data_8R4P
# 
_entry.id   8R4P 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8R4P         pdb_00008r4p 10.2210/pdb8r4p/pdb 
WWPDB D_1292133063 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8R4P 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              Thomas.boren@umu.se 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Boren 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5113-3303 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Persson, K.'    1 0000-0003-0807-0348 
'Boren, T.'      2 0000-0001-5113-3303 
'Bugaytsova, J.' 3 0000-0003-2452-5437 
# 
_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                     'Structure of BabA from Helicobacter pylori strain 17875' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Persson, K.'    1 0000-0003-0807-0348 
primary 'Boren, T.'      2 0000-0001-5113-3303 
primary 'Bugaytsova, J.' 3 0000-0003-2452-5437 
# 
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 'Adhesin binding fucosylated histo-blood group antigen' 61281.641 1   ? ? ? ? 
2 non-polymer syn 'CADMIUM ION'                                           112.411   10  ? ? ? ? 
3 water       nat water                                                   18.015    205 ? ? ? ? 
# 
_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       
;MKYLLPTAAAGLLLLAAQPAMAEDDGFYTSVGYQIGEAAQMVTNTKGIQDLSDNYENLSKLLTRYSTLNTLIKLSADPSA
INAARENLGASAKNLIGDTKNSPAYQAVLLAINAAVGFWNVLGYATQCGGNANGQESTSSTTIFNNEPGYRSTSITCSLN
RYKPGYYGPMSIENFKKLNEAYQILQTALNKGLPALKENNGTVSVTYTYTCSGEGNDNCSKKATGVSDQNGGTKTKTQTI
DGKTVTTTISSKVVDSQAKGNTTRVSYTEITNKLDGVPDSAQALLAQASTLINTINTACPYFSVTNKSGGPQMEPTRGKL
CGFTEEISAIQKMITDAQELVNQTSVINEHEQSTPVGGNNGKPFNPFTDASFAQGMLANASAQAKMLNLAHQVGQTINPD
NLTGTFKNFVTGFLATCNNKSTAGTSGTQGSPPGTVTTQTFASGCAYVEQTITNLNNSIAHFGTQEQQIQQAENIADTLV
NFKSRYSELGNTYNSITTALSKVPNAQSLQNVVGKKNNPYSPQGIETNYYLNQNSYNQIQTINQELKKKKKKGSEQKLIS
EEDLSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYLLPTAAAGLLLLAAQPAMAEDDGFYTSVGYQIGEAAQMVTNTKGIQDLSDNYENLSKLLTRYSTLNTLIKLSADPSA
INAARENLGASAKNLIGDTKNSPAYQAVLLAINAAVGFWNVLGYATQCGGNANGQESTSSTTIFNNEPGYRSTSITCSLN
RYKPGYYGPMSIENFKKLNEAYQILQTALNKGLPALKENNGTVSVTYTYTCSGEGNDNCSKKATGVSDQNGGTKTKTQTI
DGKTVTTTISSKVVDSQAKGNTTRVSYTEITNKLDGVPDSAQALLAQASTLINTINTACPYFSVTNKSGGPQMEPTRGKL
CGFTEEISAIQKMITDAQELVNQTSVINEHEQSTPVGGNNGKPFNPFTDASFAQGMLANASAQAKMLNLAHQVGQTINPD
NLTGTFKNFVTGFLATCNNKSTAGTSGTQGSPPGTVTTQTFASGCAYVEQTITNLNNSIAHFGTQEQQIQQAENIADTLV
NFKSRYSELGNTYNSITTALSKVPNAQSLQNVVGKKNNPYSPQGIETNYYLNQNSYNQIQTINQELKKKKKKGSEQKLIS
EEDLSHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CADMIUM ION' CD  
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   TYR n 
1 4   LEU n 
1 5   LEU n 
1 6   PRO n 
1 7   THR n 
1 8   ALA n 
1 9   ALA n 
1 10  ALA n 
1 11  GLY n 
1 12  LEU n 
1 13  LEU n 
1 14  LEU n 
1 15  LEU n 
1 16  ALA n 
1 17  ALA n 
1 18  GLN n 
1 19  PRO n 
1 20  ALA n 
1 21  MET n 
1 22  ALA n 
1 23  GLU n 
1 24  ASP n 
1 25  ASP n 
1 26  GLY n 
1 27  PHE n 
1 28  TYR n 
1 29  THR n 
1 30  SER n 
1 31  VAL n 
1 32  GLY n 
1 33  TYR n 
1 34  GLN n 
1 35  ILE n 
1 36  GLY n 
1 37  GLU n 
1 38  ALA n 
1 39  ALA n 
1 40  GLN n 
1 41  MET n 
1 42  VAL n 
1 43  THR n 
1 44  ASN n 
1 45  THR n 
1 46  LYS n 
1 47  GLY n 
1 48  ILE n 
1 49  GLN n 
1 50  ASP n 
1 51  LEU n 
1 52  SER n 
1 53  ASP n 
1 54  ASN n 
1 55  TYR n 
1 56  GLU n 
1 57  ASN n 
1 58  LEU n 
1 59  SER n 
1 60  LYS n 
1 61  LEU n 
1 62  LEU n 
1 63  THR n 
1 64  ARG n 
1 65  TYR n 
1 66  SER n 
1 67  THR n 
1 68  LEU n 
1 69  ASN n 
1 70  THR n 
1 71  LEU n 
1 72  ILE n 
1 73  LYS n 
1 74  LEU n 
1 75  SER n 
1 76  ALA n 
1 77  ASP n 
1 78  PRO n 
1 79  SER n 
1 80  ALA n 
1 81  ILE n 
1 82  ASN n 
1 83  ALA n 
1 84  ALA n 
1 85  ARG n 
1 86  GLU n 
1 87  ASN n 
1 88  LEU n 
1 89  GLY n 
1 90  ALA n 
1 91  SER n 
1 92  ALA n 
1 93  LYS n 
1 94  ASN n 
1 95  LEU n 
1 96  ILE n 
1 97  GLY n 
1 98  ASP n 
1 99  THR n 
1 100 LYS n 
1 101 ASN n 
1 102 SER n 
1 103 PRO n 
1 104 ALA n 
1 105 TYR n 
1 106 GLN n 
1 107 ALA n 
1 108 VAL n 
1 109 LEU n 
1 110 LEU n 
1 111 ALA n 
1 112 ILE n 
1 113 ASN n 
1 114 ALA n 
1 115 ALA n 
1 116 VAL n 
1 117 GLY n 
1 118 PHE n 
1 119 TRP n 
1 120 ASN n 
1 121 VAL n 
1 122 LEU n 
1 123 GLY n 
1 124 TYR n 
1 125 ALA n 
1 126 THR n 
1 127 GLN n 
1 128 CYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 ALA n 
1 133 ASN n 
1 134 GLY n 
1 135 GLN n 
1 136 GLU n 
1 137 SER n 
1 138 THR n 
1 139 SER n 
1 140 SER n 
1 141 THR n 
1 142 THR n 
1 143 ILE n 
1 144 PHE n 
1 145 ASN n 
1 146 ASN n 
1 147 GLU n 
1 148 PRO n 
1 149 GLY n 
1 150 TYR n 
1 151 ARG n 
1 152 SER n 
1 153 THR n 
1 154 SER n 
1 155 ILE n 
1 156 THR n 
1 157 CYS n 
1 158 SER n 
1 159 LEU n 
1 160 ASN n 
1 161 ARG n 
1 162 TYR n 
1 163 LYS n 
1 164 PRO n 
1 165 GLY n 
1 166 TYR n 
1 167 TYR n 
1 168 GLY n 
1 169 PRO n 
1 170 MET n 
1 171 SER n 
1 172 ILE n 
1 173 GLU n 
1 174 ASN n 
1 175 PHE n 
1 176 LYS n 
1 177 LYS n 
1 178 LEU n 
1 179 ASN n 
1 180 GLU n 
1 181 ALA n 
1 182 TYR n 
1 183 GLN n 
1 184 ILE n 
1 185 LEU n 
1 186 GLN n 
1 187 THR n 
1 188 ALA n 
1 189 LEU n 
1 190 ASN n 
1 191 LYS n 
1 192 GLY n 
1 193 LEU n 
1 194 PRO n 
1 195 ALA n 
1 196 LEU n 
1 197 LYS n 
1 198 GLU n 
1 199 ASN n 
1 200 ASN n 
1 201 GLY n 
1 202 THR n 
1 203 VAL n 
1 204 SER n 
1 205 VAL n 
1 206 THR n 
1 207 TYR n 
1 208 THR n 
1 209 TYR n 
1 210 THR n 
1 211 CYS n 
1 212 SER n 
1 213 GLY n 
1 214 GLU n 
1 215 GLY n 
1 216 ASN n 
1 217 ASP n 
1 218 ASN n 
1 219 CYS n 
1 220 SER n 
1 221 LYS n 
1 222 LYS n 
1 223 ALA n 
1 224 THR n 
1 225 GLY n 
1 226 VAL n 
1 227 SER n 
1 228 ASP n 
1 229 GLN n 
1 230 ASN n 
1 231 GLY n 
1 232 GLY n 
1 233 THR n 
1 234 LYS n 
1 235 THR n 
1 236 LYS n 
1 237 THR n 
1 238 GLN n 
1 239 THR n 
1 240 ILE n 
1 241 ASP n 
1 242 GLY n 
1 243 LYS n 
1 244 THR n 
1 245 VAL n 
1 246 THR n 
1 247 THR n 
1 248 THR n 
1 249 ILE n 
1 250 SER n 
1 251 SER n 
1 252 LYS n 
1 253 VAL n 
1 254 VAL n 
1 255 ASP n 
1 256 SER n 
1 257 GLN n 
1 258 ALA n 
1 259 LYS n 
1 260 GLY n 
1 261 ASN n 
1 262 THR n 
1 263 THR n 
1 264 ARG n 
1 265 VAL n 
1 266 SER n 
1 267 TYR n 
1 268 THR n 
1 269 GLU n 
1 270 ILE n 
1 271 THR n 
1 272 ASN n 
1 273 LYS n 
1 274 LEU n 
1 275 ASP n 
1 276 GLY n 
1 277 VAL n 
1 278 PRO n 
1 279 ASP n 
1 280 SER n 
1 281 ALA n 
1 282 GLN n 
1 283 ALA n 
1 284 LEU n 
1 285 LEU n 
1 286 ALA n 
1 287 GLN n 
1 288 ALA n 
1 289 SER n 
1 290 THR n 
1 291 LEU n 
1 292 ILE n 
1 293 ASN n 
1 294 THR n 
1 295 ILE n 
1 296 ASN n 
1 297 THR n 
1 298 ALA n 
1 299 CYS n 
1 300 PRO n 
1 301 TYR n 
1 302 PHE n 
1 303 SER n 
1 304 VAL n 
1 305 THR n 
1 306 ASN n 
1 307 LYS n 
1 308 SER n 
1 309 GLY n 
1 310 GLY n 
1 311 PRO n 
1 312 GLN n 
1 313 MET n 
1 314 GLU n 
1 315 PRO n 
1 316 THR n 
1 317 ARG n 
1 318 GLY n 
1 319 LYS n 
1 320 LEU n 
1 321 CYS n 
1 322 GLY n 
1 323 PHE n 
1 324 THR n 
1 325 GLU n 
1 326 GLU n 
1 327 ILE n 
1 328 SER n 
1 329 ALA n 
1 330 ILE n 
1 331 GLN n 
1 332 LYS n 
1 333 MET n 
1 334 ILE n 
1 335 THR n 
1 336 ASP n 
1 337 ALA n 
1 338 GLN n 
1 339 GLU n 
1 340 LEU n 
1 341 VAL n 
1 342 ASN n 
1 343 GLN n 
1 344 THR n 
1 345 SER n 
1 346 VAL n 
1 347 ILE n 
1 348 ASN n 
1 349 GLU n 
1 350 HIS n 
1 351 GLU n 
1 352 GLN n 
1 353 SER n 
1 354 THR n 
1 355 PRO n 
1 356 VAL n 
1 357 GLY n 
1 358 GLY n 
1 359 ASN n 
1 360 ASN n 
1 361 GLY n 
1 362 LYS n 
1 363 PRO n 
1 364 PHE n 
1 365 ASN n 
1 366 PRO n 
1 367 PHE n 
1 368 THR n 
1 369 ASP n 
1 370 ALA n 
1 371 SER n 
1 372 PHE n 
1 373 ALA n 
1 374 GLN n 
1 375 GLY n 
1 376 MET n 
1 377 LEU n 
1 378 ALA n 
1 379 ASN n 
1 380 ALA n 
1 381 SER n 
1 382 ALA n 
1 383 GLN n 
1 384 ALA n 
1 385 LYS n 
1 386 MET n 
1 387 LEU n 
1 388 ASN n 
1 389 LEU n 
1 390 ALA n 
1 391 HIS n 
1 392 GLN n 
1 393 VAL n 
1 394 GLY n 
1 395 GLN n 
1 396 THR n 
1 397 ILE n 
1 398 ASN n 
1 399 PRO n 
1 400 ASP n 
1 401 ASN n 
1 402 LEU n 
1 403 THR n 
1 404 GLY n 
1 405 THR n 
1 406 PHE n 
1 407 LYS n 
1 408 ASN n 
1 409 PHE n 
1 410 VAL n 
1 411 THR n 
1 412 GLY n 
1 413 PHE n 
1 414 LEU n 
1 415 ALA n 
1 416 THR n 
1 417 CYS n 
1 418 ASN n 
1 419 ASN n 
1 420 LYS n 
1 421 SER n 
1 422 THR n 
1 423 ALA n 
1 424 GLY n 
1 425 THR n 
1 426 SER n 
1 427 GLY n 
1 428 THR n 
1 429 GLN n 
1 430 GLY n 
1 431 SER n 
1 432 PRO n 
1 433 PRO n 
1 434 GLY n 
1 435 THR n 
1 436 VAL n 
1 437 THR n 
1 438 THR n 
1 439 GLN n 
1 440 THR n 
1 441 PHE n 
1 442 ALA n 
1 443 SER n 
1 444 GLY n 
1 445 CYS n 
1 446 ALA n 
1 447 TYR n 
1 448 VAL n 
1 449 GLU n 
1 450 GLN n 
1 451 THR n 
1 452 ILE n 
1 453 THR n 
1 454 ASN n 
1 455 LEU n 
1 456 ASN n 
1 457 ASN n 
1 458 SER n 
1 459 ILE n 
1 460 ALA n 
1 461 HIS n 
1 462 PHE n 
1 463 GLY n 
1 464 THR n 
1 465 GLN n 
1 466 GLU n 
1 467 GLN n 
1 468 GLN n 
1 469 ILE n 
1 470 GLN n 
1 471 GLN n 
1 472 ALA n 
1 473 GLU n 
1 474 ASN n 
1 475 ILE n 
1 476 ALA n 
1 477 ASP n 
1 478 THR n 
1 479 LEU n 
1 480 VAL n 
1 481 ASN n 
1 482 PHE n 
1 483 LYS n 
1 484 SER n 
1 485 ARG n 
1 486 TYR n 
1 487 SER n 
1 488 GLU n 
1 489 LEU n 
1 490 GLY n 
1 491 ASN n 
1 492 THR n 
1 493 TYR n 
1 494 ASN n 
1 495 SER n 
1 496 ILE n 
1 497 THR n 
1 498 THR n 
1 499 ALA n 
1 500 LEU n 
1 501 SER n 
1 502 LYS n 
1 503 VAL n 
1 504 PRO n 
1 505 ASN n 
1 506 ALA n 
1 507 GLN n 
1 508 SER n 
1 509 LEU n 
1 510 GLN n 
1 511 ASN n 
1 512 VAL n 
1 513 VAL n 
1 514 GLY n 
1 515 LYS n 
1 516 LYS n 
1 517 ASN n 
1 518 ASN n 
1 519 PRO n 
1 520 TYR n 
1 521 SER n 
1 522 PRO n 
1 523 GLN n 
1 524 GLY n 
1 525 ILE n 
1 526 GLU n 
1 527 THR n 
1 528 ASN n 
1 529 TYR n 
1 530 TYR n 
1 531 LEU n 
1 532 ASN n 
1 533 GLN n 
1 534 ASN n 
1 535 SER n 
1 536 TYR n 
1 537 ASN n 
1 538 GLN n 
1 539 ILE n 
1 540 GLN n 
1 541 THR n 
1 542 ILE n 
1 543 ASN n 
1 544 GLN n 
1 545 GLU n 
1 546 LEU n 
1 547 LYS n 
1 548 LYS n 
1 549 LYS n 
1 550 LYS n 
1 551 LYS n 
1 552 LYS n 
1 553 GLY n 
1 554 SER n 
1 555 GLU n 
1 556 GLN n 
1 557 LYS n 
1 558 LEU n 
1 559 ILE n 
1 560 SER n 
1 561 GLU n 
1 562 GLU n 
1 563 ASP n 
1 564 LEU n 
1 565 SER n 
1 566 HIS n 
1 567 HIS n 
1 568 HIS n 
1 569 HIS n 
1 570 HIS n 
1 571 HIS 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                   571 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 babA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    17875 
_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      'Helicobacter pylori' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     210 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CD  non-polymer         . 'CADMIUM ION'   ? 'Cd 2'           112.411 
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 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -21 ?   ?   ?   A . n 
A 1 2   LYS 2   -20 ?   ?   ?   A . n 
A 1 3   TYR 3   -19 ?   ?   ?   A . n 
A 1 4   LEU 4   -18 ?   ?   ?   A . n 
A 1 5   LEU 5   -17 ?   ?   ?   A . n 
A 1 6   PRO 6   -16 ?   ?   ?   A . n 
A 1 7   THR 7   -15 ?   ?   ?   A . n 
A 1 8   ALA 8   -14 ?   ?   ?   A . n 
A 1 9   ALA 9   -13 ?   ?   ?   A . n 
A 1 10  ALA 10  -12 ?   ?   ?   A . n 
A 1 11  GLY 11  -11 ?   ?   ?   A . n 
A 1 12  LEU 12  -10 ?   ?   ?   A . n 
A 1 13  LEU 13  -9  ?   ?   ?   A . n 
A 1 14  LEU 14  -8  ?   ?   ?   A . n 
A 1 15  LEU 15  -7  ?   ?   ?   A . n 
A 1 16  ALA 16  -6  ?   ?   ?   A . n 
A 1 17  ALA 17  -5  ?   ?   ?   A . n 
A 1 18  GLN 18  -4  ?   ?   ?   A . n 
A 1 19  PRO 19  -3  ?   ?   ?   A . n 
A 1 20  ALA 20  -2  ?   ?   ?   A . n 
A 1 21  MET 21  -1  ?   ?   ?   A . n 
A 1 22  ALA 22  0   ?   ?   ?   A . n 
A 1 23  GLU 23  1   ?   ?   ?   A . n 
A 1 24  ASP 24  2   ?   ?   ?   A . n 
A 1 25  ASP 25  3   ?   ?   ?   A . n 
A 1 26  GLY 26  4   ?   ?   ?   A . n 
A 1 27  PHE 27  5   ?   ?   ?   A . n 
A 1 28  TYR 28  6   ?   ?   ?   A . n 
A 1 29  THR 29  7   ?   ?   ?   A . n 
A 1 30  SER 30  8   ?   ?   ?   A . n 
A 1 31  VAL 31  9   ?   ?   ?   A . n 
A 1 32  GLY 32  10  ?   ?   ?   A . n 
A 1 33  TYR 33  11  ?   ?   ?   A . n 
A 1 34  GLN 34  12  ?   ?   ?   A . n 
A 1 35  ILE 35  13  ?   ?   ?   A . n 
A 1 36  GLY 36  14  ?   ?   ?   A . n 
A 1 37  GLU 37  15  ?   ?   ?   A . n 
A 1 38  ALA 38  16  ?   ?   ?   A . n 
A 1 39  ALA 39  17  ?   ?   ?   A . n 
A 1 40  GLN 40  18  ?   ?   ?   A . n 
A 1 41  MET 41  19  ?   ?   ?   A . n 
A 1 42  VAL 42  20  ?   ?   ?   A . n 
A 1 43  THR 43  21  ?   ?   ?   A . n 
A 1 44  ASN 44  22  ?   ?   ?   A . n 
A 1 45  THR 45  23  ?   ?   ?   A . n 
A 1 46  LYS 46  24  ?   ?   ?   A . n 
A 1 47  GLY 47  25  ?   ?   ?   A . n 
A 1 48  ILE 48  26  26  ILE ILE A . n 
A 1 49  GLN 49  27  27  GLN GLN A . n 
A 1 50  ASP 50  28  28  ASP ASP A . n 
A 1 51  LEU 51  29  29  LEU LEU A . n 
A 1 52  SER 52  30  30  SER SER A . n 
A 1 53  ASP 53  31  31  ASP ASP A . n 
A 1 54  ASN 54  32  32  ASN ASN A . n 
A 1 55  TYR 55  33  33  TYR TYR A . n 
A 1 56  GLU 56  34  34  GLU GLU A . n 
A 1 57  ASN 57  35  35  ASN ASN A . n 
A 1 58  LEU 58  36  36  LEU LEU A . n 
A 1 59  SER 59  37  37  SER SER A . n 
A 1 60  LYS 60  38  38  LYS LYS A . n 
A 1 61  LEU 61  39  39  LEU LEU A . n 
A 1 62  LEU 62  40  40  LEU LEU A . n 
A 1 63  THR 63  41  41  THR THR A . n 
A 1 64  ARG 64  42  42  ARG ARG A . n 
A 1 65  TYR 65  43  43  TYR TYR A . n 
A 1 66  SER 66  44  44  SER SER A . n 
A 1 67  THR 67  45  45  THR THR A . n 
A 1 68  LEU 68  46  46  LEU LEU A . n 
A 1 69  ASN 69  47  47  ASN ASN A . n 
A 1 70  THR 70  48  48  THR THR A . n 
A 1 71  LEU 71  49  49  LEU LEU A . n 
A 1 72  ILE 72  50  50  ILE ILE A . n 
A 1 73  LYS 73  51  51  LYS LYS A . n 
A 1 74  LEU 74  52  52  LEU LEU A . n 
A 1 75  SER 75  53  53  SER SER A . n 
A 1 76  ALA 76  54  54  ALA ALA A . n 
A 1 77  ASP 77  55  55  ASP ASP A . n 
A 1 78  PRO 78  56  56  PRO PRO A . n 
A 1 79  SER 79  57  57  SER SER A . n 
A 1 80  ALA 80  58  58  ALA ALA A . n 
A 1 81  ILE 81  59  59  ILE ILE A . n 
A 1 82  ASN 82  60  60  ASN ASN A . n 
A 1 83  ALA 83  61  61  ALA ALA A . n 
A 1 84  ALA 84  62  62  ALA ALA A . n 
A 1 85  ARG 85  63  63  ARG ARG A . n 
A 1 86  GLU 86  64  64  GLU GLU A . n 
A 1 87  ASN 87  65  65  ASN ASN A . n 
A 1 88  LEU 88  66  66  LEU LEU A . n 
A 1 89  GLY 89  67  67  GLY GLY A . n 
A 1 90  ALA 90  68  68  ALA ALA A . n 
A 1 91  SER 91  69  69  SER SER A . n 
A 1 92  ALA 92  70  70  ALA ALA A . n 
A 1 93  LYS 93  71  71  LYS LYS A . n 
A 1 94  ASN 94  72  72  ASN ASN A . n 
A 1 95  LEU 95  73  73  LEU LEU A . n 
A 1 96  ILE 96  74  74  ILE ILE A . n 
A 1 97  GLY 97  75  75  GLY GLY A . n 
A 1 98  ASP 98  76  76  ASP ASP A . n 
A 1 99  THR 99  77  77  THR THR A . n 
A 1 100 LYS 100 78  78  LYS LYS A . n 
A 1 101 ASN 101 79  79  ASN ASN A . n 
A 1 102 SER 102 80  80  SER SER A . n 
A 1 103 PRO 103 81  81  PRO PRO A . n 
A 1 104 ALA 104 82  82  ALA ALA A . n 
A 1 105 TYR 105 83  83  TYR TYR A . n 
A 1 106 GLN 106 84  84  GLN GLN A . n 
A 1 107 ALA 107 85  85  ALA ALA A . n 
A 1 108 VAL 108 86  86  VAL VAL A . n 
A 1 109 LEU 109 87  87  LEU LEU A . n 
A 1 110 LEU 110 88  88  LEU LEU A . n 
A 1 111 ALA 111 89  89  ALA ALA A . n 
A 1 112 ILE 112 90  90  ILE ILE A . n 
A 1 113 ASN 113 91  91  ASN ASN A . n 
A 1 114 ALA 114 92  92  ALA ALA A . n 
A 1 115 ALA 115 93  93  ALA ALA A . n 
A 1 116 VAL 116 94  94  VAL VAL A . n 
A 1 117 GLY 117 95  95  GLY GLY A . n 
A 1 118 PHE 118 96  96  PHE PHE A . n 
A 1 119 TRP 119 97  97  TRP TRP A . n 
A 1 120 ASN 120 98  98  ASN ASN A . n 
A 1 121 VAL 121 99  99  VAL VAL A . n 
A 1 122 LEU 122 100 100 LEU LEU A . n 
A 1 123 GLY 123 101 101 GLY GLY A . n 
A 1 124 TYR 124 102 102 TYR TYR A . n 
A 1 125 ALA 125 103 103 ALA ALA A . n 
A 1 126 THR 126 104 104 THR THR A . n 
A 1 127 GLN 127 105 105 GLN GLN A . n 
A 1 128 CYS 128 106 106 CYS CYS A . n 
A 1 129 GLY 129 107 107 GLY GLY A . n 
A 1 130 GLY 130 108 108 GLY GLY A . n 
A 1 131 ASN 131 109 109 ASN ASN A . n 
A 1 132 ALA 132 110 110 ALA ALA A . n 
A 1 133 ASN 133 111 111 ASN ASN A . n 
A 1 134 GLY 134 112 112 GLY GLY A . n 
A 1 135 GLN 135 113 113 GLN GLN A . n 
A 1 136 GLU 136 114 114 GLU GLU A . n 
A 1 137 SER 137 115 115 SER SER A . n 
A 1 138 THR 138 116 116 THR THR A . n 
A 1 139 SER 139 117 117 SER SER A . n 
A 1 140 SER 140 118 118 SER SER A . n 
A 1 141 THR 141 119 119 THR THR A . n 
A 1 142 THR 142 120 120 THR THR A . n 
A 1 143 ILE 143 121 121 ILE ILE A . n 
A 1 144 PHE 144 122 122 PHE PHE A . n 
A 1 145 ASN 145 123 123 ASN ASN A . n 
A 1 146 ASN 146 124 124 ASN ASN A . n 
A 1 147 GLU 147 125 125 GLU GLU A . n 
A 1 148 PRO 148 126 126 PRO PRO A . n 
A 1 149 GLY 149 127 127 GLY GLY A . n 
A 1 150 TYR 150 128 128 TYR TYR A . n 
A 1 151 ARG 151 129 129 ARG ARG A . n 
A 1 152 SER 152 130 130 SER SER A . n 
A 1 153 THR 153 131 131 THR THR A . n 
A 1 154 SER 154 132 132 SER SER A . n 
A 1 155 ILE 155 133 133 ILE ILE A . n 
A 1 156 THR 156 134 134 THR THR A . n 
A 1 157 CYS 157 135 135 CYS CYS A . n 
A 1 158 SER 158 136 136 SER SER A . n 
A 1 159 LEU 159 137 137 LEU LEU A . n 
A 1 160 ASN 160 138 138 ASN ASN A . n 
A 1 161 ARG 161 139 139 ARG ARG A . n 
A 1 162 TYR 162 140 140 TYR TYR A . n 
A 1 163 LYS 163 141 141 LYS LYS A . n 
A 1 164 PRO 164 142 142 PRO PRO A . n 
A 1 165 GLY 165 143 143 GLY GLY A . n 
A 1 166 TYR 166 144 144 TYR TYR A . n 
A 1 167 TYR 167 145 145 TYR TYR A . n 
A 1 168 GLY 168 146 146 GLY GLY A . n 
A 1 169 PRO 169 147 147 PRO PRO A . n 
A 1 170 MET 170 148 148 MET MET A . n 
A 1 171 SER 171 149 149 SER SER A . n 
A 1 172 ILE 172 150 150 ILE ILE A . n 
A 1 173 GLU 173 151 151 GLU GLU A . n 
A 1 174 ASN 174 152 152 ASN ASN A . n 
A 1 175 PHE 175 153 153 PHE PHE A . n 
A 1 176 LYS 176 154 154 LYS LYS A . n 
A 1 177 LYS 177 155 155 LYS LYS A . n 
A 1 178 LEU 178 156 156 LEU LEU A . n 
A 1 179 ASN 179 157 157 ASN ASN A . n 
A 1 180 GLU 180 158 158 GLU GLU A . n 
A 1 181 ALA 181 159 159 ALA ALA A . n 
A 1 182 TYR 182 160 160 TYR TYR A . n 
A 1 183 GLN 183 161 161 GLN GLN A . n 
A 1 184 ILE 184 162 162 ILE ILE A . n 
A 1 185 LEU 185 163 163 LEU LEU A . n 
A 1 186 GLN 186 164 164 GLN GLN A . n 
A 1 187 THR 187 165 165 THR THR A . n 
A 1 188 ALA 188 166 166 ALA ALA A . n 
A 1 189 LEU 189 167 167 LEU LEU A . n 
A 1 190 ASN 190 168 168 ASN ASN A . n 
A 1 191 LYS 191 169 169 LYS LYS A . n 
A 1 192 GLY 192 170 170 GLY GLY A . n 
A 1 193 LEU 193 171 171 LEU LEU A . n 
A 1 194 PRO 194 172 172 PRO PRO A . n 
A 1 195 ALA 195 173 173 ALA ALA A . n 
A 1 196 LEU 196 174 174 LEU LEU A . n 
A 1 197 LYS 197 175 175 LYS LYS A . n 
A 1 198 GLU 198 176 176 GLU GLU A . n 
A 1 199 ASN 199 177 177 ASN ASN A . n 
A 1 200 ASN 200 178 178 ASN ASN A . n 
A 1 201 GLY 201 179 179 GLY GLY A . n 
A 1 202 THR 202 180 180 THR THR A . n 
A 1 203 VAL 203 181 181 VAL VAL A . n 
A 1 204 SER 204 182 182 SER SER A . n 
A 1 205 VAL 205 183 183 VAL VAL A . n 
A 1 206 THR 206 184 184 THR THR A . n 
A 1 207 TYR 207 185 185 TYR TYR A . n 
A 1 208 THR 208 186 186 THR THR A . n 
A 1 209 TYR 209 187 187 TYR TYR A . n 
A 1 210 THR 210 188 188 THR THR A . n 
A 1 211 CYS 211 189 189 CYS CYS A . n 
A 1 212 SER 212 190 190 SER SER A . n 
A 1 213 GLY 213 191 191 GLY GLY A . n 
A 1 214 GLU 214 192 192 GLU GLU A . n 
A 1 215 GLY 215 193 193 GLY GLY A . n 
A 1 216 ASN 216 194 194 ASN ASN A . n 
A 1 217 ASP 217 195 195 ASP ASP A . n 
A 1 218 ASN 218 196 196 ASN ASN A . n 
A 1 219 CYS 219 197 197 CYS CYS A . n 
A 1 220 SER 220 198 198 SER SER A . n 
A 1 221 LYS 221 199 199 LYS LYS A . n 
A 1 222 LYS 222 200 200 LYS LYS A . n 
A 1 223 ALA 223 201 201 ALA ALA A . n 
A 1 224 THR 224 202 202 THR THR A . n 
A 1 225 GLY 225 203 203 GLY GLY A . n 
A 1 226 VAL 226 204 204 VAL VAL A . n 
A 1 227 SER 227 205 205 SER SER A . n 
A 1 228 ASP 228 206 206 ASP ASP A . n 
A 1 229 GLN 229 207 207 GLN GLN A . n 
A 1 230 ASN 230 208 208 ASN ASN A . n 
A 1 231 GLY 231 209 209 GLY GLY A . n 
A 1 232 GLY 232 210 210 GLY GLY A . n 
A 1 233 THR 233 211 211 THR THR A . n 
A 1 234 LYS 234 212 212 LYS LYS A . n 
A 1 235 THR 235 213 213 THR THR A . n 
A 1 236 LYS 236 214 214 LYS LYS A . n 
A 1 237 THR 237 215 215 THR THR A . n 
A 1 238 GLN 238 216 216 GLN GLN A . n 
A 1 239 THR 239 217 217 THR THR A . n 
A 1 240 ILE 240 218 218 ILE ILE A . n 
A 1 241 ASP 241 219 219 ASP ASP A . n 
A 1 242 GLY 242 220 220 GLY GLY A . n 
A 1 243 LYS 243 221 221 LYS LYS A . n 
A 1 244 THR 244 222 222 THR THR A . n 
A 1 245 VAL 245 223 223 VAL VAL A . n 
A 1 246 THR 246 224 224 THR THR A . n 
A 1 247 THR 247 225 225 THR THR A . n 
A 1 248 THR 248 226 226 THR THR A . n 
A 1 249 ILE 249 227 227 ILE ILE A . n 
A 1 250 SER 250 228 228 SER SER A . n 
A 1 251 SER 251 229 229 SER SER A . n 
A 1 252 LYS 252 230 230 LYS LYS A . n 
A 1 253 VAL 253 231 231 VAL VAL A . n 
A 1 254 VAL 254 232 232 VAL VAL A . n 
A 1 255 ASP 255 233 233 ASP ASP A . n 
A 1 256 SER 256 234 234 SER SER A . n 
A 1 257 GLN 257 235 235 GLN GLN A . n 
A 1 258 ALA 258 236 236 ALA ALA A . n 
A 1 259 LYS 259 237 237 LYS LYS A . n 
A 1 260 GLY 260 238 238 GLY GLY A . n 
A 1 261 ASN 261 239 239 ASN ASN A . n 
A 1 262 THR 262 240 240 THR THR A . n 
A 1 263 THR 263 241 241 THR THR A . n 
A 1 264 ARG 264 242 242 ARG ARG A . n 
A 1 265 VAL 265 243 243 VAL VAL A . n 
A 1 266 SER 266 244 244 SER SER A . n 
A 1 267 TYR 267 245 245 TYR TYR A . n 
A 1 268 THR 268 246 246 THR THR A . n 
A 1 269 GLU 269 247 247 GLU GLU A . n 
A 1 270 ILE 270 248 248 ILE ILE A . n 
A 1 271 THR 271 249 249 THR THR A . n 
A 1 272 ASN 272 250 250 ASN ASN A . n 
A 1 273 LYS 273 251 251 LYS LYS A . n 
A 1 274 LEU 274 252 252 LEU LEU A . n 
A 1 275 ASP 275 253 253 ASP ASP A . n 
A 1 276 GLY 276 254 254 GLY GLY A . n 
A 1 277 VAL 277 255 255 VAL VAL A . n 
A 1 278 PRO 278 256 256 PRO PRO A . n 
A 1 279 ASP 279 257 257 ASP ASP A . n 
A 1 280 SER 280 258 258 SER SER A . n 
A 1 281 ALA 281 259 259 ALA ALA A . n 
A 1 282 GLN 282 260 260 GLN GLN A . n 
A 1 283 ALA 283 261 261 ALA ALA A . n 
A 1 284 LEU 284 262 262 LEU LEU A . n 
A 1 285 LEU 285 263 263 LEU LEU A . n 
A 1 286 ALA 286 264 264 ALA ALA A . n 
A 1 287 GLN 287 265 265 GLN GLN A . n 
A 1 288 ALA 288 266 266 ALA ALA A . n 
A 1 289 SER 289 267 267 SER SER A . n 
A 1 290 THR 290 268 268 THR THR A . n 
A 1 291 LEU 291 269 269 LEU LEU A . n 
A 1 292 ILE 292 270 270 ILE ILE A . n 
A 1 293 ASN 293 271 271 ASN ASN A . n 
A 1 294 THR 294 272 272 THR THR A . n 
A 1 295 ILE 295 273 273 ILE ILE A . n 
A 1 296 ASN 296 274 274 ASN ASN A . n 
A 1 297 THR 297 275 275 THR THR A . n 
A 1 298 ALA 298 276 276 ALA ALA A . n 
A 1 299 CYS 299 277 277 CYS CYS A . n 
A 1 300 PRO 300 278 278 PRO PRO A . n 
A 1 301 TYR 301 279 279 TYR TYR A . n 
A 1 302 PHE 302 280 280 PHE PHE A . n 
A 1 303 SER 303 281 281 SER SER A . n 
A 1 304 VAL 304 282 282 VAL VAL A . n 
A 1 305 THR 305 283 ?   ?   ?   A . n 
A 1 306 ASN 306 284 ?   ?   ?   A . n 
A 1 307 LYS 307 285 ?   ?   ?   A . n 
A 1 308 SER 308 286 ?   ?   ?   A . n 
A 1 309 GLY 309 287 ?   ?   ?   A . n 
A 1 310 GLY 310 288 ?   ?   ?   A . n 
A 1 311 PRO 311 289 ?   ?   ?   A . n 
A 1 312 GLN 312 290 ?   ?   ?   A . n 
A 1 313 MET 313 291 ?   ?   ?   A . n 
A 1 314 GLU 314 292 ?   ?   ?   A . n 
A 1 315 PRO 315 293 ?   ?   ?   A . n 
A 1 316 THR 316 294 294 THR THR A . n 
A 1 317 ARG 317 295 295 ARG ARG A . n 
A 1 318 GLY 318 296 296 GLY GLY A . n 
A 1 319 LYS 319 297 297 LYS LYS A . n 
A 1 320 LEU 320 298 298 LEU LEU A . n 
A 1 321 CYS 321 299 299 CYS CYS A . n 
A 1 322 GLY 322 300 300 GLY GLY A . n 
A 1 323 PHE 323 301 301 PHE PHE A . n 
A 1 324 THR 324 302 302 THR THR A . n 
A 1 325 GLU 325 303 303 GLU GLU A . n 
A 1 326 GLU 326 304 304 GLU GLU A . n 
A 1 327 ILE 327 305 305 ILE ILE A . n 
A 1 328 SER 328 306 306 SER SER A . n 
A 1 329 ALA 329 307 307 ALA ALA A . n 
A 1 330 ILE 330 308 308 ILE ILE A . n 
A 1 331 GLN 331 309 309 GLN GLN A . n 
A 1 332 LYS 332 310 310 LYS LYS A . n 
A 1 333 MET 333 311 311 MET MET A . n 
A 1 334 ILE 334 312 312 ILE ILE A . n 
A 1 335 THR 335 313 313 THR THR A . n 
A 1 336 ASP 336 314 314 ASP ASP A . n 
A 1 337 ALA 337 315 315 ALA ALA A . n 
A 1 338 GLN 338 316 316 GLN GLN A . n 
A 1 339 GLU 339 317 317 GLU GLU A . n 
A 1 340 LEU 340 318 318 LEU LEU A . n 
A 1 341 VAL 341 319 319 VAL VAL A . n 
A 1 342 ASN 342 320 320 ASN ASN A . n 
A 1 343 GLN 343 321 321 GLN GLN A . n 
A 1 344 THR 344 322 322 THR THR A . n 
A 1 345 SER 345 323 323 SER SER A . n 
A 1 346 VAL 346 324 324 VAL VAL A . n 
A 1 347 ILE 347 325 325 ILE ILE A . n 
A 1 348 ASN 348 326 326 ASN ASN A . n 
A 1 349 GLU 349 327 327 GLU GLU A . n 
A 1 350 HIS 350 328 328 HIS HIS A . n 
A 1 351 GLU 351 329 329 GLU GLU A . n 
A 1 352 GLN 352 330 330 GLN GLN A . n 
A 1 353 SER 353 331 331 SER SER A . n 
A 1 354 THR 354 332 332 THR THR A . n 
A 1 355 PRO 355 333 333 PRO PRO A . n 
A 1 356 VAL 356 334 334 VAL VAL A . n 
A 1 357 GLY 357 335 335 GLY GLY A . n 
A 1 358 GLY 358 336 336 GLY GLY A . n 
A 1 359 ASN 359 337 337 ASN ASN A . n 
A 1 360 ASN 360 338 338 ASN ASN A . n 
A 1 361 GLY 361 339 339 GLY GLY A . n 
A 1 362 LYS 362 340 340 LYS LYS A . n 
A 1 363 PRO 363 341 341 PRO PRO A . n 
A 1 364 PHE 364 342 342 PHE PHE A . n 
A 1 365 ASN 365 343 343 ASN ASN A . n 
A 1 366 PRO 366 344 344 PRO PRO A . n 
A 1 367 PHE 367 345 345 PHE PHE A . n 
A 1 368 THR 368 346 346 THR THR A . n 
A 1 369 ASP 369 347 347 ASP ASP A . n 
A 1 370 ALA 370 348 348 ALA ALA A . n 
A 1 371 SER 371 349 349 SER SER A . n 
A 1 372 PHE 372 350 350 PHE PHE A . n 
A 1 373 ALA 373 351 351 ALA ALA A . n 
A 1 374 GLN 374 352 352 GLN GLN A . n 
A 1 375 GLY 375 353 353 GLY GLY A . n 
A 1 376 MET 376 354 354 MET MET A . n 
A 1 377 LEU 377 355 355 LEU LEU A . n 
A 1 378 ALA 378 356 356 ALA ALA A . n 
A 1 379 ASN 379 357 357 ASN ASN A . n 
A 1 380 ALA 380 358 358 ALA ALA A . n 
A 1 381 SER 381 359 359 SER SER A . n 
A 1 382 ALA 382 360 360 ALA ALA A . n 
A 1 383 GLN 383 361 361 GLN GLN A . n 
A 1 384 ALA 384 362 362 ALA ALA A . n 
A 1 385 LYS 385 363 363 LYS LYS A . n 
A 1 386 MET 386 364 364 MET MET A . n 
A 1 387 LEU 387 365 365 LEU LEU A . n 
A 1 388 ASN 388 366 366 ASN ASN A . n 
A 1 389 LEU 389 367 367 LEU LEU A . n 
A 1 390 ALA 390 368 368 ALA ALA A . n 
A 1 391 HIS 391 369 369 HIS HIS A . n 
A 1 392 GLN 392 370 370 GLN GLN A . n 
A 1 393 VAL 393 371 371 VAL VAL A . n 
A 1 394 GLY 394 372 372 GLY GLY A . n 
A 1 395 GLN 395 373 373 GLN GLN A . n 
A 1 396 THR 396 374 374 THR THR A . n 
A 1 397 ILE 397 375 375 ILE ILE A . n 
A 1 398 ASN 398 376 376 ASN ASN A . n 
A 1 399 PRO 399 377 377 PRO PRO A . n 
A 1 400 ASP 400 378 378 ASP ASP A . n 
A 1 401 ASN 401 379 379 ASN ASN A . n 
A 1 402 LEU 402 380 380 LEU LEU A . n 
A 1 403 THR 403 381 381 THR THR A . n 
A 1 404 GLY 404 382 382 GLY GLY A . n 
A 1 405 THR 405 383 383 THR THR A . n 
A 1 406 PHE 406 384 384 PHE PHE A . n 
A 1 407 LYS 407 385 385 LYS LYS A . n 
A 1 408 ASN 408 386 386 ASN ASN A . n 
A 1 409 PHE 409 387 387 PHE PHE A . n 
A 1 410 VAL 410 388 388 VAL VAL A . n 
A 1 411 THR 411 389 389 THR THR A . n 
A 1 412 GLY 412 390 390 GLY GLY A . n 
A 1 413 PHE 413 391 391 PHE PHE A . n 
A 1 414 LEU 414 392 392 LEU LEU A . n 
A 1 415 ALA 415 393 393 ALA ALA A . n 
A 1 416 THR 416 394 394 THR THR A . n 
A 1 417 CYS 417 395 395 CYS CYS A . n 
A 1 418 ASN 418 396 396 ASN ASN A . n 
A 1 419 ASN 419 397 397 ASN ASN A . n 
A 1 420 LYS 420 398 ?   ?   ?   A . n 
A 1 421 SER 421 399 ?   ?   ?   A . n 
A 1 422 THR 422 400 ?   ?   ?   A . n 
A 1 423 ALA 423 401 ?   ?   ?   A . n 
A 1 424 GLY 424 402 ?   ?   ?   A . n 
A 1 425 THR 425 403 ?   ?   ?   A . n 
A 1 426 SER 426 404 ?   ?   ?   A . n 
A 1 427 GLY 427 405 ?   ?   ?   A . n 
A 1 428 THR 428 406 ?   ?   ?   A . n 
A 1 429 GLN 429 407 ?   ?   ?   A . n 
A 1 430 GLY 430 408 ?   ?   ?   A . n 
A 1 431 SER 431 409 409 SER SER A . n 
A 1 432 PRO 432 410 410 PRO PRO A . n 
A 1 433 PRO 433 411 411 PRO PRO A . n 
A 1 434 GLY 434 412 412 GLY GLY A . n 
A 1 435 THR 435 413 413 THR THR A . n 
A 1 436 VAL 436 414 414 VAL VAL A . n 
A 1 437 THR 437 415 415 THR THR A . n 
A 1 438 THR 438 416 416 THR THR A . n 
A 1 439 GLN 439 417 417 GLN GLN A . n 
A 1 440 THR 440 418 418 THR THR A . n 
A 1 441 PHE 441 419 419 PHE PHE A . n 
A 1 442 ALA 442 420 420 ALA ALA A . n 
A 1 443 SER 443 421 421 SER SER A . n 
A 1 444 GLY 444 422 422 GLY GLY A . n 
A 1 445 CYS 445 423 423 CYS CYS A . n 
A 1 446 ALA 446 424 424 ALA ALA A . n 
A 1 447 TYR 447 425 425 TYR TYR A . n 
A 1 448 VAL 448 426 426 VAL VAL A . n 
A 1 449 GLU 449 427 427 GLU GLU A . n 
A 1 450 GLN 450 428 428 GLN GLN A . n 
A 1 451 THR 451 429 429 THR THR A . n 
A 1 452 ILE 452 430 430 ILE ILE A . n 
A 1 453 THR 453 431 431 THR THR A . n 
A 1 454 ASN 454 432 432 ASN ASN A . n 
A 1 455 LEU 455 433 433 LEU LEU A . n 
A 1 456 ASN 456 434 434 ASN ASN A . n 
A 1 457 ASN 457 435 435 ASN ASN A . n 
A 1 458 SER 458 436 436 SER SER A . n 
A 1 459 ILE 459 437 437 ILE ILE A . n 
A 1 460 ALA 460 438 438 ALA ALA A . n 
A 1 461 HIS 461 439 439 HIS HIS A . n 
A 1 462 PHE 462 440 440 PHE PHE A . n 
A 1 463 GLY 463 441 441 GLY GLY A . n 
A 1 464 THR 464 442 442 THR THR A . n 
A 1 465 GLN 465 443 443 GLN GLN A . n 
A 1 466 GLU 466 444 444 GLU GLU A . n 
A 1 467 GLN 467 445 445 GLN GLN A . n 
A 1 468 GLN 468 446 446 GLN GLN A . n 
A 1 469 ILE 469 447 447 ILE ILE A . n 
A 1 470 GLN 470 448 448 GLN GLN A . n 
A 1 471 GLN 471 449 449 GLN GLN A . n 
A 1 472 ALA 472 450 450 ALA ALA A . n 
A 1 473 GLU 473 451 451 GLU GLU A . n 
A 1 474 ASN 474 452 452 ASN ASN A . n 
A 1 475 ILE 475 453 453 ILE ILE A . n 
A 1 476 ALA 476 454 454 ALA ALA A . n 
A 1 477 ASP 477 455 455 ASP ASP A . n 
A 1 478 THR 478 456 456 THR THR A . n 
A 1 479 LEU 479 457 457 LEU LEU A . n 
A 1 480 VAL 480 458 458 VAL VAL A . n 
A 1 481 ASN 481 459 459 ASN ASN A . n 
A 1 482 PHE 482 460 460 PHE PHE A . n 
A 1 483 LYS 483 461 461 LYS LYS A . n 
A 1 484 SER 484 462 462 SER SER A . n 
A 1 485 ARG 485 463 463 ARG ARG A . n 
A 1 486 TYR 486 464 464 TYR TYR A . n 
A 1 487 SER 487 465 465 SER SER A . n 
A 1 488 GLU 488 466 466 GLU GLU A . n 
A 1 489 LEU 489 467 467 LEU LEU A . n 
A 1 490 GLY 490 468 468 GLY GLY A . n 
A 1 491 ASN 491 469 469 ASN ASN A . n 
A 1 492 THR 492 470 470 THR THR A . n 
A 1 493 TYR 493 471 471 TYR TYR A . n 
A 1 494 ASN 494 472 472 ASN ASN A . n 
A 1 495 SER 495 473 473 SER SER A . n 
A 1 496 ILE 496 474 474 ILE ILE A . n 
A 1 497 THR 497 475 475 THR THR A . n 
A 1 498 THR 498 476 476 THR THR A . n 
A 1 499 ALA 499 477 477 ALA ALA A . n 
A 1 500 LEU 500 478 478 LEU LEU A . n 
A 1 501 SER 501 479 479 SER SER A . n 
A 1 502 LYS 502 480 480 LYS LYS A . n 
A 1 503 VAL 503 481 481 VAL VAL A . n 
A 1 504 PRO 504 482 482 PRO PRO A . n 
A 1 505 ASN 505 483 483 ASN ASN A . n 
A 1 506 ALA 506 484 484 ALA ALA A . n 
A 1 507 GLN 507 485 485 GLN GLN A . n 
A 1 508 SER 508 486 486 SER SER A . n 
A 1 509 LEU 509 487 487 LEU LEU A . n 
A 1 510 GLN 510 488 488 GLN GLN A . n 
A 1 511 ASN 511 489 489 ASN ASN A . n 
A 1 512 VAL 512 490 490 VAL VAL A . n 
A 1 513 VAL 513 491 491 VAL VAL A . n 
A 1 514 GLY 514 492 492 GLY GLY A . n 
A 1 515 LYS 515 493 493 LYS LYS A . n 
A 1 516 LYS 516 494 494 LYS LYS A . n 
A 1 517 ASN 517 495 495 ASN ASN A . n 
A 1 518 ASN 518 496 496 ASN ASN A . n 
A 1 519 PRO 519 497 497 PRO PRO A . n 
A 1 520 TYR 520 498 498 TYR TYR A . n 
A 1 521 SER 521 499 499 SER SER A . n 
A 1 522 PRO 522 500 500 PRO PRO A . n 
A 1 523 GLN 523 501 501 GLN GLN A . n 
A 1 524 GLY 524 502 502 GLY GLY A . n 
A 1 525 ILE 525 503 503 ILE ILE A . n 
A 1 526 GLU 526 504 504 GLU GLU A . n 
A 1 527 THR 527 505 505 THR THR A . n 
A 1 528 ASN 528 506 506 ASN ASN A . n 
A 1 529 TYR 529 507 507 TYR TYR A . n 
A 1 530 TYR 530 508 508 TYR TYR A . n 
A 1 531 LEU 531 509 509 LEU LEU A . n 
A 1 532 ASN 532 510 510 ASN ASN A . n 
A 1 533 GLN 533 511 511 GLN GLN A . n 
A 1 534 ASN 534 512 512 ASN ASN A . n 
A 1 535 SER 535 513 513 SER SER A . n 
A 1 536 TYR 536 514 514 TYR TYR A . n 
A 1 537 ASN 537 515 515 ASN ASN A . n 
A 1 538 GLN 538 516 516 GLN GLN A . n 
A 1 539 ILE 539 517 517 ILE ILE A . n 
A 1 540 GLN 540 518 518 GLN GLN A . n 
A 1 541 THR 541 519 519 THR THR A . n 
A 1 542 ILE 542 520 520 ILE ILE A . n 
A 1 543 ASN 543 521 521 ASN ASN A . n 
A 1 544 GLN 544 522 522 GLN GLN A . n 
A 1 545 GLU 545 523 523 GLU GLU A . n 
A 1 546 LEU 546 524 524 LEU LEU A . n 
A 1 547 LYS 547 525 ?   ?   ?   A . n 
A 1 548 LYS 548 526 ?   ?   ?   A . n 
A 1 549 LYS 549 527 ?   ?   ?   A . n 
A 1 550 LYS 550 528 ?   ?   ?   A . n 
A 1 551 LYS 551 529 ?   ?   ?   A . n 
A 1 552 LYS 552 530 ?   ?   ?   A . n 
A 1 553 GLY 553 531 ?   ?   ?   A . n 
A 1 554 SER 554 532 ?   ?   ?   A . n 
A 1 555 GLU 555 533 ?   ?   ?   A . n 
A 1 556 GLN 556 534 ?   ?   ?   A . n 
A 1 557 LYS 557 535 ?   ?   ?   A . n 
A 1 558 LEU 558 536 ?   ?   ?   A . n 
A 1 559 ILE 559 537 ?   ?   ?   A . n 
A 1 560 SER 560 538 ?   ?   ?   A . n 
A 1 561 GLU 561 539 ?   ?   ?   A . n 
A 1 562 GLU 562 540 ?   ?   ?   A . n 
A 1 563 ASP 563 541 ?   ?   ?   A . n 
A 1 564 LEU 564 542 ?   ?   ?   A . n 
A 1 565 SER 565 543 ?   ?   ?   A . n 
A 1 566 HIS 566 544 ?   ?   ?   A . n 
A 1 567 HIS 567 545 ?   ?   ?   A . n 
A 1 568 HIS 568 546 ?   ?   ?   A . n 
A 1 569 HIS 569 547 ?   ?   ?   A . n 
A 1 570 HIS 570 548 ?   ?   ?   A . n 
A 1 571 HIS 571 549 ?   ?   ?   A . 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 
B 2 CD  1   601 1   CD  CD  A . 
C 2 CD  1   602 2   CD  CD  A . 
D 2 CD  1   603 3   CD  CD  A . 
E 2 CD  1   604 4   CD  CD  A . 
F 2 CD  1   605 5   CD  CD  A . 
G 2 CD  1   606 6   CD  CD  A . 
H 2 CD  1   607 7   CD  CD  A . 
I 2 CD  1   608 8   CD  CD  A . 
J 2 CD  1   609 9   CD  CD  A . 
K 2 CD  1   610 10  CD  CD  A . 
L 3 HOH 1   701 37  HOH HOH A . 
L 3 HOH 2   702 183 HOH HOH A . 
L 3 HOH 3   703 306 HOH HOH A . 
L 3 HOH 4   704 227 HOH HOH A . 
L 3 HOH 5   705 159 HOH HOH A . 
L 3 HOH 6   706 66  HOH HOH A . 
L 3 HOH 7   707 78  HOH HOH A . 
L 3 HOH 8   708 92  HOH HOH A . 
L 3 HOH 9   709 197 HOH HOH A . 
L 3 HOH 10  710 209 HOH HOH A . 
L 3 HOH 11  711 85  HOH HOH A . 
L 3 HOH 12  712 38  HOH HOH A . 
L 3 HOH 13  713 140 HOH HOH A . 
L 3 HOH 14  714 107 HOH HOH A . 
L 3 HOH 15  715 263 HOH HOH A . 
L 3 HOH 16  716 282 HOH HOH A . 
L 3 HOH 17  717 116 HOH HOH A . 
L 3 HOH 18  718 50  HOH HOH A . 
L 3 HOH 19  719 114 HOH HOH A . 
L 3 HOH 20  720 150 HOH HOH A . 
L 3 HOH 21  721 5   HOH HOH A . 
L 3 HOH 22  722 71  HOH HOH A . 
L 3 HOH 23  723 258 HOH HOH A . 
L 3 HOH 24  724 250 HOH HOH A . 
L 3 HOH 25  725 44  HOH HOH A . 
L 3 HOH 26  726 296 HOH HOH A . 
L 3 HOH 27  727 54  HOH HOH A . 
L 3 HOH 28  728 89  HOH HOH A . 
L 3 HOH 29  729 7   HOH HOH A . 
L 3 HOH 30  730 15  HOH HOH A . 
L 3 HOH 31  731 148 HOH HOH A . 
L 3 HOH 32  732 6   HOH HOH A . 
L 3 HOH 33  733 65  HOH HOH A . 
L 3 HOH 34  734 36  HOH HOH A . 
L 3 HOH 35  735 156 HOH HOH A . 
L 3 HOH 36  736 112 HOH HOH A . 
L 3 HOH 37  737 17  HOH HOH A . 
L 3 HOH 38  738 67  HOH HOH A . 
L 3 HOH 39  739 135 HOH HOH A . 
L 3 HOH 40  740 27  HOH HOH A . 
L 3 HOH 41  741 21  HOH HOH A . 
L 3 HOH 42  742 24  HOH HOH A . 
L 3 HOH 43  743 286 HOH HOH A . 
L 3 HOH 44  744 185 HOH HOH A . 
L 3 HOH 45  745 195 HOH HOH A . 
L 3 HOH 46  746 82  HOH HOH A . 
L 3 HOH 47  747 97  HOH HOH A . 
L 3 HOH 48  748 270 HOH HOH A . 
L 3 HOH 49  749 39  HOH HOH A . 
L 3 HOH 50  750 131 HOH HOH A . 
L 3 HOH 51  751 312 HOH HOH A . 
L 3 HOH 52  752 188 HOH HOH A . 
L 3 HOH 53  753 291 HOH HOH A . 
L 3 HOH 54  754 59  HOH HOH A . 
L 3 HOH 55  755 33  HOH HOH A . 
L 3 HOH 56  756 9   HOH HOH A . 
L 3 HOH 57  757 244 HOH HOH A . 
L 3 HOH 58  758 229 HOH HOH A . 
L 3 HOH 59  759 218 HOH HOH A . 
L 3 HOH 60  760 14  HOH HOH A . 
L 3 HOH 61  761 23  HOH HOH A . 
L 3 HOH 62  762 111 HOH HOH A . 
L 3 HOH 63  763 18  HOH HOH A . 
L 3 HOH 64  764 34  HOH HOH A . 
L 3 HOH 65  765 31  HOH HOH A . 
L 3 HOH 66  766 129 HOH HOH A . 
L 3 HOH 67  767 271 HOH HOH A . 
L 3 HOH 68  768 173 HOH HOH A . 
L 3 HOH 69  769 75  HOH HOH A . 
L 3 HOH 70  770 311 HOH HOH A . 
L 3 HOH 71  771 275 HOH HOH A . 
L 3 HOH 72  772 29  HOH HOH A . 
L 3 HOH 73  773 184 HOH HOH A . 
L 3 HOH 74  774 19  HOH HOH A . 
L 3 HOH 75  775 252 HOH HOH A . 
L 3 HOH 76  776 191 HOH HOH A . 
L 3 HOH 77  777 28  HOH HOH A . 
L 3 HOH 78  778 143 HOH HOH A . 
L 3 HOH 79  779 249 HOH HOH A . 
L 3 HOH 80  780 40  HOH HOH A . 
L 3 HOH 81  781 16  HOH HOH A . 
L 3 HOH 82  782 25  HOH HOH A . 
L 3 HOH 83  783 272 HOH HOH A . 
L 3 HOH 84  784 22  HOH HOH A . 
L 3 HOH 85  785 164 HOH HOH A . 
L 3 HOH 86  786 64  HOH HOH A . 
L 3 HOH 87  787 45  HOH HOH A . 
L 3 HOH 88  788 295 HOH HOH A . 
L 3 HOH 89  789 251 HOH HOH A . 
L 3 HOH 90  790 240 HOH HOH A . 
L 3 HOH 91  791 160 HOH HOH A . 
L 3 HOH 92  792 236 HOH HOH A . 
L 3 HOH 93  793 170 HOH HOH A . 
L 3 HOH 94  794 228 HOH HOH A . 
L 3 HOH 95  795 266 HOH HOH A . 
L 3 HOH 96  796 117 HOH HOH A . 
L 3 HOH 97  797 167 HOH HOH A . 
L 3 HOH 98  798 238 HOH HOH A . 
L 3 HOH 99  799 95  HOH HOH A . 
L 3 HOH 100 800 47  HOH HOH A . 
L 3 HOH 101 801 104 HOH HOH A . 
L 3 HOH 102 802 130 HOH HOH A . 
L 3 HOH 103 803 11  HOH HOH A . 
L 3 HOH 104 804 146 HOH HOH A . 
L 3 HOH 105 805 77  HOH HOH A . 
L 3 HOH 106 806 181 HOH HOH A . 
L 3 HOH 107 807 283 HOH HOH A . 
L 3 HOH 108 808 127 HOH HOH A . 
L 3 HOH 109 809 125 HOH HOH A . 
L 3 HOH 110 810 98  HOH HOH A . 
L 3 HOH 111 811 274 HOH HOH A . 
L 3 HOH 112 812 48  HOH HOH A . 
L 3 HOH 113 813 61  HOH HOH A . 
L 3 HOH 114 814 86  HOH HOH A . 
L 3 HOH 115 815 105 HOH HOH A . 
L 3 HOH 116 816 182 HOH HOH A . 
L 3 HOH 117 817 128 HOH HOH A . 
L 3 HOH 118 818 56  HOH HOH A . 
L 3 HOH 119 819 298 HOH HOH A . 
L 3 HOH 120 820 142 HOH HOH A . 
L 3 HOH 121 821 172 HOH HOH A . 
L 3 HOH 122 822 168 HOH HOH A . 
L 3 HOH 123 823 76  HOH HOH A . 
L 3 HOH 124 824 53  HOH HOH A . 
L 3 HOH 125 825 80  HOH HOH A . 
L 3 HOH 126 826 93  HOH HOH A . 
L 3 HOH 127 827 176 HOH HOH A . 
L 3 HOH 128 828 69  HOH HOH A . 
L 3 HOH 129 829 308 HOH HOH A . 
L 3 HOH 130 830 72  HOH HOH A . 
L 3 HOH 131 831 264 HOH HOH A . 
L 3 HOH 132 832 293 HOH HOH A . 
L 3 HOH 133 833 223 HOH HOH A . 
L 3 HOH 134 834 243 HOH HOH A . 
L 3 HOH 135 835 20  HOH HOH A . 
L 3 HOH 136 836 254 HOH HOH A . 
L 3 HOH 137 837 115 HOH HOH A . 
L 3 HOH 138 838 247 HOH HOH A . 
L 3 HOH 139 839 62  HOH HOH A . 
L 3 HOH 140 840 57  HOH HOH A . 
L 3 HOH 141 841 79  HOH HOH A . 
L 3 HOH 142 842 241 HOH HOH A . 
L 3 HOH 143 843 171 HOH HOH A . 
L 3 HOH 144 844 297 HOH HOH A . 
L 3 HOH 145 845 189 HOH HOH A . 
L 3 HOH 146 846 269 HOH HOH A . 
L 3 HOH 147 847 101 HOH HOH A . 
L 3 HOH 148 848 287 HOH HOH A . 
L 3 HOH 149 849 242 HOH HOH A . 
L 3 HOH 150 850 154 HOH HOH A . 
L 3 HOH 151 851 12  HOH HOH A . 
L 3 HOH 152 852 144 HOH HOH A . 
L 3 HOH 153 853 246 HOH HOH A . 
L 3 HOH 154 854 32  HOH HOH A . 
L 3 HOH 155 855 225 HOH HOH A . 
L 3 HOH 156 856 284 HOH HOH A . 
L 3 HOH 157 857 4   HOH HOH A . 
L 3 HOH 158 858 13  HOH HOH A . 
L 3 HOH 159 859 245 HOH HOH A . 
L 3 HOH 160 860 316 HOH HOH A . 
L 3 HOH 161 861 256 HOH HOH A . 
L 3 HOH 162 862 73  HOH HOH A . 
L 3 HOH 163 863 304 HOH HOH A . 
L 3 HOH 164 864 83  HOH HOH A . 
L 3 HOH 165 865 103 HOH HOH A . 
L 3 HOH 166 866 217 HOH HOH A . 
L 3 HOH 167 867 268 HOH HOH A . 
L 3 HOH 168 868 187 HOH HOH A . 
L 3 HOH 169 869 139 HOH HOH A . 
L 3 HOH 170 870 177 HOH HOH A . 
L 3 HOH 171 871 310 HOH HOH A . 
L 3 HOH 172 872 281 HOH HOH A . 
L 3 HOH 173 873 200 HOH HOH A . 
L 3 HOH 174 874 294 HOH HOH A . 
L 3 HOH 175 875 309 HOH HOH A . 
L 3 HOH 176 876 248 HOH HOH A . 
L 3 HOH 177 877 213 HOH HOH A . 
L 3 HOH 178 878 74  HOH HOH A . 
L 3 HOH 179 879 279 HOH HOH A . 
L 3 HOH 180 880 257 HOH HOH A . 
L 3 HOH 181 881 315 HOH HOH A . 
L 3 HOH 182 882 299 HOH HOH A . 
L 3 HOH 183 883 166 HOH HOH A . 
L 3 HOH 184 884 273 HOH HOH A . 
L 3 HOH 185 885 123 HOH HOH A . 
L 3 HOH 186 886 70  HOH HOH A . 
L 3 HOH 187 887 278 HOH HOH A . 
L 3 HOH 188 888 260 HOH HOH A . 
L 3 HOH 189 889 49  HOH HOH A . 
L 3 HOH 190 890 205 HOH HOH A . 
L 3 HOH 191 891 277 HOH HOH A . 
L 3 HOH 192 892 313 HOH HOH A . 
L 3 HOH 193 893 265 HOH HOH A . 
L 3 HOH 194 894 84  HOH HOH A . 
L 3 HOH 195 895 81  HOH HOH A . 
L 3 HOH 196 896 305 HOH HOH A . 
L 3 HOH 197 897 26  HOH HOH A . 
L 3 HOH 198 898 221 HOH HOH A . 
L 3 HOH 199 899 290 HOH HOH A . 
L 3 HOH 200 900 314 HOH HOH A . 
L 3 HOH 201 901 55  HOH HOH A . 
L 3 HOH 202 902 276 HOH HOH A . 
L 3 HOH 203 903 292 HOH HOH A . 
L 3 HOH 204 904 233 HOH HOH A . 
L 3 HOH 205 905 259 HOH HOH A . 
# 
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  ? ? ? '(1.17.1_3660: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R4P 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.613 
_cell.length_a_esd                 ? 
_cell.length_b                     96.953 
_cell.length_b_esd                 ? 
_cell.length_c                     97.408 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8R4P 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8R4P 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.18 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M cadmium chloride
0.1 M sodium acetate pH 4.6
30% (v/v) PEG 400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 X 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          33.89 
_reflns.entry_id                                       8R4P 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2 
_reflns.d_resolution_low                               36.64 
_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                                     35796 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.53 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.83 
_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                                0.08534 
_reflns.pdbx_Rpim_I_all                                0.03854 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07556 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2 
_reflns_shell.d_res_low                                     2.071 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3574 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.5 
_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                               1.089 
_reflns_shell.pdbx_Rpim_I_all                               0.4935 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.535 
_reflns_shell.pdbx_CC_star                                  0.835 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.94 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.9625 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8R4P 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             36.64 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     35794 
_refine.ls_number_reflns_R_free                  1783 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.55 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2124 
_refine.ls_R_factor_R_free                       0.2470 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2106 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.50 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        36.64 
_refine_hist.number_atoms_solvent             205 
_refine_hist.number_atoms_total               3814 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3599 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002 ? 3660 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.461 ? 4982 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.086 ? 506  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.035 ? 584  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.002 ? 662  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.05  . . 136 2618 100.00 . . . . 0.2712 . . . . . . . . . . . 0.2858 
'X-RAY DIFFRACTION' 2.05 2.11  . . 140 2610 100.00 . . . . 0.2744 . . . . . . . . . . . 0.3440 
'X-RAY DIFFRACTION' 2.11 2.18  . . 138 2582 100.00 . . . . 0.2523 . . . . . . . . . . . 0.3086 
'X-RAY DIFFRACTION' 2.18 2.26  . . 135 2617 100.00 . . . . 0.2453 . . . . . . . . . . . 0.2739 
'X-RAY DIFFRACTION' 2.26 2.35  . . 136 2615 100.00 . . . . 0.2279 . . . . . . . . . . . 0.2746 
'X-RAY DIFFRACTION' 2.35 2.46  . . 135 2606 99.00  . . . . 0.2160 . . . . . . . . . . . 0.2471 
'X-RAY DIFFRACTION' 2.46 2.59  . . 136 2618 99.00  . . . . 0.2260 . . . . . . . . . . . 0.2527 
'X-RAY DIFFRACTION' 2.59 2.75  . . 132 2548 96.00  . . . . 0.2202 . . . . . . . . . . . 0.2618 
'X-RAY DIFFRACTION' 2.75 2.96  . . 138 2619 98.00  . . . . 0.2139 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 2.96 3.26  . . 136 2631 99.00  . . . . 0.2157 . . . . . . . . . . . 0.2512 
'X-RAY DIFFRACTION' 3.26 3.73  . . 140 2629 98.00  . . . . 0.1983 . . . . . . . . . . . 0.2283 
'X-RAY DIFFRACTION' 3.73 4.70  . . 137 2615 97.00  . . . . 0.1729 . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 4.70 36.64 . . 144 2703 95.00  . . . . 0.2089 . . . . . . . . . . . 0.2433 
# 
_struct.entry_id                     8R4P 
_struct.title                        'Structure of BabA from Helicobacter pylori strain 17875' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8R4P 
_struct_keywords.text            'ADHESIN, LECTIN, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O52269_HELPX 
_struct_ref.pdbx_db_accession          O52269 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EDDGFYTSVGYQIGEAAQMVTNTKGIQDLSDNYENLSKLLTRYSTLNTLIKLSADPSAINAARENLGASAKNLIGDTKNS
PAYQAVLLAINAAVGFWNVLGYATQCGGNANGQESTSSTTIFNNEPGYRSTSITCSLNRYKPGYYGPMSIENFKKLNEAY
QILQTALNKGLPALKENNGTVSVTYTYTCSGEGNDNCSKKATGVSDQNGGTKTKTQTIDGKTVTTTISSKVVDSQAKGNT
TRVSYTEITNKLDGVPDSAQALLAQASTLINTINTACPYFSVTNKSGGPQMEPTRGKLCGFTEEISAIQKMITDAQELVN
QTSVINEHEQSTPVGGNNGKPFNPFTDASFAQGMLANASAQAKMLNLAHQVGQTINPDNLTGTFKNFVTGFLATCNNKST
AGTSGTQGSPPGTVTTQTFASGCAYVEQTITNLNNSIAHFGTQEQQIQQAENIADTLVNFKSRYSELGNTYNSITTALSK
VPNAQSLQNVVGKKNNPYSPQGIETNYYLNQNSYNQIQTINQEL
;
_struct_ref.pdbx_align_begin           21 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8R4P 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 23 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 546 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O52269 
_struct_ref_seq.db_align_beg                  21 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  544 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       524 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8R4P MET A 1   ? UNP O52269 ? ? 'initiating methionine' -21 1  
1 8R4P LYS A 2   ? UNP O52269 ? ? 'expression tag'        -20 2  
1 8R4P TYR A 3   ? UNP O52269 ? ? 'expression tag'        -19 3  
1 8R4P LEU A 4   ? UNP O52269 ? ? 'expression tag'        -18 4  
1 8R4P LEU A 5   ? UNP O52269 ? ? 'expression tag'        -17 5  
1 8R4P PRO A 6   ? UNP O52269 ? ? 'expression tag'        -16 6  
1 8R4P THR A 7   ? UNP O52269 ? ? 'expression tag'        -15 7  
1 8R4P ALA A 8   ? UNP O52269 ? ? 'expression tag'        -14 8  
1 8R4P ALA A 9   ? UNP O52269 ? ? 'expression tag'        -13 9  
1 8R4P ALA A 10  ? UNP O52269 ? ? 'expression tag'        -12 10 
1 8R4P GLY A 11  ? UNP O52269 ? ? 'expression tag'        -11 11 
1 8R4P LEU A 12  ? UNP O52269 ? ? 'expression tag'        -10 12 
1 8R4P LEU A 13  ? UNP O52269 ? ? 'expression tag'        -9  13 
1 8R4P LEU A 14  ? UNP O52269 ? ? 'expression tag'        -8  14 
1 8R4P LEU A 15  ? UNP O52269 ? ? 'expression tag'        -7  15 
1 8R4P ALA A 16  ? UNP O52269 ? ? 'expression tag'        -6  16 
1 8R4P ALA A 17  ? UNP O52269 ? ? 'expression tag'        -5  17 
1 8R4P GLN A 18  ? UNP O52269 ? ? 'expression tag'        -4  18 
1 8R4P PRO A 19  ? UNP O52269 ? ? 'expression tag'        -3  19 
1 8R4P ALA A 20  ? UNP O52269 ? ? 'expression tag'        -2  20 
1 8R4P MET A 21  ? UNP O52269 ? ? 'expression tag'        -1  21 
1 8R4P ALA A 22  ? UNP O52269 ? ? 'expression tag'        0   22 
1 8R4P LYS A 547 ? UNP O52269 ? ? 'expression tag'        525 23 
1 8R4P LYS A 548 ? UNP O52269 ? ? 'expression tag'        526 24 
1 8R4P LYS A 549 ? UNP O52269 ? ? 'expression tag'        527 25 
1 8R4P LYS A 550 ? UNP O52269 ? ? 'expression tag'        528 26 
1 8R4P LYS A 551 ? UNP O52269 ? ? 'expression tag'        529 27 
1 8R4P LYS A 552 ? UNP O52269 ? ? 'expression tag'        530 28 
1 8R4P GLY A 553 ? UNP O52269 ? ? 'expression tag'        531 29 
1 8R4P SER A 554 ? UNP O52269 ? ? 'expression tag'        532 30 
1 8R4P GLU A 555 ? UNP O52269 ? ? 'expression tag'        533 31 
1 8R4P GLN A 556 ? UNP O52269 ? ? 'expression tag'        534 32 
1 8R4P LYS A 557 ? UNP O52269 ? ? 'expression tag'        535 33 
1 8R4P LEU A 558 ? UNP O52269 ? ? 'expression tag'        536 34 
1 8R4P ILE A 559 ? UNP O52269 ? ? 'expression tag'        537 35 
1 8R4P SER A 560 ? UNP O52269 ? ? 'expression tag'        538 36 
1 8R4P GLU A 561 ? UNP O52269 ? ? 'expression tag'        539 37 
1 8R4P GLU A 562 ? UNP O52269 ? ? 'expression tag'        540 38 
1 8R4P ASP A 563 ? UNP O52269 ? ? 'expression tag'        541 39 
1 8R4P LEU A 564 ? UNP O52269 ? ? 'expression tag'        542 40 
1 8R4P SER A 565 ? UNP O52269 ? ? 'expression tag'        543 41 
1 8R4P HIS A 566 ? UNP O52269 ? ? 'expression tag'        544 42 
1 8R4P HIS A 567 ? UNP O52269 ? ? 'expression tag'        545 43 
1 8R4P HIS A 568 ? UNP O52269 ? ? 'expression tag'        546 44 
1 8R4P HIS A 569 ? UNP O52269 ? ? 'expression tag'        547 45 
1 8R4P HIS A 570 ? UNP O52269 ? ? 'expression tag'        548 46 
1 8R4P HIS A 571 ? UNP O52269 ? ? 'expression tag'        549 47 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 970   ? 
1 MORE         -48   ? 
1 'SSA (A^2)'  22140 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ILE A 48  ? ASP A 50  ? ILE A 26  ASP A 28  5 ? 3  
HELX_P HELX_P2  AA2 LEU A 51  ? ALA A 76  ? LEU A 29  ALA A 54  1 ? 26 
HELX_P HELX_P3  AA3 ASP A 77  ? ASP A 98  ? ASP A 55  ASP A 76  1 ? 22 
HELX_P HELX_P4  AA4 SER A 102 ? GLY A 123 ? SER A 80  GLY A 101 1 ? 22 
HELX_P HELX_P5  AA5 TYR A 124 ? THR A 126 ? TYR A 102 THR A 104 5 ? 3  
HELX_P HELX_P6  AA6 ASN A 131 ? GLN A 135 ? ASN A 109 GLN A 113 5 ? 5  
HELX_P HELX_P7  AA7 SER A 171 ? GLY A 192 ? SER A 149 GLY A 170 1 ? 22 
HELX_P HELX_P8  AA8 SER A 220 ? GLY A 225 ? SER A 198 GLY A 203 1 ? 6  
HELX_P HELX_P9  AA9 SER A 280 ? CYS A 299 ? SER A 258 CYS A 277 1 ? 20 
HELX_P HELX_P10 AB1 PHE A 323 ? GLU A 349 ? PHE A 301 GLU A 327 1 ? 27 
HELX_P HELX_P11 AB2 PHE A 372 ? ASN A 398 ? PHE A 350 ASN A 376 1 ? 27 
HELX_P HELX_P12 AB3 PRO A 399 ? LEU A 402 ? PRO A 377 LEU A 380 5 ? 4  
HELX_P HELX_P13 AB4 THR A 403 ? PHE A 413 ? THR A 381 PHE A 391 1 ? 11 
HELX_P HELX_P14 AB5 TYR A 447 ? PHE A 462 ? TYR A 425 PHE A 440 1 ? 16 
HELX_P HELX_P15 AB6 PHE A 462 ? ASN A 481 ? PHE A 440 ASN A 459 1 ? 20 
HELX_P HELX_P16 AB7 ASN A 481 ? SER A 501 ? ASN A 459 SER A 479 1 ? 21 
HELX_P HELX_P17 AB8 LEU A 509 ? ASN A 511 ? LEU A 487 ASN A 489 5 ? 3  
HELX_P HELX_P18 AB9 ASN A 532 ? LEU A 546 ? ASN A 510 LEU A 524 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 128 SG  ? ? ? 1_555 A CYS 157 SG ? ? A CYS 106 A CYS 135 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf2  disulf ? ? A CYS 211 SG  ? ? ? 1_555 A CYS 219 SG ? ? A CYS 189 A CYS 197 1_555 ? ? ? ? ? ? ? 1.914 ? ? 
disulf3  disulf ? ? A CYS 299 SG  ? ? ? 1_555 A CYS 321 SG ? ? A CYS 277 A CYS 299 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf4  disulf ? ? A CYS 417 SG  ? ? ? 1_555 A CYS 445 SG ? ? A CYS 395 A CYS 423 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc1  metalc ? ? A ASP 53  OD1 ? ? ? 1_555 B CD  .   CD ? ? A ASP 31  A CD  601 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
metalc2  metalc ? ? A GLU 56  OE1 ? ? ? 1_555 B CD  .   CD ? ? A GLU 34  A CD  601 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc3  metalc ? ? A GLU 56  OE2 ? ? ? 1_555 B CD  .   CD ? ? A GLU 34  A CD  601 1_555 ? ? ? ? ? ? ? 2.537 ? ? 
metalc4  metalc ? ? A ASN 94  OD1 ? ? ? 1_555 C CD  .   CD ? ? A ASN 72  A CD  602 1_555 ? ? ? ? ? ? ? 2.667 ? ? 
metalc5  metalc ? ? A ASP 98  OD2 ? ? ? 1_555 C CD  .   CD ? ? A ASP 76  A CD  602 1_555 ? ? ? ? ? ? ? 2.484 ? ? 
metalc6  metalc ? ? A GLU 173 OE1 ? ? ? 1_555 B CD  .   CD ? ? A GLU 151 A CD  601 3_656 ? ? ? ? ? ? ? 2.684 ? ? 
metalc7  metalc ? ? A GLU 173 OE2 ? ? ? 1_555 B CD  .   CD ? ? A GLU 151 A CD  601 3_656 ? ? ? ? ? ? ? 2.679 ? ? 
metalc8  metalc ? ? A GLU 198 OE1 ? ? ? 1_555 D CD  .   CD ? ? A GLU 176 A CD  603 1_555 ? ? ? ? ? ? ? 2.614 ? ? 
metalc9  metalc ? ? A THR 453 OG1 ? ? ? 1_555 D CD  .   CD ? ? A THR 431 A CD  603 4_466 ? ? ? ? ? ? ? 2.653 ? ? 
metalc10 metalc ? ? D CD  .   CD  ? ? ? 1_555 L HOH .   O  ? ? A CD  603 A HOH 789 1_555 ? ? ? ? ? ? ? 2.658 ? ? 
metalc11 metalc ? ? I CD  .   CD  ? ? ? 1_555 L HOH .   O  ? ? A CD  608 A HOH 850 1_555 ? ? ? ? ? ? ? 2.692 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 53  ? A ASP 31  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE1 ? A GLU 56  ? A GLU 34  ? 1_555 81.2  ? 
