B 1 22  ? -109.701 14.270  265.326 1.00 38.12  ? 22  PRO B CA  1 
ATOM   4196 C  C   . PRO B 1 22  ? -109.156 13.482  266.507 1.00 37.12  ? 22  PRO B C   1 
ATOM   4197 O  O   . PRO B 1 22  ? -108.598 14.030  267.459 1.00 41.22  ? 22  PRO B O   1 
ATOM   4198 C  CB  . PRO B 1 22  ? -108.568 14.740  264.401 1.00 36.65  ? 22  PRO B CB  1 
ATOM   4199 C  CG  . PRO B 1 22  ? -108.344 16.210  264.735 1.00 35.84  ? 22  PRO B CG  1 
ATOM   4200 C  CD  . PRO B 1 22  ? -109.377 16.647  265.735 1.00 36.58  ? 22  PRO B CD  1 
ATOM   4201 N  N   . VAL B 1 23  ? -109.332 12.165  266.435 1.00 34.51  ? 23  VAL B N   1 
ATOM   4202 C  CA  . VAL B 1 23  ? -108.924 11.248  267.492 1.00 33.95  ? 23  VAL B CA  1 
ATOM   4203 C  C   . VAL B 1 23  ? -107.965 10.238  266.882 1.00 36.46  ? 23  VAL B C   1 
ATOM   4204 O  O   . VAL B 1 23  ? -108.383 9.354   266.123 1.00 35.33  ? 23  VAL B O   1 
ATOM   4205 C  CB  . VAL B 1 23  ? -110.124 10.547  268.140 1.00 36.14  ? 23  VAL B CB  1 
ATOM   4206 C  CG1 . VAL B 1 23  ? -109.651 9.504   269.140 1.00 38.16  ? 23  VAL B CG1 1 
ATOM   4207 C  CG2 . VAL B 1 23  ? -111.024 11.568  268.810 1.00 40.08  ? 23  VAL B CG2 1 
ATOM   4208 N  N   . ILE B 1 24  ? -106.681 10.365  267.215 1.00 51.99  ? 24  ILE B N   1 
ATOM   4209 C  CA  . ILE B 1 24  ? -105.673 9.456   266.689 1.00 35.74  ? 24  ILE B CA  1 
ATOM   4210 C  C   . ILE B 1 24  ? -105.839 8.089   267.339 1.00 34.32  ? 24  ILE B C   1 
ATOM   4211 O  O   . ILE B 1 24  ? -105.870 7.969   268.570 1.00 35.71  ? 24  ILE B O   1 
ATOM   4212 C  CB  . ILE B 1 24  ? -104.266 10.021  266.928 1.00 32.23  ? 24  ILE B CB  1 
ATOM   4213 C  CG1 . ILE B 1 24  ? -104.147 11.421  266.327 1.00 35.48  ? 24  ILE B CG1 1 
ATOM   4214 C  CG2 . ILE B 1 24  ? -103.224 9.110   266.319 1.00 33.08  ? 24  ILE B CG2 1 
ATOM   4215 C  CD1 . ILE B 1 24  ? -102.797 12.066  266.549 1.00 48.03  ? 24  ILE B CD1 1 
ATOM   4216 N  N   . ASP B 1 25  ? -105.948 7.053   266.512 1.00 35.88  ? 25  ASP B N   1 
ATOM   4217 C  CA  . ASP B 1 25  ? -106.156 5.704   267.018 1.00 37.22  ? 25  ASP B CA  1 
ATOM   4218 C  C   . ASP B 1 25  ? -104.938 5.226   267.801 1.00 37.75  ? 25  ASP B C   1 
ATOM   4219 O  O   . ASP B 1 25  ? -103.799 5.609   267.521 1.00 55.11  ? 25  ASP B O   1 
ATOM   4220 C  CB  . ASP B 1 25  ? -106.442 4.741   265.867 1.00 37.13  ? 25  ASP B CB  1 
ATOM   4221 C  CG  . ASP B 1 25  ? -107.478 5.280   264.901 1.00 43.97  ? 25  ASP B CG  1 
ATOM   4222 O  OD1 . ASP B 1 25  ? -108.328 6.089   265.328 1.00 51.12  ? 25  ASP B OD1 1 
ATOM   4223 O  OD2 . ASP B 1 25  ? -107.440 4.895   263.713 1.00 40.67  ? 25  ASP B OD2 1 
ATOM   4224 N  N   . TRP B 1 26  ? -105.190 4.377   268.794 1.00 35.17  ? 26  TRP B N   1 
ATOM   4225 C  CA  . TRP B 1 26  ? -104.105 3.827   269.593 1.00 37.65  ? 26  TRP B CA  1 
ATOM   4226 C  C   . TRP B 1 26  ? -103.318 2.800   268.789 1.00 38.59  ? 26  TRP B C   1 
ATOM   4227 O  O   . TRP B 1 26  ? -103.887 2.015   268.026 1.00 40.38  ? 26  TRP B O   1 
ATOM   4228 C  CB  . TRP B 1 26  ? -104.647 3.184   270.868 1.00 51.34  ? 26  TRP B CB  1 
ATOM   4229 C  CG  . TRP B 1 26  ? -103.568 2.640   271.760 1.00 63.09  ? 26  TRP B CG  1 
ATOM   4230 C  CD1 . TRP B 1 26  ? -102.920 3.302   272.762 1.00 47.69  ? 26  TRP B CD1 1 
ATOM   4231 C  CD2 . TRP B 1 26  ? -103.006 1.322   271.722 1.00 43.09  ? 26  TRP B CD2 1 
ATOM   4232 N  NE1 . TRP B 1 26  ? -101.994 2.478   273.353 1.00 39.70  ? 26  TRP B NE1 1 
ATOM   4233 C  CE2 . TRP B 1 26  ? -102.026 1.257   272.732 1.00 40.40  ? 26  TRP B CE2 1 
ATOM   4234 C  CE3 . TRP B 1 26  ? -103.237 0.191   270.933 1.00 43.34  ? 26  TRP B CE3 1 
ATOM   4235 C  CZ2 . TRP B 1 26  ? -101.279 0.106   272.974 1.00 57.94  ? 26  TRP B CZ2 1 
ATOM   4236 C  CZ3 . TRP B 1 26  ? -102.494 -0.951  271.175 1.00 55.70  ? 26  TRP B CZ3 1 
ATOM   4237 C  CH2 . TRP B 1 26  ? -101.527 -0.985  272.187 1.00 49.50  ? 26  TRP B CH2 1 
ATOM   4238 N  N   . ALA B 1 27  ? -102.002 2.809   268.971 1.00 38.73  ? 27  ALA B N   1 
ATOM   4239 C  CA  . ALA B 1 27  ? -101.111 1.870   268.302 1.00 38.25  ? 27  ALA B CA  1 
ATOM   4240 C  C   . ALA B 1 27  ? -99.753  1.941   268.984 1.00 38.78  ? 27  ALA B C   1 
ATOM   4241 O  O   . ALA B 1 27  ? -99.467  2.867   269.747 1.00 36.34  ? 27  ALA B O   1 
ATOM   4242 C  CB  . ALA B 1 27  ? -100.986 2.170   266.806 1.00 37.80  ? 27  ALA B CB  1 
ATOM   4243 N  N   . ASP B 1 28  ? -98.920  0.943   268.703 1.00 48.37  ? 28  ASP B N   1 
ATOM   4244 C  CA  . ASP B 1 28  ? -97.549  0.940   269.193 1.00 35.79  ? 28  ASP B CA  1 
ATOM   4245 C  C   . ASP B 1 28  ? -96.717  1.883   268.333 1.00 32.03  ? 28  ASP B C   1 
ATOM   4246 O  O   . ASP B 1 28  ? -96.602  1.685   267.119 1.00 29.52  ? 28  ASP B O   1 
ATOM   4247 C  CB  . ASP B 1 28  ? -96.971  -0.473  269.164 1.00 38.13  ? 28  ASP B CB  1 
ATOM   4248 C  CG  . ASP B 1 28  ? -95.500  -0.509  269.531 1.00 40.66  ? 28  ASP B CG  1 
ATOM   4249 O  OD1 . ASP B 1 28  ? -95.063  0.348   270.328 1.00 39.78  ? 28  ASP B OD1 1 
ATOM   4250 O  OD2 . ASP B 1 28  ? -94.779  -1.390  269.019 1.00 49.83  ? 28  ASP B OD2 1 
ATOM   4251 N  N   . ARG B 1 29  ? -96.144  2.909   268.958 1.00 32.20  ? 29  ARG B N   1 
ATOM   4252 C  CA  . ARG B 1 29  ? -95.383  3.927   268.245 1.00 31.26  ? 29  ARG B CA  1 
ATOM   4253 C  C   . ARG B 1 29  ? -93.911  3.910   268.643 1.00 31.67  ? 29  ARG B C   1 
ATOM   4254 O  O   . ARG B 1 29  ? -93.242  4.945   268.633 1.00 29.12  ? 29  ARG B O   1 
ATOM   4255 C  CB  . ARG B 1 29  ? -95.999  5.306   268.469 1.00 27.65  ? 29  ARG B CB  1 
ATOM   4256 C  CG  . ARG B 1 29  ? -97.323  5.466   267.748 1.00 29.97  ? 29  ARG B CG  1 
ATOM   4257 C  CD  . ARG B 1 29  ? -98.057  6.732   268.136 1.00 42.48  ? 29  ARG B CD  1 
ATOM   4258 N  NE  . ARG B 1 29  ? -99.306  6.841   267.390 1.00 30.80  ? 29  ARG B NE  1 
ATOM   4259 C  CZ  . ARG B 1 29  ? -100.463 6.336   267.803 1.00 32.59  ? 29  ARG B CZ  1 
ATOM   4260 N  NH1 . ARG B 1 29  ? -100.532 5.691   268.959 1.00 40.79  ? 29  ARG B NH1 1 
ATOM   4261 N  NH2 . ARG B 1 29  ? -101.552 6.472   267.060 1.00 38.81  ? 29  ARG B NH2 1 
ATOM   4262 N  N   . ASN B 1 30  ? -93.400  2.734   268.997 1.00 31.26  ? 30  ASN B N   1 
ATOM   4263 C  CA  . ASN B 1 30  ? -91.976  2.529   269.250 1.00 31.17  ? 30  ASN B CA  1 
ATOM   4264 C  C   . ASN B 1 30  ? -91.381  1.898   267.997 1.00 32.62  ? 30  ASN B C   1 
ATOM   4265 O  O   . ASN B 1 30  ? -91.491  0.688   267.785 1.00 63.85  ? 30  ASN B O   1 
ATOM   4266 C  CB  . ASN B 1 30  ? -91.757  1.654   270.480 1.00 33.14  ? 30  ASN B CB  1 
ATOM   4267 C  CG  . ASN B 1 30  ? -92.180  2.337   271.766 1.00 40.94  ? 30  ASN B CG  1 
ATOM   4268 O  OD1 . ASN B 1 30  ? -91.447  3.159   272.315 1.00 44.81  ? 30  ASN B OD1 1 
ATOM   4269 N  ND2 . ASN B 1 30  ? -93.367  1.998   272.253 1.00 39.89  ? 30  ASN B ND2 1 
ATOM   4270 N  N   . TYR B 1 31  ? -90.760  2.722   267.162 1.00 27.26  ? 31  TYR B N   1 
ATOM   4271 C  CA  . TYR B 1 31  ? -90.163  2.274   265.914 1.00 25.64  ? 31  TYR B CA  1 
ATOM   4272 C  C   . TYR B 1 31  ? -88.650  2.176   266.058 1.00 24.58  ? 31  TYR B C   1 
ATOM   4273 O  O   . TYR B 1 31  ? -88.045  2.791   266.939 1.00 25.61  ? 31  TYR B O   1 
ATOM   4274 C  CB  . TYR B 1 31  ? -90.525  3.222   264.767 1.00 26.95  ? 31  TYR B CB  1 
ATOM   4275 C  CG  . TYR B 1 31  ? -92.004  3.262   264.453 1.00 29.87  ? 31  TYR B CG  1 
ATOM   4276 C  CD1 . TYR B 1 31  ? -92.867  4.068   265.184 1.00 28.01  ? 31  TYR B CD1 1 
ATOM   4277 C  CD2 . TYR B 1 31  ? -92.538  2.490   263.430 1.00 38.69  ? 31  TYR B CD2 1 
ATOM   4278 C  CE1 . TYR B 1 31  ? -94.219  4.105   264.902 1.00 28.17  ? 31  TYR B CE1 1 
ATOM   4279 C  CE2 . TYR B 1 31  ? -93.890  2.521   263.141 1.00 35.12  ? 31  TYR B CE2 1 
ATOM   4280 C  CZ  . TYR B 1 31  ? -94.725  3.330   263.881 1.00 26.67  ? 31  TYR B CZ  1 
ATOM   4281 O  OH  . TYR B 1 31  ? -96.072  3.366   263.600 1.00 26.67  ? 31  TYR B OH  1 
ATOM   4282 N  N   . ALA B 1 32  ? -88.041  1.390   265.174 1.00 22.63  ? 32  ALA B N   1 
ATOM   4283 C  CA  . ALA B 1 32  ? -86.602  1.169   265.220 1.00 19.80  ? 32  ALA B CA  1 
ATOM   4284 C  C   . ALA B 1 32  ? -86.069  0.997   263.808 1.00 21.13  ? 32  ALA B C   1 
ATOM   4285 O  O   . ALA B 1 32  ? -86.612  0.206   263.030 1.00 25.09  ? 32  ALA B O   1 
ATOM   4286 C  CB  . ALA B 1 32  ? -86.259  -0.060  266.069 1.00 23.35  ? 32  ALA B CB  1 
ATOM   4287 N  N   . LEU B 1 33  ? -85.010  1.741   263.482 1.00 23.41  ? 33  LEU B N   1 
ATOM   4288 C  CA  . LEU B 1 33  ? -84.346  1.566   262.196 1.00 25.31  ? 33  LEU B CA  1 
ATOM   4289 C  C   . LEU B 1 33  ? -83.633  0.224   262.100 1.00 25.43  ? 33  LEU B C   1 
ATOM   4290 O  O   . LEU B 1 33  ? -83.405  -0.266  260.989 1.00 27.64  ? 33  LEU B O   1 
ATOM   4291 C  CB  . LEU B 1 33  ? -83.354  2.706   261.957 1.00 21.33  ? 33  LEU B CB  1 
ATOM   4292 C  CG  . LEU B 1 33  ? -83.958  4.062   261.590 1.00 21.94  ? 33  LEU B CG  1 
ATOM   4293 C  CD1 . LEU B 1 33  ? -82.999  5.192   261.928 1.00 24.20  ? 33  LEU B CD1 1 
ATOM   4294 C  CD2 . LEU B 1 33  ? -84.330  4.099   260.115 1.00 25.90  ? 33  LEU B CD2 1 
ATOM   4295 N  N   . VAL B 1 34  ? -83.274  -0.372  263.234 1.00 24.19  ? 34  VAL B N   1 
ATOM   4296 C  CA  . VAL B 1 34  ? -82.677  -1.703  263.290 1.00 24.49  ? 34  VAL B CA  1 
ATOM   4297 C  C   . VAL B 1 34  ? -83.446  -2.468  264.360 1.00 24.06  ? 34  VAL B C   1 
ATOM   4298 O  O   . VAL B 1 34  ? -83.206  -2.283  265.558 1.00 27.37  ? 34  VAL B O   1 
ATOM   4299 C  CB  . VAL B 1 34  ? -81.177  -1.666  263.608 1.00 26.37  ? 34  VAL B CB  1 
ATOM   4300 C  CG1 . VAL B 1 34  ? -80.601  -3.074  263.608 1.00 32.37  ? 34  VAL B CG1 1 
ATOM   4301 C  CG2 . VAL B 1 34  ? -80.437  -0.781  262.614 1.00 26.53  ? 34  VAL B CG2 1 
ATOM   4302 N  N   . GLU B 1 35  ? -84.376  -3.321  263.937 1.00 23.41  ? 35  GLU B N   1 
ATOM   4303 C  CA  . GLU B 1 35  ? -85.197  -4.067  264.880 1.00 24.96  ? 35  GLU B CA  1 
ATOM   4304 C  C   . GLU B 1 35  ? -84.406  -5.209  265.503 1.00 24.58  ? 35  GLU B C   1 
ATOM   4305 O  O   . GLU B 1 35  ? -83.563  -5.830  264.851 1.00 25.67  ? 35  GLU B O   1 
ATOM   4306 C  CB  . GLU B 1 35  ? -86.447  -4.617  264.192 1.00 31.24  ? 35  GLU B CB  1 
ATOM   4307 C  CG  . GLU B 1 35  ? -87.420  -3.552  263.718 1.00 37.18  ? 35  GLU B CG  1 
ATOM   4308 C  CD  . GLU B 1 35  ? -88.748  -4.138  263.284 1.00 47.10  ? 35  GLU B CD  1 
ATOM   4309 O  OE1 . GLU B 1 35  ? -89.229  -5.078  263.952 1.00 66.34  ? 35  GLU B OE1 1 
ATOM   4310 O  OE2 . GLU B 1 35  ? -89.317  -3.657  262.283 1.00 78.01  ? 35  GLU B OE2 1 
ATOM   4311 N  N   . ILE B 1 36  ? -84.691  -5.486  266.773 1.00 26.29  ? 36  ILE B N   1 
ATOM   4312 C  CA  . ILE B 1 36  ? -84.025  -6.537  267.533 1.00 25.77  ? 36  ILE B CA  1 
ATOM   4313 C  C   . ILE B 1 36  ? -85.084  -7.542  267.959 1.00 22.95  ? 36  ILE B C   1 
ATOM   4314 O  O   . ILE B 1 36  ? -85.966  -7.222  268.766 1.00 23.54  ? 36  ILE B O   1 
ATOM   4315 C  CB  . ILE B 1 36  ? -83.275  -5.984  268.751 1.00 25.29  ? 36  ILE B CB  1 
ATOM   4316 C  CG1 . ILE B 1 36  ? -82.147  -5.052  268.307 1.00 30.50  ? 36  ILE B CG1 1 
ATOM   4317 C  CG2 . ILE B 1 36  ? -82.732  -7.121  269.602 1.00 25.05  ? 36  ILE B CG2 1 
ATOM   4318 C  CD1 . ILE B 1 36  ? -81.125  -5.715  267.414 1.00 22.86  ? 36  ILE B CD1 1 
ATOM   4319 N  N   . ASN B 1 37  ? -85.004  -8.755  267.418 1.00 23.48  ? 37  ASN B N   1 
ATOM   4320 C  CA  . ASN B 1 37  ? -85.904  -9.833  267.810 1.00 23.22  ? 37  ASN B CA  1 
ATOM   4321 C  C   . ASN B 1 37  ? -85.404  -10.400 269.132 1.00 23.24  ? 37  ASN B C   1 
ATOM   4322 O  O   . ASN B 1 37  ? -84.358  -11.054 269.177 1.00 26.48  ? 37  ASN B O   1 
ATOM   4323 C  CB  . ASN B 1 37  ? -85.956  -10.901 266.719 1.00 20.16  ? 37  ASN B CB  1 
ATOM   4324 C  CG  . ASN B 1 37  ? -86.890  -12.057 267.056 1.00 24.44  ? 37  ASN B CG  1 
ATOM   4325 O  OD1 . ASN B 1 37  ? -87.320  -12.227 268.197 1.00 31.73  ? 37  ASN B OD1 1 
ATOM   4326 N  ND2 . ASN B 1 37  ? -87.202  -12.865 266.050 1.00 25.64  ? 37  ASN B ND2 1 
ATOM   4327 N  N   . TYR B 1 38  ? -86.147  -10.153 270.209 1.00 23.52  ? 38  TYR B N   1 
ATOM   4328 C  CA  . TYR B 1 38  ? -85.725  -10.567 271.540 1.00 29.40  ? 38  TYR B CA  1 
ATOM   4329 C  C   . TYR B 1 38  ? -85.952  -12.048 271.812 1.00 37.68  ? 38  TYR B C   1 
ATOM   4330 O  O   . TYR B 1 38  ? -85.667  -12.506 272.924 1.00 36.15  ? 38  TYR B O   1 
ATOM   4331 C  CB  . TYR B 1 38  ? -86.439  -9.728  272.602 1.00 25.47  ? 38  TYR B CB  1 
ATOM   4332 C  CG  . TYR B 1 38  ? -85.896  -8.323  272.711 1.00 24.63  ? 38  TYR B CG  1 
ATOM   4333 C  CD1 . TYR B 1 38  ? -84.886  -8.020  273.611 1.00 29.35  ? 38  TYR B CD1 1 
ATOM   4334 C  CD2 . TYR B 1 38  ? -86.388  -7.302  271.909 1.00 26.05  ? 38  TYR B CD2 1 
ATOM   4335 C  CE1 . TYR B 1 38  ? -84.381  -6.742  273.713 1.00 32.88  ? 38  TYR B CE1 1 
ATOM   4336 C  CE2 . TYR B 1 38  ? -85.890  -6.017  272.005 1.00 27.91  ? 38  TYR B CE2 1 
ATOM   4337 C  CZ  . TYR B 1 38  ? -84.887  -5.744  272.910 1.00 30.07  ? 38  TYR B CZ  1 
ATOM   4338 O  OH  . TYR B 1 38  ? -84.384  -4.469  273.016 1.00 33.47  ? 38  TYR B OH  1 
ATOM   4339 N  N   . GLU B 1 39  ? -86.457  -12.804 270.839 1.00 25.54  ? 39  GLU B N   1 
ATOM   4340 C  CA  . GLU B 1 39  ? -86.571  -14.249 270.963 1.00 25.44  ? 39  GLU B CA  1 
ATOM   4341 C  C   . GLU B 1 39  ? -85.608  -15.001 270.058 1.00 25.91  ? 39  GLU B C   1 
ATOM   4342 O  O   . GLU B 1 39  ? -85.486  -16.224 270.193 1.00 36.44  ? 39  GLU B O   1 
ATOM   4343 C  CB  . GLU B 1 39  ? -88.007  -14.702 270.660 1.00 29.43  ? 39  GLU B CB  1 
ATOM   4344 C  CG  . GLU B 1 39  ? -89.056  -14.118 271.593 1.00 28.91  ? 39  GLU B CG  1 
ATOM   4345 C  CD  . GLU B 1 39  ? -88.945  -14.653 273.008 1.00 35.14  ? 39  GLU B CD  1 
ATOM   4346 O  OE1 . GLU B 1 39  ? -88.364  -15.743 273.192 1.00 33.37  ? 39  GLU B OE1 1 
ATOM   4347 O  OE2 . GLU B 1 39  ? -89.442  -13.984 273.938 1.00 33.64  ? 39  GLU B OE2 1 
ATOM   4348 N  N   . ALA B 1 40  ? -84.923  -14.311 269.152 1.00 25.33  ? 40  ALA B N   1 
ATOM   4349 C  CA  . ALA B 1 40  ? -84.026  -14.965 268.214 1.00 28.87  ? 40  ALA B CA  1 
ATOM   4350 C  C   . ALA B 1 40  ? -82.719  -15.354 268.891 1.00 34.88  ? 40  ALA B C   1 
ATOM   4351 O  O   . ALA B 1 40  ? -82.242  -14.683 269.811 1.00 30.87  ? 40  ALA B O   1 
ATOM   4352 C  CB  . ALA B 1 40  ? -83.739  -14.054 267.022 1.00 31.56  ? 40  ALA B CB  1 
ATOM   4353 N  N   . THR B 1 41  ? -82.140  -16.457 268.421 1.00 52.44  ? 41  THR B N   1 
ATOM   4354 C  CA  . THR B 1 41  ? -80.844  -16.925 268.891 1.00 32.69  ? 41  THR B CA  1 
ATOM   4355 C  C   . THR B 1 41  ? -79.739  -16.774 267.859 1.00 28.87  ? 41  THR B C   1 
ATOM   4356 O  O   . THR B 1 41  ? -78.586  -16.563 268.237 1.00 39.96  ? 41  THR B O   1 
ATOM   4357 C  CB  . THR B 1 41  ? -80.929  -18.397 269.314 1.00 35.68  ? 41  THR B CB  1 
ATOM   4358 O  OG1 . THR B 1 41  ? -81.790  -19.106 268.414 1.00 42.79  ? 41  THR B OG1 1 
ATOM   4359 C  CG2 . THR B 1 41  ? -81.479  -18.513 270.727 1.00 36.97  ? 41  THR B CG2 1 
ATOM   4360 N  N   . ALA B 1 42  ? -80.063  -16.873 266.574 1.00 28.96  ? 42  ALA B N   1 
ATOM   4361 C  CA  . ALA B 1 42  ? -79.075  -16.683 265.524 1.00 27.07  ? 42  ALA B CA  1 
ATOM   4362 C  C   . ALA B 1 42  ? -78.926  -15.203 265.194 1.00 29.34  ? 42  ALA B C   1 
ATOM   4363 O  O   . ALA B 1 42  ? -79.858  -14.411 265.356 1.00 33.54  ? 42  ALA B O   1 
ATOM   4364 C  CB  . ALA B 1 42  ? -79.466  -17.462 264.268 1.00 33.17  ? 42  ALA B CB  1 
ATOM   4365 N  N   . TYR B 1 43  ? -77.732  -14.835 264.724 1.00 30.38  ? 43  TYR B N   1 
ATOM   4366 C  CA  . TYR B 1 43  ? -77.466  -13.437 264.404 1.00 30.75  ? 43  TYR B CA  1 
ATOM   4367 C  C   . TYR B 1 43  ? -78.273  -12.969 263.200 1.00 31.74  ? 43  TYR B C   1 
ATOM   4368 O  O   . TYR B 1 43  ? -78.633  -11.789 263.120 1.00 41.57  ? 43  TYR B O   1 
ATOM   4369 C  CB  . TYR B 1 43  ? -75.972  -13.230 264.153 1.00 29.91  ? 43  TYR B CB  1 
ATOM   4370 C  CG  . TYR B 1 43  ? -75.571  -11.780 264.004 1.00 25.68  ? 43  TYR B CG  1 
ATOM   4371 C  CD1 . TYR B 1 43  ? -75.303  -10.995 265.117 1.00 22.46  ? 43  TYR B CD1 1 
ATOM   4372 C  CD2 . TYR B 1 43  ? -75.461  -11.196 262.749 1.00 26.73  ? 43  TYR B CD2 1 
ATOM   4373 C  CE1 . TYR B 1 43  ? -74.937  -9.670  264.984 1.00 22.76  ? 43  TYR B CE1 1 
ATOM   4374 C  CE2 . TYR B 1 43  ? -75.095  -9.873  262.607 1.00 25.93  ? 43  TYR B CE2 1 
ATOM   4375 C  CZ  . TYR B 1 43  ? -74.835  -9.114  263.728 1.00 23.20  ? 43  TYR B CZ  1 
ATOM   4376 O  OH  . TYR B 1 43  ? -74.470  -7.795  263.592 1.00 22.84  ? 43  TYR B OH  1 
ATOM   4377 N  N   . GLU B 1 44  ? -78.565  -13.869 262.258 1.00 26.90  ? 44  GLU B N   1 
ATOM   4378 C  CA  . GLU B 1 44  ? -79.321  -13.477 261.074 1.00 29.86  ? 44  GLU B CA  1 
ATOM   4379 C  C   . GLU B 1 44  ? -80.762  -13.120 261.415 1.00 28.27  ? 44  GLU B C   1 
ATOM   4380 O  O   . GLU B 1 44  ? -81.371  -12.290 260.730 1.00 33.18  ? 44  GLU B O   1 
ATOM   4381 C  CB  . GLU B 1 44  ? -79.282  -14.592 260.031 1.00 45.59  ? 44  GLU B CB  1 
ATOM   4382 C  CG  . GLU B 1 44  ? -77.916  -14.798 259.399 1.00 34.15  ? 44  GLU B CG  1 
ATOM   4383 C  CD  . GLU B 1 44  ? -77.673  -13.866 258.230 1.00 37.62  ? 44  GLU B CD  1 
ATOM   4384 O  OE1 . GLU B 1 44  ? -78.659  -13.440 257.593 1.00 34.91  ? 44  GLU B OE1 1 
ATOM   4385 O  OE2 . GLU B 1 44  ? -76.496  -13.556 257.949 1.00 74.60  ? 44  GLU B OE2 1 
ATOM   4386 N  N   . ASN B 1 45  ? -81.323  -13.730 262.456 1.00 26.66  ? 45  ASN B N   1 
ATOM   4387 C  CA  . ASN B 1 45  ? -82.671  -13.417 262.909 1.00 26.43  ? 45  ASN B CA  1 
ATOM   4388 C  C   . ASN B 1 45  ? -82.690  -12.417 264.056 1.00 26.12  ? 45  ASN B C   1 
ATOM   4389 O  O   . ASN B 1 45  ? -83.773  -11.998 264.476 1.00 27.15  ? 45  ASN B O   1 
ATOM   4390 C  CB  . ASN B 1 45  ? -83.400  -14.698 263.331 1.00 28.31  ? 45  ASN B CB  1 
ATOM   4391 C  CG  . ASN B 1 45  ? -83.444  -15.733 262.227 1.00 33.10  ? 45  ASN B CG  1 
ATOM   4392 O  OD1 . ASN B 1 45  ? -83.448  -15.395 261.044 1.00 30.74  ? 45  ASN B OD1 1 
ATOM   4393 N  ND2 . ASN B 1 45  ? -83.478  -17.005 262.609 1.00 60.67  ? 45  ASN B ND2 1 
ATOM   4394 N  N   . LEU B 1 46  ? -81.524  -12.024 264.568 1.00 26.52  ? 46  LEU B N   1 
ATOM   4395 C  CA  . LEU B 1 46  ? -81.475  -11.092 265.689 1.00 27.03  ? 46  LEU B CA  1 
ATOM   4396 C  C   . LEU B 1 46  ? -81.779  -9.666  265.247 1.00 23.96  ? 46  LEU B C   1 
ATOM   4397 O  O   . LEU B 1 46  ? -82.604  -8.981  265.861 1.00 22.31  ? 46  LEU B O   1 
ATOM   4398 C  CB  . LEU B 1 46  ? -80.105  -11.158 266.366 1.00 26.01  ? 46  LEU B CB  1 
ATOM   4399 C  CG  . LEU B 1 46  ? -79.842  -10.096 267.435 1.00 26.54  ? 46  LEU B CG  1 
ATOM   4400 C  CD1 . LEU B 1 46  ? -80.800  -10.260 268.602 1.00 25.51  ? 46  LEU B CD1 1 
ATOM   4401 C  CD2 . LEU B 1 46  ? -78.398  -10.151 267.908 1.00 24.67  ? 46  LEU B CD2 1 
ATOM   4402 N  N   . ILE B 1 47  ? -81.126  -9.205  264.186 1.00 27.14  ? 47  ILE B N   1 
ATOM   4403 C  CA  . ILE B 1 47  ? -81.228  -7.819  263.755 1.00 29.65  ? 47  ILE B CA  1 
ATOM   4404 C  C   . ILE B 1 47  ? -82.053  -7.739  262.477 1.00 32.14  ? 47  ILE B C   1 
ATOM   4405 O  O   . ILE B 1 47  ? -82.204  -8.712  261.732 1.00 35.21  ? 47  ILE B O   1 
ATOM   4406 C  CB  . ILE B 1 47  ? -79.839  -7.182  263.546 1.00 23.12  ? 47  ILE B CB  1 
ATOM   4407 C  CG1 . ILE B 1 47  ? -79.102  -7.877  262.401 1.00 25.73  ? 47  ILE B CG1 1 
ATOM   4408 C  CG2 . ILE B 1 47  ? -79.023  -7.263  264.822 1.00 28.93  ? 47  ILE B CG2 1 
ATOM   4409 C  CD1 . ILE B 1 47  ? -77.765  -7.253  262.071 1.00 28.80  ? 47  ILE B CD1 1 
ATOM   4410 N  N   . LYS B 1 48  ? -82.597  -6.550  262.232 1.00 34.00  ? 48  LYS B N   1 
ATOM   4411 C  CA  . LYS B 1 48  ? -83.328  -6.248  261.001 1.00 28.47  ? 48  LYS B CA  1 
ATOM   4412 C  C   . LYS B 1 48  ? -83.007  -4.819  260.597 1.00 26.25  ? 48  LYS B C   1 
ATOM   4413 O  O   . LYS B 1 48  ? -83.753  -3.882  260.906 1.00 25.50  ? 48  LYS B O   1 
ATOM   4414 C  CB  . LYS B 1 48  ? -84.835  -6.446  261.183 1.00 30.23  ? 48  LYS B CB  1 
ATOM   4415 C  CG  . LYS B 1 48  ? -85.628  -6.342  259.887 1.00 36.40  ? 48  LYS B CG  1 
ATOM   4416 C  CD  . LYS B 1 48  ? -87.113  -6.565  260.119 1.00 46.52  ? 48  LYS B CD  1 
ATOM   4417 C  CE  . LYS B 1 48  ? -87.814  -6.981  258.834 1.00 51.80  ? 48  LYS B CE  1 
ATOM   4418 N  NZ  . LYS B 1 48  ? -88.912  -7.956  259.085 1.00 46.83  ? 48  LYS B NZ  1 
ATOM   4419 N  N   . PRO B 1 49  ? -81.885  -4.611  259.910 1.00 27.06  ? 49  PRO B N   1 
ATOM   4420 C  CA  . PRO B 1 49  ? -81.520  -3.252  259.493 1.00 33.41  ? 49  PRO B CA  1 
ATOM   4421 C  C   . PRO B 1 49  ? -82.471  -2.727  258.429 1.00 29.80  ? 49  PRO B C   1 
ATOM   4422 O  O   . PRO B 1 49  ? -82.837  -3.437  257.490 1.00 27.47  ? 49  PRO B O   1 
ATOM   4423 C  CB  . PRO B 1 49  ? -80.099  -3.417  258.939 1.00 31.99  ? 49  PRO B CB  1 
ATOM   4424 C  CG  . PRO B 1 49  ? -79.615  -4.731  259.482 1.00 25.54  ? 49  PRO B CG  1 
ATOM   4425 C  CD  . PRO B 1 49  ? -80.834  -5.588  259.587 1.00 23.73  ? 49  PRO B CD  1 
ATOM   4426 N  N   . LYS B 1 50  ? -82.868  -1.466  258.584 1.00 27.43  ? 50  LYS B N   1 
ATOM   4427 C  CA  . LYS B 1 50  ? -83.785  -0.815  257.658 1.00 29.57  ? 50  LYS B CA  1 
ATOM   4428 C  C   . LYS B 1 50  ? -83.177  0.490   257.172 1.00 33.47  ? 50  LYS B C   1 
ATOM   4429 O  O   . LYS B 1 50  ? -82.656  1.273   257.974 1.00 38.15  ? 50  LYS B O   1 
ATOM   4430 C  CB  . LYS B 1 50  ? -85.143  -0.545  258.312 1.00 31.10  ? 50  LYS B CB  1 
ATOM   4431 C  CG  . LYS B 1 50  ? -85.935  -1.793  258.648 1.00 35.03  ? 50  LYS B CG  1 
ATOM   4432 C  CD  . LYS B 1 50  ? -87.314  -1.436  259.169 1.00 31.67  ? 50  LYS B CD  1 
ATOM   4433 C  CE  . LYS B 1 50  ? -88.083  -2.678  259.574 1.00 44.25  ? 50  LYS B CE  1 
ATOM   4434 N  NZ  . LYS B 1 50  ? -89.455  -2.352  260.052 1.00 42.08  ? 50  LYS B NZ  1 
ATOM   4435 N  N   . GLU B 1 51  ? -83.242  0.717   255.858 1.00 35.23  ? 51  GLU B N   1 
ATOM   4436 C  CA  . GLU B 1 51  ? -82.850  2.011   255.310 1.00 43.82  ? 51  GLU B CA  1 
ATOM   4437 C  C   . GLU B 1 51  ? -83.720  3.124   255.876 1.00 37.34  ? 51  GLU B C   1 
ATOM   4438 O  O   . GLU B 1 51  ? -83.226  4.212   256.194 1.00 36.87  ? 51  GLU B O   1 
ATOM   4439 C  CB  . GLU B 1 51  ? -82.946  1.984   253.784 1.00 50.98  ? 51  GLU B CB  1 
ATOM   4440 C  CG  . GLU B 1 51  ? -81.980  1.030   253.096 1.00 56.10  ? 51  GLU B CG  1 
ATOM   4441 C  CD  . GLU B 1 51  ? -80.545  1.526   253.108 1.00 76.77  ? 51  GLU B CD  1 
ATOM   4442 O  OE1 . GLU B 1 51  ? -80.308  2.674   253.541 1.00 78.51  ? 51  GLU B OE1 1 
ATOM   4443 O  OE2 . GLU B 1 51  ? -79.653  0.767   252.677 1.00 67.24  ? 51  GLU B OE2 1 
ATOM   4444 N  N   . GLN B 1 52  ? -85.017  2.864   256.015 1.00 35.80  ? 52  GLN B N   1 
ATOM   4445 C  CA  . GLN B 1 52  ? -85.972  3.849   256.493 1.00 33.89  ? 52  GLN B CA  1 
ATOM   4446 C  C   . GLN B 1 52  ? -86.998  3.156   257.376 1.00 34.15  ? 52  GLN B C   1 
ATOM   4447 O  O   . GLN B 1 52  ? -87.121  1.929   257.374 1.00 60.63  ? 52  GLN B O   1 
ATOM   4448 C  CB  . GLN B 1 52  ? -86.677  4.555   255.329 1.00 37.05  ? 52  GLN B CB  1 
ATOM   4449 C  CG  . GLN B 1 52  ? -87.649  3.654   254.582 1.00 34.76  ? 52  GLN B CG  1 
ATOM   4450 C  CD  . GLN B 1 52  ? -88.013  4.189   253.213 1.00 37.60  ? 52  GLN B CD  1 
ATOM   4451 O  OE1 . GLN B 1 52  ? -87.175  4.755   252.512 1.00 65.26  ? 52  GLN B OE1 1 
ATOM   4452 N  NE2 . GLN B 1 52  ? -89.270  4.011   252.824 1.00 40.52  ? 52  GLN B NE2 1 
ATOM   4453 N  N   . VAL B 1 53  ? -87.737  3.959   258.133 1.00 30.33  ? 53  VAL B N   1 
ATOM   4454 C  CA  . VAL B 1 53  ? -88.855  3.478   258.932 1.00 32.31  ? 53  VAL B CA  1 
ATOM   4455 C  C   . VAL B 1 53  ? -90.079  4.311   258.577 1.00 47.26  ? 53  VAL B C   1 
ATOM   4456 O  O   . VAL B 1 53  ? -89.971  5.517   258.327 1.00 50.80  ? 53  VAL B O   1 
ATOM   4457 C  CB  . VAL B 1 53  ? -88.551  3.533   260.446 1.00 27.08  ? 53  VAL B CB  1 
ATOM   4458 C  CG1 . VAL B 1 53  ? -88.437  4.970   260.933 1.00 28.35  ? 53  VAL B CG1 1 
ATOM   4459 C  CG2 . VAL B 1 53  ? -89.609  2.773   261.233 1.00 31.72  ? 53  VAL B CG2 1 
ATOM   4460 N  N   . ASP B 1 54  ? -91.238  3.661   258.523 1.00 29.15  ? 54  ASP B N   1 
ATOM   4461 C  CA  . ASP B 1 54  ? -92.485  4.300   258.118 1.00 29.09  ? 54  ASP B CA  1 
ATOM   4462 C  C   . ASP B 1 54  ? -93.365  4.480   259.348 1.00 30.34  ? 54  ASP B C   1 
ATOM   4463 O  O   . ASP B 1 54  ? -93.926  3.509   259.865 1.00 38.81  ? 54  ASP B O   1 
ATOM   4464 C  CB  . ASP B 1 54  ? -93.197  3.477   257.047 1.00 32.30  ? 54  ASP B CB  1 
ATOM   4465 C  CG  . ASP B 1 54  ? -92.442  3.452   255.734 1.00 32.71  ? 54  ASP B CG  1 
ATOM   4466 O  OD1 . ASP B 1 54  ? -92.421  4.489   255.039 1.00 32.33  ? 54  ASP B OD1 1 
ATOM   4467 O  OD2 . ASP B 1 54  ? -91.871  2.394   255.395 1.00 38.55  ? 54  ASP B OD2 1 
ATOM   4468 N  N   . VAL B 1 55  ? -93.481  5.721   259.813 1.00 30.09  ? 55  VAL B N   1 
ATOM   4469 C  CA  . VAL B 1 55  ? -94.376  6.048   260.918 1.00 24.55  ? 55  VAL B CA  1 
ATOM   4470 C  C   . VAL B 1 55  ? -95.790  6.148   260.356 1.00 26.44  ? 55  VAL B C   1 
ATOM   4471 O  O   . VAL B 1 55  ? -96.104  7.068   259.598 1.00 43.04  ? 55  VAL B O   1 
ATOM   4472 C  CB  . VAL B 1 55  ? -93.961  7.348   261.616 1.00 23.74  ? 55  VAL B CB  1 
ATOM   4473 C  CG1 . VAL B 1 55  ? -95.016  7.765   262.627 1.00 25.73  ? 55  VAL B CG1 1 
ATOM   4474 C  CG2 . VAL B 1 55  ? -92.613  7.172   262.295 1.00 25.97  ? 55  VAL B CG2 1 
ATOM   4475 N  N   . GLN B 1 56  ? -96.642  5.196   260.720 1.00 26.98  ? 56  GLN B N   1 
ATOM   4476 C  CA  . GLN B 1 56  ? -98.018  5.152   260.250 1.00 26.43  ? 56  GLN B CA  1 
ATOM   4477 C  C   . GLN B 1 56  ? -98.953  5.658   261.340 1.00 28.22  ? 56  GLN B C   1 
ATOM   4478 O  O   . GLN B 1 56  ? -98.814  5.291   262.511 1.00 31.28  ? 56  GLN B O   1 
ATOM   4479 C  CB  . GLN B 1 56  ? -98.409  3.732   259.839 1.00 26.68  ? 56  GLN B CB  1 
ATOM   4480 C  CG  . GLN B 1 56  ? -97.708  3.240   258.584 1.00 31.89  ? 56  GLN B CG  1 
ATOM   4481 C  CD  . GLN B 1 56  ? -97.975  1.776   258.303 1.00 34.71  ? 56  GLN B CD  1 
ATOM   4482 O  OE1 . GLN B 1 56  ? -99.090  1.392   257.949 1.00 30.32  ? 56  GLN B OE1 1 
ATOM   4483 N  NE2 . GLN B 1 56  ? -96.950  0.947   258.462 1.00 33.76  ? 56  GLN B NE2 1 
ATOM   4484 N  N   . VAL B 1 57  ? -99.903  6.503   260.948 1.00 25.79  ? 57  VAL B N   1 
ATOM   4485 C  CA  . VAL B 1 57  ? -100.852 7.102   261.879 1.00 23.74  ? 57  VAL B CA  1 
ATOM   4486 C  C   . VAL B 1 57  ? -102.232 7.107   261.238 1.00 25.84  ? 57  VAL B C   1 
ATOM   4487 O  O   . VAL B 1 57  ? -102.386 7.505   260.078 1.00 29.19  ? 57  VAL B O   1 
ATOM   4488 C  CB  . VAL B 1 57  ? -100.429 8.528   262.287 1.00 24.30  ? 57  VAL B CB  1 
ATOM   4489 C  CG1 . VAL B 1 57  ? -100.074 9.358   261.065 1.00 32.65  ? 57  VAL B CG1 1 
ATOM   4490 C  CG2 . VAL B 1 57  ? -101.528 9.202   263.092 1.00 30.84  ? 57  VAL B CG2 1 
ATOM   4491 N  N   . SER B 1 58  ? -103.231 6.652   261.988 1.00 27.29  ? 58  SER B N   1 
ATOM   4492 C  CA  . SER B 1 58  ? -104.618 6.668   261.553 1.00 34.27  ? 58  SER B CA  1 
ATOM   4493 C  C   . SER B 1 58  ? -105.467 7.316   262.637 1.00 45.09  ? 58  SER B C   1 
ATOM   4494 O  O   . SER B 1 58  ? -105.075 7.379   263.806 1.00 40.32  ? 58  SER B O   1 
ATOM   4495 C  CB  . SER B 1 58  ? -105.131 5.255   261.244 1.00 37.10  ? 58  SER B CB  1 
ATOM   4496 O  OG  . SER B 1 58  ? -106.402 5.302   260.622 1.00 65.99  ? 58  SER B OG  1 
ATOM   4497 N  N   . TRP B 1 59  ? -106.642 7.798   262.241 1.00 47.92  ? 59  TRP B N   1 
ATOM   4498 C  CA  . TRP B 1 59  ? -107.483 8.559   263.152 1.00 38.55  ? 59  TRP B CA  1 
ATOM   4499 C  C   . TRP B 1 59  ? -108.945 8.410   262.755 1.00 39.89  ? 59  TRP B C   1 
ATOM   4500 O  O   . TRP B 1 59  ? -109.274 7.955   261.656 1.00 44.56  ? 59  TRP B O   1 
ATOM   4501 C  CB  . TRP B 1 59  ? -107.083 10.038  263.167 1.00 41.82  ? 59  TRP B CB  1 
ATOM   4502 C  CG  . TRP B 1 59  ? -107.318 10.730  261.857 1.00 41.62  ? 59  TRP B CG  1 
ATOM   4503 C  CD1 . TRP B 1 59  ? -108.425 11.438  261.490 1.00 39.36  ? 59  TRP B CD1 1 
ATOM   4504 C  CD2 . TRP B 1 59  ? -106.426 10.771  260.736 1.00 37.43  ? 59  TRP B CD2 1 
ATOM   4505 N  NE1 . TRP B 1 59  ? -108.277 11.920  260.212 1.00 34.21  ? 59  TRP B NE1 1 
ATOM   4506 C  CE2 . TRP B 1 59  ? -107.058 11.525  259.727 1.00 36.52  ? 59  TRP B CE2 1 
ATOM   4507 C  CE3 . TRP B 1 59  ? -105.155 10.245  260.488 1.00 35.97  ? 59  TRP B CE3 1 
ATOM   4508 C  CZ2 . TRP B 1 59  ? -106.463 11.766  258.492 1.00 35.47  ? 59  TRP B CZ2 1 
ATOM   4509 C  CZ3 . TRP B 1 59  ? -104.566 10.486  259.260 1.00 35.38  ? 59  TRP B CZ3 1 
ATOM   4510 C  CH2 . TRP B 1 59  ? -105.219 11.239  258.278 1.00 34.44  ? 59  TRP B CH2 1 
ATOM   4511 N  N   . ASN B 1 60  ? -109.821 8.801   263.676 1.00 38.80  ? 60  ASN B N   1 
ATOM   4512 C  CA  . ASN B 1 60  ? -111.252 8.893   263.437 1.00 40.55  ? 60  ASN B CA  1 
ATOM   4513 C  C   . ASN B 1 60  ? -111.724 10.305  263.757 1.00 41.24  ? 60  ASN B C   1 
ATOM   4514 O  O   . ASN B 1 60  ? -111.033 11.075  264.430 1.00 41.50  ? 60  ASN B O   1 
ATOM   4515 C  CB  . ASN B 1 60  ? -112.031 7.872   264.277 1.00 43.38  ? 60  ASN B CB  1 
ATOM   4516 C  CG  . ASN B 1 60  ? -111.834 6.449   263.795 1.00 52.35  ? 60  ASN B CG  1 
ATOM   4517 O  OD1 . ASN B 1 60  ? -111.707 6.200   262.596 1.00 59.88  ? 60  ASN B OD1 1 
ATOM   4518 N  ND2 . ASN B 1 60  ? -111.813 5.506   264.729 1.00 56.23  ? 60  ASN B ND2 1 
ATOM   4519 N  N   . VAL B 1 61  ? -112.914 10.641  263.267 1.00 42.11  ? 61  VAL B N   1 
ATOM   4520 C  CA  . VAL B 1 61  ? -113.481 11.975  263.416 1.00 41.37  ? 61  VAL B CA  1 
ATOM   4521 C  C   . VAL B 1 61  ? -114.801 11.863  264.164 1.00 40.60  ? 61  VAL B C   1 
ATOM   4522 O  O   . VAL B 1 61  ? -115.648 11.030  263.819 1.00 39.87  ? 61  VAL B O   1 
ATOM   4523 C  CB  . VAL B 1 61  ? -113.685 12.661  262.053 1.00 44.51  ? 61  VAL B CB  1 
ATOM   4524 C  CG1 . VAL B 1 61  ? -114.193 14.079  262.247 1.00 65.56  ? 61  VAL B CG1 1 
ATOM   4525 C  CG2 . VAL B 1 61  ? -112.389 12.656  261.257 1.00 51.23  ? 61  VAL B CG2 1 
ATOM   4526 N  N   . TRP B 1 62  ? -114.974 12.700  265.185 1.00 40.98  ? 62  TRP B N   1 
ATOM   4527 C  CA  . TRP B 1 62  ? -116.201 12.754  265.964 1.00 53.76  ? 62  TRP B CA  1 
ATOM   4528 C  C   . TRP B 1 62  ? -116.813 14.144  265.863 1.00 48.50  ? 62  TRP B C   1 
ATOM   4529 O  O   . TRP B 1 62  ? -116.102 15.144  265.722 1.00 48.29  ? 62  TRP B O   1 
ATOM   4530 C  CB  . TRP B 1 62  ? -115.953 12.415  267.440 1.00 47.24  ? 62  TRP B CB  1 
ATOM   4531 C  CG  . TRP B 1 62  ? -115.248 11.111  267.671 1.00 44.45  ? 62  TRP B CG  1 
ATOM   4532 C  CD1 . TRP B 1 62  ? -115.139 10.068  266.798 1.00 55.49  ? 62  TRP B CD1 1 
ATOM   4533 C  CD2 . TRP B 1 62  ? -114.555 10.713  268.859 1.00 56.41  ? 62  TRP B CD2 1 
ATOM   4534 N  NE1 . TRP B 1 62  ? -114.418 9.047   267.368 1.00 46.68  ? 62  TRP B NE1 1 
ATOM   4535 C  CE2 . TRP B 1 62  ? -114.049 9.418   268.634 1.00 41.59  ? 62  TRP B CE2 1 
ATOM   4536 C  CE3 . TRP B 1 62  ? -114.314 11.326  270.092 1.00 50.39  ? 62  TRP B CE3 1 
ATOM   4537 C  CZ2 . TRP B 1 62  ? -113.315 8.727   269.594 1.00 43.82  ? 62  TRP B CZ2 1 
ATOM   4538 C  CZ3 . TRP B 1 62  ? -113.585 10.637  271.045 1.00 44.83  ? 62  TRP B CZ3 1 
ATOM   4539 C  CH2 . TRP B 1 62  ? -113.095 9.351   270.791 1.00 43.23  ? 62  TRP B CH2 1 
ATOM   4540 N  N   . ASN B 1 63  ? -118.144 14.191  265.941 1.00 50.37  ? 63  ASN B N   1 
ATOM   4541 C  CA  . ASN B 1 63  ? -118.911 15.437  265.953 1.00 49.14  ? 63  ASN B CA  1 
ATOM   4542 C  C   . ASN B 1 63  ? -118.604 16.274  264.706 1.00 52.39  ? 63  ASN B C   1 
ATOM   4543 O  O   . ASN B 1 63  ? -117.942 17.311  264.753 1.00 51.81  ? 63  ASN B O   1 
ATOM   4544 C  CB  . ASN B 1 63  ? -118.639 16.225  267.243 1.00 64.67  ? 63  ASN B CB  1 
ATOM   4545 C  CG  . ASN B 1 63  ? -119.386 17.549  267.297 1.00 67.86  ? 63  ASN B CG  1 
ATOM   4546 O  OD1 . ASN B 1 63  ? -120.375 17.749  266.592 1.00 54.53  ? 63  ASN B OD1 1 
ATOM   4547 N  ND2 . ASN B 1 63  ? -118.906 18.465  268.132 1.00 58.53  ? 63  ASN B ND2 1 
ATOM   4548 N  N   . GLY B 1 64  ? -119.100 15.780  263.581 1.00 53.23  ? 64  GLY B N   1 
ATOM   4549 C  CA  . GLY B 1 64  ? -119.026 16.499  262.327 1.00 65.39  ? 64  GLY B CA  1 
ATOM   4550 C  C   . GLY B 1 64  ? -118.327 15.698  261.249 1.00 61.50  ? 64  GLY B C   1 
ATOM   4551 O  O   . GLY B 1 64  ? -118.060 14.501  261.389 1.00 53.69  ? 64  GLY B O   1 
ATOM   4552 N  N   . ASP B 1 65  ? -118.023 16.389  260.153 1.00 61.69  ? 65  ASP B N   1 
ATOM   4553 C  CA  . ASP B 1 65  ? -117.434 15.778  258.975 1.00 54.84  ? 65  ASP B CA  1 
ATOM   4554 C  C   . ASP B 1 65  ? -115.934 15.572  259.155 1.00 53.21  ? 65  ASP B C   1 
ATOM   4555 O  O   . ASP B 1 65  ? -115.301 16.137  260.051 1.00 50.41  ? 65  ASP B O   1 
ATOM   4556 C  CB  . ASP B 1 65  ? -117.695 16.641  257.741 1.00 60.14  ? 65  ASP B CB  1 
ATOM   4557 C  CG  . ASP B 1 65  ? -117.136 18.042  257.884 1.00 65.33  ? 65  ASP B CG  1 
ATOM   4558 O  OD1 . ASP B 1 65  ? -117.844 18.909  258.438 1.00 65.24  ? 65  ASP B OD1 1 
ATOM   4559 O  OD2 . ASP B 1 65  ? -115.989 18.277  257.450 1.00 90.58  ? 65  ASP B OD2 1 
ATOM   4560 N  N   . ILE B 1 66  ? -115.366 14.749  258.270 1.00 51.10  ? 66  ILE B N   1 
ATOM   4561 C  CA  . ILE B 1 66  ? -113.948 14.417  258.330 1.00 47.29  ? 66  ILE B CA  1 
ATOM   4562 C  C   . ILE B 1 66  ? -113.049 15.543  257.849 1.00 47.93  ? 66  ILE B C   1 
ATOM   4563 O  O   . ILE B 1 66  ? -111.831 15.473  258.038 1.00 57.58  ? 66  ILE B O   1 
ATOM   4564 C  CB  . ILE B 1 66  ? -113.662 13.149  257.501 1.00 49.88  ? 66  ILE B CB  1 
ATOM   4565 C  CG1 . ILE B 1 66  ? -114.088 13.363  256.047 1.00 56.99  ? 66  ILE B CG1 1 
ATOM   4566 C  CG2 . ILE B 1 66  ? -114.377 11.949  258.102 1.00 70.03  ? 66  ILE B CG2 1 
ATOM   4567 C  CD1 . ILE B 1 66  ? -113.778 12.193  255.141 1.00 48.85  ? 66  ILE B CD1 1 
ATOM   4568 N  N   . GLY B 1 67  ? -113.612 16.578  257.232 1.00 45.12  ? 67  GLY B N   1 
ATOM   4569 C  CA  . GLY B 1 67  ? -112.825 17.651  256.668 1.00 42.61  ? 67  GLY B CA  1 
ATOM   4570 C  C   . GLY B 1 67  ? -112.439 17.383  255.225 1.00 42.43  ? 67  GLY B C   1 
ATOM   4571 O  O   . GLY B 1 67  ? -112.657 16.303  254.670 1.00 43.21  ? 67  GLY B O   1 
ATOM   4572 N  N   . ASP B 1 68  ? -111.843 18.400  254.606 1.00 46.92  ? 68  ASP B N   1 
ATOM   4573 C  CA  . ASP B 1 68  ? -111.460 18.336  253.201 1.00 44.42  ? 68  ASP B CA  1 
ATOM   4574 C  C   . ASP B 1 68  ? -110.009 17.926  252.991 1.00 44.16  ? 68  ASP B C   1 
ATOM   4575 O  O   . ASP B 1 68  ? -109.715 17.167  252.063 1.00 47.76  ? 68  ASP B O   1 
ATOM   4576 C  CB  . ASP B 1 68  ? -111.710 19.687  252.524 1.00 45.22  ? 68  ASP B CB  1 
ATOM   4577 C  CG  . ASP B 1 68  ? -113.165 20.107  252.584 1.00 51.00  ? 68  ASP B CG  1 
ATOM   4578 O  OD1 . ASP B 1 68  ? -114.038 19.220  252.686 1.00 80.27  ? 68  ASP B OD1 1 
ATOM   4579 O  OD2 . ASP B 1 68  ? -113.436 21.325  252.523 1.00 67.29  ? 68  ASP B OD2 1 
ATOM   4580 N  N   . ILE B 1 69  ? -109.091 18.409  253.828 1.00 38.40  ? 69  ILE B N   1 
ATOM   4581 C  CA  . ILE B 1 69  ? -107.674 18.100  253.692 1.00 37.24  ? 69  ILE B CA  1 
ATOM   4582 C  C   . ILE B 1 69  ? -107.096 17.843  255.078 1.00 41.10  ? 69  ILE B C   1 
ATOM   4583 O  O   . ILE B 1 69  ? -107.542 18.417  256.076 1.00 44.57  ? 69  ILE B O   1 
ATOM   4584 C  CB  . ILE B 1 69  ? -106.912 19.230  252.957 1.00 36.64  ? 69  ILE B CB  1 
ATOM   4585 C  CG1 . ILE B 1 69  ? -105.571 18.723  252.424 1.00 46.77  ? 69  ILE B CG1 1 
ATOM   4586 C  CG2 . ILE B 1 69  ? -106.718 20.439  253.862 1.00 41.59  ? 69  ILE B CG2 1 
ATOM   4587 C  CD1 . ILE B 1 69  ? -104.975 19.603  251.347 1.00 57.73  ? 69  ILE B CD1 1 
ATOM   4588 N  N   . ALA B 1 70  ? -106.104 16.955  255.137 1.00 43.18  ? 70  ALA B N   1 
ATOM   4589 C  CA  . ALA B 1 70  ? -105.531 16.508  256.398 1.00 38.88  ? 70  ALA B CA  1 
ATOM   4590 C  C   . ALA B 1 70  ? -104.020 16.677  256.382 1.00 38.80  ? 70  ALA B C   1 
ATOM   4591 O  O   . ALA B 1 70  ? -103.368 16.421  255.366 1.00 40.00  ? 70  ALA B O   1 
ATOM   4592 C  CB  . ALA B 1 70  ? -105.887 15.043  256.680 1.00 64.17  ? 70  ALA B CB  1 
ATOM   4593 N  N   . TYR B 1 71  ? -103.470 17.103  257.517 1.00 36.70  ? 71  TYR B N   1 
ATOM   4594 C  CA  . TYR B 1 71  ? -102.037 17.282  257.693 1.00 33.02  ? 71  TYR B CA  1 
ATOM   4595 C  C   . TYR B 1 71  ? -101.555 16.478  258.893 1.00 30.72  ? 71  TYR B C   1 
ATOM   4596 O  O   . TYR B 1 71  ? -102.292 16.275  259.863 1.00 32.23  ? 71  TYR B O   1 
ATOM   4597 C  CB  . TYR B 1 71  ? -101.673 18.760  257.898 1.00 37.12  ? 71  TYR B CB  1 
ATOM   4598 C  CG  . TYR B 1 71  ? -102.052 19.669  256.752 1.00 38.82  ? 71  TYR B CG  1 
ATOM   4599 C  CD1 . TYR B 1 71  ? -101.261 19.747  255.617 1.00 38.23  ? 71  TYR B CD1 1 
ATOM   4600 C  CD2 . TYR B 1 71  ? -103.195 20.454  256.809 1.00 38.59  ? 71  TYR B CD2 1 
ATOM   4601 C  CE1 . TYR B 1 71  ? -101.599 20.574  254.566 1.00 40.40  ? 71  TYR B CE1 1 
ATOM   4602 C  CE2 . TYR B 1 71  ? -103.542 21.287  255.762 1.00 42.01  ? 71  TYR B CE2 1 
ATOM   4603 C  CZ  . TYR B 1 71  ? -102.739 21.342  254.643 1.00 42.15  ? 71  TYR B CZ  1 
ATOM   4604 O  OH  . TYR B 1 71  ? -103.073 22.166  253.596 1.00 42.67  ? 71  TYR B OH  1 
ATOM   4605 N  N   . VAL B 1 72  ? -100.307 16.023  258.818 1.00 28.69  ? 72  VAL B N   1 
ATOM   4606 C  CA  . VAL B 1 72  ? -99.631  15.356  259.926 1.00 27.88  ? 72  VAL B CA  1 
ATOM   4607 C  C   . VAL B 1 72  ? -98.511  16.268  260.404 1.00 27.84  ? 72  VAL B C   1 
ATOM   4608 O  O   . VAL B 1 72  ? -97.746  16.799  259.590 1.00 26.93  ? 72  VAL B O   1 
ATOM   4609 C  CB  . VAL B 1 72  ? -99.087  13.978  259.513 1.00 25.08  ? 72  VAL B CB  1 
ATOM   4610 C  CG1 . VAL B 1 72  ? -98.323  13.343  260.663 1.00 25.15  ? 72  VAL B CG1 1 
ATOM   4611 C  CG2 . VAL B 1 72  ? -100.225 13.079  259.072 1.00 26.05  ? 72  VAL B CG2 1 
ATOM   4612 N  N   . LEU B 1 73  ? -98.416  16.453  261.718 1.00 25.87  ? 73  LEU B N   1 
ATOM   4613 C  CA  . LEU B 1 73  ? -97.510  17.429  262.308 1.00 25.73  ? 73  LEU B CA  1 
ATOM   4614 C  C   . LEU B 1 73  ? -96.499  16.730  263.205 1.00 28.69  ? 73  LEU B C   1 
ATOM   4615 O  O   . LEU B 1 73  ? -96.872  16.145  264.227 1.00 25.86  ? 73  LEU B O   1 
ATOM   4616 C  CB  . LEU B 1 73  ? -98.286  18.478  263.107 1.00 27.72  ? 73  LEU B CB  1 
ATOM   4617 C  CG  . LEU B 1 73  ? -99.321  19.297  262.335 1.00 32.43  ? 73  LEU B CG  1 
ATOM   4618 C  CD1 . LEU B 1 73  ? -99.953  20.340  263.241 1.00 35.84  ? 73  LEU B CD1 1 
ATOM   4619 C  CD2 . LEU B 1 73  ? -98.687  19.951  261.118 1.00 40.78  ? 73  LEU B CD2 1 
ATOM   4620 N  N   . PHE B 1 74  ? -95.227  16.794  262.821 1.00 32.42  ? 74  PHE B N   1 
ATOM   4621 C  CA  . PHE B 1 74  ? -94.118  16.451  263.702 1.00 30.54  ? 74  PHE B CA  1 
ATOM   4622 C  C   . PHE B 1 74  ? -93.515  17.745  264.227 1.00 31.51  ? 74  PHE B C   1 
ATOM   4623 O  O   . PHE B 1 74  ? -93.261  18.670  263.449 1.00 43.31  ? 74  PHE B O   1 
ATOM   4624 C  CB  . PHE B 1 74  ? -93.041  15.641  262.978 1.00 31.42  ? 74  PHE B CB  1 
ATOM   4625 C  CG  . PHE B 1 74  ? -93.497  14.293  262.497 1.00 30.57  ? 74  PHE B CG  1 
ATOM   4626 C  CD1 . PHE B 1 74  ? -94.710  13.759  262.899 1.00 41.64  ? 74  PHE B CD1 1 
ATOM   4627 C  CD2 . PHE B 1 74  ? -92.696  13.552  261.646 1.00 29.82  ? 74  PHE B CD2 1 
ATOM   4628 C  CE1 . PHE B 1 74  ? -95.116  12.517  262.449 1.00 56.38  ? 74  PHE B CE1 1 
ATOM   4629 C  CE2 . PHE B 1 74  ? -93.095  12.312  261.198 1.00 28.84  ? 74  PHE B CE2 1 
ATOM   4630 C  CZ  . PHE B 1 74  ? -94.306  11.794  261.599 1.00 43.51  ? 74  PHE B CZ  1 
ATOM   4631 N  N   . ASP B 1 75  ? -93.290  17.811  265.541 1.00 29.18  ? 75  ASP B N   1 
ATOM   4632 C  CA  . ASP B 1 75  ? -92.735  19.006  266.180 1.00 34.56  ? 75  ASP B CA  1 
ATOM   4633 C  C   . ASP B 1 75  ? -93.571  20.246  265.877 1.00 37.64  ? 75  ASP B C   1 
ATOM   4634 O  O   . ASP B 1 75  ? -93.041  21.358  265.808 1.00 39.42  ? 75  ASP B O   1 
ATOM   4635 C  CB  . ASP B 1 75  ? -91.282  19.242  265.756 1.00 44.60  ? 75  ASP B CB  1 
ATOM   4636 C  CG  . ASP B 1 75  ? -90.409  18.024  265.956 1.00 58.19  ? 75  ASP B CG  1 
ATOM   4637 O  OD1 . ASP B 1 75  ? -90.561  17.350  266.995 1.00 61.25  ? 75  ASP B OD1 1 
ATOM   4638 O  OD2 . ASP B 1 75  ? -89.575  17.738  265.071 1.00 48.12  ? 75  ASP B OD2 1 
ATOM   4639 N  N   . GLU B 1 76  ? -94.879  20.057  265.687 1.00 36.94  ? 76  GLU B N   1 
ATOM   4640 C  CA  . GLU B 1 76  ? -95.785  21.111  265.226 1.00 37.50  ? 76  GLU B CA  1 
ATOM   4641 C  C   . GLU B 1 76  ? -95.379  21.647  263.854 1.00 36.69  ? 76  GLU B C   1 
ATOM   4642 O  O   . GLU B 1 76  ? -95.565  22.829  263.560 1.00 44.61  ? 76  GLU B O   1 
ATOM   4643 C  CB  . GLU B 1 76  ? -95.879  22.260  266.237 1.00 39.25  ? 76  GLU B CB  1 
ATOM   4644 C  CG  . GLU B 1 76  ? -96.429  21.867  267.598 1.00 48.30  ? 76  GLU B CG  1 
ATOM   4645 C  CD  . GLU B 1 76  ? -97.943  21.795  267.619 1.00 40.07  ? 76  GLU B CD  1 
ATOM   4646 O  OE1 . GLU B 1 76  ? -98.581  22.353  266.701 1.00 46.39  ? 76  GLU B OE1 1 
ATOM   4647 O  OE2 . GLU B 1 76  ? -98.496  21.189  268.560 1.00 39.95  ? 76  GLU B OE2 1 
ATOM   4648 N  N   . GLN B 1 77  ? -94.825  20.785  263.000 1.00 36.94  ? 77  GLN B N   1 
ATOM   4649 C  CA  . GLN B 1 77  ? -94.431  21.169  261.652 1.00 36.76  ? 77  GLN B CA  1 
ATOM   4650 C  C   . GLN B 1 77  ? -94.978  20.160  260.651 1.00 34.79  ? 77  GLN B C   1 
ATOM   4651 O  O   . GLN B 1 77  ? -95.107  18.969  260.949 1.00 35.41  ? 77  GLN B O   1 
ATOM   4652 C  CB  . GLN B 1 77  ? -92.899  21.285  261.521 1.00 44.57  ? 77  GLN B CB  1 
ATOM   4653 C  CG  . GLN B 1 77  ? -92.211  20.096  260.866 1.00 48.64  ? 77  GLN B CG  1 
ATOM   4654 C  CD  . GLN B 1 77  ? -90.707  20.271  260.771 1.00 68.74  ? 77  GLN B CD  1 
ATOM   4655 O  OE1 . GLN B 1 77  ? -90.196  21.390  260.827 1.00 55.72  ? 77  GLN B OE1 1 
ATOM   4656 N  NE2 . GLN B 1 77  ? -89.990  19.162  260.629 1.00 73.38  ? 77  GLN B NE2 1 
ATOM   4657 N  N   . GLN B 1 78  ? -95.304  20.654  259.459 1.00 34.46  ? 78  GLN B N   1 
ATOM   4658 C  CA  . GLN B 1 78  ? -95.917  19.822  258.431 1.00 37.85  ? 78  GLN B CA  1 
ATOM   4659 C  C   . GLN B 1 78  ? -94.926  18.785  257.917 1.00 33.51  ? 78  GLN B C   1 
ATOM   4660 O  O   . GLN B 1 78  ? -93.778  19.112  257.601 1.00 38.27  ? 78  GLN B O   1 
ATOM   4661 C  CB  . GLN B 1 78  ? -96.411  20.693  257.278 1.00 37.56  ? 78  GLN B CB  1 
ATOM   4662 C  CG  . GLN B 1 78  ? -97.503  20.062  256.434 1.00 34.81  ? 78  GLN B CG  1 
ATOM   4663 C  CD  . GLN B 1 78  ? -97.677  20.760  255.099 1.00 33.51  ? 78  GLN B CD  1 
ATOM   4664 O  OE1 . GLN B 1 78  ? -96.956  20.481  254.143 1.00 45.77  ? 78  GLN B OE1 1 
ATOM   4665 N  NE2 . GLN B 1 78  ? -98.631  21.679  255.032 1.00 36.55  ? 78  GLN B NE2 1 
ATOM   4666 N  N   . VAL B 1 79  ? -95.370  17.530  257.832 1.00 30.45  ? 79  VAL B N   1 
ATOM   4667 C  CA  . VAL B 1 79  ? -94.522  16.445  257.349 1.00 31.71  ? 79  VAL B CA  1 
ATOM   4668 C  C   . VAL B 1 79  ? -95.283  15.583  256.348 1.00 36.09  ? 79  VAL B C   1 
ATOM   4669 O  O   . VAL B 1 79  ? -94.681  14.786  255.619 1.00 52.48  ? 79  VAL B O   1 
ATOM   4670 C  CB  . VAL B 1 79  ? -93.991  15.584  258.511 1.00 30.96  ? 79  VAL B CB  1 
ATOM   4671 C  CG1 . VAL B 1 79  ? -93.189  16.430  259.487 1.00 36.17  ? 79  VAL B CG1 1 
ATOM   4672 C  CG2 . VAL B 1 79  ? -95.138  14.884  259.222 1.00 41.35  ? 79  VAL B CG2 1 
ATOM   4673 N  N   . TRP B 1 80  ? -96.604  15.731  256.304 1.00 32.61  ? 80  TRP B N   1 
ATOM   4674 C  CA  . TRP B 1 80  ? -97.429  14.919  255.419 1.00 35.01  ? 80  TRP B CA  1 
ATOM   4675 C  C   . TRP B 1 80  ? -98.760  15.623  255.208 1.00 41.17  ? 80  TRP B C   1 
ATOM   4676 O  O   . TRP B 1 80  ? -99.233  16.352  256.084 1.00 40.38  ? 80  TRP B O   1 
ATOM   4677 C  CB  . TRP B 1 80  ? -97.650  13.515  255.994 1.00 36.25  ? 80  TRP B CB  1 
ATOM   4678 C  CG  . TRP B 1 80  ? -98.358  12.569  255.068 1.00 42.94  ? 80  TRP B CG  1 
ATOM   4679 C  CD1 . TRP B 1 80  ? -97.783  11.728  254.160 1.00 56.81  ? 80  TRP B CD1 1 
ATOM   4680 C  CD2 . TRP B 1 80  ? -99.773  12.360  254.966 1.00 36.77  ? 80  TRP B CD2 1 
ATOM   4681 N  NE1 . TRP B 1 80  ? -98.750  11.012  253.498 1.00 43.29  ? 80  TRP B NE1 1 
ATOM   4682 C  CE2 . TRP B 1 80  ? -99.980  11.382  253.973 1.00 39.91  ? 80  TRP B CE2 1 
ATOM   4683 C  CE3 . TRP B 1 80  ? -100.884 12.908  255.615 1.00 35.12  ? 80  TRP B CE3 1 
ATOM   4684 C  CZ2 . TRP B 1 80  ? -101.251 10.939  253.615 1.00 44.58  ? 80  TRP B CZ2 1 
ATOM   4685 C  CZ3 . TRP B 1 80  ? -102.145 12.467  255.258 1.00 36.55  ? 80  TRP B CZ3 1 
ATOM   4686 C  CH2 . TRP B 1 80  ? -102.318 11.493  254.267 1.00 39.98  ? 80  TRP B CH2 1 
ATOM   4687 N  N   . LYS B 1 81  ? -99.359  15.400  254.039 1.00 33.67  ? 81  LYS B N   1 
ATOM   4688 C  CA  . LYS B 1 81  ? -100.657 15.988  253.749 1.00 34.05  ? 81  LYS B CA  1 
ATOM   4689 C  C   . LYS B 1 81  ? -101.394 15.137  252.726 1.00 35.75  ? 81  LYS B C   1 
ATOM   4690 O  O   . LYS B 1 81  ? -100.789 14.406  251.938 1.00 40.80  ? 81  LYS B O   1 
ATOM   4691 C  CB  . LYS B 1 81  ? -100.527 17.434  253.255 1.00 39.71  ? 81  LYS B CB  1 
ATOM   4692 C  CG  . LYS B 1 81  ? -99.968  17.603  251.856 1.00 43.29  ? 81  LYS B CG  1 
ATOM   4693 C  CD  . LYS B 1 81  ? -100.399 18.945  251.281 1.00 65.17  ? 81  LYS B CD  1 
ATOM   4694 C  CE  . LYS B 1 81  ? -99.827  19.178  249.895 1.00 62.31  ? 81  LYS B CE  1 
ATOM   4695 N  NZ  . LYS B 1 81  ? -98.353  19.381  249.941 1.00 49.30  ? 81  LYS B NZ  1 
ATOM   4696 N  N   . GLY B 1 82  ? -102.718 15.248  252.755 1.00 37.45  ? 82  GLY B N   1 
ATOM   4697 C  CA  . GLY B 1 82  ? -103.561 14.487  251.854 1.00 42.14  ? 82  GLY B CA  1 
ATOM   4698 C  C   . GLY B 1 82  ? -105.017 14.662  252.235 1.00 41.10  ? 82  GLY B C   1 
ATOM   4699 O  O   . GLY B 1 82  ? -105.366 15.576  252.982 1.00 44.18  ? 82  GLY B O   1 
ATOM   4700 N  N   . ASP B 1 83  ? -105.856 13.774  251.713 1.00 41.91  ? 83  ASP B N   1 
ATOM   4701 C  CA  . ASP B 1 83  ? -107.279 13.819  252.016 1.00 46.50  ? 83  ASP B CA  1 
ATOM   4702 C  C   . ASP B 1 83  ? -107.554 13.091  253.324 1.00 48.55  ? 83  ASP B C   1 
ATOM   4703 O  O   . ASP B 1 83  ? -106.932 12.068  253.627 1.00 55.39  ? 83  ASP B O   1 
ATOM   4704 C  CB  . ASP B 1 83  ? -108.090 13.190  250.881 1.00 52.37  ? 83  ASP B CB  1 
ATOM   4705 C  CG  . ASP B 1 83  ? -109.591 13.408  251.030 1.00 67.05  ? 83  ASP B CG  1 
ATOM   4706 O  OD1 . ASP B 1 83  ? -110.087 13.528  252.172 1.00 70.56  ? 83  ASP B OD1 1 
ATOM   4707 O  OD2 . ASP B 1 83  ? -110.282 13.461  249.992 1.00 93.72  ? 83  ASP B OD2 1 
ATOM   4708 N  N   . ALA B 1 84  ? -108.491 13.629  254.104 1.00 44.19  ? 84  ALA B N   1 
ATOM   4709 C  CA  . ALA B 1 84  ? -108.941 12.973  255.323 1.00 45.31  ? 84  ALA B CA  1 
ATOM   4710 C  C   . ALA B 1 84  ? -109.896 11.821  255.048 1.00 43.69  ? 84  ALA B C   1 
ATOM   4711 O  O   . ALA B 1 84  ? -110.300 11.134  255.993 1.00 44.30  ? 84  ALA B O   1 
ATOM   4712 C  CB  . ALA B 1 84  ? -109.608 13.986  256.256 1.00 42.10  ? 84  ALA B CB  1 
ATOM   4713 N  N   . GLU B 1 85  ? -110.271 11.605  253.784 1.00 47.66  ? 85  GLU B N   1 
ATOM   4714 C  CA  . GLU B 1 85  ? -111.085 10.446  253.431 1.00 56.36  ? 85  GLU B CA  1 
ATOM   4715 C  C   . GLU B 1 85  ? -110.394 9.149   253.827 1.00 58.11  ? 85  GLU B C   1 
ATOM   4716 O  O   . GLU B 1 85  ? -111.033 8.228   254.351 1.00 69.65  ? 85  GLU B O   1 
ATOM   4717 C  CB  . GLU B 1 85  ? -111.379 10.457  251.930 1.00 59.35  ? 85  GLU B CB  1 
ATOM   4718 C  CG  . GLU B 1 85  ? -111.432 9.077   251.293 1.00 60.46  ? 85  GLU B CG  1 
ATOM   4719 C  CD  . GLU B 1 85  ? -111.327 9.126   249.783 1.00 72.49  ? 85  GLU B CD  1 
ATOM   4720 O  OE1 . GLU B 1 85  ? -111.116 10.228  249.236 1.00 80.42  ? 85  GLU B OE1 1 
ATOM   4721 O  OE2 . GLU B 1 85  ? -111.448 8.060   249.143 1.00 63.81  ? 85  GLU B OE2 1 
ATOM   4722 N  N   . SER B 1 86  ? -109.084 9.063   253.593 1.00 52.36  ? 86  SER B N   1 
ATOM   4723 C  CA  . SER B 1 86  ? -108.357 7.834   253.887 1.00 50.43  ? 86  SER B CA  1 
ATOM   4724 C  C   . SER B 1 86  ? -108.244 7.586   255.384 1.00 45.71  ? 86  SER B C   1 
ATOM   4725 O  O   . SER B 1 86  ? -108.165 6.428   255.810 1.00 47.15  ? 86  SER B O   1 
ATOM   4726 C  CB  . SER B 1 86  ? -106.967 7.886   253.254 1.00 58.30  ? 86  SER B CB  1 
ATOM   4727 O  OG  . SER B 1 86  ? -106.242 9.013   253.717 1.00 65.33  ? 86  SER B OG  1 
ATOM   4728 N  N   . LYS B 1 87  ? -108.238 8.650   256.193 1.00 42.43  ? 87  LYS B N   1 
ATOM   4729 C  CA  . LYS B 1 87  ? -107.981 8.545   257.632 1.00 40.81  ? 87  LYS B CA  1 
ATOM   4730 C  C   . LYS B 1 87  ? -106.689 7.779   257.899 1.00 45.44  ? 87  LYS B C   1 
ATOM   4731 O  O   . LYS B 1 87  ? -106.556 7.080   258.906 1.00 51.52  ? 87  LYS B O   1 
ATOM   4732 C  CB  . LYS B 1 87  ? -109.158 7.894   258.364 1.00 41.35  ? 87  LYS B CB  1 
ATOM   4733 C  CG  . LYS B 1 87  ? -110.482 8.622   258.198 1.00 43.34  ? 87  LYS B CG  1 
ATOM   4734 C  CD  . LYS B 1 87  ? -111.592 7.918   258.965 1.00 48.99  ? 87  LYS B CD  1 
ATOM   4735 C  CE  . LYS B 1 87  ? -112.914 8.655   258.831 1.00 58.21  ? 87  LYS B CE  1 
ATOM   4736 N  NZ  . LYS B 1 87  ? -113.996 8.013   259.629 1.00 57.49  ? 87  LYS B NZ  1 
ATOM   4737 N  N   . ARG B 1 88  ? -105.729 7.912   256.987 1.00 41.62  ? 88  ARG B N   1 
ATOM   4738 C  CA  . ARG B 1 88  ? -104.507 7.125   256.993 1.00 40.18  ? 88  ARG B CA  1 
ATOM   4739 C  C   . ARG B 1 88  ? -103.348 8.004   256.552 1.00 39.13  ? 88  ARG B C   1 
ATOM   4740 O  O   . ARG B 1 88  ? -103.511 8.867   255.685 1.00 56.26  ? 88  ARG B O   1 
ATOM   4741 C  CB  . ARG B 1 88  ? -104.632 5.911   256.061 1.00 48.64  ? 88  ARG B CB  1 
ATOM   4742 C  CG  . ARG B 1 88  ? -103.372 5.072   255.932 1.00 54.97  ? 88  ARG B CG  1 
ATOM   4743 C  CD  . ARG B 1 88  ? -103.558 3.957   254.916 1.00 87.49  ? 88  ARG B CD  1 
ATOM   4744 N  NE  . ARG B 1 88  ? -103.757 4.478   253.566 1.00 82.54  ? 88  ARG B NE  1 
ATOM   4745 C  CZ  . ARG B 1 88  ? -102.774 4.739   252.711 1.00 73.03  ? 88  ARG B CZ  1 
ATOM   4746 N  NH1 . ARG B 1 88  ? -101.512 4.531   253.063 1.00 76.36  ? 88  ARG B NH1 1 
ATOM   4747 N  NH2 . ARG B 1 88  ? -103.050 5.210   251.503 1.00 64.96  ? 88  ARG B NH2 1 
ATOM   4748 N  N   . ALA B 1 89  ? -102.182 7.783   257.152 1.00 35.83  ? 89  ALA B N   1 
ATOM   4749 C  CA  . ALA B 1 89  ? -100.989 8.526   256.782 1.00 32.63  ? 89  ALA B CA  1 
ATOM   4750 C  C   . ALA B 1 89  ? -99.764  7.664   257.039 1.00 30.46  ? 89  ALA B C   1 
ATOM   4751 O  O   . ALA B 1 89  ? -99.674  6.989   258.068 1.00 29.76  ? 89  ALA B O   1 
ATOM   4752 C  CB  . ALA B 1 89  ? -100.886 9.843   257.558 1.00 35.48  ? 89  ALA B CB  1 
ATOM   4753 N  N   . THR B 1 90  ? -98.828  7.689   256.092 1.00 29.12  ? 90  THR B N   1 
ATOM   4754 C  CA  . THR B 1 90  ? -97.566  6.968   256.205 1.00 25.87  ? 90  THR B CA  1 
ATOM   4755 C  C   . THR B 1 90  ? -96.435  7.956   255.972 1.00 28.75  ? 90  THR B C   1 
ATOM   4756 O  O   . THR B 1 90  ? -96.311  8.510   254.875 1.00 28.28  ? 90  THR B O   1 
ATOM   4757 C  CB  . THR B 1 90  ? -97.491  5.816   255.200 1.00 27.51  ? 90  THR B CB  1 
ATOM   4758 O  OG1 . THR B 1 90  ? -98.648  4.982   255.338 1.00 37.34  ? 90  THR B OG1 1 
ATOM   4759 C  CG2 . THR B 1 90  ? -96.242  4.983   255.441 1.00 34.16  ? 90  THR B CG2 1 
ATOM   4760 N  N   . ILE B 1 91  ? -95.617  8.177   256.997 1.00 29.53  ? 91  ILE B N   1 
ATOM   4761 C  CA  . ILE B 1 91  ? -94.535  9.154   256.950 1.00 27.08  ? 91  ILE B CA  1 
ATOM   4762 C  C   . ILE B 1 91  ? -93.209  8.414   257.034 1.00 29.14  ? 91  ILE B C   1 
ATOM   4763 O  O   . ILE B 1 91  ? -93.025  7.551   257.901 1.00 27.38  ? 91  ILE B O   1 
ATOM   4764 C  CB  . ILE B 1 91  ? -94.655  10.193  258.078 1.00 27.88  ? 91  ILE B CB  1 
ATOM   4765 C  CG1 . ILE B 1 91  ? -96.033  10.858  258.059 1.00 28.90  ? 91  ILE B CG1 1 
ATOM   4766 C  CG2 . ILE B 1 91  ? -93.568  11.244  257.941 1.00 31.73  ? 91  ILE B CG2 1 
ATOM   4767 C  CD1 . ILE B 1 91  ? -97.032  10.241  259.017 1.00 29.01  ? 91  ILE B CD1 1 
ATOM   4768 N  N   . LYS B 1 92  ? -92.289  8.756   256.138 1.00 29.46  ? 92  LYS B N   1 
ATOM   4769 C  CA  . LYS B 1 92  ? -90.967  8.146   256.096 1.00 26.31  ? 92  LYS B CA  1 
ATOM   4770 C  C   . LYS B 1 92  ? -90.025  8.918   257.013 1.00 25.22  ? 92  LYS B C   1 
ATOM   4771 O  O   . LYS B 1 92  ? -89.862  10.133  256.861 1.00 34.92  ? 92  LYS B O   1 
ATOM   4772 C  CB  . LYS B 1 92  ? -90.436  8.132   254.664 1.00 25.95  ? 92  LYS B CB  1 
ATOM   4773 C  CG  . LYS B 1 92  ? -89.029  7.590   254.521 1.00 30.14  ? 92  LYS B CG  1 
ATOM   4774 C  CD  . LYS B 1 92  ? -88.579  7.622   253.070 1.00 34.58  ? 92  LYS B CD  1 
ATOM   4775 C  CE  . LYS B 1 92  ? -88.376  9.049   252.588 1.00 29.84  ? 92  LYS B CE  1 
ATOM   4776 N  NZ  . LYS B 1 92  ? -87.905  9.096   251.177 1.00 29.65  ? 92  LYS B NZ  1 
ATOM   4777 N  N   . VAL B 1 93  ? -89.409  8.214   257.959 1.00 24.78  ? 93  VAL B N   1 
ATOM   4778 C  CA  . VAL B 1 93  ? -88.476  8.805   258.910 1.00 25.15  ? 93  VAL B CA  1 
ATOM   4779 C  C   . VAL B 1 93  ? -87.116  8.150   258.714 1.00 30.98  ? 93  VAL B C   1 
ATOM   4780 O  O   . VAL B 1 93  ? -87.023  6.920   258.619 1.00 42.22  ? 93  VAL B O   1 