2  OD1 ? A ASP 53  ? A ASP 31  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE2 ? A GLU 56  ? A GLU 34  ? 1_555 84.2  ? 
3  OE1 ? A GLU 56  ? A GLU 34  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE2 ? A GLU 56  ? A GLU 34  ? 1_555 51.5  ? 
4  OD1 ? A ASP 53  ? A ASP 31  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE1 ? A GLU 173 ? A GLU 151 ? 1_555 170.5 ? 
5  OE1 ? A GLU 56  ? A GLU 34  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE1 ? A GLU 173 ? A GLU 151 ? 1_555 92.7  ? 
6  OE2 ? A GLU 56  ? A GLU 34  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE1 ? A GLU 173 ? A GLU 151 ? 1_555 86.2  ? 
7  OD1 ? A ASP 53  ? A ASP 31  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE2 ? A GLU 173 ? A GLU 151 ? 1_555 169.4 ? 
8  OE1 ? A GLU 56  ? A GLU 34  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE2 ? A GLU 173 ? A GLU 151 ? 1_555 92.3  ? 
9  OE2 ? A GLU 56  ? A GLU 34  ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE2 ? A GLU 173 ? A GLU 151 ? 1_555 85.2  ? 
10 OE1 ? A GLU 173 ? A GLU 151 ? 1_555 CD ? B CD . ? A CD 601 ? 1_555 OE2 ? A GLU 173 ? A GLU 151 ? 1_555 1.1   ? 
11 OD1 ? A ASN 94  ? A ASN 72  ? 1_555 CD ? C CD . ? A CD 602 ? 1_555 OD2 ? A ASP 98  ? A ASP 76  ? 1_555 80.3  ? 
12 OE1 ? A GLU 198 ? A GLU 176 ? 1_555 CD ? D CD . ? A CD 603 ? 1_555 OG1 ? A THR 453 ? A THR 431 ? 1_555 13.3  ? 
13 OE1 ? A GLU 198 ? A GLU 176 ? 1_555 CD ? D CD . ? A CD 603 ? 1_555 O   ? L HOH .   ? A HOH 789 ? 1_555 143.1 ? 
14 OG1 ? A THR 453 ? A THR 431 ? 1_555 CD ? D CD . ? A CD 603 ? 1_555 O   ? L HOH .   ? A HOH 789 ? 1_555 156.3 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 128 ? CYS A 157 ? CYS A 106 ? 1_555 CYS A 135 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 211 ? CYS A 219 ? CYS A 189 ? 1_555 CYS A 197 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 299 ? CYS A 321 ? CYS A 277 ? 1_555 CYS A 299 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 417 ? CYS A 445 ? CYS A 395 ? 1_555 CYS A 423 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           357 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            335 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   GLY 
_struct_mon_prot_cis.pdbx_label_seq_id_2    358 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    GLY 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     336 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       16.47 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
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 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? 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 SER A 152 ? CYS A 157 ? SER A 130 CYS A 135 
AA1 2 THR A 141 ? GLY A 149 ? THR A 119 GLY A 127 
AA1 3 THR A 202 ? SER A 212 ? THR A 180 SER A 190 
AA1 4 TYR A 267 ? PRO A 278 ? TYR A 245 PRO A 256 
AA1 5 LYS A 243 ? VAL A 254 ? LYS A 221 VAL A 232 
AA1 6 THR A 233 ? ILE A 240 ? THR A 211 ILE A 218 
AA2 1 TYR A 301 ? PHE A 302 ? TYR A 279 PHE A 280 
AA2 2 GLY A 318 ? LYS A 319 ? GLY A 296 LYS A 297 
AA3 1 VAL A 513 ? ASN A 517 ? VAL A 491 ASN A 495 
AA3 2 THR A 527 ? LEU A 531 ? THR A 505 LEU A 509 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O CYS A 157 ? O CYS A 135 N THR A 142 ? N THR A 120 
AA1 2 3 N THR A 141 ? N THR A 119 O SER A 212 ? O SER A 190 
AA1 3 4 N VAL A 205 ? N VAL A 183 O LEU A 274 ? O LEU A 252 
AA1 4 5 O ASP A 275 ? O ASP A 253 N THR A 246 ? N THR A 224 
AA1 5 6 O ILE A 249 ? O ILE A 227 N LYS A 234 ? N LYS A 212 
AA2 1 2 N PHE A 302 ? N PHE A 280 O GLY A 318 ? O GLY A 296 
AA3 1 2 N GLY A 514 ? N GLY A 492 O TYR A 530 ? O TYR A 508 
# 
_pdbx_entry_details.entry_id                   8R4P 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             451 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             451 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.182 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.070 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASN 337 ? ? CA A ASN 337 ? ? C A ASN 337 ? ? 124.10 110.40 13.70 2.00 N 
2 1 CB A ASN 397 ? ? CA A ASN 397 ? ? C A ASN 397 ? ? 123.54 110.40 13.14 2.00 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 77  ? ? -113.38 -71.68 
2  1 SER A 117 ? ? -155.49 51.21  
3  1 SER A 136 ? ? -144.12 32.39  
4  1 TYR A 145 ? ? 59.34   16.66  
5  1 VAL A 204 ? ? -82.89  -99.55 
6  1 SER A 205 ? ? -177.67 -96.03 
7  1 ALA A 236 ? ? 178.31  133.72 
8  1 SER A 244 ? ? -30.89  113.92 
9  1 HIS A 328 ? ? -143.95 58.28  
10 1 ASN A 337 ? ? -140.52 10.22  
11 1 PHE A 391 ? ? -136.71 -58.62 
12 1 ALA A 393 ? ? -88.84  36.06  
13 1 CYS A 395 ? ? -167.61 99.92  
14 1 ASN A 483 ? ? 61.19   72.02  
15 1 SER A 486 ? ? -132.72 -53.34 
16 1 TYR A 498 ? ? -88.06  36.72  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       905 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.16 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 -21 ? A MET 1   
2  1 Y 1 A LYS -20 ? A LYS 2   
3  1 Y 1 A TYR -19 ? A TYR 3   
4  1 Y 1 A LEU -18 ? A LEU 4   
5  1 Y 1 A LEU -17 ? A LEU 5   
6  1 Y 1 A PRO -16 ? A PRO 6   
7  1 Y 1 A THR -15 ? A THR 7   
8  1 Y 1 A ALA -14 ? A ALA 8   
9  1 Y 1 A ALA -13 ? A ALA 9   
10 1 Y 1 A ALA -12 ? A ALA 10  
11 1 Y 1 A GLY -11 ? A GLY 11  
12 1 Y 1 A LEU -10 ? A LEU 12  
13 1 Y 1 A LEU -9  ? A LEU 13  
14 1 Y 1 A LEU -8  ? A LEU 14  
15 1 Y 1 A LEU -7  ? A LEU 15  
16 1 Y 1 A ALA -6  ? A ALA 16  
17 1 Y 1 A ALA -5  ? A ALA 17  
18 1 Y 1 A GLN -4  ? A GLN 18  
19 1 Y 1 A PRO -3  ? A PRO 19  
20 1 Y 1 A ALA -2  ? A ALA 20  
21 1 Y 1 A MET -1  ? A MET 21  
22 1 Y 1 A ALA 0   ? A ALA 22  
23 1 Y 1 A GLU 1   ? A GLU 23  
24 1 Y 1 A ASP 2   ? A ASP 24  
25 1 Y 1 A ASP 3   ? A ASP 25  
26 1 Y 1 A GLY 4   ? A GLY 26  
27 1 Y 1 A PHE 5   ? A PHE 27  
28 1 Y 1 A TYR 6   ? A TYR 28  
29 1 Y 1 A THR 7   ? A THR 29  
30 1 Y 1 A SER 8   ? A SER 30  
31 1 Y 1 A VAL 9   ? A VAL 31  
32 1 Y 1 A GLY 10  ? A GLY 32  
33 1 Y 1 A TYR 11  ? A TYR 33  
34 1 Y 1 A GLN 12  ? A GLN 34  
35 1 Y 1 A ILE 13  ? A ILE 35  
36 1 Y 1 A GLY 14  ? A GLY 36  
37 1 Y 1 A GLU 15  ? A GLU 37  
38 1 Y 1 A ALA 16  ? A ALA 38  
39 1 Y 1 A ALA 17  ? A ALA 39  
40 1 Y 1 A GLN 18  ? A GLN 40  
41 1 Y 1 A MET 19  ? A MET 41  
42 1 Y 1 A VAL 20  ? A VAL 42  
43 1 Y 1 A THR 21  ? A THR 43  
44 1 Y 1 A ASN 22  ? A ASN 44  
45 1 Y 1 A THR 23  ? A THR 45  
46 1 Y 1 A LYS 24  ? A LYS 46  
47 1 Y 1 A GLY 25  ? A GLY 47  
48 1 Y 1 A THR 283 ? A THR 305 
49 1 Y 1 A ASN 284 ? A ASN 306 
50 1 Y 1 A LYS 285 ? A LYS 307 
51 1 Y 1 A SER 286 ? A SER 308 
52 1 Y 1 A GLY 287 ? A GLY 309 
53 1 Y 1 A GLY 288 ? A GLY 310 
54 1 Y 1 A PRO 289 ? A PRO 311 
55 1 Y 1 A GLN 290 ? A GLN 312 
56 1 Y 1 A MET 291 ? A MET 313 
57 1 Y 1 A GLU 292 ? A GLU 314 
58 1 Y 1 A PRO 293 ? A PRO 315 
59 1 Y 1 A LYS 398 ? A LYS 420 
60 1 Y 1 A SER 399 ? A SER 421 
61 1 Y 1 A THR 400 ? A THR 422 
62 1 Y 1 A ALA 401 ? A ALA 423 
63 1 Y 1 A GLY 402 ? A GLY 424 
64 1 Y 1 A THR 403 ? A THR 425 
65 1 Y 1 A SER 404 ? A SER 426 
66 1 Y 1 A GLY 405 ? A GLY 427 
67 1 Y 1 A THR 406 ? A THR 428 
68 1 Y 1 A GLN 407 ? A GLN 429 
69 1 Y 1 A GLY 408 ? A GLY 430 
70 1 Y 1 A LYS 525 ? A LYS 547 
71 1 Y 1 A LYS 526 ? A LYS 548 
72 1 Y 1 A LYS 527 ? A LYS 549 
73 1 Y 1 A LYS 528 ? A LYS 550 
74 1 Y 1 A LYS 529 ? A LYS 551 
75 1 Y 1 A LYS 530 ? A LYS 552 
76 1 Y 1 A GLY 531 ? A GLY 553 
77 1 Y 1 A SER 532 ? A SER 554 
78 1 Y 1 A GLU 533 ? A GLU 555 
79 1 Y 1 A GLN 534 ? A GLN 556 
80 1 Y 1 A LYS 535 ? A LYS 557 
81 1 Y 1 A LEU 536 ? A LEU 558 
82 1 Y 1 A ILE 537 ? A ILE 559 
83 1 Y 1 A SER 538 ? A SER 560 
84 1 Y 1 A GLU 539 ? A GLU 561 
85 1 Y 1 A GLU 540 ? A GLU 562 
86 1 Y 1 A ASP 541 ? A ASP 563 
87 1 Y 1 A LEU 542 ? A LEU 564 
88 1 Y 1 A SER 543 ? A SER 565 
89 1 Y 1 A HIS 544 ? A HIS 566 
90 1 Y 1 A HIS 545 ? A HIS 567 
91 1 Y 1 A HIS 546 ? A HIS 568 
92 1 Y 1 A HIS 547 ? A HIS 569 
93 1 Y 1 A HIS 548 ? A HIS 570 
94 1 Y 1 A HIS 549 ? A HIS 571 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CD  CD   CD N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swedish Research Council' Sweden 2022-01295    1 
Cancerfonden               Sweden 'CAN 21/1875' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4zh0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R4P 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.017981 
_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]   0.010314 
_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]   0.010266 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CD 
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 48  ? -3.351 37.212  64.191 1.00 67.32  ? 26  ILE A N   1 
ATOM   2    C  CA  . ILE A 1 48  ? -2.043 37.566  63.650 1.00 77.65  ? 26  ILE A CA  1 
ATOM   3    C  C   . ILE A 1 48  ? -1.657 38.961  64.099 1.00 71.32  ? 26  ILE A C   1 
ATOM   4    O  O   . ILE A 1 48  ? -0.483 39.238  64.341 1.00 65.76  ? 26  ILE A O   1 
ATOM   5    C  CB  . ILE A 1 48  ? -2.013 37.486  62.119 1.00 80.88  ? 26  ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 48  ? -2.797 36.276  61.634 1.00 88.85  ? 26  ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 48  ? -0.580 37.440  61.612 1.00 75.77  ? 26  ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 48  ? -4.129 36.654  61.090 1.00 85.75  ? 26  ILE A CD1 1 
ATOM   9    N  N   . GLN A 1 49  ? -2.649 39.848  64.197 1.00 62.23  ? 27  GLN A N   1 
ATOM   10   C  CA  . GLN A 1 49  ? -2.376 41.191  64.692 1.00 62.76  ? 27  GLN A CA  1 
ATOM   11   C  C   . GLN A 1 49  ? -1.851 41.169  66.121 1.00 61.58  ? 27  GLN A C   1 
ATOM   12   O  O   . GLN A 1 49  ? -1.166 42.111  66.534 1.00 64.02  ? 27  GLN A O   1 
ATOM   13   C  CB  . GLN A 1 49  ? -3.634 42.058  64.591 1.00 58.58  ? 27  GLN A CB  1 
ATOM   14   C  CG  . GLN A 1 49  ? -4.720 41.710  65.586 1.00 56.96  ? 27  GLN A CG  1 
ATOM   15   C  CD  . GLN A 1 49  ? -5.686 40.657  65.072 1.00 59.40  ? 27  GLN A CD  1 
ATOM   16   O  OE1 . GLN A 1 49  ? -5.627 40.256  63.910 1.00 58.38  ? 27  GLN A OE1 1 
ATOM   17   N  NE2 . GLN A 1 49  ? -6.584 40.205  65.941 1.00 50.27  ? 27  GLN A NE2 1 
ATOM   18   N  N   . ASP A 1 50  ? -2.143 40.107  66.877 1.00 63.16  ? 28  ASP A N   1 
ATOM   19   C  CA  . ASP A 1 50  ? -1.528 39.907  68.182 1.00 62.81  ? 28  ASP A CA  1 
ATOM   20   C  C   . ASP A 1 50  ? -0.085 39.431  68.081 1.00 64.39  ? 28  ASP A C   1 
ATOM   21   O  O   . ASP A 1 50  ? 0.592  39.347  69.111 1.00 56.99  ? 28  ASP A O   1 
ATOM   22   C  CB  . ASP A 1 50  ? -2.341 38.898  68.999 1.00 57.48  ? 28  ASP A CB  1 
ATOM   23   C  CG  . ASP A 1 50  ? -3.812 39.256  69.074 1.00 64.66  ? 28  ASP A CG  1 
ATOM   24   O  OD1 . ASP A 1 50  ? -4.129 40.376  69.526 1.00 55.60  ? 28  ASP A OD1 1 
ATOM   25   O  OD2 . ASP A 1 50  ? -4.651 38.416  68.686 1.00 56.22  ? 28  ASP A OD2 1 
ATOM   26   N  N   . LEU A 1 51  ? 0.346  39.073  66.874 1.00 63.42  ? 29  LEU A N   1 
ATOM   27   C  CA  . LEU A 1 51  ? 1.728  38.576  66.687 1.00 64.11  ? 29  LEU A CA  1 
ATOM   28   C  C   . LEU A 1 51  ? 2.621  39.678  66.121 1.00 59.55  ? 29  LEU A C   1 
ATOM   29   O  O   . LEU A 1 51  ? 3.765  39.386  65.823 1.00 54.91  ? 29  LEU A O   1 
ATOM   30   C  CB  . LEU A 1 51  ? 1.700  37.365  65.755 1.00 63.14  ? 29  LEU A CB  1 
ATOM   31   C  CG  . LEU A 1 51  ? 1.152  36.071  66.340 1.00 69.99  ? 29  LEU A CG  1 
ATOM   32   C  CD1 . LEU A 1 51  ? 0.906  35.052  65.245 1.00 80.40  ? 29  LEU A CD1 1 
ATOM   33   C  CD2 . LEU A 1 51  ? 2.119  35.502  67.351 1.00 69.24  ? 29  LEU A CD2 1 
ATOM   34   N  N   . SER A 1 52  ? 2.122  40.903  66.018 1.00 57.43  ? 30  SER A N   1 
ATOM   35   C  CA  . SER A 1 52  ? 2.952  41.966  65.405 1.00 56.90  ? 30  SER A CA  1 
ATOM   36   C  C   . SER A 1 52  ? 4.165  42.281  66.272 1.00 54.93  ? 30  SER A C   1 
ATOM   37   O  O   . SER A 1 52  ? 5.206  42.479  65.717 1.00 56.19  ? 30  SER A O   1 
ATOM   38   C  CB  . SER A 1 52  ? 2.170  43.189  65.052 1.00 58.78  ? 30  SER A CB  1 
ATOM   39   O  OG  . SER A 1 52  ? 1.488  43.687  66.175 1.00 57.14  ? 30  SER A OG  1 
ATOM   40   N  N   . ASP A 1 53  ? 4.028  42.303  67.593 1.00 49.44  ? 31  ASP A N   1 
ATOM   41   C  CA  . ASP A 1 53  ? 5.220  42.581  68.430 1.00 50.92  ? 31  ASP A CA  1 
ATOM   42   C  C   . ASP A 1 53  ? 6.180  41.386  68.338 1.00 50.28  ? 31  ASP A C   1 
ATOM   43   O  O   . ASP A 1 53  ? 7.353  41.599  68.359 1.00 39.93  ? 31  ASP A O   1 
ATOM   44   C  CB  . ASP A 1 53  ? 4.861  43.178  69.787 1.00 54.29  ? 31  ASP A CB  1 
ATOM   45   C  CG  . ASP A 1 53  ? 4.583  44.682  69.764 1.00 70.12  ? 31  ASP A CG  1 
ATOM   46   O  OD1 . ASP A 1 53  ? 5.039  45.398  68.827 1.00 69.57  ? 31  ASP A OD1 1 
ATOM   47   O  OD2 . ASP A 1 53  ? 3.922  45.152  70.695 1.00 69.70  ? 31  ASP A OD2 1 
ATOM   48   N  N   . ASN A 1 54  ? 5.660  40.177  68.202 1.00 48.00  ? 32  ASN A N   1 
ATOM   49   C  CA  . ASN A 1 54  ? 6.506  38.981  68.037 1.00 50.62  ? 32  ASN A CA  1 
ATOM   50   C  C   . ASN A 1 54  ? 7.318  39.100  66.750 1.00 50.69  ? 32  ASN A C   1 
ATOM   51   O  O   . ASN A 1 54  ? 8.490  38.842  66.801 1.00 47.99  ? 32  ASN A O   1 
ATOM   52   C  CB  . ASN A 1 54  ? 5.672  37.719  67.946 1.00 49.64  ? 32  ASN A CB  1 
ATOM   53   C  CG  . ASN A 1 54  ? 4.673  37.641  69.068 1.00 60.11  ? 32  ASN A CG  1 
ATOM   54   O  OD1 . ASN A 1 54  ? 3.787  38.462  69.150 1.00 59.96  ? 32  ASN A OD1 1 
ATOM   55   N  ND2 . ASN A 1 54  ? 4.830  36.674  69.940 1.00 60.01  ? 32  ASN A ND2 1 
ATOM   56   N  N   . TYR A 1 55  ? 6.690  39.472  65.640 1.00 47.87  ? 33  TYR A N   1 
ATOM   57   C  CA  . TYR A 1 55  ? 7.432  39.587  64.358 1.00 49.86  ? 33  TYR A CA  1 
ATOM   58   C  C   . TYR A 1 55  ? 8.408  40.763  64.418 1.00 45.60  ? 33  TYR A C   1 
ATOM   59   O  O   . TYR A 1 55  ? 9.428  40.702  63.814 1.00 46.28  ? 33  TYR A O   1 
ATOM   60   C  CB  . TYR A 1 55  ? 6.495  39.597  63.156 1.00 44.86  ? 33  TYR A CB  1 
ATOM   61   C  CG  . TYR A 1 55  ? 6.047  38.230  62.708 1.00 53.82  ? 33  TYR A CG  1 
ATOM   62   C  CD1 . TYR A 1 55  ? 6.890  37.391  62.024 1.00 50.99  ? 33  TYR A CD1 1 
ATOM   63   C  CD2 . TYR A 1 55  ? 4.788  37.766  62.997 1.00 52.48  ? 33  TYR A CD2 1 
ATOM   64   C  CE1 . TYR A 1 55  ? 6.500  36.131  61.630 1.00 55.77  ? 33  TYR A CE1 1 
ATOM   65   C  CE2 . TYR A 1 55  ? 4.370  36.511  62.615 1.00 54.81  ? 33  TYR A CE2 1 
ATOM   66   C  CZ  . TYR A 1 55  ? 5.231  35.685  61.928 1.00 60.24  ? 33  TYR A CZ  1 
ATOM   67   O  OH  . TYR A 1 55  ? 4.825  34.452  61.544 1.00 53.37  ? 33  TYR A OH  1 
ATOM   68   N  N   . GLU A 1 56  ? 8.056  41.801  65.151 1.00 43.88  ? 34  GLU A N   1 
ATOM   69   C  CA  . GLU A 1 56  ? 8.930  42.969  65.323 1.00 48.73  ? 34  GLU A CA  1 
ATOM   70   C  C   . GLU A 1 56  ? 10.210 42.524  66.031 1.00 47.14  ? 34  GLU A C   1 
ATOM   71   O  O   . GLU A 1 56  ? 11.266 42.767  65.506 1.00 42.20  ? 34  GLU A O   1 
ATOM   72   C  CB  . GLU A 1 56  ? 8.155  43.982  66.145 1.00 45.55  ? 34  GLU A CB  1 
ATOM   73   C  CG  . GLU A 1 56  ? 8.710  45.383  66.169 1.00 54.54  ? 34  GLU A CG  1 
ATOM   74   C  CD  . GLU A 1 56  ? 7.978  46.183  67.238 1.00 70.87  ? 34  GLU A CD  1 
ATOM   75   O  OE1 . GLU A 1 56  ? 7.044  46.911  66.895 1.00 78.25  ? 34  GLU A OE1 1 
ATOM   76   O  OE2 . GLU A 1 56  ? 8.293  46.011  68.413 1.00 68.48  ? 34  GLU A OE2 1 
ATOM   77   N  N   . ASN A 1 57  ? 10.077 41.843  67.161 1.00 42.66  ? 35  ASN A N   1 
ATOM   78   C  CA  . ASN A 1 57  ? 11.250 41.419  67.964 1.00 52.10  ? 35  ASN A CA  1 
ATOM   79   C  C   . ASN A 1 57  ? 12.075 40.403  67.185 1.00 42.28  ? 35  ASN A C   1 
ATOM   80   O  O   . ASN A 1 57  ? 13.279 40.424  67.258 1.00 37.58  ? 35  ASN A O   1 
ATOM   81   C  CB  . ASN A 1 57  ? 10.828 40.886  69.331 1.00 51.54  ? 35  ASN A CB  1 
ATOM   82   C  CG  . ASN A 1 57  ? 10.589 42.017  70.295 1.00 58.44  ? 35  ASN A CG  1 
ATOM   83   O  OD1 . ASN A 1 57  ? 11.388 42.933  70.368 1.00 61.02  ? 35  ASN A OD1 1 
ATOM   84   N  ND2 . ASN A 1 57  ? 9.474  41.983  70.995 1.00 65.41  ? 35  ASN A ND2 1 
ATOM   85   N  N   . LEU A 1 58  ? 11.381 39.510  66.520 1.00 36.51  ? 36  LEU A N   1 
ATOM   86   C  CA  . LEU A 1 58  ? 12.069 38.501  65.722 1.00 42.76  ? 36  LEU A CA  1 
ATOM   87   C  C   . LEU A 1 58  ? 12.841 39.143  64.575 1.00 41.54  ? 36  LEU A C   1 
ATOM   88   O  O   . LEU A 1 58  ? 13.978 38.753  64.286 1.00 40.94  ? 36  LEU A O   1 
ATOM   89   C  CB  . LEU A 1 58  ? 11.058 37.483  65.193 1.00 46.01  ? 36  LEU A CB  1 
ATOM   90   C  CG  . LEU A 1 58  ? 11.585 36.211  64.528 1.00 43.77  ? 36  LEU A CG  1 
ATOM   91   C  CD1 . LEU A 1 58  ? 12.581 35.498  65.428 1.00 48.28  ? 36  LEU A CD1 1 
ATOM   92   C  CD2 . LEU A 1 58  ? 10.425 35.294  64.174 1.00 48.84  ? 36  LEU A CD2 1 
ATOM   93   N  N   . SER A 1 59  ? 12.241 40.138  63.917 1.00 41.12  ? 37  SER A N   1 
ATOM   94   C  CA  . SER A 1 59  ? 12.932 40.834  62.836 1.00 42.73  ? 37  SER A CA  1 
ATOM   95   C  C   . SER A 1 59  ? 14.132 41.614  63.357 1.00 39.28  ? 37  SER A C   1 
ATOM   96   O  O   . SER A 1 59  ? 15.194 41.626  62.722 1.00 41.76  ? 37  SER A O   1 
ATOM   97   C  CB  . SER A 1 59  ? 11.964 41.766  62.108 1.00 49.47  ? 37  SER A CB  1 
ATOM   98   O  OG  . SER A 1 59  ? 12.630 42.922  61.631 1.00 54.75  ? 37  SER A OG  1 
ATOM   99   N  N   . LYS A 1 60  ? 13.984 42.273  64.509 1.00 36.38  ? 38  LYS A N   1 
ATOM   100  C  CA  . LYS A 1 60  ? 15.098 43.027  65.075 1.00 33.61  ? 38  LYS A CA  1 
ATOM   101  C  C   . LYS A 1 60  ? 16.240 42.104  65.475 1.00 37.89  ? 38  LYS A C   1 
ATOM   102  O  O   . LYS A 1 60  ? 17.414 42.421  65.249 1.00 37.61  ? 38  LYS A O   1 
ATOM   103  C  CB  . LYS A 1 60  ? 14.625 43.845  66.277 1.00 37.81  ? 38  LYS A CB  1 
ATOM   104  C  CG  . LYS A 1 60  ? 13.964 45.165  65.911 1.00 46.23  ? 38  LYS A CG  1 
ATOM   105  C  CD  . LYS A 1 60  ? 13.366 45.841  67.136 1.00 48.84  ? 38  LYS A CD  1 
ATOM   106  C  CE  . LYS A 1 60  ? 12.668 47.139  66.765 1.00 58.53  ? 38  LYS A CE  1 
ATOM   107  N  NZ  . LYS A 1 60  ? 12.554 48.060  67.929 1.00 57.10  ? 38  LYS A NZ  1 
ATOM   108  N  N   . LEU A 1 61  ? 15.916 40.953  66.069 1.00 35.70  ? 39  LEU A N   1 
ATOM   109  C  CA  . LEU A 1 61  ? 16.955 40.013  66.476 1.00 37.39  ? 39  LEU A CA  1 
ATOM   110  C  C   . LEU A 1 61  ? 17.675 39.425  65.269 1.00 34.06  ? 39  LEU A C   1 
ATOM   111  O  O   . LEU A 1 61  ? 18.905 39.298  65.275 1.00 31.40  ? 39  LEU A O   1 
ATOM   112  C  CB  . LEU A 1 61  ? 16.348 38.900  67.330 1.00 31.25  ? 39  LEU A CB  1 
ATOM   113  C  CG  . LEU A 1 61  ? 15.976 39.244  68.773 1.00 33.43  ? 39  LEU A CG  1 
ATOM   114  C  CD1 . LEU A 1 61  ? 15.103 38.150  69.367 1.00 36.75  ? 39  LEU A CD1 1 
ATOM   115  C  CD2 . LEU A 1 61  ? 17.225 39.458  69.616 1.00 29.62  ? 39  LEU A CD2 1 
ATOM   116  N  N   . LEU A 1 62  ? 16.924 39.060  64.225 1.00 40.67  ? 40  LEU A N   1 
ATOM   117  C  CA  . LEU A 1 62  ? 17.536 38.463  63.043 1.00 40.03  ? 40  LEU A CA  1 
ATOM   118  C  C   . LEU A 1 62  ? 18.476 39.434  62.343 1.00 43.06  ? 40  LEU A C   1 
ATOM   119  O  O   . LEU A 1 62  ? 19.498 39.016  61.787 1.00 39.84  ? 40  LEU A O   1 
ATOM   120  C  CB  . LEU A 1 62  ? 16.451 37.984  62.078 1.00 39.49  ? 40  LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 62  ? 15.723 36.702  62.483 1.00 33.61  ? 40  LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 62  ? 14.452 36.519  61.668 1.00 48.82  ? 40  LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 62  ? 16.639 35.498  62.335 1.00 38.44  ? 40  LEU A CD2 1 
ATOM   124  N  N   . THR A 1 63  ? 18.152 40.729  62.359 1.00 34.68  ? 41  THR A N   1 
ATOM   125  C  CA  . THR A 1 63  ? 19.028 41.721  61.746 1.00 37.50  ? 41  THR A CA  1 
ATOM   126  C  C   . THR A 1 63  ? 20.338 41.842  62.516 1.00 39.26  ? 41  THR A C   1 
ATOM   127  O  O   . THR A 1 63  ? 21.421 41.869  61.919 1.00 39.47  ? 41  THR A O   1 
ATOM   128  C  CB  . THR A 1 63  ? 18.316 43.072  61.667 1.00 37.28  ? 41  THR A CB  1 
ATOM   129  O  OG1 . THR A 1 63  ? 17.264 42.998  60.697 1.00 34.18  ? 41  THR A OG1 1 
ATOM   130  C  CG2 . THR A 1 63  ? 19.289 44.174  61.268 1.00 34.92  ? 41  THR A CG2 1 
ATOM   131  N  N   . ARG A 1 64  ? 20.259 41.911  63.847 1.00 36.17  ? 42  ARG A N   1 
ATOM   132  C  CA  . ARG A 1 64  ? 21.474 41.914  64.656 1.00 39.13  ? 42  ARG A CA  1 
ATOM   133  C  C   . ARG A 1 64  ? 22.234 40.604  64.503 1.00 38.57  ? 42  ARG A C   1 
ATOM   134  O  O   . ARG A 1 64  ? 23.469 40.595  64.445 1.00 33.73  ? 42  ARG A O   1 
ATOM   135  C  CB  . ARG A 1 64  ? 21.130 42.163  66.125 1.00 34.44  ? 42  ARG A CB  1 
ATOM   136  C  CG  . ARG A 1 64  ? 20.243 43.373  66.358 1.00 46.88  ? 42  ARG A CG  1 
ATOM   137  C  CD  . ARG A 1 64  ? 20.616 44.098  67.639 1.00 51.98  ? 42  ARG A CD  1 
ATOM   138  N  NE  . ARG A 1 64  ? 20.688 43.196  68.786 1.00 45.39  ? 42  ARG A NE  1 
ATOM   139  C  CZ  . ARG A 1 64  ? 19.753 43.104  69.726 1.00 50.54  ? 42  ARG A CZ  1 
ATOM   140  N  NH1 . ARG A 1 64  ? 18.665 43.860  69.659 1.00 49.51  ? 42  ARG A NH1 1 
ATOM   141  N  NH2 . ARG A 1 64  ? 19.904 42.257  70.735 1.00 34.96  ? 42  ARG A NH2 1 
ATOM   142  N  N   . TYR A 1 65  ? 21.506 39.486  64.432 1.00 29.90  ? 43  TYR A N   1 
ATOM   143  C  CA  . TYR A 1 65  ? 22.134 38.181  64.252 1.00 34.65  ? 43  TYR A CA  1 
ATOM   144  C  C   . TYR A 1 65  ? 22.922 38.125  62.949 1.00 40.90  ? 43  TYR A C   1 
ATOM   145  O  O   . TYR A 1 65  ? 24.088 37.715  62.932 1.00 32.06  ? 43  TYR A O   1 
ATOM   146  C  CB  . TYR A 1 65  ? 21.059 37.092  64.287 1.00 28.37  ? 43  TYR A CB  1 
ATOM   147  C  CG  . TYR A 1 65  ? 21.542 35.676  64.048 1.00 33.68  ? 43  TYR A CG  1 
ATOM   148  C  CD1 . TYR A 1 65  ? 22.149 34.944  65.061 1.00 30.04  ? 43  TYR A CD1 1 
ATOM   149  C  CD2 . TYR A 1 65  ? 21.358 35.061  62.816 1.00 37.39  ? 43  TYR A CD2 1 
ATOM   150  C  CE1 . TYR A 1 65  ? 22.576 33.643  64.847 1.00 36.64  ? 43  TYR A CE1 1 
ATOM   151  C  CE2 . TYR A 1 65  ? 21.781 33.764  62.592 1.00 34.73  ? 43  TYR A CE2 1 
ATOM   152  C  CZ  . TYR A 1 65  ? 22.388 33.060  63.610 1.00 36.36  ? 43  TYR A CZ  1 
ATOM   153  O  OH  . TYR A 1 65  ? 22.808 31.768  63.387 1.00 37.42  ? 43  TYR A OH  1 
ATOM   154  N  N   . SER A 1 66  ? 22.301 38.546  61.843 1.00 39.25  ? 44  SER A N   1 
ATOM   155  C  CA  . SER A 1 66  ? 22.980 38.504  60.552 1.00 41.13  ? 44  SER A CA  1 
ATOM   156  C  C   . SER A 1 66  ? 24.150 39.479  60.510 1.00 38.54  ? 44  SER A C   1 
ATOM   157  O  O   . SER A 1 66  ? 25.224 39.145  59.995 1.00 40.24  ? 44  SER A O   1 
ATOM   158  C  CB  . SER A 1 66  ? 21.991 38.804  59.427 1.00 46.46  ? 44  SER A CB  1 
ATOM   159  O  OG  . SER A 1 66  ? 22.664 39.287  58.277 1.00 46.88  ? 44  SER A OG  1 
ATOM   160  N  N   . THR A 1 67  ? 23.957 40.689  61.039 1.00 37.22  ? 45  THR A N   1 
ATOM   161  C  CA  . THR A 1 67  ? 25.043 41.663  61.081 1.00 38.72  ? 45  THR A CA  1 
ATOM   162  C  C   . THR A 1 67  ? 26.207 41.147  61.917 1.00 42.89  ? 45  THR A C   1 
ATOM   163  O  O   . THR A 1 67  ? 27.365 41.186  61.485 1.00 39.12  ? 45  THR A O   1 
ATOM   164  C  CB  . THR A 1 67  ? 24.536 42.996  61.635 1.00 43.14  ? 45  THR A CB  1 
ATOM   165  O  OG1 . THR A 1 67  ? 23.466 43.482  60.816 1.00 43.21  ? 45  THR A OG1 1 
ATOM   166  C  CG2 . THR A 1 67  ? 25.657 44.025  61.661 1.00 43.26  ? 45  THR A CG2 1 
ATOM   167  N  N   . LEU A 1 68  ? 25.914 40.652  63.123 1.00 39.21  ? 46  LEU A N   1 
ATOM   168  C  CA  . LEU A 1 68  ? 26.969 40.124  63.981 1.00 38.91  ? 46  LEU A CA  1 
ATOM   169  C  C   . LEU A 1 68  ? 27.641 38.912  63.349 1.00 36.67  ? 46  LEU A C   1 
ATOM   170  O  O   . LEU A 1 68  ? 28.868 38.776  63.406 1.00 35.76  ? 46  LEU A O   1 
ATOM   171  C  CB  . LEU A 1 68  ? 26.397 39.762  65.352 1.00 38.57  ? 46  LEU A CB  1 
ATOM   172  C  CG  . LEU A 1 68  ? 27.263 40.063  66.575 1.00 44.43  ? 46  LEU A CG  1 
ATOM   173  C  CD1 . LEU A 1 68  ? 28.054 41.348  66.381 1.00 48.14  ? 46  LEU A CD1 1 
ATOM   174  C  CD2 . LEU A 1 68  ? 26.399 40.147  67.823 1.00 37.66  ? 46  LEU A CD2 1 
ATOM   175  N  N   . ASN A 1 69  ? 26.855 38.025  62.734 1.00 36.05  ? 47  ASN A N   1 
ATOM   176  C  CA  . ASN A 1 69  ? 27.427 36.840  62.102 1.00 37.16  ? 47  ASN A CA  1 
ATOM   177  C  C   . ASN A 1 69  ? 28.368 37.224  60.968 1.00 34.50  ? 47  ASN A C   1 
ATOM   178  O  O   . ASN A 1 69  ? 29.479 36.693  60.860 1.00 35.91  ? 47  ASN A O   1 
ATOM   179  C  CB  . ASN A 1 69  ? 26.314 35.925  61.591 1.00 34.01  ? 47  ASN A CB  1 
ATOM   180  C  CG  . ASN A 1 69  ? 26.786 34.503  61.369 1.00 41.62  ? 47  ASN A CG  1 
ATOM   181  O  OD1 . ASN A 1 69  ? 27.650 34.005  62.091 1.00 34.63  ? 47  ASN A OD1 1 
ATOM   182  N  ND2 . ASN A 1 69  ? 26.225 33.842  60.363 1.00 37.84  ? 47  ASN A ND2 1 
ATOM   183  N  N   . THR A 1 70  ? 27.937 38.153  60.111 1.00 32.35  ? 48  THR A N   1 
ATOM   184  C  CA  . THR A 1 70  ? 28.788 38.598  59.012 1.00 36.59  ? 48  THR A CA  1 
ATOM   185  C  C   . THR A 1 70  ? 30.038 39.294  59.533 1.00 39.45  ? 48  THR A C   1 
ATOM   186  O  O   . THR A 1 70  ? 31.138 39.090  59.005 1.00 37.17  ? 48  THR A O   1 
ATOM   187  C  CB  . THR A 1 70  ? 28.003 39.526  58.084 1.00 38.71  ? 48  THR A CB  1 
ATOM   188  O  OG1 . THR A 1 70  ? 26.819 38.859  57.630 1.00 37.44  ? 48  THR A OG1 1 
ATOM   189  C  CG2 . THR A 1 70  ? 28.849 39.921  56.881 1.00 39.69  ? 48  THR A CG2 1 
ATOM   190  N  N   . LEU A 1 71  ? 29.891 40.114  60.577 1.00 38.18  ? 49  LEU A N   1 
ATOM   191  C  CA  . LEU A 1 71  ? 31.046 40.793  61.156 1.00 38.06  ? 49  LEU A CA  1 
ATOM   192  C  C   . LEU A 1 71  ? 32.018 39.798  61.777 1.00 41.21  ? 49  LEU A C   1 
ATOM   193  O  O   . LEU A 1 71  ? 33.239 39.960  61.668 1.00 38.16  ? 49  LEU A O   1 
ATOM   194  C  CB  . LEU A 1 71  ? 30.587 41.812  62.198 1.00 41.80  ? 49  LEU A CB  1 
ATOM   195  C  CG  . LEU A 1 71  ? 30.588 43.280  61.773 1.00 38.34  ? 49  LEU A CG  1 
ATOM   196  C  CD1 . LEU A 1 71  ? 30.240 44.176  62.952 1.00 29.81  ? 49  LEU A CD1 1 
ATOM   197  C  CD2 . LEU A 1 71  ? 31.934 43.663  61.180 1.00 40.72  ? 49  LEU A CD2 1 
ATOM   198  N  N   . ILE A 1 72  ? 31.494 38.763  62.437 1.00 38.40  ? 50  ILE A N   1 
ATOM   199  C  CA  . ILE A 1 72  ? 32.354 37.750  63.041 1.00 35.56  ? 50  ILE A CA  1 
ATOM   200  C  C   . ILE A 1 72  ? 33.111 36.983  61.963 1.00 32.18  ? 50  ILE A C   1 
ATOM   201  O  O   . ILE A 1 72  ? 34.315 36.728  62.093 1.00 33.87  ? 50  ILE A O   1 
ATOM   202  C  CB  . ILE A 1 72  ? 31.522 36.808  63.931 1.00 35.63  ? 50  ILE A CB  1 
ATOM   203  C  CG1 . ILE A 1 72  ? 31.127 37.508  65.235 1.00 34.81  ? 50  ILE A CG1 1 
ATOM   204  C  CG2 . ILE A 1 72  ? 32.283 35.523  64.217 1.00 26.87  ? 50  ILE A CG2 1 
ATOM   205  C  CD1 . ILE A 1 72  ? 32.300 37.886  66.109 1.00 43.64  ? 50  ILE A CD1 1 
ATOM   206  N  N   . LYS A 1 73  ? 32.423 36.610  60.882 1.00 31.44  ? 51  LYS A N   1 
ATOM   207  C  CA  . LYS A 1 73  ? 33.084 35.899  59.792 1.00 33.30  ? 51  LYS A CA  1 
ATOM   208  C  C   . LYS A 1 73  ? 34.141 36.773  59.127 1.00 38.78  ? 51  LYS A C   1 
ATOM   209  O  O   . LYS A 1 73  ? 35.212 36.284  58.748 1.00 33.60  ? 51  LYS A O   1 
ATOM   210  C  CB  . LYS A 1 73  ? 32.050 35.429  58.770 1.00 35.51  ? 51  LYS A CB  1 
ATOM   211  C  CG  . LYS A 1 73  ? 31.151 34.305  59.265 1.00 39.67  ? 51  LYS A CG  1 
ATOM   212  C  CD  . LYS A 1 73  ? 30.228 33.810  58.162 1.00 48.49  ? 51  LYS A CD  1 
ATOM   213  C  CE  . LYS A 1 73  ? 29.397 32.622  58.624 1.00 55.98  ? 51  LYS A CE  1 
ATOM   214  N  NZ  . LYS A 1 73  ? 30.247 31.477  59.057 1.00 55.41  ? 51  LYS A NZ  1 
ATOM   215  N  N   . LEU A 1 74  ? 33.859 38.070  58.979 1.00 36.26  ? 52  LEU A N   1 
ATOM   216  C  CA  . LEU A 1 74  ? 34.845 38.987  58.414 1.00 35.40  ? 52  LEU A CA  1 
ATOM   217  C  C   . LEU A 1 74  ? 36.086 39.065  59.293 1.00 36.61  ? 52  LEU A C   1 
ATOM   218  O  O   . LEU A 1 74  ? 37.213 38.891  58.817 1.00 42.56  ? 52  LEU A O   1 
ATOM   219  C  CB  . LEU A 1 74  ? 34.232 40.378  58.239 1.00 39.96  ? 52  LEU A CB  1 
ATOM   220  C  CG  . LEU A 1 74  ? 33.513 40.708  56.930 1.00 39.87  ? 52  LEU A CG  1 
ATOM   221  C  CD1 . LEU A 1 74  ? 33.272 42.206  56.832 1.00 39.64  ? 52  LEU A CD1 1 
ATOM   222  C  CD2 . LEU A 1 74  ? 34.303 40.211  55.732 1.00 40.64  ? 52  LEU A CD2 1 
ATOM   223  N  N   . SER A 1 75  ? 35.893 39.324  60.589 1.00 35.08  ? 53  SER A N   1 
ATOM   224  C  CA  . SER A 1 75  ? 37.008 39.499  61.511 1.00 33.81  ? 53  SER A CA  1 
ATOM   225  C  C   . SER A 1 75  ? 37.773 38.210  61.773 1.00 42.16  ? 53  SER A C   1 
ATOM   226  O  O   . SER A 1 75  ? 38.870 38.268  62.339 1.00 43.05  ? 53  SER A O   1 
ATOM   227  C  CB  . SER A 1 75  ? 36.502 40.086  62.830 1.00 36.11  ? 53  SER A CB  1 
ATOM   228  O  OG  . SER A 1 75  ? 35.661 41.202  62.590 1.00 37.24  ? 53  SER A OG  1 
ATOM   229  N  N   . ALA A 1 76  ? 37.229 37.059  61.393 1.00 38.85  ? 54  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 76  ? 37.957 35.801  61.475 1.00 40.55  ? 54  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 76  ? 38.718 35.484  60.195 1.00 43.71  ? 54  ALA A C   1 
ATOM   232  O  O   . ALA A 1 76  ? 39.443 34.484  60.153 1.00 43.06  ? 54  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 76  ? 36.998 34.653  61.803 1.00 42.95  ? 54  ALA A CB  1 
ATOM   234  N  N   . ASP A 1 77  ? 38.577 36.311  59.159 1.00 44.18  ? 55  ASP A N   1 
ATOM   235  C  CA  . ASP A 1 77  ? 39.201 36.053  57.872 1.00 40.60  ? 55  ASP A CA  1 
ATOM   236  C  C   . ASP A 1 77  ? 40.403 36.968  57.697 1.00 44.77  ? 55  ASP A C   1 
ATOM   237  O  O   . ASP A 1 77  ? 40.226 38.193  57.606 1.00 37.31  ? 55  ASP A O   1 
ATOM   238  C  CB  . ASP A 1 77  ? 38.198 36.268  56.741 1.00 38.05  ? 55  ASP A CB  1 
ATOM   239  C  CG  . ASP A 1 77  ? 38.771 35.937  55.377 1.00 44.32  ? 55  ASP A CG  1 
ATOM   240  O  OD1 . ASP A 1 77  ? 39.827 35.273  55.313 1.00 55.22  ? 55  ASP A OD1 1 
ATOM   241  O  OD2 . ASP A 1 77  ? 38.162 36.342  54.365 1.00 48.52  ? 55  ASP A OD2 1 
ATOM   242  N  N   . PRO A 1 78  ? 41.626 36.436  57.634 1.00 44.65  ? 56  PRO A N   1 
ATOM   243  C  CA  . PRO A 1 78  ? 42.798 37.315  57.477 1.00 45.95  ? 56  PRO A CA  1 
ATOM   244  C  C   . PRO A 1 78  ? 42.796 38.091  56.173 1.00 39.35  ? 56  PRO A C   1 
ATOM   245  O  O   . PRO A 1 78  ? 43.357 39.192  56.118 1.00 36.10  ? 56  PRO A O   1 
ATOM   246  C  CB  . PRO A 1 78  ? 43.984 36.340  57.548 1.00 49.98  ? 56  PRO A CB  1 
ATOM   247  C  CG  . PRO A 1 78  ? 43.427 35.071  58.118 1.00 47.87  ? 56  PRO A CG  1 
ATOM   248  C  CD  . PRO A 1 78  ? 42.001 35.015  57.692 1.00 46.77  ? 56  PRO A CD  1 
ATOM   249  N  N   . SER A 1 79  ? 42.181 37.549  55.119 1.00 35.21  ? 57  SER A N   1 
ATOM   250  C  CA  . SER A 1 79  ? 42.145 38.252  53.842 1.00 37.11  ? 57  SER A CA  1 
ATOM   251  C  C   . SER A 1 79  ? 41.229 39.467  53.906 1.00 42.92  ? 57  SER A C   1 
ATOM   252  O  O   . SER A 1 79  ? 41.519 40.503  53.296 1.00 39.25  ? 57  SER A O   1 
ATOM   253  C  CB  . SER A 1 79  ? 41.702 37.301  52.731 1.00 41.05  ? 57  SER A CB  1 
ATOM   254  O  OG  . SER A 1 79  ? 41.212 38.020  51.613 1.00 58.23  ? 57  SER A OG  1 
ATOM   255  N  N   . ALA A 1 80  ? 40.115 39.358  54.632 1.00 38.66  ? 58  ALA A N   1 
ATOM   256  C  CA  . ALA A 1 80  ? 39.257 40.520  54.833 1.00 37.73  ? 58  ALA A CA  1 
ATOM   257  C  C   . ALA A 1 80  ? 39.933 41.548  55.730 1.00 25.51  ? 58  ALA A C   1 
ATOM   258  O  O   . ALA A 1 80  ? 39.804 42.758  55.507 1.00 32.99  ? 58  ALA A O   1 
ATOM   259  C  CB  . ALA A 1 80  ? 37.917 40.088  55.425 1.00 32.95  ? 58  ALA A CB  1 
ATOM   260  N  N   . ILE A 1 81  ? 40.662 41.083  56.746 1.00 32.18  ? 59  ILE A N   1 
ATOM   261  C  CA  . ILE A 1 81  ? 41.368 41.993  57.643 1.00 31.90  ? 59  ILE A CA  1 
ATOM   262  C  C   . ILE A 1 81  ? 42.443 42.759  56.882 1.00 39.00  ? 59  ILE A C   1 
ATOM   263  O  O   . ILE A 1 81  ? 42.562 43.984  57.002 1.00 29.61  ? 59  ILE A O   1 
ATOM   264  C  CB  . ILE A 1 81  ? 41.966 41.216  58.830 1.00 39.22  ? 59  ILE A CB  1 
ATOM   265  C  CG1 . ILE A 1 81  ? 40.854 40.594  59.676 1.00 34.75  ? 59  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A 1 81  ? 42.848 42.121  59.674 1.00 30.98  ? 59  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A 1 81  ? 41.352 39.564  60.665 1.00 31.38  ? 59  ILE A CD1 1 
ATOM   268  N  N   . ASN A 1 82  ? 43.240 42.045  56.084 1.00 36.61  ? 60  ASN A N   1 
ATOM   269  C  CA  . ASN A 1 82  ? 44.318 42.692  55.344 1.00 34.19  ? 60  ASN A CA  1 
ATOM   270  C  C   . ASN A 1 82  ? 43.782 43.637  54.276 1.00 34.05  ? 60  ASN A C   1 
ATOM   271  O  O   . ASN A 1 82  ? 44.409 44.663  53.991 1.00 34.40  ? 60  ASN A O   1 
ATOM   272  C  CB  . ASN A 1 82  ? 45.230 41.637  54.719 1.00 40.07  ? 60  ASN A CB  1 
ATOM   273  C  CG  . ASN A 1 82  ? 46.041 40.883  55.755 1.00 45.49  ? 60  ASN A CG  1 
ATOM   274  O  OD1 . ASN A 1 82  ? 46.602 41.478  56.676 1.00 51.24  ? 60  ASN A OD1 1 
ATOM   275  N  ND2 . ASN A 1 82  ? 46.103 39.565  55.613 1.00 43.88  ? 60  ASN A ND2 1 
ATOM   276  N  N   . ALA A 1 83  ? 42.634 43.314  53.678 1.00 37.46  ? 61  ALA A N   1 
ATOM   277  C  CA  . ALA A 1 83  ? 42.025 44.232  52.721 1.00 34.31  ? 61  ALA A CA  1 
ATOM   278  C  C   . ALA A 1 83  ? 41.548 45.504  53.410 1.00 36.01  ? 61  ALA A C   1 
ATOM   279  O  O   . ALA A 1 83  ? 41.656 46.601  52.849 1.00 34.53  ? 61  ALA A O   1 
ATOM   280  C  CB  . ALA A 1 83  ? 40.870 43.545  51.994 1.00 35.01  ? 61  ALA A CB  1 
ATOM   281  N  N   . ALA A 1 84  ? 41.021 45.376  54.630 1.00 33.56  ? 62  ALA A N   1 
ATOM   282  C  CA  . ALA A 1 84  ? 40.598 46.554  55.379 1.00 32.61  ? 62  ALA A CA  1 
ATOM   283  C  C   . ALA A 1 84  ? 41.797 47.386  55.816 1.00 30.58  ? 62  ALA A C   1 
ATOM   284  O  O   . ALA A 1 84  ? 41.749 48.622  55.778 1.00 25.67  ? 62  ALA A O   1 
ATOM   285  C  CB  . ALA A 1 84  ? 39.763 46.134  56.588 1.00 28.09  ? 62  ALA A CB  1 
ATOM   286  N  N   A ARG A 1 85  ? 42.882 46.727  56.230 0.67 28.71  ? 63  ARG A N   1 
ATOM   287  N  N   B ARG A 1 85  ? 42.879 46.729  56.238 0.33 28.94  ? 63  ARG A N   1 
ATOM   288  C  CA  A ARG A 1 85  ? 44.079 47.457  56.635 0.67 32.96  ? 63  ARG A CA  1 
ATOM   289  C  CA  B ARG A 1 85  ? 44.076 47.462  56.633 0.33 32.81  ? 63  ARG A CA  1 
ATOM   290  C  C   A ARG A 1 85  ? 44.737 48.156  55.452 0.67 30.91  ? 63  ARG A C   1 
ATOM   291  C  C   B ARG A 1 85  ? 44.718 48.168  55.447 0.33 30.96  ? 63  ARG A C   1 
ATOM   292  O  O   A ARG A 1 85  ? 45.322 49.232  55.617 0.67 27.69  ? 63  ARG A O   1 
ATOM   293  O  O   B ARG A 1 85  ? 45.277 49.259  55.606 0.33 27.87  ? 63  ARG A O   1 
ATOM   294  C  CB  A ARG A 1 85  ? 45.067 46.509  57.316 0.67 32.20  ? 63  ARG A CB  1 
ATOM   295  C  CB  B ARG A 1 85  ? 45.078 46.516  57.292 0.33 32.30  ? 63  ARG A CB  1 
ATOM   296  C  CG  A ARG A 1 85  ? 44.736 46.223  58.774 0.67 37.19  ? 63  ARG A CG  1 
ATOM   297  C  CG  B ARG A 1 85  ? 44.781 46.199  58.750 0.33 37.09  ? 63  ARG A CG  1 
ATOM   298  C  CD  A ARG A 1 85  ? 45.587 45.096  59.335 0.67 37.12  ? 63  ARG A CD  1 
ATOM   299  C  CD  B ARG A 1 85  ? 45.734 45.141  59.297 0.33 37.20  ? 63  ARG A CD  1 
ATOM   300  N  NE  A ARG A 1 85  ? 47.016 45.378  59.232 0.67 39.83  ? 63  ARG A NE  1 
ATOM   301  N  NE  B ARG A 1 85  ? 47.101 45.323  58.813 0.33 40.82  ? 63  ARG A NE  1 
ATOM   302  C  CZ  A ARG A 1 85  ? 47.737 45.943  60.195 0.67 39.00  ? 63  ARG A CZ  1 
ATOM   303  C  CZ  B ARG A 1 85  ? 47.661 44.585  57.859 0.33 38.83  ? 63  ARG A CZ  1 
ATOM   304  N  NH1 A ARG A 1 85  ? 47.163 46.288  61.340 0.67 38.13  ? 63  ARG A NH1 1 
ATOM   305  N  NH1 B ARG A 1 85  ? 46.969 43.617  57.278 0.33 40.98  ? 63  ARG A NH1 1 
ATOM   306  N  NH2 A ARG A 1 85  ? 49.032 46.159  60.015 0.67 40.95  ? 63  ARG A NH2 1 
ATOM   307  N  NH2 B ARG A 1 85  ? 48.906 44.823  57.479 0.33 46.67  ? 63  ARG A NH2 1 
ATOM   308  N  N   . GLU A 1 86  ? 44.653 47.566  54.257 1.00 31.90  ? 64  GLU A N   1 
ATOM   309  C  CA  . GLU A 1 86  ? 45.181 48.229  53.069 1.00 33.68  ? 64  GLU A CA  1 
ATOM   310  C  C   . GLU A 1 86  ? 44.333 49.439  52.698 1.00 30.80  ? 64  GLU A C   1 
ATOM   311  O  O   . GLU A 1 86  ? 44.867 50.474  52.283 1.00 34.39  ? 64  GLU A O   1 
ATOM   312  C  CB  . GLU A 1 86  ? 45.247 47.246  51.900 1.00 34.33  ? 64  GLU A CB  1 
ATOM   313  C  CG  . GLU A 1 86  ? 46.356 46.213  52.009 1.00 35.98  ? 64  GLU A CG  1 
ATOM   314  C  CD  . GLU A 1 86  ? 46.235 45.121  50.964 1.00 64.37  ? 64  GLU A CD  1 
ATOM   315  O  OE1 . GLU A 1 86  ? 45.854 45.436  49.817 1.00 73.54  ? 64  GLU A OE1 1 
ATOM   316  O  OE2 . GLU A 1 86  ? 46.516 43.949  51.290 1.00 63.95  ? 64  GLU A OE2 1 
ATOM   317  N  N   . ASN A 1 87  ? 43.010 49.323  52.841 1.00 29.69  ? 65  ASN A N   1 
ATOM   318  C  CA  . ASN A 1 87  ? 42.130 50.460  52.587 1.00 30.74  ? 65  ASN A CA  1 
ATOM   319  C  C   . ASN A 1 87  ? 42.435 51.611  53.534 1.00 27.47  ? 65  ASN A C   1 
ATOM   320  O  O   . ASN A 1 87  ? 42.429 52.779  53.126 1.00 30.09  ? 65  ASN A O   1 
ATOM   321  C  CB  . ASN A 1 87  ? 40.667 50.038  52.728 1.00 30.52  ? 65  ASN A CB  1 
ATOM   322  C  CG  . ASN A 1 87  ? 40.217 49.107  51.623 1.00 32.37  ? 65  ASN A CG  1 
ATOM   323  O  OD1 . ASN A 1 87  ? 40.846 49.025  50.569 1.00 34.46  ? 65  ASN A OD1 1 
ATOM   324  N  ND2 . ASN A 1 87  ? 39.117 48.401  51.858 1.00 28.80  ? 65  ASN A ND2 1 
ATOM   325  N  N   . LEU A 1 88  ? 42.695 51.299  54.807 1.00 25.43  ? 66  LEU A N   1 
ATOM   326  C  CA  . LEU A 1 88  ? 43.015 52.338  55.779 1.00 24.52  ? 66  LEU A CA  1 
ATOM   327  C  C   . LEU A 1 88  ? 44.263 53.108  55.371 1.00 30.86  ? 66  LEU A C   1 
ATOM   328  O  O   . LEU A 1 88  ? 44.317 54.335  55.509 1.00 25.14  ? 66  LEU A O   1 
ATOM   329  C  CB  . LEU A 1 88  ? 43.199 51.719  57.164 1.00 27.21  ? 66  LEU A CB  1 
ATOM   330  C  CG  . LEU A 1 88  ? 41.923 51.293  57.891 1.00 28.92  ? 66  LEU A CG  1 
ATOM   331  C  CD1 . LEU A 1 88  ? 42.258 50.697  59.248 1.00 22.02  ? 66  LEU A CD1 1 
ATOM   332  C  CD2 . LEU A 1 88  ? 40.975 52.472  58.038 1.00 27.56  ? 66  LEU A CD2 1 
ATOM   333  N  N   . GLY A 1 89  ? 45.278 52.405  54.865 1.00 28.07  ? 67  GLY A N   1 
ATOM   334  C  CA  . GLY A 1 89  ? 46.485 53.085  54.428 1.00 29.63  ? 67  GLY A CA  1 
ATOM   335  C  C   . GLY A 1 89  ? 46.238 54.018  53.258 1.00 30.05  ? 67  GLY A C   1 
ATOM   336  O  O   . GLY A 1 89  ? 46.792 55.119  53.202 1.00 29.12  ? 67  GLY A O   1 
ATOM   337  N  N   . ALA A 1 90  ? 45.392 53.599  52.314 1.00 27.51  ? 68  ALA A N   1 
ATOM   338  C  CA  . ALA A 1 90  ? 45.141 54.415  51.131 1.00 32.76  ? 68  ALA A CA  1 
ATOM   339  C  C   . ALA A 1 90  ? 44.275 55.625  51.460 1.00 28.95  ? 68  ALA A C   1 
ATOM   340  O  O   . ALA A 1 90  ? 44.522 56.727  50.955 1.00 29.97  ? 68  ALA A O   1 
ATOM   341  C  CB  . ALA A 1 90  ? 44.491 53.568  50.037 1.00 29.33  ? 68  ALA A CB  1 
ATOM   342  N  N   . SER A 1 91  ? 43.253 55.445  52.301 1.00 25.96  ? 69  SER A N   1 
ATOM   343  C  CA  . SER A 1 91  ? 42.411 56.577  52.674 1.00 25.91  ? 69  SER A CA  1 
ATOM   344  C  C   . SER A 1 91  ? 43.147 57.539  53.597 1.00 28.04  ? 69  SER A C   1 
ATOM   345  O  O   . SER A 1 91  ? 42.898 58.750  53.553 1.00 28.43  ? 69  SER A O   1 
ATOM   346  C  CB  . SER A 1 91  ? 41.119 56.087  53.329 1.00 26.60  ? 69  SER A CB  1 
ATOM   347  O  OG  . SER A 1 91  ? 41.373 55.493  54.590 1.00 27.11  ? 69  SER A OG  1 
ATOM   348  N  N   . ALA A 1 92  ? 44.051 57.027  54.437 1.00 25.82  ? 70  ALA A N   1 
ATOM   349  C  CA  . ALA A 1 92  ? 44.888 57.913  55.238 1.00 30.78  ? 70  ALA A CA  1 
ATOM   350  C  C   . ALA A 1 92  ? 45.799 58.751  54.352 1.00 27.72  ? 70  ALA A C   1 
ATOM   351  O  O   . ALA A 1 92  ? 45.956 59.957  54.574 1.00 25.16  ? 70  ALA A O   1 
ATOM   352  C  CB  . ALA A 1 92  ? 45.712 57.104  56.239 1.00 27.57  ? 70  ALA A CB  1 
ATOM   353  N  N   . LYS A 1 93  ? 46.402 58.128  53.335 1.00 25.86  ? 71  LYS A N   1 
ATOM   354  C  CA  . LYS A 1 93  ? 47.280 58.862  52.431 1.00 27.82  ? 71  LYS A CA  1 
ATOM   355  C  C   . LYS A 1 93  ? 46.522 59.957  51.693 1.00 27.11  ? 71  LYS A C   1 
ATOM   356  O  O   . LYS A 1 93  ? 47.070 61.032  51.429 1.00 29.32  ? 71  LYS A O   1 
ATOM   357  C  CB  . LYS A 1 93  ? 47.936 57.902  51.438 1.00 29.24  ? 71  LYS A CB  1 
ATOM   358  C  CG  . LYS A 1 93  ? 49.064 57.073  52.033 1.00 43.63  ? 71  LYS A CG  1 
ATOM   359  C  CD  . LYS A 1 93  ? 49.576 56.038  51.043 1.00 55.56  ? 71  LYS A CD  1 
ATOM   360  C  CE  . LYS A 1 93  ? 50.657 55.169  51.667 1.00 55.66  ? 71  LYS A CE  1 
ATOM   361  N  NZ  . LYS A 1 93  ? 51.081 54.066  50.760 1.00 62.56  ? 71  LYS A NZ  1 
ATOM   362  N  N   . ASN A 1 94  ? 45.257 59.703  51.353 1.00 28.65  ? 72  ASN A N   1 
ATOM   363  C  CA  . ASN A 1 94  ? 44.461 60.729  50.690 1.00 27.24  ? 72  ASN A CA  1 
ATOM   364  C  C   . ASN A 1 94  ? 44.092 61.846  51.656 1.00 27.16  ? 72  ASN A C   1 
ATOM   365  O  O   . ASN A 1 94  ? 44.151 63.027  51.298 1.00 29.38  ? 72  ASN A O   1 
ATOM   366  C  CB  . ASN A 1 94  ? 43.203 60.111  50.081 1.00 29.19  ? 72  ASN A CB  1 
ATOM   367  C  CG  . ASN A 1 94  ? 43.487 59.371  48.791 1.00 34.74  ? 72  ASN A CG  1 
ATOM   368  O  OD1 . ASN A 1 94  ? 44.500 59.614  48.139 1.00 28.60  ? 72  ASN A OD1 1 
ATOM   369  N  ND2 . ASN A 1 94  ? 42.596 58.462  48.418 1.00 29.28  ? 72  ASN A ND2 1 
ATOM   370  N  N   . LEU A 1 95  ? 43.721 61.492  52.888 1.00 28.45  ? 73  LEU A N   1 
ATOM   371  C  CA  . LEU A 1 95  ? 43.293 62.499  53.855 1.00 28.67  ? 73  LEU A CA  1 
ATOM   372  C  C   . LEU A 1 95  ? 44.412 63.489  54.157 1.00 29.79  ? 73  LEU A C   1 
ATOM   373  O  O   . LEU A 1 95  ? 44.187 64.704  54.194 1.00 26.11  ? 73  LEU A O   1 
ATOM   374  C  CB  . LEU A 1 95  ? 42.812 61.820  55.136 1.00 26.76  ? 73  LEU A CB  1 
ATOM   375  C  CG  . LEU A 1 95  ? 41.360 61.340  55.110 1.00 28.03  ? 73  LEU A CG  1 
ATOM   376  C  CD1 . LEU A 1 95  ? 41.037 60.514  56.344 1.00 29.85  ? 73  LEU A CD1 1 
ATOM   377  C  CD2 . LEU A 1 95  ? 40.418 62.526  54.991 1.00 25.37  ? 73  LEU A CD2 1 
ATOM   378  N  N   . ILE A 1 96  ? 45.631 62.989  54.370 1.00 27.39  ? 74  ILE A N   1 
ATOM   379  C  CA  . ILE A 1 96  ? 46.746 63.854  54.745 1.00 30.60  ? 74  ILE A CA  1 
ATOM   380  C  C   . ILE A 1 96  ? 47.631 64.236  53.566 1.00 32.51  ? 74  ILE A C   1 
ATOM   381  O  O   . ILE A 1 96  ? 48.518 65.089  53.728 1.00 26.76  ? 74  ILE A O   1 
ATOM   382  C  CB  . ILE A 1 96  ? 47.604 63.210  55.856 1.00 27.79  ? 74  ILE A CB  1 
ATOM   383  C  CG1 . ILE A 1 96  ? 48.324 61.966  55.332 1.00 35.74  ? 74  ILE A CG1 1 
ATOM   384  C  CG2 . ILE A 1 96  ? 46.744 62.867  57.062 1.00 28.77  ? 74  ILE A CG2 1 
ATOM   385  C  CD1 . ILE A 1 96  ? 49.323 61.386  56.310 1.00 30.84  ? 74  ILE A CD1 1 
ATOM   386  N  N   . GLY A 1 97  ? 47.415 63.653  52.388 1.00 29.86  ? 75  GLY A N   1 
ATOM   387  C  CA  . GLY A 1 97  ? 48.253 63.950  51.242 1.00 27.32  ? 75  GLY A CA  1 
ATOM   388  C  C   . GLY A 1 97  ? 47.576 64.773  50.165 1.00 28.12  ? 75  GLY A C   1 
ATOM   389  O  O   . GLY A 1 97  ? 48.250 65.462  49.393 1.00 29.16  ? 75  GLY A O   1 
ATOM   390  N  N   . ASP A 1 98  ? 46.321 64.776  49.997 1.00 27.11  ? 76  ASP A N   1 
ATOM   391  C  CA  . ASP A 1 98  ? 45.542 65.504  49.008 1.00 26.81  ? 76  ASP A CA  1 
ATOM   392  C  C   . ASP A 1 98  ? 45.243 66.923  49.471 1.00 30.71  ? 76  ASP A C   1 
ATOM   393  O  O   . ASP A 1 98  ? 45.361 67.266  50.651 1.00 27.72  ? 76  ASP A O   1 
ATOM   394  C  CB  . ASP A 1 98  ? 44.210 64.816  48.728 1.00 27.47  ? 76  ASP A CB  1 
ATOM   395  C  CG  . ASP A 1 98  ? 44.364 63.539  47.966 1.00 27.95  ? 76  ASP A CG  1 
ATOM   396  O  OD1 . ASP A 1 98  ? 45.463 63.338  47.413 1.00 29.86  ? 76  ASP A OD1 1 
ATOM   397  O  OD2 . ASP A 1 98  ? 43.399 62.744  47.922 1.00 27.23  ? 76  ASP A OD2 1 
ATOM   398  N  N   . THR A 1 99  ? 44.893 67.721  48.559 1.00 28.85  ? 77  THR A N   1 
ATOM   399  C  CA  . THR A 1 99  ? 44.326 69.038  48.820 1.00 24.99  ? 77  THR A CA  1 
ATOM   400  C  C   . THR A 1 99  ? 42.874 69.072  48.359 1.00 31.48  ? 77  THR A C   1 
ATOM   401  O  O   . THR A 1 99  ? 41.963 69.068  49.191 1.00 29.80  ? 77  THR A O   1 
ATOM   402  C  CB  . THR A 1 99  ? 45.149 70.133  48.135 1.00 30.10  ? 77  THR A CB  1 
ATOM   403  O  OG1 . THR A 1 99  ? 45.223 69.869  46.729 1.00 28.34  ? 77  THR A OG1 1 
ATOM   404  C  CG2 . THR A 1 99  ? 46.556 70.182  48.714 1.00 27.13  ? 77  THR A CG2 1 
ATOM   405  N  N   . LYS A 1 100 ? 42.632 69.076  47.044 1.00 28.12  ? 78  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 100 ? 41.268 69.153  46.529 1.00 29.23  ? 78  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 100 ? 40.414 67.989  47.017 1.00 32.75  ? 78  LYS A C   1 
ATOM   408  O  O   . LYS A 1 100 ? 39.252 68.179  47.398 1.00 32.33  ? 78  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 100 ? 41.290 69.191  45.000 1.00 33.19  ? 78  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 100 ? 40.042 68.614  44.347 1.00 39.12  ? 78  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 100 ? 40.005 68.897  42.855 1.00 50.21  ? 78  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 100 ? 38.909 68.093  42.171 1.00 53.72  ? 78  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 100 ? 38.313 68.830  41.024 1.00 60.29  ? 78  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 101 ? 40.971 66.781  47.024 1.00 26.56  ? 79  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 101 ? 40.207 65.576  47.312 1.00 28.51  ? 79  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 101 ? 40.272 65.156  48.776 1.00 26.92  ? 79  ASN A C   1 
ATOM   417  O  O   . ASN A 1 101 ? 39.865 64.037  49.103 1.00 27.98  ? 79  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 101 ? 40.690 64.426  46.424 1.00 28.31  ? 79  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 101 ? 40.274 64.598  44.977 1.00 35.79  ? 79  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 101 ? 39.282 65.262  44.680 1.00 38.21  ? 79  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 101 ? 41.034 64.000  44.067 1.00 34.50  ? 79  ASN A ND2 1 
ATOM   422  N  N   . SER A 1 102 ? 40.770 66.014  49.660 1.00 26.35  ? 80  SER A N   1 
ATOM   423  C  CA  . SER A 1 102 ? 40.808 65.694  51.081 1.00 25.46  ? 80  SER A CA  1 
ATOM   424  C  C   . SER A 1 102 ? 39.792 66.551  51.818 1.00 25.27  ? 80  SER A C   1 
ATOM   425  O  O   . SER A 1 102 ? 39.966 67.778  51.893 1.00 22.60  ? 80  SER A O   1 
ATOM   426  C  CB  . SER A 1 102 ? 42.208 65.916  51.655 1.00 22.68  ? 80  SER A CB  1 
ATOM   427  O  OG  . SER A 1 102 ? 42.197 65.803  53.070 1.00 24.67  ? 80  SER A OG  1 
ATOM   428  N  N   . PRO A 1 103 ? 38.721 65.967  52.365 1.00 26.97  ? 81  PRO A N   1 
ATOM   429  C  CA  . PRO A 1 103 ? 37.794 66.771  53.177 1.00 22.18  ? 81  PRO A CA  1 
ATOM   430  C  C   . PRO A 1 103 ? 38.468 67.402  54.378 1.00 23.95  ? 81  PRO A C   1 
ATOM   431  O  O   . PRO A 1 103 ? 38.087 68.506  54.790 1.00 24.81  ? 81  PRO A O   1 
ATOM   432  C  CB  . PRO A 1 103 ? 36.721 65.755  53.597 1.00 22.30  ? 81  PRO A CB  1 
ATOM   433  C  CG  . PRO A 1 103 ? 36.845 64.627  52.611 1.00 21.00  ? 81  PRO A CG  1 
ATOM   434  C  CD  . PRO A 1 103 ? 38.302 64.558  52.276 1.00 21.40  ? 81  PRO A CD  1 
ATOM   435  N  N   . ALA A 1 104 ? 39.469 66.729  54.949 1.00 23.48  ? 82  ALA A N   1 
ATOM   436  C  CA  . ALA A 1 104 ? 40.211 67.296  56.069 1.00 27.22  ? 82  ALA A CA  1 
ATOM   437  C  C   . ALA A 1 104 ? 40.921 68.579  55.661 1.00 22.40  ? 82  ALA A C   1 
ATOM   438  O  O   . ALA A 1 104 ? 40.859 69.591  56.370 1.00 25.89  ? 82  ALA A O   1 
ATOM   439  C  CB  . ALA A 1 104 ? 41.212 66.270  56.597 1.00 19.94  ? 82  ALA A CB  1 
ATOM   440  N  N   . TYR A 1 105 ? 41.606 68.554  54.516 1.00 23.22  ? 83  TYR A N   1 
ATOM   441  C  CA  . TYR A 1 105 ? 42.281 69.750  54.021 1.00 26.26  ? 83  TYR A CA  1 
ATOM   442  C  C   . TYR A 1 105 ? 41.283 70.872  53.761 1.00 24.78  ? 83  TYR A C   1 
ATOM   443  O  O   . TYR A 1 105 ? 41.517 72.027  54.134 1.00 21.67  ? 83  TYR A O   1 
ATOM   444  C  CB  . TYR A 1 105 ? 43.062 69.415  52.748 1.00 23.51  ? 83  TYR A CB  1 
ATOM   445  C  CG  . TYR A 1 105 ? 43.730 70.604  52.091 1.00 29.33  ? 83  TYR A CG  1 
ATOM   446  C  CD1 . TYR A 1 105 ? 43.066 71.359  51.130 1.00 25.09  ? 83  TYR A CD1 1 
ATOM   447  C  CD2 . TYR A 1 105 ? 45.029 70.965  52.424 1.00 30.60  ? 83  TYR A CD2 1 
ATOM   448  C  CE1 . TYR A 1 105 ? 43.674 72.442  50.527 1.00 30.96  ? 83  TYR A CE1 1 
ATOM   449  C  CE2 . TYR A 1 105 ? 45.644 72.046  51.825 1.00 28.78  ? 83  TYR A CE2 1 
ATOM   450  C  CZ  . TYR A 1 105 ? 44.962 72.781  50.877 1.00 26.96  ? 83  TYR A CZ  1 
ATOM   451  O  OH  . TYR A 1 105 ? 45.571 73.858  50.277 1.00 28.27  ? 83  TYR A OH  1 
ATOM   452  N  N   . GLN A 1 106 ? 40.160 70.546  53.116 1.00 24.13  ? 84  GLN A N   1 
ATOM   453  C  CA  . GLN A 1 106 ? 39.180 71.570  52.770 1.00 25.49  ? 84  GLN A CA  1 
ATOM   454  C  C   . GLN A 1 106 ? 38.571 72.201  54.016 1.00 24.86  ? 84  GLN A C   1 
ATOM   455  O  O   . GLN A 1 106 ? 38.290 73.406  54.036 1.00 24.31  ? 84  GLN A O   1 
ATOM   456  C  CB  . GLN A 1 106 ? 38.089 70.970  51.883 1.00 26.82  ? 84  GLN A CB  1 
ATOM   457  C  CG  . GLN A 1 106 ? 38.588 70.465  50.537 1.00 29.92  ? 84  GLN A CG  1 
ATOM   458  C  CD  . GLN A 1 106 ? 39.129 71.578  49.662 1.00 27.69  ? 84  GLN A CD  1 
ATOM   459  O  OE1 . GLN A 1 106 ? 38.702 72.728  49.765 1.00 23.11  ? 84  GLN A OE1 1 
ATOM   460  N  NE2 . GLN A 1 106 ? 40.077 71.243  48.795 1.00 28.95  ? 84  GLN A NE2 1 
ATOM   461  N  N   . ALA A 1 107 ? 38.361 71.406  55.067 1.00 22.57  ? 85  ALA A N   1 
ATOM   462  C  CA  . ALA A 1 107 ? 37.779 71.946  56.292 1.00 26.11  ? 85  ALA A CA  1 
ATOM   463  C  C   . ALA A 1 107 ? 38.757 72.866  57.010 1.00 28.43  ? 85  ALA A C   1 
ATOM   464  O  O   . ALA A 1 107 ? 38.356 73.897  57.563 1.00 21.59  ? 85  ALA A O   1 
ATOM   465  C  CB  . ALA A 1 107 ? 37.339 70.809  57.213 1.00 20.74  ? 85  ALA A CB  1 
ATOM   466  N  N   . VAL A 1 108 ? 40.042 72.505  57.020 1.00 22.20  ? 86  VAL A N   1 
ATOM   467  C  CA  . VAL A 1 108 ? 41.055 73.385  57.597 1.00 26.37  ? 86  VAL A CA  1 
ATOM   468  C  C   . VAL A 1 108 ? 41.095 74.704  56.838 1.00 24.57  ? 86  VAL A C   1 
ATOM   469  O  O   . VAL A 1 108 ? 41.102 75.788  57.434 1.00 26.37  ? 86  VAL A O   1 
ATOM   470  C  CB  . VAL A 1 108 ? 42.430 72.693  57.596 1.00 22.84  ? 86  VAL A CB  1 
ATOM   471  C  CG1 . VAL A 1 108 ? 43.532 73.695  57.908 1.00 25.38  ? 86  VAL A CG1 1 
ATOM   472  C  CG2 . VAL A 1 108 ? 42.444 71.545  58.589 1.00 25.39  ? 86  VAL A CG2 1 
ATOM   473  N  N   . LEU A 1 109 ? 41.112 74.625  55.506 1.00 22.94  ? 87  LEU A N   1 
ATOM   474  C  CA  . LEU A 1 109 ? 41.118 75.829  54.682 1.00 23.13  ? 87  LEU A CA  1 
ATOM   475  C  C   . LEU A 1 109 ? 39.873 76.675  54.926 1.00 20.32  ? 87  LEU A C   1 
ATOM   476  O  O   . LEU A 1 109 ? 39.945 77.909  54.935 1.00 23.26  ? 87  LEU A O   1 
ATOM   477  C  CB  . LEU A 1 109 ? 41.229 75.438  53.208 1.00 22.54  ? 87  LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 109 ? 41.394 76.539  52.161 1.00 31.65  ? 87  LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 109 ? 42.550 77.453  52.520 1.00 24.88  ? 87  LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 109 ? 41.605 75.923  50.786 1.00 24.54  ? 87  LEU A CD2 1 
ATOM   481  N  N   . LEU A 1 110 ? 38.725 76.028  55.139 1.00 22.43  ? 88  LEU A N   1 
ATOM   482  C  CA  . LEU A 1 110 ? 37.485 76.770  55.354 1.00 19.94  ? 88  LEU A CA  1 
ATOM   483  C  C   . LEU A 1 110 ? 37.523 77.539  56.669 1.00 24.36  ? 88  LEU A C   1 
ATOM   484  O  O   . LEU A 1 110 ? 37.141 78.714  56.722 1.00 23.78  ? 88  LEU A O   1 
ATOM   485  C  CB  . LEU A 1 110 ? 36.289 75.817  55.321 1.00 18.60  ? 88  LEU A CB  1 
ATOM   486  C  CG  . LEU A 1 110 ? 34.919 76.458  55.555 1.00 22.19  ? 88  LEU A CG  1 
ATOM   487  C  CD1 . LEU A 1 110 ? 34.678 77.584  54.561 1.00 22.64  ? 88  LEU A CD1 1 
ATOM   488  C  CD2 . LEU A 1 110 ? 33.813 75.418  55.468 1.00 24.01  ? 88  LEU A CD2 1 
ATOM   489  N  N   . ALA A 1 111 ? 37.978 76.891  57.745 1.00 21.18  ? 89  ALA A N   1 
ATOM   490  C  CA  . ALA A 1 111 ? 38.063 77.571  59.034 1.00 22.53  ? 89  ALA A CA  1 
ATOM   491  C  C   . ALA A 1 111 ? 39.015 78.759  58.970 1.00 21.99  ? 89  ALA A C   1 
ATOM   492  O  O   . ALA A 1 111 ? 38.752 79.810  59.567 1.00 22.96  ? 89  ALA A O   1 
ATOM   493  C  CB  . ALA A 1 111 ? 38.501 76.585  60.117 1.00 23.36  ? 89  ALA A CB  1 
ATOM   494  N  N   . ILE A 1 112 ? 40.124 78.614  58.243 1.00 26.42  ? 90  ILE A N   1 
ATOM   495  C  CA  . ILE A 1 112 ? 41.074 79.712  58.097 1.00 22.84  ? 90  ILE A CA  1 
ATOM   496  C  C   . ILE A 1 112 ? 40.455 80.849  57.295 1.00 27.51  ? 90  ILE A C   1 
ATOM   497  O  O   . ILE A 1 112 ? 40.565 82.025  57.662 1.00 24.78  ? 90  ILE A O   1 
ATOM   498  C  CB  . ILE A 1 112 ? 42.374 79.209  57.443 1.00 26.64  ? 90  ILE A CB  1 
ATOM   499  C  CG1 . ILE A 1 112 ? 43.111 78.249  58.377 1.00 27.53  ? 90  ILE A CG1 1 
ATOM   500  C  CG2 . ILE A 1 112 ? 43.268 80.378  57.056 1.00 29.38  ? 90  ILE A CG2 1 
ATOM   501  C  CD1 . ILE A 1 112 ? 44.202 77.459  57.689 1.00 25.96  ? 90  ILE A CD1 1 
ATOM   502  N  N   . ASN A 1 113 ? 39.792 80.514  56.187 1.00 24.61  ? 91  ASN A N   1 
ATOM   503  C  CA  . ASN A 1 113 ? 39.253 81.540  55.302 1.00 26.63  ? 91  ASN A CA  1 
ATOM   504  C  C   . ASN A 1 113 ? 38.077 82.275  55.932 1.00 25.78  ? 91  ASN A C   1 
ATOM   505  O  O   . ASN A 1 113 ? 37.884 83.467  55.669 1.00 25.94  ? 91  ASN A O   1 
ATOM   506  C  CB  . ASN A 1 113 ? 38.841 80.913  53.971 1.00 25.12  ? 91  ASN A CB  1 
ATOM   507  C  CG  . ASN A 1 113 ? 40.022 80.689  53.045 1.00 31.85  ? 91  ASN A CG  1 
ATOM   508  O  OD1 . ASN A 1 113 ? 41.012 81.418  53.097 1.00 27.34  ? 91  ASN A OD1 1 
ATOM   509  N  ND2 . ASN A 1 113 ? 39.918 79.684  52.184 1.00 27.98  ? 91  ASN A ND2 1 
ATOM   510  N  N   . ALA A 1 114 ? 37.282 81.588  56.755 1.00 23.00  ? 92  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 114 ? 36.188 82.261  57.447 1.00 29.60  ? 92  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 114 ? 36.716 83.330  58.394 1.00 26.33  ? 92  ALA A C   1 
ATOM   513  O  O   . ALA A 1 114 ? 36.112 84.400  58.533 1.00 28.30  ? 92  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 114 ? 35.338 81.241  58.205 1.00 23.42  ? 92  ALA A CB  1 
ATOM   515  N  N   . ALA A 1 115 ? 37.850 83.062  59.047 1.00 22.68  ? 93  ALA A N   1 
ATOM   516  C  CA  . ALA A 1 115 ? 38.437 84.042  59.956 1.00 29.31  ? 93  ALA A CA  1 
ATOM   517  C  C   . ALA A 1 115 ? 38.985 85.241  59.192 1.00 25.18  ? 93  ALA A C   1 
ATOM   518  O  O   . ALA A 1 115 ? 38.733 86.393  59.563 1.00 26.47  ? 93  ALA A O   1 
ATOM   519  C  CB  . ALA A 1 115 ? 39.537 83.389  60.794 1.00 20.72  ? 93  ALA A CB  1 
ATOM   520  N  N   . VAL A 1 116 ? 39.744 84.986  58.123 1.00 26.44  ? 94  VAL A N   1 
ATOM   521  C  CA  . VAL A 1 116 ? 40.296 86.075  57.319 1.00 31.08  ? 94  VAL A CA  1 
ATOM   522  C  C   . VAL A 1 116 ? 39.173 86.890  56.689 1.00 31.65  ? 94  VAL A C   1 
ATOM   523  O  O   . VAL A 1 116 ? 39.181 88.126  56.724 1.00 26.67  ? 94  VAL A O   1 
ATOM   524  C  CB  . VAL A 1 116 ? 41.255 85.521  56.250 1.00 29.81  ? 94  VAL A CB  1 
ATOM   525  C  CG1 . VAL A 1 116 ? 41.778 86.646  55.366 1.00 28.58  ? 94  VAL A CG1 1 
ATOM   526  C  CG2 . VAL A 1 116 ? 42.405 84.769  56.902 1.00 25.31  ? 94  VAL A CG2 1 
ATOM   527  N  N   . GLY A 1 117 ? 38.187 86.206  56.102 1.00 28.46  ? 95  GLY A N   1 
ATOM   528  C  CA  . GLY A 1 117 ? 37.081 86.907  55.475 1.00 26.83  ? 95  GLY A CA  1 
ATOM   529  C  C   . GLY A 1 117 ? 36.252 87.714  56.454 1.00 26.88  ? 95  GLY A C   1 
ATOM   530  O  O   . GLY A 1 117 ? 35.684 88.747  56.088 1.00 25.55  ? 95  GLY A O   1 
ATOM   531  N  N   . PHE A 1 118 ? 36.165 87.256  57.705 1.00 26.30  ? 96  PHE A N   1 
ATOM   532  C  CA  . PHE A 1 118 ? 35.437 88.010  58.721 1.00 32.01  ? 96  PHE A CA  1 
ATOM   533  C  C   . PHE A 1 118 ? 36.069 89.377  58.945 1.00 32.40  ? 96  PHE A C   1 
ATOM   534  O  O   . PHE A 1 118 ? 35.364 90.390  59.030 1.00 26.82  ? 96  PHE A O   1 
ATOM   535  C  CB  . PHE A 1 118 ? 35.394 87.215  60.027 1.00 29.27  ? 96  PHE A CB  1 
ATOM   536  C  CG  . PHE A 1 118 ? 34.640 87.899  61.134 1.00 31.61  ? 96  PHE A CG  1 
ATOM   537  C  CD1 . PHE A 1 118 ? 33.255 87.884  61.160 1.00 27.64  ? 96  PHE A CD1 1 
ATOM   538  C  CD2 . PHE A 1 118 ? 35.318 88.545  62.155 1.00 26.94  ? 96  PHE A CD2 1 
ATOM   539  C  CE1 . PHE A 1 118 ? 32.560 88.507  62.180 1.00 29.87  ? 96  PHE A CE1 1 
ATOM   540  C  CE2 . PHE A 1 118 ? 34.628 89.170  63.178 1.00 36.26  ? 96  PHE A CE2 1 
ATOM   541  C  CZ  . PHE A 1 118 ? 33.247 89.149  63.191 1.00 32.47  ? 96  PHE A CZ  1 
ATOM   542  N  N   . TRP A 1 119 ? 37.400 89.427  59.034 1.00 27.45  ? 97  TRP A N   1 
ATOM   543  C  CA  . TRP A 1 119 ? 38.082 90.702  59.222 1.00 28.35  ? 97  TRP A CA  1 
ATOM   544  C  C   . TRP A 1 119 ? 38.031 91.548  57.956 1.00 35.85  ? 97  TRP A C   1 
ATOM   545  O  O   . TRP A 1 119 ? 37.930 92.778  58.029 1.00 32.41  ? 97  TRP A O   1 
ATOM   546  C  CB  . TRP A 1 119 ? 39.528 90.466  59.653 1.00 29.79  ? 97  TRP A CB  1 
ATOM   547  C  CG  . TRP A 1 119 ? 40.322 91.726  59.796 1.00 34.55  ? 97  TRP A CG  1 
ATOM   548  C  CD1 . TRP A 1 119 ? 41.433 92.079  59.087 1.00 28.45  ? 97  TRP A CD1 1 
ATOM   549  C  CD2 . TRP A 1 119 ? 40.068 92.802  60.707 1.00 33.52  ? 97  TRP A CD2 1 
ATOM   550  N  NE1 . TRP A 1 119 ? 41.886 93.308  59.499 1.00 32.78  ? 97  TRP A NE1 1 
ATOM   551  C  CE2 . TRP A 1 119 ? 41.066 93.774  60.493 1.00 32.24  ? 97  TRP A CE2 1 
ATOM   552  C  CE3 . TRP A 1 119 ? 39.094 93.039  61.683 1.00 30.83  ? 97  TRP A CE3 1 
ATOM   553  C  CZ2 . TRP A 1 119 ? 41.119 94.962  61.219 1.00 36.08  ? 97  TRP A CZ2 1 
ATOM   554  C  CZ3 . TRP A 1 119 ? 39.148 94.220  62.402 1.00 32.28  ? 97  TRP A CZ3 1 
ATOM   555  C  CH2 . TRP A 1 119 ? 40.154 95.166  62.167 1.00 34.11  ? 97  TRP A CH2 1 
ATOM   556  N  N   . ASN A 1 120 ? 38.104 90.907  56.786 1.00 28.02  ? 98  ASN A N   1 
ATOM   557  C  CA  . ASN A 1 120 ? 37.988 91.643  55.532 1.00 32.63  ? 98  ASN A CA  1 
ATOM   558  C  C   . ASN A 1 120 ? 36.639 92.340  55.417 1.00 32.80  ? 98  ASN A C   1 
ATOM   559  O  O   . ASN A 1 120 ? 36.542 93.406  54.797 1.00 32.47  ? 98  ASN A O   1 
ATOM   560  C  CB  . ASN A 1 120 ? 38.199 90.700  54.346 1.00 24.54  ? 98  ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 120 ? 39.665 90.470  54.033 1.00 31.29  ? 98  ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 120 ? 40.541 91.151  54.566 1.00 34.74  ? 98  ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 120 ? 39.940 89.506  53.161 1.00 32.45  ? 98  ASN A ND2 1 
ATOM   564  N  N   . VAL A 1 121 ? 35.592 91.762  56.008 1.00 31.66  ? 99  VAL A N   1 
ATOM   565  C  CA  . VAL A 1 121 ? 34.272 92.383  55.955 1.00 31.61  ? 99  VAL A CA  1 
ATOM   566  C  C   . VAL A 1 121 ? 34.217 93.612  56.857 1.00 34.54  ? 99  VAL A C   1 
ATOM   567  O  O   . VAL A 1 121 ? 33.682 94.658  56.469 1.00 35.29  ? 99  VAL A O   1 
ATOM   568  C  CB  . VAL A 1 121 ? 33.185 91.359  56.333 1.00 30.87  ? 99  VAL A CB  1 
ATOM   569  C  CG1 . VAL A 1 121 ? 31.853 92.057  56.575 1.00 31.23  ? 99  VAL A CG1 1 
ATOM   570  C  CG2 . VAL A 1 121 ? 33.044 90.299  55.248 1.00 30.94  ? 99  VAL A CG2 1 
ATOM   571  N  N   . LEU A 1 122 ? 34.778 93.515  58.064 1.00 31.98  ? 100 LEU A N   1 
ATOM   572  C  CA  . LEU A 1 122 ? 34.544 94.507  59.104 1.00 30.80  ? 100 LEU A CA  1 
ATOM   573  C  C   . LEU A 1 122 ? 35.751 95.372  59.438 1.00 35.54  ? 100 LEU A C   1 
ATOM   574  O  O   . LEU A 1 122 ? 35.601 96.336  60.198 1.00 38.54  ? 100 LEU A O   1 
ATOM   575  C  CB  . LEU A 1 122 ? 34.063 93.815  60.388 1.00 27.12  ? 100 LEU A CB  1 
ATOM   576  C  CG  . LEU A 1 122 ? 32.708 93.113  60.300 1.00 32.99  ? 100 LEU A CG  1 
ATOM   577  C  CD1 . LEU A 1 122 ? 32.539 92.128  61.444 1.00 37.73  ? 100 LEU A CD1 1 
ATOM   578  C  CD2 . LEU A 1 122 ? 31.580 94.131  60.293 1.00 32.62  ? 100 LEU A CD2 1 
ATOM   579  N  N   . GLY A 1 123 ? 36.932 95.065  58.900 1.00 31.79  ? 101 GLY A N   1 
ATOM   580  C  CA  . GLY A 1 123 ? 38.124 95.805  59.288 1.00 33.49  ? 101 GLY A CA  1 
ATOM   581  C  C   . GLY A 1 123 ? 38.042 97.285  58.963 1.00 37.54  ? 101 GLY A C   1 
ATOM   582  O  O   . GLY A 1 123 ? 38.505 98.126  59.739 1.00 33.21  ? 101 GLY A O   1 
ATOM   583  N  N   . TYR A 1 124 ? 37.444 97.626  57.819 1.00 35.86  ? 102 TYR A N   1 
ATOM   584  C  CA  . TYR A 1 124 ? 37.398 99.022  57.394 1.00 39.26  ? 102 TYR A CA  1 
ATOM   585  C  C   . TYR A 1 124 ? 36.557 99.877  58.335 1.00 38.46  ? 102 TYR A C   1 
ATOM   586  O  O   . TYR A 1 124 ? 36.862 101.057 58.541 1.00 43.31  ? 102 TYR A O   1 
ATOM   587  C  CB  . TYR A 1 124 ? 36.854 99.118  55.967 1.00 36.59  ? 102 TYR A CB  1 
ATOM   588  C  CG  . TYR A 1 124 ? 35.344 99.083  55.887 1.00 39.46  ? 102 TYR A CG  1 
ATOM   589  C  CD1 . TYR A 1 124 ? 34.650 97.892  56.049 1.00 39.82  ? 102 TYR A CD1 1 
ATOM   590  C  CD2 . TYR A 1 124 ? 34.612 100.243 55.661 1.00 36.04  ? 102 TYR A CD2 1 
ATOM   591  C  CE1 . TYR A 1 124 ? 33.271 97.853  55.982 1.00 39.19  ? 102 TYR A CE1 1 
ATOM   592  C  CE2 . TYR A 1 124 ? 33.231 100.214 55.594 1.00 32.41  ? 102 TYR A CE2 1 
ATOM   593  C  CZ  . TYR A 1 124 ? 32.567 99.017  55.754 1.00 39.33  ? 102 TYR A CZ  1 
ATOM   594  O  OH  . TYR A 1 124 ? 31.193 98.981  55.687 1.00 36.84  ? 102 TYR A OH  1 
ATOM   595  N  N   . ALA A 1 125 ? 35.501 99.308  58.909 1.00 41.18  ? 103 ALA A N   1 
ATOM   596  C  CA  . ALA A 1 125 ? 34.602 100.042 59.788 1.00 42.23  ? 103 ALA A CA  1 
ATOM   597  C  C   . ALA A 1 125 ? 35.069 100.052 61.237 1.00 42.32  ? 103 ALA A C   1 
ATOM   598  O  O   . ALA A 1 125 ? 34.425 100.689 62.077 1.00 40.65  ? 103 ALA A O   1 
ATOM   599  C  CB  . ALA A 1 125 ? 33.190 99.451  59.708 1.00 33.02  ? 103 ALA A CB  1 
ATOM   600  N  N   . THR A 1 126 ? 36.173 99.378  61.543 1.00 34.72  ? 104 THR A N   1 
ATOM   601  C  CA  . THR A 1 126 ? 36.613 99.212  62.921 1.00 35.91  ? 104 THR A CA  1 
ATOM   602  C  C   . THR A 1 126 ? 37.383 100.439 63.394 1.00 40.80  ? 104 THR A C   1 
ATOM   603  O  O   . THR A 1 126 ? 38.323 100.888 62.731 1.00 39.80  ? 104 THR A O   1 
ATOM   604  C  CB  . THR A 1 126 ? 37.482 97.959  63.043 1.00 39.54  ? 104 THR A CB  1 
ATOM   605  O  OG1 . THR A 1 126 ? 36.673 96.796  62.829 1.00 37.16  ? 104 THR A OG1 1 
ATOM   606  C  CG2 . THR A 1 126 ? 38.120 97.882  64.418 1.00 35.97  ? 104 THR A CG2 1 
ATOM   607  N  N   . GLN A 1 127 ? 36.981 100.978 64.542 1.00 37.39  ? 105 GLN A N   1 
ATOM   608  C  CA  . GLN A 1 127 ? 37.659 102.126 65.129 1.00 41.41  ? 105 GLN A CA  1 
ATOM   609  C  C   . GLN A 1 127 ? 38.973 101.686 65.763 1.00 35.88  ? 105 GLN A C   1 
ATOM   610  O  O   . GLN A 1 127 ? 39.001 100.743 66.559 1.00 36.48  ? 105 GLN A O   1 
ATOM   611  C  CB  . GLN A 1 127 ? 36.766 102.788 66.179 1.00 41.36  ? 105 GLN A CB  1 
ATOM   612  C  CG  . GLN A 1 127 ? 36.700 104.301 66.084 1.00 48.50  ? 105 GLN A CG  1 
ATOM   613  C  CD  . GLN A 1 127 ? 35.775 104.906 67.122 1.00 54.68  ? 105 GLN A CD  1 
ATOM   614  O  OE1 . GLN A 1 127 ? 35.801 104.525 68.293 1.00 49.29  ? 105 GLN A OE1 1 
ATOM   615  N  NE2 . GLN A 1 127 ? 34.948 105.854 66.695 1.00 49.40  ? 105 GLN A NE2 1 
ATOM   616  N  N   . CYS A 1 128 ? 40.061 102.367 65.412 1.00 35.25  ? 106 CYS A N   1 
ATOM   617  C  CA  . CYS A 1 128 ? 41.355 102.089 66.013 1.00 38.87  ? 106 CYS A CA  1 
ATOM   618  C  C   . CYS A 1 128 ? 42.102 103.400 66.209 1.00 38.81  ? 106 CYS A C   1 
ATOM   619  O  O   . CYS A 1 128 ? 41.731 104.442 65.661 1.00 43.72  ? 106 CYS A O   1 
ATOM   620  C  CB  . CYS A 1 128 ? 42.177 101.098 65.171 1.00 38.25  ? 106 CYS A CB  1 
ATOM   621  S  SG  . CYS A 1 128 ? 42.507 101.573 63.462 1.00 38.72  ? 106 CYS A SG  1 
ATOM   622  N  N   . GLY A 1 129 ? 43.156 103.344 67.007 1.00 41.08  ? 107 GLY A N   1 
ATOM   623  C  CA  . GLY A 1 129 ? 43.956 104.515 67.290 1.00 43.56  ? 107 GLY A CA  1 
ATOM   624  C  C   . GLY A 1 129 ? 44.554 104.434 68.680 1.00 43.74  ? 107 GLY A C   1 
ATOM   625  O  O   . GLY A 1 129 ? 44.514 103.399 69.339 1.00 43.14  ? 107 GLY A O   1 
ATOM   626  N  N   . GLY A 1 130 ? 45.114 105.559 69.108 1.00 48.07  ? 108 GLY A N   1 
ATOM   627  C  CA  . GLY A 1 130 ? 45.760 105.659 70.401 1.00 40.43  ? 108 GLY A CA  1 
ATOM   628  C  C   . GLY A 1 130 ? 47.269 105.552 70.303 1.00 45.92  ? 108 GLY A C   1 
ATOM   629  O  O   . GLY A 1 130 ? 47.864 105.525 69.222 1.00 43.90  ? 108 GLY A O   1 
ATOM   630  N  N   . ASN A 1 131 ? 47.893 105.486 71.475 1.00 42.30  ? 109 ASN A N   1 
ATOM   631  C  CA  . ASN A 1 131 ? 49.338 105.391 71.603 1.00 48.35  ? 109 ASN A CA  1 
ATOM   632  C  C   . ASN A 1 131 ? 49.723 104.009 72.132 1.00 51.81  ? 109 ASN A C   1 
ATOM   633  O  O   . ASN A 1 131 ? 48.882 103.114 72.269 1.00 49.76  ? 109 ASN A O   1 
ATOM   634  C  CB  . ASN A 1 131 ? 49.859 106.515 72.502 1.00 50.46  ? 109 ASN A CB  1 
ATOM   635  C  CG  . ASN A 1 131 ? 50.094 107.807 71.743 1.00 57.56  ? 109 ASN A CG  1 
ATOM   636  O  OD1 . ASN A 1 131 ? 50.373 107.794 70.543 1.00 52.17  ? 109 ASN A OD1 1 
ATOM   637  N  ND2 . ASN A 1 131 ? 49.982 108.932 72.439 1.00 55.25  ? 109 ASN A ND2 1 
ATOM   638  N  N   . ALA A 1 132 ? 51.009 103.839 72.431 1.00 47.96  ? 110 ALA A N   1 
ATOM   639  C  CA  . ALA A 1 132 ? 51.512 102.553 72.890 1.00 49.88  ? 110 ALA A CA  1 
ATOM   640  C  C   . ALA A 1 132 ? 50.923 102.189 74.250 1.00 54.42  ? 110 ALA A C   1 
ATOM   641  O  O   . ALA A 1 132 ? 50.635 103.054 75.081 1.00 53.10  ? 110 ALA A O   1 
ATOM   642  C  CB  . ALA A 1 132 ? 53.038 102.573 72.969 1.00 52.16  ? 110 ALA A CB  1 
ATOM   643  N  N   . ASN A 1 133 ? 50.748 100.884 74.465 1.00 57.30  ? 111 ASN A N   1 
ATOM   644  C  CA  . ASN A 1 133 ? 50.180 100.341 75.701 1.00 59.66  ? 111 ASN A CA  1 
ATOM   645  C  C   . ASN A 1 133 ? 48.782 100.905 75.964 1.00 59.60  ? 111 ASN A C   1 
ATOM   646  O  O   . ASN A 1 133 ? 48.447 101.306 77.080 1.00 58.02  ? 111 ASN A O   1 
ATOM   647  C  CB  . ASN A 1 133 ? 51.110 100.587 76.893 1.00 64.43  ? 111 ASN A CB  1 
ATOM   648  C  CG  . ASN A 1 133 ? 50.736 99.754  78.107 1.00 75.19  ? 111 ASN A CG  1 
ATOM   649  O  OD1 . ASN A 1 133 ? 50.493 100.288 79.190 1.00 76.72  ? 111 ASN A OD1 1 
ATOM   650  N  ND2 . ASN A 1 133 ? 50.677 98.441  77.928 1.00 70.54  ? 111 ASN A ND2 1 
ATOM   651  N  N   . GLY A 1 134 ? 47.965 100.943 74.913 1.00 51.99  ? 112 GLY A N   1 
ATOM   652  C  CA  . GLY A 1 134 ? 46.564 101.295 75.053 1.00 46.76  ? 112 GLY A CA  1 
ATOM   653  C  C   . GLY A 1 134 ? 46.288 102.675 75.599 1.00 56.51  ? 112 GLY A C   1 
ATOM   654  O  O   . GLY A 1 134 ? 45.163 102.944 76.022 1.00 56.83  ? 112 GLY A O   1 
ATOM   655  N  N   . GLN A 1 135 ? 47.279 103.562 75.606 1.00 58.29  ? 113 GLN A N   1 
ATOM   656  C  CA  . GLN A 1 135 ? 47.074 104.915 76.102 1.00 61.03  ? 113 GLN A CA  1 
ATOM   657  C  C   . GLN A 1 135 ? 46.362 105.761 75.057 1.00 52.27  ? 113 GLN A C   1 
ATOM   658  O  O   . GLN A 1 135 ? 46.615 105.633 73.856 1.00 51.81  ? 113 GLN A O   1 
ATOM   659  C  CB  . GLN A 1 135 ? 48.411 105.557 76.469 1.00 58.95  ? 113 GLN A CB  1 
ATOM   660  C  CG  . GLN A 1 135 ? 49.099 104.925 77.667 1.00 59.18  ? 113 GLN A CG  1 
ATOM   661  C  CD  . GLN A 1 135 ? 48.164 104.742 78.845 1.00 64.01  ? 113 GLN A CD  1 
ATOM   662  O  OE1 . GLN A 1 135 ? 47.524 105.691 79.299 1.00 55.88  ? 113 GLN A OE1 1 
ATOM   663  N  NE2 . GLN A 1 135 ? 48.079 103.515 79.345 1.00 68.79  ? 113 GLN A NE2 1 
ATOM   664  N  N   . GLU A 1 136 ? 45.462 106.627 75.519 1.00 58.31  ? 114 GLU A N   1 
ATOM   665  C  CA  . GLU A 1 136 ? 44.819 107.567 74.614 1.00 53.75  ? 114 GLU A CA  1 
ATOM   666  C  C   . GLU A 1 136 ? 45.857 108.522 74.036 1.00 52.85  ? 114 GLU A C   1 
ATOM   667  O  O   . GLU A 1 136 ? 46.888 108.805 74.653 1.00 55.67  ? 114 GLU A O   1 
ATOM   668  C  CB  . GLU A 1 136 ? 43.715 108.342 75.338 1.00 62.17  ? 114 GLU A CB  1 
ATOM   669  C  CG  . GLU A 1 136 ? 44.199 109.215 76.485 1.00 57.94  ? 114 GLU A CG  1 
ATOM   670  C  CD  . GLU A 1 136 ? 43.057 109.864 77.243 1.00 74.38  ? 114 GLU A CD  1 
ATOM   671  O  OE1 . GLU A 1 136 ? 41.936 109.924 76.697 1.00 83.38  ? 114 GLU A OE1 1 
ATOM   672  O  OE2 . GLU A 1 136 ? 43.283 110.317 78.386 1.00 67.38  ? 114 GLU A OE2 1 
ATOM   673  N  N   . SER A 1 137 ? 45.587 109.008 72.829 1.00 56.64  ? 115 SER A N   1 
ATOM   674  C  CA  . SER A 1 137 ? 46.525 109.849 72.105 1.00 55.58  ? 115 SER A CA  1 
ATOM   675  C  C   . SER A 1 137 ? 45.889 111.195 71.783 1.00 54.36  ? 115 SER A C   1 
ATOM   676  O  O   . SER A 1 137 ? 44.664 111.343 71.774 1.00 51.10  ? 115 SER A O   1 
ATOM   677  C  CB  . SER A 1 137 ? 46.996 109.170 70.813 1.00 53.17  ? 115 SER A CB  1 
ATOM   678  O  OG  . SER A 1 137 ? 45.907 108.940 69.935 1.00 48.67  ? 115 SER A OG  1 
ATOM   679  N  N   . THR A 1 138 ? 46.746 112.179 71.515 1.00 54.89  ? 116 THR A N   1 
ATOM   680  C  CA  . THR A 1 138 ? 46.297 113.529 71.198 1.00 59.19  ? 116 THR A CA  1 
ATOM   681  C  C   . THR A 1 138 ? 46.175 113.751 69.694 1.00 53.46  ? 116 THR A C   1 
ATOM   682  O  O   . THR A 1 138 ? 45.173 114.301 69.224 1.00 51.25  ? 116 THR A O   1 
ATOM   683  C  CB  . THR A 1 138 ? 47.256 114.558 71.808 1.00 59.05  ? 116 THR A CB  1 
ATOM   684  O  OG1 . THR A 1 138 ? 47.281 114.403 73.232 1.00 56.73  ? 116 THR A OG1 1 
ATOM   685  C  CG2 . THR A 1 138 ? 46.812 115.972 71.465 1.00 54.95  ? 116 THR A CG2 1 
ATOM   686  N  N   . SER A 1 139 ? 47.179 113.328 68.929 1.00 53.74  ? 117 SER A N   1 
ATOM   687  C  CA  . SER A 1 139 ? 47.165 113.516 67.484 1.00 58.54  ? 117 SER A CA  1 
ATOM   688  C  C   . SER A 1 139 ? 48.043 112.480 66.794 1.00 56.10  ? 117 SER A C   1 
ATOM   689  O  O   . SER A 1 139 ? 48.899 112.829 65.976 1.00 56.49  ? 117 SER A O   1 
ATOM   690  C  CB  . SER A 1 139 ? 47.630 114.930 67.126 1.00 51.85  ? 117 SER A CB  1 
ATOM   691  O  OG  . SER A 1 139 ? 48.818 115.265 67.821 1.00 48.06  ? 117 SER A OG  1 
ATOM   692  N  N   . SER A 1 140 ? 47.835 111.207 67.115 1.00 53.38  ? 118 SER A N   1 
ATOM   693  C  CA  . SER A 1 140 ? 48.631 110.116 66.571 1.00 52.62  ? 118 SER A CA  1 
ATOM   694  C  C   . SER A 1 140 ? 47.871 109.446 65.436 1.00 50.89  ? 118 SER A C   1 
ATOM   695  O  O   . SER A 1 140 ? 46.714 109.049 65.608 1.00 53.81  ? 118 SER A O   1 
ATOM   696  C  CB  . SER A 1 140 ? 48.958 109.092 67.659 1.00 49.04  ? 118 SER A CB  1 
ATOM   697  O  OG  . SER A 1 140 ? 49.872 109.625 68.599 1.00 56.40  ? 118 SER A OG  1 
ATOM   698  N  N   . THR A 1 141 ? 48.523 109.369 64.291 1.00 49.77  ? 119 THR A N   1 
ATOM   699  C  CA  . THR A 1 141 ? 47.959 108.708 63.102 1.00 49.66  ? 119 THR A CA  1 
ATOM   700  C  C   . THR A 1 141 ? 48.849 107.517 62.757 1.00 52.22  ? 119 THR A C   1 
ATOM   701  O  O   . THR A 1 141 ? 49.955 107.731 62.321 1.00 49.79  ? 119 THR A O   1 
ATOM   702  C  CB  . THR A 1 141 ? 47.861 109.670 61.927 1.00 51.71  ? 119 THR A CB  1 
ATOM   703  O  OG1 . THR A 1 141 ? 46.765 110.514 62.224 1.00 49.67  ? 119 THR A OG1 1 
ATOM   704  C  CG2 . THR A 1 141 ? 47.541 108.965 60.631 1.00 52.33  ? 119 THR A CG2 1 
ATOM   705  N  N   . THR A 1 142 ? 48.359 106.307 63.001 1.00 50.89  ? 120 THR A N   1 
ATOM   706  C  CA  . THR A 1 142 ? 49.114 105.061 62.721 1.00 47.74  ? 120 THR A CA  1 
ATOM   707  C  C   . THR A 1 142 ? 48.404 104.314 61.591 1.00 43.22  ? 120 THR A C   1 
ATOM   708  O  O   . THR A 1 142 ? 47.258 103.995 61.754 1.00 40.15  ? 120 THR A O   1 
ATOM   709  C  CB  . THR A 1 142 ? 49.260 104.243 64.001 1.00 48.36  ? 120 THR A CB  1 
ATOM   710  O  OG1 . THR A 1 142 ? 49.596 105.125 65.062 1.00 45.06  ? 120 THR A OG1 1 
ATOM   711  C  CG2 . THR A 1 142 ? 50.299 103.158 63.894 1.00 45.33  ? 120 THR A CG2 1 
ATOM   712  N  N   . ILE A 1 143 ? 49.087 104.112 60.473 1.00 41.24  ? 121 ILE A N   1 
ATOM   713  C  CA  . ILE A 1 143 ? 48.504 103.468 59.302 1.00 42.04  ? 121 ILE A CA  1 
ATOM   714  C  C   . ILE A 1 143 ? 49.172 102.115 59.111 1.00 44.60  ? 121 ILE A C   1 
ATOM   715  O  O   . ILE A 1 143 ? 50.404 102.019 59.122 1.00 35.22  ? 121 ILE A O   1 
ATOM   716  C  CB  . ILE A 1 143 ? 48.664 104.338 58.043 1.00 42.75  ? 121 ILE A CB  1 
ATOM   717  C  CG1 . ILE A 1 143 ? 48.151 105.755 58.303 1.00 46.00  ? 121 ILE A CG1 1 
ATOM   718  C  CG2 . ILE A 1 143 ? 47.933 103.712 56.869 1.00 42.05  ? 121 ILE A CG2 1 
ATOM   719  C  CD1 . ILE A 1 143 ? 48.239 106.662 57.095 1.00 45.59  ? 121 ILE A CD1 1 
ATOM   720  N  N   . PHE A 1 144 ? 48.363 101.075 58.933 1.00 40.93  ? 122 PHE A N   1 
ATOM   721  C  CA  . PHE A 1 144 ? 48.849 99.721  58.692 1.00 39.78  ? 122 PHE A CA  1 
ATOM   722  C  C   . PHE A 1 144 ? 48.569 99.356  57.240 1.00 34.33  ? 122 PHE A C   1 
ATOM   723  O  O   . PHE A 1 144 ? 47.413 99.366  56.806 1.00 34.32  ? 122 PHE A O   1 
ATOM   724  C  CB  . PHE A 1 144 ? 48.190 98.723  59.644 1.00 35.18  ? 122 PHE A CB  1 
ATOM   725  C  CG  . PHE A 1 144 ? 48.614 98.883  61.077 1.00 34.28  ? 122 PHE A CG  1 
ATOM   726  C  CD1 . PHE A 1 144 ? 48.012 99.828  61.892 1.00 38.02  ? 122 PHE A CD1 1 
ATOM   727  C  CD2 . PHE A 1 144 ? 49.618 98.090  61.608 1.00 39.66  ? 122 PHE A CD2 1 
ATOM   728  C  CE1 . PHE A 1 144 ? 48.402 99.978  63.209 1.00 37.83  ? 122 PHE A CE1 1 
ATOM   729  C  CE2 . PHE A 1 144 ? 50.013 98.236  62.925 1.00 36.30  ? 122 PHE A CE2 1 
ATOM   730  C  CZ  . PHE A 1 144 ? 49.403 99.181  63.726 1.00 39.83  ? 122 PHE A CZ  1 
ATOM   731  N  N   . ASN A 1 145 ? 49.623 99.036  56.498 1.00 32.02  ? 123 ASN A N   1 
ATOM   732  C  CA  . ASN A 1 145 ? 49.514 98.778  55.071 1.00 34.46  ? 123 ASN A CA  1 
ATOM   733  C  C   . ASN A 1 145 ? 49.129 97.326  54.802 1.00 31.98  ? 123 ASN A C   1 
ATOM   734  O  O   . ASN A 1 145 ? 49.279 96.447  55.655 1.00 34.79  ? 123 ASN A O   1 
ATOM   735  C  CB  . ASN A 1 145 ? 50.827 99.119  54.366 1.00 33.76  ? 123 ASN A CB  1 
ATOM   736  C  CG  . ASN A 1 145 ? 51.293 100.532 54.663 1.00 43.19  ? 123 ASN A CG  1 
ATOM   737  O  OD1 . ASN A 1 145 ? 50.492 101.466 54.696 1.00 34.03  ? 123 ASN A OD1 1 
ATOM   738  N  ND2 . ASN A 1 145 ? 52.592 100.694 54.885 1.00 30.92  ? 123 ASN A ND2 1 
ATOM   739  N  N   . ASN A 1 146 ? 48.634 97.088  53.587 1.00 36.44  ? 124 ASN A N   1 
ATOM   740  C  CA  . ASN A 1 146 ? 48.097 95.790  53.176 1.00 37.54  ? 124 ASN A CA  1 
ATOM   741  C  C   . ASN A 1 146 ? 47.001 95.328  54.134 1.00 35.74  ? 124 ASN A C   1 
ATOM   742  O  O   . ASN A 1 146 ? 47.036 94.224  54.683 1.00 33.11  ? 124 ASN A O   1 
ATOM   743  C  CB  . ASN A 1 146 ? 49.206 94.742  53.054 1.00 31.55  ? 124 ASN A CB  1 
ATOM   744  C  CG  . ASN A 1 146 ? 48.765 93.520  52.267 1.00 36.55  ? 124 ASN A CG  1 
ATOM   745  O  OD1 . ASN A 1 146 ? 48.980 92.384  52.690 1.00 34.07  ? 124 ASN A OD1 1 
ATOM   746  N  ND2 . ASN A 1 146 ? 48.148 93.750  51.114 1.00 26.36  ? 124 ASN A ND2 1 
ATOM   747  N  N   . GLU A 1 147 ? 46.013 96.202  54.334 1.00 38.71  ? 125 GLU A N   1 
ATOM   748  C  CA  . GLU A 1 147 ? 44.858 95.937  55.175 1.00 31.35  ? 125 GLU A CA  1 
ATOM   749  C  C   . GLU A 1 147 ? 43.618 96.439  54.448 1.00 34.33  ? 125 GLU A C   1 
ATOM   750  O  O   . GLU A 1 147 ? 43.679 97.466  53.756 1.00 41.38  ? 125 GLU A O   1 
ATOM   751  C  CB  . GLU A 1 147 ? 44.977 96.620  56.544 1.00 33.43  ? 125 GLU A CB  1 
ATOM   752  C  CG  . GLU A 1 147 ? 45.883 95.893  57.521 1.00 31.62  ? 125 GLU A CG  1 
ATOM   753  C  CD  . GLU A 1 147 ? 45.126 94.923  58.409 1.00 32.69  ? 125 GLU A CD  1 
ATOM   754  O  OE1 . GLU A 1 147 ? 43.882 94.866  58.305 1.00 30.48  ? 125 GLU A OE1 1 
ATOM   755  O  OE2 . GLU A 1 147 ? 45.775 94.218  59.209 1.00 31.03  ? 125 GLU A OE2 1 
ATOM   756  N  N   . PRO A 1 148 ? 42.484 95.747  54.582 1.00 33.53  ? 126 PRO A N   1 
ATOM   757  C  CA  . PRO A 1 148 ? 41.278 96.118  53.808 1.00 39.82  ? 126 PRO A CA  1 
ATOM   758  C  C   . PRO A 1 148 ? 40.583 97.361  54.352 1.00 31.05  ? 126 PRO A C   1 
ATOM   759  O  O   . PRO A 1 148 ? 39.516 97.312  54.973 1.00 36.12  ? 126 PRO A O   1 
ATOM   760  C  CB  . PRO A 1 148 ? 40.415 94.858  53.928 1.00 29.92  ? 126 PRO A CB  1 
ATOM   761  C  CG  . PRO A 1 148 ? 40.787 94.289  55.257 1.00 33.94  ? 126 PRO A CG  1 
ATOM   762  C  CD  . PRO A 1 148 ? 42.256 94.564  55.431 1.00 34.67  ? 126 PRO A CD  1 
ATOM   763  N  N   . GLY A 1 149 ? 41.194 98.520  54.111 1.00 40.36  ? 127 GLY A N   1 
ATOM   764  C  CA  . GLY A 1 149 ? 40.603 99.772  54.530 1.00 40.07  ? 127 GLY A CA  1 
ATOM   765  C  C   . GLY A 1 149 ? 39.541 100.267 53.566 1.00 38.87  ? 127 GLY A C   1 
ATOM   766  O  O   . GLY A 1 149 ? 39.362 99.745  52.466 1.00 34.10  ? 127 GLY A O   1 
ATOM   767  N  N   . TYR A 1 150 ? 38.821 101.301 54.001 1.00 38.54  ? 128 TYR A N   1 
ATOM   768  C  CA  . TYR A 1 150 ? 37.764 101.882 53.181 1.00 38.99  ? 128 TYR A CA  1 
ATOM   769  C  C   . TYR A 1 150 ? 38.340 102.495 51.912 1.00 38.71  ? 128 TYR A C   1 
ATOM   770  O  O   . TYR A 1 150 ? 39.017 103.527 51.969 1.00 38.24  ? 128 TYR A O   1 
ATOM   771  C  CB  . TYR A 1 150 ? 36.982 102.938 53.964 1.00 38.30  ? 128 TYR A CB  1 
ATOM   772  C  CG  . TYR A 1 150 ? 35.859 103.558 53.163 1.00 43.24  ? 128 TYR A CG  1 
ATOM   773  C  CD1 . TYR A 1 150 ? 34.714 102.832 52.865 1.00 43.05  ? 128 TYR A CD1 1 
ATOM   774  C  CD2 . TYR A 1 150 ? 35.948 104.863 52.694 1.00 41.56  ? 128 TYR A CD2 1 
ATOM   775  C  CE1 . TYR A 1 150 ? 33.685 103.389 52.129 1.00 45.26  ? 128 TYR A CE1 1 
ATOM   776  C  CE2 . TYR A 1 150 ? 34.924 105.429 51.955 1.00 34.07  ? 128 TYR A CE2 1 
ATOM   777  C  CZ  . TYR A 1 150 ? 33.795 104.686 51.677 1.00 44.87  ? 128 TYR A CZ  1 
ATOM   778  O  OH  . TYR A 1 150 ? 32.770 105.238 50.944 1.00 47.94  ? 128 TYR A OH  1 
ATOM   779  N  N   . ARG A 1 151 ? 38.075 101.863 50.768 1.00 39.11  ? 129 ARG A N   1 
ATOM   780  C  CA  . ARG A 1 151 ? 38.583 102.323 49.474 1.00 40.22  ? 129 ARG A CA  1 
ATOM   781  C  C   . ARG A 1 151 ? 40.102 102.475 49.505 1.00 39.05  ? 129 ARG A C   1 
ATOM   782  O  O   . ARG A 1 151 ? 40.674 103.372 48.883 1.00 36.01  ? 129 ARG A O   1 
ATOM   783  C  CB  . ARG A 1 151 ? 37.908 103.628 49.051 1.00 40.43  ? 129 ARG A CB  1 
ATOM   784  C  CG  . ARG A 1 151 ? 36.444 103.471 48.673 1.00 44.31  ? 129 ARG A CG  1 
ATOM   785  C  CD  . ARG A 1 151 ? 35.801 104.814 48.368 1.00 48.60  ? 129 ARG A CD  1 
ATOM   786  N  NE  . ARG A 1 151 ? 34.459 104.663 47.814 1.00 49.66  ? 129 ARG A NE  1 
ATOM   787  C  CZ  . ARG A 1 151 ? 33.605 105.667 47.635 1.00 51.31  ? 129 ARG A CZ  1 
ATOM   788  N  NH1 . ARG A 1 151 ? 33.952 106.903 47.968 1.00 50.31  ? 129 ARG A NH1 1 
ATOM   789  N  NH2 . ARG A 1 151 ? 32.405 105.435 47.123 1.00 50.03  ? 129 ARG A NH2 1 
ATOM   790  N  N   . SER A 1 152 ? 40.763 101.583 50.239 1.00 37.02  ? 130 SER A N   1 
ATOM   791  C  CA  . SER A 1 152 ? 42.198 101.688 50.449 1.00 35.36  ? 130 SER A CA  1 
ATOM   792  C  C   . SER A 1 152 ? 42.764 100.311 50.754 1.00 41.66  ? 130 SER A C   1 
ATOM   793  O  O   . SER A 1 152 ? 42.063 99.438  51.274 1.00 41.78  ? 130 SER A O   1 
ATOM   794  C  CB  . SER A 1 152 ? 42.520 102.661 51.590 1.00 38.53  ? 130 SER A CB  1 
ATOM   795  O  OG  . SER A 1 152 ? 43.835 102.460 52.078 1.00 38.14  ? 130 SER A OG  1 
ATOM   796  N  N   . THR A 1 153 ? 44.040 100.127 50.414 1.00 39.52  ? 131 THR A N   1 
ATOM   797  C  CA  . THR A 1 153 ? 44.797 98.955  50.828 1.00 43.01  ? 131 THR A CA  1 
ATOM   798  C  C   . THR A 1 153 ? 45.500 99.171  52.161 1.00 36.75  ? 131 THR A C   1 
ATOM   799  O  O   . THR A 1 153 ? 46.465 98.463  52.470 1.00 34.29  ? 131 THR A O   1 
ATOM   800  C  CB  . THR A 1 153 ? 45.816 98.567  49.753 1.00 39.81  ? 131 THR A CB  1 
ATOM   801  O  OG1 . THR A 1 153 ? 46.785 99.613  49.607 1.00 37.31  ? 131 THR A OG1 1 
ATOM   802  C  CG2 . THR A 1 153 ? 45.123 98.328  48.421 1.00 37.21  ? 131 THR A CG2 1 
ATOM   803  N  N   . SER A 1 154 ? 45.039 100.138 52.951 1.00 40.26  ? 132 SER A N   1 
ATOM   804  C  CA  . SER A 1 154 ? 45.582 100.404 54.272 1.00 36.59  ? 132 SER A CA  1 
ATOM   805  C  C   . SER A 1 154 ? 44.439 100.742 55.216 1.00 35.42  ? 132 SER A C   1 
ATOM   806  O  O   . SER A 1 154 ? 43.425 101.313 54.807 1.00 39.98  ? 132 SER A O   1 
ATOM   807  C  CB  . SER A 1 154 ? 46.595 101.559 54.252 1.00 35.14  ? 132 SER A CB  1 
ATOM   808  O  OG  . SER A 1 154 ? 47.805 101.175 53.624 1.00 46.27  ? 132 SER A OG  1 
ATOM   809  N  N   . ILE A 1 155 ? 44.608 100.373 56.482 1.00 35.87  ? 133 ILE A N   1 
ATOM   810  C  CA  . ILE A 1 155 ? 43.703 100.776 57.551 1.00 38.90  ? 133 ILE A CA  1 
ATOM   811  C  C   . ILE A 1 155 ? 44.410 101.838 58.379 1.00 41.54  ? 133 ILE A C   1 
ATOM   812  O  O   . ILE A 1 155 ? 45.531 101.619 58.856 1.00 38.96  ? 133 ILE A O   1 
ATOM   813  C  CB  . ILE A 1 155 ? 43.280 99.583  58.426 1.00 35.16  ? 133 ILE A CB  1 
ATOM   814  C  CG1 . ILE A 1 155 ? 42.203 98.757  57.718 1.00 36.69  ? 133 ILE A CG1 1 
ATOM   815  C  CG2 . ILE A 1 155 ? 42.765 100.070 59.772 1.00 31.09  ? 133 ILE A CG2 1 
ATOM   816  C  CD1 . ILE A 1 155 ? 41.625 97.647  58.573 1.00 35.81  ? 133 ILE A CD1 1 
ATOM   817  N  N   . THR A 1 156 ? 43.764 102.987 58.539 1.00 45.06  ? 134 THR A N   1 
ATOM   818  C  CA  . THR A 1 156 ? 44.343 104.114 59.256 1.00 38.87  ? 134 THR A CA  1 
ATOM   819  C  C   . THR A 1 156 ? 43.756 104.187 60.659 1.00 32.32  ? 134 THR A C   1 
ATOM   820  O  O   . THR A 1 156 ? 42.533 104.180 60.829 1.00 40.12  ? 134 THR A O   1 
ATOM   821  C  CB  . THR A 1 156 ? 44.090 105.423 58.508 1.00 41.04  ? 134 THR A CB  1 
ATOM   822  O  OG1 . THR A 1 156 ? 44.723 105.367 57.223 1.00 43.63  ? 134 THR A OG1 1 
ATOM   823  C  CG2 . THR A 1 156 ? 44.652 106.602 59.292 1.00 46.59  ? 134 THR A CG2 1 
ATOM   824  N  N   . CYS A 1 157 ? 44.631 104.253 61.656 1.00 39.74  ? 135 CYS A N   1 
ATOM   825  C  CA  . CYS A 1 157 ? 44.237 104.339 63.058 1.00 37.52  ? 135 CYS A CA  1 
ATOM   826  C  C   . CYS A 1 157 ? 44.546 105.753 63.537 1.00 43.34  ? 135 CYS A C   1 
ATOM   827  O  O   . CYS A 1 157 ? 45.699 106.085 63.825 1.00 46.45  ? 135 CYS A O   1 
ATOM   828  C  CB  . CYS A 1 157 ? 44.955 103.278 63.880 1.00 31.69  ? 135 CYS A CB  1 
ATOM   829  S  SG  . CYS A 1 157 ? 44.537 101.604 63.350 1.00 37.09  ? 135 CYS A SG  1 
ATOM   830  N  N   . SER A 1 158 ? 43.505 106.586 63.619 1.00 49.05  ? 136 SER A N   1 
ATOM   831  C  CA  . SER A 1 158 ? 43.691 107.999 63.921 1.00 51.98  ? 136 SER A CA  1 
ATOM   832  C  C   . SER A 1 158 ? 42.565 108.552 64.787 1.00 55.45  ? 136 SER A C   1 
ATOM   833  O  O   . SER A 1 158 ? 42.205 109.728 64.659 1.00 58.88  ? 136 SER A O   1 
ATOM   834  C  CB  . SER A 1 158 ? 43.806 108.820 62.635 1.00 52.24  ? 136 SER A CB  1 
ATOM   835  O  OG  . SER A 1 158 ? 42.562 108.877 61.957 1.00 59.54  ? 136 SER A OG  1 
ATOM   836  N  N   . LEU A 1 159 ? 41.993 107.734 65.666 1.00 46.69  ? 137 LEU A N   1 
ATOM   837  C  CA  . LEU A 1 159 ? 41.007 108.220 66.622 1.00 51.71  ? 137 LEU A CA  1 
ATOM   838  C  C   . LEU A 1 159 ? 41.730 108.675 67.883 1.00 51.76  ? 137 LEU A C   1 
ATOM   839  O  O   . LEU A 1 159 ? 42.366 107.866 68.567 1.00 48.40  ? 137 LEU A O   1 
ATOM   840  C  CB  . LEU A 1 159 ? 39.966 107.154 66.958 1.00 50.76  ? 137 LEU A CB  1 
ATOM   841  C  CG  . LEU A 1 159 ? 38.853 107.701 67.858 1.00 54.00  ? 137 LEU A CG  1 
ATOM   842  C  CD1 . LEU A 1 159 ? 37.680 108.202 67.029 1.00 59.33  ? 137 LEU A CD1 1 
ATOM   843  C  CD2 . LEU A 1 159 ? 38.390 106.671 68.869 1.00 60.42  ? 137 LEU A CD2 1 
ATOM   844  N  N   . ASN A 1 160 ? 41.635 109.965 68.183 1.00 54.63  ? 138 ASN A N   1 
ATOM   845  C  CA  . ASN A 1 160 ? 42.303 110.565 69.327 1.00 56.77  ? 138 ASN A CA  1 
ATOM   846  C  C   . ASN A 1 160 ? 41.282 110.975 70.380 1.00 54.81  ? 138 ASN A C   1 
ATOM   847  O  O   . ASN A 1 160 ? 40.071 110.971 70.146 1.00 54.34  ? 138 ASN A O   1 
ATOM   848  C  CB  . ASN A 1 160 ? 43.137 111.776 68.891 1.00 53.91  ? 138 ASN A CB  1 
ATOM   849  C  CG  . ASN A 1 160 ? 44.274 111.397 67.965 1.00 52.27  ? 138 ASN A CG  1 
ATOM   850  O  OD1 . ASN A 1 160 ? 45.248 110.771 68.382 1.00 55.43  ? 138 ASN A OD1 1 
ATOM   851  N  ND2 . ASN A 1 160 ? 44.156 111.776 66.700 1.00 51.67  ? 138 ASN A ND2 1 
ATOM   852  N  N   . ARG A 1 161 ? 41.800 111.327 71.559 1.00 59.14  ? 139 ARG A N   1 
ATOM   853  C  CA  . ARG A 1 161 ? 41.011 111.809 72.692 1.00 66.70  ? 139 ARG A CA  1 
ATOM   854  C  C   . ARG A 1 161 ? 40.014 110.772 73.202 1.00 64.41  ? 139 ARG A C   1 
ATOM   855  O  O   . ARG A 1 161 ? 39.035 111.123 73.868 1.00 66.31  ? 139 ARG A O   1 
ATOM   856  C  CB  . ARG A 1 161 ? 40.283 113.114 72.349 1.00 68.58  ? 139 ARG A CB  1 
ATOM   857  C  CG  . ARG A 1 161 ? 41.174 114.188 71.743 1.00 60.99  ? 139 ARG A CG  1 
ATOM   858  C  CD  . ARG A 1 161 ? 40.516 115.562 71.789 1.00 79.50  ? 139 ARG A CD  1 
ATOM   859  N  NE  . ARG A 1 161 ? 39.091 115.517 71.465 1.00 83.15  ? 139 ARG A NE  1 
ATOM   860  C  CZ  . ARG A 1 161 ? 38.115 115.610 72.363 1.00 83.00  ? 139 ARG A CZ  1 
ATOM   861  N  NH1 . ARG A 1 161 ? 38.406 115.749 73.649 1.00 76.60  ? 139 ARG A NH1 1 
ATOM   862  N  NH2 . ARG A 1 161 ? 36.848 115.558 71.976 1.00 80.07  ? 139 ARG A NH2 1 
ATOM   863  N  N   . TYR A 1 162 ? 40.244 109.495 72.905 1.00 64.11  ? 140 TYR A N   1 
ATOM   864  C  CA  . TYR A 1 162 ? 39.428 108.408 73.431 1.00 60.62  ? 140 TYR A CA  1 
ATOM   865  C  C   . TYR A 1 162 ? 40.347 107.261 73.815 1.00 56.30  ? 140 TYR A C   1 
ATOM   866  O  O   . TYR A 1 162 ? 41.194 106.850 73.016 1.00 59.48  ? 140 TYR A O   1 
ATOM   867  C  CB  . TYR A 1 162 ? 38.387 107.933 72.408 1.00 60.82  ? 140 TYR A CB  1 
ATOM   868  C  CG  . TYR A 1 162 ? 37.261 108.911 72.155 1.00 68.62  ? 140 TYR A CG  1 
ATOM   869  C  CD1 . TYR A 1 162 ? 36.145 108.948 72.981 1.00 75.52  ? 140 TYR A CD1 1 
ATOM   870  C  CD2 . TYR A 1 162 ? 37.309 109.790 71.081 1.00 70.11  ? 140 TYR A CD2 1 
ATOM   871  C  CE1 . TYR A 1 162 ? 35.112 109.839 72.748 1.00 74.99  ? 140 TYR A CE1 1 
ATOM   872  C  CE2 . TYR A 1 162 ? 36.282 110.683 70.840 1.00 66.81  ? 140 TYR A CE2 1 
ATOM   873  C  CZ  . TYR A 1 162 ? 35.186 110.703 71.676 1.00 77.89  ? 140 TYR A CZ  1 
ATOM   874  O  OH  . TYR A 1 162 ? 34.163 111.592 71.438 1.00 86.82  ? 140 TYR A OH  1 
ATOM   875  N  N   . LYS A 1 163 ? 40.182 106.750 75.029 1.00 52.65  ? 141 LYS A N   1 
ATOM   876  C  CA  . LYS A 1 163 ? 41.033 105.661 75.494 1.00 52.68  ? 141 LYS A CA  1 
ATOM   877  C  C   . LYS A 1 163 ? 40.605 104.350 74.842 1.00 53.55  ? 141 LYS A C   1 
ATOM   878  O  O   . LYS A 1 163 ? 39.417 104.014 74.863 1.00 49.74  ? 141 LYS A O   1 
ATOM   879  C  CB  . LYS A 1 163 ? 40.970 105.533 77.012 1.00 56.02  ? 141 LYS A CB  1 
ATOM   880  C  CG  . LYS A 1 163 ? 41.761 104.356 77.563 1.00 54.96  ? 141 LYS A CG  1 
ATOM   881  C  CD  . LYS A 1 163 ? 42.637 104.773 78.733 1.00 67.07  ? 141 LYS A CD  1 
ATOM   882  C  CE  . LYS A 1 163 ? 42.894 103.606 79.672 1.00 65.22  ? 141 LYS A CE  1 
ATOM   883  N  NZ  . LYS A 1 163 ? 41.627 103.041 80.214 1.00 66.42  ? 141 LYS A NZ  1 
ATOM   884  N  N   . PRO A 1 164 ? 41.532 103.599 74.248 1.00 43.32  ? 142 PRO A N   1 
ATOM   885  C  CA  . PRO A 1 164 ? 41.163 102.317 73.636 1.00 46.96  ? 142 PRO A CA  1 
ATOM   886  C  C   . PRO A 1 164 ? 40.626 101.330 74.662 1.00 44.24  ? 142 PRO A C   1 
ATOM   887  O  O   . PRO A 1 164 ? 41.034 101.321 75.825 1.00 50.59  ? 142 PRO A O   1 
ATOM   888  C  CB  . PRO A 1 164 ? 42.480 101.824 73.025 1.00 46.62  ? 142 PRO A CB  1 
ATOM   889  C  CG  . PRO A 1 164 ? 43.289 103.062 72.820 1.00 47.93  ? 142 PRO A CG  1 
ATOM   890  C  CD  . PRO A 1 164 ? 42.926 103.973 73.956 1.00 50.91  ? 142 PRO A CD  1 
ATOM   891  N  N   . GLY A 1 165 ? 39.701 100.492 74.214 1.00 41.99  ? 143 GLY A N   1 
ATOM   892  C  CA  . GLY A 1 165 ? 39.140 99.472  75.072 1.00 37.94  ? 143 GLY A CA  1 
ATOM   893  C  C   . GLY A 1 165 ? 37.849 98.923  74.496 1.00 38.56  ? 143 GLY A C   1 
ATOM   894  O  O   . GLY A 1 165 ? 37.474 99.217  73.362 1.00 38.39  ? 143 GLY A O   1 
ATOM   895  N  N   . TYR A 1 166 ? 37.187 98.108  75.318 1.00 38.01  ? 144 TYR A N   1 
ATOM   896  C  CA  . TYR A 1 166 ? 35.906 97.509  74.960 1.00 37.88  ? 144 TYR A CA  1 
ATOM   897  C  C   . TYR A 1 166 ? 34.909 98.577  74.529 1.00 43.76  ? 144 TYR A C   1 
ATOM   898  O  O   . TYR A 1 166 ? 34.748 99.601  75.199 1.00 40.85  ? 144 TYR A O   1 
ATOM   899  C  CB  . TYR A 1 166 ? 35.363 96.723  76.158 1.00 36.49  ? 144 TYR A CB  1 
ATOM   900  C  CG  . TYR A 1 166 ? 34.135 95.881  75.884 1.00 41.82  ? 144 TYR A CG  1 
ATOM   901  C  CD1 . TYR A 1 166 ? 32.864 96.444  75.887 1.00 37.30  ? 144 TYR A CD1 1 
ATOM   902  C  CD2 . TYR A 1 166 ? 34.245 94.517  75.648 1.00 36.99  ? 144 TYR A CD2 1 
ATOM   903  C  CE1 . TYR A 1 166 ? 31.740 95.674  75.648 1.00 41.26  ? 144 TYR A CE1 1 
ATOM   904  C  CE2 . TYR A 1 166 ? 33.127 93.739  75.410 1.00 36.02  ? 144 TYR A CE2 1 
ATOM   905  C  CZ  . TYR A 1 166 ? 31.878 94.322  75.411 1.00 42.37  ? 144 TYR A CZ  1 
ATOM   906  O  OH  . TYR A 1 166 ? 30.763 93.550  75.173 1.00 38.50  ? 144 TYR A OH  1 
ATOM   907  N  N   . TYR A 1 167 ? 34.248 98.331  73.396 1.00 38.09  ? 145 TYR A N   1 
ATOM   908  C  CA  . TYR A 1 167 ? 33.268 99.242  72.806 1.00 39.57  ? 145 TYR A CA  1 
ATOM   909  C  C   . TYR A 1 167 ? 33.866 100.609 72.479 1.00 39.88  ? 145 TYR A C   1 
ATOM   910  O  O   . TYR A 1 167 ? 33.131 101.579 72.272 1.00 39.42  ? 145 TYR A O   1 
ATOM   911  C  CB  . TYR A 1 167 ? 32.039 99.402  73.709 1.00 38.49  ? 145 TYR A CB  1 
ATOM   912  C  CG  . TYR A 1 167 ? 30.720 99.349  72.969 1.00 38.91  ? 145 TYR A CG  1 
ATOM   913  C  CD1 . TYR A 1 167 ? 30.530 100.068 71.796 1.00 40.40  ? 145 TYR A CD1 1 
ATOM   914  C  CD2 . TYR A 1 167 ? 29.664 98.582  73.444 1.00 35.85  ? 145 TYR A CD2 1 
ATOM   915  C  CE1 . TYR A 1 167 ? 29.328 100.027 71.117 1.00 41.99  ? 145 TYR A CE1 1 
ATOM   916  C  CE2 . TYR A 1 167 ? 28.457 98.533  72.771 1.00 40.84  ? 145 TYR A CE2 1 
ATOM   917  C  CZ  . TYR A 1 167 ? 28.295 99.258  71.608 1.00 47.11  ? 145 TYR A CZ  1 
ATOM   918  O  OH  . TYR A 1 167 ? 27.097 99.215  70.933 1.00 53.24  ? 145 TYR A OH  1 
ATOM   919  N  N   . GLY A 1 168 ? 35.191 100.705 72.432 1.00 41.51  ? 146 GLY A N   1 
ATOM   920  C  CA  . GLY A 1 168 ? 35.857 101.915 72.016 1.00 39.83  ? 146 GLY A CA  1 
ATOM   921  C  C   . GLY A 1 168 ? 36.769 101.640 70.841 1.00 47.26  ? 146 GLY A C   1 
ATOM   922  O  O   . GLY A 1 168 ? 36.528 100.728 70.045 1.00 40.84  ? 146 GLY A O   1 
ATOM   923  N  N   . PRO A 1 169 ? 37.833 102.423 70.702 1.00 47.74  ? 147 PRO A N   1 
ATOM   924  C  CA  . PRO A 1 169 ? 38.822 102.125 69.663 1.00 45.46  ? 147 PRO A CA  1 
ATOM   925  C  C   . PRO A 1 169 ? 39.680 100.932 70.049 1.00 45.04  ? 147 PRO A C   1 
ATOM   926  O  O   . PRO A 1 169 ? 39.960 100.690 71.225 1.00 38.94  ? 147 PRO A O   1 
ATOM   927  C  CB  . PRO A 1 169 ? 39.658 103.407 69.590 1.00 47.39  ? 147 PRO A CB  1 
ATOM   928  C  CG  . PRO A 1 169 ? 39.524 104.012 70.948 1.00 52.53  ? 147 PRO A CG  1 
ATOM   929  C  CD  . PRO A 1 169 ? 38.139 103.670 71.424 1.00 54.96  ? 147 PRO A CD  1 
ATOM   930  N  N   . MET A 1 170 ? 40.090 100.172 69.039 1.00 37.36  ? 148 MET A N   1 
ATOM   931  C  CA  . MET A 1 170 ? 41.056 99.109  69.270 1.00 37.43  ? 148 MET A CA  1 
ATOM   932  C  C   . MET A 1 170 ? 42.437 99.717  69.471 1.00 32.43  ? 148 MET A C   1 
ATOM   933  O  O   . MET A 1 170 ? 42.847 100.609 68.722 1.00 36.58  ? 148 MET A O   1 
ATOM   934  C  CB  . MET A 1 170 ? 41.074 98.124  68.102 1.00 29.37  ? 148 MET A CB  1 
ATOM   935  C  CG  . MET A 1 170 ? 42.022 96.950  68.312 1.00 39.59  ? 148 MET A CG  1 
ATOM   936  S  SD  . MET A 1 170 ? 42.226 95.897  66.861 1.00 38.09  ? 148 MET A SD  1 
ATOM   937  C  CE  . MET A 1 170 ? 40.528 95.462  66.505 1.00 37.35  ? 148 MET A CE  1 
ATOM   938  N  N   . SER A 1 171 ? 43.147 99.244  70.490 1.00 35.14  ? 149 SER A N   1 
ATOM   939  C  CA  . SER A 1 171 ? 44.484 99.749  70.757 1.00 41.88  ? 149 SER A CA  1 
ATOM   940  C  C   . SER A 1 171 ? 45.430 99.382  69.617 1.00 44.82  ? 149 SER A C   1 
ATOM   941  O  O   . SER A 1 171 ? 45.212 98.421  68.872 1.00 37.57  ? 149 SER A O   1 
ATOM   942  C  CB  . SER A 1 171 ? 45.016 99.193  72.078 1.00 36.28  ? 149 SER A CB  1 
ATOM   943  O  OG  . SER A 1 171 ? 45.016 97.776  72.069 1.00 43.77  ? 149 SER A OG  1 
ATOM   944  N  N   . ILE A 1 172 ? 46.494 100.177 69.481 1.00 37.56  ? 150 ILE A N   1 
ATOM   945  C  CA  . ILE A 1 172 ? 47.518 99.878  68.485 1.00 38.06  ? 150 ILE A CA  1 
ATOM   946  C  C   . ILE A 1 172 ? 48.209 98.564  68.814 1.00 41.69  ? 150 ILE A C   1 
ATOM   947  O  O   . ILE A 1 172 ? 48.615 97.821  67.911 1.00 40.76  ? 150 ILE A O   1 
ATOM   948  C  CB  . ILE A 1 172 ? 48.522 101.044 68.387 1.00 37.05  ? 150 ILE A CB  1 
ATOM   949  C  CG1 . ILE A 1 172 ? 47.806 102.322 67.952 1.00 35.06  ? 150 ILE A CG1 1 
ATOM   950  C  CG2 . ILE A 1 172 ? 49.645 100.715 67.413 1.00 33.87  ? 150 ILE A CG2 1 
ATOM   951  C  CD1 . ILE A 1 172 ? 47.053 102.181 66.648 1.00 36.04  ? 150 ILE A CD1 1 
ATOM   952  N  N   . GLU A 1 173 ? 48.340 98.245  70.104 1.00 36.07  ? 151 GLU A N   1 
ATOM   953  C  CA  . GLU A 1 173 ? 48.935 96.971  70.491 1.00 39.33  ? 151 GLU A CA  1 
ATOM   954  C  C   . GLU A 1 173 ? 48.094 95.799  70.002 1.00 38.54  ? 151 GLU A C   1 
ATOM   955  O  O   . GLU A 1 173 ? 48.631 94.808  69.493 1.00 45.09  ? 151 GLU A O   1 
ATOM   956  C  CB  . GLU A 1 173 ? 49.105 96.905  72.007 1.00 42.55  ? 151 GLU A CB  1 
ATOM   957  C  CG  . GLU A 1 173 ? 49.638 95.572  72.492 1.00 46.74  ? 151 GLU A CG  1 
ATOM   958  C  CD  . GLU A 1 173 ? 49.582 95.433  73.995 1.00 60.23  ? 151 GLU A CD  1 
ATOM   959  O  OE1 . GLU A 1 173 ? 48.501 95.093  74.520 1.00 59.63  ? 151 GLU A OE1 1 
ATOM   960  O  OE2 . GLU A 1 173 ? 50.621 95.663  74.648 1.00 71.36  ? 151 GLU A OE2 1 
ATOM   961  N  N   . ASN A 1 174 ? 46.771 95.893  70.152 1.00 39.69  ? 152 ASN A N   1 
ATOM   962  C  CA  . ASN A 1 174 ? 45.903 94.823  69.672 1.00 40.13  ? 152 ASN A CA  1 
ATOM   963  C  C   . ASN A 1 174 ? 45.871 94.779  68.150 1.00 35.76  ? 152 ASN A C   1 
ATOM   964  O  O   . ASN A 1 174 ? 45.814 93.695  67.558 1.00 36.91  ? 152 ASN A O   1 
ATOM   965  C  CB  . ASN A 1 174 ? 44.494 94.993  70.237 1.00 41.32  ? 152 ASN A CB  1 
ATOM   966  C  CG  . ASN A 1 174 ? 44.327 94.332  71.590 1.00 44.56  ? 152 ASN A CG  1 
ATOM   967  O  OD1 . ASN A 1 174 ? 45.005 93.352  71.902 1.00 43.60  ? 152 ASN A OD1 1 
ATOM   968  N  ND2 . ASN A 1 174 ? 43.422 94.865  72.402 1.00 35.02  ? 152 ASN A ND2 1 
ATOM   969  N  N   . PHE A 1 175 ? 45.910 95.944  67.498 1.00 36.03  ? 153 PHE A N   1 
ATOM   970  C  CA  . PHE A 1 175 ? 45.915 95.951  66.039 1.00 35.82  ? 153 PHE A CA  1 
ATOM   971  C  C   . PHE A 1 175 ? 47.201 95.347  65.491 1.00 35.96  ? 153 PHE A C   1 
ATOM   972  O  O   . PHE A 1 175 ? 47.172 94.627  64.487 1.00 36.12  ? 153 PHE A O   1 
ATOM   973  C  CB  . PHE A 1 175 ? 45.717 97.367  65.502 1.00 31.96  ? 153 PHE A CB  1 
ATOM   974  C  CG  . PHE A 1 175 ? 45.222 97.403  64.084 1.00 30.43  ? 153 PHE A CG  1 
ATOM   975  C  CD1 . PHE A 1 175 ? 46.100 97.235  63.026 1.00 31.30  ? 153 PHE A CD1 1 
ATOM   976  C  CD2 . PHE A 1 175 ? 43.876 97.578  63.810 1.00 33.21  ? 153 PHE A CD2 1 
ATOM   977  C  CE1 . PHE A 1 175 ? 45.648 97.254  61.721 1.00 30.66  ? 153 PHE A CE1 1 
ATOM   978  C  CE2 . PHE A 1 175 ? 43.418 97.599  62.506 1.00 35.93  ? 153 PHE A CE2 1 
ATOM   979  C  CZ  . PHE A 1 175 ? 44.307 97.436  61.461 1.00 27.67  ? 153 PHE A CZ  1 
ATOM   980  N  N   . LYS A 1 176 ? 48.337 95.626  66.135 1.00 31.25  ? 154 LYS A N   1 
ATOM   981  C  CA  . LYS A 1 176 ? 49.593 95.014  65.715 1.00 34.00  ? 154 LYS A CA  1 
ATOM   982  C  C   . LYS A 1 176 ? 49.526 93.497  65.843 1.00 36.04  ? 154 LYS A C   1 
ATOM   983  O  O   . LYS A 1 176 ? 49.938 92.765  64.935 1.00 34.01  ? 154 LYS A O   1 
ATOM   984  C  CB  . LYS A 1 176 ? 50.753 95.576  66.538 1.00 37.34  ? 154 LYS A CB  1 
ATOM   985  C  CG  . LYS A 1 176 ? 51.194 96.971  66.123 1.00 30.37  ? 154 LYS A CG  1 
ATOM   986  C  CD  . LYS A 1 176 ? 52.322 97.477  67.010 1.00 49.60  ? 154 LYS A CD  1 
ATOM   987  C  CE  . LYS A 1 176 ? 52.902 98.781  66.483 1.00 45.77  ? 154 LYS A CE  1 
ATOM   988  N  NZ  . LYS A 1 176 ? 54.046 99.257  67.310 1.00 36.12  ? 154 LYS A NZ  1 
ATOM   989  N  N   . LYS A 1 177 ? 49.005 93.008  66.971 1.00 31.68  ? 155 LYS A N   1 
ATOM   990  C  CA  . LYS A 1 177 ? 48.788 91.574  67.132 1.00 32.40  ? 155 LYS A CA  1 
ATOM   991  C  C   . LYS A 1 177 ? 47.841 91.041  66.064 1.00 35.88  ? 155 LYS A C   1 
ATOM   992  O  O   . LYS A 1 177 ? 48.092 89.987  65.467 1.00 36.09  ? 155 LYS A O   1 
ATOM   993  C  CB  . LYS A 1 177 ? 48.240 91.288  68.530 1.00 30.24  ? 155 LYS A CB  1 
ATOM   994  C  CG  . LYS A 1 177 ? 48.218 89.821  68.919 1.00 37.09  ? 155 LYS A CG  1 
ATOM   995  C  CD  . LYS A 1 177 ? 47.964 89.659  70.410 1.00 41.64  ? 155 LYS A CD  1 
ATOM   996  C  CE  . LYS A 1 177 ? 46.578 89.097  70.680 1.00 52.32  ? 155 LYS A CE  1 
ATOM   997  N  NZ  . LYS A 1 177 ? 45.994 89.618  71.948 1.00 54.49  ? 155 LYS A NZ  1 
ATOM   998  N  N   . LEU A 1 178 ? 46.746 91.761  65.810 1.00 28.93  ? 156 LEU A N   1 
ATOM   999  C  CA  . LEU A 1 178 ? 45.817 91.369  64.756 1.00 33.31  ? 156 LEU A CA  1 
ATOM   1000 C  C   . LEU A 1 178 ? 46.491 91.409  63.391 1.00 35.15  ? 156 LEU A C   1 
ATOM   1001 O  O   . LEU A 1 178 ? 46.385 90.461  62.603 1.00 30.55  ? 156 LEU A O   1 
ATOM   1002 C  CB  . LEU A 1 178 ? 44.593 92.289  64.781 1.00 30.11  ? 156 LEU A CB  1 
ATOM   1003 C  CG  . LEU A 1 178 ? 43.349 91.926  63.964 1.00 33.28  ? 156 LEU A CG  1 
ATOM   1004 C  CD1 . LEU A 1 178 ? 42.117 92.564  64.581 1.00 30.74  ? 156 LEU A CD1 1 
ATOM   1005 C  CD2 . LEU A 1 178 ? 43.481 92.342  62.503 1.00 34.69  ? 156 LEU A CD2 1 
ATOM   1006 N  N   . ASN A 1 179 ? 47.192 92.507  63.095 1.00 30.45  ? 157 ASN A N   1 
ATOM   1007 C  CA  . ASN A 1 179 ? 47.769 92.691  61.767 1.00 30.66  ? 157 ASN A CA  1 
ATOM   1008 C  C   . ASN A 1 179 ? 48.808 91.623  61.455 1.00 32.10  ? 157 ASN A C   1 
ATOM   1009 O  O   . ASN A 1 179 ? 48.856 91.106  60.333 1.00 34.13  ? 157 ASN A O   1 
ATOM   1010 C  CB  . ASN A 1 179 ? 48.385 94.087  61.652 1.00 31.06  ? 157 ASN A CB  1 
ATOM   1011 C  CG  . ASN A 1 179 ? 49.021 94.333  60.299 1.00 29.89  ? 157 ASN A CG  1 
ATOM   1012 O  OD1 . ASN A 1 179 ? 50.241 94.441  60.183 1.00 36.65  ? 157 ASN A OD1 1 
ATOM   1013 N  ND2 . ASN A 1 179 ? 48.194 94.419  59.267 1.00 27.04  ? 157 ASN A ND2 1 
ATOM   1014 N  N   . GLU A 1 180 ? 49.646 91.273  62.434 1.00 28.56  ? 158 GLU A N   1 
ATOM   1015 C  CA  . GLU A 1 180 ? 50.696 90.290  62.187 1.00 31.69  ? 158 GLU A CA  1 
ATOM   1016 C  C   . GLU A 1 180 ? 50.107 88.941  61.794 1.00 31.06  ? 158 GLU A C   1 
ATOM   1017 O  O   . GLU A 1 180 ? 50.578 88.297  60.850 1.00 29.81  ? 158 GLU A O   1 
ATOM   1018 C  CB  . GLU A 1 180 ? 51.590 90.148  63.418 1.00 29.39  ? 158 GLU A CB  1 
ATOM   1019 C  CG  . GLU A 1 180 ? 52.767 89.212  63.197 1.00 33.73  ? 158 GLU A CG  1 
ATOM   1020 C  CD  . GLU A 1 180 ? 53.685 89.125  64.398 1.00 46.54  ? 158 GLU A CD  1 
ATOM   1021 O  OE1 . GLU A 1 180 ? 53.411 89.804  65.410 1.00 53.97  ? 158 GLU A OE1 1 
ATOM   1022 O  OE2 . GLU A 1 180 ? 54.681 88.375  64.330 1.00 47.88  ? 158 GLU A OE2 1 
ATOM   1023 N  N   . ALA A 1 181 ? 49.073 88.495  62.511 1.00 24.92  ? 159 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 181 ? 48.413 87.247  62.144 1.00 32.43  ? 159 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 181 ? 47.727 87.367  60.788 1.00 24.81  ? 159 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 181 ? 47.729 86.416  59.998 1.00 26.86  ? 159 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 181 ? 47.409 86.845  63.223 1.00 28.80  ? 159 ALA A CB  1 