ATOM   4781 C  CB  . VAL B 1 93  ? -88.964  8.642   260.362 1.00 24.24  ? 93  VAL B CB  1 
ATOM   4782 C  CG1 . VAL B 1 93  ? -87.908  9.130   261.340 1.00 24.51  ? 93  VAL B CG1 1 
ATOM   4783 C  CG2 . VAL B 1 93  ? -90.268  9.395   260.564 1.00 26.51  ? 93  VAL B CG2 1 
ATOM   4784 N  N   . LEU B 1 94  ? -86.067  8.970   258.652 1.00 25.17  ? 94  LEU B N   1 
ATOM   4785 C  CA  . LEU B 1 94  ? -84.717  8.490   258.388 1.00 22.70  ? 94  LEU B CA  1 
ATOM   4786 C  C   . LEU B 1 94  ? -83.797  8.532   259.597 1.00 23.68  ? 94  LEU B C   1 
ATOM   4787 O  O   . LEU B 1 94  ? -82.842  7.756   259.651 1.00 24.43  ? 94  LEU B O   1 
ATOM   4788 C  CB  . LEU B 1 94  ? -84.074  9.306   257.258 1.00 24.95  ? 94  LEU B CB  1 
ATOM   4789 C  CG  . LEU B 1 94  ? -84.239  8.834   255.810 1.00 30.23  ? 94  LEU B CG  1 
ATOM   4790 C  CD1 . LEU B 1 94  ? -85.693  8.548   255.476 1.00 26.71  ? 94  LEU B CD1 1 
ATOM   4791 C  CD2 . LEU B 1 94  ? -83.662  9.862   254.846 1.00 23.80  ? 94  LEU B CD2 1 
ATOM   4792 N  N   . VAL B 1 95  ? -84.050  9.415   260.560 1.00 28.79  ? 95  VAL B N   1 
ATOM   4793 C  CA  . VAL B 1 95  ? -83.149  9.622   261.686 1.00 23.36  ? 95  VAL B CA  1 
ATOM   4794 C  C   . VAL B 1 95  ? -83.874  9.278   262.980 1.00 23.21  ? 95  VAL B C   1 
ATOM   4795 O  O   . VAL B 1 95  ? -85.080  9.502   263.118 1.00 23.93  ? 95  VAL B O   1 
ATOM   4796 C  CB  . VAL B 1 95  ? -82.615  11.071  261.728 1.00 28.41  ? 95  VAL B CB  1 
ATOM   4797 C  CG1 . VAL B 1 95  ? -81.464  11.193  262.717 1.00 29.56  ? 95  VAL B CG1 1 
ATOM   4798 C  CG2 . VAL B 1 95  ? -82.184  11.519  260.340 1.00 56.52  ? 95  VAL B CG2 1 
ATOM   4799 N  N   . SER B 1 96  ? -83.123  8.729   263.932 1.00 23.87  ? 96  SER B N   1 
ATOM   4800 C  CA  . SER B 1 96  ? -83.676  8.402   265.236 1.00 21.67  ? 96  SER B CA  1 
ATOM   4801 C  C   . SER B 1 96  ? -84.043  9.671   266.000 1.00 25.59  ? 96  SER B C   1 
ATOM   4802 O  O   . SER B 1 96  ? -83.550  10.767  265.717 1.00 32.42  ? 96  SER B O   1 
ATOM   4803 C  CB  . SER B 1 96  ? -82.680  7.575   266.049 1.00 19.15  ? 96  SER B CB  1 
ATOM   4804 O  OG  . SER B 1 96  ? -81.414  8.209   266.096 1.00 17.17  ? 96  SER B OG  1 
ATOM   4805 N  N   . GLY B 1 97  ? -84.923  9.510   266.985 1.00 25.09  ? 97  GLY B N   1 
ATOM   4806 C  CA  . GLY B 1 97  ? -85.350  10.626  267.806 1.00 24.32  ? 97  GLY B CA  1 
ATOM   4807 C  C   . GLY B 1 97  ? -86.810  10.561  268.203 1.00 24.86  ? 97  GLY B C   1 
ATOM   4808 O  O   . GLY B 1 97  ? -87.576  9.762   267.658 1.00 22.69  ? 97  GLY B O   1 
ATOM   4809 N  N   . GLN B 1 98  ? -87.205  11.401  269.154 1.00 25.48  ? 98  GLN B N   1 
ATOM   4810 C  CA  . GLN B 1 98  ? -88.578  11.469  269.628 1.00 26.11  ? 98  GLN B CA  1 
ATOM   4811 C  C   . GLN B 1 98  ? -89.226  12.768  269.167 1.00 26.55  ? 98  GLN B C   1 
ATOM   4812 O  O   . GLN B 1 98  ? -88.552  13.786  268.983 1.00 25.69  ? 98  GLN B O   1 
ATOM   4813 C  CB  . GLN B 1 98  ? -88.638  11.371  271.154 1.00 27.94  ? 98  GLN B CB  1 
ATOM   4814 C  CG  . GLN B 1 98  ? -88.119  10.061  271.715 1.00 40.21  ? 98  GLN B CG  1 
ATOM   4815 C  CD  . GLN B 1 98  ? -88.195  10.009  273.227 1.00 54.31  ? 98  GLN B CD  1 
ATOM   4816 O  OE1 . GLN B 1 98  ? -88.285  11.042  273.891 1.00 33.36  ? 98  GLN B OE1 1 
ATOM   4817 N  NE2 . GLN B 1 98  ? -88.159  8.803   273.781 1.00 67.50  ? 98  GLN B NE2 1 
ATOM   4818 N  N   . PHE B 1 99  ? -90.544  12.723  268.985 1.00 26.44  ? 99  PHE B N   1 
ATOM   4819 C  CA  . PHE B 1 99  ? -91.293  13.895  268.553 1.00 23.28  ? 99  PHE B CA  1 
ATOM   4820 C  C   . PHE B 1 99  ? -92.775  13.658  268.800 1.00 23.38  ? 99  PHE B C   1 
ATOM   4821 O  O   . PHE B 1 99  ? -93.235  12.517  268.892 1.00 24.55  ? 99  PHE B O   1 
ATOM   4822 C  CB  . PHE B 1 99  ? -91.034  14.218  267.076 1.00 24.60  ? 99  PHE B CB  1 
ATOM   4823 C  CG  . PHE B 1 99  ? -91.164  13.034  266.161 1.00 23.75  ? 99  PHE B CG  1 
ATOM   4824 C  CD1 . PHE B 1 99  ? -92.395  12.675  265.638 1.00 25.40  ? 99  PHE B CD1 1 
ATOM   4825 C  CD2 . PHE B 1 99  ? -90.052  12.282  265.822 1.00 25.17  ? 99  PHE B CD2 1 
ATOM   4826 C  CE1 . PHE B 1 99  ? -92.515  11.588  264.795 1.00 26.19  ? 99  PHE B CE1 1 
ATOM   4827 C  CE2 . PHE B 1 99  ? -90.166  11.193  264.981 1.00 41.06  ? 99  PHE B CE2 1 
ATOM   4828 C  CZ  . PHE B 1 99  ? -91.399  10.846  264.467 1.00 29.77  ? 99  PHE B CZ  1 
ATOM   4829 N  N   . ASN B 1 100 ? -93.516  14.759  268.907 1.00 25.10  ? 100 ASN B N   1 
ATOM   4830 C  CA  . ASN B 1 100 ? -94.960  14.710  269.089 1.00 21.84  ? 100 ASN B CA  1 
ATOM   4831 C  C   . ASN B 1 100 ? -95.646  14.749  267.730 1.00 22.35  ? 100 ASN B C   1 
ATOM   4832 O  O   . ASN B 1 100 ? -95.366  15.630  266.911 1.00 34.58  ? 100 ASN B O   1 
ATOM   4833 C  CB  . ASN B 1 100 ? -95.439  15.875  269.956 1.00 18.61  ? 100 ASN B CB  1 
ATOM   4834 C  CG  . ASN B 1 100 ? -94.803  15.878  271.331 1.00 20.92  ? 100 ASN B CG  1 
ATOM   4835 O  OD1 . ASN B 1 100 ? -94.462  14.827  271.872 1.00 28.33  ? 100 ASN B OD1 1 
ATOM   4836 N  ND2 . ASN B 1 100 ? -94.641  17.064  271.905 1.00 16.08  ? 100 ASN B ND2 1 
ATOM   4837 N  N   . MET B 1 101 ? -96.542  13.795  267.495 1.00 21.57  ? 101 MET B N   1 
ATOM   4838 C  CA  . MET B 1 101 ? -97.259  13.681  266.233 1.00 20.46  ? 101 MET B CA  1 
ATOM   4839 C  C   . MET B 1 101 ? -98.712  14.089  266.429 1.00 21.51  ? 101 MET B C   1 
ATOM   4840 O  O   . MET B 1 101 ? -99.364  13.643  267.379 1.00 22.02  ? 101 MET B O   1 
ATOM   4841 C  CB  . MET B 1 101 ? -97.178  12.257  265.683 1.00 18.77  ? 101 MET B CB  1 
ATOM   4842 C  CG  . MET B 1 101 ? -97.935  12.058  264.384 1.00 18.00  ? 101 MET B CG  1 
ATOM   4843 S  SD  . MET B 1 101 ? -97.766  10.383  263.750 1.00 5.00   ? 101 MET B SD  1 
ATOM   4844 C  CE  . MET B 1 101 ? -98.345  9.435   265.154 1.00 18.67  ? 101 MET B CE  1 
ATOM   4845 N  N   . ARG B 1 102 ? -99.213  14.934  265.530 1.00 22.41  ? 102 ARG B N   1 
ATOM   4846 C  CA  . ARG B 1 102 ? -100.577 15.434  265.605 1.00 23.51  ? 102 ARG B CA  1 
ATOM   4847 C  C   . ARG B 1 102 ? -101.194 15.412  264.215 1.00 26.12  ? 102 ARG B C   1 
ATOM   4848 O  O   . ARG B 1 102 ? -100.502 15.587  263.209 1.00 25.04  ? 102 ARG B O   1 
ATOM   4849 C  CB  . ARG B 1 102 ? -100.624 16.859  266.180 1.00 27.02  ? 102 ARG B CB  1 
ATOM   4850 C  CG  . ARG B 1 102 ? -100.034 16.973  267.575 1.00 29.01  ? 102 ARG B CG  1 
ATOM   4851 C  CD  . ARG B 1 102 ? -99.947  18.412  268.056 1.00 35.50  ? 102 ARG B CD  1 
ATOM   4852 N  NE  . ARG B 1 102 ? -101.258 19.014  268.282 1.00 52.43  ? 102 ARG B NE  1 
ATOM   4853 C  CZ  . ARG B 1 102 ? -101.501 19.940  269.205 1.00 47.54  ? 102 ARG B CZ  1 
ATOM   4854 N  NH1 . ARG B 1 102 ? -100.520 20.369  269.987 1.00 57.49  ? 102 ARG B NH1 1 
ATOM   4855 N  NH2 . ARG B 1 102 ? -102.722 20.437  269.350 1.00 41.67  ? 102 ARG B NH2 1 
ATOM   4856 N  N   . VAL B 1 103 ? -102.505 15.192  264.169 1.00 28.50  ? 103 VAL B N   1 
ATOM   4857 C  CA  . VAL B 1 103 ? -103.265 15.197  262.924 1.00 25.29  ? 103 VAL B CA  1 
ATOM   4858 C  C   . VAL B 1 103 ? -104.002 16.523  262.811 1.00 25.45  ? 103 VAL B C   1 
ATOM   4859 O  O   . VAL B 1 103 ? -104.586 17.010  263.787 1.00 28.97  ? 103 VAL B O   1 
ATOM   4860 C  CB  . VAL B 1 103 ? -104.242 14.007  262.860 1.00 26.22  ? 103 VAL B CB  1 
ATOM   4861 C  CG1 . VAL B 1 103 ? -105.043 14.042  261.567 1.00 30.53  ? 103 VAL B CG1 1 
ATOM   4862 C  CG2 . VAL B 1 103 ? -103.483 12.698  262.976 1.00 31.34  ? 103 VAL B CG2 1 
ATOM   4863 N  N   . LYS B 1 104 ? -103.972 17.110  261.617 1.00 26.94  ? 104 LYS B N   1 
ATOM   4864 C  CA  . LYS B 1 104 ? -104.529 18.435  261.363 1.00 30.39  ? 104 LYS B CA  1 
ATOM   4865 C  C   . LYS B 1 104 ? -105.621 18.313  260.309 1.00 32.07  ? 104 LYS B C   1 
ATOM   4866 O  O   . LYS B 1 104 ? -105.334 18.030  259.142 1.00 33.97  ? 104 LYS B O   1 
ATOM   4867 C  CB  . LYS B 1 104 ? -103.432 19.397  260.910 1.00 46.91  ? 104 LYS B CB  1 
ATOM   4868 C  CG  . LYS B 1 104 ? -103.883 20.827  260.667 1.00 45.17  ? 104 LYS B CG  1 
ATOM   4869 C  CD  . LYS B 1 104 ? -104.190 21.542  261.968 1.00 68.58  ? 104 LYS B CD  1 
ATOM   4870 C  CE  . LYS B 1 104 ? -103.796 23.009  261.892 1.00 63.42  ? 104 LYS B CE  1 
ATOM   4871 N  NZ  . LYS B 1 104 ? -104.309 23.668  260.660 1.00 66.59  ? 104 LYS B NZ  1 
ATOM   4872 N  N   . LEU B 1 105 ? -106.869 18.525  260.718 1.00 34.93  ? 105 LEU B N   1 
ATOM   4873 C  CA  . LEU B 1 105 ? -108.008 18.527  259.809 1.00 36.34  ? 105 LEU B CA  1 
ATOM   4874 C  C   . LEU B 1 105 ? -108.400 19.965  259.505 1.00 35.33  ? 105 LEU B C   1 
ATOM   4875 O  O   . LEU B 1 105 ? -108.611 20.759  260.427 1.00 35.73  ? 105 LEU B O   1 
ATOM   4876 C  CB  . LEU B 1 105 ? -109.196 17.779  260.414 1.00 37.49  ? 105 LEU B CB  1 
ATOM   4877 C  CG  . LEU B 1 105 ? -108.980 16.329  260.846 1.00 37.13  ? 105 LEU B CG  1 
ATOM   4878 C  CD1 . LEU B 1 105 ? -110.277 15.744  261.382 1.00 41.25  ? 105 LEU B CD1 1 
ATOM   4879 C  CD2 . LEU B 1 105 ? -108.449 15.496  259.692 1.00 64.09  ? 105 LEU B CD2 1 
ATOM   4880 N  N   . CYS B 1 106 ? -108.506 20.296  258.220 1.00 32.82  ? 106 CYS B N   1 
ATOM   4881 C  CA  . CYS B 1 106 ? -108.818 21.652  257.791 1.00 35.39  ? 106 CYS B CA  1 
ATOM   4882 C  C   . CYS B 1 106 ? -110.028 21.651  256.868 1.00 36.83  ? 106 CYS B C   1 
ATOM   4883 O  O   . CYS B 1 106 ? -110.267 20.695  256.126 1.00 39.61  ? 106 CYS B O   1 
ATOM   4884 C  CB  . CYS B 1 106 ? -107.629 22.304  257.074 1.00 32.64  ? 106 CYS B CB  1 
ATOM   4885 S  SG  . CYS B 1 106 ? -106.332 22.938  258.162 1.00 41.76  ? 106 CYS B SG  1 
ATOM   4886 N  N   . ASN B 1 107 ? -110.788 22.746  256.921 1.00 38.67  ? 107 ASN B N   1 
ATOM   4887 C  CA  . ASN B 1 107 ? -111.954 22.945  256.073 1.00 39.59  ? 107 ASN B CA  1 
ATOM   4888 C  C   . ASN B 1 107 ? -111.933 24.379  255.556 1.00 38.72  ? 107 ASN B C   1 
ATOM   4889 O  O   . ASN B 1 107 ? -110.990 25.136  255.806 1.00 42.95  ? 107 ASN B O   1 
ATOM   4890 C  CB  . ASN B 1 107 ? -113.250 22.636  256.833 1.00 42.42  ? 107 ASN B CB  1 
ATOM   4891 C  CG  . ASN B 1 107 ? -114.405 22.294  255.910 1.00 53.87  ? 107 ASN B CG  1 
ATOM   4892 O  OD1 . ASN B 1 107 ? -114.456 22.748  254.767 1.00 63.11  ? 107 ASN B OD1 1 
ATOM   4893 N  ND2 . ASN B 1 107 ? -115.338 21.488  256.402 1.00 48.51  ? 107 ASN B ND2 1 
ATOM   4894 N  N   . GLU B 1 108 ? -112.987 24.753  254.827 1.00 38.60  ? 108 GLU B N   1 
ATOM   4895 C  CA  . GLU B 1 108 ? -113.055 26.093  254.252 1.00 38.00  ? 108 GLU B CA  1 
ATOM   4896 C  C   . GLU B 1 108 ? -113.084 27.161  255.339 1.00 38.50  ? 108 GLU B C   1 
ATOM   4897 O  O   . GLU B 1 108 ? -112.487 28.233  255.182 1.00 37.26  ? 108 GLU B O   1 
ATOM   4898 C  CB  . GLU B 1 108 ? -114.281 26.207  253.342 1.00 47.37  ? 108 GLU B CB  1 
ATOM   4899 C  CG  . GLU B 1 108 ? -114.383 27.510  252.553 1.00 41.29  ? 108 GLU B CG  1 
ATOM   4900 C  CD  . GLU B 1 108 ? -115.007 28.640  253.351 1.00 49.67  ? 108 GLU B CD  1 
ATOM   4901 O  OE1 . GLU B 1 108 ? -115.955 28.374  254.120 1.00 40.14  ? 108 GLU B OE1 1 
ATOM   4902 O  OE2 . GLU B 1 108 ? -114.549 29.794  253.212 1.00 59.01  ? 108 GLU B OE2 1 
ATOM   4903 N  N   . ASP B 1 109 ? -113.771 26.890  256.447 1.00 43.40  ? 109 ASP B N   1 
ATOM   4904 C  CA  . ASP B 1 109 ? -113.840 27.844  257.547 1.00 47.16  ? 109 ASP B CA  1 
ATOM   4905 C  C   . ASP B 1 109 ? -112.523 27.858  258.313 1.00 49.49  ? 109 ASP B C   1 
ATOM   4906 O  O   . ASP B 1 109 ? -111.750 28.817  258.214 1.00 63.53  ? 109 ASP B O   1 
ATOM   4907 C  CB  . ASP B 1 109 ? -115.003 27.504  258.484 1.00 52.61  ? 109 ASP B CB  1 
ATOM   4908 C  CG  . ASP B 1 109 ? -115.392 28.666  259.384 1.00 59.30  ? 109 ASP B CG  1 
ATOM   4909 O  OD1 . ASP B 1 109 ? -114.522 29.504  259.702 1.00 119.37 ? 109 ASP B OD1 1 
ATOM   4910 O  OD2 . ASP B 1 109 ? -116.574 28.739  259.779 1.00 49.81  ? 109 ASP B OD2 1 
ATOM   4911 N  N   . GLY B 1 110 ? -112.262 26.802  259.077 1.00 50.31  ? 110 GLY B N   1 
ATOM   4912 C  CA  . GLY B 1 110 ? -111.045 26.717  259.859 1.00 61.67  ? 110 GLY B CA  1 
ATOM   4913 C  C   . GLY B 1 110 ? -110.499 25.308  259.955 1.00 49.83  ? 110 GLY B C   1 
ATOM   4914 O  O   . GLY B 1 110 ? -110.803 24.459  259.112 1.00 72.57  ? 110 GLY B O   1 
ATOM   4915 N  N   . CYS B 1 111 ? -109.694 25.044  260.982 1.00 36.13  ? 111 CYS B N   1 
ATOM   4916 C  CA  . CYS B 1 111 ? -109.076 23.742  261.168 1.00 34.95  ? 111 CYS B CA  1 
ATOM   4917 C  C   . CYS B 1 111 ? -109.225 23.291  262.613 1.00 33.29  ? 111 CYS B C   1 
ATOM   4918 O  O   . CYS B 1 111 ? -109.342 24.109  263.529 1.00 39.50  ? 111 CYS B O   1 
ATOM   4919 C  CB  . CYS B 1 111 ? -107.590 23.766  260.789 1.00 35.42  ? 111 CYS B CB  1 
ATOM   4920 S  SG  . CYS B 1 111 ? -107.227 24.463  259.161 1.00 34.02  ? 111 CYS B SG  1 
ATOM   4921 N  N   . SER B 1 112 ? -109.218 21.974  262.806 1.00 33.95  ? 112 SER B N   1 
ATOM   4922 C  CA  . SER B 1 112 ? -109.251 21.359  264.126 1.00 33.91  ? 112 SER B CA  1 
ATOM   4923 C  C   . SER B 1 112 ? -108.026 20.472  264.291 1.00 38.43  ? 112 SER B C   1 
ATOM   4924 O  O   . SER B 1 112 ? -107.611 19.790  263.348 1.00 38.61  ? 112 SER B O   1 
ATOM   4925 C  CB  . SER B 1 112 ? -110.528 20.539  264.329 1.00 38.04  ? 112 SER B CB  1 
ATOM   4926 O  OG  . SER B 1 112 ? -110.588 19.457  263.417 1.00 39.69  ? 112 SER B OG  1 
ATOM   4927 N  N   . VAL B 1 113 ? -107.449 20.481  265.490 1.00 37.64  ? 113 VAL B N   1 
ATOM   4928 C  CA  . VAL B 1 113 ? -106.189 19.802  265.763 1.00 36.87  ? 113 VAL B CA  1 
ATOM   4929 C  C   . VAL B 1 113 ? -106.431 18.698  266.782 1.00 43.40  ? 113 VAL B C   1 
ATOM   4930 O  O   . VAL B 1 113 ? -107.203 18.874  267.732 1.00 52.38  ? 113 VAL B O   1 
ATOM   4931 C  CB  . VAL B 1 113 ? -105.114 20.785  266.271 1.00 44.61  ? 113 VAL B CB  1 
ATOM   4932 C  CG1 . VAL B 1 113 ? -103.742 20.130  266.251 1.00 68.20  ? 113 VAL B CG1 1 
ATOM   4933 C  CG2 . VAL B 1 113 ? -105.122 22.060  265.441 1.00 57.93  ? 113 VAL B CG2 1 
ATOM   4934 N  N   . SER B 1 114 ? -105.763 17.564  266.585 1.00 36.63  ? 114 SER B N   1 
ATOM   4935 C  CA  . SER B 1 114 ? -105.901 16.420  267.472 1.00 32.63  ? 114 SER B CA  1 
ATOM   4936 C  C   . SER B 1 114 ? -104.973 16.558  268.676 1.00 30.95  ? 114 SER B C   1 
ATOM   4937 O  O   . SER B 1 114 ? -104.173 17.492  268.783 1.00 34.17  ? 114 SER B O   1 
ATOM   4938 C  CB  . SER B 1 114 ? -105.613 15.127  266.714 1.00 34.07  ? 114 SER B CB  1 
ATOM   4939 O  OG  . SER B 1 114 ? -104.261 15.074  266.297 1.00 30.55  ? 114 SER B OG  1 
ATOM   4940 N  N   . ASP B 1 115 ? -105.083 15.605  269.603 1.00 31.80  ? 115 ASP B N   1 
ATOM   4941 C  CA  . ASP B 1 115 ? -104.189 15.561  270.747 1.00 29.54  ? 115 ASP B CA  1 
ATOM   4942 C  C   . ASP B 1 115 ? -102.843 14.963  270.344 1.00 36.43  ? 115 ASP B C   1 
ATOM   4943 O  O   . ASP B 1 115 ? -102.781 14.068  269.497 1.00 29.15  ? 115 ASP B O   1 
ATOM   4944 C  CB  . ASP B 1 115 ? -104.803 14.740  271.876 1.00 23.87  ? 115 ASP B CB  1 
ATOM   4945 C  CG  . ASP B 1 115 ? -105.835 15.518  272.667 1.00 23.01  ? 115 ASP B CG  1 
ATOM   4946 O  OD1 . ASP B 1 115 ? -105.740 16.762  272.704 1.00 23.55  ? 115 ASP B OD1 1 
ATOM   4947 O  OD2 . ASP B 1 115 ? -106.741 14.886  273.249 1.00 30.01  ? 115 ASP B OD2 1 
ATOM   4948 N  N   . PRO B 1 116 ? -101.749 15.442  270.934 1.00 24.98  ? 116 PRO B N   1 
ATOM   4949 C  CA  . PRO B 1 116 ? -100.425 14.951  270.537 1.00 23.13  ? 116 PRO B CA  1 
ATOM   4950 C  C   . PRO B 1 116 ? -100.089 13.611  271.174 1.00 21.59  ? 116 PRO B C   1 
ATOM   4951 O  O   . PRO B 1 116 ? -100.404 13.352  272.338 1.00 21.06  ? 116 PRO B O   1 
ATOM   4952 C  CB  . PRO B 1 116 ? -99.483  16.051  271.040 1.00 23.61  ? 116 PRO B CB  1 
ATOM   4953 C  CG  . PRO B 1 116 ? -100.182 16.603  272.233 1.00 22.77  ? 116 PRO B CG  1 
ATOM   4954 C  CD  . PRO B 1 116 ? -101.659 16.535  271.920 1.00 28.73  ? 116 PRO B CD  1 
ATOM   4955 N  N   . VAL B 1 117 ? -99.435  12.757  270.390 1.00 20.59  ? 117 VAL B N   1 
ATOM   4956 C  CA  . VAL B 1 117 ? -98.916  11.482  270.867 1.00 19.12  ? 117 VAL B CA  1 
ATOM   4957 C  C   . VAL B 1 117 ? -97.411  11.471  270.648 1.00 22.21  ? 117 VAL B C   1 
ATOM   4958 O  O   . VAL B 1 117 ? -96.887  12.158  269.765 1.00 27.92  ? 117 VAL B O   1 
ATOM   4959 C  CB  . VAL B 1 117 ? -99.579  10.277  270.167 1.00 20.51  ? 117 VAL B CB  1 
ATOM   4960 C  CG1 . VAL B 1 117 ? -101.074 10.266  270.436 1.00 26.88  ? 117 VAL B CG1 1 
ATOM   4961 C  CG2 . VAL B 1 117 ? -99.299  10.311  268.674 1.00 22.55  ? 117 VAL B CG2 1 
ATOM   4962 N  N   . LEU B 1 118 ? -96.713  10.686  271.463 1.00 24.96  ? 118 LEU B N   1 
ATOM   4963 C  CA  . LEU B 1 118 ? -95.257  10.634  271.430 1.00 23.12  ? 118 LEU B CA  1 
ATOM   4964 C  C   . LEU B 1 118 ? -94.809  9.479   270.542 1.00 23.15  ? 118 LEU B C   1 
ATOM   4965 O  O   . LEU B 1 118 ? -95.159  8.321   270.795 1.00 23.19  ? 118 LEU B O   1 
ATOM   4966 C  CB  . LEU B 1 118 ? -94.691  10.478  272.840 1.00 25.45  ? 118 LEU B CB  1 
ATOM   4967 C  CG  . LEU B 1 118 ? -93.210  10.110  272.949 1.00 24.67  ? 118 LEU B CG  1 
ATOM   4968 C  CD1 . LEU B 1 118 ? -92.339  11.145  272.253 1.00 37.57  ? 118 LEU B CD1 1 
ATOM   4969 C  CD2 . LEU B 1 118 ? -92.806  9.955   274.409 1.00 23.42  ? 118 LEU B CD2 1 
ATOM   4970 N  N   . VAL B 1 119 ? -94.039  9.798   269.504 1.00 23.93  ? 119 VAL B N   1 
ATOM   4971 C  CA  . VAL B 1 119 ? -93.464  8.804   268.606 1.00 22.98  ? 119 VAL B CA  1 
ATOM   4972 C  C   . VAL B 1 119 ? -91.983  8.669   268.923 1.00 26.64  ? 119 VAL B C   1 
ATOM   4973 O  O   . VAL B 1 119 ? -91.297  9.666   269.180 1.00 40.52  ? 119 VAL B O   1 
ATOM   4974 C  CB  . VAL B 1 119 ? -93.679  9.192   267.131 1.00 20.02  ? 119 VAL B CB  1 
ATOM   4975 C  CG1 . VAL B 1 119 ? -93.171  8.094   266.206 1.00 22.03  ? 119 VAL B CG1 1 
ATOM   4976 C  CG2 . VAL B 1 119 ? -95.144  9.476   266.870 1.00 35.53  ? 119 VAL B CG2 1 
ATOM   4977 N  N   . LYS B 1 120 ? -91.487  7.434   268.914 1.00 27.19  ? 120 LYS B N   1 
ATOM   4978 C  CA  . LYS B 1 120 ? -90.080  7.151   269.167 1.00 25.25  ? 120 LYS B CA  1 
ATOM   4979 C  C   . LYS B 1 120 ? -89.512  6.380   267.986 1.00 23.36  ? 120 LYS B C   1 
ATOM   4980 O  O   . LYS B 1 120 ? -90.028  5.316   267.628 1.00 32.05  ? 120 LYS B O   1 
ATOM   4981 C  CB  . LYS B 1 120 ? -89.899  6.358   270.463 1.00 29.29  ? 120 LYS B CB  1 
ATOM   4982 C  CG  . LYS B 1 120 ? -90.714  6.882   271.628 1.00 31.46  ? 120 LYS B CG  1 
ATOM   4983 C  CD  . LYS B 1 120 ? -90.373  6.144   272.908 1.00 50.63  ? 120 LYS B CD  1 
ATOM   4984 C  CE  . LYS B 1 120 ? -91.476  6.300   273.936 1.00 48.55  ? 120 LYS B CE  1 
ATOM   4985 N  NZ  . LYS B 1 120 ? -92.739  5.644   273.494 1.00 37.63  ? 120 LYS B NZ  1 
ATOM   4986 N  N   . VAL B 1 121 ? -88.458  6.920   267.382 1.00 21.11  ? 121 VAL B N   1 
ATOM   4987 C  CA  . VAL B 1 121 ? -87.721  6.254   266.316 1.00 19.92  ? 121 VAL B CA  1 
ATOM   4988 C  C   . VAL B 1 121 ? -86.349  5.897   266.867 1.00 22.98  ? 121 VAL B C   1 
ATOM   4989 O  O   . VAL B 1 121 ? -85.623  6.772   267.357 1.00 24.61  ? 121 VAL B O   1 
ATOM   4990 C  CB  . VAL B 1 121 ? -87.608  7.135   265.064 1.00 21.30  ? 121 VAL B CB  1 
ATOM   4991 C  CG1 . VAL B 1 121 ? -86.875  6.392   263.961 1.00 34.29  ? 121 VAL B CG1 1 
ATOM   4992 C  CG2 . VAL B 1 121 ? -88.989  7.564   264.596 1.00 22.50  ? 121 VAL B CG2 1 
ATOM   4993 N  N   . ALA B 1 122 ? -85.996  4.619   266.796 1.00 22.94  ? 122 ALA B N   1 
ATOM   4994 C  CA  . ALA B 1 122 ? -84.789  4.108   267.421 1.00 20.90  ? 122 ALA B CA  1 
ATOM   4995 C  C   . ALA B 1 122 ? -83.726  3.784   266.381 1.00 21.33  ? 122 ALA B C   1 
ATOM   4996 O  O   . ALA B 1 122 ? -84.032  3.433   265.238 1.00 29.58  ? 122 ALA B O   1 
ATOM   4997 C  CB  . ALA B 1 122 ? -85.088  2.859   268.250 1.00 18.88  ? 122 ALA B CB  1 
ATOM   4998 N  N   . ASP B 1 123 ? -82.469  3.904   266.799 1.00 21.14  ? 123 ASP B N   1 
ATOM   4999 C  CA  . ASP B 1 123 ? -81.332  3.525   265.974 1.00 21.19  ? 123 ASP B CA  1 
ATOM   5000 C  C   . ASP B 1 123 ? -80.155  3.249   266.895 1.00 20.26  ? 123 ASP B C   1 
ATOM   5001 O  O   . ASP B 1 123 ? -80.131  3.686   268.048 1.00 20.50  ? 123 ASP B O   1 
ATOM   5002 C  CB  . ASP B 1 123 ? -80.986  4.609   264.948 1.00 21.57  ? 123 ASP B CB  1 
ATOM   5003 C  CG  . ASP B 1 123 ? -80.023  4.119   263.884 1.00 22.41  ? 123 ASP B CG  1 
ATOM   5004 O  OD1 . ASP B 1 123 ? -79.794  2.894   263.808 1.00 25.91  ? 123 ASP B OD1 1 
ATOM   5005 O  OD2 . ASP B 1 123 ? -79.498  4.958   263.123 1.00 26.88  ? 123 ASP B OD2 1 
ATOM   5006 N  N   . THR B 1 124 ? -79.174  2.517   266.369 1.00 18.76  ? 124 THR B N   1 
ATOM   5007 C  CA  . THR B 1 124 ? -78.034  2.105   267.179 1.00 18.72  ? 124 THR B CA  1 
ATOM   5008 C  C   . THR B 1 124 ? -77.063  3.239   267.479 1.00 20.07  ? 124 THR B C   1 
ATOM   5009 O  O   . THR B 1 124 ? -76.042  2.991   268.130 1.00 20.88  ? 124 THR B O   1 
ATOM   5010 C  CB  . THR B 1 124 ? -77.295  0.955   266.494 1.00 18.95  ? 124 THR B CB  1 
ATOM   5011 O  OG1 . THR B 1 124 ? -76.907  1.350   265.172 1.00 20.33  ? 124 THR B OG1 1 
ATOM   5012 C  CG2 . THR B 1 124 ? -78.193  -0.272  266.415 1.00 18.51  ? 124 THR B CG2 1 
ATOM   5013 N  N   . ASP B 1 125 ? -77.339  4.463   267.030 1.00 17.56  ? 125 ASP B N   1 
ATOM   5014 C  CA  . ASP B 1 125 ? -76.531  5.605   267.437 1.00 16.16  ? 125 ASP B CA  1 
ATOM   5015 C  C   . ASP B 1 125 ? -76.971  6.187   268.774 1.00 20.79  ? 125 ASP B C   1 
ATOM   5016 O  O   . ASP B 1 125 ? -76.241  7.004   269.345 1.00 20.39  ? 125 ASP B O   1 
ATOM   5017 C  CB  . ASP B 1 125 ? -76.562  6.693   266.358 1.00 14.75  ? 125 ASP B CB  1 
ATOM   5018 C  CG  . ASP B 1 125 ? -77.968  7.021   265.891 1.00 19.63  ? 125 ASP B CG  1 
ATOM   5019 O  OD1 . ASP B 1 125 ? -78.925  6.829   266.670 1.00 24.28  ? 125 ASP B OD1 1 
ATOM   5020 O  OD2 . ASP B 1 125 ? -78.115  7.480   264.739 1.00 17.78  ? 125 ASP B OD2 1 
ATOM   5021 N  N   . GLY B 1 126 ? -78.133  5.789   269.282 1.00 21.30  ? 126 GLY B N   1 
ATOM   5022 C  CA  . GLY B 1 126 ? -78.604  6.245   270.571 1.00 23.53  ? 126 GLY B CA  1 
ATOM   5023 C  C   . GLY B 1 126 ? -79.429  7.511   270.556 1.00 21.21  ? 126 GLY B C   1 
ATOM   5024 O  O   . GLY B 1 126 ? -79.680  8.076   271.627 1.00 26.01  ? 126 GLY B O   1 
ATOM   5025 N  N   . GLY B 1 127 ? -79.867  7.971   269.383 1.00 18.41  ? 127 GLY B N   1 
ATOM   5026 C  CA  . GLY B 1 127 ? -80.654  9.192   269.291 1.00 19.68  ? 127 GLY B CA  1 
ATOM   5027 C  C   . GLY B 1 127 ? -81.980  9.141   270.021 1.00 19.13  ? 127 GLY B C   1 
ATOM   5028 O  O   . GLY B 1 127 ? -82.608  10.191  270.203 1.00 34.71  ? 127 GLY B O   1 
ATOM   5029 N  N   . HIS B 1 128 ? -82.419  7.958   270.440 1.00 20.43  ? 128 HIS B N   1 
ATOM   5030 C  CA  . HIS B 1 128 ? -83.658  7.787   271.184 1.00 21.38  ? 128 HIS B CA  1 
ATOM   5031 C  C   . HIS B 1 128 ? -83.425  7.524   272.665 1.00 19.45  ? 128 HIS B C   1 
ATOM   5032 O  O   . HIS B 1 128 ? -84.394  7.407   273.420 1.00 18.89  ? 128 HIS B O   1 
ATOM   5033 C  CB  . HIS B 1 128 ? -84.469  6.636   270.584 1.00 20.69  ? 128 HIS B CB  1 
ATOM   5034 C  CG  . HIS B 1 128 ? -83.791  5.307   270.698 1.00 20.94  ? 128 HIS B CG  1 
ATOM   5035 N  ND1 . HIS B 1 128 ? -82.741  4.936   269.886 1.00 20.37  ? 128 HIS B ND1 1 
ATOM   5036 C  CD2 . HIS B 1 128 ? -84.005  4.265   271.535 1.00 21.18  ? 128 HIS B CD2 1 
ATOM   5037 C  CE1 . HIS B 1 128 ? -82.340  3.721   270.215 1.00 21.50  ? 128 HIS B CE1 1 
ATOM   5038 N  NE2 . HIS B 1 128 ? -83.090  3.292   271.213 1.00 24.97  ? 128 HIS B NE2 1 
ATOM   5039 N  N   . LEU B 1 129 ? -82.171  7.427   273.095 1.00 19.12  ? 129 LEU B N   1 
ATOM   5040 C  CA  . LEU B 1 129 ? -81.826  7.057   274.458 1.00 19.71  ? 129 LEU B CA  1 
ATOM   5041 C  C   . LEU B 1 129 ? -81.359  8.274   275.247 1.00 21.72  ? 129 LEU B C   1 
ATOM   5042 O  O   . LEU B 1 129 ? -80.962  9.298   274.683 1.00 26.93  ? 129 LEU B O   1 
ATOM   5043 C  CB  . LEU B 1 129 ? -80.736  5.979   274.470 1.00 20.69  ? 129 LEU B CB  1 
ATOM   5044 C  CG  . LEU B 1 129 ? -81.117  4.628   273.862 1.00 21.24  ? 129 LEU B CG  1 
ATOM   5045 C  CD1 . LEU B 1 129 ? -79.942  3.668   273.916 1.00 28.71  ? 129 LEU B CD1 1 
ATOM   5046 C  CD2 . LEU B 1 129 ? -82.322  4.041   274.576 1.00 24.54  ? 129 LEU B CD2 1 
ATOM   5047 N  N   . ALA B 1 130 ? -81.413  8.142   276.590 1.00 22.79  ? 130 ALA B N   1 
ATOM   5048 C  CA  . ALA B 1 130 ? -81.014  9.131   277.577 1.00 22.71  ? 130 ALA B CA  1 
ATOM   5049 C  C   . ALA B 1 130 ? -79.609  8.838   278.092 1.00 27.47  ? 130 ALA B C   1 
ATOM   5050 O  O   . ALA B 1 130 ? -79.190  7.678   278.140 1.00 42.07  ? 130 ALA B O   1 
ATOM   5051 C  CB  . ALA B 1 130 ? -81.995  9.149   278.753 1.00 26.95  ? 130 ALA B CB  1 
ATOM   5052 N  N   . PRO B 1 131 ? -78.859  9.871   278.475 1.00 25.14  ? 131 PRO B N   1 
ATOM   5053 C  CA  . PRO B 1 131 ? -77.479  9.656   278.929 1.00 23.96  ? 131 PRO B CA  1 
ATOM   5054 C  C   . PRO B 1 131 ? -77.416  8.756   280.155 1.00 23.75  ? 131 PRO B C   1 
ATOM   5055 O  O   . PRO B 1 131 ? -78.134  8.958   281.137 1.00 24.43  ? 131 PRO B O   1 
ATOM   5056 C  CB  . PRO B 1 131 ? -76.992  11.073  279.248 1.00 23.82  ? 131 PRO B CB  1 
ATOM   5057 C  CG  . PRO B 1 131 ? -77.804  11.944  278.363 1.00 24.67  ? 131 PRO B CG  1 
ATOM   5058 C  CD  . PRO B 1 131 ? -79.166  11.304  278.327 1.00 42.35  ? 131 PRO B CD  1 
ATOM   5059 N  N   . LEU B 1 132 ? -76.543  7.753   280.087 1.00 23.04  ? 132 LEU B N   1 
ATOM   5060 C  CA  . LEU B 1 132 ? -76.283  6.846   281.204 1.00 27.55  ? 132 LEU B CA  1 
ATOM   5061 C  C   . LEU B 1 132 ? -75.020  7.341   281.901 1.00 26.09  ? 132 LEU B C   1 
ATOM   5062 O  O   . LEU B 1 132 ? -73.900  7.010   281.511 1.00 24.22  ? 132 LEU B O   1 
ATOM   5063 C  CB  . LEU B 1 132 ? -76.143  5.408   280.720 1.00 26.96  ? 132 LEU B CB  1 
ATOM   5064 C  CG  . LEU B 1 132 ? -75.720  4.369   281.761 1.00 23.85  ? 132 LEU B CG  1 
ATOM   5065 C  CD1 . LEU B 1 132 ? -76.664  4.383   282.951 1.00 24.40  ? 132 LEU B CD1 1 
ATOM   5066 C  CD2 . LEU B 1 132 ? -75.657  2.983   281.138 1.00 28.01  ? 132 LEU B CD2 1 
ATOM   5067 N  N   . GLU B 1 133 ? -75.208  8.149   282.939 1.00 26.38  ? 133 GLU B N   1 
ATOM   5068 C  CA  . GLU B 1 133 ? -74.086  8.727   283.662 1.00 30.10  ? 133 GLU B CA  1 
ATOM   5069 C  C   . GLU B 1 133 ? -73.524  7.726   284.662 1.00 31.14  ? 133 GLU B C   1 
ATOM   5070 O  O   . GLU B 1 133 ? -74.270  7.001   285.326 1.00 40.92  ? 133 GLU B O   1 
ATOM   5071 C  CB  . GLU B 1 133 ? -74.519  10.006  284.380 1.00 34.55  ? 133 GLU B CB  1 
ATOM   5072 C  CG  . GLU B 1 133 ? -73.387  10.754  285.062 1.00 58.32  ? 133 GLU B CG  1 
ATOM   5073 C  CD  . GLU B 1 133 ? -73.817  12.111  285.579 1.00 47.21  ? 133 GLU B CD  1 
ATOM   5074 O  OE1 . GLU B 1 133 ? -74.080  13.007  284.750 1.00 46.67  ? 133 GLU B OE1 1 
ATOM   5075 O  OE2 . GLU B 1 133 ? -73.894  12.281  286.814 1.00 50.67  ? 133 GLU B OE2 1 
ATOM   5076 N  N   . TYR B 1 134 ? -72.197  7.688   284.763 1.00 29.95  ? 134 TYR B N   1 
ATOM   5077 C  CA  . TYR B 1 134 ? -71.524  6.764   285.667 1.00 32.34  ? 134 TYR B CA  1 
ATOM   5078 C  C   . TYR B 1 134 ? -71.533  7.317   287.087 1.00 32.48  ? 134 TYR B C   1 
ATOM   5079 O  O   . TYR B 1 134 ? -70.973  8.387   287.347 1.00 33.91  ? 134 TYR B O   1 
ATOM   5080 C  CB  . TYR B 1 134 ? -70.091  6.511   285.203 1.00 28.96  ? 134 TYR B CB  1 
ATOM   5081 C  CG  . TYR B 1 134 ? -69.236  5.813   286.238 1.00 27.10  ? 134 TYR B CG  1 
ATOM   5082 C  CD1 . TYR B 1 134 ? -69.382  4.455   286.488 1.00 43.80  ? 134 TYR B CD1 1 
ATOM   5083 C  CD2 . TYR B 1 134 ? -68.284  6.514   286.967 1.00 26.20  ? 134 TYR B CD2 1 
ATOM   5084 C  CE1 . TYR B 1 134 ? -68.604  3.815   287.436 1.00 39.19  ? 134 TYR B CE1 1 
ATOM   5085 C  CE2 . TYR B 1 134 ? -67.502  5.882   287.914 1.00 25.56  ? 134 TYR B CE2 1 
ATOM   5086 C  CZ  . TYR B 1 134 ? -67.666  4.534   288.146 1.00 25.08  ? 134 TYR B CZ  1 
ATOM   5087 O  OH  . TYR B 1 134 ? -66.888  3.904   289.090 1.00 23.49  ? 134 TYR B OH  1 
ATOM   5088 N  N   . THR B 1 135 ? -72.166  6.587   288.001 1.00 32.55  ? 135 THR B N   1 
ATOM   5089 C  CA  . THR B 1 135 ? -72.072  6.900   289.419 1.00 30.66  ? 135 THR B CA  1 
ATOM   5090 C  C   . THR B 1 135 ? -70.752  6.366   289.959 1.00 37.04  ? 135 THR B C   1 
ATOM   5091 O  O   . THR B 1 135 ? -70.410  5.200   289.742 1.00 53.85  ? 135 THR B O   1 
ATOM   5092 C  CB  . THR B 1 135 ? -73.247  6.296   290.186 1.00 37.97  ? 135 THR B CB  1 
ATOM   5093 O  OG1 . THR B 1 135 ? -74.477  6.806   289.657 1.00 64.43  ? 135 THR B OG1 1 
ATOM   5094 C  CG2 . THR B 1 135 ? -73.154  6.643   291.664 1.00 38.53  ? 135 THR B CG2 1 
ATOM   5095 N  N   . TRP B 1 136 ? -70.009  7.221   290.656 1.00 29.54  ? 136 TRP B N   1 
ATOM   5096 C  CA  . TRP B 1 136 ? -68.655  6.880   291.083 1.00 28.94  ? 136 TRP B CA  1 
ATOM   5097 C  C   . TRP B 1 136 ? -68.711  5.849   292.205 1.00 27.88  ? 136 TRP B C   1 
ATOM   5098 O  O   . TRP B 1 136 ? -69.190  6.139   293.305 1.00 27.26  ? 136 TRP B O   1 
ATOM   5099 C  CB  . TRP B 1 136 ? -67.916  8.141   291.516 1.00 29.21  ? 136 TRP B CB  1 
ATOM   5100 C  CG  . TRP B 1 136 ? -67.772  9.124   290.396 1.00 28.87  ? 136 TRP B CG  1 
ATOM   5101 C  CD1 . TRP B 1 136 ? -68.635  10.130  290.072 1.00 30.74  ? 136 TRP B CD1 1 
ATOM   5102 C  CD2 . TRP B 1 136 ? -66.716  9.175   289.428 1.00 28.71  ? 136 TRP B CD2 1 
ATOM   5103 N  NE1 . TRP B 1 136 ? -68.175  10.813  288.973 1.00 31.74  ? 136 TRP B NE1 1 
ATOM   5104 C  CE2 . TRP B 1 136 ? -66.999  10.246  288.558 1.00 30.32  ? 136 TRP B CE2 1 
ATOM   5105 C  CE3 . TRP B 1 136 ? -65.555  8.424   289.219 1.00 29.26  ? 136 TRP B CE3 1 
ATOM   5106 C  CZ2 . TRP B 1 136 ? -66.165  10.584  287.495 1.00 31.38  ? 136 TRP B CZ2 1 
ATOM   5107 C  CZ3 . TRP B 1 136 ? -64.729  8.762   288.163 1.00 27.03  ? 136 TRP B CZ3 1 
ATOM   5108 C  CH2 . TRP B 1 136 ? -65.038  9.832   287.315 1.00 27.59  ? 136 TRP B CH2 1 
ATOM   5109 N  N   . LEU B 1 137 ? -68.217  4.646   291.925 1.00 26.91  ? 137 LEU B N   1 
ATOM   5110 C  CA  . LEU B 1 137 ? -68.271  3.525   292.850 1.00 29.00  ? 137 LEU B CA  1 
ATOM   5111 C  C   . LEU B 1 137 ? -66.873  3.158   293.332 1.00 27.38  ? 137 LEU B C   1 
ATOM   5112 O  O   . LEU B 1 137 ? -65.877  3.405   292.646 1.00 27.85  ? 137 LEU B O   1 
ATOM   5113 C  CB  . LEU B 1 137 ? -68.915  2.299   292.194 1.00 27.77  ? 137 LEU B CB  1 
ATOM   5114 C  CG  . LEU B 1 137 ? -70.319  2.442   291.609 1.00 24.69  ? 137 LEU B CG  1 
ATOM   5115 C  CD1 . LEU B 1 137 ? -70.760  1.133   290.976 1.00 19.93  ? 137 LEU B CD1 1 
ATOM   5116 C  CD2 . LEU B 1 137 ? -71.305  2.879   292.679 1.00 32.69  ? 137 LEU B CD2 1 
ATOM   5117 N  N   . GLU B 1 138 ? -66.820  2.561   294.520 1.00 27.46  ? 138 GLU B N   1 
ATOM   5118 C  CA  . GLU B 1 138 ? -65.599  1.975   295.094 1.00 31.42  ? 138 GLU B CA  1 
ATOM   5119 C  C   . GLU B 1 138 ? -64.550  3.078   295.226 1.00 37.05  ? 138 GLU B C   1 
ATOM   5120 O  O   . GLU B 1 138 ? -64.858  4.143   295.785 1.00 65.92  ? 138 GLU B O   1 
ATOM   5121 C  CB  . GLU B 1 138 ? -65.187  0.772   294.253 1.00 28.94  ? 138 GLU B CB  1 
ATOM   5122 C  CG  . GLU B 1 138 ? -66.286  -0.257  294.058 1.00 30.08  ? 138 GLU B CG  1 
ATOM   5123 C  CD  . GLU B 1 138 ? -65.797  -1.496  293.337 1.00 22.92  ? 138 GLU B CD  1 
ATOM   5124 O  OE1 . GLU B 1 138 ? -65.219  -2.381  294.002 1.00 23.46  ? 138 GLU B OE1 1 
ATOM   5125 O  OE2 . GLU B 1 138 ? -65.987  -1.585  292.106 1.00 21.49  ? 138 GLU B OE2 1 
ATOM   5126 N  N   . ASN B 1 139 ? -63.325  2.878   294.745 1.00 32.50  ? 139 ASN B N   1 
ATOM   5127 C  CA  . ASN B 1 139 ? -62.250  3.849   294.888 1.00 33.90  ? 139 ASN B CA  1 
ATOM   5128 C  C   . ASN B 1 139 ? -61.987  4.631   293.608 1.00 32.43  ? 139 ASN B C   1 
ATOM   5129 O  O   . ASN B 1 139 ? -60.964  5.316   293.513 1.00 31.21  ? 139 ASN B O   1 
ATOM   5130 C  CB  . ASN B 1 139 ? -60.968  3.147   295.340 1.00 43.17  ? 139 ASN B CB  1 
ATOM   5131 C  CG  . ASN B 1 139 ? -61.155  2.367   296.626 1.00 38.04  ? 139 ASN B CG  1 
ATOM   5132 O  OD1 . ASN B 1 139 ? -61.973  2.728   297.470 1.00 58.45  ? 139 ASN B OD1 1 
ATOM   5133 N  ND2 . ASN B 1 139 ? -60.396  1.288   296.779 1.00 53.80  ? 139 ASN B ND2 1 
ATOM   5134 N  N   . ASN B 1 140 ? -62.877  4.542   292.624 1.00 31.53  ? 140 ASN B N   1 
ATOM   5135 C  CA  . ASN B 1 140 ? -62.692  5.281   291.382 1.00 27.29  ? 140 ASN B CA  1 
ATOM   5136 C  C   . ASN B 1 140 ? -62.846  6.776   291.631 1.00 25.95  ? 140 ASN B C   1 
ATOM   5137 O  O   . ASN B 1 140 ? -63.845  7.223   292.202 1.00 26.87  ? 140 ASN B O   1 
ATOM   5138 C  CB  . ASN B 1 140 ? -63.695  4.813   290.330 1.00 38.10  ? 140 ASN B CB  1 
ATOM   5139 C  CG  . ASN B 1 140 ? -63.412  3.407   289.841 1.00 43.47  ? 140 ASN B CG  1 
ATOM   5140 O  OD1 . ASN B 1 140 ? -62.591  3.204   288.947 1.00 48.08  ? 140 ASN B OD1 1 
ATOM   5141 N  ND2 . ASN B 1 140 ? -64.093  2.428   290.425 1.00 38.93  ? 140 ASN B ND2 1 
ATOM   5142 N  N   . LYS B 1 141 ? -61.851  7.548   291.202 1.00 27.54  ? 141 LYS B N   1 
ATOM   5143 C  CA  . LYS B 1 141 ? -61.846  8.986   291.394 1.00 27.08  ? 141 LYS B CA  1 
ATOM   5144 C  C   . LYS B 1 141 ? -61.695  9.698   290.056 1.00 35.68  ? 141 LYS B C   1 
ATOM   5145 O  O   . LYS B 1 141 ? -61.038  9.183   289.145 1.00 24.75  ? 141 LYS B O   1 
ATOM   5146 C  CB  . LYS B 1 141 ? -60.714  9.414   292.336 1.00 25.20  ? 141 LYS B CB  1 
ATOM   5147 C  CG  . LYS B 1 141 ? -60.817  8.807   293.725 1.00 33.98  ? 141 LYS B CG  1 
ATOM   5148 C  CD  . LYS B 1 141 ? -59.645  9.210   294.602 1.00 32.17  ? 141 LYS B CD  1 
ATOM   5149 C  CE  . LYS B 1 141 ? -59.700  8.504   295.947 1.00 42.33  ? 141 LYS B CE  1 
ATOM   5150 N  NZ  . LYS B 1 141 ? -58.539  8.857   296.811 1.00 36.33  ? 141 LYS B NZ  1 
ATOM   5151 N  N   . PRO B 1 142 ? -62.302  10.875  289.902 1.00 28.29  ? 142 PRO B N   1 
ATOM   5152 C  CA  . PRO B 1 142 ? -62.229  11.584  288.621 1.00 28.31  ? 142 PRO B CA  1 
ATOM   5153 C  C   . PRO B 1 142 ? -60.801  11.971  288.266 1.00 23.10  ? 142 PRO B C   1 
ATOM   5154 O  O   . PRO B 1 142 ? -59.920  12.078  289.121 1.00 24.51  ? 142 PRO B O   1 
ATOM   5155 C  CB  . PRO B 1 142 ? -63.101  12.825  288.850 1.00 26.56  ? 142 PRO B CB  1 
ATOM   5156 C  CG  . PRO B 1 142 ? -63.991  12.464  289.992 1.00 29.25  ? 142 PRO B CG  1 
ATOM   5157 C  CD  . PRO B 1 142 ? -63.172  11.568  290.867 1.00 25.28  ? 142 PRO B CD  1 
ATOM   5158 N  N   . GLY B 1 143 ? -60.583  12.183  286.971 1.00 22.60  ? 143 GLY B N   1 
ATOM   5159 C  CA  . GLY B 1 143 ? -59.269  12.527  286.469 1.00 23.34  ? 143 GLY B CA  1 
ATOM   5160 C  C   . GLY B 1 143 ? -58.776  11.553  285.420 1.00 23.56  ? 143 GLY B C   1 
ATOM   5161 O  O   . GLY B 1 143 ? -58.596  10.365  285.704 1.00 24.47  ? 143 GLY B O   1 
ATOM   5162 N  N   . ARG B 1 144 ? -58.558  12.041  284.203 1.00 23.00  ? 144 ARG B N   1 
ATOM   5163 C  CA  . ARG B 1 144 ? -58.107  11.219  283.091 1.00 25.35  ? 144 ARG B CA  1 
ATOM   5164 C  C   . ARG B 1 144 ? -56.776  11.742  282.572 1.00 30.46  ? 144 ARG B C   1 
ATOM   5165 O  O   . ARG B 1 144 ? -56.548  12.955  282.537 1.00 34.12  ? 144 ARG B O   1 
ATOM   5166 C  CB  . ARG B 1 144 ? -59.140  11.207  281.957 1.00 26.09  ? 144 ARG B CB  1 
ATOM   5167 C  CG  . ARG B 1 144 ? -58.846  10.194  280.861 1.00 27.60  ? 144 ARG B CG  1 
ATOM   5168 C  CD  . ARG B 1 144 ? -59.961  10.136  279.828 1.00 24.08  ? 144 ARG B CD  1 
ATOM   5169 N  NE  . ARG B 1 144 ? -59.964  11.301  278.949 1.00 24.42  ? 144 ARG B NE  1 
ATOM   5170 C  CZ  . ARG B 1 144 ? -60.811  12.319  279.058 1.00 28.28  ? 144 ARG B CZ  1 
ATOM   5171 N  NH1 . ARG B 1 144 ? -61.731  12.319  280.012 1.00 28.91  ? 144 ARG B NH1 1 
ATOM   5172 N  NH2 . ARG B 1 144 ? -60.740  13.336  278.211 1.00 55.53  ? 144 ARG B NH2 1 
ATOM   5173 N  N   . ARG B 1 145 ? -55.898  10.822  282.178 1.00 33.78  ? 145 ARG B N   1 
ATOM   5174 C  CA  . ARG B 1 145 ? -54.647  11.215  281.543 1.00 32.96  ? 145 ARG B CA  1 
ATOM   5175 C  C   . ARG B 1 145 ? -54.946  11.913  280.224 1.00 33.73  ? 145 ARG B C   1 
ATOM   5176 O  O   . ARG B 1 145 ? -55.517  11.316  279.307 1.00 32.61  ? 145 ARG B O   1 
ATOM   5177 C  CB  . ARG B 1 145 ? -53.756  9.995   281.321 1.00 56.90  ? 145 ARG B CB  1 
ATOM   5178 C  CG  . ARG B 1 145 ? -52.400  10.329  280.724 1.00 43.64  ? 145 ARG B CG  1 
ATOM   5179 C  CD  . ARG B 1 145 ? -51.589  11.198  281.671 1.00 41.76  ? 145 ARG B CD  1 
ATOM   5180 N  NE  . ARG B 1 145 ? -50.271  11.515  281.130 1.00 38.77  ? 145 ARG B NE  1 
ATOM   5181 C  CZ  . ARG B 1 145 ? -49.165  10.836  281.413 1.00 36.09  ? 145 ARG B CZ  1 
ATOM   5182 N  NH1 . ARG B 1 145 ? -49.213  9.799   282.237 1.00 33.64  ? 145 ARG B NH1 1 
ATOM   5183 N  NH2 . ARG B 1 145 ? -48.010  11.196  280.873 1.00 49.76  ? 145 ARG B NH2 1 
ATOM   5184 N  N   . GLU B 1 146 ? -54.555  13.181  280.134 1.00 38.23  ? 146 GLU B N   1 
ATOM   5185 C  CA  . GLU B 1 146 ? -55.025  14.054  279.067 1.00 37.27  ? 146 GLU B CA  1 
ATOM   5186 C  C   . GLU B 1 146 ? -54.191  13.973  277.797 1.00 34.84  ? 146 GLU B C   1 
ATOM   5187 O  O   . GLU B 1 146 ? -54.723  14.204  276.705 1.00 36.33  ? 146 GLU B O   1 
ATOM   5188 C  CB  . GLU B 1 146 ? -55.059  15.499  279.570 1.00 39.93  ? 146 GLU B CB  1 
ATOM   5189 C  CG  . GLU B 1 146 ? -53.932  15.848  280.523 1.00 42.26  ? 146 GLU B CG  1 
ATOM   5190 C  CD  . GLU B 1 146 ? -54.263  17.037  281.403 1.00 60.71  ? 146 GLU B CD  1 
ATOM   5191 O  OE1 . GLU B 1 146 ? -54.347  18.166  280.876 1.00 67.17  ? 146 GLU B OE1 1 
ATOM   5192 O  OE2 . GLU B 1 146 ? -54.438  16.842  282.624 1.00 63.54  ? 146 GLU B OE2 1 
ATOM   5193 N  N   . ASP B 1 147 ? -52.906  13.650  277.901 1.00 35.90  ? 147 ASP B N   1 
ATOM   5194 C  CA  . ASP B 1 147 ? -52.019  13.662  276.747 1.00 39.34  ? 147 ASP B CA  1 
ATOM   5195 C  C   . ASP B 1 147 ? -51.751  12.277  276.175 1.00 54.87  ? 147 ASP B C   1 
ATOM   5196 O  O   . ASP B 1 147 ? -51.089  12.172  275.137 1.00 66.40  ? 147 ASP B O   1 
ATOM   5197 C  CB  . ASP B 1 147 ? -50.691  14.333  277.114 1.00 43.72  ? 147 ASP B CB  1 
ATOM   5198 C  CG  . ASP B 1 147 ? -50.024  13.687  278.310 1.00 54.02  ? 147 ASP B CG  1 
ATOM   5199 O  OD1 . ASP B 1 147 ? -50.748  13.234  279.222 1.00 54.83  ? 147 ASP B OD1 1 
ATOM   5200 O  OD2 . ASP B 1 147 ? -48.777  13.631  278.339 1.00 56.27  ? 147 ASP B OD2 1 
ATOM   5201 N  N   . LYS B 1 148 ? -52.243  11.216  276.812 1.00 42.09  ? 148 LYS B N   1 
ATOM   5202 C  CA  . LYS B 1 148 ? -51.945  9.861   276.372 1.00 37.67  ? 148 LYS B CA  1 
ATOM   5203 C  C   . LYS B 1 148 ? -53.204  9.006   276.430 1.00 32.18  ? 148 LYS B C   1 
ATOM   5204 O  O   . LYS B 1 148 ? -54.191  9.355   277.083 1.00 31.85  ? 148 LYS B O   1 
ATOM   5205 C  CB  . LYS B 1 148 ? -50.822  9.238   277.214 1.00 39.92  ? 148 LYS B CB  1 
ATOM   5206 C  CG  . LYS B 1 148 ? -49.493  9.967   277.072 1.00 49.03  ? 148 LYS B CG  1 
ATOM   5207 C  CD  . LYS B 1 148 ? -48.385  9.308   277.869 1.00 40.91  ? 148 LYS B CD  1 
ATOM   5208 C  CE  . LYS B 1 148 ? -47.021  9.824   277.436 1.00 54.88  ? 148 LYS B CE  1 
ATOM   5209 N  NZ  . LYS B 1 148 ? -47.126  10.863  276.370 1.00 59.46  ? 148 LYS B NZ  1 
ATOM   5210 N  N   . ILE B 1 149 ? -53.150  7.874   275.734 1.00 32.96  ? 149 ILE B N   1 
ATOM   5211 C  CA  . ILE B 1 149 ? -54.312  7.008   275.569 1.00 30.72  ? 149 ILE B CA  1 
ATOM   5212 C  C   . ILE B 1 149 ? -54.465  6.124   276.798 1.00 27.03  ? 149 ILE B C   1 
ATOM   5213 O  O   . ILE B 1 149 ? -53.501  5.499   277.254 1.00 26.61  ? 149 ILE B O   1 
ATOM   5214 C  CB  . ILE B 1 149 ? -54.178  6.161   274.293 1.00 26.77  ? 149 ILE B CB  1 
ATOM   5215 C  CG1 . ILE B 1 149 ? -54.108  7.062   273.060 1.00 25.55  ? 149 ILE B CG1 1 
ATOM   5216 C  CG2 . ILE B 1 149 ? -55.335  5.182   274.176 1.00 25.95  ? 149 ILE B CG2 1 
ATOM   5217 C  CD1 . ILE B 1 149 ? -55.347  7.900   272.848 1.00 35.30  ? 149 ILE B CD1 1 
ATOM   5218 N  N   . VAL B 1 150 ? -55.681  6.064   277.335 1.00 26.06  ? 150 VAL B N   1 
ATOM   5219 C  CA  . VAL B 1 150 ? -56.011  5.212   278.474 1.00 22.96  ? 150 VAL B CA  1 
ATOM   5220 C  C   . VAL B 1 150 ? -57.194  4.350   278.053 1.00 26.19  ? 150 VAL B C   1 
ATOM   5221 O  O   . VAL B 1 150 ? -58.342  4.811   278.062 1.00 33.55  ? 150 VAL B O   1 
ATOM   5222 C  CB  . VAL B 1 150 ? -56.333  6.017   279.737 1.00 23.30  ? 150 VAL B CB  1 
ATOM   5223 C  CG1 . VAL B 1 150 ? -56.734  5.085   280.870 1.00 22.42  ? 150 VAL B CG1 1 
ATOM   5224 C  CG2 . VAL B 1 150 ? -55.138  6.861   280.140 1.00 28.75  ? 150 VAL B CG2 1 
ATOM   5225 N  N   . ALA B 1 151 ? -56.924  3.104   277.683 1.00 32.53  ? 151 ALA B N   1 
ATOM   5226 C  CA  . ALA B 1 151 ? -57.949  2.172   277.241 1.00 30.14  ? 151 ALA B CA  1 
ATOM   5227 C  C   . ALA B 1 151 ? -58.183  1.102   278.299 1.00 23.23  ? 151 ALA B C   1 
ATOM   5228 O  O   . ALA B 1 151 ? -57.405  0.937   279.241 1.00 28.24  ? 151 ALA B O   1 
ATOM   5229 C  CB  . ALA B 1 151 ? -57.561  1.530   275.904 1.00 27.18  ? 151 ALA B CB  1 
ATOM   5230 N  N   . ALA B 1 152 ? -59.282  0.371   278.130 1.00 26.40  ? 152 ALA B N   1 
ATOM   5231 C  CA  . ALA B 1 152 ? -59.633  -0.712  279.037 1.00 23.36  ? 152 ALA B CA  1 
ATOM   5232 C  C   . ALA B 1 152 ? -60.520  -1.698  278.295 1.00 20.91  ? 152 ALA B C   1 
ATOM   5233 O  O   . ALA B 1 152 ? -61.174  -1.352  277.308 1.00 22.88  ? 152 ALA B O   1 
ATOM   5234 C  CB  . ALA B 1 152 ? -60.333  -0.192  280.297 1.00 18.54  ? 152 ALA B CB  1 
ATOM   5235 N  N   . TYR B 1 153 ? -60.535  -2.932  278.788 1.00 17.09  ? 153 TYR B N   1 
ATOM   5236 C  CA  . TYR B 1 153 ? -61.274  -4.021  278.166 1.00 18.70  ? 153 TYR B CA  1 
ATOM   5237 C  C   . TYR B 1 153 ? -62.509  -4.352  278.991 1.00 18.43  ? 153 TYR B C   1 
ATOM   5238 O  O   . TYR B 1 153 ? -62.412  -4.571  280.203 1.00 18.77  ? 153 TYR B O   1 
ATOM   5239 C  CB  . TYR B 1 153 ? -60.399  -5.265  278.024 1.00 19.71  ? 153 TYR B CB  1 
ATOM   5240 C  CG  . TYR B 1 153 ? -59.692  -5.387  276.695 1.00 19.88  ? 153 TYR B CG  1 
ATOM   5241 C  CD1 . TYR B 1 153 ? -60.336  -5.936  275.595 1.00 20.12  ? 153 TYR B CD1 1 
ATOM   5242 C  CD2 . TYR B 1 153 ? -58.377  -4.973  276.543 1.00 21.31  ? 153 TYR B CD2 1 
ATOM   5243 C  CE1 . TYR B 1 153 ? -59.696  -6.057  274.378 1.00 21.95  ? 153 TYR B CE1 1 
ATOM   5244 C  CE2 . TYR B 1 153 ? -57.726  -5.092  275.330 1.00 22.96  ? 153 TYR B CE2 1 
ATOM   5245 C  CZ  . TYR B 1 153 ? -58.391  -5.633  274.250 1.00 22.10  ? 153 TYR B CZ  1 
ATOM   5246 O  OH  . TYR B 1 153 ? -57.751  -5.753  273.038 1.00 23.04  ? 153 TYR B OH  1 
ATOM   5247 N  N   . PHE B 1 154 ? -63.661  -4.398  278.328 1.00 18.27  ? 154 PHE B N   1 
ATOM   5248 C  CA  . PHE B 1 154 ? -64.911  -4.838  278.931 1.00 19.30  ? 154 PHE B CA  1 
ATOM   5249 C  C   . PHE B 1 154 ? -65.275  -6.201  278.361 1.00 20.68  ? 154 PHE B C   1 
ATOM   5250 O  O   . PHE B 1 154 ? -65.334  -6.371  277.139 1.00 17.47  ? 154 PHE B O   1 
ATOM   5251 C  CB  . PHE B 1 154 ? -66.033  -3.832  278.670 1.00 18.26  ? 154 PHE B CB  1 
ATOM   5252 C  CG  . PHE B 1 154 ? -67.379  -4.281  279.166 1.00 20.30  ? 154 PHE B CG  1 
ATOM   5253 C  CD1 . PHE B 1 154 ? -67.715  -4.157  280.504 1.00 20.52  ? 154 PHE B CD1 1 
ATOM   5254 C  CD2 . PHE B 1 154 ? -68.309  -4.822  278.294 1.00 19.02  ? 154 PHE B CD2 1 
ATOM   5255 C  CE1 . PHE B 1 154 ? -68.951  -4.569  280.964 1.00 20.12  ? 154 PHE B CE1 1 
ATOM   5256 C  CE2 . PHE B 1 154 ? -69.547  -5.236  278.748 1.00 17.75  ? 154 PHE B CE2 1 
ATOM   5257 C  CZ  . PHE B 1 154 ? -69.868  -5.108  280.085 1.00 17.10  ? 154 PHE B CZ  1 
ATOM   5258 N  N   . VAL B 1 155 ? -65.513  -7.166  279.242 1.00 19.97  ? 155 VAL B N   1 
ATOM   5259 C  CA  . VAL B 1 155 ? -65.823  -8.530  278.833 1.00 21.03  ? 155 VAL B CA  1 
ATOM   5260 C  C   . VAL B 1 155 ? -67.327  -8.673  278.653 1.00 21.87  ? 155 VAL B C   1 
ATOM   5261 O  O   . VAL B 1 155 ? -68.119  -8.170  279.460 1.00 19.94  ? 155 VAL B O   1 
ATOM   5262 C  CB  . VAL B 1 155 ? -65.279  -9.547  279.854 1.00 22.83  ? 155 VAL B CB  1 
ATOM   5263 C  CG1 . VAL B 1 155 ? -63.760  -9.598  279.790 1.00 20.78  ? 155 VAL B CG1 1 
ATOM   5264 C  CG2 . VAL B 1 155 ? -65.738  -9.194  281.258 1.00 36.56  ? 155 VAL B CG2 1 
ATOM   5265 N  N   . GLU B 1 156 ? -67.723  -9.358  277.579 1.00 22.65  ? 156 GLU B N   1 
ATOM   5266 C  CA  . GLU B 1 156 ? -69.143  -9.551  277.297 1.00 22.46  ? 156 GLU B CA  1 
ATOM   5267 C  C   . GLU B 1 156 ? -69.814  -10.389 278.377 1.00 22.79  ? 156 GLU B C   1 
ATOM   5268 O  O   . GLU B 1 156 ? -70.933  -10.085 278.806 1.00 22.78  ? 156 GLU B O   1 
ATOM   5269 C  CB  . GLU B 1 156 ? -69.313  -10.203 275.925 1.00 25.08  ? 156 GLU B CB  1 
ATOM   5270 C  CG  . GLU B 1 156 ? -70.746  -10.545 275.558 1.00 25.53  ? 156 GLU B CG  1 
ATOM   5271 C  CD  . GLU B 1 156 ? -70.880  -10.997 274.117 1.00 26.79  ? 156 GLU B CD  1 
ATOM   5272 O  OE1 . GLU B 1 156 ? -70.934  -12.221 273.877 1.00 27.30  ? 156 GLU B OE1 1 
ATOM   5273 O  OE2 . GLU B 1 156 ? -70.930  -10.127 273.222 1.00 26.22  ? 156 GLU B OE2 1 
ATOM   5274 N  N   . TRP B 1 157 ? -69.143  -11.442 278.834 1.00 21.62  ? 157 TRP B N   1 
ATOM   5275 C  CA  . TRP B 1 157 ? -69.681  -12.343 279.843 1.00 20.71  ? 157 TRP B CA  1 
ATOM   5276 C  C   . TRP B 1 157 ? -69.551  -11.801 281.262 1.00 24.46  ? 157 TRP B C   1 
ATOM   5277 O  O   . TRP B 1 157 ? -69.849  -12.528 282.215 1.00 24.00  ? 157 TRP B O   1 
ATOM   5278 C  CB  . TRP B 1 157 ? -68.988  -13.704 279.742 1.00 22.14  ? 157 TRP B CB  1 
ATOM   5279 C  CG  . TRP B 1 157 ? -67.506  -13.626 279.936 1.00 26.72  ? 157 TRP B CG  1 
ATOM   5280 C  CD1 . TRP B 1 157 ? -66.819  -13.825 281.097 1.00 28.08  ? 157 TRP B CD1 1 
ATOM   5281 C  CD2 . TRP B 1 157 ? -66.526  -13.318 278.938 1.00 24.26  ? 157 TRP B CD2 1 
ATOM   5282 N  NE1 . TRP B 1 157 ? -65.471  -13.664 280.883 1.00 25.69  ? 157 TRP B NE1 1 
ATOM   5283 C  CE2 . TRP B 1 157 ? -65.265  -13.352 279.565 1.00 22.16  ? 157 TRP B CE2 1 
ATOM   5284 C  CE3 . TRP B 1 157 ? -66.592  -13.019 277.574 1.00 25.23  ? 157 TRP B CE3 1 
ATOM   5285 C  CZ2 . TRP B 1 157 ? -64.082  -13.099 278.877 1.00 28.44  ? 157 TRP B CZ2 1 
ATOM   5286 C  CZ3 . TRP B 1 157 ? -65.416  -12.767 276.892 1.00 25.71  ? 157 TRP B CZ3 1 
ATOM   5287 C  CH2 . TRP B 1 157 ? -64.178  -12.809 277.544 1.00 29.42  ? 157 TRP B CH2 1 
ATOM   5288 N  N   . GLY B 1 158 ? -69.118  -10.551 281.427 1.00 26.02  ? 158 GLY B N   1 
ATOM   5289 C  CA  . GLY B 1 158 ? -68.970  -9.985  282.756 1.00 25.44  ? 158 GLY B CA  1 
ATOM   5290 C  C   . GLY B 1 158 ? -70.271  -9.619  283.435 1.00 25.72  ? 158 GLY B C   1 
ATOM   5291 O  O   . GLY B 1 158 ? -70.259  -9.315  284.633 1.00 26.76  ? 158 GLY B O   1 
ATOM   5292 N  N   . VAL B 1 159 ? -71.392  -9.644  282.705 1.00 25.17  ? 159 VAL B N   1 
ATOM   5293 C  CA  . VAL B 1 159 ? -72.683  -9.280  283.278 1.00 23.77  ? 159 VAL B CA  1 
ATOM   5294 C  C   . VAL B 1 159 ? -73.364  -10.446 283.976 1.00 23.86  ? 159 VAL B C   1 
ATOM   5295 O  O   . VAL B 1 159 ? -74.506  -10.301 284.434 1.00 22.15  ? 159 VAL B O   1 
ATOM   5296 C  CB  . VAL B 1 159 ? -73.625  -8.711  282.198 1.00 21.86  ? 159 VAL B CB  1 
ATOM   5297 C  CG1 . VAL B 1 159 ? -73.017  -7.471  281.573 1.00 20.10  ? 159 VAL B CG1 1 
ATOM   5298 C  CG2 . VAL B 1 159 ? -73.914  -9.764  281.145 1.00 20.19  ? 159 VAL B CG2 1 
ATOM   5299 N  N   . TYR B 1 160 ? -72.707  -11.601 284.068 1.00 24.83  ? 160 TYR B N   1 
ATOM   5300 C  CA  . TYR B 1 160 ? -73.299  -12.752 284.739 1.00 26.06  ? 160 TYR B CA  1 
ATOM   5301 C  C   . TYR B 1 160 ? -72.747  -12.905 286.150 1.00 25.71  ? 160 TYR B C   1 
ATOM   5302 O  O   . TYR B 1 160 ? -73.061  -12.102 287.035 1.00 33.96  ? 160 TYR B O   1 
ATOM   5303 C  CB  . TYR B 1 160 ? -73.061  -14.027 283.930 1.00 23.94  ? 160 TYR B CB  1 
ATOM   5304 C  CG  . TYR B 1 160 ? -73.665  -13.989 282.547 1.00 21.21  ? 160 TYR B CG  1 
ATOM   5305 C  CD1 . TYR B 1 160 ? -75.039  -13.898 282.375 1.00 23.88  ? 160 TYR B CD1 1 
ATOM   5306 C  CD2 . TYR B 1 160 ? -72.866  -14.055 281.413 1.00 21.56  ? 160 TYR B CD2 1 
ATOM   5307 C  CE1 . TYR B 1 160 ? -75.600  -13.863 281.117 1.00 22.52  ? 160 TYR B CE1 1 
ATOM   5308 C  CE2 . TYR B 1 160 ? -73.420  -14.023 280.148 1.00 22.39  ? 160 TYR B CE2 1 
ATOM   5309 C  CZ  . TYR B 1 160 ? -74.788  -13.928 280.007 1.00 21.48  ? 160 TYR B CZ  1 
ATOM   5310 O  OH  . TYR B 1 160 ? -75.351  -13.895 278.755 1.00 22.46  ? 160 TYR B OH  1 
ATOM   5311 N  N   . GLY B 1 161 ? -71.928  -13.935 286.367 1.00 20.22  ? 161 GLY B N   1 
ATOM   5312 C  CA  . GLY B 1 161 ? -71.396  -14.175 287.698 1.00 19.70  ? 161 GLY B CA  1 
ATOM   5313 C  C   . GLY B 1 161 ? -70.536  -13.033 288.201 1.00 20.27  ? 161 GLY B C   1 
ATOM   5314 O  O   . GLY B 1 161 ? -70.544  -12.715 289.393 1.00 24.87  ? 161 GLY B O   1 
ATOM   5315 N  N   . ARG B 1 162 ? -69.785  -12.396 287.300 1.00 23.31  ? 162 ARG B N   1 
ATOM   5316 C  CA  . ARG B 1 162 ? -68.952  -11.268 287.703 1.00 25.06  ? 162 ARG B CA  1 
ATOM   5317 C  C   . ARG B 1 162 ? -69.792  -10.062 288.100 1.00 24.39  ? 162 ARG B C   1 
ATOM   5318 O  O   . ARG B 1 162 ? -69.338  -9.232  288.895 1.00 27.81  ? 162 ARG B O   1 
ATOM   5319 C  CB  . ARG B 1 162 ? -67.982  -10.905 286.579 1.00 22.77  ? 162 ARG B CB  1 
ATOM   5320 C  CG  . ARG B 1 162 ? -66.930  -11.972 286.320 1.00 25.82  ? 162 ARG B CG  1 
ATOM   5321 C  CD  . ARG B 1 162 ? -66.029  -11.611 285.152 1.00 25.32  ? 162 ARG B CD  1 
ATOM   5322 N  NE  . ARG B 1 162 ? -64.818  -12.427 285.132 1.00 26.80  ? 162 ARG B NE  1 
ATOM   5323 C  CZ  . ARG B 1 162 ? -64.746  -13.648 284.611 1.00 29.45  ? 162 ARG B CZ  1 
ATOM   5324 N  NH1 . ARG B 1 162 ? -65.818  -14.204 284.065 1.00 44.89  ? 162 ARG B NH1 1 
ATOM   5325 N  NH2 . ARG B 1 162 ? -63.600  -14.315 284.639 1.00 28.75  ? 162 ARG B NH2 1 
ATOM   5326 N  N   . ASN B 1 163 ? -71.010  -9.955  287.566 1.00 22.66  ? 163 ASN B N   1 
ATOM   5327 C  CA  . ASN B 1 163 ? -71.955  -8.895  287.920 1.00 23.42  ? 163 ASN B CA  1 
ATOM   5328 C  C   . ASN B 1 163 ? -71.333  -7.512  287.716 1.00 22.96  ? 163 ASN B C   1 
ATOM   5329 O  O   . ASN B 1 163 ? -71.158  -6.730  288.652 1.00 25.24  ? 163 ASN B O   1 
ATOM   5330 C  CB  . ASN B 1 163 ? -72.455  -9.071  289.358 1.00 23.87  ? 163 ASN B CB  1 
ATOM   5331 C  CG  . ASN B 1 163 ? -73.672  -8.223  289.659 1.00 22.92  ? 163 ASN B CG  1 
ATOM   5332 O  OD1 . ASN B 1 163 ? -74.549  -8.052  288.812 1.00 18.54  ? 163 ASN B OD1 1 
ATOM   5333 N  ND2 . ASN B 1 163 ? -73.733  -7.683  290.870 1.00 31.16  ? 163 ASN B ND2 1 
ATOM   5334 N  N   . PHE B 1 164 ? -70.997  -7.224  286.462 1.00 19.68  ? 164 PHE B N   1 
ATOM   5335 C  CA  . PHE B 1 164 ? -70.364  -5.960  286.088 1.00 19.32  ? 164 PHE B CA  1 
ATOM   5336 C  C   . PHE B 1 164 ? -70.874  -5.527  284.723 1.00 18.33  ? 164 PHE B C   1 
ATOM   5337 O  O   . PHE B 1 164 ? -70.242  -5.783  283.691 1.00 18.96  ? 164 PHE B O   1 
ATOM   5338 C  CB  . PHE B 1 164 ? -68.839  -6.088  286.087 1.00 19.93  ? 164 PHE B CB  1 
ATOM   5339 C  CG  . PHE B 1 164 ? -68.121  -4.785  286.284 1.00 15.80  ? 164 PHE B CG  1 
ATOM   5340 C  CD1 . PHE B 1 164 ? -67.843  -3.962  285.206 1.00 14.54  ? 164 PHE B CD1 1 
ATOM   5341 C  CD2 . PHE B 1 164 ? -67.714  -4.387  287.546 1.00 16.74  ? 164 PHE B CD2 1 
ATOM   5342 C  CE1 . PHE B 1 164 ? -67.180  -2.764  285.384 1.00 16.51  ? 164 PHE B CE1 1 
ATOM   5343 C  CE2 . PHE B 1 164 ? -67.049  -3.191  287.731 1.00 17.18  ? 164 PHE B CE2 1 
ATOM   5344 C  CZ  . PHE B 1 164 ? -66.782  -2.379  286.648 1.00 18.90  ? 164 PHE B CZ  1 
ATOM   5345 N  N   . PRO B 1 165 ? -72.021  -4.864  284.679 1.00 16.99  ? 165 PRO B N   1 
ATOM   5346 C  CA  . PRO B 1 165 ? -72.536  -4.326  283.418 1.00 19.42  ? 165 PRO B CA  1 
ATOM   5347 C  C   . PRO B 1 165 ? -71.770  -3.068  283.019 1.00 20.89  ? 165 PRO B C   1 
ATOM   5348 O  O   . PRO B 1 165 ? -70.835  -2.636  283.690 1.00 16.65  ? 165 PRO B O   1 
ATOM   5349 C  CB  . PRO B 1 165 ? -73.998  -4.021  283.745 1.00 19.86  ? 165 PRO B CB  1 
ATOM   5350 C  CG  . PRO B 1 165 ? -73.984  -3.720  285.204 1.00 18.39  ? 165 PRO B CG  1 
ATOM   5351 C  CD  . PRO B 1 165 ? -72.945  -4.627  285.801 1.00 16.44  ? 165 PRO B CD  1 
ATOM   5352 N  N   . VAL B 1 166 ? -72.194  -2.475  281.900 1.00 19.56  ? 166 VAL B N   1 
ATOM   5353 C  CA  . VAL B 1 166 ? -71.517  -1.288  281.387 1.00 21.11  ? 166 VAL B CA  1 
ATOM   5354 C  C   . VAL B 1 166 ? -71.689  -0.107  282.334 1.00 19.79  ? 166 VAL B C   1 
ATOM   5355 O  O   . VAL B 1 166 ? -70.781  0.722   282.475 1.00 17.91  ? 166 VAL B O   1 
ATOM   5356 C  CB  . VAL B 1 166 ? -72.028  -0.955  279.974 1.00 21.13  ? 166 VAL B CB  1 
ATOM   5357 C  CG1 . VAL B 1 166 ? -71.299  0.255   279.416 1.00 20.11  ? 166 VAL B CG1 1 
ATOM   5358 C  CG2 . VAL B 1 166 ? -71.860  -2.155  279.056 1.00 20.52  ? 166 VAL B CG2 1 
ATOM   5359 N  N   . ASP B 1 167 ? -72.837  -0.014  283.009 1.00 20.81  ? 167 ASP B N   1 
ATOM   5360 C  CA  . ASP B 1 167 ? -73.098  1.109   283.903 1.00 18.84  ? 167 ASP B CA  1 
ATOM   5361 C  C   . ASP B 1 167 ? -72.154  1.151   285.099 1.00 17.17  ? 167 ASP B C   1 
ATOM   5362 O  O   . ASP B 1 167 ? -72.162  2.145   285.834 1.00 21.69  ? 167 ASP B O   1 
ATOM   5363 C  CB  . ASP B 1 167 ? -74.552  1.071   284.382 1.00 16.49  ? 167 ASP B CB  1 
ATOM   5364 C  CG  . ASP B 1 167 ? -74.920  -0.248  285.031 1.00 15.26  ? 167 ASP B CG  1 
ATOM   5365 O  OD1 . ASP B 1 167 ? -74.544  -0.465  286.201 1.00 13.40  ? 167 ASP B OD1 1 
ATOM   5366 O  OD2 . ASP B 1 167 ? -75.596  -1.064  284.371 1.00 16.72  ? 167 ASP B OD2 1 