ATOM   1028 N  N   . TYR A 1 182 ? 47.144 88.532  60.499 1.00 25.51  ? 160 TYR A N   1 
ATOM   1029 C  CA  . TYR A 1 182 ? 46.494 88.737  59.209 1.00 26.55  ? 160 TYR A CA  1 
ATOM   1030 C  C   . TYR A 1 182 ? 47.493 88.643  58.062 1.00 29.81  ? 160 TYR A C   1 
ATOM   1031 O  O   . TYR A 1 182 ? 47.216 88.002  57.042 1.00 26.18  ? 160 TYR A O   1 
ATOM   1032 C  CB  . TYR A 1 182 ? 45.783 90.091  59.195 1.00 26.38  ? 160 TYR A CB  1 
ATOM   1033 C  CG  . TYR A 1 182 ? 45.067 90.403  57.899 1.00 25.91  ? 160 TYR A CG  1 
ATOM   1034 C  CD1 . TYR A 1 182 ? 43.835 89.831  57.606 1.00 25.39  ? 160 TYR A CD1 1 
ATOM   1035 C  CD2 . TYR A 1 182 ? 45.619 91.277  56.972 1.00 30.14  ? 160 TYR A CD2 1 
ATOM   1036 C  CE1 . TYR A 1 182 ? 43.176 90.118  56.424 1.00 31.27  ? 160 TYR A CE1 1 
ATOM   1037 C  CE2 . TYR A 1 182 ? 44.968 91.570  55.788 1.00 30.28  ? 160 TYR A CE2 1 
ATOM   1038 C  CZ  . TYR A 1 182 ? 43.748 90.989  55.520 1.00 27.53  ? 160 TYR A CZ  1 
ATOM   1039 O  OH  . TYR A 1 182 ? 43.098 91.279  54.342 1.00 28.34  ? 160 TYR A OH  1 
ATOM   1040 N  N   . GLN A 1 183 ? 48.663 89.271  58.210 1.00 31.52  ? 161 GLN A N   1 
ATOM   1041 C  CA  . GLN A 1 183 ? 49.657 89.230  57.142 1.00 28.68  ? 161 GLN A CA  1 
ATOM   1042 C  C   . GLN A 1 183 ? 50.217 87.824  56.960 1.00 31.92  ? 161 GLN A C   1 
ATOM   1043 O  O   . GLN A 1 183 ? 50.448 87.385  55.827 1.00 30.09  ? 161 GLN A O   1 
ATOM   1044 C  CB  . GLN A 1 183 ? 50.786 90.222  57.428 1.00 28.20  ? 161 GLN A CB  1 
ATOM   1045 C  CG  . GLN A 1 183 ? 50.328 91.660  57.640 1.00 28.43  ? 161 GLN A CG  1 
ATOM   1046 C  CD  . GLN A 1 183 ? 49.773 92.300  56.381 1.00 33.01  ? 161 GLN A CD  1 
ATOM   1047 O  OE1 . GLN A 1 183 ? 49.072 93.310  56.439 1.00 32.45  ? 161 GLN A OE1 1 
ATOM   1048 N  NE2 . GLN A 1 183 ? 50.084 91.709  55.233 1.00 36.12  ? 161 GLN A NE2 1 
ATOM   1049 N  N   . ILE A 1 184 ? 50.445 87.106  58.062 1.00 24.98  ? 162 ILE A N   1 
ATOM   1050 C  CA  . ILE A 1 184 ? 50.944 85.735  57.970 1.00 23.19  ? 162 ILE A CA  1 
ATOM   1051 C  C   . ILE A 1 184 ? 49.932 84.855  57.249 1.00 31.29  ? 162 ILE A C   1 
ATOM   1052 O  O   . ILE A 1 184 ? 50.284 84.067  56.362 1.00 29.03  ? 162 ILE A O   1 
ATOM   1053 C  CB  . ILE A 1 184 ? 51.271 85.187  59.371 1.00 26.27  ? 162 ILE A CB  1 
ATOM   1054 C  CG1 . ILE A 1 184 ? 52.534 85.848  59.927 1.00 29.69  ? 162 ILE A CG1 1 
ATOM   1055 C  CG2 . ILE A 1 184 ? 51.437 83.673  59.331 1.00 28.83  ? 162 ILE A CG2 1 
ATOM   1056 C  CD1 . ILE A 1 184 ? 52.830 85.475  61.363 1.00 31.07  ? 162 ILE A CD1 1 
ATOM   1057 N  N   . LEU A 1 185 ? 48.656 84.983  57.615 1.00 23.64  ? 163 LEU A N   1 
ATOM   1058 C  CA  . LEU A 1 185 ? 47.619 84.167  56.994 1.00 26.64  ? 163 LEU A CA  1 
ATOM   1059 C  C   . LEU A 1 185 ? 47.488 84.483  55.510 1.00 26.09  ? 163 LEU A C   1 
ATOM   1060 O  O   . LEU A 1 185 ? 47.420 83.575  54.674 1.00 25.69  ? 163 LEU A O   1 
ATOM   1061 C  CB  . LEU A 1 185 ? 46.288 84.378  57.716 1.00 26.16  ? 163 LEU A CB  1 
ATOM   1062 C  CG  . LEU A 1 185 ? 46.192 83.723  59.097 1.00 31.72  ? 163 LEU A CG  1 
ATOM   1063 C  CD1 . LEU A 1 185 ? 45.030 84.297  59.895 1.00 29.02  ? 163 LEU A CD1 1 
ATOM   1064 C  CD2 . LEU A 1 185 ? 46.072 82.211  58.969 1.00 29.46  ? 163 LEU A CD2 1 
ATOM   1065 N  N   . GLN A 1 186 ? 47.468 85.772  55.163 1.00 25.61  ? 164 GLN A N   1 
ATOM   1066 C  CA  . GLN A 1 186 ? 47.301 86.158  53.765 1.00 26.40  ? 164 GLN A CA  1 
ATOM   1067 C  C   . GLN A 1 186 ? 48.496 85.731  52.922 1.00 29.15  ? 164 GLN A C   1 
ATOM   1068 O  O   . GLN A 1 186 ? 48.330 85.301  51.774 1.00 27.04  ? 164 GLN A O   1 
ATOM   1069 C  CB  . GLN A 1 186 ? 47.081 87.667  53.663 1.00 22.26  ? 164 GLN A CB  1 
ATOM   1070 C  CG  . GLN A 1 186 ? 45.731 88.135  54.190 1.00 26.16  ? 164 GLN A CG  1 
ATOM   1071 C  CD  . GLN A 1 186 ? 44.590 87.829  53.239 1.00 31.64  ? 164 GLN A CD  1 
ATOM   1072 O  OE1 . GLN A 1 186 ? 44.262 86.667  52.994 1.00 37.79  ? 164 GLN A OE1 1 
ATOM   1073 N  NE2 . GLN A 1 186 ? 43.976 88.874  52.698 1.00 37.66  ? 164 GLN A NE2 1 
ATOM   1074 N  N   . THR A 1 187 ? 49.707 85.841  53.471 1.00 30.06  ? 165 THR A N   1 
ATOM   1075 C  CA  . THR A 1 187 ? 50.891 85.413  52.734 1.00 32.43  ? 165 THR A CA  1 
ATOM   1076 C  C   . THR A 1 187 ? 50.901 83.902  52.540 1.00 27.67  ? 165 THR A C   1 
ATOM   1077 O  O   . THR A 1 187 ? 51.225 83.411  51.452 1.00 27.71  ? 165 THR A O   1 
ATOM   1078 C  CB  . THR A 1 187 ? 52.159 85.869  53.459 1.00 29.79  ? 165 THR A CB  1 
ATOM   1079 O  OG1 . THR A 1 187 ? 52.149 87.296  53.590 1.00 29.45  ? 165 THR A OG1 1 
ATOM   1080 C  CG2 . THR A 1 187 ? 53.404 85.444  52.688 1.00 26.55  ? 165 THR A CG2 1 
ATOM   1081 N  N   . ALA A 1 188 ? 50.541 83.148  53.580 1.00 25.57  ? 166 ALA A N   1 
ATOM   1082 C  CA  . ALA A 1 188 ? 50.517 81.694  53.462 1.00 24.71  ? 166 ALA A CA  1 
ATOM   1083 C  C   . ALA A 1 188 ? 49.395 81.232  52.539 1.00 25.54  ? 166 ALA A C   1 
ATOM   1084 O  O   . ALA A 1 188 ? 49.578 80.294  51.754 1.00 28.25  ? 166 ALA A O   1 
ATOM   1085 C  CB  . ALA A 1 188 ? 50.376 81.058  54.844 1.00 29.54  ? 166 ALA A CB  1 
ATOM   1086 N  N   . LEU A 1 189 ? 48.228 81.877  52.617 1.00 24.74  ? 167 LEU A N   1 
ATOM   1087 C  CA  . LEU A 1 189 ? 47.137 81.523  51.715 1.00 26.37  ? 167 LEU A CA  1 
ATOM   1088 C  C   . LEU A 1 189 ? 47.486 81.840  50.268 1.00 29.82  ? 167 LEU A C   1 
ATOM   1089 O  O   . LEU A 1 189 ? 47.049 81.129  49.356 1.00 28.18  ? 167 LEU A O   1 
ATOM   1090 C  CB  . LEU A 1 189 ? 45.854 82.247  52.123 1.00 29.03  ? 167 LEU A CB  1 
ATOM   1091 C  CG  . LEU A 1 189 ? 45.171 81.750  53.398 1.00 28.39  ? 167 LEU A CG  1 
ATOM   1092 C  CD1 . LEU A 1 189 ? 44.073 82.707  53.829 1.00 25.73  ? 167 LEU A CD1 1 
ATOM   1093 C  CD2 . LEU A 1 189 ? 44.623 80.344  53.208 1.00 29.95  ? 167 LEU A CD2 1 
ATOM   1094 N  N   . ASN A 1 190 ? 48.272 82.895  50.039 1.00 24.23  ? 168 ASN A N   1 
ATOM   1095 C  CA  . ASN A 1 190 ? 48.696 83.219  48.681 1.00 27.88  ? 168 ASN A CA  1 
ATOM   1096 C  C   . ASN A 1 190 ? 49.643 82.160  48.133 1.00 31.01  ? 168 ASN A C   1 
ATOM   1097 O  O   . ASN A 1 190 ? 49.526 81.758  46.970 1.00 29.78  ? 168 ASN A O   1 
ATOM   1098 C  CB  . ASN A 1 190 ? 49.357 84.597  48.649 1.00 32.34  ? 168 ASN A CB  1 
ATOM   1099 C  CG  . ASN A 1 190 ? 49.974 84.911  47.303 1.00 33.29  ? 168 ASN A CG  1 
ATOM   1100 O  OD1 . ASN A 1 190 ? 51.185 84.791  47.119 1.00 36.04  ? 168 ASN A OD1 1 
ATOM   1101 N  ND2 . ASN A 1 190 ? 49.141 85.312  46.350 1.00 29.76  ? 168 ASN A ND2 1 
ATOM   1102 N  N   . LYS A 1 191 ? 50.591 81.699  48.952 1.00 27.73  ? 169 LYS A N   1 
ATOM   1103 C  CA  . LYS A 1 191 ? 51.436 80.585  48.535 1.00 27.81  ? 169 LYS A CA  1 
ATOM   1104 C  C   . LYS A 1 191 ? 50.623 79.303  48.417 1.00 29.99  ? 169 LYS A C   1 
ATOM   1105 O  O   . LYS A 1 191 ? 50.855 78.492  47.513 1.00 28.77  ? 169 LYS A O   1 
ATOM   1106 C  CB  . LYS A 1 191 ? 52.591 80.393  49.518 1.00 31.39  ? 169 LYS A CB  1 
ATOM   1107 C  CG  . LYS A 1 191 ? 53.521 79.243  49.152 1.00 34.51  ? 169 LYS A CG  1 
ATOM   1108 C  CD  . LYS A 1 191 ? 54.197 78.643  50.375 1.00 32.00  ? 169 LYS A CD  1 
ATOM   1109 C  CE  . LYS A 1 191 ? 55.288 77.659  49.974 1.00 36.67  ? 169 LYS A CE  1 
ATOM   1110 N  NZ  . LYS A 1 191 ? 55.971 77.064  51.156 1.00 35.79  ? 169 LYS A NZ  1 
ATOM   1111 N  N   . GLY A 1 192 ? 49.660 79.111  49.314 1.00 29.92  ? 170 GLY A N   1 
ATOM   1112 C  CA  . GLY A 1 192 ? 48.855 77.908  49.321 1.00 30.70  ? 170 GLY A CA  1 
ATOM   1113 C  C   . GLY A 1 192 ? 49.113 77.052  50.542 1.00 28.41  ? 170 GLY A C   1 
ATOM   1114 O  O   . GLY A 1 192 ? 50.264 76.736  50.854 1.00 31.28  ? 170 GLY A O   1 
ATOM   1115 N  N   . LEU A 1 193 ? 48.054 76.688  51.248 1.00 28.44  ? 171 LEU A N   1 
ATOM   1116 C  CA  . LEU A 1 193 ? 48.198 75.794  52.388 1.00 26.60  ? 171 LEU A CA  1 
ATOM   1117 C  C   . LEU A 1 193 ? 48.610 74.412  51.895 1.00 29.76  ? 171 LEU A C   1 
ATOM   1118 O  O   . LEU A 1 193 ? 47.950 73.853  51.011 1.00 25.47  ? 171 LEU A O   1 
ATOM   1119 C  CB  . LEU A 1 193 ? 46.890 75.713  53.173 1.00 28.42  ? 171 LEU A CB  1 
ATOM   1120 C  CG  . LEU A 1 193 ? 46.820 74.659  54.282 1.00 34.94  ? 171 LEU A CG  1 
ATOM   1121 C  CD1 . LEU A 1 193 ? 47.572 75.126  55.521 1.00 24.97  ? 171 LEU A CD1 1 
ATOM   1122 C  CD2 . LEU A 1 193 ? 45.374 74.330  54.621 1.00 31.30  ? 171 LEU A CD2 1 
ATOM   1123 N  N   . PRO A 1 194 ? 49.687 73.838  52.417 1.00 24.15  ? 172 PRO A N   1 
ATOM   1124 C  CA  . PRO A 1 194 ? 50.103 72.504  51.978 1.00 31.30  ? 172 PRO A CA  1 
ATOM   1125 C  C   . PRO A 1 194 ? 49.214 71.426  52.584 1.00 27.67  ? 172 PRO A C   1 
ATOM   1126 O  O   . PRO A 1 194 ? 48.373 71.681  53.447 1.00 28.29  ? 172 PRO A O   1 
ATOM   1127 C  CB  . PRO A 1 194 ? 51.537 72.397  52.498 1.00 25.32  ? 172 PRO A CB  1 
ATOM   1128 C  CG  . PRO A 1 194 ? 51.529 73.232  53.730 1.00 29.61  ? 172 PRO A CG  1 
ATOM   1129 C  CD  . PRO A 1 194 ? 50.581 74.379  53.456 1.00 30.17  ? 172 PRO A CD  1 
ATOM   1130 N  N   . ALA A 1 195 ? 49.420 70.202  52.106 1.00 25.68  ? 173 ALA A N   1 
ATOM   1131 C  CA  . ALA A 1 195 ? 48.678 69.064  52.622 1.00 27.63  ? 173 ALA A CA  1 
ATOM   1132 C  C   . ALA A 1 195 ? 48.978 68.863  54.105 1.00 28.43  ? 173 ALA A C   1 
ATOM   1133 O  O   . ALA A 1 195 ? 49.999 69.315  54.629 1.00 24.23  ? 173 ALA A O   1 
ATOM   1134 C  CB  . ALA A 1 195 ? 49.017 67.799  51.834 1.00 26.54  ? 173 ALA A CB  1 
ATOM   1135 N  N   . LEU A 1 196 ? 48.061 68.167  54.782 1.00 27.28  ? 174 LEU A N   1 
ATOM   1136 C  CA  . LEU A 1 196 ? 48.155 68.020  56.232 1.00 27.44  ? 174 LEU A CA  1 
ATOM   1137 C  C   . LEU A 1 196 ? 49.434 67.307  56.652 1.00 28.61  ? 174 LEU A C   1 
ATOM   1138 O  O   . LEU A 1 196 ? 49.947 67.552  57.749 1.00 28.19  ? 174 LEU A O   1 
ATOM   1139 C  CB  . LEU A 1 196 ? 46.932 67.271  56.759 1.00 23.03  ? 174 LEU A CB  1 
ATOM   1140 C  CG  . LEU A 1 196 ? 45.784 68.110  57.324 1.00 30.68  ? 174 LEU A CG  1 
ATOM   1141 C  CD1 . LEU A 1 196 ? 45.374 69.215  56.360 1.00 28.35  ? 174 LEU A CD1 1 
ATOM   1142 C  CD2 . LEU A 1 196 ? 44.598 67.220  57.654 1.00 27.98  ? 174 LEU A CD2 1 
ATOM   1143 N  N   . LYS A 1 197 ? 49.967 66.431  55.798 1.00 27.30  ? 175 LYS A N   1 
ATOM   1144 C  CA  . LYS A 1 197 ? 51.202 65.726  56.119 1.00 27.20  ? 175 LYS A CA  1 
ATOM   1145 C  C   . LYS A 1 197 ? 52.428 66.631  56.095 1.00 32.76  ? 175 LYS A C   1 
ATOM   1146 O  O   . LYS A 1 197 ? 53.502 66.195  56.522 1.00 37.14  ? 175 LYS A O   1 
ATOM   1147 C  CB  . LYS A 1 197 ? 51.410 64.564  55.146 1.00 26.65  ? 175 LYS A CB  1 
ATOM   1148 C  CG  . LYS A 1 197 ? 51.944 64.982  53.782 1.00 37.38  ? 175 LYS A CG  1 
ATOM   1149 C  CD  . LYS A 1 197 ? 52.346 63.774  52.948 1.00 38.44  ? 175 LYS A CD  1 
ATOM   1150 C  CE  . LYS A 1 197 ? 52.697 64.170  51.520 1.00 42.50  ? 175 LYS A CE  1 
ATOM   1151 N  NZ  . LYS A 1 197 ? 53.807 65.163  51.468 1.00 56.72  ? 175 LYS A NZ  1 
ATOM   1152 N  N   . GLU A 1 198 ? 52.296 67.868  55.623 1.00 29.54  ? 176 GLU A N   1 
ATOM   1153 C  CA  . GLU A 1 198 ? 53.438 68.751  55.423 1.00 29.58  ? 176 GLU A CA  1 
ATOM   1154 C  C   . GLU A 1 198 ? 53.724 69.541  56.694 1.00 32.66  ? 176 GLU A C   1 
ATOM   1155 O  O   . GLU A 1 198 ? 52.895 70.347  57.130 1.00 27.74  ? 176 GLU A O   1 
ATOM   1156 C  CB  . GLU A 1 198 ? 53.183 69.708  54.261 1.00 33.09  ? 176 GLU A CB  1 
ATOM   1157 C  CG  . GLU A 1 198 ? 54.349 70.629  54.001 1.00 32.01  ? 176 GLU A CG  1 
ATOM   1158 C  CD  . GLU A 1 198 ? 55.591 69.853  53.647 1.00 39.57  ? 176 GLU A CD  1 
ATOM   1159 O  OE1 . GLU A 1 198 ? 55.551 69.149  52.619 1.00 37.47  ? 176 GLU A OE1 1 
ATOM   1160 O  OE2 . GLU A 1 198 ? 56.589 69.929  54.397 1.00 31.22  ? 176 GLU A OE2 1 
ATOM   1161 N  N   . ASN A 1 199 ? 54.908 69.330  57.269 1.00 27.81  ? 177 ASN A N   1 
ATOM   1162 C  CA  . ASN A 1 199 ? 55.327 70.041  58.467 1.00 29.36  ? 177 ASN A CA  1 
ATOM   1163 C  C   . ASN A 1 199 ? 56.522 70.957  58.250 1.00 34.65  ? 177 ASN A C   1 
ATOM   1164 O  O   . ASN A 1 199 ? 56.898 71.680  59.180 1.00 31.75  ? 177 ASN A O   1 
ATOM   1165 C  CB  . ASN A 1 199 ? 55.662 69.045  59.588 1.00 33.26  ? 177 ASN A CB  1 
ATOM   1166 C  CG  . ASN A 1 199 ? 54.498 68.138  59.928 1.00 37.44  ? 177 ASN A CG  1 
ATOM   1167 O  OD1 . ASN A 1 199 ? 53.471 68.590  60.434 1.00 48.66  ? 177 ASN A OD1 1 
ATOM   1168 N  ND2 . ASN A 1 199 ? 54.652 66.850  59.651 1.00 41.49  ? 177 ASN A ND2 1 
ATOM   1169 N  N   . ASN A 1 200 ? 57.123 70.957  57.060 1.00 29.21  ? 178 ASN A N   1 
ATOM   1170 C  CA  . ASN A 1 200 ? 58.347 71.705  56.806 1.00 29.57  ? 178 ASN A CA  1 
ATOM   1171 C  C   . ASN A 1 200 ? 58.148 72.869  55.842 1.00 30.14  ? 178 ASN A C   1 
ATOM   1172 O  O   . ASN A 1 200 ? 59.134 73.472  55.405 1.00 32.56  ? 178 ASN A O   1 
ATOM   1173 C  CB  . ASN A 1 200 ? 59.433 70.766  56.275 1.00 29.78  ? 178 ASN A CB  1 
ATOM   1174 C  CG  . ASN A 1 200 ? 59.680 69.584  57.194 1.00 38.41  ? 178 ASN A CG  1 
ATOM   1175 O  OD1 . ASN A 1 200 ? 59.759 69.736  58.412 1.00 39.11  ? 178 ASN A OD1 1 
ATOM   1176 N  ND2 . ASN A 1 200 ? 59.796 68.396  56.612 1.00 41.44  ? 178 ASN A ND2 1 
ATOM   1177 N  N   . GLY A 1 201 ? 56.904 73.204  55.504 1.00 29.25  ? 179 GLY A N   1 
ATOM   1178 C  CA  . GLY A 1 201 ? 56.654 74.324  54.608 1.00 27.44  ? 179 GLY A CA  1 
ATOM   1179 C  C   . GLY A 1 201 ? 56.726 75.652  55.347 1.00 30.21  ? 179 GLY A C   1 
ATOM   1180 O  O   . GLY A 1 201 ? 56.233 75.794  56.466 1.00 28.57  ? 179 GLY A O   1 
ATOM   1181 N  N   . THR A 1 202 ? 57.359 76.634  54.705 1.00 26.27  ? 180 THR A N   1 
ATOM   1182 C  CA  . THR A 1 202 ? 57.553 77.948  55.301 1.00 27.81  ? 180 THR A CA  1 
ATOM   1183 C  C   . THR A 1 202 ? 57.224 79.046  54.298 1.00 25.99  ? 180 THR A C   1 
ATOM   1184 O  O   . THR A 1 202 ? 57.135 78.813  53.090 1.00 26.02  ? 180 THR A O   1 
ATOM   1185 C  CB  . THR A 1 202 ? 58.992 78.150  55.801 1.00 28.38  ? 180 THR A CB  1 
ATOM   1186 O  OG1 . THR A 1 202 ? 59.901 78.059  54.695 1.00 28.12  ? 180 THR A OG1 1 
ATOM   1187 C  CG2 . THR A 1 202 ? 59.357 77.112  56.853 1.00 28.72  ? 180 THR A CG2 1 
ATOM   1188 N  N   . VAL A 1 203 ? 57.049 80.259  54.827 1.00 25.50  ? 181 VAL A N   1 
ATOM   1189 C  CA  . VAL A 1 203 ? 56.886 81.463  54.024 1.00 21.20  ? 181 VAL A CA  1 
ATOM   1190 C  C   . VAL A 1 203 ? 57.702 82.580  54.658 1.00 24.24  ? 181 VAL A C   1 
ATOM   1191 O  O   . VAL A 1 203 ? 58.059 82.531  55.837 1.00 34.07  ? 181 VAL A O   1 
ATOM   1192 C  CB  . VAL A 1 203 ? 55.411 81.915  53.898 1.00 33.10  ? 181 VAL A CB  1 
ATOM   1193 C  CG1 . VAL A 1 203 ? 54.631 80.976  53.000 1.00 28.98  ? 181 VAL A CG1 1 
ATOM   1194 C  CG2 . VAL A 1 203 ? 54.765 82.023  55.274 1.00 29.09  ? 181 VAL A CG2 1 
ATOM   1195 N  N   . SER A 1 204 ? 57.998 83.593  53.851 1.00 27.44  ? 182 SER A N   1 
ATOM   1196 C  CA  . SER A 1 204 ? 58.525 84.860  54.337 1.00 28.75  ? 182 SER A CA  1 
ATOM   1197 C  C   . SER A 1 204 ? 57.404 85.889  54.305 1.00 31.89  ? 182 SER A C   1 
ATOM   1198 O  O   . SER A 1 204 ? 56.677 85.988  53.311 1.00 28.93  ? 182 SER A O   1 
ATOM   1199 C  CB  . SER A 1 204 ? 59.709 85.334  53.492 1.00 33.96  ? 182 SER A CB  1 
ATOM   1200 O  OG  . SER A 1 204 ? 60.931 84.820  53.992 1.00 37.64  ? 182 SER A OG  1 
ATOM   1201 N  N   . VAL A 1 205 ? 57.255 86.639  55.394 1.00 25.61  ? 183 VAL A N   1 
ATOM   1202 C  CA  . VAL A 1 205 ? 56.188 87.621  55.534 1.00 29.65  ? 183 VAL A CA  1 
ATOM   1203 C  C   . VAL A 1 205 ? 56.816 88.990  55.747 1.00 29.24  ? 183 VAL A C   1 
ATOM   1204 O  O   . VAL A 1 205 ? 57.699 89.150  56.597 1.00 32.47  ? 183 VAL A O   1 
ATOM   1205 C  CB  . VAL A 1 205 ? 55.237 87.269  56.693 1.00 32.64  ? 183 VAL A CB  1 
ATOM   1206 C  CG1 . VAL A 1 205 ? 54.122 88.299  56.797 1.00 28.71  ? 183 VAL A CG1 1 
ATOM   1207 C  CG2 . VAL A 1 205 ? 54.661 85.872  56.503 1.00 31.41  ? 183 VAL A CG2 1 
ATOM   1208 N  N   . THR A 1 206 ? 56.362 89.971  54.971 1.00 29.23  ? 184 THR A N   1 
ATOM   1209 C  CA  . THR A 1 206 ? 56.816 91.349  55.092 1.00 29.11  ? 184 THR A CA  1 
ATOM   1210 C  C   . THR A 1 206 ? 55.601 92.260  55.155 1.00 34.43  ? 184 THR A C   1 
ATOM   1211 O  O   . THR A 1 206 ? 54.694 92.145  54.325 1.00 36.37  ? 184 THR A O   1 
ATOM   1212 C  CB  . THR A 1 206 ? 57.715 91.749  53.915 1.00 37.64  ? 184 THR A CB  1 
ATOM   1213 O  OG1 . THR A 1 206 ? 58.876 90.909  53.889 1.00 37.19  ? 184 THR A OG1 1 
ATOM   1214 C  CG2 . THR A 1 206 ? 58.151 93.200  54.044 1.00 37.77  ? 184 THR A CG2 1 
ATOM   1215 N  N   . TYR A 1 207 ? 55.579 93.155  56.142 1.00 32.65  ? 185 TYR A N   1 
ATOM   1216 C  CA  . TYR A 1 207 ? 54.510 94.137  56.250 1.00 30.09  ? 185 TYR A CA  1 
ATOM   1217 C  C   . TYR A 1 207 ? 55.068 95.419  56.850 1.00 33.63  ? 185 TYR A C   1 
ATOM   1218 O  O   . TYR A 1 207 ? 56.092 95.413  57.540 1.00 32.22  ? 185 TYR A O   1 
ATOM   1219 C  CB  . TYR A 1 207 ? 53.330 93.612  57.082 1.00 32.98  ? 185 TYR A CB  1 
ATOM   1220 C  CG  . TYR A 1 207 ? 53.660 93.268  58.518 1.00 33.44  ? 185 TYR A CG  1 
ATOM   1221 C  CD1 . TYR A 1 207 ? 54.068 91.988  58.870 1.00 33.96  ? 185 TYR A CD1 1 
ATOM   1222 C  CD2 . TYR A 1 207 ? 53.546 94.219  59.526 1.00 34.86  ? 185 TYR A CD2 1 
ATOM   1223 C  CE1 . TYR A 1 207 ? 54.363 91.667  60.182 1.00 35.30  ? 185 TYR A CE1 1 
ATOM   1224 C  CE2 . TYR A 1 207 ? 53.841 93.907  60.840 1.00 34.79  ? 185 TYR A CE2 1 
ATOM   1225 C  CZ  . TYR A 1 207 ? 54.247 92.630  61.163 1.00 34.76  ? 185 TYR A CZ  1 
ATOM   1226 O  OH  . TYR A 1 207 ? 54.541 92.316  62.470 1.00 36.75  ? 185 TYR A OH  1 
ATOM   1227 N  N   . THR A 1 208 ? 54.378 96.524  56.575 1.00 37.86  ? 186 THR A N   1 
ATOM   1228 C  CA  . THR A 1 208 ? 54.823 97.850  56.974 1.00 38.90  ? 186 THR A CA  1 
ATOM   1229 C  C   . THR A 1 208 ? 53.693 98.598  57.668 1.00 39.71  ? 186 THR A C   1 
ATOM   1230 O  O   . THR A 1 208 ? 52.512 98.373  57.389 1.00 36.21  ? 186 THR A O   1 
ATOM   1231 C  CB  . THR A 1 208 ? 55.298 98.676  55.766 1.00 32.25  ? 186 THR A CB  1 
ATOM   1232 O  OG1 . THR A 1 208 ? 54.188 98.932  54.897 1.00 37.96  ? 186 THR A OG1 1 
ATOM   1233 C  CG2 . THR A 1 208 ? 56.371 97.934  54.990 1.00 32.01  ? 186 THR A CG2 1 
ATOM   1234 N  N   . TYR A 1 209 ? 54.099 99.481  58.564 1.00 38.74  ? 187 TYR A N   1 
ATOM   1235 C  CA  . TYR A 1 209 ? 53.186 100.458 59.193 1.00 37.74  ? 187 TYR A CA  1 
ATOM   1236 C  C   . TYR A 1 209 ? 53.908 101.800 59.351 1.00 43.29  ? 187 TYR A C   1 
ATOM   1237 O  O   . TYR A 1 209 ? 55.102 101.806 59.523 1.00 38.23  ? 187 TYR A O   1 
ATOM   1238 C  CB  . TYR A 1 209 ? 52.508 99.971  60.465 1.00 36.79  ? 187 TYR A CB  1 
ATOM   1239 C  CG  . TYR A 1 209 ? 53.413 99.596  61.596 1.00 39.82  ? 187 TYR A CG  1 
ATOM   1240 C  CD1 . TYR A 1 209 ? 53.829 98.305  61.752 1.00 36.91  ? 187 TYR A CD1 1 
ATOM   1241 C  CD2 . TYR A 1 209 ? 53.808 100.519 62.534 1.00 45.71  ? 187 TYR A CD2 1 
ATOM   1242 C  CE1 . TYR A 1 209 ? 54.625 97.921  62.800 1.00 39.15  ? 187 TYR A CE1 1 
ATOM   1243 C  CE2 . TYR A 1 209 ? 54.604 100.156 63.596 1.00 44.23  ? 187 TYR A CE2 1 
ATOM   1244 C  CZ  . TYR A 1 209 ? 55.019 98.853  63.722 1.00 46.02  ? 187 TYR A CZ  1 
ATOM   1245 O  OH  . TYR A 1 209 ? 55.801 98.460  64.743 1.00 45.52  ? 187 TYR A OH  1 
ATOM   1246 N  N   . THR A 1 210 ? 53.148 102.885 59.274 1.00 41.97  ? 188 THR A N   1 
ATOM   1247 C  CA  . THR A 1 210 ? 53.695 104.257 59.372 1.00 45.54  ? 188 THR A CA  1 
ATOM   1248 C  C   . THR A 1 210 ? 53.132 104.978 60.591 1.00 48.60  ? 188 THR A C   1 
ATOM   1249 O  O   . THR A 1 210 ? 52.010 104.693 60.968 1.00 47.88  ? 188 THR A O   1 
ATOM   1250 C  CB  . THR A 1 210 ? 53.445 105.056 58.094 1.00 39.70  ? 188 THR A CB  1 
ATOM   1251 O  OG1 . THR A 1 210 ? 52.056 105.183 57.834 1.00 39.13  ? 188 THR A OG1 1 
ATOM   1252 C  CG2 . THR A 1 210 ? 54.112 104.446 56.892 1.00 43.08  ? 188 THR A CG2 1 
ATOM   1253 N  N   . CYS A 1 211 ? 53.924 105.862 61.177 1.00 46.59  ? 189 CYS A N   1 
ATOM   1254 C  CA  . CYS A 1 211 ? 53.475 106.672 62.333 1.00 54.38  ? 189 CYS A CA  1 
ATOM   1255 C  C   . CYS A 1 211 ? 53.623 108.152 62.019 1.00 60.06  ? 189 CYS A C   1 
ATOM   1256 O  O   . CYS A 1 211 ? 54.734 108.614 61.801 1.00 53.17  ? 189 CYS A O   1 
ATOM   1257 C  CB  . CYS A 1 211 ? 54.327 106.472 63.560 1.00 51.79  ? 189 CYS A CB  1 
ATOM   1258 S  SG  . CYS A 1 211 ? 53.972 104.923 64.391 1.00 54.41  ? 189 CYS A SG  1 
ATOM   1259 N  N   . SER A 1 212 ? 52.498 108.826 61.997 1.00 51.74  ? 190 SER A N   1 
ATOM   1260 C  CA  . SER A 1 212 ? 52.456 110.267 61.722 1.00 54.33  ? 190 SER A CA  1 
ATOM   1261 C  C   . SER A 1 212 ? 51.816 110.955 62.922 1.00 57.34  ? 190 SER A C   1 
ATOM   1262 O  O   . SER A 1 212 ? 51.251 110.304 63.775 1.00 50.35  ? 190 SER A O   1 
ATOM   1263 C  CB  . SER A 1 212 ? 51.681 110.492 60.480 1.00 53.33  ? 190 SER A CB  1 
ATOM   1264 O  OG  . SER A 1 212 ? 50.799 111.588 60.587 1.00 69.27  ? 190 SER A OG  1 
ATOM   1265 N  N   . GLY A 1 213 ? 51.949 112.261 62.947 1.00 61.15  ? 191 GLY A N   1 
ATOM   1266 C  CA  . GLY A 1 213 ? 51.334 113.093 63.970 1.00 54.17  ? 191 GLY A CA  1 
ATOM   1267 C  C   . GLY A 1 213 ? 52.236 113.328 65.165 1.00 56.28  ? 191 GLY A C   1 
ATOM   1268 O  O   . GLY A 1 213 ? 53.087 112.511 65.517 1.00 51.72  ? 191 GLY A O   1 
ATOM   1269 N  N   . GLU A 1 214 ? 52.029 114.474 65.811 1.00 58.36  ? 192 GLU A N   1 
ATOM   1270 C  CA  . GLU A 1 214 ? 52.844 114.858 66.956 1.00 53.70  ? 192 GLU A CA  1 
ATOM   1271 C  C   . GLU A 1 214 ? 52.455 114.046 68.185 1.00 49.84  ? 192 GLU A C   1 
ATOM   1272 O  O   . GLU A 1 214 ? 51.275 113.951 68.535 1.00 54.42  ? 192 GLU A O   1 
ATOM   1273 C  CB  . GLU A 1 214 ? 52.686 116.352 67.236 1.00 59.50  ? 192 GLU A CB  1 
ATOM   1274 C  CG  . GLU A 1 214 ? 53.316 116.817 68.539 1.00 66.81  ? 192 GLU A CG  1 
ATOM   1275 C  CD  . GLU A 1 214 ? 53.652 118.296 68.526 1.00 79.07  ? 192 GLU A CD  1 
ATOM   1276 O  OE1 . GLU A 1 214 ? 54.116 118.791 67.477 1.00 77.64  ? 192 GLU A OE1 1 
ATOM   1277 O  OE2 . GLU A 1 214 ? 53.452 118.962 69.563 1.00 82.63  ? 192 GLU A OE2 1 
ATOM   1278 N  N   . GLY A 1 215 ? 53.454 113.463 68.846 1.00 41.20  ? 193 GLY A N   1 
ATOM   1279 C  CA  . GLY A 1 215 ? 53.227 112.648 70.018 1.00 52.87  ? 193 GLY A CA  1 
ATOM   1280 C  C   . GLY A 1 215 ? 53.023 111.173 69.749 1.00 55.39  ? 193 GLY A C   1 
ATOM   1281 O  O   . GLY A 1 215 ? 52.765 110.419 70.696 1.00 54.01  ? 193 GLY A O   1 
ATOM   1282 N  N   . ASN A 1 216 ? 53.189 110.749 68.505 1.00 54.45  ? 194 ASN A N   1 
ATOM   1283 C  CA  . ASN A 1 216 ? 52.994 109.325 68.146 1.00 51.36  ? 194 ASN A CA  1 
ATOM   1284 C  C   . ASN A 1 216 ? 54.190 108.516 68.586 1.00 44.03  ? 194 ASN A C   1 
ATOM   1285 O  O   . ASN A 1 216 ? 55.251 108.774 68.119 1.00 55.93  ? 194 ASN A O   1 
ATOM   1286 C  CB  . ASN A 1 216 ? 52.576 109.171 66.688 1.00 57.27  ? 194 ASN A CB  1 
ATOM   1287 C  CG  . ASN A 1 216 ? 51.975 107.825 66.350 1.00 47.91  ? 194 ASN A CG  1 
ATOM   1288 O  OD1 . ASN A 1 216 ? 52.194 106.857 67.040 1.00 41.53  ? 194 ASN A OD1 1 
ATOM   1289 N  ND2 . ASN A 1 216 ? 51.232 107.776 65.274 1.00 43.10  ? 194 ASN A ND2 1 
ATOM   1290 N  N   . ASP A 1 217 ? 53.989 107.611 69.512 1.00 44.50  ? 195 ASP A N   1 
ATOM   1291 C  CA  . ASP A 1 217 ? 55.063 106.748 69.984 1.00 50.28  ? 195 ASP A CA  1 
ATOM   1292 C  C   . ASP A 1 217 ? 54.860 105.294 69.570 1.00 52.39  ? 195 ASP A C   1 
ATOM   1293 O  O   . ASP A 1 217 ? 55.501 104.398 70.130 1.00 54.66  ? 195 ASP A O   1 
ATOM   1294 C  CB  . ASP A 1 217 ? 55.195 106.851 71.504 1.00 56.94  ? 195 ASP A CB  1 
ATOM   1295 C  CG  . ASP A 1 217 ? 54.027 106.214 72.239 1.00 60.91  ? 195 ASP A CG  1 
ATOM   1296 O  OD1 . ASP A 1 217 ? 52.929 106.118 71.650 1.00 61.08  ? 195 ASP A OD1 1 
ATOM   1297 O  OD2 . ASP A 1 217 ? 54.206 105.807 73.406 1.00 58.67  ? 195 ASP A OD2 1 
ATOM   1298 N  N   . ASN A 1 218 ? 54.026 105.078 68.562 1.00 51.77  ? 196 ASN A N   1 
ATOM   1299 C  CA  . ASN A 1 218 ? 53.711 103.708 68.082 1.00 54.97  ? 196 ASN A CA  1 
ATOM   1300 C  C   . ASN A 1 218 ? 54.874 103.138 67.267 1.00 60.69  ? 196 ASN A C   1 
ATOM   1301 O  O   . ASN A 1 218 ? 55.124 101.974 67.377 1.00 60.40  ? 196 ASN A O   1 
ATOM   1302 C  CB  . ASN A 1 218 ? 52.366 103.668 67.375 1.00 42.42  ? 196 ASN A CB  1 
ATOM   1303 C  CG  . ASN A 1 218 ? 51.238 103.755 68.370 1.00 48.46  ? 196 ASN A CG  1 
ATOM   1304 O  OD1 . ASN A 1 218 ? 51.291 103.098 69.384 1.00 46.61  ? 196 ASN A OD1 1 
ATOM   1305 N  ND2 . ASN A 1 218 ? 50.238 104.555 68.095 1.00 42.36  ? 196 ASN A ND2 1 
ATOM   1306 N  N   . CYS A 1 219 ? 55.578 103.959 66.508 1.00 58.72  ? 197 CYS A N   1 
ATOM   1307 C  CA  . CYS A 1 219 ? 56.728 103.424 65.753 1.00 63.06  ? 197 CYS A CA  1 
ATOM   1308 C  C   . CYS A 1 219 ? 57.958 103.834 66.528 1.00 57.83  ? 197 CYS A C   1 
ATOM   1309 O  O   . CYS A 1 219 ? 59.022 103.875 65.989 1.00 58.12  ? 197 CYS A O   1 
ATOM   1310 C  CB  . CYS A 1 219 ? 56.807 104.016 64.367 1.00 53.36  ? 197 CYS A CB  1 
ATOM   1311 S  SG  . CYS A 1 219 ? 55.268 103.865 63.461 1.00 60.87  ? 197 CYS A SG  1 
ATOM   1312 N  N   . SER A 1 220 ? 57.785 103.990 67.822 1.00 63.02  ? 198 SER A N   1 
ATOM   1313 C  CA  . SER A 1 220 ? 58.928 104.429 68.651 1.00 59.56  ? 198 SER A CA  1 
ATOM   1314 C  C   . SER A 1 220 ? 59.833 103.262 68.998 1.00 66.89  ? 198 SER A C   1 
ATOM   1315 O  O   . SER A 1 220 ? 59.431 102.153 68.779 1.00 64.97  ? 198 SER A O   1 
ATOM   1316 C  CB  . SER A 1 220 ? 58.453 105.118 69.874 1.00 56.78  ? 198 SER A CB  1 
ATOM   1317 O  OG  . SER A 1 220 ? 58.445 104.248 70.979 1.00 62.29  ? 198 SER A OG  1 
ATOM   1318 N  N   . LYS A 1 221 ? 60.973 103.542 69.630 1.00 57.08  ? 199 LYS A N   1 
ATOM   1319 C  CA  . LYS A 1 221 ? 61.976 102.499 69.922 1.00 56.10  ? 199 LYS A CA  1 
ATOM   1320 C  C   . LYS A 1 221 ? 61.459 101.528 70.985 1.00 63.26  ? 199 LYS A C   1 
ATOM   1321 O  O   . LYS A 1 221 ? 61.593 100.329 70.812 1.00 62.73  ? 199 LYS A O   1 
ATOM   1322 C  CB  . LYS A 1 221 ? 63.278 103.189 70.322 1.00 30.00  ? 199 LYS A CB  1 
ATOM   1323 C  CG  . LYS A 1 221 ? 64.260 102.386 71.153 1.00 30.00  ? 199 LYS A CG  1 
ATOM   1324 C  CD  . LYS A 1 221 ? 64.953 103.248 72.157 1.00 30.00  ? 199 LYS A CD  1 
ATOM   1325 C  CE  . LYS A 1 221 ? 66.145 103.982 71.601 1.00 30.00  ? 199 LYS A CE  1 
ATOM   1326 N  NZ  . LYS A 1 221 ? 66.649 104.998 72.554 1.00 30.00  ? 199 LYS A NZ  1 
ATOM   1327 N  N   . LYS A 1 222 ? 60.842 102.021 72.044 1.00 67.17  ? 200 LYS A N   1 
ATOM   1328 C  CA  . LYS A 1 222 ? 60.382 101.072 73.084 1.00 64.58  ? 200 LYS A CA  1 
ATOM   1329 C  C   . LYS A 1 222 ? 59.256 100.202 72.521 1.00 63.83  ? 200 LYS A C   1 
ATOM   1330 O  O   . LYS A 1 222 ? 59.174 99.046  72.909 1.00 66.65  ? 200 LYS A O   1 
ATOM   1331 C  CB  . LYS A 1 222 ? 59.990 101.757 74.389 1.00 30.00  ? 200 LYS A CB  1 
ATOM   1332 C  CG  . LYS A 1 222 ? 59.611 100.769 75.483 1.00 30.00  ? 200 LYS A CG  1 
ATOM   1333 C  CD  . LYS A 1 222 ? 59.094 101.344 76.782 1.00 30.00  ? 200 LYS A CD  1 
ATOM   1334 C  CE  . LYS A 1 222 ? 59.051 100.310 77.888 1.00 30.00  ? 200 LYS A CE  1 
ATOM   1335 N  NZ  . LYS A 1 222 ? 58.188 99.162  77.529 1.00 30.00  ? 200 LYS A NZ  1 
ATOM   1336 N  N   . ALA A 1 223 ? 58.405 100.760 71.679 1.00 57.20  ? 201 ALA A N   1 
ATOM   1337 C  CA  . ALA A 1 223 ? 57.390 99.932  71.005 1.00 57.21  ? 201 ALA A CA  1 
ATOM   1338 C  C   . ALA A 1 223 ? 58.046 98.922  70.062 1.00 62.02  ? 201 ALA A C   1 
ATOM   1339 O  O   . ALA A 1 223 ? 57.733 97.739  70.181 1.00 60.71  ? 201 ALA A O   1 
ATOM   1340 C  CB  . ALA A 1 223 ? 56.465 100.812 70.245 1.00 54.48  ? 201 ALA A CB  1 
ATOM   1341 N  N   . THR A 1 224 ? 58.881 99.391  69.143 1.00 59.11  ? 202 THR A N   1 
ATOM   1342 C  CA  . THR A 1 224 ? 59.482 98.516  68.106 1.00 57.70  ? 202 THR A CA  1 
ATOM   1343 C  C   . THR A 1 224 ? 60.750 97.854  68.603 1.00 54.66  ? 202 THR A C   1 
ATOM   1344 O  O   . THR A 1 224 ? 61.122 96.853  68.060 1.00 59.72  ? 202 THR A O   1 
ATOM   1345 C  CB  . THR A 1 224 ? 59.792 99.315  66.845 1.00 57.78  ? 202 THR A CB  1 
ATOM   1346 O  OG1 . THR A 1 224 ? 60.898 100.138 67.163 1.00 61.02  ? 202 THR A OG1 1 
ATOM   1347 C  CG2 . THR A 1 224 ? 58.627 100.160 66.397 1.00 52.45  ? 202 THR A CG2 1 
ATOM   1348 N  N   . GLY A 1 225 ? 61.386 98.450  69.593 1.00 63.91  ? 203 GLY A N   1 
ATOM   1349 C  CA  . GLY A 1 225 ? 62.609 97.869  70.160 1.00 62.40  ? 203 GLY A CA  1 
ATOM   1350 C  C   . GLY A 1 225 ? 63.737 97.799  69.159 1.00 65.92  ? 203 GLY A C   1 
ATOM   1351 O  O   . GLY A 1 225 ? 64.478 96.849  69.221 1.00 83.09  ? 203 GLY A O   1 
ATOM   1352 N  N   . VAL A 1 226 ? 63.860 98.765  68.261 1.00 63.95  ? 204 VAL A N   1 
ATOM   1353 C  CA  . VAL A 1 226 ? 64.994 98.716  67.300 1.00 70.09  ? 204 VAL A CA  1 
ATOM   1354 C  C   . VAL A 1 226 ? 66.237 99.297  67.973 1.00 83.26  ? 204 VAL A C   1 
ATOM   1355 O  O   . VAL A 1 226 ? 66.903 98.549  68.698 1.00 85.66  ? 204 VAL A O   1 
ATOM   1356 C  CB  . VAL A 1 226 ? 64.660 99.415  65.975 1.00 66.85  ? 204 VAL A CB  1 
ATOM   1357 C  CG1 . VAL A 1 226 ? 65.711 99.158  64.913 1.00 72.25  ? 204 VAL A CG1 1 
ATOM   1358 C  CG2 . VAL A 1 226 ? 63.337 98.917  65.447 1.00 64.91  ? 204 VAL A CG2 1 
ATOM   1359 N  N   . SER A 1 227 ? 66.542 100.567 67.677 1.00 86.39  ? 205 SER A N   1 
ATOM   1360 C  CA  . SER A 1 227 ? 67.682 101.393 68.163 1.00 88.62  ? 205 SER A CA  1 
ATOM   1361 C  C   . SER A 1 227 ? 67.510 102.788 67.550 1.00 89.61  ? 205 SER A C   1 
ATOM   1362 O  O   . SER A 1 227 ? 66.679 103.565 68.038 1.00 90.35  ? 205 SER A O   1 
ATOM   1363 C  CB  . SER A 1 227 ? 69.028 100.797 67.829 1.00 85.08  ? 205 SER A CB  1 
ATOM   1364 O  OG  . SER A 1 227 ? 69.007 100.092 66.598 1.00 82.35  ? 205 SER A OG  1 
ATOM   1365 N  N   . ASP A 1 228 ? 68.177 103.055 66.436 1.00 87.24  ? 206 ASP A N   1 
ATOM   1366 C  CA  . ASP A 1 228 ? 68.033 104.364 65.744 1.00 89.77  ? 206 ASP A CA  1 
ATOM   1367 C  C   . ASP A 1 228 ? 66.677 104.349 65.027 1.00 80.71  ? 206 ASP A C   1 
ATOM   1368 O  O   . ASP A 1 228 ? 66.247 103.292 64.657 1.00 82.36  ? 206 ASP A O   1 
ATOM   1369 C  CB  . ASP A 1 228 ? 69.263 104.617 64.860 1.00 90.29  ? 206 ASP A CB  1 
ATOM   1370 C  CG  . ASP A 1 228 ? 70.440 103.687 65.151 1.00 93.53  ? 206 ASP A CG  1 
ATOM   1371 O  OD1 . ASP A 1 228 ? 70.809 103.544 66.330 1.00 94.77  ? 206 ASP A OD1 1 
ATOM   1372 O  OD2 . ASP A 1 228 ? 70.990 103.117 64.193 1.00 93.55  ? 206 ASP A OD2 1 
ATOM   1373 N  N   . GLN A 1 229 ? 66.010 105.474 64.837 1.00 83.07  ? 207 GLN A N   1 
ATOM   1374 C  CA  . GLN A 1 229 ? 64.681 105.379 64.177 1.00 83.23  ? 207 GLN A CA  1 
ATOM   1375 C  C   . GLN A 1 229 ? 64.793 105.762 62.708 1.00 82.95  ? 207 GLN A C   1 
ATOM   1376 O  O   . GLN A 1 229 ? 63.919 105.397 61.917 1.00 80.45  ? 207 GLN A O   1 
ATOM   1377 C  CB  . GLN A 1 229 ? 63.656 106.309 64.828 1.00 86.01  ? 207 GLN A CB  1 
ATOM   1378 C  CG  . GLN A 1 229 ? 63.114 105.804 66.156 1.00 76.49  ? 207 GLN A CG  1 
ATOM   1379 C  CD  . GLN A 1 229 ? 61.974 106.627 66.693 1.00 73.18  ? 207 GLN A CD  1 
ATOM   1380 O  OE1 . GLN A 1 229 ? 61.125 107.100 65.944 1.00 68.23  ? 207 GLN A OE1 1 
ATOM   1381 N  NE2 . GLN A 1 229 ? 61.950 106.782 68.009 1.00 65.81  ? 207 GLN A NE2 1 
ATOM   1382 N  N   . ASN A 1 230 ? 65.810 106.530 62.361 1.00 84.14  ? 208 ASN A N   1 
ATOM   1383 C  CA  . ASN A 1 230 ? 65.892 106.898 60.954 1.00 85.89  ? 208 ASN A CA  1 
ATOM   1384 C  C   . ASN A 1 230 ? 66.508 105.809 60.086 1.00 82.09  ? 208 ASN A C   1 
ATOM   1385 O  O   . ASN A 1 230 ? 66.222 105.764 58.884 1.00 84.20  ? 208 ASN A O   1 
ATOM   1386 C  CB  . ASN A 1 230 ? 66.701 108.188 60.797 1.00 84.60  ? 208 ASN A CB  1 
ATOM   1387 C  CG  . ASN A 1 230 ? 66.568 108.808 59.414 1.00 87.95  ? 208 ASN A CG  1 
ATOM   1388 O  OD1 . ASN A 1 230 ? 65.767 108.354 58.595 1.00 89.97  ? 208 ASN A OD1 1 
ATOM   1389 N  ND2 . ASN A 1 230 ? 67.360 109.841 59.145 1.00 87.13  ? 208 ASN A ND2 1 
ATOM   1390 N  N   . GLY A 1 231 ? 67.335 104.934 60.655 1.00 81.81  ? 209 GLY A N   1 
ATOM   1391 C  CA  . GLY A 1 231 ? 67.986 103.904 59.868 1.00 82.54  ? 209 GLY A CA  1 
ATOM   1392 C  C   . GLY A 1 231 ? 68.297 102.629 60.626 1.00 79.31  ? 209 GLY A C   1 
ATOM   1393 O  O   . GLY A 1 231 ? 68.940 101.723 60.087 1.00 78.37  ? 209 GLY A O   1 
ATOM   1394 N  N   . GLY A 1 232 ? 67.842 102.542 61.874 1.00 71.41  ? 210 GLY A N   1 
ATOM   1395 C  CA  . GLY A 1 232 ? 68.120 101.370 62.676 1.00 70.35  ? 210 GLY A CA  1 
ATOM   1396 C  C   . GLY A 1 232 ? 67.359 100.145 62.206 1.00 71.44  ? 210 GLY A C   1 
ATOM   1397 O  O   . GLY A 1 232 ? 66.322 100.227 61.546 1.00 66.29  ? 210 GLY A O   1 
ATOM   1398 N  N   . THR A 1 233 ? 67.896 98.979  62.564 1.00 67.06  ? 211 THR A N   1 
ATOM   1399 C  CA  . THR A 1 233 ? 67.258 97.708  62.254 1.00 63.39  ? 211 THR A CA  1 
ATOM   1400 C  C   . THR A 1 233 ? 67.608 96.697  63.338 1.00 64.86  ? 211 THR A C   1 
ATOM   1401 O  O   . THR A 1 233 ? 68.660 96.791  63.977 1.00 68.88  ? 211 THR A O   1 
ATOM   1402 C  CB  . THR A 1 233 ? 67.675 97.180  60.876 1.00 60.99  ? 211 THR A CB  1 
ATOM   1403 O  OG1 . THR A 1 233 ? 67.305 95.800  60.760 1.00 67.32  ? 211 THR A OG1 1 
ATOM   1404 C  CG2 . THR A 1 233 ? 69.177 97.317  60.684 1.00 70.66  ? 211 THR A CG2 1 
ATOM   1405 N  N   . LYS A 1 234 ? 66.713 95.729  63.539 1.00 60.09  ? 212 LYS A N   1 
ATOM   1406 C  CA  . LYS A 1 234 ? 66.862 94.721  64.581 1.00 63.33  ? 212 LYS A CA  1 
ATOM   1407 C  C   . LYS A 1 234 ? 66.512 93.354  64.009 1.00 66.43  ? 212 LYS A C   1 
ATOM   1408 O  O   . LYS A 1 234 ? 65.514 93.208  63.299 1.00 63.45  ? 212 LYS A O   1 
ATOM   1409 C  CB  . LYS A 1 234 ? 65.966 95.045  65.795 1.00 62.20  ? 212 LYS A CB  1 
ATOM   1410 C  CG  . LYS A 1 234 ? 66.121 94.134  67.028 1.00 64.45  ? 212 LYS A CG  1 
ATOM   1411 C  CD  . LYS A 1 234 ? 67.483 93.453  67.111 1.00 76.27  ? 212 LYS A CD  1 
ATOM   1412 C  CE  . LYS A 1 234 ? 67.906 93.088  68.508 1.00 77.54  ? 212 LYS A CE  1 
ATOM   1413 N  NZ  . LYS A 1 234 ? 69.341 92.688  68.483 1.00 77.67  ? 212 LYS A NZ  1 
ATOM   1414 N  N   . THR A 1 235 ? 67.346 92.360  64.315 1.00 64.17  ? 213 THR A N   1 
ATOM   1415 C  CA  . THR A 1 235 ? 67.104 90.964  63.971 1.00 63.06  ? 213 THR A CA  1 
ATOM   1416 C  C   . THR A 1 235 ? 66.953 90.161  65.257 1.00 69.17  ? 213 THR A C   1 
ATOM   1417 O  O   . THR A 1 235 ? 67.897 90.070  66.049 1.00 68.55  ? 213 THR A O   1 
ATOM   1418 C  CB  . THR A 1 235 ? 68.246 90.400  63.122 1.00 52.61  ? 213 THR A CB  1 
ATOM   1419 O  OG1 . THR A 1 235 ? 68.185 90.958  61.804 1.00 60.84  ? 213 THR A OG1 1 
ATOM   1420 C  CG2 . THR A 1 235 ? 68.147 88.885  63.029 1.00 58.20  ? 213 THR A CG2 1 
ATOM   1421 N  N   . LYS A 1 236 ? 65.770 89.586  65.464 1.00 65.78  ? 214 LYS A N   1 
ATOM   1422 C  CA  . LYS A 1 236 ? 65.477 88.717  66.599 1.00 66.52  ? 214 LYS A CA  1 
ATOM   1423 C  C   . LYS A 1 236 ? 65.005 87.356  66.092 1.00 69.07  ? 214 LYS A C   1 
ATOM   1424 O  O   . LYS A 1 236 ? 64.877 87.127  64.887 1.00 59.68  ? 214 LYS A O   1 
ATOM   1425 C  CB  . LYS A 1 236 ? 64.424 89.343  67.520 1.00 66.17  ? 214 LYS A CB  1 
ATOM   1426 C  CG  . LYS A 1 236 ? 64.453 90.862  67.577 1.00 73.06  ? 214 LYS A CG  1 
ATOM   1427 C  CD  . LYS A 1 236 ? 63.152 91.427  68.134 1.00 81.73  ? 214 LYS A CD  1 
ATOM   1428 C  CE  . LYS A 1 236 ? 61.945 90.622  67.672 1.00 69.52  ? 214 LYS A CE  1 
ATOM   1429 N  NZ  . LYS A 1 236 ? 60.670 91.370  67.860 1.00 78.60  ? 214 LYS A NZ  1 
ATOM   1430 N  N   . THR A 1 237 ? 64.751 86.441  67.030 1.00 72.45  ? 215 THR A N   1 
ATOM   1431 C  CA  . THR A 1 237 ? 64.247 85.107  66.720 1.00 72.02  ? 215 THR A CA  1 
ATOM   1432 C  C   . THR A 1 237 ? 63.110 84.761  67.671 1.00 75.26  ? 215 THR A C   1 
ATOM   1433 O  O   . THR A 1 237 ? 63.246 84.922  68.889 1.00 73.03  ? 215 THR A O   1 
ATOM   1434 C  CB  . THR A 1 237 ? 65.348 84.040  66.820 1.00 61.47  ? 215 THR A CB  1 
ATOM   1435 O  OG1 . THR A 1 237 ? 65.721 83.858  68.191 1.00 67.41  ? 215 THR A OG1 1 
ATOM   1436 C  CG2 . THR A 1 237 ? 66.576 84.435  66.008 1.00 61.42  ? 215 THR A CG2 1 
ATOM   1437 N  N   . GLN A 1 238 ? 61.994 84.286  67.116 1.00 82.11  ? 216 GLN A N   1 
ATOM   1438 C  CA  . GLN A 1 238 ? 60.830 83.865  67.895 1.00 80.52  ? 216 GLN A CA  1 
ATOM   1439 C  C   . GLN A 1 238 ? 60.389 82.500  67.384 1.00 82.87  ? 216 GLN A C   1 
ATOM   1440 O  O   . GLN A 1 238 ? 59.941 82.382  66.240 1.00 85.48  ? 216 GLN A O   1 
ATOM   1441 C  CB  . GLN A 1 238 ? 59.687 84.876  67.781 1.00 78.81  ? 216 GLN A CB  1 
ATOM   1442 C  CG  . GLN A 1 238 ? 60.102 86.332  67.899 1.00 83.84  ? 216 GLN A CG  1 
ATOM   1443 C  CD  . GLN A 1 238 ? 59.505 87.194  66.802 1.00 84.60  ? 216 GLN A CD  1 
ATOM   1444 O  OE1 . GLN A 1 238 ? 59.271 86.726  65.688 1.00 83.21  ? 216 GLN A OE1 1 
ATOM   1445 N  NE2 . GLN A 1 238 ? 59.252 88.460  67.116 1.00 73.80  ? 216 GLN A NE2 1 
ATOM   1446 N  N   . THR A 1 239 ? 60.492 81.475  68.225 1.00 82.47  ? 217 THR A N   1 
ATOM   1447 C  CA  . THR A 1 239 ? 60.174 80.117  67.798 1.00 84.63  ? 217 THR A CA  1 
ATOM   1448 C  C   . THR A 1 239 ? 58.662 79.919  67.758 1.00 87.79  ? 217 THR A C   1 
ATOM   1449 O  O   . THR A 1 239 ? 57.993 79.979  68.796 1.00 92.31  ? 217 THR A O   1 
ATOM   1450 C  CB  . THR A 1 239 ? 60.828 79.094  68.724 1.00 83.90  ? 217 THR A CB  1 
ATOM   1451 O  OG1 . THR A 1 239 ? 62.252 79.240  68.665 1.00 81.86  ? 217 THR A OG1 1 
ATOM   1452 C  CG2 . THR A 1 239 ? 60.457 77.682  68.297 1.00 77.63  ? 217 THR A CG2 1 
ATOM   1453 N  N   . ILE A 1 240 ? 58.130 79.673  66.563 1.00 81.54  ? 218 ILE A N   1 
ATOM   1454 C  CA  . ILE A 1 240 ? 56.700 79.480  66.342 1.00 81.13  ? 218 ILE A CA  1 
ATOM   1455 C  C   . ILE A 1 240 ? 56.468 78.021  65.975 1.00 82.92  ? 218 ILE A C   1 
ATOM   1456 O  O   . ILE A 1 240 ? 57.028 77.526  64.989 1.00 81.83  ? 218 ILE A O   1 
ATOM   1457 C  CB  . ILE A 1 240 ? 56.166 80.410  65.240 1.00 78.32  ? 218 ILE A CB  1 
ATOM   1458 C  CG1 . ILE A 1 240 ? 56.019 81.840  65.761 1.00 81.14  ? 218 ILE A CG1 1 
ATOM   1459 C  CG2 . ILE A 1 240 ? 54.834 79.899  64.705 1.00 74.33  ? 218 ILE A CG2 1 
ATOM   1460 C  CD1 . ILE A 1 240 ? 55.443 82.800  64.740 1.00 70.69  ? 218 ILE A CD1 1 
ATOM   1461 N  N   . ASP A 1 241 ? 55.638 77.335  66.766 1.00 88.93  ? 219 ASP A N   1 
ATOM   1462 C  CA  . ASP A 1 241 ? 55.241 75.950  66.493 1.00 85.72  ? 219 ASP A CA  1 
ATOM   1463 C  C   . ASP A 1 241 ? 56.456 75.037  66.335 1.00 87.54  ? 219 ASP A C   1 
ATOM   1464 O  O   . ASP A 1 241 ? 56.463 74.119  65.513 1.00 81.09  ? 219 ASP A O   1 
ATOM   1465 C  CB  . ASP A 1 241 ? 54.339 75.869  65.258 1.00 78.40  ? 219 ASP A CB  1 
ATOM   1466 C  CG  . ASP A 1 241 ? 52.946 76.410  65.516 1.00 82.59  ? 219 ASP A CG  1 
ATOM   1467 O  OD1 . ASP A 1 241 ? 52.819 77.616  65.811 1.00 78.67  ? 219 ASP A OD1 1 
ATOM   1468 O  OD2 . ASP A 1 241 ? 51.976 75.629  65.418 1.00 73.62  ? 219 ASP A OD2 1 
ATOM   1469 N  N   . GLY A 1 242 ? 57.493 75.291  67.130 1.00 92.09  ? 220 GLY A N   1 
ATOM   1470 C  CA  . GLY A 1 242 ? 58.727 74.544  67.030 1.00 87.19  ? 220 GLY A CA  1 
ATOM   1471 C  C   . GLY A 1 242 ? 59.638 74.957  65.895 1.00 84.70  ? 220 GLY A C   1 
ATOM   1472 O  O   . GLY A 1 242 ? 60.675 74.313  65.691 1.00 87.32  ? 220 GLY A O   1 
ATOM   1473 N  N   . LYS A 1 243 ? 59.290 76.003  65.152 1.00 83.24  ? 221 LYS A N   1 
ATOM   1474 C  CA  . LYS A 1 243 ? 60.097 76.483  64.040 1.00 76.16  ? 221 LYS A CA  1 
ATOM   1475 C  C   . LYS A 1 243 ? 60.875 77.722  64.458 1.00 70.90  ? 221 LYS A C   1 
ATOM   1476 O  O   . LYS A 1 243 ? 60.325 78.627  65.092 1.00 69.53  ? 221 LYS A O   1 
ATOM   1477 C  CB  . LYS A 1 243 ? 59.221 76.813  62.830 1.00 69.09  ? 221 LYS A CB  1 
ATOM   1478 C  CG  . LYS A 1 243 ? 58.478 75.627  62.241 1.00 71.96  ? 221 LYS A CG  1 
ATOM   1479 C  CD  . LYS A 1 243 ? 59.311 74.363  62.276 1.00 68.03  ? 221 LYS A CD  1 
ATOM   1480 C  CE  . LYS A 1 243 ? 60.263 74.315  61.098 1.00 77.05  ? 221 LYS A CE  1 
ATOM   1481 N  NZ  . LYS A 1 243 ? 60.227 72.994  60.417 1.00 65.84  ? 221 LYS A NZ  1 
ATOM   1482 N  N   . THR A 1 244 ? 62.153 77.760  64.096 1.00 66.13  ? 222 THR A N   1 
ATOM   1483 C  CA  . THR A 1 244 ? 62.988 78.930  64.351 1.00 70.13  ? 222 THR A CA  1 
ATOM   1484 C  C   . THR A 1 244 ? 62.635 80.009  63.334 1.00 57.94  ? 222 THR A C   1 
ATOM   1485 O  O   . THR A 1 244 ? 62.955 79.882  62.147 1.00 57.70  ? 222 THR A O   1 
ATOM   1486 C  CB  . THR A 1 244 ? 64.467 78.560  64.273 1.00 70.43  ? 222 THR A CB  1 
ATOM   1487 O  OG1 . THR A 1 244 ? 64.765 78.046  62.970 1.00 74.97  ? 222 THR A OG1 1 
ATOM   1488 C  CG2 . THR A 1 244 ? 64.804 77.502  65.313 1.00 64.06  ? 222 THR A CG2 1 
ATOM   1489 N  N   . VAL A 1 245 ? 61.968 81.066  63.791 1.00 47.72  ? 223 VAL A N   1 
ATOM   1490 C  CA  . VAL A 1 245 ? 61.528 82.162  62.935 1.00 45.36  ? 223 VAL A CA  1 
ATOM   1491 C  C   . VAL A 1 245 ? 62.441 83.353  63.181 1.00 56.14  ? 223 VAL A C   1 
ATOM   1492 O  O   . VAL A 1 245 ? 62.553 83.836  64.315 1.00 57.67  ? 223 VAL A O   1 
ATOM   1493 C  CB  . VAL A 1 245 ? 60.060 82.534  63.198 1.00 50.38  ? 223 VAL A CB  1 
ATOM   1494 C  CG1 . VAL A 1 245 ? 59.633 83.692  62.310 1.00 43.83  ? 223 VAL A CG1 1 
ATOM   1495 C  CG2 . VAL A 1 245 ? 59.157 81.324  63.001 1.00 54.18  ? 223 VAL A CG2 1 
ATOM   1496 N  N   . THR A 1 246 ? 63.089 83.830  62.122 1.00 45.50  ? 224 THR A N   1 
ATOM   1497 C  CA  . THR A 1 246 ? 63.959 84.996  62.205 1.00 49.94  ? 224 THR A CA  1 
ATOM   1498 C  C   . THR A 1 246 ? 63.163 86.239  61.826 1.00 47.16  ? 224 THR A C   1 
ATOM   1499 O  O   . THR A 1 246 ? 62.599 86.312  60.728 1.00 42.43  ? 224 THR A O   1 
ATOM   1500 C  CB  . THR A 1 246 ? 65.176 84.835  61.296 1.00 41.75  ? 224 THR A CB  1 
ATOM   1501 O  OG1 . THR A 1 246 ? 66.012 83.786  61.798 1.00 51.16  ? 224 THR A OG1 1 
ATOM   1502 C  CG2 . THR A 1 246 ? 65.975 86.128  61.246 1.00 50.61  ? 224 THR A CG2 1 
ATOM   1503 N  N   . THR A 1 247 ? 63.118 87.210  62.732 1.00 48.68  ? 225 THR A N   1 
ATOM   1504 C  CA  . THR A 1 247 ? 62.368 88.443  62.539 1.00 49.08  ? 225 THR A CA  1 
ATOM   1505 C  C   . THR A 1 247 ? 63.334 89.613  62.422 1.00 50.10  ? 225 THR A C   1 
ATOM   1506 O  O   . THR A 1 247 ? 64.252 89.747  63.238 1.00 53.82  ? 225 THR A O   1 
ATOM   1507 C  CB  . THR A 1 247 ? 61.395 88.676  63.696 1.00 54.66  ? 225 THR A CB  1 
ATOM   1508 O  OG1 . THR A 1 247 ? 60.684 87.463  63.971 1.00 50.96  ? 225 THR A OG1 1 
ATOM   1509 C  CG2 . THR A 1 247 ? 60.403 89.773  63.346 1.00 49.00  ? 225 THR A CG2 1 
ATOM   1510 N  N   . THR A 1 248 ? 63.125 90.453  61.411 1.00 48.72  ? 226 THR A N   1 
ATOM   1511 C  CA  . THR A 1 248 ? 63.966 91.620  61.160 1.00 50.26  ? 226 THR A CA  1 
ATOM   1512 C  C   . THR A 1 248 ? 63.078 92.857  61.119 1.00 49.77  ? 226 THR A C   1 
ATOM   1513 O  O   . THR A 1 248 ? 62.273 93.019  60.195 1.00 45.67  ? 226 THR A O   1 
ATOM   1514 C  CB  . THR A 1 248 ? 64.753 91.466  59.859 1.00 52.32  ? 226 THR A CB  1 
ATOM   1515 O  OG1 . THR A 1 248 ? 65.492 90.239  59.890 1.00 53.54  ? 226 THR A OG1 1 
ATOM   1516 C  CG2 . THR A 1 248 ? 65.720 92.627  59.683 1.00 52.93  ? 226 THR A CG2 1 
ATOM   1517 N  N   . ILE A 1 249 ? 63.226 93.726  62.115 1.00 45.97  ? 227 ILE A N   1 
ATOM   1518 C  CA  . ILE A 1 249 ? 62.448 94.955  62.227 1.00 52.24  ? 227 ILE A CA  1 
ATOM   1519 C  C   . ILE A 1 249 ? 63.346 96.125  61.854 1.00 53.88  ? 227 ILE A C   1 
ATOM   1520 O  O   . ILE A 1 249 ? 64.448 96.266  62.398 1.00 54.84  ? 227 ILE A O   1 
ATOM   1521 C  CB  . ILE A 1 249 ? 61.871 95.134  63.643 1.00 50.17  ? 227 ILE A CB  1 
ATOM   1522 C  CG1 . ILE A 1 249 ? 60.966 93.956  64.007 1.00 57.76  ? 227 ILE A CG1 1 
ATOM   1523 C  CG2 . ILE A 1 249 ? 61.105 96.443  63.745 1.00 43.26  ? 227 ILE A CG2 1 
ATOM   1524 C  CD1 . ILE A 1 249 ? 61.631 92.925  64.890 1.00 60.69  ? 227 ILE A CD1 1 
ATOM   1525 N  N   . SER A 1 250 ? 62.877 96.961  60.932 1.00 51.16  ? 228 SER A N   1 
ATOM   1526 C  CA  . SER A 1 250 ? 63.625 98.117  60.463 1.00 56.86  ? 228 SER A CA  1 
ATOM   1527 C  C   . SER A 1 250 ? 62.814 99.384  60.691 1.00 52.38  ? 228 SER A C   1 
ATOM   1528 O  O   . SER A 1 250 ? 61.583 99.379  60.594 1.00 51.26  ? 228 SER A O   1 
ATOM   1529 C  CB  . SER A 1 250 ? 63.977 97.987  58.976 1.00 42.38  ? 228 SER A CB  1 
ATOM   1530 O  OG  . SER A 1 250 ? 64.918 96.950  58.764 1.00 51.46  ? 228 SER A OG  1 
ATOM   1531 N  N   . SER A 1 251 ? 63.517 100.474 60.990 1.00 63.29  ? 229 SER A N   1 
ATOM   1532 C  CA  . SER A 1 251 ? 62.897 101.766 61.246 1.00 60.64  ? 229 SER A CA  1 
ATOM   1533 C  C   . SER A 1 251 ? 63.501 102.816 60.326 1.00 68.93  ? 229 SER A C   1 
ATOM   1534 O  O   . SER A 1 251 ? 64.718 102.851 60.122 1.00 64.55  ? 229 SER A O   1 
ATOM   1535 C  CB  . SER A 1 251 ? 63.073 102.190 62.709 1.00 66.02  ? 229 SER A CB  1 
ATOM   1536 O  OG  . SER A 1 251 ? 62.177 103.235 63.045 1.00 65.81  ? 229 SER A OG  1 
ATOM   1537 N  N   . LYS A 1 252 ? 62.643 103.676 59.780 1.00 70.53  ? 230 LYS A N   1 
ATOM   1538 C  CA  . LYS A 1 252 ? 63.063 104.712 58.846 1.00 71.78  ? 230 LYS A CA  1 
ATOM   1539 C  C   . LYS A 1 252 ? 62.211 105.952 59.064 1.00 74.50  ? 230 LYS A C   1 
ATOM   1540 O  O   . LYS A 1 252 ? 60.979 105.869 59.057 1.00 70.26  ? 230 LYS A O   1 
ATOM   1541 C  CB  . LYS A 1 252 ? 62.940 104.226 57.396 1.00 67.90  ? 230 LYS A CB  1 
ATOM   1542 C  CG  . LYS A 1 252 ? 63.234 105.286 56.348 1.00 74.53  ? 230 LYS A CG  1 
ATOM   1543 C  CD  . LYS A 1 252 ? 63.512 104.653 54.994 1.00 70.42  ? 230 LYS A CD  1 
ATOM   1544 C  CE  . LYS A 1 252 ? 64.069 105.666 54.008 1.00 71.84  ? 230 LYS A CE  1 
ATOM   1545 N  NZ  . LYS A 1 252 ? 64.057 105.146 52.612 1.00 76.18  ? 230 LYS A NZ  1 
ATOM   1546 N  N   . VAL A 1 253 ? 62.866 107.095 59.257 1.00 77.35  ? 231 VAL A N   1 
ATOM   1547 C  CA  . VAL A 1 253 ? 62.189 108.368 59.481 1.00 73.68  ? 231 VAL A CA  1 
ATOM   1548 C  C   . VAL A 1 253 ? 62.182 109.153 58.178 1.00 69.29  ? 231 VAL A C   1 
ATOM   1549 O  O   . VAL A 1 253 ? 63.227 109.313 57.534 1.00 77.25  ? 231 VAL A O   1 
ATOM   1550 C  CB  . VAL A 1 253 ? 62.867 109.171 60.605 1.00 74.49  ? 231 VAL A CB  1 
ATOM   1551 C  CG1 . VAL A 1 253 ? 62.386 110.615 60.593 1.00 71.24  ? 231 VAL A CG1 1 
ATOM   1552 C  CG2 . VAL A 1 253 ? 62.590 108.531 61.954 1.00 74.48  ? 231 VAL A CG2 1 
ATOM   1553 N  N   . VAL A 1 254 ? 61.008 109.640 57.788 1.00 67.90  ? 232 VAL A N   1 
ATOM   1554 C  CA  . VAL A 1 254 ? 60.833 110.417 56.566 1.00 75.02  ? 232 VAL A CA  1 
ATOM   1555 C  C   . VAL A 1 254 ? 60.326 111.791 56.984 1.00 78.98  ? 232 VAL A C   1 
ATOM   1556 O  O   . VAL A 1 254 ? 59.150 111.950 57.332 1.00 74.97  ? 232 VAL A O   1 
ATOM   1557 C  CB  . VAL A 1 254 ? 59.869 109.744 55.582 1.00 72.33  ? 232 VAL A CB  1 
ATOM   1558 C  CG1 . VAL A 1 254 ? 59.829 110.511 54.269 1.00 73.10  ? 232 VAL A CG1 1 
ATOM   1559 C  CG2 . VAL A 1 254 ? 60.270 108.294 55.350 1.00 68.21  ? 232 VAL A CG2 1 
ATOM   1560 N  N   . ASP A 1 255 ? 61.208 112.788 56.956 1.00 86.59  ? 233 ASP A N   1 
ATOM   1561 C  CA  . ASP A 1 255 ? 60.801 114.145 57.285 1.00 85.50  ? 233 ASP A CA  1 
ATOM   1562 C  C   . ASP A 1 255 ? 59.810 114.667 56.249 1.00 84.01  ? 233 ASP A C   1 
ATOM   1563 O  O   . ASP A 1 255 ? 59.762 114.205 55.105 1.00 80.23  ? 233 ASP A O   1 
ATOM   1564 C  CB  . ASP A 1 255 ? 62.017 115.069 57.369 1.00 91.13  ? 233 ASP A CB  1 
ATOM   1565 C  CG  . ASP A 1 255 ? 61.692 116.402 58.018 1.00 91.60  ? 233 ASP A CG  1 
ATOM   1566 O  OD1 . ASP A 1 255 ? 61.562 116.446 59.259 1.00 94.09  ? 233 ASP A OD1 1 
ATOM   1567 O  OD2 . ASP A 1 255 ? 61.563 117.406 57.288 1.00 91.01  ? 233 ASP A OD2 1 
ATOM   1568 N  N   . SER A 1 256 ? 59.007 115.650 56.669 1.00 83.35  ? 234 SER A N   1 
ATOM   1569 C  CA  . SER A 1 256 ? 57.959 116.177 55.800 1.00 85.52  ? 234 SER A CA  1 
ATOM   1570 C  C   . SER A 1 256 ? 58.529 116.776 54.521 1.00 92.48  ? 234 SER A C   1 
ATOM   1571 O  O   . SER A 1 256 ? 57.836 116.820 53.497 1.00 90.43  ? 234 SER A O   1 
ATOM   1572 C  CB  . SER A 1 256 ? 57.127 117.216 56.552 1.00 80.80  ? 234 SER A CB  1 
ATOM   1573 O  OG  . SER A 1 256 ? 57.940 118.266 57.043 1.00 83.90  ? 234 SER A OG  1 
ATOM   1574 N  N   . GLN A 1 257 ? 59.778 117.238 54.550 1.00 96.95  ? 235 GLN A N   1 
ATOM   1575 C  CA  . GLN A 1 257 ? 60.438 117.748 53.353 1.00 99.13  ? 235 GLN A CA  1 
ATOM   1576 C  C   . GLN A 1 257 ? 61.223 116.606 52.709 1.00 99.11  ? 235 GLN A C   1 
ATOM   1577 O  O   . GLN A 1 257 ? 62.178 116.083 53.295 1.00 100.22 ? 235 GLN A O   1 
ATOM   1578 C  CB  . GLN A 1 257 ? 61.326 118.950 53.684 1.00 103.49 ? 235 GLN A CB  1 
ATOM   1579 C  CG  . GLN A 1 257 ? 62.530 118.675 54.579 1.00 104.58 ? 235 GLN A CG  1 
ATOM   1580 C  CD  . GLN A 1 257 ? 62.899 119.855 55.454 1.00 97.24  ? 235 GLN A CD  1 
ATOM   1581 O  OE1 . GLN A 1 257 ? 62.073 120.725 55.726 1.00 98.72  ? 235 GLN A OE1 1 
ATOM   1582 N  NE2 . GLN A 1 257 ? 64.150 119.891 55.899 1.00 89.81  ? 235 GLN A NE2 1 
ATOM   1583 N  N   . ALA A 1 258 ? 60.796 116.208 51.509 1.00 96.29  ? 236 ALA A N   1 
ATOM   1584 C  CA  . ALA A 1 258 ? 61.416 115.141 50.730 1.00 93.22  ? 236 ALA A CA  1 
ATOM   1585 C  C   . ALA A 1 258 ? 60.635 114.940 49.440 1.00 95.20  ? 236 ALA A C   1 
ATOM   1586 O  O   . ALA A 1 258 ? 59.402 114.881 49.464 1.00 100.39 ? 236 ALA A O   1 
ATOM   1587 C  CB  . ALA A 1 258 ? 61.466 113.825 51.514 1.00 92.25  ? 236 ALA A CB  1 
ATOM   1588 N  N   . LYS A 1 259 ? 61.331 114.838 48.311 1.00 92.05  ? 237 LYS A N   1 
ATOM   1589 C  CA  . LYS A 1 259 ? 60.653 114.565 47.050 1.00 92.50  ? 237 LYS A CA  1 