ATOM   5367 N  N   . LYS B 1 168 ? -71.348  0.112   285.313 1.00 16.20  ? 168 LYS B N   1 
ATOM   5368 C  CA  . LYS B 1 168 ? -70.323  0.125   286.346 1.00 18.53  ? 168 LYS B CA  1 
ATOM   5369 C  C   . LYS B 1 168 ? -68.954  0.541   285.824 1.00 19.98  ? 168 LYS B C   1 
ATOM   5370 O  O   . LYS B 1 168 ? -68.053  0.792   286.630 1.00 17.75  ? 168 LYS B O   1 
ATOM   5371 C  CB  . LYS B 1 168 ? -70.207  -1.256  287.004 1.00 17.74  ? 168 LYS B CB  1 
ATOM   5372 C  CG  . LYS B 1 168 ? -71.432  -1.691  287.789 1.00 18.04  ? 168 LYS B CG  1 
ATOM   5373 C  CD  . LYS B 1 168 ? -71.161  -2.990  288.533 1.00 21.34  ? 168 LYS B CD  1 
ATOM   5374 C  CE  . LYS B 1 168 ? -72.327  -3.377  289.427 1.00 26.89  ? 168 LYS B CE  1 
ATOM   5375 N  NZ  . LYS B 1 168 ? -72.037  -4.616  290.202 1.00 50.51  ? 168 LYS B NZ  1 
ATOM   5376 N  N   . VAL B 1 169 ? -68.778  0.620   284.509 1.00 18.68  ? 169 VAL B N   1 
ATOM   5377 C  CA  . VAL B 1 169 ? -67.476  0.909   283.913 1.00 17.47  ? 169 VAL B CA  1 
ATOM   5378 C  C   . VAL B 1 169 ? -67.150  2.387   284.095 1.00 19.81  ? 169 VAL B C   1 
ATOM   5379 O  O   . VAL B 1 169 ? -67.892  3.251   283.605 1.00 20.29  ? 169 VAL B O   1 
ATOM   5380 C  CB  . VAL B 1 169 ? -67.445  0.519   282.427 1.00 14.69  ? 169 VAL B CB  1 
ATOM   5381 C  CG1 . VAL B 1 169 ? -66.071  0.786   281.841 1.00 14.62  ? 169 VAL B CG1 1 
ATOM   5382 C  CG2 . VAL B 1 169 ? -67.833  -0.940  282.254 1.00 14.57  ? 169 VAL B CG2 1 
ATOM   5383 N  N   . PRO B 1 170 ? -66.064  2.723   284.790 1.00 18.77  ? 170 PRO B N   1 
ATOM   5384 C  CA  . PRO B 1 170 ? -65.692  4.137   284.943 1.00 19.56  ? 170 PRO B CA  1 
ATOM   5385 C  C   . PRO B 1 170 ? -65.175  4.744   283.648 1.00 19.67  ? 170 PRO B C   1 
ATOM   5386 O  O   . PRO B 1 170 ? -63.967  4.935   283.475 1.00 22.45  ? 170 PRO B O   1 
ATOM   5387 C  CB  . PRO B 1 170 ? -64.603  4.099   286.024 1.00 21.43  ? 170 PRO B CB  1 
ATOM   5388 C  CG  . PRO B 1 170 ? -64.068  2.710   285.980 1.00 21.65  ? 170 PRO B CG  1 
ATOM   5389 C  CD  . PRO B 1 170 ? -65.198  1.825   285.572 1.00 18.76  ? 170 PRO B CD  1 
ATOM   5390 N  N   . LEU B 1 171 ? -66.090  5.052   282.735 1.00 21.05  ? 171 LEU B N   1 
ATOM   5391 C  CA  . LEU B 1 171 ? -65.775  5.638   281.436 1.00 24.15  ? 171 LEU B CA  1 
ATOM   5392 C  C   . LEU B 1 171 ? -65.205  7.056   281.506 1.00 22.02  ? 171 LEU B C   1 
ATOM   5393 O  O   . LEU B 1 171 ? -64.370  7.405   280.661 1.00 21.51  ? 171 LEU B O   1 
ATOM   5394 C  CB  . LEU B 1 171 ? -67.019  5.624   280.547 1.00 21.59  ? 171 LEU B CB  1 
ATOM   5395 C  CG  . LEU B 1 171 ? -67.570  4.229   280.255 1.00 19.80  ? 171 LEU B CG  1 
ATOM   5396 C  CD1 . LEU B 1 171 ? -68.884  4.323   279.509 1.00 38.73  ? 171 LEU B CD1 1 
ATOM   5397 C  CD2 . LEU B 1 171 ? -66.558  3.425   279.459 1.00 25.52  ? 171 LEU B CD2 1 
ATOM   5398 N  N   . PRO B 1 172 ? -65.627  7.915   282.447 1.00 21.83  ? 172 PRO B N   1 
ATOM   5399 C  CA  . PRO B 1 172 ? -64.994  9.244   282.532 1.00 24.68  ? 172 PRO B CA  1 
ATOM   5400 C  C   . PRO B 1 172 ? -63.483  9.200   282.693 1.00 29.07  ? 172 PRO B C   1 
ATOM   5401 O  O   . PRO B 1 172 ? -62.800  10.149  282.286 1.00 37.28  ? 172 PRO B O   1 
ATOM   5402 C  CB  . PRO B 1 172 ? -65.672  9.876   283.753 1.00 26.16  ? 172 PRO B CB  1 
ATOM   5403 C  CG  . PRO B 1 172 ? -67.000  9.247   283.797 1.00 44.62  ? 172 PRO B CG  1 
ATOM   5404 C  CD  . PRO B 1 172 ? -66.817  7.837   283.318 1.00 23.30  ? 172 PRO B CD  1 
ATOM   5405 N  N   . ASN B 1 173 ? -62.936  8.131   283.272 1.00 26.96  ? 173 ASN B N   1 
ATOM   5406 C  CA  . ASN B 1 173 ? -61.496  7.970   283.411 1.00 22.86  ? 173 ASN B CA  1 
ATOM   5407 C  C   . ASN B 1 173 ? -60.901  7.097   282.312 1.00 23.02  ? 173 ASN B C   1 
ATOM   5408 O  O   . ASN B 1 173 ? -59.818  6.531   282.497 1.00 24.44  ? 173 ASN B O   1 
ATOM   5409 C  CB  . ASN B 1 173 ? -61.158  7.395   284.786 1.00 21.97  ? 173 ASN B CB  1 
ATOM   5410 C  CG  . ASN B 1 173 ? -61.559  8.318   285.917 1.00 25.86  ? 173 ASN B CG  1 
ATOM   5411 O  OD1 . ASN B 1 173 ? -61.766  9.514   285.712 1.00 24.99  ? 173 ASN B OD1 1 
ATOM   5412 N  ND2 . ASN B 1 173 ? -61.668  7.769   287.120 1.00 29.15  ? 173 ASN B ND2 1 
ATOM   5413 N  N   . LEU B 1 174 ? -61.584  6.978   281.176 1.00 21.68  ? 174 LEU B N   1 
ATOM   5414 C  CA  . LEU B 1 174 ? -61.110  6.170   280.063 1.00 21.90  ? 174 LEU B CA  1 
ATOM   5415 C  C   . LEU B 1 174 ? -61.294  6.934   278.763 1.00 21.86  ? 174 LEU B C   1 
ATOM   5416 O  O   . LEU B 1 174 ? -62.307  7.612   278.568 1.00 22.92  ? 174 LEU B O   1 
ATOM   5417 C  CB  . LEU B 1 174 ? -61.854  4.830   279.981 1.00 21.58  ? 174 LEU B CB  1 
ATOM   5418 C  CG  . LEU B 1 174 ? -61.693  3.867   281.156 1.00 19.58  ? 174 LEU B CG  1 
ATOM   5419 C  CD1 . LEU B 1 174 ? -62.589  2.655   280.970 1.00 27.19  ? 174 LEU B CD1 1 
ATOM   5420 C  CD2 . LEU B 1 174 ? -60.243  3.443   281.289 1.00 20.43  ? 174 LEU B CD2 1 
ATOM   5421 N  N   . SER B 1 175 ? -60.308  6.820   277.876 1.00 22.26  ? 175 SER B N   1 
ATOM   5422 C  CA  . SER B 1 175 ? -60.415  7.397   276.543 1.00 22.92  ? 175 SER B CA  1 
ATOM   5423 C  C   . SER B 1 175 ? -60.946  6.401   275.525 1.00 24.82  ? 175 SER B C   1 
ATOM   5424 O  O   . SER B 1 175 ? -61.597  6.805   274.554 1.00 22.50  ? 175 SER B O   1 
ATOM   5425 C  CB  . SER B 1 175 ? -59.054  7.921   276.079 1.00 22.22  ? 175 SER B CB  1 
ATOM   5426 O  OG  . SER B 1 175 ? -58.149  6.854   275.858 1.00 22.46  ? 175 SER B OG  1 
ATOM   5427 N  N   . HIS B 1 176 ? -60.685  5.112   275.725 1.00 26.31  ? 176 HIS B N   1 
ATOM   5428 C  CA  . HIS B 1 176 ? -61.144  4.072   274.819 1.00 26.39  ? 176 HIS B CA  1 
ATOM   5429 C  C   . HIS B 1 176 ? -61.709  2.909   275.619 1.00 27.73  ? 176 HIS B C   1 
ATOM   5430 O  O   . HIS B 1 176 ? -61.187  2.563   276.682 1.00 24.83  ? 176 HIS B O   1 
ATOM   5431 C  CB  . HIS B 1 176 ? -60.012  3.580   273.910 1.00 25.15  ? 176 HIS B CB  1 
ATOM   5432 C  CG  . HIS B 1 176 ? -59.536  4.606   272.931 1.00 24.42  ? 176 HIS B CG  1 
ATOM   5433 N  ND1 . HIS B 1 176 ? -58.763  5.685   273.300 1.00 23.84  ? 176 HIS B ND1 1 
ATOM   5434 C  CD2 . HIS B 1 176 ? -59.727  4.719   271.595 1.00 25.92  ? 176 HIS B CD2 1 
ATOM   5435 C  CE1 . HIS B 1 176 ? -58.496  6.418   272.234 1.00 30.26  ? 176 HIS B CE1 1 
ATOM   5436 N  NE2 . HIS B 1 176 ? -59.069  5.854   271.186 1.00 34.17  ? 176 HIS B NE2 1 
ATOM   5437 N  N   . LEU B 1 177 ? -62.781  2.315   275.100 1.00 26.50  ? 177 LEU B N   1 
ATOM   5438 C  CA  . LEU B 1 177 ? -63.412  1.144   275.694 1.00 25.67  ? 177 LEU B CA  1 
ATOM   5439 C  C   . LEU B 1 177 ? -63.386  0.029   274.660 1.00 22.14  ? 177 LEU B C   1 
ATOM   5440 O  O   . LEU B 1 177 ? -63.970  0.166   273.580 1.00 26.56  ? 177 LEU B O   1 
ATOM   5441 C  CB  . LEU B 1 177 ? -64.846  1.455   276.135 1.00 23.56  ? 177 LEU B CB  1 
ATOM   5442 C  CG  . LEU B 1 177 ? -65.562  0.506   277.104 1.00 17.98  ? 177 LEU B CG  1 
ATOM   5443 C  CD1 . LEU B 1 177 ? -66.112  -0.733  276.405 1.00 19.33  ? 177 LEU B CD1 1 
ATOM   5444 C  CD2 . LEU B 1 177 ? -64.638  0.113   278.246 1.00 18.94  ? 177 LEU B CD2 1 
ATOM   5445 N  N   . LEU B 1 178 ? -62.707  -1.067  274.988 1.00 19.56  ? 178 LEU B N   1 
ATOM   5446 C  CA  . LEU B 1 178 ? -62.526  -2.184  274.069 1.00 21.94  ? 178 LEU B CA  1 
ATOM   5447 C  C   . LEU B 1 178 ? -63.496  -3.296  274.453 1.00 21.53  ? 178 LEU B C   1 
ATOM   5448 O  O   . LEU B 1 178 ? -63.354  -3.915  275.513 1.00 21.64  ? 178 LEU B O   1 
ATOM   5449 C  CB  . LEU B 1 178 ? -61.079  -2.669  274.093 1.00 20.90  ? 178 LEU B CB  1 
ATOM   5450 C  CG  . LEU B 1 178 ? -60.055  -1.583  273.748 1.00 24.50  ? 178 LEU B CG  1 
ATOM   5451 C  CD1 . LEU B 1 178 ? -58.638  -2.125  273.787 1.00 20.39  ? 178 LEU B CD1 1 
ATOM   5452 C  CD2 . LEU B 1 178 ? -60.359  -0.975  272.388 1.00 25.12  ? 178 LEU B CD2 1 
ATOM   5453 N  N   . TYR B 1 179 ? -64.478  -3.544  273.590 1.00 21.23  ? 179 TYR B N   1 
ATOM   5454 C  CA  . TYR B 1 179 ? -65.515  -4.540  273.843 1.00 20.38  ? 179 TYR B CA  1 
ATOM   5455 C  C   . TYR B 1 179 ? -65.048  -5.892  273.314 1.00 20.48  ? 179 TYR B C   1 
ATOM   5456 O  O   . TYR B 1 179 ? -64.952  -6.093  272.100 1.00 21.11  ? 179 TYR B O   1 
ATOM   5457 C  CB  . TYR B 1 179 ? -66.830  -4.121  273.191 1.00 19.13  ? 179 TYR B CB  1 
ATOM   5458 C  CG  . TYR B 1 179 ? -67.972  -5.078  273.446 1.00 22.37  ? 179 TYR B CG  1 
ATOM   5459 C  CD1 . TYR B 1 179 ? -68.730  -4.992  274.605 1.00 21.64  ? 179 TYR B CD1 1 
ATOM   5460 C  CD2 . TYR B 1 179 ? -68.293  -6.067  272.525 1.00 22.98  ? 179 TYR B CD2 1 
ATOM   5461 C  CE1 . TYR B 1 179 ? -69.774  -5.864  274.841 1.00 19.77  ? 179 TYR B CE1 1 
ATOM   5462 C  CE2 . TYR B 1 179 ? -69.334  -6.943  272.752 1.00 18.65  ? 179 TYR B CE2 1 
ATOM   5463 C  CZ  . TYR B 1 179 ? -70.071  -6.837  273.912 1.00 17.98  ? 179 TYR B CZ  1 
ATOM   5464 O  OH  . TYR B 1 179 ? -71.110  -7.707  274.141 1.00 21.08  ? 179 TYR B OH  1 
ATOM   5465 N  N   . GLY B 1 180 ? -64.773  -6.819  274.225 1.00 19.74  ? 180 GLY B N   1 
ATOM   5466 C  CA  . GLY B 1 180 ? -64.353  -8.155  273.847 1.00 20.17  ? 180 GLY B CA  1 
ATOM   5467 C  C   . GLY B 1 180 ? -65.313  -9.234  274.309 1.00 19.83  ? 180 GLY B C   1 
ATOM   5468 O  O   . GLY B 1 180 ? -65.769  -9.217  275.453 1.00 17.13  ? 180 GLY B O   1 
ATOM   5469 N  N   . PHE B 1 181 ? -65.620  -10.178 273.423 1.00 21.70  ? 181 PHE B N   1 
ATOM   5470 C  CA  . PHE B 1 181 ? -65.054  -10.200 272.078 1.00 21.43  ? 181 PHE B CA  1 
ATOM   5471 C  C   . PHE B 1 181 ? -66.129  -10.403 271.016 1.00 21.19  ? 181 PHE B C   1 
ATOM   5472 O  O   . PHE B 1 181 ? -67.163  -11.014 271.277 1.00 19.35  ? 181 PHE B O   1 
ATOM   5473 C  CB  . PHE B 1 181 ? -64.000  -11.302 271.960 1.00 18.58  ? 181 PHE B CB  1 
ATOM   5474 C  CG  . PHE B 1 181 ? -62.785  -11.074 272.810 1.00 20.04  ? 181 PHE B CG  1 
ATOM   5475 C  CD1 . PHE B 1 181 ? -61.820  -10.157 272.430 1.00 20.13  ? 181 PHE B CD1 1 
ATOM   5476 C  CD2 . PHE B 1 181 ? -62.605  -11.778 273.989 1.00 21.04  ? 181 PHE B CD2 1 
ATOM   5477 C  CE1 . PHE B 1 181 ? -60.701  -9.945  273.209 1.00 20.26  ? 181 PHE B CE1 1 
ATOM   5478 C  CE2 . PHE B 1 181 ? -61.487  -11.570 274.773 1.00 19.28  ? 181 PHE B CE2 1 
ATOM   5479 C  CZ  . PHE B 1 181 ? -60.534  -10.653 274.381 1.00 20.57  ? 181 PHE B CZ  1 
ATOM   5480 N  N   . ILE B 1 182 ? -65.876  -9.890  269.815 1.00 23.64  ? 182 ILE B N   1 
ATOM   5481 C  CA  . ILE B 1 182 ? -66.766  -10.079 268.675 1.00 22.52  ? 182 ILE B CA  1 
ATOM   5482 C  C   . ILE B 1 182 ? -66.267  -11.296 267.896 1.00 21.53  ? 182 ILE B C   1 
ATOM   5483 O  O   . ILE B 1 182 ? -65.186  -11.221 267.288 1.00 20.40  ? 182 ILE B O   1 
ATOM   5484 C  CB  . ILE B 1 182 ? -66.815  -8.833  267.784 1.00 22.08  ? 182 ILE B CB  1 
ATOM   5485 C  CG1 . ILE B 1 182 ? -67.449  -7.668  268.543 1.00 24.85  ? 182 ILE B CG1 1 
ATOM   5486 C  CG2 . ILE B 1 182 ? -67.583  -9.121  266.505 1.00 22.15  ? 182 ILE B CG2 1 
ATOM   5487 C  CD1 . ILE B 1 182 ? -68.820  -7.980  269.094 1.00 20.66  ? 182 ILE B CD1 1 
ATOM   5488 N  N   . PRO B 1 183 ? -66.999  -12.403 267.883 1.00 24.16  ? 183 PRO B N   1 
ATOM   5489 C  CA  . PRO B 1 183 ? -66.478  -13.635 267.286 1.00 26.82  ? 183 PRO B CA  1 
ATOM   5490 C  C   . PRO B 1 183 ? -66.568  -13.616 265.766 1.00 30.50  ? 183 PRO B C   1 
ATOM   5491 O  O   . PRO B 1 183 ? -67.105  -12.696 265.150 1.00 29.31  ? 183 PRO B O   1 
ATOM   5492 C  CB  . PRO B 1 183 ? -67.393  -14.711 267.874 1.00 25.46  ? 183 PRO B CB  1 
ATOM   5493 C  CG  . PRO B 1 183 ? -68.683  -14.010 268.049 1.00 26.12  ? 183 PRO B CG  1 
ATOM   5494 C  CD  . PRO B 1 183 ? -68.340  -12.600 268.459 1.00 25.30  ? 183 PRO B CD  1 
ATOM   5495 N  N   . ILE B 1 184 ? -66.020  -14.671 265.171 1.00 34.46  ? 184 ILE B N   1 
ATOM   5496 C  CA  . ILE B 1 184 ? -66.058  -14.899 263.733 1.00 32.75  ? 184 ILE B CA  1 
ATOM   5497 C  C   . ILE B 1 184 ? -66.706  -16.255 263.495 1.00 32.61  ? 184 ILE B C   1 
ATOM   5498 O  O   . ILE B 1 184 ? -66.286  -17.258 264.083 1.00 34.49  ? 184 ILE B O   1 
ATOM   5499 C  CB  . ILE B 1 184 ? -64.650  -14.847 263.112 1.00 32.25  ? 184 ILE B CB  1 
ATOM   5500 C  CG1 . ILE B 1 184 ? -63.951  -13.538 263.481 1.00 30.15  ? 184 ILE B CG1 1 
ATOM   5501 C  CG2 . ILE B 1 184 ? -64.732  -14.989 261.609 1.00 35.07  ? 184 ILE B CG2 1 
ATOM   5502 C  CD1 . ILE B 1 184 ? -62.564  -13.405 262.895 1.00 28.76  ? 184 ILE B CD1 1 
ATOM   5503 N  N   . CYS B 1 185 ? -67.725  -16.281 262.640 1.00 35.07  ? 185 CYS B N   1 
ATOM   5504 C  CA  . CYS B 1 185 ? -68.502  -17.494 262.429 1.00 36.37  ? 185 CYS B CA  1 
ATOM   5505 C  C   . CYS B 1 185 ? -67.652  -18.594 261.801 1.00 37.30  ? 185 CYS B C   1 
ATOM   5506 O  O   . CYS B 1 185 ? -66.741  -18.337 261.010 1.00 39.20  ? 185 CYS B O   1 
ATOM   5507 C  CB  . CYS B 1 185 ? -69.714  -17.204 261.544 1.00 39.74  ? 185 CYS B CB  1 
ATOM   5508 S  SG  . CYS B 1 185 ? -71.023  -16.237 262.338 1.00 46.00  ? 185 CYS B SG  1 
ATOM   5509 N  N   . GLY B 1 186 ? -67.967  -19.835 262.166 1.00 37.45  ? 186 GLY B N   1 
ATOM   5510 C  CA  . GLY B 1 186 ? -67.249  -20.992 261.668 1.00 38.03  ? 186 GLY B CA  1 
ATOM   5511 C  C   . GLY B 1 186 ? -67.548  -22.248 262.461 1.00 37.03  ? 186 GLY B C   1 
ATOM   5512 O  O   . GLY B 1 186 ? -67.764  -22.184 263.675 1.00 34.51  ? 186 GLY B O   1 
ATOM   5513 N  N   . GLY B 1 187 ? -67.562  -23.391 261.791 1.00 44.24  ? 187 GLY B N   1 
ATOM   5514 C  CA  . GLY B 1 187 ? -67.867  -24.673 262.410 1.00 39.79  ? 187 GLY B CA  1 
ATOM   5515 C  C   . GLY B 1 187 ? -66.620  -25.416 262.838 1.00 30.29  ? 187 GLY B C   1 
ATOM   5516 O  O   . GLY B 1 187 ? -65.673  -24.827 263.372 1.00 32.45  ? 187 GLY B O   1 
ATOM   5517 N  N   . ASP B 1 188 ? -66.620  -26.727 262.608 1.00 25.97  ? 188 ASP B N   1 
ATOM   5518 C  CA  . ASP B 1 188 ? -65.466  -27.547 262.947 1.00 26.66  ? 188 ASP B CA  1 
ATOM   5519 C  C   . ASP B 1 188 ? -64.281  -27.192 262.061 1.00 28.10  ? 188 ASP B C   1 
ATOM   5520 O  O   . ASP B 1 188 ? -64.424  -27.002 260.850 1.00 39.94  ? 188 ASP B O   1 
ATOM   5521 C  CB  . ASP B 1 188 ? -65.803  -29.031 262.801 1.00 29.55  ? 188 ASP B CB  1 
ATOM   5522 C  CG  . ASP B 1 188 ? -66.796  -29.508 263.840 1.00 31.26  ? 188 ASP B CG  1 
ATOM   5523 O  OD1 . ASP B 1 188 ? -66.690  -29.078 265.007 1.00 44.56  ? 188 ASP B OD1 1 
ATOM   5524 O  OD2 . ASP B 1 188 ? -67.683  -30.314 263.489 1.00 33.52  ? 188 ASP B OD2 1 
ATOM   5525 N  N   . GLY B 1 189 ? -63.101  -27.105 262.673 1.00 28.78  ? 189 GLY B N   1 
ATOM   5526 C  CA  . GLY B 1 189 ? -61.901  -26.709 261.973 1.00 30.02  ? 189 GLY B CA  1 
ATOM   5527 C  C   . GLY B 1 189 ? -61.696  -25.217 261.843 1.00 28.80  ? 189 GLY B C   1 
ATOM   5528 O  O   . GLY B 1 189 ? -60.578  -24.785 261.540 1.00 29.08  ? 189 GLY B O   1 
ATOM   5529 N  N   . ILE B 1 190 ? -62.734  -24.412 262.061 1.00 30.28  ? 190 ILE B N   1 
ATOM   5530 C  CA  . ILE B 1 190 ? -62.607  -22.962 261.981 1.00 28.94  ? 190 ILE B CA  1 
ATOM   5531 C  C   . ILE B 1 190 ? -62.557  -22.305 263.359 1.00 28.53  ? 190 ILE B C   1 
ATOM   5532 O  O   . ILE B 1 190 ? -62.008  -21.201 263.485 1.00 29.47  ? 190 ILE B O   1 
ATOM   5533 C  CB  . ILE B 1 190 ? -63.753  -22.363 261.138 1.00 29.55  ? 190 ILE B CB  1 
ATOM   5534 C  CG1 . ILE B 1 190 ? -63.961  -23.190 259.868 1.00 33.26  ? 190 ILE B CG1 1 
ATOM   5535 C  CG2 . ILE B 1 190 ? -63.461  -20.916 260.769 1.00 33.63  ? 190 ILE B CG2 1 
ATOM   5536 C  CD1 . ILE B 1 190 ? -65.102  -22.709 259.001 1.00 51.15  ? 190 ILE B CD1 1 
ATOM   5537 N  N   . ASN B 1 191 ? -63.097  -22.950 264.389 1.00 28.84  ? 191 ASN B N   1 
ATOM   5538 C  CA  . ASN B 1 191 ? -63.089  -22.422 265.751 1.00 30.26  ? 191 ASN B CA  1 
ATOM   5539 C  C   . ASN B 1 191 ? -62.924  -23.562 266.748 1.00 28.17  ? 191 ASN B C   1 
ATOM   5540 O  O   . ASN B 1 191 ? -63.661  -23.675 267.728 1.00 28.18  ? 191 ASN B O   1 
ATOM   5541 C  CB  . ASN B 1 191 ? -64.361  -21.629 266.043 1.00 30.23  ? 191 ASN B CB  1 
ATOM   5542 C  CG  . ASN B 1 191 ? -64.337  -20.246 265.431 1.00 32.61  ? 191 ASN B CG  1 
ATOM   5543 O  OD1 . ASN B 1 191 ? -63.645  -19.353 265.917 1.00 33.13  ? 191 ASN B OD1 1 
ATOM   5544 N  ND2 . ASN B 1 191 ? -65.094  -20.062 264.358 1.00 44.11  ? 191 ASN B ND2 1 
ATOM   5545 N  N   . ASP B 1 192 ? -61.940  -24.429 266.498 1.00 29.17  ? 192 ASP B N   1 
ATOM   5546 C  CA  . ASP B 1 192 ? -61.696  -25.559 267.387 1.00 32.44  ? 192 ASP B CA  1 
ATOM   5547 C  C   . ASP B 1 192 ? -61.169  -25.128 268.750 1.00 29.81  ? 192 ASP B C   1 
ATOM   5548 O  O   . ASP B 1 192 ? -61.251  -25.908 269.705 1.00 27.16  ? 192 ASP B O   1 
ATOM   5549 C  CB  . ASP B 1 192 ? -60.714  -26.540 266.742 1.00 41.00  ? 192 ASP B CB  1 
ATOM   5550 C  CG  . ASP B 1 192 ? -61.252  -27.153 265.463 1.00 34.21  ? 192 ASP B CG  1 
ATOM   5551 O  OD1 . ASP B 1 192 ? -62.485  -27.138 265.264 1.00 27.39  ? 192 ASP B OD1 1 
ATOM   5552 O  OD2 . ASP B 1 192 ? -60.441  -27.661 264.662 1.00 36.19  ? 192 ASP B OD2 1 
ATOM   5553 N  N   . ALA B 1 193 ? -60.627  -23.914 268.864 1.00 28.79  ? 193 ALA B N   1 
ATOM   5554 C  CA  . ALA B 1 193 ? -60.155  -23.435 270.158 1.00 25.70  ? 193 ALA B CA  1 
ATOM   5555 C  C   . ALA B 1 193 ? -61.300  -23.156 271.121 1.00 25.14  ? 193 ALA B C   1 
ATOM   5556 O  O   . ALA B 1 193 ? -61.074  -23.104 272.334 1.00 26.96  ? 193 ALA B O   1 
ATOM   5557 C  CB  . ALA B 1 193 ? -59.308  -22.175 269.982 1.00 23.71  ? 193 ALA B CB  1 
ATOM   5558 N  N   . LEU B 1 194 ? -62.520  -22.977 270.610 1.00 24.88  ? 194 LEU B N   1 
ATOM   5559 C  CA  . LEU B 1 194 ? -63.663  -22.720 271.477 1.00 27.19  ? 194 LEU B CA  1 
ATOM   5560 C  C   . LEU B 1 194 ? -64.108  -23.962 272.234 1.00 30.87  ? 194 LEU B C   1 
ATOM   5561 O  O   . LEU B 1 194 ? -64.760  -23.836 273.276 1.00 46.10  ? 194 LEU B O   1 
ATOM   5562 C  CB  . LEU B 1 194 ? -64.830  -22.170 270.658 1.00 27.53  ? 194 LEU B CB  1 
ATOM   5563 C  CG  . LEU B 1 194 ? -64.748  -20.697 270.268 1.00 26.17  ? 194 LEU B CG  1 
ATOM   5564 C  CD1 . LEU B 1 194 ? -65.889  -20.345 269.335 1.00 28.01  ? 194 LEU B CD1 1 
ATOM   5565 C  CD2 . LEU B 1 194 ? -64.768  -19.814 271.504 1.00 26.38  ? 194 LEU B CD2 1 
ATOM   5566 N  N   . LYS B 1 195 ? -63.775  -25.153 271.735 1.00 27.01  ? 195 LYS B N   1 
ATOM   5567 C  CA  . LYS B 1 195 ? -64.157  -26.389 272.406 1.00 27.83  ? 195 LYS B CA  1 
ATOM   5568 C  C   . LYS B 1 195 ? -63.448  -26.578 273.740 1.00 25.34  ? 195 LYS B C   1 
ATOM   5569 O  O   . LYS B 1 195 ? -63.845  -27.457 274.513 1.00 23.56  ? 195 LYS B O   1 
ATOM   5570 C  CB  . LYS B 1 195 ? -63.880  -27.582 271.489 1.00 30.89  ? 195 LYS B CB  1 
ATOM   5571 C  CG  . LYS B 1 195 ? -64.582  -27.488 270.142 1.00 30.36  ? 195 LYS B CG  1 
ATOM   5572 C  CD  . LYS B 1 195 ? -64.097  -28.557 269.177 1.00 42.08  ? 195 LYS B CD  1 
ATOM   5573 C  CE  . LYS B 1 195 ? -64.890  -28.523 267.880 1.00 37.45  ? 195 LYS B CE  1 
ATOM   5574 N  NZ  . LYS B 1 195 ? -64.352  -29.477 266.871 1.00 39.60  ? 195 LYS B NZ  1 
ATOM   5575 N  N   . THR B 1 196 ? -62.416  -25.782 274.028 1.00 26.31  ? 196 THR B N   1 
ATOM   5576 C  CA  . THR B 1 196 ? -61.764  -25.854 275.331 1.00 27.07  ? 196 THR B CA  1 
ATOM   5577 C  C   . THR B 1 196 ? -62.688  -25.370 276.442 1.00 29.05  ? 196 THR B C   1 
ATOM   5578 O  O   . THR B 1 196 ? -62.572  -25.823 277.586 1.00 31.90  ? 196 THR B O   1 
ATOM   5579 C  CB  . THR B 1 196 ? -60.472  -25.035 275.313 1.00 27.94  ? 196 THR B CB  1 
ATOM   5580 O  OG1 . THR B 1 196 ? -59.696  -25.393 274.162 1.00 23.58  ? 196 THR B OG1 1 
ATOM   5581 C  CG2 . THR B 1 196 ? -59.648  -25.295 276.565 1.00 36.86  ? 196 THR B CG2 1 
ATOM   5582 N  N   . ILE B 1 197 ? -63.611  -24.465 276.126 1.00 31.40  ? 197 ILE B N   1 
ATOM   5583 C  CA  . ILE B 1 197 ? -64.577  -23.946 277.086 1.00 31.50  ? 197 ILE B CA  1 
ATOM   5584 C  C   . ILE B 1 197 ? -65.911  -24.638 276.847 1.00 36.72  ? 197 ILE B C   1 
ATOM   5585 O  O   . ILE B 1 197 ? -66.369  -24.742 275.702 1.00 48.52  ? 197 ILE B O   1 
ATOM   5586 C  CB  . ILE B 1 197 ? -64.717  -22.419 276.965 1.00 31.89  ? 197 ILE B CB  1 
ATOM   5587 C  CG1 . ILE B 1 197 ? -63.343  -21.752 277.048 1.00 33.30  ? 197 ILE B CG1 1 
ATOM   5588 C  CG2 . ILE B 1 197 ? -65.638  -21.880 278.047 1.00 36.24  ? 197 ILE B CG2 1 
ATOM   5589 C  CD1 . ILE B 1 197 ? -63.385  -20.253 276.877 1.00 35.87  ? 197 ILE B CD1 1 
ATOM   5590 N  N   . SER B 1 198 ? -66.534  -25.110 277.924 1.00 36.93  ? 198 SER B N   1 
ATOM   5591 C  CA  . SER B 1 198 ? -67.773  -25.866 277.806 1.00 46.76  ? 198 SER B CA  1 
ATOM   5592 C  C   . SER B 1 198 ? -68.909  -24.967 277.333 1.00 35.53  ? 198 SER B C   1 
ATOM   5593 O  O   . SER B 1 198 ? -69.145  -23.894 277.896 1.00 34.50  ? 198 SER B O   1 
ATOM   5594 C  CB  . SER B 1 198 ? -68.129  -26.506 279.147 1.00 45.56  ? 198 SER B CB  1 
ATOM   5595 O  OG  . SER B 1 198 ? -66.979  -27.056 279.767 1.00 51.61  ? 198 SER B OG  1 
ATOM   5596 N  N   . GLY B 1 199 ? -69.613  -25.409 276.291 1.00 36.02  ? 199 GLY B N   1 
ATOM   5597 C  CA  . GLY B 1 199 ? -70.724  -24.664 275.739 1.00 32.42  ? 199 GLY B CA  1 
ATOM   5598 C  C   . GLY B 1 199 ? -70.356  -23.427 274.952 1.00 32.11  ? 199 GLY B C   1 
ATOM   5599 O  O   . GLY B 1 199 ? -71.245  -22.814 274.350 1.00 31.06  ? 199 GLY B O   1 
ATOM   5600 N  N   . SER B 1 200 ? -69.080  -23.035 274.931 1.00 34.26  ? 200 SER B N   1 
ATOM   5601 C  CA  . SER B 1 200 ? -68.690  -21.838 274.194 1.00 31.79  ? 200 SER B CA  1 
ATOM   5602 C  C   . SER B 1 200 ? -68.731  -22.075 272.691 1.00 29.80  ? 200 SER B C   1 
ATOM   5603 O  O   . SER B 1 200 ? -69.216  -21.224 271.936 1.00 27.47  ? 200 SER B O   1 
ATOM   5604 C  CB  . SER B 1 200 ? -67.297  -21.386 274.629 1.00 30.51  ? 200 SER B CB  1 
ATOM   5605 O  OG  . SER B 1 200 ? -66.897  -20.224 273.927 1.00 31.69  ? 200 SER B OG  1 
ATOM   5606 N  N   . PHE B 1 201 ? -68.223  -23.223 272.236 1.00 30.91  ? 201 PHE B N   1 
ATOM   5607 C  CA  . PHE B 1 201 ? -68.274  -23.536 270.811 1.00 31.69  ? 201 PHE B CA  1 
ATOM   5608 C  C   . PHE B 1 201 ? -69.712  -23.707 270.340 1.00 33.59  ? 201 PHE B C   1 
ATOM   5609 O  O   . PHE B 1 201 ? -70.065  -23.286 269.232 1.00 42.92  ? 201 PHE B O   1 
ATOM   5610 C  CB  . PHE B 1 201 ? -67.458  -24.796 270.519 1.00 28.24  ? 201 PHE B CB  1 
ATOM   5611 C  CG  . PHE B 1 201 ? -67.502  -25.230 269.079 1.00 32.60  ? 201 PHE B CG  1 
ATOM   5612 C  CD1 . PHE B 1 201 ? -66.651  -24.664 268.145 1.00 31.85  ? 201 PHE B CD1 1 
ATOM   5613 C  CD2 . PHE B 1 201 ? -68.391  -26.208 268.662 1.00 32.75  ? 201 PHE B CD2 1 
ATOM   5614 C  CE1 . PHE B 1 201 ? -66.689  -25.061 266.821 1.00 29.92  ? 201 PHE B CE1 1 
ATOM   5615 C  CE2 . PHE B 1 201 ? -68.433  -26.607 267.339 1.00 29.98  ? 201 PHE B CE2 1 
ATOM   5616 C  CZ  . PHE B 1 201 ? -67.581  -26.033 266.419 1.00 27.16  ? 201 PHE B CZ  1 
ATOM   5617 N  N   . GLU B 1 202 ? -70.558  -24.319 271.172 1.00 40.11  ? 202 GLU B N   1 
ATOM   5618 C  CA  . GLU B 1 202 ? -71.953  -24.518 270.794 1.00 33.36  ? 202 GLU B CA  1 
ATOM   5619 C  C   . GLU B 1 202 ? -72.709  -23.198 270.726 1.00 31.41  ? 202 GLU B C   1 
ATOM   5620 O  O   . GLU B 1 202 ? -73.622  -23.051 269.905 1.00 32.63  ? 202 GLU B O   1 
ATOM   5621 C  CB  . GLU B 1 202 ? -72.641  -25.466 271.778 1.00 35.98  ? 202 GLU B CB  1 
ATOM   5622 C  CG  . GLU B 1 202 ? -72.037  -26.865 271.859 1.00 40.42  ? 202 GLU B CG  1 
ATOM   5623 C  CD  . GLU B 1 202 ? -70.783  -26.923 272.714 1.00 34.07  ? 202 GLU B CD  1 
ATOM   5624 O  OE1 . GLU B 1 202 ? -69.749  -26.355 272.302 1.00 35.35  ? 202 GLU B OE1 1 
ATOM   5625 O  OE2 . GLU B 1 202 ? -70.832  -27.534 273.801 1.00 34.25  ? 202 GLU B OE2 1 
ATOM   5626 N  N   . SER B 1 203 ? -72.347  -22.233 271.575 1.00 35.79  ? 203 SER B N   1 
ATOM   5627 C  CA  . SER B 1 203 ? -73.047  -20.953 271.583 1.00 30.05  ? 203 SER B CA  1 
ATOM   5628 C  C   . SER B 1 203 ? -72.800  -20.176 270.296 1.00 27.91  ? 203 SER B C   1 
ATOM   5629 O  O   . SER B 1 203 ? -73.716  -19.538 269.765 1.00 28.77  ? 203 SER B O   1 
ATOM   5630 C  CB  . SER B 1 203 ? -72.621  -20.128 272.796 1.00 31.21  ? 203 SER B CB  1 
ATOM   5631 O  OG  . SER B 1 203 ? -72.863  -20.833 274.001 1.00 52.48  ? 203 SER B OG  1 
ATOM   5632 N  N   . LEU B 1 204 ? -71.569  -20.216 269.779 1.00 30.87  ? 204 LEU B N   1 
ATOM   5633 C  CA  . LEU B 1 204 ? -71.277  -19.511 268.536 1.00 27.83  ? 204 LEU B CA  1 
ATOM   5634 C  C   . LEU B 1 204 ? -72.005  -20.145 267.358 1.00 29.04  ? 204 LEU B C   1 
ATOM   5635 O  O   . LEU B 1 204 ? -72.515  -19.436 266.484 1.00 29.79  ? 204 LEU B O   1 
ATOM   5636 C  CB  . LEU B 1 204 ? -69.771  -19.484 268.282 1.00 27.97  ? 204 LEU B CB  1 
ATOM   5637 C  CG  . LEU B 1 204 ? -69.374  -18.708 267.026 1.00 30.51  ? 204 LEU B CG  1 
ATOM   5638 C  CD1 . LEU B 1 204 ? -69.859  -17.275 267.132 1.00 32.57  ? 204 LEU B CD1 1 
ATOM   5639 C  CD2 . LEU B 1 204 ? -67.875  -18.754 266.793 1.00 58.76  ? 204 LEU B CD2 1 
ATOM   5640 N  N   . GLN B 1 205 ? -72.060  -21.478 267.316 1.00 31.35  ? 205 GLN B N   1 
ATOM   5641 C  CA  . GLN B 1 205 ? -72.815  -22.156 266.267 1.00 31.57  ? 205 GLN B CA  1 
ATOM   5642 C  C   . GLN B 1 205 ? -74.292  -21.794 266.343 1.00 29.91  ? 205 GLN B C   1 
ATOM   5643 O  O   . GLN B 1 205 ? -74.924  -21.493 265.324 1.00 28.23  ? 205 GLN B O   1 
ATOM   5644 C  CB  . GLN B 1 205 ? -72.625  -23.670 266.377 1.00 34.20  ? 205 GLN B CB  1 
ATOM   5645 C  CG  . GLN B 1 205 ? -71.176  -24.126 266.346 1.00 41.28  ? 205 GLN B CG  1 
ATOM   5646 C  CD  . GLN B 1 205 ? -70.442  -23.655 265.108 1.00 44.78  ? 205 GLN B CD  1 
ATOM   5647 O  OE1 . GLN B 1 205 ? -70.941  -23.784 263.990 1.00 37.09  ? 205 GLN B OE1 1 
ATOM   5648 N  NE2 . GLN B 1 205 ? -69.248  -23.107 265.300 1.00 42.83  ? 205 GLN B NE2 1 
ATOM   5649 N  N   . ARG B 1 206 ? -74.859  -21.815 267.552 1.00 29.75  ? 206 ARG B N   1 
ATOM   5650 C  CA  . ARG B 1 206 ? -76.247  -21.403 267.725 1.00 29.14  ? 206 ARG B CA  1 
ATOM   5651 C  C   . ARG B 1 206 ? -76.430  -19.926 267.405 1.00 28.03  ? 206 ARG B C   1 
ATOM   5652 O  O   . ARG B 1 206 ? -77.527  -19.503 267.023 1.00 36.71  ? 206 ARG B O   1 
ATOM   5653 C  CB  . ARG B 1 206 ? -76.705  -21.711 269.151 1.00 32.76  ? 206 ARG B CB  1 
ATOM   5654 C  CG  . ARG B 1 206 ? -78.203  -21.584 269.373 1.00 40.50  ? 206 ARG B CG  1 
ATOM   5655 C  CD  . ARG B 1 206 ? -78.618  -22.150 270.724 1.00 38.34  ? 206 ARG B CD  1 
ATOM   5656 N  NE  . ARG B 1 206 ? -78.063  -21.394 271.844 1.00 52.94  ? 206 ARG B NE  1 
ATOM   5657 C  CZ  . ARG B 1 206 ? -77.031  -21.794 272.580 1.00 58.59  ? 206 ARG B CZ  1 
ATOM   5658 N  NH1 . ARG B 1 206 ? -76.433  -22.949 272.317 1.00 49.99  ? 206 ARG B NH1 1 
ATOM   5659 N  NH2 . ARG B 1 206 ? -76.595  -21.041 273.581 1.00 49.01  ? 206 ARG B NH2 1 
ATOM   5660 N  N   . SER B 1 207 ? -75.370  -19.128 267.547 1.00 25.90  ? 207 SER B N   1 
ATOM   5661 C  CA  . SER B 1 207 ? -75.438  -17.723 267.168 1.00 26.42  ? 207 SER B CA  1 
ATOM   5662 C  C   . SER B 1 207 ? -75.185  -17.523 265.679 1.00 25.98  ? 207 SER B C   1 
ATOM   5663 O  O   . SER B 1 207 ? -75.692  -16.560 265.093 1.00 25.49  ? 207 SER B O   1 
ATOM   5664 C  CB  . SER B 1 207 ? -74.436  -16.908 267.986 1.00 31.23  ? 207 SER B CB  1 
ATOM   5665 O  OG  . SER B 1 207 ? -74.452  -15.545 267.602 1.00 51.68  ? 207 SER B OG  1 
ATOM   5666 N  N   . CYS B 1 208 ? -74.410  -18.411 265.055 1.00 28.71  ? 208 CYS B N   1 
ATOM   5667 C  CA  . CYS B 1 208 ? -74.117  -18.343 263.628 1.00 35.62  ? 208 CYS B CA  1 
ATOM   5668 C  C   . CYS B 1 208 ? -74.949  -19.330 262.816 1.00 27.21  ? 208 CYS B C   1 
ATOM   5669 O  O   . CYS B 1 208 ? -74.521  -19.756 261.737 1.00 37.49  ? 208 CYS B O   1 
ATOM   5670 C  CB  . CYS B 1 208 ? -72.629  -18.585 263.371 1.00 38.32  ? 208 CYS B CB  1 
ATOM   5671 S  SG  . CYS B 1 208 ? -71.504  -17.315 263.993 1.00 31.09  ? 208 CYS B SG  1 
ATOM   5672 N  N   . LYS B 1 209 ? -76.125  -19.709 263.310 1.00 24.01  ? 209 LYS B N   1 
ATOM   5673 C  CA  . LYS B 1 209 ? -76.966  -20.647 262.577 1.00 24.55  ? 209 LYS B CA  1 
ATOM   5674 C  C   . LYS B 1 209 ? -77.460  -20.004 261.288 1.00 24.15  ? 209 LYS B C   1 
ATOM   5675 O  O   . LYS B 1 209 ? -77.990  -18.888 261.301 1.00 20.46  ? 209 LYS B O   1 
ATOM   5676 C  CB  . LYS B 1 209 ? -78.148  -21.097 263.434 1.00 22.97  ? 209 LYS B CB  1 
ATOM   5677 C  CG  . LYS B 1 209 ? -78.631  -22.500 263.104 1.00 22.13  ? 209 LYS B CG  1 
ATOM   5678 C  CD  . LYS B 1 209 ? -79.782  -22.929 263.996 1.00 27.15  ? 209 LYS B CD  1 
ATOM   5679 C  CE  . LYS B 1 209 ? -81.117  -22.480 263.425 1.00 43.05  ? 209 LYS B CE  1 
ATOM   5680 N  NZ  . LYS B 1 209 ? -82.263  -23.154 264.095 1.00 24.40  ? 209 LYS B NZ  1 
ATOM   5681 N  N   . GLY B 1 210 ? -77.275  -20.706 260.171 1.00 28.61  ? 210 GLY B N   1 
ATOM   5682 C  CA  . GLY B 1 210 ? -77.609  -20.177 258.866 1.00 28.83  ? 210 GLY B CA  1 
ATOM   5683 C  C   . GLY B 1 210 ? -76.683  -19.097 258.355 1.00 28.11  ? 210 GLY B C   1 
ATOM   5684 O  O   . GLY B 1 210 ? -76.743  -18.770 257.163 1.00 30.48  ? 210 GLY B O   1 
ATOM   5685 N  N   . ARG B 1 211 ? -75.832  -18.533 259.207 1.00 29.31  ? 211 ARG B N   1 
ATOM   5686 C  CA  . ARG B 1 211 ? -74.901  -17.489 258.808 1.00 32.29  ? 211 ARG B CA  1 
ATOM   5687 C  C   . ARG B 1 211 ? -73.617  -18.127 258.297 1.00 30.46  ? 211 ARG B C   1 
ATOM   5688 O  O   . ARG B 1 211 ? -73.175  -19.157 258.813 1.00 31.82  ? 211 ARG B O   1 
ATOM   5689 C  CB  . ARG B 1 211 ? -74.609  -16.564 259.989 1.00 33.57  ? 211 ARG B CB  1 
ATOM   5690 C  CG  . ARG B 1 211 ? -74.194  -15.156 259.609 1.00 36.39  ? 211 ARG B CG  1 
ATOM   5691 C  CD  . ARG B 1 211 ? -73.704  -14.395 260.832 1.00 36.63  ? 211 ARG B CD  1 
ATOM   5692 N  NE  . ARG B 1 211 ? -73.764  -12.947 260.649 1.00 37.14  ? 211 ARG B NE  1 
ATOM   5693 C  CZ  . ARG B 1 211 ? -72.943  -12.249 259.872 1.00 40.40  ? 211 ARG B CZ  1 
ATOM   5694 N  NH1 . ARG B 1 211 ? -71.984  -12.858 259.191 1.00 42.65  ? 211 ARG B NH1 1 
ATOM   5695 N  NH2 . ARG B 1 211 ? -73.083  -10.935 259.775 1.00 40.42  ? 211 ARG B NH2 1 
ATOM   5696 N  N   . GLU B 1 212 ? -73.022  -17.514 257.280 1.00 34.20  ? 212 GLU B N   1 
ATOM   5697 C  CA  . GLU B 1 212 ? -71.904  -18.142 256.595 1.00 41.85  ? 212 GLU B CA  1 
ATOM   5698 C  C   . GLU B 1 212 ? -70.580  -17.796 257.272 1.00 47.03  ? 212 GLU B C   1 
ATOM   5699 O  O   . GLU B 1 212 ? -70.477  -16.845 258.051 1.00 49.32  ? 212 GLU B O   1 
ATOM   5700 C  CB  . GLU B 1 212 ? -71.886  -17.744 255.120 1.00 47.36  ? 212 GLU B CB  1 
ATOM   5701 C  CG  . GLU B 1 212 ? -72.546  -18.790 254.230 1.00 63.21  ? 212 GLU B CG  1 
ATOM   5702 C  CD  . GLU B 1 212 ? -71.985  -18.822 252.824 1.00 64.64  ? 212 GLU B CD  1 
ATOM   5703 O  OE1 . GLU B 1 212 ? -71.082  -18.016 252.522 1.00 65.59  ? 212 GLU B OE1 1 
ATOM   5704 O  OE2 . GLU B 1 212 ? -72.452  -19.657 252.020 1.00 56.46  ? 212 GLU B OE2 1 
ATOM   5705 N  N   . ASP B 1 213 ? -69.560  -18.588 256.953 1.00 62.76  ? 213 ASP B N   1 
ATOM   5706 C  CA  . ASP B 1 213 ? -68.335  -18.661 257.734 1.00 55.08  ? 213 ASP B CA  1 
ATOM   5707 C  C   . ASP B 1 213 ? -67.437  -17.447 257.496 1.00 51.39  ? 213 ASP B C   1 
ATOM   5708 O  O   . ASP B 1 213 ? -67.639  -16.652 256.574 1.00 60.36  ? 213 ASP B O   1 
ATOM   5709 C  CB  . ASP B 1 213 ? -67.576  -19.944 257.400 1.00 57.27  ? 213 ASP B CB  1 
ATOM   5710 C  CG  . ASP B 1 213 ? -68.430  -21.183 257.567 1.00 56.64  ? 213 ASP B CG  1 
ATOM   5711 O  OD1 . ASP B 1 213 ? -69.219  -21.486 256.648 1.00 63.58  ? 213 ASP B OD1 1 
ATOM   5712 O  OD2 . ASP B 1 213 ? -68.313  -21.854 258.613 1.00 51.43  ? 213 ASP B OD2 1 
ATOM   5713 N  N   . PHE B 1 214 ? -66.423  -17.323 258.359 1.00 46.54  ? 214 PHE B N   1 
ATOM   5714 C  CA  . PHE B 1 214 ? -65.405  -16.275 258.266 1.00 47.09  ? 214 PHE B CA  1 
ATOM   5715 C  C   . PHE B 1 214 ? -66.032  -14.885 258.271 1.00 44.26  ? 214 PHE B C   1 
ATOM   5716 O  O   . PHE B 1 214 ? -65.627  -13.998 257.518 1.00 45.64  ? 214 PHE B O   1 
ATOM   5717 C  CB  . PHE B 1 214 ? -64.520  -16.469 257.034 1.00 49.81  ? 214 PHE B CB  1 
ATOM   5718 C  CG  . PHE B 1 214 ? -63.693  -17.717 257.081 1.00 64.05  ? 214 PHE B CG  1 
ATOM   5719 C  CD1 . PHE B 1 214 ? -62.479  -17.733 257.744 1.00 47.74  ? 214 PHE B CD1 1 
ATOM   5720 C  CD2 . PHE B 1 214 ? -64.134  -18.877 256.467 1.00 76.30  ? 214 PHE B CD2 1 
ATOM   5721 C  CE1 . PHE B 1 214 ? -61.719  -18.883 257.792 1.00 46.47  ? 214 PHE B CE1 1 
ATOM   5722 C  CE2 . PHE B 1 214 ? -63.377  -20.030 256.511 1.00 61.04  ? 214 PHE B CE2 1 
ATOM   5723 C  CZ  . PHE B 1 214 ? -62.168  -20.034 257.173 1.00 59.38  ? 214 PHE B CZ  1 
ATOM   5724 N  N   . LYS B 1 215 ? -67.022  -14.692 259.138 1.00 51.55  ? 215 LYS B N   1 
ATOM   5725 C  CA  . LYS B 1 215 ? -67.776  -13.450 259.177 1.00 43.99  ? 215 LYS B CA  1 
ATOM   5726 C  C   . LYS B 1 215 ? -68.191  -13.161 260.612 1.00 39.17  ? 215 LYS B C   1 
ATOM   5727 O  O   . LYS B 1 215 ? -68.553  -14.076 261.358 1.00 64.26  ? 215 LYS B O   1 
ATOM   5728 C  CB  . LYS B 1 215 ? -68.994  -13.529 258.256 1.00 43.96  ? 215 LYS B CB  1 
ATOM   5729 C  CG  . LYS B 1 215 ? -68.875  -12.673 257.014 1.00 50.04  ? 215 LYS B CG  1 
ATOM   5730 C  CD  . LYS B 1 215 ? -69.424  -11.296 257.282 1.00 67.10  ? 215 LYS B CD  1 
ATOM   5731 C  CE  . LYS B 1 215 ? -69.482  -10.456 256.024 1.00 71.76  ? 215 LYS B CE  1 
ATOM   5732 N  NZ  . LYS B 1 215 ? -68.161  -9.884  255.712 1.00 49.32  ? 215 LYS B NZ  1 
ATOM   5733 N  N   . VAL B 1 216 ? -68.140  -11.882 260.991 1.00 33.91  ? 216 VAL B N   1 
ATOM   5734 C  CA  . VAL B 1 216 ? -68.335  -11.515 262.386 1.00 33.23  ? 216 VAL B CA  1 
ATOM   5735 C  C   . VAL B 1 216 ? -69.801  -11.662 262.771 1.00 36.89  ? 216 VAL B C   1 
ATOM   5736 O  O   . VAL B 1 216 ? -70.707  -11.586 261.931 1.00 37.62  ? 216 VAL B O   1 
ATOM   5737 C  CB  . VAL B 1 216 ? -67.839  -10.083 262.657 1.00 34.91  ? 216 VAL B CB  1 
ATOM   5738 C  CG1 . VAL B 1 216 ? -66.378  -9.943  262.274 1.00 34.13  ? 216 VAL B CG1 1 
ATOM   5739 C  CG2 . VAL B 1 216 ? -68.699  -9.073  261.919 1.00 42.89  ? 216 VAL B CG2 1 
ATOM   5740 N  N   . ALA B 1 217 ? -70.031  -11.877 264.063 1.00 38.31  ? 217 ALA B N   1 
ATOM   5741 C  CA  . ALA B 1 217 ? -71.373  -11.929 264.625 1.00 39.85  ? 217 ALA B CA  1 
ATOM   5742 C  C   . ALA B 1 217 ? -71.314  -11.493 266.082 1.00 34.71  ? 217 ALA B C   1 
ATOM   5743 O  O   . ALA B 1 217 ? -70.502  -10.637 266.444 1.00 41.30  ? 217 ALA B O   1 
ATOM   5744 C  CB  . ALA B 1 217 ? -71.964  -13.334 264.497 1.00 41.51  ? 217 ALA B CB  1 
ATOM   5745 N  N   . ILE B 1 218 ? -72.164  -12.071 266.925 1.00 31.66  ? 218 ILE B N   1 
ATOM   5746 C  CA  . ILE B 1 218 ? -72.132  -11.829 268.361 1.00 29.43  ? 218 ILE B CA  1 
ATOM   5747 C  C   . ILE B 1 218 ? -72.118  -13.176 269.066 1.00 30.12  ? 218 ILE B C   1 
ATOM   5748 O  O   . ILE B 1 218 ? -72.932  -14.052 268.754 1.00 32.03  ? 218 ILE B O   1 
ATOM   5749 C  CB  . ILE B 1 218 ? -73.324  -10.977 268.835 1.00 25.32  ? 218 ILE B CB  1 
ATOM   5750 C  CG1 . ILE B 1 218 ? -73.336  -9.627  268.115 1.00 24.23  ? 218 ILE B CG1 1 
ATOM   5751 C  CG2 . ILE B 1 218 ? -73.264  -10.776 270.337 1.00 24.74  ? 218 ILE B CG2 1 
ATOM   5752 C  CD1 . ILE B 1 218 ? -74.510  -8.750  268.482 1.00 25.60  ? 218 ILE B CD1 1 
ATOM   5753 N  N   . HIS B 1 219 ? -71.190  -13.343 270.009 1.00 28.99  ? 219 HIS B N   1 
ATOM   5754 C  CA  . HIS B 1 219 ? -71.058  -14.620 270.701 1.00 28.62  ? 219 HIS B CA  1 
ATOM   5755 C  C   . HIS B 1 219 ? -72.279  -14.903 271.565 1.00 27.55  ? 219 HIS B C   1 
ATOM   5756 O  O   . HIS B 1 219 ? -72.850  -15.999 271.514 1.00 25.03  ? 219 HIS B O   1 
ATOM   5757 C  CB  . HIS B 1 219 ? -69.784  -14.624 271.546 1.00 26.80  ? 219 HIS B CB  1 
ATOM   5758 C  CG  . HIS B 1 219 ? -69.266  -15.994 271.851 1.00 24.28  ? 219 HIS B CG  1 
ATOM   5759 N  ND1 . HIS B 1 219 ? -68.166  -16.211 272.653 1.00 24.03  ? 219 HIS B ND1 1 
ATOM   5760 C  CD2 . HIS B 1 219 ? -69.693  -17.217 271.459 1.00 24.68  ? 219 HIS B CD2 1 
ATOM   5761 C  CE1 . HIS B 1 219 ? -67.940  -17.510 272.744 1.00 32.23  ? 219 HIS B CE1 1 
ATOM   5762 N  NE2 . HIS B 1 219 ? -68.853  -18.142 272.029 1.00 26.46  ? 219 HIS B NE2 1 
ATOM   5763 N  N   . ASP B 1 220 ? -72.697  -13.923 272.361 1.00 26.36  ? 220 ASP B N   1 
ATOM   5764 C  CA  . ASP B 1 220 ? -73.850  -14.056 273.247 1.00 24.64  ? 220 ASP B CA  1 
ATOM   5765 C  C   . ASP B 1 220 ? -74.765  -12.865 273.007 1.00 25.12  ? 220 ASP B C   1 
ATOM   5766 O  O   . ASP B 1 220 ? -74.579  -11.794 273.603 1.00 40.12  ? 220 ASP B O   1 
ATOM   5767 C  CB  . ASP B 1 220 ? -73.413  -14.145 274.707 1.00 24.74  ? 220 ASP B CB  1 
ATOM   5768 C  CG  . ASP B 1 220 ? -74.581  -14.285 275.659 1.00 24.85  ? 220 ASP B CG  1 
ATOM   5769 O  OD1 . ASP B 1 220 ? -75.677  -14.678 275.211 1.00 24.93  ? 220 ASP B OD1 1 
ATOM   5770 O  OD2 . ASP B 1 220 ? -74.398  -14.003 276.860 1.00 23.09  ? 220 ASP B OD2 1 
ATOM   5771 N  N   . PRO B 1 221 ? -75.770  -13.012 272.139 1.00 25.16  ? 221 PRO B N   1 
ATOM   5772 C  CA  . PRO B 1 221 ? -76.680  -11.887 271.880 1.00 25.07  ? 221 PRO B CA  1 
ATOM   5773 C  C   . PRO B 1 221 ? -77.541  -11.526 273.074 1.00 23.45  ? 221 PRO B C   1 
ATOM   5774 O  O   . PRO B 1 221 ? -78.080  -10.413 273.112 1.00 20.82  ? 221 PRO B O   1 
ATOM   5775 C  CB  . PRO B 1 221 ? -77.529  -12.393 270.709 1.00 24.63  ? 221 PRO B CB  1 
ATOM   5776 C  CG  . PRO B 1 221 ? -77.579  -13.868 270.930 1.00 31.56  ? 221 PRO B CG  1 
ATOM   5777 C  CD  . PRO B 1 221 ? -76.208  -14.239 271.452 1.00 26.23  ? 221 PRO B CD  1 
ATOM   5778 N  N   . TRP B 1 222 ? -77.688  -12.427 274.045 1.00 26.49  ? 222 TRP B N   1 
ATOM   5779 C  CA  . TRP B 1 222 ? -78.424  -12.101 275.261 1.00 25.03  ? 222 TRP B CA  1 
ATOM   5780 C  C   . TRP B 1 222 ? -77.732  -10.991 276.041 1.00 23.61  ? 222 TRP B C   1 
ATOM   5781 O  O   . TRP B 1 222 ? -78.299  -9.913  276.252 1.00 31.47  ? 222 TRP B O   1 
ATOM   5782 C  CB  . TRP B 1 222 ? -78.586  -13.351 276.127 1.00 28.02  ? 222 TRP B CB  1 
ATOM   5783 C  CG  . TRP B 1 222 ? -79.164  -13.043 277.461 1.00 26.60  ? 222 TRP B CG  1 
ATOM   5784 C  CD1 . TRP B 1 222 ? -78.527  -13.108 278.665 1.00 25.70  ? 222 TRP B CD1 1 
ATOM   5785 C  CD2 . TRP B 1 222 ? -80.482  -12.561 277.729 1.00 25.12  ? 222 TRP B CD2 1 
ATOM   5786 N  NE1 . TRP B 1 222 ? -79.378  -12.726 279.671 1.00 23.42  ? 222 TRP B NE1 1 
ATOM   5787 C  CE2 . TRP B 1 222 ? -80.585  -12.383 279.122 1.00 25.09  ? 222 TRP B CE2 1 
ATOM   5788 C  CE3 . TRP B 1 222 ? -81.591  -12.277 276.929 1.00 26.27  ? 222 TRP B CE3 1 
ATOM   5789 C  CZ2 . TRP B 1 222 ? -81.751  -11.931 279.730 1.00 29.52  ? 222 TRP B CZ2 1 
ATOM   5790 C  CZ3 . TRP B 1 222 ? -82.745  -11.827 277.533 1.00 33.25  ? 222 TRP B CZ3 1 
ATOM   5791 C  CH2 . TRP B 1 222 ? -82.816  -11.655 278.920 1.00 41.30  ? 222 TRP B CH2 1 
ATOM   5792 N  N   . ALA B 1 223 ? -76.497  -11.239 276.480 1.00 21.84  ? 223 ALA B N   1 
ATOM   5793 C  CA  . ALA B 1 223 ? -75.756  -10.230 277.225 1.00 23.00  ? 223 ALA B CA  1 
ATOM   5794 C  C   . ALA B 1 223 ? -75.444  -9.003  276.382 1.00 22.80  ? 223 ALA B C   1 
ATOM   5795 O  O   . ALA B 1 223 ? -75.211  -7.925  276.938 1.00 22.87  ? 223 ALA B O   1 
ATOM   5796 C  CB  . ALA B 1 223 ? -74.460  -10.830 277.768 1.00 27.77  ? 223 ALA B CB  1 
ATOM   5797 N  N   . ALA B 1 224 ? -75.448  -9.138  275.056 1.00 20.12  ? 224 ALA B N   1 
ATOM   5798 C  CA  . ALA B 1 224 ? -75.040  -8.034  274.197 1.00 18.31  ? 224 ALA B CA  1 
ATOM   5799 C  C   . ALA B 1 224 ? -76.154  -7.009  274.020 1.00 20.83  ? 224 ALA B C   1 
ATOM   5800 O  O   . ALA B 1 224 ? -75.931  -5.807  274.201 1.00 26.07  ? 224 ALA B O   1 
ATOM   5801 C  CB  . ALA B 1 224 ? -74.588  -8.567  272.838 1.00 20.22  ? 224 ALA B CB  1 
ATOM   5802 N  N   . VAL B 1 225 ? -77.358  -7.457  273.666 1.00 19.21  ? 225 VAL B N   1 
ATOM   5803 C  CA  . VAL B 1 225 ? -78.391  -6.526  273.227 1.00 16.52  ? 225 VAL B CA  1 
ATOM   5804 C  C   . VAL B 1 225 ? -79.764  -6.911  273.766 1.00 19.03  ? 225 VAL B C   1 
ATOM   5805 O  O   . VAL B 1 225 ? -80.728  -6.149  273.630 1.00 22.86  ? 225 VAL B O   1 
ATOM   5806 C  CB  . VAL B 1 225 ? -78.410  -6.441  271.688 1.00 16.89  ? 225 VAL B CB  1 
ATOM   5807 C  CG1 . VAL B 1 225 ? -79.118  -7.650  271.094 1.00 20.49  ? 225 VAL B CG1 1 
ATOM   5808 C  CG2 . VAL B 1 225 ? -79.046  -5.138  271.220 1.00 20.62  ? 225 VAL B CG2 1 
ATOM   5809 N  N   . GLN B 1 226 ? -79.873  -8.083  274.391 1.00 22.89  ? 226 GLN B N   1 
ATOM   5810 C  CA  . GLN B 1 226 ? -81.173  -8.576  274.831 1.00 25.37  ? 226 GLN B CA  1 
ATOM   5811 C  C   . GLN B 1 226 ? -81.395  -8.530  276.335 1.00 26.21  ? 226 GLN B C   1 
ATOM   5812 O  O   . GLN B 1 226 ? -82.541  -8.382  276.765 1.00 24.86  ? 226 GLN B O   1 
ATOM   5813 C  CB  . GLN B 1 226 ? -81.391  -10.017 274.354 1.00 22.55  ? 226 GLN B CB  1 
ATOM   5814 C  CG  . GLN B 1 226 ? -81.493  -10.179 272.850 1.00 24.55  ? 226 GLN B CG  1 
ATOM   5815 C  CD  . GLN B 1 226 ? -81.715  -11.622 272.443 1.00 27.12  ? 226 GLN B CD  1 
ATOM   5816 O  OE1 . GLN B 1 226 ? -81.504  -12.541 273.234 1.00 26.76  ? 226 GLN B OE1 1 
ATOM   5817 N  NE2 . GLN B 1 226 ? -82.152  -11.828 271.207 1.00 37.77  ? 226 GLN B NE2 1 
ATOM   5818 N  N   . LYS B 1 227 ? -80.353  -8.657  277.145 1.00 26.00  ? 227 LYS B N   1 
ATOM   5819 C  CA  . LYS B 1 227 ? -80.553  -8.744  278.589 1.00 25.92  ? 227 LYS B CA  1 
ATOM   5820 C  C   . LYS B 1 227 ? -80.977  -7.388  279.144 1.00 29.73  ? 227 LYS B C   1 
ATOM   5821 O  O   . LYS B 1 227 ? -80.337  -6.374  278.845 1.00 43.27  ? 227 LYS B O   1 
ATOM   5822 C  CB  . LYS B 1 227 ? -79.284  -9.222  279.288 1.00 24.89  ? 227 LYS B CB  1 
ATOM   5823 C  CG  . LYS B 1 227 ? -79.456  -9.411  280.788 1.00 24.23  ? 227 LYS B CG  1 
ATOM   5824 C  CD  . LYS B 1 227 ? -78.216  -10.008 281.427 1.00 25.36  ? 227 LYS B CD  1 
ATOM   5825 C  CE  . LYS B 1 227 ? -78.481  -10.392 282.874 1.00 30.70  ? 227 LYS B CE  1 
ATOM   5826 N  NZ  . LYS B 1 227 ? -79.025  -9.253  283.663 1.00 31.31  ? 227 LYS B NZ  1 
ATOM   5827 N  N   . PRO B 1 228 ? -82.042  -7.326  279.942 1.00 30.35  ? 228 PRO B N   1 
ATOM   5828 C  CA  . PRO B 1 228 ? -82.447  -6.044  280.534 1.00 27.10  ? 228 PRO B CA  1 
ATOM   5829 C  C   . PRO B 1 228 ? -81.380  -5.517  281.483 1.00 28.08  ? 228 PRO B C   1 
ATOM   5830 O  O   . PRO B 1 228 ? -80.905  -6.230  282.369 1.00 37.31  ? 228 PRO B O   1 
ATOM   5831 C  CB  . PRO B 1 228 ? -83.744  -6.391  281.276 1.00 31.67  ? 228 PRO B CB  1 
ATOM   5832 C  CG  . PRO B 1 228 ? -84.234  -7.648  280.627 1.00 48.82  ? 228 PRO B CG  1 
ATOM   5833 C  CD  . PRO B 1 228 ? -83.000  -8.402  280.244 1.00 30.72  ? 228 PRO B CD  1 
ATOM   5834 N  N   . GLN B 1 229 ? -81.005  -4.255  281.291 1.00 28.87  ? 229 GLN B N   1 
ATOM   5835 C  CA  . GLN B 1 229 ? -79.970  -3.615  282.089 1.00 26.62  ? 229 GLN B CA  1 
ATOM   5836 C  C   . GLN B 1 229 ? -80.454  -2.243  282.547 1.00 27.50  ? 229 GLN B C   1 
ATOM   5837 O  O   . GLN B 1 229 ? -81.572  -1.816  282.238 1.00 29.76  ? 229 GLN B O   1 
ATOM   5838 C  CB  . GLN B 1 229 ? -78.657  -3.506  281.302 1.00 25.98  ? 229 GLN B CB  1 
ATOM   5839 C  CG  . GLN B 1 229 ? -78.010  -4.845  280.963 1.00 28.21  ? 229 GLN B CG  1 
ATOM   5840 C  CD  . GLN B 1 229 ? -77.412  -5.538  282.178 1.00 26.67  ? 229 GLN B CD  1 
ATOM   5841 O  OE1 . GLN B 1 229 ? -77.443  -5.011  283.290 1.00 24.75  ? 229 GLN B OE1 1 
ATOM   5842 N  NE2 . GLN B 1 229 ? -76.860  -6.727  281.966 1.00 38.15  ? 229 GLN B NE2 1 
ATOM   5843 N  N   . LYS B 1 230 ? -79.596  -1.553  283.298 1.00 29.71  ? 230 LYS B N   1 
ATOM   5844 C  CA  . LYS B 1 230 ? -79.930  -0.229  283.810 1.00 27.89  ? 230 LYS B CA  1 
ATOM   5845 C  C   . LYS B 1 230 ? -80.143  0.752   282.661 1.00 24.68  ? 230 LYS B C   1 
ATOM   5846 O  O   . LYS B 1 230 ? -79.430  0.713   281.655 1.00 24.91  ? 230 LYS B O   1 
ATOM   5847 C  CB  . LYS B 1 230 ? -78.814  0.268   284.731 1.00 24.30  ? 230 LYS B CB  1 
ATOM   5848 C  CG  . LYS B 1 230 ? -79.062  1.629   285.349 1.00 25.75  ? 230 LYS B CG  1 
ATOM   5849 C  CD  . LYS B 1 230 ? -78.134  1.835   286.534 1.00 31.58  ? 230 LYS B CD  1 
ATOM   5850 C  CE  . LYS B 1 230 ? -78.226  3.250   287.077 1.00 38.04  ? 230 LYS B CE  1 
ATOM   5851 N  NZ  . LYS B 1 230 ? -77.543  4.244   286.209 1.00 26.72  ? 230 LYS B NZ  1 
ATOM   5852 N  N   . SER B 1 231 ? -81.143  1.625   282.812 1.00 27.02  ? 231 SER B N   1 
ATOM   5853 C  CA  . SER B 1 231 ? -81.585  2.622   281.838 1.00 29.33  ? 231 SER B CA  1 
ATOM   5854 C  C   . SER B 1 231 ? -82.144  2.000   280.563 1.00 30.86  ? 231 SER B C   1 
ATOM   5855 O  O   . SER B 1 231 ? -82.556  2.742   279.658 1.00 41.42  ? 231 SER B O   1 
ATOM   5856 C  CB  . SER B 1 231 ? -80.476  3.611   281.451 1.00 29.63  ? 231 SER B CB  1 
ATOM   5857 O  OG  . SER B 1 231 ? -79.531  3.005   280.589 1.00 36.92  ? 231 SER B OG  1 
ATOM   5858 N  N   . VAL B 1 232 ? -82.150  0.675   280.443 1.00 33.41  ? 232 VAL B N   1 
ATOM   5859 C  CA  . VAL B 1 232 ? -82.714  -0.018  279.289 1.00 33.55  ? 232 VAL B CA  1 
ATOM   5860 C  C   . VAL B 1 232 ? -83.430  -1.268  279.778 1.00 38.08  ? 232 VAL B C   1 
ATOM   5861 O  O   . VAL B 1 232 ? -83.268  -2.354  279.208 1.00 35.59  ? 232 VAL B O   1 
ATOM   5862 C  CB  . VAL B 1 232 ? -81.639  -0.383  278.249 1.00 28.34  ? 232 VAL B CB  1 
ATOM   5863 C  CG1 . VAL B 1 232 ? -81.284  0.818   277.379 1.00 30.65  ? 232 VAL B CG1 1 
ATOM   5864 C  CG2 . VAL B 1 232 ? -80.398  -0.909  278.944 1.00 36.49  ? 232 VAL B CG2 1 
ATOM   5865 N  N   . SER B 1 233 ? -84.242  -1.119  280.824 1.00 35.24  ? 233 SER B N   1 
ATOM   5866 C  CA  . SER B 1 233 ? -84.900  -2.247  281.466 1.00 36.98  ? 233 SER B CA  1 
ATOM   5867 C  C   . SER B 1 233 ? -86.374  -2.373  281.111 1.00 40.95  ? 233 SER B C   1 
ATOM   5868 O  O   . SER B 1 233 ? -86.976  -3.407  281.415 1.00 44.07  ? 233 SER B O   1 
ATOM   5869 C  CB  . SER B 1 233 ? -84.750  -2.151  282.988 1.00 41.70  ? 233 SER B CB  1 
ATOM   5870 O  OG  . SER B 1 233 ? -85.275  -0.932  283.485 1.00 85.24  ? 233 SER B OG  1 
ATOM   5871 N  N   . ALA B 1 234 ? -86.974  -1.353  280.499 1.00 43.54  ? 234 ALA B N   1 
ATOM   5872 C  CA  . ALA B 1 234 ? -88.324  -1.501  279.976 1.00 49.54  ? 234 ALA B CA  1 
ATOM   5873 C  C   . ALA B 1 234 ? -88.337  -2.571  278.892 1.00 52.13  ? 234 ALA B C   1 
ATOM   5874 O  O   . ALA B 1 234 ? -87.333  -2.812  278.218 1.00 58.61  ? 234 ALA B O   1 
ATOM   5875 C  CB  . ALA B 1 234 ? -88.834  -0.171  279.422 1.00 71.83  ? 234 ALA B CB  1 
ATOM   5876 N  N   . TRP B 1 235 ? -89.480  -3.235  278.729 1.00 52.23  ? 235 TRP B N   1 
ATOM   5877 C  CA  . TRP B 1 235 ? -89.508  -4.365  277.811 1.00 57.93  ? 235 TRP B CA  1 
ATOM   5878 C  C   . TRP B 1 235 ? -89.861  -3.975  276.384 1.00 58.17  ? 235 TRP B C   1 
ATOM   5879 O  O   . TRP B 1 235 ? -89.628  -4.772  275.469 1.00 78.06  ? 235 TRP B O   1 
ATOM   5880 C  CB  . TRP B 1 235 ? -90.479  -5.446  278.291 1.00 70.96  ? 235 TRP B CB  1 
ATOM   5881 C  CG  . TRP B 1 235 ? -90.018  -6.806  277.864 1.00 105.19 ? 235 TRP B CG  1 
ATOM   5882 C  CD1 . TRP B 1 235 ? -88.891  -7.449  278.283 1.00 92.25  ? 235 TRP B CD1 1 
ATOM   5883 C  CD2 . TRP B 1 235 ? -90.635  -7.668  276.900 1.00 105.53 ? 235 TRP B CD2 1 
ATOM   5884 N  NE1 . TRP B 1 235 ? -88.779  -8.665  277.659 1.00 87.48  ? 235 TRP B NE1 1 
ATOM   5885 C  CE2 . TRP B 1 235 ? -89.836  -8.825  276.805 1.00 80.65  ? 235 TRP B CE2 1 
ATOM   5886 C  CE3 . TRP B 1 235 ? -91.790  -7.580  276.118 1.00 101.56 ? 235 TRP B CE3 1 
ATOM   5887 C  CZ2 . TRP B 1 235 ? -90.154  -9.885  275.961 1.00 74.26  ? 235 TRP B CZ2 1 
ATOM   5888 C  CZ3 . TRP B 1 235 ? -92.104  -8.636  275.279 1.00 98.52  ? 235 TRP B CZ3 1 
ATOM   5889 C  CH2 . TRP B 1 235 ? -91.289  -9.772  275.208 1.00 80.44  ? 235 TRP B CH2 1 
ATOM   5890 N  N   . ASN B 1 236 ? -90.416  -2.784  276.164 1.00 55.90  ? 236 ASN B N   1 
ATOM   5891 C  CA  . ASN B 1 236 ? -90.526  -2.241  274.818 1.00 66.54  ? 236 ASN B CA  1 
ATOM   5892 C  C   . ASN B 1 236 ? -89.265  -1.493  274.401 1.00 47.17  ? 236 ASN B C   1 
ATOM   5893 O  O   . ASN B 1 236 ? -89.295  -0.728  273.429 1.00 38.79  ? 236 ASN B O   1 
ATOM   5894 C  CB  . ASN B 1 236 ? -91.762  -1.340  274.696 1.00 60.43  ? 236 ASN B CB  1 
ATOM   5895 C  CG  . ASN B 1 236 ? -91.718  -0.135  275.620 1.00 53.76  ? 236 ASN B CG  1 
ATOM   5896 O  OD1 . ASN B 1 236 ? -90.706  0.146   276.261 1.00 54.39  ? 236 ASN B OD1 1 
ATOM   5897 N  ND2 . ASN B 1 236 ? -92.827  0.592   275.681 1.00 65.05  ? 236 ASN B ND2 1 
ATOM   5898 N  N   . GLU B 1 237 ? -88.168  -1.697  275.119 1.00 44.93  ? 237 GLU B N   1 
ATOM   5899 C  CA  . GLU B 1 237 ? -86.904  -1.054  274.794 1.00 40.77  ? 237 GLU B CA  1 
ATOM   5900 C  C   . GLU B 1 237 ? -86.352  -1.640  273.503 1.00 38.90  ? 237 GLU B C   1 
ATOM   5901 O  O   . GLU B 1 237 ? -86.196  -2.865  273.407 1.00 52.36  ? 237 GLU B O   1 
ATOM   5902 C  CB  . GLU B 1 237 ? -85.905  -1.244  275.931 1.00 41.83  ? 237 GLU B CB  1 
ATOM   5903 C  CG  . GLU B 1 237 ? -84.751  -0.259  275.927 1.00 57.90  ? 237 GLU B CG  1 
ATOM   5904 C  CD  . GLU B 1 237 ? -85.217  1.179   276.043 1.00 55.08  ? 237 GLU B CD  1 
ATOM   5905 O  OE1 . GLU B 1 237 ? -85.918  1.499   277.025 1.00 48.11  ? 237 GLU B OE1 1 
ATOM   5906 O  OE2 . GLU B 1 237 ? -84.883  1.988   275.152 1.00 40.73  ? 237 GLU B OE2 1 
ATOM   5907 N  N   . PRO B 1 238 ? -86.049  -0.822  272.495 1.00 34.84  ? 238 PRO B N   1 
ATOM   5908 C  CA  . PRO B 1 238 ? -85.537  -1.381  271.235 1.00 30.45  ? 238 PRO B CA  1 
ATOM   5909 C  C   . PRO B 1 238 ? -84.153  -1.991  271.365 1.00 34.39  ? 238 PRO B C   1 
ATOM   5910 O  O   . PRO B 1 238 ? -83.827  -2.916  270.611 1.00 30.87  ? 238 PRO B O   1 
ATOM   5911 C  CB  . PRO B 1 238 ? -85.534  -0.170  270.294 1.00 26.39  ? 238 PRO B CB  1 
ATOM   5912 C  CG  . PRO B 1 238 ? -85.437  1.007   271.209 1.00 28.58  ? 238 PRO B CG  1 
ATOM   5913 C  CD  . PRO B 1 238 ? -86.198  0.641   272.440 1.00 32.80  ? 238 PRO B CD  1 
ATOM   5914 N  N   . TYR B 1 239 ? -83.331  -1.511  272.298 1.00 55.89  ? 239 TYR B N   1 
ATOM   5915 C  CA  . TYR B 1 239 ? -81.970  -2.009  272.467 1.00 32.79  ? 239 TYR B CA  1 
ATOM   5916 C  C   . TYR B 1 239 ? -81.673  -2.145  273.951 1.00 30.25  ? 239 TYR B C   1 
ATOM   5917 O  O   . TYR B 1 239 ? -81.770  -1.166  274.697 1.00 39.25  ? 239 TYR B O   1 
ATOM   5918 C  CB  . TYR B 1 239 ? -80.953  -1.074  271.804 1.00 24.67  ? 239 TYR B CB  1 
ATOM   5919 C  CG  . TYR B 1 239 ? -81.224  -0.811  270.342 1.00 21.78  ? 239 TYR B CG  1 
ATOM   5920 C  CD1 . TYR B 1 239 ? -81.078  -1.816  269.397 1.00 20.24  ? 239 TYR B CD1 1 
ATOM   5921 C  CD2 . TYR B 1 239 ? -81.628  0.443   269.907 1.00 21.17  ? 239 TYR B CD2 1 
ATOM   5922 C  CE1 . TYR B 1 239 ? -81.327  -1.580  268.059 1.00 20.45  ? 239 TYR B CE1 1 
ATOM   5923 C  CE2 . TYR B 1 239 ? -81.879  0.690   268.571 1.00 29.22  ? 239 TYR B CE2 1 
ATOM   5924 C  CZ  . TYR B 1 239 ? -81.727  -0.326  267.652 1.00 23.22  ? 239 TYR B CZ  1 
ATOM   5925 O  OH  . TYR B 1 239 ? -81.975  -0.087  266.320 1.00 19.57  ? 239 TYR B OH  1 
ATOM   5926 N  N   . LYS B 1 240 ? -81.312  -3.356  274.377 1.00 26.73  ? 240 LYS B N   1 
ATOM   5927 C  CA  . LYS B 1 240 ? -80.879  -3.585  275.750 1.00 24.01  ? 240 LYS B CA  1 
ATOM   5928 C  C   . LYS B 1 240 ? -79.455  -4.123  275.777 1.00 23.78  ? 240 LYS B C   1 
ATOM   5929 O  O   . LYS B 1 240 ? -78.642  -3.792  274.908 1.00 23.50  ? 240 LYS B O   1 
ATOM   5930 C  CB  . LYS B 1 240 ? -81.808  -4.564  276.469 1.00 27.24  ? 240 LYS B CB  1 
ATOM   5931 C  CG  . LYS B 1 240 ? -83.290  -4.310  276.288 1.00 33.85  ? 240 LYS B CG  1 
ATOM   5932 C  CD  . LYS B 1 240 ? -84.083  -5.383  277.013 1.00 33.35  ? 240 LYS B CD  1 
ATOM   5933 C  CE  . LYS B 1 240 ? -85.556  -5.332  276.667 1.00 42.99  ? 240 LYS B CE  1 
ATOM   5934 N  NZ  . LYS B 1 240 ? -86.232  -6.592  277.074 1.00 45.63  ? 240 LYS B NZ  1 
ATOM   5935 N  N   . GLY B 1 241 ? -79.153  -4.958  276.768 1.00 28.38  ? 241 GLY B N   1 
ATOM   5936 C  CA  . GLY B 1 241 ? -77.863  -5.600  276.888 1.00 37.37  ? 241 GLY B CA  1 
ATOM   5937 C  C   . GLY B 1 241 ? -76.723  -4.603  277.036 1.00 20.39  ? 241 GLY B C   1 
ATOM   5938 O  O   . GLY B 1 241 ? -76.908  -3.433  277.382 1.00 21.26  ? 241 GLY B O   1 
ATOM   5939 N  N   . ASN B 1 242 ? -75.516  -5.098  276.760 1.00 19.15  ? 242 ASN B N   1 
ATOM   5940 C  CA  . ASN B 1 242 ? -74.340  -4.238  276.819 1.00 20.17  ? 242 ASN B CA  1 
ATOM   5941 C  C   . ASN B 1 242 ? -74.373  -3.186  275.719 1.00 22.28  ? 242 ASN B C   1 
ATOM   5942 O  O   . ASN B 1 242 ? -73.958  -2.042  275.936 1.00 23.25  ? 242 ASN B O   1 
ATOM   5943 C  CB  . ASN B 1 242 ? -73.069  -5.079  276.721 1.00 20.96  ? 242 ASN B CB  1 
ATOM   5944 C  CG  . ASN B 1 242 ? -72.987  -6.127  277.806 1.00 22.00  ? 242 ASN B CG  1 
ATOM   5945 O  OD1 . ASN B 1 242 ? -73.589  -5.979  278.868 1.00 20.72  ? 242 ASN B OD1 1 
ATOM   5946 N  ND2 . ASN B 1 242 ? -72.245  -7.196  277.545 1.00 25.14  ? 242 ASN B ND2 1 
ATOM   5947 N  N   . PHE B 1 243 ? -74.867  -3.552  274.534 1.00 20.31  ? 243 PHE B N   1 
ATOM   5948 C  CA  . PHE B 1 243 ? -74.937  -2.591  273.438 1.00 19.35  ? 243 PHE B CA  1 
ATOM   5949 C  C   . PHE B 1 243 ? -75.863  -1.432  273.779 1.00 19.89  ? 243 PHE B C   1 
ATOM   5950 O  O   . PHE B 1 243 ? -75.538  -0.270  273.511 1.00 21.83  ? 243 PHE B O   1 
ATOM   5951 C  CB  . PHE B 1 243 ? -75.397  -3.283  272.155 1.00 17.75  ? 243 PHE B CB  1 