ATOM   1590 C  C   . LYS A 1 259 ? 60.060 113.163 47.090 1.00 92.84  ? 237 LYS A C   1 
ATOM   1591 O  O   . LYS A 1 259 ? 60.776 112.184 47.326 1.00 95.84  ? 237 LYS A O   1 
ATOM   1592 C  CB  . LYS A 1 259 ? 61.615 114.713 45.874 1.00 90.02  ? 237 LYS A CB  1 
ATOM   1593 C  CG  . LYS A 1 259 ? 60.955 115.271 44.621 1.00 89.24  ? 237 LYS A CG  1 
ATOM   1594 C  CD  . LYS A 1 259 ? 61.567 114.690 43.356 1.00 82.62  ? 237 LYS A CD  1 
ATOM   1595 C  CE  . LYS A 1 259 ? 60.629 114.851 42.167 1.00 81.00  ? 237 LYS A CE  1 
ATOM   1596 N  NZ  . LYS A 1 259 ? 59.400 114.019 42.306 1.00 79.13  ? 237 LYS A NZ  1 
ATOM   1597 N  N   . GLY A 1 260 ? 58.747 113.068 46.871 1.00 92.70  ? 238 GLY A N   1 
ATOM   1598 C  CA  . GLY A 1 260 ? 58.005 111.831 46.991 1.00 91.12  ? 238 GLY A CA  1 
ATOM   1599 C  C   . GLY A 1 260 ? 57.061 111.808 48.178 1.00 88.75  ? 238 GLY A C   1 
ATOM   1600 O  O   . GLY A 1 260 ? 56.010 111.159 48.110 1.00 93.35  ? 238 GLY A O   1 
ATOM   1601 N  N   . ASN A 1 261 ? 57.416 112.499 49.262 1.00 83.79  ? 239 ASN A N   1 
ATOM   1602 C  CA  . ASN A 1 261 ? 56.555 112.616 50.439 1.00 86.00  ? 239 ASN A CA  1 
ATOM   1603 C  C   . ASN A 1 261 ? 55.462 113.634 50.125 1.00 89.70  ? 239 ASN A C   1 
ATOM   1604 O  O   . ASN A 1 261 ? 55.517 114.804 50.514 1.00 93.64  ? 239 ASN A O   1 
ATOM   1605 C  CB  . ASN A 1 261 ? 57.373 113.015 51.661 1.00 81.71  ? 239 ASN A CB  1 
ATOM   1606 C  CG  . ASN A 1 261 ? 56.621 112.812 52.962 1.00 81.38  ? 239 ASN A CG  1 
ATOM   1607 O  OD1 . ASN A 1 261 ? 55.399 112.681 52.972 1.00 76.94  ? 239 ASN A OD1 1 
ATOM   1608 N  ND2 . ASN A 1 261 ? 57.352 112.786 54.070 1.00 81.02  ? 239 ASN A ND2 1 
ATOM   1609 N  N   . THR A 1 262 ? 54.449 113.166 49.388 1.00 89.15  ? 240 THR A N   1 
ATOM   1610 C  CA  . THR A 1 262 ? 53.303 114.021 48.978 1.00 90.82  ? 240 THR A CA  1 
ATOM   1611 C  C   . THR A 1 262 ? 52.401 114.291 50.188 1.00 92.97  ? 240 THR A C   1 
ATOM   1612 O  O   . THR A 1 262 ? 51.555 115.203 50.100 1.00 97.68  ? 240 THR A O   1 
ATOM   1613 C  CB  . THR A 1 262 ? 52.518 113.379 47.826 1.00 92.53  ? 240 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 262 ? 51.649 112.390 48.379 1.00 94.54  ? 240 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 262 ? 53.414 112.748 46.783 1.00 85.76  ? 240 THR A CG2 1 
ATOM   1616 N  N   . THR A 1 263 ? 52.582 113.524 51.268 1.00 92.28  ? 241 THR A N   1 
ATOM   1617 C  CA  . THR A 1 263 ? 51.765 113.694 52.500 1.00 92.50  ? 241 THR A CA  1 
ATOM   1618 C  C   . THR A 1 263 ? 52.213 114.961 53.239 1.00 92.46  ? 241 THR A C   1 
ATOM   1619 O  O   . THR A 1 263 ? 51.381 115.547 53.960 1.00 90.00  ? 241 THR A O   1 
ATOM   1620 C  CB  . THR A 1 263 ? 51.861 112.457 53.401 1.00 93.92  ? 241 THR A CB  1 
ATOM   1621 O  OG1 . THR A 1 263 ? 51.098 112.708 54.582 1.00 94.82  ? 241 THR A OG1 1 
ATOM   1622 C  CG2 . THR A 1 263 ? 53.286 112.111 53.777 1.00 87.63  ? 241 THR A CG2 1 
ATOM   1623 N  N   . ARG A 1 264 ? 53.481 115.351 53.064 1.00 91.77  ? 242 ARG A N   1 
ATOM   1624 C  CA  . ARG A 1 264 ? 54.049 116.560 53.721 1.00 90.93  ? 242 ARG A CA  1 
ATOM   1625 C  C   . ARG A 1 264 ? 53.773 116.501 55.228 1.00 91.22  ? 242 ARG A C   1 
ATOM   1626 O  O   . ARG A 1 264 ? 53.282 117.507 55.778 1.00 93.09  ? 242 ARG A O   1 
ATOM   1627 C  CB  . ARG A 1 264 ? 53.473 117.835 53.096 1.00 91.60  ? 242 ARG A CB  1 
ATOM   1628 C  CG  . ARG A 1 264 ? 54.386 118.492 52.071 1.00 93.68  ? 242 ARG A CG  1 
ATOM   1629 C  CD  . ARG A 1 264 ? 55.409 117.525 51.506 1.00 93.15  ? 242 ARG A CD  1 
ATOM   1630 N  NE  . ARG A 1 264 ? 55.560 117.660 50.064 1.00 95.25  ? 242 ARG A NE  1 
ATOM   1631 C  CZ  . ARG A 1 264 ? 56.686 117.421 49.401 1.00 90.78  ? 242 ARG A CZ  1 
ATOM   1632 N  NH1 . ARG A 1 264 ? 57.768 117.032 50.053 1.00 89.25  ? 242 ARG A NH1 1 
ATOM   1633 N  NH2 . ARG A 1 264 ? 56.725 117.572 48.089 1.00 88.89  ? 242 ARG A NH2 1 
ATOM   1634 N  N   . VAL A 1 265 ? 54.087 115.365 55.859 1.00 86.64  ? 243 VAL A N   1 
ATOM   1635 C  CA  . VAL A 1 265 ? 53.872 115.175 57.325 1.00 78.46  ? 243 VAL A CA  1 
ATOM   1636 C  C   . VAL A 1 265 ? 54.939 114.206 57.848 1.00 72.24  ? 243 VAL A C   1 
ATOM   1637 O  O   . VAL A 1 265 ? 54.760 112.983 57.680 1.00 75.48  ? 243 VAL A O   1 
ATOM   1638 C  CB  . VAL A 1 265 ? 52.451 114.659 57.625 1.00 78.04  ? 243 VAL A CB  1 
ATOM   1639 C  CG1 . VAL A 1 265 ? 52.430 113.731 58.830 1.00 79.71  ? 243 VAL A CG1 1 
ATOM   1640 C  CG2 . VAL A 1 265 ? 51.462 115.800 57.812 1.00 79.93  ? 243 VAL A CG2 1 
ATOM   1641 N  N   . SER A 1 266 ? 56.049 114.708 58.379 1.00 78.54  ? 244 SER A N   1 
ATOM   1642 C  CA  . SER A 1 266 ? 57.161 113.913 58.973 1.00 76.20  ? 244 SER A CA  1 
ATOM   1643 C  C   . SER A 1 266 ? 56.674 112.598 59.609 1.00 72.31  ? 244 SER A C   1 
ATOM   1644 O  O   . SER A 1 266 ? 55.836 112.650 60.503 1.00 70.44  ? 244 SER A O   1 
ATOM   1645 C  CB  . SER A 1 266 ? 57.862 114.736 59.979 1.00 74.81  ? 244 SER A CB  1 
ATOM   1646 O  OG  . SER A 1 266 ? 58.700 113.916 60.767 1.00 85.83  ? 244 SER A OG  1 
ATOM   1647 N  N   . TYR A 1 267 ? 57.070 111.460 59.045 1.00 70.11  ? 245 TYR A N   1 
ATOM   1648 C  CA  . TYR A 1 267 ? 56.533 110.173 59.543 1.00 70.62  ? 245 TYR A CA  1 
ATOM   1649 C  C   . TYR A 1 267 ? 57.574 109.067 59.566 1.00 65.32  ? 245 TYR A C   1 
ATOM   1650 O  O   . TYR A 1 267 ? 58.465 109.029 58.757 1.00 69.15  ? 245 TYR A O   1 
ATOM   1651 C  CB  . TYR A 1 267 ? 55.361 109.733 58.675 1.00 60.19  ? 245 TYR A CB  1 
ATOM   1652 C  CG  . TYR A 1 267 ? 55.742 109.210 57.319 1.00 63.18  ? 245 TYR A CG  1 
ATOM   1653 C  CD1 . TYR A 1 267 ? 56.227 107.932 57.160 1.00 64.97  ? 245 TYR A CD1 1 
ATOM   1654 C  CD2 . TYR A 1 267 ? 55.596 109.978 56.189 1.00 65.22  ? 245 TYR A CD2 1 
ATOM   1655 C  CE1 . TYR A 1 267 ? 56.561 107.433 55.917 1.00 62.87  ? 245 TYR A CE1 1 
ATOM   1656 C  CE2 . TYR A 1 267 ? 55.916 109.494 54.937 1.00 66.20  ? 245 TYR A CE2 1 
ATOM   1657 C  CZ  . TYR A 1 267 ? 56.389 108.209 54.797 1.00 68.39  ? 245 TYR A CZ  1 
ATOM   1658 O  OH  . TYR A 1 267 ? 56.741 107.725 53.579 1.00 69.01  ? 245 TYR A OH  1 
ATOM   1659 N  N   . THR A 1 268 ? 57.411 108.169 60.519 1.00 62.51  ? 246 THR A N   1 
ATOM   1660 C  CA  . THR A 1 268 ? 58.310 107.007 60.617 1.00 64.01  ? 246 THR A CA  1 
ATOM   1661 C  C   . THR A 1 268 ? 57.653 105.826 59.901 1.00 60.57  ? 246 THR A C   1 
ATOM   1662 O  O   . THR A 1 268 ? 56.448 105.842 59.753 1.00 55.73  ? 246 THR A O   1 
ATOM   1663 C  CB  . THR A 1 268 ? 58.594 106.686 62.077 1.00 58.57  ? 246 THR A CB  1 
ATOM   1664 O  OG1 . THR A 1 268 ? 58.853 107.931 62.706 1.00 62.55  ? 246 THR A OG1 1 
ATOM   1665 C  CG2 . THR A 1 268 ? 59.796 105.800 62.234 1.00 65.58  ? 246 THR A CG2 1 
ATOM   1666 N  N   . GLU A 1 269 ? 58.460 104.898 59.414 1.00 59.80  ? 247 GLU A N   1 
ATOM   1667 C  CA  . GLU A 1 269 ? 57.972 103.679 58.783 1.00 55.12  ? 247 GLU A CA  1 
ATOM   1668 C  C   . GLU A 1 269 ? 58.683 102.481 59.391 1.00 55.41  ? 247 GLU A C   1 
ATOM   1669 O  O   . GLU A 1 269 ? 59.917 102.444 59.435 1.00 55.67  ? 247 GLU A O   1 
ATOM   1670 C  CB  . GLU A 1 269 ? 58.186 103.706 57.266 1.00 62.36  ? 247 GLU A CB  1 
ATOM   1671 C  CG  . GLU A 1 269 ? 58.221 102.324 56.628 1.00 53.75  ? 247 GLU A CG  1 
ATOM   1672 C  CD  . GLU A 1 269 ? 58.165 102.376 55.115 1.00 59.58  ? 247 GLU A CD  1 
ATOM   1673 O  OE1 . GLU A 1 269 ? 57.062 102.582 54.567 1.00 65.13  ? 247 GLU A OE1 1 
ATOM   1674 O  OE2 . GLU A 1 269 ? 59.224 102.210 54.474 1.00 63.42  ? 247 GLU A OE2 1 
ATOM   1675 N  N   . ILE A 1 270 ? 57.905 101.507 59.856 1.00 46.22  ? 248 ILE A N   1 
ATOM   1676 C  CA  . ILE A 1 270 ? 58.431 100.272 60.425 1.00 44.44  ? 248 ILE A CA  1 
ATOM   1677 C  C   . ILE A 1 270 ? 58.136 99.144  59.449 1.00 42.46  ? 248 ILE A C   1 
ATOM   1678 O  O   . ILE A 1 270 ? 56.975 98.911  59.092 1.00 38.54  ? 248 ILE A O   1 
ATOM   1679 C  CB  . ILE A 1 270 ? 57.825 99.973  61.803 1.00 45.14  ? 248 ILE A CB  1 
ATOM   1680 C  CG1 . ILE A 1 270 ? 58.086 101.131 62.764 1.00 52.77  ? 248 ILE A CG1 1 
ATOM   1681 C  CG2 . ILE A 1 270 ? 58.394 98.677  62.362 1.00 44.80  ? 248 ILE A CG2 1 
ATOM   1682 C  CD1 . ILE A 1 270 ? 59.547 101.357 63.057 1.00 49.45  ? 248 ILE A CD1 1 
ATOM   1683 N  N   . THR A 1 271 ? 59.184 98.437  59.064 1.00 50.20  ? 249 THR A N   1 
ATOM   1684 C  CA  . THR A 1 271 ? 59.084 97.280  58.146 1.00 47.65  ? 249 THR A CA  1 
ATOM   1685 C  C   . THR A 1 271 ? 59.397 96.028  58.949 1.00 43.40  ? 249 THR A C   1 
ATOM   1686 O  O   . THR A 1 271 ? 60.374 96.016  59.623 1.00 43.84  ? 249 THR A O   1 
ATOM   1687 C  CB  . THR A 1 271 ? 59.942 97.450  56.894 1.00 44.98  ? 249 THR A CB  1 
ATOM   1688 O  OG1 . THR A 1 271 ? 61.272 97.512  57.367 1.00 52.94  ? 249 THR A OG1 1 
ATOM   1689 C  CG2 . THR A 1 271 ? 59.635 98.711  56.140 1.00 40.26  ? 249 THR A CG2 1 
ATOM   1690 N  N   . ASN A 1 272 ? 58.504 95.060  58.888 1.00 37.94  ? 250 ASN A N   1 
ATOM   1691 C  CA  . ASN A 1 272 ? 58.649 93.802  59.640 1.00 41.48  ? 250 ASN A CA  1 
ATOM   1692 C  C   . ASN A 1 272 ? 58.893 92.679  58.648 1.00 36.56  ? 250 ASN A C   1 
ATOM   1693 O  O   . ASN A 1 272 ? 58.102 92.538  57.753 1.00 38.89  ? 250 ASN A O   1 
ATOM   1694 C  CB  . ASN A 1 272 ? 57.414 93.535  60.485 1.00 34.10  ? 250 ASN A CB  1 
ATOM   1695 C  CG  . ASN A 1 272 ? 57.377 94.418  61.699 1.00 45.29  ? 250 ASN A CG  1 
ATOM   1696 O  OD1 . ASN A 1 272 ? 56.991 95.558  61.617 1.00 42.61  ? 250 ASN A OD1 1 
ATOM   1697 N  ND2 . ASN A 1 272 ? 57.815 93.893  62.816 1.00 49.39  ? 250 ASN A ND2 1 
ATOM   1698 N  N   . LYS A 1 273 ? 59.968 91.934  58.836 1.00 41.24  ? 251 LYS A N   1 
ATOM   1699 C  CA  . LYS A 1 273 ? 60.261 90.823  57.911 1.00 38.59  ? 251 LYS A CA  1 
ATOM   1700 C  C   . LYS A 1 273 ? 60.441 89.546  58.713 1.00 41.32  ? 251 LYS A C   1 
ATOM   1701 O  O   . LYS A 1 273 ? 61.343 89.499  59.510 1.00 47.09  ? 251 LYS A O   1 
ATOM   1702 C  CB  . LYS A 1 273 ? 61.459 91.135  57.026 1.00 43.67  ? 251 LYS A CB  1 
ATOM   1703 C  CG  . LYS A 1 273 ? 61.956 89.954  56.211 1.00 47.86  ? 251 LYS A CG  1 
ATOM   1704 C  CD  . LYS A 1 273 ? 63.011 90.330  55.203 1.00 49.42  ? 251 LYS A CD  1 
ATOM   1705 C  CE  . LYS A 1 273 ? 63.200 89.311  54.109 1.00 51.75  ? 251 LYS A CE  1 
ATOM   1706 N  NZ  . LYS A 1 273 ? 62.049 89.312  53.179 1.00 53.72  ? 251 LYS A NZ  1 
ATOM   1707 N  N   . LEU A 1 274 ? 59.575 88.571  58.482 1.00 34.15  ? 252 LEU A N   1 
ATOM   1708 C  CA  . LEU A 1 274 ? 59.608 87.283  59.203 1.00 30.22  ? 252 LEU A CA  1 
ATOM   1709 C  C   . LEU A 1 274 ? 60.074 86.212  58.235 1.00 35.39  ? 252 LEU A C   1 
ATOM   1710 O  O   . LEU A 1 274 ? 59.538 86.131  57.154 1.00 32.15  ? 252 LEU A O   1 
ATOM   1711 C  CB  . LEU A 1 274 ? 58.215 86.933  59.727 1.00 35.02  ? 252 LEU A CB  1 
ATOM   1712 C  CG  . LEU A 1 274 ? 57.678 87.779  60.877 1.00 42.22  ? 252 LEU A CG  1 
ATOM   1713 C  CD1 . LEU A 1 274 ? 57.011 88.999  60.345 1.00 43.83  ? 252 LEU A CD1 1 
ATOM   1714 C  CD2 . LEU A 1 274 ? 56.680 87.008  61.717 1.00 43.52  ? 252 LEU A CD2 1 
ATOM   1715 N  N   A ASP A 1 275 ? 61.171 85.550  58.579 0.70 32.81  ? 253 ASP A N   1 
ATOM   1716 N  N   B ASP A 1 275 ? 61.159 85.546  58.609 0.30 33.17  ? 253 ASP A N   1 
ATOM   1717 C  CA  A ASP A 1 275 ? 61.738 84.504  57.740 0.70 35.68  ? 253 ASP A CA  1 
ATOM   1718 C  CA  B ASP A 1 275 ? 61.782 84.491  57.827 0.30 35.75  ? 253 ASP A CA  1 
ATOM   1719 C  C   A ASP A 1 275 ? 61.544 83.141  58.392 0.70 35.83  ? 253 ASP A C   1 
ATOM   1720 C  C   B ASP A 1 275 ? 61.447 83.137  58.439 0.30 35.83  ? 253 ASP A C   1 
ATOM   1721 O  O   A ASP A 1 275 ? 61.772 82.976  59.594 0.70 37.86  ? 253 ASP A O   1 
ATOM   1722 O  O   B ASP A 1 275 ? 61.483 82.974  59.663 0.30 38.16  ? 253 ASP A O   1 
ATOM   1723 C  CB  A ASP A 1 275 ? 63.226 84.753  57.473 0.70 38.13  ? 253 ASP A CB  1 
ATOM   1724 C  CB  B ASP A 1 275 ? 63.302 84.690  57.784 0.30 38.40  ? 253 ASP A CB  1 
ATOM   1725 C  CG  A ASP A 1 275 ? 63.459 85.866  56.466 0.70 40.23  ? 253 ASP A CG  1 
ATOM   1726 C  CG  B ASP A 1 275 ? 64.024 83.580  57.047 0.30 37.84  ? 253 ASP A CG  1 
ATOM   1727 O  OD1 A ASP A 1 275 ? 62.742 85.907  55.444 0.70 35.77  ? 253 ASP A OD1 1 
ATOM   1728 O  OD1 B ASP A 1 275 ? 64.145 82.462  57.594 0.30 37.08  ? 253 ASP A OD1 1 
ATOM   1729 O  OD2 A ASP A 1 275 ? 64.359 86.700  56.697 0.70 46.19  ? 253 ASP A OD2 1 
ATOM   1730 O  OD2 B ASP A 1 275 ? 64.492 83.835  55.921 0.30 44.44  ? 253 ASP A OD2 1 
ATOM   1731 N  N   . GLY A 1 276 ? 61.122 82.169  57.587 1.00 31.06  ? 254 GLY A N   1 
ATOM   1732 C  CA  . GLY A 1 276 ? 60.893 80.821  58.072 1.00 29.99  ? 254 GLY A CA  1 
ATOM   1733 C  C   . GLY A 1 276 ? 59.596 80.617  58.822 1.00 31.95  ? 254 GLY A C   1 
ATOM   1734 O  O   . GLY A 1 276 ? 59.514 79.720  59.666 1.00 28.92  ? 254 GLY A O   1 
ATOM   1735 N  N   . VAL A 1 277 ? 58.580 81.421  58.537 1.00 32.61  ? 255 VAL A N   1 
ATOM   1736 C  CA  . VAL A 1 277 ? 57.285 81.281  59.216 1.00 29.20  ? 255 VAL A CA  1 
ATOM   1737 C  C   . VAL A 1 277 ? 56.626 79.979  58.772 1.00 31.85  ? 255 VAL A C   1 
ATOM   1738 O  O   . VAL A 1 277 ? 56.503 79.736  57.561 1.00 30.47  ? 255 VAL A O   1 
ATOM   1739 C  CB  . VAL A 1 277 ? 56.391 82.480  58.903 1.00 34.92  ? 255 VAL A CB  1 
ATOM   1740 C  CG1 . VAL A 1 277 ? 54.995 82.276  59.479 1.00 29.81  ? 255 VAL A CG1 1 
ATOM   1741 C  CG2 . VAL A 1 277 ? 57.013 83.749  59.445 1.00 33.47  ? 255 VAL A CG2 1 
ATOM   1742 N  N   . PRO A 1 278 ? 56.170 79.131  59.694 1.00 33.28  ? 256 PRO A N   1 
ATOM   1743 C  CA  . PRO A 1 278 ? 55.573 77.851  59.286 1.00 30.08  ? 256 PRO A CA  1 
ATOM   1744 C  C   . PRO A 1 278 ? 54.282 78.065  58.510 1.00 31.69  ? 256 PRO A C   1 
ATOM   1745 O  O   . PRO A 1 278 ? 53.377 78.771  58.962 1.00 26.85  ? 256 PRO A O   1 
ATOM   1746 C  CB  . PRO A 1 278 ? 55.313 77.130  60.617 1.00 34.20  ? 256 PRO A CB  1 
ATOM   1747 C  CG  . PRO A 1 278 ? 55.966 77.965  61.676 1.00 43.39  ? 256 PRO A CG  1 
ATOM   1748 C  CD  . PRO A 1 278 ? 56.077 79.347  61.146 1.00 36.84  ? 256 PRO A CD  1 
ATOM   1749 N  N   . ASP A 1 279 ? 54.211 77.457  57.330 1.00 31.87  ? 257 ASP A N   1 
ATOM   1750 C  CA  . ASP A 1 279 ? 52.993 77.399  56.525 1.00 32.28  ? 257 ASP A CA  1 
ATOM   1751 C  C   . ASP A 1 279 ? 52.479 75.969  56.654 1.00 40.03  ? 257 ASP A C   1 
ATOM   1752 O  O   . ASP A 1 279 ? 52.840 75.088  55.872 1.00 33.66  ? 257 ASP A O   1 
ATOM   1753 C  CB  . ASP A 1 279 ? 53.259 77.788  55.069 1.00 31.32  ? 257 ASP A CB  1 
ATOM   1754 C  CG  . ASP A 1 279 ? 51.997 77.785  54.216 1.00 39.51  ? 257 ASP A CG  1 
ATOM   1755 O  OD1 . ASP A 1 279 ? 50.890 77.611  54.770 1.00 35.79  ? 257 ASP A OD1 1 
ATOM   1756 O  OD2 . ASP A 1 279 ? 52.112 77.961  52.983 1.00 36.18  ? 257 ASP A OD2 1 
ATOM   1757 N  N   . SER A 1 280 ? 51.648 75.743  57.668 1.00 31.23  ? 258 SER A N   1 
ATOM   1758 C  CA  . SER A 1 280 ? 51.123 74.420  57.965 1.00 31.78  ? 258 SER A CA  1 
ATOM   1759 C  C   . SER A 1 280 ? 49.736 74.575  58.564 1.00 29.49  ? 258 SER A C   1 
ATOM   1760 O  O   . SER A 1 280 ? 49.377 75.639  59.074 1.00 23.08  ? 258 SER A O   1 
ATOM   1761 C  CB  . SER A 1 280 ? 52.039 73.651  58.924 1.00 33.81  ? 258 SER A CB  1 
ATOM   1762 O  OG  . SER A 1 280 ? 51.886 74.120  60.254 1.00 31.64  ? 258 SER A OG  1 
ATOM   1763 N  N   . ALA A 1 281 ? 48.957 73.491  58.498 1.00 22.71  ? 259 ALA A N   1 
ATOM   1764 C  CA  . ALA A 1 281 ? 47.595 73.518  59.024 1.00 23.86  ? 259 ALA A CA  1 
ATOM   1765 C  C   . ALA A 1 281 ? 47.573 73.976  60.477 1.00 28.73  ? 259 ALA A C   1 
ATOM   1766 O  O   . ALA A 1 281 ? 46.851 74.913  60.835 1.00 24.73  ? 259 ALA A O   1 
ATOM   1767 C  CB  . ALA A 1 281 ? 46.954 72.136  58.884 1.00 24.46  ? 259 ALA A CB  1 
ATOM   1768 N  N   . GLN A 1 282 ? 48.381 73.335  61.325 1.00 28.10  ? 260 GLN A N   1 
ATOM   1769 C  CA  . GLN A 1 282 ? 48.402 73.684  62.743 1.00 25.98  ? 260 GLN A CA  1 
ATOM   1770 C  C   . GLN A 1 282 ? 48.864 75.120  62.959 1.00 28.43  ? 260 GLN A C   1 
ATOM   1771 O  O   . GLN A 1 282 ? 48.289 75.848  63.778 1.00 29.76  ? 260 GLN A O   1 
ATOM   1772 C  CB  . GLN A 1 282 ? 49.300 72.707  63.502 1.00 37.54  ? 260 GLN A CB  1 
ATOM   1773 C  CG  . GLN A 1 282 ? 49.622 73.121  64.927 1.00 48.69  ? 260 GLN A CG  1 
ATOM   1774 C  CD  . GLN A 1 282 ? 50.772 72.325  65.514 1.00 63.67  ? 260 GLN A CD  1 
ATOM   1775 O  OE1 . GLN A 1 282 ? 51.917 72.778  65.520 1.00 66.44  ? 260 GLN A OE1 1 
ATOM   1776 N  NE2 . GLN A 1 282 ? 50.472 71.129  66.008 1.00 61.01  ? 260 GLN A NE2 1 
ATOM   1777 N  N   . ALA A 1 283 ? 49.897 75.549  62.230 1.00 30.97  ? 261 ALA A N   1 
ATOM   1778 C  CA  . ALA A 1 283 ? 50.412 76.903  62.411 1.00 32.80  ? 261 ALA A CA  1 
ATOM   1779 C  C   . ALA A 1 283 ? 49.401 77.950  61.959 1.00 28.56  ? 261 ALA A C   1 
ATOM   1780 O  O   . ALA A 1 283 ? 49.214 78.970  62.632 1.00 28.81  ? 261 ALA A O   1 
ATOM   1781 C  CB  . ALA A 1 283 ? 51.731 77.070  61.656 1.00 29.10  ? 261 ALA A CB  1 
ATOM   1782 N  N   . LEU A 1 284 ? 48.737 77.718  60.824 1.00 23.48  ? 262 LEU A N   1 
ATOM   1783 C  CA  . LEU A 1 284 ? 47.797 78.709  60.310 1.00 23.19  ? 262 LEU A CA  1 
ATOM   1784 C  C   . LEU A 1 284 ? 46.521 78.751  61.143 1.00 25.98  ? 262 LEU A C   1 
ATOM   1785 O  O   . LEU A 1 284 ? 45.940 79.825  61.344 1.00 22.91  ? 262 LEU A O   1 
ATOM   1786 C  CB  . LEU A 1 284 ? 47.476 78.420  58.845 1.00 29.45  ? 262 LEU A CB  1 
ATOM   1787 C  CG  . LEU A 1 284 ? 48.603 78.649  57.836 1.00 27.26  ? 262 LEU A CG  1 
ATOM   1788 C  CD1 . LEU A 1 284 ? 48.036 78.779  56.430 1.00 25.68  ? 262 LEU A CD1 1 
ATOM   1789 C  CD2 . LEU A 1 284 ? 49.421 79.880  58.206 1.00 28.00  ? 262 LEU A CD2 1 
ATOM   1790 N  N   . LEU A 1 285 ? 46.064 77.595  61.631 1.00 22.98  ? 263 LEU A N   1 
ATOM   1791 C  CA  . LEU A 1 285 ? 44.900 77.583  62.511 1.00 27.12  ? 263 LEU A CA  1 
ATOM   1792 C  C   . LEU A 1 285 ? 45.163 78.370  63.787 1.00 23.95  ? 263 LEU A C   1 
ATOM   1793 O  O   . LEU A 1 285 ? 44.253 79.019  64.315 1.00 24.81  ? 263 LEU A O   1 
ATOM   1794 C  CB  . LEU A 1 285 ? 44.503 76.145  62.839 1.00 20.18  ? 263 LEU A CB  1 
ATOM   1795 C  CG  . LEU A 1 285 ? 43.800 75.374  61.720 1.00 24.13  ? 263 LEU A CG  1 
ATOM   1796 C  CD1 . LEU A 1 285 ? 43.665 73.901  62.083 1.00 24.50  ? 263 LEU A CD1 1 
ATOM   1797 C  CD2 . LEU A 1 285 ? 42.440 75.985  61.408 1.00 26.77  ? 263 LEU A CD2 1 
ATOM   1798 N  N   . ALA A 1 286 ? 46.400 78.335  64.289 1.00 24.49  ? 264 ALA A N   1 
ATOM   1799 C  CA  . ALA A 1 286 ? 46.754 79.150  65.445 1.00 29.43  ? 264 ALA A CA  1 
ATOM   1800 C  C   . ALA A 1 286 ? 46.707 80.633  65.105 1.00 26.88  ? 264 ALA A C   1 
ATOM   1801 O  O   . ALA A 1 286 ? 46.227 81.444  65.905 1.00 25.20  ? 264 ALA A O   1 
ATOM   1802 C  CB  . ALA A 1 286 ? 48.140 78.758  65.959 1.00 28.37  ? 264 ALA A CB  1 
ATOM   1803 N  N   . GLN A 1 287 ? 47.199 81.006  63.920 1.00 21.67  ? 265 GLN A N   1 
ATOM   1804 C  CA  . GLN A 1 287 ? 47.113 82.399  63.492 1.00 25.36  ? 265 GLN A CA  1 
ATOM   1805 C  C   . GLN A 1 287 ? 45.663 82.831  63.316 1.00 30.68  ? 265 GLN A C   1 
ATOM   1806 O  O   . GLN A 1 287 ? 45.287 83.943  63.705 1.00 28.04  ? 265 GLN A O   1 
ATOM   1807 C  CB  . GLN A 1 287 ? 47.896 82.598  62.194 1.00 26.03  ? 265 GLN A CB  1 
ATOM   1808 C  CG  . GLN A 1 287 ? 49.384 82.296  62.312 1.00 31.11  ? 265 GLN A CG  1 
ATOM   1809 C  CD  . GLN A 1 287 ? 50.116 83.298  63.186 1.00 32.24  ? 265 GLN A CD  1 
ATOM   1810 O  OE1 . GLN A 1 287 ? 49.689 84.443  63.328 1.00 29.28  ? 265 GLN A OE1 1 
ATOM   1811 N  NE2 . GLN A 1 287 ? 51.224 82.869  63.777 1.00 37.51  ? 265 GLN A NE2 1 
ATOM   1812 N  N   . ALA A 1 288 ? 44.832 81.964  62.731 1.00 25.27  ? 266 ALA A N   1 
ATOM   1813 C  CA  . ALA A 1 288 ? 43.412 82.274  62.605 1.00 22.48  ? 266 ALA A CA  1 
ATOM   1814 C  C   . ALA A 1 288 ? 42.759 82.411  63.973 1.00 28.39  ? 266 ALA A C   1 
ATOM   1815 O  O   . ALA A 1 288 ? 41.916 83.291  64.183 1.00 26.54  ? 266 ALA A O   1 
ATOM   1816 C  CB  . ALA A 1 288 ? 42.709 81.198  61.778 1.00 22.55  ? 266 ALA A CB  1 
ATOM   1817 N  N   . SER A 1 289 ? 43.137 81.547  64.919 1.00 25.46  ? 267 SER A N   1 
ATOM   1818 C  CA  . SER A 1 289 ? 42.640 81.678  66.284 1.00 27.00  ? 267 SER A CA  1 
ATOM   1819 C  C   . SER A 1 289 ? 43.029 83.023  66.883 1.00 32.22  ? 267 SER A C   1 
ATOM   1820 O  O   . SER A 1 289 ? 42.207 83.687  67.525 1.00 27.47  ? 267 SER A O   1 
ATOM   1821 C  CB  . SER A 1 289 ? 43.171 80.533  67.146 1.00 27.95  ? 267 SER A CB  1 
ATOM   1822 O  OG  . SER A 1 289 ? 42.724 80.656  68.485 1.00 31.49  ? 267 SER A OG  1 
ATOM   1823 N  N   . THR A 1 290 ? 44.281 83.442  66.679 1.00 28.57  ? 268 THR A N   1 
ATOM   1824 C  CA  . THR A 1 290 ? 44.721 84.740  67.177 1.00 26.88  ? 268 THR A CA  1 
ATOM   1825 C  C   . THR A 1 290 ? 43.914 85.872  66.553 1.00 30.82  ? 268 THR A C   1 
ATOM   1826 O  O   . THR A 1 290 ? 43.542 86.832  67.238 1.00 28.63  ? 268 THR A O   1 
ATOM   1827 C  CB  . THR A 1 290 ? 46.215 84.926  66.901 1.00 28.91  ? 268 THR A CB  1 
ATOM   1828 O  OG1 . THR A 1 290 ? 46.969 84.045  67.742 1.00 29.49  ? 268 THR A OG1 1 
ATOM   1829 C  CG2 . THR A 1 290 ? 46.642 86.362  67.170 1.00 28.88  ? 268 THR A CG2 1 
ATOM   1830 N  N   . LEU A 1 291 ? 43.612 85.763  65.257 1.00 30.07  ? 269 LEU A N   1 
ATOM   1831 C  CA  . LEU A 1 291 ? 42.872 86.817  64.570 1.00 25.65  ? 269 LEU A CA  1 
ATOM   1832 C  C   . LEU A 1 291 ? 41.475 86.989  65.160 1.00 29.40  ? 269 LEU A C   1 
ATOM   1833 O  O   . LEU A 1 291 ? 41.090 88.095  65.558 1.00 28.93  ? 269 LEU A O   1 
ATOM   1834 C  CB  . LEU A 1 291 ? 42.796 86.507  63.073 1.00 25.89  ? 269 LEU A CB  1 
ATOM   1835 C  CG  . LEU A 1 291 ? 41.955 87.426  62.182 1.00 33.59  ? 269 LEU A CG  1 
ATOM   1836 C  CD1 . LEU A 1 291 ? 42.318 88.879  62.405 1.00 34.16  ? 269 LEU A CD1 1 
ATOM   1837 C  CD2 . LEU A 1 291 ? 42.125 87.057  60.714 1.00 31.24  ? 269 LEU A CD2 1 
ATOM   1838 N  N   . ILE A 1 292 ? 40.702 85.903  65.230 1.00 22.71  ? 270 ILE A N   1 
ATOM   1839 C  CA  . ILE A 1 292 ? 39.316 86.020  65.679 1.00 24.79  ? 270 ILE A CA  1 
ATOM   1840 C  C   . ILE A 1 292 ? 39.243 86.340  67.168 1.00 30.67  ? 270 ILE A C   1 
ATOM   1841 O  O   . ILE A 1 292 ? 38.324 87.038  67.613 1.00 28.47  ? 270 ILE A O   1 
ATOM   1842 C  CB  . ILE A 1 292 ? 38.524 84.744  65.331 1.00 31.01  ? 270 ILE A CB  1 
ATOM   1843 C  CG1 . ILE A 1 292 ? 37.020 85.002  65.444 1.00 27.46  ? 270 ILE A CG1 1 
ATOM   1844 C  CG2 . ILE A 1 292 ? 38.934 83.576  66.219 1.00 24.40  ? 270 ILE A CG2 1 
ATOM   1845 C  CD1 . ILE A 1 292 ? 36.502 86.019  64.450 1.00 28.98  ? 270 ILE A CD1 1 
ATOM   1846 N  N   . ASN A 1 293 ? 40.203 85.858  67.961 1.00 29.08  ? 271 ASN A N   1 
ATOM   1847 C  CA  . ASN A 1 293 ? 40.147 86.094  69.399 1.00 32.16  ? 271 ASN A CA  1 
ATOM   1848 C  C   . ASN A 1 293 ? 40.634 87.489  69.768 1.00 39.31  ? 271 ASN A C   1 
ATOM   1849 O  O   . ASN A 1 293 ? 40.170 88.055  70.763 1.00 35.75  ? 271 ASN A O   1 
ATOM   1850 C  CB  . ASN A 1 293 ? 40.954 85.031  70.142 1.00 29.42  ? 271 ASN A CB  1 
ATOM   1851 C  CG  . ASN A 1 293 ? 40.179 83.741  70.328 1.00 32.45  ? 271 ASN A CG  1 
ATOM   1852 O  OD1 . ASN A 1 293 ? 39.058 83.746  70.837 1.00 32.12  ? 271 ASN A OD1 1 
ATOM   1853 N  ND2 . ASN A 1 293 ? 40.769 82.628  69.908 1.00 32.80  ? 271 ASN A ND2 1 
ATOM   1854 N  N   . THR A 1 294 ? 41.561 88.055  68.992 1.00 26.48  ? 272 THR A N   1 
ATOM   1855 C  CA  . THR A 1 294 ? 41.920 89.455  69.191 1.00 23.96  ? 272 THR A CA  1 
ATOM   1856 C  C   . THR A 1 294 ? 40.730 90.361  68.908 1.00 35.30  ? 272 THR A C   1 
ATOM   1857 O  O   . THR A 1 294 ? 40.506 91.348  69.620 1.00 30.22  ? 272 THR A O   1 
ATOM   1858 C  CB  . THR A 1 294 ? 43.105 89.833  68.302 1.00 28.05  ? 272 THR A CB  1 
ATOM   1859 O  OG1 . THR A 1 294 ? 44.209 88.966  68.581 1.00 23.43  ? 272 THR A OG1 1 
ATOM   1860 C  CG2 . THR A 1 294 ? 43.528 91.275  68.555 1.00 34.34  ? 272 THR A CG2 1 
ATOM   1861 N  N   . ILE A 1 295 ? 39.949 90.034  67.876 1.00 30.68  ? 273 ILE A N   1 
ATOM   1862 C  CA  . ILE A 1 295 ? 38.724 90.778  67.599 1.00 31.07  ? 273 ILE A CA  1 
ATOM   1863 C  C   . ILE A 1 295 ? 37.751 90.646  68.762 1.00 37.24  ? 273 ILE A C   1 
ATOM   1864 O  O   . ILE A 1 295 ? 37.145 91.631  69.201 1.00 31.66  ? 273 ILE A O   1 
ATOM   1865 C  CB  . ILE A 1 295 ? 38.095 90.296  66.278 1.00 36.15  ? 273 ILE A CB  1 
ATOM   1866 C  CG1 . ILE A 1 295 ? 39.025 90.590  65.101 1.00 31.85  ? 273 ILE A CG1 1 
ATOM   1867 C  CG2 . ILE A 1 295 ? 36.733 90.942  66.063 1.00 29.52  ? 273 ILE A CG2 1 
ATOM   1868 C  CD1 . ILE A 1 295 ? 38.466 90.153  63.761 1.00 31.94  ? 273 ILE A CD1 1 
ATOM   1869 N  N   . ASN A 1 296 ? 37.594 89.428  69.288 1.00 27.92  ? 274 ASN A N   1 
ATOM   1870 C  CA  . ASN A 1 296 ? 36.645 89.206  70.374 1.00 32.80  ? 274 ASN A CA  1 
ATOM   1871 C  C   . ASN A 1 296 ? 37.123 89.846  71.672 1.00 36.23  ? 274 ASN A C   1 
ATOM   1872 O  O   . ASN A 1 296 ? 36.311 90.355  72.454 1.00 33.63  ? 274 ASN A O   1 
ATOM   1873 C  CB  . ASN A 1 296 ? 36.414 87.707  70.571 1.00 28.89  ? 274 ASN A CB  1 
ATOM   1874 C  CG  . ASN A 1 296 ? 35.200 87.413  71.433 1.00 26.68  ? 274 ASN A CG  1 
ATOM   1875 O  OD1 . ASN A 1 296 ? 34.120 87.959  71.212 1.00 28.84  ? 274 ASN A OD1 1 
ATOM   1876 N  ND2 . ASN A 1 296 ? 35.374 86.547  72.425 1.00 31.10  ? 274 ASN A ND2 1 
ATOM   1877 N  N   . THR A 1 297 ? 38.434 89.830  71.921 1.00 32.34  ? 275 THR A N   1 
ATOM   1878 C  CA  . THR A 1 297 ? 38.963 90.372  73.169 1.00 34.84  ? 275 THR A CA  1 
ATOM   1879 C  C   . THR A 1 297 ? 38.935 91.895  73.167 1.00 40.42  ? 275 THR A C   1 
ATOM   1880 O  O   . THR A 1 297 ? 38.456 92.515  74.121 1.00 35.61  ? 275 THR A O   1 
ATOM   1881 C  CB  . THR A 1 297 ? 40.386 89.865  73.407 1.00 32.75  ? 275 THR A CB  1 
ATOM   1882 O  OG1 . THR A 1 297 ? 40.369 88.438  73.531 1.00 33.96  ? 275 THR A OG1 1 
ATOM   1883 C  CG2 . THR A 1 297 ? 40.962 90.471  74.677 1.00 39.64  ? 275 THR A CG2 1 
ATOM   1884 N  N   . ALA A 1 298 ? 39.440 92.514  72.099 1.00 31.04  ? 276 ALA A N   1 
ATOM   1885 C  CA  . ALA A 1 298 ? 39.391 93.968  72.009 1.00 38.30  ? 276 ALA A CA  1 
ATOM   1886 C  C   . ALA A 1 298 ? 37.956 94.467  71.898 1.00 34.82  ? 276 ALA A C   1 
ATOM   1887 O  O   . ALA A 1 298 ? 37.600 95.483  72.506 1.00 35.37  ? 276 ALA A O   1 
ATOM   1888 C  CB  . ALA A 1 298 ? 40.221 94.452  70.821 1.00 37.76  ? 276 ALA A CB  1 
ATOM   1889 N  N   . CYS A 1 299 ? 37.118 93.764  71.135 1.00 30.47  ? 277 CYS A N   1 
ATOM   1890 C  CA  . CYS A 1 299 ? 35.730 94.130  70.873 1.00 29.89  ? 277 CYS A CA  1 
ATOM   1891 C  C   . CYS A 1 299 ? 35.569 95.652  70.657 1.00 40.03  ? 277 CYS A C   1 
ATOM   1892 O  O   . CYS A 1 299 ? 34.909 96.317  71.450 1.00 38.30  ? 277 CYS A O   1 
ATOM   1893 C  CB  . CYS A 1 299 ? 34.815 93.640  71.992 1.00 30.06  ? 277 CYS A CB  1 
ATOM   1894 S  SG  . CYS A 1 299 ? 33.068 94.023  71.761 1.00 34.54  ? 277 CYS A SG  1 
ATOM   1895 N  N   . PRO A 1 300 ? 36.195 96.204  69.624 1.00 39.26  ? 278 PRO A N   1 
ATOM   1896 C  CA  . PRO A 1 300 ? 36.173 97.661  69.456 1.00 37.72  ? 278 PRO A CA  1 
ATOM   1897 C  C   . PRO A 1 300 ? 34.857 98.137  68.854 1.00 41.61  ? 278 PRO A C   1 
ATOM   1898 O  O   . PRO A 1 300 ? 34.037 97.363  68.356 1.00 35.80  ? 278 PRO A O   1 
ATOM   1899 C  CB  . PRO A 1 300 ? 37.344 97.919  68.513 1.00 37.85  ? 278 PRO A CB  1 
ATOM   1900 C  CG  . PRO A 1 300 ? 37.426 96.693  67.690 1.00 35.15  ? 278 PRO A CG  1 
ATOM   1901 C  CD  . PRO A 1 300 ? 36.922 95.542  68.534 1.00 35.91  ? 278 PRO A CD  1 
ATOM   1902 N  N   . TYR A 1 301 ? 34.669 99.448  68.931 1.00 36.34  ? 279 TYR A N   1 
ATOM   1903 C  CA  . TYR A 1 301 ? 33.533 100.098 68.302 1.00 38.44  ? 279 TYR A CA  1 
ATOM   1904 C  C   . TYR A 1 301 ? 33.684 100.073 66.785 1.00 35.22  ? 279 TYR A C   1 
ATOM   1905 O  O   . TYR A 1 301 ? 34.794 100.103 66.247 1.00 36.85  ? 279 TYR A O   1 
ATOM   1906 C  CB  . TYR A 1 301 ? 33.416 101.540 68.809 1.00 37.03  ? 279 TYR A CB  1 
ATOM   1907 C  CG  . TYR A 1 301 ? 32.342 102.377 68.149 1.00 39.60  ? 279 TYR A CG  1 
ATOM   1908 C  CD1 . TYR A 1 301 ? 31.032 102.348 68.608 1.00 41.42  ? 279 TYR A CD1 1 
ATOM   1909 C  CD2 . TYR A 1 301 ? 32.644 103.212 67.081 1.00 47.59  ? 279 TYR A CD2 1 
ATOM   1910 C  CE1 . TYR A 1 301 ? 30.050 103.119 68.013 1.00 47.65  ? 279 TYR A CE1 1 
ATOM   1911 C  CE2 . TYR A 1 301 ? 31.669 103.985 66.480 1.00 42.55  ? 279 TYR A CE2 1 
ATOM   1912 C  CZ  . TYR A 1 301 ? 30.375 103.935 66.949 1.00 44.61  ? 279 TYR A CZ  1 
ATOM   1913 O  OH  . TYR A 1 301 ? 29.403 104.703 66.353 1.00 56.30  ? 279 TYR A OH  1 
ATOM   1914 N  N   . PHE A 1 302 ? 32.549 100.007 66.091 1.00 35.25  ? 280 PHE A N   1 
ATOM   1915 C  CA  . PHE A 1 302 ? 32.549 100.022 64.635 1.00 40.49  ? 280 PHE A CA  1 
ATOM   1916 C  C   . PHE A 1 302 ? 31.307 100.749 64.140 1.00 40.62  ? 280 PHE A C   1 
ATOM   1917 O  O   . PHE A 1 302 ? 30.288 100.824 64.831 1.00 41.96  ? 280 PHE A O   1 
ATOM   1918 C  CB  . PHE A 1 302 ? 32.606 98.602  64.050 1.00 41.77  ? 280 PHE A CB  1 
ATOM   1919 C  CG  . PHE A 1 302 ? 31.271 97.907  64.010 1.00 37.80  ? 280 PHE A CG  1 
ATOM   1920 C  CD1 . PHE A 1 302 ? 30.811 97.205  65.111 1.00 34.73  ? 280 PHE A CD1 1 
ATOM   1921 C  CD2 . PHE A 1 302 ? 30.479 97.953  62.871 1.00 38.82  ? 280 PHE A CD2 1 
ATOM   1922 C  CE1 . PHE A 1 302 ? 29.585 96.567  65.082 1.00 40.21  ? 280 PHE A CE1 1 
ATOM   1923 C  CE2 . PHE A 1 302 ? 29.251 97.320  62.838 1.00 43.51  ? 280 PHE A CE2 1 
ATOM   1924 C  CZ  . PHE A 1 302 ? 28.804 96.626  63.944 1.00 42.10  ? 280 PHE A CZ  1 
ATOM   1925 N  N   . SER A 1 303 ? 31.405 101.277 62.922 1.00 37.95  ? 281 SER A N   1 
ATOM   1926 C  CA  . SER A 1 303 ? 30.271 101.913 62.257 1.00 51.89  ? 281 SER A CA  1 
ATOM   1927 C  C   . SER A 1 303 ? 30.466 101.775 60.756 1.00 50.48  ? 281 SER A C   1 
ATOM   1928 O  O   . SER A 1 303 ? 31.478 102.235 60.219 1.00 48.76  ? 281 SER A O   1 
ATOM   1929 C  CB  . SER A 1 303 ? 30.145 103.386 62.653 1.00 51.99  ? 281 SER A CB  1 
ATOM   1930 O  OG  . SER A 1 303 ? 30.721 104.230 61.671 1.00 60.66  ? 281 SER A OG  1 
ATOM   1931 N  N   . VAL A 1 304 ? 29.507 101.143 60.086 1.00 53.54  ? 282 VAL A N   1 
ATOM   1932 C  CA  . VAL A 1 304 ? 29.611 100.899 58.652 1.00 55.77  ? 282 VAL A CA  1 
ATOM   1933 C  C   . VAL A 1 304 ? 29.110 102.102 57.861 1.00 54.01  ? 282 VAL A C   1 
ATOM   1934 O  O   . VAL A 1 304 ? 28.501 103.015 58.418 1.00 61.24  ? 282 VAL A O   1 
ATOM   1935 C  CB  . VAL A 1 304 ? 28.842 99.630  58.247 1.00 48.83  ? 282 VAL A CB  1 
ATOM   1936 C  CG1 . VAL A 1 304 ? 29.410 98.414  58.964 1.00 48.25  ? 282 VAL A CG1 1 
ATOM   1937 C  CG2 . VAL A 1 304 ? 27.360 99.791  58.541 1.00 62.86  ? 282 VAL A CG2 1 
ATOM   1938 N  N   . THR A 1 316 ? 24.550 100.553 60.228 1.00 65.54  ? 294 THR A N   1 
ATOM   1939 C  CA  . THR A 1 316 ? 24.592 99.942  61.551 1.00 57.14  ? 294 THR A CA  1 
ATOM   1940 C  C   . THR A 1 316 ? 25.891 100.294 62.272 1.00 57.77  ? 294 THR A C   1 
ATOM   1941 O  O   . THR A 1 316 ? 26.866 100.715 61.648 1.00 57.07  ? 294 THR A O   1 
ATOM   1942 C  CB  . THR A 1 316 ? 24.444 98.406  61.470 1.00 67.00  ? 294 THR A CB  1 
ATOM   1943 O  OG1 . THR A 1 316 ? 23.987 97.899  62.730 1.00 67.10  ? 294 THR A OG1 1 
ATOM   1944 C  CG2 . THR A 1 316 ? 25.770 97.750  61.115 1.00 62.86  ? 294 THR A CG2 1 
ATOM   1945 N  N   . ARG A 1 317 ? 25.893 100.127 63.591 1.00 58.65  ? 295 ARG A N   1 
ATOM   1946 C  CA  . ARG A 1 317 ? 27.062 100.435 64.400 1.00 55.25  ? 295 ARG A CA  1 
ATOM   1947 C  C   . ARG A 1 317 ? 26.975 99.653  65.700 1.00 49.08  ? 295 ARG A C   1 
ATOM   1948 O  O   . ARG A 1 317 ? 25.908 99.165  66.083 1.00 55.21  ? 295 ARG A O   1 
ATOM   1949 C  CB  . ARG A 1 317 ? 27.175 101.938 64.680 1.00 57.23  ? 295 ARG A CB  1 
ATOM   1950 C  CG  . ARG A 1 317 ? 25.970 102.526 65.397 1.00 59.42  ? 295 ARG A CG  1 
ATOM   1951 C  CD  . ARG A 1 317 ? 26.232 103.957 65.842 1.00 64.37  ? 295 ARG A CD  1 
ATOM   1952 N  NE  . ARG A 1 317 ? 26.594 104.823 64.724 1.00 69.97  ? 295 ARG A NE  1 
ATOM   1953 C  CZ  . ARG A 1 317 ? 25.716 105.404 63.913 1.00 70.90  ? 295 ARG A CZ  1 
ATOM   1954 N  NH1 . ARG A 1 317 ? 24.416 105.212 64.093 1.00 67.47  ? 295 ARG A NH1 1 
ATOM   1955 N  NH2 . ARG A 1 317 ? 26.136 106.177 62.921 1.00 73.22  ? 295 ARG A NH2 1 
ATOM   1956 N  N   . GLY A 1 318 ? 28.114 99.539  66.374 1.00 43.71  ? 296 GLY A N   1 
ATOM   1957 C  CA  . GLY A 1 318 ? 28.163 98.835  67.637 1.00 45.23  ? 296 GLY A CA  1 
ATOM   1958 C  C   . GLY A 1 318 ? 29.541 98.315  67.982 1.00 40.67  ? 296 GLY A C   1 
ATOM   1959 O  O   . GLY A 1 318 ? 30.550 98.985  67.741 1.00 40.13  ? 296 GLY A O   1 
ATOM   1960 N  N   . LYS A 1 319 ? 29.593 97.114  68.544 1.00 36.29  ? 297 LYS A N   1 
ATOM   1961 C  CA  . LYS A 1 319 ? 30.835 96.500  68.984 1.00 37.23  ? 297 LYS A CA  1 
ATOM   1962 C  C   . LYS A 1 319 ? 31.113 95.256  68.150 1.00 35.61  ? 297 LYS A C   1 
ATOM   1963 O  O   . LYS A 1 319 ? 30.185 94.546  67.754 1.00 39.13  ? 297 LYS A O   1 
ATOM   1964 C  CB  . LYS A 1 319 ? 30.761 96.141  70.471 1.00 39.49  ? 297 LYS A CB  1 
ATOM   1965 C  CG  . LYS A 1 319 ? 29.684 95.124  70.813 1.00 35.60  ? 297 LYS A CG  1 
ATOM   1966 C  CD  . LYS A 1 319 ? 29.525 94.945  72.314 1.00 36.95  ? 297 LYS A CD  1 
ATOM   1967 C  CE  . LYS A 1 319 ? 28.540 93.826  72.626 1.00 34.85  ? 297 LYS A CE  1 
ATOM   1968 N  NZ  . LYS A 1 319 ? 28.344 93.634  74.090 1.00 35.12  ? 297 LYS A NZ  1 
ATOM   1969 N  N   . LEU A 1 320 ? 32.395 94.993  67.882 1.00 34.61  ? 298 LEU A N   1 
ATOM   1970 C  CA  . LEU A 1 320 ? 32.748 93.869  67.018 1.00 38.89  ? 298 LEU A CA  1 
ATOM   1971 C  C   . LEU A 1 320 ? 32.378 92.539  67.665 1.00 30.60  ? 298 LEU A C   1 
ATOM   1972 O  O   . LEU A 1 320 ? 31.939 91.603  66.985 1.00 38.05  ? 298 LEU A O   1 
ATOM   1973 C  CB  . LEU A 1 320 ? 34.239 93.911  66.682 1.00 37.32  ? 298 LEU A CB  1 
ATOM   1974 C  CG  . LEU A 1 320 ? 34.638 94.761  65.469 1.00 39.19  ? 298 LEU A CG  1 
ATOM   1975 C  CD1 . LEU A 1 320 ? 36.027 94.391  64.963 1.00 32.17  ? 298 LEU A CD1 1 
ATOM   1976 C  CD2 . LEU A 1 320 ? 33.613 94.649  64.346 1.00 37.06  ? 298 LEU A CD2 1 
ATOM   1977 N  N   . CYS A 1 321 ? 32.535 92.434  68.979 1.00 33.56  ? 299 CYS A N   1 
ATOM   1978 C  CA  . CYS A 1 321 ? 32.106 91.205  69.635 1.00 31.38  ? 299 CYS A CA  1 
ATOM   1979 C  C   . CYS A 1 321 ? 30.583 91.068  69.724 1.00 32.49  ? 299 CYS A C   1 
ATOM   1980 O  O   . CYS A 1 321 ? 30.092 90.071  70.273 1.00 40.62  ? 299 CYS A O   1 
ATOM   1981 C  CB  . CYS A 1 321 ? 32.736 91.117  71.023 1.00 33.65  ? 299 CYS A CB  1 
ATOM   1982 S  SG  . CYS A 1 321 ? 32.109 92.297  72.223 1.00 40.55  ? 299 CYS A SG  1 
ATOM   1983 N  N   . GLY A 1 322 ? 29.827 92.033  69.192 1.00 33.85  ? 300 GLY A N   1 
ATOM   1984 C  CA  . GLY A 1 322 ? 28.389 91.881  69.063 1.00 30.70  ? 300 GLY A CA  1 
ATOM   1985 C  C   . GLY A 1 322 ? 27.976 90.941  67.950 1.00 34.83  ? 300 GLY A C   1 
ATOM   1986 O  O   . GLY A 1 322 ? 26.831 90.475  67.936 1.00 33.56  ? 300 GLY A O   1 
ATOM   1987 N  N   . PHE A 1 323 ? 28.881 90.656  67.012 1.00 33.02  ? 301 PHE A N   1 
ATOM   1988 C  CA  . PHE A 1 323 ? 28.668 89.610  66.014 1.00 31.71  ? 301 PHE A CA  1 
ATOM   1989 C  C   . PHE A 1 323 ? 28.893 88.245  66.665 1.00 32.28  ? 301 PHE A C   1 
ATOM   1990 O  O   . PHE A 1 323 ? 29.802 87.488  66.324 1.00 32.82  ? 301 PHE A O   1 
ATOM   1991 C  CB  . PHE A 1 323 ? 29.582 89.820  64.814 1.00 32.71  ? 301 PHE A CB  1 
ATOM   1992 C  CG  . PHE A 1 323 ? 29.282 91.067  64.037 1.00 34.36  ? 301 PHE A CG  1 
ATOM   1993 C  CD1 . PHE A 1 323 ? 28.260 91.089  63.102 1.00 38.69  ? 301 PHE A CD1 1 
ATOM   1994 C  CD2 . PHE A 1 323 ? 30.015 92.222  64.248 1.00 36.79  ? 301 PHE A CD2 1 
ATOM   1995 C  CE1 . PHE A 1 323 ? 27.978 92.238  62.389 1.00 32.39  ? 301 PHE A CE1 1 
ATOM   1996 C  CE2 . PHE A 1 323 ? 29.739 93.374  63.538 1.00 36.88  ? 301 PHE A CE2 1 
ATOM   1997 C  CZ  . PHE A 1 323 ? 28.718 93.382  62.608 1.00 31.29  ? 301 PHE A CZ  1 
ATOM   1998 N  N   . THR A 1 324 ? 28.027 87.950  67.634 1.00 26.34  ? 302 THR A N   1 
ATOM   1999 C  CA  . THR A 1 324 ? 28.245 86.810  68.516 1.00 26.68  ? 302 THR A CA  1 
ATOM   2000 C  C   . THR A 1 324 ? 28.072 85.489  67.777 1.00 33.76  ? 302 THR A C   1 
ATOM   2001 O  O   . THR A 1 324 ? 28.793 84.520  68.046 1.00 28.74  ? 302 THR A O   1 
ATOM   2002 C  CB  . THR A 1 324 ? 27.291 86.896  69.706 1.00 36.82  ? 302 THR A CB  1 
ATOM   2003 O  OG1 . THR A 1 324 ? 25.939 86.943  69.235 1.00 32.52  ? 302 THR A OG1 1 
ATOM   2004 C  CG2 . THR A 1 324 ? 27.574 88.142  70.528 1.00 33.90  ? 302 THR A CG2 1 
ATOM   2005 N  N   . GLU A 1 325 ? 27.124 85.430  66.841 1.00 31.29  ? 303 GLU A N   1 
ATOM   2006 C  CA  . GLU A 1 325 ? 26.922 84.208  66.072 1.00 32.69  ? 303 GLU A CA  1 
ATOM   2007 C  C   . GLU A 1 325 ? 28.101 83.935  65.150 1.00 30.55  ? 303 GLU A C   1 
ATOM   2008 O  O   . GLU A 1 325 ? 28.546 82.788  65.020 1.00 29.75  ? 303 GLU A O   1 
ATOM   2009 C  CB  . GLU A 1 325 ? 25.636 84.310  65.261 1.00 36.06  ? 303 GLU A CB  1 
ATOM   2010 C  CG  . GLU A 1 325 ? 24.381 84.183  66.082 1.00 44.41  ? 303 GLU A CG  1 
ATOM   2011 C  CD  . GLU A 1 325 ? 23.226 83.683  65.254 1.00 50.00  ? 303 GLU A CD  1 
ATOM   2012 O  OE1 . GLU A 1 325 ? 22.495 84.525  64.692 1.00 48.98  ? 303 GLU A OE1 1 
ATOM   2013 O  OE2 . GLU A 1 325 ? 23.065 82.449  65.152 1.00 59.02  ? 303 GLU A OE2 1 
ATOM   2014 N  N   . GLU A 1 326 ? 28.610 84.978  64.494 1.00 28.18  ? 304 GLU A N   1 
ATOM   2015 C  CA  . GLU A 1 326 ? 29.735 84.809  63.584 1.00 32.54  ? 304 GLU A CA  1 
ATOM   2016 C  C   . GLU A 1 326 ? 30.993 84.393  64.334 1.00 29.21  ? 304 GLU A C   1 
ATOM   2017 O  O   . GLU A 1 326 ? 31.716 83.492  63.893 1.00 26.47  ? 304 GLU A O   1 
ATOM   2018 C  CB  . GLU A 1 326 ? 29.969 86.106  62.807 1.00 27.11  ? 304 GLU A CB  1 
ATOM   2019 C  CG  . GLU A 1 326 ? 28.882 86.427  61.786 1.00 31.76  ? 304 GLU A CG  1 
ATOM   2020 C  CD  . GLU A 1 326 ? 27.645 87.053  62.410 1.00 40.12  ? 304 GLU A CD  1 
ATOM   2021 O  OE1 . GLU A 1 326 ? 27.702 87.451  63.594 1.00 30.67  ? 304 GLU A OE1 1 
ATOM   2022 O  OE2 . GLU A 1 326 ? 26.611 87.144  61.715 1.00 34.06  ? 304 GLU A OE2 1 
ATOM   2023 N  N   . ILE A 1 327 ? 31.262 85.027  65.479 1.00 28.03  ? 305 ILE A N   1 
ATOM   2024 C  CA  . ILE A 1 327 ? 32.466 84.712  66.241 1.00 27.66  ? 305 ILE A CA  1 
ATOM   2025 C  C   . ILE A 1 327 ? 32.382 83.305  66.822 1.00 26.01  ? 305 ILE A C   1 
ATOM   2026 O  O   . ILE A 1 327 ? 33.365 82.554  66.805 1.00 25.04  ? 305 ILE A O   1 
ATOM   2027 C  CB  . ILE A 1 327 ? 32.694 85.768  67.338 1.00 25.87  ? 305 ILE A CB  1 
ATOM   2028 C  CG1 . ILE A 1 327 ? 32.972 87.135  66.711 1.00 26.40  ? 305 ILE A CG1 1 
ATOM   2029 C  CG2 . ILE A 1 327 ? 33.839 85.357  68.251 1.00 28.24  ? 305 ILE A CG2 1 
ATOM   2030 C  CD1 . ILE A 1 327 ? 33.053 88.259  67.716 1.00 32.49  ? 305 ILE A CD1 1 
ATOM   2031 N  N   . SER A 1 328 ? 31.213 82.926  67.346 1.00 24.36  ? 306 SER A N   1 
ATOM   2032 C  CA  . SER A 1 328 ? 31.043 81.576  67.876 1.00 27.60  ? 306 SER A CA  1 
ATOM   2033 C  C   . SER A 1 328 ? 31.269 80.530  66.794 1.00 26.18  ? 306 SER A C   1 
ATOM   2034 O  O   . SER A 1 328 ? 31.878 79.483  67.046 1.00 25.94  ? 306 SER A O   1 
ATOM   2035 C  CB  . SER A 1 328 ? 29.648 81.421  68.485 1.00 33.90  ? 306 SER A CB  1 
ATOM   2036 O  OG  . SER A 1 328 ? 29.513 80.167  69.131 1.00 38.30  ? 306 SER A OG  1 
ATOM   2037 N  N   . ALA A 1 329 ? 30.784 80.800  65.581 1.00 26.18  ? 307 ALA A N   1 
ATOM   2038 C  CA  . ALA A 1 329 ? 30.966 79.861  64.482 1.00 32.28  ? 307 ALA A CA  1 
ATOM   2039 C  C   . ALA A 1 329 ? 32.435 79.733  64.098 1.00 25.94  ? 307 ALA A C   1 
ATOM   2040 O  O   . ALA A 1 329 ? 32.931 78.621  63.878 1.00 27.76  ? 307 ALA A O   1 
ATOM   2041 C  CB  . ALA A 1 329 ? 30.132 80.300  63.279 1.00 25.05  ? 307 ALA A CB  1 
ATOM   2042 N  N   . ILE A 1 330 ? 33.149 80.857  64.020 1.00 25.82  ? 308 ILE A N   1 
ATOM   2043 C  CA  . ILE A 1 330 ? 34.548 80.819  63.606 1.00 27.93  ? 308 ILE A CA  1 
ATOM   2044 C  C   . ILE A 1 330 ? 35.406 80.150  64.672 1.00 25.88  ? 308 ILE A C   1 
ATOM   2045 O  O   . ILE A 1 330 ? 36.314 79.372  64.357 1.00 23.30  ? 308 ILE A O   1 
ATOM   2046 C  CB  . ILE A 1 330 ? 35.042 82.237  63.270 1.00 25.22  ? 308 ILE A CB  1 
ATOM   2047 C  CG1 . ILE A 1 330 ? 34.310 82.763  62.033 1.00 28.18  ? 308 ILE A CG1 1 
ATOM   2048 C  CG2 . ILE A 1 330 ? 36.544 82.244  63.029 1.00 26.00  ? 308 ILE A CG2 1 
ATOM   2049 C  CD1 . ILE A 1 330 ? 34.369 84.264  61.875 1.00 28.14  ? 308 ILE A CD1 1 
ATOM   2050 N  N   . GLN A 1 331 ? 35.130 80.430  65.949 1.00 24.49  ? 309 GLN A N   1 
ATOM   2051 C  CA  . GLN A 1 331 ? 35.851 79.757  67.025 1.00 27.93  ? 309 GLN A CA  1 
ATOM   2052 C  C   . GLN A 1 331 ? 35.616 78.252  66.987 1.00 28.74  ? 309 GLN A C   1 
ATOM   2053 O  O   . GLN A 1 331 ? 36.542 77.465  67.213 1.00 29.74  ? 309 GLN A O   1 
ATOM   2054 C  CB  . GLN A 1 331 ? 35.430 80.329  68.380 1.00 22.59  ? 309 GLN A CB  1 
ATOM   2055 C  CG  . GLN A 1 331 ? 35.963 81.726  68.666 1.00 23.42  ? 309 GLN A CG  1 
ATOM   2056 C  CD  . GLN A 1 331 ? 35.468 82.274  69.990 1.00 28.96  ? 309 GLN A CD  1 
ATOM   2057 O  OE1 . GLN A 1 331 ? 34.313 82.070  70.364 1.00 34.05  ? 309 GLN A OE1 1 
ATOM   2058 N  NE2 . GLN A 1 331 ? 36.342 82.972  70.708 1.00 28.07  ? 309 GLN A NE2 1 
ATOM   2059 N  N   . LYS A 1 332 ? 34.381 77.835  66.699 1.00 26.01  ? 310 LYS A N   1 
ATOM   2060 C  CA  . LYS A 1 332 ? 34.077 76.409  66.636 1.00 30.12  ? 310 LYS A CA  1 
ATOM   2061 C  C   . LYS A 1 332 ? 34.748 75.751  65.436 1.00 25.54  ? 310 LYS A C   1 
ATOM   2062 O  O   . LYS A 1 332 ? 35.290 74.646  65.551 1.00 27.21  ? 310 LYS A O   1 
ATOM   2063 C  CB  . LYS A 1 332 ? 32.563 76.201  66.589 1.00 29.08  ? 310 LYS A CB  1 
ATOM   2064 C  CG  . LYS A 1 332 ? 32.139 74.752  66.404 1.00 30.48  ? 310 LYS A CG  1 
ATOM   2065 C  CD  . LYS A 1 332 ? 30.633 74.639  66.219 1.00 37.32  ? 310 LYS A CD  1 
ATOM   2066 C  CE  . LYS A 1 332 ? 30.255 73.337  65.531 1.00 49.57  ? 310 LYS A CE  1 
ATOM   2067 N  NZ  . LYS A 1 332 ? 28.843 73.351  65.055 1.00 54.47  ? 310 LYS A NZ  1 
ATOM   2068 N  N   . MET A 1 333 ? 34.723 76.414  64.277 1.00 21.48  ? 311 MET A N   1 
ATOM   2069 C  CA  . MET A 1 333 ? 35.353 75.849  63.087 1.00 23.35  ? 311 MET A CA  1 
ATOM   2070 C  C   . MET A 1 333 ? 36.858 75.706  63.274 1.00 23.88  ? 311 MET A C   1 
ATOM   2071 O  O   . MET A 1 333 ? 37.446 74.690  62.883 1.00 25.42  ? 311 MET A O   1 
ATOM   2072 C  CB  . MET A 1 333 ? 35.046 76.717  61.867 1.00 23.97  ? 311 MET A CB  1 
ATOM   2073 C  CG  . MET A 1 333 ? 33.595 76.663  61.413 1.00 28.23  ? 311 MET A CG  1 
ATOM   2074 S  SD  . MET A 1 333 ? 33.289 77.672  59.948 1.00 42.88  ? 311 MET A SD  1 
ATOM   2075 C  CE  . MET A 1 333 ? 33.263 79.313  60.649 1.00 36.15  ? 311 MET A CE  1 
ATOM   2076 N  N   . ILE A 1 334 ? 37.500 76.714  63.869 1.00 25.72  ? 312 ILE A N   1 
ATOM   2077 C  CA  . ILE A 1 334 ? 38.936 76.631  64.121 1.00 27.31  ? 312 ILE A CA  1 
ATOM   2078 C  C   . ILE A 1 334 ? 39.237 75.518  65.116 1.00 26.63  ? 312 ILE A C   1 
ATOM   2079 O  O   . ILE A 1 334 ? 40.181 74.739  64.933 1.00 26.63  ? 312 ILE A O   1 
ATOM   2080 C  CB  . ILE A 1 334 ? 39.473 77.991  64.608 1.00 26.31  ? 312 ILE A CB  1 
ATOM   2081 C  CG1 . ILE A 1 334 ? 39.375 79.035  63.492 1.00 24.66  ? 312 ILE A CG1 1 
ATOM   2082 C  CG2 . ILE A 1 334 ? 40.910 77.859  65.085 1.00 26.42  ? 312 ILE A CG2 1 
ATOM   2083 C  CD1 . ILE A 1 334 ? 39.703 80.445  63.941 1.00 22.67  ? 312 ILE A CD1 1 
ATOM   2084 N  N   . THR A 1 335 ? 38.432 75.416  66.178 1.00 23.53  ? 313 THR A N   1 
ATOM   2085 C  CA  . THR A 1 335 ? 38.637 74.367  67.173 1.00 28.35  ? 313 THR A CA  1 
ATOM   2086 C  C   . THR A 1 335 ? 38.426 72.985  66.566 1.00 25.56  ? 313 THR A C   1 
ATOM   2087 O  O   . THR A 1 335 ? 39.229 72.070  66.782 1.00 24.08  ? 313 THR A O   1 
ATOM   2088 C  CB  . THR A 1 335 ? 37.698 74.580  68.362 1.00 26.57  ? 313 THR A CB  1 
ATOM   2089 O  OG1 . THR A 1 335 ? 37.989 75.837  68.983 1.00 36.67  ? 313 THR A OG1 1 
ATOM   2090 C  CG2 . THR A 1 335 ? 37.868 73.465  69.386 1.00 29.52  ? 313 THR A CG2 1 
ATOM   2091 N  N   . ASP A 1 336 ? 37.341 72.814  65.802 1.00 22.98  ? 314 ASP A N   1 
ATOM   2092 C  CA  . ASP A 1 336 ? 37.100 71.540  65.131 1.00 25.74  ? 314 ASP A CA  1 
ATOM   2093 C  C   . ASP A 1 336 ? 38.229 71.202  64.167 1.00 22.24  ? 314 ASP A C   1 
ATOM   2094 O  O   . ASP A 1 336 ? 38.644 70.042  64.065 1.00 24.87  ? 314 ASP A O   1 
ATOM   2095 C  CB  . ASP A 1 336 ? 35.766 71.579  64.384 1.00 24.61  ? 314 ASP A CB  1 
ATOM   2096 C  CG  . ASP A 1 336 ? 34.573 71.497  65.312 1.00 29.29  ? 314 ASP A CG  1 
ATOM   2097 O  OD1 . ASP A 1 336 ? 34.774 71.322  66.532 1.00 27.90  ? 314 ASP A OD1 1 
ATOM   2098 O  OD2 . ASP A 1 336 ? 33.432 71.610  64.818 1.00 31.74  ? 314 ASP A OD2 1 
ATOM   2099 N  N   . ALA A 1 337 ? 38.733 72.206  63.443 1.00 24.65  ? 315 ALA A N   1 
ATOM   2100 C  CA  . ALA A 1 337 ? 39.813 71.967  62.493 1.00 29.15  ? 315 ALA A CA  1 
ATOM   2101 C  C   . ALA A 1 337 ? 41.098 71.567  63.206 1.00 25.26  ? 315 ALA A C   1 
ATOM   2102 O  O   . ALA A 1 337 ? 41.828 70.689  62.733 1.00 25.14  ? 315 ALA A O   1 
ATOM   2103 C  CB  . ALA A 1 337 ? 40.038 73.208  61.630 1.00 22.49  ? 315 ALA A CB  1 
ATOM   2104 N  N   . GLN A 1 338 ? 41.392 72.202  64.344 1.00 24.56  ? 316 GLN A N   1 
ATOM   2105 C  CA  . GLN A 1 338 ? 42.570 71.823  65.119 1.00 27.15  ? 316 GLN A CA  1 
ATOM   2106 C  C   . GLN A 1 338 ? 42.452 70.393  65.625 1.00 29.12  ? 316 GLN A C   1 
ATOM   2107 O  O   . GLN A 1 338 ? 43.418 69.623  65.570 1.00 26.00  ? 316 GLN A O   1 
ATOM   2108 C  CB  . GLN A 1 338 ? 42.763 72.788  66.289 1.00 20.89  ? 316 GLN A CB  1 
ATOM   2109 C  CG  . GLN A 1 338 ? 43.214 74.179  65.881 1.00 26.26  ? 316 GLN A CG  1 
ATOM   2110 C  CD  . GLN A 1 338 ? 43.147 75.168  67.028 1.00 31.97  ? 316 GLN A CD  1 
ATOM   2111 O  OE1 . GLN A 1 338 ? 42.214 75.142  67.831 1.00 31.13  ? 316 GLN A OE1 1 
ATOM   2112 N  NE2 . GLN A 1 338 ? 44.140 76.046  67.112 1.00 29.32  ? 316 GLN A NE2 1 
ATOM   2113 N  N   . GLU A 1 339 ? 41.272 70.021  66.125 1.00 25.22  ? 317 GLU A N   1 
ATOM   2114 C  CA  . GLU A 1 339 ? 41.055 68.649  66.568 1.00 29.05  ? 317 GLU A CA  1 
ATOM   2115 C  C   . GLU A 1 339 ? 41.131 67.679  65.397 1.00 28.67  ? 317 GLU A C   1 
ATOM   2116 O  O   . GLU A 1 339 ? 41.623 66.553  65.542 1.00 25.65  ? 317 GLU A O   1 
ATOM   2117 C  CB  . GLU A 1 339 ? 39.706 68.545  67.278 1.00 27.78  ? 317 GLU A CB  1 
ATOM   2118 C  CG  . GLU A 1 339 ? 39.321 67.140  67.691 1.00 34.38  ? 317 GLU A CG  1 
ATOM   2119 C  CD  . GLU A 1 339 ? 40.194 66.593  68.800 1.00 45.28  ? 317 GLU A CD  1 
ATOM   2120 O  OE1 . GLU A 1 339 ? 40.976 67.368  69.391 1.00 43.56  ? 317 GLU A OE1 1 
ATOM   2121 O  OE2 . GLU A 1 339 ? 40.096 65.383  69.082 1.00 53.34  ? 317 GLU A OE2 1 
ATOM   2122 N  N   . LEU A 1 340 ? 40.649 68.105  64.229 1.00 31.01  ? 318 LEU A N   1 
ATOM   2123 C  CA  . LEU A 1 340 ? 40.777 67.305  63.017 1.00 26.28  ? 318 LEU A CA  1 
ATOM   2124 C  C   . LEU A 1 340 ? 42.243 67.049  62.686 1.00 31.03  ? 318 LEU A C   1 
ATOM   2125 O  O   . LEU A 1 340 ? 42.639 65.916  62.389 1.00 27.37  ? 318 LEU A O   1 
ATOM   2126 C  CB  . LEU A 1 340 ? 40.065 68.025  61.869 1.00 32.79  ? 318 LEU A CB  1 
ATOM   2127 C  CG  . LEU A 1 340 ? 40.104 67.534  60.424 1.00 35.61  ? 318 LEU A CG  1 
ATOM   2128 C  CD1 . LEU A 1 340 ? 38.821 67.950  59.732 1.00 37.41  ? 318 LEU A CD1 1 
ATOM   2129 C  CD2 . LEU A 1 340 ? 41.302 68.107  59.688 1.00 32.62  ? 318 LEU A CD2 1 
ATOM   2130 N  N   . VAL A 1 341 ? 43.067 68.099  62.739 1.00 25.43  ? 319 VAL A N   1 
ATOM   2131 C  CA  . VAL A 1 341 ? 44.487 67.962  62.431 1.00 28.19  ? 319 VAL A CA  1 
ATOM   2132 C  C   . VAL A 1 341 ? 45.191 67.108  63.479 1.00 29.58  ? 319 VAL A C   1 
ATOM   2133 O  O   . VAL A 1 341 ? 46.123 66.360  63.157 1.00 26.25  ? 319 VAL A O   1 
ATOM   2134 C  CB  . VAL A 1 341 ? 45.131 69.356  62.300 1.00 28.94  ? 319 VAL A CB  1 
ATOM   2135 C  CG1 . VAL A 1 341 ? 46.646 69.253  62.179 1.00 29.30  ? 319 VAL A CG1 1 
ATOM   2136 C  CG2 . VAL A 1 341 ? 44.555 70.088  61.103 1.00 27.32  ? 319 VAL A CG2 1 
ATOM   2137 N  N   . ASN A 1 342 ? 44.754 67.188  64.741 1.00 26.09  ? 320 ASN A N   1 
ATOM   2138 C  CA  . ASN A 1 342 ? 45.357 66.374  65.793 1.00 29.14  ? 320 ASN A CA  1 
ATOM   2139 C  C   . ASN A 1 342 ? 45.255 64.885  65.488 1.00 31.52  ? 320 ASN A C   1 
ATOM   2140 O  O   . ASN A 1 342 ? 46.078 64.096  65.966 1.00 32.94  ? 320 ASN A O   1 
ATOM   2141 C  CB  . ASN A 1 342 ? 44.696 66.675  67.139 1.00 30.89  ? 320 ASN A CB  1 
ATOM   2142 C  CG  . ASN A 1 342 ? 45.136 68.001  67.726 1.00 39.38  ? 320 ASN A CG  1 
ATOM   2143 O  OD1 . ASN A 1 342 ? 46.122 68.593  67.287 1.00 42.39  ? 320 ASN A OD1 1 
ATOM   2144 N  ND2 . ASN A 1 342 ? 44.405 68.473  68.729 1.00 42.13  ? 320 ASN A ND2 1 
ATOM   2145 N  N   . GLN A 1 343 ? 44.261 64.481  64.695 1.00 28.82  ? 321 GLN A N   1 
ATOM   2146 C  CA  . GLN A 1 343 ? 44.074 63.066  64.397 1.00 28.58  ? 321 GLN A CA  1 
ATOM   2147 C  C   . GLN A 1 343 ? 45.137 62.518  63.456 1.00 33.98  ? 321 GLN A C   1 
ATOM   2148 O  O   . GLN A 1 343 ? 45.272 61.294  63.346 1.00 35.05  ? 321 GLN A O   1 
ATOM   2149 C  CB  . GLN A 1 343 ? 42.688 62.835  63.794 1.00 27.14  ? 321 GLN A CB  1 
ATOM   2150 C  CG  . GLN A 1 343 ? 41.544 63.386  64.626 1.00 32.61  ? 321 GLN A CG  1 
ATOM   2151 C  CD  . GLN A 1 343 ? 41.439 62.717  65.981 1.00 37.17  ? 321 GLN A CD  1 
ATOM   2152 O  OE1 . GLN A 1 343 ? 41.468 63.380  67.018 1.00 36.82  ? 321 GLN A OE1 1 
ATOM   2153 N  NE2 . GLN A 1 343 ? 41.318 61.395  65.979 1.00 31.49  ? 321 GLN A NE2 1 
ATOM   2154 N  N   . THR A 1 344 ? 45.891 63.385  62.773 1.00 30.39  ? 322 THR A N   1 
ATOM   2155 C  CA  . THR A 1 344 ? 46.916 62.898  61.854 1.00 34.42  ? 322 THR A CA  1 
ATOM   2156 C  C   . THR A 1 344 ? 48.016 62.152  62.598 1.00 35.23  ? 322 THR A C   1 
ATOM   2157 O  O   . THR A 1 344 ? 48.545 61.152  62.097 1.00 37.27  ? 322 THR A O   1 
ATOM   2158 C  CB  . THR A 1 344 ? 47.507 64.059  61.052 1.00 33.07  ? 322 THR A CB  1 
ATOM   2159 O  OG1 . THR A 1 344 ? 48.170 64.968  61.938 1.00 45.07  ? 322 THR A OG1 1 
ATOM   2160 C  CG2 . THR A 1 344 ? 46.415 64.797  60.296 1.00 23.34  ? 322 THR A CG2 1 
ATOM   2161 N  N   . SER A 1 345 ? 48.375 62.619  63.796 1.00 34.06  ? 323 SER A N   1 
ATOM   2162 C  CA  . SER A 1 345 ? 49.402 61.932  64.572 1.00 39.83  ? 323 SER A CA  1 
ATOM   2163 C  C   . SER A 1 345 ? 48.898 60.600  65.112 1.00 34.90  ? 323 SER A C   1 
ATOM   2164 O  O   . SER A 1 345 ? 49.689 59.668  65.292 1.00 39.51  ? 323 SER A O   1 
ATOM   2165 C  CB  . SER A 1 345 ? 49.888 62.823  65.716 1.00 40.70  ? 323 SER A CB  1 
ATOM   2166 O  OG  . SER A 1 345 ? 48.800 63.365  66.443 1.00 50.83  ? 323 SER A OG  1 
ATOM   2167 N  N   . VAL A 1 346 ? 47.594 60.494  65.380 1.00 37.40  ? 324 VAL A N   1 
ATOM   2168 C  CA  . VAL A 1 346 ? 47.019 59.209  65.766 1.00 36.74  ? 324 VAL A CA  1 
ATOM   2169 C  C   . VAL A 1 346 ? 47.155 58.209  64.626 1.00 34.31  ? 324 VAL A C   1 
ATOM   2170 O  O   . VAL A 1 346 ? 47.535 57.051  64.836 1.00 34.28  ? 324 VAL A O   1 
ATOM   2171 C  CB  . VAL A 1 346 ? 45.549 59.385  66.192 1.00 34.89  ? 324 VAL A CB  1 
ATOM   2172 C  CG1 . VAL A 1 346 ? 44.963 58.055  66.645 1.00 36.11  ? 324 VAL A CG1 1 
ATOM   2173 C  CG2 . VAL A 1 346 ? 45.434 60.430  67.290 1.00 33.92  ? 324 VAL A CG2 1 
ATOM   2174 N  N   . ILE A 1 347 ? 46.855 58.645  63.401 1.00 30.38  ? 325 ILE A N   1 
ATOM   2175 C  CA  . ILE A 1 347 ? 47.029 57.782  62.237 1.00 37.24  ? 325 ILE A CA  1 
ATOM   2176 C  C   . ILE A 1 347 ? 48.503 57.468  62.019 1.00 36.40  ? 325 ILE A C   1 
ATOM   2177 O  O   . ILE A 1 347 ? 48.869 56.329  61.703 1.00 35.12  ? 325 ILE A O   1 
ATOM   2178 C  CB  . ILE A 1 347 ? 46.400 58.438  60.995 1.00 29.47  ? 325 ILE A CB  1 
ATOM   2179 C  CG1 . ILE A 1 347 ? 44.895 58.621  61.191 1.00 32.22  ? 325 ILE A CG1 1 
ATOM   2180 C  CG2 . ILE A 1 347 ? 46.684 57.613  59.748 1.00 31.92  ? 325 ILE A CG2 1 
ATOM   2181 C  CD1 . ILE A 1 347 ? 44.270 59.567  60.195 1.00 30.61  ? 325 ILE A CD1 1 
ATOM   2182 N  N   . ASN A 1 348 ? 49.372 58.469  62.189 1.00 32.72  ? 326 ASN A N   1 
ATOM   2183 C  CA  . ASN A 1 348 ? 50.800 58.270  61.954 1.00 38.28  ? 326 ASN A CA  1 
ATOM   2184 C  C   . ASN A 1 348 ? 51.374 57.203  62.877 1.00 37.22  ? 326 ASN A C   1 
ATOM   2185 O  O   . ASN A 1 348 ? 52.194 56.380  62.453 1.00 42.83  ? 326 ASN A O   1 
ATOM   2186 C  CB  . ASN A 1 348 ? 51.550 59.590  62.135 1.00 36.24  ? 326 ASN A CB  1 
ATOM   2187 C  CG  . ASN A 1 348 ? 51.380 60.527  60.953 1.00 48.21  ? 326 ASN A CG  1 
ATOM   2188 O  OD1 . ASN A 1 348 ? 50.985 60.109  59.865 1.00 43.09  ? 326 ASN A OD1 1 
ATOM   2189 N  ND2 . ASN A 1 348 ? 51.680 61.805  61.163 1.00 43.26  ? 326 ASN A ND2 1 
ATOM   2190 N  N   . GLU A 1 349 ? 50.956 57.196  64.141 1.00 35.42  ? 327 GLU A N   1 
ATOM   2191 C  CA  . GLU A 1 349 ? 51.467 56.247  65.121 1.00 42.92  ? 327 GLU A CA  1 
ATOM   2192 C  C   . GLU A 1 349 ? 50.755 54.898  65.078 1.00 41.95  ? 327 GLU A C   1 
ATOM   2193 O  O   . GLU A 1 349 ? 50.953 54.086  65.989 1.00 41.94  ? 327 GLU A O   1 
ATOM   2194 C  CB  . GLU A 1 349 ? 51.365 56.840  66.529 1.00 45.23  ? 327 GLU A CB  1 
ATOM   2195 C  CG  . GLU A 1 349 ? 52.637 57.526  67.011 1.00 69.85  ? 327 GLU A CG  1 
ATOM   2196 C  CD  . GLU A 1 349 ? 53.707 56.542  67.449 1.00 76.78  ? 327 GLU A CD  1 
ATOM   2197 O  OE1 . GLU A 1 349 ? 53.353 55.407  67.832 1.00 74.61  ? 327 GLU A OE1 1 
ATOM   2198 O  OE2 . GLU A 1 349 ? 54.902 56.904  67.413 1.00 78.04  ? 327 GLU A OE2 1 
ATOM   2199 N  N   . HIS A 1 350 ? 49.942 54.635  64.054 1.00 35.78  ? 328 HIS A N   1 
ATOM   2200 C  CA  . HIS A 1 350 ? 49.216 53.374  63.936 1.00 33.78  ? 328 HIS A CA  1 
ATOM   2201 C  C   . HIS A 1 350 ? 49.131 52.953  62.469 1.00 38.43  ? 328 HIS A C   1 
ATOM   2202 O  O   . HIS A 1 350 ? 48.055 52.767  61.906 1.00 34.05  ? 328 HIS A O   1 
ATOM   2203 C  CB  . HIS A 1 350 ? 47.822 53.482  64.547 1.00 32.99  ? 328 HIS A CB  1 
ATOM   2204 C  CG  . HIS A 1 350 ? 47.829 53.705  66.025 1.00 39.70  ? 328 HIS A CG  1 
ATOM   2205 N  ND1 . HIS A 1 350 ? 47.607 54.941  66.592 1.00 37.07  ? 328 HIS A ND1 1 
ATOM   2206 C  CD2 . HIS A 1 350 ? 48.041 52.850  67.053 1.00 30.27  ? 328 HIS A CD2 1 
ATOM   2207 C  CE1 . HIS A 1 350 ? 47.677 54.837  67.907 1.00 34.89  ? 328 HIS A CE1 1 
ATOM   2208 N  NE2 . HIS A 1 350 ? 47.940 53.579  68.212 1.00 38.82  ? 328 HIS A NE2 1 
ATOM   2209 N  N   . GLU A 1 351 ? 50.290 52.794  61.835 1.00 37.34  ? 329 GLU A N   1 
ATOM   2210 C  CA  . GLU A 1 351 ? 50.318 52.324  60.459 1.00 41.99  ? 329 GLU A CA  1 
ATOM   2211 C  C   . GLU A 1 351 ? 49.715 50.927  60.366 1.00 34.59  ? 329 GLU A C   1 
ATOM   2212 O  O   . GLU A 1 351 ? 49.799 50.123  61.298 1.00 39.28  ? 329 GLU A O   1 
ATOM   2213 C  CB  . GLU A 1 351 ? 51.751 52.330  59.916 1.00 43.88  ? 329 GLU A CB  1 
ATOM   2214 C  CG  . GLU A 1 351 ? 52.745 51.470  60.695 1.00 52.08  ? 329 GLU A CG  1 
ATOM   2215 C  CD  . GLU A 1 351 ? 52.677 49.999  60.324 1.00 56.42  ? 329 GLU A CD  1 
ATOM   2216 O  OE1 . GLU A 1 351 ? 52.405 49.693  59.144 1.00 53.16  ? 329 GLU A OE1 1 
ATOM   2217 O  OE2 . GLU A 1 351 ? 52.894 49.149  61.213 1.00 56.66  ? 329 GLU A OE2 1 
ATOM   2218 N  N   . GLN A 1 352 ? 49.090 50.646  59.223 1.00 33.00  ? 330 GLN A N   1 
ATOM   2219 C  CA  . GLN A 1 352 ? 48.461 49.355  58.970 1.00 39.90  ? 330 GLN A CA  1 
ATOM   2220 C  C   . GLN A 1 352 ? 49.130 48.615  57.818 1.00 39.47  ? 330 GLN A C   1 
ATOM   2221 O  O   . GLN A 1 352 ? 48.516 47.734  57.208 1.00 38.05  ? 330 GLN A O   1 
ATOM   2222 C  CB  . GLN A 1 352 ? 46.968 49.541  58.693 1.00 35.67  ? 330 GLN A CB  1 
ATOM   2223 C  CG  . GLN A 1 352 ? 46.225 50.257  59.811 1.00 33.70  ? 330 GLN A CG  1 
ATOM   2224 C  CD  . GLN A 1 352 ? 46.196 49.450  61.093 1.00 37.48  ? 330 GLN A CD  1 
ATOM   2225 O  OE1 . GLN A 1 352 ? 45.779 48.293  61.099 1.00 38.72  ? 330 GLN A OE1 1 
ATOM   2226 N  NE2 . GLN A 1 352 ? 46.648 50.054  62.186 1.00 34.27  ? 330 GLN A NE2 1 
ATOM   2227 N  N   . SER A 1 353 ? 50.383 48.956  57.514 1.00 39.71  ? 331 SER A N   1 
ATOM   2228 C  CA  . SER A 1 353 ? 51.070 48.373  56.367 1.00 48.64  ? 331 SER A CA  1 
ATOM   2229 C  C   . SER A 1 353 ? 51.649 46.998  56.679 1.00 48.47  ? 331 SER A C   1 
ATOM   2230 O  O   . SER A 1 353 ? 51.653 46.116  55.814 1.00 54.34  ? 331 SER A O   1 
ATOM   2231 C  CB  . SER A 1 353 ? 52.180 49.311  55.897 1.00 45.38  ? 331 SER A CB  1 
ATOM   2232 O  OG  . SER A 1 353 ? 53.067 49.620  56.960 1.00 49.17  ? 331 SER A OG  1 
ATOM   2233 N  N   . THR A 1 354 ? 52.128 46.795  57.902 1.00 51.28  ? 332 THR A N   1 
ATOM   2234 C  CA  . THR A 1 354 ? 52.820 45.559  58.233 1.00 55.03  ? 332 THR A CA  1 
ATOM   2235 C  C   . THR A 1 354 ? 51.832 44.396  58.304 1.00 55.01  ? 332 THR A C   1 
ATOM   2236 O  O   . THR A 1 354 ? 50.724 44.552  58.825 1.00 53.04  ? 332 THR A O   1 
ATOM   2237 C  CB  . THR A 1 354 ? 53.558 45.700  59.563 1.00 57.93  ? 332 THR A CB  1 
ATOM   2238 O  OG1 . THR A 1 354 ? 52.631 46.071  60.591 1.00 60.21  ? 332 THR A OG1 1 
ATOM   2239 C  CG2 . THR A 1 354 ? 54.640 46.764  59.458 1.00 54.81  ? 332 THR A CG2 1 
ATOM   2240 N  N   . PRO A 1 355 ? 52.223 43.212  57.824 1.00 63.52  ? 333 PRO A N   1 
ATOM   2241 C  CA  . PRO A 1 355 ? 51.320 42.079  57.695 1.00 60.79  ? 333 PRO A CA  1 
ATOM   2242 C  C   . PRO A 1 355 ? 50.855 41.596  59.064 1.00 61.76  ? 333 PRO A C   1 
ATOM   2243 O  O   . PRO A 1 355 ? 51.531 41.852  59.998 1.00 63.08  ? 333 PRO A O   1 
ATOM   2244 C  CB  . PRO A 1 355 ? 52.193 41.015  57.042 1.00 63.05  ? 333 PRO A CB  1 
ATOM   2245 C  CG  . PRO A 1 355 ? 53.309 41.794  56.424 1.00 65.40  ? 333 PRO A CG  1 
ATOM   2246 C  CD  . PRO A 1 355 ? 53.574 42.911  57.399 1.00 62.40  ? 333 PRO A CD  1 
ATOM   2247 N  N   . VAL A 1 356 ? 49.694 40.984  59.136 1.00 54.39  ? 334 VAL A N   1 
ATOM   2248 C  CA  . VAL A 1 356 ? 49.298 40.526  60.486 1.00 62.25  ? 334 VAL A CA  1 
ATOM   2249 C  C   . VAL A 1 356 ? 48.623 39.182  60.359 1.00 61.34  ? 334 VAL A C   1 
ATOM   2250 O  O   . VAL A 1 356 ? 48.183 38.834  59.279 1.00 61.17  ? 334 VAL A O   1 
ATOM   2251 C  CB  . VAL A 1 356 ? 48.376 41.506  61.225 1.00 55.06  ? 334 VAL A CB  1 
ATOM   2252 C  CG1 . VAL A 1 356 ? 49.103 42.763  61.659 1.00 57.85  ? 334 VAL A CG1 1 
ATOM   2253 C  CG2 . VAL A 1 356 ? 47.134 41.824  60.426 1.00 51.03  ? 334 VAL A CG2 1 
ATOM   2254 N  N   . GLY A 1 357 ? 48.563 38.473  61.466 1.00 60.62  ? 335 GLY A N   1 
ATOM   2255 C  CA  . GLY A 1 357 ? 47.836 37.212  61.375 1.00 70.31  ? 335 GLY A CA  1 
ATOM   2256 C  C   . GLY A 1 357 ? 48.572 36.061  61.983 1.00 68.62  ? 335 GLY A C   1 
ATOM   2257 O  O   . GLY A 1 357 ? 49.274 36.228  62.947 1.00 72.50  ? 335 GLY A O   1 
ATOM   2258 N  N   . GLY A 1 358 ? 48.349 34.919  61.372 1.00 73.21  ? 336 GLY A N   1 
ATOM   2259 C  CA  . GLY A 1 358 ? 47.758 34.960  60.025 1.00 80.88  ? 336 GLY A CA  1 
ATOM   2260 C  C   . GLY A 1 358 ? 48.798 35.070  58.920 1.00 99.94  ? 336 GLY A C   1 
ATOM   2261 O  O   . GLY A 1 358 ? 48.388 35.168  57.758 1.00 105.18 ? 336 GLY A O   1 
ATOM   2262 N  N   . ASN A 1 359 ? 50.082 35.165  59.272 1.00 102.11 ? 337 ASN A N   1 
ATOM   2263 C  CA  . ASN A 1 359 ? 51.189 35.164  58.278 1.00 107.41 ? 337 ASN A CA  1 
ATOM   2264 C  C   . ASN A 1 359 ? 52.362 34.334  58.841 1.00 112.24 ? 337 ASN A C   1 
ATOM   2265 O  O   . ASN A 1 359 ? 53.459 34.374  58.244 1.00 111.90 ? 337 ASN A O   1 
ATOM   2266 C  CB  . ASN A 1 359 ? 51.349 36.535  57.608 1.00 106.88 ? 337 ASN A CB  1 
ATOM   2267 C  CG  . ASN A 1 359 ? 52.444 37.410  58.172 1.00 100.13 ? 337 ASN A CG  1 
ATOM   2268 O  OD1 . ASN A 1 359 ? 52.335 37.925  59.284 1.00 95.16  ? 337 ASN A OD1 1 
ATOM   2269 N  ND2 . ASN A 1 359 ? 53.477 37.628  57.374 1.00 93.24  ? 337 ASN A ND2 1 
ATOM   2270 N  N   . ASN A 1 360 ? 52.080 33.629  59.956 1.00 114.68 ? 338 ASN A N   1 
ATOM   2271 C  CA  . ASN A 1 360 ? 52.880 32.646  60.742 1.00 116.13 ? 338 ASN A CA  1 
ATOM   2272 C  C   . ASN A 1 360 ? 52.523 31.245  60.231 1.00 112.02 ? 338 ASN A C   1 
ATOM   2273 O  O   . ASN A 1 360 ? 51.874 31.114  59.165 1.00 107.64 ? 338 ASN A O   1 
ATOM   2274 C  CB  . ASN A 1 360 ? 52.486 32.689  62.225 1.00 108.75 ? 338 ASN A CB  1 
ATOM   2275 C  CG  . ASN A 1 360 ? 51.071 33.209  62.356 1.00 105.84 ? 338 ASN A CG  1 
ATOM   2276 O  OD1 . ASN A 1 360 ? 50.491 33.564  61.344 1.00 99.81  ? 338 ASN A OD1 1 
ATOM   2277 N  ND2 . ASN A 1 360 ? 50.503 33.241  63.548 1.00 99.69  ? 338 ASN A ND2 1 
ATOM   2278 N  N   . GLY A 1 361 ? 52.949 30.219  60.951 1.00 108.52 ? 339 GLY A N   1 
ATOM   2279 C  CA  . GLY A 1 361 ? 52.691 28.834  60.512 1.00 107.46 ? 339 GLY A CA  1 
ATOM   2280 C  C   . GLY A 1 361 ? 51.241 28.377  60.539 1.00 107.58 ? 339 GLY A C   1 
ATOM   2281 O  O   . GLY A 1 361 ? 50.865 27.631  59.629 1.00 110.31 ? 339 GLY A O   1 
ATOM   2282 N  N   . LYS A 1 362 ? 50.478 28.770  61.563 1.00 105.49 ? 340 LYS A N   1 
ATOM   2283 C  CA  . LYS A 1 362 ? 49.111 28.248  61.860 1.00 92.31  ? 340 LYS A CA  1 
ATOM   2284 C  C   . LYS A 1 362 ? 47.987 29.201  61.435 1.00 90.21  ? 340 LYS A C   1 
ATOM   2285 O  O   . LYS A 1 362 ? 48.279 30.344  61.141 1.00 92.94  ? 340 LYS A O   1 
ATOM   2286 C  CB  . LYS A 1 362 ? 49.048 28.000  63.363 1.00 90.87  ? 340 LYS A CB  1 
ATOM   2287 C  CG  . LYS A 1 362 ? 49.938 26.882  63.892 1.00 96.35  ? 340 LYS A CG  1 
ATOM   2288 C  CD  . LYS A 1 362 ? 49.905 26.635  65.397 1.00 99.87  ? 340 LYS A CD  1 
ATOM   2289 C  CE  . LYS A 1 362 ? 50.794 25.495  65.854 1.00 95.11  ? 340 LYS A CE  1 
ATOM   2290 N  NZ  . LYS A 1 362 ? 50.758 25.297  67.321 1.00 94.70  ? 340 LYS A NZ  1 
ATOM   2291 N  N   . PRO A 1 363 ? 46.711 28.762  61.403 1.00 82.40  ? 341 PRO A N   1 
ATOM   2292 C  CA  . PRO A 1 363 ? 45.575 29.592  60.975 1.00 77.14  ? 341 PRO A CA  1 
ATOM   2293 C  C   . PRO A 1 363 ? 45.279 30.715  61.974 1.00 64.36  ? 341 PRO A C   1 
ATOM   2294 O  O   . PRO A 1 363 ? 45.446 30.525  63.131 1.00 68.10  ? 341 PRO A O   1 
ATOM   2295 C  CB  . PRO A 1 363 ? 44.404 28.620  61.030 1.00 71.90  ? 341 PRO A CB  1 
ATOM   2296 C  CG  . PRO A 1 363 ? 44.800 27.734  62.154 1.00 80.03  ? 341 PRO A CG  1 
ATOM   2297 C  CD  . PRO A 1 363 ? 46.261 27.473  61.884 1.00 81.70  ? 341 PRO A CD  1 
ATOM   2298 N  N   . PHE A 1 364 ? 44.774 31.835  61.488 1.00 56.26  ? 342 PHE A N   1 
ATOM   2299 C  CA  . PHE A 1 364 ? 44.538 33.002  62.371 1.00 53.97  ? 342 PHE A CA  1 
ATOM   2300 C  C   . PHE A 1 364 ? 43.517 32.702  63.466 1.00 45.59  ? 342 PHE A C   1 
ATOM   2301 O  O   . PHE A 1 364 ? 42.447 32.279  63.167 1.00 40.68  ? 342 PHE A O   1 
ATOM   2302 C  CB  . PHE A 1 364 ? 44.033 34.139  61.492 1.00 53.31  ? 342 PHE A CB  1 
ATOM   2303 C  CG  . PHE A 1 364 ? 43.621 35.383  62.214 1.00 46.51  ? 342 PHE A CG  1 
ATOM   2304 C  CD1 . PHE A 1 364 ? 44.549 36.144  62.879 1.00 47.27  ? 342 PHE A CD1 1 
ATOM   2305 C  CD2 . PHE A 1 364 ? 42.312 35.799  62.190 1.00 44.25  ? 342 PHE A CD2 1 
ATOM   2306 C  CE1 . PHE A 1 364 ? 44.171 37.303  63.521 1.00 50.54  ? 342 PHE A CE1 1 
ATOM   2307 C  CE2 . PHE A 1 364 ? 41.939 36.958  62.839 1.00 44.20  ? 342 PHE A CE2 1 
ATOM   2308 C  CZ  . PHE A 1 364 ? 42.866 37.706  63.503 1.00 39.80  ? 342 PHE A CZ  1 
ATOM   2309 N  N   . ASN A 1 365 ? 43.884 33.014  64.704 1.00 52.03  ? 343 ASN A N   1 
ATOM   2310 C  CA  . ASN A 1 365 ? 42.992 32.851  65.845 1.00 49.05  ? 343 ASN A CA  1 
ATOM   2311 C  C   . ASN A 1 365 ? 42.526 34.222  66.314 1.00 40.28  ? 343 ASN A C   1 
ATOM   2312 O  O   . ASN A 1 365 ? 43.345 35.005  66.821 1.00 41.91  ? 343 ASN A O   1 
ATOM   2313 C  CB  . ASN A 1 365 ? 43.701 32.109  66.980 1.00 43.36  ? 343 ASN A CB  1 
ATOM   2314 C  CG  . ASN A 1 365 ? 42.755 31.704  68.092 1.00 46.67  ? 343 ASN A CG  1 
ATOM   2315 O  OD1 . ASN A 1 365 ? 42.420 32.509  68.961 1.00 43.97  ? 343 ASN A OD1 1 
ATOM   2316 N  ND2 . ASN A 1 365 ? 42.324 30.449  68.075 1.00 54.70  ? 343 ASN A ND2 1 
ATOM   2317 N  N   . PRO A 1 366 ? 41.241 34.561  66.171 1.00 38.43  ? 344 PRO A N   1 
ATOM   2318 C  CA  . PRO A 1 366 ? 40.791 35.908  66.564 1.00 38.27  ? 344 PRO A CA  1 
ATOM   2319 C  C   . PRO A 1 366 ? 40.863 36.167  68.059 1.00 41.54  ? 344 PRO A C   1 
ATOM   2320 O  O   . PRO A 1 366 ? 40.820 37.335  68.467 1.00 35.55  ? 344 PRO A O   1 
ATOM   2321 C  CB  . PRO A 1 366 ? 39.341 35.961  66.060 1.00 38.20  ? 344 PRO A CB  1 
ATOM   2322 C  CG  . PRO A 1 366 ? 39.208 34.818  65.094 1.00 42.95  ? 344 PRO A CG  1 
ATOM   2323 C  CD  . PRO A 1 366 ? 40.160 33.769  65.567 1.00 42.41  ? 344 PRO A CD  1 
ATOM   2324 N  N   . PHE A 1 367 ? 40.968 35.126  68.889 1.00 35.74  ? 345 PHE A N   1 
ATOM   2325 C  CA  . PHE A 1 367 ? 41.059 35.332  70.330 1.00 36.11  ? 345 PHE A CA  1 
ATOM   2326 C  C   . PHE A 1 367 ? 42.470 35.697  70.772 1.00 40.84  ? 345 PHE A C   1 
ATOM   2327 O  O   . PHE A 1 367 ? 42.635 36.410  71.768 1.00 41.72  ? 345 PHE A O   1 
ATOM   2328 C  CB  . PHE A 1 367 ? 40.602 34.078  71.080 1.00 45.83  ? 345 PHE A CB  1 
ATOM   2329 C  CG  . PHE A 1 367 ? 39.166 33.709  70.841 1.00 38.36  ? 345 PHE A CG  1 
ATOM   2330 C  CD1 . PHE A 1 367 ? 38.819 32.852  69.809 1.00 41.11  ? 345 PHE A CD1 1 
ATOM   2331 C  CD2 . PHE A 1 367 ? 38.163 34.207  71.657 1.00 43.72  ? 345 PHE A CD2 1 
ATOM   2332 C  CE1 . PHE A 1 367 ? 37.499 32.507  69.589 1.00 45.37  ? 345 PHE A CE1 1 
ATOM   2333 C  CE2 . PHE A 1 367 ? 36.841 33.865  71.442 1.00 38.81  ? 345 PHE A CE2 1 
ATOM   2334 C  CZ  . PHE A 1 367 ? 36.509 33.015  70.407 1.00 36.81  ? 345 PHE A CZ  1 
ATOM   2335 N  N   . THR A 1 368 ? 43.492 35.226  70.054 1.00 46.11  ? 346 THR A N   1 
ATOM   2336 C  CA  . THR A 1 368 ? 44.873 35.379  70.488 1.00 46.03  ? 346 THR A CA  1 
ATOM   2337 C  C   . THR A 1 368 ? 45.775 36.106  69.501 1.00 45.18  ? 346 THR A C   1 
ATOM   2338 O  O   . THR A 1 368 ? 46.781 36.682  69.930 1.00 47.22  ? 346 THR A O   1 
ATOM   2339 C  CB  . THR A 1 368 ? 45.496 34.004  70.786 1.00 45.42  ? 346 THR A CB  1 
ATOM   2340 O  OG1 . THR A 1 368 ? 45.399 33.172  69.623 1.00 43.24  ? 346 THR A OG1 1 
ATOM   2341 C  CG2 . THR A 1 368 ? 44.775 33.331  71.945 1.00 50.28  ? 346 THR A CG2 1 
ATOM   2342 N  N   . ASP A 1 369 ? 45.458 36.098  68.206 1.00 37.42  ? 347 ASP A N   1 
ATOM   2343 C  CA  . ASP A 1 369 ? 46.308 36.707  67.191 1.00 44.14  ? 347 ASP A CA  1 
ATOM   2344 C  C   . ASP A 1 369 ? 45.862 38.118  66.820 1.00 39.17  ? 347 ASP A C   1 
ATOM   2345 O  O   . ASP A 1 369 ? 46.235 38.618  65.754 1.00 46.49  ? 347 ASP A O   1 
ATOM   2346 C  CB  . ASP A 1 369 ? 46.349 35.829  65.940 1.00 42.96  ? 347 ASP A CB  1 
ATOM   2347 C  CG  . ASP A 1 369 ? 46.789 34.409  66.236 1.00 44.53  ? 347 ASP A CG  1 
ATOM   2348 O  OD1 . ASP A 1 369 ? 47.177 34.131  67.390 1.00 43.59  ? 347 ASP A OD1 1 
ATOM   2349 O  OD2 . ASP A 1 369 ? 46.743 33.570  65.312 1.00 43.80  ? 347 ASP A OD2 1 
ATOM   2350 N  N   . ALA A 1 370 ? 45.081 38.772  67.676 1.00 32.04  ? 348 ALA A N   1 
ATOM   2351 C  CA  . ALA A 1 370 ? 44.483 40.068  67.374 1.00 42.29  ? 348 ALA A CA  1 
ATOM   2352 C  C   . ALA A 1 370 ? 45.129 41.196  68.172 1.00 40.03  ? 348 ALA A C   1 
ATOM   2353 O  O   . ALA A 1 370 ? 44.462 42.144  68.588 1.00 42.14  ? 348 ALA A O   1 
ATOM   2354 C  CB  . ALA A 1 370 ? 42.978 40.038  67.626 1.00 34.39  ? 348 ALA A CB  1 
ATOM   2355 N  N   . SER A 1 371 ? 46.441 41.104  68.393 1.00 34.98  ? 349 SER A N   1 
ATOM   2356 C  CA  . SER A 1 371 ? 47.157 42.176  69.077 1.00 37.47  ? 349 SER A CA  1 
ATOM   2357 C  C   . SER A 1 371 ? 47.050 43.495  68.323 1.00 28.55  ? 349 SER A C   1 
ATOM   2358 O  O   . SER A 1 371 ? 46.987 44.564  68.942 1.00 33.45  ? 349 SER A O   1 
ATOM   2359 C  CB  . SER A 1 371 ? 48.623 41.795  69.245 1.00 41.53  ? 349 SER A CB  1 
ATOM   2360 O  OG  . SER A 1 371 ? 49.124 41.240  68.043 1.00 49.77  ? 349 SER A OG  1 
ATOM   2361 N  N   . PHE A 1 372 ? 47.016 43.436  66.992 1.00 32.01  ? 350 PHE A N   1 
ATOM   2362 C  CA  . PHE A 1 372 ? 47.006 44.619  66.141 1.00 41.10  ? 350 PHE A CA  1 
ATOM   2363 C  C   . PHE A 1 372 ? 45.675 45.357  66.150 1.00 34.12  ? 350 PHE A C   1 
ATOM   2364 O  O   . PHE A 1 372 ? 45.608 46.469  65.618 1.00 32.99  ? 350 PHE A O   1 
ATOM   2365 C  CB  . PHE A 1 372 ? 47.336 44.213  64.706 1.00 38.35  ? 350 PHE A CB  1 
ATOM   2366 C  CG  . PHE A 1 372 ? 46.294 43.325  64.082 1.00 40.94  ? 350 PHE A CG  1 
ATOM   2367 C  CD1 . PHE A 1 372 ? 46.350 41.951  64.246 1.00 41.45  ? 350 PHE A CD1 1 
ATOM   2368 C  CD2 . PHE A 1 372 ? 45.249 43.865  63.350 1.00 32.01  ? 350 PHE A CD2 1 
ATOM   2369 C  CE1 . PHE A 1 372 ? 45.389 41.132  63.683 1.00 42.63  ? 350 PHE A CE1 1 
ATOM   2370 C  CE2 . PHE A 1 372 ? 44.286 43.053  62.787 1.00 37.98  ? 350 PHE A CE2 1 
ATOM   2371 C  CZ  . PHE A 1 372 ? 44.357 41.684  62.952 1.00 38.69  ? 350 PHE A CZ  1 
ATOM   2372 N  N   . ALA A 1 373 ? 44.623 44.765  66.720 1.00 33.42  ? 351 ALA A N   1 
ATOM   2373 C  CA  . ALA A 1 373 ? 43.275 45.293  66.525 1.00 33.95  ? 351 ALA A CA  1 
ATOM   2374 C  C   . ALA A 1 373 ? 43.097 46.653  67.191 1.00 33.16  ? 351 ALA A C   1 
ATOM   2375 O  O   . ALA A 1 373 ? 42.403 47.524  66.653 1.00 31.25  ? 351 ALA A O   1 
ATOM   2376 C  CB  . ALA A 1 373 ? 42.245 44.297  67.053 1.00 32.47  ? 351 ALA A CB  1 
ATOM   2377 N  N   . GLN A 1 374 ? 43.711 46.854  68.359 1.00 33.05  ? 352 GLN A N   1 
ATOM   2378 C  CA  . GLN A 1 374 ? 43.574 48.130  69.055 1.00 38.43  ? 352 GLN A CA  1 
ATOM   2379 C  C   . GLN A 1 374 ? 44.142 49.272  68.220 1.00 35.84  ? 352 GLN A C   1 
ATOM   2380 O  O   . GLN A 1 374 ? 43.522 50.335  68.097 1.00 37.47  ? 352 GLN A O   1 
ATOM   2381 C  CB  . GLN A 1 374 ? 44.260 48.062  70.419 1.00 37.47  ? 352 GLN A CB  1 
ATOM   2382 C  CG  . GLN A 1 374 ? 43.737 49.079  71.423 1.00 47.60  ? 352 GLN A CG  1 
ATOM   2383 C  CD  . GLN A 1 374 ? 42.484 48.604  72.136 1.00 66.77  ? 352 GLN A CD  1 
ATOM   2384 O  OE1 . GLN A 1 374 ? 42.532 47.684  72.953 1.00 59.55  ? 352 GLN A OE1 1 
ATOM   2385 N  NE2 . GLN A 1 374 ? 41.354 49.233  71.831 1.00 52.93  ? 352 GLN A NE2 1 
ATOM   2386 N  N   . GLY A 1 375 ? 45.324 49.068  67.636 1.00 33.38  ? 353 GLY A N   1 
ATOM   2387 C  CA  . GLY A 1 375 ? 45.887 50.085  66.765 1.00 38.15  ? 353 GLY A CA  1 
ATOM   2388 C  C   . GLY A 1 375 ? 45.080 50.269  65.494 1.00 34.74  ? 353 GLY A C   1 
ATOM   2389 O  O   . GLY A 1 375 ? 44.890 51.395  65.025 1.00 33.28  ? 353 GLY A O   1 
ATOM   2390 N  N   . MET A 1 376 ? 44.597 49.166  64.918 1.00 30.48  ? 354 MET A N   1 
ATOM   2391 C  CA  . MET A 1 376 ? 43.729 49.258  63.749 1.00 28.92  ? 354 MET A CA  1 
ATOM   2392 C  C   . MET A 1 376 ? 42.455 50.027  64.075 1.00 34.24  ? 354 MET A C   1 
ATOM   2393 O  O   . MET A 1 376 ? 41.964 50.809  63.252 1.00 31.97  ? 354 MET A O   1 
ATOM   2394 C  CB  . MET A 1 376 ? 43.397 47.857  63.235 1.00 31.62  ? 354 MET A CB  1 
ATOM   2395 C  CG  . MET A 1 376 ? 42.558 47.829  61.969 1.00 29.09  ? 354 MET A CG  1 
ATOM   2396 S  SD  . MET A 1 376 ? 42.099 46.148  61.505 1.00 32.07  ? 354 MET A SD  1 
ATOM   2397 C  CE  . MET A 1 376 ? 41.111 46.449  60.043 1.00 26.80  ? 354 MET A CE  1 
ATOM   2398 N  N   . LEU A 1 377 ? 41.909 49.823  65.276 1.00 29.05  ? 355 LEU A N   1 
ATOM   2399 C  CA  . LEU A 1 377 ? 40.720 50.564  65.681 1.00 32.78  ? 355 LEU A CA  1 
ATOM   2400 C  C   . LEU A 1 377 ? 41.031 52.042  65.871 1.00 35.97  ? 355 LEU A C   1 
ATOM   2401 O  O   . LEU A 1 377 ? 40.249 52.903  65.452 1.00 30.16  ? 355 LEU A O   1 
ATOM   2402 C  CB  . LEU A 1 377 ? 40.138 49.967  66.962 1.00 31.99  ? 355 LEU A CB  1 
ATOM   2403 C  CG  . LEU A 1 377 ? 38.847 50.608  67.478 1.00 37.77  ? 355 LEU A CG  1 
ATOM   2404 C  CD1 . LEU A 1 377 ? 37.763 50.574  66.408 1.00 31.50  ? 355 LEU A CD1 1 
ATOM   2405 C  CD2 . LEU A 1 377 ? 38.373 49.923  68.751 1.00 34.00  ? 355 LEU A CD2 1 
ATOM   2406 N  N   . ALA A 1 378 ? 42.170 52.356  66.494 1.00 29.82  ? 356 ALA A N   1 
ATOM   2407 C  CA  . ALA A 1 378 ? 42.550 53.753  66.683 1.00 33.54  ? 356 ALA A CA  1 
ATOM   2408 C  C   . ALA A 1 378 ? 42.767 54.451  65.347 1.00 31.04  ? 356 ALA A C   1 
ATOM   2409 O  O   . ALA A 1 378 ? 42.378 55.613  65.174 1.00 32.11  ? 356 ALA A O   1 
ATOM   2410 C  CB  . ALA A 1 378 ? 43.809 53.844  67.546 1.00 33.42  ? 356 ALA A CB  1 
ATOM   2411 N  N   . ASN A 1 379 ? 43.387 53.757  64.391 1.00 32.86  ? 357 ASN A N   1 
ATOM   2412 C  CA  . ASN A 1 379 ? 43.580 54.319  63.059 1.00 27.45  ? 357 ASN A CA  1 
ATOM   2413 C  C   . ASN A 1 379 ? 42.240 54.630  62.402 1.00 28.72  ? 357 ASN A C   1 
ATOM   2414 O  O   . ASN A 1 379 ? 41.983 55.766  61.987 1.00 27.19  ? 357 ASN A O   1 
ATOM   2415 C  CB  . ASN A 1 379 ? 44.399 53.349  62.202 1.00 23.73  ? 357 ASN A CB  1 
ATOM   2416 C  CG  . ASN A 1 379 ? 44.771 53.928  60.849 1.00 29.14  ? 357 ASN A CG  1 
ATOM   2417 O  OD1 . ASN A 1 379 ? 43.904 54.244  60.035 1.00 27.36  ? 357 ASN A OD1 1 
ATOM   2418 N  ND2 . ASN A 1 379 ? 46.068 54.060  60.599 1.00 30.92  ? 357 ASN A ND2 1 
ATOM   2419 N  N   . ALA A 1 380 ? 41.370 53.622  62.299 1.00 26.28  ? 358 ALA A N   1 
ATOM   2420 C  CA  . ALA A 1 380 ? 40.065 53.831  61.679 1.00 29.95  ? 358 ALA A CA  1 
ATOM   2421 C  C   . ALA A 1 380 ? 39.244 54.855  62.452 1.00 27.80  ? 358 ALA A C   1 
ATOM   2422 O  O   . ALA A 1 380 ? 38.536 55.672  61.852 1.00 30.00  ? 358 ALA A O   1 
ATOM   2423 C  CB  . ALA A 1 380 ? 39.314 52.504  61.575 1.00 27.71  ? 358 ALA A CB  1 
ATOM   2424 N  N   . SER A 1 381 ? 39.327 54.828  63.786 1.00 25.59  ? 359 SER A N   1 
ATOM   2425 C  CA  . SER A 1 381 ? 38.621 55.818  64.595 1.00 32.77  ? 359 SER A CA  1 
ATOM   2426 C  C   . SER A 1 381 ? 39.068 57.231  64.249 1.00 27.50  ? 359 SER A C   1 
ATOM   2427 O  O   . SER A 1 381 ? 38.242 58.144  64.140 1.00 27.08  ? 359 SER A O   1 
ATOM   2428 C  CB  . SER A 1 381 ? 38.848 55.548  66.082 1.00 28.77  ? 359 SER A CB  1 
ATOM   2429 O  OG  . SER A 1 381 ? 37.838 54.713  66.616 1.00 44.58  ? 359 SER A OG  1 
ATOM   2430 N  N   . ALA A 1 382 ? 40.375 57.428  64.064 1.00 24.76  ? 360 ALA A N   1 
ATOM   2431 C  CA  . ALA A 1 382 ? 40.892 58.763  63.784 1.00 28.81  ? 360 ALA A CA  1 
ATOM   2432 C  C   . ALA A 1 382 ? 40.441 59.257  62.416 1.00 29.54  ? 360 ALA A C   1 
ATOM   2433 O  O   . ALA A 1 382 ? 40.143 60.445  62.248 1.00 29.42  ? 360 ALA A O   1 
ATOM   2434 C  CB  . ALA A 1 382 ? 42.417 58.765  63.883 1.00 27.09  ? 360 ALA A CB  1 
ATOM   2435 N  N   . GLN A 1 383 ? 40.384 58.362  61.427 1.00 25.08  ? 361 GLN A N   1 
ATOM   2436 C  CA  . GLN A 1 383 ? 39.937 58.766  60.097 1.00 27.77  ? 361 GLN A CA  1 
ATOM   2437 C  C   . GLN A 1 383 ? 38.451 59.103  60.094 1.00 27.74  ? 361 GLN A C   1 
ATOM   2438 O  O   . GLN A 1 383 ? 38.034 60.084  59.467 1.00 27.79  ? 361 GLN A O   1 
ATOM   2439 C  CB  . GLN A 1 383 ? 40.246 57.667  59.080 1.00 25.00  ? 361 GLN A CB  1 
ATOM   2440 C  CG  . GLN A 1 383 ? 41.720 57.304  58.998 1.00 26.15  ? 361 GLN A CG  1 
ATOM   2441 C  CD  . GLN A 1 383 ? 42.068 56.538  57.737 1.00 31.79  ? 361 GLN A CD  1 
ATOM   2442 O  OE1 . GLN A 1 383 ? 41.544 56.822  56.661 1.00 34.53  ? 361 GLN A OE1 1 
ATOM   2443 N  NE2 . GLN A 1 383 ? 42.952 55.557  57.864 1.00 19.84  ? 361 GLN A NE2 1 
ATOM   2444 N  N   . ALA A 1 384 ? 37.637 58.302  60.787 1.00 23.86  ? 362 ALA A N   1 
ATOM   2445 C  CA  . ALA A 1 384 ? 36.217 58.620  60.902 1.00 22.87  ? 362 ALA A CA  1 
ATOM   2446 C  C   . ALA A 1 384 ? 36.010 59.952  61.610 1.00 27.01  ? 362 ALA A C   1 
ATOM   2447 O  O   . ALA A 1 384 ? 35.159 60.755  61.207 1.00 26.65  ? 362 ALA A O   1 
ATOM   2448 C  CB  . ALA A 1 384 ? 35.485 57.499  61.640 1.00 24.75  ? 362 ALA A CB  1 
ATOM   2449 N  N   . LYS A 1 385 ? 36.790 60.209  62.662 1.00 25.20  ? 363 LYS A N   1 
ATOM   2450 C  CA  . LYS A 1 385 ? 36.667 61.466  63.391 1.00 26.20  ? 363 LYS A CA  1 
ATOM   2451 C  C   . LYS A 1 385 ? 37.083 62.650  62.525 1.00 26.90  ? 363 LYS A C   1 
ATOM   2452 O  O   . LYS A 1 385 ? 36.474 63.724  62.601 1.00 24.74  ? 363 LYS A O   1 
ATOM   2453 C  CB  . LYS A 1 385 ? 37.506 61.408  64.666 1.00 29.49  ? 363 LYS A CB  1 
ATOM   2454 C  CG  . LYS A 1 385 ? 37.430 62.655  65.522 1.00 34.99  ? 363 LYS A CG  1 
ATOM   2455 C  CD  . LYS A 1 385 ? 37.425 62.298  66.998 1.00 39.21  ? 363 LYS A CD  1 
ATOM   2456 C  CE  . LYS A 1 385 ? 38.162 63.342  67.810 1.00 51.68  ? 363 LYS A CE  1 
ATOM   2457 N  NZ  . LYS A 1 385 ? 37.826 63.276  69.259 1.00 51.85  ? 363 LYS A NZ  1 
ATOM   2458 N  N   . MET A 1 386 ? 38.117 62.474  61.700 1.00 24.73  ? 364 MET A N   1 
ATOM   2459 C  CA  . MET A 1 386 ? 38.529 63.535  60.786 1.00 29.70  ? 364 MET A CA  1 
ATOM   2460 C  C   . MET A 1 386 ? 37.413 63.881  59.811 1.00 23.91  ? 364 MET A C   1 
ATOM   2461 O  O   . MET A 1 386 ? 37.134 65.059  59.558 1.00 26.72  ? 364 MET A O   1 
ATOM   2462 C  CB  . MET A 1 386 ? 39.789 63.116  60.029 1.00 26.79  ? 364 MET A CB  1 
ATOM   2463 C  CG  . MET A 1 386 ? 41.074 63.370  60.785 1.00 42.45  ? 364 MET A CG  1 
ATOM   2464 S  SD  . MET A 1 386 ? 42.522 62.648  59.993 1.00 40.48  ? 364 MET A SD  1 
ATOM   2465 C  CE  . MET A 1 386 ? 42.601 63.604  58.487 1.00 24.32  ? 364 MET A CE  1 
ATOM   2466 N  N   . LEU A 1 387 ? 36.760 62.859  59.252 1.00 20.81  ? 365 LEU A N   1 
ATOM   2467 C  CA  . LEU A 1 387 ? 35.686 63.095  58.293 1.00 27.20  ? 365 LEU A CA  1 
ATOM   2468 C  C   . LEU A 1 387 ? 34.478 63.745  58.957 1.00 22.32  ? 365 LEU A C   1 
ATOM   2469 O  O   . LEU A 1 387 ? 33.855 64.643  58.379 1.00 28.76  ? 365 LEU A O   1 
ATOM   2470 C  CB  . LEU A 1 387 ? 35.281 61.782  57.625 1.00 25.79  ? 365 LEU A CB  1 
ATOM   2471 C  CG  . LEU A 1 387 ? 36.279 61.171  56.640 1.00 28.19  ? 365 LEU A CG  1 
ATOM   2472 C  CD1 . LEU A 1 387 ? 35.838 59.772  56.245 1.00 30.86  ? 365 LEU A CD1 1 
ATOM   2473 C  CD2 . LEU A 1 387 ? 36.429 62.057  55.413 1.00 25.35  ? 365 LEU A CD2 1 
ATOM   2474 N  N   . ASN A 1 388 ? 34.124 63.298  60.164 1.00 27.38  ? 366 ASN A N   1 
ATOM   2475 C  CA  . ASN A 1 388 ? 32.985 63.890  60.858 1.00 26.96  ? 366 ASN A CA  1 
ATOM   2476 C  C   . ASN A 1 388 ? 33.258 65.344  61.219 1.00 26.10  ? 366 ASN A C   1 
ATOM   2477 O  O   . ASN A 1 388 ? 32.389 66.206  61.046 1.00 26.79  ? 366 ASN A O   1 
ATOM   2478 C  CB  . ASN A 1 388 ? 32.648 63.081  62.109 1.00 29.46  ? 366 ASN A CB  1 
ATOM   2479 C  CG  . ASN A 1 388 ? 31.500 63.681  62.897 1.00 42.82  ? 366 ASN A CG  1 
ATOM   2480 O  OD1 . ASN A 1 388 ? 31.711 64.429  63.852 1.00 43.64  ? 366 ASN A OD1 1 
ATOM   2481 N  ND2 . ASN A 1 388 ? 30.275 63.359  62.497 1.00 49.02  ? 366 ASN A ND2 1 
ATOM   2482 N  N   . LEU A 1 389 ? 34.462 65.635  61.716 1.00 21.40  ? 367 LEU A N   1 
ATOM   2483 C  CA  . LEU A 1 389 ? 34.811 67.012  62.047 1.00 24.59  ? 367 LEU A CA  1 
ATOM   2484 C  C   . LEU A 1 389 ? 34.877 67.882  60.798 1.00 27.88  ? 367 LEU A C   1 
ATOM   2485 O  O   . LEU A 1 389 ? 34.506 69.060  60.837 1.00 23.90  ? 367 LEU A O   1 
ATOM   2486 C  CB  . LEU A 1 389 ? 36.140 67.048  62.798 1.00 24.64  ? 367 LEU A CB  1 
ATOM   2487 C  CG  . LEU A 1 389 ? 36.082 66.567  64.247 1.00 30.30  ? 367 LEU A CG  1 
ATOM   2488 C  CD1 . LEU A 1 389 ? 37.482 66.323  64.777 1.00 29.26  ? 367 LEU A CD1 1 
ATOM   2489 C  CD2 . LEU A 1 389 ? 35.336 67.568  65.117 1.00 33.95  ? 367 LEU A CD2 1 
ATOM   2490 N  N   . ALA A 1 390 ? 35.348 67.320  59.681 1.00 28.25  ? 368 ALA A N   1 
ATOM   2491 C  CA  . ALA A 1 390 ? 35.385 68.082  58.437 1.00 25.48  ? 368 ALA A CA  1 
ATOM   2492 C  C   . ALA A 1 390 ? 33.983 68.479  57.996 1.00 29.39  ? 368 ALA A C   1 
ATOM   2493 O  O   . ALA A 1 390 ? 33.756 69.618  57.570 1.00 29.86  ? 368 ALA A O   1 
ATOM   2494 C  CB  . ALA A 1 390 ? 36.086 67.275  57.344 1.00 25.92  ? 368 ALA A CB  1 
ATOM   2495 N  N   . HIS A 1 391 ? 33.026 67.553  58.098 1.00 30.51  ? 369 HIS A N   1 
ATOM   2496 C  CA  . HIS A 1 391 ? 31.641 67.883  57.777 1.00 31.92  ? 369 HIS A CA  1 
ATOM   2497 C  C   . HIS A 1 391 ? 31.077 68.902  58.758 1.00 35.09  ? 369 HIS A C   1 
ATOM   2498 O  O   . HIS A 1 391 ? 30.300 69.782  58.368 1.00 29.18  ? 369 HIS A O   1 
ATOM   2499 C  CB  . HIS A 1 391 ? 30.789 66.614  57.773 1.00 38.87  ? 369 HIS A CB  1 
ATOM   2500 C  CG  . HIS A 1 391 ? 29.485 66.764  57.053 1.00 53.30  ? 369 HIS A CG  1 
ATOM   2501 N  ND1 . HIS A 1 391 ? 28.273 66.469  57.638 1.00 51.35  ? 369 HIS A ND1 1 
ATOM   2502 C  CD2 . HIS A 1 391 ? 29.204 67.174  55.793 1.00 48.03  ? 369 HIS A CD2 1 
ATOM   2503 C  CE1 . HIS A 1 391 ? 27.302 66.691  56.770 1.00 57.21  ? 369 HIS A CE1 1 
ATOM   2504 N  NE2 . HIS A 1 391 ? 27.840 67.122  55.644 1.00 55.62  ? 369 HIS A NE2 1 
ATOM   2505 N  N   . GLN A 1 392 ? 31.459 68.799  60.035 1.00 31.09  ? 370 GLN A N   1 
ATOM   2506 C  CA  . GLN A 1 392 ? 30.979 69.746  61.037 1.00 32.07  ? 370 GLN A CA  1 
ATOM   2507 C  C   . GLN A 1 392 ? 31.419 71.167  60.713 1.00 27.47  ? 370 GLN A C   1 
ATOM   2508 O  O   . GLN A 1 392 ? 30.650 72.118  60.890 1.00 32.23  ? 370 GLN A O   1 
ATOM   2509 C  CB  . GLN A 1 392 ? 31.480 69.343  62.424 1.00 29.91  ? 370 GLN A CB  1 
ATOM   2510 C  CG  . GLN A 1 392 ? 30.532 68.452  63.204 1.00 46.43  ? 370 GLN A CG  1 
ATOM   2511 C  CD  . GLN A 1 392 ? 30.896 68.372  64.674 1.00 46.78  ? 370 GLN A CD  1 
ATOM   2512 O  OE1 . GLN A 1 392 ? 31.017 67.285  65.237 1.00 56.73  ? 370 GLN A OE1 1 
ATOM   2513 N  NE2 . GLN A 1 392 ? 31.077 69.529  65.303 1.00 48.56  ? 370 GLN A NE2 1 
ATOM   2514 N  N   . VAL A 1 393 ? 32.659 71.331  60.246 1.00 24.71  ? 371 VAL A N   1 
ATOM   2515 C  CA  . VAL A 1 393 ? 33.145 72.658  59.877 1.00 25.35  ? 371 VAL A CA  1 
ATOM   2516 C  C   . VAL A 1 393 ? 32.300 73.237  58.751 1.00 25.26  ? 371 VAL A C   1 
ATOM   2517 O  O   . VAL A 1 393 ? 31.959 74.427  58.758 1.00 23.20  ? 371 VAL A O   1 
ATOM   2518 C  CB  . VAL A 1 393 ? 34.637 72.594  59.498 1.00 26.60  ? 371 VAL A CB  1 
ATOM   2519 C  CG1 . VAL A 1 393 ? 35.112 73.935  58.952 1.00 24.01  ? 371 VAL A CG1 1 
ATOM   2520 C  CG2 . VAL A 1 393 ? 35.469 72.179  60.702 1.00 24.58  ? 371 VAL A CG2 1 
ATOM   2521 N  N   . GLY A 1 394 ? 31.935 72.406  57.774 1.00 24.97  ? 372 GLY A N   1 
ATOM   2522 C  CA  . GLY A 1 394 ? 31.077 72.881  56.700 1.00 31.39  ? 372 GLY A CA  1 
ATOM   2523 C  C   . GLY A 1 394 ? 29.693 73.263  57.187 1.00 32.80  ? 372 GLY A C   1 
ATOM   2524 O  O   . GLY A 1 394 ? 29.179 74.335  56.857 1.00 33.59  ? 372 GLY A O   1 
ATOM   2525 N  N   . GLN A 1 395 ? 29.072 72.389  57.987 1.00 33.23  ? 373 GLN A N   1 
ATOM   2526 C  CA  . GLN A 1 395 ? 27.719 72.648  58.473 1.00 31.83  ? 373 GLN A CA  1 
ATOM   2527 C  C   . GLN A 1 395 ? 27.640 73.933  59.286 1.00 33.67  ? 373 GLN A C   1 
ATOM   2528 O  O   . GLN A 1 395 ? 26.594 74.592  59.305 1.00 28.90  ? 373 GLN A O   1 
ATOM   2529 C  CB  . GLN A 1 395 ? 27.228 71.478  59.325 1.00 34.10  ? 373 GLN A CB  1 
ATOM   2530 C  CG  . GLN A 1 395 ? 27.050 70.165  58.589 1.00 39.43  ? 373 GLN A CG  1 
ATOM   2531 C  CD  . GLN A 1 395 ? 26.823 69.010  59.545 1.00 51.41  ? 373 GLN A CD  1 
ATOM   2532 O  OE1 . GLN A 1 395 ? 26.244 67.988  59.181 1.00 68.26  ? 373 GLN A OE1 1 
ATOM   2533 N  NE2 . GLN A 1 395 ? 27.278 69.171  60.783 1.00 49.59  ? 373 GLN A NE2 1 
ATOM   2534 N  N   . THR A 1 396 ? 28.728 74.300  59.967 1.00 26.33  ? 374 THR A N   1 
ATOM   2535 C  CA  . THR A 1 396 ? 28.701 75.462  60.850 1.00 27.87  ? 374 THR A CA  1 
ATOM   2536 C  C   . THR A 1 396 ? 28.520 76.761  60.074 1.00 32.06  ? 374 THR A C   1 
ATOM   2537 O  O   . THR A 1 396 ? 27.860 77.686  60.561 1.00 32.77  ? 374 THR A O   1 
ATOM   2538 C  CB  . THR A 1 396 ? 29.987 75.512  61.679 1.00 28.55  ? 374 THR A CB  1 
ATOM   2539 O  OG1 . THR A 1 396 ? 30.139 74.282  62.400 1.00 25.85  ? 374 THR A OG1 1 
ATOM   2540 C  CG2 . THR A 1 396 ? 29.947 76.666  62.669 1.00 31.65  ? 374 THR A CG2 1 
ATOM   2541 N  N   . ILE A 1 397 ? 29.080 76.845  58.869 1.00 25.86  ? 375 ILE A N   1 
ATOM   2542 C  CA  . ILE A 1 397 ? 29.081 78.085  58.097 1.00 27.69  ? 375 ILE A CA  1 
ATOM   2543 C  C   . ILE A 1 397 ? 28.231 78.002  56.837 1.00 28.66  ? 375 ILE A C   1 
ATOM   2544 O  O   . ILE A 1 397 ? 27.978 79.046  56.214 1.00 32.11  ? 375 ILE A O   1 
ATOM   2545 C  CB  . ILE A 1 397 ? 30.520 78.517  57.738 1.00 29.87  ? 375 ILE A CB  1 
ATOM   2546 C  CG1 . ILE A 1 397 ? 30.603 80.032  57.531 1.00 32.50  ? 375 ILE A CG1 1 
ATOM   2547 C  CG2 . ILE A 1 397 ? 31.017 77.764  56.513 1.00 35.85  ? 375 ILE A CG2 1 
ATOM   2548 C  CD1 . ILE A 1 397 ? 30.331 80.836  58.783 1.00 32.82  ? 375 ILE A CD1 1 
ATOM   2549 N  N   . ASN A 1 398 ? 27.781 76.814  56.446 1.00 33.11  ? 376 ASN A N   1 
ATOM   2550 C  CA  . ASN A 1 398 ? 27.002 76.650  55.223 1.00 33.77  ? 376 ASN A CA  1 
ATOM   2551 C  C   . ASN A 1 398 ? 25.739 77.503  55.279 1.00 36.52  ? 376 ASN A C   1 
ATOM   2552 O  O   . ASN A 1 398 ? 24.911 77.310  56.182 1.00 35.73  ? 376 ASN A O   1 
ATOM   2553 C  CB  . ASN A 1 398 ? 26.637 75.180  55.019 1.00 32.05  ? 376 ASN A CB  1 
ATOM   2554 C  CG  . ASN A 1 398 ? 26.164 74.883  53.605 1.00 42.87  ? 376 ASN A CG  1 
ATOM   2555 O  OD1 . ASN A 1 398 ? 25.406 75.651  53.012 1.00 41.57  ? 376 ASN A OD1 1 
ATOM   2556 N  ND2 . ASN A 1 398 ? 26.610 73.757  53.061 1.00 41.41  ? 376 ASN A ND2 1 
ATOM   2557 N  N   . PRO A 1 399 ? 25.553 78.445  54.349 1.00 41.03  ? 377 PRO A N   1 
ATOM   2558 C  CA  . PRO A 1 399 ? 24.346 79.289  54.386 1.00 38.09  ? 377 PRO A CA  1 
ATOM   2559 C  C   . PRO A 1 399 ? 23.046 78.505  54.368 1.00 41.86  ? 377 PRO A C   1 
ATOM   2560 O  O   . PRO A 1 399 ? 22.038 78.988  54.899 1.00 39.98  ? 377 PRO A O   1 
ATOM   2561 C  CB  . PRO A 1 399 ? 24.491 80.156  53.128 1.00 39.68  ? 377 PRO A CB  1 
ATOM   2562 C  CG  . PRO A 1 399 ? 25.949 80.168  52.834 1.00 43.20  ? 377 PRO A CG  1 
ATOM   2563 C  CD  . PRO A 1 399 ? 26.476 78.834  53.269 1.00 39.58  ? 377 PRO A CD  1 
ATOM   2564 N  N   . ASP A 1 400 ? 23.036 77.308  53.776 1.00 43.77  ? 378 ASP A N   1 
ATOM   2565 C  CA  . ASP A 1 400 ? 21.819 76.507  53.728 1.00 45.68  ? 378 ASP A CA  1 
ATOM   2566 C  C   . ASP A 1 400 ? 21.347 76.084  55.113 1.00 48.55  ? 378 ASP A C   1 
ATOM   2567 O  O   . ASP A 1 400 ? 20.168 75.754  55.280 1.00 52.31  ? 378 ASP A O   1 
ATOM   2568 C  CB  . ASP A 1 400 ? 22.036 75.270  52.854 1.00 51.60  ? 378 ASP A CB  1 
ATOM   2569 C  CG  . ASP A 1 400 ? 22.444 75.621  51.436 1.00 56.70  ? 378 ASP A CG  1 
ATOM   2570 O  OD1 . ASP A 1 400 ? 22.460 76.825  51.100 1.00 63.43  ? 378 ASP A OD1 1 
ATOM   2571 O  OD2 . ASP A 1 400 ? 22.748 74.693  50.657 1.00 61.97  ? 378 ASP A OD2 1 
ATOM   2572 N  N   . ASN A 1 401 ? 22.233 76.084  56.107 1.00 44.65  ? 379 ASN A N   1 
ATOM   2573 C  CA  . ASN A 1 401 ? 21.877 75.726  57.473 1.00 42.31  ? 379 ASN A CA  1 
ATOM   2574 C  C   . ASN A 1 401 ? 21.698 76.939  58.376 1.00 48.20  ? 379 ASN A C   1 
ATOM   2575 O  O   . ASN A 1 401 ? 21.485 76.771  59.580 1.00 43.14  ? 379 ASN A O   1 
ATOM   2576 C  CB  . ASN A 1 401 ? 22.938 74.795  58.071 1.00 45.31  ? 379 ASN A CB  1 
ATOM   2577 C  CG  . ASN A 1 401 ? 23.271 73.630  57.162 1.00 51.78  ? 379 ASN A CG  1 
ATOM   2578 O  OD1 . ASN A 1 401 ? 24.438 73.277  56.988 1.00 49.23  ? 379 ASN A OD1 1 
ATOM   2579 N  ND2 . ASN A 1 401 ? 22.245 73.023  56.576 1.00 55.66  ? 379 ASN A ND2 1 
ATOM   2580 N  N   . LEU A 1 402 ? 21.779 78.147  57.830 1.00 44.53  ? 380 LEU A N   1 
ATOM   2581 C  CA  . LEU A 1 402 ? 21.685 79.373  58.608 1.00 40.80  ? 380 LEU A CA  1 
ATOM   2582 C  C   . LEU A 1 402 ? 20.394 80.112  58.282 1.00 44.08  ? 380 LEU A C   1 
ATOM   2583 O  O   . LEU A 1 402 ? 19.701 79.812  57.307 1.00 40.42  ? 380 LEU A O   1 
ATOM   2584 C  CB  . LEU A 1 402 ? 22.895 80.276  58.344 1.00 38.57  ? 380 LEU A CB  1 
ATOM   2585 C  CG  . LEU A 1 402 ? 24.258 79.582  58.367 1.00 41.04  ? 380 LEU A CG  1 
ATOM   2586 C  CD1 . LEU A 1 402 ? 25.366 80.560  58.018 1.00 31.86  ? 380 LEU A CD1 1 
ATOM   2587 C  CD2 . LEU A 1 402 ? 24.512 78.937  59.720 1.00 32.33  ? 380 LEU A CD2 1 
ATOM   2588 N  N   . THR A 1 403 ? 20.080 81.095  59.121 1.00 42.72  ? 381 THR A N   1 
ATOM   2589 C  CA  . THR A 1 403 ? 18.897 81.921  58.930 1.00 44.71  ? 381 THR A CA  1 
ATOM   2590 C  C   . THR A 1 403 ? 19.117 83.251  59.635 1.00 52.17  ? 381 THR A C   1 
ATOM   2591 O  O   . THR A 1 403 ? 20.086 83.432  60.376 1.00 48.26  ? 381 THR A O   1 
ATOM   2592 C  CB  . THR A 1 403 ? 17.635 81.229  59.455 1.00 56.52  ? 381 THR A CB  1 
ATOM   2593 O  OG1 . THR A 1 403 ? 16.497 82.066  59.217 1.00 53.00  ? 381 THR A OG1 1 
ATOM   2594 C  CG2 . THR A 1 403 ? 17.759 80.962  60.947 1.00 48.58  ? 381 THR A CG2 1 
ATOM   2595 N  N   . GLY A 1 404 ? 18.200 84.186  59.386 1.00 51.82  ? 382 GLY A N   1 
ATOM   2596 C  CA  . GLY A 1 404 ? 18.240 85.469  60.057 1.00 46.89  ? 382 GLY A CA  1 
ATOM   2597 C  C   . GLY A 1 404 ? 19.459 86.296  59.679 1.00 46.80  ? 382 GLY A C   1 
ATOM   2598 O  O   . GLY A 1 404 ? 19.942 86.273  58.543 1.00 47.17  ? 382 GLY A O   1 
ATOM   2599 N  N   . THR A 1 405 ? 19.965 87.039  60.667 1.00 38.78  ? 383 THR A N   1 
ATOM   2600 C  CA  . THR A 1 405 ? 21.097 87.930  60.430 1.00 44.46  ? 383 THR A CA  1 
ATOM   2601 C  C   . THR A 1 405 ? 22.369 87.159  60.098 1.00 32.74  ? 383 THR A C   1 
ATOM   2602 O  O   . THR A 1 405 ? 23.185 87.632  59.299 1.00 38.79  ? 383 THR A O   1 
ATOM   2603 C  CB  . THR A 1 405 ? 21.327 88.819  61.652 1.00 43.20  ? 383 THR A CB  1 
ATOM   2604 O  OG1 . THR A 1 405 ? 21.511 87.997  62.812 1.00 39.88  ? 383 THR A OG1 1 
ATOM   2605 C  CG2 . THR A 1 405 ? 20.131 89.736  61.876 1.00 37.98  ? 383 THR A CG2 1 
ATOM   2606 N  N   . PHE A 1 406 ? 22.554 85.981  60.698 1.00 36.84  ? 384 PHE A N   1 
ATOM   2607 C  CA  . PHE A 1 406 ? 23.751 85.187  60.436 1.00 39.49  ? 384 PHE A CA  1 
ATOM   2608 C  C   . PHE A 1 406 ? 23.829 84.785  58.967 1.00 34.85  ? 384 PHE A C   1 
ATOM   2609 O  O   . PHE A 1 406 ? 24.877 84.931  58.327 1.00 34.39  ? 384 PHE A O   1 
ATOM   2610 C  CB  . PHE A 1 406 ? 23.761 83.957  61.348 1.00 36.25  ? 384 PHE A CB  1 
ATOM   2611 C  CG  . PHE A 1 406 ? 25.067 83.203  61.359 1.00 32.96  ? 384 PHE A CG  1 
ATOM   2612 C  CD1 . PHE A 1 406 ? 26.228 83.767  60.853 1.00 30.50  ? 384 PHE A CD1 1 
ATOM   2613 C  CD2 . PHE A 1 406 ? 25.129 81.924  61.888 1.00 32.35  ? 384 PHE A CD2 1 
ATOM   2614 C  CE1 . PHE A 1 406 ? 27.420 83.065  60.867 1.00 35.14  ? 384 PHE A CE1 1 
ATOM   2615 C  CE2 . PHE A 1 406 ? 26.318 81.219  61.908 1.00 32.96  ? 384 PHE A CE2 1 
ATOM   2616 C  CZ  . PHE A 1 406 ? 27.464 81.790  61.396 1.00 29.98  ? 384 PHE A CZ  1 
ATOM   2617 N  N   . LYS A 1 407 ? 22.724 84.278  58.413 1.00 34.90  ? 385 LYS A N   1 
ATOM   2618 C  CA  . LYS A 1 407 ? 22.715 83.908  57.001 1.00 39.29  ? 385 LYS A CA  1 
ATOM   2619 C  C   . LYS A 1 407 ? 22.970 85.118  56.111 1.00 38.75  ? 385 LYS A C   1 
ATOM   2620 O  O   . LYS A 1 407 ? 23.708 85.027  55.123 1.00 36.53  ? 385 LYS A O   1 
ATOM   2621 C  CB  . LYS A 1 407 ? 21.385 83.247  56.635 1.00 38.81  ? 385 LYS A CB  1 
ATOM   2622 C  CG  . LYS A 1 407 ? 21.201 83.028  55.140 1.00 46.16  ? 385 LYS A CG  1 
ATOM   2623 C  CD  . LYS A 1 407 ? 20.061 82.069  54.841 1.00 42.89  ? 385 LYS A CD  1 
ATOM   2624 C  CE  . LYS A 1 407 ? 19.883 81.887  53.341 1.00 42.16  ? 385 LYS A CE  1 
ATOM   2625 N  NZ  . LYS A 1 407 ? 18.868 80.847  53.019 1.00 45.98  ? 385 LYS A NZ  1 
ATOM   2626 N  N   . ASN A 1 408 ? 22.371 86.263  56.449 1.00 39.29  ? 386 ASN A N   1 
ATOM   2627 C  CA  . ASN A 1 408 ? 22.584 87.470  55.656 1.00 37.34  ? 386 ASN A CA  1 
ATOM   2628 C  C   . ASN A 1 408 ? 24.037 87.921  55.700 1.00 37.46  ? 386 ASN A C   1 
ATOM   2629 O  O   . ASN A 1 408 ? 24.550 88.454  54.709 1.00 31.34  ? 386 ASN A O   1 
ATOM   2630 C  CB  . ASN A 1 408 ? 21.664 88.589  56.146 1.00 37.04  ? 386 ASN A CB  1 
ATOM   2631 C  CG  . ASN A 1 408 ? 20.197 88.270  55.937 1.00 51.73  ? 386 ASN A CG  1 
ATOM   2632 O  OD1 . ASN A 1 408 ? 19.840 87.477  55.066 1.00 51.68  ? 386 ASN A OD1 1 
ATOM   2633 N  ND2 . ASN A 1 408 ? 19.337 88.889  56.738 1.00 51.60  ? 386 ASN A ND2 1 
ATOM   2634 N  N   . PHE A 1 409 ? 24.714 87.720  56.833 1.00 29.50  ? 387 PHE A N   1 
ATOM   2635 C  CA  . PHE A 1 409 ? 26.135 88.046  56.911 1.00 36.95  ? 387 PHE A CA  1 
ATOM   2636 C  C   . PHE A 1 409 ? 26.956 87.155  55.987 1.00 28.50  ? 387 PHE A C   1 
ATOM   2637 O  O   . PHE A 1 409 ? 27.872 87.632  55.308 1.00 32.84  ? 387 PHE A O   1 
ATOM   2638 C  CB  . PHE A 1 409 ? 26.621 87.918  58.357 1.00 31.84  ? 387 PHE A CB  1 
ATOM   2639 C  CG  . PHE A 1 409 ? 28.038 88.381  58.569 1.00 34.37  ? 387 PHE A CG  1 
ATOM   2640 C  CD1 . PHE A 1 409 ? 29.105 87.523  58.352 1.00 34.66  ? 387 PHE A CD1 1 
ATOM   2641 C  CD2 . PHE A 1 409 ? 28.301 89.673  58.994 1.00 33.84  ? 387 PHE A CD2 1 
ATOM   2642 C  CE1 . PHE A 1 409 ? 30.404 87.947  58.545 1.00 27.85  ? 387 PHE A CE1 1 
ATOM   2643 C  CE2 . PHE A 1 409 ? 29.600 90.102  59.192 1.00 41.84  ? 387 PHE A CE2 1 
ATOM   2644 C  CZ  . PHE A 1 409 ? 30.653 89.237  58.967 1.00 35.44  ? 387 PHE A CZ  1 
ATOM   2645 N  N   . VAL A 1 410 ? 26.640 85.860  55.945 1.00 28.42  ? 388 VAL A N   1 
ATOM   2646 C  CA  . VAL A 1 410 ? 27.430 84.929  55.146 1.00 30.79  ? 388 VAL A CA  1 
ATOM   2647 C  C   . VAL A 1 410 ? 27.135 85.114  53.661 1.00 31.76  ? 388 VAL A C   1 
ATOM   2648 O  O   . VAL A 1 410 ? 28.050 85.299  52.851 1.00 31.20  ? 388 VAL A O   1 
ATOM   2649 C  CB  . VAL A 1 410 ? 27.172 83.482  55.601 1.00 31.03  ? 388 VAL A CB  1 
ATOM   2650 C  CG1 . VAL A 1 410 ? 27.938 82.506  54.725 1.00 24.72  ? 388 VAL A CG1 1 
ATOM   2651 C  CG2 . VAL A 1 410 ? 27.562 83.312  57.061 1.00 30.26  ? 388 VAL A CG2 1 
ATOM   2652 N  N   . THR A 1 411 ? 25.854 85.074  53.283 1.00 28.61  ? 389 THR A N   1 
ATOM   2653 C  CA  . THR A 1 411 ? 25.502 85.177  51.869 1.00 33.68  ? 389 THR A CA  1 
ATOM   2654 C  C   . THR A 1 411 ? 25.796 86.566  51.318 1.00 32.09  ? 389 THR A C   1 
ATOM   2655 O  O   . THR A 1 411 ? 26.194 86.707  50.157 1.00 40.32  ? 389 THR A O   1 
ATOM   2656 C  CB  . THR A 1 411 ? 24.026 84.833  51.659 1.00 34.25  ? 389 THR A CB  1 
ATOM   2657 O  OG1 . THR A 1 411 ? 23.206 85.848  52.251 1.00 36.17  ? 389 THR A OG1 1 
ATOM   2658 C  CG2 . THR A 1 411 ? 23.693 83.489  52.281 1.00 34.09  ? 389 THR A CG2 1 
ATOM   2659 N  N   . GLY A 1 412 ? 25.610 87.601  52.131 1.00 33.42  ? 390 GLY A N   1 
ATOM   2660 C  CA  . GLY A 1 412 ? 25.750 88.958  51.647 1.00 32.18  ? 390 GLY A CA  1 
ATOM   2661 C  C   . GLY A 1 412 ? 27.148 89.533  51.739 1.00 33.70  ? 390 GLY A C   1 
ATOM   2662 O  O   . GLY A 1 412 ? 27.480 90.467  51.002 1.00 34.36  ? 390 GLY A O   1 
ATOM   2663 N  N   . PHE A 1 413 ? 27.983 88.992  52.626 1.00 33.60  ? 391 PHE A N   1 
ATOM   2664 C  CA  . PHE A 1 413 ? 29.267 89.626  52.899 1.00 32.01  ? 391 PHE A CA  1 
ATOM   2665 C  C   . PHE A 1 413 ? 30.417 88.628  52.985 1.00 31.50  ? 391 PHE A C   1 
ATOM   2666 O  O   . PHE A 1 413 ? 31.388 88.736  52.228 1.00 37.57  ? 391 PHE A O   1 
ATOM   2667 C  CB  . PHE A 1 413 ? 29.175 90.444  54.190 1.00 33.49  ? 391 PHE A CB  1 
ATOM   2668 C  CG  . PHE A 1 413 ? 28.134 91.527  54.142 1.00 34.66  ? 391 PHE A CG  1 
ATOM   2669 C  CD1 . PHE A 1 413 ? 28.442 92.781  53.643 1.00 36.30  ? 391 PHE A CD1 1 
ATOM   2670 C  CD2 . PHE A 1 413 ? 26.842 91.286  54.583 1.00 36.71  ? 391 PHE A CD2 1 
ATOM   2671 C  CE1 . PHE A 1 413 ? 27.486 93.777  53.591 1.00 40.63  ? 391 PHE A CE1 1 
ATOM   2672 C  CE2 . PHE A 1 413 ? 25.880 92.278  54.534 1.00 43.09  ? 391 PHE A CE2 1 
ATOM   2673 C  CZ  . PHE A 1 413 ? 26.202 93.525  54.038 1.00 38.22  ? 391 PHE A CZ  1 
ATOM   2674 N  N   . LEU A 1 414 ? 30.326 87.662  53.903 1.00 27.29  ? 392 LEU A N   1 
ATOM   2675 C  CA  . LEU A 1 414 ? 31.440 86.742  54.123 1.00 31.60  ? 392 LEU A CA  1 
ATOM   2676 C  C   . LEU A 1 414 ? 31.748 85.934  52.867 1.00 27.26  ? 392 LEU A C   1 
ATOM   2677 O  O   . LEU A 1 414 ? 32.903 85.860  52.431 1.00 28.07  ? 392 LEU A O   1 
ATOM   2678 C  CB  . LEU A 1 414 ? 31.134 85.813  55.299 1.00 23.87  ? 392 LEU A CB  1 
ATOM   2679 C  CG  . LEU A 1 414 ? 32.279 84.885  55.720 1.00 28.83  ? 392 LEU A CG  1 
ATOM   2680 C  CD1 . LEU A 1 414 ? 33.494 85.691  56.159 1.00 30.23  ? 392 LEU A CD1 1 
ATOM   2681 C  CD2 . LEU A 1 414 ? 31.839 83.931  56.821 1.00 25.76  ? 392 LEU A CD2 1 
ATOM   2682 N  N   . ALA A 1 415 ? 30.727 85.325  52.269 1.00 27.10  ? 393 ALA A N   1 
ATOM   2683 C  CA  . ALA A 1 415 ? 30.903 84.477  51.090 1.00 30.11  ? 393 ALA A CA  1 
ATOM   2684 C  C   . ALA A 1 415 ? 30.821 85.261  49.792 1.00 37.19  ? 393 ALA A C   1 
ATOM   2685 O  O   . ALA A 1 415 ? 30.287 84.768  48.792 1.00 39.24  ? 393 ALA A O   1 
ATOM   2686 C  CB  . ALA A 1 415 ? 29.876 83.350  51.107 1.00 28.31  ? 393 ALA A CB  1 
ATOM   2687 N  N   . THR A 1 416 ? 31.328 86.495  49.780 1.00 36.61  ? 394 THR A N   1 
ATOM   2688 C  CA  . THR A 1 416 ? 31.415 87.300  48.567 1.00 37.34  ? 394 THR A CA  1 
ATOM   2689 C  C   . THR A 1 416 ? 32.785 87.962  48.506 1.00 41.32  ? 394 THR A C   1 
ATOM   2690 O  O   . THR A 1 416 ? 33.651 87.729  49.359 1.00 38.48  ? 394 THR A O   1 
ATOM   2691 C  CB  . THR A 1 416 ? 30.314 88.368  48.494 1.00 35.09  ? 394 THR A CB  1 
ATOM   2692 O  OG1 . THR A 1 416 ? 30.588 89.399  49.450 1.00 35.24  ? 394 THR A OG1 1 
ATOM   2693 C  CG2 . THR A 1 416 ? 28.943 87.772  48.763 1.00 30.15  ? 394 THR A CG2 1 
ATOM   2694 N  N   . CYS A 1 417 ? 32.969 88.803  47.481 1.00 34.59  ? 395 CYS A N   1 
ATOM   2695 C  CA  . CYS A 1 417 ? 34.234 89.493  47.245 1.00 39.10  ? 395 CYS A CA  1 
ATOM   2696 C  C   . CYS A 1 417 ? 34.120 90.610  46.217 1.00 48.95  ? 395 CYS A C   1 
ATOM   2697 O  O   . CYS A 1 417 ? 34.171 90.357  45.008 1.00 50.54  ? 395 CYS A O   1 
ATOM   2698 C  CB  . CYS A 1 417 ? 35.298 88.521  46.769 1.00 39.51  ? 395 CYS A CB  1 
ATOM   2699 S  SG  . CYS A 1 417 ? 36.961 89.300  46.618 1.00 41.48  ? 395 CYS A SG  1 
ATOM   2700 N  N   . ASN A 1 418 ? 34.019 91.853  46.688 1.00 47.36  ? 396 ASN A N   1 
ATOM   2701 C  CA  . ASN A 1 418 ? 33.972 92.986  45.777 1.00 51.82  ? 396 ASN A CA  1 
ATOM   2702 C  C   . ASN A 1 418 ? 35.288 93.199  45.049 1.00 52.53  ? 396 ASN A C   1 
ATOM   2703 O  O   . ASN A 1 418 ? 35.309 93.959  44.081 1.00 58.46  ? 396 ASN A O   1 
ATOM   2704 C  CB  . ASN A 1 418 ? 33.594 94.257  46.533 1.00 43.34  ? 396 ASN A CB  1 
ATOM   2705 C  CG  . ASN A 1 418 ? 32.331 94.094  47.350 1.00 40.70  ? 396 ASN A CG  1 
ATOM   2706 O  OD1 . ASN A 1 418 ? 31.483 93.263  47.042 1.00 41.86  ? 396 ASN A OD1 1 
ATOM   2707 N  ND2 . ASN A 1 418 ? 32.208 94.886  48.414 1.00 40.02  ? 396 ASN A ND2 1 
ATOM   2708 N  N   . ASN A 1 419 ? 36.295 92.467  45.431 1.00 57.13  ? 397 ASN A N   1 
ATOM   2709 C  CA  . ASN A 1 419 ? 37.578 92.675  44.746 1.00 53.65  ? 397 ASN A CA  1 
ATOM   2710 C  C   . ASN A 1 419 ? 37.451 91.972  43.400 1.00 64.17  ? 397 ASN A C   1 
ATOM   2711 O  O   . ASN A 1 419 ? 37.483 92.674  42.411 1.00 60.24  ? 397 ASN A O   1 
ATOM   2712 C  CB  . ASN A 1 419 ? 38.691 92.379  45.752 1.00 53.77  ? 397 ASN A CB  1 
ATOM   2713 C  CG  . ASN A 1 419 ? 39.829 91.588  45.191 1.00 61.53  ? 397 ASN A CG  1 
ATOM   2714 O  OD1 . ASN A 1 419 ? 40.029 91.603  44.002 1.00 74.73  ? 397 ASN A OD1 1 
ATOM   2715 N  ND2 . ASN A 1 419 ? 40.593 90.938  46.047 1.00 59.92  ? 397 ASN A ND2 1 
ATOM   2716 N  N   . SER A 1 431 ? 41.275 86.769  41.131 1.00 58.83  ? 409 SER A N   1 