ATOM   5952 C  CG  . PHE B 1 243 ? -74.339  -4.129  271.504 1.00 19.70  ? 243 PHE B CG  1 
ATOM   5953 C  CD1 . PHE B 1 243 ? -73.098  -4.298  272.096 1.00 19.70  ? 243 PHE B CD1 1 
ATOM   5954 C  CD2 . PHE B 1 243 ? -74.586  -4.750  270.292 1.00 22.89  ? 243 PHE B CD2 1 
ATOM   5955 C  CE1 . PHE B 1 243 ? -72.127  -5.074  271.494 1.00 23.87  ? 243 PHE B CE1 1 
ATOM   5956 C  CE2 . PHE B 1 243 ? -73.619  -5.526  269.685 1.00 24.37  ? 243 PHE B CE2 1 
ATOM   5957 C  CZ  . PHE B 1 243 ? -72.388  -5.689  270.287 1.00 24.97  ? 243 PHE B CZ  1 
ATOM   5958 N  N   . GLY B 1 244 ? -77.018  -1.727  274.378 1.00 21.44  ? 244 GLY B N   1 
ATOM   5959 C  CA  . GLY B 1 244 ? -77.951  -0.667  274.723 1.00 23.72  ? 244 GLY B CA  1 
ATOM   5960 C  C   . GLY B 1 244 ? -77.374  0.323   275.715 1.00 21.00  ? 244 GLY B C   1 
ATOM   5961 O  O   . GLY B 1 244 ? -77.587  1.532   275.596 1.00 23.33  ? 244 GLY B O   1 
ATOM   5962 N  N   . GLN B 1 245 ? -76.633  -0.174  276.707 1.00 19.46  ? 245 GLN B N   1 
ATOM   5963 C  CA  . GLN B 1 245 ? -76.005  0.725   277.669 1.00 21.70  ? 245 GLN B CA  1 
ATOM   5964 C  C   . GLN B 1 245 ? -74.846  1.487   277.037 1.00 21.66  ? 245 GLN B C   1 
ATOM   5965 O  O   . GLN B 1 245 ? -74.628  2.663   277.350 1.00 20.22  ? 245 GLN B O   1 
ATOM   5966 C  CB  . GLN B 1 245 ? -75.532  -0.058  278.893 1.00 21.03  ? 245 GLN B CB  1 
ATOM   5967 C  CG  . GLN B 1 245 ? -76.654  -0.499  279.818 1.00 19.76  ? 245 GLN B CG  1 
ATOM   5968 C  CD  . GLN B 1 245 ? -76.138  -1.150  281.086 1.00 25.72  ? 245 GLN B CD  1 
ATOM   5969 O  OE1 . GLN B 1 245 ? -75.214  -1.962  281.050 1.00 39.11  ? 245 GLN B OE1 1 
ATOM   5970 N  NE2 . GLN B 1 245 ? -76.734  -0.793  282.218 1.00 22.98  ? 245 GLN B NE2 1 
ATOM   5971 N  N   . LEU B 1 246 ? -74.095  0.836   276.144 1.00 34.13  ? 246 LEU B N   1 
ATOM   5972 C  CA  . LEU B 1 246 ? -72.995  1.518   275.467 1.00 20.79  ? 246 LEU B CA  1 
ATOM   5973 C  C   . LEU B 1 246 ? -73.499  2.688   274.632 1.00 21.99  ? 246 LEU B C   1 
ATOM   5974 O  O   . LEU B 1 246 ? -72.829  3.722   274.533 1.00 22.28  ? 246 LEU B O   1 
ATOM   5975 C  CB  . LEU B 1 246 ? -72.217  0.531   274.597 1.00 20.71  ? 246 LEU B CB  1 
ATOM   5976 C  CG  . LEU B 1 246 ? -71.290  -0.445  275.324 1.00 20.89  ? 246 LEU B CG  1 
ATOM   5977 C  CD1 . LEU B 1 246 ? -70.743  -1.481  274.358 1.00 32.41  ? 246 LEU B CD1 1 
ATOM   5978 C  CD2 . LEU B 1 246 ? -70.154  0.307   275.995 1.00 21.17  ? 246 LEU B CD2 1 
ATOM   5979 N  N   . MET B 1 247 ? -74.677  2.545   274.021 1.00 23.12  ? 247 MET B N   1 
ATOM   5980 C  CA  . MET B 1 247 ? -75.272  3.663   273.297 1.00 22.71  ? 247 MET B CA  1 
ATOM   5981 C  C   . MET B 1 247 ? -75.589  4.812   274.245 1.00 22.09  ? 247 MET B C   1 
ATOM   5982 O  O   . MET B 1 247 ? -75.284  5.975   273.957 1.00 20.53  ? 247 MET B O   1 
ATOM   5983 C  CB  . MET B 1 247 ? -76.537  3.208   272.570 1.00 19.69  ? 247 MET B CB  1 
ATOM   5984 C  CG  . MET B 1 247 ? -76.332  2.059   271.602 1.00 16.54  ? 247 MET B CG  1 
ATOM   5985 S  SD  . MET B 1 247 ? -77.896  1.451   270.946 1.00 18.11  ? 247 MET B SD  1 
ATOM   5986 C  CE  . MET B 1 247 ? -77.354  -0.023  270.088 1.00 21.58  ? 247 MET B CE  1 
ATOM   5987 N  N   . ALA B 1 248 ? -76.200  4.500   275.390 1.00 23.11  ? 248 ALA B N   1 
ATOM   5988 C  CA  . ALA B 1 248 ? -76.561  5.539   276.346 1.00 27.31  ? 248 ALA B CA  1 
ATOM   5989 C  C   . ALA B 1 248 ? -75.343  6.074   277.086 1.00 27.92  ? 248 ALA B C   1 
ATOM   5990 O  O   . ALA B 1 248 ? -75.293  7.266   277.409 1.00 30.89  ? 248 ALA B O   1 
ATOM   5991 C  CB  . ALA B 1 248 ? -77.591  5.001   277.339 1.00 32.03  ? 248 ALA B CB  1 
ATOM   5992 N  N   . ALA B 1 249 ? -74.358  5.217   277.365 1.00 26.36  ? 249 ALA B N   1 
ATOM   5993 C  CA  . ALA B 1 249 ? -73.154  5.681   278.044 1.00 25.89  ? 249 ALA B CA  1 
ATOM   5994 C  C   . ALA B 1 249 ? -72.303  6.561   277.139 1.00 20.33  ? 249 ALA B C   1 
ATOM   5995 O  O   . ALA B 1 249 ? -71.621  7.470   277.626 1.00 21.50  ? 249 ALA B O   1 
ATOM   5996 C  CB  . ALA B 1 249 ? -72.339  4.491   278.546 1.00 35.49  ? 249 ALA B CB  1 
ATOM   5997 N  N   . LYS B 1 250 ? -72.329  6.309   275.828 1.00 21.00  ? 250 LYS B N   1 
ATOM   5998 C  CA  . LYS B 1 250 ? -71.575  7.145   274.901 1.00 19.33  ? 250 LYS B CA  1 
ATOM   5999 C  C   . LYS B 1 250 ? -72.121  8.565   274.857 1.00 19.39  ? 250 LYS B C   1 
ATOM   6000 O  O   . LYS B 1 250 ? -71.373  9.507   274.575 1.00 18.44  ? 250 LYS B O   1 
ATOM   6001 C  CB  . LYS B 1 250 ? -71.593  6.527   273.504 1.00 24.27  ? 250 LYS B CB  1 
ATOM   6002 C  CG  . LYS B 1 250 ? -70.562  7.106   272.552 1.00 19.29  ? 250 LYS B CG  1 
ATOM   6003 C  CD  . LYS B 1 250 ? -70.465  6.274   271.287 1.00 17.30  ? 250 LYS B CD  1 
ATOM   6004 C  CE  . LYS B 1 250 ? -69.388  6.803   270.360 1.00 16.27  ? 250 LYS B CE  1 
ATOM   6005 N  NZ  . LYS B 1 250 ? -69.288  5.979   269.127 1.00 18.71  ? 250 LYS B NZ  1 
ATOM   6006 N  N   . LEU B 1 251 ? -73.416  8.739   275.125 1.00 17.79  ? 251 LEU B N   1 
ATOM   6007 C  CA  . LEU B 1 251 ? -73.980  10.082  275.194 1.00 17.32  ? 251 LEU B CA  1 
ATOM   6008 C  C   . LEU B 1 251 ? -73.470  10.821  276.424 1.00 19.90  ? 251 LEU B C   1 
ATOM   6009 O  O   . LEU B 1 251 ? -73.039  11.976  276.333 1.00 34.74  ? 251 LEU B O   1 
ATOM   6010 C  CB  . LEU B 1 251 ? -75.507  10.011  275.196 1.00 17.96  ? 251 LEU B CB  1 
ATOM   6011 C  CG  . LEU B 1 251 ? -76.140  9.288   274.005 1.00 21.13  ? 251 LEU B CG  1 
ATOM   6012 C  CD1 . LEU B 1 251 ? -77.655  9.268   274.128 1.00 21.00  ? 251 LEU B CD1 1 
ATOM   6013 C  CD2 . LEU B 1 251 ? -75.713  9.936   272.696 1.00 16.62  ? 251 LEU B CD2 1 
ATOM   6014 N  N   . ALA B 1 252 ? -73.501  10.164  277.586 1.00 18.42  ? 252 ALA B N   1 
ATOM   6015 C  CA  . ALA B 1 252 ? -72.986  10.777  278.804 1.00 17.95  ? 252 ALA B CA  1 
ATOM   6016 C  C   . ALA B 1 252 ? -71.476  10.969  278.761 1.00 18.56  ? 252 ALA B C   1 
ATOM   6017 O  O   . ALA B 1 252 ? -70.956  11.843  279.461 1.00 19.04  ? 252 ALA B O   1 
ATOM   6018 C  CB  . ALA B 1 252 ? -73.368  9.935   280.021 1.00 30.28  ? 252 ALA B CB  1 
ATOM   6019 N  N   . ASN B 1 253 ? -70.764  10.176  277.963 1.00 18.22  ? 253 ASN B N   1 
ATOM   6020 C  CA  . ASN B 1 253 ? -69.317  10.299  277.795 1.00 17.62  ? 253 ASN B CA  1 
ATOM   6021 C  C   . ASN B 1 253 ? -69.022  10.450  276.309 1.00 19.18  ? 253 ASN B C   1 
ATOM   6022 O  O   . ASN B 1 253 ? -68.637  9.483   275.638 1.00 32.51  ? 253 ASN B O   1 
ATOM   6023 C  CB  . ASN B 1 253 ? -68.585  9.095   278.388 1.00 20.45  ? 253 ASN B CB  1 
ATOM   6024 C  CG  . ASN B 1 253 ? -68.927  8.867   279.845 1.00 24.63  ? 253 ASN B CG  1 
ATOM   6025 O  OD1 . ASN B 1 253 ? -68.260  9.385   280.740 1.00 25.93  ? 253 ASN B OD1 1 
ATOM   6026 N  ND2 . ASN B 1 253 ? -69.971  8.086   280.092 1.00 25.30  ? 253 ASN B ND2 1 
ATOM   6027 N  N   . PRO B 1 254 ? -69.200  11.654  275.758 1.00 20.12  ? 254 PRO B N   1 
ATOM   6028 C  CA  . PRO B 1 254 ? -68.934  11.845  274.323 1.00 21.05  ? 254 PRO B CA  1 
ATOM   6029 C  C   . PRO B 1 254 ? -67.460  11.793  273.967 1.00 22.48  ? 254 PRO B C   1 
ATOM   6030 O  O   . PRO B 1 254 ? -67.133  11.572  272.794 1.00 22.18  ? 254 PRO B O   1 
ATOM   6031 C  CB  . PRO B 1 254 ? -69.532  13.228  274.039 1.00 22.67  ? 254 PRO B CB  1 
ATOM   6032 C  CG  . PRO B 1 254 ? -69.436  13.941  275.344 1.00 18.73  ? 254 PRO B CG  1 
ATOM   6033 C  CD  . PRO B 1 254 ? -69.652  12.896  276.408 1.00 19.19  ? 254 PRO B CD  1 
ATOM   6034 N  N   . HIS B 1 255 ? -66.562  11.989  274.934 1.00 21.92  ? 255 HIS B N   1 
ATOM   6035 C  CA  . HIS B 1 255 ? -65.136  11.846  274.663 1.00 21.63  ? 255 HIS B CA  1 
ATOM   6036 C  C   . HIS B 1 255 ? -64.761  10.396  274.393 1.00 19.94  ? 255 HIS B C   1 
ATOM   6037 O  O   . HIS B 1 255 ? -63.758  10.129  273.722 1.00 20.98  ? 255 HIS B O   1 
ATOM   6038 C  CB  . HIS B 1 255 ? -64.324  12.373  275.844 1.00 28.87  ? 255 HIS B CB  1 
ATOM   6039 C  CG  . HIS B 1 255 ? -64.416  11.511  277.063 1.00 25.20  ? 255 HIS B CG  1 
ATOM   6040 N  ND1 . HIS B 1 255 ? -65.430  11.634  277.988 1.00 30.95  ? 255 HIS B ND1 1 
ATOM   6041 C  CD2 . HIS B 1 255 ? -63.628  10.501  277.503 1.00 24.63  ? 255 HIS B CD2 1 
ATOM   6042 C  CE1 . HIS B 1 255 ? -65.259  10.743  278.948 1.00 40.90  ? 255 HIS B CE1 1 
ATOM   6043 N  NE2 . HIS B 1 255 ? -64.173  10.042  278.677 1.00 38.45  ? 255 HIS B NE2 1 
ATOM   6044 N  N   . LEU B 1 256 ? -65.550  9.457   274.906 1.00 21.81  ? 256 LEU B N   1 
ATOM   6045 C  CA  . LEU B 1 256 ? -65.202  8.046   274.840 1.00 21.39  ? 256 LEU B CA  1 
ATOM   6046 C  C   . LEU B 1 256 ? -65.232  7.535   273.405 1.00 20.21  ? 256 LEU B C   1 
ATOM   6047 O  O   . LEU B 1 256 ? -66.107  7.896   272.614 1.00 20.29  ? 256 LEU B O   1 
ATOM   6048 C  CB  . LEU B 1 256 ? -66.165  7.230   275.702 1.00 19.56  ? 256 LEU B CB  1 
ATOM   6049 C  CG  . LEU B 1 256 ? -65.994  5.712   275.693 1.00 21.08  ? 256 LEU B CG  1 
ATOM   6050 C  CD1 . LEU B 1 256 ? -64.735  5.306   276.444 1.00 35.82  ? 256 LEU B CD1 1 
ATOM   6051 C  CD2 . LEU B 1 256 ? -67.221  5.033   276.278 1.00 20.53  ? 256 LEU B CD2 1 
ATOM   6052 N  N   . LYS B 1 257 ? -64.260  6.690   273.075 1.00 20.17  ? 257 LYS B N   1 
ATOM   6053 C  CA  . LYS B 1 257 ? -64.210  5.988   271.800 1.00 21.98  ? 257 LYS B CA  1 
ATOM   6054 C  C   . LYS B 1 257 ? -64.395  4.501   272.062 1.00 23.24  ? 257 LYS B C   1 
ATOM   6055 O  O   . LYS B 1 257 ? -63.653  3.910   272.853 1.00 52.65  ? 257 LYS B O   1 
ATOM   6056 C  CB  . LYS B 1 257 ? -62.882  6.243   271.083 1.00 36.48  ? 257 LYS B CB  1 
ATOM   6057 C  CG  . LYS B 1 257 ? -62.367  7.671   271.202 1.00 28.10  ? 257 LYS B CG  1 
ATOM   6058 C  CD  . LYS B 1 257 ? -63.296  8.665   270.525 1.00 32.39  ? 257 LYS B CD  1 
ATOM   6059 C  CE  . LYS B 1 257 ? -62.732  10.076  270.590 1.00 31.66  ? 257 LYS B CE  1 
ATOM   6060 N  NZ  . LYS B 1 257 ? -63.662  11.081  270.005 1.00 29.38  ? 257 LYS B NZ  1 
ATOM   6061 N  N   . ILE B 1 258 ? -65.384  3.900   271.408 1.00 20.50  ? 258 ILE B N   1 
ATOM   6062 C  CA  . ILE B 1 258 ? -65.745  2.504   271.628 1.00 21.28  ? 258 ILE B CA  1 
ATOM   6063 C  C   . ILE B 1 258 ? -65.297  1.693   270.422 1.00 20.71  ? 258 ILE B C   1 
ATOM   6064 O  O   . ILE B 1 258 ? -65.654  2.013   269.282 1.00 21.22  ? 258 ILE B O   1 
ATOM   6065 C  CB  . ILE B 1 258 ? -67.255  2.347   271.872 1.00 22.74  ? 258 ILE B CB  1 
ATOM   6066 C  CG1 . ILE B 1 258 ? -67.679  3.165   273.091 1.00 20.75  ? 258 ILE B CG1 1 
ATOM   6067 C  CG2 . ILE B 1 258 ? -67.608  0.886   272.077 1.00 21.78  ? 258 ILE B CG2 1 
ATOM   6068 C  CD1 . ILE B 1 258 ? -69.144  3.039   273.432 1.00 19.26  ? 258 ILE B CD1 1 
ATOM   6069 N  N   . LEU B 1 259 ? -64.514  0.643   270.673 1.00 18.91  ? 259 LEU B N   1 
ATOM   6070 C  CA  . LEU B 1 259 ? -63.980  -0.187  269.610 1.00 20.97  ? 259 LEU B CA  1 
ATOM   6071 C  C   . LEU B 1 259 ? -64.354  -1.648  269.826 1.00 22.82  ? 259 LEU B C   1 
ATOM   6072 O  O   . LEU B 1 259 ? -64.299  -2.144  270.957 1.00 22.83  ? 259 LEU B O   1 
ATOM   6073 C  CB  . LEU B 1 259 ? -62.449  -0.069  269.521 1.00 22.12  ? 259 LEU B CB  1 
ATOM   6074 C  CG  . LEU B 1 259 ? -61.844  1.218   268.954 1.00 23.01  ? 259 LEU B CG  1 
ATOM   6075 C  CD1 . LEU B 1 259 ? -61.849  2.340   269.984 1.00 30.52  ? 259 LEU B CD1 1 
ATOM   6076 C  CD2 . LEU B 1 259 ? -60.435  0.958   268.444 1.00 23.90  ? 259 LEU B CD2 1 
ATOM   6077 N  N   . PRO B 1 260 ? -64.742  -2.360  268.767 1.00 19.92  ? 260 PRO B N   1 
ATOM   6078 C  CA  . PRO B 1 260 ? -65.042  -3.791  268.900 1.00 20.43  ? 260 PRO B CA  1 
ATOM   6079 C  C   . PRO B 1 260 ? -63.772  -4.626  268.807 1.00 23.44  ? 260 PRO B C   1 
ATOM   6080 O  O   . PRO B 1 260 ? -62.987  -4.485  267.866 1.00 24.44  ? 260 PRO B O   1 
ATOM   6081 C  CB  . PRO B 1 260 ? -65.979  -4.062  267.719 1.00 22.79  ? 260 PRO B CB  1 
ATOM   6082 C  CG  . PRO B 1 260 ? -65.529  -3.083  266.682 1.00 22.19  ? 260 PRO B CG  1 
ATOM   6083 C  CD  . PRO B 1 260 ? -65.081  -1.847  267.429 1.00 19.23  ? 260 PRO B CD  1 
ATOM   6084 N  N   . SER B 1 261 ? -63.574  -5.498  269.791 1.00 29.95  ? 261 SER B N   1 
ATOM   6085 C  CA  . SER B 1 261 ? -62.420  -6.391  269.820 1.00 24.50  ? 261 SER B CA  1 
ATOM   6086 C  C   . SER B 1 261 ? -62.800  -7.693  269.127 1.00 20.37  ? 261 SER B C   1 
ATOM   6087 O  O   . SER B 1 261 ? -63.592  -8.480  269.657 1.00 19.41  ? 261 SER B O   1 
ATOM   6088 C  CB  . SER B 1 261 ? -61.963  -6.637  271.255 1.00 22.93  ? 261 SER B CB  1 
ATOM   6089 O  OG  . SER B 1 261 ? -61.440  -5.453  271.829 1.00 40.39  ? 261 SER B OG  1 
ATOM   6090 N  N   . ILE B 1 262 ? -62.240  -7.919  267.944 1.00 19.25  ? 262 ILE B N   1 
ATOM   6091 C  CA  . ILE B 1 262 ? -62.549  -9.087  267.130 1.00 19.44  ? 262 ILE B CA  1 
ATOM   6092 C  C   . ILE B 1 262 ? -61.467  -10.129 267.374 1.00 20.92  ? 262 ILE B C   1 
ATOM   6093 O  O   . ILE B 1 262 ? -60.323  -9.965  266.938 1.00 33.70  ? 262 ILE B O   1 
ATOM   6094 C  CB  . ILE B 1 262 ? -62.646  -8.727  265.642 1.00 20.12  ? 262 ILE B CB  1 
ATOM   6095 C  CG1 . ILE B 1 262 ? -63.685  -7.626  265.427 1.00 18.88  ? 262 ILE B CG1 1 
ATOM   6096 C  CG2 . ILE B 1 262 ? -62.990  -9.958  264.818 1.00 21.79  ? 262 ILE B CG2 1 
ATOM   6097 C  CD1 . ILE B 1 262 ? -63.824  -7.195  263.985 1.00 24.55  ? 262 ILE B CD1 1 
ATOM   6098 N  N   . GLY B 1 263 ? -61.824  -11.205 268.070 1.00 19.66  ? 263 GLY B N   1 
ATOM   6099 C  CA  . GLY B 1 263 ? -60.891  -12.291 268.294 1.00 23.59  ? 263 GLY B CA  1 
ATOM   6100 C  C   . GLY B 1 263 ? -60.668  -12.627 269.753 1.00 27.45  ? 263 GLY B C   1 
ATOM   6101 O  O   . GLY B 1 263 ? -61.623  -12.858 270.500 1.00 31.90  ? 263 GLY B O   1 
ATOM   6102 N  N   . GLY B 1 264 ? -59.411  -12.658 270.168 1.00 26.56  ? 264 GLY B N   1 
ATOM   6103 C  CA  . GLY B 1 264 ? -59.043  -13.022 271.517 1.00 27.03  ? 264 GLY B CA  1 
ATOM   6104 C  C   . GLY B 1 264 ? -58.268  -14.323 271.568 1.00 30.23  ? 264 GLY B C   1 
ATOM   6105 O  O   . GLY B 1 264 ? -57.708  -14.796 270.575 1.00 41.13  ? 264 GLY B O   1 
ATOM   6106 N  N   . TRP B 1 265 ? -58.242  -14.915 272.763 1.00 29.79  ? 265 TRP B N   1 
ATOM   6107 C  CA  . TRP B 1 265 ? -57.525  -16.173 272.946 1.00 31.05  ? 265 TRP B CA  1 
ATOM   6108 C  C   . TRP B 1 265 ? -58.244  -17.327 272.258 1.00 26.70  ? 265 TRP B C   1 
ATOM   6109 O  O   . TRP B 1 265 ? -57.608  -18.153 271.592 1.00 27.50  ? 265 TRP B O   1 
ATOM   6110 C  CB  . TRP B 1 265 ? -57.350  -16.463 274.437 1.00 41.70  ? 265 TRP B CB  1 
ATOM   6111 C  CG  . TRP B 1 265 ? -56.612  -17.736 274.731 1.00 33.00  ? 265 TRP B CG  1 
ATOM   6112 C  CD1 . TRP B 1 265 ? -57.135  -18.886 275.249 1.00 29.28  ? 265 TRP B CD1 1 
ATOM   6113 C  CD2 . TRP B 1 265 ? -55.215  -17.986 274.532 1.00 32.80  ? 265 TRP B CD2 1 
ATOM   6114 N  NE1 . TRP B 1 265 ? -56.152  -19.836 275.382 1.00 28.45  ? 265 TRP B NE1 1 
ATOM   6115 C  CE2 . TRP B 1 265 ? -54.964  -19.309 274.948 1.00 33.19  ? 265 TRP B CE2 1 
ATOM   6116 C  CE3 . TRP B 1 265 ? -54.152  -17.221 274.040 1.00 32.88  ? 265 TRP B CE3 1 
ATOM   6117 C  CZ2 . TRP B 1 265 ? -53.696  -19.883 274.888 1.00 37.52  ? 265 TRP B CZ2 1 
ATOM   6118 C  CZ3 . TRP B 1 265 ? -52.894  -17.793 273.981 1.00 32.42  ? 265 TRP B CZ3 1 
ATOM   6119 C  CH2 . TRP B 1 265 ? -52.677  -19.111 274.403 1.00 35.53  ? 265 TRP B CH2 1 
ATOM   6120 N  N   . THR B 1 266 ? -59.567  -17.398 272.399 1.00 25.69  ? 266 THR B N   1 
ATOM   6121 C  CA  . THR B 1 266 ? -60.341  -18.525 271.899 1.00 24.50  ? 266 THR B CA  1 
ATOM   6122 C  C   . THR B 1 266 ? -60.976  -18.275 270.537 1.00 25.50  ? 266 THR B C   1 
ATOM   6123 O  O   . THR B 1 266 ? -61.433  -19.231 269.903 1.00 25.94  ? 266 THR B O   1 
ATOM   6124 C  CB  . THR B 1 266 ? -61.443  -18.894 272.900 1.00 22.42  ? 266 THR B CB  1 
ATOM   6125 O  OG1 . THR B 1 266 ? -62.319  -17.775 273.082 1.00 20.38  ? 266 THR B OG1 1 
ATOM   6126 C  CG2 . THR B 1 266 ? -60.837  -19.276 274.240 1.00 23.52  ? 266 THR B CG2 1 
ATOM   6127 N  N   . LEU B 1 267 ? -61.015  -17.028 270.071 1.00 27.46  ? 267 LEU B N   1 
ATOM   6128 C  CA  . LEU B 1 267 ? -61.701  -16.686 268.832 1.00 25.21  ? 267 LEU B CA  1 
ATOM   6129 C  C   . LEU B 1 267 ? -60.744  -16.306 267.709 1.00 37.59  ? 267 LEU B C   1 
ATOM   6130 O  O   . LEU B 1 267 ? -61.183  -15.746 266.699 1.00 56.84  ? 267 LEU B O   1 
ATOM   6131 C  CB  . LEU B 1 267 ? -62.693  -15.547 269.081 1.00 23.64  ? 267 LEU B CB  1 
ATOM   6132 C  CG  . LEU B 1 267 ? -63.877  -15.886 269.986 1.00 26.04  ? 267 LEU B CG  1 
ATOM   6133 C  CD1 . LEU B 1 267 ? -64.608  -14.625 270.417 1.00 23.35  ? 267 LEU B CD1 1 
ATOM   6134 C  CD2 . LEU B 1 267 ? -64.823  -16.843 269.284 1.00 36.17  ? 267 LEU B CD2 1 
ATOM   6135 N  N   . SER B 1 268 ? -59.453  -16.599 267.853 1.00 30.16  ? 268 SER B N   1 
ATOM   6136 C  CA  . SER B 1 268 ? -58.465  -16.231 266.849 1.00 28.32  ? 268 SER B CA  1 
ATOM   6137 C  C   . SER B 1 268 ? -58.281  -17.287 265.768 1.00 27.76  ? 268 SER B C   1 
ATOM   6138 O  O   . SER B 1 268 ? -57.535  -17.044 264.813 1.00 26.33  ? 268 SER B O   1 
ATOM   6139 C  CB  . SER B 1 268 ? -57.114  -15.953 267.516 1.00 35.28  ? 268 SER B CB  1 
ATOM   6140 O  OG  . SER B 1 268 ? -57.185  -14.818 268.360 1.00 38.57  ? 268 SER B OG  1 
ATOM   6141 N  N   . ASP B 1 269 ? -58.941  -18.437 265.888 1.00 31.00  ? 269 ASP B N   1 
ATOM   6142 C  CA  . ASP B 1 269 ? -58.724  -19.521 264.933 1.00 32.43  ? 269 ASP B CA  1 
ATOM   6143 C  C   . ASP B 1 269 ? -59.084  -19.171 263.491 1.00 32.46  ? 269 ASP B C   1 
ATOM   6144 O  O   . ASP B 1 269 ? -58.325  -19.569 262.590 1.00 32.41  ? 269 ASP B O   1 
ATOM   6145 C  CB  . ASP B 1 269 ? -59.488  -20.769 265.393 1.00 31.74  ? 269 ASP B CB  1 
ATOM   6146 C  CG  . ASP B 1 269 ? -58.811  -21.468 266.552 1.00 30.55  ? 269 ASP B CG  1 
ATOM   6147 O  OD1 . ASP B 1 269 ? -58.035  -20.806 267.272 1.00 25.58  ? 269 ASP B OD1 1 
ATOM   6148 O  OD2 . ASP B 1 269 ? -59.052  -22.678 266.741 1.00 43.28  ? 269 ASP B OD2 1 
ATOM   6149 N  N   . PRO B 1 270 ? -60.185  -18.472 263.189 1.00 30.04  ? 270 PRO B N   1 
ATOM   6150 C  CA  . PRO B 1 270 ? -60.469  -18.153 261.779 1.00 29.15  ? 270 PRO B CA  1 
ATOM   6151 C  C   . PRO B 1 270 ? -59.423  -17.266 261.126 1.00 30.31  ? 270 PRO B C   1 
ATOM   6152 O  O   . PRO B 1 270 ? -59.384  -17.190 259.892 1.00 34.04  ? 270 PRO B O   1 
ATOM   6153 C  CB  . PRO B 1 270 ? -61.832  -17.451 261.843 1.00 33.32  ? 270 PRO B CB  1 
ATOM   6154 C  CG  . PRO B 1 270 ? -62.445  -17.932 263.104 1.00 44.51  ? 270 PRO B CG  1 
ATOM   6155 C  CD  . PRO B 1 270 ? -61.305  -18.075 264.062 1.00 31.11  ? 270 PRO B CD  1 
ATOM   6156 N  N   . PHE B 1 271 ? -58.576  -16.595 261.910 1.00 33.09  ? 271 PHE B N   1 
ATOM   6157 C  CA  . PHE B 1 271 ? -57.580  -15.698 261.334 1.00 34.34  ? 271 PHE B CA  1 
ATOM   6158 C  C   . PHE B 1 271 ? -56.543  -16.459 260.517 1.00 35.11  ? 271 PHE B C   1 
ATOM   6159 O  O   . PHE B 1 271 ? -56.107  -15.985 259.461 1.00 40.26  ? 271 PHE B O   1 
ATOM   6160 C  CB  . PHE B 1 271 ? -56.897  -14.897 262.442 1.00 33.43  ? 271 PHE B CB  1 
ATOM   6161 C  CG  . PHE B 1 271 ? -57.737  -13.785 262.997 1.00 29.26  ? 271 PHE B CG  1 
ATOM   6162 C  CD1 . PHE B 1 271 ? -58.442  -12.943 262.154 1.00 28.09  ? 271 PHE B CD1 1 
ATOM   6163 C  CD2 . PHE B 1 271 ? -57.822  -13.581 264.363 1.00 29.58  ? 271 PHE B CD2 1 
ATOM   6164 C  CE1 . PHE B 1 271 ? -59.214  -11.918 262.664 1.00 28.40  ? 271 PHE B CE1 1 
ATOM   6165 C  CE2 . PHE B 1 271 ? -58.593  -12.558 264.879 1.00 24.69  ? 271 PHE B CE2 1 
ATOM   6166 C  CZ  . PHE B 1 271 ? -59.290  -11.726 264.028 1.00 26.13  ? 271 PHE B CZ  1 
ATOM   6167 N  N   . TYR B 1 272 ? -56.135  -17.640 260.988 1.00 33.85  ? 272 TYR B N   1 
ATOM   6168 C  CA  . TYR B 1 272 ? -55.073  -18.387 260.322 1.00 37.81  ? 272 TYR B CA  1 
ATOM   6169 C  C   . TYR B 1 272 ? -55.452  -18.812 258.910 1.00 43.28  ? 272 TYR B C   1 
ATOM   6170 O  O   . TYR B 1 272 ? -54.562  -19.029 258.081 1.00 49.46  ? 272 TYR B O   1 
ATOM   6171 C  CB  . TYR B 1 272 ? -54.696  -19.618 261.149 1.00 38.30  ? 272 TYR B CB  1 
ATOM   6172 C  CG  . TYR B 1 272 ? -54.216  -19.300 262.547 1.00 35.05  ? 272 TYR B CG  1 
ATOM   6173 C  CD1 . TYR B 1 272 ? -55.109  -19.209 263.605 1.00 35.52  ? 272 TYR B CD1 1 
ATOM   6174 C  CD2 . TYR B 1 272 ? -52.868  -19.094 262.808 1.00 42.73  ? 272 TYR B CD2 1 
ATOM   6175 C  CE1 . TYR B 1 272 ? -54.674  -18.918 264.884 1.00 36.11  ? 272 TYR B CE1 1 
ATOM   6176 C  CE2 . TYR B 1 272 ? -52.424  -18.803 264.083 1.00 41.22  ? 272 TYR B CE2 1 
ATOM   6177 C  CZ  . TYR B 1 272 ? -53.331  -18.717 265.117 1.00 38.13  ? 272 TYR B CZ  1 
ATOM   6178 O  OH  . TYR B 1 272 ? -52.894  -18.428 266.389 1.00 39.03  ? 272 TYR B OH  1 
ATOM   6179 N  N   . PHE B 1 273 ? -56.744  -18.936 258.617 1.00 40.56  ? 273 PHE B N   1 
ATOM   6180 C  CA  . PHE B 1 273 ? -57.204  -19.352 257.299 1.00 38.15  ? 273 PHE B CA  1 
ATOM   6181 C  C   . PHE B 1 273 ? -57.398  -18.185 256.342 1.00 35.34  ? 273 PHE B C   1 
ATOM   6182 O  O   . PHE B 1 273 ? -57.716  -18.412 255.170 1.00 35.35  ? 273 PHE B O   1 
ATOM   6183 C  CB  . PHE B 1 273 ? -58.516  -20.131 257.422 1.00 36.17  ? 273 PHE B CB  1 
ATOM   6184 C  CG  . PHE B 1 273 ? -58.421  -21.340 258.302 1.00 34.17  ? 273 PHE B CG  1 
ATOM   6185 C  CD1 . PHE B 1 273 ? -57.958  -22.543 257.798 1.00 39.43  ? 273 PHE B CD1 1 
ATOM   6186 C  CD2 . PHE B 1 273 ? -58.791  -21.274 259.634 1.00 32.23  ? 273 PHE B CD2 1 
ATOM   6187 C  CE1 . PHE B 1 273 ? -57.868  -23.659 258.606 1.00 53.91  ? 273 PHE B CE1 1 
ATOM   6188 C  CE2 . PHE B 1 273 ? -58.704  -22.385 260.447 1.00 33.94  ? 273 PHE B CE2 1 
ATOM   6189 C  CZ  . PHE B 1 273 ? -58.241  -23.579 259.932 1.00 40.68  ? 273 PHE B CZ  1 
ATOM   6190 N  N   . MET B 1 274 ? -57.213  -16.951 256.804 1.00 34.80  ? 274 MET B N   1 
ATOM   6191 C  CA  . MET B 1 274 ? -57.437  -15.777 255.971 1.00 37.92  ? 274 MET B CA  1 
ATOM   6192 C  C   . MET B 1 274 ? -56.310  -15.521 254.979 1.00 44.34  ? 274 MET B C   1 
ATOM   6193 O  O   . MET B 1 274 ? -56.300  -14.463 254.340 1.00 51.97  ? 274 MET B O   1 
ATOM   6194 C  CB  . MET B 1 274 ? -57.659  -14.542 256.848 1.00 37.35  ? 274 MET B CB  1 
ATOM   6195 C  CG  . MET B 1 274 ? -58.885  -14.652 257.737 1.00 40.45  ? 274 MET B CG  1 
ATOM   6196 S  SD  . MET B 1 274 ? -59.335  -13.106 258.541 1.00 33.90  ? 274 MET B SD  1 
ATOM   6197 C  CE  . MET B 1 274 ? -60.692  -13.657 259.571 1.00 32.92  ? 274 MET B CE  1 
ATOM   6198 N  N   . HIS B 1 275 ? -55.363  -16.452 254.833 1.00 44.05  ? 275 HIS B N   1 
ATOM   6199 C  CA  . HIS B 1 275 ? -54.411  -16.346 253.734 1.00 46.48  ? 275 HIS B CA  1 
ATOM   6200 C  C   . HIS B 1 275 ? -55.111  -16.500 252.391 1.00 45.78  ? 275 HIS B C   1 
ATOM   6201 O  O   . HIS B 1 275 ? -54.637  -15.971 251.379 1.00 47.27  ? 275 HIS B O   1 
ATOM   6202 C  CB  . HIS B 1 275 ? -53.300  -17.386 253.887 1.00 47.49  ? 275 HIS B CB  1 
ATOM   6203 C  CG  . HIS B 1 275 ? -53.793  -18.798 253.939 1.00 55.17  ? 275 HIS B CG  1 
ATOM   6204 N  ND1 . HIS B 1 275 ? -54.167  -19.413 255.115 1.00 69.29  ? 275 HIS B ND1 1 
ATOM   6205 C  CD2 . HIS B 1 275 ? -53.966  -19.718 252.962 1.00 50.14  ? 275 HIS B CD2 1 
ATOM   6206 C  CE1 . HIS B 1 275 ? -54.553  -20.650 254.858 1.00 48.91  ? 275 HIS B CE1 1 
ATOM   6207 N  NE2 . HIS B 1 275 ? -54.441  -20.860 253.559 1.00 50.17  ? 275 HIS B NE2 1 
ATOM   6208 N  N   . ASP B 1 276 ? -56.234  -17.214 252.365 1.00 44.99  ? 276 ASP B N   1 
ATOM   6209 C  CA  . ASP B 1 276 ? -57.092  -17.223 251.189 1.00 46.22  ? 276 ASP B CA  1 
ATOM   6210 C  C   . ASP B 1 276 ? -57.668  -15.831 250.966 1.00 49.51  ? 276 ASP B C   1 
ATOM   6211 O  O   . ASP B 1 276 ? -58.185  -15.203 251.895 1.00 51.55  ? 276 ASP B O   1 
ATOM   6212 C  CB  . ASP B 1 276 ? -58.217  -18.243 251.363 1.00 47.12  ? 276 ASP B CB  1 
ATOM   6213 C  CG  . ASP B 1 276 ? -58.948  -18.535 250.066 1.00 47.23  ? 276 ASP B CG  1 
ATOM   6214 O  OD1 . ASP B 1 276 ? -58.613  -17.914 249.036 1.00 53.77  ? 276 ASP B OD1 1 
ATOM   6215 O  OD2 . ASP B 1 276 ? -59.863  -19.383 250.078 1.00 46.18  ? 276 ASP B OD2 1 
ATOM   6216 N  N   . VAL B 1 277 ? -57.577  -15.347 249.725 1.00 54.78  ? 277 VAL B N   1 
ATOM   6217 C  CA  . VAL B 1 277 ? -58.020  -13.990 249.434 1.00 54.54  ? 277 VAL B CA  1 
ATOM   6218 C  C   . VAL B 1 277 ? -59.538  -13.875 249.414 1.00 52.87  ? 277 VAL B C   1 
ATOM   6219 O  O   . VAL B 1 277 ? -60.071  -12.777 249.610 1.00 52.25  ? 277 VAL B O   1 
ATOM   6220 C  CB  . VAL B 1 277 ? -57.421  -13.502 248.101 1.00 61.40  ? 277 VAL B CB  1 
ATOM   6221 C  CG1 . VAL B 1 277 ? -55.929  -13.794 248.053 1.00 62.21  ? 277 VAL B CG1 1 
ATOM   6222 C  CG2 . VAL B 1 277 ? -58.131  -14.147 246.922 1.00 91.80  ? 277 VAL B CG2 1 
ATOM   6223 N  N   . GLU B 1 278 ? -60.255  -14.978 249.193 1.00 59.35  ? 278 GLU B N   1 
ATOM   6224 C  CA  . GLU B 1 278 ? -61.707  -14.933 249.090 1.00 56.68  ? 278 GLU B CA  1 
ATOM   6225 C  C   . GLU B 1 278 ? -62.418  -15.304 250.385 1.00 51.85  ? 278 GLU B C   1 
ATOM   6226 O  O   . GLU B 1 278 ? -63.635  -15.119 250.474 1.00 61.66  ? 278 GLU B O   1 
ATOM   6227 C  CB  . GLU B 1 278 ? -62.191  -15.840 247.954 1.00 64.25  ? 278 GLU B CB  1 
ATOM   6228 C  CG  . GLU B 1 278 ? -62.910  -15.075 246.853 1.00 80.06  ? 278 GLU B CG  1 
ATOM   6229 C  CD  . GLU B 1 278 ? -63.011  -15.854 245.558 1.00 100.68 ? 278 GLU B CD  1 
ATOM   6230 O  OE1 . GLU B 1 278 ? -63.381  -17.045 245.603 1.00 82.68  ? 278 GLU B OE1 1 
ATOM   6231 O  OE2 . GLU B 1 278 ? -62.719  -15.270 244.493 1.00 103.03 ? 278 GLU B OE2 1 
ATOM   6232 N  N   . LYS B 1 279 ? -61.701  -15.824 251.380 1.00 48.83  ? 279 LYS B N   1 
ATOM   6233 C  CA  . LYS B 1 279 ? -62.234  -15.927 252.731 1.00 45.43  ? 279 LYS B CA  1 
ATOM   6234 C  C   . LYS B 1 279 ? -61.770  -14.787 253.626 1.00 42.97  ? 279 LYS B C   1 
ATOM   6235 O  O   . LYS B 1 279 ? -62.230  -14.688 254.768 1.00 44.85  ? 279 LYS B O   1 
ATOM   6236 C  CB  . LYS B 1 279 ? -61.852  -17.270 253.368 1.00 46.20  ? 279 LYS B CB  1 
ATOM   6237 C  CG  . LYS B 1 279 ? -62.095  -18.475 252.475 1.00 50.87  ? 279 LYS B CG  1 
ATOM   6238 C  CD  . LYS B 1 279 ? -61.937  -19.774 253.249 1.00 52.40  ? 279 LYS B CD  1 
ATOM   6239 C  CE  . LYS B 1 279 ? -61.584  -20.934 252.332 1.00 70.52  ? 279 LYS B CE  1 
ATOM   6240 N  NZ  . LYS B 1 279 ? -61.468  -22.218 253.079 1.00 48.60  ? 279 LYS B NZ  1 
ATOM   6241 N  N   . ARG B 1 280 ? -60.877  -13.929 253.134 1.00 44.69  ? 280 ARG B N   1 
ATOM   6242 C  CA  . ARG B 1 280 ? -60.441  -12.741 253.855 1.00 42.29  ? 280 ARG B CA  1 
ATOM   6243 C  C   . ARG B 1 280 ? -61.305  -11.530 253.525 1.00 41.63  ? 280 ARG B C   1 
ATOM   6244 O  O   . ARG B 1 280 ? -61.803  -10.854 254.430 1.00 43.21  ? 280 ARG B O   1 
ATOM   6245 C  CB  . ARG B 1 280 ? -58.976  -12.439 253.532 1.00 48.50  ? 280 ARG B CB  1 
ATOM   6246 C  CG  . ARG B 1 280 ? -58.394  -11.272 254.307 1.00 46.77  ? 280 ARG B CG  1 
ATOM   6247 C  CD  . ARG B 1 280 ? -56.937  -11.036 253.943 1.00 51.50  ? 280 ARG B CD  1 
ATOM   6248 N  NE  . ARG B 1 280 ? -56.792  -10.674 252.535 1.00 52.02  ? 280 ARG B NE  1 
ATOM   6249 C  CZ  . ARG B 1 280 ? -56.417  -11.519 251.581 1.00 73.25  ? 280 ARG B CZ  1 
ATOM   6250 N  NH1 . ARG B 1 280 ? -56.128  -12.778 251.882 1.00 57.24  ? 280 ARG B NH1 1 
ATOM   6251 N  NH2 . ARG B 1 280 ? -56.323  -11.103 250.325 1.00 80.28  ? 280 ARG B NH2 1 
ATOM   6252 N  N   . ASN B 1 281 ? -61.489  -11.242 252.233 1.00 44.18  ? 281 ASN B N   1 
ATOM   6253 C  CA  . ASN B 1 281 ? -62.337  -10.122 251.845 1.00 44.26  ? 281 ASN B CA  1 
ATOM   6254 C  C   . ASN B 1 281 ? -63.774  -10.324 252.298 1.00 43.78  ? 281 ASN B C   1 
ATOM   6255 O  O   . ASN B 1 281 ? -64.506  -9.342  252.462 1.00 48.52  ? 281 ASN B O   1 
ATOM   6256 C  CB  . ASN B 1 281 ? -62.285  -9.906  250.331 1.00 45.53  ? 281 ASN B CB  1 
ATOM   6257 C  CG  . ASN B 1 281 ? -62.757  -11.114 249.553 1.00 52.33  ? 281 ASN B CG  1 
ATOM   6258 O  OD1 . ASN B 1 281 ? -62.927  -12.198 250.109 1.00 86.32  ? 281 ASN B OD1 1 
ATOM   6259 N  ND2 . ASN B 1 281 ? -62.971  -10.934 248.254 1.00 50.05  ? 281 ASN B ND2 1 
ATOM   6260 N  N   . VAL B 1 282 ? -64.195  -11.574 252.498 1.00 45.13  ? 282 VAL B N   1 
ATOM   6261 C  CA  . VAL B 1 282 ? -65.473  -11.828 253.157 1.00 43.01  ? 282 VAL B CA  1 
ATOM   6262 C  C   . VAL B 1 282 ? -65.462  -11.241 254.561 1.00 41.41  ? 282 VAL B C   1 
ATOM   6263 O  O   . VAL B 1 282 ? -66.354  -10.475 254.939 1.00 48.38  ? 282 VAL B O   1 
ATOM   6264 C  CB  . VAL B 1 282 ? -65.779  -13.336 253.178 1.00 47.60  ? 282 VAL B CB  1 
ATOM   6265 C  CG1 . VAL B 1 282 ? -66.893  -13.634 254.164 1.00 42.94  ? 282 VAL B CG1 1 
ATOM   6266 C  CG2 . VAL B 1 282 ? -66.174  -13.811 251.793 1.00 59.87  ? 282 VAL B CG2 1 
ATOM   6267 N  N   . PHE B 1 283 ? -64.436  -11.575 255.348 1.00 40.65  ? 283 PHE B N   1 
ATOM   6268 C  CA  . PHE B 1 283 ? -64.361  -11.094 256.725 1.00 38.30  ? 283 PHE B CA  1 
ATOM   6269 C  C   . PHE B 1 283 ? -64.324  -9.572  256.793 1.00 40.14  ? 283 PHE B C   1 
ATOM   6270 O  O   . PHE B 1 283 ? -64.895  -8.972  257.711 1.00 45.96  ? 283 PHE B O   1 
ATOM   6271 C  CB  . PHE B 1 283 ? -63.132  -11.686 257.413 1.00 43.90  ? 283 PHE B CB  1 
ATOM   6272 C  CG  . PHE B 1 283 ? -62.748  -10.977 258.678 1.00 32.55  ? 283 PHE B CG  1 
ATOM   6273 C  CD1 . PHE B 1 283 ? -63.491  -11.141 259.834 1.00 30.51  ? 283 PHE B CD1 1 
ATOM   6274 C  CD2 . PHE B 1 283 ? -61.641  -10.147 258.711 1.00 35.85  ? 283 PHE B CD2 1 
ATOM   6275 C  CE1 . PHE B 1 283 ? -63.137  -10.488 260.997 1.00 29.80  ? 283 PHE B CE1 1 
ATOM   6276 C  CE2 . PHE B 1 283 ? -61.283  -9.492  259.871 1.00 34.03  ? 283 PHE B CE2 1 
ATOM   6277 C  CZ  . PHE B 1 283 ? -62.032  -9.663  261.016 1.00 30.14  ? 283 PHE B CZ  1 
ATOM   6278 N  N   . VAL B 1 284 ? -63.658  -8.931  255.832 1.00 40.78  ? 284 VAL B N   1 
ATOM   6279 C  CA  . VAL B 1 284 ? -63.462  -7.486  255.900 1.00 42.68  ? 284 VAL B CA  1 
ATOM   6280 C  C   . VAL B 1 284 ? -64.782  -6.743  255.727 1.00 44.24  ? 284 VAL B C   1 
ATOM   6281 O  O   . VAL B 1 284 ? -64.945  -5.624  256.231 1.00 66.75  ? 284 VAL B O   1 
ATOM   6282 C  CB  . VAL B 1 284 ? -62.418  -7.060  254.847 1.00 56.69  ? 284 VAL B CB  1 
ATOM   6283 C  CG1 . VAL B 1 284 ? -62.268  -5.545  254.796 1.00 45.72  ? 284 VAL B CG1 1 
ATOM   6284 C  CG2 . VAL B 1 284 ? -61.079  -7.725  255.129 1.00 54.94  ? 284 VAL B CG2 1 
ATOM   6285 N  N   . ASP B 1 285 ? -65.759  -7.360  255.060 1.00 41.91  ? 285 ASP B N   1 
ATOM   6286 C  CA  . ASP B 1 285 ? -66.915  -6.606  254.583 1.00 43.28  ? 285 ASP B CA  1 
ATOM   6287 C  C   . ASP B 1 285 ? -67.880  -6.248  255.711 1.00 44.80  ? 285 ASP B C   1 
ATOM   6288 O  O   . ASP B 1 285 ? -68.475  -5.165  255.693 1.00 45.05  ? 285 ASP B O   1 
ATOM   6289 C  CB  . ASP B 1 285 ? -67.629  -7.390  253.485 1.00 42.22  ? 285 ASP B CB  1 
ATOM   6290 C  CG  . ASP B 1 285 ? -66.867  -7.372  252.176 1.00 40.80  ? 285 ASP B CG  1 
ATOM   6291 O  OD1 . ASP B 1 285 ? -65.722  -6.874  252.167 1.00 48.38  ? 285 ASP B OD1 1 
ATOM   6292 O  OD2 . ASP B 1 285 ? -67.409  -7.850  251.160 1.00 35.97  ? 285 ASP B OD2 1 
ATOM   6293 N  N   . SER B 1 286 ? -68.075  -7.137  256.689 1.00 44.18  ? 286 SER B N   1 
ATOM   6294 C  CA  . SER B 1 286 ? -68.949  -6.771  257.803 1.00 47.26  ? 286 SER B CA  1 
ATOM   6295 C  C   . SER B 1 286 ? -68.332  -5.702  258.688 1.00 44.86  ? 286 SER B C   1 
ATOM   6296 O  O   . SER B 1 286 ? -69.060  -4.871  259.239 1.00 42.80  ? 286 SER B O   1 
ATOM   6297 C  CB  . SER B 1 286 ? -69.336  -7.988  258.637 1.00 51.49  ? 286 SER B CB  1 
ATOM   6298 O  OG  . SER B 1 286 ? -70.525  -8.569  258.129 1.00 100.21 ? 286 SER B OG  1 
ATOM   6299 N  N   . VAL B 1 287 ? -67.006  -5.680  258.827 1.00 45.23  ? 287 VAL B N   1 
ATOM   6300 C  CA  . VAL B 1 287 ? -66.388  -4.573  259.546 1.00 48.18  ? 287 VAL B CA  1 
ATOM   6301 C  C   . VAL B 1 287 ? -66.800  -3.238  258.941 1.00 65.36  ? 287 VAL B C   1 
ATOM   6302 O  O   . VAL B 1 287 ? -66.748  -2.206  259.615 1.00 85.46  ? 287 VAL B O   1 
ATOM   6303 C  CB  . VAL B 1 287 ? -64.858  -4.751  259.570 1.00 64.52  ? 287 VAL B CB  1 
ATOM   6304 C  CG1 . VAL B 1 287 ? -64.236  -3.764  260.519 1.00 68.12  ? 287 VAL B CG1 1 
ATOM   6305 C  CG2 . VAL B 1 287 ? -64.501  -6.177  259.969 1.00 52.83  ? 287 VAL B CG2 1 
ATOM   6306 N  N   . LYS B 1 288 ? -67.247  -3.244  257.687 1.00 47.28  ? 288 LYS B N   1 
ATOM   6307 C  CA  . LYS B 1 288 ? -67.963  -2.128  257.092 1.00 45.51  ? 288 LYS B CA  1 
ATOM   6308 C  C   . LYS B 1 288 ? -69.457  -2.196  257.382 1.00 42.30  ? 288 LYS B C   1 
ATOM   6309 O  O   . LYS B 1 288 ? -70.092  -1.158  257.580 1.00 48.99  ? 288 LYS B O   1 
ATOM   6310 C  CB  . LYS B 1 288 ? -67.723  -2.108  255.580 1.00 48.62  ? 288 LYS B CB  1 
ATOM   6311 C  CG  . LYS B 1 288 ? -68.538  -1.097  254.777 1.00 43.48  ? 288 LYS B CG  1 
ATOM   6312 C  CD  . LYS B 1 288 ? -68.035  -1.042  253.344 1.00 41.14  ? 288 LYS B CD  1 
ATOM   6313 C  CE  . LYS B 1 288 ? -68.699  0.070   252.568 1.00 50.30  ? 288 LYS B CE  1 
ATOM   6314 N  NZ  . LYS B 1 288 ? -68.071  0.269   251.239 1.00 67.92  ? 288 LYS B NZ  1 
ATOM   6315 N  N   . GLU B 1 289 ? -70.027  -3.402  257.423 1.00 42.39  ? 289 GLU B N   1 
ATOM   6316 C  CA  . GLU B 1 289 ? -71.460  -3.594  257.627 1.00 39.58  ? 289 GLU B CA  1 
ATOM   6317 C  C   . GLU B 1 289 ? -71.837  -3.659  259.105 1.00 35.86  ? 289 GLU B C   1 
ATOM   6318 O  O   . GLU B 1 289 ? -72.870  -3.111  259.504 1.00 49.09  ? 289 GLU B O   1 
ATOM   6319 C  CB  . GLU B 1 289 ? -71.916  -4.873  256.918 1.00 41.57  ? 289 GLU B CB  1 
ATOM   6320 C  CG  . GLU B 1 289 ? -73.386  -5.212  257.092 1.00 42.47  ? 289 GLU B CG  1 
ATOM   6321 C  CD  . GLU B 1 289 ? -74.270  -4.526  256.068 1.00 44.05  ? 289 GLU B CD  1 
ATOM   6322 O  OE1 . GLU B 1 289 ? -73.747  -4.122  255.010 1.00 50.26  ? 289 GLU B OE1 1 
ATOM   6323 O  OE2 . GLU B 1 289 ? -75.488  -4.394  256.315 1.00 46.27  ? 289 GLU B OE2 1 
ATOM   6324 N  N   . PHE B 1 290 ? -71.023  -4.336  259.920 1.00 35.40  ? 290 PHE B N   1 
ATOM   6325 C  CA  . PHE B 1 290 ? -71.251  -4.374  261.363 1.00 33.89  ? 290 PHE B CA  1 
ATOM   6326 C  C   . PHE B 1 290 ? -71.258  -2.971  261.956 1.00 31.15  ? 290 PHE B C   1 
ATOM   6327 O  O   . PHE B 1 290 ? -72.007  -2.689  262.898 1.00 35.39  ? 290 PHE B O   1 
ATOM   6328 C  CB  . PHE B 1 290 ? -70.173  -5.239  262.026 1.00 35.09  ? 290 PHE B CB  1 
ATOM   6329 C  CG  . PHE B 1 290 ? -70.459  -5.610  263.454 1.00 28.08  ? 290 PHE B CG  1 
ATOM   6330 C  CD1 . PHE B 1 290 ? -70.149  -4.740  264.486 1.00 28.19  ? 290 PHE B CD1 1 
ATOM   6331 C  CD2 . PHE B 1 290 ? -71.001  -6.844  263.766 1.00 30.54  ? 290 PHE B CD2 1 
ATOM   6332 C  CE1 . PHE B 1 290 ? -70.396  -5.084  265.799 1.00 28.39  ? 290 PHE B CE1 1 
ATOM   6333 C  CE2 . PHE B 1 290 ? -71.251  -7.194  265.080 1.00 35.98  ? 290 PHE B CE2 1 
ATOM   6334 C  CZ  . PHE B 1 290 ? -70.948  -6.313  266.097 1.00 28.53  ? 290 PHE B CZ  1 
ATOM   6335 N  N   . LEU B 1 291 ? -70.433  -2.074  261.413 1.00 30.60  ? 291 LEU B N   1 
ATOM   6336 C  CA  . LEU B 1 291 ? -70.362  -0.714  261.932 1.00 29.13  ? 291 LEU B CA  1 
ATOM   6337 C  C   . LEU B 1 291 ? -71.503  0.166   261.441 1.00 27.81  ? 291 LEU B C   1 
ATOM   6338 O  O   . LEU B 1 291 ? -71.830  1.155   262.106 1.00 28.01  ? 291 LEU B O   1 
ATOM   6339 C  CB  . LEU B 1 291 ? -69.019  -0.078  261.567 1.00 33.52  ? 291 LEU B CB  1 
ATOM   6340 C  CG  . LEU B 1 291 ? -67.796  -0.715  262.231 1.00 33.46  ? 291 LEU B CG  1 
ATOM   6341 C  CD1 . LEU B 1 291 ? -66.516  0.024   261.862 1.00 36.37  ? 291 LEU B CD1 1 
ATOM   6342 C  CD2 . LEU B 1 291 ? -67.966  -0.787  263.736 1.00 27.48  ? 291 LEU B CD2 1 
ATOM   6343 N  N   . GLN B 1 292 ? -72.108  -0.157  260.295 1.00 25.77  ? 292 GLN B N   1 
ATOM   6344 C  CA  . GLN B 1 292 ? -73.319  0.548   259.888 1.00 25.99  ? 292 GLN B CA  1 
ATOM   6345 C  C   . GLN B 1 292 ? -74.530  0.062   260.674 1.00 27.67  ? 292 GLN B C   1 
ATOM   6346 O  O   . GLN B 1 292 ? -75.421  0.854   260.998 1.00 35.63  ? 292 GLN B O   1 
ATOM   6347 C  CB  . GLN B 1 292 ? -73.558  0.384   258.387 1.00 30.35  ? 292 GLN B CB  1 
ATOM   6348 C  CG  . GLN B 1 292 ? -72.385  0.804   257.525 1.00 36.82  ? 292 GLN B CG  1 
ATOM   6349 C  CD  . GLN B 1 292 ? -72.593  0.480   256.059 1.00 39.19  ? 292 GLN B CD  1 
ATOM   6350 O  OE1 . GLN B 1 292 ? -73.707  0.186   255.629 1.00 49.27  ? 292 GLN B OE1 1 
ATOM   6351 N  NE2 . GLN B 1 292 ? -71.516  0.532   255.283 1.00 43.35  ? 292 GLN B NE2 1 
ATOM   6352 N  N   . VAL B 1 293 ? -74.585  -1.235  260.980 1.00 27.33  ? 293 VAL B N   1 
ATOM   6353 C  CA  . VAL B 1 293 ? -75.633  -1.739  261.860 1.00 25.80  ? 293 VAL B CA  1 
ATOM   6354 C  C   . VAL B 1 293 ? -75.435  -1.204  263.271 1.00 23.91  ? 293 VAL B C   1 
ATOM   6355 O  O   . VAL B 1 293 ? -76.352  -0.637  263.874 1.00 22.94  ? 293 VAL B O   1 
ATOM   6356 C  CB  . VAL B 1 293 ? -75.661  -3.278  261.837 1.00 25.81  ? 293 VAL B CB  1 
ATOM   6357 C  CG1 . VAL B 1 293 ? -76.498  -3.810  262.991 1.00 23.60  ? 293 VAL B CG1 1 
ATOM   6358 C  CG2 . VAL B 1 293 ? -76.198  -3.778  260.506 1.00 29.32  ? 293 VAL B CG2 1 
ATOM   6359 N  N   . TRP B 1 294 ? -74.231  -1.363  263.811 1.00 25.05  ? 294 TRP B N   1 
ATOM   6360 C  CA  . TRP B 1 294 ? -73.881  -0.887  265.146 1.00 24.29  ? 294 TRP B CA  1 
ATOM   6361 C  C   . TRP B 1 294 ? -72.999  0.346   264.982 1.00 25.34  ? 294 TRP B C   1 
ATOM   6362 O  O   . TRP B 1 294 ? -71.784  0.234   264.800 1.00 29.95  ? 294 TRP B O   1 
ATOM   6363 C  CB  . TRP B 1 294 ? -73.185  -1.983  265.943 1.00 25.66  ? 294 TRP B CB  1 
ATOM   6364 C  CG  . TRP B 1 294 ? -73.914  -3.285  265.882 1.00 24.85  ? 294 TRP B CG  1 
ATOM   6365 C  CD1 . TRP B 1 294 ? -73.587  -4.373  265.128 1.00 25.46  ? 294 TRP B CD1 1 
ATOM   6366 C  CD2 . TRP B 1 294 ? -75.111  -3.630  266.587 1.00 23.58  ? 294 TRP B CD2 1 
ATOM   6367 N  NE1 . TRP B 1 294 ? -74.499  -5.380  265.329 1.00 37.60  ? 294 TRP B NE1 1 
ATOM   6368 C  CE2 . TRP B 1 294 ? -75.446  -4.948  266.220 1.00 26.21  ? 294 TRP B CE2 1 
ATOM   6369 C  CE3 . TRP B 1 294 ? -75.929  -2.955  267.497 1.00 22.37  ? 294 TRP B CE3 1 
ATOM   6370 C  CZ2 . TRP B 1 294 ? -76.563  -5.603  266.731 1.00 27.51  ? 294 TRP B CZ2 1 
ATOM   6371 C  CZ3 . TRP B 1 294 ? -77.037  -3.607  268.002 1.00 21.78  ? 294 TRP B CZ3 1 
ATOM   6372 C  CH2 . TRP B 1 294 ? -77.344  -4.917  267.618 1.00 26.74  ? 294 TRP B CH2 1 
ATOM   6373 N  N   . LYS B 1 295 ? -73.620  1.523   265.051 1.00 26.52  ? 295 LYS B N   1 
ATOM   6374 C  CA  . LYS B 1 295 ? -72.925  2.776   264.797 1.00 25.39  ? 295 LYS B CA  1 
ATOM   6375 C  C   . LYS B 1 295 ? -72.182  3.309   266.014 1.00 21.72  ? 295 LYS B C   1 
ATOM   6376 O  O   . LYS B 1 295 ? -71.355  4.214   265.865 1.00 24.09  ? 295 LYS B O   1 
ATOM   6377 C  CB  . LYS B 1 295 ? -73.924  3.824   264.301 1.00 19.26  ? 295 LYS B CB  1 
ATOM   6378 C  CG  . LYS B 1 295 ? -74.675  3.401   263.047 1.00 22.00  ? 295 LYS B CG  1 
ATOM   6379 C  CD  . LYS B 1 295 ? -75.788  4.374   262.698 1.00 20.57  ? 295 LYS B CD  1 
ATOM   6380 C  CE  . LYS B 1 295 ? -76.541  3.919   261.458 1.00 20.03  ? 295 LYS B CE  1 
ATOM   6381 N  NZ  . LYS B 1 295 ? -77.737  4.762   261.185 1.00 18.70  ? 295 LYS B NZ  1 
ATOM   6382 N  N   . PHE B 1 296 ? -72.447  2.772   267.207 1.00 20.82  ? 296 PHE B N   1 
ATOM   6383 C  CA  . PHE B 1 296 ? -71.812  3.281   268.416 1.00 21.55  ? 296 PHE B CA  1 
ATOM   6384 C  C   . PHE B 1 296 ? -70.348  2.877   268.536 1.00 21.82  ? 296 PHE B C   1 
ATOM   6385 O  O   . PHE B 1 296 ? -69.655  3.397   269.416 1.00 19.44  ? 296 PHE B O   1 
ATOM   6386 C  CB  . PHE B 1 296 ? -72.590  2.822   269.652 1.00 30.13  ? 296 PHE B CB  1 
ATOM   6387 C  CG  . PHE B 1 296 ? -72.581  1.335   269.863 1.00 24.75  ? 296 PHE B CG  1 
ATOM   6388 C  CD1 . PHE B 1 296 ? -73.484  0.523   269.199 1.00 24.18  ? 296 PHE B CD1 1 
ATOM   6389 C  CD2 . PHE B 1 296 ? -71.681  0.752   270.739 1.00 22.27  ? 296 PHE B CD2 1 
ATOM   6390 C  CE1 . PHE B 1 296 ? -73.483  -0.843  269.393 1.00 36.10  ? 296 PHE B CE1 1 
ATOM   6391 C  CE2 . PHE B 1 296 ? -71.675  -0.615  270.938 1.00 20.68  ? 296 PHE B CE2 1 
ATOM   6392 C  CZ  . PHE B 1 296 ? -72.578  -1.413  270.264 1.00 31.66  ? 296 PHE B CZ  1 
ATOM   6393 N  N   . PHE B 1 297 ? -69.866  1.973   267.689 1.00 20.75  ? 297 PHE B N   1 
ATOM   6394 C  CA  . PHE B 1 297 ? -68.445  1.663   267.650 1.00 20.86  ? 297 PHE B CA  1 
ATOM   6395 C  C   . PHE B 1 297 ? -67.705  2.705   266.819 1.00 22.09  ? 297 PHE B C   1 
ATOM   6396 O  O   . PHE B 1 297 ? -68.233  3.240   265.841 1.00 23.13  ? 297 PHE B O   1 
ATOM   6397 C  CB  . PHE B 1 297 ? -68.208  0.269   267.067 1.00 21.26  ? 297 PHE B CB  1 
ATOM   6398 C  CG  . PHE B 1 297 ? -68.658  -0.854  267.960 1.00 21.66  ? 297 PHE B CG  1 
ATOM   6399 C  CD1 . PHE B 1 297 ? -68.082  -1.043  269.204 1.00 20.82  ? 297 PHE B CD1 1 
ATOM   6400 C  CD2 . PHE B 1 297 ? -69.645  -1.732  267.545 1.00 20.87  ? 297 PHE B CD2 1 
ATOM   6401 C  CE1 . PHE B 1 297 ? -68.490  -2.079  270.024 1.00 16.60  ? 297 PHE B CE1 1 
ATOM   6402 C  CE2 . PHE B 1 297 ? -70.056  -2.770  268.360 1.00 17.87  ? 297 PHE B CE2 1 
ATOM   6403 C  CZ  . PHE B 1 297 ? -69.477  -2.944  269.601 1.00 16.22  ? 297 PHE B CZ  1 
ATOM   6404 N  N   . ASP B 1 298 ? -66.465  2.991   267.218 1.00 22.59  ? 298 ASP B N   1 
ATOM   6405 C  CA  . ASP B 1 298 ? -65.661  4.023   266.574 1.00 23.89  ? 298 ASP B CA  1 
ATOM   6406 C  C   . ASP B 1 298 ? -64.462  3.464   265.819 1.00 24.03  ? 298 ASP B C   1 
ATOM   6407 O  O   . ASP B 1 298 ? -63.568  4.231   265.447 1.00 29.05  ? 298 ASP B O   1 
ATOM   6408 C  CB  . ASP B 1 298 ? -65.186  5.048   267.606 1.00 19.25  ? 298 ASP B CB  1 
ATOM   6409 C  CG  . ASP B 1 298 ? -66.332  5.762   268.286 1.00 24.16  ? 298 ASP B CG  1 
ATOM   6410 O  OD1 . ASP B 1 298 ? -67.011  6.572   267.620 1.00 24.77  ? 298 ASP B OD1 1 
ATOM   6411 O  OD2 . ASP B 1 298 ? -66.554  5.515   269.490 1.00 43.11  ? 298 ASP B OD2 1 
ATOM   6412 N  N   . GLY B 1 299 ? -64.415  2.157   265.582 1.00 20.64  ? 299 GLY B N   1 
ATOM   6413 C  CA  . GLY B 1 299 ? -63.291  1.598   264.858 1.00 24.08  ? 299 GLY B CA  1 
ATOM   6414 C  C   . GLY B 1 299 ? -63.214  0.087   264.859 1.00 35.86  ? 299 GLY B C   1 
ATOM   6415 O  O   . GLY B 1 299 ? -64.237  -0.596  264.759 1.00 28.91  ? 299 GLY B O   1 
ATOM   6416 N  N   . VAL B 1 300 ? -61.995  -0.448  264.930 1.00 30.69  ? 300 VAL B N   1 
ATOM   6417 C  CA  . VAL B 1 300 ? -61.755  -1.887  264.939 1.00 21.80  ? 300 VAL B CA  1 
ATOM   6418 C  C   . VAL B 1 300 ? -60.626  -2.182  265.915 1.00 23.66  ? 300 VAL B C   1 
ATOM   6419 O  O   . VAL B 1 300 ? -59.685  -1.392  266.050 1.00 28.39  ? 300 VAL B O   1 
ATOM   6420 C  CB  . VAL B 1 300 ? -61.385  -2.433  263.541 1.00 24.95  ? 300 VAL B CB  1 
ATOM   6421 C  CG1 . VAL B 1 300 ? -61.575  -3.944  263.487 1.00 22.86  ? 300 VAL B CG1 1 
ATOM   6422 C  CG2 . VAL B 1 300 ? -62.171  -1.742  262.444 1.00 32.85  ? 300 VAL B CG2 1 
ATOM   6423 N  N   . ASP B 1 301 ? -60.717  -3.324  266.591 1.00 23.45  ? 301 ASP B N   1 
ATOM   6424 C  CA  . ASP B 1 301 ? -59.616  -3.860  267.381 1.00 22.19  ? 301 ASP B CA  1 
ATOM   6425 C  C   . ASP B 1 301 ? -59.373  -5.293  266.936 1.00 21.59  ? 301 ASP B C   1 
ATOM   6426 O  O   . ASP B 1 301 ? -60.237  -6.156  267.119 1.00 22.57  ? 301 ASP B O   1 
ATOM   6427 C  CB  . ASP B 1 301 ? -59.914  -3.803  268.881 1.00 23.24  ? 301 ASP B CB  1 
ATOM   6428 C  CG  . ASP B 1 301 ? -58.706  -4.161  269.724 1.00 20.34  ? 301 ASP B CG  1 
ATOM   6429 O  OD1 . ASP B 1 301 ? -57.573  -3.864  269.292 1.00 19.63  ? 301 ASP B OD1 1 
ATOM   6430 O  OD2 . ASP B 1 301 ? -58.888  -4.740  270.815 1.00 18.25  ? 301 ASP B OD2 1 
ATOM   6431 N  N   . VAL B 1 302 ? -58.208  -5.541  266.349 1.00 23.14  ? 302 VAL B N   1 
ATOM   6432 C  CA  . VAL B 1 302 ? -57.856  -6.849  265.812 1.00 21.92  ? 302 VAL B CA  1 
ATOM   6433 C  C   . VAL B 1 302 ? -57.051  -7.586  266.872 1.00 21.90  ? 302 VAL B C   1 
ATOM   6434 O  O   . VAL B 1 302 ? -55.913  -7.213  267.174 1.00 22.37  ? 302 VAL B O   1 
ATOM   6435 C  CB  . VAL B 1 302 ? -57.072  -6.727  264.499 1.00 19.90  ? 302 VAL B CB  1 
ATOM   6436 C  CG1 . VAL B 1 302 ? -56.770  -8.105  263.936 1.00 26.75  ? 302 VAL B CG1 1 
ATOM   6437 C  CG2 . VAL B 1 302 ? -57.849  -5.890  263.494 1.00 20.47  ? 302 VAL B CG2 1 
ATOM   6438 N  N   . ASP B 1 303 ? -57.635  -8.638  267.441 1.00 20.83  ? 303 ASP B N   1 
ATOM   6439 C  CA  . ASP B 1 303 ? -56.955  -9.409  268.473 1.00 21.39  ? 303 ASP B CA  1 
ATOM   6440 C  C   . ASP B 1 303 ? -56.574  -10.793 267.964 1.00 25.37  ? 303 ASP B C   1 
ATOM   6441 O  O   . ASP B 1 303 ? -56.996  -11.809 268.526 1.00 29.10  ? 303 ASP B O   1 
ATOM   6442 C  CB  . ASP B 1 303 ? -57.831  -9.517  269.721 1.00 22.58  ? 303 ASP B CB  1 
ATOM   6443 C  CG  . ASP B 1 303 ? -58.145  -8.164  270.328 1.00 22.57  ? 303 ASP B CG  1 
ATOM   6444 O  OD1 . ASP B 1 303 ? -57.363  -7.696  271.181 1.00 21.78  ? 303 ASP B OD1 1 
ATOM   6445 O  OD2 . ASP B 1 303 ? -59.168  -7.562  269.945 1.00 25.06  ? 303 ASP B OD2 1 
ATOM   6446 N  N   . TRP B 1 304 ? -55.778  -10.840 266.897 1.00 32.99  ? 304 TRP B N   1 
ATOM   6447 C  CA  . TRP B 1 304 ? -55.269  -12.101 266.369 1.00 31.32  ? 304 TRP B CA  1 
ATOM   6448 C  C   . TRP B 1 304 ? -54.217  -12.646 267.326 1.00 34.83  ? 304 TRP B C   1 
ATOM   6449 O  O   . TRP B 1 304 ? -53.142  -12.057 267.479 1.00 61.71  ? 304 TRP B O   1 
ATOM   6450 C  CB  . TRP B 1 304 ? -54.695  -11.885 264.971 1.00 30.87  ? 304 TRP B CB  1 
ATOM   6451 C  CG  . TRP B 1 304 ? -54.249  -13.135 264.257 1.00 32.94  ? 304 TRP B CG  1 
ATOM   6452 C  CD1 . TRP B 1 304 ? -54.118  -14.388 264.784 1.00 33.52  ? 304 TRP B CD1 1 
ATOM   6453 C  CD2 . TRP B 1 304 ? -53.883  -13.244 262.875 1.00 35.09  ? 304 TRP B CD2 1 
ATOM   6454 N  NE1 . TRP B 1 304 ? -53.688  -15.266 263.819 1.00 35.49  ? 304 TRP B NE1 1 
ATOM   6455 C  CE2 . TRP B 1 304 ? -53.537  -14.589 262.639 1.00 36.64  ? 304 TRP B CE2 1 
ATOM   6456 C  CE3 . TRP B 1 304 ? -53.814  -12.334 261.816 1.00 35.62  ? 304 TRP B CE3 1 
ATOM   6457 C  CZ2 . TRP B 1 304 ? -53.130  -15.045 261.387 1.00 42.17  ? 304 TRP B CZ2 1 
ATOM   6458 C  CZ3 . TRP B 1 304 ? -53.408  -12.789 260.575 1.00 36.33  ? 304 TRP B CZ3 1 
ATOM   6459 C  CH2 . TRP B 1 304 ? -53.072  -14.132 260.371 1.00 41.92  ? 304 TRP B CH2 1 
ATOM   6460 N  N   . GLU B 1 305 ? -54.519  -13.768 267.970 1.00 30.08  ? 305 GLU B N   1 
ATOM   6461 C  CA  . GLU B 1 305 ? -53.623  -14.331 268.972 1.00 32.02  ? 305 GLU B CA  1 
ATOM   6462 C  C   . GLU B 1 305 ? -53.292  -15.796 268.702 1.00 39.60  ? 305 GLU B C   1 
ATOM   6463 O  O   . GLU B 1 305 ? -54.059  -16.684 269.070 1.00 52.78  ? 305 GLU B O   1 
ATOM   6464 C  CB  . GLU B 1 305 ? -54.234  -14.195 270.367 1.00 30.60  ? 305 GLU B CB  1 
ATOM   6465 C  CG  . GLU B 1 305 ? -54.469  -12.763 270.812 1.00 30.06  ? 305 GLU B CG  1 
ATOM   6466 C  CD  . GLU B 1 305 ? -55.027  -12.678 272.218 1.00 32.59  ? 305 GLU B CD  1 
ATOM   6467 O  OE1 . GLU B 1 305 ? -54.981  -13.696 272.940 1.00 45.63  ? 305 GLU B OE1 1 
ATOM   6468 O  OE2 . GLU B 1 305 ? -55.511  -11.593 272.602 1.00 35.79  ? 305 GLU B OE2 1 
ATOM   6469 N  N   . PHE B 1 306 ? -52.154  -16.051 268.060 1.00 54.58  ? 306 PHE B N   1 
ATOM   6470 C  CA  . PHE B 1 306 ? -51.277  -15.005 267.546 1.00 38.13  ? 306 PHE B CA  1 
ATOM   6471 C  C   . PHE B 1 306 ? -50.902  -15.343 266.108 1.00 41.95  ? 306 PHE B C   1 
ATOM   6472 O  O   . PHE B 1 306 ? -50.939  -16.509 265.718 1.00 58.57  ? 306 PHE B O   1 
ATOM   6473 C  CB  . PHE B 1 306 ? -50.013  -14.867 268.402 1.00 39.65  ? 306 PHE B CB  1 
ATOM   6474 C  CG  . PHE B 1 306 ? -50.284  -14.729 269.871 1.00 34.69  ? 306 PHE B CG  1 
ATOM   6475 C  CD1 . PHE B 1 306 ? -50.602  -13.498 270.418 1.00 34.83  ? 306 PHE B CD1 1 
ATOM   6476 C  CD2 . PHE B 1 306 ? -50.198  -15.827 270.709 1.00 37.10  ? 306 PHE B CD2 1 
ATOM   6477 C  CE1 . PHE B 1 306 ? -50.852  -13.371 271.769 1.00 34.07  ? 306 PHE B CE1 1 
ATOM   6478 C  CE2 . PHE B 1 306 ? -50.440  -15.703 272.062 1.00 40.41  ? 306 PHE B CE2 1 
ATOM   6479 C  CZ  . PHE B 1 306 ? -50.766  -14.473 272.593 1.00 34.32  ? 306 PHE B CZ  1 
ATOM   6480 N  N   . PRO B 1 307 ? -50.545  -14.334 265.312 1.00 39.20  ? 307 PRO B N   1 
ATOM   6481 C  CA  . PRO B 1 307 ? -50.074  -14.623 263.952 1.00 40.81  ? 307 PRO B CA  1 
ATOM   6482 C  C   . PRO B 1 307 ? -48.751  -15.369 263.976 1.00 43.28  ? 307 PRO B C   1 
ATOM   6483 O  O   . PRO B 1 307 ? -47.708  -14.795 264.305 1.00 44.88  ? 307 PRO B O   1 
ATOM   6484 C  CB  . PRO B 1 307 ? -49.938  -13.234 263.314 1.00 41.42  ? 307 PRO B CB  1 
ATOM   6485 C  CG  . PRO B 1 307 ? -50.682  -12.297 264.221 1.00 40.77  ? 307 PRO B CG  1 
ATOM   6486 C  CD  . PRO B 1 307 ? -50.590  -12.889 265.587 1.00 38.83  ? 307 PRO B CD  1 
ATOM   6487 N  N   . GLY B 1 308 ? -48.789  -16.655 263.641 1.00 48.13  ? 308 GLY B N   1 
ATOM   6488 C  CA  . GLY B 1 308 ? -47.623  -17.517 263.695 1.00 50.54  ? 308 GLY B CA  1 
ATOM   6489 C  C   . GLY B 1 308 ? -47.775  -18.727 264.595 1.00 54.18  ? 308 GLY B C   1 
ATOM   6490 O  O   . GLY B 1 308 ? -46.927  -19.630 264.535 1.00 54.81  ? 308 GLY B O   1 
ATOM   6491 N  N   . GLY B 1 309 ? -48.811  -18.788 265.433 1.00 47.79  ? 309 GLY B N   1 
ATOM   6492 C  CA  . GLY B 1 309 ? -49.027  -19.935 266.293 1.00 48.66  ? 309 GLY B CA  1 
ATOM   6493 C  C   . GLY B 1 309 ? -49.114  -19.609 267.770 1.00 45.42  ? 309 GLY B C   1 
ATOM   6494 O  O   . GLY B 1 309 ? -49.391  -18.467 268.149 1.00 46.22  ? 309 GLY B O   1 
ATOM   6495 N  N   . LYS B 1 310 ? -48.894  -20.629 268.607 1.00 41.30  ? 310 LYS B N   1 
ATOM   6496 C  CA  . LYS B 1 310 ? -48.860  -20.513 270.062 1.00 40.58  ? 310 LYS B CA  1 
ATOM   6497 C  C   . LYS B 1 310 ? -50.244  -20.196 270.622 1.00 44.23  ? 310 LYS B C   1 
ATOM   6498 O  O   . LYS B 1 310 ? -50.434  -20.162 271.842 1.00 42.05  ? 310 LYS B O   1 
ATOM   6499 C  CB  . LYS B 1 310 ? -47.817  -19.466 270.496 1.00 42.29  ? 310 LYS B CB  1 
ATOM   6500 C  CG  . LYS B 1 310 ? -47.642  -19.344 272.019 1.00 47.77  ? 310 LYS B CG  1 
ATOM   6501 C  CD  . LYS B 1 310 ? -46.257  -18.916 272.437 1.00 77.61  ? 310 LYS B CD  1 
ATOM   6502 C  CE  . LYS B 1 310 ? -46.155  -18.926 273.961 1.00 72.33  ? 310 LYS B CE  1 
ATOM   6503 N  NZ  . LYS B 1 310 ? -47.260  -18.164 274.629 1.00 47.76  ? 310 LYS B NZ  1 
ATOM   6504 N  N   . GLY B 1 311 ? -51.230  -20.021 269.743 1.00 41.88  ? 311 GLY B N   1 
ATOM   6505 C  CA  . GLY B 1 311 ? -52.599  -19.799 270.165 1.00 37.94  ? 311 GLY B CA  1 
ATOM   6506 C  C   . GLY B 1 311 ? -53.173  -20.950 270.966 1.00 45.56  ? 311 GLY B C   1 
ATOM   6507 O  O   . GLY B 1 311 ? -52.477  -21.932 271.243 1.00 37.69  ? 311 GLY B O   1 
ATOM   6508 N  N   . ALA B 1 312 ? -54.447  -20.838 271.345 1.00 34.95  ? 312 ALA B N   1 
ATOM   6509 C  CA  . ALA B 1 312 ? -55.080  -21.894 272.125 1.00 31.31  ? 312 ALA B CA  1 
ATOM   6510 C  C   . ALA B 1 312 ? -55.077  -23.222 271.381 1.00 31.64  ? 312 ALA B C   1 
ATOM   6511 O  O   . ALA B 1 312 ? -55.046  -24.285 272.010 1.00 33.83  ? 312 ALA B O   1 
ATOM   6512 C  CB  . ALA B 1 312 ? -56.507  -21.489 272.490 1.00 34.43  ? 312 ALA B CB  1 
ATOM   6513 N  N   . ASN B 1 313 ? -55.100  -23.184 270.049 1.00 32.08  ? 313 ASN B N   1 
ATOM   6514 C  CA  . ASN B 1 313 ? -55.072  -24.398 269.249 1.00 43.45  ? 313 ASN B CA  1 
ATOM   6515 C  C   . ASN B 1 313 ? -53.656  -24.633 268.747 1.00 38.01  ? 313 ASN B C   1 
ATOM   6516 O  O   . ASN B 1 313 ? -53.177  -23.868 267.896 1.00 39.27  ? 313 ASN B O   1 
ATOM   6517 C  CB  . ASN B 1 313 ? -56.043  -24.291 268.075 1.00 45.63  ? 313 ASN B CB  1 
ATOM   6518 C  CG  . ASN B 1 313 ? -56.339  -25.634 267.439 1.00 41.35  ? 313 ASN B CG  1 
ATOM   6519 O  OD1 . ASN B 1 313 ? -56.237  -26.676 268.086 1.00 58.02  ? 313 ASN B OD1 1 
ATOM   6520 N  ND2 . ASN B 1 313 ? -56.712  -25.616 266.165 1.00 38.56  ? 313 ASN B ND2 1 
ATOM   6521 N  N   . PRO B 1 314 ? -52.950  -25.660 269.232 1.00 37.65  ? 314 PRO B N   1 
ATOM   6522 C  CA  . PRO B 1 314 ? -51.573  -25.890 268.769 1.00 42.37  ? 314 PRO B CA  1 
ATOM   6523 C  C   . PRO B 1 314 ? -51.484  -26.435 267.353 1.00 36.56  ? 314 PRO B C   1 
ATOM   6524 O  O   . PRO B 1 314 ? -50.376  -26.495 266.804 1.00 36.50  ? 314 PRO B O   1 
ATOM   6525 C  CB  . PRO B 1 314 ? -51.032  -26.901 269.785 1.00 44.80  ? 314 PRO B CB  1 
ATOM   6526 C  CG  . PRO B 1 314 ? -52.244  -27.660 270.214 1.00 50.42  ? 314 PRO B CG  1 
ATOM   6527 C  CD  . PRO B 1 314 ? -53.372  -26.657 270.230 1.00 41.43  ? 314 PRO B CD  1 
ATOM   6528 N  N   . SER B 1 315 ? -52.605  -26.832 266.747 1.00 36.42  ? 315 SER B N   1 
ATOM   6529 C  CA  . SER B 1 315 ? -52.563  -27.347 265.383 1.00 38.68  ? 315 SER B CA  1 
ATOM   6530 C  C   . SER B 1 315 ? -52.331  -26.234 264.369 1.00 37.49  ? 315 SER B C   1 
ATOM   6531 O  O   . SER B 1 315 ? -51.734  -26.474 263.313 1.00 39.33  ? 315 SER B O   1 
ATOM   6532 C  CB  . SER B 1 315 ? -53.858  -28.092 265.063 1.00 41.44  ? 315 SER B CB  1 
ATOM   6533 O  OG  . SER B 1 315 ? -54.113  -29.107 266.018 1.00 63.20  ? 315 SER B OG  1 
ATOM   6534 N  N   . LEU B 1 316 ? -52.788  -25.023 264.668 1.00 38.70  ? 316 LEU B N   1 
ATOM   6535 C  CA  . LEU B 1 316 ? -52.673  -23.901 263.751 1.00 39.27  ? 316 LEU B CA  1 
ATOM   6536 C  C   . LEU B 1 316 ? -51.393  -23.120 264.016 1.00 40.46  ? 316 LEU B C   1 
ATOM   6537 O  O   . LEU B 1 316 ? -50.933  -23.010 265.155 1.00 43.53  ? 316 LEU B O   1 