ATOM   2717 C  CA  . SER A 1 431 ? 42.102 87.440  42.165 1.00 60.85  ? 409 SER A CA  1 
ATOM   2718 C  C   . SER A 1 431 ? 42.723 86.395  43.098 1.00 56.46  ? 409 SER A C   1 
ATOM   2719 O  O   . SER A 1 431 ? 41.987 85.790  43.850 1.00 57.49  ? 409 SER A O   1 
ATOM   2720 C  CB  . SER A 1 431 ? 41.286 88.418  42.929 1.00 58.08  ? 409 SER A CB  1 
ATOM   2721 O  OG  . SER A 1 431 ? 42.093 89.089  43.865 1.00 68.02  ? 409 SER A OG  1 
ATOM   2722 N  N   . PRO A 1 432 ? 44.057 86.231  43.147 1.00 47.60  ? 410 PRO A N   1 
ATOM   2723 C  CA  . PRO A 1 432 ? 44.679 85.203  43.948 1.00 50.55  ? 410 PRO A CA  1 
ATOM   2724 C  C   . PRO A 1 432 ? 44.369 85.338  45.434 1.00 46.26  ? 410 PRO A C   1 
ATOM   2725 O  O   . PRO A 1 432 ? 44.248 86.415  45.927 1.00 44.94  ? 410 PRO A O   1 
ATOM   2726 C  CB  . PRO A 1 432 ? 46.174 85.491  43.829 1.00 53.62  ? 410 PRO A CB  1 
ATOM   2727 C  CG  . PRO A 1 432 ? 46.300 86.270  42.576 1.00 47.56  ? 410 PRO A CG  1 
ATOM   2728 C  CD  . PRO A 1 432 ? 45.039 87.085  42.545 1.00 53.80  ? 410 PRO A CD  1 
ATOM   2729 N  N   . PRO A 1 433 ? 44.367 84.232  46.190 1.00 42.31  ? 411 PRO A N   1 
ATOM   2730 C  CA  . PRO A 1 433 ? 44.178 84.294  47.615 1.00 37.03  ? 411 PRO A CA  1 
ATOM   2731 C  C   . PRO A 1 433 ? 45.244 85.180  48.270 1.00 34.94  ? 411 PRO A C   1 
ATOM   2732 O  O   . PRO A 1 433 ? 46.369 85.176  47.866 1.00 35.21  ? 411 PRO A O   1 
ATOM   2733 C  CB  . PRO A 1 433 ? 44.364 82.860  48.107 1.00 36.63  ? 411 PRO A CB  1 
ATOM   2734 C  CG  . PRO A 1 433 ? 44.212 82.003  46.896 1.00 43.23  ? 411 PRO A CG  1 
ATOM   2735 C  CD  . PRO A 1 433 ? 44.501 82.880  45.703 1.00 47.79  ? 411 PRO A CD  1 
ATOM   2736 N  N   . GLY A 1 434 ? 44.826 85.894  49.305 1.00 32.45  ? 412 GLY A N   1 
ATOM   2737 C  CA  . GLY A 1 434 ? 45.713 86.786  50.064 1.00 38.26  ? 412 GLY A CA  1 
ATOM   2738 C  C   . GLY A 1 434 ? 45.911 88.117  49.370 1.00 37.81  ? 412 GLY A C   1 
ATOM   2739 O  O   . GLY A 1 434 ? 46.863 88.766  49.659 1.00 42.83  ? 412 GLY A O   1 
ATOM   2740 N  N   . THR A 1 435 ? 44.995 88.493  48.496 1.00 36.34  ? 413 THR A N   1 
ATOM   2741 C  CA  . THR A 1 435 ? 45.121 89.760  47.752 1.00 38.37  ? 413 THR A CA  1 
ATOM   2742 C  C   . THR A 1 435 ? 44.305 90.846  48.442 1.00 39.65  ? 413 THR A C   1 
ATOM   2743 O  O   . THR A 1 435 ? 43.130 90.632  48.654 1.00 41.06  ? 413 THR A O   1 
ATOM   2744 C  CB  . THR A 1 435 ? 44.623 89.594  46.315 1.00 46.28  ? 413 THR A CB  1 
ATOM   2745 O  OG1 . THR A 1 435 ? 45.466 88.658  45.668 1.00 48.26  ? 413 THR A OG1 1 
ATOM   2746 C  CG2 . THR A 1 435 ? 44.615 90.881  45.533 1.00 45.85  ? 413 THR A CG2 1 
ATOM   2747 N  N   . VAL A 1 436 ? 44.942 91.959  48.769 1.00 34.15  ? 414 VAL A N   1 
ATOM   2748 C  CA  . VAL A 1 436 ? 44.212 93.097  49.376 1.00 42.03  ? 414 VAL A CA  1 
ATOM   2749 C  C   . VAL A 1 436 ? 44.139 94.224  48.347 1.00 39.97  ? 414 VAL A C   1 
ATOM   2750 O  O   . VAL A 1 436 ? 45.160 94.656  47.911 1.00 39.32  ? 414 VAL A O   1 
ATOM   2751 C  CB  . VAL A 1 436 ? 44.880 93.570  50.671 1.00 38.27  ? 414 VAL A CB  1 
ATOM   2752 C  CG1 . VAL A 1 436 ? 44.234 94.824  51.195 1.00 40.32  ? 414 VAL A CG1 1 
ATOM   2753 C  CG2 . VAL A 1 436 ? 44.857 92.498  51.719 1.00 39.28  ? 414 VAL A CG2 1 
ATOM   2754 N  N   . THR A 1 437 ? 42.936 94.648  48.003 1.00 42.08  ? 415 THR A N   1 
ATOM   2755 C  CA  . THR A 1 437 ? 42.710 95.747  47.073 1.00 41.95  ? 415 THR A CA  1 
ATOM   2756 C  C   . THR A 1 437 ? 41.885 96.832  47.758 1.00 43.78  ? 415 THR A C   1 
ATOM   2757 O  O   . THR A 1 437 ? 41.449 96.685  48.903 1.00 38.47  ? 415 THR A O   1 
ATOM   2758 C  CB  . THR A 1 437 ? 42.006 95.263  45.800 1.00 41.13  ? 415 THR A CB  1 
ATOM   2759 O  OG1 . THR A 1 437 ? 40.622 95.020  46.081 1.00 42.66  ? 415 THR A OG1 1 
ATOM   2760 C  CG2 . THR A 1 437 ? 42.649 93.985  45.280 1.00 43.83  ? 415 THR A CG2 1 
ATOM   2761 N  N   . THR A 1 438 ? 41.667 97.933  47.038 1.00 40.98  ? 416 THR A N   1 
ATOM   2762 C  CA  . THR A 1 438 ? 40.853 99.021  47.564 1.00 43.58  ? 416 THR A CA  1 
ATOM   2763 C  C   . THR A 1 438 ? 39.373 98.668  47.632 1.00 38.88  ? 416 THR A C   1 
ATOM   2764 O  O   . THR A 1 438 ? 38.606 99.412  48.251 1.00 41.95  ? 416 THR A O   1 
ATOM   2765 C  CB  . THR A 1 438 ? 41.037 100.283 46.717 1.00 44.41  ? 416 THR A CB  1 
ATOM   2766 O  OG1 . THR A 1 438 ? 40.677 100.006 45.358 1.00 48.45  ? 416 THR A OG1 1 
ATOM   2767 C  CG2 . THR A 1 438 ? 42.482 100.756 46.771 1.00 33.80  ? 416 THR A CG2 1 
ATOM   2768 N  N   . GLN A 1 439 ? 38.955 97.563  47.018 1.00 37.23  ? 417 GLN A N   1 
ATOM   2769 C  CA  . GLN A 1 439 ? 37.565 97.127  47.055 1.00 44.82  ? 417 GLN A CA  1 
ATOM   2770 C  C   . GLN A 1 439 ? 37.371 95.870  47.893 1.00 41.64  ? 417 GLN A C   1 
ATOM   2771 O  O   . GLN A 1 439 ? 36.295 95.265  47.845 1.00 46.14  ? 417 GLN A O   1 
ATOM   2772 C  CB  . GLN A 1 439 ? 37.045 96.901  45.634 1.00 51.62  ? 417 GLN A CB  1 
ATOM   2773 C  CG  . GLN A 1 439 ? 36.826 98.182  44.842 1.00 53.59  ? 417 GLN A CG  1 
ATOM   2774 C  CD  . GLN A 1 439 ? 35.817 99.108  45.496 1.00 61.99  ? 417 GLN A CD  1 
ATOM   2775 O  OE1 . GLN A 1 439 ? 34.738 98.679  45.906 1.00 58.84  ? 417 GLN A OE1 1 
ATOM   2776 N  NE2 . GLN A 1 439 ? 36.164 100.386 45.596 1.00 55.58  ? 417 GLN A NE2 1 
ATOM   2777 N  N   . THR A 1 440 ? 38.385 95.462  48.659 1.00 36.41  ? 418 THR A N   1 
ATOM   2778 C  CA  . THR A 1 440 ? 38.248 94.281  49.506 1.00 38.17  ? 418 THR A CA  1 
ATOM   2779 C  C   . THR A 1 440 ? 37.233 94.511  50.620 1.00 36.81  ? 418 THR A C   1 
ATOM   2780 O  O   . THR A 1 440 ? 36.474 93.600  50.971 1.00 33.01  ? 418 THR A O   1 
ATOM   2781 C  CB  . THR A 1 440 ? 39.606 93.897  50.097 1.00 38.69  ? 418 THR A CB  1 
ATOM   2782 O  OG1 . THR A 1 440 ? 40.540 93.648  49.039 1.00 38.29  ? 418 THR A OG1 1 
ATOM   2783 C  CG2 . THR A 1 440 ? 39.486 92.650  50.966 1.00 33.97  ? 418 THR A CG2 1 
ATOM   2784 N  N   . PHE A 1 441 ? 37.195 95.725  51.171 1.00 37.39  ? 419 PHE A N   1 
ATOM   2785 C  CA  . PHE A 1 441 ? 36.398 96.005  52.359 1.00 32.77  ? 419 PHE A CA  1 
ATOM   2786 C  C   . PHE A 1 441 ? 34.928 95.665  52.138 1.00 36.66  ? 419 PHE A C   1 
ATOM   2787 O  O   . PHE A 1 441 ? 34.425 95.672  51.011 1.00 40.21  ? 419 PHE A O   1 
ATOM   2788 C  CB  . PHE A 1 441 ? 36.541 97.475  52.761 1.00 34.24  ? 419 PHE A CB  1 
ATOM   2789 C  CG  . PHE A 1 441 ? 35.848 98.434  51.831 1.00 34.29  ? 419 PHE A CG  1 
ATOM   2790 C  CD1 . PHE A 1 441 ? 36.454 98.840  50.653 1.00 35.40  ? 419 PHE A CD1 1 
ATOM   2791 C  CD2 . PHE A 1 441 ? 34.595 98.938  52.142 1.00 41.22  ? 419 PHE A CD2 1 
ATOM   2792 C  CE1 . PHE A 1 441 ? 35.820 99.724  49.798 1.00 39.90  ? 419 PHE A CE1 1 
ATOM   2793 C  CE2 . PHE A 1 441 ? 33.956 99.821  51.292 1.00 40.31  ? 419 PHE A CE2 1 
ATOM   2794 C  CZ  . PHE A 1 441 ? 34.570 100.215 50.118 1.00 42.50  ? 419 PHE A CZ  1 
ATOM   2795 N  N   . ALA A 1 442 ? 34.244 95.356  53.240 1.00 33.65  ? 420 ALA A N   1 
ATOM   2796 C  CA  . ALA A 1 442 ? 32.845 94.935  53.274 1.00 37.36  ? 420 ALA A CA  1 
ATOM   2797 C  C   . ALA A 1 442 ? 32.598 93.638  52.515 1.00 32.50  ? 420 ALA A C   1 
ATOM   2798 O  O   . ALA A 1 442 ? 31.442 93.303  52.227 1.00 29.90  ? 420 ALA A O   1 
ATOM   2799 C  CB  . ALA A 1 442 ? 31.910 96.033  52.750 1.00 40.35  ? 420 ALA A CB  1 
ATOM   2800 N  N   . SER A 1 443 ? 33.653 92.894  52.187 1.00 34.88  ? 421 SER A N   1 
ATOM   2801 C  CA  . SER A 1 443 ? 33.530 91.625  51.485 1.00 37.44  ? 421 SER A CA  1 
ATOM   2802 C  C   . SER A 1 443 ? 34.528 90.637  52.070 1.00 32.40  ? 421 SER A C   1 
ATOM   2803 O  O   . SER A 1 443 ? 35.574 91.029  52.593 1.00 32.21  ? 421 SER A O   1 
ATOM   2804 C  CB  . SER A 1 443 ? 33.761 91.789  49.976 1.00 34.71  ? 421 SER A CB  1 
ATOM   2805 O  OG  . SER A 1 443 ? 35.119 92.074  49.687 1.00 40.07  ? 421 SER A OG  1 
ATOM   2806 N  N   . GLY A 1 444 ? 34.186 89.350  51.989 1.00 33.31  ? 422 GLY A N   1 
ATOM   2807 C  CA  . GLY A 1 444 ? 35.051 88.328  52.556 1.00 28.66  ? 422 GLY A CA  1 
ATOM   2808 C  C   . GLY A 1 444 ? 36.342 88.168  51.777 1.00 27.45  ? 422 GLY A C   1 
ATOM   2809 O  O   . GLY A 1 444 ? 37.435 88.244  52.343 1.00 30.11  ? 422 GLY A O   1 
ATOM   2810 N  N   . CYS A 1 445 ? 36.233 87.949  50.467 1.00 30.54  ? 423 CYS A N   1 
ATOM   2811 C  CA  . CYS A 1 445 ? 37.401 87.881  49.590 1.00 26.21  ? 423 CYS A CA  1 
ATOM   2812 C  C   . CYS A 1 445 ? 38.393 86.811  50.041 1.00 30.77  ? 423 CYS A C   1 
ATOM   2813 O  O   . CYS A 1 445 ? 39.598 86.925  49.823 1.00 32.83  ? 423 CYS A O   1 
ATOM   2814 C  CB  . CYS A 1 445 ? 38.073 89.256  49.503 1.00 35.35  ? 423 CYS A CB  1 
ATOM   2815 S  SG  . CYS A 1 445 ? 37.229 90.377  48.331 1.00 37.61  ? 423 CYS A SG  1 
ATOM   2816 N  N   . ALA A 1 446 ? 37.887 85.767  50.682 1.00 30.61  ? 424 ALA A N   1 
ATOM   2817 C  CA  . ALA A 1 446 ? 38.713 84.662  51.142 1.00 24.25  ? 424 ALA A CA  1 
ATOM   2818 C  C   . ALA A 1 446 ? 38.254 83.330  50.565 1.00 32.58  ? 424 ALA A C   1 
ATOM   2819 O  O   . ALA A 1 446 ? 38.517 82.279  51.157 1.00 28.24  ? 424 ALA A O   1 
ATOM   2820 C  CB  . ALA A 1 446 ? 38.718 84.608  52.668 1.00 26.55  ? 424 ALA A CB  1 
ATOM   2821 N  N   . TYR A 1 447 ? 37.574 83.394  49.435 1.00 29.23  ? 425 TYR A N   1 
ATOM   2822 C  CA  . TYR A 1 447 ? 37.079 82.194  48.730 1.00 33.07  ? 425 TYR A CA  1 
ATOM   2823 C  C   . TYR A 1 447 ? 36.257 81.304  49.661 1.00 28.86  ? 425 TYR A C   1 
ATOM   2824 O  O   . TYR A 1 447 ? 36.289 80.152  49.523 1.00 29.96  ? 425 TYR A O   1 
ATOM   2825 C  CB  . TYR A 1 447 ? 38.244 81.407  48.139 1.00 35.23  ? 425 TYR A CB  1 
ATOM   2826 C  CG  . TYR A 1 447 ? 38.946 82.090  47.012 1.00 40.06  ? 425 TYR A CG  1 
ATOM   2827 C  CD1 . TYR A 1 447 ? 38.490 81.890  45.741 1.00 38.38  ? 425 TYR A CD1 1 
ATOM   2828 C  CD2 . TYR A 1 447 ? 40.053 82.886  47.199 1.00 37.94  ? 425 TYR A CD2 1 
ATOM   2829 C  CE1 . TYR A 1 447 ? 39.098 82.485  44.669 1.00 43.37  ? 425 TYR A CE1 1 
ATOM   2830 C  CE2 . TYR A 1 447 ? 40.688 83.486  46.134 1.00 40.19  ? 425 TYR A CE2 1 
ATOM   2831 C  CZ  . TYR A 1 447 ? 40.205 83.265  44.864 1.00 46.98  ? 425 TYR A CZ  1 
ATOM   2832 O  OH  . TYR A 1 447 ? 40.736 83.786  43.742 1.00 50.25  ? 425 TYR A OH  1 
ATOM   2833 N  N   . VAL A 1 448 ? 35.514 81.891  50.559 1.00 26.49  ? 426 VAL A N   1 
ATOM   2834 C  CA  . VAL A 1 448 ? 34.691 81.129  51.495 1.00 27.95  ? 426 VAL A CA  1 
ATOM   2835 C  C   . VAL A 1 448 ? 33.631 80.334  50.745 1.00 29.43  ? 426 VAL A C   1 
ATOM   2836 O  O   . VAL A 1 448 ? 33.364 79.168  51.062 1.00 26.55  ? 426 VAL A O   1 
ATOM   2837 C  CB  . VAL A 1 448 ? 34.063 82.072  52.538 1.00 24.56  ? 426 VAL A CB  1 
ATOM   2838 C  CG1 . VAL A 1 448 ? 32.976 81.356  53.327 1.00 25.04  ? 426 VAL A CG1 1 
ATOM   2839 C  CG2 . VAL A 1 448 ? 35.134 82.624  53.467 1.00 21.02  ? 426 VAL A CG2 1 
ATOM   2840 N  N   . GLU A 1 449 ? 33.017 80.948  49.733 1.00 26.56  ? 427 GLU A N   1 
ATOM   2841 C  CA  . GLU A 1 449 ? 31.982 80.263  48.969 1.00 27.89  ? 427 GLU A CA  1 
ATOM   2842 C  C   . GLU A 1 449 ? 32.559 79.078  48.202 1.00 25.34  ? 427 GLU A C   1 
ATOM   2843 O  O   . GLU A 1 449 ? 31.984 77.983  48.207 1.00 26.14  ? 427 GLU A O   1 
ATOM   2844 C  CB  . GLU A 1 449 ? 31.305 81.252  48.021 1.00 27.88  ? 427 GLU A CB  1 
ATOM   2845 C  CG  . GLU A 1 449 ? 29.909 80.850  47.613 1.00 36.59  ? 427 GLU A CG  1 
ATOM   2846 C  CD  . GLU A 1 449 ? 29.921 79.765  46.568 1.00 38.68  ? 427 GLU A CD  1 
ATOM   2847 O  OE1 . GLU A 1 449 ? 30.834 79.786  45.716 1.00 30.20  ? 427 GLU A OE1 1 
ATOM   2848 O  OE2 . GLU A 1 449 ? 29.032 78.889  46.611 1.00 42.59  ? 427 GLU A OE2 1 
ATOM   2849 N  N   . GLN A 1 450 ? 33.701 79.277  47.542 1.00 22.26  ? 428 GLN A N   1 
ATOM   2850 C  CA  . GLN A 1 450 ? 34.314 78.194  46.781 1.00 26.85  ? 428 GLN A CA  1 
ATOM   2851 C  C   . GLN A 1 450 ? 34.792 77.072  47.695 1.00 31.91  ? 428 GLN A C   1 
ATOM   2852 O  O   . GLN A 1 450 ? 34.697 75.891  47.340 1.00 25.87  ? 428 GLN A O   1 
ATOM   2853 C  CB  . GLN A 1 450 ? 35.470 78.738  45.942 1.00 28.76  ? 428 GLN A CB  1 
ATOM   2854 C  CG  . GLN A 1 450 ? 36.299 77.680  45.237 1.00 25.60  ? 428 GLN A CG  1 
ATOM   2855 C  CD  . GLN A 1 450 ? 37.579 78.246  44.657 1.00 36.61  ? 428 GLN A CD  1 
ATOM   2856 O  OE1 . GLN A 1 450 ? 38.648 78.137  45.258 1.00 33.52  ? 428 GLN A OE1 1 
ATOM   2857 N  NE2 . GLN A 1 450 ? 37.474 78.863  43.486 1.00 33.47  ? 428 GLN A NE2 1 
ATOM   2858 N  N   . THR A 1 451 ? 35.300 77.419  48.881 1.00 26.75  ? 429 THR A N   1 
ATOM   2859 C  CA  . THR A 1 451 ? 35.820 76.397  49.786 1.00 27.44  ? 429 THR A CA  1 
ATOM   2860 C  C   . THR A 1 451 ? 34.696 75.543  50.363 1.00 25.97  ? 429 THR A C   1 
ATOM   2861 O  O   . THR A 1 451 ? 34.871 74.335  50.568 1.00 24.95  ? 429 THR A O   1 
ATOM   2862 C  CB  . THR A 1 451 ? 36.637 77.047  50.904 1.00 27.13  ? 429 THR A CB  1 
ATOM   2863 O  OG1 . THR A 1 451 ? 37.630 77.909  50.332 1.00 27.31  ? 429 THR A OG1 1 
ATOM   2864 C  CG2 . THR A 1 451 ? 37.331 75.986  51.741 1.00 26.55  ? 429 THR A CG2 1 
ATOM   2865 N  N   . ILE A 1 452 ? 33.536 76.148  50.631 1.00 26.11  ? 430 ILE A N   1 
ATOM   2866 C  CA  . ILE A 1 452 ? 32.376 75.368  51.055 1.00 27.77  ? 430 ILE A CA  1 
ATOM   2867 C  C   . ILE A 1 452 ? 31.998 74.360  49.979 1.00 28.25  ? 430 ILE A C   1 
ATOM   2868 O  O   . ILE A 1 452 ? 31.716 73.190  50.269 1.00 23.50  ? 430 ILE A O   1 
ATOM   2869 C  CB  . ILE A 1 452 ? 31.195 76.299  51.392 1.00 27.74  ? 430 ILE A CB  1 
ATOM   2870 C  CG1 . ILE A 1 452 ? 31.464 77.066  52.687 1.00 24.61  ? 430 ILE A CG1 1 
ATOM   2871 C  CG2 . ILE A 1 452 ? 29.900 75.507  51.497 1.00 28.23  ? 430 ILE A CG2 1 
ATOM   2872 C  CD1 . ILE A 1 452 ? 30.649 78.334  52.820 1.00 29.46  ? 430 ILE A CD1 1 
ATOM   2873 N  N   . THR A 1 453 ? 31.996 74.797  48.719 1.00 27.49  ? 431 THR A N   1 
ATOM   2874 C  CA  . THR A 1 453 ? 31.660 73.901  47.619 1.00 32.39  ? 431 THR A CA  1 
ATOM   2875 C  C   . THR A 1 453 ? 32.698 72.799  47.467 1.00 22.50  ? 431 THR A C   1 
ATOM   2876 O  O   . THR A 1 453 ? 32.349 71.627  47.288 1.00 24.82  ? 431 THR A O   1 
ATOM   2877 C  CB  . THR A 1 453 ? 31.534 74.700  46.324 1.00 28.94  ? 431 THR A CB  1 
ATOM   2878 O  OG1 . THR A 1 453 ? 30.585 75.752  46.519 1.00 23.65  ? 431 THR A OG1 1 
ATOM   2879 C  CG2 . THR A 1 453 ? 31.077 73.806  45.178 1.00 25.97  ? 431 THR A CG2 1 
ATOM   2880 N  N   . ASN A 1 454 ? 33.982 73.156  47.538 1.00 24.36  ? 432 ASN A N   1 
ATOM   2881 C  CA  . ASN A 1 454 ? 35.034 72.156  47.401 1.00 24.88  ? 432 ASN A CA  1 
ATOM   2882 C  C   . ASN A 1 454 ? 35.052 71.193  48.580 1.00 25.57  ? 432 ASN A C   1 
ATOM   2883 O  O   . ASN A 1 454 ? 35.397 70.018  48.412 1.00 24.09  ? 432 ASN A O   1 
ATOM   2884 C  CB  . ASN A 1 454 ? 36.392 72.842  47.245 1.00 27.45  ? 432 ASN A CB  1 
ATOM   2885 C  CG  . ASN A 1 454 ? 36.537 73.539  45.907 1.00 32.33  ? 432 ASN A CG  1 
ATOM   2886 O  OD1 . ASN A 1 454 ? 35.747 73.313  44.991 1.00 31.11  ? 432 ASN A OD1 1 
ATOM   2887 N  ND2 . ASN A 1 454 ? 37.546 74.394  45.789 1.00 29.69  ? 432 ASN A ND2 1 
ATOM   2888 N  N   . LEU A 1 455 ? 34.682 71.662  49.773 1.00 25.12  ? 433 LEU A N   1 
ATOM   2889 C  CA  . LEU A 1 455 ? 34.606 70.767  50.923 1.00 23.72  ? 433 LEU A CA  1 
ATOM   2890 C  C   . LEU A 1 455 ? 33.525 69.713  50.723 1.00 24.12  ? 433 LEU A C   1 
ATOM   2891 O  O   . LEU A 1 455 ? 33.753 68.520  50.947 1.00 23.86  ? 433 LEU A O   1 
ATOM   2892 C  CB  . LEU A 1 455 ? 34.346 71.569  52.198 1.00 25.06  ? 433 LEU A CB  1 
ATOM   2893 C  CG  . LEU A 1 455 ? 33.989 70.764  53.449 1.00 25.49  ? 433 LEU A CG  1 
ATOM   2894 C  CD1 . LEU A 1 455 ? 35.097 69.785  53.813 1.00 23.27  ? 433 LEU A CD1 1 
ATOM   2895 C  CD2 . LEU A 1 455 ? 33.697 71.695  54.610 1.00 25.19  ? 433 LEU A CD2 1 
ATOM   2896 N  N   . ASN A 1 456 ? 32.335 70.137  50.295 1.00 25.97  ? 434 ASN A N   1 
ATOM   2897 C  CA  . ASN A 1 456 ? 31.252 69.182  50.104 1.00 29.23  ? 434 ASN A CA  1 
ATOM   2898 C  C   . ASN A 1 456 ? 31.480 68.311  48.876 1.00 26.60  ? 434 ASN A C   1 
ATOM   2899 O  O   . ASN A 1 456 ? 31.056 67.150  48.856 1.00 26.87  ? 434 ASN A O   1 
ATOM   2900 C  CB  . ASN A 1 456 ? 29.920 69.920  50.020 1.00 28.47  ? 434 ASN A CB  1 
ATOM   2901 C  CG  . ASN A 1 456 ? 29.441 70.388  51.377 1.00 28.59  ? 434 ASN A CG  1 
ATOM   2902 O  OD1 . ASN A 1 456 ? 29.665 69.718  52.385 1.00 36.62  ? 434 ASN A OD1 1 
ATOM   2903 N  ND2 . ASN A 1 456 ? 28.789 71.543  51.414 1.00 38.50  ? 434 ASN A ND2 1 
ATOM   2904 N  N   . ASN A 1 457 ? 32.154 68.844  47.852 1.00 20.61  ? 435 ASN A N   1 
ATOM   2905 C  CA  . ASN A 1 457 ? 32.564 68.008  46.727 1.00 21.43  ? 435 ASN A CA  1 
ATOM   2906 C  C   . ASN A 1 457 ? 33.532 66.921  47.176 1.00 24.83  ? 435 ASN A C   1 
ATOM   2907 O  O   . ASN A 1 457 ? 33.425 65.766  46.746 1.00 24.12  ? 435 ASN A O   1 
ATOM   2908 C  CB  . ASN A 1 457 ? 33.207 68.864  45.635 1.00 26.09  ? 435 ASN A CB  1 
ATOM   2909 C  CG  . ASN A 1 457 ? 32.195 69.667  44.844 1.00 27.58  ? 435 ASN A CG  1 
ATOM   2910 O  OD1 . ASN A 1 457 ? 30.987 69.540  45.044 1.00 28.94  ? 435 ASN A OD1 1 
ATOM   2911 N  ND2 . ASN A 1 457 ? 32.687 70.499  43.932 1.00 20.53  ? 435 ASN A ND2 1 
ATOM   2912 N  N   . SER A 1 458 ? 34.489 67.274  48.039 1.00 22.06  ? 436 SER A N   1 
ATOM   2913 C  CA  . SER A 1 458 ? 35.469 66.294  48.496 1.00 26.24  ? 436 SER A CA  1 
ATOM   2914 C  C   . SER A 1 458 ? 34.839 65.253  49.411 1.00 24.65  ? 436 SER A C   1 
ATOM   2915 O  O   . SER A 1 458 ? 35.264 64.092  49.409 1.00 23.63  ? 436 SER A O   1 
ATOM   2916 C  CB  . SER A 1 458 ? 36.626 66.997  49.206 1.00 24.09  ? 436 SER A CB  1 
ATOM   2917 O  OG  . SER A 1 458 ? 36.188 67.615  50.403 1.00 31.55  ? 436 SER A OG  1 
ATOM   2918 N  N   . ILE A 1 459 ? 33.835 65.643  50.199 1.00 26.57  ? 437 ILE A N   1 
ATOM   2919 C  CA  . ILE A 1 459 ? 33.142 64.676  51.044 1.00 25.90  ? 437 ILE A CA  1 
ATOM   2920 C  C   . ILE A 1 459 ? 32.400 63.658  50.186 1.00 26.31  ? 437 ILE A C   1 
ATOM   2921 O  O   . ILE A 1 459 ? 32.422 62.453  50.468 1.00 27.77  ? 437 ILE A O   1 
ATOM   2922 C  CB  . ILE A 1 459 ? 32.197 65.401  52.019 1.00 32.46  ? 437 ILE A CB  1 
ATOM   2923 C  CG1 . ILE A 1 459 ? 33.004 66.119  53.103 1.00 28.78  ? 437 ILE A CG1 1 
ATOM   2924 C  CG2 . ILE A 1 459 ? 31.211 64.422  52.643 1.00 28.48  ? 437 ILE A CG2 1 
ATOM   2925 C  CD1 . ILE A 1 459 ? 32.164 66.960  54.036 1.00 26.35  ? 437 ILE A CD1 1 
ATOM   2926 N  N   . ALA A 1 460 ? 31.741 64.121  49.122 1.00 27.17  ? 438 ALA A N   1 
ATOM   2927 C  CA  . ALA A 1 460 ? 31.079 63.200  48.204 1.00 29.87  ? 438 ALA A CA  1 
ATOM   2928 C  C   . ALA A 1 460 ? 32.090 62.314  47.488 1.00 28.71  ? 438 ALA A C   1 
ATOM   2929 O  O   . ALA A 1 460 ? 31.846 61.118  47.292 1.00 30.78  ? 438 ALA A O   1 
ATOM   2930 C  CB  . ALA A 1 460 ? 30.237 63.980  47.194 1.00 20.71  ? 438 ALA A CB  1 
ATOM   2931 N  N   . HIS A 1 461 ? 33.233 62.884  47.095 1.00 27.67  ? 439 HIS A N   1 
ATOM   2932 C  CA  . HIS A 1 461 ? 34.279 62.096  46.449 1.00 28.36  ? 439 HIS A CA  1 
ATOM   2933 C  C   . HIS A 1 461 ? 34.836 61.030  47.384 1.00 27.33  ? 439 HIS A C   1 
ATOM   2934 O  O   . HIS A 1 461 ? 35.304 59.983  46.923 1.00 29.66  ? 439 HIS A O   1 
ATOM   2935 C  CB  . HIS A 1 461 ? 35.396 63.024  45.961 1.00 27.50  ? 439 HIS A CB  1 
ATOM   2936 C  CG  . HIS A 1 461 ? 36.632 62.310  45.507 1.00 32.54  ? 439 HIS A CG  1 
ATOM   2937 N  ND1 . HIS A 1 461 ? 36.854 61.966  44.191 1.00 39.03  ? 439 HIS A ND1 1 
ATOM   2938 C  CD2 . HIS A 1 461 ? 37.721 61.887  46.192 1.00 30.12  ? 439 HIS A CD2 1 
ATOM   2939 C  CE1 . HIS A 1 461 ? 38.022 61.359  44.086 1.00 39.37  ? 439 HIS A CE1 1 
ATOM   2940 N  NE2 . HIS A 1 461 ? 38.569 61.297  45.287 1.00 36.29  ? 439 HIS A NE2 1 
ATOM   2941 N  N   . PHE A 1 462 ? 34.782 61.268  48.692 1.00 24.72  ? 440 PHE A N   1 
ATOM   2942 C  CA  . PHE A 1 462 ? 35.337 60.358  49.685 1.00 29.14  ? 440 PHE A CA  1 
ATOM   2943 C  C   . PHE A 1 462 ? 34.345 59.291  50.137 1.00 30.56  ? 440 PHE A C   1 
ATOM   2944 O  O   . PHE A 1 462 ? 34.652 58.539  51.068 1.00 31.22  ? 440 PHE A O   1 
ATOM   2945 C  CB  . PHE A 1 462 ? 35.828 61.152  50.901 1.00 24.03  ? 440 PHE A CB  1 
ATOM   2946 C  CG  . PHE A 1 462 ? 37.137 60.668  51.455 1.00 25.08  ? 440 PHE A CG  1 
ATOM   2947 C  CD1 . PHE A 1 462 ? 38.333 61.046  50.870 1.00 23.12  ? 440 PHE A CD1 1 
ATOM   2948 C  CD2 . PHE A 1 462 ? 37.172 59.841  52.565 1.00 31.34  ? 440 PHE A CD2 1 
ATOM   2949 C  CE1 . PHE A 1 462 ? 39.541 60.604  51.378 1.00 29.65  ? 440 PHE A CE1 1 
ATOM   2950 C  CE2 . PHE A 1 462 ? 38.378 59.396  53.080 1.00 22.76  ? 440 PHE A CE2 1 
ATOM   2951 C  CZ  . PHE A 1 462 ? 39.562 59.777  52.484 1.00 25.90  ? 440 PHE A CZ  1 
ATOM   2952 N  N   . GLY A 1 463 ? 33.179 59.201  49.492 1.00 26.99  ? 441 GLY A N   1 
ATOM   2953 C  CA  . GLY A 1 463 ? 32.129 58.321  49.987 1.00 30.91  ? 441 GLY A CA  1 
ATOM   2954 C  C   . GLY A 1 463 ? 32.556 56.867  50.067 1.00 29.18  ? 441 GLY A C   1 
ATOM   2955 O  O   . GLY A 1 463 ? 32.328 56.193  51.075 1.00 28.41  ? 441 GLY A O   1 
ATOM   2956 N  N   . THR A 1 464 ? 33.183 56.366  49.033 1.00 29.69  ? 442 THR A N   1 
ATOM   2957 C  CA  . THR A 1 464 ? 33.649 54.960  49.024 1.00 30.98  ? 442 THR A CA  1 
ATOM   2958 C  C   . THR A 1 464 ? 34.653 54.729  50.165 1.00 34.51  ? 442 THR A C   1 
ATOM   2959 O  O   . THR A 1 464 ? 34.519 53.777  50.868 1.00 29.83  ? 442 THR A O   1 
ATOM   2960 C  CB  . THR A 1 464 ? 34.218 54.619  47.644 1.00 28.53  ? 442 THR A CB  1 
ATOM   2961 O  OG1 . THR A 1 464 ? 33.139 54.527  46.734 1.00 36.18  ? 442 THR A OG1 1 
ATOM   2962 C  CG2 . THR A 1 464 ? 34.970 53.318  47.607 1.00 38.95  ? 442 THR A CG2 1 
ATOM   2963 N  N   . GLN A 1 465 ? 35.618 55.629  50.306 1.00 30.54  ? 443 GLN A N   1 
ATOM   2964 C  CA  . GLN A 1 465 ? 36.673 55.560  51.340 1.00 31.51  ? 443 GLN A CA  1 
ATOM   2965 C  C   . GLN A 1 465 ? 36.042 55.633  52.728 1.00 29.78  ? 443 GLN A C   1 
ATOM   2966 O  O   . GLN A 1 465 ? 36.497 54.938  53.591 1.00 31.99  ? 443 GLN A O   1 
ATOM   2967 C  CB  . GLN A 1 465 ? 37.728 56.629  51.072 1.00 29.38  ? 443 GLN A CB  1 
ATOM   2968 C  CG  . GLN A 1 465 ? 38.543 56.352  49.823 1.00 28.39  ? 443 GLN A CG  1 
ATOM   2969 C  CD  . GLN A 1 465 ? 39.484 57.465  49.463 1.00 25.70  ? 443 GLN A CD  1 
ATOM   2970 O  OE1 . GLN A 1 465 ? 40.590 57.517  49.925 1.00 31.54  ? 443 GLN A OE1 1 
ATOM   2971 N  NE2 . GLN A 1 465 ? 39.037 58.361  48.632 1.00 28.67  ? 443 GLN A NE2 1 
ATOM   2972 N  N   . GLU A 1 466 ? 35.020 56.453  52.887 1.00 27.23  ? 444 GLU A N   1 
ATOM   2973 C  CA  . GLU A 1 466 ? 34.333 56.545  54.183 1.00 30.74  ? 444 GLU A CA  1 
ATOM   2974 C  C   . GLU A 1 466 ? 33.766 55.175  54.539 1.00 30.71  ? 444 GLU A C   1 
ATOM   2975 O  O   . GLU A 1 466 ? 33.942 54.794  55.643 1.00 31.35  ? 444 GLU A O   1 
ATOM   2976 C  CB  . GLU A 1 466 ? 33.260 57.621  54.170 1.00 29.74  ? 444 GLU A CB  1 
ATOM   2977 C  CG  . GLU A 1 466 ? 32.519 57.722  55.481 1.00 37.16  ? 444 GLU A CG  1 
ATOM   2978 C  CD  . GLU A 1 466 ? 31.371 56.737  55.688 1.00 42.89  ? 444 GLU A CD  1 
ATOM   2979 O  OE1 . GLU A 1 466 ? 30.904 56.166  54.734 1.00 53.99  ? 444 GLU A OE1 1 
ATOM   2980 O  OE2 . GLU A 1 466 ? 30.938 56.569  56.814 1.00 45.54  ? 444 GLU A OE2 1 
ATOM   2981 N  N   . GLN A 1 467 ? 33.105 54.523  53.593 1.00 30.78  ? 445 GLN A N   1 
ATOM   2982 C  CA  . GLN A 1 467 ? 32.510 53.183  53.779 1.00 33.30  ? 445 GLN A CA  1 
ATOM   2983 C  C   . GLN A 1 467 ? 33.604 52.203  54.175 1.00 31.54  ? 445 GLN A C   1 
ATOM   2984 O  O   . GLN A 1 467 ? 33.386 51.475  55.095 1.00 33.38  ? 445 GLN A O   1 
ATOM   2985 C  CB  . GLN A 1 467 ? 31.849 52.693  52.499 1.00 34.14  ? 445 GLN A CB  1 
ATOM   2986 C  CG  . GLN A 1 467 ? 30.538 53.383  52.215 1.00 41.64  ? 445 GLN A CG  1 
ATOM   2987 C  CD  . GLN A 1 467 ? 29.762 52.720  51.111 1.00 57.84  ? 445 GLN A CD  1 
ATOM   2988 O  OE1 . GLN A 1 467 ? 28.989 51.804  51.342 1.00 65.31  ? 445 GLN A OE1 1 
ATOM   2989 N  NE2 . GLN A 1 467 ? 29.935 53.204  49.898 1.00 51.99  ? 445 GLN A NE2 1 
ATOM   2990 N  N   . GLN A 1 468 ? 34.731 52.231  53.484 1.00 27.24  ? 446 GLN A N   1 
ATOM   2991 C  CA  . GLN A 1 468 ? 35.832 51.332  53.811 1.00 28.42  ? 446 GLN A CA  1 
ATOM   2992 C  C   . GLN A 1 468 ? 36.369 51.611  55.209 1.00 28.57  ? 446 GLN A C   1 
ATOM   2993 O  O   . GLN A 1 468 ? 36.744 50.682  55.934 1.00 27.22  ? 446 GLN A O   1 
ATOM   2994 C  CB  . GLN A 1 468 ? 36.942 51.465  52.768 1.00 29.19  ? 446 GLN A CB  1 
ATOM   2995 C  CG  . GLN A 1 468 ? 36.513 51.107  51.352 1.00 32.29  ? 446 GLN A CG  1 
ATOM   2996 C  CD  . GLN A 1 468 ? 37.605 51.364  50.330 1.00 34.26  ? 446 GLN A CD  1 
ATOM   2997 O  OE1 . GLN A 1 468 ? 38.340 52.347  50.423 1.00 37.48  ? 446 GLN A OE1 1 
ATOM   2998 N  NE2 . GLN A 1 468 ? 37.717 50.477  49.347 1.00 40.76  ? 446 GLN A NE2 1 
ATOM   2999 N  N   . ILE A 1 469 ? 36.415 52.886  55.604 1.00 27.24  ? 447 ILE A N   1 
ATOM   3000 C  CA  . ILE A 1 469 ? 36.812 53.226  56.968 1.00 25.56  ? 447 ILE A CA  1 
ATOM   3001 C  C   . ILE A 1 469 ? 35.816 52.652  57.966 1.00 26.80  ? 447 ILE A C   1 
ATOM   3002 O  O   . ILE A 1 469 ? 36.201 52.117  59.013 1.00 25.46  ? 447 ILE A O   1 
ATOM   3003 C  CB  . ILE A 1 469 ? 36.948 54.752  57.124 1.00 26.34  ? 447 ILE A CB  1 
ATOM   3004 C  CG1 . ILE A 1 469 ? 38.194 55.262  56.399 1.00 26.74  ? 447 ILE A CG1 1 
ATOM   3005 C  CG2 . ILE A 1 469 ? 37.000 55.137  58.595 1.00 20.64  ? 447 ILE A CG2 1 
ATOM   3006 C  CD1 . ILE A 1 469 ? 38.154 56.749  56.107 1.00 29.51  ? 447 ILE A CD1 1 
ATOM   3007 N  N   . GLN A 1 470 ? 34.536 52.752  57.653 1.00 26.29  ? 448 GLN A N   1 
ATOM   3008 C  CA  . GLN A 1 470 ? 33.504 52.211  58.565 1.00 28.20  ? 448 GLN A CA  1 
ATOM   3009 C  C   . GLN A 1 470 ? 33.691 50.706  58.734 1.00 26.74  ? 448 GLN A C   1 
ATOM   3010 O  O   . GLN A 1 470 ? 33.709 50.267  59.827 1.00 30.21  ? 448 GLN A O   1 
ATOM   3011 C  CB  . GLN A 1 470 ? 32.101 52.513  58.065 1.00 29.17  ? 448 GLN A CB  1 
ATOM   3012 C  CG  . GLN A 1 470 ? 31.028 51.914  58.942 1.00 38.69  ? 448 GLN A CG  1 
ATOM   3013 C  CD  . GLN A 1 470 ? 30.758 52.794  60.126 1.00 50.34  ? 448 GLN A CD  1 
ATOM   3014 O  OE1 . GLN A 1 470 ? 30.404 53.948  59.982 1.00 60.16  ? 448 GLN A OE1 1 
ATOM   3015 N  NE2 . GLN A 1 470 ? 30.907 52.245  61.309 1.00 47.89  ? 448 GLN A NE2 1 
ATOM   3016 N  N   . GLN A 1 471 ? 33.842 49.987  57.639 1.00 30.18  ? 449 GLN A N   1 
ATOM   3017 C  CA  . GLN A 1 471 ? 34.018 48.522  57.673 1.00 31.28  ? 449 GLN A CA  1 
ATOM   3018 C  C   . GLN A 1 471 ? 35.269 48.178  58.488 1.00 30.29  ? 449 GLN A C   1 
ATOM   3019 O  O   . GLN A 1 471 ? 35.178 47.341  59.340 1.00 25.63  ? 449 GLN A O   1 
ATOM   3020 C  CB  . GLN A 1 471 ? 34.015 47.956  56.262 1.00 32.75  ? 449 GLN A CB  1 
ATOM   3021 C  CG  . GLN A 1 471 ? 34.043 46.447  56.220 1.00 33.09  ? 449 GLN A CG  1 
ATOM   3022 C  CD  . GLN A 1 471 ? 34.621 45.909  54.937 1.00 45.51  ? 449 GLN A CD  1 
ATOM   3023 O  OE1 . GLN A 1 471 ? 35.778 46.121  54.630 1.00 44.36  ? 449 GLN A OE1 1 
ATOM   3024 N  NE2 . GLN A 1 471 ? 33.807 45.204  54.179 1.00 46.37  ? 449 GLN A NE2 1 
ATOM   3025 N  N   . ALA A 1 472 ? 36.367 48.886  58.243 1.00 28.46  ? 450 ALA A N   1 
ATOM   3026 C  CA  . ALA A 1 472 ? 37.636 48.664  58.968 1.00 27.09  ? 450 ALA A CA  1 
ATOM   3027 C  C   . ALA A 1 472 ? 37.392 48.872  60.454 1.00 29.92  ? 450 ALA A C   1 
ATOM   3028 O  O   . ALA A 1 472 ? 37.797 48.057  61.217 1.00 28.03  ? 450 ALA A O   1 
ATOM   3029 C  CB  . ALA A 1 472 ? 38.702 49.582  58.454 1.00 27.67  ? 450 ALA A CB  1 
ATOM   3030 N  N   . GLU A 1 473 ? 36.715 49.957  60.780 1.00 25.29  ? 451 GLU A N   1 
ATOM   3031 C  CA  . GLU A 1 473 ? 36.348 50.284  62.161 1.00 25.66  ? 451 GLU A CA  1 
ATOM   3032 C  C   . GLU A 1 473 ? 35.554 49.113  62.734 1.00 25.89  ? 451 GLU A C   1 
ATOM   3033 O  O   . GLU A 1 473 ? 35.917 48.661  63.756 1.00 30.02  ? 451 GLU A O   1 
ATOM   3034 C  CB  . GLU A 1 473 ? 35.567 51.592  62.195 1.00 26.71  ? 451 GLU A CB  1 
ATOM   3035 C  CG  . GLU A 1 473 ? 35.541 52.198  63.555 1.00 34.83  ? 451 GLU A CG  1 
ATOM   3036 C  CD  . GLU A 1 473 ? 35.142 53.651  63.674 1.00 44.21  ? 451 GLU A CD  1 
ATOM   3037 O  OE1 . GLU A 1 473 ? 34.972 54.288  62.693 1.00 46.48  ? 451 GLU A OE1 1 
ATOM   3038 O  OE2 . GLU A 1 473 ? 35.007 54.091  64.781 1.00 43.96  ? 451 GLU A OE2 1 
ATOM   3039 N  N   . ASN A 1 474 ? 34.551 48.637  62.022 1.00 24.08  ? 452 ASN A N   1 
ATOM   3040 C  CA  . ASN A 1 474 ? 33.716 47.552  62.529 1.00 31.43  ? 452 ASN A CA  1 
ATOM   3041 C  C   . ASN A 1 474 ? 34.525 46.274  62.718 1.00 27.39  ? 452 ASN A C   1 
ATOM   3042 O  O   . ASN A 1 474 ? 34.377 45.582  63.733 1.00 27.59  ? 452 ASN A O   1 
ATOM   3043 C  CB  . ASN A 1 474 ? 32.543 47.306  61.580 1.00 31.59  ? 452 ASN A CB  1 
ATOM   3044 C  CG  . ASN A 1 474 ? 31.477 48.380  61.680 1.00 34.77  ? 452 ASN A CG  1 
ATOM   3045 O  OD1 . ASN A 1 474 ? 31.480 49.192  62.606 1.00 33.31  ? 452 ASN A OD1 1 
ATOM   3046 N  ND2 . ASN A 1 474 ? 30.558 48.390  60.721 1.00 33.83  ? 452 ASN A ND2 1 
ATOM   3047 N  N   . ILE A 1 475 ? 35.380 45.942  61.748 1.00 29.59  ? 453 ILE A N   1 
ATOM   3048 C  CA  . ILE A 1 475 ? 36.217 44.750  61.867 1.00 25.89  ? 453 ILE A CA  1 
ATOM   3049 C  C   . ILE A 1 475 ? 37.163 44.886  63.053 1.00 32.38  ? 453 ILE A C   1 
ATOM   3050 O  O   . ILE A 1 475 ? 37.315 43.962  63.862 1.00 26.78  ? 453 ILE A O   1 
ATOM   3051 C  CB  . ILE A 1 475 ? 36.988 44.503  60.557 1.00 32.25  ? 453 ILE A CB  1 
ATOM   3052 C  CG1 . ILE A 1 475 ? 36.035 44.051  59.449 1.00 34.37  ? 453 ILE A CG1 1 
ATOM   3053 C  CG2 . ILE A 1 475 ? 38.093 43.478  60.769 1.00 31.61  ? 453 ILE A CG2 1 
ATOM   3054 C  CD1 . ILE A 1 475 ? 36.682 43.981  58.081 1.00 30.42  ? 453 ILE A CD1 1 
ATOM   3055 N  N   . ALA A 1 476 ? 37.807 46.049  63.179 1.00 26.25  ? 454 ALA A N   1 
ATOM   3056 C  CA  . ALA A 1 476 ? 38.753 46.258  64.270 1.00 31.06  ? 454 ALA A CA  1 
ATOM   3057 C  C   . ALA A 1 476 ? 38.053 46.247  65.623 1.00 32.15  ? 454 ALA A C   1 
ATOM   3058 O  O   . ALA A 1 476 ? 38.578 45.687  66.593 1.00 34.32  ? 454 ALA A O   1 
ATOM   3059 C  CB  . ALA A 1 476 ? 39.507 47.570  64.066 1.00 30.43  ? 454 ALA A CB  1 
ATOM   3060 N  N   . ASP A 1 477 ? 36.872 46.863  65.710 1.00 30.16  ? 455 ASP A N   1 
ATOM   3061 C  CA  . ASP A 1 477 ? 36.124 46.844  66.963 1.00 27.80  ? 455 ASP A CA  1 
ATOM   3062 C  C   . ASP A 1 477 ? 35.693 45.428  67.320 1.00 31.61  ? 455 ASP A C   1 
ATOM   3063 O  O   . ASP A 1 477 ? 35.695 45.047  68.497 1.00 35.16  ? 455 ASP A O   1 
ATOM   3064 C  CB  . ASP A 1 477 ? 34.908 47.765  66.865 1.00 33.99  ? 455 ASP A CB  1 
ATOM   3065 C  CG  . ASP A 1 477 ? 34.073 47.762  68.131 1.00 37.87  ? 455 ASP A CG  1 
ATOM   3066 O  OD1 . ASP A 1 477 ? 34.429 48.491  69.080 1.00 38.70  ? 455 ASP A OD1 1 
ATOM   3067 O  OD2 . ASP A 1 477 ? 33.064 47.029  68.178 1.00 44.53  ? 455 ASP A OD2 1 
ATOM   3068 N  N   . THR A 1 478 ? 35.320 44.633  66.315 1.00 26.72  ? 456 THR A N   1 
ATOM   3069 C  CA  . THR A 1 478 ? 34.939 43.249  66.568 1.00 30.90  ? 456 THR A CA  1 
ATOM   3070 C  C   . THR A 1 478 ? 36.117 42.444  67.103 1.00 35.51  ? 456 THR A C   1 
ATOM   3071 O  O   . THR A 1 478 ? 35.965 41.669  68.052 1.00 28.38  ? 456 THR A O   1 
ATOM   3072 C  CB  . THR A 1 478 ? 34.391 42.612  65.291 1.00 33.22  ? 456 THR A CB  1 
ATOM   3073 O  OG1 . THR A 1 478 ? 33.269 43.369  64.822 1.00 28.88  ? 456 THR A OG1 1 
ATOM   3074 C  CG2 . THR A 1 478 ? 33.954 41.176  65.553 1.00 35.16  ? 456 THR A CG2 1 
ATOM   3075 N  N   . LEU A 1 479 ? 37.302 42.624  66.516 1.00 30.19  ? 457 LEU A N   1 
ATOM   3076 C  CA  . LEU A 1 479 ? 38.467 41.865  66.959 1.00 26.49  ? 457 LEU A CA  1 
ATOM   3077 C  C   . LEU A 1 479 ? 38.876 42.244  68.378 1.00 32.40  ? 457 LEU A C   1 
ATOM   3078 O  O   . LEU A 1 479 ? 39.289 41.380  69.161 1.00 34.99  ? 457 LEU A O   1 
ATOM   3079 C  CB  . LEU A 1 479 ? 39.629 42.077  65.989 1.00 28.56  ? 457 LEU A CB  1 
ATOM   3080 C  CG  . LEU A 1 479 ? 39.564 41.280  64.688 1.00 30.08  ? 457 LEU A CG  1 
ATOM   3081 C  CD1 . LEU A 1 479 ? 40.593 41.788  63.687 1.00 32.65  ? 457 LEU A CD1 1 
ATOM   3082 C  CD2 . LEU A 1 479 ? 39.764 39.800  64.967 1.00 32.37  ? 457 LEU A CD2 1 
ATOM   3083 N  N   . VAL A 1 480 ? 38.769 43.529  68.727 1.00 31.46  ? 458 VAL A N   1 
ATOM   3084 C  CA  . VAL A 1 480 ? 39.116 43.967  70.077 1.00 33.76  ? 458 VAL A CA  1 
ATOM   3085 C  C   . VAL A 1 480 ? 38.200 43.312  71.104 1.00 37.84  ? 458 VAL A C   1 
ATOM   3086 O  O   . VAL A 1 480 ? 38.635 42.935  72.199 1.00 32.75  ? 458 VAL A O   1 
ATOM   3087 C  CB  . VAL A 1 480 ? 39.065 45.505  70.168 1.00 34.41  ? 458 VAL A CB  1 
ATOM   3088 C  CG1 . VAL A 1 480 ? 39.052 45.963  71.621 1.00 35.43  ? 458 VAL A CG1 1 
ATOM   3089 C  CG2 . VAL A 1 480 ? 40.241 46.124  69.428 1.00 36.42  ? 458 VAL A CG2 1 
ATOM   3090 N  N   . ASN A 1 481 ? 36.924 43.150  70.763 1.00 33.83  ? 459 ASN A N   1 
ATOM   3091 C  CA  . ASN A 1 481 ? 35.920 42.599  71.667 1.00 39.77  ? 459 ASN A CA  1 
ATOM   3092 C  C   . ASN A 1 481 ? 35.402 41.248  71.180 1.00 28.12  ? 459 ASN A C   1 
ATOM   3093 O  O   . ASN A 1 481 ? 34.227 40.925  71.354 1.00 31.54  ? 459 ASN A O   1 
ATOM   3094 C  CB  . ASN A 1 481 ? 34.758 43.575  71.833 1.00 33.81  ? 459 ASN A CB  1 
ATOM   3095 C  CG  . ASN A 1 481 ? 35.216 44.969  72.213 1.00 35.60  ? 459 ASN A CG  1 
ATOM   3096 O  OD1 . ASN A 1 481 ? 35.552 45.230  73.367 1.00 38.97  ? 459 ASN A OD1 1 
ATOM   3097 N  ND2 . ASN A 1 481 ? 35.231 45.874  71.240 1.00 40.84  ? 459 ASN A ND2 1 
ATOM   3098 N  N   . PHE A 1 482 ? 36.280 40.434  70.584 1.00 33.62  ? 460 PHE A N   1 
ATOM   3099 C  CA  . PHE A 1 482 ? 35.822 39.242  69.872 1.00 30.07  ? 460 PHE A CA  1 
ATOM   3100 C  C   . PHE A 1 482 ? 35.116 38.263  70.800 1.00 34.26  ? 460 PHE A C   1 
ATOM   3101 O  O   . PHE A 1 482 ? 34.062 37.718  70.454 1.00 32.13  ? 460 PHE A O   1 
ATOM   3102 C  CB  . PHE A 1 482 ? 36.993 38.559  69.167 1.00 29.11  ? 460 PHE A CB  1 
ATOM   3103 C  CG  . PHE A 1 482 ? 36.565 37.564  68.129 1.00 28.99  ? 460 PHE A CG  1 
ATOM   3104 C  CD1 . PHE A 1 482 ? 36.297 37.969  66.831 1.00 30.86  ? 460 PHE A CD1 1 
ATOM   3105 C  CD2 . PHE A 1 482 ? 36.410 36.226  68.454 1.00 36.19  ? 460 PHE A CD2 1 
ATOM   3106 C  CE1 . PHE A 1 482 ? 35.894 37.056  65.874 1.00 30.92  ? 460 PHE A CE1 1 
ATOM   3107 C  CE2 . PHE A 1 482 ? 36.008 35.308  67.502 1.00 33.86  ? 460 PHE A CE2 1 
ATOM   3108 C  CZ  . PHE A 1 482 ? 35.750 35.723  66.210 1.00 33.71  ? 460 PHE A CZ  1 
ATOM   3109 N  N   . LYS A 1 483 ? 35.691 38.014  71.979 1.00 37.38  ? 461 LYS A N   1 
ATOM   3110 C  CA  . LYS A 1 483 ? 35.070 37.080  72.913 1.00 35.91  ? 461 LYS A CA  1 
ATOM   3111 C  C   . LYS A 1 483 ? 33.660 37.525  73.277 1.00 33.61  ? 461 LYS A C   1 
ATOM   3112 O  O   . LYS A 1 483 ? 32.725 36.714  73.281 1.00 33.93  ? 461 LYS A O   1 
ATOM   3113 C  CB  . LYS A 1 483 ? 35.935 36.941  74.166 1.00 38.26  ? 461 LYS A CB  1 
ATOM   3114 C  CG  . LYS A 1 483 ? 35.498 35.830  75.107 1.00 44.86  ? 461 LYS A CG  1 
ATOM   3115 C  CD  . LYS A 1 483 ? 36.467 35.686  76.270 1.00 43.39  ? 461 LYS A CD  1 
ATOM   3116 C  CE  . LYS A 1 483 ? 35.744 35.301  77.551 1.00 62.83  ? 461 LYS A CE  1 
ATOM   3117 N  NZ  . LYS A 1 483 ? 34.946 34.054  77.390 1.00 55.46  ? 461 LYS A NZ  1 
ATOM   3118 N  N   . SER A 1 484 ? 33.482 38.816  73.563 1.00 36.00  ? 462 SER A N   1 
ATOM   3119 C  CA  . SER A 1 484 ? 32.159 39.321  73.917 1.00 37.99  ? 462 SER A CA  1 
ATOM   3120 C  C   . SER A 1 484 ? 31.234 39.353  72.706 1.00 35.41  ? 462 SER A C   1 
ATOM   3121 O  O   . SER A 1 484 ? 30.055 38.994  72.812 1.00 32.46  ? 462 SER A O   1 
ATOM   3122 C  CB  . SER A 1 484 ? 32.280 40.711  74.540 1.00 35.70  ? 462 SER A CB  1 
ATOM   3123 O  OG  . SER A 1 484 ? 31.026 41.169  75.013 1.00 53.01  ? 462 SER A OG  1 
ATOM   3124 N  N   . ARG A 1 485 ? 31.745 39.782  71.548 1.00 30.60  ? 463 ARG A N   1 
ATOM   3125 C  CA  . ARG A 1 485 ? 30.911 39.836  70.351 1.00 30.67  ? 463 ARG A CA  1 
ATOM   3126 C  C   . ARG A 1 485 ? 30.496 38.440  69.906 1.00 34.62  ? 463 ARG A C   1 
ATOM   3127 O  O   . ARG A 1 485 ? 29.350 38.228  69.493 1.00 30.95  ? 463 ARG A O   1 
ATOM   3128 C  CB  . ARG A 1 485 ? 31.646 40.557  69.221 1.00 29.30  ? 463 ARG A CB  1 
ATOM   3129 C  CG  . ARG A 1 485 ? 31.997 42.004  69.521 1.00 35.30  ? 463 ARG A CG  1 
ATOM   3130 C  CD  . ARG A 1 485 ? 30.767 42.895  69.570 1.00 31.97  ? 463 ARG A CD  1 
ATOM   3131 N  NE  . ARG A 1 485 ? 31.138 44.307  69.591 1.00 35.43  ? 463 ARG A NE  1 
ATOM   3132 C  CZ  . ARG A 1 485 ? 31.410 44.991  70.698 1.00 36.34  ? 463 ARG A CZ  1 
ATOM   3133 N  NH1 . ARG A 1 485 ? 31.349 44.393  71.880 1.00 39.03  ? 463 ARG A NH1 1 
ATOM   3134 N  NH2 . ARG A 1 485 ? 31.744 46.272  70.624 1.00 37.91  ? 463 ARG A NH2 1 
ATOM   3135 N  N   . TYR A 1 486 ? 31.419 37.478  69.974 1.00 29.07  ? 464 TYR A N   1 
ATOM   3136 C  CA  . TYR A 1 486 ? 31.069 36.102  69.645 1.00 29.64  ? 464 TYR A CA  1 
ATOM   3137 C  C   . TYR A 1 486 ? 30.067 35.544  70.643 1.00 31.68  ? 464 TYR A C   1 
ATOM   3138 O  O   . TYR A 1 486 ? 29.133 34.828  70.265 1.00 29.71  ? 464 TYR A O   1 
ATOM   3139 C  CB  . TYR A 1 486 ? 32.326 35.235  69.606 1.00 33.59  ? 464 TYR A CB  1 
ATOM   3140 C  CG  . TYR A 1 486 ? 32.059 33.795  69.250 1.00 37.00  ? 464 TYR A CG  1 
ATOM   3141 C  CD1 . TYR A 1 486 ? 31.407 33.465  68.070 1.00 41.09  ? 464 TYR A CD1 1 
ATOM   3142 C  CD2 . TYR A 1 486 ? 32.456 32.765  70.091 1.00 39.12  ? 464 TYR A CD2 1 
ATOM   3143 C  CE1 . TYR A 1 486 ? 31.157 32.152  67.738 1.00 39.68  ? 464 TYR A CE1 1 
ATOM   3144 C  CE2 . TYR A 1 486 ? 32.212 31.446  69.767 1.00 35.51  ? 464 TYR A CE2 1 
ATOM   3145 C  CZ  . TYR A 1 486 ? 31.561 31.146  68.590 1.00 47.50  ? 464 TYR A CZ  1 
ATOM   3146 O  OH  . TYR A 1 486 ? 31.316 29.835  68.256 1.00 48.86  ? 464 TYR A OH  1 
ATOM   3147 N  N   . SER A 1 487 ? 30.239 35.870  71.923 1.00 31.05  ? 465 SER A N   1 
ATOM   3148 C  CA  . SER A 1 487 ? 29.276 35.423  72.921 1.00 34.51  ? 465 SER A CA  1 
ATOM   3149 C  C   . SER A 1 487 ? 27.918 36.088  72.722 1.00 34.62  ? 465 SER A C   1 
ATOM   3150 O  O   . SER A 1 487 ? 26.881 35.447  72.929 1.00 30.71  ? 465 SER A O   1 
ATOM   3151 C  CB  . SER A 1 487 ? 29.802 35.700  74.322 1.00 34.62  ? 465 SER A CB  1 
ATOM   3152 O  OG  . SER A 1 487 ? 28.761 35.625  75.278 1.00 39.46  ? 465 SER A OG  1 
ATOM   3153 N  N   . GLU A 1 488 ? 27.898 37.356  72.300 1.00 32.02  ? 466 GLU A N   1 
ATOM   3154 C  CA  . GLU A 1 488 ? 26.628 38.022  72.024 1.00 31.68  ? 466 GLU A CA  1 
ATOM   3155 C  C   . GLU A 1 488 ? 25.905 37.363  70.857 1.00 27.53  ? 466 GLU A C   1 
ATOM   3156 O  O   . GLU A 1 488 ? 24.671 37.297  70.839 1.00 30.41  ? 466 GLU A O   1 
ATOM   3157 C  CB  . GLU A 1 488 ? 26.862 39.506  71.742 1.00 26.27  ? 466 GLU A CB  1 
ATOM   3158 C  CG  . GLU A 1 488 ? 25.583 40.303  71.528 1.00 32.86  ? 466 GLU A CG  1 
ATOM   3159 C  CD  . GLU A 1 488 ? 25.849 41.767  71.244 1.00 37.92  ? 466 GLU A CD  1 
ATOM   3160 O  OE1 . GLU A 1 488 ? 27.021 42.189  71.331 1.00 34.62  ? 466 GLU A OE1 1 
ATOM   3161 O  OE2 . GLU A 1 488 ? 24.883 42.493  70.932 1.00 35.32  ? 466 GLU A OE2 1 
ATOM   3162 N  N   . LEU A 1 489 ? 26.661 36.868  69.873 1.00 30.80  ? 467 LEU A N   1 
ATOM   3163 C  CA  . LEU A 1 489 ? 26.051 36.164  68.750 1.00 27.65  ? 467 LEU A CA  1 
ATOM   3164 C  C   . LEU A 1 489 ? 25.288 34.932  69.220 1.00 28.67  ? 467 LEU A C   1 
ATOM   3165 O  O   . LEU A 1 489 ? 24.170 34.670  68.759 1.00 26.86  ? 467 LEU A O   1 
ATOM   3166 C  CB  . LEU A 1 489 ? 27.123 35.774  67.733 1.00 26.06  ? 467 LEU A CB  1 
ATOM   3167 C  CG  . LEU A 1 489 ? 26.649 34.973  66.519 1.00 36.02  ? 467 LEU A CG  1 
ATOM   3168 C  CD1 . LEU A 1 489 ? 25.664 35.786  65.694 1.00 35.12  ? 467 LEU A CD1 1 
ATOM   3169 C  CD2 . LEU A 1 489 ? 27.833 34.534  65.671 1.00 31.78  ? 467 LEU A CD2 1 
ATOM   3170 N  N   . GLY A 1 490 ? 25.876 34.164  70.139 1.00 33.33  ? 468 GLY A N   1 
ATOM   3171 C  CA  . GLY A 1 490 ? 25.188 32.996  70.662 1.00 28.91  ? 468 GLY A CA  1 
ATOM   3172 C  C   . GLY A 1 490 ? 23.964 33.357  71.481 1.00 26.26  ? 468 GLY A C   1 
ATOM   3173 O  O   . GLY A 1 490 ? 22.924 32.700  71.379 1.00 35.52  ? 468 GLY A O   1 
ATOM   3174 N  N   . ASN A 1 491 ? 24.068 34.403  72.305 1.00 26.52  ? 469 ASN A N   1 
ATOM   3175 C  CA  . ASN A 1 491 ? 22.918 34.845  73.089 1.00 30.13  ? 469 ASN A CA  1 
ATOM   3176 C  C   . ASN A 1 491 ? 21.797 35.341  72.187 1.00 33.00  ? 469 ASN A C   1 
ATOM   3177 O  O   . ASN A 1 491 ? 20.614 35.118  72.472 1.00 26.75  ? 469 ASN A O   1 
ATOM   3178 C  CB  . ASN A 1 491 ? 23.340 35.939  74.069 1.00 27.46  ? 469 ASN A CB  1 
ATOM   3179 C  CG  . ASN A 1 491 ? 24.434 35.484  75.009 1.00 27.71  ? 469 ASN A CG  1 
ATOM   3180 O  OD1 . ASN A 1 491 ? 24.732 34.295  75.097 1.00 25.37  ? 469 ASN A OD1 1 
ATOM   3181 N  ND2 . ASN A 1 491 ? 25.042 36.429  75.716 1.00 26.69  ? 469 ASN A ND2 1 
ATOM   3182 N  N   . THR A 1 492 ? 22.150 36.024  71.095 1.00 30.68  ? 470 THR A N   1 
ATOM   3183 C  CA  . THR A 1 492 ? 21.142 36.464  70.137 1.00 29.16  ? 470 THR A CA  1 
ATOM   3184 C  C   . THR A 1 492 ? 20.466 35.273  69.471 1.00 29.30  ? 470 THR A C   1 
ATOM   3185 O  O   . THR A 1 492 ? 19.244 35.268  69.281 1.00 28.45  ? 470 THR A O   1 
ATOM   3186 C  CB  . THR A 1 492 ? 21.782 37.378  69.091 1.00 27.76  ? 470 THR A CB  1 
ATOM   3187 O  OG1 . THR A 1 492 ? 22.461 38.453  69.753 1.00 29.10  ? 470 THR A OG1 1 
ATOM   3188 C  CG2 . THR A 1 492 ? 20.725 37.952  68.160 1.00 33.43  ? 470 THR A CG2 1 
ATOM   3189 N  N   . TYR A 1 493 ? 21.249 34.251  69.113 1.00 31.23  ? 471 TYR A N   1 
ATOM   3190 C  CA  . TYR A 1 493 ? 20.674 33.016  68.590 1.00 29.83  ? 471 TYR A CA  1 
ATOM   3191 C  C   . TYR A 1 493 ? 19.668 32.421  69.567 1.00 31.61  ? 471 TYR A C   1 
ATOM   3192 O  O   . TYR A 1 493 ? 18.594 31.961  69.162 1.00 30.04  ? 471 TYR A O   1 
ATOM   3193 C  CB  . TYR A 1 493 ? 21.792 32.015  68.288 1.00 28.41  ? 471 TYR A CB  1 
ATOM   3194 C  CG  . TYR A 1 493 ? 21.322 30.669  67.781 1.00 35.46  ? 471 TYR A CG  1 
ATOM   3195 C  CD1 . TYR A 1 493 ? 21.030 29.634  68.662 1.00 40.85  ? 471 TYR A CD1 1 
ATOM   3196 C  CD2 . TYR A 1 493 ? 21.186 30.427  66.421 1.00 38.95  ? 471 TYR A CD2 1 
ATOM   3197 C  CE1 . TYR A 1 493 ? 20.604 28.402  68.202 1.00 35.57  ? 471 TYR A CE1 1 
ATOM   3198 C  CE2 . TYR A 1 493 ? 20.763 29.197  65.952 1.00 37.33  ? 471 TYR A CE2 1 
ATOM   3199 C  CZ  . TYR A 1 493 ? 20.474 28.189  66.847 1.00 41.79  ? 471 TYR A CZ  1 
ATOM   3200 O  OH  . TYR A 1 493 ? 20.052 26.964  66.384 1.00 41.86  ? 471 TYR A OH  1 
ATOM   3201 N  N   . ASN A 1 494 ? 19.998 32.426  70.862 1.00 30.30  ? 472 ASN A N   1 
ATOM   3202 C  CA  . ASN A 1 494 ? 19.096 31.860  71.860 1.00 34.91  ? 472 ASN A CA  1 
ATOM   3203 C  C   . ASN A 1 494 ? 17.806 32.665  71.964 1.00 29.56  ? 472 ASN A C   1 
ATOM   3204 O  O   . ASN A 1 494 ? 16.720 32.090  72.098 1.00 30.13  ? 472 ASN A O   1 
ATOM   3205 C  CB  . ASN A 1 494 ? 19.796 31.788  73.217 1.00 30.93  ? 472 ASN A CB  1 
ATOM   3206 C  CG  . ASN A 1 494 ? 20.894 30.742  73.252 1.00 33.63  ? 472 ASN A CG  1 
ATOM   3207 O  OD1 . ASN A 1 494 ? 20.923 29.828  72.427 1.00 35.05  ? 472 ASN A OD1 1 
ATOM   3208 N  ND2 . ASN A 1 494 ? 21.802 30.870  74.211 1.00 31.20  ? 472 ASN A ND2 1 
ATOM   3209 N  N   . SER A 1 495 ? 17.904 33.995  71.906 1.00 26.55  ? 473 SER A N   1 
ATOM   3210 C  CA  . SER A 1 495 ? 16.701 34.820  71.929 1.00 29.09  ? 473 SER A CA  1 
ATOM   3211 C  C   . SER A 1 495 ? 15.856 34.609  70.680 1.00 37.67  ? 473 SER A C   1 
ATOM   3212 O  O   . SER A 1 495 ? 14.631 34.775  70.727 1.00 34.86  ? 473 SER A O   1 
ATOM   3213 C  CB  . SER A 1 495 ? 17.072 36.296  72.073 1.00 29.09  ? 473 SER A CB  1 
ATOM   3214 O  OG  . SER A 1 495 ? 17.668 36.558  73.332 1.00 27.89  ? 473 SER A OG  1 
ATOM   3215 N  N   . ILE A 1 496 ? 16.485 34.239  69.563 1.00 28.28  ? 474 ILE A N   1 
ATOM   3216 C  CA  . ILE A 1 496 ? 15.737 33.996  68.334 1.00 32.33  ? 474 ILE A CA  1 
ATOM   3217 C  C   . ILE A 1 496 ? 14.972 32.682  68.427 1.00 35.85  ? 474 ILE A C   1 
ATOM   3218 O  O   . ILE A 1 496 ? 13.785 32.612  68.087 1.00 31.93  ? 474 ILE A O   1 
ATOM   3219 C  CB  . ILE A 1 496 ? 16.681 34.018  67.118 1.00 33.79  ? 474 ILE A CB  1 
ATOM   3220 C  CG1 . ILE A 1 496 ? 17.148 35.446  66.839 1.00 30.20  ? 474 ILE A CG1 1 
ATOM   3221 C  CG2 . ILE A 1 496 ? 15.992 33.435  65.891 1.00 30.01  ? 474 ILE A CG2 1 
ATOM   3222 C  CD1 . ILE A 1 496 ? 18.210 35.542  65.773 1.00 38.74  ? 474 ILE A CD1 1 
ATOM   3223 N  N   . THR A 1 497 ? 15.640 31.619  68.887 1.00 33.32  ? 475 THR A N   1 
ATOM   3224 C  CA  . THR A 1 497 ? 14.962 30.335  69.038 1.00 33.50  ? 475 THR A CA  1 
ATOM   3225 C  C   . THR A 1 497 ? 13.819 30.432  70.040 1.00 37.56  ? 475 THR A C   1 
ATOM   3226 O  O   . THR A 1 497 ? 12.760 29.823  69.847 1.00 42.97  ? 475 THR A O   1 
ATOM   3227 C  CB  . THR A 1 497 ? 15.955 29.252  69.463 1.00 39.93  ? 475 THR A CB  1 
ATOM   3228 O  OG1 . THR A 1 497 ? 16.523 29.590  70.734 1.00 45.10  ? 475 THR A OG1 1 
ATOM   3229 C  CG2 . THR A 1 497 ? 17.067 29.113  68.433 1.00 32.03  ? 475 THR A CG2 1 
ATOM   3230 N  N   . THR A 1 498 ? 14.012 31.199  71.116 1.00 34.96  ? 476 THR A N   1 
ATOM   3231 C  CA  . THR A 1 498 ? 12.931 31.427  72.068 1.00 39.39  ? 476 THR A CA  1 
ATOM   3232 C  C   . THR A 1 498 ? 11.772 32.166  71.409 1.00 42.97  ? 476 THR A C   1 
ATOM   3233 O  O   . THR A 1 498 ? 10.607 31.779  71.556 1.00 43.65  ? 476 THR A O   1 
ATOM   3234 C  CB  . THR A 1 498 ? 13.450 32.210  73.276 1.00 35.78  ? 476 THR A CB  1 
ATOM   3235 O  OG1 . THR A 1 498 ? 14.373 31.401  74.015 1.00 35.54  ? 476 THR A OG1 1 
ATOM   3236 C  CG2 . THR A 1 498 ? 12.300 32.618  74.185 1.00 34.91  ? 476 THR A CG2 1 
ATOM   3237 N  N   . ALA A 1 499 ? 12.076 33.234  70.667 1.00 37.84  ? 477 ALA A N   1 
ATOM   3238 C  CA  . ALA A 1 499 ? 11.025 34.001  70.007 1.00 43.96  ? 477 ALA A CA  1 
ATOM   3239 C  C   . ALA A 1 499 ? 10.336 33.193  68.914 1.00 44.89  ? 477 ALA A C   1 
ATOM   3240 O  O   . ALA A 1 499 ? 9.148  33.404  68.648 1.00 44.80  ? 477 ALA A O   1 
ATOM   3241 C  CB  . ALA A 1 499 ? 11.599 35.294  69.429 1.00 41.99  ? 477 ALA A CB  1 
ATOM   3242 N  N   . LEU A 1 500 ? 11.059 32.271  68.273 1.00 40.56  ? 478 LEU A N   1 
ATOM   3243 C  CA  . LEU A 1 500 ? 10.448 31.435  67.245 1.00 45.79  ? 478 LEU A CA  1 
ATOM   3244 C  C   . LEU A 1 500 ? 9.392  30.506  67.829 1.00 53.26  ? 478 LEU A C   1 
ATOM   3245 O  O   . LEU A 1 500 ? 8.411  30.180  67.150 1.00 56.04  ? 478 LEU A O   1 
ATOM   3246 C  CB  . LEU A 1 500 ? 11.519 30.620  66.521 1.00 42.59  ? 478 LEU A CB  1 
ATOM   3247 C  CG  . LEU A 1 500 ? 12.340 31.341  65.452 1.00 48.87  ? 478 LEU A CG  1 
ATOM   3248 C  CD1 . LEU A 1 500 ? 13.476 30.452  64.977 1.00 46.40  ? 478 LEU A CD1 1 
ATOM   3249 C  CD2 . LEU A 1 500 ? 11.458 31.761  64.287 1.00 52.69  ? 478 LEU A CD2 1 
ATOM   3250 N  N   . SER A 1 501 ? 9.571  30.073  69.077 1.00 48.10  ? 479 SER A N   1 
ATOM   3251 C  CA  . SER A 1 501 ? 8.631  29.165  69.723 1.00 49.91  ? 479 SER A CA  1 
ATOM   3252 C  C   . SER A 1 501 ? 7.302  29.823  70.064 1.00 54.27  ? 479 SER A C   1 
ATOM   3253 O  O   . SER A 1 501 ? 6.397  29.129  70.542 1.00 60.00  ? 479 SER A O   1 
ATOM   3254 C  CB  . SER A 1 501 ? 9.258  28.585  70.993 1.00 50.55  ? 479 SER A CB  1 
ATOM   3255 O  OG  . SER A 1 501 ? 9.216  29.523  72.056 1.00 50.43  ? 479 SER A OG  1 
ATOM   3256 N  N   . LYS A 1 502 ? 7.190  31.121  69.879 1.00 51.17  ? 480 LYS A N   1 
ATOM   3257 C  CA  . LYS A 1 502 ? 5.943  31.816  70.257 1.00 60.68  ? 480 LYS A CA  1 
ATOM   3258 C  C   . LYS A 1 502 ? 5.176  32.319  69.031 1.00 65.29  ? 480 LYS A C   1 
ATOM   3259 O  O   . LYS A 1 502 ? 4.261  33.108  69.212 1.00 64.61  ? 480 LYS A O   1 
ATOM   3260 C  CB  . LYS A 1 502 ? 6.294  32.938  71.233 1.00 58.41  ? 480 LYS A CB  1 
ATOM   3261 C  CG  . LYS A 1 502 ? 6.970  32.479  72.513 1.00 53.55  ? 480 LYS A CG  1 
ATOM   3262 C  CD  . LYS A 1 502 ? 7.835  33.508  73.165 1.00 57.28  ? 480 LYS A CD  1 
ATOM   3263 C  CE  . LYS A 1 502 ? 7.795  33.431  74.675 1.00 56.50  ? 480 LYS A CE  1 
ATOM   3264 N  NZ  . LYS A 1 502 ? 8.672  34.439  75.321 1.00 55.84  ? 480 LYS A NZ  1 
ATOM   3265 N  N   . VAL A 1 503 ? 5.616  31.947  67.843 1.00 64.34  ? 481 VAL A N   1 
ATOM   3266 C  CA  . VAL A 1 503 ? 4.871  32.346  66.626 1.00 72.63  ? 481 VAL A CA  1 
ATOM   3267 C  C   . VAL A 1 503 ? 4.147  31.091  66.169 1.00 83.32  ? 481 VAL A C   1 
ATOM   3268 O  O   . VAL A 1 503 ? 4.811  30.092  65.969 1.00 86.75  ? 481 VAL A O   1 
ATOM   3269 C  CB  . VAL A 1 503 ? 5.773  32.939  65.540 1.00 68.72  ? 481 VAL A CB  1 
ATOM   3270 C  CG1 . VAL A 1 503 ? 6.449  34.189  66.030 1.00 63.31  ? 481 VAL A CG1 1 
ATOM   3271 C  CG2 . VAL A 1 503 ? 6.808  31.952  65.072 1.00 78.37  ? 481 VAL A CG2 1 
ATOM   3272 N  N   . PRO A 1 504 ? 2.838  31.185  65.886 1.00 90.98  ? 482 PRO A N   1 
ATOM   3273 C  CA  . PRO A 1 504 ? 1.958  30.049  65.622 1.00 90.61  ? 482 PRO A CA  1 
ATOM   3274 C  C   . PRO A 1 504 ? 2.366  29.230  64.408 1.00 94.99  ? 482 PRO A C   1 
ATOM   3275 O  O   . PRO A 1 504 ? 2.765  29.837  63.455 1.00 92.28  ? 482 PRO A O   1 
ATOM   3276 C  CB  . PRO A 1 504 ? 0.636  30.693  65.227 1.00 92.28  ? 482 PRO A CB  1 
ATOM   3277 C  CG  . PRO A 1 504 ? 1.067  32.018  64.705 1.00 30.00  ? 482 PRO A CG  1 
ATOM   3278 C  CD  . PRO A 1 504 ? 2.148  32.444  65.670 1.00 92.28  ? 482 PRO A CD  1 
ATOM   3279 N  N   . ASN A 1 505 ? 2.026  27.939  64.470 1.00 102.46 ? 483 ASN A N   1 