ATOM   6538 C  CB  . LEU B 1 316 ? -53.880  -22.973 263.885 1.00 39.55  ? 316 LEU B CB  1 
ATOM   6539 C  CG  . LEU B 1 316 ? -55.253  -23.646 263.898 1.00 37.02  ? 316 LEU B CG  1 
ATOM   6540 C  CD1 . LEU B 1 316 ? -56.338  -22.644 264.259 1.00 58.17  ? 316 LEU B CD1 1 
ATOM   6541 C  CD2 . LEU B 1 316 ? -55.545  -24.299 262.556 1.00 33.34  ? 316 LEU B CD2 1 
ATOM   6542 N  N   . GLY B 1 317 ? -50.819  -22.574 262.947 1.00 42.48  ? 317 GLY B N   1 
ATOM   6543 C  CA  . GLY B 1 317 ? -49.650  -21.732 263.093 1.00 51.02  ? 317 GLY B CA  1 
ATOM   6544 C  C   . GLY B 1 317 ? -48.628  -21.845 261.983 1.00 71.95  ? 317 GLY B C   1 
ATOM   6545 O  O   . GLY B 1 317 ? -48.163  -22.941 261.654 1.00 90.84  ? 317 GLY B O   1 
ATOM   6546 N  N   . ASP B 1 318 ? -48.276  -20.705 261.394 1.00 63.50  ? 318 ASP B N   1 
ATOM   6547 C  CA  . ASP B 1 318 ? -47.165  -20.623 260.453 1.00 65.13  ? 318 ASP B CA  1 
ATOM   6548 C  C   . ASP B 1 318 ? -46.611  -19.211 260.533 1.00 67.01  ? 318 ASP B C   1 
ATOM   6549 O  O   . ASP B 1 318 ? -47.346  -18.245 260.306 1.00 72.67  ? 318 ASP B O   1 
ATOM   6550 C  CB  . ASP B 1 318 ? -47.604  -20.960 259.028 1.00 66.43  ? 318 ASP B CB  1 
ATOM   6551 C  CG  . ASP B 1 318 ? -46.438  -21.026 258.063 1.00 72.65  ? 318 ASP B CG  1 
ATOM   6552 O  OD1 . ASP B 1 318 ? -45.278  -21.065 258.525 1.00 81.52  ? 318 ASP B OD1 1 
ATOM   6553 O  OD2 . ASP B 1 318 ? -46.679  -21.045 256.841 1.00 68.46  ? 318 ASP B OD2 1 
ATOM   6554 N  N   . ALA B 1 319 ? -45.322  -19.097 260.854 1.00 67.93  ? 319 ALA B N   1 
ATOM   6555 C  CA  . ALA B 1 319 ? -44.748  -17.802 261.203 1.00 72.11  ? 319 ALA B CA  1 
ATOM   6556 C  C   . ALA B 1 319 ? -44.772  -16.839 260.021 1.00 72.14  ? 319 ALA B C   1 
ATOM   6557 O  O   . ALA B 1 319 ? -45.399  -15.776 260.081 1.00 69.64  ? 319 ALA B O   1 
ATOM   6558 C  CB  . ALA B 1 319 ? -43.321  -17.989 261.721 1.00 103.63 ? 319 ALA B CB  1 
ATOM   6559 N  N   . GLU B 1 320 ? -44.096  -17.197 258.933 1.00 75.87  ? 320 GLU B N   1 
ATOM   6560 C  CA  . GLU B 1 320 ? -43.813  -16.254 257.860 1.00 80.67  ? 320 GLU B CA  1 
ATOM   6561 C  C   . GLU B 1 320 ? -44.837  -16.285 256.730 1.00 74.05  ? 320 GLU B C   1 
ATOM   6562 O  O   . GLU B 1 320 ? -44.622  -15.630 255.705 1.00 74.47  ? 320 GLU B O   1 
ATOM   6563 C  CB  . GLU B 1 320 ? -42.408  -16.503 257.307 1.00 127.86 ? 320 GLU B CB  1 
ATOM   6564 C  CG  . GLU B 1 320 ? -41.304  -16.174 258.303 1.00 130.68 ? 320 GLU B CG  1 
ATOM   6565 C  CD  . GLU B 1 320 ? -39.917  -16.454 257.761 1.00 140.67 ? 320 GLU B CD  1 
ATOM   6566 O  OE1 . GLU B 1 320 ? -39.812  -17.084 256.689 1.00 149.25 ? 320 GLU B OE1 1 
ATOM   6567 O  OE2 . GLU B 1 320 ? -38.932  -16.043 258.410 1.00 137.96 ? 320 GLU B OE2 1 
ATOM   6568 N  N   . ARG B 1 321 ? -45.940  -17.018 256.884 1.00 71.08  ? 321 ARG B N   1 
ATOM   6569 C  CA  . ARG B 1 321 ? -47.058  -16.903 255.954 1.00 69.78  ? 321 ARG B CA  1 
ATOM   6570 C  C   . ARG B 1 321 ? -48.201  -16.082 256.534 1.00 74.10  ? 321 ARG B C   1 
ATOM   6571 O  O   . ARG B 1 321 ? -48.735  -15.197 255.858 1.00 93.22  ? 321 ARG B O   1 
ATOM   6572 C  CB  . ARG B 1 321 ? -47.574  -18.284 255.530 1.00 68.36  ? 321 ARG B CB  1 
ATOM   6573 C  CG  . ARG B 1 321 ? -48.493  -18.219 254.314 1.00 64.30  ? 321 ARG B CG  1 
ATOM   6574 C  CD  . ARG B 1 321 ? -48.492  -19.498 253.487 1.00 61.25  ? 321 ARG B CD  1 
ATOM   6575 N  NE  . ARG B 1 321 ? -48.085  -20.675 254.249 1.00 70.00  ? 321 ARG B NE  1 
ATOM   6576 C  CZ  . ARG B 1 321 ? -47.020  -21.416 253.966 1.00 60.57  ? 321 ARG B CZ  1 
ATOM   6577 N  NH1 . ARG B 1 321 ? -46.244  -21.103 252.939 1.00 58.32  ? 321 ARG B NH1 1 
ATOM   6578 N  NH2 . ARG B 1 321 ? -46.727  -22.472 254.714 1.00 73.18  ? 321 ARG B NH2 1 
ATOM   6579 N  N   . ASP B 1 322 ? -48.587  -16.354 257.783 1.00 74.81  ? 322 ASP B N   1 
ATOM   6580 C  CA  . ASP B 1 322 ? -49.561  -15.505 258.456 1.00 67.84  ? 322 ASP B CA  1 
ATOM   6581 C  C   . ASP B 1 322 ? -49.025  -14.100 258.679 1.00 61.65  ? 322 ASP B C   1 
ATOM   6582 O  O   . ASP B 1 322 ? -49.815  -13.166 258.855 1.00 60.23  ? 322 ASP B O   1 
ATOM   6583 C  CB  . ASP B 1 322 ? -49.972  -16.128 259.789 1.00 93.63  ? 322 ASP B CB  1 
ATOM   6584 C  CG  . ASP B 1 322 ? -50.816  -17.373 259.612 1.00 113.66 ? 322 ASP B CG  1 
ATOM   6585 O  OD1 . ASP B 1 322 ? -51.366  -17.569 258.509 1.00 122.11 ? 322 ASP B OD1 1 
ATOM   6586 O  OD2 . ASP B 1 322 ? -50.924  -18.158 260.576 1.00 110.95 ? 322 ASP B OD2 1 
ATOM   6587 N  N   . ALA B 1 323 ? -47.700  -13.930 258.676 1.00 62.64  ? 323 ALA B N   1 
ATOM   6588 C  CA  . ALA B 1 323 ? -47.126  -12.593 258.762 1.00 62.81  ? 323 ALA B CA  1 
ATOM   6589 C  C   . ALA B 1 323 ? -47.508  -11.747 257.557 1.00 59.37  ? 323 ALA B C   1 
ATOM   6590 O  O   . ALA B 1 323 ? -47.631  -10.523 257.672 1.00 59.80  ? 323 ALA B O   1 
ATOM   6591 C  CB  . ALA B 1 323 ? -45.605  -12.681 258.893 1.00 90.62  ? 323 ALA B CB  1 
ATOM   6592 N  N   . LYS B 1 324 ? -47.700  -12.377 256.397 1.00 57.93  ? 324 LYS B N   1 
ATOM   6593 C  CA  . LYS B 1 324 ? -48.177  -11.649 255.228 1.00 55.64  ? 324 LYS B CA  1 
ATOM   6594 C  C   . LYS B 1 324 ? -49.679  -11.408 255.305 1.00 63.46  ? 324 LYS B C   1 
ATOM   6595 O  O   . LYS B 1 324 ? -50.163  -10.349 254.892 1.00 81.20  ? 324 LYS B O   1 
ATOM   6596 C  CB  . LYS B 1 324 ? -47.823  -12.414 253.953 1.00 61.62  ? 324 LYS B CB  1 
ATOM   6597 C  CG  . LYS B 1 324 ? -46.344  -12.730 253.809 1.00 82.81  ? 324 LYS B CG  1 
ATOM   6598 C  CD  . LYS B 1 324 ? -45.527  -11.472 253.573 1.00 90.98  ? 324 LYS B CD  1 
ATOM   6599 C  CE  . LYS B 1 324 ? -44.070  -11.807 253.295 1.00 92.04  ? 324 LYS B CE  1 
ATOM   6600 N  NZ  . LYS B 1 324 ? -43.377  -12.332 254.505 1.00 98.23  ? 324 LYS B NZ  1 
ATOM   6601 N  N   . THR B 1 325 ? -50.427  -12.380 255.834 1.00 76.72  ? 325 THR B N   1 
ATOM   6602 C  CA  . THR B 1 325 ? -51.870  -12.214 255.979 1.00 54.08  ? 325 THR B CA  1 
ATOM   6603 C  C   . THR B 1 325 ? -52.197  -11.091 256.954 1.00 45.65  ? 325 THR B C   1 
ATOM   6604 O  O   . THR B 1 325 ? -53.081  -10.267 256.690 1.00 46.07  ? 325 THR B O   1 
ATOM   6605 C  CB  . THR B 1 325 ? -52.503  -13.527 256.445 1.00 53.04  ? 325 THR B CB  1 
ATOM   6606 O  OG1 . THR B 1 325 ? -52.240  -14.556 255.483 1.00 50.64  ? 325 THR B OG1 1 
ATOM   6607 C  CG2 . THR B 1 325 ? -54.007  -13.367 256.610 1.00 57.43  ? 325 THR B CG2 1 
ATOM   6608 N  N   . TYR B 1 326 ? -51.488  -11.039 258.084 1.00 45.14  ? 326 TYR B N   1 
ATOM   6609 C  CA  . TYR B 1 326 ? -51.733  -9.998  259.077 1.00 41.74  ? 326 TYR B CA  1 
ATOM   6610 C  C   . TYR B 1 326 ? -51.511  -8.609  258.490 1.00 42.00  ? 326 TYR B C   1 
ATOM   6611 O  O   . TYR B 1 326 ? -52.239  -7.666  258.818 1.00 41.29  ? 326 TYR B O   1 
ATOM   6612 C  CB  . TYR B 1 326 ? -50.832  -10.226 260.292 1.00 42.48  ? 326 TYR B CB  1 
ATOM   6613 C  CG  . TYR B 1 326 ? -51.012  -9.232  261.418 1.00 37.93  ? 326 TYR B CG  1 
ATOM   6614 C  CD1 . TYR B 1 326 ? -51.961  -9.440  262.410 1.00 39.05  ? 326 TYR B CD1 1 
ATOM   6615 C  CD2 . TYR B 1 326 ? -50.217  -8.097  261.501 1.00 41.75  ? 326 TYR B CD2 1 
ATOM   6616 C  CE1 . TYR B 1 326 ? -52.119  -8.539  263.446 1.00 41.74  ? 326 TYR B CE1 1 
ATOM   6617 C  CE2 . TYR B 1 326 ? -50.365  -7.195  262.533 1.00 40.33  ? 326 TYR B CE2 1 
ATOM   6618 C  CZ  . TYR B 1 326 ? -51.319  -7.418  263.501 1.00 38.44  ? 326 TYR B CZ  1 
ATOM   6619 O  OH  . TYR B 1 326 ? -51.469  -6.516  264.527 1.00 32.55  ? 326 TYR B OH  1 
ATOM   6620 N  N   . ILE B 1 327 ? -50.512  -8.465  257.618 1.00 45.52  ? 327 ILE B N   1 
ATOM   6621 C  CA  . ILE B 1 327 ? -50.271  -7.179  256.972 1.00 45.02  ? 327 ILE B CA  1 
ATOM   6622 C  C   . ILE B 1 327 ? -51.396  -6.856  255.998 1.00 58.16  ? 327 ILE B C   1 
ATOM   6623 O  O   . ILE B 1 327 ? -51.988  -5.771  256.041 1.00 80.61  ? 327 ILE B O   1 
ATOM   6624 C  CB  . ILE B 1 327 ? -48.903  -7.181  256.267 1.00 47.29  ? 327 ILE B CB  1 
ATOM   6625 C  CG1 . ILE B 1 327 ? -47.772  -7.300  257.290 1.00 55.92  ? 327 ILE B CG1 1 
ATOM   6626 C  CG2 . ILE B 1 327 ? -48.738  -5.928  255.420 1.00 49.62  ? 327 ILE B CG2 1 
ATOM   6627 C  CD1 . ILE B 1 327 ? -47.803  -6.236  258.362 1.00 58.87  ? 327 ILE B CD1 1 
ATOM   6628 N  N   . LEU B 1 328 ? -51.712  -7.800  255.109 1.00 46.97  ? 328 LEU B N   1 
ATOM   6629 C  CA  . LEU B 1 328 ? -52.705  -7.544  254.072 1.00 45.11  ? 328 LEU B CA  1 
ATOM   6630 C  C   . LEU B 1 328 ? -54.110  -7.420  254.652 1.00 44.46  ? 328 LEU B C   1 
ATOM   6631 O  O   . LEU B 1 328 ? -54.958  -6.732  254.072 1.00 45.12  ? 328 LEU B O   1 
ATOM   6632 C  CB  . LEU B 1 328 ? -52.633  -8.650  253.019 1.00 47.85  ? 328 LEU B CB  1 
ATOM   6633 C  CG  . LEU B 1 328 ? -53.653  -8.706  251.885 1.00 59.12  ? 328 LEU B CG  1 
ATOM   6634 C  CD1 . LEU B 1 328 ? -53.539  -7.481  251.000 1.00 76.56  ? 328 LEU B CD1 1 
ATOM   6635 C  CD2 . LEU B 1 328 ? -53.402  -9.961  251.077 1.00 62.16  ? 328 LEU B CD2 1 
ATOM   6636 N  N   . LEU B 1 329 ? -54.373  -8.060  255.794 1.00 43.56  ? 329 LEU B N   1 
ATOM   6637 C  CA  . LEU B 1 329 ? -55.660  -7.877  256.458 1.00 37.91  ? 329 LEU B CA  1 
ATOM   6638 C  C   . LEU B 1 329 ? -55.812  -6.455  256.982 1.00 35.84  ? 329 LEU B C   1 
ATOM   6639 O  O   . LEU B 1 329 ? -56.875  -5.842  256.832 1.00 40.19  ? 329 LEU B O   1 
ATOM   6640 C  CB  . LEU B 1 329 ? -55.815  -8.883  257.598 1.00 34.39  ? 329 LEU B CB  1 
ATOM   6641 C  CG  . LEU B 1 329 ? -57.155  -8.867  258.337 1.00 31.78  ? 329 LEU B CG  1 
ATOM   6642 C  CD1 . LEU B 1 329 ? -58.303  -9.154  257.382 1.00 33.71  ? 329 LEU B CD1 1 
ATOM   6643 C  CD2 . LEU B 1 329 ? -57.151  -9.858  259.490 1.00 30.19  ? 329 LEU B CD2 1 
ATOM   6644 N  N   . LEU B 1 330 ? -54.759  -5.913  257.597 1.00 33.33  ? 330 LEU B N   1 
ATOM   6645 C  CA  . LEU B 1 330 ? -54.833  -4.561  258.139 1.00 32.21  ? 330 LEU B CA  1 
ATOM   6646 C  C   . LEU B 1 330 ? -54.914  -3.522  257.028 1.00 35.97  ? 330 LEU B C   1 
ATOM   6647 O  O   . LEU B 1 330 ? -55.586  -2.496  257.179 1.00 37.28  ? 330 LEU B O   1 
ATOM   6648 C  CB  . LEU B 1 330 ? -53.629  -4.294  259.036 1.00 34.41  ? 330 LEU B CB  1 
ATOM   6649 C  CG  . LEU B 1 330 ? -53.539  -5.141  260.305 1.00 35.16  ? 330 LEU B CG  1 
ATOM   6650 C  CD1 . LEU B 1 330 ? -52.315  -4.745  261.103 1.00 37.27  ? 330 LEU B CD1 1 
ATOM   6651 C  CD2 . LEU B 1 330 ? -54.800  -4.995  261.139 1.00 46.09  ? 330 LEU B CD2 1 
ATOM   6652 N  N   . GLU B 1 331 ? -54.230  -3.768  255.907 1.00 42.53  ? 331 GLU B N   1 
ATOM   6653 C  CA  . GLU B 1 331 ? -54.313  -2.850  254.776 1.00 46.61  ? 331 GLU B CA  1 
ATOM   6654 C  C   . GLU B 1 331 ? -55.731  -2.785  254.225 1.00 48.27  ? 331 GLU B C   1 
ATOM   6655 O  O   . GLU B 1 331 ? -56.248  -1.698  253.942 1.00 39.33  ? 331 GLU B O   1 
ATOM   6656 C  CB  . GLU B 1 331 ? -53.337  -3.277  253.680 1.00 44.24  ? 331 GLU B CB  1 
ATOM   6657 C  CG  . GLU B 1 331 ? -51.873  -3.184  254.073 1.00 44.14  ? 331 GLU B CG  1 
ATOM   6658 C  CD  . GLU B 1 331 ? -50.948  -3.660  252.972 1.00 43.93  ? 331 GLU B CD  1 
ATOM   6659 O  OE1 . GLU B 1 331 ? -51.440  -4.289  252.012 1.00 38.33  ? 331 GLU B OE1 1 
ATOM   6660 O  OE2 . GLU B 1 331 ? -49.730  -3.403  253.067 1.00 54.78  ? 331 GLU B OE2 1 
ATOM   6661 N  N   . GLU B 1 332 ? -56.377  -3.942  254.073 1.00 39.78  ? 332 GLU B N   1 
ATOM   6662 C  CA  . GLU B 1 332 ? -57.745  -3.967  253.566 1.00 37.77  ? 332 GLU B CA  1 
ATOM   6663 C  C   . GLU B 1 332 ? -58.721  -3.384  254.581 1.00 34.97  ? 332 GLU B C   1 
ATOM   6664 O  O   . GLU B 1 332 ? -59.684  -2.706  254.205 1.00 32.94  ? 332 GLU B O   1 
ATOM   6665 C  CB  . GLU B 1 332 ? -58.137  -5.398  253.199 1.00 39.74  ? 332 GLU B CB  1 
ATOM   6666 C  CG  . GLU B 1 332 ? -57.324  -5.983  252.054 1.00 40.57  ? 332 GLU B CG  1 
ATOM   6667 C  CD  . GLU B 1 332 ? -57.460  -7.489  251.950 1.00 44.37  ? 332 GLU B CD  1 
ATOM   6668 O  OE1 . GLU B 1 332 ? -58.147  -8.086  252.805 1.00 49.81  ? 332 GLU B OE1 1 
ATOM   6669 O  OE2 . GLU B 1 332 ? -56.876  -8.077  251.016 1.00 49.84  ? 332 GLU B OE2 1 
ATOM   6670 N  N   . LEU B 1 333 ? -58.489  -3.638  255.872 1.00 34.01  ? 333 LEU B N   1 
ATOM   6671 C  CA  . LEU B 1 333 ? -59.345  -3.059  256.902 1.00 32.21  ? 333 LEU B CA  1 
ATOM   6672 C  C   . LEU B 1 333 ? -59.193  -1.545  256.955 1.00 34.19  ? 333 LEU B C   1 
ATOM   6673 O  O   . LEU B 1 333 ? -60.179  -0.823  257.143 1.00 34.09  ? 333 LEU B O   1 
ATOM   6674 C  CB  . LEU B 1 333 ? -59.025  -3.676  258.264 1.00 30.52  ? 333 LEU B CB  1 
ATOM   6675 C  CG  . LEU B 1 333 ? -59.574  -5.076  258.546 1.00 32.26  ? 333 LEU B CG  1 
ATOM   6676 C  CD1 . LEU B 1 333 ? -59.169  -5.535  259.938 1.00 28.52  ? 333 LEU B CD1 1 
ATOM   6677 C  CD2 . LEU B 1 333 ? -61.084  -5.108  258.386 1.00 40.48  ? 333 LEU B CD2 1 
ATOM   6678 N  N   . ARG B 1 334 ? -57.966  -1.046  256.790 1.00 33.94  ? 334 ARG B N   1 
ATOM   6679 C  CA  . ARG B 1 334 ? -57.751  0.397   256.794 1.00 42.18  ? 334 ARG B CA  1 
ATOM   6680 C  C   . ARG B 1 334 ? -58.403  1.055   255.585 1.00 38.79  ? 334 ARG B C   1 
ATOM   6681 O  O   . ARG B 1 334 ? -59.037  2.109   255.711 1.00 37.36  ? 334 ARG B O   1 
ATOM   6682 C  CB  . ARG B 1 334 ? -56.255  0.704   256.831 1.00 38.15  ? 334 ARG B CB  1 
ATOM   6683 C  CG  . ARG B 1 334 ? -55.916  2.187   256.884 1.00 36.91  ? 334 ARG B CG  1 
ATOM   6684 C  CD  . ARG B 1 334 ? -56.360  2.818   258.195 1.00 34.81  ? 334 ARG B CD  1 
ATOM   6685 N  NE  . ARG B 1 334 ? -57.672  3.449   258.088 1.00 35.95  ? 334 ARG B NE  1 
ATOM   6686 C  CZ  . ARG B 1 334 ? -58.299  4.042   259.098 1.00 36.64  ? 334 ARG B CZ  1 
ATOM   6687 N  NH1 . ARG B 1 334 ? -57.735  4.088   260.297 1.00 35.06  ? 334 ARG B NH1 1 
ATOM   6688 N  NH2 . ARG B 1 334 ? -59.492  4.591   258.909 1.00 38.03  ? 334 ARG B NH2 1 
ATOM   6689 N  N   . ALA B 1 335 ? -58.261  0.446   254.404 1.00 38.14  ? 335 ALA B N   1 
ATOM   6690 C  CA  . ALA B 1 335 ? -58.887  1.001   253.209 1.00 36.16  ? 335 ALA B CA  1 
ATOM   6691 C  C   . ALA B 1 335 ? -60.405  0.958   253.305 1.00 37.86  ? 335 ALA B C   1 
ATOM   6692 O  O   . ALA B 1 335 ? -61.087  1.848   252.783 1.00 54.76  ? 335 ALA B O   1 
ATOM   6693 C  CB  . ALA B 1 335 ? -58.412  0.248   251.967 1.00 50.68  ? 335 ALA B CB  1 
ATOM   6694 N  N   . MET B 1 336 ? -60.951  -0.063  253.967 1.00 36.54  ? 336 MET B N   1 
ATOM   6695 C  CA  . MET B 1 336 ? -62.398  -0.150  254.131 1.00 40.20  ? 336 MET B CA  1 
ATOM   6696 C  C   . MET B 1 336 ? -62.909  0.913   255.096 1.00 37.81  ? 336 MET B C   1 
ATOM   6697 O  O   . MET B 1 336 ? -63.947  1.537   254.846 1.00 37.99  ? 336 MET B O   1 
ATOM   6698 C  CB  . MET B 1 336 ? -62.779  -1.554  254.605 1.00 47.97  ? 336 MET B CB  1 
ATOM   6699 C  CG  . MET B 1 336 ? -64.218  -1.721  255.067 1.00 31.03  ? 336 MET B CG  1 
ATOM   6700 S  SD  . MET B 1 336 ? -64.463  -1.279  256.798 1.00 20.90  ? 336 MET B SD  1 
ATOM   6701 C  CE  . MET B 1 336 ? -63.138  -2.212  257.548 1.00 37.68  ? 336 MET B CE  1 
ATOM   6702 N  N   . LEU B 1 337 ? -62.199  1.128   256.207 1.00 44.16  ? 337 LEU B N   1 
ATOM   6703 C  CA  . LEU B 1 337 ? -62.614  2.149   257.163 1.00 37.51  ? 337 LEU B CA  1 
ATOM   6704 C  C   . LEU B 1 337 ? -62.548  3.540   256.547 1.00 53.05  ? 337 LEU B C   1 
ATOM   6705 O  O   . LEU B 1 337 ? -63.380  4.402   256.854 1.00 49.40  ? 337 LEU B O   1 
ATOM   6706 C  CB  . LEU B 1 337 ? -61.746  2.084   258.417 1.00 41.05  ? 337 LEU B CB  1 
ATOM   6707 C  CG  . LEU B 1 337 ? -61.904  0.867   259.324 1.00 34.79  ? 337 LEU B CG  1 
ATOM   6708 C  CD1 . LEU B 1 337 ? -60.962  0.996   260.505 1.00 39.94  ? 337 LEU B CD1 1 
ATOM   6709 C  CD2 . LEU B 1 337 ? -63.343  0.727   259.792 1.00 34.26  ? 337 LEU B CD2 1 
ATOM   6710 N  N   . ASP B 1 338 ? -61.559  3.781   255.682 1.00 38.59  ? 338 ASP B N   1 
ATOM   6711 C  CA  . ASP B 1 338 ? -61.467  5.071   255.010 1.00 38.13  ? 338 ASP B CA  1 
ATOM   6712 C  C   . ASP B 1 338 ? -62.686  5.331   254.137 1.00 38.70  ? 338 ASP B C   1 
ATOM   6713 O  O   . ASP B 1 338 ? -63.098  6.485   253.975 1.00 41.49  ? 338 ASP B O   1 
ATOM   6714 C  CB  . ASP B 1 338 ? -60.186  5.140   254.180 1.00 39.09  ? 338 ASP B CB  1 
ATOM   6715 C  CG  . ASP B 1 338 ? -58.936  5.070   255.035 1.00 37.97  ? 338 ASP B CG  1 
ATOM   6716 O  OD1 . ASP B 1 338 ? -59.001  5.463   256.219 1.00 33.59  ? 338 ASP B OD1 1 
ATOM   6717 O  OD2 . ASP B 1 338 ? -57.890  4.618   254.525 1.00 60.01  ? 338 ASP B OD2 1 
ATOM   6718 N  N   . ASP B 1 339 ? -63.274  4.277   253.568 1.00 37.21  ? 339 ASP B N   1 
ATOM   6719 C  CA  . ASP B 1 339 ? -64.548  4.435   252.877 1.00 36.71  ? 339 ASP B CA  1 
ATOM   6720 C  C   . ASP B 1 339 ? -65.643  4.847   253.850 1.00 39.55  ? 339 ASP B C   1 
ATOM   6721 O  O   . ASP B 1 339 ? -66.465  5.715   253.537 1.00 61.13  ? 339 ASP B O   1 
ATOM   6722 C  CB  . ASP B 1 339 ? -64.926  3.139   252.160 1.00 40.31  ? 339 ASP B CB  1 
ATOM   6723 C  CG  . ASP B 1 339 ? -63.964  2.789   251.044 1.00 41.99  ? 339 ASP B CG  1 
ATOM   6724 O  OD1 . ASP B 1 339 ? -62.858  3.367   251.008 1.00 50.60  ? 339 ASP B OD1 1 
ATOM   6725 O  OD2 . ASP B 1 339 ? -64.314  1.934   250.202 1.00 50.26  ? 339 ASP B OD2 1 
ATOM   6726 N  N   . LEU B 1 340 ? -65.662  4.241   255.040 1.00 39.20  ? 340 LEU B N   1 
ATOM   6727 C  CA  . LEU B 1 340 ? -66.652  4.606   256.049 1.00 46.29  ? 340 LEU B CA  1 
ATOM   6728 C  C   . LEU B 1 340 ? -66.471  6.047   256.508 1.00 41.12  ? 340 LEU B C   1 
ATOM   6729 O  O   . LEU B 1 340 ? -67.453  6.747   256.781 1.00 38.40  ? 340 LEU B O   1 
ATOM   6730 C  CB  . LEU B 1 340 ? -66.561  3.654   257.243 1.00 38.90  ? 340 LEU B CB  1 
ATOM   6731 C  CG  . LEU B 1 340 ? -67.391  2.371   257.202 1.00 42.42  ? 340 LEU B CG  1 
ATOM   6732 C  CD1 . LEU B 1 340 ? -67.050  1.485   258.388 1.00 80.75  ? 340 LEU B CD1 1 
ATOM   6733 C  CD2 . LEU B 1 340 ? -68.873  2.698   257.193 1.00 43.53  ? 340 LEU B CD2 1 
ATOM   6734 N  N   . GLU B 1 341 ? -65.220  6.507   256.604 1.00 36.50  ? 341 GLU B N   1 
ATOM   6735 C  CA  . GLU B 1 341 ? -64.971  7.875   257.047 1.00 34.50  ? 341 GLU B CA  1 
ATOM   6736 C  C   . GLU B 1 341 ? -65.525  8.886   256.052 1.00 36.00  ? 341 GLU B C   1 
ATOM   6737 O  O   . GLU B 1 341 ? -66.136  9.885   256.447 1.00 35.67  ? 341 GLU B O   1 
ATOM   6738 C  CB  . GLU B 1 341 ? -63.474  8.092   257.266 1.00 34.32  ? 341 GLU B CB  1 
ATOM   6739 C  CG  . GLU B 1 341 ? -62.907  7.312   258.441 1.00 34.65  ? 341 GLU B CG  1 
ATOM   6740 C  CD  . GLU B 1 341 ? -61.441  7.606   258.683 1.00 31.51  ? 341 GLU B CD  1 
ATOM   6741 O  OE1 . GLU B 1 341 ? -60.830  8.315   257.856 1.00 36.82  ? 341 GLU B OE1 1 
ATOM   6742 O  OE2 . GLU B 1 341 ? -60.900  7.131   259.703 1.00 31.83  ? 341 GLU B OE2 1 
ATOM   6743 N  N   . ALA B 1 342 ? -65.324  8.644   254.755 1.00 51.15  ? 342 ALA B N   1 
ATOM   6744 C  CA  . ALA B 1 342 ? -65.944  9.490   253.744 1.00 38.82  ? 342 ALA B CA  1 
ATOM   6745 C  C   . ALA B 1 342 ? -67.432  9.207   253.596 1.00 39.40  ? 342 ALA B C   1 
ATOM   6746 O  O   . ALA B 1 342 ? -68.168  10.064  253.097 1.00 42.45  ? 342 ALA B O   1 
ATOM   6747 C  CB  . ALA B 1 342 ? -65.242  9.308   252.398 1.00 52.58  ? 342 ALA B CB  1 
ATOM   6748 N  N   . GLN B 1 343 ? -67.887  8.027   254.021 1.00 42.57  ? 343 GLN B N   1 
ATOM   6749 C  CA  . GLN B 1 343 ? -69.302  7.687   253.938 1.00 43.42  ? 343 GLN B CA  1 
ATOM   6750 C  C   . GLN B 1 343 ? -70.105  8.357   255.045 1.00 42.55  ? 343 GLN B C   1 
ATOM   6751 O  O   . GLN B 1 343 ? -71.222  8.831   254.807 1.00 73.61  ? 343 GLN B O   1 
ATOM   6752 C  CB  . GLN B 1 343 ? -69.476  6.169   254.005 1.00 49.52  ? 343 GLN B CB  1 
ATOM   6753 C  CG  . GLN B 1 343 ? -70.650  5.621   253.217 1.00 55.35  ? 343 GLN B CG  1 
ATOM   6754 C  CD  . GLN B 1 343 ? -70.920  4.163   253.536 1.00 77.60  ? 343 GLN B CD  1 
ATOM   6755 O  OE1 . GLN B 1 343 ? -70.287  3.583   254.417 1.00 73.64  ? 343 GLN B OE1 1 
ATOM   6756 N  NE2 . GLN B 1 343 ? -71.864  3.564   252.820 1.00 99.83  ? 343 GLN B NE2 1 
ATOM   6757 N  N   . THR B 1 344 ? -69.553  8.410   256.258 1.00 35.67  ? 344 THR B N   1 
ATOM   6758 C  CA  . THR B 1 344 ? -70.267  8.928   257.415 1.00 33.31  ? 344 THR B CA  1 
ATOM   6759 C  C   . THR B 1 344 ? -69.712  10.243  257.942 1.00 31.69  ? 344 THR B C   1 
ATOM   6760 O  O   . THR B 1 344 ? -70.313  10.825  258.851 1.00 34.32  ? 344 THR B O   1 
ATOM   6761 C  CB  . THR B 1 344 ? -70.252  7.895   258.551 1.00 34.24  ? 344 THR B CB  1 
ATOM   6762 O  OG1 . THR B 1 344 ? -68.906  7.700   259.002 1.00 33.19  ? 344 THR B OG1 1 
ATOM   6763 C  CG2 . THR B 1 344 ? -70.815  6.566   258.070 1.00 39.65  ? 344 THR B CG2 1 
ATOM   6764 N  N   . GLY B 1 345 ? -68.594  10.726  257.405 1.00 31.80  ? 345 GLY B N   1 
ATOM   6765 C  CA  . GLY B 1 345 ? -67.971  11.912  257.955 1.00 29.53  ? 345 GLY B CA  1 
ATOM   6766 C  C   . GLY B 1 345 ? -67.350  11.723  259.319 1.00 26.89  ? 345 GLY B C   1 
ATOM   6767 O  O   . GLY B 1 345 ? -66.984  12.712  259.961 1.00 28.88  ? 345 GLY B O   1 
ATOM   6768 N  N   . ARG B 1 346 ? -67.215  10.483  259.780 1.00 26.46  ? 346 ARG B N   1 
ATOM   6769 C  CA  . ARG B 1 346 ? -66.695  10.175  261.100 1.00 26.61  ? 346 ARG B CA  1 
ATOM   6770 C  C   . ARG B 1 346 ? -65.216  9.808   261.013 1.00 29.28  ? 346 ARG B C   1 
ATOM   6771 O  O   . ARG B 1 346 ? -64.608  9.793   259.939 1.00 29.02  ? 346 ARG B O   1 
ATOM   6772 C  CB  . ARG B 1 346 ? -67.503  9.041   261.733 1.00 26.64  ? 346 ARG B CB  1 
ATOM   6773 C  CG  . ARG B 1 346 ? -68.983  9.339   261.887 1.00 34.86  ? 346 ARG B CG  1 
ATOM   6774 C  CD  . ARG B 1 346 ? -69.754  8.087   262.271 1.00 29.14  ? 346 ARG B CD  1 
ATOM   6775 N  NE  . ARG B 1 346 ? -69.212  7.450   263.467 1.00 21.97  ? 346 ARG B NE  1 
ATOM   6776 C  CZ  . ARG B 1 346 ? -69.712  6.349   264.017 1.00 21.54  ? 346 ARG B CZ  1 
ATOM   6777 N  NH1 . ARG B 1 346 ? -70.771  5.759   263.479 1.00 21.45  ? 346 ARG B NH1 1 
ATOM   6778 N  NH2 . ARG B 1 346 ? -69.155  5.836   265.105 1.00 26.27  ? 346 ARG B NH2 1 
ATOM   6779 N  N   . VAL B 1 347 ? -64.633  9.503   262.168 1.00 27.61  ? 347 VAL B N   1 
ATOM   6780 C  CA  . VAL B 1 347 ? -63.246  9.066   262.272 1.00 28.69  ? 347 VAL B CA  1 
ATOM   6781 C  C   . VAL B 1 347 ? -63.248  7.644   262.812 1.00 31.46  ? 347 VAL B C   1 
ATOM   6782 O  O   . VAL B 1 347 ? -63.737  7.397   263.922 1.00 40.95  ? 347 VAL B O   1 
ATOM   6783 C  CB  . VAL B 1 347 ? -62.418  9.994   263.175 1.00 34.31  ? 347 VAL B CB  1 
ATOM   6784 C  CG1 . VAL B 1 347 ? -61.002  9.462   263.324 1.00 36.92  ? 347 VAL B CG1 1 
ATOM   6785 C  CG2 . VAL B 1 347 ? -62.408  11.408  262.615 1.00 59.46  ? 347 VAL B CG2 1 
ATOM   6786 N  N   . TYR B 1 348 ? -62.710  6.712   262.031 1.00 30.18  ? 348 TYR B N   1 
ATOM   6787 C  CA  . TYR B 1 348 ? -62.641  5.308   262.411 1.00 29.55  ? 348 TYR B CA  1 
ATOM   6788 C  C   . TYR B 1 348 ? -61.191  4.911   262.644 1.00 32.32  ? 348 TYR B C   1 
ATOM   6789 O  O   . TYR B 1 348 ? -60.318  5.217   261.825 1.00 35.07  ? 348 TYR B O   1 
ATOM   6790 C  CB  . TYR B 1 348 ? -63.269  4.415   261.338 1.00 32.18  ? 348 TYR B CB  1 
ATOM   6791 C  CG  . TYR B 1 348 ? -64.780  4.397   261.368 1.00 34.51  ? 348 TYR B CG  1 
ATOM   6792 C  CD1 . TYR B 1 348 ? -65.466  3.595   262.270 1.00 33.60  ? 348 TYR B CD1 1 
ATOM   6793 C  CD2 . TYR B 1 348 ? -65.522  5.178   260.491 1.00 53.67  ? 348 TYR B CD2 1 
ATOM   6794 C  CE1 . TYR B 1 348 ? -66.847  3.574   262.303 1.00 32.19  ? 348 TYR B CE1 1 
ATOM   6795 C  CE2 . TYR B 1 348 ? -66.905  5.163   260.516 1.00 44.56  ? 348 TYR B CE2 1 
ATOM   6796 C  CZ  . TYR B 1 348 ? -67.561  4.359   261.423 1.00 32.63  ? 348 TYR B CZ  1 
ATOM   6797 O  OH  . TYR B 1 348 ? -68.937  4.339   261.452 1.00 31.40  ? 348 TYR B OH  1 
ATOM   6798 N  N   . GLU B 1 349 ? -60.942  4.233   263.758 1.00 31.73  ? 349 GLU B N   1 
ATOM   6799 C  CA  . GLU B 1 349 ? -59.614  3.771   264.128 1.00 31.92  ? 349 GLU B CA  1 
ATOM   6800 C  C   . GLU B 1 349 ? -59.449  2.295   263.786 1.00 27.96  ? 349 GLU B C   1 
ATOM   6801 O  O   . GLU B 1 349 ? -60.419  1.546   263.658 1.00 25.23  ? 349 GLU B O   1 
ATOM   6802 C  CB  . GLU B 1 349 ? -59.363  3.994   265.622 1.00 30.24  ? 349 GLU B CB  1 
ATOM   6803 C  CG  . GLU B 1 349 ? -59.408  5.451   266.050 1.00 30.25  ? 349 GLU B CG  1 
ATOM   6804 C  CD  . GLU B 1 349 ? -59.320  5.619   267.553 1.00 24.04  ? 349 GLU B CD  1 
ATOM   6805 O  OE1 . GLU B 1 349 ? -58.806  4.702   268.227 1.00 26.14  ? 349 GLU B OE1 1 
ATOM   6806 O  OE2 . GLU B 1 349 ? -59.764  6.669   268.063 1.00 29.68  ? 349 GLU B OE2 1 
ATOM   6807 N  N   . LEU B 1 350 ? -58.193  1.883   263.634 1.00 31.23  ? 350 LEU B N   1 
ATOM   6808 C  CA  . LEU B 1 350 ? -57.844  0.488   263.376 1.00 29.83  ? 350 LEU B CA  1 
ATOM   6809 C  C   . LEU B 1 350 ? -56.684  0.133   264.299 1.00 24.77  ? 350 LEU B C   1 
ATOM   6810 O  O   . LEU B 1 350 ? -55.540  0.519   264.045 1.00 24.24  ? 350 LEU B O   1 
ATOM   6811 C  CB  . LEU B 1 350 ? -57.483  0.263   261.911 1.00 28.37  ? 350 LEU B CB  1 
ATOM   6812 C  CG  . LEU B 1 350 ? -57.040  -1.154  261.538 1.00 26.68  ? 350 LEU B CG  1 
ATOM   6813 C  CD1 . LEU B 1 350 ? -58.092  -2.175  261.940 1.00 23.82  ? 350 LEU B CD1 1 
ATOM   6814 C  CD2 . LEU B 1 350 ? -56.744  -1.245  260.051 1.00 38.34  ? 350 LEU B CD2 1 
ATOM   6815 N  N   . THR B 1 351 ? -56.980  -0.592  265.371 1.00 23.50  ? 351 THR B N   1 
ATOM   6816 C  CA  . THR B 1 351 ? -55.986  -0.971  266.360 1.00 24.60  ? 351 THR B CA  1 
ATOM   6817 C  C   . THR B 1 351 ? -55.858  -2.487  266.411 1.00 22.46  ? 351 THR B C   1 
ATOM   6818 O  O   . THR B 1 351 ? -56.664  -3.226  265.841 1.00 19.43  ? 351 THR B O   1 
ATOM   6819 C  CB  . THR B 1 351 ? -56.348  -0.427  267.746 1.00 23.66  ? 351 THR B CB  1 
ATOM   6820 O  OG1 . THR B 1 351 ? -57.517  -1.099  268.232 1.00 20.36  ? 351 THR B OG1 1 
ATOM   6821 C  CG2 . THR B 1 351 ? -56.620  1.066   267.677 1.00 27.55  ? 351 THR B CG2 1 
ATOM   6822 N  N   . SER B 1 352 ? -54.824  -2.944  267.113 1.00 26.28  ? 352 SER B N   1 
ATOM   6823 C  CA  . SER B 1 352 ? -54.564  -4.367  267.258 1.00 24.59  ? 352 SER B CA  1 
ATOM   6824 C  C   . SER B 1 352 ? -53.774  -4.604  268.534 1.00 24.03  ? 352 SER B C   1 
ATOM   6825 O  O   . SER B 1 352 ? -52.881  -3.824  268.874 1.00 23.77  ? 352 SER B O   1 
ATOM   6826 C  CB  . SER B 1 352 ? -53.796  -4.925  266.057 1.00 27.37  ? 352 SER B CB  1 
ATOM   6827 O  OG  . SER B 1 352 ? -53.407  -6.268  266.286 1.00 35.72  ? 352 SER B OG  1 
ATOM   6828 N  N   . ALA B 1 353 ? -54.109  -5.684  269.232 1.00 24.09  ? 353 ALA B N   1 
ATOM   6829 C  CA  . ALA B 1 353 ? -53.416  -6.077  270.450 1.00 22.14  ? 353 ALA B CA  1 
ATOM   6830 C  C   . ALA B 1 353 ? -52.457  -7.216  270.138 1.00 22.40  ? 353 ALA B C   1 
ATOM   6831 O  O   . ALA B 1 353 ? -52.865  -8.246  269.592 1.00 22.22  ? 353 ALA B O   1 
ATOM   6832 C  CB  . ALA B 1 353 ? -54.406  -6.496  271.537 1.00 21.32  ? 353 ALA B CB  1 
ATOM   6833 N  N   . ILE B 1 354 ? -51.185  -7.024  270.479 1.00 23.29  ? 354 ILE B N   1 
ATOM   6834 C  CA  . ILE B 1 354 ? -50.148  -8.008  270.210 1.00 24.76  ? 354 ILE B CA  1 
ATOM   6835 C  C   . ILE B 1 354 ? -49.535  -8.441  271.534 1.00 24.15  ? 354 ILE B C   1 
ATOM   6836 O  O   . ILE B 1 354 ? -49.637  -7.753  272.551 1.00 27.00  ? 354 ILE B O   1 
ATOM   6837 C  CB  . ILE B 1 354 ? -49.063  -7.463  269.263 1.00 31.21  ? 354 ILE B CB  1 
ATOM   6838 C  CG1 . ILE B 1 354 ? -48.238  -6.387  269.971 1.00 29.36  ? 354 ILE B CG1 1 
ATOM   6839 C  CG2 . ILE B 1 354 ? -49.702  -6.892  268.010 1.00 31.38  ? 354 ILE B CG2 1 
ATOM   6840 C  CD1 . ILE B 1 354 ? -47.015  -5.952  269.201 1.00 31.67  ? 354 ILE B CD1 1 
ATOM   6841 N  N   . SER B 1 355 ? -48.888  -9.601  271.507 1.00 31.78  ? 355 SER B N   1 
ATOM   6842 C  CA  . SER B 1 355 ? -48.254  -10.124 272.703 1.00 30.95  ? 355 SER B CA  1 
ATOM   6843 C  C   . SER B 1 355 ? -46.907  -9.451  272.940 1.00 35.01  ? 355 SER B C   1 
ATOM   6844 O  O   . SER B 1 355 ? -46.280  -8.908  272.026 1.00 33.17  ? 355 SER B O   1 
ATOM   6845 C  CB  . SER B 1 355 ? -48.065  -11.635 272.599 1.00 27.27  ? 355 SER B CB  1 
ATOM   6846 O  OG  . SER B 1 355 ? -47.554  -12.166 273.809 1.00 27.96  ? 355 SER B OG  1 
ATOM   6847 N  N   . ALA B 1 356 ? -46.463  -9.500  274.194 1.00 35.88  ? 356 ALA B N   1 
ATOM   6848 C  CA  . ALA B 1 356 ? -45.189  -8.928  274.599 1.00 28.63  ? 356 ALA B CA  1 
ATOM   6849 C  C   . ALA B 1 356 ? -44.049  -9.938  274.541 1.00 30.31  ? 356 ALA B C   1 
ATOM   6850 O  O   . ALA B 1 356 ? -43.030  -9.748  275.216 1.00 30.96  ? 356 ALA B O   1 
ATOM   6851 C  CB  . ALA B 1 356 ? -45.303  -8.341  276.006 1.00 27.28  ? 356 ALA B CB  1 
ATOM   6852 N  N   . GLY B 1 357 ? -44.196  -11.002 273.755 1.00 34.68  ? 357 GLY B N   1 
ATOM   6853 C  CA  . GLY B 1 357 ? -43.171  -12.010 273.621 1.00 38.03  ? 357 GLY B CA  1 
ATOM   6854 C  C   . GLY B 1 357 ? -42.298  -11.745 272.413 1.00 31.76  ? 357 GLY B C   1 
ATOM   6855 O  O   . GLY B 1 357 ? -42.791  -11.653 271.287 1.00 29.97  ? 357 GLY B O   1 
ATOM   6856 N  N   . TYR B 1 358 ? -40.990  -11.624 272.654 1.00 34.84  ? 358 TYR B N   1 
ATOM   6857 C  CA  . TYR B 1 358 ? -40.056  -11.343 271.568 1.00 32.69  ? 358 TYR B CA  1 
ATOM   6858 C  C   . TYR B 1 358 ? -40.108  -12.426 270.500 1.00 33.99  ? 358 TYR B C   1 
ATOM   6859 O  O   . TYR B 1 358 ? -39.961  -12.139 269.307 1.00 34.56  ? 358 TYR B O   1 
ATOM   6860 C  CB  . TYR B 1 358 ? -38.638  -11.202 272.122 1.00 28.85  ? 358 TYR B CB  1 
ATOM   6861 C  CG  . TYR B 1 358 ? -38.037  -12.506 272.594 1.00 30.76  ? 358 TYR B CG  1 
ATOM   6862 C  CD1 . TYR B 1 358 ? -38.298  -12.991 273.867 1.00 33.38  ? 358 TYR B CD1 1 
ATOM   6863 C  CD2 . TYR B 1 358 ? -37.204  -13.248 271.767 1.00 31.83  ? 358 TYR B CD2 1 
ATOM   6864 C  CE1 . TYR B 1 358 ? -37.753  -14.183 274.301 1.00 35.44  ? 358 TYR B CE1 1 
ATOM   6865 C  CE2 . TYR B 1 358 ? -36.654  -14.439 272.192 1.00 34.01  ? 358 TYR B CE2 1 
ATOM   6866 C  CZ  . TYR B 1 358 ? -36.931  -14.901 273.460 1.00 34.59  ? 358 TYR B CZ  1 
ATOM   6867 O  OH  . TYR B 1 358 ? -36.384  -16.087 273.887 1.00 51.65  ? 358 TYR B OH  1 
ATOM   6868 N  N   . ASP B 1 359 ? -40.316  -13.680 270.909 1.00 32.59  ? 359 ASP B N   1 
ATOM   6869 C  CA  . ASP B 1 359 ? -40.473  -14.762 269.946 1.00 30.80  ? 359 ASP B CA  1 
ATOM   6870 C  C   . ASP B 1 359 ? -41.729  -14.597 269.103 1.00 34.34  ? 359 ASP B C   1 
ATOM   6871 O  O   . ASP B 1 359 ? -41.817  -15.189 268.022 1.00 36.41  ? 359 ASP B O   1 
ATOM   6872 C  CB  . ASP B 1 359 ? -40.502  -16.109 270.669 1.00 30.94  ? 359 ASP B CB  1 
ATOM   6873 C  CG  . ASP B 1 359 ? -41.584  -16.177 271.729 1.00 34.27  ? 359 ASP B CG  1 
ATOM   6874 O  OD1 . ASP B 1 359 ? -41.847  -15.142 272.377 1.00 35.00  ? 359 ASP B OD1 1 
ATOM   6875 O  OD2 . ASP B 1 359 ? -42.169  -17.264 271.916 1.00 46.73  ? 359 ASP B OD2 1 
ATOM   6876 N  N   . LYS B 1 360 ? -42.695  -13.811 269.573 1.00 35.63  ? 360 LYS B N   1 
ATOM   6877 C  CA  . LYS B 1 360 ? -43.912  -13.506 268.833 1.00 34.24  ? 360 LYS B CA  1 
ATOM   6878 C  C   . LYS B 1 360 ? -43.843  -12.160 268.129 1.00 34.01  ? 360 LYS B C   1 
ATOM   6879 O  O   . LYS B 1 360 ? -44.358  -12.020 267.015 1.00 36.69  ? 360 LYS B O   1 
ATOM   6880 C  CB  . LYS B 1 360 ? -45.116  -13.524 269.778 1.00 33.29  ? 360 LYS B CB  1 
ATOM   6881 C  CG  . LYS B 1 360 ? -45.096  -14.672 270.772 1.00 36.37  ? 360 LYS B CG  1 
ATOM   6882 C  CD  . LYS B 1 360 ? -46.001  -14.376 271.950 1.00 52.72  ? 360 LYS B CD  1 
ATOM   6883 C  CE  . LYS B 1 360 ? -45.935  -15.467 272.999 1.00 42.59  ? 360 LYS B CE  1 
ATOM   6884 N  NZ  . LYS B 1 360 ? -44.531  -15.820 273.343 1.00 40.17  ? 360 LYS B NZ  1 
ATOM   6885 N  N   . ILE B 1 361 ? -43.217  -11.163 268.760 1.00 34.09  ? 361 ILE B N   1 
ATOM   6886 C  CA  . ILE B 1 361 ? -43.029  -9.866  268.116 1.00 35.75  ? 361 ILE B CA  1 
ATOM   6887 C  C   . ILE B 1 361 ? -42.110  -9.996  266.909 1.00 44.78  ? 361 ILE B C   1 
ATOM   6888 O  O   . ILE B 1 361 ? -42.238  -9.244  265.935 1.00 47.76  ? 361 ILE B O   1 
ATOM   6889 C  CB  . ILE B 1 361 ? -42.489  -8.842  269.136 1.00 33.47  ? 361 ILE B CB  1 
ATOM   6890 C  CG1 . ILE B 1 361 ? -43.435  -8.726  270.332 1.00 39.38  ? 361 ILE B CG1 1 
ATOM   6891 C  CG2 . ILE B 1 361 ? -42.293  -7.481  268.489 1.00 39.28  ? 361 ILE B CG2 1 
ATOM   6892 C  CD1 . ILE B 1 361 ? -42.980  -7.729  271.376 1.00 35.18  ? 361 ILE B CD1 1 
ATOM   6893 N  N   . ALA B 1 362 ? -41.181  -10.953 266.941 1.00 50.09  ? 362 ALA B N   1 
ATOM   6894 C  CA  . ALA B 1 362 ? -40.273  -11.153 265.820 1.00 41.60  ? 362 ALA B CA  1 
ATOM   6895 C  C   . ALA B 1 362 ? -40.934  -11.849 264.638 1.00 46.30  ? 362 ALA B C   1 
ATOM   6896 O  O   . ALA B 1 362 ? -40.417  -11.761 263.520 1.00 51.03  ? 362 ALA B O   1 
ATOM   6897 C  CB  . ALA B 1 362 ? -39.049  -11.956 266.265 1.00 40.37  ? 362 ALA B CB  1 
ATOM   6898 N  N   . VAL B 1 363 ? -42.054  -12.538 264.856 1.00 45.46  ? 363 VAL B N   1 
ATOM   6899 C  CA  . VAL B 1 363 ? -42.757  -13.224 263.776 1.00 47.44  ? 363 VAL B CA  1 
ATOM   6900 C  C   . VAL B 1 363 ? -43.301  -12.183 262.809 1.00 49.23  ? 363 VAL B C   1 
ATOM   6901 O  O   . VAL B 1 363 ? -42.756  -11.988 261.716 1.00 50.16  ? 363 VAL B O   1 
ATOM   6902 C  CB  . VAL B 1 363 ? -43.883  -14.124 264.317 1.00 48.36  ? 363 VAL B CB  1 
ATOM   6903 C  CG1 . VAL B 1 363 ? -44.687  -14.714 263.169 1.00 59.46  ? 363 VAL B CG1 1 
ATOM   6904 C  CG2 . VAL B 1 363 ? -43.306  -15.227 265.186 1.00 47.87  ? 363 VAL B CG2 1 
ATOM   6905 N  N   . VAL B 1 364 ? -44.375  -11.509 263.202 1.00 53.89  ? 364 VAL B N   1 
ATOM   6906 C  CA  . VAL B 1 364 ? -44.907  -10.389 262.437 1.00 66.19  ? 364 VAL B CA  1 
ATOM   6907 C  C   . VAL B 1 364 ? -44.266  -9.115  262.959 1.00 62.39  ? 364 VAL B C   1 
ATOM   6908 O  O   . VAL B 1 364 ? -44.332  -8.822  264.157 1.00 72.88  ? 364 VAL B O   1 
ATOM   6909 C  CB  . VAL B 1 364 ? -46.437  -10.318 262.546 1.00 65.48  ? 364 VAL B CB  1 
ATOM   6910 C  CG1 . VAL B 1 364 ? -46.968  -9.204  261.661 1.00 61.89  ? 364 VAL B CG1 1 
ATOM   6911 C  CG2 . VAL B 1 364 ? -47.048  -11.647 262.171 1.00 86.85  ? 364 VAL B CG2 1 
ATOM   6912 N  N   . ASN B 1 365 ? -43.645  -8.359  262.064 1.00 53.83  ? 365 ASN B N   1 
ATOM   6913 C  CA  . ASN B 1 365 ? -42.881  -7.179  262.435 1.00 57.29  ? 365 ASN B CA  1 
ATOM   6914 C  C   . ASN B 1 365 ? -43.590  -5.940  261.901 1.00 52.61  ? 365 ASN B C   1 
ATOM   6915 O  O   . ASN B 1 365 ? -43.944  -5.883  260.718 1.00 48.89  ? 365 ASN B O   1 
ATOM   6916 C  CB  . ASN B 1 365 ? -41.452  -7.292  261.910 1.00 68.95  ? 365 ASN B CB  1 
ATOM   6917 C  CG  . ASN B 1 365 ? -40.484  -7.782  262.970 1.00 81.50  ? 365 ASN B CG  1 
ATOM   6918 O  OD1 . ASN B 1 365 ? -39.776  -6.992  263.594 1.00 64.67  ? 365 ASN B OD1 1 
ATOM   6919 N  ND2 . ASN B 1 365 ? -40.455  -9.091  263.184 1.00 87.06  ? 365 ASN B ND2 1 
ATOM   6920 N  N   . TYR B 1 366 ? -43.780  -4.950  262.773 1.00 50.07  ? 366 TYR B N   1 
ATOM   6921 C  CA  . TYR B 1 366 ? -44.847  -3.969  262.627 1.00 44.51  ? 366 TYR B CA  1 
ATOM   6922 C  C   . TYR B 1 366 ? -44.397  -2.642  262.029 1.00 45.17  ? 366 TYR B C   1 
ATOM   6923 O  O   . TYR B 1 366 ? -45.147  -1.663  262.104 1.00 53.94  ? 366 TYR B O   1 
ATOM   6924 C  CB  . TYR B 1 366 ? -45.509  -3.721  263.984 1.00 45.67  ? 366 TYR B CB  1 
ATOM   6925 C  CG  . TYR B 1 366 ? -46.011  -4.982  264.649 1.00 49.65  ? 366 TYR B CG  1 
ATOM   6926 C  CD1 . TYR B 1 366 ? -47.314  -5.421  264.462 1.00 56.96  ? 366 TYR B CD1 1 
ATOM   6927 C  CD2 . TYR B 1 366 ? -45.179  -5.732  265.469 1.00 50.57  ? 366 TYR B CD2 1 
ATOM   6928 C  CE1 . TYR B 1 366 ? -47.771  -6.575  265.069 1.00 54.14  ? 366 TYR B CE1 1 
ATOM   6929 C  CE2 . TYR B 1 366 ? -45.627  -6.882  266.082 1.00 48.86  ? 366 TYR B CE2 1 
ATOM   6930 C  CZ  . TYR B 1 366 ? -46.923  -7.301  265.878 1.00 46.45  ? 366 TYR B CZ  1 
ATOM   6931 O  OH  . TYR B 1 366 ? -47.367  -8.451  266.489 1.00 61.73  ? 366 TYR B OH  1 
ATOM   6932 N  N   . ALA B 1 367 ? -43.200  -2.571  261.441 1.00 48.32  ? 367 ALA B N   1 
ATOM   6933 C  CA  . ALA B 1 367 ? -42.842  -1.359  260.711 1.00 43.24  ? 367 ALA B CA  1 
ATOM   6934 C  C   . ALA B 1 367 ? -43.748  -1.165  259.505 1.00 40.18  ? 367 ALA B C   1 
ATOM   6935 O  O   . ALA B 1 367 ? -44.026  -0.026  259.111 1.00 39.44  ? 367 ALA B O   1 
ATOM   6936 C  CB  . ALA B 1 367 ? -41.379  -1.399  260.272 1.00 49.82  ? 367 ALA B CB  1 
ATOM   6937 N  N   . GLU B 1 368 ? -44.218  -2.262  258.913 1.00 47.02  ? 368 GLU B N   1 
ATOM   6938 C  CA  . GLU B 1 368 ? -45.216  -2.203  257.856 1.00 42.74  ? 368 GLU B CA  1 
ATOM   6939 C  C   . GLU B 1 368 ? -46.634  -2.157  258.403 1.00 60.07  ? 368 GLU B C   1 
ATOM   6940 O  O   . GLU B 1 368 ? -47.503  -1.514  257.801 1.00 56.08  ? 368 GLU B O   1 
ATOM   6941 C  CB  . GLU B 1 368 ? -45.068  -3.411  256.926 1.00 41.30  ? 368 GLU B CB  1 
ATOM   6942 C  CG  . GLU B 1 368 ? -44.024  -3.238  255.840 1.00 39.95  ? 368 GLU B CG  1 
ATOM   6943 C  CD  . GLU B 1 368 ? -44.431  -2.213  254.802 1.00 35.09  ? 368 GLU B CD  1 
ATOM   6944 O  OE1 . GLU B 1 368 ? -45.648  -2.035  254.584 1.00 35.93  ? 368 GLU B OE1 1 
ATOM   6945 O  OE2 . GLU B 1 368 ? -43.535  -1.582  254.206 1.00 40.30  ? 368 GLU B OE2 1 
ATOM   6946 N  N   . ALA B 1 369 ? -46.884  -2.820  259.535 1.00 53.08  ? 369 ALA B N   1 
ATOM   6947 C  CA  . ALA B 1 369 ? -48.226  -2.836  260.106 1.00 54.15  ? 369 ALA B CA  1 
ATOM   6948 C  C   . ALA B 1 369 ? -48.632  -1.469  260.638 1.00 39.13  ? 369 ALA B C   1 
ATOM   6949 O  O   . ALA B 1 369 ? -49.828  -1.163  260.702 1.00 41.71  ? 369 ALA B O   1 
ATOM   6950 C  CB  . ALA B 1 369 ? -48.314  -3.883  261.217 1.00 67.66  ? 369 ALA B CB  1 
ATOM   6951 N  N   . GLN B 1 370 ? -47.663  -0.637  261.024 1.00 37.63  ? 370 GLN B N   1 
ATOM   6952 C  CA  . GLN B 1 370 ? -47.984  0.691   261.531 1.00 35.80  ? 370 GLN B CA  1 
ATOM   6953 C  C   . GLN B 1 370 ? -48.473  1.634   260.440 1.00 33.53  ? 370 GLN B C   1 
ATOM   6954 O  O   . GLN B 1 370 ? -49.002  2.703   260.763 1.00 33.26  ? 370 GLN B O   1 
ATOM   6955 C  CB  . GLN B 1 370 ? -46.769  1.299   262.234 1.00 40.57  ? 370 GLN B CB  1 
ATOM   6956 C  CG  . GLN B 1 370 ? -45.690  1.805   261.293 1.00 45.69  ? 370 GLN B CG  1 
ATOM   6957 C  CD  . GLN B 1 370 ? -44.570  2.518   262.025 1.00 42.75  ? 370 GLN B CD  1 
ATOM   6958 O  OE1 . GLN B 1 370 ? -44.655  2.760   263.229 1.00 43.72  ? 370 GLN B OE1 1 
ATOM   6959 N  NE2 . GLN B 1 370 ? -43.513  2.862   261.299 1.00 45.71  ? 370 GLN B NE2 1 
ATOM   6960 N  N   . LYS B 1 371 ? -48.314  1.270   259.167 1.00 33.08  ? 371 LYS B N   1 
ATOM   6961 C  CA  . LYS B 1 371 ? -48.842  2.079   258.075 1.00 33.72  ? 371 LYS B CA  1 
ATOM   6962 C  C   . LYS B 1 371 ? -50.357  1.996   257.960 1.00 34.15  ? 371 LYS B C   1 
ATOM   6963 O  O   . LYS B 1 371 ? -50.939  2.704   257.131 1.00 40.65  ? 371 LYS B O   1 
ATOM   6964 C  CB  . LYS B 1 371 ? -48.191  1.664   256.754 1.00 35.87  ? 371 LYS B CB  1 
ATOM   6965 C  CG  . LYS B 1 371 ? -46.684  1.857   256.732 1.00 47.59  ? 371 LYS B CG  1 
ATOM   6966 C  CD  . LYS B 1 371 ? -46.129  1.750   255.324 1.00 35.87  ? 371 LYS B CD  1 
ATOM   6967 C  CE  . LYS B 1 371 ? -44.622  1.941   255.315 1.00 38.28  ? 371 LYS B CE  1 
ATOM   6968 N  NZ  . LYS B 1 371 ? -43.900  0.730   255.787 1.00 50.14  ? 371 LYS B NZ  1 
ATOM   6969 N  N   . SER B 1 372 ? -51.004  1.152   258.762 1.00 32.66  ? 372 SER B N   1 
ATOM   6970 C  CA  . SER B 1 372 ? -52.457  1.081   258.818 1.00 30.36  ? 372 SER B CA  1 
ATOM   6971 C  C   . SER B 1 372 ? -53.018  1.107   260.231 1.00 36.67  ? 372 SER B C   1 
ATOM   6972 O  O   . SER B 1 372 ? -54.188  1.471   260.399 1.00 67.28  ? 372 SER B O   1 
ATOM   6973 C  CB  . SER B 1 372 ? -52.962  -0.186  258.113 1.00 32.74  ? 372 SER B CB  1 
ATOM   6974 O  OG  . SER B 1 372 ? -52.458  -1.348  258.743 1.00 35.19  ? 372 SER B OG  1 
ATOM   6975 N  N   . LEU B 1 373 ? -52.236  0.741   261.244 1.00 33.04  ? 373 LEU B N   1 
ATOM   6976 C  CA  . LEU B 1 373 ? -52.710  0.764   262.619 1.00 30.41  ? 373 LEU B CA  1 
ATOM   6977 C  C   . LEU B 1 373 ? -52.553  2.153   263.220 1.00 27.82  ? 373 LEU B C   1 
ATOM   6978 O  O   . LEU B 1 373 ? -51.590  2.868   262.929 1.00 29.26  ? 373 LEU B O   1 
ATOM   6979 C  CB  . LEU B 1 373 ? -51.949  -0.255  263.466 1.00 29.74  ? 373 LEU B CB  1 
ATOM   6980 C  CG  . LEU B 1 373 ? -52.159  -1.725  263.109 1.00 33.94  ? 373 LEU B CG  1 
ATOM   6981 C  CD1 . LEU B 1 373 ? -51.360  -2.623  264.039 1.00 28.89  ? 373 LEU B CD1 1 
ATOM   6982 C  CD2 . LEU B 1 373 ? -53.638  -2.069  263.168 1.00 40.68  ? 373 LEU B CD2 1 
ATOM   6983 N  N   . GLY B 1 374 ? -53.511  2.532   264.061 1.00 28.72  ? 374 GLY B N   1 
ATOM   6984 C  CA  . GLY B 1 374 ? -53.438  3.792   264.771 1.00 32.24  ? 374 GLY B CA  1 
ATOM   6985 C  C   . GLY B 1 374 ? -52.846  3.628   266.155 1.00 33.19  ? 374 GLY B C   1 
ATOM   6986 O  O   . GLY B 1 374 ? -52.228  4.554   266.689 1.00 42.14  ? 374 GLY B O   1 
ATOM   6987 N  N   . LYS B 1 375 ? -53.035  2.447   266.741 1.00 27.32  ? 375 LYS B N   1 
ATOM   6988 C  CA  . LYS B 1 375 ? -52.491  2.120   268.051 1.00 28.84  ? 375 LYS B CA  1 
ATOM   6989 C  C   . LYS B 1 375 ? -52.224  0.623   268.114 1.00 27.80  ? 375 LYS B C   1 
ATOM   6990 O  O   . LYS B 1 375 ? -52.914  -0.173  267.472 1.00 39.04  ? 375 LYS B O   1 
ATOM   6991 C  CB  . LYS B 1 375 ? -53.439  2.537   269.184 1.00 27.85  ? 375 LYS B CB  1 
ATOM   6992 C  CG  . LYS B 1 375 ? -53.383  4.015   269.536 1.00 33.62  ? 375 LYS B CG  1 
ATOM   6993 C  CD  . LYS B 1 375 ? -54.620  4.456   270.297 1.00 42.70  ? 375 LYS B CD  1 
ATOM   6994 C  CE  . LYS B 1 375 ? -55.762  4.764   269.345 1.00 29.92  ? 375 LYS B CE  1 
ATOM   6995 N  NZ  . LYS B 1 375 ? -57.033  4.117   269.768 1.00 27.47  ? 375 LYS B NZ  1 
ATOM   6996 N  N   . ILE B 1 376 ? -51.212  0.250   268.893 1.00 26.84  ? 376 ILE B N   1 
ATOM   6997 C  CA  . ILE B 1 376 ? -50.824  -1.143  269.083 1.00 25.63  ? 376 ILE B CA  1 
ATOM   6998 C  C   . ILE B 1 376 ? -50.869  -1.439  270.574 1.00 24.35  ? 376 ILE B C   1 
ATOM   6999 O  O   . ILE B 1 376 ? -50.121  -0.838  271.355 1.00 26.13  ? 376 ILE B O   1 
ATOM   7000 C  CB  . ILE B 1 376 ? -49.428  -1.433  268.510 1.00 26.43  ? 376 ILE B CB  1 
ATOM   7001 C  CG1 . ILE B 1 376 ? -49.408  -1.184  267.000 1.00 25.71  ? 376 ILE B CG1 1 
ATOM   7002 C  CG2 . ILE B 1 376 ? -49.011  -2.859  268.825 1.00 23.93  ? 376 ILE B CG2 1 
ATOM   7003 C  CD1 . ILE B 1 376 ? -48.067  -1.457  266.356 1.00 26.85  ? 376 ILE B CD1 1 
ATOM   7004 N  N   . PHE B 1 377 ? -51.743  -2.363  270.968 1.00 24.37  ? 377 PHE B N   1 
ATOM   7005 C  CA  . PHE B 1 377 ? -51.927  -2.711  272.376 1.00 23.70  ? 377 PHE B CA  1 
ATOM   7006 C  C   . PHE B 1 377 ? -50.978  -3.849  272.724 1.00 25.95  ? 377 PHE B C   1 
ATOM   7007 O  O   . PHE B 1 377 ? -51.285  -5.026  272.537 1.00 29.46  ? 377 PHE B O   1 
ATOM   7008 C  CB  . PHE B 1 377 ? -53.378  -3.083  272.652 1.00 22.47  ? 377 PHE B CB  1 
ATOM   7009 C  CG  . PHE B 1 377 ? -54.344  -1.952  272.443 1.00 25.80  ? 377 PHE B CG  1 
ATOM   7010 C  CD1 . PHE B 1 377 ? -54.351  -0.864  273.299 1.00 24.53  ? 377 PHE B CD1 1 
ATOM   7011 C  CD2 . PHE B 1 377 ? -55.251  -1.982  271.398 1.00 26.20  ? 377 PHE B CD2 1 
ATOM   7012 C  CE1 . PHE B 1 377 ? -55.238  0.177   273.113 1.00 25.94  ? 377 PHE B CE1 1 
ATOM   7013 C  CE2 . PHE B 1 377 ? -56.143  -0.944  271.208 1.00 25.63  ? 377 PHE B CE2 1 
ATOM   7014 C  CZ  . PHE B 1 377 ? -56.136  0.137   272.065 1.00 30.75  ? 377 PHE B CZ  1 
ATOM   7015 N  N   . LEU B 1 378 ? -49.807  -3.493  273.248 1.00 25.72  ? 378 LEU B N   1 
ATOM   7016 C  CA  . LEU B 1 378 ? -48.804  -4.487  273.617 1.00 22.09  ? 378 LEU B CA  1 
ATOM   7017 C  C   . LEU B 1 378 ? -49.242  -5.195  274.893 1.00 26.92  ? 378 LEU B C   1 
ATOM   7018 O  O   . LEU B 1 378 ? -49.197  -4.614  275.982 1.00 38.90  ? 378 LEU B O   1 
ATOM   7019 C  CB  . LEU B 1 378 ? -47.444  -3.820  273.797 1.00 23.54  ? 378 LEU B CB  1 
ATOM   7020 C  CG  . LEU B 1 378 ? -46.290  -4.741  274.189 1.00 26.97  ? 378 LEU B CG  1 
ATOM   7021 C  CD1 . LEU B 1 378 ? -45.993  -5.717  273.065 1.00 32.03  ? 378 LEU B CD1 1 
ATOM   7022 C  CD2 . LEU B 1 378 ? -45.054  -3.932  274.541 1.00 26.34  ? 378 LEU B CD2 1 
ATOM   7023 N  N   . MET B 1 379 ? -49.665  -6.452  274.761 1.00 29.25  ? 379 MET B N   1 
ATOM   7024 C  CA  . MET B 1 379 ? -50.170  -7.244  275.882 1.00 26.17  ? 379 MET B CA  1 
ATOM   7025 C  C   . MET B 1 379 ? -49.001  -7.641  276.780 1.00 28.46  ? 379 MET B C   1 
ATOM   7026 O  O   . MET B 1 379 ? -48.441  -8.736  276.689 1.00 28.36  ? 379 MET B O   1 
ATOM   7027 C  CB  . MET B 1 379 ? -50.922  -8.464  275.365 1.00 20.78  ? 379 MET B CB  1 
ATOM   7028 C  CG  . MET B 1 379 ? -52.187  -8.119  274.597 1.00 20.04  ? 379 MET B CG  1 
ATOM   7029 S  SD  . MET B 1 379 ? -52.908  -9.541  273.762 1.00 17.67  ? 379 MET B SD  1 
ATOM   7030 C  CE  . MET B 1 379 ? -52.659  -10.816 274.991 1.00 38.98  ? 379 MET B CE  1 
ATOM   7031 N  N   . SER B 1 380 ? -48.636  -6.727  277.678 1.00 27.62  ? 380 SER B N   1 
ATOM   7032 C  CA  . SER B 1 380 ? -47.480  -6.916  278.555 1.00 27.44  ? 380 SER B CA  1 
ATOM   7033 C  C   . SER B 1 380 ? -47.903  -7.543  279.885 1.00 25.61  ? 380 SER B C   1 
ATOM   7034 O  O   . SER B 1 380 ? -47.710  -6.987  280.966 1.00 24.95  ? 380 SER B O   1 
ATOM   7035 C  CB  . SER B 1 380 ? -46.763  -5.589  278.773 1.00 29.60  ? 380 SER B CB  1 
ATOM   7036 O  OG  . SER B 1 380 ? -47.637  -4.626  279.336 1.00 26.23  ? 380 SER B OG  1 
ATOM   7037 N  N   . TYR B 1 381 ? -48.487  -8.732  279.786 1.00 26.27  ? 381 TYR B N   1 
ATOM   7038 C  CA  . TYR B 1 381 ? -48.897  -9.489  280.962 1.00 32.12  ? 381 TYR B CA  1 
ATOM   7039 C  C   . TYR B 1 381 ? -48.960  -10.965 280.588 1.00 37.71  ? 381 TYR B C   1 
ATOM   7040 O  O   . TYR B 1 381 ? -48.717  -11.346 279.440 1.00 40.10  ? 381 TYR B O   1 
ATOM   7041 C  CB  . TYR B 1 381 ? -50.232  -8.979  281.514 1.00 38.30  ? 381 TYR B CB  1 
ATOM   7042 C  CG  . TYR B 1 381 ? -51.234  -8.580  280.456 1.00 26.26  ? 381 TYR B CG  1 
ATOM   7043 C  CD1 . TYR B 1 381 ? -52.004  -9.533  279.803 1.00 32.76  ? 381 TYR B CD1 1 
ATOM   7044 C  CD2 . TYR B 1 381 ? -51.416  -7.246  280.116 1.00 26.02  ? 381 TYR B CD2 1 
ATOM   7045 C  CE1 . TYR B 1 381 ? -52.923  -9.168  278.836 1.00 35.73  ? 381 TYR B CE1 1 
ATOM   7046 C  CE2 . TYR B 1 381 ? -52.331  -6.872  279.152 1.00 28.76  ? 381 TYR B CE2 1 
ATOM   7047 C  CZ  . TYR B 1 381 ? -53.082  -7.837  278.516 1.00 29.96  ? 381 TYR B CZ  1 
ATOM   7048 O  OH  . TYR B 1 381 ? -53.995  -7.467  277.555 1.00 24.93  ? 381 TYR B OH  1 
ATOM   7049 N  N   . ASP B 1 382 ? -49.286  -11.795 281.582 1.00 30.11  ? 382 ASP B N   1 
ATOM   7050 C  CA  . ASP B 1 382 ? -49.320  -13.250 281.426 1.00 27.04  ? 382 ASP B CA  1 
ATOM   7051 C  C   . ASP B 1 382 ? -47.963  -13.797 280.988 1.00 26.24  ? 382 ASP B C   1 
ATOM   7052 O  O   . ASP B 1 382 ? -47.879  -14.749 280.211 1.00 29.17  ? 382 ASP B O   1 
ATOM   7053 C  CB  . ASP B 1 382 ? -50.422  -13.684 280.456 1.00 28.06  ? 382 ASP B CB  1 
ATOM   7054 C  CG  . ASP B 1 382 ? -51.811  -13.390 280.984 1.00 29.52  ? 382 ASP B CG  1 
ATOM   7055 O  OD1 . ASP B 1 382 ? -51.995  -13.411 282.218 1.00 29.90  ? 382 ASP B OD1 1 
ATOM   7056 O  OD2 . ASP B 1 382 ? -52.719  -13.136 280.166 1.00 40.80  ? 382 ASP B OD2 1 
ATOM   7057 N  N   . PHE B 1 383 ? -46.888  -13.183 281.489 1.00 28.64  ? 383 PHE B N   1 
ATOM   7058 C  CA  . PHE B 1 383 ? -45.554  -13.718 281.237 1.00 36.43  ? 383 PHE B CA  1 
ATOM   7059 C  C   . PHE B 1 383 ? -45.363  -15.057 281.934 1.00 30.94  ? 383 PHE B C   1 
ATOM   7060 O  O   . PHE B 1 383 ? -44.795  -15.992 281.357 1.00 29.05  ? 383 PHE B O   1 
ATOM   7061 C  CB  . PHE B 1 383 ? -44.488  -12.722 281.697 1.00 35.06  ? 383 PHE B CB  1 
ATOM   7062 C  CG  . PHE B 1 383 ? -44.439  -11.464 280.881 1.00 27.10  ? 383 PHE B CG  1 
ATOM   7063 C  CD1 . PHE B 1 383 ? -44.595  -11.506 279.507 1.00 27.13  ? 383 PHE B CD1 1 
ATOM   7064 C  CD2 . PHE B 1 383 ? -44.238  -10.237 281.490 1.00 27.12  ? 383 PHE B CD2 1 
ATOM   7065 C  CE1 . PHE B 1 383 ? -44.549  -10.351 278.755 1.00 25.30  ? 383 PHE B CE1 1 
ATOM   7066 C  CE2 . PHE B 1 383 ? -44.192  -9.077  280.743 1.00 27.14  ? 383 PHE B CE2 1 
ATOM   7067 C  CZ  . PHE B 1 383 ? -44.348  -9.134  279.374 1.00 25.66  ? 383 PHE B CZ  1 
ATOM   7068 N  N   . LYS B 1 384 ? -45.829  -15.166 283.175 1.00 32.89  ? 384 LYS B N   1 
ATOM   7069 C  CA  . LYS B 1 384 ? -45.746  -16.392 283.949 1.00 31.48  ? 384 LYS B CA  1 
ATOM   7070 C  C   . LYS B 1 384 ? -47.129  -16.724 284.490 1.00 29.79  ? 384 LYS B C   1 
ATOM   7071 O  O   . LYS B 1 384 ? -47.977  -15.846 284.658 1.00 31.14  ? 384 LYS B O   1 
ATOM   7072 C  CB  . LYS B 1 384 ? -44.742  -16.259 285.101 1.00 29.89  ? 384 LYS B CB  1 
ATOM   7073 C  CG  . LYS B 1 384 ? -43.375  -15.748 284.673 1.00 31.86  ? 384 LYS B CG  1 
ATOM   7074 C  CD  . LYS B 1 384 ? -42.650  -16.728 283.767 1.00 42.51  ? 384 LYS B CD  1 
ATOM   7075 C  CE  . LYS B 1 384 ? -41.250  -16.228 283.443 1.00 38.43  ? 384 LYS B CE  1 
ATOM   7076 N  NZ  . LYS B 1 384 ? -40.471  -17.215 282.650 1.00 41.07  ? 384 LYS B NZ  1 
ATOM   7077 N  N   . GLY B 1 385 ? -47.353  -18.007 284.762 1.00 30.47  ? 385 GLY B N   1 
ATOM   7078 C  CA  . GLY B 1 385 ? -48.658  -18.426 285.231 1.00 30.81  ? 385 GLY B CA  1 
ATOM   7079 C  C   . GLY B 1 385 ? -48.604  -19.781 285.901 1.00 36.44  ? 385 GLY B C   1 
ATOM   7080 O  O   . GLY B 1 385 ? -47.547  -20.405 286.019 1.00 28.65  ? 385 GLY B O   1 
ATOM   7081 N  N   . ALA B 1 386 ? -49.779  -20.230 286.341 1.00 37.58  ? 386 ALA B N   1 
ATOM   7082 C  CA  . ALA B 1 386 ? -49.924  -21.508 287.025 1.00 28.86  ? 386 ALA B CA  1 
ATOM   7083 C  C   . ALA B 1 386 ? -49.895  -22.699 286.078 1.00 29.99  ? 386 ALA B C   1 
ATOM   7084 O  O   . ALA B 1 386 ? -49.967  -23.841 286.545 1.00 29.77  ? 386 ALA B O   1 
ATOM   7085 C  CB  . ALA B 1 386 ? -51.223  -21.524 287.834 1.00 29.23  ? 386 ALA B CB  1 
ATOM   7086 N  N   . TRP B 1 387 ? -49.796  -22.466 284.767 1.00 28.76  ? 387 TRP B N   1 
ATOM   7087 C  CA  . TRP B 1 387 ? -49.664  -23.568 283.823 1.00 30.16  ? 387 TRP B CA  1 
ATOM   7088 C  C   . TRP B 1 387 ? -48.351  -24.318 283.995 1.00 38.63  ? 387 TRP B C   1 
ATOM   7089 O  O   . TRP B 1 387 ? -48.217  -25.435 283.484 1.00 58.60  ? 387 TRP B O   1 
ATOM   7090 C  CB  . TRP B 1 387 ? -49.789  -23.047 282.391 1.00 30.13  ? 387 TRP B CB  1 
ATOM   7091 C  CG  . TRP B 1 387 ? -48.914  -21.866 282.108 1.00 31.06  ? 387 TRP B CG  1 
ATOM   7092 C  CD1 . TRP B 1 387 ? -47.573  -21.879 281.857 1.00 32.65  ? 387 TRP B CD1 1 
ATOM   7093 C  CD2 . TRP B 1 387 ? -49.320  -20.494 282.046 1.00 34.18  ? 387 TRP B CD2 1 
ATOM   7094 N  NE1 . TRP B 1 387 ? -47.119  -20.601 281.643 1.00 34.75  ? 387 TRP B NE1 1 
ATOM   7095 C  CE2 . TRP B 1 387 ? -48.172  -19.731 281.753 1.00 33.84  ? 387 TRP B CE2 1 
ATOM   7096 C  CE3 . TRP B 1 387 ? -50.543  -19.836 282.209 1.00 37.78  ? 387 TRP B CE3 1 
ATOM   7097 C  CZ2 . TRP B 1 387 ? -48.211  -18.345 281.620 1.00 42.06  ? 387 TRP B CZ2 1 
ATOM   7098 C  CZ3 . TRP B 1 387 ? -50.579  -18.460 282.077 1.00 32.78  ? 387 TRP B CZ3 1 
ATOM   7099 C  CH2 . TRP B 1 387 ? -49.421  -17.730 281.786 1.00 38.42  ? 387 TRP B CH2 1 
ATOM   7100 N  N   . SER B 1 388 ? -47.384  -23.732 284.698 1.00 35.08  ? 388 SER B N   1 
ATOM   7101 C  CA  . SER B 1 388 ? -46.110  -24.384 284.978 1.00 33.60  ? 388 SER B CA  1 
ATOM   7102 C  C   . SER B 1 388 ? -45.724  -24.089 286.418 1.00 34.43  ? 388 SER B C   1 
ATOM   7103 O  O   . SER B 1 388 ? -45.498  -22.929 286.775 1.00 38.25  ? 388 SER B O   1 
ATOM   7104 C  CB  . SER B 1 388 ? -45.016  -23.904 284.019 1.00 34.65  ? 388 SER B CB  1 
ATOM   7105 O  OG  . SER B 1 388 ? -43.760  -24.466 284.358 1.00 35.75  ? 388 SER B OG  1 
ATOM   7106 N  N   . ASN B 1 389 ? -45.658  -25.133 287.243 1.00 36.39  ? 389 ASN B N   1 
ATOM   7107 C  CA  . ASN B 1 389 ? -45.210  -24.983 288.621 1.00 34.20  ? 389 ASN B CA  1 
ATOM   7108 C  C   . ASN B 1 389 ? -43.704  -24.798 288.733 1.00 37.13  ? 389 ASN B C   1 
ATOM   7109 O  O   . ASN B 1 389 ? -43.220  -24.437 289.811 1.00 41.79  ? 389 ASN B O   1 
ATOM   7110 C  CB  . ASN B 1 389 ? -45.637  -26.195 289.451 1.00 37.75  ? 389 ASN B CB  1 
ATOM   7111 C  CG  . ASN B 1 389 ? -47.141  -26.305 289.591 1.00 44.09  ? 389 ASN B CG  1 
ATOM   7112 O  OD1 . ASN B 1 389 ? -47.874  -25.364 289.291 1.00 64.16  ? 389 ASN B OD1 1 
ATOM   7113 N  ND2 . ASN B 1 389 ? -47.609  -27.458 290.055 1.00 57.09  ? 389 ASN B ND2 1 
ATOM   7114 N  N   . THR B 1 390 ? -42.958  -25.039 287.656 1.00 36.37  ? 390 THR B N   1 
ATOM   7115 C  CA  . THR B 1 390 ? -41.510  -24.881 287.662 1.00 32.77  ? 390 THR B CA  1 
ATOM   7116 C  C   . THR B 1 390 ? -41.092  -23.458 287.308 1.00 33.16  ? 390 THR B C   1 
ATOM   7117 O  O   . THR B 1 390 ? -40.334  -22.826 288.050 1.00 44.21  ? 390 THR B O   1 
ATOM   7118 C  CB  . THR B 1 390 ? -40.869  -25.873 286.686 1.00 34.38  ? 390 THR B CB  1 
ATOM   7119 O  OG1 . THR B 1 390 ? -41.353  -25.621 285.361 1.00 36.43  ? 390 THR B OG1 1 
ATOM   7120 C  CG2 . THR B 1 390 ? -41.210  -27.302 287.079 1.00 37.79  ? 390 THR B CG2 1 
ATOM   7121 N  N   . ASP B 1 391 ? -41.583  -22.942 286.180 1.00 33.64  ? 391 ASP B N   1 
ATOM   7122 C  CA  . ASP B 1 391 ? -41.208  -21.613 285.698 1.00 35.96  ? 391 ASP B CA  1 
ATOM   7123 C  C   . ASP B 1 391 ? -42.003  -20.565 286.474 1.00 32.28  ? 391 ASP B C   1 
ATOM   7124 O  O   . ASP B 1 391 ? -42.989  -19.997 285.998 1.00 32.02  ? 391 ASP B O   1 
ATOM   7125 C  CB  . ASP B 1 391 ? -41.444  -21.502 284.197 1.00 38.42  ? 391 ASP B CB  1 
ATOM   7126 C  CG  . ASP B 1 391 ? -40.965  -20.182 283.625 1.00 42.35  ? 391 ASP B CG  1 
ATOM   7127 O  OD1 . ASP B 1 391 ? -40.187  -19.481 284.306 1.00 72.97  ? 391 ASP B OD1 1 
ATOM   7128 O  OD2 . ASP B 1 391 ? -41.367  -19.845 282.492 1.00 41.49  ? 391 ASP B OD2 1 
ATOM   7129 N  N   . LEU B 1 392 ? -41.556  -20.308 287.699 1.00 31.04  ? 392 LEU B N   1 
ATOM   7130 C  CA  . LEU B 1 392 ? -42.159  -19.288 288.543 1.00 29.95  ? 392 LEU B CA  1 
ATOM   7131 C  C   . LEU B 1 392 ? -41.496  -17.944 288.275 1.00 31.55  ? 392 LEU B C   1 
ATOM   7132 O  O   . LEU B 1 392 ? -40.265  -17.847 288.240 1.00 34.05  ? 392 LEU B O   1 
ATOM   7133 C  CB  . LEU B 1 392 ? -42.029  -19.657 290.021 1.00 30.25  ? 392 LEU B CB  1 
ATOM   7134 C  CG  . LEU B 1 392 ? -42.550  -21.030 290.447 1.00 30.95  ? 392 LEU B CG  1 
ATOM   7135 C  CD1 . LEU B 1 392 ? -42.572  -21.142 291.963 1.00 32.71  ? 392 LEU B CD1 1 
ATOM   7136 C  CD2 . LEU B 1 392 ? -43.931  -21.278 289.872 1.00 36.76  ? 392 LEU B CD2 1 
ATOM   7137 N  N   . GLY B 1 393 ? -42.311  -16.916 288.085 1.00 32.82  ? 393 GLY B N   1 
ATOM   7138 C  CA  . GLY B 1 393 ? -41.785  -15.595 287.819 1.00 33.87  ? 393 GLY B CA  1 
ATOM   7139 C  C   . GLY B 1 393 ? -42.883  -14.558 287.868 1.00 34.21  ? 393 GLY B C   1 
ATOM   7140 O  O   . GLY B 1 393 ? -43.986  -14.815 288.352 1.00 39.08  ? 393 GLY B O   1 
ATOM   7141 N  N   . TYR B 1 394 ? -42.565  -13.374 287.352 1.00 33.87  ? 394 TYR B N   1 
ATOM   7142 C  CA  . TYR B 1 394 ? -43.522  -12.277 287.333 1.00 32.56  ? 394 TYR B CA  1 
ATOM   7143 C  C   . TYR B 1 394 ? -44.494  -12.442 286.173 1.00 31.78  ? 394 TYR B C   1 
ATOM   7144 O  O   . TYR B 1 394 ? -44.079  -12.607 285.021 1.00 31.51  ? 394 TYR B O   1 
ATOM   7145 C  CB  . TYR B 1 394 ? -42.800  -10.933 287.228 1.00 30.11  ? 394 TYR B CB  1 
ATOM   7146 C  CG  . TYR B 1 394 ? -41.955  -10.590 288.432 1.00 29.27  ? 394 TYR B CG  1 
ATOM   7147 C  CD1 . TYR B 1 394 ? -42.178  -11.200 289.658 1.00 34.94  ? 394 TYR B CD1 1 
ATOM   7148 C  CD2 . TYR B 1 394 ? -40.941  -9.646  288.346 1.00 28.90  ? 394 TYR B CD2 1 
ATOM   7149 C  CE1 . TYR B 1 394 ? -41.410  -10.887 290.760 1.00 33.50  ? 394 TYR B CE1 1 
ATOM   7150 C  CE2 . TYR B 1 394 ? -40.169  -9.325  289.446 1.00 31.22  ? 394 TYR B CE2 1 
ATOM   7151 C  CZ  . TYR B 1 394 ? -40.408  -9.950  290.650 1.00 29.64  ? 394 TYR B CZ  1 
ATOM   7152 O  OH  . TYR B 1 394 ? -39.644  -9.639  291.752 1.00 26.65  ? 394 TYR B OH  1 
ATOM   7153 N  N   . GLN B 1 395 ? -45.791  -12.401 286.482 1.00 28.80  ? 395 GLN B N   1 
ATOM   7154 C  CA  . GLN B 1 395 ? -46.802  -12.437 285.431 1.00 27.19  ? 395 GLN B CA  1 
ATOM   7155 C  C   . GLN B 1 395 ? -46.691  -11.218 284.526 1.00 30.61  ? 395 GLN B C   1 
ATOM   7156 O  O   . GLN B 1 395 ? -46.810  -11.329 283.300 1.00 29.56  ? 395 GLN B O   1 
ATOM   7157 C  CB  . GLN B 1 395 ? -48.196  -12.521 286.049 1.00 28.76  ? 395 GLN B CB  1 
ATOM   7158 C  CG  . GLN B 1 395 ? -49.299  -11.972 285.164 1.00 28.68  ? 395 GLN B CG  1 
ATOM   7159 C  CD  . GLN B 1 395 ? -50.511  -11.533 285.954 1.00 35.67  ? 395 GLN B CD  1 
ATOM   7160 O  OE1 . GLN B 1 395 ? -50.942  -12.215 286.882 1.00 66.48  ? 395 GLN B OE1 1 
ATOM   7161 N  NE2 . GLN B 1 395 ? -51.067  -10.386 285.592 1.00 31.84  ? 395 GLN B NE2 1 
ATOM   7162 N  N   . THR B 1 396 ? -46.465  -10.045 285.113 1.00 33.86  ? 396 THR B N   1 
ATOM   7163 C  CA  . THR B 1 396 ? -46.264  -8.825  284.348 1.00 27.03  ? 396 THR B CA  1 
ATOM   7164 C  C   . THR B 1 396 ? -45.260  -7.949  285.082 1.00 27.40  ? 396 THR B C   1 
ATOM   7165 O  O   . THR B 1 396 ? -45.302  -7.837  286.311 1.00 25.58  ? 396 THR B O   1 
ATOM   7166 C  CB  . THR B 1 396 ? -47.581  -8.071  284.124 1.00 25.35  ? 396 THR B CB  1 
ATOM   7167 O  OG1 . THR B 1 396 ? -47.321  -6.841  283.436 1.00 26.97  ? 396 THR B OG1 1 
ATOM   7168 C  CG2 . THR B 1 396 ? -48.277  -7.780  285.448 1.00 30.00  ? 396 THR B CG2 1 
ATOM   7169 N  N   . THR B 1 397 ? -44.353  -7.343  284.321 1.00 35.91  ? 397 THR B N   1 
ATOM   7170 C  CA  . THR B 1 397 ? -43.294  -6.527  284.896 1.00 29.09  ? 397 THR B CA  1 
ATOM   7171 C  C   . THR B 1 397 ? -42.700  -5.652  283.805 1.00 26.86  ? 397 THR B C   1 
ATOM   7172 O  O   . THR B 1 397 ? -42.802  -5.958  282.614 1.00 26.43  ? 397 THR B O   1 
ATOM   7173 C  CB  . THR B 1 397 ? -42.202  -7.388  285.537 1.00 27.43  ? 397 THR B CB  1 
ATOM   7174 O  OG1 . THR B 1 397 ? -41.121  -6.549  285.957 1.00 26.61  ? 397 THR B OG1 1 
ATOM   7175 C  CG2 . THR B 1 397 ? -41.684  -8.417  284.545 1.00 27.51  ? 397 THR B CG2 1 
ATOM   7176 N  N   . VAL B 1 398 ? -42.068  -4.560  284.231 1.00 27.93  ? 398 VAL B N   1 
ATOM   7177 C  CA  . VAL B 1 398 ? -41.427  -3.650  283.286 1.00 28.65  ? 398 VAL B CA  1 
ATOM   7178 C  C   . VAL B 1 398 ? -40.038  -4.153  282.915 1.00 29.62  ? 398 VAL B C   1 
ATOM   7179 O  O   . VAL B 1 398 ? -39.736  -4.386  281.739 1.00 27.92  ? 398 VAL B O   1 
ATOM   7180 C  CB  . VAL B 1 398 ? -41.372  -2.224  283.863 1.00 26.39  ? 398 VAL B CB  1 
ATOM   7181 C  CG1 . VAL B 1 398 ? -40.805  -1.261  282.833 1.00 27.32  ? 398 VAL B CG1 1 
ATOM   7182 C  CG2 . VAL B 1 398 ? -42.754  -1.780  284.310 1.00 26.31  ? 398 VAL B CG2 1 
ATOM   7183 N  N   . TYR B 1 399 ? -39.177  -4.326  283.911 1.00 28.83  ? 399 TYR B N   1 
ATOM   7184 C  CA  . TYR B 1 399 ? -37.811  -4.784  283.713 1.00 30.84  ? 399 TYR B CA  1 
ATOM   7185 C  C   . TYR B 1 399 ? -37.674  -6.224  284.195 1.00 33.76  ? 399 TYR B C   1 
ATOM   7186 O  O   . TYR B 1 399 ? -38.646  -6.867  284.602 1.00 32.83  ? 399 TYR B O   1 
ATOM   7187 C  CB  . TYR B 1 399 ? -36.827  -3.866  284.440 1.00 31.40  ? 399 TYR B CB  1 
ATOM   7188 C  CG  . TYR B 1 399 ? -36.929  -2.417  284.029 1.00 28.50  ? 399 TYR B CG  1 
ATOM   7189 C  CD1 . TYR B 1 399 ? -36.396  -1.978  282.826 1.00 27.53  ? 399 TYR B CD1 1 
ATOM   7190 C  CD2 . TYR B 1 399 ? -37.561  -1.489  284.844 1.00 34.21  ? 399 TYR B CD2 1 
ATOM   7191 C  CE1 . TYR B 1 399 ? -36.489  -0.654  282.449 1.00 28.52  ? 399 TYR B CE1 1 
ATOM   7192 C  CE2 . TYR B 1 399 ? -37.658  -0.163  284.473 1.00 30.22  ? 399 TYR B CE2 1 
ATOM   7193 C  CZ  . TYR B 1 399 ? -37.121  0.249   283.274 1.00 31.26  ? 399 TYR B CZ  1 
ATOM   7194 O  OH  . TYR B 1 399 ? -37.215  1.569   282.899 1.00 52.30  ? 399 TYR B OH  1 
ATOM   7195 N  N   . ALA B 1 400 ? -36.446  -6.730  284.145 1.00 42.72  ? 400 ALA B N   1 
ATOM   7196 C  CA  . ALA B 1 400 ? -36.184  -8.092  284.578 1.00 34.82  ? 400 ALA B CA  1 
ATOM   7197 C  C   . ALA B 1 400 ? -36.109  -8.165  286.102 1.00 31.16  ? 400 ALA B C   1 
ATOM   7198 O  O   . ALA B 1 400 ? -35.642  -7.226  286.751 1.00 40.67  ? 400 ALA B O   1 
ATOM   7199 C  CB  . ALA B 1 400 ? -34.884  -8.601  283.969 1.00 44.63  ? 400 ALA B CB  1 
ATOM   7200 N  N   . PRO B 1 401 ? -36.565  -9.271  286.692 1.00 29.31  ? 401 PRO B N   1 
ATOM   7201 C  CA  . PRO B 1 401 ? -36.624  -9.371  288.157 1.00 30.11  ? 401 PRO B CA  1 
ATOM   7202 C  C   . PRO B 1 401 ? -35.256  -9.219  288.807 1.00 35.75  ? 401 PRO B C   1 
ATOM   7203 O  O   . PRO B 1 401 ? -34.205  -9.286  288.166 1.00 36.98  ? 401 PRO B O   1 
ATOM   7204 C  CB  . PRO B 1 401 ? -37.196  -10.773 288.393 1.00 31.20  ? 401 PRO B CB  1 
ATOM   7205 C  CG  . PRO B 1 401 ? -37.957  -11.079 287.152 1.00 31.06  ? 401 PRO B CG  1 
ATOM   7206 C  CD  . PRO B 1 401 ? -37.197  -10.427 286.034 1.00 33.41  ? 401 PRO B CD  1 
ATOM   7207 N  N   . SER B 1 402 ? -35.288  -9.010  290.126 1.00 48.79  ? 402 SER B N   1 
ATOM   7208 C  CA  . SER B 1 402 ? -34.051  -8.879  290.891 1.00 34.60  ? 402 SER B CA  1 
ATOM   7209 C  C   . SER B 1 402 ? -33.306  -10.205 290.970 1.00 37.86  ? 402 SER B C   1 
ATOM   7210 O  O   . SER B 1 402 ? -32.072  -10.237 290.896 1.00 63.81  ? 402 SER B O   1 
ATOM   7211 C  CB  . SER B 1 402 ? -34.360  -8.352  292.292 1.00 36.15  ? 402 SER B CB  1 
ATOM   7212 O  OG  . SER B 1 402 ? -33.387  -8.782  293.228 1.00 34.87  ? 402 SER B OG  1 
ATOM   7213 N  N   . TRP B 1 403 ? -34.036  -11.308 291.120 1.00 33.90  ? 403 TRP B N   1 
ATOM   7214 C  CA  . TRP B 1 403 ? -33.441  -12.635 291.213 1.00 35.22  ? 403 TRP B CA  1 
ATOM   7215 C  C   . TRP B 1 403 ? -33.121  -13.243 289.852 1.00 38.60  ? 403 TRP B C   1 
ATOM   7216 O  O   . TRP B 1 403 ? -32.600  -14.363 289.800 1.00 71.39  ? 403 TRP B O   1 
ATOM   7217 C  CB  . TRP B 1 403 ? -34.375  -13.562 291.996 1.00 46.11  ? 403 TRP B CB  1 
ATOM   7218 C  CG  . TRP B 1 403 ? -35.818  -13.348 291.662 1.00 32.53  ? 403 TRP B CG  1 
ATOM   7219 C  CD1 . TRP B 1 403 ? -36.709  -12.568 292.339 1.00 30.99  ? 403 TRP B CD1 1 
ATOM   7220 C  CD2 . TRP B 1 403 ? -36.538  -13.917 290.563 1.00 30.55  ? 403 TRP B CD2 1 
ATOM   7221 N  NE1 . TRP B 1 403 ? -37.938  -12.615 291.730 1.00 32.28  ? 403 TRP B NE1 1 
ATOM   7222 C  CE2 . TRP B 1 403 ? -37.860  -13.438 290.637 1.00 33.44  ? 403 TRP B CE2 1 
ATOM   7223 C  CE3 . TRP B 1 403 ? -36.193  -14.787 289.525 1.00 31.38  ? 403 TRP B CE3 1 
ATOM   7224 C  CZ2 . TRP B 1 403 ? -38.837  -13.798 289.711 1.00 37.03  ? 403 TRP B CZ2 1 
ATOM   7225 C  CZ3 . TRP B 1 403 ? -37.164  -15.142 288.607 1.00 31.77  ? 403 TRP B CZ3 1 
ATOM   7226 C  CH2 . TRP B 1 403 ? -38.469  -14.650 288.707 1.00 32.48  ? 403 TRP B CH2 1 
ATOM   7227 N  N   . ASN B 1 404 ? -33.415  -12.539 288.759 1.00 35.98  ? 404 ASN B N   1 
ATOM   7228 C  CA  . ASN B 1 404 ? -33.081  -13.017 287.415 1.00 38.62  ? 404 ASN B CA  1 
ATOM   7229 C  C   . ASN B 1 404 ? -33.089  -11.766 286.529 1.00 42.67  ? 404 ASN B C   1 
ATOM   7230 O  O   . ASN B 1 404 ? -34.134  -11.372 286.014 1.00 53.60  ? 404 ASN B O   1 
ATOM   7231 C  CB  . ASN B 1 404 ? -34.063  -14.069 286.929 1.00 40.77  ? 404 ASN B CB  1 
ATOM   7232 C  CG  . ASN B 1 404 ? -33.723  -14.615 285.549 1.00 55.00  ? 404 ASN B CG  1 
ATOM   7233 O  OD1 . ASN B 1 404 ? -33.004  -13.991 284.769 1.00 65.17  ? 404 ASN B OD1 1 
ATOM   7234 N  ND2 . ASN B 1 404 ? -34.245  -15.798 285.247 1.00 49.84  ? 404 ASN B ND2 1 
ATOM   7235 N  N   . SER B 1 405 ? -31.913  -11.162 286.362 1.00 49.59  ? 405 SER B N   1 
ATOM   7236 C  CA  . SER B 1 405 ? -31.804  -9.795  285.870 1.00 62.61  ? 405 SER B CA  1 
ATOM   7237 C  C   . SER B 1 405 ? -31.747  -9.688  284.348 1.00 55.10  ? 405 SER B C   1 
ATOM   7238 O  O   . SER B 1 405 ? -31.455  -8.604  283.833 1.00 65.15  ? 405 SER B O   1 
ATOM   7239 C  CB  . SER B 1 405 ? -30.577  -9.116  286.481 1.00 69.13  ? 405 SER B CB  1 
ATOM   7240 O  OG  . SER B 1 405 ? -30.220  -7.960  285.745 1.00 80.39  ? 405 SER B OG  1 
ATOM   7241 N  N   . GLU B 1 406 ? -32.027  -10.765 283.621 1.00 52.00  ? 406 GLU B N   1 
ATOM   7242 C  CA  . GLU B 1 406 ? -32.179  -10.704 282.167 1.00 65.34  ? 406 GLU B CA  1 
ATOM   7243 C  C   . GLU B 1 406 ? -33.231  -11.714 281.707 1.00 69.81  ? 406 GLU B C   1 
ATOM   7244 O  O   . GLU B 1 406 ? -32.983  -12.595 280.886 1.00 58.95  ? 406 GLU B O   1 
ATOM   7245 C  CB  . GLU B 1 406 ? -30.845  -10.914 281.452 1.00 68.53  ? 406 GLU B CB  1 
ATOM   7246 C  CG  . GLU B 1 406 ? -29.966  -9.662  281.333 1.00 62.41  ? 406 GLU B CG  1 
ATOM   7247 C  CD  . GLU B 1 406 ? -30.751  -8.420  280.921 1.00 59.58  ? 406 GLU B CD  1 
ATOM   7248 O  OE1 . GLU B 1 406 ? -31.602  -8.518  280.013 1.00 60.43  ? 406 GLU B OE1 1 
ATOM   7249 O  OE2 . GLU B 1 406 ? -30.516  -7.341  281.508 1.00 62.83  ? 406 GLU B OE2 1 
ATOM   7250 N  N   . GLU B 1 407 ? -34.442  -11.579 282.240 1.00 52.01  ? 407 GLU B N   1 
ATOM   7251 C  CA  . GLU B 1 407 ? -35.593  -12.279 281.692 1.00 44.79  ? 407 GLU B CA  1 
ATOM   7252 C  C   . GLU B 1 407 ? -36.072  -11.548 280.445 1.00 45.45  ? 407 GLU B C   1 
ATOM   7253 O  O   . GLU B 1 407 ? -36.330  -10.341 280.484 1.00 71.41  ? 407 GLU B O   1 
ATOM   7254 C  CB  . GLU B 1 407 ? -36.713  -12.360 282.728 1.00 43.49  ? 407 GLU B CB  1 
ATOM   7255 C  CG  . GLU B 1 407 ? -38.025  -12.899 282.184 1.00 41.13  ? 407 GLU B CG  1 
ATOM   7256 C  CD  . GLU B 1 407 ? -37.949  -14.367 281.816 1.00 39.84  ? 407 GLU B CD  1 
ATOM   7257 O  OE1 . GLU B 1 407 ? -37.645  -15.190 282.705 1.00 48.52  ? 407 GLU B OE1 1 
ATOM   7258 O  OE2 . GLU B 1 407 ? -38.189  -14.695 280.636 1.00 39.90  ? 407 GLU B OE2 1 
ATOM   7259 N  N   . LEU B 1 408 ? -36.175  -12.272 279.332 1.00 41.20  ? 408 LEU B N   1 
ATOM   7260 C  CA  . LEU B 1 408 ? -36.577  -11.644 278.081 1.00 38.82  ? 408 LEU B CA  1 
ATOM   7261 C  C   . LEU B 1 408 ? -38.077  -11.404 277.986 1.00 51.47  ? 408 LEU B C   1 
ATOM   7262 O  O   . LEU B 1 408 ? -38.516  -10.714 277.059 1.00 52.13  ? 408 LEU B O   1 
ATOM   7263 C  CB  . LEU B 1 408 ? -36.110  -12.486 276.891 1.00 38.07  ? 408 LEU B CB  1 
ATOM   7264 C  CG  . LEU B 1 408 ? -34.595  -12.629 276.740 1.00 44.62  ? 408 LEU B CG  1 
ATOM   7265 C  CD1 . LEU B 1 408 ? -34.249  -13.814 275.852 1.00 48.80  ? 408 LEU B CD1 1 
ATOM   7266 C  CD2 . LEU B 1 408 ? -33.986  -11.345 276.195 1.00 39.99  ? 408 LEU B CD2 1 
ATOM   7267 N  N   . TYR B 1 409 ? -38.869  -11.946 278.909 1.00 38.71  ? 409 TYR B N   1 
ATOM   7268 C  CA  . TYR B 1 409 ? -40.305  -11.675 278.952 1.00 33.78  ? 409 TYR B CA  1 
ATOM   7269 C  C   . TYR B 1 409 ? -40.586  -10.556 279.954 1.00 37.81  ? 409 TYR B C   1 
ATOM   7270 O  O   . TYR B 1 409 ? -41.089  -10.766 281.059 1.00 39.61  ? 409 TYR B O   1 
ATOM   7271 C  CB  . TYR B 1 409 ? -41.082  -12.942 279.292 1.00 31.87  ? 409 TYR B CB  1 
ATOM   7272 C  CG  . TYR B 1 409 ? -41.515  -13.737 278.082 1.00 32.26  ? 409 TYR B CG  1 
ATOM   7273 C  CD1 . TYR B 1 409 ? -41.002  -13.460 276.823 1.00 34.36  ? 409 TYR B CD1 1 
ATOM   7274 C  CD2 . TYR B 1 409 ? -42.453  -14.754 278.198 1.00 30.53  ? 409 TYR B CD2 1 
ATOM   7275 C  CE1 . TYR B 1 409 ? -41.399  -14.182 275.715 1.00 33.48  ? 409 TYR B CE1 1 
ATOM   7276 C  CE2 . TYR B 1 409 ? -42.857  -15.481 277.096 1.00 33.95  ? 409 TYR B CE2 1 
ATOM   7277 C  CZ  . TYR B 1 409 ? -42.328  -15.190 275.857 1.00 35.67  ? 409 TYR B CZ  1 
ATOM   7278 O  OH  . TYR B 1 409 ? -42.727  -15.911 274.755 1.00 29.99  ? 409 TYR B OH  1 
ATOM   7279 N  N   . THR B 1 410 ? -40.234  -9.341  279.539 1.00 30.98  ? 410 THR B N   1 
ATOM   7280 C  CA  . THR B 1 410 ? -40.503  -8.134  280.305 1.00 27.35  ? 410 THR B CA  1 
ATOM   7281 C  C   . THR B 1 410 ? -41.089  -7.077  279.382 1.00 28.70  ? 410 THR B C   1 
ATOM   7282 O  O   . THR B 1 410 ? -41.007  -7.178  278.155 1.00 29.21  ? 410 THR B O   1 
ATOM   7283 C  CB  . THR B 1 410 ? -39.238  -7.587  280.983 1.00 33.36  ? 410 THR B CB  1 
ATOM   7284 O  OG1 . THR B 1 410 ? -38.296  -7.174  279.984 1.00 33.61  ? 410 THR B OG1 1 
ATOM   7285 C  CG2 . THR B 1 410 ? -38.607  -8.642  281.877 1.00 58.85  ? 410 THR B CG2 1 
ATOM   7286 N  N   . THR B 1 411 ? -41.687  -6.050  279.991 1.00 29.43  ? 411 THR B N   1 
ATOM   7287 C  CA  . THR B 1 411 ? -42.289  -4.982  279.201 1.00 28.37  ? 411 THR B CA  1 
ATOM   7288 C  C   . THR B 1 411 ? -41.224  -4.153  278.494 1.00 26.60  ? 411 THR B C   1 
ATOM   7289 O  O   . THR B 1 411 ? -41.419  -3.736  277.346 1.00 26.58  ? 411 THR B O   1 
ATOM   7290 C  CB  . THR B 1 411 ? -43.158  -4.091  280.087 1.00 27.23  ? 411 THR B CB  1 
ATOM   7291 O  OG1 . THR B 1 411 ? -44.092  -4.903  280.810 1.00 28.63  ? 411 THR B OG1 1 
ATOM   7292 C  CG2 . THR B 1 411 ? -43.924  -3.085  279.243 1.00 29.12  ? 411 THR B CG2 1 
ATOM   7293 N  N   . HIS B 1 412 ? -40.093  -3.907  279.159 1.00 26.63  ? 412 HIS B N   1 
ATOM   7294 C  CA  . HIS B 1 412 ? -39.013  -3.144  278.540 1.00 30.55  ? 412 HIS B CA  1 
ATOM   7295 C  C   . HIS B 1 412 ? -38.544  -3.803  277.250 1.00 30.97  ? 412 HIS B C   1 
ATOM   7296 O  O   . HIS B 1 412 ? -38.516  -3.171  276.188 1.00 32.53  ? 412 HIS B O   1 
ATOM   7297 C  CB  . HIS B 1 412 ? -37.849  -2.985  279.522 1.00 34.34  ? 412 HIS B CB  1 
ATOM   7298 C  CG  . HIS B 1 412 ? -36.684  -2.227  278.962 1.00 38.49  ? 412 HIS B CG  1 
ATOM   7299 N  ND1 . HIS B 1 412 ? -35.876  -2.729  277.964 1.00 40.39  ? 412 HIS B ND1 1 
ATOM   7300 C  CD2 . HIS B 1 412 ? -36.200  -0.995  279.251 1.00 42.38  ? 412 HIS B CD2 1 
ATOM   7301 C  CE1 . HIS B 1 412 ? -34.942  -1.845  277.668 1.00 63.65  ? 412 HIS B CE1 1 
ATOM   7302 N  NE2 . HIS B 1 412 ? -35.115  -0.784  278.435 1.00 79.68  ? 412 HIS B NE2 1 
ATOM   7303 N  N   . TYR B 1 413 ? -38.167  -5.081  277.326 1.00 31.90  ? 413 TYR B N   1 
ATOM   7304 C  CA  . TYR B 1 413 ? -37.684  -5.778  276.139 1.00 29.93  ? 413 TYR B CA  1 
ATOM   7305 C  C   . TYR B 1 413 ? -38.758  -5.835  275.060 1.00 28.02  ? 413 TYR B C   1 
ATOM   7306 O  O   . TYR B 1 413 ? -38.457  -5.715  273.867 1.00 27.87  ? 413 TYR B O   1 
ATOM   7307 C  CB  . TYR B 1 413 ? -37.219  -7.184  276.510 1.00 27.51  ? 413 TYR B CB  1 
ATOM   7308 C  CG  . TYR B 1 413 ? -36.365  -7.837  275.451 1.00 27.10  ? 413 TYR B CG  1 
ATOM   7309 C  CD1 . TYR B 1 413 ? -35.009  -7.558  275.357 1.00 23.33  ? 413 TYR B CD1 1 
ATOM   7310 C  CD2 . TYR B 1 413 ? -36.915  -8.725  274.539 1.00 30.00  ? 413 TYR B CD2 1 
ATOM   7311 C  CE1 . TYR B 1 413 ? -34.223  -8.150  274.389 1.00 22.63  ? 413 TYR B CE1 1 
ATOM   7312 C  CE2 . TYR B 1 413 ? -36.138  -9.322  273.568 1.00 33.52  ? 413 TYR B CE2 1 
ATOM   7313 C  CZ  . TYR B 1 413 ? -34.794  -9.032  273.496 1.00 23.81  ? 413 TYR B CZ  1 
ATOM   7314 O  OH  . TYR B 1 413 ? -34.019  -9.626  272.528 1.00 27.30  ? 413 TYR B OH  1 
ATOM   7315 N  N   . ALA B 1 414 ? -40.018  -6.010  275.462 1.00 28.12  ? 414 ALA B N   1 
ATOM   7316 C  CA  . ALA B 1 414 ? -41.109  -6.032  274.494 1.00 27.82  ? 414 ALA B CA  1 
ATOM   7317 C  C   . ALA B 1 414 ? -41.301  -4.662  273.856 1.00 38.22  ? 414 ALA B C   1 
ATOM   7318 O  O   . ALA B 1 414 ? -41.463  -4.552  272.635 1.00 39.51  ? 414 ALA B O   1 
ATOM   7319 C  CB  . ALA B 1 414 ? -42.396  -6.499  275.169 1.00 30.01  ? 414 ALA B CB  1 
ATOM   7320 N  N   . VAL B 1 415 ? -41.296  -3.604  274.671 1.00 32.34  ? 415 VAL B N   1 
ATOM   7321 C  CA  . VAL B 1 415 ? -41.371  -2.250  274.128 1.00 31.34  ? 415 VAL B CA  1 
ATOM   7322 C  C   . VAL B 1 415 ? -40.160  -1.966  273.252 1.00 30.63  ? 415 VAL B C   1 
ATOM   7323 O  O   . VAL B 1 415 ? -40.287  -1.422  272.148 1.00 32.79  ? 415 VAL B O   1 
ATOM   7324 C  CB  . VAL B 1 415 ? -41.500  -1.222  275.268 1.00 33.83  ? 415 VAL B CB  1 
ATOM   7325 C  CG1 . VAL B 1 415 ? -41.231  0.182   274.753 1.00 33.37  ? 415 VAL B CG1 1 
ATOM   7326 C  CG2 . VAL B 1 415 ? -42.881  -1.299  275.901 1.00 60.81  ? 415 VAL B CG2 1 
ATOM   7327 N  N   . ASP B 1 416 ? -38.970  -2.345  273.721 1.00 33.13  ? 416 ASP B N   1 
ATOM   7328 C  CA  . ASP B 1 416 ? -37.758  -2.096  272.950 1.00 37.59  ? 416 ASP B CA  1 
ATOM   7329 C  C   . ASP B 1 416 ? -37.707  -2.948  271.688 1.00 34.25  ? 416 ASP B C   1 
ATOM   7330 O  O   . ASP B 1 416 ? -37.068  -2.555  270.706 1.00 35.20  ? 416 ASP B O   1 
ATOM   7331 C  CB  . ASP B 1 416 ? -36.525  -2.351  273.815 1.00 33.11  ? 416 ASP B CB  1 
ATOM   7332 C  CG  . ASP B 1 416 ? -35.366  -1.443  273.457 1.00 36.14  ? 416 ASP B CG  1 
ATOM   7333 O  OD1 . ASP B 1 416 ? -35.010  -0.578  274.285 1.00 37.28  ? 416 ASP B OD1 1 
ATOM   7334 O  OD2 . ASP B 1 416 ? -34.811  -1.595  272.349 1.00 59.69  ? 416 ASP B OD2 1 
ATOM   7335 N  N   . ALA B 1 417 ? -38.366  -4.110  271.694 1.00 34.27  ? 417 ALA B N   1 
ATOM   7336 C  CA  . ALA B 1 417 ? -38.386  -4.952  270.501 1.00 30.26  ? 417 ALA B CA  1 
ATOM   7337 C  C   . ALA B 1 417 ? -39.092  -4.253  269.347 1.00 31.71  ? 417 ALA B C   1 
ATOM   7338 O  O   . ALA B 1 417 ? -38.656  -4.346  268.194 1.00 32.87  ? 417 ALA B O   1 
ATOM   7339 C  CB  . ALA B 1 417 ? -39.059  -6.288  270.810 1.00 34.69  ? 417 ALA B CB  1 
ATOM   7340 N  N   . LEU B 1 418 ? -40.187  -3.549  269.639 1.00 33.15  ? 418 LEU B N   1 
ATOM   7341 C  CA  . LEU B 1 418 ? -40.879  -2.797  268.597 1.00 36.36  ? 418 LEU B CA  1 
ATOM   7342 C  C   . LEU B 1 418 ? -40.045  -1.611  268.132 1.00 53.19  ? 418 LEU B C   1 
ATOM   7343 O  O   . LEU B 1 418 ? -40.031  -1.284  266.940 1.00 72.99  ? 418 LEU B O   1 
ATOM   7344 C  CB  . LEU B 1 418 ? -42.240  -2.326  269.107 1.00 33.83  ? 418 LEU B CB  1 
ATOM   7345 C  CG  . LEU B 1 418 ? -43.271  -3.409  269.426 1.00 32.94  ? 418 LEU B CG  1 
ATOM   7346 C  CD1 . LEU B 1 418 ? -44.481  -2.806  270.118 1.00 33.56  ? 418 LEU B CD1 1 
ATOM   7347 C  CD2 . LEU B 1 418 ? -43.685  -4.124  268.157 1.00 34.28  ? 418 LEU B CD2 1 
ATOM   7348 N  N   . LEU B 1 419 ? -39.336  -0.962  269.059 1.00 37.24  ? 419 LEU B N   1 
ATOM   7349 C  CA  . LEU B 1 419 ? -38.563  0.226   268.711 1.00 35.98  ? 419 LEU B CA  1 
ATOM   7350 C  C   . LEU B 1 419 ? -37.421  -0.111  267.761 1.00 41.32  ? 419 LEU B C   1 
ATOM   7351 O  O   . LEU B 1 419 ? -37.080  0.692   266.885 1.00 51.13  ? 419 LEU B O   1 
ATOM   7352 C  CB  . LEU B 1 419 ? -38.024  0.888   269.978 1.00 32.90  ? 419 LEU B CB  1 
ATOM   7353 C  CG  . LEU B 1 419 ? -39.056  1.446   270.958 1.00 34.95  ? 419 LEU B CG  1 
ATOM   7354 C  CD1 . LEU B 1 419 ? -38.366  2.112   272.139 1.00 26.44  ? 419 LEU B CD1 1 
ATOM   7355 C  CD2 . LEU B 1 419 ? -39.995  2.422   270.263 1.00 35.78  ? 419 LEU B CD2 1 
ATOM   7356 N  N   . LYS B 1 420 ? -36.822  -1.295  267.912 1.00 43.08  ? 420 LYS B N   1 
ATOM   7357 C  CA  . LYS B 1 420 ? -35.670  -1.664  267.096 1.00 50.07  ? 420 LYS B CA  1 
ATOM   7358 C  C   . LYS B 1 420 ? -36.009  -1.769  265.616 1.00 59.23  ? 420 LYS B C   1 
ATOM   7359 O  O   . LYS B 1 420 ? -35.096  -1.798  264.784 1.00 99.52  ? 420 LYS B O   1 
ATOM   7360 C  CB  . LYS B 1 420 ? -35.081  -2.990  267.579 1.00 43.46  ? 420 LYS B CB  1 
ATOM   7361 C  CG  . LYS B 1 420 ? -34.411  -2.925  268.939 1.00 41.79  ? 420 LYS B CG  1 
ATOM   7362 C  CD  . LYS B 1 420 ? -32.905  -3.079  268.809 1.00 39.53  ? 420 LYS B CD  1 
ATOM   7363 C  CE  . LYS B 1 420 ? -32.368  -4.093  269.804 1.00 37.69  ? 420 LYS B CE  1 
ATOM   7364 N  NZ  . LYS B 1 420 ? -30.881  -4.096  269.837 1.00 38.19  ? 420 LYS B NZ  1 
ATOM   7365 N  N   . GLN B 1 421 ? -37.291  -1.836  265.268 1.00 47.83  ? 421 GLN B N   1 
ATOM   7366 C  CA  . GLN B 1 421 ? -37.694  -1.939  263.873 1.00 53.84  ? 421 GLN B CA  1 
ATOM   7367 C  C   . GLN B 1 421 ? -37.987  -0.592  263.229 1.00 56.34  ? 421 GLN B C   1 
ATOM   7368 O  O   . GLN B 1 421 ? -37.947  -0.484  261.998 1.00 59.31  ? 421 GLN B O   1 
ATOM   7369 C  CB  . GLN B 1 421 ? -38.937  -2.821  263.747 1.00 55.93  ? 421 GLN B CB  1 
ATOM   7370 C  CG  . GLN B 1 421 ? -39.199  -3.287  262.337 1.00 59.42  ? 421 GLN B CG  1 
ATOM   7371 C  CD  . GLN B 1 421 ? -40.443  -4.125  262.227 1.00 83.31  ? 421 GLN B CD  1 
ATOM   7372 O  OE1 . GLN B 1 421 ? -41.070  -4.462  263.232 1.00 75.92  ? 421 GLN B OE1 1 
ATOM   7373 N  NE2 . GLN B 1 421 ? -40.826  -4.449  260.998 1.00 86.38  ? 421 GLN B NE2 1 
ATOM   7374 N  N   . GLY B 1 422 ? -38.271  0.433   264.025 1.00 51.30  ? 422 GLY B N   1 
ATOM   7375 C  CA  . GLY B 1 422 ? -38.763  1.695   263.513 1.00 55.89  ? 422 GLY B CA  1 
ATOM   7376 C  C   . GLY B 1 422 ? -40.201  1.986   263.876 1.00 48.70  ? 422 GLY B C   1 
ATOM   7377 O  O   . GLY B 1 422 ? -40.747  2.993   263.409 1.00 67.79  ? 422 GLY B O   1 
ATOM   7378 N  N   . VAL B 1 423 ? -40.835  1.130   264.678 1.00 45.11  ? 423 VAL B N   1 
ATOM   7379 C  CA  . VAL B 1 423 ? -42.181  1.405   265.163 1.00 45.64  ? 423 VAL B CA  1 
ATOM   7380 C  C   . VAL B 1 423 ? -42.140  2.660   266.018 1.00 45.66  ? 423 VAL B C   1 
ATOM   7381 O  O   . VAL B 1 423 ? -41.421  2.722   267.023 1.00 44.04  ? 423 VAL B O   1 
ATOM   7382 C  CB  . VAL B 1 423 ? -42.728  0.209   265.948 1.00 43.64  ? 423 VAL B CB  1 
ATOM   7383 C  CG1 . VAL B 1 423 ? -44.075  0.550   266.567 1.00 45.85  ? 423 VAL B CG1 1 
ATOM   7384 C  CG2 . VAL B 1 423 ? -42.840  -1.012  265.048 1.00 62.52  ? 423 VAL B CG2 1 
ATOM   7385 N  N   . ASP B 1 424 ? -42.896  3.673   265.613 1.00 46.23  ? 424 ASP B N   1 
ATOM   7386 C  CA  . ASP B 1 424 ? -42.919  4.916   266.364 1.00 46.26  ? 424 ASP B CA  1 
ATOM   7387 C  C   . ASP B 1 424 ? -43.482  4.662   267.760 1.00 42.31  ? 424 ASP B C   1 
ATOM   7388 O  O   . ASP B 1 424 ? -44.416  3.866   267.917 1.00 54.04  ? 424 ASP B O   1 
ATOM   7389 C  CB  . ASP B 1 424 ? -43.763  5.967   265.642 1.00 54.12  ? 424 ASP B CB  1 
ATOM   7390 C  CG  . ASP B 1 424 ? -43.321  6.191   264.211 1.00 72.35  ? 424 ASP B CG  1 
ATOM   7391 O  OD1 . ASP B 1 424 ? -42.188  5.794   263.867 1.00 86.85  ? 424 ASP B OD1 1 
ATOM   7392 O  OD2 . ASP B 1 424 ? -44.110  6.762   263.429 1.00 56.89  ? 424 ASP B OD2 1 
ATOM   7393 N  N   . PRO B 1 425 ? -42.939  5.308   268.796 1.00 36.79  ? 425 PRO B N   1 
ATOM   7394 C  CA  . PRO B 1 425 ? -43.487  5.132   270.149 1.00 37.15  ? 425 PRO B CA  1 
ATOM   7395 C  C   . PRO B 1 425 ? -44.887  5.699   270.321 1.00 43.16  ? 425 PRO B C   1 
ATOM   7396 O  O   . PRO B 1 425 ? -45.453  5.582   271.413 1.00 37.81  ? 425 PRO B O   1 
ATOM   7397 C  CB  . PRO B 1 425 ? -42.477  5.876   271.040 1.00 35.39  ? 425 PRO B CB  1 
ATOM   7398 C  CG  . PRO B 1 425 ? -41.276  6.131   270.172 1.00 36.41  ? 425 PRO B CG  1 
ATOM   7399 C  CD  . PRO B 1 425 ? -41.787  6.223   268.777 1.00 38.73  ? 425 PRO B CD  1 
ATOM   7400 N  N   . ASN B 1 426 ? -45.459  6.307   269.280 1.00 52.64  ? 426 ASN B N   1 
ATOM   7401 C  CA  . ASN B 1 426 ? -46.806  6.857   269.380 1.00 42.25  ? 426 ASN B CA  1 
ATOM   7402 C  C   . ASN B 1 426 ? -47.848  5.757   269.539 1.00 39.83  ? 426 ASN B C   1 
ATOM   7403 O  O   . ASN B 1 426 ? -48.836  5.929   270.261 1.00 59.80  ? 426 ASN B O   1 
ATOM   7404 C  CB  . ASN B 1 426 ? -47.109  7.700   268.142 1.00 47.76  ? 426 ASN B CB  1 
ATOM   7405 C  CG  . ASN B 1 426 ? -47.021  6.895   266.856 1.00 75.43  ? 426 ASN B CG  1 
ATOM   7406 O  OD1 . ASN B 1 426 ? -46.586  5.744   266.861 1.00 74.39  ? 426 ASN B OD1 1 
ATOM   7407 N  ND2 . ASN B 1 426 ? -47.437  7.498   265.748 1.00 59.65  ? 426 ASN B ND2 1 
ATOM   7408 N  N   . LYS B 1 427 ? -47.645  4.621   268.876 1.00 34.76  ? 427 LYS B N   1 
ATOM   7409 C  CA  . LYS B 1 427 ? -48.658  3.580   268.777 1.00 34.94  ? 427 LYS B CA  1 
ATOM   7410 C  C   . LYS B 1 427 ? -48.464  2.450   269.778 1.00 36.15  ? 427 LYS B C   1 
ATOM   7411 O  O   . LYS B 1 427 ? -49.318  1.562   269.858 1.00 37.36  ? 427 LYS B O   1 
ATOM   7412 C  CB  . LYS B 1 427 ? -48.681  3.017   267.352 1.00 34.70  ? 427 LYS B CB  1 
ATOM   7413 C  CG  . LYS B 1 427 ? -49.129  4.033   266.313 1.00 36.27  ? 427 LYS B CG  1 
ATOM   7414 C  CD  . LYS B 1 427 ? -48.907  3.545   264.894 1.00 37.77  ? 427 LYS B CD  1 
ATOM   7415 C  CE  . LYS B 1 427 ? -49.128  4.674   263.899 1.00 32.72  ? 427 LYS B CE  1 
ATOM   7416 N  NZ  . LYS B 1 427 ? -48.879  4.244   262.498 1.00 32.97  ? 427 LYS B NZ  1 
ATOM   7417 N  N   . ILE B 1 428 ? -47.379  2.461   270.545 1.00 40.98  ? 428 ILE B N   1 
ATOM   7418 C  CA  . ILE B 1 428 ? -47.121  1.403   271.517 1.00 32.15  ? 428 ILE B CA  1 
ATOM   7419 C  C   . ILE B 1 428 ? -47.872  1.724   272.803 1.00 31.01  ? 428 ILE B C   1 
ATOM   7420 O  O   . ILE B 1 428 ? -47.613  2.744   273.450 1.00 39.04  ? 428 ILE B O   1 
ATOM   7421 C  CB  . ILE B 1 428 ? -45.617  1.244   271.777 1.00 34.50  ? 428 ILE B CB  1 
ATOM   7422 C  CG1 . ILE B 1 428 ? -44.882  0.962   270.466 1.00 35.48  ? 428 ILE B CG1 1 
ATOM   7423 C  CG2 . ILE B 1 428 ? -45.367  0.130   272.781 1.00 32.65  ? 428 ILE B CG2 1 
ATOM   7424 C  CD1 . ILE B 1 428 ? -43.382  0.869   270.614 1.00 36.33  ? 428 ILE B CD1 1 
ATOM   7425 N  N   . ILE B 1 429 ? -48.804  0.851   273.176 1.00 30.40  ? 429 ILE B N   1 
ATOM   7426 C  CA  . ILE B 1 429 ? -49.627  1.020   274.368 1.00 28.19  ? 429 ILE B CA  1 
ATOM   7427 C  C   . ILE B 1 429 ? -49.273  -0.095  275.343 1.00 26.58  ? 429 ILE B C   1 
ATOM   7428 O  O   . ILE B 1 429 ? -49.513  -1.276  275.060 1.00 24.42  ? 429 ILE B O   1 
ATOM   7429 C  CB  . ILE B 1 429 ? -51.124  1.002   274.029 1.00 24.06  ? 429 ILE B CB  1 
ATOM   7430 C  CG1 . ILE B 1 429 ? -51.424  1.966   272.880 1.00 25.67  ? 429 ILE B CG1 1 
ATOM   7431 C  CG2 . ILE B 1 429 ? -51.948  1.372   275.249 1.00 25.08  ? 429 ILE B CG2 1 
ATOM   7432 C  CD1 . ILE B 1 429 ? -51.108  3.407   273.194 1.00 28.17  ? 429 ILE B CD1 1 
ATOM   7433 N  N   . VAL B 1 430 ? -48.709  0.277   276.487 1.00 25.58  ? 430 VAL B N   1 
ATOM   7434 C  CA  . VAL B 1 430 ? -48.276  -0.699  277.481 1.00 24.33  ? 430 VAL B CA  1 
ATOM   7435 C  C   . VAL B 1 430 ? -49.494  -1.260  278.201 1.00 23.70  ? 430 VAL B C   1 
ATOM   7436 O  O   . VAL B 1 430 ? -50.375  -0.510  278.639 1.00 20.71  ? 430 VAL B O   1 
ATOM   7437 C  CB  . VAL B 1 430 ? -47.287  -0.066  278.471 1.00 24.16  ? 430 VAL B CB  1 
ATOM   7438 C  CG1 . VAL B 1 430 ? -46.997  -1.021  279.619 1.00 25.18  ? 430 VAL B CG1 1 
ATOM   7439 C  CG2 . VAL B 1 430 ? -46.006  0.315   277.756 1.00 43.39  ? 430 VAL B CG2 1 
ATOM   7440 N  N   . GLY B 1 431 ? -49.541  -2.582  278.334 1.00 26.08  ? 431 GLY B N   1 
ATOM   7441 C  CA  . GLY B 1 431 ? -50.665  -3.241  278.968 1.00 24.25  ? 431 GLY B CA  1 
ATOM   7442 C  C   . GLY B 1 431 ? -50.515  -3.310  280.480 1.00 22.39  ? 431 GLY B C   1 
ATOM   7443 O  O   . GLY B 1 431 ? -49.452  -3.640  281.003 1.00 29.29  ? 431 GLY B O   1 
ATOM   7444 N  N   . VAL B 1 432 ? -51.599  -2.983  281.172 1.00 21.41  ? 432 VAL B N   1 
ATOM   7445 C  CA  . VAL B 1 432 ? -51.681  -3.090  282.623 1.00 21.73  ? 432 VAL B CA  1 
ATOM   7446 C  C   . VAL B 1 432 ? -52.619  -4.240  282.955 1.00 18.97  ? 432 VAL B C   1 
ATOM   7447 O  O   . VAL B 1 432 ? -53.744  -4.303  282.441 1.00 20.77  ? 432 VAL B O   1 
ATOM   7448 C  CB  . VAL B 1 432 ? -52.164  -1.775  283.258 1.00 25.24  ? 432 VAL B CB  1 
ATOM   7449 C  CG1 . VAL B 1 432 ? -52.259  -1.917  284.769 1.00 26.93  ? 432 VAL B CG1 1 
ATOM   7450 C  CG2 . VAL B 1 432 ? -51.229  -0.636  282.879 1.00 29.59  ? 432 VAL B CG2 1 
ATOM   7451 N  N   . ALA B 1 433 ? -52.153  -5.153  283.803 1.00 22.04  ? 433 ALA B N   1 
ATOM   7452 C  CA  . ALA B 1 433 ? -52.927  -6.319  284.214 1.00 25.55  ? 433 ALA B CA  1 
ATOM   7453 C  C   . ALA B 1 433 ? -53.687  -5.999  285.496 1.00 25.92  ? 433 ALA B C   1 
ATOM   7454 O  O   . ALA B 1 433 ? -53.084  -5.828  286.561 1.00 51.96  ? 433 ALA B O   1 
ATOM   7455 C  CB  . ALA B 1 433 ? -52.017  -7.528  284.408 1.00 24.51  ? 433 ALA B CB  1 
ATOM   7456 N  N   . MET B 1 434 ? -55.016  -5.929  285.388 1.00 22.74  ? 434 MET B N   1 
ATOM   7457 C  CA  . MET B 1 434 ? -55.900  -5.722  286.528 1.00 22.78  ? 434 MET B CA  1 
ATOM   7458 C  C   . MET B 1 434 ? -56.220  -7.014  287.273 1.00 29.06  ? 434 MET B C   1 
ATOM   7459 O  O   . MET B 1 434 ? -57.304  -7.137  287.862 1.00 38.91  ? 434 MET B O   1 
ATOM   7460 C  CB  . MET B 1 434 ? -57.184  -5.027  286.073 1.00 22.65  ? 434 MET B CB  1 
ATOM   7461 C  CG  . MET B 1 434 ? -56.973  -3.563  285.692 1.00 28.98  ? 434 MET B CG  1 
ATOM   7462 S  SD  . MET B 1 434 ? -58.493  -2.722  285.215 1.00 9.33   ? 434 MET B SD  1 
ATOM   7463 C  CE  . MET B 1 434 ? -57.941  -1.022  285.247 1.00 16.63  ? 434 MET B CE  1 
ATOM   7464 N  N   . TYR B 1 435 ? -55.295  -7.973  287.278 1.00 26.18  ? 435 TYR B N   1 
ATOM   7465 C  CA  . TYR B 1 435 ? -55.498  -9.259  287.930 1.00 23.95  ? 435 TYR B CA  1 
ATOM   7466 C  C   . TYR B 1 435 ? -54.140  -9.823  288.336 1.00 26.34  ? 435 TYR B C   1 
ATOM   7467 O  O   . TYR B 1 435 ? -53.089  -9.256  288.025 1.00 33.86  ? 435 TYR B O   1 
ATOM   7468 C  CB  . TYR B 1 435 ? -56.254  -10.225 287.010 1.00 22.26  ? 435 TYR B CB  1 
ATOM   7469 C  CG  . TYR B 1 435 ? -55.549  -10.479 285.694 1.00 23.65  ? 435 TYR B CG  1 
ATOM   7470 C  CD1 . TYR B 1 435 ? -55.760  -9.649  284.603 1.00 20.38  ? 435 TYR B CD1 1 
ATOM   7471 C  CD2 . TYR B 1 435 ? -54.671  -11.546 285.544 1.00 27.46  ? 435 TYR B CD2 1 
ATOM   7472 C  CE1 . TYR B 1 435 ? -55.117  -9.868  283.402 1.00 20.21  ? 435 TYR B CE1 1 
ATOM   7473 C  CE2 . TYR B 1 435 ? -54.020  -11.774 284.340 1.00 28.74  ? 435 TYR B CE2 1 
ATOM   7474 C  CZ  . TYR B 1 435 ? -54.250  -10.930 283.273 1.00 25.30  ? 435 TYR B CZ  1 
ATOM   7475 O  OH  . TYR B 1 435 ? -53.608  -11.152 282.077 1.00 24.23  ? 435 TYR B OH  1 
ATOM   7476 N  N   . GLY B 1 436 ? -54.167  -10.958 289.027 1.00 25.46  ? 436 GLY B N   1 
ATOM   7477 C  CA  . GLY B 1 436 ? -52.934  -11.594 289.440 1.00 24.21  ? 436 GLY B CA  1 
ATOM   7478 C  C   . GLY B 1 436 ? -52.946  -13.100 289.289 1.00 26.76  ? 436 GLY B C   1 
ATOM   7479 O  O   . GLY B 1 436 ? -53.875  -13.767 289.751 1.00 36.52  ? 436 GLY B O   1 
ATOM   7480 N  N   . ARG B 1 437 ? -51.928  -13.649 288.630 1.00 28.31  ? 437 ARG B N   1 
ATOM   7481 C  CA  . ARG B 1 437 ? -51.777  -15.091 288.505 1.00 29.79  ? 437 ARG B CA  1 
ATOM   7482 C  C   . ARG B 1 437 ? -50.887  -15.601 289.628 1.00 31.47  ? 437 ARG B C   1 
ATOM   7483 O  O   . ARG B 1 437 ? -49.951  -14.917 290.051 1.00 28.20  ? 437 ARG B O   1 
ATOM   7484 C  CB  . ARG B 1 437 ? -51.183  -15.458 287.144 1.00 27.49  ? 437 ARG B CB  1 
ATOM   7485 C  CG  . ARG B 1 437 ? -52.110  -15.158 285.978 1.00 39.19  ? 437 ARG B CG  1 
ATOM   7486 C  CD  . ARG B 1 437 ? -51.491  -15.572 284.656 1.00 43.68  ? 437 ARG B CD  1 
ATOM   7487 N  NE  . ARG B 1 437 ? -52.483  -15.620 283.587 1.00 28.82  ? 437 ARG B NE  1 
ATOM   7488 C  CZ  . ARG B 1 437 ? -53.255  -16.673 283.341 1.00 29.62  ? 437 ARG B CZ  1 
ATOM   7489 N  NH1 . ARG B 1 437 ? -53.146  -17.762 284.087 1.00 34.46  ? 437 ARG B NH1 1 
ATOM   7490 N  NH2 . ARG B 1 437 ? -54.134  -16.637 282.350 1.00 33.24  ? 437 ARG B NH2 1 
ATOM   7491 N  N   . GLY B 1 438 ? -51.187  -16.802 290.120 1.00 32.21  ? 438 GLY B N   1 
ATOM   7492 C  CA  . GLY B 1 438 ? -50.479  -17.296 291.282 1.00 25.03  ? 438 GLY B CA  1 
ATOM   7493 C  C   . GLY B 1 438 ? -50.427  -18.805 291.362 1.00 27.85  ? 438 GLY B C   1 
ATOM   7494 O  O   . GLY B 1 438 ? -51.080  -19.524 290.601 1.00 30.64  ? 438 GLY B O   1 
ATOM   7495 N  N   . TRP B 1 439 ? -49.627  -19.272 292.316 1.00 29.72  ? 439 TRP B N   1 
ATOM   7496 C  CA  . TRP B 1 439 ? -49.454  -20.685 292.607 1.00 26.31  ? 439 TRP B CA  1 
ATOM   7497 C  C   . TRP B 1 439 ? -49.711  -20.913 294.090 1.00 29.72  ? 439 TRP B C   1 
ATOM   7498 O  O   . TRP B 1 439 ? -49.589  -19.998 294.908 1.00 31.93  ? 439 TRP B O   1 
ATOM   7499 C  CB  . TRP B 1 439 ? -48.044  -21.167 292.237 1.00 25.39  ? 439 TRP B CB  1 
ATOM   7500 C  CG  . TRP B 1 439 ? -47.610  -20.774 290.856 1.00 25.04  ? 439 TRP B CG  1 
ATOM   7501 C  CD1 . TRP B 1 439 ? -47.643  -21.550 289.735 1.00 28.86  ? 439 TRP B CD1 1 
ATOM   7502 C  CD2 . TRP B 1 439 ? -47.083  -19.504 290.450 1.00 24.05  ? 439 TRP B CD2 1 
ATOM   7503 N  NE1 . TRP B 1 439 ? -47.165  -20.845 288.657 1.00 27.92  ? 439 TRP B NE1 1 
ATOM   7504 C  CE2 . TRP B 1 439 ? -46.817  -19.586 289.069 1.00 26.86  ? 439 TRP B CE2 1 
ATOM   7505 C  CE3 . TRP B 1 439 ? -46.809  -18.308 291.119 1.00 24.50  ? 439 TRP B CE3 1 
ATOM   7506 C  CZ2 . TRP B 1 439 ? -46.290  -18.518 288.346 1.00 26.95  ? 439 TRP B CZ2 1 
ATOM   7507 C  CZ3 . TRP B 1 439 ? -46.288  -17.249 290.400 1.00 24.62  ? 439 TRP B CZ3 1 
ATOM   7508 C  CH2 . TRP B 1 439 ? -46.034  -17.361 289.028 1.00 23.86  ? 439 TRP B CH2 1 
ATOM   7509 N  N   . THR B 1 440 ? -50.069  -22.147 294.434 1.00 32.83  ? 440 THR B N   1 
ATOM   7510 C  CA  . THR B 1 440 ? -50.353  -22.511 295.814 1.00 38.04  ? 440 THR B CA  1 
ATOM   7511 C  C   . THR B 1 440 ? -49.334  -23.526 296.311 1.00 49.10  ? 440 THR B C   1 
ATOM   7512 O  O   . THR B 1 440 ? -48.785  -24.314 295.534 1.00 40.55  ? 440 THR B O   1 
ATOM   7513 C  CB  . THR B 1 440 ? -51.771  -23.081 295.968 1.00 38.52  ? 440 THR B CB  1 
ATOM   7514 O  OG1 . THR B 1 440 ? -52.023  -23.370 297.349 1.00 39.14  ? 440 THR B OG1 1 
ATOM   7515 C  CG2 . THR B 1 440 ? -51.932  -24.355 295.155 1.00 52.76  ? 440 THR B CG2 1 
ATOM   7516 N  N   . GLY B 1 441 ? -49.081  -23.491 297.617 1.00 50.31  ? 441 GLY B N   1 
ATOM   7517 C  CA  . GLY B 1 441 ? -48.161  -24.433 298.236 1.00 46.79  ? 441 GLY B CA  1 
ATOM   7518 C  C   . GLY B 1 441 ? -46.763  -24.405 297.660 1.00 41.17  ? 441 GLY B C   1 
ATOM   7519 O  O   . GLY B 1 441 ? -46.141  -25.462 297.495 1.00 42.92  ? 441 GLY B O   1 
ATOM   7520 N  N   . VAL B 1 442 ? -46.254  -23.216 297.345 1.00 39.57  ? 442 VAL B N   1 
ATOM   7521 C  CA  . VAL B 1 442 ? -44.919  -23.093 296.770 1.00 39.93  ? 442 VAL B CA  1 
ATOM   7522 C  C   . VAL B 1 442 ? -43.892  -23.495 297.822 1.00 39.85  ? 442 VAL B C   1 
ATOM   7523 O  O   . VAL B 1 442 ? -43.763  -22.845 298.866 1.00 37.19  ? 442 VAL B O   1 
ATOM   7524 C  CB  . VAL B 1 442 ? -44.669  -21.668 296.261 1.00 35.84  ? 442 VAL B CB  1 
ATOM   7525 C  CG1 . VAL B 1 442 ? -43.236  -21.523 295.780 1.00 42.56  ? 442 VAL B CG1 1 
ATOM   7526 C  CG2 . VAL B 1 442 ? -45.651  -21.324 295.152 1.00 35.53  ? 442 VAL B CG2 1 
ATOM   7527 N  N   . THR B 1 443 ? -43.157  -24.570 297.549 1.00 39.85  ? 443 THR B N   1 
ATOM   7528 C  CA  . THR B 1 443 ? -42.204  -25.137 298.493 1.00 39.11  ? 443 THR B CA  1 
ATOM   7529 C  C   . THR B 1 443 ? -40.846  -25.291 297.817 1.00 39.66  ? 443 THR B C   1 
ATOM   7530 O  O   . THR B 1 443 ? -40.680  -24.996 296.629 1.00 39.57  ? 443 THR B O   1 
ATOM   7531 C  CB  . THR B 1 443 ? -42.695  -26.487 299.029 1.00 51.81  ? 443 THR B CB  1 
ATOM   7532 O  OG1 . THR B 1 443 ? -41.823  -26.937 300.073 1.00 49.93  ? 443 THR B OG1 1 
ATOM   7533 C  CG2 . THR B 1 443 ? -42.721  -27.525 297.914 1.00 56.80  ? 443 THR B CG2 1 
ATOM   7534 N  N   . ASN B 1 444 ? -39.869  -25.761 298.599 1.00 44.50  ? 444 ASN B N   1 
ATOM   7535 C  CA  . ASN B 1 444 ? -38.517  -26.038 298.122 1.00 40.66  ? 444 ASN B CA  1 
ATOM   7536 C  C   . ASN B 1 444 ? -37.906  -24.794 297.489 1.00 38.55  ? 444 ASN B C   1 
ATOM   7537 O  O   . ASN B 1 444 ? -37.810  -24.702 296.262 1.00 40.19  ? 444 ASN B O   1 
ATOM   7538 C  CB  . ASN B 1 444 ? -38.533  -27.218 297.138 1.00 41.39  ? 444 ASN B CB  1 
ATOM   7539 C  CG  . ASN B 1 444 ? -37.136  -27.655 296.703 1.00 38.51  ? 444 ASN B CG  1 
ATOM   7540 O  OD1 . ASN B 1 444 ? -36.208  -26.852 296.650 1.00 47.55  ? 444 ASN B OD1 1 
ATOM   7541 N  ND2 . ASN B 1 444 ? -36.986  -28.948 296.408 1.00 47.35  ? 444 ASN B ND2 1 
ATOM   7542 N  N   . TYR B 1 445 ? -37.477  -23.840 298.313 1.00 38.09  ? 445 TYR B N   1 
ATOM   7543 C  CA  . TYR B 1 445 ? -36.877  -22.615 297.807 1.00 38.88  ? 445 TYR B CA  1 
ATOM   7544 C  C   . TYR B 1 445 ? -35.859  -22.090 298.807 1.00 40.08  ? 445 TYR B C   1 
ATOM   7545 O  O   . TYR B 1 445 ? -36.070  -22.168 300.020 1.00 42.64  ? 445 TYR B O   1 
ATOM   7546 C  CB  . TYR B 1 445 ? -37.936  -21.539 297.531 1.00 37.95  ? 445 TYR B CB  1 
ATOM   7547 C  CG  . TYR B 1 445 ? -38.851  -21.250 298.701 1.00 37.86  ? 445 TYR B CG  1 
ATOM   7548 C  CD1 . TYR B 1 445 ? -38.537  -20.261 299.625 1.00 39.75  ? 445 TYR B CD1 1 
ATOM   7549 C  CD2 . TYR B 1 445 ? -40.031  -21.959 298.876 1.00 47.39  ? 445 TYR B CD2 1 
ATOM   7550 C  CE1 . TYR B 1 445 ? -39.370  -19.992 300.694 1.00 38.72  ? 445 TYR B CE1 1 
ATOM   7551 C  CE2 . TYR B 1 445 ? -40.871  -21.696 299.942 1.00 62.14  ? 445 TYR B CE2 1 
ATOM   7552 C  CZ  . TYR B 1 445 ? -40.536  -20.712 300.847 1.00 41.46  ? 445 TYR B CZ  1 
ATOM   7553 O  OH  . TYR B 1 445 ? -41.368  -20.448 301.910 1.00 38.79  ? 445 TYR B OH  1 
ATOM   7554 N  N   . THR B 1 446 ? -34.754  -21.562 298.286 1.00 40.60  ? 446 THR B N   1 
ATOM   7555 C  CA  . THR B 1 446 ? -33.789  -20.845 299.103 1.00 41.99  ? 446 THR B CA  1 
ATOM   7556 C  C   . THR B 1 446 ? -34.221  -19.389 299.241 1.00 45.80  ? 446 THR B C   1 
ATOM   7557 O  O   . THR B 1 446 ? -35.279  -18.982 298.751 1.00 54.43  ? 446 THR B O   1 
ATOM   7558 C  CB  . THR B 1 446 ? -32.393  -20.931 298.490 1.00 45.89  ? 446 THR B CB  1 
ATOM   7559 O  OG1 . THR B 1 446 ? -32.379  -20.233 297.238 1.00 41.77  ? 446 THR B OG1 1 
ATOM   7560 C  CG2 . THR B 1 446 ? -31.995  -22.377 298.261 1.00 62.83  ? 446 THR B CG2 1 
ATOM   7561 N  N   . ASN B 1 447 ? -33.392  -18.598 299.917 1.00 49.19  ? 447 ASN B N   1 
ATOM   7562 C  CA  . ASN B 1 447 ? -33.579  -17.144 299.995 1.00 73.34  ? 447 ASN B CA  1 
ATOM   7563 C  C   . ASN B 1 447 ? -34.958  -16.885 300.614 1.00 52.79  ? 447 ASN B C   1 
ATOM   7564 O  O   . ASN B 1 447 ? -35.462  -17.701 301.397 1.00 50.50  ? 447 ASN B O   1 
ATOM   7565 C  CB  . ASN B 1 447 ? -33.358  -16.549 298.603 1.00 77.73  ? 447 ASN B CB  1 
ATOM   7566 C  CG  . ASN B 1 447 ? -33.355  -15.029 298.589 1.00 70.18  ? 447 ASN B CG  1 
ATOM   7567 O  OD1 . ASN B 1 447 ? -33.817  -14.382 299.528 1.00 70.10  ? 447 ASN B OD1 1 
ATOM   7568 N  ND2 . ASN B 1 447 ? -32.849  -14.453 297.504 1.00 58.85  ? 447 ASN B ND2 1 
ATOM   7569 N  N   . ASP B 1 448 ? -35.574  -15.750 300.285 1.00 49.44  ? 448 ASP B N   1 
ATOM   7570 C  CA  . ASP B 1 448 ? -36.991  -15.522 300.537 1.00 48.42  ? 448 ASP B CA  1 
ATOM   7571 C  C   . ASP B 1 448 ? -37.729  -15.159 299.255 1.00 66.28  ? 448 ASP B C   1 
ATOM   7572 O  O   . ASP B 1 448 ? -38.842  -14.629 299.312 1.00 79.92  ? 448 ASP B O   1 
ATOM   7573 C  CB  . ASP B 1 448 ? -37.197  -14.445 301.603 1.00 48.16  ? 448 ASP B CB  1 
ATOM   7574 C  CG  . ASP B 1 448 ? -37.112  -14.999 303.011 1.00 46.84  ? 448 ASP B CG  1 
ATOM   7575 O  OD1 . ASP B 1 448 ? -37.449  -16.187 303.202 1.00 43.87  ? 448 ASP B OD1 1 
ATOM   7576 O  OD2 . ASP B 1 448 ? -36.717  -14.249 303.927 1.00 55.89  ? 448 ASP B OD2 1 
ATOM   7577 N  N   . ASN B 1 449 ? -37.123  -15.423 298.099 1.00 49.39  ? 449 ASN B N   1 
ATOM   7578 C  CA  . ASN B 1 449 ? -37.817  -15.309 296.825 1.00 57.61  ? 449 ASN B CA  1 
ATOM   7579 C  C   . ASN B 1 449 ? -38.468  -16.652 296.512 1.00 45.21  ? 449 ASN B C   1 
ATOM   7580 O  O   . ASN B 1 449 ? -37.795  -17.687 296.462 1.00 44.16  ? 449 ASN B O   1 
ATOM   7581 C  CB  . ASN B 1 449 ? -36.870  -14.856 295.709 1.00 45.06  ? 449 ASN B CB  1 
ATOM   7582 C  CG  . ASN B 1 449 ? -35.865  -15.918 295.310 1.00 44.36  ? 449 ASN B CG  1 
ATOM   7583 O  OD1 . ASN B 1 449 ? -35.344  -16.647 296.151 1.00 47.85  ? 449 ASN B OD1 1 
ATOM   7584 N  ND2 . ASN B 1 449 ? -35.592  -16.012 294.014 1.00 40.47  ? 449 ASN B ND2 1 
ATOM   7585 N  N   . TYR B 1 450 ? -39.783  -16.636 296.345 1.00 43.45  ? 450 TYR B N   1 
ATOM   7586 C  CA  . TYR B 1 450 ? -40.565  -17.849 296.171 1.00 44.11  ? 450 TYR B CA  1 
ATOM   7587 C  C   . TYR B 1 450 ? -40.716  -18.239 294.709 1.00 47.47  ? 450 TYR B C   1 
ATOM   7588 O  O   . TYR B 1 450 ? -41.475  -19.162 294.396 1.00 69.20  ? 450 TYR B O   1 
ATOM   7589 C  CB  . TYR B 1 450 ? -41.926  -17.666 296.840 1.00 65.59  ? 450 TYR B CB  1 
ATOM   7590 C  CG  . TYR B 1 450 ? -41.825  -16.799 298.075 1.00 48.15  ? 450 TYR B CG  1 
ATOM   7591 C  CD1 . TYR B 1 450 ? -41.401  -17.333 299.285 1.00 52.19  ? 450 TYR B CD1 1 
ATOM   7592 C  CD2 . TYR B 1 450 ? -42.118  -15.442 298.025 1.00 47.26  ? 450 TYR B CD2 1 
ATOM   7593 C  CE1 . TYR B 1 450 ? -41.291  -16.545 300.414 1.00 50.43  ? 450 TYR B CE1 1 
ATOM   7594 C  CE2 . TYR B 1 450 ? -42.009  -14.646 299.150 1.00 47.14  ? 450 TYR B CE2 1 
ATOM   7595 C  CZ  . TYR B 1 450 ? -41.599  -15.204 300.342 1.00 50.54  ? 450 TYR B CZ  1 
ATOM   7596 O  OH  . TYR B 1 450 ? -41.489  -14.417 301.465 1.00 44.59  ? 450 TYR B OH  1 
ATOM   7597 N  N   . PHE B 1 451 ? -40.007  -17.557 293.813 1.00 37.40  ? 451 PHE B N   1 
ATOM   7598 C  CA  . PHE B 1 451 ? -39.924  -17.950 292.416 1.00 37.89  ? 451 PHE B CA  1 
ATOM   7599 C  C   . PHE B 1 451 ? -38.799  -18.942 292.158 1.00 41.91  ? 451 PHE B C   1 
ATOM   7600 O  O   . PHE B 1 451 ? -38.772  -19.564 291.090 1.00 39.70  ? 451 PHE B O   1 
ATOM   7601 C  CB  . PHE B 1 451 ? -39.744  -16.710 291.538 1.00 33.56  ? 451 PHE B CB  1 
ATOM   7602 C  CG  . PHE B 1 451 ? -40.758  -15.637 291.803 1.00 35.37  ? 451 PHE B CG  1 
ATOM   7603 C  CD1 . PHE B 1 451 ? -42.019  -15.706 291.237 1.00 35.35  ? 451 PHE B CD1 1 
ATOM   7604 C  CD2 . PHE B 1 451 ? -40.460  -14.571 292.635 1.00 33.21  ? 451 PHE B CD2 1 
ATOM   7605 C  CE1 . PHE B 1 451 ? -42.958  -14.725 291.480 1.00 32.75  ? 451 PHE B CE1 1 
ATOM   7606 C  CE2 . PHE B 1 451 ? -41.397  -13.588 292.885 1.00 35.76  ? 451 PHE B CE2 1 
ATOM   7607 C  CZ  . PHE B 1 451 ? -42.649  -13.666 292.307 1.00 35.32  ? 451 PHE B CZ  1 
ATOM   7608 N  N   . SER B 1 452 ? -37.876  -19.099 293.107 1.00 44.35  ? 452 SER B N   1 
ATOM   7609 C  CA  . SER B 1 452 ? -36.888  -20.166 293.056 1.00 41.16  ? 452 SER B CA  1 
ATOM   7610 C  C   . SER B 1 452 ? -37.475  -21.518 293.429 1.00 39.72  ? 452 SER B C   1 
ATOM   7611 O  O   . SER B 1 452 ? -36.838  -22.546 293.175 1.00 38.43  ? 452 SER B O   1 
ATOM   7612 C  CB  . SER B 1 452 ? -35.719  -19.845 293.992 1.00 41.07  ? 452 SER B CB  1 
ATOM   7613 O  OG  . SER B 1 452 ? -36.176  -19.611 295.315 1.00 40.75  ? 452 SER B OG  1 
ATOM   7614 N  N   . GLY B 1 453 ? -38.665  -21.541 294.017 1.00 39.53  ? 453 GLY B N   1 
ATOM   7615 C  CA  . GLY B 1 453 ? -39.279  -22.762 294.489 1.00 38.34  ? 453 GLY B CA  1 
ATOM   7616 C  C   . GLY B 1 453 ? -40.104  -23.463 293.436 1.00 44.11  ? 453 GLY B C   1 
ATOM   7617 O  O   . GLY B 1 453 ? -39.887  -23.320 292.230 1.00 50.20  ? 453 GLY B O   1 
ATOM   7618 N  N   . THR B 1 454 ? -41.071  -24.242 293.913 1.00 45.30  ? 454 THR B N   1 
ATOM   7619 C  CA  . THR B 1 454 ? -41.964  -24.998 293.049 1.00 43.96  ? 454 THR B CA  1 
ATOM   7620 C  C   . THR B 1 454 ? -43.343  -25.039 293.683 1.00 37.56  ? 454 THR B C   1 
ATOM   7621 O  O   . THR B 1 454 ? -43.486  -25.455 294.836 1.00 37.57  ? 454 THR B O   1 
ATOM   7622 C  CB  . THR B 1 454 ? -41.448  -26.422 292.821 1.00 38.80  ? 454 THR B CB  1 
ATOM   7623 O  OG1 . THR B 1 454 ? -40.105  -26.372 292.325 1.00 38.23  ? 454 THR B OG1 1 
ATOM   7624 C  CG2 . THR B 1 454 ? -42.328  -27.150 291.817 1.00 46.82  ? 454 THR B CG2 1 
ATOM   7625 N  N   . GLY B 1 455 ? -44.351  -24.598 292.934 1.00 37.66  ? 455 GLY B N   1 
ATOM   7626 C  CA  . GLY B 1 455 ? -45.709  -24.677 293.417 1.00 52.04  ? 455 GLY B CA  1 
ATOM   7627 C  C   . GLY B 1 455 ? -46.300  -26.062 293.249 1.00 41.77  ? 455 GLY B C   1 
ATOM   7628 O  O   . GLY B 1 455 ? -45.780  -26.912 292.528 1.00 41.12  ? 455 GLY B O   1 
ATOM   7629 N  N   . ASN B 1 456 ? -47.411  -26.293 293.943 1.00 45.09  ? 456 ASN B N   1 
ATOM   7630 C  CA  . ASN B 1 456 ? -48.107  -27.567 293.832 1.00 51.15  ? 456 ASN B CA  1 
ATOM   7631 C  C   . ASN B 1 456 ? -49.550  -27.327 293.411 1.00 48.99  ? 456 ASN B C   1 
ATOM   7632 O  O   . ASN B 1 456 ? -50.485  -27.688 294.133 1.00 51.18  ? 456 ASN B O   1 
ATOM   7633 C  CB  . ASN B 1 456 ? -48.043  -28.335 295.155 1.00 58.59  ? 456 ASN B CB  1 
ATOM   7634 C  CG  . ASN B 1 456 ? -48.431  -29.796 295.004 1.00 92.14  ? 456 ASN B CG  1 
ATOM   7635 O  OD1 . ASN B 1 456 ? -49.051  -30.190 294.017 1.00 75.54  ? 456 ASN B OD1 1 
ATOM   7636 N  ND2 . ASN B 1 456 ? -48.063  -30.608 295.988 1.00 136.60 ? 456 ASN B ND2 1 
ATOM   7637 N  N   . GLY B 1 457 ? -49.738  -26.712 292.246 1.00 46.61  ? 457 GLY B N   1 
ATOM   7638 C  CA  . GLY B 1 457 ? -51.057  -26.420 291.743 1.00 52.11  ? 457 GLY B CA  1 
ATOM   7639 C  C   . GLY B 1 457 ? -51.331  -24.932 291.671 1.00 40.07  ? 457 GLY B C   1 
ATOM   7640 O  O   . GLY B 1 457 ? -50.571  -24.110 292.191 1.00 41.42  ? 457 GLY B O   1 
ATOM   7641 N  N   . PRO B 1 458 ? -52.426  -24.558 291.017 1.00 37.91  ? 458 PRO B N   1 
ATOM   7642 C  CA  . PRO B 1 458 ? -52.780  -23.141 290.915 1.00 38.08  ? 458 PRO B CA  1 
ATOM   7643 C  C   . PRO B 1 458 ? -53.393  -22.613 292.201 1.00 33.14  ? 458 PRO B C   1 
ATOM   7644 O  O   . PRO B 1 458 ? -54.063  -23.331 292.945 1.00 31.88  ? 458 PRO B O   1 
ATOM   7645 C  CB  . PRO B 1 458 ? -53.802  -23.119 289.772 1.00 34.62  ? 458 PRO B CB  1 
ATOM   7646 C  CG  . PRO B 1 458 ? -54.440  -24.462 289.834 1.00 37.72  ? 458 PRO B CG  1 
ATOM   7647 C  CD  . PRO B 1 458 ? -53.359  -25.419 290.269 1.00 59.80  ? 458 PRO B CD  1 
ATOM   7648 N  N   . VAL B 1 459 ? -53.151  -21.325 292.452 1.00 33.88  ? 459 VAL B N   1 
ATOM   7649 C  CA  . VAL B 1 459 ? -53.729  -20.675 293.620 1.00 33.14  ? 459 VAL B CA  1 
ATOM   7650 C  C   . VAL B 1 459 ? -55.241  -20.582 293.452 1.00 34.82  ? 459 VAL B C   1 
ATOM   7651 O  O   . VAL B 1 459 ? -55.769  -20.566 292.331 1.00 33.93  ? 459 VAL B O   1 
ATOM   7652 C  CB  . VAL B 1 459 ? -53.101  -19.284 293.834 1.00 33.15  ? 459 VAL B CB  1 
ATOM   7653 C  CG1 . VAL B 1 459 ? -53.629  -18.291 292.807 1.00 29.60  ? 459 VAL B CG1 1 
ATOM   7654 C  CG2 . VAL B 1 459 ? -53.346  -18.788 295.254 1.00 32.93  ? 459 VAL B CG2 1 
ATOM   7655 N  N   . SER B 1 460 ? -55.950  -20.541 294.577 1.00 37.54  ? 460 SER B N   1 
ATOM   7656 C  CA  . SER B 1 460 ? -57.402  -20.416 294.550 1.00 42.30  ? 460 SER B CA  1 
ATOM   7657 C  C   . SER B 1 460 ? -57.788  -19.057 293.978 1.00 34.20  ? 460 SER B C   1 
ATOM   7658 O  O   . SER B 1 460 ? -57.501  -18.017 294.580 1.00 36.92  ? 460 SER B O   1 
ATOM   7659 C  CB  . SER B 1 460 ? -57.975  -20.595 295.953 1.00 60.64  ? 460 SER B CB  1 
ATOM   7660 O  OG  . SER B 1 460 ? -57.373  -21.697 296.610 1.00 66.77  ? 460 SER B OG  1 
ATOM   7661 N  N   . GLY B 1 461 ? -58.436  -19.066 292.812 1.00 33.94  ? 461 GLY B N   1 
ATOM   7662 C  CA  . GLY B 1 461 ? -58.800  -17.850 292.123 1.00 33.06  ? 461 GLY B CA  1 
ATOM   7663 C  C   . GLY B 1 461 ? -60.255  -17.460 292.340 1.00 34.72  ? 461 GLY B C   1 
ATOM   7664 O  O   . GLY B 1 461 ? -61.043  -18.165 292.966 1.00 50.23  ? 461 GLY B O   1 
ATOM   7665 N  N   . THR B 1 462 ? -60.601  -16.293 291.797 1.00 33.94  ? 462 THR B N   1 
ATOM   7666 C  CA  . THR B 1 462 ? -61.959  -15.777 291.901 1.00 33.19  ? 462 THR B CA  1 
ATOM   7667 C  C   . THR B 1 462 ? -62.901  -16.582 291.018 1.00 31.44  ? 462 THR B C   1 
ATOM   7668 O  O   . THR B 1 462 ? -63.767  -17.307 291.517 1.00 36.96  ? 462 THR B O   1 
ATOM   7669 C  CB  . THR B 1 462 ? -62.011  -14.300 291.506 1.00 33.45  ? 462 THR B CB  1 
ATOM   7670 O  OG1 . THR B 1 462 ? -60.937  -13.594 292.139 1.00 32.40  ? 462 THR B OG1 1 
ATOM   7671 C  CG2 . THR B 1 462 ? -63.332  -13.686 291.940 1.00 53.16  ? 462 THR B CG2 1 
ATOM   7672 N  N   . TRP B 1 463 ? -62.736  -16.460 289.702 1.00 32.57  ? 463 TRP B N   1 
ATOM   7673 C  CA  . TRP B 1 463 ? -63.573  -17.158 288.736 1.00 34.72  ? 463 TRP B CA  1 
ATOM   7674 C  C   . TRP B 1 463 ? -62.876  -18.375 288.142 1.00 34.61  ? 463 TRP B C   1 
ATOM   7675 O  O   . TRP B 1 463 ? -63.478  -19.447 288.035 1.00 30.17  ? 463 TRP B O   1 
ATOM   7676 C  CB  . TRP B 1 463 ? -63.992  -16.195 287.619 1.00 34.68  ? 463 TRP B CB  1 
ATOM   7677 C  CG  . TRP B 1 463 ? -64.280  -14.814 288.116 1.00 31.45  ? 463 TRP B CG  1 
ATOM   7678 C  CD1 . TRP B 1 463 ? -63.511  -13.702 287.936 1.00 38.05  ? 463 TRP B CD1 1 
ATOM   7679 C  CD2 . TRP B 1 463 ? -65.408  -14.399 288.896 1.00 32.38  ? 463 TRP B CD2 1 
ATOM   7680 N  NE1 . TRP B 1 463 ? -64.094  -12.618 288.545 1.00 32.51  ? 463 TRP B NE1 1 
ATOM   7681 C  CE2 . TRP B 1 463 ? -65.259  -13.020 289.143 1.00 30.64  ? 463 TRP B CE2 1 
ATOM   7682 C  CE3 . TRP B 1 463 ? -66.530  -15.058 289.406 1.00 45.45  ? 463 TRP B CE3 1 
ATOM   7683 C  CZ2 . TRP B 1 463 ? -66.190  -12.288 289.876 1.00 31.49  ? 463 TRP B CZ2 1 
ATOM   7684 C  CZ3 . TRP B 1 463 ? -67.454  -14.330 290.133 1.00 56.91  ? 463 TRP B CZ3 1 
ATOM   7685 C  CH2 . TRP B 1 463 ? -67.278  -12.960 290.362 1.00 34.90  ? 463 TRP B CH2 1 
ATOM   7686 N  N   . GLU B 1 464 ? -61.611  -18.229 287.758 1.00 34.95  ? 464 GLU B N   1 
ATOM   7687 C  CA  . GLU B 1 464 ? -60.818  -19.311 287.195 1.00 33.29  ? 464 GLU B CA  1 
ATOM   7688 C  C   . GLU B 1 464 ? -59.611  -19.566 288.085 1.00 31.78  ? 464 GLU B C   1 
ATOM   7689 O  O   . GLU B 1 464 ? -59.002  -18.624 288.603 1.00 42.14  ? 464 GLU B O   1 
ATOM   7690 C  CB  . GLU B 1 464 ? -60.367  -18.976 285.767 1.00 34.88  ? 464 GLU B CB  1 
ATOM   7691 C  CG  . GLU B 1 464 ? -59.148  -19.749 285.290 1.00 38.82  ? 464 GLU B CG  1 
ATOM   7692 C  CD  . GLU B 1 464 ? -58.807  -19.470 283.840 1.00 48.67  ? 464 GLU B CD  1 
ATOM   7693 O  OE1 . GLU B 1 464 ? -59.720  -19.099 283.072 1.00 46.43  ? 464 GLU B OE1 1 
ATOM   7694 O  OE2 . GLU B 1 464 ? -57.624  -19.621 283.468 1.00 50.26  ? 464 GLU B OE2 1 
ATOM   7695 N  N   . ASP B 1 465 ? -59.276  -20.841 288.270 1.00 34.02  ? 465 ASP B N   1 
ATOM   7696 C  CA  . ASP B 1 465 ? -58.110  -21.198 289.065 1.00 35.09  ? 465 ASP B CA  1 
ATOM   7697 C  C   . ASP B 1 465 ? -56.836  -20.687 288.403 1.00 33.13  ? 465 ASP B C   1 
ATOM   7698 O  O   . ASP B 1 465 ? -56.693  -20.721 287.178 1.00 29.94  ? 465 ASP B O   1 
ATOM   7699 C  CB  . ASP B 1 465 ? -58.036  -22.714 289.251 1.00 35.05  ? 465 ASP B CB  1 
ATOM   7700 C  CG  . ASP B 1 465 ? -58.925  -23.205 290.374 1.00 39.15  ? 465 ASP B CG  1 
ATOM   7701 O  OD1 . ASP B 1 465 ? -59.680  -22.386 290.936 1.00 39.42  ? 465 ASP B OD1 1 
ATOM   7702 O  OD2 . ASP B 1 465 ? -58.867  -24.411 290.695 1.00 45.89  ? 465 ASP B OD2 1 
ATOM   7703 N  N   . GLY B 1 466 ? -55.905  -20.210 289.227 1.00 36.26  ? 466 GLY B N   1 
ATOM   7704 C  CA  . GLY B 1 466 ? -54.665  -19.649 288.741 1.00 45.04  ? 466 GLY B CA  1 
ATOM   7705 C  C   . GLY B 1 466 ? -54.718  -18.174 288.410 1.00 33.38  ? 466 GLY B C   1 
ATOM   7706 O  O   . GLY B 1 466 ? -53.673  -17.591 288.095 1.00 31.64  ? 466 GLY B O   1 
ATOM   7707 N  N   . VAL B 1 467 ? -55.895  -17.554 288.461 1.00 29.35  ? 467 VAL B N   1 
ATOM   7708 C  CA  . VAL B 1 467 ? -56.063  -16.131 288.193 1.00 28.97  ? 467 VAL B CA  1 
ATOM   7709 C  C   . VAL B 1 467 ? -56.938  -15.541 289.289 1.00 28.35  ? 467 VAL B C   1 