ATOM   3280 C  CA  . ASN A 1 505 ? 2.480  26.901  63.514 1.00 105.69 ? 483 ASN A CA  1 
ATOM   3281 C  C   . ASN A 1 505 ? 3.994  26.925  63.690 1.00 107.45 ? 483 ASN A C   1 
ATOM   3282 O  O   . ASN A 1 505 ? 4.677  27.564  62.916 1.00 105.23 ? 483 ASN A O   1 
ATOM   3283 C  CB  . ASN A 1 505 ? 1.921  27.057  62.094 1.00 103.47 ? 483 ASN A CB  1 
ATOM   3284 C  CG  . ASN A 1 505 ? 0.441  27.375  62.085 1.00 108.53 ? 483 ASN A CG  1 
ATOM   3285 O  OD1 . ASN A 1 505 ? -0.309 26.836  62.889 1.00 108.93 ? 483 ASN A OD1 1 
ATOM   3286 N  ND2 . ASN A 1 505 ? 0.017  28.251  61.192 1.00 108.80 ? 483 ASN A ND2 1 
ATOM   3287 N  N   . ALA A 1 506 ? 4.448  26.412  64.827 1.00 110.66 ? 484 ALA A N   1 
ATOM   3288 C  CA  . ALA A 1 506 ? 5.887  26.504  65.115 1.00 106.12 ? 484 ALA A CA  1 
ATOM   3289 C  C   . ALA A 1 506 ? 6.704  25.794  64.042 1.00 106.37 ? 484 ALA A C   1 
ATOM   3290 O  O   . ALA A 1 506 ? 7.452  26.482  63.344 1.00 102.99 ? 484 ALA A O   1 
ATOM   3291 C  CB  . ALA A 1 506 ? 6.160  25.889  66.469 1.00 101.28 ? 484 ALA A CB  1 
ATOM   3292 N  N   . GLN A 1 507 ? 6.407  24.548  63.701 1.00 106.34 ? 485 GLN A N   1 
ATOM   3293 C  CA  . GLN A 1 507 ? 7.375  23.926  62.756 1.00 106.99 ? 485 GLN A CA  1 
ATOM   3294 C  C   . GLN A 1 507 ? 7.051  24.288  61.297 1.00 105.80 ? 485 GLN A C   1 
ATOM   3295 O  O   . GLN A 1 507 ? 6.501  23.438  60.604 1.00 102.82 ? 485 GLN A O   1 
ATOM   3296 C  CB  . GLN A 1 507 ? 7.676  22.481  63.153 1.00 102.59 ? 485 GLN A CB  1 
ATOM   3297 C  CG  . GLN A 1 507 ? 8.790  22.395  64.192 1.00 105.70 ? 485 GLN A CG  1 
ATOM   3298 C  CD  . GLN A 1 507 ? 8.805  21.103  64.974 1.00 111.53 ? 485 GLN A CD  1 
ATOM   3299 O  OE1 . GLN A 1 507 ? 8.044  20.185  64.698 1.00 111.50 ? 485 GLN A OE1 1 
ATOM   3300 N  NE2 . GLN A 1 507 ? 9.676  21.024  65.966 1.00 103.85 ? 485 GLN A NE2 1 
ATOM   3301 N  N   . SER A 1 508 ? 7.362  25.537  60.901 1.00 102.72 ? 486 SER A N   1 
ATOM   3302 C  CA  . SER A 1 508 ? 7.175  26.087  59.537 1.00 95.63  ? 486 SER A CA  1 
ATOM   3303 C  C   . SER A 1 508 ? 8.429  26.823  59.044 1.00 94.78  ? 486 SER A C   1 
ATOM   3304 O  O   . SER A 1 508 ? 8.852  26.511  57.938 1.00 86.94  ? 486 SER A O   1 
ATOM   3305 C  CB  . SER A 1 508 ? 5.982  26.976  59.514 1.00 92.61  ? 486 SER A CB  1 
ATOM   3306 O  OG  . SER A 1 508 ? 5.892  27.717  60.712 1.00 99.67  ? 486 SER A OG  1 
ATOM   3307 N  N   . LEU A 1 509 ? 8.949  27.794  59.822 1.00 89.10  ? 487 LEU A N   1 
ATOM   3308 C  CA  . LEU A 1 509 ? 10.119 28.667  59.477 1.00 78.06  ? 487 LEU A CA  1 
ATOM   3309 C  C   . LEU A 1 509 ? 11.267 28.507  60.470 1.00 75.19  ? 487 LEU A C   1 
ATOM   3310 O  O   . LEU A 1 509 ? 11.977 29.478  60.681 1.00 68.30  ? 487 LEU A O   1 
ATOM   3311 C  CB  . LEU A 1 509 ? 9.703  30.133  59.516 1.00 72.99  ? 487 LEU A CB  1 
ATOM   3312 C  CG  . LEU A 1 509 ? 8.869  30.610  58.344 1.00 83.16  ? 487 LEU A CG  1 
ATOM   3313 C  CD1 . LEU A 1 509 ? 8.068  31.837  58.723 1.00 78.19  ? 487 LEU A CD1 1 
ATOM   3314 C  CD2 . LEU A 1 509 ? 9.764  30.884  57.157 1.00 79.81  ? 487 LEU A CD2 1 
ATOM   3315 N  N   . GLN A 1 510 ? 11.414 27.338  61.067 1.00 78.80  ? 488 GLN A N   1 
ATOM   3316 C  CA  . GLN A 1 510 ? 12.489 27.092  62.057 1.00 74.25  ? 488 GLN A CA  1 
ATOM   3317 C  C   . GLN A 1 510 ? 13.870 27.050  61.385 1.00 68.89  ? 488 GLN A C   1 
ATOM   3318 O  O   . GLN A 1 510 ? 14.849 27.084  62.103 1.00 74.15  ? 488 GLN A O   1 
ATOM   3319 C  CB  . GLN A 1 510 ? 12.063 25.880  62.876 1.00 84.83  ? 488 GLN A CB  1 
ATOM   3320 C  CG  . GLN A 1 510 ? 10.626 25.999  63.369 1.00 89.24  ? 488 GLN A CG  1 
ATOM   3321 C  CD  . GLN A 1 510 ? 10.506 26.757  64.668 1.00 86.48  ? 488 GLN A CD  1 
ATOM   3322 O  OE1 . GLN A 1 510 ? 9.767  27.714  64.795 1.00 83.28  ? 488 GLN A OE1 1 
ATOM   3323 N  NE2 . GLN A 1 510 ? 11.261 26.338  65.663 1.00 82.54  ? 488 GLN A NE2 1 
ATOM   3324 N  N   . ASN A 1 511 ? 13.929 26.934  60.063 1.00 63.71  ? 489 ASN A N   1 
ATOM   3325 C  CA  . ASN A 1 511 ? 15.125 26.946  59.234 1.00 64.96  ? 489 ASN A CA  1 
ATOM   3326 C  C   . ASN A 1 511 ? 15.878 28.269  59.288 1.00 55.55  ? 489 ASN A C   1 
ATOM   3327 O  O   . ASN A 1 511 ? 17.027 28.318  58.836 1.00 57.37  ? 489 ASN A O   1 
ATOM   3328 C  CB  . ASN A 1 511 ? 14.736 26.644  57.787 1.00 68.60  ? 489 ASN A CB  1 
ATOM   3329 C  CG  . ASN A 1 511 ? 13.515 27.429  57.341 1.00 67.95  ? 489 ASN A CG  1 
ATOM   3330 O  OD1 . ASN A 1 511 ? 13.139 28.419  57.969 1.00 73.81  ? 489 ASN A OD1 1 
ATOM   3331 N  ND2 . ASN A 1 511 ? 12.889 26.991  56.255 1.00 74.89  ? 489 ASN A ND2 1 
ATOM   3332 N  N   . VAL A 1 512 ? 15.270 29.326  59.834 1.00 53.28  ? 490 VAL A N   1 
ATOM   3333 C  CA  . VAL A 1 512 ? 15.820 30.672  59.682 1.00 45.52  ? 490 VAL A CA  1 
ATOM   3334 C  C   . VAL A 1 512 ? 17.208 30.773  60.308 1.00 41.04  ? 490 VAL A C   1 
ATOM   3335 O  O   . VAL A 1 512 ? 18.096 31.444  59.769 1.00 41.68  ? 490 VAL A O   1 
ATOM   3336 C  CB  . VAL A 1 512 ? 14.844 31.717  60.260 1.00 50.75  ? 490 VAL A CB  1 
ATOM   3337 C  CG1 . VAL A 1 512 ? 14.713 31.583  61.772 1.00 49.65  ? 490 VAL A CG1 1 
ATOM   3338 C  CG2 . VAL A 1 512 ? 15.278 33.123  59.876 1.00 46.83  ? 490 VAL A CG2 1 
ATOM   3339 N  N   . VAL A 1 513 ? 17.429 30.098  61.436 1.00 37.61  ? 491 VAL A N   1 
ATOM   3340 C  CA  . VAL A 1 513 ? 18.724 30.121  62.103 1.00 45.10  ? 491 VAL A CA  1 
ATOM   3341 C  C   . VAL A 1 513 ? 19.151 28.695  62.412 1.00 40.18  ? 491 VAL A C   1 
ATOM   3342 O  O   . VAL A 1 513 ? 18.322 27.815  62.667 1.00 46.04  ? 491 VAL A O   1 
ATOM   3343 C  CB  . VAL A 1 513 ? 18.708 30.973  63.394 1.00 41.61  ? 491 VAL A CB  1 
ATOM   3344 C  CG1 . VAL A 1 513 ? 18.502 32.442  63.062 1.00 34.72  ? 491 VAL A CG1 1 
ATOM   3345 C  CG2 . VAL A 1 513 ? 17.638 30.477  64.354 1.00 36.71  ? 491 VAL A CG2 1 
ATOM   3346 N  N   . GLY A 1 514 ? 20.461 28.473  62.384 1.00 39.36  ? 492 GLY A N   1 
ATOM   3347 C  CA  . GLY A 1 514 ? 21.015 27.170  62.692 1.00 41.68  ? 492 GLY A CA  1 
ATOM   3348 C  C   . GLY A 1 514 ? 22.453 27.301  63.132 1.00 44.80  ? 492 GLY A C   1 
ATOM   3349 O  O   . GLY A 1 514 ? 23.098 28.332  62.921 1.00 40.83  ? 492 GLY A O   1 
ATOM   3350 N  N   . LYS A 1 515 ? 22.952 26.236  63.756 1.00 43.52  ? 493 LYS A N   1 
ATOM   3351 C  CA  . LYS A 1 515 ? 24.322 26.215  64.242 1.00 50.05  ? 493 LYS A CA  1 
ATOM   3352 C  C   . LYS A 1 515 ? 24.856 24.793  64.171 1.00 51.49  ? 493 LYS A C   1 
ATOM   3353 O  O   . LYS A 1 515 ? 24.103 23.823  64.290 1.00 46.91  ? 493 LYS A O   1 
ATOM   3354 C  CB  . LYS A 1 515 ? 24.422 26.753  65.675 1.00 46.53  ? 493 LYS A CB  1 
ATOM   3355 C  CG  . LYS A 1 515 ? 23.716 25.894  66.712 1.00 45.38  ? 493 LYS A CG  1 
ATOM   3356 C  CD  . LYS A 1 515 ? 23.815 26.503  68.101 1.00 43.36  ? 493 LYS A CD  1 
ATOM   3357 C  CE  . LYS A 1 515 ? 23.269 25.551  69.154 1.00 54.22  ? 493 LYS A CE  1 
ATOM   3358 N  NZ  . LYS A 1 515 ? 23.184 26.190  70.496 1.00 58.32  ? 493 LYS A NZ  1 
ATOM   3359 N  N   . LYS A 1 516 ? 26.166 24.682  63.967 1.00 45.03  ? 494 LYS A N   1 
ATOM   3360 C  CA  . LYS A 1 516 ? 26.858 23.402  63.934 1.00 51.99  ? 494 LYS A CA  1 
ATOM   3361 C  C   . LYS A 1 516 ? 28.122 23.497  64.772 1.00 57.31  ? 494 LYS A C   1 
ATOM   3362 O  O   . LYS A 1 516 ? 28.834 24.505  64.724 1.00 55.08  ? 494 LYS A O   1 
ATOM   3363 C  CB  . LYS A 1 516 ? 27.222 22.987  62.501 1.00 57.56  ? 494 LYS A CB  1 
ATOM   3364 C  CG  . LYS A 1 516 ? 26.038 22.695  61.596 1.00 62.83  ? 494 LYS A CG  1 
ATOM   3365 C  CD  . LYS A 1 516 ? 26.485 21.945  60.348 1.00 62.80  ? 494 LYS A CD  1 
ATOM   3366 C  CE  . LYS A 1 516 ? 25.369 21.848  59.321 1.00 69.87  ? 494 LYS A CE  1 
ATOM   3367 N  NZ  . LYS A 1 516 ? 25.246 23.095  58.515 1.00 73.35  ? 494 LYS A NZ  1 
ATOM   3368 N  N   . ASN A 1 517 ? 28.397 22.447  65.541 1.00 59.10  ? 495 ASN A N   1 
ATOM   3369 C  CA  . ASN A 1 517 ? 29.649 22.382  66.279 1.00 59.50  ? 495 ASN A CA  1 
ATOM   3370 C  C   . ASN A 1 517 ? 30.810 22.184  65.313 1.00 61.88  ? 495 ASN A C   1 
ATOM   3371 O  O   . ASN A 1 517 ? 30.696 21.464  64.317 1.00 64.23  ? 495 ASN A O   1 
ATOM   3372 C  CB  . ASN A 1 517 ? 29.612 21.248  67.304 1.00 60.72  ? 495 ASN A CB  1 
ATOM   3373 C  CG  . ASN A 1 517 ? 30.987 20.906  67.847 1.00 76.14  ? 495 ASN A CG  1 
ATOM   3374 O  OD1 . ASN A 1 517 ? 31.465 19.782  67.697 1.00 81.30  ? 495 ASN A OD1 1 
ATOM   3375 N  ND2 . ASN A 1 517 ? 31.633 21.880  68.480 1.00 66.25  ? 495 ASN A ND2 1 
ATOM   3376 N  N   . ASN A 1 518 ? 31.930 22.838  65.607 1.00 64.67  ? 496 ASN A N   1 
ATOM   3377 C  CA  . ASN A 1 518 ? 33.127 22.784  64.770 1.00 74.47  ? 496 ASN A CA  1 
ATOM   3378 C  C   . ASN A 1 518 ? 34.296 22.333  65.634 1.00 76.78  ? 496 ASN A C   1 
ATOM   3379 O  O   . ASN A 1 518 ? 35.077 23.157  66.128 1.00 80.41  ? 496 ASN A O   1 
ATOM   3380 C  CB  . ASN A 1 518 ? 33.398 24.139  64.114 1.00 70.50  ? 496 ASN A CB  1 
ATOM   3381 C  CG  . ASN A 1 518 ? 32.777 24.251  62.736 1.00 78.28  ? 496 ASN A CG  1 
ATOM   3382 O  OD1 . ASN A 1 518 ? 31.643 24.707  62.589 1.00 75.29  ? 496 ASN A OD1 1 
ATOM   3383 N  ND2 . ASN A 1 518 ? 33.517 23.831  61.716 1.00 82.43  ? 496 ASN A ND2 1 
ATOM   3384 N  N   . PRO A 1 519 ? 34.448 21.022  65.836 1.00 83.46  ? 497 PRO A N   1 
ATOM   3385 C  CA  . PRO A 1 519 ? 35.518 20.531  66.715 1.00 92.15  ? 497 PRO A CA  1 
ATOM   3386 C  C   . PRO A 1 519 ? 36.896 20.644  66.083 1.00 91.00  ? 497 PRO A C   1 
ATOM   3387 O  O   . PRO A 1 519 ? 37.827 21.172  66.700 1.00 92.17  ? 497 PRO A O   1 
ATOM   3388 C  CB  . PRO A 1 519 ? 35.126 19.068  66.959 1.00 92.22  ? 497 PRO A CB  1 
ATOM   3389 C  CG  . PRO A 1 519 ? 34.337 18.684  65.750 1.00 90.46  ? 497 PRO A CG  1 
ATOM   3390 C  CD  . PRO A 1 519 ? 33.633 19.928  65.276 1.00 79.71  ? 497 PRO A CD  1 
ATOM   3391 N  N   . TYR A 1 520 ? 37.037 20.158  64.852 1.00 84.99  ? 498 TYR A N   1 
ATOM   3392 C  CA  . TYR A 1 520 ? 38.323 20.146  64.156 1.00 90.68  ? 498 TYR A CA  1 
ATOM   3393 C  C   . TYR A 1 520 ? 38.573 21.433  63.386 1.00 95.25  ? 498 TYR A C   1 
ATOM   3394 O  O   . TYR A 1 520 ? 39.146 21.415  62.292 1.00 98.06  ? 498 TYR A O   1 
ATOM   3395 C  CB  . TYR A 1 520 ? 38.397 18.933  63.233 1.00 96.68  ? 498 TYR A CB  1 
ATOM   3396 C  CG  . TYR A 1 520 ? 38.772 17.648  63.943 1.00 95.34  ? 498 TYR A CG  1 
ATOM   3397 C  CD1 . TYR A 1 520 ? 38.170 17.294  65.144 1.00 92.13  ? 498 TYR A CD1 1 
ATOM   3398 C  CD2 . TYR A 1 520 ? 39.729 16.792  63.413 1.00 93.76  ? 498 TYR A CD2 1 
ATOM   3399 C  CE1 . TYR A 1 520 ? 38.508 16.126  65.797 1.00 93.93  ? 498 TYR A CE1 1 
ATOM   3400 C  CE2 . TYR A 1 520 ? 40.074 15.619  64.061 1.00 94.42  ? 498 TYR A CE2 1 
ATOM   3401 C  CZ  . TYR A 1 520 ? 39.459 15.292  65.252 1.00 86.94  ? 498 TYR A CZ  1 
ATOM   3402 O  OH  . TYR A 1 520 ? 39.796 14.129  65.903 1.00 71.99  ? 498 TYR A OH  1 
ATOM   3403 N  N   . SER A 1 521 ? 38.147 22.568  63.938 1.00 98.38  ? 499 SER A N   1 
ATOM   3404 C  CA  . SER A 1 521 ? 38.410 23.876  63.356 1.00 90.45  ? 499 SER A CA  1 
ATOM   3405 C  C   . SER A 1 521 ? 39.318 24.659  64.291 1.00 89.20  ? 499 SER A C   1 
ATOM   3406 O  O   . SER A 1 521 ? 38.943 24.910  65.446 1.00 80.94  ? 499 SER A O   1 
ATOM   3407 C  CB  . SER A 1 521 ? 37.107 24.631  63.106 1.00 88.38  ? 499 SER A CB  1 
ATOM   3408 O  OG  . SER A 1 521 ? 36.097 23.739  62.670 1.00 93.00  ? 499 SER A OG  1 
ATOM   3409 N  N   . PRO A 1 522 ? 40.502 25.066  63.839 1.00 88.84  ? 500 PRO A N   1 
ATOM   3410 C  CA  . PRO A 1 522 ? 41.539 25.565  64.753 1.00 89.95  ? 500 PRO A CA  1 
ATOM   3411 C  C   . PRO A 1 522 ? 41.512 27.061  65.034 1.00 87.09  ? 500 PRO A C   1 
ATOM   3412 O  O   . PRO A 1 522 ? 42.475 27.568  65.616 1.00 80.45  ? 500 PRO A O   1 
ATOM   3413 C  CB  . PRO A 1 522 ? 42.825 25.190  64.007 1.00 93.97  ? 500 PRO A CB  1 
ATOM   3414 C  CG  . PRO A 1 522 ? 42.446 25.292  62.559 1.00 92.98  ? 500 PRO A CG  1 
ATOM   3415 C  CD  . PRO A 1 522 ? 40.974 24.996  62.445 1.00 88.72  ? 500 PRO A CD  1 
ATOM   3416 N  N   . GLN A 1 523 ? 40.459 27.781  64.654 1.00 65.79  ? 501 GLN A N   1 
ATOM   3417 C  CA  . GLN A 1 523 ? 40.373 29.204  64.957 1.00 61.00  ? 501 GLN A CA  1 
ATOM   3418 C  C   . GLN A 1 523 ? 39.835 29.479  66.356 1.00 61.34  ? 501 GLN A C   1 
ATOM   3419 O  O   . GLN A 1 523 ? 39.539 30.636  66.673 1.00 61.75  ? 501 GLN A O   1 
ATOM   3420 C  CB  . GLN A 1 523 ? 39.505 29.916  63.915 1.00 54.60  ? 501 GLN A CB  1 
ATOM   3421 C  CG  . GLN A 1 523 ? 40.120 29.956  62.523 1.00 55.57  ? 501 GLN A CG  1 
ATOM   3422 C  CD  . GLN A 1 523 ? 39.516 31.034  61.645 1.00 55.04  ? 501 GLN A CD  1 
ATOM   3423 O  OE1 . GLN A 1 523 ? 38.396 30.895  61.153 1.00 58.02  ? 501 GLN A OE1 1 
ATOM   3424 N  NE2 . GLN A 1 523 ? 40.258 32.117  61.442 1.00 48.10  ? 501 GLN A NE2 1 
ATOM   3425 N  N   . GLY A 1 524 ? 39.710 28.453  67.197 1.00 59.70  ? 502 GLY A N   1 
ATOM   3426 C  CA  . GLY A 1 524 ? 39.166 28.628  68.528 1.00 52.52  ? 502 GLY A CA  1 
ATOM   3427 C  C   . GLY A 1 524 ? 37.688 28.932  68.577 1.00 46.23  ? 502 GLY A C   1 
ATOM   3428 O  O   . GLY A 1 524 ? 37.172 29.268  69.647 1.00 60.33  ? 502 GLY A O   1 
ATOM   3429 N  N   . ILE A 1 525 ? 36.990 28.822  67.452 1.00 49.51  ? 503 ILE A N   1 
ATOM   3430 C  CA  . ILE A 1 525 ? 35.572 29.139  67.350 1.00 51.66  ? 503 ILE A CA  1 
ATOM   3431 C  C   . ILE A 1 525 ? 34.829 27.812  67.258 1.00 54.05  ? 503 ILE A C   1 
ATOM   3432 O  O   . ILE A 1 525 ? 34.800 27.171  66.202 1.00 46.53  ? 503 ILE A O   1 
ATOM   3433 C  CB  . ILE A 1 525 ? 35.282 30.045  66.148 1.00 53.78  ? 503 ILE A CB  1 
ATOM   3434 C  CG1 . ILE A 1 525 ? 36.297 31.190  66.100 1.00 53.96  ? 503 ILE A CG1 1 
ATOM   3435 C  CG2 . ILE A 1 525 ? 33.874 30.593  66.214 1.00 50.83  ? 503 ILE A CG2 1 
ATOM   3436 C  CD1 . ILE A 1 525 ? 36.284 31.970  64.806 1.00 44.47  ? 503 ILE A CD1 1 
ATOM   3437 N  N   . GLU A 1 526 ? 34.222 27.396  68.371 1.00 56.09  ? 504 GLU A N   1 
ATOM   3438 C  CA  . GLU A 1 526 ? 33.636 26.065  68.473 1.00 57.66  ? 504 GLU A CA  1 
ATOM   3439 C  C   . GLU A 1 526 ? 32.329 25.918  67.707 1.00 58.00  ? 504 GLU A C   1 
ATOM   3440 O  O   . GLU A 1 526 ? 31.946 24.789  67.380 1.00 49.18  ? 504 GLU A O   1 
ATOM   3441 C  CB  . GLU A 1 526 ? 33.402 25.710  69.943 1.00 59.16  ? 504 GLU A CB  1 
ATOM   3442 C  CG  . GLU A 1 526 ? 32.409 26.621  70.654 1.00 67.26  ? 504 GLU A CG  1 
ATOM   3443 C  CD  . GLU A 1 526 ? 33.085 27.626  71.569 1.00 75.43  ? 504 GLU A CD  1 
ATOM   3444 O  OE1 . GLU A 1 526 ? 32.931 27.506  72.803 1.00 77.18  ? 504 GLU A OE1 1 
ATOM   3445 O  OE2 . GLU A 1 526 ? 33.767 28.538  71.054 1.00 67.82  ? 504 GLU A OE2 1 
ATOM   3446 N  N   . THR A 1 527 ? 31.640 27.016  67.410 1.00 54.14  ? 505 THR A N   1 
ATOM   3447 C  CA  . THR A 1 527 ? 30.313 26.956  66.811 1.00 42.38  ? 505 THR A CA  1 
ATOM   3448 C  C   . THR A 1 527 ? 30.214 27.933  65.651 1.00 46.40  ? 505 THR A C   1 
ATOM   3449 O  O   . THR A 1 527 ? 30.484 29.128  65.814 1.00 41.90  ? 505 THR A O   1 
ATOM   3450 C  CB  . THR A 1 527 ? 29.227 27.267  67.847 1.00 45.27  ? 505 THR A CB  1 
ATOM   3451 O  OG1 . THR A 1 527 ? 29.366 26.386  68.969 1.00 55.55  ? 505 THR A OG1 1 
ATOM   3452 C  CG2 . THR A 1 527 ? 27.842 27.093  67.239 1.00 43.96  ? 505 THR A CG2 1 
ATOM   3453 N  N   . ASN A 1 528 ? 29.828 27.422  64.486 1.00 46.22  ? 506 ASN A N   1 
ATOM   3454 C  CA  . ASN A 1 528 ? 29.515 28.246  63.327 1.00 44.60  ? 506 ASN A CA  1 
ATOM   3455 C  C   . ASN A 1 528 ? 28.011 28.477  63.282 1.00 42.95  ? 506 ASN A C   1 
ATOM   3456 O  O   . ASN A 1 528 ? 27.229 27.538  63.463 1.00 45.38  ? 506 ASN A O   1 
ATOM   3457 C  CB  . ASN A 1 528 ? 29.989 27.582  62.033 1.00 52.57  ? 506 ASN A CB  1 
ATOM   3458 C  CG  . ASN A 1 528 ? 31.494 27.645  61.862 1.00 57.86  ? 506 ASN A CG  1 
ATOM   3459 O  OD1 . ASN A 1 528 ? 32.226 27.949  62.804 1.00 59.34  ? 506 ASN A OD1 1 
ATOM   3460 N  ND2 . ASN A 1 528 ? 31.964 27.357  60.654 1.00 67.86  ? 506 ASN A ND2 1 
ATOM   3461 N  N   . TYR A 1 529 ? 27.611 29.722  63.047 1.00 44.31  ? 507 TYR A N   1 
ATOM   3462 C  CA  . TYR A 1 529 ? 26.207 30.103  63.021 1.00 39.00  ? 507 TYR A CA  1 
ATOM   3463 C  C   . TYR A 1 529 ? 25.771 30.379  61.589 1.00 37.56  ? 507 TYR A C   1 
ATOM   3464 O  O   . TYR A 1 529 ? 26.500 31.011  60.818 1.00 38.43  ? 507 TYR A O   1 
ATOM   3465 C  CB  . TYR A 1 529 ? 25.958 31.329  63.903 1.00 38.06  ? 507 TYR A CB  1 
ATOM   3466 C  CG  . TYR A 1 529 ? 26.100 31.039  65.382 1.00 42.89  ? 507 TYR A CG  1 
ATOM   3467 C  CD1 . TYR A 1 529 ? 27.347 31.044  65.994 1.00 37.44  ? 507 TYR A CD1 1 
ATOM   3468 C  CD2 . TYR A 1 529 ? 24.989 30.750  66.163 1.00 39.81  ? 507 TYR A CD2 1 
ATOM   3469 C  CE1 . TYR A 1 529 ? 27.483 30.776  67.344 1.00 42.07  ? 507 TYR A CE1 1 
ATOM   3470 C  CE2 . TYR A 1 529 ? 25.114 30.481  67.513 1.00 33.34  ? 507 TYR A CE2 1 
ATOM   3471 C  CZ  . TYR A 1 529 ? 26.363 30.495  68.098 1.00 38.40  ? 507 TYR A CZ  1 
ATOM   3472 O  OH  . TYR A 1 529 ? 26.492 30.226  69.442 1.00 40.09  ? 507 TYR A OH  1 
ATOM   3473 N  N   . TYR A 1 530 ? 24.582 29.898  61.238 1.00 38.25  ? 508 TYR A N   1 
ATOM   3474 C  CA  . TYR A 1 530 ? 24.063 29.991  59.884 1.00 44.76  ? 508 TYR A CA  1 
ATOM   3475 C  C   . TYR A 1 530 ? 22.734 30.734  59.876 1.00 43.82  ? 508 TYR A C   1 
ATOM   3476 O  O   . TYR A 1 530 ? 22.071 30.882  60.907 1.00 38.12  ? 508 TYR A O   1 
ATOM   3477 C  CB  . TYR A 1 530 ? 23.889 28.600  59.261 1.00 42.29  ? 508 TYR A CB  1 
ATOM   3478 C  CG  . TYR A 1 530 ? 25.166 27.794  59.212 1.00 53.70  ? 508 TYR A CG  1 
ATOM   3479 C  CD1 . TYR A 1 530 ? 26.156 28.084  58.282 1.00 53.38  ? 508 TYR A CD1 1 
ATOM   3480 C  CD2 . TYR A 1 530 ? 25.384 26.746  60.096 1.00 53.38  ? 508 TYR A CD2 1 
ATOM   3481 C  CE1 . TYR A 1 530 ? 27.326 27.351  58.233 1.00 48.68  ? 508 TYR A CE1 1 
ATOM   3482 C  CE2 . TYR A 1 530 ? 26.551 26.007  60.055 1.00 52.23  ? 508 TYR A CE2 1 
ATOM   3483 C  CZ  . TYR A 1 530 ? 27.518 26.314  59.121 1.00 57.97  ? 508 TYR A CZ  1 
ATOM   3484 O  OH  . TYR A 1 530 ? 28.682 25.582  59.076 1.00 64.92  ? 508 TYR A OH  1 
ATOM   3485 N  N   . LEU A 1 531 ? 22.349 31.197  58.689 1.00 45.53  ? 509 LEU A N   1 
ATOM   3486 C  CA  . LEU A 1 531 ? 21.121 31.967  58.523 1.00 50.65  ? 509 LEU A CA  1 
ATOM   3487 C  C   . LEU A 1 531 ? 20.507 31.628  57.176 1.00 55.10  ? 509 LEU A C   1 
ATOM   3488 O  O   . LEU A 1 531 ? 21.170 31.755  56.142 1.00 58.97  ? 509 LEU A O   1 
ATOM   3489 C  CB  . LEU A 1 531 ? 21.398 33.468  58.625 1.00 47.80  ? 509 LEU A CB  1 
ATOM   3490 C  CG  . LEU A 1 531 ? 20.231 34.398  58.289 1.00 51.89  ? 509 LEU A CG  1 
ATOM   3491 C  CD1 . LEU A 1 531 ? 19.246 34.473  59.447 1.00 53.38  ? 509 LEU A CD1 1 
ATOM   3492 C  CD2 . LEU A 1 531 ? 20.739 35.781  57.921 1.00 50.94  ? 509 LEU A CD2 1 
ATOM   3493 N  N   . ASN A 1 532 ? 19.247 31.199  57.189 1.00 49.30  ? 510 ASN A N   1 
ATOM   3494 C  CA  . ASN A 1 532 ? 18.499 30.938  55.961 1.00 51.69  ? 510 ASN A CA  1 
ATOM   3495 C  C   . ASN A 1 532 ? 18.019 32.276  55.415 1.00 56.77  ? 510 ASN A C   1 
ATOM   3496 O  O   . ASN A 1 532 ? 17.066 32.864  55.932 1.00 50.79  ? 510 ASN A O   1 
ATOM   3497 C  CB  . ASN A 1 532 ? 17.334 29.993  56.233 1.00 53.30  ? 510 ASN A CB  1 
ATOM   3498 C  CG  . ASN A 1 532 ? 16.696 29.465  54.962 1.00 53.94  ? 510 ASN A CG  1 
ATOM   3499 O  OD1 . ASN A 1 532 ? 16.290 30.232  54.090 1.00 57.59  ? 510 ASN A OD1 1 
ATOM   3500 N  ND2 . ASN A 1 532 ? 16.600 28.145  54.855 1.00 55.36  ? 510 ASN A ND2 1 
ATOM   3501 N  N   . GLN A 1 533 ? 18.682 32.762  54.363 1.00 59.30  ? 511 GLN A N   1 
ATOM   3502 C  CA  . GLN A 1 533 ? 18.350 34.077  53.823 1.00 53.43  ? 511 GLN A CA  1 
ATOM   3503 C  C   . GLN A 1 533 ? 16.928 34.123  53.279 1.00 57.04  ? 511 GLN A C   1 
ATOM   3504 O  O   . GLN A 1 533 ? 16.292 35.183  53.299 1.00 53.04  ? 511 GLN A O   1 
ATOM   3505 C  CB  . GLN A 1 533 ? 19.351 34.468  52.734 1.00 60.01  ? 511 GLN A CB  1 
ATOM   3506 C  CG  . GLN A 1 533 ? 20.664 35.025  53.267 1.00 66.69  ? 511 GLN A CG  1 
ATOM   3507 C  CD  . GLN A 1 533 ? 20.554 36.474  53.711 1.00 71.27  ? 511 GLN A CD  1 
ATOM   3508 O  OE1 . GLN A 1 533 ? 19.493 37.089  53.610 1.00 74.15  ? 511 GLN A OE1 1 
ATOM   3509 N  NE2 . GLN A 1 533 ? 21.657 37.026  54.204 1.00 68.73  ? 511 GLN A NE2 1 
ATOM   3510 N  N   . ASN A 1 534 ? 16.410 32.992  52.795 1.00 56.83  ? 512 ASN A N   1 
ATOM   3511 C  CA  . ASN A 1 534 ? 15.032 32.950  52.317 1.00 59.88  ? 512 ASN A CA  1 
ATOM   3512 C  C   . ASN A 1 534 ? 14.053 33.170  53.464 1.00 60.14  ? 512 ASN A C   1 
ATOM   3513 O  O   . ASN A 1 534 ? 13.236 34.099  53.432 1.00 61.55  ? 512 ASN A O   1 
ATOM   3514 C  CB  . ASN A 1 534 ? 14.761 31.614  51.617 1.00 66.59  ? 512 ASN A CB  1 
ATOM   3515 C  CG  . ASN A 1 534 ? 13.339 31.502  51.088 1.00 70.83  ? 512 ASN A CG  1 
ATOM   3516 O  OD1 . ASN A 1 534 ? 12.375 31.458  51.854 1.00 73.52  ? 512 ASN A OD1 1 
ATOM   3517 N  ND2 . ASN A 1 534 ? 13.206 31.453  49.768 1.00 79.63  ? 512 ASN A ND2 1 
ATOM   3518 N  N   . SER A 1 535 ? 14.118 32.317  54.489 1.00 57.17  ? 513 SER A N   1 
ATOM   3519 C  CA  . SER A 1 535 ? 13.222 32.461  55.632 1.00 58.77  ? 513 SER A CA  1 
ATOM   3520 C  C   . SER A 1 535 ? 13.461 33.771  56.368 1.00 53.17  ? 513 SER A C   1 
ATOM   3521 O  O   . SER A 1 535 ? 12.529 34.330  56.958 1.00 55.67  ? 513 SER A O   1 
ATOM   3522 C  CB  . SER A 1 535 ? 13.388 31.277  56.581 1.00 52.89  ? 513 SER A CB  1 
ATOM   3523 O  OG  . SER A 1 535 ? 13.293 30.052  55.878 1.00 59.65  ? 513 SER A OG  1 
ATOM   3524 N  N   . TYR A 1 536 ? 14.699 34.271  56.353 1.00 51.32  ? 514 TYR A N   1 
ATOM   3525 C  CA  . TYR A 1 536 ? 14.962 35.605  56.880 1.00 51.91  ? 514 TYR A CA  1 
ATOM   3526 C  C   . TYR A 1 536 ? 14.159 36.654  56.123 1.00 53.26  ? 514 TYR A C   1 
ATOM   3527 O  O   . TYR A 1 536 ? 13.604 37.578  56.728 1.00 50.61  ? 514 TYR A O   1 
ATOM   3528 C  CB  . TYR A 1 536 ? 16.459 35.913  56.804 1.00 51.11  ? 514 TYR A CB  1 
ATOM   3529 C  CG  . TYR A 1 536 ? 16.829 37.340  57.155 1.00 49.41  ? 514 TYR A CG  1 
ATOM   3530 C  CD1 . TYR A 1 536 ? 17.124 37.699  58.464 1.00 48.95  ? 514 TYR A CD1 1 
ATOM   3531 C  CD2 . TYR A 1 536 ? 16.895 38.327  56.177 1.00 54.67  ? 514 TYR A CD2 1 
ATOM   3532 C  CE1 . TYR A 1 536 ? 17.466 38.999  58.790 1.00 50.65  ? 514 TYR A CE1 1 
ATOM   3533 C  CE2 . TYR A 1 536 ? 17.233 39.629  56.494 1.00 49.87  ? 514 TYR A CE2 1 
ATOM   3534 C  CZ  . TYR A 1 536 ? 17.518 39.959  57.802 1.00 53.22  ? 514 TYR A CZ  1 
ATOM   3535 O  OH  . TYR A 1 536 ? 17.858 41.254  58.122 1.00 50.38  ? 514 TYR A OH  1 
ATOM   3536 N  N   . ASN A 1 537 ? 14.077 36.520  54.797 1.00 56.83  ? 515 ASN A N   1 
ATOM   3537 C  CA  . ASN A 1 537 ? 13.361 37.506  53.996 1.00 56.43  ? 515 ASN A CA  1 
ATOM   3538 C  C   . ASN A 1 537 ? 11.868 37.492  54.299 1.00 51.13  ? 515 ASN A C   1 
ATOM   3539 O  O   . ASN A 1 537 ? 11.253 38.554  54.447 1.00 44.99  ? 515 ASN A O   1 
ATOM   3540 C  CB  . ASN A 1 537 ? 13.609 37.256  52.509 1.00 53.09  ? 515 ASN A CB  1 
ATOM   3541 C  CG  . ASN A 1 537 ? 15.010 37.642  52.079 1.00 57.85  ? 515 ASN A CG  1 
ATOM   3542 O  OD1 . ASN A 1 537 ? 15.642 38.505  52.688 1.00 59.32  ? 515 ASN A OD1 1 
ATOM   3543 N  ND2 . ASN A 1 537 ? 15.504 37.002  51.026 1.00 53.78  ? 515 ASN A ND2 1 
ATOM   3544 N  N   . GLN A 1 538 ? 11.270 36.302  54.405 1.00 55.13  ? 516 GLN A N   1 
ATOM   3545 C  CA  . GLN A 1 538 ? 9.832  36.220  54.642 1.00 49.75  ? 516 GLN A CA  1 
ATOM   3546 C  C   . GLN A 1 538 ? 9.455  36.819  55.991 1.00 59.76  ? 516 GLN A C   1 
ATOM   3547 O  O   . GLN A 1 538 ? 8.468  37.557  56.094 1.00 56.83  ? 516 GLN A O   1 
ATOM   3548 C  CB  . GLN A 1 538 ? 9.360  34.769  54.546 1.00 57.12  ? 516 GLN A CB  1 
ATOM   3549 C  CG  . GLN A 1 538 ? 7.908  34.573  54.959 1.00 74.76  ? 516 GLN A CG  1 
ATOM   3550 C  CD  . GLN A 1 538 ? 7.398  33.171  54.687 1.00 82.69  ? 516 GLN A CD  1 
ATOM   3551 O  OE1 . GLN A 1 538 ? 8.162  32.278  54.331 1.00 82.00  ? 516 GLN A OE1 1 
ATOM   3552 N  NE2 . GLN A 1 538 ? 6.096  32.973  54.857 1.00 71.22  ? 516 GLN A NE2 1 
ATOM   3553 N  N   . ILE A 1 539 ? 10.231 36.520  57.036 1.00 59.58  ? 517 ILE A N   1 
ATOM   3554 C  CA  . ILE A 1 539 ? 9.942  37.068  58.359 1.00 49.19  ? 517 ILE A CA  1 
ATOM   3555 C  C   . ILE A 1 539 ? 9.995  38.591  58.330 1.00 53.64  ? 517 ILE A C   1 
ATOM   3556 O  O   . ILE A 1 539 ? 9.160  39.268  58.942 1.00 52.56  ? 517 ILE A O   1 
ATOM   3557 C  CB  . ILE A 1 539 ? 10.912 36.485  59.405 1.00 49.17  ? 517 ILE A CB  1 
ATOM   3558 C  CG1 . ILE A 1 539 ? 10.644 34.992  59.609 1.00 49.17  ? 517 ILE A CG1 1 
ATOM   3559 C  CG2 . ILE A 1 539 ? 10.794 37.232  60.727 1.00 42.40  ? 517 ILE A CG2 1 
ATOM   3560 C  CD1 . ILE A 1 539 ? 11.565 34.338  60.619 1.00 46.65  ? 517 ILE A CD1 1 
ATOM   3561 N  N   . GLN A 1 540 ? 10.969 39.154  57.609 1.00 48.91  ? 518 GLN A N   1 
ATOM   3562 C  CA  . GLN A 1 540 ? 11.067 40.607  57.518 1.00 55.36  ? 518 GLN A CA  1 
ATOM   3563 C  C   . GLN A 1 540 ? 9.866  41.199  56.789 1.00 55.22  ? 518 GLN A C   1 
ATOM   3564 O  O   . GLN A 1 540 ? 9.375  42.270  57.164 1.00 56.92  ? 518 GLN A O   1 
ATOM   3565 C  CB  . GLN A 1 540 ? 12.368 41.010  56.823 1.00 51.24  ? 518 GLN A CB  1 
ATOM   3566 C  CG  . GLN A 1 540 ? 13.635 40.558  57.538 1.00 52.61  ? 518 GLN A CG  1 
ATOM   3567 C  CD  . GLN A 1 540 ? 13.924 41.353  58.796 1.00 53.05  ? 518 GLN A CD  1 
ATOM   3568 O  OE1 . GLN A 1 540 ? 13.349 42.418  59.020 1.00 56.46  ? 518 GLN A OE1 1 
ATOM   3569 N  NE2 . GLN A 1 540 ? 14.822 40.836  59.627 1.00 51.02  ? 518 GLN A NE2 1 
ATOM   3570 N  N   . THR A 1 541 ? 9.375  40.518  55.748 1.00 50.49  ? 519 THR A N   1 
ATOM   3571 C  CA  . THR A 1 541 ? 8.207  41.021  55.029 1.00 55.34  ? 519 THR A CA  1 
ATOM   3572 C  C   . THR A 1 541 ? 6.960  40.986  55.903 1.00 56.20  ? 519 THR A C   1 
ATOM   3573 O  O   . THR A 1 541 ? 6.175  41.942  55.907 1.00 59.90  ? 519 THR A O   1 
ATOM   3574 C  CB  . THR A 1 541 ? 7.977  40.219  53.746 1.00 54.37  ? 519 THR A CB  1 
ATOM   3575 O  OG1 . THR A 1 541 ? 7.682  38.856  54.076 1.00 63.41  ? 519 THR A OG1 1 
ATOM   3576 C  CG2 . THR A 1 541 ? 9.200  40.279  52.843 1.00 48.81  ? 519 THR A CG2 1 
ATOM   3577 N  N   . ILE A 1 542 ? 6.757  39.893  56.644 1.00 54.80  ? 520 ILE A N   1 
ATOM   3578 C  CA  . ILE A 1 542 ? 5.612  39.811  57.549 1.00 54.93  ? 520 ILE A CA  1 
ATOM   3579 C  C   . ILE A 1 542 ? 5.671  40.929  58.580 1.00 56.17  ? 520 ILE A C   1 
ATOM   3580 O  O   . ILE A 1 542 ? 4.643  41.515  58.944 1.00 58.45  ? 520 ILE A O   1 
ATOM   3581 C  CB  . ILE A 1 542 ? 5.551  38.427  58.221 1.00 55.88  ? 520 ILE A CB  1 
ATOM   3582 C  CG1 . ILE A 1 542 ? 5.539  37.315  57.172 1.00 60.30  ? 520 ILE A CG1 1 
ATOM   3583 C  CG2 . ILE A 1 542 ? 4.325  38.318  59.114 1.00 58.68  ? 520 ILE A CG2 1 
ATOM   3584 C  CD1 . ILE A 1 542 ? 6.034  35.987  57.698 1.00 59.83  ? 520 ILE A CD1 1 
ATOM   3585 N  N   . ASN A 1 543 ? 6.861  41.206  59.070 1.00 47.13  ? 521 ASN A N   1 
ATOM   3586 C  CA  . ASN A 1 543 ? 7.027  42.274  60.072 1.00 51.60  ? 521 ASN A CA  1 
ATOM   3587 C  C   . ASN A 1 543 ? 6.577  43.579  59.431 1.00 53.26  ? 521 ASN A C   1 
ATOM   3588 O  O   . ASN A 1 543 ? 5.872  44.334  60.040 1.00 50.35  ? 521 ASN A O   1 
ATOM   3589 C  CB  . ASN A 1 543 ? 8.482  42.409  60.493 1.00 50.19  ? 521 ASN A CB  1 
ATOM   3590 C  CG  . ASN A 1 543 ? 8.677  43.553  61.452 1.00 48.28  ? 521 ASN A CG  1 
ATOM   3591 O  OD1 . ASN A 1 543 ? 7.913  43.704  62.374 1.00 43.37  ? 521 ASN A OD1 1 
ATOM   3592 N  ND2 . ASN A 1 543 ? 9.683  44.363  61.212 1.00 48.12  ? 521 ASN A ND2 1 
ATOM   3593 N  N   . GLN A 1 544 ? 6.971  43.779  58.191 1.00 55.25  ? 522 GLN A N   1 
ATOM   3594 C  CA  . GLN A 1 544 ? 6.619  45.000  57.447 1.00 57.11  ? 522 GLN A CA  1 
ATOM   3595 C  C   . GLN A 1 544 ? 5.117  45.011  57.200 1.00 51.99  ? 522 GLN A C   1 
ATOM   3596 O  O   . GLN A 1 544 ? 4.536  46.051  57.323 1.00 54.34  ? 522 GLN A O   1 
ATOM   3597 C  CB  . GLN A 1 544 ? 7.441  45.038  56.170 1.00 59.22  ? 522 GLN A CB  1 
ATOM   3598 C  CG  . GLN A 1 544 ? 8.904  45.258  56.465 1.00 59.14  ? 522 GLN A CG  1 
ATOM   3599 C  CD  . GLN A 1 544 ? 9.151  46.686  56.860 1.00 66.50  ? 522 GLN A CD  1 
ATOM   3600 O  OE1 . GLN A 1 544 ? 9.681  46.974  57.918 1.00 64.23  ? 522 GLN A OE1 1 
ATOM   3601 N  NE2 . GLN A 1 544 ? 8.751  47.599  55.998 1.00 74.18  ? 522 GLN A NE2 1 
ATOM   3602 N  N   . GLU A 1 545 ? 4.522  43.849  56.953 1.00 57.69  ? 523 GLU A N   1 
ATOM   3603 C  CA  . GLU A 1 545 ? 3.057  43.755  56.737 1.00 60.23  ? 523 GLU A CA  1 
ATOM   3604 C  C   . GLU A 1 545 ? 2.264  44.128  58.001 1.00 58.93  ? 523 GLU A C   1 
ATOM   3605 O  O   . GLU A 1 545 ? 1.158  44.588  57.839 1.00 57.79  ? 523 GLU A O   1 
ATOM   3606 C  CB  . GLU A 1 545 ? 2.681  42.381  56.187 1.00 65.48  ? 523 GLU A CB  1 
ATOM   3607 C  CG  . GLU A 1 545 ? 3.109  42.166  54.741 1.00 67.40  ? 523 GLU A CG  1 
ATOM   3608 C  CD  . GLU A 1 545 ? 3.025  40.729  54.261 1.00 75.83  ? 523 GLU A CD  1 
ATOM   3609 O  OE1 . GLU A 1 545 ? 2.805  39.847  55.091 1.00 74.75  ? 523 GLU A OE1 1 
ATOM   3610 O  OE2 . GLU A 1 545 ? 3.151  40.499  53.062 1.00 77.81  ? 523 GLU A OE2 1 
ATOM   3611 N  N   . LEU A 1 546 ? 2.807  43.955  59.205 1.00 53.74  ? 524 LEU A N   1 
ATOM   3612 C  CA  . LEU A 1 546 ? 2.059  44.304  60.437 1.00 53.78  ? 524 LEU A CA  1 
ATOM   3613 C  C   . LEU A 1 546 ? 2.518  45.638  61.025 1.00 49.62  ? 524 LEU A C   1 
ATOM   3614 O  O   . LEU A 1 546 ? 3.362  46.279  60.420 1.00 53.96  ? 524 LEU A O   1 
ATOM   3615 C  CB  . LEU A 1 546 ? 2.207  43.173  61.447 1.00 53.18  ? 524 LEU A CB  1 
ATOM   3616 C  CG  . LEU A 1 546 ? 1.943  41.784  60.885 1.00 58.72  ? 524 LEU A CG  1 
ATOM   3617 C  CD1 . LEU A 1 546 ? 2.609  40.719  61.717 1.00 53.10  ? 524 LEU A CD1 1 
ATOM   3618 C  CD2 . LEU A 1 546 ? 0.457  41.525  60.783 1.00 63.80  ? 524 LEU A CD2 1 
HETATM 3619 CD CD  . CD  B 2 .   ? 6.333  47.438  69.159 0.77 70.48  ? 601 CD  A CD  1 
HETATM 3620 CD CD  . CD  C 2 .   ? 44.170 61.271  46.076 1.00 35.40  ? 602 CD  A CD  1 
HETATM 3621 CD CD  . CD  D 2 .   ? 57.871 67.967  52.849 1.00 35.63  ? 603 CD  A CD  1 
HETATM 3622 CD CD  . CD  E 2 .   ? 63.870 81.288  54.903 0.43 50.15  ? 604 CD  A CD  1 
HETATM 3623 CD CD  . CD  F 2 .   ? 20.625 82.629  63.906 0.57 62.17  ? 605 CD  A CD  1 
HETATM 3624 CD CD  . CD  G 2 .   ? 41.988 65.314  71.047 0.79 77.50  ? 606 CD  A CD  1 
HETATM 3625 CD CD  . CD  H 2 .   ? 47.298 54.054  70.923 1.00 103.05 ? 607 CD  A CD  1 
HETATM 3626 CD CD  . CD  I 2 .   ? 34.661 84.432  46.402 0.72 42.63  ? 608 CD  A CD  1 
HETATM 3627 CD CD  . CD  J 2 .   ? 27.319 69.485  53.816 0.42 47.96  ? 609 CD  A CD  1 
HETATM 3628 CD CD  . CD  K 2 .   ? 27.521 76.141  47.810 0.48 71.23  ? 610 CD  A CD  1 
HETATM 3629 O  O   . HOH L 3 .   ? 37.311 63.175  48.752 1.00 38.36  ? 701 HOH A O   1 
HETATM 3630 O  O   . HOH L 3 .   ? 24.038 85.490  69.338 1.00 39.04  ? 702 HOH A O   1 
HETATM 3631 O  O   . HOH L 3 .   ? 42.579 78.600  69.713 1.00 46.66  ? 703 HOH A O   1 
HETATM 3632 O  O   . HOH L 3 .   ? 33.815 56.200  64.848 1.00 45.50  ? 704 HOH A O   1 
HETATM 3633 O  O   . HOH L 3 .   ? 47.767 105.593 66.796 1.00 47.37  ? 705 HOH A O   1 
HETATM 3634 O  O   . HOH L 3 .   ? 27.897 72.609  49.406 1.00 35.90  ? 706 HOH A O   1 
HETATM 3635 O  O   . HOH L 3 .   ? 35.549 58.941  44.725 1.00 45.97  ? 707 HOH A O   1 
HETATM 3636 O  O   . HOH L 3 .   ? 56.434 96.053  64.898 1.00 42.04  ? 708 HOH A O   1 
HETATM 3637 O  O   . HOH L 3 .   ? 52.396 91.245  53.898 1.00 43.63  ? 709 HOH A O   1 
HETATM 3638 O  O   . HOH L 3 .   ? 2.306  38.523  71.174 1.00 55.10  ? 710 HOH A O   1 
HETATM 3639 O  O   . HOH L 3 .   ? 44.038 91.089  72.543 1.00 44.25  ? 711 HOH A O   1 
HETATM 3640 O  O   . HOH L 3 .   ? 50.538 70.251  58.039 1.00 29.94  ? 712 HOH A O   1 
HETATM 3641 O  O   . HOH L 3 .   ? 64.117 88.356  58.900 1.00 48.07  ? 713 HOH A O   1 
HETATM 3642 O  O   . HOH L 3 .   ? 48.144 38.672  69.134 1.00 43.04  ? 714 HOH A O   1 
HETATM 3643 O  O   . HOH L 3 .   ? 40.951 59.510  67.665 1.00 42.29  ? 715 HOH A O   1 
HETATM 3644 O  O   . HOH L 3 .   ? 61.137 101.284 53.043 1.00 58.46  ? 716 HOH A O   1 
HETATM 3645 O  O   . HOH L 3 .   ? 32.094 78.421  69.375 1.00 31.22  ? 717 HOH A O   1 
HETATM 3646 O  O   . HOH L 3 .   ? 34.594 74.774  43.198 1.00 36.69  ? 718 HOH A O   1 
HETATM 3647 O  O   . HOH L 3 .   ? 48.710 52.167  57.163 1.00 44.04  ? 719 HOH A O   1 
HETATM 3648 O  O   . HOH L 3 .   ? 38.333 101.750 45.201 1.00 51.47  ? 720 HOH A O   1 
HETATM 3649 O  O   . HOH L 3 .   ? 46.715 75.075  65.706 1.00 26.10  ? 721 HOH A O   1 
HETATM 3650 O  O   . HOH L 3 .   ? 50.899 93.729  70.200 1.00 43.07  ? 722 HOH A O   1 
HETATM 3651 O  O   . HOH L 3 .   ? 62.454 77.882  55.243 1.00 34.66  ? 723 HOH A O   1 
HETATM 3652 O  O   . HOH L 3 .   ? 52.383 75.384  50.117 1.00 40.31  ? 724 HOH A O   1 
HETATM 3653 O  O   . HOH L 3 .   ? 40.349 39.147  70.300 1.00 31.25  ? 725 HOH A O   1 
HETATM 3654 O  O   . HOH L 3 .   ? 20.960 85.137  62.607 1.00 49.90  ? 726 HOH A O   1 
HETATM 3655 O  O   . HOH L 3 .   ? 40.802 53.264  50.648 1.00 37.43  ? 727 HOH A O   1 
HETATM 3656 O  O   A HOH L 3 .   ? 24.594 88.113  63.111 0.57 33.58  ? 728 HOH A O   1 
HETATM 3657 O  O   B HOH L 3 .   ? 24.939 89.985  61.726 0.43 28.53  ? 728 HOH A O   1 
HETATM 3658 O  O   . HOH L 3 .   ? 61.291 82.284  54.653 1.00 25.04  ? 729 HOH A O   1 
HETATM 3659 O  O   . HOH L 3 .   ? 49.942 88.297  66.322 1.00 30.06  ? 730 HOH A O   1 
HETATM 3660 O  O   . HOH L 3 .   ? 34.334 96.897  48.554 1.00 43.26  ? 731 HOH A O   1 
HETATM 3661 O  O   . HOH L 3 .   ? 39.368 74.552  47.963 1.00 25.39  ? 732 HOH A O   1 
HETATM 3662 O  O   . HOH L 3 .   ? 49.958 111.886 69.982 1.00 54.39  ? 733 HOH A O   1 
HETATM 3663 O  O   . HOH L 3 .   ? 37.493 95.770  55.732 1.00 33.27  ? 734 HOH A O   1 
HETATM 3664 O  O   . HOH L 3 .   ? 66.782 85.098  56.384 1.00 54.25  ? 735 HOH A O   1 
HETATM 3665 O  O   . HOH L 3 .   ? 29.238 42.386  72.784 1.00 38.54  ? 736 HOH A O   1 
HETATM 3666 O  O   . HOH L 3 .   ? 50.686 95.912  58.010 1.00 34.83  ? 737 HOH A O   1 
HETATM 3667 O  O   . HOH L 3 .   ? 39.814 97.499  51.110 1.00 33.08  ? 738 HOH A O   1 
HETATM 3668 O  O   . HOH L 3 .   ? 50.910 86.194  64.920 1.00 38.41  ? 739 HOH A O   1 
HETATM 3669 O  O   . HOH L 3 .   ? 47.523 47.715  64.248 1.00 32.21  ? 740 HOH A O   1 
HETATM 3670 O  O   . HOH L 3 .   ? 36.894 69.366  46.305 1.00 30.14  ? 741 HOH A O   1 
HETATM 3671 O  O   . HOH L 3 .   ? 56.746 84.374  51.189 1.00 27.68  ? 742 HOH A O   1 
HETATM 3672 O  O   . HOH L 3 .   ? 4.998  43.897  63.457 1.00 50.92  ? 743 HOH A O   1 
HETATM 3673 O  O   . HOH L 3 .   ? 24.888 91.718  69.294 1.00 42.70  ? 744 HOH A O   1 
HETATM 3674 O  O   . HOH L 3 .   ? 11.096 44.043  58.959 1.00 51.38  ? 745 HOH A O   1 
HETATM 3675 O  O   . HOH L 3 .   ? 45.676 56.582  48.537 1.00 33.05  ? 746 HOH A O   1 
HETATM 3676 O  O   . HOH L 3 .   ? 47.607 92.031  49.092 1.00 40.29  ? 747 HOH A O   1 
HETATM 3677 O  O   . HOH L 3 .   ? 41.798 73.966  70.212 1.00 50.36  ? 748 HOH A O   1 
HETATM 3678 O  O   . HOH L 3 .   ? 13.371 35.944  72.794 1.00 27.82  ? 749 HOH A O   1 
HETATM 3679 O  O   . HOH L 3 .   ? 26.079 77.639  62.577 1.00 38.47  ? 750 HOH A O   1 
HETATM 3680 O  O   . HOH L 3 .   ? 8.108  35.825  69.198 1.00 54.75  ? 751 HOH A O   1 
HETATM 3681 O  O   . HOH L 3 .   ? 39.136 97.559  71.725 1.00 36.81  ? 752 HOH A O   1 
HETATM 3682 O  O   . HOH L 3 .   ? 45.973 71.948  45.180 1.00 50.74  ? 753 HOH A O   1 
HETATM 3683 O  O   . HOH L 3 .   ? 51.321 79.843  64.087 1.00 36.42  ? 754 HOH A O   1 
HETATM 3684 O  O   . HOH L 3 .   ? 32.213 65.142  44.407 1.00 31.34  ? 755 HOH A O   1 
HETATM 3685 O  O   . HOH L 3 .   ? 35.286 85.040  50.899 1.00 30.77  ? 756 HOH A O   1 
HETATM 3686 O  O   . HOH L 3 .   ? 52.807 96.058  76.201 1.00 63.06  ? 757 HOH A O   1 
HETATM 3687 O  O   . HOH L 3 .   ? 44.883 107.618 67.014 1.00 46.21  ? 758 HOH A O   1 
HETATM 3688 O  O   . HOH L 3 .   ? 36.813 66.178  45.360 1.00 39.20  ? 759 HOH A O   1 
HETATM 3689 O  O   . HOH L 3 .   ? 39.370 34.474  52.752 1.00 42.86  ? 760 HOH A O   1 
HETATM 3690 O  O   . HOH L 3 .   ? 36.183 57.637  47.990 1.00 25.12  ? 761 HOH A O   1 
HETATM 3691 O  O   . HOH L 3 .   ? 47.901 50.075  55.345 1.00 36.71  ? 762 HOH A O   1 
HETATM 3692 O  O   . HOH L 3 .   ? 45.670 66.938  53.343 1.00 26.68  ? 763 HOH A O   1 
HETATM 3693 O  O   . HOH L 3 .   ? 39.054 77.218  48.104 1.00 30.05  ? 764 HOH A O   1 
HETATM 3694 O  O   A HOH L 3 .   ? 38.079 40.652  73.597 0.42 26.27  ? 765 HOH A O   1 
HETATM 3695 O  O   B HOH L 3 .   ? 38.435 38.644  72.689 0.58 26.96  ? 765 HOH A O   1 
HETATM 3696 O  O   . HOH L 3 .   ? 52.741 84.457  49.431 1.00 34.13  ? 766 HOH A O   1 
HETATM 3697 O  O   . HOH L 3 .   ? 46.363 102.520 71.385 1.00 46.61  ? 767 HOH A O   1 
HETATM 3698 O  O   . HOH L 3 .   ? 54.095 89.151  53.062 1.00 35.50  ? 768 HOH A O   1 
HETATM 3699 O  O   . HOH L 3 .   ? 61.311 73.688  57.061 1.00 42.14  ? 769 HOH A O   1 
HETATM 3700 O  O   . HOH L 3 .   ? 61.624 78.051  60.244 1.00 54.71  ? 770 HOH A O   1 
HETATM 3701 O  O   . HOH L 3 .   ? 42.746 87.073  73.800 1.00 41.54  ? 771 HOH A O   1 
HETATM 3702 O  O   . HOH L 3 .   ? 41.595 55.153  48.910 1.00 37.96  ? 772 HOH A O   1 
HETATM 3703 O  O   . HOH L 3 .   ? 37.533 43.720  54.262 1.00 40.43  ? 773 HOH A O   1 
HETATM 3704 O  O   . HOH L 3 .   ? 44.873 79.429  49.544 1.00 33.56  ? 774 HOH A O   1 
HETATM 3705 O  O   . HOH L 3 .   ? 27.082 80.525  65.671 1.00 43.12  ? 775 HOH A O   1 
HETATM 3706 O  O   . HOH L 3 .   ? 30.180 69.911  55.111 1.00 41.16  ? 776 HOH A O   1 
HETATM 3707 O  O   . HOH L 3 .   ? 41.789 82.802  50.812 1.00 32.67  ? 777 HOH A O   1 
HETATM 3708 O  O   . HOH L 3 .   ? 31.858 44.999  66.690 1.00 34.89  ? 778 HOH A O   1 
HETATM 3709 O  O   . HOH L 3 .   ? 49.826 61.037  51.958 1.00 32.19  ? 779 HOH A O   1 
HETATM 3710 O  O   . HOH L 3 .   ? 29.638 32.167  62.841 1.00 37.54  ? 780 HOH A O   1 
HETATM 3711 O  O   . HOH L 3 .   ? 31.334 87.576  71.252 1.00 29.13  ? 781 HOH A O   1 
HETATM 3712 O  O   . HOH L 3 .   ? 60.846 87.685  51.215 1.00 32.03  ? 782 HOH A O   1 
HETATM 3713 O  O   . HOH L 3 .   ? 54.328 75.052  52.257 1.00 40.41  ? 783 HOH A O   1 
HETATM 3714 O  O   . HOH L 3 .   ? 54.342 72.719  56.633 1.00 31.42  ? 784 HOH A O   1 
HETATM 3715 O  O   . HOH L 3 .   ? 42.445 85.676  51.074 1.00 31.68  ? 785 HOH A O   1 
HETATM 3716 O  O   . HOH L 3 .   ? 56.960 74.514  50.458 1.00 32.10  ? 786 HOH A O   1 
HETATM 3717 O  O   . HOH L 3 .   ? 28.702 66.285  50.154 1.00 33.81  ? 787 HOH A O   1 
HETATM 3718 O  O   . HOH L 3 .   ? 37.161 65.817  70.303 1.00 54.87  ? 788 HOH A O   1 
HETATM 3719 O  O   . HOH L 3 .   ? 60.322 68.269  53.832 1.00 18.20  ? 789 HOH A O   1 
HETATM 3720 O  O   . HOH L 3 .   ? 20.464 39.293  55.420 1.00 63.28  ? 790 HOH A O   1 
HETATM 3721 O  O   . HOH L 3 .   ? 49.348 71.700  56.328 1.00 29.72  ? 791 HOH A O   1 
HETATM 3722 O  O   . HOH L 3 .   ? 41.693 50.862  48.569 1.00 47.90  ? 792 HOH A O   1 
HETATM 3723 O  O   . HOH L 3 .   ? 33.009 33.897  73.567 1.00 42.39  ? 793 HOH A O   1 
HETATM 3724 O  O   . HOH L 3 .   ? 48.952 55.545  55.019 1.00 40.49  ? 794 HOH A O   1 
HETATM 3725 O  O   . HOH L 3 .   ? 34.584 43.143  75.065 1.00 41.27  ? 795 HOH A O   1 
HETATM 3726 O  O   . HOH L 3 .   ? 49.945 71.014  60.734 1.00 29.04  ? 796 HOH A O   1 
HETATM 3727 O  O   . HOH L 3 .   ? 61.397 100.968 57.482 1.00 57.48  ? 797 HOH A O   1 
HETATM 3728 O  O   . HOH L 3 .   ? 27.514 84.051  48.706 1.00 48.41  ? 798 HOH A O   1 
HETATM 3729 O  O   . HOH L 3 .   ? 24.967 73.032  49.909 1.00 58.71  ? 799 HOH A O   1 
HETATM 3730 O  O   . HOH L 3 .   ? 37.637 48.308  54.511 1.00 29.74  ? 800 HOH A O   1 
HETATM 3731 O  O   . HOH L 3 .   ? 45.487 76.914  49.973 1.00 32.09  ? 801 HOH A O   1 
HETATM 3732 O  O   . HOH L 3 .   ? 44.341 44.706  70.168 1.00 42.54  ? 802 HOH A O   1 
HETATM 3733 O  O   . HOH L 3 .   ? 51.408 94.343  63.027 1.00 32.92  ? 803 HOH A O   1 
HETATM 3734 O  O   . HOH L 3 .   ? 47.505 47.354  68.410 1.00 40.37  ? 804 HOH A O   1 
HETATM 3735 O  O   . HOH L 3 .   ? 54.138 94.501  64.303 1.00 39.09  ? 805 HOH A O   1 
HETATM 3736 O  O   . HOH L 3 .   ? 41.552 57.108  67.504 1.00 36.44  ? 806 HOH A O   1 
HETATM 3737 O  O   . HOH L 3 .   ? 28.866 32.734  75.324 1.00 36.80  ? 807 HOH A O   1 
HETATM 3738 O  O   . HOH L 3 .   ? 44.359 74.077  47.659 1.00 44.28  ? 808 HOH A O   1 
HETATM 3739 O  O   . HOH L 3 .   ? 56.691 67.077  56.879 1.00 43.98  ? 809 HOH A O   1 
HETATM 3740 O  O   . HOH L 3 .   ? 51.439 49.872  63.693 1.00 47.86  ? 810 HOH A O   1 
HETATM 3741 O  O   . HOH L 3 .   ? 46.534 80.764  68.726 1.00 42.99  ? 811 HOH A O   1 
HETATM 3742 O  O   . HOH L 3 .   ? 47.627 50.679  51.350 1.00 37.36  ? 812 HOH A O   1 
HETATM 3743 O  O   . HOH L 3 .   ? 48.353 53.008  50.774 1.00 45.53  ? 813 HOH A O   1 
HETATM 3744 O  O   . HOH L 3 .   ? 52.205 95.909  54.707 1.00 37.17  ? 814 HOH A O   1 
HETATM 3745 O  O   . HOH L 3 .   ? 41.807 97.381  72.322 1.00 36.83  ? 815 HOH A O   1 
HETATM 3746 O  O   . HOH L 3 .   ? 18.020 46.050  67.801 1.00 49.74  ? 816 HOH A O   1 
HETATM 3747 O  O   . HOH L 3 .   ? 36.977 77.589  71.126 1.00 41.71  ? 817 HOH A O   1 
HETATM 3748 O  O   . HOH L 3 .   ? 40.374 60.853  47.798 1.00 37.16  ? 818 HOH A O   1 
HETATM 3749 O  O   . HOH L 3 .   ? 38.494 49.890  72.230 1.00 45.44  ? 819 HOH A O   1 
HETATM 3750 O  O   . HOH L 3 .   ? 35.650 40.672  74.415 1.00 30.96  ? 820 HOH A O   1 
HETATM 3751 O  O   . HOH L 3 .   ? 28.847 31.950  70.981 1.00 43.07  ? 821 HOH A O   1 
HETATM 3752 O  O   . HOH L 3 .   ? 31.843 103.585 57.586 1.00 61.48  ? 822 HOH A O   1 
HETATM 3753 O  O   . HOH L 3 .   ? 41.761 73.183  47.261 1.00 37.70  ? 823 HOH A O   1 
HETATM 3754 O  O   . HOH L 3 .   ? 39.660 50.241  47.082 1.00 54.62  ? 824 HOH A O   1 
HETATM 3755 O  O   . HOH L 3 .   ? 41.712 89.000  50.729 1.00 37.83  ? 825 HOH A O   1 
HETATM 3756 O  O   A HOH L 3 .   ? 39.112 102.209 56.921 0.49 26.65  ? 826 HOH A O   1 
HETATM 3757 O  O   B HOH L 3 .   ? 38.483 102.632 58.600 0.51 25.69  ? 826 HOH A O   1 
HETATM 3758 O  O   . HOH L 3 .   ? 37.092 85.421  47.269 1.00 34.55  ? 827 HOH A O   1 
HETATM 3759 O  O   . HOH L 3 .   ? 28.158 71.937  54.887 1.00 37.65  ? 828 HOH A O   1 
HETATM 3760 O  O   . HOH L 3 .   ? 41.946 46.337  49.785 1.00 45.63  ? 829 HOH A O   1 
HETATM 3761 O  O   . HOH L 3 .   ? 53.065 53.569  63.139 1.00 43.81  ? 830 HOH A O   1 
HETATM 3762 O  O   . HOH L 3 .   ? 35.536 58.324  65.476 1.00 38.99  ? 831 HOH A O   1 
HETATM 3763 O  O   . HOH L 3 .   ? 47.473 59.183  47.740 1.00 47.64  ? 832 HOH A O   1 
HETATM 3764 O  O   . HOH L 3 .   ? 47.882 61.784  48.378 1.00 42.39  ? 833 HOH A O   1 
HETATM 3765 O  O   A HOH L 3 .   ? 25.217 68.656  55.549 0.52 40.93  ? 834 HOH A O   1 
HETATM 3766 O  O   B HOH L 3 .   ? 24.749 70.599  54.883 0.48 36.25  ? 834 HOH A O   1 
HETATM 3767 O  O   . HOH L 3 .   ? 49.288 89.277  51.421 1.00 38.61  ? 835 HOH A O   1 
HETATM 3768 O  O   . HOH L 3 .   ? 51.044 66.559  48.848 1.00 46.55  ? 836 HOH A O   1 
HETATM 3769 O  O   . HOH L 3 .   ? 33.294 101.992 46.905 1.00 58.79  ? 837 HOH A O   1 
HETATM 3770 O  O   . HOH L 3 .   ? 16.180 82.272  53.292 1.00 25.94  ? 838 HOH A O   1 
HETATM 3771 O  O   . HOH L 3 .   ? 49.483 98.664  51.108 1.00 42.14  ? 839 HOH A O   1 
HETATM 3772 O  O   . HOH L 3 .   ? 35.729 70.031  43.907 1.00 36.35  ? 840 HOH A O   1 
HETATM 3773 O  O   . HOH L 3 .   ? 47.283 67.699  45.974 1.00 48.03  ? 841 HOH A O   1 
HETATM 3774 O  O   . HOH L 3 .   ? 51.403 99.163  71.985 1.00 39.75  ? 842 HOH A O   1 
HETATM 3775 O  O   . HOH L 3 .   ? 39.406 53.329  53.579 1.00 33.02  ? 843 HOH A O   1 
HETATM 3776 O  O   . HOH L 3 .   ? 38.165 75.235  42.871 1.00 43.11  ? 844 HOH A O   1 
HETATM 3777 O  O   . HOH L 3 .   ? 25.252 87.663  65.685 1.00 39.92  ? 845 HOH A O   1 
HETATM 3778 O  O   . HOH L 3 .   ? 29.591 62.872  59.471 1.00 55.25  ? 846 HOH A O   1 
HETATM 3779 O  O   . HOH L 3 .   ? 52.968 85.062  65.198 1.00 48.61  ? 847 HOH A O   1 
HETATM 3780 O  O   . HOH L 3 .   ? 25.053 32.194  57.420 1.00 50.78  ? 848 HOH A O   1 
HETATM 3781 O  O   . HOH L 3 .   ? 51.831 64.937  60.657 1.00 42.97  ? 849 HOH A O   1 
HETATM 3782 O  O   . HOH L 3 .   ? 33.395 83.969  48.732 1.00 21.61  ? 850 HOH A O   1 
HETATM 3783 O  O   . HOH L 3 .   ? 34.777 81.790  45.850 1.00 28.69  ? 851 HOH A O   1 
HETATM 3784 O  O   . HOH L 3 .   ? 47.304 54.071  57.628 1.00 37.89  ? 852 HOH A O   1 
HETATM 3785 O  O   . HOH L 3 .   ? 41.661 60.356  45.547 1.00 25.13  ? 853 HOH A O   1 
HETATM 3786 O  O   . HOH L 3 .   ? 21.621 80.804  61.980 1.00 35.52  ? 854 HOH A O   1 
HETATM 3787 O  O   . HOH L 3 .   ? 37.076 103.487 60.717 1.00 49.30  ? 855 HOH A O   1 
HETATM 3788 O  O   . HOH L 3 .   ? 45.151 78.413  69.135 1.00 44.78  ? 856 HOH A O   1 
HETATM 3789 O  O   . HOH L 3 .   ? 43.940 66.409  45.648 1.00 18.86  ? 857 HOH A O   1 
HETATM 3790 O  O   A HOH L 3 .   ? 39.080 79.263  68.294 0.37 25.91  ? 858 HOH A O   1 
HETATM 3791 O  O   B HOH L 3 .   ? 38.739 80.222  70.503 0.63 22.42  ? 858 HOH A O   1 
HETATM 3792 O  O   . HOH L 3 .   ? 24.491 35.948  58.502 1.00 39.21  ? 859 HOH A O   1 
HETATM 3793 O  O   . HOH L 3 .   ? 36.194 48.955  71.968 1.00 49.19  ? 860 HOH A O   1 
HETATM 3794 O  O   . HOH L 3 .   ? 25.396 70.820  52.082 1.00 55.17  ? 861 HOH A O   1 
HETATM 3795 O  O   . HOH L 3 .   ? 42.238 80.279  49.804 1.00 30.28  ? 862 HOH A O   1 
HETATM 3796 O  O   . HOH L 3 .   ? 27.077 79.299  49.365 1.00 58.93  ? 863 HOH A O   1 
HETATM 3797 O  O   . HOH L 3 .   ? 26.729 95.277  68.401 1.00 40.34  ? 864 HOH A O   1 
HETATM 3798 O  O   . HOH L 3 .   ? 28.521 79.379  43.242 1.00 39.09  ? 865 HOH A O   1 
HETATM 3799 O  O   . HOH L 3 .   ? 29.437 60.887  51.021 1.00 44.94  ? 866 HOH A O   1 
HETATM 3800 O  O   . HOH L 3 .   ? 51.300 64.292  48.327 1.00 49.61  ? 867 HOH A O   1 
HETATM 3801 O  O   . HOH L 3 .   ? 21.062 28.069  76.070 1.00 44.48  ? 868 HOH A O   1 
HETATM 3802 O  O   . HOH L 3 .   ? 32.017 49.991  65.927 1.00 57.01  ? 869 HOH A O   1 
HETATM 3803 O  O   . HOH L 3 .   ? 8.522  49.432  68.950 1.00 58.92  ? 870 HOH A O   1 
HETATM 3804 O  O   . HOH L 3 .   ? 46.216 51.194  70.249 1.00 61.82  ? 871 HOH A O   1 
HETATM 3805 O  O   . HOH L 3 .   ? 28.601 78.177  66.301 1.00 42.92  ? 872 HOH A O   1 
HETATM 3806 O  O   . HOH L 3 .   ? 28.928 101.137 54.126 1.00 60.22  ? 873 HOH A O   1 
HETATM 3807 O  O   . HOH L 3 .   ? 24.225 66.653  55.841 1.00 58.61  ? 874 HOH A O   1 
HETATM 3808 O  O   . HOH L 3 .   ? 55.283 72.532  51.125 1.00 40.78  ? 875 HOH A O   1 
HETATM 3809 O  O   . HOH L 3 .   ? 18.651 85.124  52.434 1.00 36.30  ? 876 HOH A O   1 
HETATM 3810 O  O   . HOH L 3 .   ? 33.931 60.381  65.055 1.00 41.50  ? 877 HOH A O   1 
HETATM 3811 O  O   . HOH L 3 .   ? 41.436 78.868  47.643 1.00 34.15  ? 878 HOH A O   1 
HETATM 3812 O  O   . HOH L 3 .   ? 26.651 93.600  65.881 1.00 46.19  ? 879 HOH A O   1 
HETATM 3813 O  O   . HOH L 3 .   ? 46.533 71.657  65.076 1.00 47.31  ? 880 HOH A O   1 
HETATM 3814 O  O   . HOH L 3 .   ? 64.338 105.314 75.531 1.00 58.96  ? 881 HOH A O   1 
HETATM 3815 O  O   . HOH L 3 .   ? 36.772 68.980  68.749 1.00 53.68  ? 882 HOH A O   1 
HETATM 3816 O  O   A HOH L 3 .   ? 30.198 63.452  56.295 0.58 36.18  ? 883 HOH A O   1 
HETATM 3817 O  O   B HOH L 3 .   ? 30.329 61.411  56.431 0.42 31.26  ? 883 HOH A O   1 
HETATM 3818 O  O   . HOH L 3 .   ? 50.713 88.880  49.639 1.00 48.07  ? 884 HOH A O   1 
HETATM 3819 O  O   . HOH L 3 .   ? 32.187 31.831  62.617 1.00 43.61  ? 885 HOH A O   1 
HETATM 3820 O  O   . HOH L 3 .   ? 25.515 95.806  71.950 1.00 55.65  ? 886 HOH A O   1 
HETATM 3821 O  O   . HOH L 3 .   ? 28.014 63.515  50.278 1.00 38.44  ? 887 HOH A O   1 
HETATM 3822 O  O   . HOH L 3 .   ? 47.681 54.162  48.557 1.00 44.08  ? 888 HOH A O   1 
HETATM 3823 O  O   . HOH L 3 .   ? 25.119 34.669  56.552 1.00 46.83  ? 889 HOH A O   1 
HETATM 3824 O  O   A HOH L 3 .   ? 16.547 88.421  52.797 0.48 45.96  ? 890 HOH A O   1 
HETATM 3825 O  O   B HOH L 3 .   ? 16.401 89.196  50.793 0.52 36.49  ? 890 HOH A O   1 
HETATM 3826 O  O   . HOH L 3 .   ? 32.880 85.738  44.736 1.00 44.72  ? 891 HOH A O   1 
HETATM 3827 O  O   . HOH L 3 .   ? 11.897 47.128  63.338 1.00 47.70  ? 892 HOH A O   1 
HETATM 3828 O  O   . HOH L 3 .   ? 23.495 78.630  63.412 1.00 46.64  ? 893 HOH A O   1 
HETATM 3829 O  O   A HOH L 3 .   ? 28.104 45.221  59.391 0.49 28.30  ? 894 HOH A O   1 
HETATM 3830 O  O   B HOH L 3 .   ? 27.886 43.361  59.163 0.51 29.03  ? 894 HOH A O   1 
HETATM 3831 O  O   . HOH L 3 .   ? 54.957 83.039  49.434 1.00 33.14  ? 895 HOH A O   1 
HETATM 3832 O  O   . HOH L 3 .   ? 30.844 103.616 54.908 1.00 58.87  ? 896 HOH A O   1 
HETATM 3833 O  O   A HOH L 3 .   ? 49.662 50.005  65.833 0.57 29.92  ? 897 HOH A O   1 
HETATM 3834 O  O   B HOH L 3 .   ? 50.688 48.731  66.804 0.43 34.42  ? 897 HOH A O   1 
HETATM 3835 O  O   . HOH L 3 .   ? 48.768 48.796  53.022 1.00 46.75  ? 898 HOH A O   1 
HETATM 3836 O  O   . HOH L 3 .   ? 48.322 58.159  69.443 1.00 50.64  ? 899 HOH A O   1 
HETATM 3837 O  O   . HOH L 3 .   ? 62.345 105.664 74.581 1.00 52.23  ? 900 HOH A O   1 
HETATM 3838 O  O   A HOH L 3 .   ? 29.929 46.890  56.219 0.44 17.79  ? 901 HOH A O   1 
HETATM 3839 O  O   B HOH L 3 .   ? 30.805 46.413  58.236 0.56 22.85  ? 901 HOH A O   1 
HETATM 3840 O  O   . HOH L 3 .   ? 42.041 30.334  73.145 1.00 54.06  ? 902 HOH A O   1 
HETATM 3841 O  O   . HOH L 3 .   ? 51.355 59.748  53.830 1.00 54.10  ? 903 HOH A O   1 
HETATM 3842 O  O   . HOH L 3 .   ? 33.139 105.515 56.042 1.00 61.26  ? 904 HOH A O   1 
HETATM 3843 O  O   . HOH L 3 .   ? 27.834 94.302  58.386 1.00 51.40  ? 905 HOH A O   1 
# 