ATOM   7710 O  O   . VAL B 1 467 ? -58.013  -16.075 289.585 1.00 29.73  ? 467 VAL B O   1 
ATOM   7711 C  CB  . VAL B 1 467 ? -56.691  -15.872 286.810 1.00 33.11  ? 467 VAL B CB  1 
ATOM   7712 C  CG1 . VAL B 1 467 ? -56.890  -14.379 286.589 1.00 25.93  ? 467 VAL B CG1 1 
ATOM   7713 C  CG2 . VAL B 1 467 ? -55.828  -16.466 285.708 1.00 36.61  ? 467 VAL B CG2 1 
ATOM   7714 N  N   . VAL B 1 468 ? -56.482  -14.443 289.886 1.00 25.24  ? 468 VAL B N   1 
ATOM   7715 C  CA  . VAL B 1 468 ? -57.206  -13.759 290.950 1.00 27.16  ? 468 VAL B CA  1 
ATOM   7716 C  C   . VAL B 1 468 ? -57.416  -12.312 290.532 1.00 26.71  ? 468 VAL B C   1 
ATOM   7717 O  O   . VAL B 1 468 ? -56.471  -11.646 290.092 1.00 24.65  ? 468 VAL B O   1 
ATOM   7718 C  CB  . VAL B 1 468 ? -56.456  -13.835 292.292 1.00 29.31  ? 468 VAL B CB  1 
ATOM   7719 C  CG1 . VAL B 1 468 ? -57.205  -13.060 293.365 1.00 28.92  ? 468 VAL B CG1 1 
ATOM   7720 C  CG2 . VAL B 1 468 ? -56.263  -15.283 292.711 1.00 35.88  ? 468 VAL B CG2 1 
ATOM   7721 N  N   . ASP B 1 469 ? -58.650  -11.831 290.661 1.00 26.89  ? 469 ASP B N   1 
ATOM   7722 C  CA  . ASP B 1 469 ? -58.937  -10.434 290.371 1.00 27.12  ? 469 ASP B CA  1 
ATOM   7723 C  C   . ASP B 1 469 ? -58.168  -9.531  291.328 1.00 26.07  ? 469 ASP B C   1 
ATOM   7724 O  O   . ASP B 1 469 ? -57.948  -9.868  292.494 1.00 28.74  ? 469 ASP B O   1 
ATOM   7725 C  CB  . ASP B 1 469 ? -60.437  -10.157 290.487 1.00 27.65  ? 469 ASP B CB  1 
ATOM   7726 C  CG  . ASP B 1 469 ? -61.246  -10.848 289.408 1.00 35.97  ? 469 ASP B CG  1 
ATOM   7727 O  OD1 . ASP B 1 469 ? -60.885  -10.726 288.219 1.00 45.69  ? 469 ASP B OD1 1 
ATOM   7728 O  OD2 . ASP B 1 469 ? -62.250  -11.507 289.749 1.00 31.92  ? 469 ASP B OD2 1 
ATOM   7729 N  N   . TYR B 1 470 ? -57.752  -8.367  290.820 1.00 24.08  ? 470 TYR B N   1 
ATOM   7730 C  CA  . TYR B 1 470 ? -57.039  -7.415  291.665 1.00 26.84  ? 470 TYR B CA  1 
ATOM   7731 C  C   . TYR B 1 470 ? -57.900  -6.951  292.831 1.00 28.48  ? 470 TYR B C   1 
ATOM   7732 O  O   . TYR B 1 470 ? -57.377  -6.675  293.917 1.00 39.63  ? 470 TYR B O   1 
ATOM   7733 C  CB  . TYR B 1 470 ? -56.580  -6.211  290.842 1.00 30.36  ? 470 TYR B CB  1 
ATOM   7734 C  CG  . TYR B 1 470 ? -56.043  -5.076  291.684 1.00 28.36  ? 470 TYR B CG  1 
ATOM   7735 C  CD1 . TYR B 1 470 ? -54.738  -5.095  292.153 1.00 25.68  ? 470 TYR B CD1 1 
ATOM   7736 C  CD2 . TYR B 1 470 ? -56.844  -3.991  292.019 1.00 28.02  ? 470 TYR B CD2 1 
ATOM   7737 C  CE1 . TYR B 1 470 ? -54.243  -4.066  292.925 1.00 29.00  ? 470 TYR B CE1 1 
ATOM   7738 C  CE2 . TYR B 1 470 ? -56.358  -2.958  292.795 1.00 26.43  ? 470 TYR B CE2 1 
ATOM   7739 C  CZ  . TYR B 1 470 ? -55.056  -3.000  293.245 1.00 29.37  ? 470 TYR B CZ  1 
ATOM   7740 O  OH  . TYR B 1 470 ? -54.562  -1.974  294.016 1.00 38.00  ? 470 TYR B OH  1 
ATOM   7741 N  N   . ARG B 1 471 ? -59.215  -6.856  292.625 1.00 25.51  ? 471 ARG B N   1 
ATOM   7742 C  CA  . ARG B 1 471 ? -60.103  -6.412  293.694 1.00 26.78  ? 471 ARG B CA  1 
ATOM   7743 C  C   . ARG B 1 471 ? -60.050  -7.360  294.885 1.00 31.32  ? 471 ARG B C   1 
ATOM   7744 O  O   . ARG B 1 471 ? -60.069  -6.920  296.040 1.00 40.11  ? 471 ARG B O   1 
ATOM   7745 C  CB  . ARG B 1 471 ? -61.533  -6.286  293.168 1.00 30.15  ? 471 ARG B CB  1 
ATOM   7746 C  CG  . ARG B 1 471 ? -62.570  -6.028  294.249 1.00 27.42  ? 471 ARG B CG  1 
ATOM   7747 C  CD  . ARG B 1 471 ? -63.862  -5.460  293.681 1.00 24.13  ? 471 ARG B CD  1 
ATOM   7748 N  NE  . ARG B 1 471 ? -64.299  -6.161  292.478 1.00 25.14  ? 471 ARG B NE  1 
ATOM   7749 C  CZ  . ARG B 1 471 ? -64.627  -5.558  291.341 1.00 27.50  ? 471 ARG B CZ  1 
ATOM   7750 N  NH1 . ARG B 1 471 ? -64.570  -4.236  291.249 1.00 24.50  ? 471 ARG B NH1 1 
ATOM   7751 N  NH2 . ARG B 1 471 ? -65.015  -6.275  290.295 1.00 38.97  ? 471 ARG B NH2 1 
ATOM   7752 N  N   . GLN B 1 472 ? -59.970  -8.665  294.624 1.00 29.27  ? 472 GLN B N   1 
ATOM   7753 C  CA  . GLN B 1 472 ? -59.922  -9.635  295.711 1.00 32.44  ? 472 GLN B CA  1 
ATOM   7754 C  C   . GLN B 1 472 ? -58.555  -9.670  296.383 1.00 33.27  ? 472 GLN B C   1 
ATOM   7755 O  O   . GLN B 1 472 ? -58.470  -9.936  297.588 1.00 57.73  ? 472 GLN B O   1 
ATOM   7756 C  CB  . GLN B 1 472 ? -60.307  -11.024 295.187 1.00 36.66  ? 472 GLN B CB  1 
ATOM   7757 C  CG  . GLN B 1 472 ? -59.902  -12.182 296.084 1.00 39.38  ? 472 GLN B CG  1 
ATOM   7758 C  CD  . GLN B 1 472 ? -60.107  -13.531 295.425 1.00 52.23  ? 472 GLN B CD  1 
ATOM   7759 O  OE1 . GLN B 1 472 ? -60.324  -13.618 294.218 1.00 52.59  ? 472 GLN B OE1 1 
ATOM   7760 N  NE2 . GLN B 1 472 ? -60.044  -14.594 296.219 1.00 50.94  ? 472 GLN B NE2 1 
ATOM   7761 N  N   . ILE B 1 473 ? -57.484  -9.392  295.633 1.00 28.04  ? 473 ILE B N   1 
ATOM   7762 C  CA  . ILE B 1 473 ? -56.146  -9.361  296.221 1.00 25.17  ? 473 ILE B CA  1 
ATOM   7763 C  C   . ILE B 1 473 ? -56.076  -8.325  297.335 1.00 30.21  ? 473 ILE B C   1 
ATOM   7764 O  O   . ILE B 1 473 ? -55.479  -8.566  298.392 1.00 33.89  ? 473 ILE B O   1 
ATOM   7765 C  CB  . ILE B 1 473 ? -55.089  -9.091  295.134 1.00 21.50  ? 473 ILE B CB  1 
ATOM   7766 C  CG1 . ILE B 1 473 ? -55.045  -10.241 294.129 1.00 24.07  ? 473 ILE B CG1 1 
ATOM   7767 C  CG2 . ILE B 1 473 ? -53.718  -8.883  295.759 1.00 24.07  ? 473 ILE B CG2 1 
ATOM   7768 C  CD1 . ILE B 1 473 ? -53.999  -10.066 293.053 1.00 25.31  ? 473 ILE B CD1 1 
ATOM   7769 N  N   . GLN B 1 474 ? -56.692  -7.159  297.122 1.00 31.13  ? 474 GLN B N   1 
ATOM   7770 C  CA  . GLN B 1 474 ? -56.671  -6.108  298.135 1.00 31.07  ? 474 GLN B CA  1 
ATOM   7771 C  C   . GLN B 1 474 ? -57.399  -6.526  299.405 1.00 34.42  ? 474 GLN B C   1 
ATOM   7772 O  O   . GLN B 1 474 ? -57.077  -6.035  300.493 1.00 37.54  ? 474 GLN B O   1 
ATOM   7773 C  CB  . GLN B 1 474 ? -57.289  -4.829  297.573 1.00 29.78  ? 474 GLN B CB  1 
ATOM   7774 C  CG  . GLN B 1 474 ? -56.564  -4.269  296.366 1.00 36.09  ? 474 GLN B CG  1 
ATOM   7775 C  CD  . GLN B 1 474 ? -55.156  -3.821  296.696 1.00 32.14  ? 474 GLN B CD  1 
ATOM   7776 O  OE1 . GLN B 1 474 ? -54.201  -4.177  296.008 1.00 35.95  ? 474 GLN B OE1 1 
ATOM   7777 N  NE2 . GLN B 1 474 ? -55.021  -3.028  297.752 1.00 42.70  ? 474 GLN B NE2 1 
ATOM   7778 N  N   . LYS B 1 475 ? -58.379  -7.424  299.293 1.00 36.04  ? 475 LYS B N   1 
ATOM   7779 C  CA  . LYS B 1 475 ? -59.158  -7.821  300.463 1.00 42.09  ? 475 LYS B CA  1 
ATOM   7780 C  C   . LYS B 1 475 ? -58.409  -8.836  301.320 1.00 40.97  ? 475 LYS B C   1 
ATOM   7781 O  O   . LYS B 1 475 ? -58.476  -8.779  302.553 1.00 60.09  ? 475 LYS B O   1 
ATOM   7782 C  CB  . LYS B 1 475 ? -60.519  -8.376  300.031 1.00 42.99  ? 475 LYS B CB  1 
ATOM   7783 C  CG  . LYS B 1 475 ? -61.282  -7.522  299.011 1.00 50.16  ? 475 LYS B CG  1 
ATOM   7784 C  CD  . LYS B 1 475 ? -61.075  -6.019  299.222 1.00 80.83  ? 475 LYS B CD  1 
ATOM   7785 C  CE  . LYS B 1 475 ? -62.230  -5.212  298.661 1.00 66.25  ? 475 LYS B CE  1 
ATOM   7786 N  NZ  . LYS B 1 475 ? -62.815  -5.856  297.459 1.00 75.94  ? 475 LYS B NZ  1 
ATOM   7787 N  N   . ASP B 1 476 ? -57.696  -9.769  300.690 1.00 37.99  ? 476 ASP B N   1 
ATOM   7788 C  CA  . ASP B 1 476 ? -56.861  -10.728 301.399 1.00 41.69  ? 476 ASP B CA  1 
ATOM   7789 C  C   . ASP B 1 476 ? -55.447  -10.207 301.630 1.00 36.95  ? 476 ASP B C   1 
ATOM   7790 O  O   . ASP B 1 476 ? -54.543  -11.001 301.911 1.00 43.60  ? 476 ASP B O   1 
ATOM   7791 C  CB  . ASP B 1 476 ? -56.809  -12.052 300.633 1.00 60.71  ? 476 ASP B CB  1 
ATOM   7792 C  CG  . ASP B 1 476 ? -58.185  -12.621 300.354 1.00 47.73  ? 476 ASP B CG  1 
ATOM   7793 O  OD1 . ASP B 1 476 ? -59.128  -12.303 301.108 1.00 45.85  ? 476 ASP B OD1 1 
ATOM   7794 O  OD2 . ASP B 1 476 ? -58.323  -13.392 299.380 1.00 36.01  ? 476 ASP B OD2 1 
ATOM   7795 N  N   . LEU B 1 477 ? -55.243  -8.891  301.528 1.00 35.59  ? 477 LEU B N   1 
ATOM   7796 C  CA  . LEU B 1 477 ? -53.889  -8.345  301.529 1.00 36.15  ? 477 LEU B CA  1 
ATOM   7797 C  C   . LEU B 1 477 ? -53.174  -8.613  302.847 1.00 52.06  ? 477 LEU B C   1 
ATOM   7798 O  O   . LEU B 1 477 ? -51.964  -8.868  302.862 1.00 47.21  ? 477 LEU B O   1 
ATOM   7799 C  CB  . LEU B 1 477 ? -53.930  -6.846  301.237 1.00 35.26  ? 477 LEU B CB  1 
ATOM   7800 C  CG  . LEU B 1 477 ? -52.578  -6.143  301.101 1.00 31.98  ? 477 LEU B CG  1 
ATOM   7801 C  CD1 . LEU B 1 477 ? -51.677  -6.903  300.141 1.00 38.92  ? 477 LEU B CD1 1 
ATOM   7802 C  CD2 . LEU B 1 477 ? -52.765  -4.706  300.641 1.00 30.83  ? 477 LEU B CD2 1 
ATOM   7803 N  N   . ASN B 1 478 ? -53.898  -8.562  303.964 1.00 39.47  ? 478 ASN B N   1 
ATOM   7804 C  CA  . ASN B 1 478 ? -53.281  -8.837  305.255 1.00 42.29  ? 478 ASN B CA  1 
ATOM   7805 C  C   . ASN B 1 478 ? -53.005  -10.325 305.452 1.00 39.40  ? 478 ASN B C   1 
ATOM   7806 O  O   . ASN B 1 478 ? -52.212  -10.685 306.328 1.00 44.16  ? 478 ASN B O   1 
ATOM   7807 C  CB  . ASN B 1 478 ? -54.166  -8.269  306.376 1.00 52.87  ? 478 ASN B CB  1 
ATOM   7808 C  CG  . ASN B 1 478 ? -53.942  -8.942  307.718 1.00 84.03  ? 478 ASN B CG  1 
ATOM   7809 O  OD1 . ASN B 1 478 ? -54.587  -9.938  308.043 1.00 102.55 ? 478 ASN B OD1 1 
ATOM   7810 N  ND2 . ASN B 1 478 ? -53.018  -8.399  308.504 1.00 82.93  ? 478 ASN B ND2 1 
ATOM   7811 N  N   . ASN B 1 479 ? -53.612  -11.193 304.638 1.00 35.67  ? 479 ASN B N   1 
ATOM   7812 C  CA  . ASN B 1 479 ? -53.211  -12.592 304.602 1.00 35.09  ? 479 ASN B CA  1 
ATOM   7813 C  C   . ASN B 1 479 ? -51.884  -12.796 303.886 1.00 33.61  ? 479 ASN B C   1 
ATOM   7814 O  O   . ASN B 1 479 ? -51.266  -13.853 304.047 1.00 45.54  ? 479 ASN B O   1 
ATOM   7815 C  CB  . ASN B 1 479 ? -54.287  -13.447 303.924 1.00 34.74  ? 479 ASN B CB  1 
ATOM   7816 C  CG  . ASN B 1 479 ? -55.617  -13.395 304.645 1.00 35.57  ? 479 ASN B CG  1 
ATOM   7817 O  OD1 . ASN B 1 479 ? -55.671  -13.167 305.853 1.00 40.82  ? 479 ASN B OD1 1 
ATOM   7818 N  ND2 . ASN B 1 479 ? -56.700  -13.606 303.907 1.00 38.50  ? 479 ASN B ND2 1 
ATOM   7819 N  N   . TYR B 1 480 ? -51.435  -11.821 303.103 1.00 33.31  ? 480 TYR B N   1 
ATOM   7820 C  CA  . TYR B 1 480 ? -50.191  -11.915 302.354 1.00 30.55  ? 480 TYR B CA  1 
ATOM   7821 C  C   . TYR B 1 480 ? -49.175  -10.906 302.874 1.00 27.87  ? 480 TYR B C   1 
ATOM   7822 O  O   . TYR B 1 480 ? -49.480  -10.039 303.697 1.00 28.62  ? 480 TYR B O   1 
ATOM   7823 C  CB  . TYR B 1 480 ? -50.427  -11.682 300.857 1.00 30.04  ? 480 TYR B CB  1 
ATOM   7824 C  CG  . TYR B 1 480 ? -51.447  -12.592 300.212 1.00 31.77  ? 480 TYR B CG  1 
ATOM   7825 C  CD1 . TYR B 1 480 ? -51.152  -13.921 299.948 1.00 31.16  ? 480 TYR B CD1 1 
ATOM   7826 C  CD2 . TYR B 1 480 ? -52.693  -12.112 299.837 1.00 33.53  ? 480 TYR B CD2 1 
ATOM   7827 C  CE1 . TYR B 1 480 ? -52.079  -14.754 299.350 1.00 43.60  ? 480 TYR B CE1 1 
ATOM   7828 C  CE2 . TYR B 1 480 ? -53.627  -12.936 299.240 1.00 33.02  ? 480 TYR B CE2 1 
ATOM   7829 C  CZ  . TYR B 1 480 ? -53.315  -14.255 298.998 1.00 37.48  ? 480 TYR B CZ  1 
ATOM   7830 O  OH  . TYR B 1 480 ? -54.244  -15.076 298.401 1.00 38.56  ? 480 TYR B OH  1 
ATOM   7831 N  N   . VAL B 1 481 ? -47.951  -11.033 302.369 1.00 25.39  ? 481 VAL B N   1 
ATOM   7832 C  CA  . VAL B 1 481 ? -46.871  -10.089 302.633 1.00 23.81  ? 481 VAL B CA  1 
ATOM   7833 C  C   . VAL B 1 481 ? -46.484  -9.454  301.306 1.00 24.25  ? 481 VAL B C   1 
ATOM   7834 O  O   . VAL B 1 481 ? -46.044  -10.152 300.384 1.00 24.45  ? 481 VAL B O   1 
ATOM   7835 C  CB  . VAL B 1 481 ? -45.660  -10.767 303.292 1.00 23.16  ? 481 VAL B CB  1 
ATOM   7836 C  CG1 . VAL B 1 481 ? -44.452  -9.844  303.251 1.00 24.40  ? 481 VAL B CG1 1 
ATOM   7837 C  CG2 . VAL B 1 481 ? -45.986  -11.159 304.723 1.00 25.91  ? 481 VAL B CG2 1 
ATOM   7838 N  N   . TYR B 1 482 ? -46.651  -8.140  301.209 1.00 27.67  ? 482 TYR B N   1 
ATOM   7839 C  CA  . TYR B 1 482 ? -46.370  -7.432  299.970 1.00 28.44  ? 482 TYR B CA  1 
ATOM   7840 C  C   . TYR B 1 482 ? -44.868  -7.271  299.772 1.00 29.97  ? 482 TYR B C   1 
ATOM   7841 O  O   . TYR B 1 482 ? -44.100  -7.152  300.731 1.00 28.11  ? 482 TYR B O   1 
ATOM   7842 C  CB  . TYR B 1 482 ? -47.050  -6.062  299.971 1.00 29.17  ? 482 TYR B CB  1 
ATOM   7843 C  CG  . TYR B 1 482 ? -46.813  -5.250  298.717 1.00 28.70  ? 482 TYR B CG  1 
ATOM   7844 C  CD1 . TYR B 1 482 ? -47.549  -5.489  297.564 1.00 28.03  ? 482 TYR B CD1 1 
ATOM   7845 C  CD2 . TYR B 1 482 ? -45.861  -4.240  298.688 1.00 27.96  ? 482 TYR B CD2 1 
ATOM   7846 C  CE1 . TYR B 1 482 ? -47.339  -4.750  296.416 1.00 25.22  ? 482 TYR B CE1 1 
ATOM   7847 C  CE2 . TYR B 1 482 ? -45.644  -3.495  297.544 1.00 25.34  ? 482 TYR B CE2 1 
ATOM   7848 C  CZ  . TYR B 1 482 ? -46.385  -3.754  296.412 1.00 26.68  ? 482 TYR B CZ  1 
ATOM   7849 O  OH  . TYR B 1 482 ? -46.174  -3.015  295.271 1.00 27.47  ? 482 TYR B OH  1 
ATOM   7850 N  N   . THR B 1 483 ? -44.453  -7.275  298.507 1.00 31.91  ? 483 THR B N   1 
ATOM   7851 C  CA  . THR B 1 483 ? -43.052  -7.091  298.152 1.00 31.37  ? 483 THR B CA  1 
ATOM   7852 C  C   . THR B 1 483 ? -42.977  -6.434  296.783 1.00 30.55  ? 483 THR B C   1 
ATOM   7853 O  O   . THR B 1 483 ? -43.552  -6.944  295.818 1.00 28.92  ? 483 THR B O   1 
ATOM   7854 C  CB  . THR B 1 483 ? -42.295  -8.424  298.141 1.00 28.41  ? 483 THR B CB  1 
ATOM   7855 O  OG1 . THR B 1 483 ? -42.421  -9.060  299.418 1.00 27.98  ? 483 THR B OG1 1 
ATOM   7856 C  CG2 . THR B 1 483 ? -40.823  -8.193  297.839 1.00 30.92  ? 483 THR B CG2 1 
ATOM   7857 N  N   . PHE B 1 484 ? -42.272  -5.309  296.706 1.00 29.38  ? 484 PHE B N   1 
ATOM   7858 C  CA  . PHE B 1 484 ? -42.119  -4.557  295.469 1.00 30.08  ? 484 PHE B CA  1 
ATOM   7859 C  C   . PHE B 1 484 ? -40.691  -4.698  294.963 1.00 30.10  ? 484 PHE B C   1 
ATOM   7860 O  O   . PHE B 1 484 ? -39.736  -4.445  295.705 1.00 43.41  ? 484 PHE B O   1 
ATOM   7861 C  CB  . PHE B 1 484 ? -42.464  -3.081  295.677 1.00 27.37  ? 484 PHE B CB  1 
ATOM   7862 C  CG  . PHE B 1 484 ? -42.311  -2.242  294.439 1.00 26.52  ? 484 PHE B CG  1 
ATOM   7863 C  CD1 . PHE B 1 484 ? -43.086  -2.489  293.319 1.00 26.94  ? 484 PHE B CD1 1 
ATOM   7864 C  CD2 . PHE B 1 484 ? -41.395  -1.205  294.398 1.00 25.07  ? 484 PHE B CD2 1 
ATOM   7865 C  CE1 . PHE B 1 484 ? -42.948  -1.719  292.179 1.00 25.99  ? 484 PHE B CE1 1 
ATOM   7866 C  CE2 . PHE B 1 484 ? -41.253  -0.431  293.262 1.00 25.13  ? 484 PHE B CE2 1 
ATOM   7867 C  CZ  . PHE B 1 484 ? -42.030  -0.689  292.151 1.00 23.95  ? 484 PHE B CZ  1 
ATOM   7868 N  N   . ASP B 1 485 ? -40.550  -5.102  293.702 1.00 26.10  ? 485 ASP B N   1 
ATOM   7869 C  CA  . ASP B 1 485 ? -39.242  -5.248  293.067 1.00 24.92  ? 485 ASP B CA  1 
ATOM   7870 C  C   . ASP B 1 485 ? -38.937  -3.946  292.339 1.00 27.06  ? 485 ASP B C   1 
ATOM   7871 O  O   . ASP B 1 485 ? -39.254  -3.779  291.162 1.00 27.67  ? 485 ASP B O   1 
ATOM   7872 C  CB  . ASP B 1 485 ? -39.232  -6.442  292.121 1.00 27.25  ? 485 ASP B CB  1 
ATOM   7873 C  CG  . ASP B 1 485 ? -37.832  -6.828  291.674 1.00 29.70  ? 485 ASP B CG  1 
ATOM   7874 O  OD1 . ASP B 1 485 ? -36.926  -5.971  291.709 1.00 31.09  ? 485 ASP B OD1 1 
ATOM   7875 O  OD2 . ASP B 1 485 ? -37.640  -7.998  291.280 1.00 37.10  ? 485 ASP B OD2 1 
ATOM   7876 N  N   . SER B 1 486 ? -38.302  -3.012  293.051 1.00 33.30  ? 486 SER B N   1 
ATOM   7877 C  CA  . SER B 1 486 ? -37.971  -1.714  292.472 1.00 30.53  ? 486 SER B CA  1 
ATOM   7878 C  C   . SER B 1 486 ? -37.010  -1.819  291.296 1.00 30.84  ? 486 SER B C   1 
ATOM   7879 O  O   . SER B 1 486 ? -36.868  -0.845  290.547 1.00 33.29  ? 486 SER B O   1 
ATOM   7880 C  CB  . SER B 1 486 ? -37.381  -0.799  293.547 1.00 28.92  ? 486 SER B CB  1 
ATOM   7881 O  OG  . SER B 1 486 ? -36.255  -1.396  294.164 1.00 33.80  ? 486 SER B OG  1 
ATOM   7882 N  N   . ALA B 1 487 ? -36.348  -2.963  291.114 1.00 29.61  ? 487 ALA B N   1 
ATOM   7883 C  CA  . ALA B 1 487 ? -35.501  -3.155  289.942 1.00 31.02  ? 487 ALA B CA  1 
ATOM   7884 C  C   . ALA B 1 487 ? -36.336  -3.439  288.702 1.00 34.23  ? 487 ALA B C   1 
ATOM   7885 O  O   . ALA B 1 487 ? -36.149  -2.805  287.657 1.00 30.42  ? 487 ALA B O   1 
ATOM   7886 C  CB  . ALA B 1 487 ? -34.507  -4.290  290.193 1.00 37.47  ? 487 ALA B CB  1 
ATOM   7887 N  N   . ALA B 1 488 ? -37.263  -4.388  288.801 1.00 31.09  ? 488 ALA B N   1 
ATOM   7888 C  CA  . ALA B 1 488 ? -38.148  -4.733  287.700 1.00 29.13  ? 488 ALA B CA  1 
ATOM   7889 C  C   . ALA B 1 488 ? -39.427  -3.909  287.681 1.00 36.46  ? 488 ALA B C   1 
ATOM   7890 O  O   . ALA B 1 488 ? -40.182  -3.994  286.707 1.00 33.24  ? 488 ALA B O   1 
ATOM   7891 C  CB  . ALA B 1 488 ? -38.506  -6.220  287.761 1.00 42.30  ? 488 ALA B CB  1 
ATOM   7892 N  N   . GLN B 1 489 ? -39.676  -3.114  288.722 1.00 34.20  ? 489 GLN B N   1 
ATOM   7893 C  CA  . GLN B 1 489 ? -40.931  -2.384  288.889 1.00 30.12  ? 489 GLN B CA  1 
ATOM   7894 C  C   . GLN B 1 489 ? -42.122  -3.335  288.801 1.00 29.25  ? 489 GLN B C   1 
ATOM   7895 O  O   . GLN B 1 489 ? -43.053  -3.146  288.015 1.00 48.11  ? 489 GLN B O   1 
ATOM   7896 C  CB  . GLN B 1 489 ? -41.050  -1.243  287.876 1.00 33.95  ? 489 GLN B CB  1 
ATOM   7897 C  CG  . GLN B 1 489 ? -39.921  -0.229  287.959 1.00 30.03  ? 489 GLN B CG  1 
ATOM   7898 C  CD  . GLN B 1 489 ? -40.130  0.955   287.037 1.00 35.97  ? 489 GLN B CD  1 
ATOM   7899 O  OE1 . GLN B 1 489 ? -40.261  0.797   285.824 1.00 42.10  ? 489 GLN B OE1 1 
ATOM   7900 N  NE2 . GLN B 1 489 ? -40.163  2.152   287.610 1.00 47.60  ? 489 GLN B NE2 1 
ATOM   7901 N  N   . ALA B 1 490 ? -42.074  -4.382  289.621 1.00 32.10  ? 490 ALA B N   1 
ATOM   7902 C  CA  . ALA B 1 490 ? -43.124  -5.383  289.687 1.00 35.99  ? 490 ALA B CA  1 
ATOM   7903 C  C   . ALA B 1 490 ? -43.477  -5.653  291.142 1.00 28.28  ? 490 ALA B C   1 
ATOM   7904 O  O   . ALA B 1 490 ? -42.690  -5.388  292.054 1.00 24.93  ? 490 ALA B O   1 
ATOM   7905 C  CB  . ALA B 1 490 ? -42.708  -6.688  289.000 1.00 26.62  ? 490 ALA B CB  1 
ATOM   7906 N  N   . SER B 1 491 ? -44.675  -6.192  291.347 1.00 29.59  ? 491 SER B N   1 
ATOM   7907 C  CA  . SER B 1 491 ? -45.189  -6.458  292.680 1.00 28.04  ? 491 SER B CA  1 
ATOM   7908 C  C   . SER B 1 491 ? -45.672  -7.897  292.771 1.00 26.92  ? 491 SER B C   1 
ATOM   7909 O  O   . SER B 1 491 ? -46.114  -8.486  291.781 1.00 24.24  ? 491 SER B O   1 
ATOM   7910 C  CB  . SER B 1 491 ? -46.337  -5.505  293.039 1.00 34.98  ? 491 SER B CB  1 
ATOM   7911 O  OG  . SER B 1 491 ? -45.921  -4.152  292.963 1.00 43.83  ? 491 SER B OG  1 
ATOM   7912 N  N   . TYR B 1 492 ? -45.579  -8.456  293.975 1.00 26.29  ? 492 TYR B N   1 
ATOM   7913 C  CA  . TYR B 1 492 ? -46.122  -9.779  294.244 1.00 25.79  ? 492 TYR B CA  1 
ATOM   7914 C  C   . TYR B 1 492 ? -46.396  -9.895  295.735 1.00 26.24  ? 492 TYR B C   1 
ATOM   7915 O  O   . TYR B 1 492 ? -45.862  -9.134  296.545 1.00 24.37  ? 492 TYR B O   1 
ATOM   7916 C  CB  . TYR B 1 492 ? -45.179  -10.893 293.771 1.00 28.39  ? 492 TYR B CB  1 
ATOM   7917 C  CG  . TYR B 1 492 ? -43.810  -10.896 294.419 1.00 30.69  ? 492 TYR B CG  1 
ATOM   7918 C  CD1 . TYR B 1 492 ? -43.595  -11.526 295.640 1.00 30.31  ? 492 TYR B CD1 1 
ATOM   7919 C  CD2 . TYR B 1 492 ? -42.730  -10.280 293.804 1.00 39.02  ? 492 TYR B CD2 1 
ATOM   7920 C  CE1 . TYR B 1 492 ? -42.346  -11.534 296.230 1.00 31.37  ? 492 TYR B CE1 1 
ATOM   7921 C  CE2 . TYR B 1 492 ? -41.477  -10.284 294.385 1.00 31.94  ? 492 TYR B CE2 1 
ATOM   7922 C  CZ  . TYR B 1 492 ? -41.290  -10.912 295.597 1.00 32.22  ? 492 TYR B CZ  1 
ATOM   7923 O  OH  . TYR B 1 492 ? -40.043  -10.916 296.178 1.00 31.44  ? 492 TYR B OH  1 
ATOM   7924 N  N   . VAL B 1 493 ? -47.240  -10.865 296.083 1.00 27.38  ? 493 VAL B N   1 
ATOM   7925 C  CA  . VAL B 1 493 ? -47.612  -11.128 297.464 1.00 27.36  ? 493 VAL B CA  1 
ATOM   7926 C  C   . VAL B 1 493 ? -47.361  -12.598 297.764 1.00 27.96  ? 493 VAL B C   1 
ATOM   7927 O  O   . VAL B 1 493 ? -47.335  -13.445 296.869 1.00 30.19  ? 493 VAL B O   1 
ATOM   7928 C  CB  . VAL B 1 493 ? -49.083  -10.763 297.751 1.00 26.47  ? 493 VAL B CB  1 
ATOM   7929 C  CG1 . VAL B 1 493 ? -49.268  -9.256  297.740 1.00 40.17  ? 493 VAL B CG1 1 
ATOM   7930 C  CG2 . VAL B 1 493 ? -50.001  -11.426 296.736 1.00 24.60  ? 493 VAL B CG2 1 
ATOM   7931 N  N   . PHE B 1 494 ? -47.174  -12.896 299.048 1.00 28.12  ? 494 PHE B N   1 
ATOM   7932 C  CA  . PHE B 1 494 ? -46.917  -14.264 299.470 1.00 28.61  ? 494 PHE B CA  1 
ATOM   7933 C  C   . PHE B 1 494 ? -47.514  -14.501 300.848 1.00 27.74  ? 494 PHE B C   1 
ATOM   7934 O  O   . PHE B 1 494 ? -47.496  -13.613 301.704 1.00 39.37  ? 494 PHE B O   1 
ATOM   7935 C  CB  . PHE B 1 494 ? -45.419  -14.575 299.490 1.00 31.22  ? 494 PHE B CB  1 
ATOM   7936 C  CG  . PHE B 1 494 ? -45.110  -16.037 299.631 1.00 34.31  ? 494 PHE B CG  1 
ATOM   7937 C  CD1 . PHE B 1 494 ? -45.193  -16.881 298.539 1.00 33.90  ? 494 PHE B CD1 1 
ATOM   7938 C  CD2 . PHE B 1 494 ? -44.744  -16.569 300.856 1.00 36.21  ? 494 PHE B CD2 1 
ATOM   7939 C  CE1 . PHE B 1 494 ? -44.914  -18.228 298.661 1.00 35.44  ? 494 PHE B CE1 1 
ATOM   7940 C  CE2 . PHE B 1 494 ? -44.463  -17.916 300.984 1.00 35.51  ? 494 PHE B CE2 1 
ATOM   7941 C  CZ  . PHE B 1 494 ? -44.548  -18.746 299.886 1.00 39.84  ? 494 PHE B CZ  1 
ATOM   7942 N  N   . ASP B 1 495 ? -48.035  -15.709 301.051 1.00 29.72  ? 495 ASP B N   1 
ATOM   7943 C  CA  . ASP B 1 495 ? -48.606  -16.133 302.325 1.00 31.02  ? 495 ASP B CA  1 
ATOM   7944 C  C   . ASP B 1 495 ? -47.827  -17.349 302.809 1.00 37.55  ? 495 ASP B C   1 
ATOM   7945 O  O   . ASP B 1 495 ? -47.896  -18.419 302.196 1.00 33.69  ? 495 ASP B O   1 
ATOM   7946 C  CB  . ASP B 1 495 ? -50.093  -16.452 302.181 1.00 36.11  ? 495 ASP B CB  1 
ATOM   7947 C  CG  . ASP B 1 495 ? -50.746  -16.806 303.502 1.00 39.58  ? 495 ASP B CG  1 
ATOM   7948 O  OD1 . ASP B 1 495 ? -50.159  -16.499 304.562 1.00 33.49  ? 495 ASP B OD1 1 
ATOM   7949 O  OD2 . ASP B 1 495 ? -51.851  -17.389 303.482 1.00 33.38  ? 495 ASP B OD2 1 
ATOM   7950 N  N   . LYS B 1 496 ? -47.089  -17.183 303.909 1.00 49.10  ? 496 LYS B N   1 
ATOM   7951 C  CA  . LYS B 1 496 ? -46.292  -18.278 304.450 1.00 42.85  ? 496 LYS B CA  1 
ATOM   7952 C  C   . LYS B 1 496 ? -47.151  -19.410 305.001 1.00 37.14  ? 496 LYS B C   1 
ATOM   7953 O  O   . LYS B 1 496 ? -46.644  -20.523 305.177 1.00 37.13  ? 496 LYS B O   1 
ATOM   7954 C  CB  . LYS B 1 496 ? -45.362  -17.759 305.548 1.00 40.90  ? 496 LYS B CB  1 
ATOM   7955 C  CG  . LYS B 1 496 ? -43.901  -18.147 305.376 1.00 52.98  ? 496 LYS B CG  1 
ATOM   7956 C  CD  . LYS B 1 496 ? -43.273  -17.437 304.189 1.00 54.35  ? 496 LYS B CD  1 
ATOM   7957 C  CE  . LYS B 1 496 ? -41.802  -17.791 304.049 1.00 53.95  ? 496 LYS B CE  1 
ATOM   7958 N  NZ  . LYS B 1 496 ? -41.593  -19.256 303.890 1.00 45.27  ? 496 LYS B NZ  1 
ATOM   7959 N  N   . SER B 1 497 ? -48.433  -19.156 305.274 1.00 32.93  ? 497 SER B N   1 
ATOM   7960 C  CA  . SER B 1 497 ? -49.268  -20.178 305.896 1.00 32.81  ? 497 SER B CA  1 
ATOM   7961 C  C   . SER B 1 497 ? -49.618  -21.288 304.913 1.00 31.11  ? 497 SER B C   1 
ATOM   7962 O  O   . SER B 1 497 ? -49.560  -22.473 305.263 1.00 33.62  ? 497 SER B O   1 
ATOM   7963 C  CB  . SER B 1 497 ? -50.537  -19.545 306.466 1.00 39.40  ? 497 SER B CB  1 
ATOM   7964 O  OG  . SER B 1 497 ? -51.384  -19.076 305.433 1.00 57.94  ? 497 SER B OG  1 
ATOM   7965 N  N   . LYS B 1 498 ? -49.984  -20.932 303.679 1.00 31.50  ? 498 LYS B N   1 
ATOM   7966 C  CA  . LYS B 1 498 ? -50.363  -21.925 302.682 1.00 35.50  ? 498 LYS B CA  1 
ATOM   7967 C  C   . LYS B 1 498 ? -49.581  -21.783 301.380 1.00 33.25  ? 498 LYS B C   1 
ATOM   7968 O  O   . LYS B 1 498 ? -49.938  -22.424 300.385 1.00 36.62  ? 498 LYS B O   1 
ATOM   7969 C  CB  . LYS B 1 498 ? -51.869  -21.858 302.399 1.00 54.55  ? 498 LYS B CB  1 
ATOM   7970 C  CG  . LYS B 1 498 ? -52.501  -23.212 302.090 1.00 75.80  ? 498 LYS B CG  1 
ATOM   7971 C  CD  . LYS B 1 498 ? -53.954  -23.072 301.662 1.00 67.18  ? 498 LYS B CD  1 
ATOM   7972 C  CE  . LYS B 1 498 ? -54.554  -24.423 301.303 1.00 50.14  ? 498 LYS B CE  1 
ATOM   7973 N  NZ  . LYS B 1 498 ? -53.623  -25.246 300.481 1.00 47.42  ? 498 LYS B NZ  1 
ATOM   7974 N  N   . GLY B 1 499 ? -48.532  -20.966 301.358 1.00 31.92  ? 499 GLY B N   1 
ATOM   7975 C  CA  . GLY B 1 499 ? -47.672  -20.887 300.186 1.00 34.66  ? 499 GLY B CA  1 
ATOM   7976 C  C   . GLY B 1 499 ? -48.338  -20.332 298.946 1.00 37.58  ? 499 GLY B C   1 
ATOM   7977 O  O   . GLY B 1 499 ? -48.133  -20.860 297.846 1.00 35.06  ? 499 GLY B O   1 
ATOM   7978 N  N   . ASP B 1 500 ? -49.131  -19.275 299.096 1.00 39.32  ? 500 ASP B N   1 
ATOM   7979 C  CA  . ASP B 1 500 ? -49.783  -18.629 297.963 1.00 36.48  ? 500 ASP B CA  1 
ATOM   7980 C  C   . ASP B 1 500 ? -48.904  -17.488 297.464 1.00 29.80  ? 500 ASP B C   1 
ATOM   7981 O  O   . ASP B 1 500 ? -48.691  -16.505 298.180 1.00 29.16  ? 500 ASP B O   1 
ATOM   7982 C  CB  . ASP B 1 500 ? -51.166  -18.110 298.353 1.00 41.06  ? 500 ASP B CB  1 
ATOM   7983 C  CG  . ASP B 1 500 ? -52.147  -19.227 298.646 1.00 59.62  ? 500 ASP B CG  1 
ATOM   7984 O  OD1 . ASP B 1 500 ? -52.010  -20.313 298.044 1.00 52.43  ? 500 ASP B OD1 1 
ATOM   7985 O  OD2 . ASP B 1 500 ? -53.057  -19.018 299.475 1.00 65.03  ? 500 ASP B OD2 1 
ATOM   7986 N  N   . LEU B 1 501 ? -48.398  -17.620 296.240 1.00 27.67  ? 501 LEU B N   1 
ATOM   7987 C  CA  . LEU B 1 501 ? -47.535  -16.619 295.619 1.00 26.94  ? 501 LEU B CA  1 
ATOM   7988 C  C   . LEU B 1 501 ? -48.246  -16.075 294.388 1.00 25.23  ? 501 LEU B C   1 
ATOM   7989 O  O   . LEU B 1 501 ? -48.388  -16.785 293.389 1.00 25.93  ? 501 LEU B O   1 
ATOM   7990 C  CB  . LEU B 1 501 ? -46.182  -17.221 295.243 1.00 29.50  ? 501 LEU B CB  1 
ATOM   7991 C  CG  . LEU B 1 501 ? -45.234  -16.318 294.452 1.00 29.81  ? 501 LEU B CG  1 
ATOM   7992 C  CD1 . LEU B 1 501 ? -44.724  -15.177 295.318 1.00 32.38  ? 501 LEU B CD1 1 
ATOM   7993 C  CD2 . LEU B 1 501 ? -44.080  -17.124 293.881 1.00 33.15  ? 501 LEU B CD2 1 
ATOM   7994 N  N   . ILE B 1 502 ? -48.676  -14.817 294.452 1.00 27.81  ? 502 ILE B N   1 
ATOM   7995 C  CA  . ILE B 1 502 ? -49.435  -14.182 293.380 1.00 30.36  ? 502 ILE B CA  1 
ATOM   7996 C  C   . ILE B 1 502 ? -48.625  -13.018 292.830 1.00 28.14  ? 502 ILE B C   1 
ATOM   7997 O  O   . ILE B 1 502 ? -48.173  -12.155 293.591 1.00 26.59  ? 502 ILE B O   1 
ATOM   7998 C  CB  . ILE B 1 502 ? -50.813  -13.699 293.869 1.00 27.11  ? 502 ILE B CB  1 
ATOM   7999 C  CG1 . ILE B 1 502 ? -51.612  -14.864 294.453 1.00 40.72  ? 502 ILE B CG1 1 
ATOM   8000 C  CG2 . ILE B 1 502 ? -51.580  -13.040 292.733 1.00 29.43  ? 502 ILE B CG2 1 
ATOM   8001 C  CD1 . ILE B 1 502 ? -52.903  -14.442 295.118 1.00 28.81  ? 502 ILE B CD1 1 
ATOM   8002 N  N   . SER B 1 503 ? -48.448  -12.994 291.511 1.00 27.40  ? 503 SER B N   1 
ATOM   8003 C  CA  . SER B 1 503 ? -47.787  -11.894 290.820 1.00 28.05  ? 503 SER B CA  1 
ATOM   8004 C  C   . SER B 1 503 ? -48.849  -11.036 290.143 1.00 28.06  ? 503 SER B C   1 
ATOM   8005 O  O   . SER B 1 503 ? -49.573  -11.519 289.266 1.00 28.83  ? 503 SER B O   1 
ATOM   8006 C  CB  . SER B 1 503 ? -46.783  -12.416 289.793 1.00 31.31  ? 503 SER B CB  1 
ATOM   8007 O  OG  . SER B 1 503 ? -46.366  -11.383 288.918 1.00 37.33  ? 503 SER B OG  1 
ATOM   8008 N  N   . PHE B 1 504 ? -48.937  -9.770  290.544 1.00 30.15  ? 504 PHE B N   1 
ATOM   8009 C  CA  . PHE B 1 504 ? -49.982  -8.878  290.064 1.00 39.70  ? 504 PHE B CA  1 
ATOM   8010 C  C   . PHE B 1 504 ? -49.408  -7.479  289.889 1.00 31.40  ? 504 PHE B C   1 
ATOM   8011 O  O   . PHE B 1 504 ? -48.222  -7.233  290.130 1.00 51.23  ? 504 PHE B O   1 
ATOM   8012 C  CB  . PHE B 1 504 ? -51.175  -8.866  291.027 1.00 34.72  ? 504 PHE B CB  1 
ATOM   8013 C  CG  . PHE B 1 504 ? -50.905  -8.144  292.315 1.00 31.22  ? 504 PHE B CG  1 
ATOM   8014 C  CD1 . PHE B 1 504 ? -50.197  -8.758  293.332 1.00 30.90  ? 504 PHE B CD1 1 
ATOM   8015 C  CD2 . PHE B 1 504 ? -51.372  -6.856  292.514 1.00 29.21  ? 504 PHE B CD2 1 
ATOM   8016 C  CE1 . PHE B 1 504 ? -49.949  -8.098  294.517 1.00 30.53  ? 504 PHE B CE1 1 
ATOM   8017 C  CE2 . PHE B 1 504 ? -51.128  -6.192  293.700 1.00 23.91  ? 504 PHE B CE2 1 
ATOM   8018 C  CZ  . PHE B 1 504 ? -50.416  -6.814  294.702 1.00 27.52  ? 504 PHE B CZ  1 
ATOM   8019 N  N   . ASP B 1 505 ? -50.268  -6.555  289.467 1.00 25.55  ? 505 ASP B N   1 
ATOM   8020 C  CA  . ASP B 1 505 ? -49.912  -5.151  289.293 1.00 26.40  ? 505 ASP B CA  1 
ATOM   8021 C  C   . ASP B 1 505 ? -50.568  -4.343  290.405 1.00 25.61  ? 505 ASP B C   1 
ATOM   8022 O  O   . ASP B 1 505 ? -51.795  -4.199  290.435 1.00 25.23  ? 505 ASP B O   1 
ATOM   8023 C  CB  . ASP B 1 505 ? -50.342  -4.638  287.920 1.00 28.03  ? 505 ASP B CB  1 
ATOM   8024 C  CG  . ASP B 1 505 ? -49.207  -4.635  286.918 1.00 33.76  ? 505 ASP B CG  1 
ATOM   8025 O  OD1 . ASP B 1 505 ? -48.036  -4.555  287.344 1.00 31.18  ? 505 ASP B OD1 1 
ATOM   8026 O  OD2 . ASP B 1 505 ? -49.486  -4.705  285.702 1.00 45.26  ? 505 ASP B OD2 1 
ATOM   8027 N  N   . SER B 1 506 ? -49.753  -3.824  291.318 1.00 25.56  ? 506 SER B N   1 
ATOM   8028 C  CA  . SER B 1 506 ? -50.233  -2.949  292.372 1.00 22.61  ? 506 SER B CA  1 
ATOM   8029 C  C   . SER B 1 506 ? -50.176  -1.499  291.899 1.00 21.47  ? 506 SER B C   1 
ATOM   8030 O  O   . SER B 1 506 ? -49.819  -1.206  290.757 1.00 23.71  ? 506 SER B O   1 
ATOM   8031 C  CB  . SER B 1 506 ? -49.413  -3.145  293.646 1.00 23.92  ? 506 SER B CB  1 
ATOM   8032 O  OG  . SER B 1 506 ? -48.081  -2.700  293.464 1.00 22.41  ? 506 SER B OG  1 
ATOM   8033 N  N   . VAL B 1 507 ? -50.532  -0.573  292.793 1.00 19.88  ? 507 VAL B N   1 
ATOM   8034 C  CA  . VAL B 1 507 ? -50.443  0.846   292.459 1.00 20.48  ? 507 VAL B CA  1 
ATOM   8035 C  C   . VAL B 1 507 ? -49.002  1.226   292.143 1.00 24.32  ? 507 VAL B C   1 
ATOM   8036 O  O   . VAL B 1 507 ? -48.740  2.054   291.261 1.00 25.72  ? 507 VAL B O   1 
ATOM   8037 C  CB  . VAL B 1 507 ? -51.017  1.702   293.603 1.00 21.14  ? 507 VAL B CB  1 
ATOM   8038 C  CG1 . VAL B 1 507 ? -50.988  3.177   293.233 1.00 23.55  ? 507 VAL B CG1 1 
ATOM   8039 C  CG2 . VAL B 1 507 ? -52.432  1.261   293.937 1.00 23.36  ? 507 VAL B CG2 1 
ATOM   8040 N  N   . ASP B 1 508 ? -48.046  0.615   292.845 1.00 27.65  ? 508 ASP B N   1 
ATOM   8041 C  CA  . ASP B 1 508 ? -46.637  0.921   292.616 1.00 25.05  ? 508 ASP B CA  1 
ATOM   8042 C  C   . ASP B 1 508 ? -46.208  0.513   291.213 1.00 24.83  ? 508 ASP B C   1 
ATOM   8043 O  O   . ASP B 1 508 ? -45.635  1.316   290.467 1.00 43.29  ? 508 ASP B O   1 
ATOM   8044 C  CB  . ASP B 1 508 ? -45.775  0.219   293.664 1.00 24.70  ? 508 ASP B CB  1 
ATOM   8045 C  CG  . ASP B 1 508 ? -46.181  0.566   295.078 1.00 26.77  ? 508 ASP B CG  1 
ATOM   8046 O  OD1 . ASP B 1 508 ? -46.580  1.725   295.314 1.00 43.37  ? 508 ASP B OD1 1 
ATOM   8047 O  OD2 . ASP B 1 508 ? -46.105  -0.322  295.953 1.00 26.86  ? 508 ASP B OD2 1 
ATOM   8048 N  N   . SER B 1 509 ? -46.479  -0.738  290.835 1.00 23.10  ? 509 SER B N   1 
ATOM   8049 C  CA  . SER B 1 509 ? -46.035  -1.233  289.537 1.00 27.94  ? 509 SER B CA  1 
ATOM   8050 C  C   . SER B 1 509 ? -46.749  -0.521  288.395 1.00 27.35  ? 509 SER B C   1 
ATOM   8051 O  O   . SER B 1 509 ? -46.153  -0.279  287.340 1.00 25.05  ? 509 SER B O   1 
ATOM   8052 C  CB  . SER B 1 509 ? -46.256  -2.741  289.450 1.00 29.42  ? 509 SER B CB  1 
ATOM   8053 O  OG  . SER B 1 509 ? -47.624  -3.054  289.627 1.00 25.02  ? 509 SER B OG  1 
ATOM   8054 N  N   . VAL B 1 510 ? -48.026  -0.181  288.582 1.00 28.01  ? 510 VAL B N   1 
ATOM   8055 C  CA  . VAL B 1 510 ? -48.741  0.581   287.561 1.00 28.67  ? 510 VAL B CA  1 
ATOM   8056 C  C   . VAL B 1 510 ? -48.106  1.953   287.387 1.00 30.17  ? 510 VAL B C   1 
ATOM   8057 O  O   . VAL B 1 510 ? -47.903  2.423   286.260 1.00 42.61  ? 510 VAL B O   1 
ATOM   8058 C  CB  . VAL B 1 510 ? -50.235  0.691   287.916 1.00 26.95  ? 510 VAL B CB  1 
ATOM   8059 C  CG1 . VAL B 1 510 ? -50.937  1.630   286.951 1.00 27.96  ? 510 VAL B CG1 1 
ATOM   8060 C  CG2 . VAL B 1 510 ? -50.889  -0.679  287.878 1.00 27.72  ? 510 VAL B CG2 1 
ATOM   8061 N  N   . LEU B 1 511 ? -47.775  2.613   288.500 1.00 36.98  ? 511 LEU B N   1 
ATOM   8062 C  CA  . LEU B 1 511 ? -47.123  3.915   288.417 1.00 30.48  ? 511 LEU B CA  1 
ATOM   8063 C  C   . LEU B 1 511 ? -45.781  3.814   287.701 1.00 35.59  ? 511 LEU B C   1 
ATOM   8064 O  O   . LEU B 1 511 ? -45.392  4.726   286.960 1.00 54.96  ? 511 LEU B O   1 
ATOM   8065 C  CB  . LEU B 1 511 ? -46.949  4.500   289.817 1.00 29.14  ? 511 LEU B CB  1 
ATOM   8066 C  CG  . LEU B 1 511 ? -47.263  5.976   289.965 1.00 37.50  ? 511 LEU B CG  1 
ATOM   8067 C  CD1 . LEU B 1 511 ? -48.738  6.215   289.837 1.00 37.37  ? 511 LEU B CD1 1 
ATOM   8068 C  CD2 . LEU B 1 511 ? -46.738  6.520   291.278 1.00 73.47  ? 511 LEU B CD2 1 
ATOM   8069 N  N   . GLY B 1 512 ? -45.063  2.707   287.901 1.00 34.69  ? 512 GLY B N   1 
ATOM   8070 C  CA  . GLY B 1 512 ? -43.839  2.488   287.148 1.00 32.03  ? 512 GLY B CA  1 
ATOM   8071 C  C   . GLY B 1 512 ? -44.090  2.375   285.658 1.00 27.29  ? 512 GLY B C   1 
ATOM   8072 O  O   . GLY B 1 512 ? -43.298  2.858   284.846 1.00 29.07  ? 512 GLY B O   1 
ATOM   8073 N  N   . LYS B 1 513 ? -45.201  1.738   285.277 1.00 24.04  ? 513 LYS B N   1 
ATOM   8074 C  CA  . LYS B 1 513 ? -45.571  1.685   283.868 1.00 26.02  ? 513 LYS B CA  1 
ATOM   8075 C  C   . LYS B 1 513 ? -45.948  3.062   283.341 1.00 28.09  ? 513 LYS B C   1 
ATOM   8076 O  O   . LYS B 1 513 ? -45.740  3.349   282.157 1.00 27.35  ? 513 LYS B O   1 
ATOM   8077 C  CB  . LYS B 1 513 ? -46.726  0.706   283.660 1.00 24.51  ? 513 LYS B CB  1 
ATOM   8078 C  CG  . LYS B 1 513 ? -46.407  -0.731  284.033 1.00 22.80  ? 513 LYS B CG  1 
ATOM   8079 C  CD  . LYS B 1 513 ? -47.545  -1.658  283.640 1.00 23.96  ? 513 LYS B CD  1 
ATOM   8080 C  CE  . LYS B 1 513 ? -47.208  -3.109  283.938 1.00 26.03  ? 513 LYS B CE  1 
ATOM   8081 N  NZ  . LYS B 1 513 ? -48.290  -4.028  283.490 1.00 24.39  ? 513 LYS B NZ  1 
ATOM   8082 N  N   . VAL B 1 514 ? -46.503  3.922   284.198 1.00 29.11  ? 514 VAL B N   1 
ATOM   8083 C  CA  . VAL B 1 514 ? -46.845  5.277   283.777 1.00 27.84  ? 514 VAL B CA  1 
ATOM   8084 C  C   . VAL B 1 514 ? -45.584  6.057   283.427 1.00 29.30  ? 514 VAL B C   1 
ATOM   8085 O  O   . VAL B 1 514 ? -45.478  6.644   282.344 1.00 30.58  ? 514 VAL B O   1 
ATOM   8086 C  CB  . VAL B 1 514 ? -47.661  5.990   284.869 1.00 26.41  ? 514 VAL B CB  1 
ATOM   8087 C  CG1 . VAL B 1 514 ? -47.962  7.419   284.454 1.00 42.34  ? 514 VAL B CG1 1 
ATOM   8088 C  CG2 . VAL B 1 514 ? -48.948  5.234   285.151 1.00 27.07  ? 514 VAL B CG2 1 
ATOM   8089 N  N   . LYS B 1 515 ? -44.607  6.067   284.337 1.00 29.31  ? 515 LYS B N   1 
ATOM   8090 C  CA  . LYS B 1 515 ? -43.373  6.800   284.081 1.00 29.79  ? 515 LYS B CA  1 
ATOM   8091 C  C   . LYS B 1 515 ? -42.541  6.141   282.988 1.00 28.91  ? 515 LYS B C   1 
ATOM   8092 O  O   . LYS B 1 515 ? -41.773  6.826   282.303 1.00 29.39  ? 515 LYS B O   1 
ATOM   8093 C  CB  . LYS B 1 515 ? -42.564  6.933   285.370 1.00 31.31  ? 515 LYS B CB  1 
ATOM   8094 C  CG  . LYS B 1 515 ? -43.357  7.528   286.524 1.00 40.79  ? 515 LYS B CG  1 
ATOM   8095 C  CD  . LYS B 1 515 ? -43.078  6.812   287.834 1.00 58.89  ? 515 LYS B CD  1 
ATOM   8096 C  CE  . LYS B 1 515 ? -41.601  6.846   288.182 1.00 64.87  ? 515 LYS B CE  1 
ATOM   8097 N  NZ  . LYS B 1 515 ? -41.326  6.148   289.468 1.00 63.89  ? 515 LYS B NZ  1 
ATOM   8098 N  N   . TYR B 1 516 ? -42.674  4.825   282.806 1.00 28.61  ? 516 TYR B N   1 
ATOM   8099 C  CA  . TYR B 1 516 ? -42.012  4.183   281.676 1.00 28.00  ? 516 TYR B CA  1 
ATOM   8100 C  C   . TYR B 1 516 ? -42.625  4.624   280.354 1.00 28.74  ? 516 TYR B C   1 
ATOM   8101 O  O   . TYR B 1 516 ? -41.922  4.705   279.341 1.00 29.30  ? 516 TYR B O   1 
ATOM   8102 C  CB  . TYR B 1 516 ? -42.077  2.661   281.811 1.00 28.83  ? 516 TYR B CB  1 
ATOM   8103 C  CG  . TYR B 1 516 ? -41.323  1.929   280.724 1.00 31.24  ? 516 TYR B CG  1 
ATOM   8104 C  CD1 . TYR B 1 516 ? -39.961  1.688   280.838 1.00 28.84  ? 516 TYR B CD1 1 
ATOM   8105 C  CD2 . TYR B 1 516 ? -41.973  1.482   279.581 1.00 35.17  ? 516 TYR B CD2 1 
ATOM   8106 C  CE1 . TYR B 1 516 ? -39.267  1.023   279.846 1.00 32.34  ? 516 TYR B CE1 1 
ATOM   8107 C  CE2 . TYR B 1 516 ? -41.288  0.816   278.583 1.00 32.55  ? 516 TYR B CE2 1 
ATOM   8108 C  CZ  . TYR B 1 516 ? -39.936  0.589   278.721 1.00 34.33  ? 516 TYR B CZ  1 
ATOM   8109 O  OH  . TYR B 1 516 ? -39.253  -0.073  277.728 1.00 56.61  ? 516 TYR B OH  1 
ATOM   8110 N  N   . VAL B 1 517 ? -43.928  4.911   280.344 1.00 30.70  ? 517 VAL B N   1 
ATOM   8111 C  CA  . VAL B 1 517 ? -44.572  5.417   279.138 1.00 30.91  ? 517 VAL B CA  1 
ATOM   8112 C  C   . VAL B 1 517 ? -44.202  6.878   278.909 1.00 31.03  ? 517 VAL B C   1 
ATOM   8113 O  O   . VAL B 1 517 ? -43.975  7.306   277.771 1.00 31.54  ? 517 VAL B O   1 
ATOM   8114 C  CB  . VAL B 1 517 ? -46.096  5.221   279.234 1.00 32.57  ? 517 VAL B CB  1 
ATOM   8115 C  CG1 . VAL B 1 517 ? -46.820  6.072   278.206 1.00 40.31  ? 517 VAL B CG1 1 
ATOM   8116 C  CG2 . VAL B 1 517 ? -46.451  3.755   279.052 1.00 35.17  ? 517 VAL B CG2 1 
ATOM   8117 N  N   . ASP B 1 518 ? -44.117  7.660   279.987 1.00 29.86  ? 518 ASP B N   1 
ATOM   8118 C  CA  . ASP B 1 518 ? -43.858  9.090   279.862 1.00 29.42  ? 518 ASP B CA  1 
ATOM   8119 C  C   . ASP B 1 518 ? -42.463  9.354   279.308 1.00 30.45  ? 518 ASP B C   1 
ATOM   8120 O  O   . ASP B 1 518 ? -42.304  10.034  278.287 1.00 30.38  ? 518 ASP B O   1 
ATOM   8121 C  CB  . ASP B 1 518 ? -44.034  9.771   281.220 1.00 30.08  ? 518 ASP B CB  1 
ATOM   8122 C  CG  . ASP B 1 518 ? -45.448  9.655   281.748 1.00 31.99  ? 518 ASP B CG  1 
ATOM   8123 O  OD1 . ASP B 1 518 ? -46.366  9.408   280.938 1.00 42.89  ? 518 ASP B OD1 1 
ATOM   8124 O  OD2 . ASP B 1 518 ? -45.643  9.812   282.971 1.00 31.08  ? 518 ASP B OD2 1 
ATOM   8125 N  N   . ARG B 1 519 ? -41.435  8.820   279.973 1.00 33.10  ? 519 ARG B N   1 
ATOM   8126 C  CA  . ARG B 1 519 ? -40.062  9.110   279.573 1.00 34.32  ? 519 ARG B CA  1 
ATOM   8127 C  C   . ARG B 1 519 ? -39.726  8.521   278.209 1.00 33.17  ? 519 ARG B C   1 
ATOM   8128 O  O   . ARG B 1 519 ? -38.853  9.047   277.509 1.00 33.55  ? 519 ARG B O   1 
ATOM   8129 C  CB  . ARG B 1 519 ? -39.085  8.583   280.624 1.00 33.20  ? 519 ARG B CB  1 
ATOM   8130 C  CG  . ARG B 1 519 ? -39.434  8.967   282.052 1.00 44.53  ? 519 ARG B CG  1 
ATOM   8131 C  CD  . ARG B 1 519 ? -38.530  8.254   283.043 1.00 39.16  ? 519 ARG B CD  1 
ATOM   8132 N  NE  . ARG B 1 519 ? -39.002  8.395   284.417 1.00 38.44  ? 519 ARG B NE  1 
ATOM   8133 C  CZ  . ARG B 1 519 ? -38.445  9.198   285.317 1.00 37.75  ? 519 ARG B CZ  1 
ATOM   8134 N  NH1 . ARG B 1 519 ? -37.397  9.936   284.985 1.00 36.47  ? 519 ARG B NH1 1 
ATOM   8135 N  NH2 . ARG B 1 519 ? -38.937  9.265   286.546 1.00 51.60  ? 519 ARG B NH2 1 
ATOM   8136 N  N   . ASN B 1 520 ? -40.398  7.442   277.814 1.00 32.75  ? 520 ASN B N   1 
ATOM   8137 C  CA  . ASN B 1 520 ? -40.097  6.752   276.568 1.00 35.21  ? 520 ASN B CA  1 
ATOM   8138 C  C   . ASN B 1 520 ? -41.043  7.131   275.436 1.00 44.60  ? 520 ASN B C   1 
ATOM   8139 O  O   . ASN B 1 520 ? -41.080  6.429   274.419 1.00 34.57  ? 520 ASN B O   1 
ATOM   8140 C  CB  . ASN B 1 520 ? -40.120  5.238   276.783 1.00 32.52  ? 520 ASN B CB  1 
ATOM   8141 C  CG  . ASN B 1 520 ? -38.897  4.737   277.524 1.00 41.07  ? 520 ASN B CG  1 
ATOM   8142 O  OD1 . ASN B 1 520 ? -37.841  4.526   276.929 1.00 34.30  ? 520 ASN B OD1 1 
ATOM   8143 N  ND2 . ASN B 1 520 ? -39.034  4.547   278.831 1.00 49.87  ? 520 ASN B ND2 1 
ATOM   8144 N  N   . LYS B 1 521 ? -41.812  8.211   275.591 1.00 33.05  ? 521 LYS B N   1 
ATOM   8145 C  CA  . LYS B 1 521 ? -42.646  8.761   274.522 1.00 34.65  ? 521 LYS B CA  1 
ATOM   8146 C  C   . LYS B 1 521 ? -43.709  7.753   274.066 1.00 39.71  ? 521 LYS B C   1 
ATOM   8147 O  O   . LYS B 1 521 ? -44.228  7.828   272.949 1.00 45.08  ? 521 LYS B O   1 
ATOM   8148 C  CB  . LYS B 1 521 ? -41.747  9.240   273.365 1.00 36.39  ? 521 LYS B CB  1 
ATOM   8149 C  CG  . LYS B 1 521 ? -42.394  9.820   272.108 1.00 54.10  ? 521 LYS B CG  1 
ATOM   8150 C  CD  . LYS B 1 521 ? -41.324  10.229  271.105 1.00 37.22  ? 521 LYS B CD  1 
ATOM   8151 C  CE  . LYS B 1 521 ? -41.911  10.500  269.731 1.00 37.80  ? 521 LYS B CE  1 
ATOM   8152 N  NZ  . LYS B 1 521 ? -40.885  10.330  268.661 1.00 38.21  ? 521 LYS B NZ  1 
ATOM   8153 N  N   . LEU B 1 522 ? -44.066  6.814   274.938 1.00 34.18  ? 522 LEU B N   1 
ATOM   8154 C  CA  . LEU B 1 522 ? -45.007  5.770   274.570 1.00 34.15  ? 522 LEU B CA  1 
ATOM   8155 C  C   . LEU B 1 522 ? -46.427  6.325   274.481 1.00 32.89  ? 522 LEU B C   1 
ATOM   8156 O  O   . LEU B 1 522 ? -46.747  7.390   275.017 1.00 34.51  ? 522 LEU B O   1 
ATOM   8157 C  CB  . LEU B 1 522 ? -44.942  4.617   275.569 1.00 38.50  ? 522 LEU B CB  1 
ATOM   8158 C  CG  . LEU B 1 522 ? -43.593  3.901   275.618 1.00 36.05  ? 522 LEU B CG  1 
ATOM   8159 C  CD1 . LEU B 1 522 ? -43.612  2.778   276.637 1.00 33.72  ? 522 LEU B CD1 1 
ATOM   8160 C  CD2 . LEU B 1 522 ? -43.224  3.372   274.240 1.00 33.57  ? 522 LEU B CD2 1 
ATOM   8161 N  N   . GLY B 1 523 ? -47.288  5.574   273.791 1.00 31.93  ? 523 GLY B N   1 
ATOM   8162 C  CA  . GLY B 1 523 ? -48.613  6.082   273.476 1.00 33.03  ? 523 GLY B CA  1 
ATOM   8163 C  C   . GLY B 1 523 ? -49.524  6.191   274.684 1.00 31.70  ? 523 GLY B C   1 
ATOM   8164 O  O   . GLY B 1 523 ? -50.238  7.184   274.844 1.00 44.25  ? 523 GLY B O   1 
ATOM   8165 N  N   . GLY B 1 524 ? -49.527  5.175   275.538 1.00 33.14  ? 524 GLY B N   1 
ATOM   8166 C  CA  . GLY B 1 524 ? -50.393  5.194   276.702 1.00 27.54  ? 524 GLY B CA  1 
ATOM   8167 C  C   . GLY B 1 524 ? -50.506  3.808   277.313 1.00 23.65  ? 524 GLY B C   1 
ATOM   8168 O  O   . GLY B 1 524 ? -49.636  2.960   277.129 1.00 29.17  ? 524 GLY B O   1 
ATOM   8169 N  N   . LEU B 1 525 ? -51.606  3.606   278.037 1.00 22.18  ? 525 LEU B N   1 
ATOM   8170 C  CA  . LEU B 1 525 ? -51.838  2.383   278.791 1.00 21.86  ? 525 LEU B CA  1 
ATOM   8171 C  C   . LEU B 1 525 ? -53.219  1.824   278.481 1.00 25.18  ? 525 LEU B C   1 
ATOM   8172 O  O   . LEU B 1 525 ? -54.188  2.576   278.350 1.00 33.95  ? 525 LEU B O   1 
ATOM   8173 C  CB  . LEU B 1 525 ? -51.711  2.633   280.298 1.00 19.28  ? 525 LEU B CB  1 
ATOM   8174 C  CG  . LEU B 1 525 ? -50.338  3.076   280.803 1.00 19.98  ? 525 LEU B CG  1 
ATOM   8175 C  CD1 . LEU B 1 525 ? -50.421  3.537   282.246 1.00 37.47  ? 525 LEU B CD1 1 
ATOM   8176 C  CD2 . LEU B 1 525 ? -49.335  1.948   280.665 1.00 25.04  ? 525 LEU B CD2 1 
ATOM   8177 N  N   . PHE B 1 526 ? -53.299  0.500   278.365 1.00 26.02  ? 526 PHE B N   1 
ATOM   8178 C  CA  . PHE B 1 526 ? -54.564  -0.208  278.229 1.00 23.56  ? 526 PHE B CA  1 
ATOM   8179 C  C   . PHE B 1 526 ? -54.588  -1.359  279.223 1.00 21.24  ? 526 PHE B C   1 
ATOM   8180 O  O   . PHE B 1 526 ? -53.541  -1.889  279.604 1.00 23.75  ? 526 PHE B O   1 
ATOM   8181 C  CB  . PHE B 1 526 ? -54.779  -0.721  276.798 1.00 24.41  ? 526 PHE B CB  1 
ATOM   8182 C  CG  . PHE B 1 526 ? -54.052  -1.998  276.491 1.00 22.76  ? 526 PHE B CG  1 
ATOM   8183 C  CD1 . PHE B 1 526 ? -52.707  -1.983  276.165 1.00 23.72  ? 526 PHE B CD1 1 
ATOM   8184 C  CD2 . PHE B 1 526 ? -54.717  -3.212  276.511 1.00 23.65  ? 526 PHE B CD2 1 
ATOM   8185 C  CE1 . PHE B 1 526 ? -52.037  -3.154  275.876 1.00 26.83  ? 526 PHE B CE1 1 
ATOM   8186 C  CE2 . PHE B 1 526 ? -54.052  -4.388  276.224 1.00 34.28  ? 526 PHE B CE2 1 
ATOM   8187 C  CZ  . PHE B 1 526 ? -52.709  -4.358  275.907 1.00 28.29  ? 526 PHE B CZ  1 
ATOM   8188 N  N   . ALA B 1 527 ? -55.790  -1.747  279.643 1.00 18.75  ? 527 ALA B N   1 
ATOM   8189 C  CA  . ALA B 1 527 ? -55.942  -2.650  280.774 1.00 19.98  ? 527 ALA B CA  1 
ATOM   8190 C  C   . ALA B 1 527 ? -56.833  -3.835  280.428 1.00 22.36  ? 527 ALA B C   1 
ATOM   8191 O  O   . ALA B 1 527 ? -57.670  -3.779  279.523 1.00 26.63  ? 527 ALA B O   1 
ATOM   8192 C  CB  . ALA B 1 527 ? -56.516  -1.919  281.995 1.00 17.25  ? 527 ALA B CB  1 
ATOM   8193 N  N   . TRP B 1 528 ? -56.625  -4.916  281.174 1.00 22.98  ? 528 TRP B N   1 
ATOM   8194 C  CA  . TRP B 1 528 ? -57.489  -6.092  281.166 1.00 21.82  ? 528 TRP B CA  1 
ATOM   8195 C  C   . TRP B 1 528 ? -57.547  -6.644  282.585 1.00 21.68  ? 528 TRP B C   1 
ATOM   8196 O  O   . TRP B 1 528 ? -56.515  -7.012  283.143 1.00 24.77  ? 528 TRP B O   1 
ATOM   8197 C  CB  . TRP B 1 528 ? -56.971  -7.164  280.200 1.00 21.82  ? 528 TRP B CB  1 
ATOM   8198 C  CG  . TRP B 1 528 ? -57.743  -8.462  280.268 1.00 22.40  ? 528 TRP B CG  1 
ATOM   8199 C  CD1 . TRP B 1 528 ? -57.630  -9.434  281.221 1.00 23.91  ? 528 TRP B CD1 1 
ATOM   8200 C  CD2 . TRP B 1 528 ? -58.728  -8.930  279.338 1.00 25.00  ? 528 TRP B CD2 1 
ATOM   8201 N  NE1 . TRP B 1 528 ? -58.492  -10.467 280.951 1.00 30.10  ? 528 TRP B NE1 1 
ATOM   8202 C  CE2 . TRP B 1 528 ? -59.175  -10.184 279.798 1.00 25.41  ? 528 TRP B CE2 1 
ATOM   8203 C  CE3 . TRP B 1 528 ? -59.275  -8.411  278.162 1.00 24.45  ? 528 TRP B CE3 1 
ATOM   8204 C  CZ2 . TRP B 1 528 ? -60.146  -10.922 279.127 1.00 28.37  ? 528 TRP B CZ2 1 
ATOM   8205 C  CZ3 . TRP B 1 528 ? -60.240  -9.145  277.498 1.00 22.93  ? 528 TRP B CZ3 1 
ATOM   8206 C  CH2 . TRP B 1 528 ? -60.663  -10.388 277.980 1.00 23.01  ? 528 TRP B CH2 1 
ATOM   8207 N  N   . GLU B 1 529 ? -58.735  -6.699  283.181 1.00 20.52  ? 529 GLU B N   1 
ATOM   8208 C  CA  . GLU B 1 529 ? -59.967  -6.215  282.571 1.00 18.58  ? 529 GLU B CA  1 
ATOM   8209 C  C   . GLU B 1 529 ? -60.625  -5.205  283.508 1.00 25.11  ? 529 GLU B C   1 
ATOM   8210 O  O   . GLU B 1 529 ? -60.341  -5.191  284.705 1.00 32.08  ? 529 GLU B O   1 
ATOM   8211 C  CB  . GLU B 1 529 ? -60.904  -7.385  282.265 1.00 20.12  ? 529 GLU B CB  1 
ATOM   8212 C  CG  . GLU B 1 529 ? -61.089  -8.348  283.430 1.00 22.36  ? 529 GLU B CG  1 
ATOM   8213 C  CD  . GLU B 1 529 ? -61.809  -9.622  283.028 1.00 34.25  ? 529 GLU B CD  1 
ATOM   8214 O  OE1 . GLU B 1 529 ? -62.860  -9.934  283.625 1.00 20.67  ? 529 GLU B OE1 1 
ATOM   8215 O  OE2 . GLU B 1 529 ? -61.321  -10.313 282.110 1.00 60.81  ? 529 GLU B OE2 1 
ATOM   8216 N  N   . ILE B 1 530 ? -61.510  -4.366  282.961 1.00 16.99  ? 530 ILE B N   1 
ATOM   8217 C  CA  . ILE B 1 530 ? -62.011  -3.220  283.717 1.00 15.89  ? 530 ILE B CA  1 
ATOM   8218 C  C   . ILE B 1 530 ? -62.844  -3.660  284.917 1.00 16.74  ? 530 ILE B C   1 
ATOM   8219 O  O   . ILE B 1 530 ? -62.923  -2.941  285.921 1.00 24.08  ? 530 ILE B O   1 
ATOM   8220 C  CB  . ILE B 1 530 ? -62.808  -2.280  282.792 1.00 14.32  ? 530 ILE B CB  1 
ATOM   8221 C  CG1 . ILE B 1 530 ? -63.104  -0.955  283.497 1.00 15.67  ? 530 ILE B CG1 1 
ATOM   8222 C  CG2 . ILE B 1 530 ? -64.105  -2.936  282.342 1.00 13.57  ? 530 ILE B CG2 1 
ATOM   8223 C  CD1 . ILE B 1 530 ? -61.877  -0.279  284.067 1.00 13.15  ? 530 ILE B CD1 1 
ATOM   8224 N  N   . ASP B 1 531 ? -63.462  -4.838  284.851 1.00 16.51  ? 531 ASP B N   1 
ATOM   8225 C  CA  . ASP B 1 531 ? -64.334  -5.282  285.931 1.00 16.90  ? 531 ASP B CA  1 
ATOM   8226 C  C   . ASP B 1 531 ? -63.568  -5.778  287.149 1.00 19.60  ? 531 ASP B C   1 
ATOM   8227 O  O   . ASP B 1 531 ? -64.151  -5.865  288.235 1.00 18.05  ? 531 ASP B O   1 
ATOM   8228 C  CB  . ASP B 1 531 ? -65.264  -6.387  285.434 1.00 14.46  ? 531 ASP B CB  1 
ATOM   8229 C  CG  . ASP B 1 531 ? -64.511  -7.570  284.878 1.00 13.68  ? 531 ASP B CG  1 
ATOM   8230 O  OD1 . ASP B 1 531 ? -64.128  -8.458  285.667 1.00 17.53  ? 531 ASP B OD1 1 
ATOM   8231 O  OD2 . ASP B 1 531 ? -64.297  -7.605  283.650 1.00 14.71  ? 531 ASP B OD2 1 
ATOM   8232 N  N   . ALA B 1 532 ? -62.286  -6.101  287.000 1.00 22.94  ? 532 ALA B N   1 
ATOM   8233 C  CA  . ALA B 1 532 ? -61.505  -6.666  288.091 1.00 25.30  ? 532 ALA B CA  1 
ATOM   8234 C  C   . ALA B 1 532 ? -60.872  -5.612  288.990 1.00 25.26  ? 532 ALA B C   1 
ATOM   8235 O  O   . ALA B 1 532 ? -60.337  -5.964  290.047 1.00 25.44  ? 532 ALA B O   1 
ATOM   8236 C  CB  . ALA B 1 532 ? -60.412  -7.583  287.535 1.00 21.56  ? 532 ALA B CB  1 
ATOM   8237 N  N   . ASP B 1 533 ? -60.920  -4.342  288.605 1.00 23.38  ? 533 ASP B N   1 
ATOM   8238 C  CA  . ASP B 1 533 ? -60.333  -3.273  289.397 1.00 26.23  ? 533 ASP B CA  1 
ATOM   8239 C  C   . ASP B 1 533 ? -61.329  -2.764  290.432 1.00 25.81  ? 533 ASP B C   1 
ATOM   8240 O  O   . ASP B 1 533 ? -62.538  -2.719  290.191 1.00 55.44  ? 533 ASP B O   1 
ATOM   8241 C  CB  . ASP B 1 533 ? -59.886  -2.120  288.496 1.00 26.28  ? 533 ASP B CB  1 
ATOM   8242 C  CG  . ASP B 1 533 ? -59.308  -0.956  289.278 1.00 28.03  ? 533 ASP B CG  1 
ATOM   8243 O  OD1 . ASP B 1 533 ? -58.739  -1.189  290.364 1.00 30.43  ? 533 ASP B OD1 1 
ATOM   8244 O  OD2 . ASP B 1 533 ? -59.431  0.196   288.810 1.00 45.45  ? 533 ASP B OD2 1 
ATOM   8245 N  N   . ASN B 1 534 ? -60.804  -2.385  291.598 1.00 22.09  ? 534 ASN B N   1 
ATOM   8246 C  CA  . ASN B 1 534 ? -61.596  -1.750  292.641 1.00 22.27  ? 534 ASN B CA  1 
ATOM   8247 C  C   . ASN B 1 534 ? -61.397  -0.239  292.673 1.00 25.93  ? 534 ASN B C   1 
ATOM   8248 O  O   . ASN B 1 534 ? -61.720  0.405   293.676 1.00 41.56  ? 534 ASN B O   1 
ATOM   8249 C  CB  . ASN B 1 534 ? -61.270  -2.362  294.006 1.00 24.69  ? 534 ASN B CB  1 
ATOM   8250 C  CG  . ASN B 1 534 ? -59.916  -1.933  294.533 1.00 25.27  ? 534 ASN B CG  1 
ATOM   8251 O  OD1 . ASN B 1 534 ? -59.010  -1.607  293.766 1.00 25.79  ? 534 ASN B OD1 1 
ATOM   8252 N  ND2 . ASN B 1 534 ? -59.772  -1.928  295.853 1.00 23.49  ? 534 ASN B ND2 1 
ATOM   8253 N  N   . GLY B 1 535 ? -60.869  0.337   291.592 1.00 25.46  ? 535 GLY B N   1 
ATOM   8254 C  CA  . GLY B 1 535 ? -60.601  1.748   291.490 1.00 26.89  ? 535 GLY B CA  1 
ATOM   8255 C  C   . GLY B 1 535 ? -59.149  2.121   291.717 1.00 26.56  ? 535 GLY B C   1 
ATOM   8256 O  O   . GLY B 1 535 ? -58.704  3.163   291.224 1.00 49.99  ? 535 GLY B O   1 
ATOM   8257 N  N   . ASP B 1 536 ? -58.400  1.289   292.443 1.00 24.04  ? 536 ASP B N   1 
ATOM   8258 C  CA  . ASP B 1 536 ? -57.022  1.633   292.782 1.00 25.85  ? 536 ASP B CA  1 
ATOM   8259 C  C   . ASP B 1 536 ? -56.137  1.696   291.544 1.00 26.03  ? 536 ASP B C   1 
ATOM   8260 O  O   . ASP B 1 536 ? -55.313  2.608   291.410 1.00 26.17  ? 536 ASP B O   1 
ATOM   8261 C  CB  . ASP B 1 536 ? -56.462  0.625   293.785 1.00 29.33  ? 536 ASP B CB  1 
ATOM   8262 C  CG  . ASP B 1 536 ? -57.196  0.649   295.111 1.00 27.98  ? 536 ASP B CG  1 
ATOM   8263 O  OD1 . ASP B 1 536 ? -57.816  1.684   295.430 1.00 28.50  ? 536 ASP B OD1 1 
ATOM   8264 O  OD2 . ASP B 1 536 ? -57.151  -0.368  295.836 1.00 24.48  ? 536 ASP B OD2 1 
ATOM   8265 N  N   . LEU B 1 537 ? -56.290  0.739   290.628 1.00 25.31  ? 537 LEU B N   1 
ATOM   8266 C  CA  . LEU B 1 537 ? -55.386  0.667   289.485 1.00 27.00  ? 537 LEU B CA  1 
ATOM   8267 C  C   . LEU B 1 537 ? -55.693  1.751   288.460 1.00 26.87  ? 537 LEU B C   1 
ATOM   8268 O  O   . LEU B 1 537 ? -54.779  2.410   287.951 1.00 26.00  ? 537 LEU B O   1 
ATOM   8269 C  CB  . LEU B 1 537 ? -55.459  -0.718  288.844 1.00 23.56  ? 537 LEU B CB  1 
ATOM   8270 C  CG  . LEU B 1 537 ? -55.017  -1.872  289.744 1.00 26.58  ? 537 LEU B CG  1 
ATOM   8271 C  CD1 . LEU B 1 537 ? -54.913  -3.164  288.954 1.00 29.83  ? 537 LEU B CD1 1 
ATOM   8272 C  CD2 . LEU B 1 537 ? -53.692  -1.541  290.408 1.00 23.80  ? 537 LEU B CD2 1 
ATOM   8273 N  N   . LEU B 1 538 ? -56.974  1.948   288.137 1.00 23.13  ? 538 LEU B N   1 
ATOM   8274 C  CA  . LEU B 1 538 ? -57.322  2.904   287.091 1.00 23.54  ? 538 LEU B CA  1 
ATOM   8275 C  C   . LEU B 1 538 ? -56.956  4.327   287.496 1.00 27.19  ? 538 LEU B C   1 
ATOM   8276 O  O   . LEU B 1 538 ? -56.559  5.136   286.648 1.00 26.21  ? 538 LEU B O   1 
ATOM   8277 C  CB  . LEU B 1 538 ? -58.809  2.802   286.754 1.00 21.93  ? 538 LEU B CB  1 
ATOM   8278 C  CG  . LEU B 1 538 ? -59.243  3.667   285.570 1.00 21.40  ? 538 LEU B CG  1 
ATOM   8279 C  CD1 . LEU B 1 538 ? -58.317  3.439   284.385 1.00 26.55  ? 538 LEU B CD1 1 
ATOM   8280 C  CD2 . LEU B 1 538 ? -60.676  3.372   285.187 1.00 21.16  ? 538 LEU B CD2 1 
ATOM   8281 N  N   . ASN B 1 539 ? -57.080  4.653   288.784 1.00 26.89  ? 539 ASN B N   1 
ATOM   8282 C  CA  . ASN B 1 539 ? -56.606  5.949   289.257 1.00 24.93  ? 539 ASN B CA  1 
ATOM   8283 C  C   . ASN B 1 539 ? -55.100  6.076   289.078 1.00 31.77  ? 539 ASN B C   1 
ATOM   8284 O  O   . ASN B 1 539 ? -54.596  7.148   288.722 1.00 59.14  ? 539 ASN B O   1 
ATOM   8285 C  CB  . ASN B 1 539 ? -56.990  6.151   290.723 1.00 23.30  ? 539 ASN B CB  1 
ATOM   8286 C  CG  . ASN B 1 539 ? -58.488  6.159   290.937 1.00 24.28  ? 539 ASN B CG  1 
ATOM   8287 O  OD1 . ASN B 1 539 ? -59.262  6.023   289.990 1.00 25.17  ? 539 ASN B OD1 1 
ATOM   8288 N  ND2 . ASN B 1 539 ? -58.907  6.316   292.187 1.00 24.89  ? 539 ASN B ND2 1 
ATOM   8289 N  N   . ALA B 1 540 ? -54.364  4.987   289.313 1.00 29.18  ? 540 ALA B N   1 
ATOM   8290 C  CA  . ALA B 1 540 ? -52.918  5.016   289.124 1.00 28.31  ? 540 ALA B CA  1 
ATOM   8291 C  C   . ALA B 1 540 ? -52.545  5.098   287.650 1.00 24.55  ? 540 ALA B C   1 
ATOM   8292 O  O   . ALA B 1 540 ? -51.509  5.678   287.307 1.00 27.19  ? 540 ALA B O   1 
ATOM   8293 C  CB  . ALA B 1 540 ? -52.280  3.785   289.766 1.00 33.63  ? 540 ALA B CB  1 
ATOM   8294 N  N   . ILE B 1 541 ? -53.371  4.528   286.769 1.00 23.61  ? 541 ILE B N   1 
ATOM   8295 C  CA  . ILE B 1 541 ? -53.091  4.586   285.336 1.00 27.76  ? 541 ILE B CA  1 
ATOM   8296 C  C   . ILE B 1 541 ? -53.120  6.028   284.845 1.00 27.11  ? 541 ILE B C   1 
ATOM   8297 O  O   . ILE B 1 541 ? -52.315  6.428   283.995 1.00 25.82  ? 541 ILE B O   1 
ATOM   8298 C  CB  . ILE B 1 541 ? -54.088  3.702   284.563 1.00 26.22  ? 541 ILE B CB  1 
ATOM   8299 C  CG1 . ILE B 1 541 ? -53.889  2.228   284.920 1.00 24.47  ? 541 ILE B CG1 1 
ATOM   8300 C  CG2 . ILE B 1 541 ? -53.949  3.907   283.063 1.00 27.97  ? 541 ILE B CG2 1 
ATOM   8301 C  CD1 . ILE B 1 541 ? -54.867  1.300   284.239 1.00 25.12  ? 541 ILE B CD1 1 
ATOM   8302 N  N   . ASN B 1 542 ? -54.035  6.834   285.381 1.00 23.82  ? 542 ASN B N   1 
ATOM   8303 C  CA  . ASN B 1 542 ? -54.224  8.208   284.940 1.00 28.52  ? 542 ASN B CA  1 
ATOM   8304 C  C   . ASN B 1 542 ? -53.435  9.212   285.774 1.00 32.62  ? 542 ASN B C   1 
ATOM   8305 O  O   . ASN B 1 542 ? -53.743  10.409  285.735 1.00 47.18  ? 542 ASN B O   1 
ATOM   8306 C  CB  . ASN B 1 542 ? -55.712  8.563   284.963 1.00 29.36  ? 542 ASN B CB  1 
ATOM   8307 C  CG  . ASN B 1 542 ? -56.522  7.734   283.988 1.00 31.65  ? 542 ASN B CG  1 
ATOM   8308 O  OD1 . ASN B 1 542 ? -56.658  8.087   282.818 1.00 29.40  ? 542 ASN B OD1 1 
ATOM   8309 N  ND2 . ASN B 1 542 ? -57.063  6.619   284.467 1.00 36.77  ? 542 ASN B ND2 1 
ATOM   8310 N  N   . ALA B 1 543 ? -52.432  8.758   286.521 1.00 32.96  ? 543 ALA B N   1 
ATOM   8311 C  CA  . ALA B 1 543 ? -51.651  9.664   287.353 1.00 34.73  ? 543 ALA B CA  1 
ATOM   8312 C  C   . ALA B 1 543 ? -50.830  10.607  286.483 1.00 34.53  ? 543 ALA B C   1 
ATOM   8313 O  O   . ALA B 1 543 ? -50.096  10.169  285.592 1.00 31.40  ? 543 ALA B O   1 
ATOM   8314 C  CB  . ALA B 1 543 ? -50.740  8.873   288.289 1.00 48.72  ? 543 ALA B CB  1 
ATOM   8315 N  N   . GLN B 1 544 ? -50.954  11.905  286.746 1.00 39.56  ? 544 GLN B N   1 
ATOM   8316 C  CA  . GLN B 1 544 ? -50.288  12.937  285.964 1.00 42.80  ? 544 GLN B CA  1 
ATOM   8317 C  C   . GLN B 1 544 ? -48.994  13.345  286.657 1.00 48.72  ? 544 GLN B C   1 
ATOM   8318 O  O   . GLN B 1 544 ? -49.011  13.744  287.827 1.00 48.92  ? 544 GLN B O   1 
ATOM   8319 C  CB  . GLN B 1 544 ? -51.202  14.149  285.778 1.00 39.23  ? 544 GLN B CB  1 
ATOM   8320 C  CG  . GLN B 1 544 ? -50.675  15.184  284.798 1.00 41.39  ? 544 GLN B CG  1 
ATOM   8321 C  CD  . GLN B 1 544 ? -50.487  14.625  283.401 1.00 43.75  ? 544 GLN B CD  1 
ATOM   8322 O  OE1 . GLN B 1 544 ? -51.456  14.333  282.702 1.00 40.12  ? 544 GLN B OE1 1 
ATOM   8323 N  NE2 . GLN B 1 544 ? -49.234  14.473  282.988 1.00 49.34  ? 544 GLN B NE2 1 
ATOM   8324 N  N   . PHE B 1 545 ? -47.882  13.244  285.937 1.00 47.19  ? 545 PHE B N   1 
ATOM   8325 C  CA  . PHE B 1 545 ? -46.592  13.694  286.447 1.00 49.51  ? 545 PHE B CA  1 
ATOM   8326 C  C   . PHE B 1 545 ? -46.144  14.964  285.730 1.00 45.84  ? 545 PHE B C   1 
ATOM   8327 O  O   . PHE B 1 545 ? -45.707  15.924  286.364 1.00 47.77  ? 545 PHE B O   1 
ATOM   8328 C  CB  . PHE B 1 545 ? -45.532  12.601  286.290 1.00 58.23  ? 545 PHE B CB  1 
ATOM   8329 C  CG  . PHE B 1 545 ? -45.714  11.437  287.223 1.00 46.34  ? 545 PHE B CG  1 
ATOM   8330 C  CD1 . PHE B 1 545 ? -45.313  11.526  288.546 1.00 39.57  ? 545 PHE B CD1 1 
ATOM   8331 C  CD2 . PHE B 1 545 ? -46.276  10.253  286.777 1.00 42.39  ? 545 PHE B CD2 1 
ATOM   8332 C  CE1 . PHE B 1 545 ? -45.475  10.458  289.408 1.00 40.24  ? 545 PHE B CE1 1 
ATOM   8333 C  CE2 . PHE B 1 545 ? -46.440  9.182   287.635 1.00 36.12  ? 545 PHE B CE2 1 
ATOM   8334 C  CZ  . PHE B 1 545 ? -46.039  9.285   288.952 1.00 38.83  ? 545 PHE B CZ  1 
HETATM 8335 C  C1  . NAG C 2 .   ? -93.459  23.303  277.107 1.00 48.77  ? 601 NAG A C1  1 
HETATM 8336 C  C2  . NAG C 2 .   ? -94.600  22.804  277.989 1.00 42.17  ? 601 NAG A C2  1 
HETATM 8337 C  C3  . NAG C 2 .   ? -95.888  22.697  277.177 1.00 47.02  ? 601 NAG A C3  1 
HETATM 8338 C  C4  . NAG C 2 .   ? -96.186  24.015  276.474 1.00 62.06  ? 601 NAG A C4  1 
HETATM 8339 C  C5  . NAG C 2 .   ? -94.977  24.463  275.659 1.00 53.96  ? 601 NAG A C5  1 
HETATM 8340 C  C6  . NAG C 2 .   ? -95.158  25.825  275.030 1.00 45.52  ? 601 NAG A C6  1 
HETATM 8341 C  C7  . NAG C 2 .   ? -93.997  21.371  279.893 1.00 51.37  ? 601 NAG A C7  1 
HETATM 8342 C  C8  . NAG C 2 .   ? -94.048  22.616  280.726 1.00 40.62  ? 601 NAG A C8  1 
HETATM 8343 N  N2  . NAG C 2 .   ? -94.270  21.522  278.592 1.00 42.30  ? 601 NAG A N2  1 
HETATM 8344 O  O1  . NAG C 2 .   ? -92.314  23.456  277.881 1.00 47.61  ? 601 NAG A O1  1 
HETATM 8345 O  O3  . NAG C 2 .   ? -96.964  22.353  278.042 1.00 56.85  ? 601 NAG A O3  1 
HETATM 8346 O  O4  . NAG C 2 .   ? -97.304  23.861  275.607 1.00 72.04  ? 601 NAG A O4  1 
HETATM 8347 O  O5  . NAG C 2 .   ? -93.823  24.549  276.509 1.00 70.18  ? 601 NAG A O5  1 
HETATM 8348 O  O6  . NAG C 2 .   ? -94.028  26.657  275.256 1.00 42.03  ? 601 NAG A O6  1 
HETATM 8349 O  O7  . NAG C 2 .   ? -93.720  20.277  280.375 1.00 61.47  ? 601 NAG A O7  1 
HETATM 8350 C  C1  . NAG D 2 .   ? -70.307  13.482  288.158 1.00 68.92  ? 602 NAG A C1  1 
HETATM 8351 C  C2  . NAG D 2 .   ? -70.577  14.971  287.944 1.00 56.89  ? 602 NAG A C2  1 
HETATM 8352 C  C3  . NAG D 2 .   ? -71.290  15.194  286.613 1.00 54.95  ? 602 NAG A C3  1 
HETATM 8353 C  C4  . NAG D 2 .   ? -70.503  14.554  285.478 1.00 54.38  ? 602 NAG A C4  1 
HETATM 8354 C  C5  . NAG D 2 .   ? -70.227  13.084  285.787 1.00 66.33  ? 602 NAG A C5  1 
HETATM 8355 C  C6  . NAG D 2 .   ? -69.335  12.425  284.761 1.00 80.62  ? 602 NAG A C6  1 
HETATM 8356 C  C7  . NAG D 2 .   ? -72.564  15.163  289.410 1.00 89.28  ? 602 NAG A C7  1 
HETATM 8357 C  C8  . NAG D 2 .   ? -73.160  15.897  290.573 1.00 61.70  ? 602 NAG A C8  1 
HETATM 8358 N  N2  . NAG D 2 .   ? -71.333  15.549  289.046 1.00 73.72  ? 602 NAG A N2  1 
HETATM 8359 O  O1  . NAG D 2 .   ? -69.603  13.307  289.344 1.00 83.00  ? 602 NAG A O1  1 
HETATM 8360 O  O3  . NAG D 2 .   ? -71.436  16.590  286.378 1.00 51.68  ? 602 NAG A O3  1 
HETATM 8361 O  O4  . NAG D 2 .   ? -71.237  14.648  284.262 1.00 52.01  ? 602 NAG A O4  1 
HETATM 8362 O  O5  . NAG D 2 .   ? -69.559  12.964  287.053 1.00 72.09  ? 602 NAG A O5  1 
HETATM 8363 O  O6  . NAG D 2 .   ? -68.470  13.367  284.142 1.00 56.02  ? 602 NAG A O6  1 
HETATM 8364 O  O7  . NAG D 2 .   ? -73.170  14.265  288.830 1.00 98.73  ? 602 NAG A O7  1 
HETATM 8365 C  C1  . NAG E 2 .   ? -116.524 15.652  305.846 1.00 41.99  ? 603 NAG A C1  1 
HETATM 8366 C  C2  . NAG E 2 .   ? -115.449 14.580  306.020 1.00 42.91  ? 603 NAG A C2  1 
HETATM 8367 C  C3  . NAG E 2 .   ? -114.326 14.786  305.006 1.00 39.23  ? 603 NAG A C3  1 
HETATM 8368 C  C4  . NAG E 2 .   ? -114.890 14.877  303.594 1.00 37.83  ? 603 NAG A C4  1 
HETATM 8369 C  C5  . NAG E 2 .   ? -115.982 15.940  303.531 1.00 37.95  ? 603 NAG A C5  1 
HETATM 8370 C  C6  . NAG E 2 .   ? -116.666 16.008  302.186 1.00 37.90  ? 603 NAG A C6  1 
HETATM 8371 C  C7  . NAG E 2 .   ? -114.370 13.520  307.955 1.00 71.89  ? 603 NAG A C7  1 
HETATM 8372 C  C8  . NAG E 2 .   ? -113.880 13.712  309.358 1.00 60.16  ? 603 NAG A C8  1 
HETATM 8373 N  N2  . NAG E 2 .   ? -114.923 14.590  307.375 1.00 73.88  ? 603 NAG A N2  1 
HETATM 8374 O  O1  . NAG E 2 .   ? -117.571 15.401  306.726 1.00 39.89  ? 603 NAG A O1  1 
HETATM 8375 O  O3  . NAG E 2 .   ? -113.406 13.704  305.089 1.00 40.46  ? 603 NAG A O3  1 
HETATM 8376 O  O4  . NAG E 2 .   ? -113.856 15.207  302.674 1.00 40.63  ? 603 NAG A O4  1 
HETATM 8377 O  O5  . NAG E 2 .   ? -116.999 15.646  304.499 1.00 41.89  ? 603 NAG A O5  1 
HETATM 8378 O  O6  . NAG E 2 .   ? -117.418 17.205  302.044 1.00 38.88  ? 603 NAG A O6  1 
HETATM 8379 O  O7  . NAG E 2 .   ? -114.268 12.445  307.372 1.00 77.74  ? 603 NAG A O7  1 
HETATM 8380 C  C1  . SN5 F 3 .   ? -110.349 14.643  302.046 1.00 34.17  ? 604 SN5 A C1  1 
HETATM 8381 S  S7  . SN5 F 3 .   ? -110.032 10.800  300.726 1.00 29.43  ? 604 SN5 A S7  1 
HETATM 8382 C  C2  . SN5 F 3 .   ? -109.689 13.360  302.395 1.00 35.39  ? 604 SN5 A C2  1 
HETATM 8383 C  C3  . SN5 F 3 .   ? -108.765 13.483  303.515 1.00 32.24  ? 604 SN5 A C3  1 
HETATM 8384 C  C4  . SN5 F 3 .   ? -107.766 14.554  303.304 1.00 37.72  ? 604 SN5 A C4  1 
HETATM 8385 C  C5  . SN5 F 3 .   ? -108.439 15.913  303.046 1.00 36.36  ? 604 SN5 A C5  1 
HETATM 8386 C  C6  . SN5 F 3 .   ? -107.461 16.894  302.736 1.00 30.97  ? 604 SN5 A C6  1 
HETATM 8387 C  C7  . SN5 F 3 .   ? -110.791 11.031  302.123 1.00 40.31  ? 604 SN5 A C7  1 
HETATM 8388 C  C8  . SN5 F 3 .   ? -111.535 9.885   302.781 1.00 41.72  ? 604 SN5 A C8  1 
HETATM 8389 N  N2  . SN5 F 3 .   ? -110.767 12.346  302.767 1.00 41.17  ? 604 SN5 A N2  1 
HETATM 8390 O  O3  . SN5 F 3 .   ? -108.046 12.189  303.702 1.00 35.93  ? 604 SN5 A O3  1 
HETATM 8391 O  O4  . SN5 F 3 .   ? -106.924 14.653  304.477 1.00 72.23  ? 604 SN5 A O4  1 
HETATM 8392 O  O5  . SN5 F 3 .   ? -109.389 15.725  301.849 1.00 37.79  ? 604 SN5 A O5  1 
HETATM 8393 O  O6  . SN5 F 3 .   ? -108.085 18.101  302.462 1.00 31.12  ? 604 SN5 A O6  1 
HETATM 8394 C  C1  . 58Y G 4 .   ? -113.285 16.376  298.222 1.00 24.11  ? 605 58Y A C1  1 
HETATM 8395 C  C2  . 58Y G 4 .   ? -112.293 17.148  298.891 1.00 24.99  ? 605 58Y A C2  1 
HETATM 8396 C  C3  . 58Y G 4 .   ? -111.090 16.362  299.192 1.00 28.26  ? 605 58Y A C3  1 
HETATM 8397 C  C4  . 58Y G 4 .   ? -111.349 14.990  299.827 1.00 29.53  ? 605 58Y A C4  1 
HETATM 8398 C  C5  . 58Y G 4 .   ? -112.559 14.240  299.251 1.00 29.98  ? 605 58Y A C5  1 
HETATM 8399 C  C6  . 58Y G 4 .   ? -112.978 13.091  300.223 1.00 30.26  ? 605 58Y A C6  1 
HETATM 8400 C  C7  . 58Y G 4 .   ? -112.121 17.732  296.463 1.00 21.55  ? 605 58Y A C7  1 
HETATM 8401 C  C8  . 58Y G 4 .   ? -110.902 17.673  295.512 1.00 19.23  ? 605 58Y A C8  1 
HETATM 8402 N  N2  . 58Y G 4 .   ? -111.718 18.206  297.781 1.00 23.74  ? 605 58Y A N2  1 
HETATM 8403 S  S1  . 58Y G 4 .   ? -112.723 16.252  296.709 1.00 29.14  ? 605 58Y A S1  1 
HETATM 8404 O  O3  . 58Y G 4 .   ? -110.259 17.143  300.082 1.00 40.19  ? 605 58Y A O3  1 
HETATM 8405 O  O4  . 58Y G 4 .   ? -111.449 15.109  301.234 1.00 30.81  ? 605 58Y A O4  1 
HETATM 8406 O  O5  . 58Y G 4 .   ? -113.635 15.005  299.047 1.00 26.00  ? 605 58Y A O5  1 
HETATM 8407 O  O6  . 58Y G 4 .   ? -114.273 13.382  300.698 1.00 30.67  ? 605 58Y A O6  1 
HETATM 8408 CL CL  . CL  H 5 .   ? -75.166  28.864  288.505 1.00 20.29  ? 606 CL  A CL  1 
HETATM 8409 S  S   . SO4 I 6 .   ? -87.971  33.442  288.377 1.00 72.14  ? 607 SO4 A S   1 
HETATM 8410 O  O1  . SO4 I 6 .   ? -87.978  32.017  288.694 1.00 42.86  ? 607 SO4 A O1  1 
HETATM 8411 O  O2  . SO4 I 6 .   ? -88.151  33.621  286.939 1.00 66.73  ? 607 SO4 A O2  1 
HETATM 8412 O  O3  . SO4 I 6 .   ? -86.694  34.023  288.781 1.00 59.57  ? 607 SO4 A O3  1 
HETATM 8413 O  O4  . SO4 I 6 .   ? -89.057  34.106  289.091 1.00 41.16  ? 607 SO4 A O4  1 
HETATM 8414 S  S   . SO4 J 6 .   ? -92.202  34.679  296.856 1.00 39.07  ? 608 SO4 A S   1 
HETATM 8415 O  O1  . SO4 J 6 .   ? -90.818  34.527  296.417 1.00 38.37  ? 608 SO4 A O1  1 
HETATM 8416 O  O2  . SO4 J 6 .   ? -92.968  35.382  295.831 1.00 50.07  ? 608 SO4 A O2  1 
HETATM 8417 O  O3  . SO4 J 6 .   ? -92.786  33.361  297.077 1.00 40.20  ? 608 SO4 A O3  1 
HETATM 8418 O  O4  . SO4 J 6 .   ? -92.238  35.443  298.099 1.00 59.96  ? 608 SO4 A O4  1 
HETATM 8419 S  S   . SO4 K 6 .   ? -65.739  34.909  280.704 1.00 41.85  ? 609 SO4 A S   1 
HETATM 8420 O  O1  . SO4 K 6 .   ? -66.141  33.796  279.849 1.00 32.69  ? 609 SO4 A O1  1 
HETATM 8421 O  O2  . SO4 K 6 .   ? -65.734  36.143  279.925 1.00 48.98  ? 609 SO4 A O2  1 
HETATM 8422 O  O3  . SO4 K 6 .   ? -66.680  35.036  281.812 1.00 42.70  ? 609 SO4 A O3  1 
HETATM 8423 O  O4  . SO4 K 6 .   ? -64.401  34.661  281.230 1.00 44.02  ? 609 SO4 A O4  1 
HETATM 8424 C  C1  . NAG L 2 .   ? -52.815  -19.015 278.614 1.00 60.90  ? 601 NAG B C1  1 
HETATM 8425 C  C2  . NAG L 2 .   ? -53.971  -19.125 279.607 1.00 37.10  ? 601 NAG B C2  1 
HETATM 8426 C  C3  . NAG L 2 .   ? -55.106  -18.185 279.209 1.00 34.41  ? 601 NAG B C3  1 
HETATM 8427 C  C4  . NAG L 2 .   ? -54.586  -16.767 279.017 1.00 33.29  ? 601 NAG B C4  1 
HETATM 8428 C  C5  . NAG L 2 .   ? -53.411  -16.765 278.044 1.00 42.51  ? 601 NAG B C5  1 
HETATM 8429 C  C6  . NAG L 2 .   ? -52.770  -15.406 277.890 1.00 34.73  ? 601 NAG B C6  1 
HETATM 8430 C  C7  . NAG L 2 .   ? -54.452  -21.199 280.830 1.00 38.25  ? 601 NAG B C7  1 
HETATM 8431 C  C8  . NAG L 2 .   ? -54.981  -22.598 280.735 1.00 41.84  ? 601 NAG B C8  1 
HETATM 8432 N  N2  . NAG L 2 .   ? -54.450  -20.495 279.694 1.00 36.16  ? 601 NAG B N2  1 
HETATM 8433 O  O1  . NAG L 2 .   ? -51.764  -19.817 279.041 1.00 42.08  ? 601 NAG B O1  1 
HETATM 8434 O  O3  . NAG L 2 .   ? -56.108  -18.200 280.219 1.00 33.01  ? 601 NAG B O3  1 
HETATM 8435 O  O4  . NAG L 2 .   ? -55.620  -15.933 278.507 1.00 33.94  ? 601 NAG B O4  1 
HETATM 8436 O  O5  . NAG L 2 .   ? -52.390  -17.654 278.519 1.00 60.04  ? 601 NAG B O5  1 
HETATM 8437 O  O6  . NAG L 2 .   ? -53.146  -14.789 276.666 1.00 37.41  ? 601 NAG B O6  1 
HETATM 8438 O  O7  . NAG L 2 .   ? -54.046  -20.728 281.888 1.00 57.62  ? 601 NAG B O7  1 
HETATM 8439 C  C1  . NAG M 2 .   ? -39.581  -19.300 277.232 1.00 54.95  ? 602 NAG B C1  1 
HETATM 8440 C  C2  . NAG M 2 .   ? -38.470  -18.249 277.249 1.00 59.02  ? 602 NAG B C2  1 
HETATM 8441 C  C3  . NAG M 2 .   ? -38.249  -17.731 278.669 1.00 52.17  ? 602 NAG B C3  1 
HETATM 8442 C  C4  . NAG M 2 .   ? -39.563  -17.261 279.278 1.00 44.89  ? 602 NAG B C4  1 
HETATM 8443 C  C5  . NAG M 2 .   ? -40.611  -18.364 279.179 1.00 46.26  ? 602 NAG B C5  1 
HETATM 8444 C  C6  . NAG M 2 .   ? -41.973  -17.934 279.670 1.00 47.00  ? 602 NAG B C6  1 
HETATM 8445 C  C7  . NAG M 2 .   ? -36.272  -18.039 276.170 1.00 77.22  ? 602 NAG B C7  1 
HETATM 8446 C  C8  . NAG M 2 .   ? -35.069  -18.773 275.660 1.00 62.64  ? 602 NAG B C8  1 
HETATM 8447 N  N2  . NAG M 2 .   ? -37.236  -18.795 276.707 1.00 89.59  ? 602 NAG B N2  1 
HETATM 8448 O  O1  . NAG M 2 .   ? -39.825  -19.690 275.920 1.00 52.21  ? 602 NAG B O1  1 
HETATM 8449 O  O3  . NAG M 2 .   ? -37.318  -16.655 278.645 1.00 68.19  ? 602 NAG B O3  1 
HETATM 8450 O  O4  . NAG M 2 .   ? -39.369  -16.915 280.645 1.00 48.46  ? 602 NAG B O4  1 
HETATM 8451 O  O5  . NAG M 2 .   ? -40.768  -18.755 277.808 1.00 62.86  ? 602 NAG B O5  1 
HETATM 8452 O  O6  . NAG M 2 .   ? -42.317  -18.588 280.884 1.00 47.25  ? 602 NAG B O6  1 
HETATM 8453 O  O7  . NAG M 2 .   ? -36.368  -16.818 276.097 1.00 63.24  ? 602 NAG B O7  1 
HETATM 8454 C  C1  . NAG N 2 .   ? -35.826  -29.169 295.574 1.00 53.24  ? 603 NAG B C1  1 
HETATM 8455 C  C2  . NAG N 2 .   ? -35.760  -28.875 294.075 1.00 38.51  ? 603 NAG B C2  1 
HETATM 8456 C  C3  . NAG N 2 .   ? -34.535  -29.543 293.455 1.00 44.11  ? 603 NAG B C3  1 
HETATM 8457 C  C4  . NAG N 2 .   ? -33.271  -29.141 294.203 1.00 37.61  ? 603 NAG B C4  1 
HETATM 8458 C  C5  . NAG N 2 .   ? -33.426  -29.451 295.687 1.00 36.14  ? 603 NAG B C5  1 
HETATM 8459 C  C6  . NAG N 2 .   ? -32.255  -28.979 296.515 1.00 38.24  ? 603 NAG B C6  1 
HETATM 8460 C  C7  . NAG N 2 .   ? -37.476  -28.717 292.325 1.00 40.43  ? 603 NAG B C7  1 
HETATM 8461 C  C8  . NAG N 2 .   ? -38.732  -29.314 291.767 1.00 42.29  ? 603 NAG B C8  1 
HETATM 8462 N  N2  . NAG N 2 .   ? -36.973  -29.319 293.407 1.00 39.09  ? 603 NAG B N2  1 
HETATM 8463 O  O3  . NAG N 2 .   ? -34.428  -29.169 292.086 1.00 52.64  ? 603 NAG B O3  1 
HETATM 8464 O  O4  . NAG N 2 .   ? -32.153  -29.853 293.688 1.00 38.64  ? 603 NAG B O4  1 
HETATM 8465 O  O5  . NAG N 2 .   ? -34.587  -28.783 296.201 1.00 38.65  ? 603 NAG B O5  1 
HETATM 8466 O  O6  . NAG N 2 .   ? -32.686  -28.422 297.749 1.00 44.06  ? 603 NAG B O6  1 
HETATM 8467 O  O7  . NAG N 2 .   ? -36.941  -27.736 291.820 1.00 43.52  ? 603 NAG B O7  1 
HETATM 8468 C  C1  . SN5 O 3 .   ? -58.785  -14.981 278.521 1.00 34.17  ? 604 SN5 B C1  1 
HETATM 8469 S  S7  . SN5 O 3 .   ? -59.386  -13.372 282.217 1.00 29.43  ? 604 SN5 B S7  1 
HETATM 8470 C  C2  . SN5 O 3 .   ? -59.590  -15.196 279.750 1.00 35.39  ? 604 SN5 B C2  1 
HETATM 8471 C  C3  . SN5 O 3 .   ? -60.571  -16.264 279.607 1.00 32.24  ? 604 SN5 B C3  1 
HETATM 8472 C  C4  . SN5 O 3 .   ? -61.444  -16.070 278.428 1.00 37.72  ? 604 SN5 B C4  1 
HETATM 8473 C  C5  . SN5 O 3 .   ? -60.626  -15.951 277.131 1.00 36.36  ? 604 SN5 B C5  1 
HETATM 8474 C  C6  . SN5 O 3 .   ? -61.480  -15.654 276.037 1.00 30.97  ? 604 SN5 B C6  1 
HETATM 8475 C  C7  . SN5 O 3 .   ? -58.704  -14.825 282.157 1.00 40.31  ? 604 SN5 B C7  1 
HETATM 8476 C  C8  . SN5 O 3 .   ? -58.122  -15.443 283.413 1.00 41.72  ? 604 SN5 B C8  1 
HETATM 8477 N  N2  . SN5 O 3 .   ? -58.643  -15.559 280.891 1.00 41.17  ? 604 SN5 B N2  1 
HETATM 8478 O  O3  . SN5 O 3 .   ? -61.424  -16.313 280.830 1.00 35.93  ? 604 SN5 B O3  1 
HETATM 8479 O  O4  . SN5 O 3 .   ? -62.350  -17.193 278.320 1.00 72.23  ? 604 SN5 B O4  1 
HETATM 8480 O  O5  . SN5 O 3 .   ? -59.619  -14.804 277.336 1.00 37.79  ? 604 SN5 B O5  1 
HETATM 8481 O  O6  . SN5 O 3 .   ? -60.724  -15.506 274.885 1.00 31.12  ? 604 SN5 B O6  1 
HETATM 8482 C  C1  . 58Y P 4 .   ? -55.441  -11.478 276.850 1.00 24.11  ? 605 58Y B C1  1 
HETATM 8483 C  C2  . 58Y P 4 .   ? -56.396  -12.139 276.027 1.00 24.99  ? 605 58Y B C2  1 
HETATM 8484 C  C3  . 58Y P 4 .   ? -57.688  -12.309 276.704 1.00 28.26  ? 605 58Y B C3  1 
HETATM 8485 C  C4  . 58Y P 4 .   ? -57.608  -12.858 278.134 1.00 29.53  ? 605 58Y B C4  1 
HETATM 8486 C  C5  . 58Y P 4 .   ? -56.440  -12.305 278.964 1.00 29.98  ? 605 58Y B C5  1 
HETATM 8487 C  C6  . 58Y P 4 .   ? -56.203  -13.215 280.211 1.00 30.26  ? 605 58Y B C6  1 
HETATM 8488 C  C7  . 58Y P 4 .   ? -56.345  -9.753  275.271 1.00 21.55  ? 605 58Y B C7  1 
HETATM 8489 C  C8  . 58Y P 4 .   ? -57.496  -8.728  275.142 1.00 19.23  ? 605 58Y B C8  1 
HETATM 8490 N  N2  . 58Y P 4 .   ? -56.788  -11.075 274.845 1.00 23.74  ? 605 58Y B N2  1 
HETATM 8491 S  S1  . 58Y P 4 .   ? -55.908  -9.929  276.817 1.00 29.14  ? 605 58Y B S1  1 
HETATM 8492 O  O3  . 58Y P 4 .   ? -58.497  -13.200 275.902 1.00 40.19  ? 605 58Y B O3  1 
HETATM 8493 O  O4  . 58Y P 4 .   ? -57.592  -14.274 278.118 1.00 30.81  ? 605 58Y B O4  1 
HETATM 8494 O  O5  . 58Y P 4 .   ? -55.283  -12.222 278.301 1.00 26.00  ? 605 58Y B O5  1 
HETATM 8495 O  O6  . 58Y P 4 .   ? -54.921  -13.788 280.085 1.00 30.67  ? 605 58Y B O6  1 
HETATM 8496 S  S   . SO4 Q 6 .   ? -69.238  -5.017  292.714 1.00 72.46  ? 606 SO4 B S   1 
HETATM 8497 O  O1  . SO4 Q 6 .   ? -68.234  -5.034  291.654 1.00 49.59  ? 606 SO4 B O1  1 
HETATM 8498 O  O2  . SO4 Q 6 .   ? -70.570  -5.092  292.120 1.00 63.28  ? 606 SO4 B O2  1 
HETATM 8499 O  O3  . SO4 Q 6 .   ? -69.035  -6.160  293.598 1.00 58.73  ? 606 SO4 B O3  1 
HETATM 8500 O  O4  . SO4 Q 6 .   ? -69.113  -3.781  293.480 1.00 54.42  ? 606 SO4 B O4  1 
HETATM 8501 S  S   . SO4 R 6 .   ? -74.423  -9.362  256.633 1.00 51.69  ? 607 SO4 B S   1 
HETATM 8502 O  O1  . SO4 R 6 .   ? -73.398  -8.980  255.667 1.00 44.74  ? 607 SO4 B O1  1 
HETATM 8503 O  O2  . SO4 R 6 .   ? -75.426  -10.195 255.976 1.00 44.55  ? 607 SO4 B O2  1 
HETATM 8504 O  O3  . SO4 R 6 .   ? -73.807  -10.110 257.723 1.00 44.32  ? 607 SO4 B O3  1 
HETATM 8505 O  O4  . SO4 R 6 .   ? -75.063  -8.163  257.167 1.00 61.44  ? 607 SO4 B O4  1 
HETATM 8506 O  O   . HOH S 7 .   ? -90.610  7.735   302.940 1.00 14.74  ? 701 HOH A O   1 
HETATM 8507 O  O   . HOH S 7 .   ? -128.915 28.225  292.534 1.00 21.38  ? 702 HOH A O   1 
HETATM 8508 O  O   . HOH S 7 .   ? -93.982  -0.761  295.379 1.00 12.16  ? 703 HOH A O   1 
HETATM 8509 O  O   . HOH S 7 .   ? -85.022  4.399   288.636 1.00 13.29  ? 704 HOH A O   1 
HETATM 8510 O  O   . HOH T 7 .   ? -61.413  1.135   287.922 1.00 26.87  ? 701 HOH B O   1 
HETATM 8511 O  O   . HOH T 7 .   ? -41.576  -12.028 283.614 1.00 25.14  ? 702 HOH B O   1 
HETATM 8512 O  O   . HOH T 7 .   ? -83.203  -18.292 266.010 1.00 21.33  ? 703 HOH B O   1 
HETATM 8513 O  O   . HOH T 7 .   ? -51.469  -1.436  295.485 1.00 19.02  ? 704 HOH B O   1 
HETATM 8514 O  O   . HOH T 7 .   ? -83.910  1.528   284.653 1.00 27.81  ? 705 HOH B O   1 
HETATM 8515 O  O   . HOH T 7 .   ? -39.636  12.072  285.273 1.00 18.00  ? 706 HOH B O   1 
HETATM 8516 O  O   . HOH T 7 .   ? -36.433  3.204   280.311 1.00 32.72  ? 707 HOH B O   1 
HETATM 8517 O  O   . HOH T 7 .   ? -85.827  2.156   282.921 1.00 33.51  ? 708 HOH B O   1 
HETATM 8518 O  O   . HOH T 7 .   ? -56.558  4.774   263.254 1.00 28.77  ? 709 HOH B O   1 
HETATM 8519 O  O   . HOH T 7 .   ? -57.791  -27.573 262.652 1.00 17.83  ? 710 HOH B O   1 
HETATM 8520 O  O   . HOH T 7 .   ? -35.071  -5.238  273.153 1.00 39.66  ? 711 HOH B O   1 
HETATM 8521 O  O   . HOH T 7 .   ? -65.173  -1.578  249.816 1.00 21.49  ? 712 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   ?   ?   ?   A . n 
A 1 8   VAL 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  TRP 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  VAL 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  VAL 14  14  ?   ?   ?   A . n 
A 1 15  SER 15  15  ?   ?   ?   A . n 
A 1 16  ASN 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  TRP 26  26  26  TRP TRP 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  ARG 29  29  29  ARG ARG A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  ASN 60  60  60  ASN ASN A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  TRP 62  62  62  TRP TRP A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  GLN 78  78  78  GLN GLN A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  TRP 80  80  80  TRP TRP A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 MET 101 101 101 MET MET A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 CYS 106 106 106 CYS CYS A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 TRP 136 136 136 TRP TRP A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 TYR 153 153 153 TYR TYR A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 TRP 157 157 157 TRP TRP A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ARG 162 162 162 ARG ARG A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 HIS 176 176 176 HIS HIS A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 TYR 179 179 179 TYR TYR A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 CYS 185 185 185 CYS CYS A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 ASN 191 191 191 ASN ASN A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 GLN 205 205 205 GLN GLN A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 CYS 208 208 208 CYS CYS A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 HIS 219 219 219 HIS HIS A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 PRO 221 221 221 PRO PRO A . n 
A 1 222 TRP 222 222 222 TRP TRP A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 GLN 226 226 226 GLN GLN A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 TRP 235 235 235 TRP TRP A . n 
A 1 236 ASN 236 236 236 ASN ASN A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 MET 247 247 247 MET MET A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 PRO 260 260 260 PRO PRO A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 TRP 265 265 265 TRP TRP A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ASP 269 269 269 ASP ASP A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 TYR 272 272 272 TYR TYR A . n 
A 1 273 PHE 273 273 273 PHE PHE A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 HIS 275 275 275 HIS HIS A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ASP 285 285 285 ASP ASP A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 PHE 290 290 290 PHE PHE A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 TRP 294 294 294 TRP TRP A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ASP 298 298 298 ASP ASP A . n 
A 1 299 GLY 299 299 299 GLY GLY A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ASP 303 303 303 ASP ASP A . n 
A 1 304 TRP 304 304 304 TRP TRP A . n 
A 1 305 GLU 305 305 305 GLU GLU A . n 
A 1 306 PHE 306 306 306 PHE PHE A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 ASN 313 313 313 ASN ASN A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 SER 315 315 315 SER SER A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ARG 321 321 321 ARG ARG A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 LYS 324 324 324 LYS LYS A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 GLU 332 332 332 GLU GLU A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 ARG 334 334 334 ARG ARG A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 MET 336 336 336 MET MET A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 GLN 343 343 343 GLN GLN A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 TYR 348 348 348 TYR TYR A . n 
A 1 349 GLU 349 349 349 GLU GLU A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 SER 352 352 352 SER SER A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 ILE 354 354 354 ILE ILE A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 TYR 358 358 358 TYR TYR A . n 
A 1 359 ASP 359 359 359 ASP ASP A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 ILE 361 361 361 ILE ILE A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 TYR 366 366 366 TYR TYR A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 LYS 371 371 371 LYS LYS A . n 
A 1 372 SER 372 372 372 SER SER A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 ILE 376 376 376 ILE ILE A . n 
A 1 377 PHE 377 377 377 PHE PHE A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 MET 379 379 379 MET MET A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 TYR 381 381 381 TYR TYR A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 PHE 383 383 383 PHE PHE A . n 
A 1 384 LYS 384 384 384 LYS LYS A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 ALA 386 386 386 ALA ALA A . n 
A 1 387 TRP 387 387 387 TRP TRP A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 ASN 389 389 389 ASN ASN A . n 
A 1 390 THR 390 390 390 THR THR A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 TYR 394 394 394 TYR TYR A . n 
A 1 395 GLN 395 395 395 GLN GLN A . n 
A 1 396 THR 396 396 396 THR THR A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 PRO 401 401 401 PRO PRO A . n 
A 1 402 SER 402 402 402 SER SER A . n 
A 1 403 TRP 403 403 403 TRP TRP A . n 
A 1 404 ASN 404 404 404 ASN ASN A . n 
A 1 405 SER 405 405 405 SER SER A . n 
A 1 406 GLU 406 406 406 GLU GLU A . n 
A 1 407 GLU 407 407 407 GLU GLU A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 TYR 409 409 409 TYR TYR A . n 
A 1 410 THR 410 410 410 THR THR A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 HIS 412 412 412 HIS HIS A . n 
A 1 413 TYR 413 413 413 TYR TYR A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 VAL 415 415 415 VAL VAL A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 GLN 421 421 421 GLN GLN A . n 
A 1 422 GLY 422 422 422 GLY GLY A . n 
A 1 423 VAL 423 423 423 VAL VAL A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 PRO 425 425 425 PRO PRO A . n 
A 1 426 ASN 426 426 426 ASN ASN A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 ILE 429 429 429 ILE ILE A . n 
A 1 430 VAL 430 430 430 VAL VAL A . n 
A 1 431 GLY 431 431 431 GLY GLY A . n 
A 1 432 VAL 432 432 432 VAL VAL A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 MET 434 434 434 MET MET A . n 
A 1 435 TYR 435 435 435 TYR TYR A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 GLY 438 438 438 GLY GLY A . n 
A 1 439 TRP 439 439 439 TRP TRP A . n 
A 1 440 THR 440 440 440 THR THR A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 VAL 442 442 442 VAL VAL A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 THR 446 446 446 THR THR A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 ASN 449 449 449 ASN ASN A . n 
A 1 450 TYR 450 450 450 TYR TYR A . n 
A 1 451 PHE 451 451 451 PHE PHE A . n 
A 1 452 SER 452 452 452 SER SER A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 THR 454 454 454 THR THR A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 PRO 458 458 458 PRO PRO A . n 
A 1 459 VAL 459 459 459 VAL VAL A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 THR 462 462 462 THR THR A . n 
A 1 463 TRP 463 463 463 TRP TRP A . n 
A 1 464 GLU 464 464 464 GLU GLU A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 VAL 467 467 467 VAL VAL A . n 
A 1 468 VAL 468 468 468 VAL VAL A . n 
A 1 469 ASP 469 469 469 ASP ASP A . n 
A 1 470 TYR 470 470 470 TYR TYR A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 GLN 472 472 472 GLN GLN A . n 
A 1 473 ILE 473 473 473 ILE ILE A . n 
A 1 474 GLN 474 474 474 GLN GLN A . n 
A 1 475 LYS 475 475 475 LYS LYS A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 ASN 478 478 478 ASN ASN A . n 
A 1 479 ASN 479 479 479 ASN ASN A . n 
A 1 480 TYR 480 480 480 TYR TYR A . n 
A 1 481 VAL 481 481 481 VAL VAL A . n 
A 1 482 TYR 482 482 482 TYR TYR A . n 
A 1 483 THR 483 483 483 THR THR A . n 
A 1 484 PHE 484 484 484 PHE PHE A . n 
A 1 485 ASP 485 485 485 ASP ASP A . n 
A 1 486 SER 486 486 486 SER SER A . n 
A 1 487 ALA 487 487 487 ALA ALA A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 GLN 489 489 489 GLN GLN A . n 
A 1 490 ALA 490 490 490 ALA ALA A . n 
A 1 491 SER 491 491 491 SER SER A . n 
A 1 492 TYR 492 492 492 TYR TYR A . n 
A 1 493 VAL 493 493 493 VAL VAL A . n 
A 1 494 PHE 494 494 494 PHE PHE A . n 
A 1 495 ASP 495 495 495 ASP ASP A . n 
A 1 496 LYS 496 496 496 LYS LYS A . n 
A 1 497 SER 497 497 497 SER SER A . n 
A 1 498 LYS 498 498 498 LYS LYS A . n 
A 1 499 GLY 499 499 499 GLY GLY A . n 
A 1 500 ASP 500 500 500 ASP ASP A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 ILE 502 502 502 ILE ILE A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 PHE 504 504 504 PHE PHE A . n 
A 1 505 ASP 505 505 505 ASP ASP A . n 
A 1 506 SER 506 506 506 SER SER A . n 
A 1 507 VAL 507 507 507 VAL VAL A . n 
A 1 508 ASP 508 508 508 ASP ASP A . n 
A 1 509 SER 509 509 509 SER SER A . n 
A 1 510 VAL 510 510 510 VAL VAL A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 LYS 513 513 513 LYS LYS A . n 
A 1 514 VAL 514 514 514 VAL VAL A . n 
A 1 515 LYS 515 515 515 LYS LYS A . n 
A 1 516 TYR 516 516 516 TYR TYR A . n 
A 1 517 VAL 517 517 517 VAL VAL A . n 
A 1 518 ASP 518 518 518 ASP ASP A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 ASN 520 520 520 ASN ASN A . n 
A 1 521 LYS 521 521 521 LYS LYS A . n 
A 1 522 LEU 522 522 522 LEU LEU A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 GLY 524 524 524 GLY GLY A . n 
A 1 525 LEU 525 525 525 LEU LEU A . n 
A 1 526 PHE 526 526 526 PHE PHE A . n 
A 1 527 ALA 527 527 527 ALA ALA A . n 
A 1 528 TRP 528 528 528 TRP TRP A . n 
A 1 529 GLU 529 529 529 GLU GLU A . n 
A 1 530 ILE 530 530 530 ILE ILE A . n 
A 1 531 ASP 531 531 531 ASP ASP A . n 
A 1 532 ALA 532 532 532 ALA ALA A . n 
A 1 533 ASP 533 533 533 ASP ASP A . n 
A 1 534 ASN 534 534 534 ASN ASN A . n 
A 1 535 GLY 535 535 535 GLY GLY A . n 
A 1 536 ASP 536 536 536 ASP ASP A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 LEU 538 538 538 LEU LEU A . n 
A 1 539 ASN 539 539 539 ASN ASN A . n 
A 1 540 ALA 540 540 540 ALA ALA A . n 
A 1 541 ILE 541 541 541 ILE ILE A . n 
A 1 542 ASN 542 542 542 ASN ASN A . n 
A 1 543 ALA 543 543 543 ALA ALA A . n 
A 1 544 GLN 544 544 544 GLN GLN A . n 
A 1 545 PHE 545 545 545 PHE PHE A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LEU 2   2   ?   ?   ?   B . n 
B 1 3   TYR 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   LEU 5   5   ?   ?   ?   B . n 
B 1 6   LEU 6   6   ?   ?   ?   B . n 
B 1 7   ASN 7   7   ?   ?   ?   B . n 
B 1 8   VAL 8   8   ?   ?   ?   B . n 
B 1 9   LEU 9   9   ?   ?   ?   B . n 
B 1 10  TRP 10  10  ?   ?   ?   B . n 
B 1 11  LEU 11  11  ?   ?   ?   B . n 
B 1 12  VAL 12  12  ?   ?   ?   B . n 
B 1 13  ALA 13  13  ?   ?   ?   B . n 
B 1 14  VAL 14  14  ?   ?   ?   B . n 
B 1 15  SER 15  15  ?   ?   ?   B . n 
B 1 16  ASN 16  16  ?   ?   ?   B . n 
B 1 17  ALA 17  17  ?   ?   ?   B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  PRO 19  19  19  PRO PRO B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  PRO 22  22  22  PRO PRO B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  TRP 26  26  26  TRP TRP 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  ARG 29  29  29  ARG ARG B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  TYR 31  31  31  TYR TYR B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  THR 41  41  41  THR THR B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  TYR 43  43  43  TYR TYR B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  PRO 49  49  49  PRO PRO B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  GLN 52  52  52  GLN GLN B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  GLN 56  56  56  GLN GLN B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  TRP 59  59  59  TRP TRP B . n 
B 1 60  ASN 60  60  60  ASN ASN B . n 
B 1 61  VAL 61  61  61  VAL VAL B . n 
B 1 62  TRP 62  62  62  TRP TRP B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ILE 66  66  66  ILE ILE B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  GLN 77  77  77  GLN GLN B . n 
B 1 78  GLN 78  78  78  GLN GLN B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  TRP 80  80  80  TRP TRP B . n 
B 1 81  LYS 81  81  81  LYS LYS B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  PHE 99  99  99  PHE PHE B . n 
B 1 100 ASN 100 100 100 ASN ASN B . n 
B 1 101 MET 101 101 101 MET MET B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LYS 104 104 104 LYS LYS B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 CYS 106 106 106 CYS CYS B . n 
B 1 107 ASN 107 107 107 ASN ASN B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 SER 114 114 114 SER SER B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 PRO 116 116 116 PRO PRO B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 ASP 123 123 123 ASP ASP B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 GLY 126 126 126 GLY GLY B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 HIS 128 128 128 HIS HIS B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 PRO 131 131 131 PRO PRO B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 TRP 136 136 136 TRP TRP B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ASN 140 140 140 ASN ASN B . n 
B 1 141 LYS 141 141 141 LYS LYS B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 ARG 145 145 145 ARG ARG B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 TYR 153 153 153 TYR TYR B . n 
B 1 154 PHE 154 154 154 PHE PHE B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 GLU 156 156 156 GLU GLU B . n 
B 1 157 TRP 157 157 157 TRP TRP B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 ARG 162 162 162 ARG ARG B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 PHE 164 164 164 PHE PHE B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 VAL 166 166 166 VAL VAL B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 ASN 173 173 173 ASN ASN B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 HIS 176 176 176 HIS HIS B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 TYR 179 179 179 TYR TYR B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 PRO 183 183 183 PRO PRO B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 CYS 185 185 185 CYS CYS B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 ILE 190 190 190 ILE ILE B . n 
B 1 191 ASN 191 191 191 ASN ASN B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 LEU 194 194 194 LEU LEU B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ILE 197 197 197 ILE ILE B . n 
B 1 198 SER 198 198 198 SER SER B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 PHE 201 201 201 PHE PHE B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 SER 203 203 203 SER SER B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 GLN 205 205 205 GLN GLN B . n 
B 1 206 ARG 206 206 206 ARG ARG B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 CYS 208 208 208 CYS CYS B . n 
B 1 209 LYS 209 209 209 LYS LYS B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 ARG 211 211 211 ARG ARG B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 PHE 214 214 214 PHE PHE B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 HIS 219 219 219 HIS HIS B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 PRO 221 221 221 PRO PRO B . n 
B 1 222 TRP 222 222 222 TRP TRP B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 GLN 226 226 226 GLN GLN B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 PRO 228 228 228 PRO PRO B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 LYS 230 230 230 LYS LYS B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 TRP 235 235 235 TRP TRP B . n 
B 1 236 ASN 236 236 236 ASN ASN B . n 
B 1 237 GLU 237 237 237 GLU GLU B . n 
B 1 238 PRO 238 238 238 PRO PRO B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 GLY 244 244 244 GLY GLY B . n 
B 1 245 GLN 245 245 245 GLN GLN B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 MET 247 247 247 MET MET B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 LYS 257 257 257 LYS LYS B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 PRO 260 260 260 PRO PRO B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 ILE 262 262 262 ILE ILE B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 TRP 265 265 265 TRP TRP B . n 
B 1 266 THR 266 266 266 THR THR B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 SER 268 268 268 SER SER B . n 
B 1 269 ASP 269 269 269 ASP ASP B . n 
B 1 270 PRO 270 270 270 PRO PRO B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 TYR 272 272 272 TYR TYR B . n 
B 1 273 PHE 273 273 273 PHE PHE B . n 
B 1 274 MET 274 274 274 MET MET B . n 
B 1 275 HIS 275 275 275 HIS HIS B . n 
B 1 276 ASP 276 276 276 ASP ASP B . n 
B 1 277 VAL 277 277 277 VAL VAL B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 LYS 279 279 279 LYS LYS B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 ASN 281 281 281 ASN ASN B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 PHE 283 283 283 PHE PHE B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 ASP 285 285 285 ASP ASP B . n 
B 1 286 SER 286 286 286 SER SER B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 LYS 288 288 288 LYS LYS B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 PHE 290 290 290 PHE PHE B . n 
B 1 291 LEU 291 291 291 LEU LEU B . n 
B 1 292 GLN 292 292 292 GLN GLN B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 TRP 294 294 294 TRP TRP B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 PHE 296 296 296 PHE PHE B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 ASP 298 298 298 ASP ASP B . n 
B 1 299 GLY 299 299 299 GLY GLY B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 ASP 301 301 301 ASP ASP B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 ASP 303 303 303 ASP ASP B . n 
B 1 304 TRP 304 304 304 TRP TRP B . n 
B 1 305 GLU 305 305 305 GLU GLU B . n 
B 1 306 PHE 306 306 306 PHE PHE B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 GLY 311 311 311 GLY GLY B . n 
B 1 312 ALA 312 312 312 ALA ALA B . n 
B 1 313 ASN 313 313 313 ASN ASN B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 SER 315 315 315 SER SER B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 GLY 317 317 317 GLY GLY B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 ALA 319 319 319 ALA ALA B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 ARG 321 321 321 ARG ARG B . n 
B 1 322 ASP 322 322 322 ASP ASP B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 LYS 324 324 324 LYS LYS B . n 
B 1 325 THR 325 325 325 THR THR B . n 
B 1 326 TYR 326 326 326 TYR TYR B . n 
B 1 327 ILE 327 327 327 ILE ILE B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 LEU 330 330 330 LEU LEU B . n 
B 1 331 GLU 331 331 331 GLU GLU B . n 
B 1 332 GLU 332 332 332 GLU GLU B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 ARG 334 334 334 ARG ARG B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 MET 336 336 336 MET MET B . n 
B 1 337 LEU 337 337 337 LEU LEU B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 ASP 339 339 339 ASP ASP B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 GLU 341 341 341 GLU GLU B . n 
B 1 342 ALA 342 342 342 ALA ALA B . n 
B 1 343 GLN 343 343 343 GLN GLN B . n 
B 1 344 THR 344 344 344 THR THR B . n 
B 1 345 GLY 345 345 345 GLY GLY B . n 
B 1 346 ARG 346 346 346 ARG ARG B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 TYR 348 348 348 TYR TYR B . n 
B 1 349 GLU 349 349 349 GLU GLU B . n 
B 1 350 LEU 350 350 350 LEU LEU B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 SER 352 352 352 SER SER B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 ILE 354 354 354 ILE ILE B . n 
B 1 355 SER 355 355 355 SER SER B . n 
B 1 356 ALA 356 356 356 ALA ALA B . n 
B 1 357 GLY 357 357 357 GLY GLY B . n 
B 1 358 TYR 358 358 358 TYR TYR B . n 
B 1 359 ASP 359 359 359 ASP ASP B . n 
B 1 360 LYS 360 360 360 LYS LYS B . n 
B 1 361 ILE 361 361 361 ILE ILE B . n 
B 1 362 ALA 362 362 362 ALA ALA B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 VAL 364 364 364 VAL VAL B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 TYR 366 366 366 TYR TYR B . n 
B 1 367 ALA 367 367 367 ALA ALA B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 GLN 370 370 370 GLN GLN B . n 
B 1 371 LYS 371 371 371 LYS LYS B . n 
B 1 372 SER 372 372 372 SER SER B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 LYS 375 375 375 LYS LYS B . n 
B 1 376 ILE 376 376 376 ILE ILE B . n 
B 1 377 PHE 377 377 377 PHE PHE B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 MET 379 379 379 MET MET B . n 
B 1 380 SER 380 380 380 SER SER B . n 
B 1 381 TYR 381 381 381 TYR TYR B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 PHE 383 383 383 PHE PHE B . n 
B 1 384 LYS 384 384 384 LYS LYS B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 ALA 386 386 386 ALA ALA B . n 
B 1 387 TRP 387 387 387 TRP TRP B . n 
B 1 388 SER 388 388 388 SER SER B . n 
B 1 389 ASN 389 389 389 ASN ASN B . n 
B 1 390 THR 390 390 390 THR THR B . n 
B 1 391 ASP 391 391 391 ASP ASP B . n 
B 1 392 LEU 392 392 392 LEU LEU B . n 
B 1 393 GLY 393 393 393 GLY GLY B . n 
B 1 394 TYR 394 394 394 TYR TYR B . n 
B 1 395 GLN 395 395 395 GLN GLN B . n 
B 1 396 THR 396 396 396 THR THR B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 VAL 398 398 398 VAL VAL B . n 
B 1 399 TYR 399 399 399 TYR TYR B . n 
B 1 400 ALA 400 400 400 ALA ALA B . n 
B 1 401 PRO 401 401 401 PRO PRO B . n 
B 1 402 SER 402 402 402 SER SER B . n 
B 1 403 TRP 403 403 403 TRP TRP B . n 
B 1 404 ASN 404 404 404 ASN ASN B . n 
B 1 405 SER 405 405 405 SER SER B . n 
B 1 406 GLU 406 406 406 GLU GLU B . n 
B 1 407 GLU 407 407 407 GLU GLU B . n 
B 1 408 LEU 408 408 408 LEU LEU B . n 
B 1 409 TYR 409 409 409 TYR TYR B . n 
B 1 410 THR 410 410 410 THR THR B . n 
B 1 411 THR 411 411 411 THR THR B . n 
B 1 412 HIS 412 412 412 HIS HIS B . n 
B 1 413 TYR 413 413 413 TYR TYR B . n 
B 1 414 ALA 414 414 414 ALA ALA B . n 
B 1 415 VAL 415 415 415 VAL VAL B . n 
B 1 416 ASP 416 416 416 ASP ASP B . n 
B 1 417 ALA 417 417 417 ALA ALA B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 LEU 419 419 419 LEU LEU B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 GLN 421 421 421 GLN GLN B . n 
B 1 422 GLY 422 422 422 GLY GLY B . n 
B 1 423 VAL 423 423 423 VAL VAL B . n 
B 1 424 ASP 424 424 424 ASP ASP B . n 
B 1 425 PRO 425 425 425 PRO PRO B . n 
B 1 426 ASN 426 426 426 ASN ASN B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 ILE 429 429 429 ILE ILE B . n 
B 1 430 VAL 430 430 430 VAL VAL B . n 
B 1 431 GLY 431 431 431 GLY GLY B . n 
B 1 432 VAL 432 432 432 VAL VAL B . n 
B 1 433 ALA 433 433 433 ALA ALA B . n 
B 1 434 MET 434 434 434 MET MET B . n 
B 1 435 TYR 435 435 435 TYR TYR B . n 
B 1 436 GLY 436 436 436 GLY GLY B . n 
B 1 437 ARG 437 437 437 ARG ARG B . n 
B 1 438 GLY 438 438 438 GLY GLY B . n 
B 1 439 TRP 439 439 439 TRP TRP B . n 
B 1 440 THR 440 440 440 THR THR B . n 
B 1 441 GLY 441 441 441 GLY GLY B . n 
B 1 442 VAL 442 442 442 VAL VAL B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 ASN 444 444 444 ASN ASN B . n 
B 1 445 TYR 445 445 445 TYR TYR B . n 
B 1 446 THR 446 446 446 THR THR B . n 
B 1 447 ASN 447 447 447 ASN ASN B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 ASN 449 449 449 ASN ASN B . n 
B 1 450 TYR 450 450 450 TYR TYR B . n 
B 1 451 PHE 451 451 451 PHE PHE B . n 
B 1 452 SER 452 452 452 SER SER B . n 
B 1 453 GLY 453 453 453 GLY GLY B . n 
B 1 454 THR 454 454 454 THR THR B . n 
B 1 455 GLY 455 455 455 GLY GLY B . n 
B 1 456 ASN 456 456 456 ASN ASN B . n 
B 1 457 GLY 457 457 457 GLY GLY B . n 
B 1 458 PRO 458 458 458 PRO PRO B . n 
B 1 459 VAL 459 459 459 VAL VAL B . n 
B 1 460 SER 460 460 460 SER SER B . n 
B 1 461 GLY 461 461 461 GLY GLY B . n 
B 1 462 THR 462 462 462 THR THR B . n 
B 1 463 TRP 463 463 463 TRP TRP B . n 
B 1 464 GLU 464 464 464 GLU GLU B . n 
B 1 465 ASP 465 465 465 ASP ASP B . n 
B 1 466 GLY 466 466 466 GLY GLY B . n 
B 1 467 VAL 467 467 467 VAL VAL B . n 
B 1 468 VAL 468 468 468 VAL VAL B . n 
B 1 469 ASP 469 469 469 ASP ASP B . n 
B 1 470 TYR 470 470 470 TYR TYR B . n 
B 1 471 ARG 471 471 471 ARG ARG B . n 
B 1 472 GLN 472 472 472 GLN GLN B . n 
B 1 473 ILE 473 473 473 ILE ILE B . n 
B 1 474 GLN 474 474 474 GLN GLN B . n 
B 1 475 LYS 475 475 475 LYS LYS B . n 
B 1 476 ASP 476 476 476 ASP ASP B . n 
B 1 477 LEU 477 477 477 LEU LEU B . n 
B 1 478 ASN 478 478 478 ASN ASN B . n 
B 1 479 ASN 479 479 479 ASN ASN B . n 
B 1 480 TYR 480 480 480 TYR TYR B . n 
B 1 481 VAL 481 481 481 VAL VAL B . n 
B 1 482 TYR 482 482 482 TYR TYR B . n 
B 1 483 THR 483 483 483 THR THR B . n 
B 1 484 PHE 484 484 484 PHE PHE B . n 
B 1 485 ASP 485 485 485 ASP ASP B . n 
B 1 486 SER 486 486 486 SER SER B . n 
B 1 487 ALA 487 487 487 ALA ALA B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 GLN 489 489 489 GLN GLN B . n 
B 1 490 ALA 490 490 490 ALA ALA B . n 
B 1 491 SER 491 491 491 SER SER B . n 
B 1 492 TYR 492 492 492 TYR TYR B . n 
B 1 493 VAL 493 493 493 VAL VAL B . n 
B 1 494 PHE 494 494 494 PHE PHE B . n 
B 1 495 ASP 495 495 495 ASP ASP B . n 
B 1 496 LYS 496 496 496 LYS LYS B . n 
B 1 497 SER 497 497 497 SER SER B . n 
B 1 498 LYS 498 498 498 LYS LYS B . n 
B 1 499 GLY 499 499 499 GLY GLY B . n 
B 1 500 ASP 500 500 500 ASP ASP B . n 
B 1 501 LEU 501 501 501 LEU LEU B . n 
B 1 502 ILE 502 502 502 ILE ILE B . n 
B 1 503 SER 503 503 503 SER SER B . n 
B 1 504 PHE 504 504 504 PHE PHE B . n 
B 1 505 ASP 505 505 505 ASP ASP B . n 
B 1 506 SER 506 506 506 SER SER B . n 
B 1 507 VAL 507 507 507 VAL VAL B . n 
B 1 508 ASP 508 508 508 ASP ASP B . n 
B 1 509 SER 509 509 509 SER SER B . n 
B 1 510 VAL 510 510 510 VAL VAL B . n 
B 1 511 LEU 511 511 511 LEU LEU B . n 
B 1 512 GLY 512 512 512 GLY GLY B . n 
B 1 513 LYS 513 513 513 LYS LYS B . n 
B 1 514 VAL 514 514 514 VAL VAL B . n 
B 1 515 LYS 515 515 515 LYS LYS B . n 
B 1 516 TYR 516 516 516 TYR TYR B . n 
B 1 517 VAL 517 517 517 VAL VAL B . n 
B 1 518 ASP 518 518 518 ASP ASP B . n 
B 1 519 ARG 519 519 519 ARG ARG B . n 
B 1 520 ASN 520 520 520 ASN ASN B . n 
B 1 521 LYS 521 521 521 LYS LYS B . n 
B 1 522 LEU 522 522 522 LEU LEU B . n 
B 1 523 GLY 523 523 523 GLY GLY B . n 
B 1 524 GLY 524 524 524 GLY GLY B . n 
B 1 525 LEU 525 525 525 LEU LEU B . n 
B 1 526 PHE 526 526 526 PHE PHE B . n 
B 1 527 ALA 527 527 527 ALA ALA B . n 
B 1 528 TRP 528 528 528 TRP TRP B . n 
B 1 529 GLU 529 529 529 GLU GLU B . n 
B 1 530 ILE 530 530 530 ILE ILE B . n 
B 1 531 ASP 531 531 531 ASP ASP B . n 
B 1 532 ALA 532 532 532 ALA ALA B . n 
B 1 533 ASP 533 533 533 ASP ASP B . n 
B 1 534 ASN 534 534 534 ASN ASN B . n 
B 1 535 GLY 535 535 535 GLY GLY B . n 
B 1 536 ASP 536 536 536 ASP ASP B . n 
B 1 537 LEU 537 537 537 LEU LEU B . n 
B 1 538 LEU 538 538 538 LEU LEU B . n 
B 1 539 ASN 539 539 539 ASN ASN B . n 
B 1 540 ALA 540 540 540 ALA ALA B . n 
B 1 541 ILE 541 541 541 ILE ILE B . n 
B 1 542 ASN 542 542 542 ASN ASN B . n 
B 1 543 ALA 543 543 543 ALA ALA B . n 
B 1 544 GLN 544 544 544 GLN GLN B . n 
B 1 545 PHE 545 545 545 PHE PHE B . n 
# 
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 NAG 1  601 546 NAG NAG A . 
D 2 NAG 1  602 547 NAG NAG A . 
E 2 NAG 1  603 550 NAG NAG A . 
F 3 SN5 1  604 561 SN5 SN5 A . 
G 4 58Y 1  605 560 58Y NGT A . 
H 5 CL  1  606 554 CL  CL  A . 
I 6 SO4 1  607 766 SO4 SO4 A . 
J 6 SO4 1  608 767 SO4 SO4 A . 
K 6 SO4 1  609 768 SO4 SO4 A . 
L 2 NAG 1  601 550 NAG NAG B . 
M 2 NAG 1  602 552 NAG NAG B . 
N 2 NAG 1  603 553 NAG NAG B . 
O 3 SN5 1  604 561 SN5 SN5 B . 
P 4 58Y 1  605 560 58Y NGT B . 
Q 6 SO4 1  606 901 SO4 SO4 B . 
R 6 SO4 1  607 902 SO4 SO4 B . 
S 7 HOH 1  701 616 HOH HOH A . 
S 7 HOH 2  702 609 HOH HOH A . 
S 7 HOH 3  703 717 HOH HOH A . 
S 7 HOH 4  704 765 HOH HOH A . 
T 7 HOH 1  701 565 HOH HOH B . 
T 7 HOH 2  702 577 HOH HOH B . 
T 7 HOH 3  703 900 HOH HOH B . 
T 7 HOH 4  704 684 HOH HOH B . 
T 7 HOH 5  705 774 HOH HOH B . 
T 7 HOH 6  706 639 HOH HOH B . 
T 7 HOH 7  707 750 HOH HOH B . 
T 7 HOH 8  708 877 HOH HOH B . 
T 7 HOH 9  709 736 HOH HOH B . 
T 7 HOH 10 710 702 HOH HOH B . 
T 7 HOH 11 711 641 HOH HOH B . 
T 7 HOH 12 712 854 HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,S 
2 1 B,L,M,N,O,P,Q,R,T     
# 
_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_
_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 2016-09-07 
2 'Structure model' 1 1 2017-09-20 
# 
_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         ? 
# 
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' 'Author supporting evidence' 
2 2 'Structure model' 'Derived calculations'       
# 
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' pdbx_audit_support    
2 2 'Structure model' pdbx_struct_oper_list 
# 
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' '_pdbx_audit_support.funding_organization'  
2 2 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.10.1_2155: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NZ  B LYS 215 ? ? O   B VAL 282 ? ? 2.05 
2 1 OH  B TYR 160 ? ? OD2 B ASP 220 ? ? 2.12 
3 1 O   B SER 286 ? ? N   B PHE 290 ? ? 2.15 
4 1 O   A GLY 264 ? ? OG  A SER 268 ? ? 2.16 
5 1 OG1 B THR 462 ? ? OE1 B GLN 472 ? ? 2.17 
# 
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 PHE A 74  ? ? -113.01 59.10   
2  1 ASP A 75  ? ? 128.39  29.89   
3  1 ASN A 107 ? ? -156.01 -158.73 
4  1 ASP A 109 ? ? -63.70  -71.34  
5  1 GLU A 138 ? ? 58.44   -128.52 
6  1 TYR A 160 ? ? -87.69  -108.97 
7  1 ASN A 191 ? ? -144.85 48.86   
8  1 ALA A 217 ? ? -157.04 -157.37 
9  1 VAL A 232 ? ? -140.87 41.10   
10 1 LYS A 240 ? ? -117.09 -155.06 
11 1 VAL A 277 ? ? -14.90  -56.79  
12 1 GLU A 278 ? ? 158.98  45.26   
13 1 ASP A 303 ? ? -112.29 66.55   
14 1 LYS A 310 ? ? 61.39   -2.70   
15 1 ASN A 404 ? ? -161.78 98.74   
16 1 GLU A 406 ? ? -150.38 61.54   
17 1 MET A 434 ? ? -80.50  34.04   
18 1 ASN A 447 ? ? 58.75   -150.23 
19 1 ASN B 63  ? ? 57.06   71.26   
20 1 ASP B 109 ? ? -74.95  -72.57  
21 1 GLU B 138 ? ? 59.71   -129.67 
22 1 TYR B 160 ? ? -100.44 -109.17 
23 1 ASN B 191 ? ? -144.31 48.72   
24 1 ALA B 217 ? ? -151.88 -146.51 
25 1 VAL B 225 ? ? -140.40 -8.19   
26 1 SER B 231 ? ? 64.42   -1.52   
27 1 VAL B 232 ? ? -141.07 46.81   
28 1 LYS B 240 ? ? -119.79 -148.05 
29 1 ASP B 303 ? ? -110.46 58.77   
30 1 LYS B 310 ? ? 68.42   -2.69   
31 1 VAL B 363 ? ? -66.11  -75.50  
32 1 SER B 380 ? ? -92.89  59.72   
33 1 GLU B 406 ? ? -146.35 57.80   
34 1 MET B 434 ? ? -83.42  30.61   
35 1 ASN B 444 ? ? 56.43   76.05   
36 1 ASN B 447 ? ? 58.72   -152.39 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ARG 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    519 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    520 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            142.47 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1  ? A MET 1  
2  1 Y 1 A LEU 2  ? A LEU 2  
3  1 Y 1 A TYR 3  ? A TYR 3  
4  1 Y 1 A LYS 4  ? A LYS 4  
5  1 Y 1 A LEU 5  ? A LEU 5  
6  1 Y 1 A LEU 6  ? A LEU 6  
7  1 Y 1 A ASN 7  ? A ASN 7  
8  1 Y 1 A VAL 8  ? A VAL 8  
9  1 Y 1 A LEU 9  ? A LEU 9  
10 1 Y 1 A TRP 10 ? A TRP 10 
11 1 Y 1 A LEU 11 ? A LEU 11 
12 1 Y 1 A VAL 12 ? A VAL 12 
13 1 Y 1 A ALA 13 ? A ALA 13 
14 1 Y 1 A VAL 14 ? A VAL 14 
15 1 Y 1 A SER 15 ? A SER 15 
16 1 Y 1 A ASN 16 ? A ASN 16 
17 1 Y 1 A ALA 17 ? A ALA 17 
18 1 Y 1 B MET 1  ? B MET 1  
19 1 Y 1 B LEU 2  ? B LEU 2  
20 1 Y 1 B TYR 3  ? B TYR 3  
21 1 Y 1 B LYS 4  ? B LYS 4  
22 1 Y 1 B LEU 5  ? B LEU 5  
23 1 Y 1 B LEU 6  ? B LEU 6  
24 1 Y 1 B ASN 7  ? B ASN 7  
25 1 Y 1 B VAL 8  ? B VAL 8  
26 1 Y 1 B LEU 9  ? B LEU 9  
27 1 Y 1 B TRP 10 ? B TRP 10 
28 1 Y 1 B LEU 11 ? B LEU 11 
29 1 Y 1 B VAL 12 ? B VAL 12 
30 1 Y 1 B ALA 13 ? B ALA 13 
31 1 Y 1 B VAL 14 ? B VAL 14 
32 1 Y 1 B SER 15 ? B SER 15 
33 1 Y 1 B ASN 16 ? B ASN 16 
34 1 Y 1 B ALA 17 ? B ALA 17 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Institute of General Medical Sciences' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           P20GM103546 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                                                                              NAG 
3 '2-deoxy-2-(ethanethioylamino)-beta-D-glucopyranose'                                                SN5 
4 '(2R,3aR,5R,6R,7R,7aR)-5-(hydroxymethyl)-2-methylhexahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol' 58Y 
5 'CHLORIDE ION'                                                                                      CL  
6 'SULFATE ION'                                                                                       SO4 
7 water                                                                                               HOH 
# 
